# Patent

## Title
Crystal structures of T. foetus inosine monophosphate dehydrogenase in complex with substrate, cofactor and analogs and uses thereof

## Abstract

The invention provides a crystalline complex containing T. foetus IMPDH in complex with inosine monophosphate (IMP), the complex specified by disclosed atomic coordinates. Also provided are crystalline complexes of containing T. foetus IMPDH with both inosine monophosphate (IMP) and mycophenolic acid, with both xanthosine monophosphate (XMP) and mycophenolic acid, with both xanthosine monophosphate (XMP) and nicotinic adenine dinucleotide (NAD), with ribovirin (1-β-D-ribofuranosyl-1,2,4-triazole-3-carboxamide, and with both ribovirin and mycophenolic acid, each complex specified by disclosed atomic coordinates. Also provided by the invention are the atomic coordinates for these complexes. Further provided by the invention are methods for identifying modulations of IMPDH that employ the atomic coordinates of the invention.

## Background
This application claims benefit of the filing date of U.S. Provisional Application No. 60/410,523, filed Sep. 13, 2002, and U.S. Provisional Application No. 60/412,044, filed Sep. 18, 2002, both of which are incorporated herein by reference.


This invention was made in part with U.S. Government support under Grant No. R01-GM56445, awarded by the National Institutes of Health. The U.S. Government has certain rights in this invention.


BACKGROUND OF THE INVENTION
This invention relates generally to drug development and, more specifically, to designing compounds that modulate inosine monophosphate dehydrogenase.
The enzyme inosine monophosphate dehydrogenase (IMPDH) is responsible for the rate-limiting step in guanine nucleotide biosynthesis. Because it is up-regulated in rapidly proliferating cells, human type II IMPDH is actively targeted for immunosuppressive, anticancer, and antiviral chemotherapy. The enzyme employs a random-in ordered-out kinetic mechanism where substrate or cofactor can bind first but product is only released after the cofactor leaves. Due to structural and kinetic differences between mammalian and microbial enzymes, most drugs that are successful in the inhibition of mammalian IMPDH are far less effective against the microbial forms of the enzyme. However, with greater knowledge of the structural mechanism of the microbial enzymes, more effective and selective inhibitors of microbial IMPDH can be developed for use as anti-microbial drugs.
Thus, there exists a need for identifying and designing compounds that modulate IMPDH activity. The present invention satisfies this need and provides related advantages as well.
SUMMARY OF THE INVENTION
The invention provides a crystalline complex containing T. foetus inosine monophospate dehydrogenase (IMPDH) in complex with inosine monophosphate (IMP), the complex specified by disclosed atomic coordinates. Also provided are crystalline complexes of containing T. foetus IMPDH with both inosine monophosphate (IMP) and mycophenolic acid, with both xanthosine monophosphate (XMP) and mycophenolic acid, with both xanthosine monophosphate (XMP) and nicotinic adenine dinucleotide (NAD), with ribavirin (1-β-D-ribofuranosyl-1,2,4-triazole-3-carboxamide), and with both ribavirin and mycophenolic acid, each complex specified by disclosed atomic coordinates. The T. foetus IMPDH structures have complete active sites. Also provided by the invention are the atomic coordinates for these complexes. Further provided by the invention are methods for identifying a modulator of IMPDH that employ the atomic coordinates of the invention.
The invention provides methods for identifying an inhibitor of IMPDH. In one embodiment, a method of the invention involves displaying a structure for IMPDH, or a portion thereof, wherein the structure has a set of atomic coordinates shown in Tables 2–7; (b) docking a structure of a candidate inhibitor to the structure of IMPDH, or the portion thereof; and (c) identifying an inhibitor of IMPDH, wherein the inhibitor has a structure that docks favorably to the structure of IMPDH, or the portion thereof. In one embodiment, the method is used to identify an inhibitor that targets the substrate binding site to which IMP or XMP binds. In another embodiment, the method is used to identify an inhibitor that targets the NAD cofactor binding site to which NAD or MOA binds. In a further embodiment, the method can include docking a candidate inhibitor to a second IMPDH structure.
In another embodiment, the invention provides a method of identifying an inhibitor of IMPDH that involves displaying the structure for the bound complex of T. foetus IMPDH with NAD set forth in Table 5, (b) docking a structure of a candidate inhibitor to said structure, or portion thereof; and identifying a compound that binds Asp-358 and Asp-261, wherein said compound has a structure that docks favorably to said structure, or portion thereof.
In a further embodiment, the invention provides a method of identifying an inhibitor of IMPDH that involves (a) selecting a candidate compound by performing rational drug design with a set of atomic coordinates set forth in Tables 2–7, wherein said selecting is performed in conjunction with computer modeling; (b) contacting said compound with IMPDH, and (c) determining the ability of said compound to reduce IMPDH activity, wherein a compound that reduces IMPDH activity is an inhibitor of IMPDH.



BRIEF DESCRIPTION OF THE DRAWINGS
FIG. 1 shows IMPDH crystals from the original ammonium sulfate condition (left) compared with those grown from the sodium malonate (right). In malonate, the crystals grew to 0.4–0.8 mm in length while the sulfate crystals grew to between 0.1 and 0.4 mm. The sulfate-grown crystals were also much more fragile. Further, the malonate in the mother liquor acted as a cryoprotectant. No detectable needle-shaped crystals, which were observed in the sulfate condition, were observed in the malonate condition.
FIG. 2 shows a ribbon diagram of the IMPDH tetramer viewed along the four-fold axis. The enzyme is in complex with the product XMP (light shading), the cofactor NAD+ (dark shading) and the potassium. Although the cofactor lies along the dimer interface, it does not make contact with the neighboring monomer. All molecular images were prepared with the program Deepview and rendered in POVRAY 3.5 beta.
FIG. 3 shows the active site loop of T. foetus IMPDH. A 2.2 Å resolution 2Fo–Fc electron density map contoured at 0.5 σ surrounds a model of the active site loop from the IMP-bound structure. The low contouring level is necessary to obtain continuous electron density.
FIG. 4 shows that a potassium ion was located at the dimer interface near the cofactor binding site. The carbon atoms of the neighboring monomer are shaded and waters are shown as spheres. The ion's hydrogen bonding partners and bond distances, clockwise from Asp264, are 2.94 Å and 2.49 Å, Asn460 (2.66 Å), Ser22 (2.57 Å), Gly20 (2.30 Å), and Phe260 (2.64 Å).
FIG. 5 shows a ribbon diagram of one IMPDH monomer looking down the barrel of the protein with bound, XMP, NAD+ (both in CPK), and the potassium ion.
FIG. 6 shows binding of the inhibitor MOA to IMPDH showing bonds (a) with IMP (substrate) and (b) with XMP (product). A notable difference is the movement of the Glu431 side chain, which binds both the substrate and the inhibitor in the IMP-bound structure.
FIG. 7 shows a comparison of the active site loop of the B. burgdorferi apo structure (purple) with those of T. foetus IMP-bound (yellow), IMP+MPA (blue), XMP+MPA (green), and XMP+NAD+ (red) shows a high degree of stability throughout the core domain of the enzyme as well as the resolved portion of active site flap during substrate and product binding. Also pictured are XMP and NAD+ in CPK and the potassium ion in gray.
FIG. 8 shows a comparison of the fit of the T. foetus product XMP and NAD+ into electron density. On the left, the T. foetus structure is shown with a 2Fo–Fc electron density map contoured at 1.0 σ, and on the right, the published human structure with 6-Cl IMP and the cofactor analog, SAD, uses a σA-weighted Fo–Fc omit map. Panel b illustrates the binding of NAD+ to the cofactor binding site of T. foetus IMPDH. NAD+ makes extensive use of hydrogen bonds with IMPDH and ordered waters. The nicotinamide ring n-bonds with the purine ring of XMP while the adenosine ring stacks between Trp269 and Arg241.
FIG. 9 shows a structural alignment demonstrates that potassium binding is conserved through all T. foetus structures presented here. The carbon atoms of a neighboring monomer are shown in dark gray. The T. foetus structure contains an aspartate at 264 while the mammalian enzyme (purple oxygens) has substituted a glutamine (b) and the bacterial enzyme (also purple oxygens) substitutes a histidine (c). Both of these side chains leave no room for the ion. An alignment of the T. foetus structure (blue), human structure (yellow) and S. pyogenes structure (green) shows that this does not appear to uniquely alter the dimer interface (d).
FIG. 10 shows a 2Fo-Fc electron density map contoured at 0.6 σ reveals that Π stacking is involved in forming the crystallographic dimer interface and that Trp416 from each monomer may occupy a position at the two-fold interface at 50% occupancy.
FIG. 11 shows structural formulas of the indicated compounds. The product XMP contains an additional keto group at the C2 position of the substrate IMP. This figure was created with Ligplot (Wallace et al., Prot. Eng. 8:127–134 (1995)) and Photoshop (Adobe Systems, San Jose, Calif.).
FIG. 12 shows a Michaelis-Menten graph. The initial velocity increases with increasing concentration of substrate. The concentrations of enzyme and cofactor were held constant.
FIG. 13 is a plot showing IMPDH inhibition with increasing concentration of RMP. The concentrations of IMP, NAD+, and enzyme are constant.
FIG. 14 shows a ribbon diagram of the IMPDH tetramer viewed looking down the four fold axis. The enzyme is in complex with the inhibitor RMP (CPK) and a sodium ion (green). A potassium ion (blue) lies in the dimer interface near the cofactor binding site. This image was made in Deepview (Guex and Peitsch, Electrophoresis 18:2714–2723 (1997)) and rendered in POVRAY 3.5 beta (www.povray.org).
FIG. 15 shows composite annealed omit electron density maps at 1.9 Å resolution surrounding the inhibitor RMP (a) contoured at 1.8 σ. The MOA-soaked RMP co-crystal structure (b) at 2.2 Å shows nearly complete density for MOA only when contoured at 0.5 σ despite soaking in saturating amounts of MOA. Soaking for longer periods did not improve occupancy.
FIG. 16 shows a diagram of RMP hydrogen bonds with IMPDH. Like IMP, RMP makes many bonds with ordered waters and main chain atoms. Only the Tyr405 hydroxyl and the Asp358 carboxylate side chains make contact with the inhibitor. Additionally, Met59, Ile318, and Gly407 make hydrophobic contacts. Solvent accessibility is indicated by the yellow border around RMP, where lighter color indicates greater accessibility. This figure was created with NACCESS (Hubbard and Thornton, University College London, Department of Biochemistry and Molecular Biology, (1993)), HBPLUS (McDonald and Thornton, J. Mol. Biol. 238:777–793 (1994)), and LIGPLOT.
FIG. 17 shows that the ion binding site (green) is composed of backbone carbonyls from the active site loop residues, including the active site cysteine, and residues from the C-terminus of the neighboring catalytic monomer (gray carbons).



DETAILED DESCRIPTION OF THE INVENTION
This invention relates to crystalline compositions of Tritrichomonas foetus (T. foetus) inosine monophospate dehydrogenase (IMPDH) complexes with its natural substrate, product, cofactor and inhibitors. The invention further relates to the discovery of high resolution crystal structures of different complexes of IMPDH, including complexes with its substrate IMP; with IMP and inhibitor mycophenolic acid (MPA); with inhibitor ribavirin; with MOA and ribavirin; with the product XMP and MOA; and with XMP and the cofactor NAD+.
As disclosed herein, six complexes of T. foetus IMPDH bound with IMP, IMP+MPA, XMP+MPA, XMP+NAD+, ribavirin and ribavirin+MOA. In particular, the high-resolution crystal structures of four T. foetus IMPDH complexes with substrate, cofactor, and inhibitors—IMP, XMP+NAD+, IMP+MPA, and XMP+MPA-represent the first T. foetus structures with a complete active site, the first IMPDH structure with the NAD+ cofactor bound, and the first with MOA bound in addition to unreacted substrate, and product. As is described in Example IV, a novel monovalent cation bound at the dimer interface that is likely unique to T. foetus and can contribute to the stability of the cofactor binding site. The active site cation appears to be present only in the covalent substrate-complex and conformations further along the catalytic cycle for most eukaryotic organisms, but it is already present in prokaryotic organisms upon substrate binding.
Current development of drugs that bind IMPDH has focused on developing highly potent inhibitors of the human form of the enzyme. The invention provides structural information useful for development of inhibitors of microbial IMPDH. Compounds designed as inhibitors of microbial IMPDH are useful for treating diseases caused by a variety of microbes, including for example, bacteria, viruses and parasites.
In one embodiment, the invention provides atomic coordinates for the bound complex of T. foetus inosine monophosphate dehydrogenase (IMPDH) (SEQ ID NO:2) with inosine monophosphate (IMP). The atomic coordinates for the IMPDH-IMP complex are provided in Table 2.
In another embodiment, the invention provides atomic coordinates for the bound complex of T. foetus IMPDH (SEQ ID NO:2) with IMP and mycophenolic acid (also referred to herein as MOA or MOA). The atomic coordinates for the IMPDH-IMP-MOA ternary complex are provided in Table 3.
In a further embodiment, this invention further provides atomic coordinates for the bound complex of T. foetus IMPDH (SEQ ID NO:1) with xanthosine monophosphate (XMP) and MOA. The atomic coordinates for the IMPDH-XMP-MOA ternary complex are provided in Table 4.
Also provided by the invention are atomic coordinates for the bound complex of T. foetus IMPDH (SEQ ID NO:1) with xanthosine monophosphate (XMP) and nicotinic adenine dinucleotide (NAD). The atomic coordinates for the IMPDH-XMP-NAD ternary complex are provided in Table 5.
The invention further provides atomic coordinates for the bound complex of T. foetus IMPDH with ribavirin (1-β-D-ribofuranosyl-1,2,4-triazole-3-carboxamide). The atomic coordinates for the IMPDH-ribavirin complex are provided in Table 7.
The invention further provides atomic coordinates for the bound complex of T. foetus IMPDH with ribavirin and MOA. The atomic coordinates for the IMPDH-ribavirin complex are provided in Table 6.
As used herein, the term “atomic coordinates” means Cartesian structure coordinates derived from mathematical equations relating to the patterns obtained on diffraction of a monochromatic beam of X-rays by the atoms (scattering centers) of IMPDH complexes in crystal form. The diffraction data are used to calculate an electron density map of the repeating unit of the crystal. The electron density maps are then used to establish the positions of the individual atoms of the IMPDH complexes. Those of skill in the art will understand that a set of atomic coordinates for an enzyme or an enzyme-complex or portion thereof, is a relative set of points that define a shape in three dimensions. Thus, it is possible that an entirely different set of coordinates could define a similar or identical shape. Moreover, slight variations in the individual coordinates will have little effect on overall shape.
The variations in coordinates discussed above can be generated because of mathematical manipulations of the atomic coordinates. For example, the atomic coordinates set forth in Tables 2–7, can be manipulated by crystallographic permutations of the atomic coordinates, fractionalization of the atomic coordinates, rotation of the atomic coordinates, integer additions or subtractions to sets of the atomic coordinates, invention of the atomic coordinates or any combination of the above.
Alternatively, modifications in the crystal structure due to mutations, additions, substitutions, and or deletions of amino acids, or other changes in any of the components that make up the crystal could also account for variations in structure coordinates. If such variations are within an acceptable standard error as compared to the original coordinates, the resulting three-dimensional shape is considered to be the same.
The atomic coordinates of the invention can be stored in a memory or computer readable medium. A memory or computer readable medium can be a hard disk, floppy disc, compact disc, magneto-optical disc, Random Access Memory, Read Only Memory or Flash Memory and the like. A computer system that contains the memory or computer readable medium used in the invention can be a single computer or multiple computers distributed in a network.
The atomic coordinates of the invention are useful for viewing or manipulating the structure of IMPDH in a conformation that binds IMP, XMP, MOA, NAD, ribavirin, and combinations thereof. The atomic coordinates shown in Tables 2–7 can be readily modified to remove one or more atoms in the structure including, for example, the atomic coordinates for IMP, XMP, MOA, NAD, ribavirin, or any combination thereof such that only a portion of the structure is viewed or manipulated. Other portions of the structures represented in Tables 2–7 that are useful in the invention include atoms of IMPDH that interact with IMP, XMP, MOA, NAD or ribavirin, such as those present in the active site loop, active site flap, or in other residues that interact with the ligands as described herein; IMP or atoms thereof that interact with IMPDH; XMP or atoms thereof that interact with IMPDH; NAD or atoms thereof that interact with IMPDH; MOA or atoms thereof that interact with IMPDH; ribavirin or atoms thereof that interact with IMPDH. A portion of the atomic coordinates useful in the invention need not be a contiguous fragment of IMPDH or its bound ligands. The atomic coordinates can be manipulated or structures viewed on any computer that supports molecular modeling software such as a personal computer, silicon graphics workstation or super computer.
Portions of IMPDH or its bound ligands can be represented as pharmacophores. As used herein the term “pharmacophore” is intended to mean a representation of relative position for two or more atoms based on their positions in a molecular structure. In addition to relative position a pharmacophore can represent other characteristics of the atoms including, for example, charge or hydrophobicity. A representation in a pharmacophore can be a point indicating, for example, the center of the atom or the representation can be a volume indicating, for example, an area in which the atom can reside making a favorable interaction with another atom. A pharmacophore can also include a volume representing locations where an atom is disallowed, for example, due to unfavorable interactions with another atom.
The atomic coordinates of the invention can be used in a variety of methods for rational drug design, such as in methods for identifying an inhibitor of IMPDH. Thus, the invention provides a method of identifying an inhibitor of IMPDH. The method includes steps of: (a) displaying a structure for IMPDH, or a portion thereof, wherein the structure has atomic coordinates shown in Tables 2–7; (b) docking a structure of a candidate inhibitor to the structure of IMPDH, or the portion thereof; and (c) identifying an inhibitor of IMPDH, wherein the inhibitor has a structure that docks favorably to the structure of IMPDH, or the portion thereof. A structure of IMPDH can be represented with a pharmacophore of an IMPDH binding site.
As used herein, the term “docking” means a computational means for performing a fitting operation between the candidate inhibitor and a portion of the structure of IMPDH. Such a portion of the structure of IMPDH can be, for example, a binding pocket.
In one embodiment, the method is used to identify an inhibitor that targets the substrate binding site to which IMP or XMP bind. Accordingly, the method can be used with a portion of IMPDH that includes atoms that interact with IMP or XMP such as those described in Examples IV and VII. The method can also be used to identify an inhibitor that targets the NAD cofactor binding site to which NAD or MOA bind. A portion of IMPDH that interacts with MOA and that is useful in a method of the invention can include, for example, atoms that interact with NAD or MOA as described in Examples V and VII. Any portion of the IMPDH structures including, for example, the active site loop, active site flap or others described herein can be used in a method of the invention.
A structure of a candidate inhibitor can be docked to a binding site of IMPDH to identify an inhibitor that is complementary in shape to the binding site or has favorable electrostatic interactions with the charged groups in the binding site. A candidate inhibitor can be identified based on structural similarity to IMP, XMP, NAD, MOA or ribavirin. For example, a molecular structure database such as the Cambridge Structure Database can be searched to identify molecules having a particular structural attribute of IMP, XMP, NAD, MOA or ribavirin or any other inhibitor that binds to IMPDH.
In one embodiment, the method is used to identify an inhibitor that targets the substrate binding site to which RIBAVIRIN binds. Accordingly, the method can be used with a portion of IMPDH that includes atoms that interact with RIBAVIRIN such as Ser317 hydroxyl, Tyr405 hydroxyl, main chain nitrogen of Ser317, main chain nitrogen of Gly381, main chain nitrogen of Arg382, the carboxylate of Asp358, the side chain of Ile318, hydrogen of Glu408 or hydrogen of Gly409. The method can also be used to identify an inhibitor that targets the NAD cofactor binding site to which MOA binds. A portion of IMPDH that interacts with MOA and that is useful in a method of the invention can include, for example, the carbonyl oxygen of Gly312, the amide nitrogen of Gly314 or the sulfhydryl of Cys319. Any portion of the IMPDH structures including, for example, the active site loop, active site flap or others described herein can be used in a method of the invention.
A structure of a candidate ligand can be docked using algorithms available in the art including, for example, those available in the software applications DOCK (Kuntz et al., J. Mol. Biol. 161:269–288 (1982)) or INSIGHT98 (Molecular Simulations Inc., San Diego, Calif.). Methods for screening a structural database to identify molecules that bind to IMPDH are described, for example, in Luecke et al., Exp. Parasitology 87:203–211 (1997).
An inhibitor that targets IMPDH can be designed to contain a moiety from a ligand that binds the substrate binding site of IMPDH and a moiety from a ligand that binds to the cofactor binding site of IMPDH. The moieties included in such an inhibitor can be portions of ligands that are bound in the structures disclosed herein or can be analogs of any portion of these ligands, so long as the portion or analog is capable of binding to IMPDH when present in the inhibitor. Accordingly, the moieties of an inhibitor so designed will function as binding moieties. The binding moieties can be linked by a third moiety that is capable of taking on a conformation that places the binding moieties in relative orientations similar to those observed in a crystal structure disclosed herein such as those having coordinates set forth in Tables 2–7. As an example, hydroxyl groups on the ribose rings of XMP and NAD, when bound in a ternary complex with IMPDH, both interact with aspartate residues of IMPDH. In particular Asp358 binds to the ribose hydroxyl of IMP or XMP and ASP261 binds to the NAD(H) nicotinamide ribose hydroxyls as shown in FIG. 10. The two aspartate residues are about 6.5 angstroms apart at the closest point as shown in FIG. 10. Accordingly, an inhibitor can be designed having two ribose moieties, or analogs thereof, linked to each other such that they can attain a conformation where they interact with these aspartates in IMPDH.
A method of the invention can further include a step of docking a candidate inhibitor to a second IMPDH structure. A second IMPDH structure used in a method of the invention can be a different conformation of the same IMPDH obtained, for example, by binding to different ligands. As described herein, the conformation of T. foetus IMPDH differs for the complexes described herein. Furthermore there are differences between the conformations of IMPDH disclosed herein and those for IMPDH bound to ribavirin phosphate and for IMPDH structures known in the art as set forth herein. Comparison of docking results for two or more different IMPDH conformations can be used to identify an inhibitor that has favorable binding interactions with IMPDH in multiple conformations. As described herein, the conformation of T. foetus IMPDH in a IMPDH-ribavirin complex differs from its conformation in an IMPDH-ribavirin -MOA ternary complex. Furthermore, the conformation of T. foetus IMPDH in a IMPDH-ribavirin complex differs from its conformation in apo IMPDH, IMPDH-IMP complex, IMPDH-XMP, IMPDH-XMP-MOA ternary complex, or IMPDH-XMP-NAD+ ternary complex. Comparison of docking results for two or more different IMPDH conformations can be used to identify an inhibitor that has favorable binding interactions with IMPDH in multiple conformations. A structure of apo IMPDH is available in the protein databank (PDB) under PDB code 1AK5. A structures of IMPDH bound to ribavirin phosphate and a structure of IMPDH bound to ribavirin and MOA in a ternary complex are described herein.
The crystal structures described herein reveal aspects of IMPDH structure and association with substrate, products and inhibitors previously unrecognized. Based on particular structural features revealed, an inhibitor of IMPDH activity can be designed. Therefore, in one embodiment, the invention provides a method of the invention for identifying an inhibitor of IMPDH can involve displaying a structure for the bound complex of T. foetus IMPDH with NAD set forth in Table 5; (b) docking a structure of a candidate inhibitor to said structure, or the portion thereof; and (c) identifying a compound that binds Asp-358 and Asp-261, wherein said compound has a structure that docks favorably to said structure, or portion thereof.
A second IMPDH structure used in a method of the invention can be from a different organism. By comparing docking interactions for a candidate inhibitor with IMPDH from different organisms, an inhibitor can be identified that is specific for a particular organism. For example, an inhibitor that is specific to T. foetus IMPDH compared to IMPDH from a mammal can be identified based on favorable docking of the candidate inhibitor to T. foetus IMPDH and less favorable or even unfavorable docking with IMPDH from the mammal. Such an inhibitor can be useful as a therapeutic agent to treat a cow infected with T. foetus as set forth below. Alternatively, comparison of docking results for IMPDH structures from two or more different organisms can be used to identify an inhibitor that has favorable docking with multiple IMPDH proteins, thereby identifying an inhibitor having relatively broad specificity. Structures for IMPDH from other organisms that are useful in the invention include, but are not limited to, those for IMPDH from mammals including, for example, humans, primates, non-human primates, Chinese hamster, agricultural animals such as cow, horse, sheep, goats, pigs; invertebrates, yeast, bacteria, or protozoa. Examples of IMPDH structures from other organisms that are useful in the invention include human type II IMPDH in a ternary complex with 6-Cl-Imp and selenazole adenine dinucleotide (PDB code 1B30); IMPDH from S. pyogenes (PDB code 1ZFJ) and Chinese hamster IMPDH in complex with MOA (PDB code 1Jr1).
The invention provides another method of identifying an inhibitor of IMPDH. The method involves (a) selecting a candidate compound by performing rational drug design with a set of atomic coordinates set forth in Tables 2–7, wherein said selecting is performed in conjunction with computer modeling; (b) contacting said compound with IMPDH, and (c) determining the ability of said compound to reduce IMPDH activity, wherein a compound that reduces IMPDH activity is an inhibitor of IMPDH.
The ability of a compound to reduce IMPDH activity can be determined using a variety of well known methods. Such methods include those described in Metz et al. Endocrinology 142:193–204 (2001) and Wilson et al. J. Biol. Chem. 266(3):1665–1671 (1991). Computer modeling can be performed using a variety of well known methods, including commercial modeling packages, such as those described herein above.
It is understood that the atomic coordinates of IMPDH disclosed herein can also be used for identifying a compound that increases the activity of IMPDH. Such a compound can be useful, for example, for increasing the viability of a microbe or as a therapeutic agent used to treat a disease or condition that is mediated by IMPDH or that can be reduced by increasing IMPDH activity.
An IMPDH inhibitor identified by a method of the invention can be used as a therapeutic agent. A therapeutic agent identified using the methods of the invention can be used to treat a disease or condition that is mediated by IMPDH or that is reduced by inhibitors of this enzyme such as ribavirin or MOA. Such an agent can be used to treat a mammal, agricultural animal, human, dog, cat or horse. For example, an inhibitor of T. foetus IMPDH can be used to treat cows infected with the T. foetus protozoan. A therapeutic agent identified using the methods of the invention can be used as an antiproliferative, antiviral, anticancer or immunosuppresive agent. A therapeutic agent identified using a method of the invention can be useful for treating a cancer such as those causing a benign or malignant tumor of the breast, prostate, colon, lung, brain or ovary. A therapeutic agent identified using a method of the invention can be useful for treating a viral infection such as one caused by hepatitis A, B or C; respiratory syncytial virus, HIV or hanta virus. A therapeutic agent identified using a method of the invention can be useful for treating a fungal infection such as one caused by Aspergillus, Penicillium, Alternaria, Cladosporium, and Fusarium. A therapeutic agent identified using a method fungal viral infection such as one caused by Aspergillus, Penicillium, Alternaria, Cladosporium, and Fusarium. A therapeutic agent identified using a method of the invention can be useful for treating a bacterial infection such as one caused by Staphylococcus spp., Streptococcus spp., Haemophilus influenzae, Pseudomonas aeruginosa, enteric Gram-negative bacilli, Moraxella lacunata, Acinetobacter spp., Neisseria gonorrhoeaei, Branhamella catarrhalisi, Clamydia trachomatis, and anaerobes. A therapeutic agent identified using a method of the invention can be useful for treating a parasitic infection such as one caused by Acanthamoeba and Toxoplasma gondii. A therapeutic agent identified using a method of the invention can be useful in combination with other treatments, for example, as an immunosuppressive agent administered following organ or cell transplantation.
It is understood that modifications which do not substantially affect the activity of the various embodiments of this invention are also included within the definition of the invention provided herein. Accordingly, the following examples are intended to illustrate but not limit the present invention.
EXAMPLE I
Cystallization of T. foetus IMPDH with Bound Substrate, Cofactor and Analogs
This example shows expression, purification, and crystallization of T. foetus IMPDH with bound IMP, IMP+MPA, XMP+MPA, and XMP+NAD+.
Protein expression and subsequent purification yielded approximately 90 mg of pure and active protein as determined by Coomassie stained SDS PAGE gels and a spectrophotometrically observed increase of NADH when enzyme is added to IMP and NAD+ using previously described methods (Digits and Hedstrom, Biochem. 38:2295–2306 (1999)). This yield could be increased substantially by optimizing the fermentation parameters, in particular by supplementing oxygen, as this was the limiting factor.
A pBAce plasmid (Chin and Wang, Mol. Biochem. Parasitol. 63:221–229 (1994)) containing T. foetus IMPDH (Beck et al., Exp. Parsitol. 78:101–112 (1994)) was transformed into Escherichia coli strain H712 (E. coli Stock Center, Yale University, New Haven, Conn.). This bacterial strain is deficient in native IMPDH and requires rich media for growth unless supplemented with a source of GMP or guanosine. Expression of T. foetus IMPDH was achieved by activation of the PhoA promoter under low phosphate conditions using supplemented MOPS minimal media using a modified version of previously published protocols (Craig et al., Proc. Natl. Acad. Sci. USA 88:2500–2504 (1991); Neidhardt et al., J. Bacteriol. 119:736–747 (1974); Yuan et al., J. Biol. Chem. 265:13528–13532 (1990)). Briefly, the cells were grown in MOPS media in a 19-liter fermentor (Wheaton Science Products, Millville, N.J.) inoculated with 0.5 liters of overnight MOPS culture of H712 containing the IMPDH plasmid. Temperature was maintained at 37° C., dissolved oxygen (DO) was maintained at greater than 40% with aeration, stirring, and glucose addition. The cells were harvested at 8 hours when the DO dropped to below 20% at roughly OD600 =1.5.
The cells were concentrated to 0.5 L by tangential flow filtration (Millipore, Inc., Bedford, Ma.), pelleted by centrifugation at 6,000 g, then re-suspended in a three fold volume of buffer A (50 mM Tris pH 8, 50 mM KCl, 10% glycerol, and 1 mM 2-mercaptoethanol) supplemented with protease inhibitors and 1 mM EDTA. The cells were then flash frozen in liquid nitrogen before storage at  ̃85° C. This mixture was lysed by French Press and clarified by centrifugation at 20,000 g. The resulting lysate was then run over a Cibacron blue column on an AKTA FPLC (Amersham-Pharmacia). Cibacron blue is a dye ligand that selectively binds many proteins that use NAD+ as a cofactor. The protein was found to elute from the column in a broad peak with a gradient of 50 mM–1M KCl over 20 column volumes. Protein elution from the column was optimized by eliminating the gradient and eluting the protein in 1 M KCl. This was followed by dialysis into buffer A and concentration to 15 mg/ml. The protein was then passed through a monoQ column (Amersham-Pharmacia) using a gradient from 50 mM to 500 mM KCl over 20 column volumes. The resulting protein was >90% pure and was dialyzed in buffer A and concentrated to 30 mg/ml for storage at −85° C.
The protein was first crystallized by optimizing previously published conditions (Whitby et al., Proteins 36:10666–10674 (1995)) by mixing 10–15 mg/ml protein in buffer A into 2.4 M ammonium sulfate, 100 mM Tris pH 8.0, 10% glycerol, 4 mM PEG 400, and 1 mM 2-mercaptoethanol well solution in 6 μl sitting drops in a 1:1 ratio of well solution to protein at 20° C. Crystals diffracting to higher resolution were obtained with the substitution of 42% saturated sodium malonate for 2.4 M ammonium sulfate. Additionally, the crystals grew to a larger size without increased mosaicity, and the malonate provided excellent cryo-protection as no other additives were necessary.
EXAMPLE II
Crystalography Data Collection for of T. foetus IMPDH Complexes
This example describes data collection for T. foetus IMPDH crystal structures with bound IMP, IMP+MPA, XMP+MPA, and XMP+NAD+.
All of the ligands were co-crystallized with the exception of NAD+ and XMP. In the NAD++XMP structure, the NAD+ and XMP were added to five to seven day old crystals and allowed to soak for five days before data collection. Attempts were made to generate XMP covalently attached to the active site cysteine (E-XMP*) by addition of IMP to IMPDH in a reaction buffer containing NAD+ and MOA using methods previously described. The resulting x-ray structure was identical to the XMP+MPA co-crystal structure: there was clearly an oxygen atom on the C2 of XMP, but no covalent bond with the active site cysteine could be discerned.
Diffraction quality crystals grew within five days and although the crystal morphology changed due to the substitution of malonate for sulfate, the space group remained P432 (FIG. 1). The cryo-frozen crystals diffracted from 1.95 to 2.2 Å using synchrotron radiation. A randomly selected test set of diffraction data (5% of all structure factors) was set aside for Rfree calculations. All model building was carried out with the program O, and the program CNS was used for refinement. The original T. foetus apo structure was used as the initial model for all structures allowing unbiased building of the active site loop and flap. One round of rigid body refinement and simulated annealing was followed by several rounds of energy minimization, B factor refinement, model building, and water picking. Composite omit, 2Fo–Fc, and FO–Fc maps were generated to guide model building. The program PROCHECK was used to validate the structures (Laskowski et al., J. App. Cryst. 26:283–291 (1993)). Crystal, refinement, and PROCHECK statistics are presented in Table 1.
Initial diffraction of T. foetus IMPDH using the published ammonium sulfate crystallization conditions only reached 3.2 Å using a RAXIS IV detector. The modified conditions improved resolution to 2.45 and resolution was further improved using synchrotron radiation. Synchrotron data were collected at the Stanford Synchrotron radiation laboratory (SSRL) beam line 9-1 and at The Advanced Light Source, Lawrence Berkeley National Laboratory (ALS) beam line 5.0.2. X-ray data collection, reduction and refinement statistics can be found in Table 1. Diffraction data were collected under cryo conditions using colorless crystals ranging in size from 0.4 to 0.8 mm. The crystals were loop-mounted and flash-cooled to −170° C. in the nitrogen stream. The data were collected from single crystals and integrated and scaled in the Denzo-Scalepack package (Otwinowski, Data Collection and Processing, SERC Daresbury Laboratory, Warrington, UK, pp. 56–62 (1993)). The published apo structure (Whitby et al., Biochem. 36:10666–10674 (1997)) was used as an initial model for all co-crystals, followed by rigid body and simulated annealing refinement. Several rounds of model building, energy minimization and B-factor refinement were then performed with the programs O (Jones et al., Acta Cryst. A47:110–119 (1991)) and CNS (Brunger et al., Akta Cyrst. D54:905–921 (1998)).
EXAMPLE III
Model Building for T. foetus IMPDH with bound IMP, IMP+MPA, XMP+MPA, and XMP+NAD+
This example describes model building for T. foetus IMPDH with bound IMP, IMP+MPA, XMP+MPA, and XMP+NAD+.
All IMPDH are homotetramers in solution under physiological conditions. In the cubic P432 spacegroup, this catalytic tetramer is formed by the crystallographic four-fold axis (FIG. 2). The active site loop, residues 313–330, was modeled in all but the XMP+NAD+ bound structure, which lacks residues 318–321. This loop is highly mobile, in part due to three glycine residues (residues 314–316) near the active site cysteine. Additionally, this loop has not been stabilized by covalently binding a substrate intermediate or inhibitor, resulting in weak electron density and high B factors. Visualization using electron density maps at lower contouring levels (0.5–0.8 σ) resulted in continuous or nearly continuous density throughout backbone of the active site loop (FIG. 3) with the exception of the NAD+ structure.
Furthermore, a larger portion of the active site flap (residues 408–433) was ordered in these structures in comparison to previous T. foetus structures. However, the distal portion of this loop was not modeled. Although there was scattered density for the 120-residue CBS domain, it was not contiguous and despite the improved resolution, this domain was not included in the model. Only the S. pyogenes structure contains the entire CBS domain (Zhang et al., Biochem. 38:4691–4700 (1999)).
The substrate IMP, product XMP, cofactor NAD+, and inhibitor MOA hetero-atoms in the structures presented here were placed into the apo model only when positive density was observed in Fo–Fc, 2Fo–Fc, and composite omit maps. The XMP was taken from the original T. foetus XMP structure (Whitby et al., supra, (1997)) and the IMP model was derived from this XMP structure. The NAD+ model was obtained from the phosphoglycerate dehydrogenase structure (Schuller et al., Nat. Struct. Biol. 2:69–76 (1995)) and the MOA model from the Chinese hamster IMPDH structure (Sintchak et al., Cell 85:921–930 (1996)). The IMP, XMP, and MOA hetero-atoms were fitted into density using 0 and minimized in CNS. The coordinates for NAD+ were fitted as above and subsequently submitted to the Dundee PRODRG Server (van Aalten et al., J. of Computer Aided Mol. Design 10:255–262 (1996)) for minimization and CNS topology file generation prior to refinement in CNS.
A cis peptide bond not previously described for IMPDH was located in all structures between Gly290 and Asn291 and is located within 7 Å of the nicotinamide portion of the NAD+ cofactor. This was present but not described in the T. foetus model co-crystallized with XMP (Whitby et al., supra, (1997)) but absent in all other structures to date. The cis bond appears to cause the chain to turn away from the active site, preventing it from entering the active site. All other IMPDH x-ray structures have this same turn but a cis peptide has not been reported in those structures.
A novel potassium ion was also identified in all structures, approximately 9 Å away from the cis peptide. This ion is coordinated by the backbone carbonyl of Phe266, the side chain carboxyl oxygens of Asp264, and the following atoms of a neighboring monomer: backbone carbonyls of Gly20 and Asn420, and the Ser22 hydroxyloxygen (FIG. 4). The potassium ion also lies near the NAD+ binding site and appears to stabilize the monomer—monomer interface as well as the cofactor binding site, but it does not make direct contact with NAD+ (FIG. 5).
A strong electron density peak was found extending from the active site cysteine thyol in the IMP and IMP+MPA bound structures. This appears to be a result of oxidation to sulfenic acid (Cys-SOH) from oxygen exposure during crystal formation and extended incubation prior to cryo-cooling for data collection. This type of oxidation has been previously described for NADH peroxidase (Stehle et al., J. Mol. Biol. 221:1325–1344 (1991)). Although it is interesting that the cysteine was modified only in the IMP-bound structures, this could be an artifact of crystallization as the active site cysteine was not resolved in the XMP+NAD structure, and the XMP+MPA structure had poor density around the cysteine.
EXAMPLE IV
Substrate and Product Binding to T. foetus IMPDH
This examples describes substrate and product binding to T. foetus IMPDH.
In all complex structures presented herein, the substrate/product sugar hydroxyls are hydrogen bonded to the carboxyl side chain of Asp358 as well as two waters. The purine O6 accepts a hydrogen-bond from the amide nitrogens of Glu408 and Gly409. The side chain of Ile318 makes van der Waals contact with the base. The nucleotide phosphate group is coordinated by the hydroxyl of Tyr405, backbone nitrogens of Ser317 Gly381, and Arg382, and three waters.
In the IMP complex structure, the purine N1 and N3 both form hydrogen bonds with waters. The water in contact with N1 is bridging it to the backbone carbonyl of Glu431, which is 4.79 Å from the N1 as well as Gln324. This portion of the active site flap was modeled into relatively poor density but the water is clearly observed, as well as the backbone from residue 429–431. The water on N3 is bridging it to the backbone nitrogen of Gly316. The phosphate group is coordinated by the hydroxyl and the main chain nitrogen of Ser317. The IMP+MPA complex differs from the IMP structure in that the purine N1 is forming a direct hydrogen bond with the Glu431 carboxylate oxygen. The other Glu431 carboxylate oxygen is in contact with the MOA ring hydroxyl.
Only in the XMP+MPA structure is the backbone carboxyl of Glu431 in direct contact with N1 and the active site flap is not shifted in this structure. The XMP+NAD+ complex structure is also characterized by the backbone carbonyl of Glu431 in direct contact with the purine N1. As in the IMP bound structure, the hydroxyl of Ser317 is pointing toward the XMP phosphate. However, the main chain nitrogen of Ser317, which was coordinating the water hydrogen bonding with N3 in the IMP structure, has moved 0.37 Å further away from the substrate and the water is no longer present.
Binding in the substrate-binding pocket is characterized by subtle conformational changes when binding IMP vs. XMP. Furthermore, a comparison with other IMPDH structures reveals few changes to the active site across species. IMP binds to the S. pyogenes enzyme in a nearly identical fashion as it binds to the T. foetus enzyme. Most noticeably, the purine ring system of the S. pyogenes IMP is rotated away from the catalytic Cys310. In T. foetus IMPDH, the ring system does not rotate away. Instead, it is the active site Cys319 that is displaced 1.3 Å from the catalytically active conformation. A structural alignment of T. foetus, S. pyogenes, and Chinese hamster IMPDH shows that the active site loops are almost identically positioned. Based on surrounding charges, bond distances, and geometry, we believe that there is a cation present in the bacterial structure at the position marked as water 179 in the coordinate entry (Zhang et al., supra, (1999)). Because the active site cysteine is displaced in the IMP-bound structure of the protist, the Cys319 backbone carbonyl disrupts the ion binding pocket. In the T. foetus XMP+MPA structure, the XMP C2 keto group causes the active site cysteine to move even further into the cation binding pocket.
Human type II IMPDH has the T. foetus Lys310 and Glu431 substituted with arginine and glutamine, accounting for part of the difference in sensitivity to MOA (Digits and Hedstrom, supra, (1999)). Glu431 is located near the N1 nitrogen of the IMP. In the structures presented here, only the IMP+MPA structure shows the side chain interacting with partially positively charged groups on both the IMP and MOA rings. In the other T. foetus structures, as well as the Chinese hamster and human type II structures, Glu431 is pointed away from the IMP, and toward the MOA or SAD inhibitors, leaving the main chain carbonyl pointed at the IMP, XMP, or 6-Cl IMP. The hamster Gln441 side chain is within hydrogen bonding distance of the MOA ring hydroxyl. The lysine or corresponding arginine is pointing between the IMP sugar hydroxyls and the MOA or cofactor. Because the arginine side chain is longer, they are near hydrogen bonding distance with one of the ribose hydroxyls of IMP and near the methyl group on the MOA ring.
RMS alignments of the substrate and product complex structures show very little movement in the core of the protein as well as the ordered portions of the active site flap. Unfortunately, the structures presented here have 10 to 14 residues missing from the active site flap, making characterization difficult. A possible explanation for this disorder is described below. The majority of conformational differences are located at the active site loop. The active site loop was resolved in all structures with the exception of the NAD+XMP co-crystal. In all cases, the loop is not well ordered with high B-factors, but overall, little movement is observed in the protein backbone of these structures with the exception of the IMP+MPA complex.
In the IMP+MPA structure, the side chains of the active site flap residues 431 to 434 move away from the active site to allow Glu431 to rotate around the Ca-C main chain bond and form hydrogen bonds with the IMP N1 and the MOA ring hydroxyl. The active site loop residues 320 to 323 shift away from the substrate+inhibitor complex with the Arg322 alpha carbon moving 7.5 Å from its position in the XMP+MPA model. It is unclear from these structures what is driving this movement of the loop, as these residues do not appear to be directly involved in substrate or cofactor binding. The nearest of these residues, Thr321, is 6.6 A away from the MOA in the XMP+MPA structure. This complex is unlikely to occur under physiological conditions since NAD+ has a far greater binding affinity than MOA. However, MOA does make a useful cofactor analog for the nicotinamide portion of the NAD+ binding site. This unique pairing may be useful in structure based drug design since a structure containing unreacted substrate and cofactor may be more difficult to obtain.
EXAMPLE IV
Cofactor and Inhibitor Binding to T. foetus IMPDH This example describes cofactor and inhibitor binding to T. foetus IMPDH.
In the two MOA complex structures (IMP+MPA and XMP+MPA), the inhibitor is bound in a similar manner (FIGS. 6a and b). One difference, however, is that the side chain of Glu431, which is hydrogen bonding with both the IMP and MOA, is shifted away from the product-inhibitor complex in the XMP+MPA structure. This may be caused by the stronger partial negative charge on the XMP due to the keto group at the C2 position of the base. The main chain nitrogen of Gly314 has moved from 3.26 Å to 3.64 Å away from the MOA ring O1. The nicotinamide portion of the NAD+ cofactor stacks with the XMP purine moiety and the nicotinamide oxygen hydrogen-bonds with the Gly314 nitrogen in the same manner as the MOA inhibitor. Additionally, the nicotinamide phosphate forms bonds with the hydroxyls of Ser262 and Ser263, as well as the main chain nitrogen of Ser263. The carboxylic acid tail of MOA also binds the Ser263 hydroxyl and nitrogen. The nicotinamide sugar hydroxyls form hydrogen bonds with Asp261. The NAD+ adenosine ring stacks between the side chains of Trp269 and Arg241. Arg241 also forms hydrogen bonds with the adenosine phosphate group.
Shown herein is the first IMPDH structure with both the XMP product and the NAD+ cofactor bound. Although the human type II structure has 6-Cl IMP and the NAD+ analog SAD bound in the respective substrate and cofactor binding sites, the 2.9 Å structure left some ambiguity in the positioning of the SAD molecule (Colby et al., Proc. Natl. Acad. Sci. USA 96:3531–3536 (1999)). At 2.15 Å and with good electron density in the cofactor binding site, we were able to accurately place the cofactor (FIG. 8). Although the cofactor lies near the monomer—monomer interface, it does not make contact with the neighboring subunit in the T. foetus tetramer. The nearest residue is Ile27, 4.7 Å away from the adenosine portion of the cofactor. This is in contrast to the human structure where the neighboring monomer makes contact with the adenosine ring. The nicotinamide sugar hydroxyls in the T. foetus structure form hydrogen bonds with Asp261 and two waters in the same manner as the substrate ribose hydroxyls interact with Asp358. Asp261 is completely conserved across species. In the human structure the cofactor sugar is further from the nicotinamide plane and one of its hydroxyls is out of reach of the human Asp274.
The proximal portion of the active site flap lies near the cofactor but the electron density is too ambiguous to discern any contacts. Similarly to the human type II structure, the adenosine portion of the cofactor is stacked between Arg241 and Trp269. These residues correspond to His253 and Phe282 of human type II IMPDH, and Arg253 and Tyr282 of human type I IMPDH. It is clear that this stacking is conserved in both the mammalian and T. foetus structures. Interestingly, the S. pyogenes model contains threonine and glycine in these positions, and with the exception of P. furious, which contains arginine and lysine residues, respectively, no bacterial sequence contains a stacking partner for the IMPDH cofactor at this location. This suggests that bacterial enzymes may have an alternate cofactor binding mechanism and may be the reason why the bacterial enzyme has a lower affinity for NAD+. If the NAD+adenosine ring is indeed not involved in base stacking in the bacterial structure, an effective inhibitor may be a mono-nucleotide nicotinamide derivative.
MPA does not appear to trap the covalently bound product. The inhibitor MOA binds to IMPDH in the nicotinamide portion of the cofactor-binding pocket using many of the same binding partners as the cofactor. The cofactor NAD+binds to IMPDH with many more interactions and therefore has a greater binding affinity to the enzyme when substrate is bound. Our failure to generate the covalent intermediate may be due to T. foetus IMPDH having a far faster release of E-XMP* than the mammalian enzyme (Digits and Hedstrom, supra, (1999)) or it may simply be that MOA does not inhibit XMP disassociation from T. foetus IMPDH. MOA does bind the T. foetus enzyme with significantly lower affinity than the mammalian form.
A novel potassium binding site was also identified. A high positive difference density peak in the Fo–Fc electron density map was observed at a dimer interface near the cofactor-binding site. This peak was surrounded by four backbone carbonyl oxygens and the carboxylate of Asp264 (FIG. 4). The charge environment indicates a cation, and the coordination and B factor are a probable indication of a potassium ion. This potassium is located too far from the substrate and cofactor to affect catalysis or to directly affect binding (FIG. 5). However, it may aid in cofactor binding by stabilizing adjacent residues, which are involved in cofactor binding. Additionally, the monovalent cation likely stabilizes the dimer interface. This ion is present in all structures presented here (FIG. 9a). The ion was not noted in the previous T. foetus structures (Whitby et al., supra, (1995); Whitby et al., supra, (1997)), but there was a water molecule placed at that location in the T. foetus XMP-bound structure. It is possible that the previous T. foetus structures were not at sufficient resolution to detect the ion.
This ion appears to be unique to T. foetus IMPDH and is not likely to represent the second ion binding site proposed for the E. coli enzyme (Kerr et al., Arch. Biochem. Biophys. 375:131–137 (2000)). A protein alignment shows that the T. foetus Asp264 is substituted with glutamine in most eukaryotic IMPDH and with histidine in prokaryotic IMPDH. A structural alignment with the human and bacterial structures (Colby et al., supra, (1999); Zhang et al., supra, (1999)) shows that the substitutions would cause steric and charge clashes with the potassium (FIGS. 9 b and c). Absence of this ion does not appear to affect the secondary structure of either human or bacterial IMPDH (FIG. 9d). The potassium ion reported in Chinese hamster IMPDH was not detected in these structures. This is likely due to the highly mobile nature of the active site loop that forms part of the T. foetus IMPDH potassium binding site. Additionally, T. foetus IMPDH retains 80% of its activity in the absence of potassium (Verham et al., Mol. Biochem. Parasitol. 24:1–12 (1987)) and it has been shown that other cations can activate bacterial IMPDH (Kerr et al., supra, (2000)). It is possible that this ion only binds in the covalently bound intermediate or similar conformations.
Possible Π stacking at crystal contacts disorder the active site flap. The entire active site flap has not been resolved in any IMPDH structure to date. It had been hypothesized that a T. foetus structure bound with substrate and MOA would resolve this loop (Digits and Hedstrom, Biochem. 39:1771–1777 (2000)). This was based on fluorescence assays where a single tryptophan on the active site flap was monitored under increasing concentrations of MOA. The resulting decrease in fluorescence suggested the tryptophan, as well as the flap, may have become ordered. Unfortunately, the flap remained disordered in all structures presented here. The reason for this may be that Trp416 is involved in Π stacking with Trp406, Arg412, and the corresponding residues of a neighboring, symmetry related monomer. This symmetry related monomer is not part of the catalytic tetramer and the space occupied by Trp416 is on a crystallographic two-fold axis, implying that each monomer can only occupy this site at 50%. Although this area has weak electron density, density large enough to fit the tryptophan side chain and the resulting spacing is reasonable for a single copy of Trp416 to fit in this space. Additional density suggests an alternate conformation for this tryptophan, adjacent to the peptide bond between Ser83 and Gln84 (FIG. 10). This tryptophan is physically able to fit in either position; however, residues 414 and 415, which also move as a result of the two conformations, have little density in either conformation and there is no usable density beyond Trp416 in either conformation. We believe that the residues beyond Trp416 are disordered, in part, because of the multiple conformations of this tryptophan. Mutation of this residue may aid in resolving this loop but it is also likely to inhibit crystallization due to the loss of this crystal contact. Furthermore, the tryptophan may be stabilizing the active site flap residues preceding it, and a mutation may cause a loss in resolution of a greater portion of the loop as is the case in most other IMPDH structures. It is possible that addition of adenosine or its analogs to this mutant protein could bridge the Π systems of the two monomers, however this hypothesis has not been tested.
EXAMPLE V
Proposed Structural Mechanism for T. foetus IMPDH
This example describes the proposed structural mechanism for T. foetus IMPDH.
An improvement upon the original T. foetus 2.3 Å apo structure structure showing the active site loop would increase the understanding of the catalytic mechanism of IMPDH. This is likely due to the increased flexibility of the T. foetus loop due to the three consecutive glycine residues present in the loop. The T. foetus Gly315 is substituted with a proline in B. burgdorferi, likely providing the active site loop with increased stability. It appears that the T. foetus loop is stabilized only by occupation of the active site. If the apo T. foetus active site loop conformation is similar to that of the B. burgdorferi loop, a hypothesis of the IMPDH structural mechanism can begin to be described.
The kinetic mechanism is random-in ordered-out with NADH leaving before XMP is released from the enzyme. When IMP binds the enzyme first, the enzyme is in an open conformation and IMP has easy access to the active site. When NAD+ binds first, the nicotinamide group blocks one entrance to the active site. Now, IMP must instead use the opening defined by the active site loop in its open configuration. An alignment of the apo B. burgdorferi structure and the T. foetus IMP-bound structure reveals an opening leading to the active site that is approximately 10 Å wide and 12 Å tall between the loop and the flap (FIG. 11). This opening, together with the flexible nature of the loop and the flap, would allow access to the active site. Additionally, Ser317 and the hydrophobic Ile318 are solvent-exposed. These two amino acids may serve as a bait to draw IMP into the structure. When IMP binds in the active site, it causes the loop to close and Ser317 to bind to the phosphate, while the Ile318 side chain forms hydrophobic interactions with the purine ring. This, in effect, closes the lid, and the substrate IMP or the product XMP must wait for NADH to leave before either nucleotide can dissociate from the enzyme.
With the exception of the IMP+MPA structure, there are no active-site bonds present in the IMP structure that are not present in the product+inhibitor or product+cofactor structure. It appears that the enzyme relies on the release of the cofactor and subsequent solvent exposure of the product with its newly formed keto group and the corresponding partial negative charge, in order for product to be released. This observation confirms kinetic studies of the T. foetus enzyme that show the off-rate of IMP at 7.7 s−1 and that of XMP at 17 s−1 without cofactor bound (Digits and Hedstrom, supra, (1999)). Additionally, the nicotinamide ring of NADH would lie near the O2 carbonyl of the product XMP; this newly developed partial charge may act to push the now less polar ring out of the active pocket.
The identification of a cation at the active site of the Chinese hamster structure and the possibility of a cation in the same location in the S. pyogenes structure are intriguing. An ion present when the substrate is bound but unreacted and still present when product is covalently bound might indicate that this ion is important in placing the active site cysteine in an orientation required for catalysis.
In the bacterial structure, Thr310 makes hydrogen bonds with an ordered water and the Glu420 main chain. This creates a stabilizing effect for several residues in the loop as well as the C-terminal portion of the active site flap. Examination of the other bacterial structure, B. burgdorferi in the apo conformation, reveals that the threonine is not in position to form bonds with the active site flap, resulting in a larger section of the C-terminal portion of the flap to be disordered. It appears that this increased stability in the S. pyogenes active site loop, and of Cys310 in particular, causes the purine to rotate away from the active site cysteine. In the T. foetus structure, Thr310 is substituted with Ile320 and this hydrophobic residue is likely to destabilize the active site loop in this conformation, allowing the cysteine to move rather than the purine. This threonine is conserved in prokaryotes while most eukaryotes carry the isoleucine. Apparently, it is the covalent bond with the substrate that is the stabilizing factor in the Chinese hamster model and it would not be surprising to find that the Ile-Thr substitution plays a role in prokaryote vs. eukaryotic enzyme kinetics.
EXAMPLE VI
Steady State Kinetic Analysis of T. foetus IMPDH
Steady-state kinetic analysis of to T. foetus IMPDH using IMP as a substrate was performed using a spectroscopic method. Initial velocity measurements were taken with increasing amounts of IMP and plotted as a Michaelis-Menten graph (FIG. 12).
From the plot, an apparent Km of 3.0 M was calculated for IMP. RMP, a competitive inhibitor for the substrate IMP, was then assayed for inhibition of the protozoan enzyme with increasing concentrations of RMP. These data were graphed as a Dixon plot (FIG. 13). The apparent Ki for RMP was determined to be 65 nM.
Steady-state kinetic analysis of T. foetus IMPDH was performed with 4.5 M enzyme in a reaction buffer containing 100 mM KCL, 50 mM Tris pH 8.0, 1 mM DTT and 1 mM NAD+. Reactions were initiated with the addition of IMP, and the production of NADH was monitored spectrophotometrically at 340 nm (340=6.22 mM−1 cm−1) using a Perkin Elmer Lambda 40 (EG&G, Inc., Wellesley, Ma) spectrophotometer at 25° C. For determination of the apparent Km value for IMP, the concentration of IMP was varied from Km/2 to 10 Km with the NAD+ concentration fixed at 1 mM. The initial velocity at various IMP concentrations was measured and was fit to the Michaelis-Menten equation by Sigma plot (SPSS Inc., Chicago, Ill.). Since RMP is known to be a competitive inhibitor with IMP, the apparent inhibition constant Ki of RMP was estimated using a Dixon plot. In the experiments, RMP concentration was varied while IMP concentration remained fixed at 40 M, and the NAD+ concentration was 1 mM. The initial velocities at various RMP concentrations were determined by the extraction of the linear portion of the reaction time-course. By plotting 1/v vs. inhibitor concentration, the apparent inhibition constant Ki was calculated using the following equation:

1/v=(Km/Vmax)(Ki[IMP]) [RMP]+1/Vmax(1+(Km/[IMP]))

EXAMPLE VII
Crystallization to T. foetus IMPDH with Ribavirin
Diffraction quality IMPDH crystals in the space group P432 grew within five days. The cryo-colored crystals diffracted to 1.90 Å for the RMP co-crystal and to 2.15 Å for the crystal with RMP and MOA using synchrotron radiation. A randomly selected test set of diffraction data (5% of all-structure factors) was set aside for Rfree monitoring. The published isomorphous T. foetus apo structure (PDB code 1AK5) was used as the initial model for both structures allowing unbiased building of the active site loop and the active site flap. One round of rigid body refinement and simulated annealing was followed by several rounds of energy minimization, B factor refinement, model building, and water picking. Composite 2Fo–Fc and Fo–Fc omit maps were generated to aid in model building. The program PROCHECK was used to validate the structures (Laskowski et al., J. App. Cryst. 26:283–291 (1993)). Crystal, refinement, and PROCHECK statistics are shown in Table 9.
IMPDH crystallized as a homotetramer with monomers related by the four-fold crystallographic axis (FIG. 14). The active site loop, residues 313–330, was modeled in both the RMP and RMP+MPA structures. The proximal portion of the active site flap (residues 408 to 416 and 431 to 433) was modeled, while the distal portion (residues 417–430) was disordered. Poor density in the region of the CBS domain was observed and no attempts were made at modeling this domain. The C-terminal amino acids 484–492 were also added to the original T. foetus model and although these nine residues do not appear to make direct contact with substrate or product, they do lie near the active site of a neighboring monomer in the catalytic tetramer and the backbone carbonyls of residues 485–487 from part of the active site cation binding pocket. Although RMP was clearly observable in the electron density of both crystal structures, density for MOA, even with saturating concentrations in the crystallization drop, was weak and was therefore modeled at 50% occupancy (FIG. 15). B factors for MOA at this level of occupancy were in agreement with the neighboring RMP atoms.
A cis peptide bond was modeled in both structures between Gly290 and Asn291. It is located near the cofactor binding site but does not appear to be close enough to directly influence cofactor binding. In addition, a strong peak of electron density was found extending from the active site cysteine sulfur in the RMP bound structure. This appears to be a result of the thiol oxidized to sulfenic acid (Cys-SOH), likely caused by exposure to oxygen during crystal formation prior to freezing.
As was observed in the IMP bound structure, the phosphate is coordinated with hydroxyls from Ser317 and Tyr405 as well as main chain nitrogens from residues 317, 381, and 382 (FIG. 16). Three solvent waters also form hydrogen bonds with the phosphate. As in all IMPDH structures, the substrate sugar hydroxyls form strong hydrogen bonds with a conserved aspartate carboxylate (Asp358). Ile318, which in the substrate and product complexes forms hydrophobic interactions with the purine ring, has moved 1.2 Å away from the RMP inhibitor. The RMP amide oxygen forms hydrogen bonds with Glu408 and Gly409. In the RMP+MPA structure the amide nitrogen is hydrogen-bonding to the MOA ring hydroxyl and the MOA inhibitor has moved 0.6 Å from its position in the XMP+MPA structure in the direction of the RMP purine ring derivative. In this position, the MOA ring O2 makes a hydrogen bond with the backbone nitrogen of Gly314, and the C3 oxygen hydrogen bonds with the catalytic sulfhydryl of Cys319.
The conformation of the active site loop in the RMP as well as the RMP+MPA structure is different from the loop conformation of the structures with bound substrate or product, resulting in a pocket surrounded by backbone carbonyl oxygens from Gly314, Gly316, and the active site Cys319, as well as carbonyls from Glu485, Gly486 and Gly487 in the neighboring catalytic monomer. A high (7.7 sigma) difference density peak was observed at the center of this pocket indicating the presence of a cation. Both Na+ and K+ ions were modeled into this site and minimized in CNS. A large peak of negative difference density was observed when K+ was modeled as well as high B factors. Because of the high concentration of sodium in the crystallization buffer, the previous observation that a sodium ion binds competitively with K+ in microbial IMPDH (Kerr et al., Arch. Biochem. Biophys. 375:131–137 (2000)), and B factors that are near that of the neighboring atoms, a Na+ ion was placed in the final model (FIG. 17).
As is described above, T. foetus IMPDH binds ribavirin in the active site substrate pocket. The RMP+MPA complex was difficult to obtain, as the MOA inhibitor was only observed with saturating amounts of MOA present in the crystallization drop. Attempts to obtain a co-crystal rather than an MOA soak were unsuccessful as the levels of MOA necessary to form the complex inhibited crystal formation. Although no data have been reported on the additive effects of ribavirin and MOA, it is unlikely that both inhibitors would occupy the substrate and cofactor binding pockets of the active site simultaneously, despite their distinct binding sites. The reason might be that MOA appears to rely on stacking its ring against the product XMP purine ring to bind to IMPDH and the RMP ring is probably too small for effective stacking.
A structure of RMP bound to human IMPDH has not been made available for direct comparison; however, we were able to compare the T. foetus RMP structure with the Chinese hamster structure that contains a covalently bound substrate intermediate (Sintchak et al., supra, (1996)). These structures show a high degree of similarity in the conformation of the active site loop, recruitment of a catalytic ion, as well as incorporation of the C terminal residues of the neighboring catalytic monomer to create the ion pocket. The reasons behind this appear to be the lack of the IMP C2 and N3 in the RMP inhibitor, which cause the hydrophobic Ile318, which normally forms hydrophobic contacts with the purine ring of the substrate or product, to move away from the more polar, less hydrophobic purine derivative. More importantly, with this portion of the purine ring absent, it is now more favorable for the active site cysteine (Cys319) to move into its catalytic position without the need for the NAD+ cofactor to bind and for catalysis to occur. This would not be the case with substrate or product present as the Cys319 sulfhydryl would be within 2.8 of the C2 position of IMP or within 1.5 of the oxygen bound to the C2 position of XMP.
It appears that in mammalian IMPDH and the presented T. foetus structures, the covalent intermdiate is necessary to recruit the ion to the active site whereas the inhibitor ribavirin allows the active site loop to occupy this position without forming a covalent bond with the enzyme. No ion was found in our T. foetus IMP bound structure. In the human IMPDH structure with the covalently bound inhibitor 6-Cl IMP, no cation was present because it was necessary for the active site loop to move from the purine ring C2 position to the inhibitor C6 position in order for the active site cysteine to form a covalent bond with the inhibitor. This movement in the loop prevented formation of the ion-binding pocket. Furthermore, the acitve site loop in the apo S. pyogenes structure is in this cation-binding conformation without a covalent intermediate and a possible ion, designated water 179 (PDB accession code IZFJ), appears to occupy the same cation position as in the Chinese hamster (PDB accession code 1JR1) and the T. foetus structures presented here. The IMP in the bacterial structure is not covalently bound and the C2 of the purine ring is rotated slightly away from the active site cysteine. In the T. foetus IMP structure, it is the loop that moves slightly away from C2 of IMP when compared to the hamster covalently bound structure and the B. burgdorferi apo structure.
The bacterial acitve site loop appears to be stabilized upon substrate binding by Thr310, which also makes hydrogen bonds with the active site flap, both directly and through an ordered water. This threonine is conserved in bacteria but is substituted with an isoleucine in eukaryotes, which appears to disrupt the structural coupling of the active site loop to the active site flap. This results in a partial destabilization of the active site loop allowing the active site cysteine to be displaced instead of the substrate. The bacterial acitve site loop is in the catalytic position immediately following substrate binding, and this could explain the ten fold higher Kcat compared to the mammalian and T. foetus enzymes (24, 2, 1.8 and 4 s−1 for S. pyogenes, T. foetus, and human type I and II, respectively) (Digits and Hedstrom, supra, (1999); Zhang et al., supra, (1999); Hager et al., Biochem. Pharmacol. 49:1323–1329 (1995)).
The mammalian and T. foetus enzymes, at some point after substrate binding, must first move the active site loop into position; recruit the active site cation and C-terminal residues of the neighboring monomer before catalysis is possible. These steps may be coupled to cofactor binding. If the positively charged NAD+ binds over the C2 position of IMP it may expose the substrate C2 to the active site cysteine thiol for subsequent nucleophilic attack. A role for the active site ion may be in stabilization of the active site loop during catalysis. The carbonyl oxygen from the active site Cys319 forms part of the cation binding site. When this site is occupied, the cysteine is in an ideal position to form a covalent bond with the C2 carbon of IMP. The cation-binding site appears to be formed before covalent bonding in bacterial IMPDH but likely occurs during covalent bond formation in mammalian and T. foetus IMPDH.
In the steady-state kinetic analysis of T. foetus IMPDH, an apparent Km of 3.0 μM for IMP was observed. This is consistent with the previously published Km value of 1.7 μM from a detailed bisubstrate kinetic analysis (Digits and Hedstrom, supra, (1999)). This value is much smaller than the Km of 14.2 and 9.2 μM, respectively, for human type I and II IMPDH (Hager et al., supra, (1995)) as well as the Km of 62 μM for S. pyogenes enzyme (Zhang et al., supra, (1999)). This result indicates the IMP binds to T. foetus IMPDH about 3 to 5-fold tighter than to mammalian enzymes. Interestingly, RMP, a nucleotide inhibitor, was shown to have a Ki of 65 nM for T. foetus IMPDH. This is about 5 to 10-fold lower than the Ki for human type I and II IMPDH, where the values are 650 nM and 390 nM, respectively (Hager et al., supra, (1995)). And it is considerably lower than the Ki of 6 μM for S. pyogenes IMPDH (Zhang et al., supra, (1999)). This result is consistent with steady-state kinetic analysis that shows that T. foetus IMPDH binds IMP (or the IMP analog RMP) more tightly than IMPDH from other species. Furthermore, the inhibition studies with RMP demonstrated that specifies specificity for an inhibitor does not occur in IMPDH. Our in vitro studies showed that RMP is a potent nanomolar inhibitor for T. foetus IMPDH and it appears that RMP is more effective against the protist form of IMPDH than the human and bacterial forms. A structural explanation for the 100 fold difference in Ki between T. foetus and S. pyogenes IMPDH could not be established from the highly conserved substrate binding site. The differences in Ki may be related, at least in part, to the kinetic mechanism. Further in vivo experiments are needed to address whether there is any clinical significance and pharmacological effects of ribavirin on T. foetus-infected cows.
Methods for Expression, Purification, and Crystallization of T. foetus IMPDH.
Recombinant T. foetus IMPDH enzyme was produced from a pBAce plasmid (Chin and Wang, supra, (1994)) containing the gene for T. foetus IMPDH (Beck et al., Exp. Parasitol. 78:101–112 (1994)) that was transformed into Escherichia coli strain H712 (E. coli Stock Center, Yale University, New Haven, Conn.). Expression of T. foetus IMPDH was achieved by modifying previously published protocols (Craig et al., Proc. Natl. Acad. Sci. USA, 88:2500–2504 (1991); Neidhardt et al., J. Bacteriol. 119:736–747 (1974); Yuan et al., J. Biol. Chem. 265:13528–13532(1990)). Briefly, the cells were grown in MOPS media in a 19-liter fermentor (Wheaton Science Products, Millville, N.J.) and were inoculated with 0.5 liters of overnight MOPS culture of H712 containing the IMPDH plasmid. The fermentation was kept at 37° C. and was maintained by aeration, stirring and glucose addition. The dissolved oxygen (DO) was maintained at greater than 40%. The cells were harvested at 8 hours when the DO dropped to below 20% at an OD600 of roughly 1.5.
The cells were concentrated to 0.5 L by tangential flow filtration (Millipore, Inc., Bedford, Mass.) and pelleted by centrifugation at 6,000 g. The pellet was re-suspended in a three fold volume of buffer A (50 mM Tris pH 8, 50 mM KCl, 10% gycerol, and 1 mM 2-mercaptoethanol) supplemented with protease inhibitors and 1 mM EDTA, and was then flash frozen in liquid nitrogen before storage at −85° C. This mixture was lysed by French Press and the lysate was clarified by centrifugation at 20,000 g. The supernatant was then run over a cibacron blue column on an AKTA FPLC (Amersham-Pharmacia). Protein was eluted from the column with 1 M KCl. This was followed by dialysis into buffer A and concentration to 15 mg/ml. The protein was then passed through a monoQ column (Amersham-Pharmacia) using a gradient from 50 to 500 mM KCl over 20 column volumes. The resulting protein was >90% pure and was dialyzed in buffer A and concentrated to 30 mg/ml for storage at −85° C.
The protein was crystallized at 20° C. by mixing 15 mg/ml protein in buffer A into 42% of saturated sodium malonate, 100 mM Tris pH 8.0, 4 mM PEG 400, and 1 mM 2-mercaptoethanol in 6 μl sitting drops in a 1:1 ration of well solution to protein. The protein was also co-crystallized with a ten-fold molar excess of RMP. For the efforts to co-crystallize both RMP and MOA with IMPDH, saturating levels of MOA were added to newly formed RMP bound crystals. These crystals were allowed to soak for several hours to several days before cryo-mounting.
Throughout this application various publications have been referenced within parentheses. The disclosures of these publications in their entireties are hereby incorporated by reference in this application in order to more fully describe the state of the art to which this invention pertains.
Although the invention has been described with reference to the disclosed embodiments, those skilled in the art will readily appreciate that the specific experiments detailed are only illustrative of the invention. It should be understood that various modifications can be made without departing from the spirit of the invention.







TABLE 1







Data collection and refinement statistics.











Structure
IMP
IMP + MPA
XMP + MPA
NAD+ + XMP














Wavelength (Å)
0.97
0.97
0.97
1.00


Resolution Range (Å)
 50–2.2
  50–1.95
 50–2.2
  20–2.15


Resolution of outer shell (Å)
 2.2–2.34
1.95–2.07
 2.2–2.34
2.15–2.28


R (Rfree) (%)
24.9 (27.1)
24.0 (26.8)
22.5 (25.6)
22.3 (24.6)


Unique reflections
32,418
45,540
32,987
33,857


Total observations
996,397
1,036,471
407,857
734,853


I/σ1 all/outer shell
21.7/2.13
25.88/1.82 
21.38/2.88 
19.03/2.22


Rsym all/outer shell (%)
 6.4/59.6
 5.7/66.8
 6.6/53.8
 8.0/57.8


Completeness all/outer shell (%)
99.9/99.8
99.0/95.7
99.5/98.7
98.4/95.9


Degrees collected
37.5
37.5
20
30


Amino acid residues in model
 2–101,
 2–106,
 2–101,
 2–101,



222–416,
222–416,
222–417,
222–317,



431–483
430–483
428–483
322–416,






428–483


Number of water molecules
159
202
183
172


Cell dimensions
154.4
153.5
155.1
153.8


a = b = c (Å)


Bond length dev. (Å)
0.006
0.006
0.005
0.007


Bond angle dev. (°)
1.2
1.2
1.1
1.3


Dihedral angle dev. (°)
22.9
22.2
22.5
23.0


Improper angle dev. (°)
0.71
0.70
0.67
0.80


Ramachandran core/allowed/
91.9/7.8/0.3
92.1/7.9/0.0
90.7/9.0/0.3
91.7/7.9/0.3


generously allowed (%)


Mosaicity (°)
0.60
0.65
0.40
0.70


















TABLE 2







HEADER
OXIDOREDUCTASE
08-AUG-02   1ME9









TITLE

INOSINE MONOPHOSPHATE DEHYDROGENASE (IMPDH) FROM









TITLE
 2
TRITRICHOMONAS FOETUS WITH IMP BOUND








COMPND
MOL_ID: 1;









COMPND
 2
MOLECULE: INOSINE-5′-MONOPHOSPHATE DEHYDROGENASE;


COMPND
 3
CHAIN: A;


COMPND
 4
SYNONYM: IMP DEHYDROGENASE, IMPDH;


COMPND
 5
EC: 1.1.1.205;


COMPND
 6
ENGINEERED: YES








SOURCE
MOL_ID: 1;









SOURCE
 2
ORGANISM_SCIENTIFIC: TRITRICHOMONAS FOETUS;


SOURCE
 3
GENE: IMPDH;


SOURCE
 4
EXPRESSION_SYSTEM: ESCHERICHIA COLI;


SOURCE
 5
EXPRESSION_SYSTEM_COMMON: BACTERIA;


SOURCE
 6
EXPRESSION_SYSTEM_STRAIN: H712;


SOURCE
 7
EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;


SOURCE
 8
EXPRESSION_SYSTEM_PLASMID: PBACE








KEYWDS
ALPHA BETA BARREL


EXPDTA
X-RAY DIFFRACTION


AUTHOR
G. L. PROSISE, H. LUECKE









JRNL
AUTH
G. L. PROSISE, H. LUECKE


JRNL
TITL
CRYSTAL STRUCTURE OF T. FOETUS INOSINE


JRNL
TITL 2
MONOPHOSPHATE DEHYDROGENASE IN COMPLEX WITH


JRNL
TITL 3
SUBSTRATE, COFACTOR, AND ANALOGS:STRUCTURAL BASIS


JRNL
TITL 4
FOR THE RANDOM-IN ORDERED-OUT KINETIC MECHANISM


JRNL
REF
TO BE PUBLISHED


JRNL
REFN









REMARK
 1



REMARK
 2


REMARK
 2
RESOLUTION. 2.20 ANGSTROMS.


REMARK
 3


REMARK
 3
REFINEMENT.










REMARK
 3
PROGRAM
: CNS 1.1


REMARK
 3
AUTHORS
: BRUNGER, ADAMS, CLORE, DELANO, GROS, GROSSE-


REMARK
 3

: KUNSTLEVE, JIANG, KUSZEWSKI, NILGES, PANNU,


REMARK
 3

: READ, RICE, SIMONSON, WARREN


REMARK
 3









REMARK
 3
REFINEMENT TARGET : ENGH & HUBER


REMARK
 3


REMARK
 3
DATA USED IN REFINEMENT.











REMARK
 3
RESOLUTION RANGE HIGH
(ANGSTROMS)
: 2.20


REMARK
 3
RESOLUTION RANGE LOW
(ANGSTROMS)
: 19.77


REMARK
 3
DATA CUTOFF
(SIGMA(F))
: 0.000











REMARK
 3
OUTLIER CUTOFF HIGH
(RMS(ABS(F)))
: NULL











REMARK
 3
COMPLETENESS (WORKING+TEST)
(%)
: 99.8


REMARK
 3
NUMBER OF REFLECTIONS

: 32418


REMARK
 3









REMARK
 3
FIT TO DATA USED IN REFINEMENT.










REMARK
 3
CROSS-VALIDATION METHOD
: THROUGHOUT


REMARK
 3
FREE R VALUE TEST SET SELECTION
: RANDOM











REMARK
 3
R VALUE
(WORKING SET)
: 0.248


REMARK
 3
FREE R VALUE

: 0.273











REMARK
 3
FREE R VALUE TEST SET SIZE
(%)
: 5.200










REMARK
 3
FREE R VALUE TEST SET COUNT
: 1691


REMARK
 3
ESTIMATED ERROR OF FREE R VALUE
: 0.007


REMARK
 3









REMARK
 3
FIT IN THE HIGHEST RESOLUTION BIN.










REMARK
 3
TOTAL NUMBER OF BINS USED
: 6











REMARK
 3
BIN RESOLUTION RANGE HIGH
(A)
: 2.20


REMARK
 3
BIN RESOLUTION RANGE LOW
(A)
: 2.34


REMARK
 3
BIN COMPLETENESS (WORKING+TEST)
(%)
: 99.80











REMARK
 3
REFLECTIONS IN BIN
(WORKING SET)
: 5035


REMARK
 3
BIN R VALUE
(WORKING SET)
: 0.2770


REMARK
 3
BIN FREE R VALUE

: 0.3040











REMARK
 3
BIN FREE R VALUE TEST SET SIZE
(%)
: 4.90










REMARK
 3
BIN FREE R VALUE TEST SET COUNT
: 262


REMARK
 3
ESTIMATED ERROR OF BIN FREE R VALUE
: 0.019


REMARK
 3









REMARK
 3
NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.










REMARK
 3
PROTEIN ATOMS
: 2685


REMARK
 3
NUCLEIC ACID ATOMS
: 0


REMARK
 3
HETEROGEN ATOMS
: 24


REMARK
 3
SOLVENT ATOMS
: 145


REMARK
 3









REMARK
 3
B VALUES.











REMARK
 3
FROM WILSON PLOT
(A**2)
: 28.10


REMARK
 3
MEAN B VALUE
(OVERALL, A**2)
: 40.20


REMARK
 3
OVERALL ANISOTROPIC B VALUE.










REMARK
 3
B11 (A**2)
: 0.00000


REMARK
 3
B22 (A**2)
: 0.00000


REMARK
 3
B33 (A**2)
: 0.00000


REMARK
 3
B12 (A**2)
: 0.00000


REMARK
 3
B13 (A**2)
: 0.00000


REMARK
 3
B23 (A**2)
: 0.00000


REMARK
 3









REMARK
 3
ESTIMATED COORDINATE ERROR.











REMARK
 3
ESD FROM LUZZATI PLOT
(A)
: 0.30


REMARK
 3
ESD FROM SIGMAA
(A)
: 0.22


REMARK
 3
LOW RESOLUTION CUTOFF
(A)
: 5.00


REMARK
 3









REMARK
 3
CROSS-VALIDATED ESTIMATED COORDINATE ERROR.











REMARK
 3
ESD FROM C-V LUZZATI PLOT
(A)
: 0.34


REMARK
 3
ESD FROM C-V SIGMAA
(A)
: 0.25


REMARK
 3









REMARK
 3
RMS DEVIATIONS FROM IDEAL VALUES.











REMARK
 3
BOND LENGTHS
(A)
: 0.006


REMARK
 3
BOND ANGLES
(DEGREES)
: 1.20


REMARK
 3
DIHEDRAL ANGLES
(DEGREES)
: 22.80


REMARK
 3
IMPROPER ANGLES
(DEGREES)
: 0.72


REMARK
 3









REMARK
 3
ISOTROPIC THERMAL MODEL : RESTRAINED


REMARK
 3












REMARK
 3
ISOTROPIC THERMAL FACTOR RESTRAINTS.
RMS
SIGMA













REMARK
 3
MAIN-CHAIN BOND
(A**2)
: 1.270
; 1.500


REMARK
 3
MAIN-CHAIN ANGLE
(A**2)
: 2.150
; 2.000


REMARK
 3
SIDE-CHAIN BOND
(A**2)
: 1.930
; 2.000


REMARK
 3
SIDE-CHAIN ANGLE
(A**2)
: 2.840
; 2.500


REMARK
 3









REMARK
 3
BULK SOLVENT MODELING.










REMARK
 3
METHOD USED
: FLAT MODEL


REMARK
 3
KSOL
: 0.36


REMARK
 3
BSOL
: 40.24


REMARK
 3









REMARK
 3
NCS MODEL : NULL


REMARK
 3











REMARK
 3
NCS RESTRAINTS.
RMS
 SIGMA/WEIGHT












REMARK
 3
GROUP 1 POSITIONAL
(A)
: NULL
; NULL


REMARK
 3
GROUP 1 B-FACTOR
(A**2)
: NULL
; NULL


REMARK
 3










REMARK
 3
PARAMETER FILE 1
: PROTEIN_REP.PARAM


REMARK
 3
PARAMETER FILE 2
: PARAM.GNSOL


REMARK
 3
PARAMETER FILE 3
: CIS_PEPTIDE.PARAM


REMARK
 3
PARAMETER FILE 4
: IMP.PAR


REMARK
 3
PARAMETER FILE 5
: ION.PARAM


REMARK
 3
PARAMETER FILE 6
: NULL


REMARK
 3
TOPOLOGY FILE 1
: PROTEIN.TOP


REMARK
 3
TOPOLOGY FILE 2
: IMP.TOP


REMARK
 3
TOPOLOGY FILE 3
: MPA.TOP


REMARK
 3
TOPOLOGY FILE 4
: ION.TOP


REMARK
 3
TOPOLOGY FILE 5
: TOPH.GNSOL


REMARK
 3
TOPOLOGY FILE 6
: NULL


REMARK
 3









REMARK
 3
OTHER REFINEMENT REMARKS: NULL


REMARK
 4









REMARK
 4
1ME9 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998


REMARK
100


REMARK
100
THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-AUG-2002.


REMARK
100
THE RCSB ID CODE IS RCSB016851.


REMARK
200


REMARK
200
EXPERIMENTAL DETAILS










REMARK
200
EXPERIMENT TYPE
: X-RAY DIFFRACTION


REMARK
200
DATE OF DATA COLLECTION
: 11-APR-2001











REMARK
200
TEMPERATURE
(KELVIN)
: 100.0










REMARK
200
PH
: 7.50


REMARK
200
NUMBER OF CRYSTALS USED
: 1


REMARK
200











REMARK
200
SYNCHROTRON
(Y/N)
: Y










REMARK
200
RADIATION SOURCE
: SSRL


REMARK
200
BEAMLINE
: 9-1


REMARK
200
X-RAY GENERATOR MODEL
: NULL











REMARK
200
MONOCHROMATIC OR LAUE
(M/L)
: M


REMARK
200
WAVELENGTH OR RANGE
(A)
: 0.97










REMARK
200
MONOCHROMATOR
: NULL


REMARK
200
OPTICS
: NULL


REMARK
200


REMARK
200
DETECTOR TYPE
: IMAGE PLATE


REMARK
200
DETECTOR MANUFACTURER
: MARRESEARCH


REMARK
200
INTENSITY-INTEGRATION SOFTWARE
: DENZO


REMARK
200
DATA SCALING SOFTWARE
: SCALEPACK


REMARK
200


REMARK
200
NUMBER OF UNIQUE REFLECTIONS
: 32513











REMARK
200
RESOLUTION RANGE HIGH
(A)
: 2.200


REMARK
200
RESOLUTION RANGE LOW
(A)
: 20.000











REMARK
200
REJECTION CRITERIA
(SIGMA(I))
: 0.000









REMARK
200



REMARK
200
OVERALL.











REMARK
200
COMPLETENESS FOR RANGE
(%)
: 99.9


REMARK
200
DATA REDUNDANCY

: 6.700


REMARK
200
R MERGE
(I)
: 0.06400


REMARK
200
R SYM
(I)
: NULL










REMARK
200
<I/SIGMA(I)> FOR THE DATA SET
: 21.7000









REMARK
200



REMARK
200
IN THE HIGHEST RESOLUTION SHELL.











REMARK
200
HIGHEST RESOLUTION SHELL, RANGE HIGH
(A)
: 2.20


REMARK
200
HIGHEST RESOLUTION SHELL, RANGE LOW
(A)
: 2.24











REMARK
200
COMPLETENESS FOR SHELL
(%)
: 99.8










REMARK
200
DATA REDUNDANCY IN SHELL
: NULL











REMARK
200
R MERGE FOR SHELL
(I)
: 0.59600


REMARK
200
R SYM FOR SHELL
(I)
: NULL










REMARK
200
<I/SIGMA(I)> FOR SHELL
: 2.130


REMARK
200


REMARK
200
DIFFRACTION PROTOCOL: SINGLE WAVELENGTH


REMARK
200
METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS


REMARK
200
SOFTWARE USED: CNS


REMARK
200
STARTING MODEL: PDB ENTRY 1AK5


REMARK
200


REMARK
200
REMARK: NULL


REMARK
280


REMARK
280
CRYSTAL


REMARK
280
SOLVENT CONTENT, VS (%): NULL


REMARK
280
MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL


REMARK
280


REMARK
280
CRYSTALLIZATION CONDITIONS: SODIUM MALONATE, TRIS, 2-









REMARK
280
MERCAPTOETHANOL, EDTA, GLYCEROL









REMARK
290



REMARK
290
CRYSTALLOGRAPHIC SYMMETRY


REMARK
290
SYMMETRY OPERATORS FOR SPACE GROUP: P 4 3 2


REMARK
290










REMARK
290
SYMOP
SYMMETRY


REMARK
290
NNNMMM
OPERATOR


REMARK
290
 1555
X, Y, Z


REMARK
290
 2555
−X, −Y, Z


REMARK
290
 3555
−X, Y, −Z


REMARK
290
 4555
X, −Y, −Z


REMARK
290
 5555
Z, X, Y


REMARK
290
 6555
Z, −X, −Y


REMARK
290
 7555
−Z, −X, Y


REMARK
290
 8555
−Z, X, −Y


REMARK
290
 9555
Y, Z, X


REMARK
290
10555
−Y, Z, −X


REMARK
290
11555
Y, −Z, −X


REMARK
290
12555
−Y, −Z, X


REMARK
290
13555
Y, X, −Z


REMARK
290
14555
−Y, −X, −Z


REMARK
290
15555
Y, −X, Z


REMARK
290
16555
−Y, X, Z


REMARK
290
17555
X, Z, −Y


REMARK
290
18555
−X, Z, Y


REMARK
290
19555
−X, −Z, −Y


REMARK
290
20555
X, −Z, Y


REMARK
290
21555
Z, Y, −X


REMARK
290
22555
Z, −Y, X


REMARK
290
23555
−Z, Y, X


REMARK
290
24555
−Z, −Y, −X


REMARK
290










REMARK
290
WHERE
NNN  −> OPERATOR NUMBER


REMARK
290

MMM −> TRANSLATION VECTOR









REMARK
290



REMARK
290
CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS


REMARK
290
THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM


REMARK
290
RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY


REMARK
290
RELATED MOLECULES.















REMARK
290
SMTRY1
1
1.000000
0.000000
0.000000
0.00000



REMARK
290
SMTRY2
1
0.000000
1.000000
0.000000
0.00000


REMARK
290
SMTRY3
1
0.000000
0.000000
1.000000
0.00000


REMARK
290
SMTRY1
2
−1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY2
2
0.000000
−1.000000
0.000000
0.00000


REMARK
290
SMTRY3
2
0.000000
0.000000
1.000000
0.00000


REMARK
290
SMTRY1
3
−1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY2
3
0.000000
1.000000
0.000000
0.00000


REMARK
290
SMTRY3
3
0.000000
0.000000
−1.000000
0.00000


REMARK
290
SMTRY1
4
1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY2
4
0.000000
−1.000000
0.000000
0.00000


REMARK
290
SMTRY3
4
0.000000
0.000000
−1.000000
0.00000


REMARK
290
SMTRY1
5
0.000000
0.000000
1.000000
0.00000


REMARK
290
SMTRY2
5
1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY3
5
0.000000
1.000000
0.000000
0.00000


REMARK
290
SMTRY1
6
0.000000
0.000000
1.000000
0.00000


REMARK
290
SMTRY2
6
−1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY3
6
0.000000
−1.000000
0.000000
0.00000


REMARK
290
SMTRY1
7
0.000000
0.000000
−1.000000
0.00000


REMARK
290
SMTRY2
7
−1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY3
7
0.000000
1.000000
0.000000
0.00000


REMARK
290
SMTRY1
8
0.000000
0.000000
−1.000000
0.00000


REMARK
290
SMTRY2
8
1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY3
8
0.000000
−1.000000
0.000000
0.00000


REMARK
290
SMTRY1
9
0.000000
1.000000
0.000000
0.00000


REMARK
290
SMTRY2
9
0.000000
0.000000
1.000000
0.00000


REMARK
290
SMTRY3
9
1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY1
10
0.000000
−1.000000
0.000000
0.00000


REMARK
290
SMTRY2
10
0.000000
0.000000
1.000000
0.00000


REMARK
290
SMTRY3
10
−1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY1
11
0.000000
1.000000
0.000000
0.00000


REMARK
290
SMTRY2
11
0.000000
0.000000
−1.000000
0.00000


REMARK
290
SMTRY3
11
−1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY1
12
0.000000
−1.000000
0.000000
0.00000


REMARK
290
SMTRY2
12
0.000000
0.000000
−1.000000
0.00000


REMARK
290
SMTRY3
12
1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY1
13
0.000000
1.000000
0.000000
0.00000


REMARK
290
SMTRY2
13
1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY3
13
0.000000
0.000000
−1.000000
0.00000


REMARK
290
SMTRY1
14
0.000000
−1.000000
0.000000
0.00000


REMARK
290
SMTRY2
14
−1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY3
14
0.000000
0.000000
−1.000000
0.00000


REMARK
290
SMTRY1
15
0.000000
1.000000
0.000000
0.00000


REMARK
290
SMTRY2
15
−1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY3
15
0.000000
0.000000
1.000000
0.00000


REMARK
290
SMTRY1
16
0.000000
−1.000000
0.000000
0.00000


REMARK
290
SMTRY2
16
1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY3
16
0.000000
0.000000
1.000000
0.00000


REMARK
290
SMTRY1
17
1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY2
17
0.000000
0.000000
1.000000
0.00000


REMARK
290
SMTRY3
17
0.000000
−1.000000
0.000000
0.00000


REMARK
290
SMTRY1
18
−1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY2
18
0.000000
0.000000
1.000000
0.00000


REMARK
290
SMTRY3
18
0.000000
1.000000
0.000000
0.00000


REMARK
290
SMTRY1
19
−1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY2
19
0.000000
0.000000
−1.000000
0.00000


REMARK
290
SMTRY3
19
0.000000
−1.000000
0.000000
0.00000


REMARK
290
SMTRY1
20
1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY2
20
0.000000
0.000000
−1.000000
0.00000


REMARK
290
SMTRY3
20
0.000000
1.000000
0.000000
0.00000


REMARK
290
SMTRY1
21
0.000000
0.000000
1.000000
0.00000


REMARK
290
SMTRY2
21
0.000000
1.000000
0.000000
0.00000


REMARK
290
SMTRY3
21
−1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY1
22
0.000000
0.000000
1.000000
0.00000


REMARK
290
SMTRY2
22
0.000000
−1.000000
0.000000
0.00000


REMARK
290
SMTRY3
22
1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY1
23
0.000000
0.000000
−1.000000
0.00000


REMARK
290
SMTRY2
23
0.000000
1.000000
0.000000
0.00000


REMARK
290
SMTRY3
23
1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY1
24
0.000000
0.000000
−1.000000
0.00000


REMARK
290
SMTRY2
24
0.000000
−1.000000
0.000000
0.00000


REMARK
290
SMTRY3
24
−1.000000
0.000000
0.000000
0.00000


REMARK
290









REMARK
290
REMARK: NULL


REMARK
300


REMARK
300
BIOMOLECULE: 1


REMARK
300
THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT


REMARK
300
WHICH CONSISTS OF 1 CHAIN(S). SEE REMARK 350 FOR


REMARK
300
INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).


REMARK
350


REMARK
350
GENERATING THE BIOMOLECULE


REMARK
350
COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN


REMARK
350
BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE


REMARK
350
MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS


REMARK
350
GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND


REMARK
350
CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.


REMARK
350


REMARK
350
BIOMOLECULE: 1


REMARK
350
APPLY THE FOLLOWING TO CHAINS: A















REMARK
350
BIOMT1
1
1.000000
0.000000
0.000000
0.00000



REMARK
350
BIOMT2
1
0.000000
1.000000
0.000000
0.00000


REMARK
350
BIOMT3
1
0.000000
0.000000
1.000000
0.00000


REMARK
350
BIOMT1
2
−1.000000
0.000000
0.000000
154.41200


REMARK
350
BIOMT2
2
0.000000
−1.000000
0.000000
154.41200


REMARK
350
BIOMT3
2
0.000000
0.000000
1.000000
0.00000


REMARK
350
BIOMT1
3
0.000000
1.000000
0.000000
0.00000


REMARK
350
BIOMT2
3
−1.000000
0.000000
0.000000
154.41200


REMARK
350
BIOMT3
3
0.000000
0.000000
1.000000
0.00000


REMARK
350
BIOMT1
4
0.000000
−1.000000
0.000000
154.41200


REMARK
350
BIOMT2
4
1.000000
0.000000
0.000000
0.00000


REMARK
350
BIOMT3
4
0.000000
0.000000
1.000000
0.00000


REMARK
465









REMARK
465
MISSING RESIDUES


REMARK
465
THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE


REMARK
465
EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN


REMARK
465
IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)


REMARK
465












REMARK
465
M
RES C
SSSEQI



REMARK
465

MET A
1


REMARK
465

GLY A
102


REMARK
465

PHE A
103


REMARK
465

VAL A
104


REMARK
465

VAL A
105


REMARK
465

SER A
106


REMARK
465

ASP A
107


REMARK
465

SER A
108


REMARK
465

ASN A
109


REMARK
465

VAL A
110


REMARK
465

LYS A
111


REMARK
465

PRO A
112


REMARK
465

ASP A
113


REMARK
465

GLN A
114


REMARK
465

THR A
115


REMARK
465

PHE A
116


REMARK
465

ALA A
117


REMARK
465

ASP A
118


REMARK
465

VAL A
119


REMARK
465

LEU A
120


REMARK
465

ALA A
121


REMARK
465

ILE A
122


REMARK
465

SER A
123


REMARK
465

GLN A
124


REMARK
465

ARG A
125


REMARK
465

THR A
126


REMARK
465

THR A
127


REMARK
465

HIS A
128


REMARK
465

ASN A
129


REMARK
465

THR A
130


REMARK
465

VAL A
131


REMARK
465

ALA A
132


REMARK
465

VAL A
133


REMARK
465

THR A
134


REMARK
465

ASP A
135


REMARK
465

ASP A
136


REMARK
465

GLY A
137


REMARK
465

THR A
138


REMARK
465

PRO A
139


REMARK
465

HIS A
140


REMARK
465

GLY A
141


REMARK
465

VAL A
142


REMARK
465

LEU A
143


REMARK
465

LEU A
144


REMARK
465

GLY A
145


REMARK
465

LEU A
146


REMARK
465

VAL A
147


REMARK
465

THR A
148


REMARK
465

GLN A
149


REMARK
465

ARG A
150


REMARK
465

ASP A
151


REMARK
465

TYR A
152


REMARK
465

PRO A
153


REMARK
465

ILE A
154


REMARK
465

ASP A
155


REMARK
465

LEU A
156


REMARK
465

THR A
157


REMARK
465

GLN A
158


REMARK
465

THR A
159


REMARK
465

GLU A
160


REMARK
465

THR A
161


REMARK
465

LYS A
162


REMARK
465

VAL A
163


REMARK
465

SER A
164


REMARK
465

ASP A
165


REMARK
465

MET A
166


REMARK
465

MET A
167


REMARK
465

THR A
168


REMARK
465

PRO A
169


REMARK
465

PHE A
170


REMARK
465

SER A
171


REMARK
465

LYS A
172


REMARK
465

LEU A
173


REMARK
465

VAL A
174


REMARK
465

THR A
175


REMARK
465

ALA A
176


REMARK
465

HIS A
177


REMARK
465

GLN A
178


REMARK
465

ASP A
179


REMARK
465

THR A
180


REMARK
465

LYS A
181


REMARK
465

LEU A
182


REMARK
465

SER A
183


REMARK
465

GLU A
184


REMARK
465

ALA A
185


REMARK
465

ASN A
186


REMARK
465

LYS A
187


REMARK
465

ILE A
188


REMARK
465

ILE A
189


REMARK
465

TRP A
190


REMARK
465

GLU A
191


REMARK
465

LYS A
192


REMARK
465

LYS A
193


REMARK
465

LEU A
194


REMARK
465

ASN A
195


REMARK
465

ALA A
196


REMARK
465

LEU A
197


REMARK
465

PRO A
198


REMARK
465

ILE A
199


REMARK
465

ILE A
200


REMARK
465

ASP A
201


REMARK
465

ASP A
202


REMARK
465

ASP A
203


REMARK
465

GLN A
204


REMARK
465

HIS A
205


REMARK
465

LEU A
206


REMARK
465

ARG A
207


REMARK
465

TYR A
208


REMARK
465

ILE A
209


REMARK
465

VAL A
210


REMARK
465

PHE A
211


REMARK
465

ARG A
212


REMARK
465

LYS A
213


REMARK
465

ASP A
214


REMARK
465

TYR A
215


REMARK
465

ASP A
216


REMARK
465

ARG A
217


REMARK
465

SER A
218


REMARK
465

GLN A
219


REMARK
465

VAL A
220


REMARK
465

CYS A
221


REMARK
465

GLN A
417


REMARK
465

ARG A
418


REMARK
465

TYR A
419


REMARK
465

ASP A
420


REMARK
465

LEU A
421


REMARK
465

GLY A
422


REMARK
465

GLY A
423


REMARK
465

LYS A
424


REMARK
465

GLN A
425


REMARK
465

LYS A
426


REMARK
465

LEU A
427


REMARK
465

SER A
428


REMARK
465

VAL A
484


REMARK
465

GLU A
485


REMARK
465

GLY A
486


REMARK
465

GLY A
487


REMARK
465

ALA A
488


REMARK
465

HIS A
489


REMARK
465

ASP A
490


REMARK
465

VAL A
491


REMARK
465

ILE A
492


REMARK
465

VAL A
493


REMARK
465

LYS A
494


REMARK
465

ASP A
495


REMARK
465

ARG A
496


REMARK
465

ILE A
497


REMARK
465

ASN A
498


REMARK
465

ASP A
499


REMARK
465

TYR A
500


REMARK
465

HIS A
501


REMARK
465

PRO A
502


REMARK
465

LYS A
503


REMARK
500









REMARK
500
GEOMETRY AND STEREOCHEMISTRY


REMARK
500
SUBTOPIC: CLOSE CONTACTS


REMARK
500


REMARK
500
THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC


REMARK
500
SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15


REMARK
500
ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A


REMARK
500
SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375


REMARK
500
INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE


REMARK
500
LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.


REMARK
500


REMARK
500
DISTANCE CUTOFF:


REMARK
500
2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS


REMARK
500
1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS


REMARK
500

















REMARK
500
ATM1
RES C
SSEQI
ATM2
RES C
SSEQI
SSYMOP
DISTANCE



REMARK
500
O
GLY A
20
K
K   A
900
16655
2.18


REMARK
500









REMARK
500
GEOMETRY AND STEREOCHEMISTRY


REMARK
500
SUBTOPIC: COVALENT BOND ANGLES


REMARK
500


REMARK
500
THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES


REMARK
500
HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE


REMARK
500
THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN


REMARK
500
IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).


REMARK
500


REMARK
500
STANDARD TABLE:


REMARK
500
FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)


REMARK
500


REMARK
500
EXPECTED VALUES: ENGH AND HUBER, 1991


REMARK
500

















REMARK
500
M
RES C
SSEQI
ATM1

ATM2

ATM3



REMARK
500

ILE A
 27
N
−
CA
−
C
ANGL. DEV. = −8.1 DEGREES


REMARK
500

SER A
 63
N
−
CA
−
C
ANGL. DEV. =   7.9 DEGREES


REMARK
500

GLY A
305
N
−
CA
−
C
ANGL. DEV. =   7.8 DEGREES


REMARK
500

GLY A
312
N
−
CA
−
C
ANGL. DEV. =   7.2 DEGREES


REMARK
500

SER A
357
N
−
CA
−
C
ANGL. DEV. = −7.4 DEGREES


REMARK
500

LYS A
472
N
−
CA
−
C
ANGL. DEV. =   8.0 DEGREES


REMARK
500

LYS A
474
N
−
CA
−
C
ANGL. DEV. = −9.2 DEGREES


REMARK
500

LEU A
477
N
−
CA
−
C
ANGL. DEV. = −7.8 DEGREES


REMARK
900









REMARK
900
RELATED ENTRIES










REMARK
900
RELATED ID: 1AK5
RELATED DB: PDB









REMARK
900
INOSINE MONOPHOSPHATE DEHYDROGENASE (IMPDH) FROM


REMARK
900
TRITRICHOMONAS FOETUS










REMARK
900
RELATED ID: 1ME7
RELATED DB: PDB









REMARK
900
1ME7 CONTAINS THE SAME PROTEIN WITH RMP AND MPA BOUND










REMARK
900
RELATED ID: 1ME8
RELATED DB: PDB









REMARK
900
1ME8 CONTAINS THE SAME PROTEIN WITH RMP BOUND










REMARK
900
RELATED ID: 1MEH
RELATED DB: PDB









REMARK
900
1MEH CONTAINS THE SAME PROTEIN WITH IMP AND MPA BOUND










REMARK
900
RELATED ID: 1MEI
RELATED DB: PDB









REMARK
900
1MEI CONTAINS THE SAME PROTEIN WITH XMP AND MYCOPHENOLIC


REMARK
900
ACID BOUND










REMARK
900
RELATED ID: 1MEW
RELATED DB: PDB









REMARK
900
1MEW CONTAINS THE SAME PROTEIN WITH XMP AND NAD BOUND








DBREF
1ME9 A 1 503 SWS P50097 IMDH_TRIFO  1 503


SEQADV
1ME9 CSO A 319 SWS P50097 CYS 319 MODIFIED RESIDUE























SEQRES
1
A
503
MET
ALA
LYS
TYR
TYR
ASN
GLU
PRO
CYS
HIS
THR
PHE
ASN


SEQRES
2
A
503
GLU
TYR
LEU
LEU
ILE
PRO
GLY
LEU
SER
THR
VAL
ASP
CYS


SEQRES
3
A
503
ILE
PRO
SER
ASN
VAL
ASN
LEU
SER
THR
PRO
LEU
VAL
LYS


SEQRES
4
A
503
PHE
GLN
LYS
GLY
GLN
GLN
SER
GLU
ILE
ASN
LEU
LYS
ILE


SEQRES
5
A
503
PRO
LEU
VAL
SER
ALA
ILE
MET
GLN
SER
VAL
SER
GLY
GLU


SEQRES
6
A
503
LYS
MET
ALA
ILE
ALA
LEU
ALA
ARG
GLU
GLY
GLY
ILE
SER


SEQRES
7
A
503
PHE
ILE
PHE
GLY
SER
GLN
SER
ILE
GLU
SER
GLN
ALA
ALA


SEQRES
8
A
503
MET
VAL
HIS
ALA
VAL
LYS
ASN
PHE
LYS
ALA
GLY
PHE
VAL


SEQRES
9
A
503
VAL
SER
ASP
SER
ASN
VAL
LYS
PRO
ASP
GLN
THR
PHE
ALA


SEQRES
10
A
503
ASP
VAL
LEU
ALA
ILE
SER
GLN
ARG
THR
THR
HIS
ASN
THR


SEQRES
11
A
503
VAL
ALA
VAL
THR
ASP
ASP
GLY
THR
PRO
HIS
GLY
VAL
LEU


SEQRES
12
A
503
LEU
GLY
LEU
VAL
THR
GLN
ARG
ASP
TYR
PRO
ILE
ASP
LEU


SEQRES
13
A
503
THR
GLN
THR
GLU
THR
LYS
VAL
SER
ASP
MET
MET
THR
PRO


SEQRES
14
A
503
PHE
SER
LYS
LEU
VAL
THR
ALA
HIS
GLN
ASP
THR
LYS
LEU


SEQRES
15
A
503
SER
GLU
ALA
ASN
LYS
ILE
ILE
TRP
GLU
LYS
LYS
LEU
ASN


SEQRES
16
A
503
ALA
LEU
PRO
ILE
ILE
ASP
ASP
ASP
GLN
HIS
LEU
ARG
TYR


SEQRES
17
A
503
ILE
VAL
PHE
ARG
LYS
ASP
TYR
ASP
ARG
SER
GLN
VAL
CYS


SEQRES
18
A
503
HIS
ASN
GLU
LEU
VAL
ASP
SER
GLN
LYS
ARG
TYR
LEU
VAL


SEQRES
19
A
503
GLY
ALA
GLY
ILE
ASN
THR
ARG
ASP
PHE
ARG
GLU
ARG
VAL


SEQRES
20
A
503
PRO
ALA
LEU
VAL
GLU
ALA
GLY
ALA
ASP
VAL
LEU
CYS
ILE


SEQRES
21
A
503
ASP
SER
SER
ASP
GLY
PHE
SER
GLU
TRP
GLN
LYS
ILE
THR


SEQRES
22
A
503
ILE
GLY
TRP
ILE
ARG
GLU
LYS
TYR
GLY
ASP
LYS
VAL
LYS


SEQRES
23
A
503
VAL
GLY
ALA
GLY
ASN
ILE
VAL
ASP
GLY
GLU
GLY
PHE
ARG


SEQRES
24
A
503
TYR
LEU
ALA
ASP
ALA
GLY
ALA
ASP
PHE
ILE
LYS
ILE
GLY


SEQRES
25
A
503
ILE
GLY
GLY
GLY
SER
ILE
CSO
ILE
THR
ARG
GLU
GLN
LYS


SEQRES
26
A
503
GLY
ILE
GLY
ARG
GLY
GLN
ALA
THR
ALA
VAL
ILE
ASP
VAL


SEQRES
27
A
503
VAL
ALA
GLU
ARG
ASN
LYS
TYR
PHE
GLU
GLU
THR
GLY
ILE


SEQRES
28
A
503
TYR
ILE
PRO
VAL
CYS
SER
ASP
GLY
GLY
ILE
VAL
TYR
ASP


SEQRES
29
A
503
TYR
HIS
MET
THR
LEU
ALA
LEU
ALA
MET
GLY
ALA
ASP
PHE


SEQRES
30
A
503
ILE
MET
LEU
GLY
ARG
TYR
PHE
ALA
ARG
PHE
GLU
GLU
SER


SEQRES
31
A
503
PRO
THR
ARG
LYS
VAL
THR
ILE
ASN
GLY
SER
VAL
MET
LYS


SEQRES
32
A
503
GLU
TYR
TRP
GLY
GLU
GLY
SER
SER
ARG
ALA
ARG
ASN
TRP


SEQRES
33
A
503
GLN
ARG
TYR
ASP
LEU
GLY
GLY
LYS
GLN
LYS
LEU
SER
PHE


SEQRES
34
A
503
GLU
GLU
GLY
VAL
ASP
SER
TYR
VAL
PRO
TYR
ALA
GLY
LYS


SEQRES
35
A
503
LEU
LYS
ASP
ASN
VAL
GLU
ALA
SER
LEU
ASN
LYS
VAL
LYS


SEQRES
36
A
503
SER
THR
MET
CYS
ASN
CYS
GLY
ALA
LEU
THR
ILE
PRO
GLN


SEQRES
37
A
503
LEU
GLN
SER
LYS
ALA
LYS
ILE
THR
LEU
VAL
SER
SER
VAL


SEQRES
38
A
503
SER
ILE
VAL
GLU
GLY
GLY
ALA
HIS
ASP
VAL
ILE
VAL
LYS


SEQRES
39
A
503
ASP
ARG
ILE
ASN
ASP
TYR
HIS
PRO
LYS








MODRES
1ME9 CSO A 319 CYS S-HYDROXYCYSTEINE












HET
CSO
A
319
7



HET
K
A
900
1


HET
IMP

602
23









HETNAM
CSO
S-HYDROXYCYSTEINE


HETNAM
K
POTASSIUM ION


HETNAM
IMP
INOSINIC ACID










FORMUL
1
CSO
 C3 H7 N1 O3 S1


FORMUL
2
K
 K1 1+


FORMUL
3
IMP
 C10 H13 N4 O8 P1


FORMUL
4
HOH
*145(H2 O1)















HELIX
1
1
THR A
11
ASN A
13
5
3


HELIX
2
2
ILE A
27
VAL A
31
5
5


HELIX
3
3
GLY A
64
GLU A
74
1
11


HELIX
4
4
SER A
85
ASN A
98
1
14


HELIX
5
5
ASP A
242
GLY A
254
1
13


HELIX
6
6
SER A
267
GLY A
282
1
16


HELIX
7
7
ASP A
283
VAL A
285
5
3


HELIX
8
8
ASP A
294
ALA A
304
1
11


HELIX
9
9
GLY A
330
GLY A
350
1
21


HELIX
10
10
TYR A
363
MET A
373
1
11


HELIX
11
11
GLY A
381
ARG A
386
1
6


HELIX
12
12
SER A
410
ASN A
415
1
6


HELIX
13
13
LYS A
442
CYS A
461
1
20


HELIX
14
14
THR A
465
ALA A
473
1
9





















SHEET
1
A 2
TYR A
15
LEU A
17
0









SHEET
2
A 2
ILE A
475
LEU A
477
−1
O
THR A
476
N
LEU A
16


SHEET
1
B 2
THR A
35
PRO A
36
0


SHEET
2
B 2
ASN A
49
LEU A
50
−1
O
LEU A
50
N
THR A
35


SHEET
1
C 2
PHE A
40
GLN A
41
0


SHEET
2
C 2
ILE A
351
TYR A
352
−1
O
TYR A
352
N
PHE A
40


SHEET
1
D 9
LEU A
54
SER A
56
0


SHEET
2
D 9
ILE A
77
ILE A
80
1
O
ILE A
77
N
SER A
56


SHEET
3
D 9
GLY A
235
ILE A
238
1
O
GLY A
237
N
ILE A
80


SHEET
4
D 9
VAL A
257
ILE A
260
1
O
CYS A
259
N
ILE A
238


SHEET
5
D 9
VAL A
287
ILE A
292
1
O
GLY A
288
N
LEU A
258


SHEET
6
D 9
PHE A
308
ILE A
311
1
O
LYS A
310
N
ALA A
289


SHEET
7
D 9
VAL A
355
ASP A
358
1
O
CYS A
356
N
ILE A
311


SHEET
8
D 9
PHE A
377
LEU A
380
1
O
MET A
379
N
SER A
357


SHEET
9
D 9
LEU A
54
SER A
56
1
N
VAL A
55
O
ILE A
378


SHEET
1
E 3
LYS A
394
ILE A
397
0


SHEET
2
E 3
SER A
400
TRP A
406
−1
O
SER A
400
N
ILE A
397


SHEET
3
E 3
ASP A
434
PRO A
438
1
O
SER A
435
N
TYR A
405












SSBOND
1
CYS A
26
CYS A
459


CISPEP
1
GLY A
290
ASN A
291   0   0.99








CRYST1
154.412 154.412 154.412 90.00 90.00 90.00 P 4 3 2  24











ORIGX1
1.000000
0.000000
0.000000
0.00000


ORIGX2
0.000000
1.000000
0.000000
0.00000


ORIGX3
0.000000
0.000000
1.000000
0.00000


SCALE1
0.006476
0.000000
0.000000
0.00000


SCALE2
0.000000
0.006476
0.000000
0.00000


SCALE3
0.000000
0.000000
0.006476
0.00000

















ATOM
1
N
ALA A
2
55.031
74.792
36.719
1.00
34.77
N


ATOM
2
CA
ALA A
2
55.778
73.707
36.025
1.00
35.14
C


ATOM
3
C
ALA A
2
57.099
73.393
36.732
1.00
35.76
C


ATOM
4
O
ALA A
2
57.541
74.137
37.609
1.00
33.95
O


ATOM
5
CB
ALA A
2
56.041
74.107
34.583
1.00
34.68
C


ATOM
6
N
LYS A
3
57.724
72.288
36.340
1.00
35.35
N


ATOM
7
CA
LYS A
3
58.992
71.873
36.927
1.00
37.15
C


ATOM
8
C
LYS A
3
60.102
72.070
35.899
1.00
36.78
C


ATOM
9
O
LYS A
3
59.954
71.708
34.735
1.00
38.00
O


ATOM
10
CB
LYS A
3
58.899
70.403
37.363
1.00
39.80
C


ATOM
11
CG
LYS A
3
60.157
69.806
37.997
1.00
44.47
C


ATOM
12
CD
LYS A
3
61.036
69.120
36.954
1.00
48.61
C


ATOM
13
CE
LYS A
3
61.897
68.023
37.579
1.00
49.58
C


ATOM
14
NZ
LYS A
3
62.832
68.555
38.611
1.00
52.93
N


ATOM
15
N
TYR A
4
61.206
72.662
36.339
1.00
36.47
N


ATOM
16
CA
TYR A
4
62.351
72.934
35.479
1.00
36.96
C


ATOM
17
C
TYR A
4
63.577
72.172
35.977
1.00
38.55
C


ATOM
18
O
TYR A
4
63.591
71.670
37.096
1.00
37.91
O


ATOM
19
CB
TYR A
4
62.635
74.442
35.472
1.00
35.25
C


ATOM
20
CG
TYR A
4
61.519
75.245
34.848
1.00
34.15
C


ATOM
21
CD1
TYR A
4
61.394
75.337
33.464
1.00
32.56
C


ATOM
22
CD2
TYR A
4
60.554
75.866
35.637
1.00
34.18
C


ATOM
23
CE1
TYR A
4
60.330
76.029
32.879
1.00
33.21
C


ATOM
24
CE2
TYR A
4
59.484
76.561
35.061
1.00
33.54
C


ATOM
25
CZ
TYR A
4
59.380
76.637
33.684
1.00
32.10
C


ATOM
26
OH
TYR A
4
58.328
77.310
33.111
1.00
30.26
O


ATOM
27
N
TYR A
5
64.608
72.091
35.144
1.00
40.78
N


ATOM
28
CA
TYR A
5
65.823
71.383
35.520
1.00
42.88
C


ATOM
29
C
TYR A
5
67.023
72.320
35.609
1.00
44.40
C


ATOM
30
O
TYR A
5
67.062
73.368
34.957
1.00
44.26
O


ATOM
31
CB
TYR A
5
66.104
70.251
34.527
1.00
42.67
C


ATOM
32
CG
TYR A
5
64.970
69.255
34.423
1.00
42.51
C


ATOM
33
CD1
TYR A
5
63.796
69.579
33.745
1.00
43.00
C


ATOM
34
CD2
TYR A
5
65.058
67.997
35.030
1.00
43.01
C


ATOM
35
CE1
TYR A
5
62.735
68.682
33.670
1.00
43.13
C


ATOM
36
CE2
TYR A
5
64.005
67.090
34.963
1.00
42.79
C


ATOM
37
CZ
TYR A
5
62.845
67.440
34.281
1.00
43.79
C


ATOM
38
OH
TYR A
5
61.794
66.556
34.202
1.00
42.47
O


ATOM
39
N
ASN A
6
67.996
71.934
36.429
1.00
45.72
N


ATOM
40
CA
ASN A
6
69.201
72.729
36.636
1.00
45.99
C


ATOM
41
C
ASN A
6
70.163
72.704
35.453
1.00
45.21
C


ATOM
42
O
ASN A
6
70.883
73.673
35.218
1.00
46.34
O


ATOM
43
CB
ASN A
6
69.926
72.243
37.893
1.00
48.66
C


ATOM
44
CG
ASN A
6
69.147
72.530
39.163
1.00
51.75
C


ATOM
45
OD1
ASN A
6
69.264
71.805
40.153
1.00
52.73
O


ATOM
46
ND2
ASN A
6
68.356
73.601
39.147
1.00
53.06
N


ATOM
47
N
GLU A
7
70.177
71.605
34.707
1.00
43.47
N


ATOM
48
CA
GLU A
7
71.079
71.486
33.564
1.00
41.57
C


ATOM
49
C
GLU A
7
70.346
71.136
32.284
1.00
38.29
C


ATOM
50
O
GLU A
7
69.314
70.472
32.315
1.00
37.72
O


ATOM
51
CB
GLU A
7
72.127
70.393
33.817
1.00
43.70
C


ATOM
52
CG
GLU A
7
73.090
70.645
34.973
1.00
46.76
C


ATOM
53
CD
GLU A
7
73.898
71.919
34.802
1.00
47.87
C


ATOM
54
OE1
GLU A
7
74.359
72.193
33.670
1.00
49.12
O


ATOM
55
OE2
GLU A
7
74.082
72.641
35.805
1.00
50.03
O


ATOM
56
N
PRO A
8
70.871
71.577
31.135
1.00
35.40
N


ATOM
57
CA
PRO A
8
70.208
71.252
29.871
1.00
34.46
C


ATOM
58
C
PRO A
8
70.554
69.795
29.540
1.00
33.72
C


ATOM
59
O
PRO A
8
71.523
69.267
30.073
1.00
33.53
O


ATOM
60
CB
PRO A
8
70.835
72.240
28.895
1.00
34.81
C


ATOM
61
CG
PRO A
8
72.234
72.402
29.433
1.00
33.93
C


ATOM
62
CD
PRO A
8
72.018
72.481
30.923
1.00
35.69
C


ATOM
63
N
CYS A
9
69.769
69.139
28.690
1.00
32.35
N


ATOM
64
CA
CYS A
9
70.080
67.760
28.330
1.00
32.79
C


ATOM
65
C
CYS A
9
71.159
67.727
27.240
1.00
30.89
C


ATOM
66
O
CYS A
9
71.332
68.694
26.501
1.00
30.36
O


ATOM
67
CB
CYS A
9
68.814
67.012
27.884
1.00
35.10
C


ATOM
68
SG
CYS A
9
67.853
67.729
26.524
1.00
42.35
S


ATOM
69
N
HIS A
10
71.888
66.618
27.157
1.00
30.90
N


ATOM
70
CA
HIS A
10
72.979
66.462
26.193
1.00
29.93
C


ATOM
71
C
HIS A
10
72.848
65.184
25.371
1.00
30.71
C


ATOM
72
O
HIS A
10
72.257
64.207
25.825
1.00
30.16
O


ATOM
73
CB
HIS A
10
74.315
66.419
26.933
1.00
29.59
C


ATOM
74
CG
HIS A
10
74.582
67.624
27.773
1.00
30.61
C


ATOM
75
ND1
HIS A
10
74.945
68.840
27.236
1.00
30.69
N


ATOM
76
CD2
HIS A
10
74.533
67.804
29.115
1.00
30.16
C


ATOM
77
CE1
HIS A
10
75.109
69.716
28.210
1.00
30.34
C


ATOM
78
NE2
HIS A
10
74.864
69.112
29.359
1.00
31.65
N


ATOM
79
N
THR A
11
73.405
65.199
24.164
1.00
30.01
N


ATOM
80
CA
THR A
11
73.368
64.032
23.286
1.00
30.68
C


ATOM
81
C
THR A
11
74.696
63.287
23.412
1.00
29.38
C


ATOM
82
O
THR A
11
75.639
63.803
24.006
1.00
29.12
O


ATOM
83
CB
THR A
11
73.194
64.437
21.816
1.00
31.25
C


ATOM
84
OG1
THR A
11
74.303
65.251
21.419
1.00
33.58
O


ATOM
85
CG2
THR A
11
71.903
65.220
21.621
1.00
34.80
C


ATOM
86
N
PHE A
12
74.768
62.085
22.846
1.00
29.78
N


ATOM
87
CA
PHE A
12
75.991
61.278
22.894
1.00
31.09
C


ATOM
88
C
PHE A
12
77.208
61.973
22.287
1.00
31.77
C


ATOM
89
O
PHE A
12
78.334
61.771
22.747
1.00
30.24
O


ATOM
90
CB
PHE A
12
75.789
59.943
22.173
1.00
28.84
C


ATOM
91
CG
PHE A
12
74.853
59.003
22.877
1.00
29.84
C


ATOM
92
CD1
PHE A
12
74.966
58.782
24.247
1.00
28.95
C


ATOM
93
CD2
PHE A
12
73.904
58.284
22.156
1.00
29.11
C


ATOM
94
CE1
PHE A
12
74.153
57.853
24.888
1.00
30.30
C


ATOM
95
CE2
PHE A
12
73.082
57.348
22.788
1.00
30.62
C


ATOM
96
CZ
PHE A
12
73.207
57.130
24.154
1.00
28.11
C


ATOM
97
N
ASN A
13
76.984
62.770
21.243
1.00
33.09
N


ATOM
98
CA
ASN A
13
78.071
63.496
20.582
1.00
33.64
C


ATOM
99
C
ASN A
13
78.783
64.499
21.487
1.00
32.75
C


ATOM
100
O
ASN A
13
79.884
64.944
21.168
1.00
33.53
O


ATOM
101
CB
ASN A
13
77.554
64.238
19.344
1.00
37.76
C


ATOM
102
CG
ASN A
13
77.564
63.377
18.098
1.00
42.14
C


ATOM
103
OD1
ASN A
13
78.553
62.701
17.804
1.00
46.22
O


ATOM
104
ND2
ASN A
13
76.471
63.408
17.348
1.00
44.81
N


ATOM
105
N
GLU A
14
78.163
64.861
22.607
1.00
31.62
N


ATOM
106
CA
GLU A
14
78.771
65.818
23.531
1.00
31.09
C


ATOM
107
C
GLU A
14
79.655
65.155
24.581
1.00
31.08
C


ATOM
108
O
GLU A
14
80.097
65.801
25.527
1.00
31.33
O


ATOM
109
CB
GLU A
14
77.684
66.629
24.232
1.00
31.42
C


ATOM
110
CG
GLU A
14
76.804
67.400
23.272
1.00
32.57
C


ATOM
111
CD
GLU A
14
75.692
68.138
23.971
1.00
31.00
C


ATOM
112
OE1
GLU A
14
75.995
68.988
24.831
1.00
32.14
O


ATOM
113
OE2
GLU A
14
74.516
67.864
23.660
1.00
32.39
O


ATOM
114
N
TYR A
15
79.928
63.869
24.418
1.00
29.84
N


ATOM
115
CA
TYR A
15
80.746
63.176
25.397
1.00
29.38
C


ATOM
116
C
TYR A
15
81.916
62.432
24.792
1.00
29.40
C


ATOM
117
O
TYR A
15
81.906
62.064
23.616
1.00
30.63
O


ATOM
118
CB
TYR A
15
79.889
62.177
26.184
1.00
29.52
C


ATOM
119
CG
TYR A
15
78.909
62.805
27.147
1.00
30.93
C


ATOM
120
CD1
TYR A
15
79.296
63.131
28.446
1.00
30.83
C


ATOM
121
CD2
TYR A
15
77.593
63.074
26.759
1.00
30.10
C


ATOM
122
CE1
TYR A
15
78.400
63.706
29.341
1.00
32.23
C


ATOM
123
CE2
TYR A
15
76.688
63.653
27.646
1.00
32.13
C


ATOM
124
CZ
TYR A
15
77.099
63.967
28.934
1.00
32.37
C


ATOM
125
OH
TYR A
15
76.225
64.565
29.809
1.00
35.93
O


ATOM
126
N
LEU A
16
82.929
62.216
25.620
1.00
30.01
N


ATOM
127
CA
LEU A
16
84.107
61.457
25.229
1.00
30.13
C


ATOM
128
C
LEU A
16
84.514
60.664
26.463
1.00
28.66
C


ATOM
129
O
LEU A
16
84.207
61.048
27.592
1.00
26.73
O


ATOM
130
CB
LEU A
16
85.260
62.374
24.788
1.00
31.28
C


ATOM
131
CG
LEU A
16
85.169
63.110
23.440
1.00
32.96
C


ATOM
132
CD1
LEU A
16
86.432
63.925
23.241
1.00
34.63
C


ATOM
133
CD2
LEU A
16
85.011
62.126
22.287
1.00
33.72
C


ATOM
134
N
LEU A
17
85.182
59.543
26.239
1.00
29.11
N


ATOM
135
CA
LEU A
17
85.652
58.696
27.327
1.00
30.34
C


ATOM
136
C
LEU A
17
87.129
58.990
27.618
1.00
30.21
C


ATOM
137
O
LEU A
17
87.943
59.094
26.698
1.00
31.80
O


ATOM
138
CB
LEU A
17
85.502
57.224
26.935
1.00
29.21
C


ATOM
139
CG
LEU A
17
84.082
56.655
26.892
1.00
28.59
C


ATOM
140
CD1
LEU A
17
84.051
55.435
25.990
1.00
25.58
C


ATOM
141
CD2
LEU A
17
83.622
56.315
28.304
1.00
25.80
C


ATOM
142
N
ILE A
18
87.466
59.144
28.892
1.00
31.07
N


ATOM
143
CA
ILE A
18
88.852
59.385
29.282
1.00
30.21
C


ATOM
144
C
ILE A
18
89.418
58.024
29.677
1.00
29.84
C


ATOM
145
O
ILE A
18
88.859
57.345
30.536
1.00
29.71
O


ATOM
146
CB
ILE A
18
88.939
60.359
30.472
1.00
30.01
C


ATOM
147
CG1
ILE A
18
88.464
61.748
30.035
1.00
30.69
C


ATOM
148
CG2
ILE A
18
90.375
60.428
30.991
1.00
28.88
C


ATOM
149
CD1
ILE A
18
88.447
62.774
31.145
1.00
31.89
C


ATOM
150
N
PRO A
19
90.528
57.601
29.045
1.00
29.50
N


ATOM
151
CA
PRO A
19
91.140
56.303
29.350
1.00
30.06
C


ATOM
152
C
PRO A
19
91.482
56.059
30.818
1.00
29.17
C


ATOM
153
O
PRO A
19
91.777
56.989
31.570
1.00
30.34
O


ATOM
154
CB
PRO A
19
92.389
56.285
28.460
1.00
30.87
C


ATOM
155
CG
PRO A
19
91.978
57.136
27.284
1.00
30.83
C


ATOM
156
CD
PRO A
19
91.265
58.285
27.966
1.00
29.93
C


ATOM
157
N
GLY A
20
91.415
54.792
31.210
1.00
27.42
N


ATOM
158
CA
GLY A
20
91.745
54.398
32.566
1.00
27.95
C


ATOM
159
C
GLY A
20
92.936
53.469
32.445
1.00
27.30
C


ATOM
160
O
GLY A
20
93.543
53.402
31.386
1.00
26.88
O


ATOM
161
N
LEU A
21
93.275
52.739
33.497
1.00
29.16
N


ATOM
162
CA
LEU A
21
94.422
51.838
33.424
1.00
29.56
C


ATOM
163
C
LEU A
21
94.130
50.584
32.611
1.00
29.75
C


ATOM
164
O
LEU A
21
93.212
49.831
32.920
1.00
29.91
O


ATOM
165
CB
LEU A
21
94.885
51.435
34.834
1.00
30.32
C


ATOM
166
CG
LEU A
21
96.026
50.403
34.888
1.00
30.63
C


ATOM
167
CD1
LEU A
21
97.262
50.967
34.183
1.00
25.74
C


ATOM
168
CD2
LEU A
21
96.342
50.047
36.348
1.00
31.08
C


ATOM
169
N
SER A
22
94.917
50.370
31.564
1.00
31.55
N


ATOM
170
CA
SER A
22
94.762
49.191
30.726
1.00
32.64
C


ATOM
171
C
SER A
22
95.789
48.167
31.189
1.00
34.68
C


ATOM
172
O
SER A
22
96.993
48.439
31.185
1.00
32.90
O


ATOM
173
CB
SER A
22
95.008
49.531
29.256
1.00
32.66
C


ATOM
174
OG
SER A
22
94.090
50.505
28.793
1.00
31.63
O


ATOM
175
N
THR A
23
95.305
46.998
31.600
1.00
36.61
N


ATOM
176
CA
THR A
23
96.170
45.923
32.075
1.00
37.91
C


ATOM
177
C
THR A
23
96.550
44.997
30.927
1.00
38.68
C


ATOM
178
O
THR A
23
95.882
44.978
29.892
1.00
39.48
O


ATOM
179
CB
THR A
23
95.478
45.107
33.174
1.00
37.72
C


ATOM
180
OG1
THR A
23
94.187
44.701
32.718
1.00
41.28
O


ATOM
181
CG2
THR A
23
95.311
45.936
34.431
1.00
38.84
C


ATOM
182
N
VAL A
24
97.624
44.232
31.117
1.00
39.25
N


ATOM
183
CA
VAL A
24
98.118
43.311
30.095
1.00
39.40
C


ATOM
184
C
VAL A
24
97.105
42.274
29.611
1.00
40.18
C


ATOM
185
O
VAL A
24
97.178
41.820
28.470
1.00
39.57
O


ATOM
186
CB
VAL A
24
99.390
42.559
30.582
1.00
40.21
C


ATOM
187
CG1
VAL A
24
100.555
43.537
30.721
1.00
38.74
C


ATOM
188
CG2
VAL A
24
99.115
41.863
31.912
1.00
40.04
C


ATOM
189
N
ASP A
25
96.160
41.896
30.464
1.00
41.79
N


ATOM
190
CA
ASP A
25
95.170
40.903
30.066
1.00
45.39
C


ATOM
191
C
ASP A
25
94.021
41.455
29.225
1.00
45.56
C


ATOM
192
O
ASP A
25
93.233
40.684
28.681
1.00
45.92
O


ATOM
193
CB
ASP A
25
94.592
40.185
31.294
1.00
48.41
C


ATOM
194
CG
ASP A
25
93.943
41.140
32.283
1.00
51.92
C


ATOM
195
OD1
ASP A
25
93.010
40.724
33.005
1.00
54.02
O


ATOM
196
OD2
ASP A
25
94.375
42.304
32.355
1.00
53.64
O


ATOM
197
N
CYS A
26
93.912
42.774
29.096
1.00
45.84
N


ATOM
198
CA
CYS A
26
92.808
43.308
28.309
1.00
45.30
C


ATOM
199
C
CYS A
26
93.109
43.487
26.838
1.00
45.23
C


ATOM
200
O
CYS A
26
93.730
44.463
26.426
1.00
44.99
O


ATOM
201
CB
CYS A
26
92.301
44.641
28.867
1.00
44.12
C


ATOM
202
SG
CYS A
26
90.582
45.050
28.364
1.00
43.07
S


ATOM
203
N
ILE A
27
92.663
42.521
26.049
1.00
46.24
N


ATOM
204
CA
ILE A
27
92.807
42.573
24.608
1.00
47.19
C


ATOM
205
C
ILE A
27
91.403
42.280
24.110
1.00
47.45
C


ATOM
206
O
ILE A
27
90.651
41.553
24.763
1.00
46.02
O


ATOM
207
CB
ILE A
27
93.796
41.507
24.077
1.00
49.39
C


ATOM
208
CG1
ILE A
27
93.511
40.151
24.728
1.00
49.86
C


ATOM
209
CG2
ILE A
27
95.229
41.964
24.329
1.00
49.14
C


ATOM
210
CD1
ILE A
27
94.444
39.039
24.270
1.00
52.58
C


ATOM
211
N
PRO A
28
91.025
42.857
22.962
1.00
47.37
N


ATOM
212
CA
PRO A
28
89.703
42.674
22.363
1.00
47.25
C


ATOM
213
C
PRO A
28
89.120
41.265
22.436
1.00
47.37
C


ATOM
214
O
PRO A
28
87.972
41.088
22.842
1.00
46.21
O


ATOM
215
CB
PRO A
28
89.919
43.146
20.929
1.00
48.82
C


ATOM
216
CG
PRO A
28
90.865
44.289
21.121
1.00
47.38
C


ATOM
217
CD
PRO A
28
91.866
43.722
22.111
1.00
48.12
C


ATOM
218
N
SER A
29
89.908
40.264
22.057
1.00
47.34
N


ATOM
219
CA
SER A
29
89.426
38.888
22.063
1.00
46.68
C


ATOM
220
C
SER A
29
89.015
38.355
23.435
1.00
45.41
C


ATOM
221
O
SER A
29
88.294
37.361
23.524
1.00
45.14
O


ATOM
222
CB
SER A
29
90.469
37.952
21.429
1.00
48.70
C


ATOM
223
OG
SER A
29
91.665
37.887
22.188
1.00
51.82
O


ATOM
224
N
ASN A
30
89.460
38.999
24.507
1.00
43.78
N


ATOM
225
CA
ASN A
30
89.079
38.528
25.832
1.00
42.85
C


ATOM
226
C
ASN A
30
87.923
39.330
26.427
1.00
40.38
C


ATOM
227
O
ASN A
30
87.454
39.033
27.528
1.00
40.36
O


ATOM
228
CB
ASN A
30
90.271
38.560
26.789
1.00
45.40
C


ATOM
229
CG
ASN A
30
91.397
37.656
26.341
1.00
48.87
C


ATOM
230
OD1
ASN A
30
91.165
36.604
25.739
1.00
50.85
O


ATOM
231
ND2
ASN A
30
92.629
38.052
26.644
1.00
50.41
N


ATOM
232
N
VAL A
31
87.461
40.342
25.703
1.00
35.43
N


ATOM
233
CA
VAL A
31
86.355
41.153
26.196
1.00
34.43
C


ATOM
234
C
VAL A
31
85.030
40.405
26.046
1.00
32.47
C


ATOM
235
O
VAL A
31
84.719
39.858
24.990
1.00
31.37
O


ATOM
236
CB
VAL A
31
86.288
42.516
25.460
1.00
34.64
C


ATOM
237
CG1
VAL A
31
85.055
43.296
25.907
1.00
34.16
C


ATOM
238
CG2
VAL A
31
87.554
43.325
25.763
1.00
33.50
C


ATOM
239
N
ASN A
32
84.262
40.376
27.125
1.00
32.26
N


ATOM
240
CA
ASN A
32
82.972
39.695
27.155
1.00
31.85
C


ATOM
241
C
ASN A
32
81.865
40.737
27.009
1.00
31.43
C


ATOM
242
O
ASN A
32
81.731
41.614
27.855
1.00
31.95
O


ATOM
243
CB
ASN A
32
82.837
38.959
28.494
1.00
33.05
C


ATOM
244
CG
ASN A
32
81.543
38.173
28.618
1.00
34.40
C


ATOM
245
OD1
ASN A
32
80.616
38.330
27.826
1.00
31.77
O


ATOM
246
ND2
ASN A
32
81.476
37.325
29.641
1.00
36.34
N


ATOM
247
N
LEU A
33
81.070
40.638
25.944
1.00
31.73
N


ATOM
248
CA
LEU A
33
79.986
41.595
25.710
1.00
31.12
C


ATOM
249
C
LEU A
33
78.604
41.067
26.088
1.00
32.02
C


ATOM
250
O
LEU A
33
77.582
41.607
25.661
1.00
32.34
O


ATOM
251
CB
LEU A
33
79.979
42.040
24.244
1.00
32.07
C


ATOM
252
CG
LEU A
33
81.202
42.819
23.763
1.00
33.24
C


ATOM
253
CD1
LEU A
33
81.030
43.165
22.300
1.00
33.95
C


ATOM
254
CD2
LEU A
33
81.380
44.091
24.601
1.00
33.50
C


ATOM
255
N
SER A
34
78.574
40.003
26.878
1.00
31.24
N


ATOM
256
CA
SER A
34
77.316
39.419
27.326
1.00
31.29
C


ATOM
257
C
SER A
34
76.559
40.452
28.180
1.00
30.51
C


ATOM
258
O
SER A
34
77.172
41.284
28.850
1.00
30.18
O


ATOM
259
CB
SER A
34
77.613
38.154
28.136
1.00
31.20
C


ATOM
260
OG
SER A
34
76.447
37.653
28.758
1.00
39.13
O


ATOM
261
N
THR A
35
75.231
40.403
28.161
1.00
29.56
N


ATOM
262
CA
THR A
35
74.445
41.364
28.923
1.00
26.77
C


ATOM
263
C
THR A
35
73.013
40.869
29.167
1.00
27.05
C


ATOM
264
O
THR A
35
72.435
40.168
28.336
1.00
27.90
O


ATOM
265
CB
THR A
35
74.416
42.737
28.181
1.00
27.30
C


ATOM
266
OG1
THR A
35
74.121
43.788
29.110
1.00
25.66
O


ATOM
267
CG2
THR A
35
73.363
42.738
27.085
1.00
26.06
C


ATOM
268
N
PRO A
36
72.423
41.233
30.318
1.00
26.43
N


ATOM
269
CA
PRO A
36
71.058
40.815
30.653
1.00
26.22
C


ATOM
270
C
PRO A
36
69.955
41.534
29.866
1.00
27.39
C


ATOM
271
O
PRO A
36
70.018
42.745
29.641
1.00
26.32
O


ATOM
272
CB
PRO A
36
70.971
41.094
32.153
1.00
26.70
C


ATOM
273
CG
PRO A
36
71.839
42.318
32.305
1.00
25.86
C


ATOM
274
CD
PRO A
36
73.036
41.988
31.429
1.00
24.23
C


ATOM
275
N
LEU A
37
68.942
40.770
29.468
1.00
27.00
N


ATOM
276
CA
LEU A
37
67.815
41.295
28.716
1.00
28.26
C


ATOM
277
C
LEU A
37
66.590
41.525
29.600
1.00
29.30
C


ATOM
278
O
LEU A
37
65.852
42.489
29.396
1.00
29.95
O


ATOM
279
CB
LEU A
37
67.444
40.334
27.580
1.00
28.03
C


ATOM
280
CG
LEU A
37
66.334
40.796
26.631
1.00
27.43
C


ATOM
281
CD1
LEU A
37
66.879
41.891
25.699
1.00
26.44
C


ATOM
282
CD2
LEU A
37
65.821
39.615
25.813
1.00
27.22
C


ATOM
283
N
VAL A
38
66.375
40.650
30.583
1.00
28.72
N


ATOM
284
CA
VAL A
38
65.214
40.768
31.464
1.00
27.01
C


ATOM
285
C
VAL A
38
65.588
40.778
32.944
1.00
28.83
C


ATOM
286
O
VAL A
38
66.633
40.263
33.340
1.00
30.63
O


ATOM
287
CB
VAL A
38
64.187
39.635
31.178
1.00
28.13
C


ATOM
288
CG1
VAL A
38
63.710
39.731
29.723
1.00
24.82
C


ATOM
289
CG2
VAL A
38
64.815
38.265
31.428
1.00
25.61
C


ATOM
290
N
LYS A
39
64.715
41.364
33.755
1.00
27.51
N


ATOM
291
CA
LYS A
39
64.950
41.516
35.183
1.00
29.76
C


ATOM
292
C
LYS A
39
65.127
40.247
36.006
1.00
30.05
C


ATOM
293
O
LYS A
39
64.584
39.196
35.684
1.00
30.31
O


ATOM
294
CB
LYS A
39
63.830
42.350
35.812
1.00
29.02
C


ATOM
295
CG
LYS A
39
62.456
41.677
35.757
1.00
29.38
C


ATOM
296
CD
LYS A
39
61.439
42.441
36.583
1.00
30.04
C


ATOM
297
CE
LYS A
39
60.065
41.781
36.528
1.00
31.85
C


ATOM
298
NZ
LYS A
39
59.125
42.424
37.483
1.00
31.72
N


ATOM
299
N
PHE A
40
65.887
40.388
37.088
1.00
30.48
N


ATOM
300
CA
PHE A
40
66.172
39.309
38.019
1.00
31.44
C


ATOM
301
C
PHE A
40
66.417
39.922
39.392
1.00
32.56
C


ATOM
302
O
PHE A
40
66.522
41.143
39.518
1.00
33.92
O


ATOM
303
CB
PHE A
40
67.411
38.516
37.575
1.00
29.74
C


ATOM
304
CG
PHE A
40
68.624
39.369
37.298
1.00
28.15
C


ATOM
305
CD1
PHE A
40
68.802
39.971
36.050
1.00
28.42
C


ATOM
306
CD2
PHE A
40
69.591
39.562
38.279
1.00
27.09
C


ATOM
307
CE1
PHE A
40
69.928
40.747
35.788
1.00
26.56
C


ATOM
308
CE2
PHE A
40
70.723
40.336
38.031
1.00
26.08
C


ATOM
309
CZ
PHE A
40
70.894
40.930
36.783
1.00
27.19
C


ATOM
310
N
GLN A
41
66.502
39.078
40.415
1.00
33.34
N


ATOM
311
CA
GLN A
41
66.740
39.538
41.778
1.00
35.08
C


ATOM
312
C
GLN A
41
68.226
39.523
42.084
1.00
32.98
C


ATOM
313
O
GLN A
41
68.999
38.848
41.411
1.00
32.25
O


ATOM
314
CB
GLN A
41
66.039
38.624
42.797
1.00
38.64
C


ATOM
315
CG
GLN A
41
64.528
38.606
42.729
1.00
45.39
C


ATOM
316
CD
GLN A
41
63.918
39.959
43.043
1.00
48.32
C


ATOM
317
OE1
GLN A
41
64.168
40.538
44.105
1.00
51.57
O


ATOM
318
NE2
GLN A
41
63.113
40.469
42.122
1.00
49.79
N


ATOM
319
N
LYS A
42
68.605
40.268
43.116
1.00
32.94
N


ATOM
320
CA
LYS A
42
69.985
40.341
43.580
1.00
34.24
C


ATOM
321
C
LYS A
42
70.530
38.925
43.835
1.00
34.61
C


ATOM
322
O
LYS A
42
69.847
38.083
44.429
1.00
32.73
O


ATOM
323
CB
LYS A
42
70.031
41.148
44.874
1.00
35.33
C


ATOM
324
CG
LYS A
42
71.390
41.217
45.521
1.00
39.95
C


ATOM
325
CD
LYS A
42
71.305
41.933
46.855
1.00
42.65
C


ATOM
326
CE
LYS A
42
72.661
42.007
47.524
1.00
44.06
C


ATOM
327
NZ
LYS A
42
72.561
42.711
48.829
1.00
48.33
N


ATOM
328
N
GLY A
43
71.752
38.666
43.381
1.00
34.34
N


ATOM
329
CA
GLY A
43
72.348
37.355
43.572
1.00
33.96
C


ATOM
330
C
GLY A
43
72.056
36.394
42.438
1.00
33.07
C


ATOM
331
O
GLY A
43
72.717
35.365
42.301
1.00
32.56
O


ATOM
332
N
GLN A
44
71.066
36.726
41.618
1.00
33.56
N


ATOM
333
CA
GLN A
44
70.695
35.883
40.484
1.00
33.80
C


ATOM
334
C
GLN A
44
71.315
36.362
39.176
1.00
34.40
C


ATOM
335
O
GLN A
44
72.039
37.353
39.140
1.00
33.77
O


ATOM
336
CB
GLN A
44
69.174
35.867
40.311
1.00
35.69
C


ATOM
337
CG
GLN A
44
68.406
35.347
41.507
1.00
38.03
C


ATOM
338
CD
GLN A
44
66.898
35.438
41.324
1.00
40.01
C


ATOM
339
OE1
GLN A
44
66.135
34.847
42.093
1.00
39.88
O


ATOM
340
NE2
GLN A
44
66.461
36.186
40.310
1.00
35.88
N


ATOM
341
N
GLN A
45
71.021
35.626
38.110
1.00
35.41
N


ATOM
342
CA
GLN A
45
71.465
35.936
36.758
1.00
36.43
C


ATOM
343
C
GLN A
45
70.174
36.046
35.957
1.00
34.87
C


ATOM
344
O
GLN A
45
69.170
35.438
36.319
1.00
33.83
O


ATOM
345
CB
GLN A
45
72.312
34.800
36.170
1.00
40.80
C


ATOM
346
CG
GLN A
45
73.682
34.634
36.801
1.00
46.43
C


ATOM
347
CD
GLN A
45
74.527
35.881
36.657
1.00
50.68
C


ATOM
348
OE1
GLN A
45
74.757
36.360
35.543
1.00
54.30
O


ATOM
349
NE2
GLN A
45
74.995
36.418
37.784
1.00
50.86
N


ATOM
350
N
SER A
46
70.194
36.820
34.881
1.00
32.16
N


ATOM
351
CA
SER A
46
69.009
36.976
34.056
1.00
32.64
C


ATOM
352
C
SER A
46
68.721
35.690
33.289
1.00
33.23
C


ATOM
353
O
SER A
46
69.643
35.015
32.836
1.00
32.72
O


ATOM
354
CB
SER A
46
69.204
38.120
33.059
1.00
30.63
C


ATOM
355
OG
SER A
46
68.058
38.282
32.252
1.00
30.42
O


ATOM
356
N
GLU A
47
67.441
35.364
33.133
1.00
33.48
N


ATOM
357
CA
GLU A
47
67.047
34.167
32.399
1.00
34.97
C


ATOM
358
C
GLU A
47
67.453
34.269
30.936
1.00
34.59
C


ATOM
359
O
GLU A
47
67.588
33.261
30.251
1.00
34.40
O


ATOM
360
CB
GLU A
47
65.536
33.963
32.492
1.00
36.97
C


ATOM
361
CG
GLU A
47
65.048
33.634
33.884
1.00
40.19
C


ATOM
362
CD
GLU A
47
63.541
33.663
33.982
1.00
43.59
C


ATOM
363
OE1
GLU A
47
62.884
32.836
33.313
1.00
46.14
O


ATOM
364
OE2
GLU A
47
63.010
34.519
34.726
1.00
45.57
O


ATOM
365
N
ILE A
48
67.633
35.494
30.452
1.00
34.08
N


ATOM
366
CA
ILE A
48
68.032
35.702
29.066
1.00
32.00
C


ATOM
367
C
ILE A
48
69.188
36.698
28.991
1.00
31.52
C


ATOM
368
O
ILE A
48
69.075
37.847
29.418
1.00
30.71
O


ATOM
369
CB
ILE A
48
66.851
36.231
28.204
1.00
32.81
C


ATOM
370
CG1
ILE A
48
65.671
35.254
28.264
1.00
33.69
C


ATOM
371
CG2
ILE A
48
67.307
36.419
26.764
1.00
32.09
C


ATOM
372
CD1
ILE A
48
64.439
35.718
27.503
1.00
34.71
C


ATOM
373
N
ASN A
49
70.306
36.241
28.449
1.00
30.86
N


ATOM
374
CA
ASN A
49
71.483
37.076
28.308
1.00
31.23
C


ATOM
375
C
ASN A
49
71.892
37.131
26.851
1.00
31.45
C


ATOM
376
O
ASN A
49
72.070
36.095
26.214
1.00
31.67
O


ATOM
377
CB
ASN A
49
72.636
36.514
29.154
1.00
30.33
C


ATOM
378
CG
ASN A
49
72.393
36.676
30.640
1.00
31.43
C


ATOM
379
OD1
ASN A
49
72.573
37.757
31.193
1.00
28.79
O


ATOM
380
ND2
ASN A
49
71.958
35.602
31.292
1.00
32.52
N


ATOM
381
N
LEU A
50
72.017
38.343
26.321
1.00
30.27
N


ATOM
382
CA
LEU A
50
72.440
38.523
24.937
1.00
30.28
C


ATOM
383
C
LEU A
50
73.947
38.255
24.904
1.00
30.37
C


ATOM
384
O
LEU A
50
74.624
38.437
25.916
1.00
30.24
O


ATOM
385
CB
LEU A
50
72.174
39.965
24.476
1.00
28.53
C


ATOM
386
CG
LEU A
50
70.755
40.537
24.591
1.00
30.96
C


ATOM
387
CD1
LEU A
50
70.767
42.022
24.227
1.00
30.43
C


ATOM
388
CD2
LEU A
50
69.807
39.769
23.673
1.00
30.05
C


ATOM
389
N
LYS A
51
74.461
37.821
23.755
1.00
30.78
N


ATOM
390
CA
LYS A
51
75.896
37.572
23.590
1.00
32.78
C


ATOM
391
C
LYS A
51
76.563
38.904
23.231
1.00
31.15
C


ATOM
392
O
LYS A
51
77.740
39.120
23.516
1.00
31.86
O


ATOM
393
CB
LYS A
51
76.157
36.549
22.470
1.00
33.00
C


ATOM
394
CG
LYS A
51
76.430
35.127
22.945
1.00
37.03
C


ATOM
395
CD
LYS A
51
75.265
34.540
23.694
1.00
39.28
C


ATOM
396
CE
LYS A
51
75.548
33.103
24.116
1.00
42.58
C


ATOM
397
NZ
LYS A
51
75.773
32.190
22.957
1.00
43.64
N


ATOM
398
N
ILE A
52
75.802
39.777
22.571
1.00
29.58
N


ATOM
399
CA
ILE A
52
76.266
41.114
22.209
1.00
28.26
C


ATOM
400
C
ILE A
52
75.126
42.049
22.607
1.00
28.67
C


ATOM
401
O
ILE A
52
73.954
41.700
22.476
1.00
30.64
O


ATOM
402
CB
ILE A
52
76.597
41.248
20.689
1.00
29.21
C


ATOM
403
CG1
ILE A
52
75.369
40.926
19.832
1.00
29.71
C


ATOM
404
CG2
ILE A
52
77.768
40.317
20.326
1.00
28.36
C


ATOM
405
CD1
ILE A
52
75.591
41.184
18.343
1.00
25.96
C


ATOM
406
N
PRO A
53
75.451
43.253
23.091
1.00
27.43
N


ATOM
407
CA
PRO A
53
74.436
44.217
23.521
1.00
27.51
C


ATOM
408
C
PRO A
53
73.665
44.991
22.453
1.00
28.48
C


ATOM
409
O
PRO A
53
73.321
46.152
22.667
1.00
28.86
O


ATOM
410
CB
PRO A
53
75.231
45.140
24.431
1.00
25.91
C


ATOM
411
CG
PRO A
53
76.535
45.245
23.685
1.00
27.35
C


ATOM
412
CD
PRO A
53
76.808
43.810
23.255
1.00
27.52
C


ATOM
413
N
LEU A
54
73.376
44.360
21.319
1.00
27.64
N


ATOM
414
CA
LEU A
54
72.639
45.048
20.266
1.00
28.10
C


ATOM
415
C
LEU A
54
71.310
44.369
19.933
1.00
28.75
C


ATOM
416
O
LEU A
54
71.233
43.142
19.847
1.00
29.19
O


ATOM
417
CB
LEU A
54
73.486
45.135
18.989
1.00
26.86
C


ATOM
418
CG
LEU A
54
74.898
45.720
19.078
1.00
27.96
C


ATOM
419
CD1
LEU A
54
75.549
45.652
17.707
1.00
25.98
C


ATOM
420
CD2
LEU A
54
74.857
47.159
19.584
1.00
28.24
C


ATOM
421
N
VAL A
55
70.261
45.171
19.770
1.00
27.85
N


ATOM
422
CA
VAL A
55
68.957
44.649
19.388
1.00
28.01
C


ATOM
423
C
VAL A
55
68.426
45.554
18.276
1.00
29.53
C


ATOM
424
O
VAL A
55
68.649
46.768
18.299
1.00
30.35
O


ATOM
425
CB
VAL A
55
67.947
44.605
20.579
1.00
26.85
C


ATOM
426
CG1
VAL A
55
68.531
43.797
21.725
1.00
25.48
C


ATOM
427
CG2
VAL A
55
67.569
45.998
21.021
1.00
26.54
C


ATOM
428
N
SER A
56
67.765
44.961
17.284
1.00
28.53
N


ATOM
429
CA
SER A
56
67.224
45.735
16.174
1.00
28.75
C


ATOM
430
C
SER A
56
65.855
46.310
16.533
1.00
27.91
C


ATOM
431
O
SER A
56
65.070
45.694
17.253
1.00
29.11
O


ATOM
432
CB
SER A
56
67.166
44.878
14.897
1.00
28.24
C


ATOM
433
OG
SER A
56
66.443
43.676
15.091
1.00
30.49
O


ATOM
434
N
ALA A
57
65.594
47.512
16.037
1.00
27.60
N


ATOM
435
CA
ALA A
57
64.363
48.241
16.318
1.00
27.21
C


ATOM
436
C
ALA A
57
63.062
47.574
15.876
1.00
29.66
C


ATOM
437
O
ALA A
57
63.030
46.784
14.931
1.00
29.73
O


ATOM
438
CB
ALA A
57
64.460
49.640
15.721
1.00
25.06
C


ATOM
439
N
ILE A
58
61.990
47.911
16.581
1.00
28.79
N


ATOM
440
CA
ILE A
58
60.660
47.379
16.302
1.00
30.03
C


ATOM
441
C
ILE A
58
60.085
48.199
15.148
1.00
30.02
C


ATOM
442
O
ILE A
58
59.148
48.983
15.327
1.00
30.35
O


ATOM
443
CB
ILE A
58
59.765
47.524
17.546
1.00
28.25
C


ATOM
444
CG1
ILE A
58
60.560
47.095
18.788
1.00
27.95
C


ATOM
445
CG2
ILE A
58
58.508
46.677
17.390
1.00
27.16
C


ATOM
446
CD1
ILE A
58
59.785
47.176
20.078
1.00
28.05
C


ATOM
447
N
MET A
59
60.661
47.998
13.965
1.00
30.49
N


ATOM
448
CA
MET A
59
60.275
48.743
12.772
1.00
31.82
C


ATOM
449
C
MET A
59
60.088
47.877
11.530
1.00
32.36
C


ATOM
450
O
MET A
59
60.864
46.954
11.282
1.00
31.48
O


ATOM
451
CB
MET A
59
61.341
49.799
12.479
1.00
30.41
C


ATOM
452
CG
MET A
59
61.619
50.738
13.635
1.00
28.79
C


ATOM
453
SD
MET A
59
62.996
51.827
13.284
1.00
31.66
S


ATOM
454
CE
MET A
59
62.278
52.935
12.079
1.00
26.93
C


ATOM
455
N
GLN A
60
59.072
48.208
10.736
1.00
34.40
N


ATOM
456
CA
GLN A
60
58.772
47.459
9.512
1.00
36.49
C


ATOM
457
C
GLN A
60
59.974
47.433
8.582
1.00
36.55
C


ATOM
458
O
GLN A
60
60.208
46.447
7.885
1.00
37.12
O


ATOM
459
CB
GLN A
60
57.604
48.092
8.741
1.00
36.94
C


ATOM
460
CG
GLN A
60
56.360
48.433
9.546
1.00
37.40
C


ATOM
461
CD
GLN A
60
55.273
49.031
8.666
1.00
40.00
C


ATOM
462
OE1
GLN A
60
55.562
49.808
7.753
1.00
39.70
O


ATOM
463
NE2
GLN A
60
54.018
48.677
8.936
1.00
40.59
N


ATOM
464
N
SER A
61
60.730
48.526
8.572
1.00
36.66
N


ATOM
465
CA
SER A
61
61.890
48.645
7.694
1.00
36.60
C


ATOM
466
C
SER A
61
63.196
48.130
8.286
1.00
36.12
C


ATOM
467
O
SER A
61
64.274
48.388
7.738
1.00
36.48
O


ATOM
468
CB
SER A
61
62.073
50.105
7.280
1.00
35.62
C


ATOM
469
OG
SER A
61
62.314
50.921
8.414
1.00
41.10
O


ATOM
470
N
VAL A
62
63.111
47.393
9.386
1.00
34.72
N


ATOM
471
CA
VAL A
62
64.320
46.893
10.020
1.00
33.57
C


ATOM
472
C
VAL A
62
64.273
45.444
10.472
1.00
33.65
C


ATOM
473
O
VAL A
62
65.067
44.625
10.022
1.00
35.33
O


ATOM
474
CB
VAL A
62
64.692
47.757
11.253
1.00
32.43
C


ATOM
475
CG1
VAL A
62
65.900
47.160
11.970
1.00
32.00
C


ATOM
476
CG2
VAL A
62
64.983
49.189
10.820
1.00
32.49
C


ATOM
477
N
SER A
63
63.337
45.133
11.361
1.00
34.80
N


ATOM
478
CA
SER A
63
63.245
43.799
11.926
1.00
34.50
C


ATOM
479
C
SER A
63
62.258
42.804
11.322
1.00
35.59
C


ATOM
480
O
SER A
63
61.149
42.610
11.830
1.00
33.23
O


ATOM
481
CB
SER A
63
62.999
43.916
13.431
1.00
33.57
C


ATOM
482
OG
SER A
63
64.061
44.620
14.062
1.00
32.53
O


ATOM
483
N
GLY A
64
62.686
42.168
10.240
1.00
36.21
N


ATOM
484
CA
GLY A
64
61.874
41.154
9.602
1.00
37.02
C


ATOM
485
C
GLY A
64
62.487
39.815
9.979
1.00
39.12
C


ATOM
486
O
GLY A
64
63.403
39.764
10.811
1.00
36.38
O


ATOM
487
N
GLU A
65
62.011
38.736
9.364
1.00
39.92
N


ATOM
488
CA
GLU A
65
62.522
37.405
9.665
1.00
42.75
C


ATOM
489
C
GLU A
65
64.015
37.240
9.395
1.00
42.41
C


ATOM
490
O
GLU A
65
64.731
36.649
10.201
1.00
41.59
O


ATOM
491
CB
GLU A
65
61.735
36.332
8.892
1.00
46.22
C


ATOM
492
CG
GLU A
65
61.608
36.565
7.385
1.00
51.45
C


ATOM
493
CD
GLU A
65
60.419
37.448
7.007
1.00
55.41
C


ATOM
494
OE1
GLU A
65
60.438
38.668
7.305
1.00
55.84
O


ATOM
495
OE2
GLU A
65
59.456
36.915
6.405
1.00
57.74
O


ATOM
496
N
LYS A
66
64.485
37.764
8.268
1.00
42.65
N


ATOM
497
CA
LYS A
66
65.895
37.647
7.914
1.00
44.04
C


ATOM
498
C
LYS A
66
66.801
38.387
8.897
1.00
41.64
C


ATOM
499
O
LYS A
66
67.854
37.879
9.287
1.00
39.47
O


ATOM
500
CB
LYS A
66
66.132
38.169
6.494
1.00
46.38
C


ATOM
501
CG
LYS A
66
65.289
37.488
5.415
1.00
52.36
C


ATOM
502
CD
LYS A
66
65.540
35.975
5.309
1.00
56.28
C


ATOM
503
CE
LYS A
66
64.795
35.174
6.387
1.00
58.02
C


ATOM
504
NZ
LYS A
66
64.957
33.692
6.235
1.00
57.63
N


ATOM
505
N
MET A
67
66.393
39.588
9.289
1.00
39.83
N


ATOM
506
CA
MET A
67
67.168
40.376
10.237
1.00
37.79
C


ATOM
507
C
MET A
67
67.305
39.592
11.541
1.00
37.63
C


ATOM
508
O
MET A
67
68.409
39.413
12.061
1.00
36.92
O


ATOM
509
CB
MET A
67
66.472
41.710
10.512
1.00
37.57
C


ATOM
510
CG
MET A
67
67.214
42.614
11.485
1.00
37.05
C


ATOM
511
SD
MET A
67
68.849
43.062
10.880
1.00
36.99
S


ATOM
512
CE
MET A
67
68.422
44.225
9.565
1.00
34.40
C


ATOM
513
N
ALA A
68
66.173
39.111
12.047
1.00
35.24
N


ATOM
514
CA
ALA A
68
66.133
38.356
13.290
1.00
35.08
C


ATOM
515
C
ALA A
68
67.079
37.157
13.296
1.00
35.81
C


ATOM
516
O
ALA A
68
67.714
36.868
14.310
1.00
34.68
O


ATOM
517
CB
ALA A
68
64.707
37.901
13.571
1.00
34.00
C


ATOM
518
N
ILE A
69
67.169
36.460
12.167
1.00
35.92
N


ATOM
519
CA
ILE A
69
68.043
35.298
12.063
1.00
36.63
C


ATOM
520
C
ILE A
69
69.510
35.729
12.016
1.00
35.80
C


ATOM
521
O
ILE A
69
70.344
35.204
12.754
1.00
37.14
O


ATOM
522
CB
ILE A
69
67.694
34.456
10.804
1.00
38.10
C


ATOM
523
CG1
ILE A
69
66.314
33.814
10.982
1.00
39.72
C


ATOM
524
CG2
ILE A
69
68.739
33.375
10.580
1.00
37.50
C


ATOM
525
CD1
ILE A
69
65.712
33.259
9.695
1.00
40.53
C


ATOM
526
N
ALA A
70
69.816
36.697
11.160
1.00
34.80
N


ATOM
527
CA
ALA A
70
71.179
37.194
11.027
1.00
34.57
C


ATOM
528
C
ALA A
70
71.727
37.773
12.332
1.00
34.76
C


ATOM
529
O
ALA A
70
72.897
37.563
12.665
1.00
34.89
O


ATOM
530
CB
ALA A
70
71.244
38.246
9.932
1.00
33.76
C


ATOM
531
N
LEU A
71
70.886
38.501
13.066
1.00
34.07
N


ATOM
532
CA
LEU A
71
71.315
39.113
14.318
1.00
32.78
C


ATOM
533
C
LEU A
71
71.451
38.095
15.436
1.00
33.19
C


ATOM
534
O
LEU A
71
72.390
38.164
16.223
1.00
32.88
O


ATOM
535
CB
LEU A
71
70.348
40.223
14.737
1.00
31.82
C


ATOM
536
CG
LEU A
71
70.677
41.001
16.021
1.00
31.91
C


ATOM
537
CD1
LEU A
71
72.140
41.434
16.021
1.00
31.18
C


ATOM
538
CD2
LEU A
71
69.758
42.226
16.127
1.00
30.99
C


ATOM
539
N
ALA A
72
70.515
37.151
15.506
1.00
33.38
N


ATOM
540
CA
ALA A
72
70.566
36.120
16.534
1.00
34.54
C


ATOM
541
C
ALA A
72
71.820
35.272
16.354
1.00
36.16
C


ATOM
542
O
ALA A
72
72.385
34.775
17.332
1.00
35.90
O


ATOM
543
CB
ALA A
72
69.318
35.234
16.468
1.00
32.94
C


ATOM
544
N
ARG A
73
72.242
35.103
15.102
1.00
37.20
N


ATOM
545
CA
ARG A
73
73.433
34.316
14.791
1.00
40.02
C


ATOM
546
C
ARG A
73
74.685
34.954
15.376
1.00
40.27
C


ATOM
547
O
ARG A
73
75.641
34.259
15.711
1.00
39.91
O


ATOM
548
CB
ARG A
73
73.618
34.177
13.276
1.00
42.94
C


ATOM
549
CG
ARG A
73
72.702
33.172
12.595
1.00
45.30
C


ATOM
550
CD
ARG A
73
72.948
33.169
11.090
1.00
48.88
C


ATOM
551
NE
ARG A
73
72.151
32.162
10.401
1.00
53.31
N


ATOM
552
CZ
ARG A
73
71.960
32.126
9.084
1.00
55.75
C


ATOM
553
NH1
ARG A
73
72.509
33.049
8.300
1.00
56.63
N


ATOM
554
NH2
ARG A
73
71.216
31.166
8.549
1.00
56.55
N


ATOM
555
N
GLU A
74
74.676
36.281
15.488
1.00
40.14
N


ATOM
556
CA
GLU A
74
75.819
37.003
16.025
1.00
38.77
C


ATOM
557
C
GLU A
74
75.711
37.229
17.531
1.00
36.73
C


ATOM
558
O
GLU A
74
76.634
37.750
18.144
1.00
37.21
O


ATOM
559
CB
GLU A
74
75.979
38.347
15.310
1.00
40.15
C


ATOM
560
CG
GLU A
74
76.113
38.239
13.796
1.00
42.93
C


ATOM
561
CD
GLU A
74
77.234
37.301
13.357
1.00
44.79
C


ATOM
562
OE1
GLU A
74
78.397
37.518
13.762
1.00
47.17
O


ATOM
563
OE2
GLU A
74
76.948
36.347
12.601
1.00
46.07
O


ATOM
564
N
GLY A
75
74.586
36.851
18.127
1.00
35.85
N


ATOM
565
CA
GLY A
75
74.436
37.026
19.562
1.00
35.85
C


ATOM
566
C
GLY A
75
73.429
38.056
20.044
1.00
35.01
C


ATOM
567
O
GLY A
75
73.169
38.148
21.243
1.00
34.48
O


ATOM
568
N
GLY A
76
72.875
38.840
19.126
1.00
34.39
N


ATOM
569
CA
GLY A
76
71.887
39.834
19.513
1.00
33.62
C


ATOM
570
C
GLY A
76
70.483
39.299
19.281
1.00
32.89
C


ATOM
571
O
GLY A
76
70.315
38.101
19.025
1.00
32.03
O


ATOM
572
N
ILE A
77
69.475
40.165
19.374
1.00
31.21
N


ATOM
573
CA
ILE A
77
68.096
39.735
19.151
1.00
31.46
C


ATOM
574
C
ILE A
77
67.282
40.820
18.439
1.00
32.84
C


ATOM
575
O
ILE A
77
67.531
42.021
18.611
1.00
31.99
O


ATOM
576
CB
ILE A
77
67.400
39.369
20.484
1.00
30.05
C


ATOM
577
CG1
ILE A
77
66.190
38.470
20.213
1.00
29.38
C


ATOM
578
CG2
ILE A
77
66.954
40.644
21.220
1.00
27.82
C


ATOM
579
CD1
ILE A
77
65.442
38.047
21.474
1.00
26.08
C


ATOM
580
N
SER A
78
66.312
40.390
17.637
1.00
32.97
N


ATOM
581
CA
SER A
78
65.456
41.317
16.904
1.00
32.44
C


ATOM
582
C
SER A
78
64.049
41.320
17.472
1.00
32.06
C


ATOM
583
O
SER A
78
63.592
40.322
18.016
1.00
34.00
O


ATOM
584
CB
SER A
78
65.382
40.930
15.424
1.00
30.67
C


ATOM
585
OG
SER A
78
66.616
41.134
14.768
1.00
30.87
O


ATOM
586
N
PHE A
79
63.369
42.453
17.351
1.00
32.02
N


ATOM
587
CA
PHE A
79
61.998
42.562
17.816
1.00
31.78
C


ATOM
588
C
PHE A
79
61.105
42.740
16.596
1.00
31.81
C


ATOM
589
O
PHE A
79
60.896
43.854
16.130
1.00
33.21
O


ATOM
590
CB
PHE A
79
61.830
43.747
18.780
1.00
30.40
C


ATOM
591
CG
PHE A
79
62.408
43.500
20.145
1.00
29.75
C


ATOM
592
CD1
PHE A
79
63.754
43.732
20.401
1.00
31.91
C


ATOM
593
CD2
PHE A
79
61.611
42.994
21.169
1.00
30.82
C


ATOM
594
CE1
PHE A
79
64.302
43.462
21.663
1.00
32.55
C


ATOM
595
CE2
PHE A
79
62.145
42.719
22.428
1.00
29.78
C


ATOM
596
CZ
PHE A
79
63.490
42.953
22.676
1.00
30.40
C


ATOM
597
N
ILE A
80
60.603
41.628
16.071
1.00
32.06
N


ATOM
598
CA
ILE A
80
59.726
41.651
14.902
1.00
32.86
C


ATOM
599
C
ILE A
80
58.677
42.748
15.075
1.00
32.33
C


ATOM
600
O
ILE A
80
57.963
42.781
16.084
1.00
32.22
O


ATOM
601
CB
ILE A
80
59.015
40.282
14.717
1.00
32.80
C


ATOM
602
CG1
ILE A
80
60.056
39.175
14.529
1.00
33.69
C


ATOM
603
CG2
ILE A
80
58.082
40.329
13.508
1.00
35.09
C


ATOM
604
CD1
ILE A
80
60.974
39.387
13.347
1.00
32.85
C


ATOM
605
N
PHE A
81
58.581
43.643
14.095
1.00
32.37
N


ATOM
606
CA
PHE A
81
57.627
44.740
14.186
1.00
33.33
C


ATOM
607
C
PHE A
81
56.188
44.274
14.368
1.00
34.02
C


ATOM
608
O
PHE A
81
55.771
43.271
13.792
1.00
33.19
O


ATOM
609
CB
PHE A
81
57.731
45.676
12.966
1.00
33.82
C


ATOM
610
CG
PHE A
81
57.438
45.016
11.643
1.00
34.92
C


ATOM
611
CD1
PHE A
81
58.376
44.191
11.033
1.00
35.21
C


ATOM
612
CD2
PHE A
81
56.224
45.241
10.995
1.00
36.11
C


ATOM
613
CE1
PHE A
81
58.113
43.600
9.791
1.00
34.85
C


ATOM
614
CE2
PHE A
81
55.947
44.658
9.756
1.00
36.53
C


ATOM
615
CZ
PHE A
81
56.895
43.836
9.153
1.00
36.94
C


ATOM
616
N
GLY A
82
55.441
45.014
15.184
1.00
33.59
N


ATOM
617
CA
GLY A
82
54.055
44.675
15.439
1.00
34.64
C


ATOM
618
C
GLY A
82
53.078
45.472
14.596
1.00
35.83
C


ATOM
619
O
GLY A
82
51.870
45.283
14.708
1.00
36.22
O


ATOM
620
N
SER A
83
53.594
46.363
13.753
1.00
35.37
N


ATOM
621
CA
SER A
83
52.744
47.173
12.886
1.00
35.72
C


ATOM
622
C
SER A
83
52.379
46.393
11.618
1.00
36.39
C


ATOM
623
O
SER A
83
52.701
46.791
10.496
1.00
35.68
O


ATOM
624
CB
SER A
83
53.456
48.476
12.522
1.00
34.36
C


ATOM
625
OG
SER A
83
54.710
48.208
11.928
1.00
35.50
O


ATOM
626
N
GLN A
84
51.714
45.264
11.826
1.00
37.28
N


ATOM
627
CA
GLN A
84
51.270
44.387
10.753
1.00
38.09
C


ATOM
628
C
GLN A
84
50.229
43.474
11.394
1.00
38.74
C


ATOM
629
O
GLN A
84
50.021
43.542
12.604
1.00
37.63
O


ATOM
630
CB
GLN A
84
52.445
43.569
10.214
1.00
39.17
C


ATOM
631
CG
GLN A
84
53.074
42.636
11.235
1.00
40.30
C


ATOM
632
CD
GLN A
84
54.255
41.877
10.668
1.00
43.44
C


ATOM
633
OE1
GLN A
84
54.155
41.259
9.607
1.00
45.87
O


ATOM
634
NE2
GLN A
84
55.383
41.912
11.375
1.00
43.38
N


ATOM
635
N
SER A
85
49.577
42.626
10.605
1.00
39.77
N


ATOM
636
CA
SER A
85
48.556
41.739
11.163
1.00
40.71
C


ATOM
637
C
SER A
85
49.138
40.766
12.182
1.00
41.13
C


ATOM
638
O
SER A
85
50.301
40.373
12.088
1.00
41.44
O


ATOM
639
CB
SER A
85
47.868
40.938
10.055
1.00
40.69
C


ATOM
640
OG
SER A
85
48.608
39.771
9.743
1.00
41.94
O


ATOM
641
N
ILE A
86
48.314
40.377
13.150
1.00
41.34
N


ATOM
642
CA
ILE A
86
48.721
39.437
14.187
1.00
43.32
C


ATOM
643
C
ILE A
86
49.213
38.134
13.552
1.00
45.69
C


ATOM
644
O
ILE A
86
50.207
37.550
13.992
1.00
45.58
O


ATOM
645
CB
ILE A
86
47.540
39.117
15.132
1.00
42.04
C


ATOM
646
CG1
ILE A
86
47.139
40.379
15.904
1.00
42.78
C


ATOM
647
CG2
ILE A
86
47.913
37.986
16.075
1.00
40.93
C


ATOM
648
CD1
ILE A
86
45.948
40.191
16.833
1.00
40.98
C


ATOM
649
N
GLU A
87
48.511
37.690
12.513
1.00
46.91
N


ATOM
650
CA
GLU A
87
48.860
36.460
11.809
1.00
48.52
C


ATOM
651
C
GLU A
87
50.201
36.612
11.104
1.00
46.94
C


ATOM
652
O
GLU A
87
51.025
35.700
11.098
1.00
47.16
O


ATOM
653
CB
GLU A
87
47.784
36.117
10.767
1.00
50.61
C


ATOM
654
CG
GLU A
87
46.364
35.944
11.318
1.00
54.49
C


ATOM
655
CD
GLU A
87
45.799
37.214
11.955
1.00
57.21
C


ATOM
656
OE1
GLU A
87
45.896
38.300
11.337
1.00
57.37
O


ATOM
657
OE2
GLU A
87
45.241
37.121
13.074
1.00
59.49
O


ATOM
658
N
SER A
88
50.408
37.778
10.508
1.00
46.26
N


ATOM
659
CA
SER A
88
51.637
38.064
9.778
1.00
45.86
C


ATOM
660
C
SER A
88
52.865
38.124
10.692
1.00
44.29
C


ATOM
661
O
SER A
88
53.921
37.584
10.363
1.00
43.79
O


ATOM
662
CB
SER A
88
51.480
39.384
9.024
1.00
46.24
C


ATOM
663
OG
SER A
88
52.551
39.587
8.126
1.00
50.64
O


ATOM
664
N
GLN A
89
52.725
38.781
11.838
1.00
42.05
N


ATOM
665
CA
GLN A
89
53.831
38.902
12.784
1.00
41.12
C


ATOM
666
C
GLN A
89
54.164
37.534
13.378
1.00
40.97
C


ATOM
667
O
GLN A
89
55.331
37.147
13.464
1.00
41.60
O


ATOM
668
CB
GLN A
89
53.474
39.895
13.904
1.00
37.36
C


ATOM
669
CG
GLN A
89
54.563
40.076
14.967
1.00
34.71
C


ATOM
670
CD
GLN A
89
54.182
41.087
16.042
1.00
32.75
C


ATOM
671
OE1
GLN A
89
53.004
41.260
16.354
1.00
29.71
O


ATOM
672
NE2
GLN A
89
55.183
41.740
16.630
1.00
30.65
N


ATOM
673
N
ALA A
90
53.132
36.798
13.778
1.00
41.05
N


ATOM
674
CA
ALA A
90
53.326
35.478
14.363
1.00
40.85
C


ATOM
675
C
ALA A
90
54.027
34.536
13.386
1.00
40.83
C


ATOM
676
O
ALA A
90
54.828
33.697
13.790
1.00
42.16
O


ATOM
677
CB
ALA A
90
51.988
34.896
14.790
1.00
40.56
C


ATOM
678
N
ALA A
91
53.733
34.676
12.099
1.00
40.30
N


ATOM
679
CA
ALA A
91
54.364
33.822
11.106
1.00
41.24
C


ATOM
680
C
ALA A
91
55.873
34.065
11.106
1.00
41.52
C


ATOM
681
O
ALA A
91
56.661
33.124
11.032
1.00
42.19
O


ATOM
682
CB
ALA A
91
53.776
34.092
9.714
1.00
38.85
C


ATOM
683
N
MET A
92
56.278
35.327
11.192
1.00
41.97
N


ATOM
684
CA
MET A
92
57.702
35.651
11.208
1.00
42.09
C


ATOM
685
C
MET A
92
58.386
35.064
12.438
1.00
41.02
C


ATOM
686
O
MET A
92
59.513
34.579
12.360
1.00
40.61
O


ATOM
687
CB
MET A
92
57.910
37.165
11.181
1.00
42.37
C


ATOM
688
CG
MET A
92
57.542
37.806
9.867
1.00
41.26
C


ATOM
689
SD
MET A
92
57.939
39.549
9.851
1.00
41.37
S


ATOM
690
CE
MET A
92
56.946
40.100
8.458
1.00
41.08
C


ATOM
691
N
VAL A
93
57.702
35.116
13.574
1.00
41.53
N


ATOM
692
CA
VAL A
93
58.256
34.578
14.808
1.00
41.04
C


ATOM
693
C
VAL A
93
58.434
33.077
14.645
1.00
42.35
C


ATOM
694
O
VAL A
93
59.480
32.524
14.979
1.00
42.28
O


ATOM
695
CB
VAL A
93
57.325
34.857
16.004
1.00
41.44
C


ATOM
696
CG1
VAL A
93
57.777
34.058
17.222
1.00
39.20
C


ATOM
697
CG2
VAL A
93
57.324
36.350
16.315
1.00
39.63
C


ATOM
698
N
HIS A
94
57.401
32.426
14.119
1.00
43.29
N


ATOM
699
CA
HIS A
94
57.421
30.984
13.898
1.00
43.16
C


ATOM
700
C
HIS A
94
58.579
30.600
12.982
1.00
42.12
C


ATOM
701
O
HIS A
94
59.320
29.657
13.261
1.00
41.10
O


ATOM
702
CB
HIS A
94
56.100
30.538
13.263
1.00
45.51
C


ATOM
703
CG
HIS A
94
55.983
29.056
13.087
1.00
46.61
C


ATOM
704
ND1
HIS A
94
55.628
28.210
14.116
1.00
46.66
N


ATOM
705
CD2
HIS A
94
56.193
28.268
12.006
1.00
46.86
C


ATOM
706
CE1
HIS A
94
55.624
26.965
13.677
1.00
46.63
C


ATOM
707
NE2
HIS A
94
55.964
26.972
12.400
1.00
47.89
N


ATOM
708
N
ALA A
95
58.727
31.339
11.888
1.00
41.47
N


ATOM
709
CA
ALA A
95
59.788
31.080
10.921
1.00
41.48
C


ATOM
710
C
ALA A
95
61.168
31.132
11.567
1.00
42.50
C


ATOM
711
O
ALA A
95
62.017
30.282
11.306
1.00
42.88
O


ATOM
712
CB
ALA A
95
59.712
32.088
9.783
1.00
40.24
C


ATOM
713
N
VAL A
96
61.394
32.138
12.407
1.00
42.32
N


ATOM
714
CA
VAL A
96
62.680
32.289
13.074
1.00
40.88
C


ATOM
715
C
VAL A
96
62.923
31.140
14.049
1.00
41.55
C


ATOM
716
O
VAL A
96
64.011
30.566
14.086
1.00
41.75
O


ATOM
717
CB
VAL A
96
62.755
33.635
13.837
1.00
40.31
C


ATOM
718
CG1
VAL A
96
64.044
33.719
14.643
1.00
38.83
C


ATOM
719
CG2
VAL A
96
62.684
34.787
12.849
1.00
40.30
C


ATOM
720
N
LYS A
97
61.897
30.802
14.823
1.00
42.33
N


ATOM
721
CA
LYS A
97
61.989
29.735
15.810
1.00
44.12
C


ATOM
722
C
LYS A
97
62.197
28.349
15.206
1.00
46.23
C


ATOM
723
O
LYS A
97
62.787
27.475
15.843
1.00
46.86
O


ATOM
724
CB
LYS A
97
60.730
29.718
16.686
1.00
43.33
C


ATOM
725
CG
LYS A
97
60.484
31.004
17.471
1.00
42.58
C


ATOM
726
CD
LYS A
97
61.669
31.349
18.374
1.00
40.95
C


ATOM
727
CE
LYS A
97
61.894
30.305
19.461
1.00
39.70
C


ATOM
728
NZ
LYS A
97
63.158
30.559
20.212
1.00
38.22
N


ATOM
729
N
ASN A
98
61.713
28.143
13.985
1.00
48.10
N


ATOM
730
CA
ASN A
98
61.844
26.842
13.338
1.00
51.26
C


ATOM
731
C
ASN A
98
62.675
26.897
12.062
1.00
52.29
C


ATOM
732
O
ASN A
98
62.383
26.192
11.096
1.00
53.51
O


ATOM
733
CB
ASN A
98
60.456
26.274
13.023
1.00
52.57
C


ATOM
734
CG
ASN A
98
59.599
26.102
14.264
1.00
54.13
C


ATOM
735
OD1
ASN A
98
59.898
25.286
15.139
1.00
56.37
O


ATOM
736
ND2
ASN A
98
58.527
26.876
14.349
1.00
55.61
N


ATOM
737
N
PHE A
99
63.713
27.728
12.063
1.00
53.22
N


ATOM
738
CA
PHE A
99
64.579
27.872
10.897
1.00
54.26
C


ATOM
739
C
PHE A
99
65.526
26.686
10.731
1.00
54.80
C


ATOM
740
O
PHE A
99
65.886
26.332
9.611
1.00
54.79
O


ATOM
741
CB
PHE A
99
65.398
29.160
11.005
1.00
53.75
C


ATOM
742
CG
PHE A
99
66.234
29.457
9.786
1.00
54.18
C


ATOM
743
CD1
PHE A
99
65.633
29.777
8.573
1.00
53.83
C


ATOM
744
CD2
PHE A
99
67.624
29.437
9.858
1.00
53.66
C


ATOM
745
CE1
PHE A
99
66.404
30.075
7.447
1.00
53.53
C


ATOM
746
CE2
PHE A
99
68.403
29.732
8.743
1.00
53.55
C


ATOM
747
CZ
PHE A
99
67.792
30.052
7.534
1.00
53.92
C


ATOM
748
N
LYS A
100
65.927
26.078
11.845
1.00
55.84
N


ATOM
749
CA
LYS A
100
66.848
24.940
11.809
1.00
57.08
C


ATOM
750
C
LYS A
100
66.159
23.588
11.633
1.00
58.33
C


ATOM
751
O
LYS A
100
66.811
22.546
11.722
1.00
58.42
O


ATOM
752
CB
LYS A
100
67.691
24.893
13.086
1.00
55.72
C


ATOM
753
CG
LYS A
100
68.611
26.083
13.298
1.00
55.04
C


ATOM
754
CD
LYS A
100
69.353
25.929
14.616
1.00
53.54
C


ATOM
755
CE
LYS A
100
70.352
27.045
14.855
1.00
51.61
C


ATOM
756
NZ
LYS A
100
71.015
26.867
16.172
1.00
50.36
N


ATOM
757
N
ALA A
101
64.850
23.601
11.395
1.00
59.54
N


ATOM
758
CA
ALA A
101
64.095
22.363
11.213
1.00
60.39
C


ATOM
759
C
ALA A
101
64.471
21.672
9.904
1.00
60.69
C


ATOM
760
O
ALA A
101
65.016
22.298
8.995
1.00
60.89
O


ATOM
761
CB
ALA A
101
62.596
22.652
11.237
1.00
60.64
C


ATOM
762
N
HIS A
222
79.198
30.290
16.950
1.00
63.01
N


ATOM
763
CA
HIS A
222
79.815
30.312
18.273
1.00
62.71
C


ATOM
764
C
HIS A
222
79.103
31.282
19.214
1.00
60.87
C


ATOM
765
O
HIS A
222
78.923
30.994
20.399
1.00
60.68
O


ATOM
766
CB
HIS A
222
81.296
30.695
18.167
1.00
65.58
C


ATOM
767
CG
HIS A
222
82.137
29.677
17.460
1.00
69.22
C


ATOM
768
ND1
HIS A
222
82.251
28.373
17.896
1.00
70.94
N


ATOM
769
CD2
HIS A
222
82.903
29.769
16.346
1.00
70.61
C


ATOM
770
CE1
HIS A
222
83.049
27.706
17.080
1.00
71.60
C


ATOM
771
NE2
HIS A
222
83.458
28.530
16.131
1.00
71.43
N


ATOM
772
N
ASN A
223
78.698
32.432
18.686
1.00
57.42
N


ATOM
773
CA
ASN A
223
78.012
33.422
19.503
1.00
55.31
C


ATOM
774
C
ASN A
223
76.518
33.511
19.219
1.00
52.14
C


ATOM
775
O
ASN A
223
75.888
34.525
19.520
1.00
49.94
O


ATOM
776
CB
ASN A
223
78.657
34.797
19.317
1.00
57.68
C


ATOM
777
CG
ASN A
223
79.984
34.925
20.050
1.00
60.74
C


ATOM
778
OD1
ASN A
223
80.713
35.904
19.870
1.00
64.29
O


ATOM
779
ND2
ASN A
223
80.299
33.942
20.890
1.00
61.50
N


ATOM
780
N
GLU A
224
75.948
32.453
18.648
1.00
48.44
N


ATOM
781
CA
GLU A
224
74.520
32.462
18.351
1.00
46.42
C


ATOM
782
C
GLU A
224
73.699
32.516
19.631
1.00
43.23
C


ATOM
783
O
GLU A
224
74.041
31.889
20.631
1.00
42.87
O


ATOM
784
CB
GLU A
224
74.109
31.226
17.538
1.00
47.17
C


ATOM
785
CG
GLU A
224
74.383
29.892
18.217
1.00
49.19
C


ATOM
786
CD
GLU A
224
73.622
28.735
17.581
1.00
50.18
C


ATOM
787
OE1
GLU A
224
73.410
28.755
16.346
1.00
51.65
O


ATOM
788
OE2
GLU A
224
73.246
27.799
18.318
1.00
49.83
O


ATOM
789
N
LEU A
225
72.615
33.279
19.590
1.00
40.90
N


ATOM
790
CA
LEU A
225
71.733
33.410
20.734
1.00
38.88
C


ATOM
791
C
LEU A
225
70.565
32.457
20.516
1.00
38.25
C


ATOM
792
O
LEU A
225
69.747
32.664
19.621
1.00
36.15
O


ATOM
793
CB
LEU A
225
71.232
34.851
20.848
1.00
37.76
C


ATOM
794
CG
LEU A
225
70.380
35.166
22.077
1.00
37.49
C


ATOM
795
CD1
LEU A
225
71.196
34.932
23.340
1.00
37.19
C


ATOM
796
CD2
LEU A
225
69.898
36.602
22.007
1.00
36.97
C


ATOM
797
N
VAL A
226
70.492
31.416
21.341
1.00
38.35
N


ATOM
798
CA
VAL A
226
69.435
30.415
21.215
1.00
39.11
C


ATOM
799
C
VAL A
226
68.830
29.993
22.551
1.00
40.13
C


ATOM
800
O
VAL A
226
69.337
30.345
23.617
1.00
40.81
O


ATOM
801
CB
VAL A
226
69.969
29.133
20.533
1.00
38.58
C


ATOM
802
CG1
VAL A
226
70.373
29.420
19.094
1.00
35.25
C


ATOM
803
CG2
VAL A
226
71.154
28.595
21.326
1.00
38.53
C


ATOM
804
N
ASP A
227
67.737
29.237
22.475
1.00
40.83
N


ATOM
805
CA
ASP A
227
67.067
28.728
23.661
1.00
41.94
C


ATOM
806
C
ASP A
227
67.601
27.323
23.970
1.00
43.67
C


ATOM
807
O
ASP A
227
68.501
26.828
23.288
1.00
43.28
O


ATOM
808
CB
ASP A
227
65.545
28.679
23.452
1.00
42.33
C


ATOM
809
CG
ASP A
227
65.139
27.889
22.210
1.00
42.71
C


ATOM
810
OD1
ASP A
227
65.753
26.838
21.924
1.00
43.47
O


ATOM
811
OD2
ASP A
227
64.185
28.314
21.525
1.00
40.79
O


ATOM
812
N
SER A
228
67.036
26.681
24.990
1.00
46.46
N


ATOM
813
CA
SER A
228
67.467
25.342
25.395
1.00
48.86
C


ATOM
814
C
SER A
228
67.336
24.291
24.287
1.00
50.18
C


ATOM
815
O
SER A
228
67.953
23.226
24.358
1.00
50.85
O


ATOM
816
CB
SER A
228
66.682
24.891
26.631
1.00
48.09
C


ATOM
817
OG
SER A
228
65.289
24.897
26.378
1.00
49.20
O


ATOM
818
N
GLN A
229
66.537
24.596
23.268
1.00
50.81
N


ATOM
819
CA
GLN A
229
66.331
23.685
22.148
1.00
51.37
C


ATOM
820
C
GLN A
229
67.229
24.081
20.984
1.00
50.93
C


ATOM
821
O
GLN A
229
67.103
23.548
19.878
1.00
49.76
O


ATOM
822
CB
GLN A
229
64.865
23.723
21.699
1.00
53.18
C


ATOM
823
CG
GLN A
229
63.873
23.346
22.784
1.00
55.38
C


ATOM
824
CD
GLN A
229
62.434
23.565
22.353
1.00
58.59
C


ATOM
825
OE1
GLN A
229
61.971
22.979
21.369
1.00
60.22
O


ATOM
826
NE2
GLN A
229
61.716
24.413
23.087
1.00
58.58
N


ATOM
827
N
LYS A
230
68.131
25.026
21.242
1.00
50.37
N


ATOM
828
CA
LYS A
230
69.065
25.515
20.231
1.00
48.94
C


ATOM
829
C
LYS A
230
68.407
26.325
19.116
1.00
46.73
C


ATOM
830
O
LYS A
230
68.991
26.513
18.048
1.00
47.20
O


ATOM
831
CB
LYS A
230
69.856
24.349
19.626
1.00
51.73
C


ATOM
832
CG
LYS A
230
70.992
23.825
20.507
1.00
54.62
C


ATOM
833
CD
LYS A
230
72.073
24.889
20.705
1.00
57.67
C


ATOM
834
CE
LYS A
230
73.357
24.307
21.302
1.00
59.53
C


ATOM
835
NZ
LYS A
230
73.161
23.692
22.653
1.00
59.91
N


ATOM
836
N
ARG A
231
67.195
26.811
19.362
1.00
45.43
N


ATOM
837
CA
ARG A
231
66.494
27.621
18.368
1.00
43.78
C


ATOM
838
C
ARG A
231
66.851
29.087
18.595
1.00
41.98
C


ATOM
839
O
ARG A
231
67.013
29.524
19.735
1.00
40.65
O


ATOM
840
CB
ARG A
231
64.979
27.445
18.495
1.00
45.11
C


ATOM
841
CG
ARG A
231
64.494
26.006
18.362
1.00
46.09
C


ATOM
842
CD
ARG A
231
62.990
25.927
18.557
1.00
47.94
C


ATOM
843
NE
ARG A
231
62.587
26.465
19.854
1.00
49.46
N


ATOM
844
CZ
ARG A
231
61.326
26.555
20.273
1.00
52.08
C


ATOM
845
NH1
ARG A
231
60.328
26.144
19.498
1.00
50.02
N


ATOM
846
NH2
ARG A
231
61.063
27.058
21.476
1.00
53.40
N


ATOM
847
N
TYR A
232
66.981
29.841
17.510
1.00
40.54
N


ATOM
848
CA
TYR A
232
67.312
31.253
17.607
1.00
38.76
C


ATOM
849
C
TYR A
232
66.284
32.005
18.451
1.00
38.33
C


ATOM
850
O
TYR A
232
65.086
31.706
18.418
1.00
37.07
O


ATOM
851
CB
TYR A
232
67.377
31.882
16.217
1.00
39.12
C


ATOM
852
CG
TYR A
232
68.502
31.363
15.353
1.00
41.29
C


ATOM
853
CD1
TYR A
232
69.821
31.371
15.809
1.00
41.57
C


ATOM
854
CD2
TYR A
232
68.253
30.883
14.070
1.00
41.51
C


ATOM
855
CE1
TYR A
232
70.867
30.915
15.002
1.00
43.44
C


ATOM
856
CE2
TYR A
232
69.288
30.425
13.257
1.00
44.33
C


ATOM
857
CZ
TYR A
232
70.591
30.444
13.727
1.00
44.76
C


ATOM
858
OH
TYR A
232
71.612
30.003
12.913
1.00
47.05
O


ATOM
859
N
LEU A
233
66.764
32.970
19.228
1.00
36.38
N


ATOM
860
CA
LEU A
233
65.879
33.775
20.052
1.00
35.39
C


ATOM
861
C
LEU A
233
65.296
34.876
19.176
1.00
33.69
C


ATOM
862
O
LEU A
233
65.937
35.338
18.230
1.00
33.90
O


ATOM
863
CB
LEU A
233
66.650
34.390
21.226
1.00
35.98
C


ATOM
864
CG
LEU A
233
66.395
33.765
22.602
1.00
39.07
C


ATOM
865
CD1
LEU A
233
66.503
32.252
22.519
1.00
37.64
C


ATOM
866
CD2
LEU A
233
67.384
34.325
23.616
1.00
38.75
C


ATOM
867
N
VAL A
234
64.072
35.279
19.475
1.00
32.47
N


ATOM
868
CA
VAL A
234
63.433
36.334
18.710
1.00
31.96
C


ATOM
869
C
VAL A
234
62.465
37.080
19.613
1.00
31.91
C


ATOM
870
O
VAL A
234
61.883
36.502
20.529
1.00
31.40
O


ATOM
871
CB
VAL A
234
62.676
35.767
17.476
1.00
31.95
C


ATOM
872
CG1
VAL A
234
61.402
35.048
17.913
1.00
29.55
C


ATOM
873
CG2
VAL A
234
62.371
36.888
16.498
1.00
29.80
C


ATOM
874
N
GLY A
235
62.319
38.375
19.366
1.00
32.16
N


ATOM
875
CA
GLY A
235
61.416
39.174
20.163
1.00
31.96
C


ATOM
876
C
GLY A
235
60.308
39.689
19.277
1.00
32.19
C


ATOM
877
O
GLY A
235
60.396
39.604
18.050
1.00
32.58
O


ATOM
878
N
ALA A
236
59.259
40.225
19.886
1.00
31.00
N


ATOM
879
CA
ALA A
236
58.154
40.746
19.109
1.00
31.50
C


ATOM
880
C
ALA A
236
57.535
41.973
19.766
1.00
30.43
C


ATOM
881
O
ALA A
236
57.275
41.981
20.965
1.00
32.80
O


ATOM
882
CB
ALA A
236
57.095
39.653
18.911
1.00
32.43
C


ATOM
883
N
GLY A
237
57.311
43.013
18.973
1.00
30.90
N


ATOM
884
CA
GLY A
237
56.710
44.218
19.504
1.00
32.34
C


ATOM
885
C
GLY A
237
55.206
44.067
19.618
1.00
32.69
C


ATOM
886
O
GLY A
237
54.595
43.345
18.837
1.00
34.22
O


ATOM
887
N
ILE A
238
54.607
44.723
20.606
1.00
32.45
N


ATOM
888
CA
ILE A
238
53.161
44.668
20.774
1.00
32.44
C


ATOM
889
C
ILE A
238
52.646
46.077
21.074
1.00
32.79
C


ATOM
890
O
ILE A
238
53.422
46.976
21.400
1.00
32.08
O


ATOM
891
CB
ILE A
238
52.739
43.709
21.927
1.00
33.39
C


ATOM
892
CG1
ILE A
238
53.212
44.253
23.278
1.00
34.02
C


ATOM
893
CG2
ILE A
238
53.309
42.320
21.686
1.00
32.20
C


ATOM
894
CD1
ILE A
238
52.721
43.433
24.483
1.00
32.19
C


ATOM
895
N
ASN A
239
51.341
46.276
20.946
1.00
32.14
N


ATOM
896
CA
ASN A
239
50.768
47.579
21.221
1.00
31.92
C


ATOM
897
C
ASN A
239
49.769
47.462
22.358
1.00
33.41
C


ATOM
898
O
ASN A
239
49.391
46.357
22.759
1.00
32.91
O


ATOM
899
CB
ASN A
239
50.111
48.161
19.958
1.00
32.71
C


ATOM
900
CG
ASN A
239
48.978
47.300
19.428
1.00
32.73
C


ATOM
901
OD1
ASN A
239
47.941
47.162
20.070
1.00
33.18
O


ATOM
902
ND2
ASN A
239
49.175
46.717
18.249
1.00
31.34
N


ATOM
903
N
THR A
240
49.351
48.608
22.878
1.00
34.02
N


ATOM
904
CA
THR A
240
48.414
48.658
23.989
1.00
35.67
C


ATOM
905
C
THR A
240
46.949
48.476
23.596
1.00
36.91
C


ATOM
906
O
THR A
240
46.061
48.629
24.435
1.00
35.65
O


ATOM
907
CB
THR A
240
48.555
49.995
24.739
1.00
34.88
C


ATOM
908
OG1
THR A
240
48.330
51.074
23.823
1.00
34.88
O


ATOM
909
CG2
THR A
240
49.952
50.125
25.343
1.00
33.05
C


ATOM
910
N
ARG A
241
46.691
48.135
22.338
1.00
39.01
N


ATOM
911
CA
ARG A
241
45.312
47.972
21.889
1.00
43.02
C


ATOM
912
C
ARG A
241
44.821
46.538
21.708
1.00
42.60
C


ATOM
913
O
ARG A
241
43.926
46.093
22.429
1.00
41.68
O


ATOM
914
CB
ARG A
241
45.087
48.752
20.588
1.00
46.62
C


ATOM
915
CG
ARG A
241
43.702
48.546
19.976
1.00
52.95
C


ATOM
916
CD
ARG A
241
43.469
49.420
18.740
1.00
57.47
C


ATOM
917
NE
ARG A
241
42.889
50.725
19.069
1.00
61.95
N


ATOM
918
CZ
ARG A
241
43.504
51.681
19.763
1.00
63.53
C


ATOM
919
NH1
ARG A
241
44.738
51.496
20.218
1.00
64.10
N


ATOM
920
NH2
ARG A
241
42.883
52.831
19.999
1.00
63.47
N


ATOM
921
N
ASP A
242
45.396
45.820
20.748
1.00
42.26
N


ATOM
922
CA
ASP A
242
44.974
44.450
20.473
1.00
43.86
C


ATOM
923
C
ASP A
242
45.832
43.360
21.119
1.00
43.63
C


ATOM
924
O
ASP A
242
45.930
42.258
20.585
1.00
44.69
O


ATOM
925
CB
ASP A
242
44.930
44.214
18.957
1.00
43.42
C


ATOM
926
CG
ASP A
242
46.295
44.361
18.295
1.00
45.14
C


ATOM
927
OD1
ASP A
242
47.320
44.022
18.931
1.00
44.30
O


ATOM
928
OD2
ASP A
242
46.344
44.799
17.123
1.00
45.01
O


ATOM
929
N
PHE A
243
46.433
43.655
22.266
1.00
43.34
N


ATOM
930
CA
PHE A
243
47.298
42.686
22.939
1.00
43.11
C


ATOM
931
C
PHE A
243
46.612
41.409
23.434
1.00
43.36
C


ATOM
932
O
PHE A
243
47.244
40.354
23.504
1.00
43.21
O


ATOM
933
CB
PHE A
243
48.043
43.368
24.097
1.00
40.53
C


ATOM
934
CG
PHE A
243
47.147
43.890
25.179
1.00
38.93
C


ATOM
935
CD1
PHE A
243
46.662
43.042
26.170
1.00
38.45
C


ATOM
936
CD2
PHE A
243
46.795
45.236
25.216
1.00
38.69
C


ATOM
937
CE1
PHE A
243
45.842
43.524
27.185
1.00
38.00
C


ATOM
938
CE2
PHE A
243
45.974
45.731
26.226
1.00
38.21
C


ATOM
939
CZ
PHE A
243
45.497
44.872
27.215
1.00
38.78
C


ATOM
940
N
ARG A
244
45.328
41.497
23.772
1.00
43.84
N


ATOM
941
CA
ARG A
244
44.598
40.325
24.253
1.00
44.76
C


ATOM
942
C
ARG A
244
44.549
39.225
23.197
1.00
44.01
C


ATOM
943
O
ARG A
244
44.455
38.047
23.526
1.00
44.85
O


ATOM
944
CB
ARG A
244
43.176
40.713
24.685
1.00
44.23
C


ATOM
945
CG
ARG A
244
43.148
41.654
25.880
1.00
43.24
C


ATOM
946
CD
ARG A
244
41.735
41.931
26.362
1.00
44.43
C


ATOM
947
NE
ARG A
244
41.721
42.938
27.420
1.00
45.36
N


ATOM
948
CZ
ARG A
244
41.970
44.231
27.224
1.00
46.55
C


ATOM
949
NH1
ARG A
244
42.247
44.678
26.003
1.00
44.24
N


ATOM
950
NH2
ARG A
244
41.953
45.077
28.248
1.00
45.03
N


ATOM
951
N
GLU A
245
44.614
39.610
21.929
1.00
44.30
N


ATOM
952
CA
GLU A
245
44.599
38.634
20.849
1.00
45.31
C


ATOM
953
C
GLU A
245
46.001
38.448
20.275
1.00
44.68
C


ATOM
954
O
GLU A
245
46.363
37.358
19.826
1.00
44.64
O


ATOM
955
CB
GLU A
245
43.640
39.071
19.733
1.00
48.37
C


ATOM
956
CG
GLU A
245
42.153
38.931
20.084
1.00
53.41
C


ATOM
957
CD
GLU A
245
41.647
39.993
21.059
1.00
57.52
C


ATOM
958
OE1
GLU A
245
40.635
39.725
21.746
1.00
59.50
O


ATOM
959
OE2
GLU A
245
42.239
41.099
21.132
1.00
59.64
O


ATOM
960
N
ARG A
246
46.794
39.514
20.309
1.00
42.77
N


ATOM
961
CA
ARG A
246
48.152
39.479
19.771
1.00
41.08
C


ATOM
962
C
ARG A
246
49.163
38.714
20.629
1.00
39.13
C


ATOM
963
O
ARG A
246
49.964
37.944
20.111
1.00
37.89
O


ATOM
964
CB
ARG A
246
48.649
40.907
19.553
1.00
42.28
C


ATOM
965
CG
ARG A
246
49.936
40.997
18.770
1.00
44.41
C


ATOM
966
CD
ARG A
246
50.355
42.442
18.584
1.00
46.22
C


ATOM
967
NE
ARG A
246
50.638
42.723
17.185
1.00
50.24
N


ATOM
968
CZ
ARG A
246
49.723
43.062
16.287
1.00
48.88
C


ATOM
969
NH1
ARG A
246
48.454
43.175
16.638
1.00
51.93
N


ATOM
970
NH2
ARG A
246
50.076
43.269
15.031
1.00
50.28
N


ATOM
971
N
VAL A
247
49.134
38.928
21.939
1.00
37.97
N


ATOM
972
CA
VAL A
247
50.075
38.246
22.822
1.00
38.70
C


ATOM
973
C
VAL A
247
49.977
36.716
22.746
1.00
39.69
C


ATOM
974
O
VAL A
247
50.980
36.041
22.499
1.00
40.53
O


ATOM
975
CB
VAL A
247
49.901
38.717
24.285
1.00
36.45
C


ATOM
976
CG1
VAL A
247
50.735
37.867
25.217
1.00
35.80
C


ATOM
977
CG2
VAL A
247
50.315
40.184
24.402
1.00
36.49
C


ATOM
978
N
PRO A
248
48.770
36.148
22.955
1.00
39.79
N


ATOM
979
CA
PRO A
248
48.615
34.688
22.895
1.00
38.65
C


ATOM
980
C
PRO A
248
49.149
34.104
21.588
1.00
37.90
C


ATOM
981
O
PRO A
248
49.773
33.044
21.579
1.00
38.24
O


ATOM
982
CB
PRO A
248
47.107
34.498
23.050
1.00
40.03
C


ATOM
983
CG
PRO A
248
46.727
35.633
23.951
1.00
39.42
C


ATOM
984
CD
PRO A
248
47.499
36.790
23.340
1.00
37.60
C


ATOM
985
N
ALA A
249
48.905
34.808
20.488
1.00
38.13
N


ATOM
986
CA
ALA A
249
49.369
34.372
19.178
1.00
38.44
C


ATOM
987
C
ALA A
249
50.899
34.403
19.100
1.00
40.66
C


ATOM
988
O
ALA A
249
51.519
33.508
18.505
1.00
40.90
O


ATOM
989
CB
ALA A
249
48.777
35.257
18.103
1.00
38.28
C


ATOM
990
N
LEU A
250
51.502
35.433
19.698
1.00
39.69
N


ATOM
991
CA
LEU A
250
52.956
35.570
19.699
1.00
39.26
C


ATOM
992
C
LEU A
250
53.585
34.501
20.587
1.00
39.24
C


ATOM
993
O
LEU A
250
54.600
33.908
20.232
1.00
38.60
O


ATOM
994
CB
LEU A
250
53.357
36.974
20.176
1.00
39.22
C


ATOM
995
CG
LEU A
250
53.642
38.057
19.119
1.00
39.75
C


ATOM
996
CD1
LEU A
250
53.046
37.699
17.772
1.00
37.78
C


ATOM
997
CD2
LEU A
250
53.099
39.387
19.610
1.00
39.06
C


ATOM
998
N
VAL A
251
52.974
34.256
21.740
1.00
40.54
N


ATOM
999
CA
VAL A
251
53.469
33.243
22.665
1.00
42.59
C


ATOM
1000
C
VAL A
251
53.413
31.878
21.985
1.00
43.82
C


ATOM
1001
O
VAL A
251
54.406
31.153
21.942
1.00
43.85
O


ATOM
1002
CB
VAL A
251
52.616
33.201
23.946
1.00
42.12
C


ATOM
1003
CG1
VAL A
251
53.101
32.088
24.865
1.00
43.50
C


ATOM
1004
CG2
VAL A
251
52.691
34.543
24.653
1.00
44.13
C


ATOM
1005
N
GLU A
252
52.243
31.537
21.451
1.00
45.33
N


ATOM
1006
CA
GLU A
252
52.055
30.268
20.759
1.00
46.43
C


ATOM
1007
C
GLU A
252
53.068
30.096
19.629
1.00
44.48
C


ATOM
1008
O
GLU A
252
53.568
28.996
19.398
1.00
44.67
O


ATOM
1009
CB
GLU A
252
50.634
30.172
20.183
1.00
49.48
C


ATOM
1010
CG
GLU A
252
49.629
29.457
21.081
1.00
55.40
C


ATOM
1011
CD
GLU A
252
49.072
30.334
22.188
1.00
57.85
C


ATOM
1012
OE1
GLU A
252
47.945
30.858
22.029
1.00
57.96
O


ATOM
1013
OE2
GLU A
252
49.762
30.500
23.216
1.00
60.59
O


ATOM
1014
N
ALA A
253
53.363
31.183
18.923
1.00
41.46
N


ATOM
1015
CA
ALA A
253
54.315
31.135
17.820
1.00
39.92
C


ATOM
1016
C
ALA A
253
55.748
30.896
18.306
1.00
39.79
C


ATOM
1017
O
ALA A
253
56.638
30.587
17.509
1.00
39.66
O


ATOM
1018
CB
ALA A
253
54.239
32.421
17.009
1.00
38.59
C


ATOM
1019
N
GLY A
254
55.971
31.046
19.609
1.00
38.49
N


ATOM
1020
CA
GLY A
254
57.297
30.813
20.156
1.00
40.23
C


ATOM
1021
C
GLY A
254
58.139
32.043
20.472
1.00
39.89
C


ATOM
1022
O
GLY A
254
59.355
31.936
20.619
1.00
39.63
O


ATOM
1023
N
ALA A
255
57.506
33.207
20.575
1.00
39.17
N


ATOM
1024
CA
ALA A
255
58.232
34.432
20.888
1.00
38.09
C


ATOM
1025
C
ALA A
255
58.933
34.287
22.238
1.00
36.72
C


ATOM
1026
O
ALA A
255
58.324
33.872
23.223
1.00
35.94
O


ATOM
1027
CB
ALA A
255
57.276
35.612
20.916
1.00
37.70
C


ATOM
1028
N
ASP A
256
60.214
34.634
22.283
1.00
35.80
N


ATOM
1029
CA
ASP A
256
60.977
34.520
23.523
1.00
35.28
C


ATOM
1030
C
ASP A
256
60.809
35.725
24.437
1.00
33.72
C


ATOM
1031
O
ASP A
256
60.921
35.610
25.656
1.00
32.72
O


ATOM
1032
CB
ASP A
256
62.451
34.307
23.199
1.00
34.79
C


ATOM
1033
CG
ASP A
256
62.682
33.041
22.404
1.00
37.41
C


ATOM
1034
OD1
ASP A
256
62.584
31.948
23.003
1.00
38.37
O


ATOM
1035
OD2
ASP A
256
62.944
33.137
21.185
1.00
34.51
O


ATOM
1036
N
VAL A
257
60.538
36.881
23.845
1.00
32.63
N


ATOM
1037
CA
VAL A
257
60.354
38.096
24.625
1.00
32.40
C


ATOM
1038
C
VAL A
257
59.502
39.085
23.845
1.00
31.76
C


ATOM
1039
O
VAL A
257
59.520
39.100
22.617
1.00
32.06
O


ATOM
1040
CB
VAL A
257
61.720
38.748
24.986
1.00
29.73
C


ATOM
1041
CG1
VAL A
257
62.435
39.181
23.730
1.00
30.67
C


ATOM
1042
CG2
VAL A
257
61.514
39.920
25.924
1.00
29.01
C


ATOM
1043
N
LEU A
258
58.749
39.899
24.572
1.00
30.18
N


ATOM
1044
CA
LEU A
258
57.886
40.894
23.957
1.00
31.57
C


ATOM
1045
C
LEU A
258
58.308
42.286
24.405
1.00
31.09
C


ATOM
1046
O
LEU A
258
59.036
42.441
25.384
1.00
31.25
O


ATOM
1047
CB
LEU A
258
56.427
40.665
24.374
1.00
29.78
C


ATOM
1048
CG
LEU A
258
55.852
39.263
24.175
1.00
31.14
C


ATOM
1049
CD1
LEU A
258
54.440
39.223
24.729
1.00
33.95
C


ATOM
1050
CD2
LEU A
258
55.870
38.887
22.696
1.00
30.48
C


ATOM
1051
N
CYS A
259
57.849
43.298
23.680
1.00
31.62
N


ATOM
1052
CA
CYS A
259
58.149
44.675
24.042
1.00
31.37
C


ATOM
1053
C
CYS A
259
57.070
45.613
23.521
1.00
30.31
C


ATOM
1054
O
CYS A
259
56.798
45.650
22.324
1.00
31.18
O


ATOM
1055
CB
CYS A
259
59.503
45.114
23.485
1.00
28.99
C


ATOM
1056
SG
CYS A
259
60.014
46.724
24.132
1.00
29.97
S


ATOM
1057
N
ILE A
260
56.456
46.362
24.428
1.00
30.30
N


ATOM
1058
CA
ILE A
260
55.431
47.317
24.042
1.00
31.13
C


ATOM
1059
C
ILE A
260
56.147
48.408
23.248
1.00
33.06
C


ATOM
1060
O
ILE A
260
57.157
48.959
23.693
1.00
32.27
O


ATOM
1061
CB
ILE A
260
54.752
47.921
25.276
1.00
30.72
C


ATOM
1062
CG1
ILE A
260
54.132
46.796
26.110
1.00
29.75
C


ATOM
1063
CG2
ILE A
260
53.695
48.946
24.851
1.00
27.83
C


ATOM
1064
CD1
ILE A
260
53.567
47.256
27.440
1.00
30.89
C


ATOM
1065
N
ASP A
261
55.620
48.701
22.068
1.00
33.30
N


ATOM
1066
CA
ASP A
261
56.204
49.682
21.172
1.00
34.73
C


ATOM
1067
C
ASP A
261
55.482
51.032
21.222
1.00
35.90
C


ATOM
1068
O
ASP A
261
54.372
51.171
20.706
1.00
37.40
O


ATOM
1069
CB
ASP A
261
56.183
49.090
19.762
1.00
34.92
C


ATOM
1070
CG
ASP A
261
56.704
50.036
18.712
1.00
36.01
C


ATOM
1071
OD1
ASP A
261
57.519
50.924
19.041
1.00
34.62
O


ATOM
1072
OD2
ASP A
261
56.303
49.871
17.541
1.00
37.89
O


ATOM
1073
N
SER A
262
56.117
52.031
21.831
1.00
35.46
N


ATOM
1074
CA
SER A
262
55.504
53.354
21.946
1.00
35.41
C


ATOM
1075
C
SER A
262
56.538
54.453
22.172
1.00
35.72
C


ATOM
1076
O
SER A
262
57.599
54.203
22.748
1.00
35.63
O


ATOM
1077
CB
SER A
262
54.499
53.339
23.101
1.00
35.49
C


ATOM
1078
OG
SER A
262
53.993
54.629
23.377
1.00
35.23
O


ATOM
1079
N
SER A
263
56.240
55.671
21.722
1.00
34.24
N


ATOM
1080
CA
SER A
263
57.183
56.770
21.922
1.00
35.35
C


ATOM
1081
C
SER A
263
57.056
57.337
23.334
1.00
34.38
C


ATOM
1082
O
SER A
263
58.021
57.862
23.886
1.00
36.61
O


ATOM
1083
CB
SER A
263
56.982
57.876
20.873
1.00
35.88
C


ATOM
1084
OG
SER A
263
55.638
58.326
20.822
1.00
39.99
O


ATOM
1085
N
ASP A
264
55.872
57.224
23.925
1.00
31.64
N


ATOM
1086
CA
ASP A
264
55.664
57.707
25.289
1.00
30.91
C


ATOM
1087
C
ASP A
264
55.128
56.564
26.155
1.00
30.07
C


ATOM
1088
O
ASP A
264
53.917
56.353
26.247
1.00
29.83
O


ATOM
1089
CB
ASP A
264
54.692
58.898
25.296
1.00
29.57
C


ATOM
1090
CG
ASP A
264
54.281
59.325
26.706
1.00
29.79
C


ATOM
1091
OD1
ASP A
264
54.945
58.947
27.696
1.00
27.03
O


ATOM
1092
OD2
ASP A
264
53.283
60.057
26.824
1.00
29.07
O


ATOM
1093
N
GLY A
265
56.042
55.838
26.792
1.00
29.18
N


ATOM
1094
CA
GLY A
265
55.659
54.712
27.627
1.00
28.22
C


ATOM
1095
C
GLY A
265
55.158
55.050
29.018
1.00
28.37
C


ATOM
1096
O
GLY A
265
54.689
54.169
29.736
1.00
28.80
O


ATOM
1097
N
PHE A
266
55.258
56.317
29.407
1.00
27.17
N


ATOM
1098
CA
PHE A
266
54.798
56.752
30.721
1.00
28.12
C


ATOM
1099
C
PHE A
266
53.275
56.847
30.584
1.00
29.95
C


ATOM
1100
O
PHE A
266
52.699
57.932
30.598
1.00
29.08
O


ATOM
1101
CB
PHE A
266
55.415
58.117
31.048
1.00
27.00
C


ATOM
1102
CG
PHE A
266
55.483
58.432
32.522
1.00
28.08
C


ATOM
1103
CD1
PHE A
266
54.761
57.684
33.456
1.00
26.54
C


ATOM
1104
CD2
PHE A
266
56.259
59.502
32.973
1.00
25.82
C


ATOM
1105
CE1
PHE A
266
54.810
57.995
34.817
1.00
26.74
C


ATOM
1106
CE2
PHE A
266
56.317
59.827
34.328
1.00
24.90
C


ATOM
1107
CZ
PHE A
266
55.593
59.074
35.257
1.00
27.12
C


ATOM
1108
N
SER A
267
52.636
55.684
30.453
1.00
31.46
N


ATOM
1109
CA
SER A
267
51.194
55.596
30.233
1.00
31.95
C


ATOM
1110
C
SER A
267
50.476
54.513
31.029
1.00
32.94
C


ATOM
1111
O
SER A
267
50.989
53.405
31.218
1.00
32.01
O


ATOM
1112
CB
SER A
267
50.938
55.343
28.746
1.00
31.54
C


ATOM
1113
OG
SER A
267
49.558
55.219
28.462
1.00
34.95
O


ATOM
1114
N
GLU A
268
49.266
54.833
31.466
1.00
33.57
N


ATOM
1115
CA
GLU A
268
48.460
53.887
32.214
1.00
35.39
C


ATOM
1116
C
GLU A
268
48.162
52.711
31.284
1.00
35.05
C


ATOM
1117
O
GLU A
268
47.945
51.589
31.736
1.00
35.30
O


ATOM
1118
CB
GLU A
268
47.159
54.551
32.677
1.00
36.81
C


ATOM
1119
CG
GLU A
268
46.306
53.672
33.576
1.00
41.82
C


ATOM
1120
CD
GLU A
268
45.047
54.369
34.076
1.00
45.55
C


ATOM
1121
OE1
GLU A
268
44.238
53.691
34.753
1.00
47.73
O


ATOM
1122
OE2
GLU A
268
44.864
55.582
33.801
1.00
43.72
O


ATOM
1123
N
TRP A
269
48.166
52.973
29.980
1.00
33.62
N


ATOM
1124
CA
TRP A
269
47.907
51.925
29.002
1.00
35.48
C


ATOM
1125
C
TRP A
269
48.958
50.813
29.063
1.00
34.72
C


ATOM
1126
O
TRP A
269
48.632
49.637
28.873
1.00
35.26
O


ATOM
1127
CB
TRP A
269
47.858
52.502
27.584
1.00
36.38
C


ATOM
1128
CG
TRP A
269
46.659
53.368
27.322
1.00
41.33
C


ATOM
1129
CD1
TRP A
269
46.656
54.711
27.068
1.00
40.88
C


ATOM
1130
CD2
TRP A
269
45.289
52.948
27.272
1.00
42.34
C


ATOM
1131
NE1
TRP A
269
45.372
55.150
26.861
1.00
42.36
N


ATOM
1132
CE2
TRP A
269
44.513
54.090
26.981
1.00
42.40
C


ATOM
1133
CE3
TRP A
269
44.642
51.715
27.445
1.00
43.39
C


ATOM
1134
CZ2
TRP A
269
43.122
54.039
26.858
1.00
44.45
C


ATOM
1135
CZ3
TRP A
269
43.258
51.663
27.322
1.00
44.28
C


ATOM
1136
CH2
TRP A
269
42.514
52.821
27.031
1.00
44.95
C


ATOM
1137
N
GLN A
270
50.216
51.176
29.313
1.00
32.85
N


ATOM
1138
CA
GLN A
270
51.274
50.171
29.406
1.00
32.10
C


ATOM
1139
C
GLN A
270
51.134
49.400
30.717
1.00
31.09
C


ATOM
1140
O
GLN A
270
51.403
48.205
30.770
1.00
30.10
O


ATOM
1141
CB
GLN A
270
52.669
50.816
29.308
1.00
30.58
C


ATOM
1142
CG
GLN A
270
52.897
51.572
28.000
1.00
29.81
C


ATOM
1143
CD
GLN A
270
54.275
51.346
27.394
1.00
29.50
C


ATOM
1144
OE1
GLN A
270
55.172
50.791
28.031
1.00
28.16
O


ATOM
1145
NE2
GLN A
270
54.448
51.789
26.156
1.00
26.58
N


ATOM
1146
N
LYS A
271
50.712
50.085
31.775
1.00
32.98
N


ATOM
1147
CA
LYS A
271
50.518
49.416
33.057
1.00
35.22
C


ATOM
1148
C
LYS A
271
49.432
48.347
32.881
1.00
34.93
C


ATOM
1149
O
LYS A
271
49.566
47.224
33.365
1.00
33.86
O


ATOM
1150
CB
LYS A
271
50.097
50.419
34.137
1.00
36.36
C


ATOM
1151
CG
LYS A
271
49.780
49.767
35.481
1.00
39.94
C


ATOM
1152
CD
LYS A
271
49.633
50.794
36.608
1.00
42.24
C


ATOM
1153
CE
LYS A
271
49.393
50.095
37.951
1.00
45.21
C


ATOM
1154
NZ
LYS A
271
49.405
51.022
39.132
1.00
47.32
N


ATOM
1155
N
ILE A
272
48.373
48.708
32.159
1.00
34.90
N


ATOM
1156
CA
ILE A
272
47.257
47.807
31.897
1.00
35.34
C


ATOM
1157
C
ILE A
272
47.698
46.602
31.071
1.00
35.48
C


ATOM
1158
O
ILE A
272
47.347
45.466
31.387
1.00
36.14
O


ATOM
1159
CB
ILE A
272
46.109
48.545
31.157
1.00
35.04
C


ATOM
1160
CG1
ILE A
272
45.467
49.565
32.101
1.00
35.36
C


ATOM
1161
CG2
ILE A
272
45.073
47.539
30.644
1.00
34.61
C


ATOM
1162
CD1
ILE A
272
44.485
50.509
31.431
1.00
33.49
C


ATOM
1163
N
THR A
273
48.469
46.851
30.016
1.00
34.92
N


ATOM
1164
CA
THR A
273
48.951
45.777
29.156
1.00
34.08
C


ATOM
1165
C
THR A
273
49.844
44.791
29.918
1.00
34.99
C


ATOM
1166
O
THR A
273
49.675
43.578
29.803
1.00
36.08
O


ATOM
1167
CB
THR A
273
49.741
46.340
27.958
1.00
34.19
C


ATOM
1168
OG1
THR A
273
48.888
47.192
27.188
1.00
35.97
O


ATOM
1169
CG2
THR A
273
50.248
45.216
27.069
1.00
32.81
C


ATOM
1170
N
ILE A
274
50.797
45.305
30.687
1.00
34.29
N


ATOM
1171
CA
ILE A
274
51.692
44.433
31.443
1.00
34.33
C


ATOM
1172
C
ILE A
274
50.900
43.660
32.493
1.00
35.70
C


ATOM
1173
O
ILE A
274
51.185
42.495
32.769
1.00
34.67
O


ATOM
1174
CB
ILE A
274
52.793
45.235
32.153
1.00
32.65
C


ATOM
1175
CG1
ILE A
274
53.699
45.902
31.113
1.00
32.10
C


ATOM
1176
CG2
ILE A
274
53.597
44.313
33.082
1.00
31.88
C


ATOM
1177
CD1
ILE A
274
54.700
46.877
31.704
1.00
30.38
C


ATOM
1178
N
GLY A
275
49.907
44.324
33.076
1.00
36.56
N


ATOM
1179
CA
GLY A
275
49.082
43.684
34.085
1.00
37.75
C


ATOM
1180
C
GLY A
275
48.326
42.496
33.520
1.00
37.44
C


ATOM
1181
O
GLY A
275
48.230
41.456
34.159
1.00
38.90
O


ATOM
1182
N
TRP A
276
47.791
42.649
32.316
1.00
36.76
N


ATOM
1183
CA
TRP A
276
47.040
41.582
31.677
1.00
37.78
C


ATOM
1184
C
TRP A
276
47.952
40.391
31.416
1.00
39.15
C


ATOM
1185
O
TRP A
276
47.535
39.238
31.545
1.00
38.18
O


ATOM
1186
CB
TRP A
276
46.452
42.069
30.355
1.00
37.54
C


ATOM
1187
CG
TRP A
276
45.547
41.082
29.704
1.00
38.13
C


ATOM
1188
CD1
TRP A
276
44.213
40.906
29.948
1.00
38.02
C


ATOM
1189
CD2
TRP A
276
45.905
40.117
28.706
1.00
38.93
C


ATOM
1190
NE1
TRP A
276
43.717
39.891
29.158
1.00
38.58
N


ATOM
1191
CE2
TRP A
276
44.734
39.390
28.387
1.00
39.11
C


ATOM
1192
CE3
TRP A
276
47.102
39.795
28.049
1.00
39.30
C


ATOM
1193
CZ2
TRP A
276
44.724
38.360
27.439
1.00
39.42
C


ATOM
1194
CZ3
TRP A
276
47.093
38.768
27.105
1.00
40.69
C


ATOM
1195
CH2
TRP A
276
45.908
38.064
26.809
1.00
40.36
C


ATOM
1196
N
ILE A
277
49.199
40.675
31.045
1.00
38.34
N


ATOM
1197
CA
ILE A
277
50.164
39.621
30.765
1.00
38.49
C


ATOM
1198
C
ILE A
277
50.535
38.850
32.033
1.00
40.03
C


ATOM
1199
O
ILE A
277
50.704
37.634
31.995
1.00
39.95
O


ATOM
1200
CB
ILE A
277
51.444
40.197
30.113
1.00
38.18
C


ATOM
1201
CG1
ILE A
277
51.112
40.752
28.725
1.00
37.35
C


ATOM
1202
CG2
ILE A
277
52.520
39.121
30.016
1.00
36.41
C


ATOM
1203
CD1
ILE A
277
52.274
41.440
28.036
1.00
35.39
C


ATOM
1204
N
ARG A
278
50.656
39.556
33.152
1.00
41.65
N


ATOM
1205
CA
ARG A
278
51.001
38.921
34.421
1.00
44.16
C


ATOM
1206
C
ARG A
278
49.871
38.043
34.950
1.00
46.24
C


ATOM
1207
O
ARG A
278
50.114
36.945
35.439
1.00
47.52
O


ATOM
1208
CB
ARG A
278
51.350
39.977
35.472
1.00
42.76
C


ATOM
1209
CG
ARG A
278
52.659
40.688
35.221
1.00
41.00
C


ATOM
1210
CD
ARG A
278
53.853
39.767
35.416
1.00
40.34
C


ATOM
1211
NE
ARG A
278
55.085
40.438
35.003
1.00
39.80
N


ATOM
1212
CZ
ARG A
278
55.819
40.075
33.957
1.00
37.53
C


ATOM
1213
NH1
ARG A
278
55.460
39.035
33.220
1.00
36.20
N


ATOM
1214
NH2
ARG A
278
56.895
40.777
33.628
1.00
37.01
N


ATOM
1215
N
GLU A
279
48.640
38.535
34.853
1.00
48.36
N


ATOM
1216
CA
GLU A
279
47.471
37.794
35.320
1.00
50.94
C


ATOM
1217
C
GLU A
279
47.248
36.513
34.512
1.00
50.49
C


ATOM
1218
O
GLU A
279
46.799
35.500
35.045
1.00
50.81
O


ATOM
1219
CB
GLU A
279
46.222
38.681
35.225
1.00
54.09
C


ATOM
1220
CG
GLU A
279
44.889
37.951
35.431
1.00
60.56
C


ATOM
1221
CD
GLU A
279
44.637
37.514
36.874
1.00
64.23
C


ATOM
1222
OE1
GLU A
279
43.642
36.788
37.106
1.00
65.99
O


ATOM
1223
OE2
GLU A
279
45.419
37.897
37.777
1.00
66.30
O


ATOM
1224
N
LYS A
280
47.586
36.567
33.230
1.00
49.08
N


ATOM
1225
CA
LYS A
280
47.399
35.444
32.323
1.00
48.34
C


ATOM
1226
C
LYS A
280
48.596
34.489
32.246
1.00
47.43
C


ATOM
1227
O
LYS A
280
48.423
33.286
32.061
1.00
47.48
O


ATOM
1228
CB
LYS A
280
47.084
36.000
30.928
1.00
50.57
C


ATOM
1229
CG
LYS A
280
46.280
35.093
30.003
1.00
53.00
C


ATOM
1230
CD
LYS A
280
47.125
33.994
29.392
1.00
55.48
C


ATOM
1231
CE
LYS A
280
46.372
33.274
28.270
1.00
56.67
C


ATOM
1232
NZ
LYS A
280
45.161
32.558
28.763
1.00
57.35
N


ATOM
1233
N
TYR A
281
49.805
35.019
32.403
1.00
45.34
N


ATOM
1234
CA
TYR A
281
51.012
34.208
32.297
1.00
41.45
C


ATOM
1235
C
TYR A
281
51.987
34.331
33.457
1.00
40.66
C


ATOM
1236
O
TYR A
281
53.025
33.672
33.457
1.00
40.87
O


ATOM
1237
CB
TYR A
281
51.773
34.580
31.028
1.00
40.75
C


ATOM
1238
CG
TYR A
281
50.998
34.455
29.742
1.00
40.09
C


ATOM
1239
CD1
TYR A
281
50.798
33.211
29.144
1.00
40.34
C


ATOM
1240
CD2
TYR A
281
50.507
35.587
29.091
1.00
39.82
C


ATOM
1241
CE1
TYR A
281
50.139
33.099
27.928
1.00
39.98
C


ATOM
1242
CE2
TYR A
281
49.841
35.484
27.877
1.00
40.22
C


ATOM
1243
CZ
TYR A
281
49.665
34.237
27.300
1.00
40.45
C


ATOM
1244
OH
TYR A
281
49.032
34.127
26.089
1.00
43.40
O


ATOM
1245
N
GLY A
282
51.679
35.165
34.440
1.00
39.75
N


ATOM
1246
CA
GLY A
282
52.617
35.333
35.533
1.00
40.40
C


ATOM
1247
C
GLY A
282
53.931
35.851
34.961
1.00
41.42
C


ATOM
1248
O
GLY A
282
53.929
36.614
33.991
1.00
38.40
O


ATOM
1249
N
ASP A
283
55.053
35.433
35.541
1.00
43.07
N


ATOM
1250
CA
ASP A
283
56.369
35.863
35.074
1.00
45.04
C


ATOM
1251
C
ASP A
283
56.955
34.932
34.008
1.00
44.74
C


ATOM
1252
O
ASP A
283
58.155
34.938
33.768
1.00
45.50
O


ATOM
1253
CB
ASP A
283
57.333
35.961
36.262
1.00
47.26
C


ATOM
1254
CG
ASP A
283
56.936
37.049
37.253
1.00
51.59
C


ATOM
1255
OD1
ASP A
283
56.921
38.243
36.865
1.00
52.49
O


ATOM
1256
OD2
ASP A
283
56.639
36.713
38.424
1.00
53.68
O


ATOM
1257
N
LYS A
284
56.103
34.143
33.363
1.00
45.94
N


ATOM
1258
CA
LYS A
284
56.542
33.197
32.334
1.00
46.43
C


ATOM
1259
C
LYS A
284
56.751
33.889
30.988
1.00
44.34
C


ATOM
1260
O
LYS A
284
57.530
33.432
30.152
1.00
45.10
O


ATOM
1261
CB
LYS A
284
55.510
32.067
32.182
1.00
50.03
C


ATOM
1262
CG
LYS A
284
55.898
30.981
31.181
1.00
54.57
C


ATOM
1263
CD
LYS A
284
54.819
29.892
31.055
1.00
57.10
C


ATOM
1264
CE
LYS A
284
53.656
30.317
30.157
1.00
58.56
C


ATOM
1265
NZ
LYS A
284
54.064
30.449
28.717
1.00
57.77
N


ATOM
1266
N
VAL A
285
56.036
34.984
30.775
1.00
41.89
N


ATOM
1267
CA
VAL A
285
56.163
35.741
29.539
1.00
38.65
C


ATOM
1268
C
VAL A
285
56.865
37.052
29.870
1.00
37.26
C


ATOM
1269
O
VAL A
285
56.445
37.785
30.768
1.00
36.50
O


ATOM
1270
CB
VAL A
285
54.784
36.024
28.918
1.00
38.41
C


ATOM
1271
CG1
VAL A
285
54.935
36.904
27.681
1.00
36.80
C


ATOM
1272
CG2
VAL A
285
54.113
34.710
28.552
1.00
37.51
C


ATOM
1273
N
LYS A
286
57.947
37.332
29.151
1.00
35.95
N


ATOM
1274
CA
LYS A
286
58.724
38.542
29.382
1.00
34.21
C


ATOM
1275
C
LYS A
286
58.260
39.677
28.485
1.00
32.46
C


ATOM
1276
O
LYS A
286
58.006
39.482
27.296
1.00
32.56
O


ATOM
1277
CB
LYS A
286
60.215
38.262
29.151
1.00
34.13
C


ATOM
1278
CG
LYS A
286
60.755
37.082
29.955
1.00
34.78
C


ATOM
1279
CD
LYS A
286
60.443
37.214
31.439
1.00
33.84
C


ATOM
1280
CE
LYS A
286
61.080
36.077
32.238
1.00
33.85
C


ATOM
1281
NZ
LYS A
286
60.846
36.204
33.710
1.00
34.7&
N


ATOM
1282
N
VAL A
287
58.154
40.867
29.062
1.00
30.53
N


ATOM
1283
CA
VAL A
287
57.702
42.028
28.311
1.00
29.76
C


ATOM
1284
C
VAL A
287
58.419
43.317
28.697
1.00
28.61
C


ATOM
1285
O
VAL A
287
58.390
43.744
29.856
1.00
29.71
O


ATOM
1286
CB
VAL A
287
56.160
42.221
28.472
1.00
28.44
C


ATOM
1287
CG1
VAL A
287
55.785
42.274
29.938
1.00
29.00
C


ATOM
1288
CG2
VAL A
287
55.707
43.487
27.769
1.00
28.47
C


ATOM
1289
N
GLY A
288
59.078
43.920
27.716
1.00
29.14
N


ATOM
1290
CA
GLY A
288
59.766
45.177
27.941
1.00
28.04
C


ATOM
1291
C
GLY A
288
58.759
46.288
27.721
1.00
28.71
C


ATOM
1292
O
GLY A
288
57.760
46.089
27.023
1.00
29.59
O


ATOM
1293
N
ALA A
289
59.007
47.454
28.310
1.00
28.36
N


ATOM
1294
CA
ALA A
289
58.090
48.585
28.174
1.00
28.55
C


ATOM
1295
C
ALA A
289
58.855
49.883
27.902
1.00
29.25
C


ATOM
1296
O
ALA A
289
60.075
49.921
28.034
1.00
30.12
O


ATOM
1297
CB
ALA A
289
57.242
48.720
29.444
1.00
26.88
C


ATOM
1298
N
GLY A
290
58.136
50.938
27.525
1.00
28.43
N


ATOM
1299
CA
GLY A
290
58.779
52.209
27.232
1.00
28.28
C


ATOM
1300
C
GLY A
290
58.137
52.867
26.021
1.00
29.46
C


ATOM
1301
O
GLY A
290
57.142
52.357
25.512
1.00
29.19
O


ATOM
1302
N
ASN A
291
58.700
53.969
25.523
1.00
28.11
N


ATOM
1303
CA
ASM A
291
59.918
54.586
26.053
1.00
27.63
C


ATOM
1304
C
ASN A
291
59.689
55.673
27.101
1.00
27.03
C


ATOM
1305
O
ASN A
291
58.656
56.336
27.113
1.00
26.50
O


ATOM
1306
CB
ASN A
291
60.723
55.200
24.902
1.00
24.57
C


ATOM
1307
CG
ASN A
291
61.251
54.163
23.946
1.00
27.24
C


ATOM
1308
OD1
ASN A
291
60.850
52.994
23.990
1.00
28.22
O


ATOM
1309
ND2
ASN A
291
62.157
54.577
23.069
1.00
24.45
N


ATOM
1310
N
ILE A
292
60.676
55.848
27.974
1.00
25.83
N


ATOM
1311
CA
ILE A
292
60.634
56.884
28.996
1.00
26.30
C


ATOM
1312
C
ILE A
292
62.000
57.576
29.002
1.00
26.52
C


ATOM
1313
O
ILE A
292
62.943
57.082
28.376
1.00
27.26
O


ATOM
1314
CB
ILE A
292
60.286
56.304
30.399
1.00
26.90
C


ATOM
1315
CG1
ILE A
292
61.132
55.066
30.705
1.00
27.05
C


ATOM
1316
CG2
ILE A
292
58.801
55.967
30.458
1.00
26.39
C


ATOM
1317
CD1
ILE A
292
62.564
55.368
31.104
1.00
28.87
C


ATOM
1318
N
VAL A
293
62.115
58.707
29.695
1.00
26.68
N


ATOM
1319
CA
VAL A
293
63.376
59.443
29.719
1.00
26.19
C


ATOM
1320
C
VAL A
293
63.856
59.935
31.080
1.00
26.51
C


ATOM
1321
O
VAL A
293
64.876
60.619
31.161
1.00
27.91
O


ATOM
1322
CB
VAL A
293
63.323
60.668
28.776
1.00
26.56
C


ATOM
1323
CG1
VAL A
293
63.327
60.216
27.331
1.00
24.86
C


ATOM
1324
CG2
VAL A
293
62.079
61.493
29.068
1.00
25.40
C


ATOM
1325
N
ASP A
294
63.127
59.618
32.143
1.00
26.19
N


ATOM
1326
CA
ASP A
294
63.547
60.039
33.477
1.00
27.16
C


ATOM
1327
C
ASP A
294
63.233
58.988
34.535
1.00
26.65
C


ATOM
1328
O
ASP A
294
62.595
57.980
34.245
1.00
27.20
O


ATOM
1329
CB
ASP A
294
62.909
61.388
33.860
1.00
26.43
C


ATOM
1330
CG
ASP A
294
61.385
61.347
33.903
1.00
29.29
C


ATOM
1331
OD1
ASP A
294
60.770
60.309
33.581
1.00
29.96
O


ATOM
1332
OD2
ASP A
294
60.791
62.383
34.262
1.00
31.71
O


ATOM
1333
N
GLY A
295
63.693
59.232
35.757
1.00
27.62
N


ATOM
1334
CA
GLY A
295
63.462
58.303
36.846
1.00
29.92
C


ATOM
1335
C
GLY A
295
62.004
57.997
37.127
1.00
30.82
C


ATOM
1336
O
GLY A
295
61.661
56.861
37.445
1.00
30.01
O


ATOM
1337
N
GLU A
296
61.146
59.009
37.025
1.00
32.13
N


ATOM
1338
CA
GLU A
296
59.713
58.831
37.265
1.00
31.92
C


ATOM
1339
C
GLU A
296
59.111
57.859
36.263
1.00
29.81
C


ATOM
1340
O
GLU A
296
58.331
56.989
36.631
1.00
30.09
O


ATOM
1341
CB
GLU A
296
58.977
60.169
37.157
1.00
35.45
C


ATOM
1342
CG
GLU A
296
58.989
61.006
38.413
1.00
42.92
C


ATOM
1343
CD
GLU A
296
58.284
62.338
38.215
1.00
48.68
C


ATOM
1344
OE1
GLU A
296
57.151
62.350
37.669
1.00
50.17
O


ATOM
1345
OE2
GLU A
296
58.865
63.375
38.609
1.00
51.29
O


ATOM
1346
N
GLY A
297
59.471
58.024
34.994
1.00
29.22
N


ATOM
1347
CA
GLY A
297
58.961
57.146
33.954
1.00
29.30
C


ATOM
1348
C
GLY A
297
59.453
55.721
34.150
1.00
28.85
C


ATOM
1349
O
GLY A
297
58.703
54.764
33.950
1.00
30.00
O


ATOM
1350
N
PHE A
298
60.721
55.585
34.529
1.00
27.55
N


ATOM
1351
CA
PHE A
298
61.325
54.276
34.783
1.00
28.20
C


ATOM
1352
C
PHE A
298
60.572
53.592
35.921
1.00
28.81
C


ATOM
1353
O
PHE A
298
60.127
52.453
35.797
1.00
29.70
O


ATOM
1354
CB
PHE A
298
62.793
54.432
35.205
1.00
26.54
C


ATOM
1355
CG
PHE A
298
63.403
53.164
35.747
1.00
27.42
C


ATOM
1356
CD1
PHE A
298
63.930
52.206
34.890
1.00
25.96
C


ATOM
1357
CD2
PHE A
298
63.380
52.895
37.112
1.00
28.67
C


ATOM
1358
CE1
PHE A
298
64.419
50.995
35.381
1.00
27.00
C


ATOM
1359
CE2
PHE A
298
63.865
51.687
37.615
1.00
29.28
C


ATOM
1360
CZ
PHE A
298
64.385
50.732
36.745
1.00
26.48
C


ATOM
1361
N
ARG A
299
60.460
54.319
37.030
1.00
29.81
N


ATOM
1362
CA
ARG A
299
59.801
53.868
38.252
1.00
31.20
C


ATOM
1363
C
ARG A
299
58.372
53.388
38.000
1.00
31.34
C


ATOM
1364
O
ARG A
299
57.948
52.355
38.529
1.00
30.36
O


ATOM
1365
CB
ARG A
299
59.811
55.020
39.257
1.00
33.79
C


ATOM
1366
CG
ARG A
299
58.887
54.867
40.443
1.00
39.24
C


ATOM
1367
CD
ARG A
299
59.563
54.163
41.591
1.00
43.20
C


ATOM
1368
NE
ARG A
299
60.787
54.835
42.029
1.00
46.01
N


ATOM
1369
CZ
ARG A
299
61.578
54.359
42.989
1.00
46.27
C


ATOM
1370
NH1
ARG A
299
61.261
53.226
43.597
1.00
46.49
N


ATOM
1371
NH2
ARG A
299
62.691
54.996
43.329
1.00
46.82
N


ATOM
1372
N
TYR A
300
57.630
54.135
37.192
1.00
29.36
N


ATOM
1373
CA
TYR A
300
56.263
53.752
36.886
1.00
30.10
C


ATOM
1374
C
TYR A
300
56.209
52.406
36.160
1.00
29.41
C


ATOM
1375
O
TYR A
300
55.416
51.538
36.510
1.00
29.12
O


ATOM
1376
CB
TYR A
300
55.584
54.813
36.025
1.00
28.91
C


ATOM
1377
CG
TYR A
300
54.123
54.518
35.770
1.00
28.90
C


ATOM
1378
CD1
TYR A
300
53.152
54.795
36.737
1.00
27.98
C


ATOM
1379
CD2
TYR A
300
53.712
53.960
34.562
1.00
27.83
C


ATOM
1380
CE1
TYR A
300
51.799
54.526
36.497
1.00
28.93
C


ATOM
1381
CE2
TYR A
300
52.368
53.687
34.314
1.00
29.78
C


ATOM
1382
CZ
TYR A
300
51.419
53.974
35.284
1.00
28.36
C


ATOM
1383
OH
TYR A
300
50.098
53.722
35.019
1.00
28.95
O


ATOM
1384
N
LEU A
301
57.047
52.230
35.145
1.00
29.18
N


ATOM
1385
CA
LEU A
301
57.037
50.970
34.416
1.00
29.02
C


ATOM
1386
C
LEU A
301
57.645
49.845
35.257
1.00
29.33
C


ATOM
1387
O
LEU A
301
57.286
48.685
35.098
1.00
30.06
O


ATOM
1388
CB
LEU A
301
57.768
51.119
33.079
1.00
25.76
C


ATOM
1389
CG
LEU A
301
57.063
52.069
32.093
1.00
26.66
C


ATOM
1390
CD1
LEU A
301
57.839
52.143
30.770
1.00
20.87
C


ATOM
1391
CD2
LEU A
301
55.631
51.577
31.848
1.00
24.96
C


ATOM
1392
N
ALA A
302
58.551
50.192
36.163
1.00
29.71
N


ATOM
1393
CA
ALA A
302
59.165
49.184
37.019
1.00
31.15
C


ATOM
1394
C
ALA A
302
58.093
48.588
37.946
1.00
31.17
C


ATOM
1395
O
ALA A
302
57.913
47.371
38.003
1.00
31.11
O


ATOM
1396
CB
ALA A
302
60.300
49.804
37.835
1.00
27.53
C


ATOM
1397
N
ASP A
303
57.381
49.455
38.660
1.00
31.61
N


ATOM
1398
CA
ASP A
303
56.327
49.016
39.565
1.00
32.39
C


ATOM
1399
C
ASP A
303
55.221
48.296
38.811
1.00
32.86
C


ATOM
1400
O
ASP A
303
54.541
47.442
39.381
1.00
33.19
O


ATOM
1401
CB
ASP A
303
55.723
50.201
40.328
1.00
33.54
C


ATOM
1402
CG
ASP A
303
56.701
50.831
41.301
1.00
36.75
C


ATOM
1403
OD1
ASP A
303
57.613
50.123
41.785
1.00
37.27
O


ATOM
1404
OD2
ASP A
303
56.546
52.033
41.601
1.00
39.52
O


ATOM
1405
N
ALA A
304
55.034
48.649
37.540
1.00
31.74
N


ATOM
1406
CA
ALA A
304
54.010
48.017
36.708
1.00
31.41
C


ATOM
1407
C
ALA A
304
54.434
46.596
36.310
1.00
31.41
C


ATOM
1408
O
ALA A
304
53.621
45.813
35.818
1.00
30.05
O


ATOM
1409
CB
ALA A
304
53.741
48.858
35.460
1.00
30.00
C


ATOM
1410
N
GLY A
305
55.711
46.272
36.505
1.00
31.95
N


ATOM
1411
CA
GLY A
305
56.179
44.929
36.195
1.00
31.25
C


ATOM
1412
C
GLY A
305
57.000
44.673
34.944
1.00
32.68
C


ATOM
1413
O
GLY A
305
57.279
43.513
34.620
1.00
33.06
O


ATOM
1414
N
ALA A
306
57.397
45.727
34.236
1.00
31.70
N


ATOM
1415
CA
ALA A
306
58.192
45.560
33.018
1.00
31.42
C


ATOM
1416
C
ALA A
306
59.463
44.744
33.294
1.00
30.89
C


ATOM
1417
O
ALA A
306
60.067
44.875
34.358
1.00
30.03
O


ATOM
1418
CB
ALA A
306
58.564
46.934
32.450
1.00
30.33
C


ATOM
1419
N
ASP A
307
59.864
43.911
32.334
1.00
30.79
N


ATOM
1420
CA
ASP A
307
61.070
43.085
32.472
1.00
30.22
C


ATOM
1421
C
ASP A
307
62.337
43.837
32.044
1.00
29.80
C


ATOM
1422
O
ASP A
307
63.449
43.468
32.407
1.00
29.77
O


ATOM
1423
CB
ASP A
307
60.908
41.790
31.673
1.00
29.98
C


ATOM
1424
CG
ASP A
307
59.931
40.835
32.328
1.00
31.85
C


ATOM
1425
OD1
ASP A
307
60.267
40.310
33.407
1.00
30.41
O


ATOM
1426
OD2
ASP A
307
58.826
40.626
31.783
1.00
32.28
O


ATOM
1427
N
PHE A
308
62.153
44.876
31.242
1.00
28.99
N


ATOM
1428
CA
PHE A
308
63.243
45.742
30.819
1.00
28.95
C


ATOM
1429
C
PHE A
308
62.560
47.025
30.362
1.00
29.95
C


ATOM
1430
O
PHE A
308
61.395
47.009
29.958
1.00
29.34
O


ATOM
1431
CB
PHE A
308
64.141
45.087
29.742
1.00
27.92
C


ATOM
1432
CG
PHE A
308
63.582
45.092
28.339
1.00
29.45
C


ATOM
1433
CD1
PHE A
308
63.520
46.272
27.594
1.00
29.48
C


ATOM
1434
CD2
PHE A
308
63.193
43.894
27.729
1.00
29.25
C


ATOM
1435
CE1
PHE A
308
63.085
46.259
26.263
1.00
28.89
C


ATOM
1436
CE2
PHE A
308
62.757
43.870
26.398
1.00
28.70
C


ATOM
1437
CZ
PHE A
308
62.704
45.056
25.664
1.00
29.12
C


ATOM
1438
N
ILE A
309
63.266
48.141
30.475
1.00
29.18
N


ATOM
1439
CA
ILE A
309
62.685
49.425
30.127
1.00
29.21
C


ATOM
1440
C
ILE A
309
63.497
50.150
29.061
1.00
27.84
C


ATOM
1441
O
ILE A
309
64.719
50.258
29.172
1.00
26.04
O


ATOM
1442
CB
ILE A
309
62.539
50.284
31.422
1.00
27.91
C


ATOM
1443
CG1
ILE A
309
61.524
49.602
32.353
1.00
26.47
C


ATOM
1444
CG2
ILE A
309
62.123
51.703
31.082
1.00
27.10
C


ATOM
1445
CD1
ILE A
309
61.390
50.207
33.733
1.00
25.58
C


ATOM
1446
N
LYS A
310
62.813
50.616
28.015
1.00
27.18
N


ATOM
1447
CA
LYS A
310
63.480
51.322
26.926
1.00
28.54
C


ATOM
1448
C
LYS A
310
63.537
52.827
27.149
1.00
27.05
C


ATOM
1449
O
LYS A
310
62.550
53.460
27.529
1.00
26.03
O


ATOM
1450
CB
LYS A
310
62.817
51.030
25.573
1.00
28.97
C


ATOM
1451
CG
LYS A
310
63.170
49.671
25.012
1.00
32.45
C


ATOM
1452
CD
LYS A
310
63.175
49.652
23.488
1.00
28.69
C


ATOM
1453
CE
LYS A
310
61.783
49.797
22.894
1.00
30.25
C


ATOM
1454
NZ
LYS A
310
61.577
51.156
22.318
1.00
30.02
N


ATOM
1455
N
ILE A
311
64.713
53.380
26.880
1.00
26.50
N


ATOM
1456
CA
ILE A
311
64.988
54.799
27.061
1.00
25.97
C


ATOM
1457
C
ILE A
311
65.140
55.546
25.744
1.00
26.10
C


ATOM
1458
O
ILE A
311
65.875
55.115
24.854
1.00
24.93
O


ATOM
1459
CB
ILE A
311
66.297
54.995
27.851
1.00
24.14
C


ATOM
1460
CG1
ILE A
311
66.229
54.208
29.162
1.00
23.37
C


ATOM
1461
CG2
ILE A
311
66.541
56.493
28.113
1.00
21.90
C


ATOM
1462
CD1
ILE A
311
67.585
53.999
29.821
1.00
22.04
C


ATOM
1463
N
GLY A
312
64.440
56.668
25.619
1.00
27.44
N


ATOM
1464
CA
GLY A
312
64.587
57.453
24.417
1.00
29.07
C


ATOM
1465
C
GLY A
312
63.364
58.017
23.740
1.00
31.30
C


ATOM
1466
O
GLY A
312
62.499
57.284
23.281
1.00
32.02
O


ATOM
1467
N
ILE A
313
63.316
59.342
23.671
1.00
34.02
N


ATOM
1468
CA
ILE A
313
62.242
60.063
23.005
1.00
35.18
C


ATOM
1469
C
ILE A
313
62.860
61.264
22.294
1.00
36.95
C


ATOM
1470
O
ILE A
313
63.446
62.143
22.937
1.00
33.67
O


ATOM
1471
CB
ILE A
313
61.184
60.588
23.991
1.00
35.37
C


ATOM
1472
CG1
ILE A
313
60.488
59.419
24.697
1.00
37.50
C


ATOM
1473
CG2
ILE A
313
60.161
61.420
23.236
1.00
36.43
C


ATOM
1474
CD1
ILE A
313
59.485
59.848
25.762
1.00
34.44
C


ATOM
1475
N
GLY A
314
62.744
61.280
20.968
1.00
39.08
N


ATOM
1476
CA
GLY A
314
63.269
62.384
20.180
1.00
42.63
C


ATOM
1477
C
GLY A
314
64.709
62.259
19.711
1.00
45.06
C


ATOM
1478
O
GLY A
314
65.204
63.127
18.984
1.00
46.48
O


ATOM
1479
N
GLY A
315
65.383
61.186
20.111
1.00
45.85
N


ATOM
1480
CA
GLY A
315
66.767
60.997
19.716
1.00
47.36
C


ATOM
1481
C
GLY A
315
66.970
60.175
18.456
1.00
48.37
C


ATOM
1482
O
GLY A
315
68.067
60.169
17.901
1.00
48.87
O


ATOM
1483
N
GLY A
316
65.929
59.482
18.002
1.00
49.42
N


ATOM
1484
CA
GLY A
316
66.042
58.666
16.802
1.00
50.45
C


ATOM
1485
C
GLY A
316
66.512
59.444
15.581
1.00
52.07
C


ATOM
1486
O
GLY A
316
66.307
60.655
15.492
1.00
51.74
O


ATOM
1487
N
SER A
317
67.137
58.748
14.634
1.00
53.21
N


ATOM
1488
CA
SER A
317
67.640
59.384
13.417
1.00
55.05
C


ATOM
1489
C
SER A
317
66.513
59.886
12.519
1.00
56.78
C


ATOM
1490
O
SER A
317
66.689
60.855
11.782
1.00
57.20
O


ATOM
1491
CB
SER A
317
68.529
58.413
12.629
1.00
53.62
C


ATOM
1492
OG
SER A
317
67.769
57.378
12.034
1.00
52.76
O


ATOM
1493
N
ILE A
318
65.360
59.226
12.575
1.00
59.64
N


ATOM
1494
CA
ILE A
318
64.210
59.634
11.770
1.00
63.21
C


ATOM
1495
C
ILE A
318
63.236
60.457
12.599
1.00
65.18
C


ATOM
1496
O
ILE A
318
62.033
60.454
12.337
1.00
66.41
O


ATOM
1497
CB
ILE A
318
63.425
58.425
11.193
1.00
62.53
C


ATOM
1498
CG1
ILE A
318
62.907
57.531
12.325
1.00
61.87
C


ATOM
1499
CG2
ILE A
318
64.292
57.668
10.216
1.00
63.60
C


ATOM
1500
CD1
ILE A
318
63.986
56.875
13.169
1.00
63.20
C


HETATM
1501
N
CSO A
319
63.755
61.160
13.601
1.00
67.42
N


HETATM
1502
CA
CSO A
319
62.906
61.974
14.457
1.00
69.97
C


HETATM
1503
CB
CSO A
319
62.908
61.424
15.883
1.00
69.24
C


HETATM
1504
SG
CSO A
319
61.855
62.386
17.013
1.00
71.47
S


HETATM
1505
C
CSO A
319
63.286
63.449
14.489
1.00
71.57
C


HETATM
1506
O
CSO A
319
64.383
63.812
14.916
1.00
71.62
O


HETATM
1507
OD
CSO A
319
60.102
62.492
16.543
1.00
68.93
O


ATOM
1508
N
ILE A
320
62.363
64.292
14.035
1.00
73.78
N


ATOM
1509
CA
ILE A
320
62.568
65.736
14.026
1.00
75.95
C


ATOM
1510
C
ILE A
320
61.613
66.330
15.064
1.00
77.00
C


ATOM
1511
O
ILE A
320
60.712
67.099
14.730
1.00
77.56
O


ATOM
1512
CB
ILE A
320
62.250
66.346
12.636
1.00
76.42
C


ATOM
1513
CG1
ILE A
320
62.907
65.512
11.529
1.00
76.94
C


ATOM
1514
CG2
ILE A
320
62.740
67.793
12.577
1.00
76.02
C


ATOM
1515
CD1
ILE A
320
64.419
65.396
11.639
1.00
77.38
C


ATOM
1516
N
THR A
321
61.821
65.948
16.322
1.00
78.28
N


ATOM
1517
CA
THR A
321
61.000
66.397
17.448
1.00
79.55
C


ATOM
1518
C
THR A
321
60.432
67.809
17.303
1.00
79.96
C


ATOM
1519
O
THR A
321
59.222
68.014
17.421
1.00
79.36
O


ATOM
1520
CB
THR A
321
61.798
66.340
18.767
1.00
79.97
C


ATOM
1521
OG1
THR A
321
62.325
65.020
18.951
1.00
80.89
O


ATOM
1522
CG2
THR A
321
60.902
66.688
19.942
1.00
79.20
C


ATOM
1523
N
ARG A
322
61.312
68.776
17.057
1.00
80.56
N


ATOM
1524
CA
ARG A
322
60.911
70.173
16.903
1.00
81.44
C


ATOM
1525
C
ARG A
322
60.282
70.402
15.533
1.00
80.96
C


ATOM
1526
O
ARG A
322
60.658
71.317
14.796
1.00
81.59
O


ATOM
1527
CB
ARG A
322
62.128
71.076
17.090
1.00
82.63
C


ATOM
1528
CG
ARG A
322
62.904
70.739
18.345
1.00
84.75
C


ATOM
1529
CD
ARG A
322
64.194
71.520
18.459
1.00
85.81
C


ATOM
1530
NE
ARG A
322
65.052
70.945
19.491
1.00
86.61
N


ATOM
1531
CZ
ARG A
322
66.238
71.432
19.834
1.00
87.87
C


ATOM
1532
NH1
ARG A
322
66.711
72.512
19.226
1.00
88.28
N


ATOM
1533
NH2
ARG A
322
66.955
70.831
20.775
1.00
88.07
N


ATOM
1534
N
GLU A
323
59.318
69.549
15.211
1.00
79.65
N


ATOM
1535
CA
GLU A
323
58.595
69.596
13.949
1.00
78.09
C


ATOM
1536
C
GLU A
323
57.395
68.679
14.153
1.00
76.08
C


ATOM
1537
O
GLU A
323
56.482
68.618
13.328
1.00
75.54
O


ATOM
1538
CB
GLU A
323
59.485
69.078
12.818
1.00
79.51
C


ATOM
1539
CG
GLU A
323
58.886
69.206
11.429
1.00
82.04
C


ATOM
1540
CD
GLU A
323
59.856
68.784
10.341
1.00
83.25
C


ATOM
1541
OE1
GLU A
323
60.262
67.601
10.328
1.00
84.45
O


ATOM
1542
OE2
GLU A
323
60.216
69.638
9.501
1.00
83.53
O


ATOM
1543
N
GLN A
324
57.419
67.969
15.278
1.00
73.73
N


ATOM
1544
CA
GLN A
324
56.358
67.047
15.656
1.00
70.84
C


ATOM
1545
C
GLN A
324
55.584
67.624
16.841
1.00
67.80
C


ATOM
1546
O
GLN A
324
54.752
68.516
16.665
1.00
68.23
O


ATOM
1547
CB
GLN A
324
56.951
65.684
16.028
1.00
72.52
C


ATOM
1548
CG
GLN A
324
57.667
64.984
14.883
1.00
74.98
C


ATOM
1549
CD
GLN A
324
56.732
64.622
13.740
1.00
77.08
C


ATOM
1550
OE1
GLN A
324
56.070
65.485
13.162
1.00
78.31
O


ATOM
1551
NE2
GLN A
324
56.678
63.338
13.407
1.00
78.07
N


ATOM
1552
N
LYS A
325
55.865
67.129
18.045
1.00
63.07
N


ATOM
1553
CA
LYS A
325
55.169
67.608
19.237
1.00
58.26
C


ATOM
1554
C
LYS A
325
56.069
68.271
20.273
1.00
54.26
C


ATOM
1555
O
LYS A
325
55.592
68.754
21.301
1.00
53.55
O


ATOM
1556
CB
LYS A
325
54.387
66.466
19.894
1.00
58.47
C


ATOM
1557
CG
LYS A
325
53.233
65.959
19.042
1.00
57.42
C


ATOM
1558
CD
LYS A
325
52.221
65.177
19.862
1.00
57.29
C


ATOM
1559
CE
LYS A
325
52.836
63.949
20.508
1.00
55.50
C


ATOM
1560
NZ
LYS A
325
51.779
63.110
21.124
1.00
55.85
N


ATOM
1561
N
GLY A
326
57.369
68.292
20.005
1.00
49.91
N


ATOM
1562
CA
GLY A
326
58.288
68.924
20.929
1.00
46.08
C


ATOM
1563
C
GLY A
326
58.462
68.239
22.271
1.00
44.72
C


ATOM
1564
O
GLY A
326
58.571
68.909
23.300
1.00
42.35
O


ATOM
1565
N
ILE A
327
58.472
66.908
22.269
1.00
42.55
N


ATOM
1566
CA
ILE A
327
58.676
66.151
23.496
1.00
41.64
C


ATOM
1567
C
ILE A
327
59.998
65.398
23.351
1.00
40.52
C


ATOM
1568
O
ILE A
327
60.387
65.011
22.248
1.00
39.17
O


ATOM
1569
CB
ILE A
327
57.526
65.136
23.764
1.00
43.00
C


ATOM
1570
CG1
ILE A
327
57.530
64.026
22.713
1.00
43.54
C


ATOM
1571
CG2
ILE A
327
56.179
65.859
23.752
1.00
43.95
C


ATOM
1572
CD1
ILE A
327
56.507
62.920
22.986
1.00
45.42
C


ATOM
1573
N
GLY A
328
60.706
65.206
24.455
1.00
39.74
N


ATOM
1574
CA
GLY A
328
61.963
64.490
24.362
1.00
38.49
C


ATOM
1575
C
GLY A
328
63.040
64.952
25.321
1.00
37.48
C


ATOM
1576
O
GLY A
328
62.810
65.790
26.201
1.00
33.46
O


ATOM
1577
N
ARG A
329
64.233
64.399
25.132
1.00
35.76
N


ATOM
1578
CA
ARG A
329
65.361
64.723
25.981
1.00
34.21
C


ATOM
1579
C
ARG A
329
66.625
64.178
25.333
1.00
32.60
C


ATOM
1580
O
ARG A
329
66.592
63.117
24.719
1.00
33.20
O


ATOM
1581
CB
ARG A
329
65.152
64.070
27.353
1.00
34.78
C


ATOM
1582
CG
ARG A
329
66.083
64.550
28.441
1.00
32.95
C


ATOM
1583
CD
ARG A
329
65.843
63.788
29.726
1.00
32.61
C


ATOM
1584
NE
ARG A
329
66.249
64.578
30.881
1.00
32.32
N


ATOM
1585
CZ
ARG A
329
66.174
64.166
32.142
1.00
33.26
C


ATOM
1586
NH1
ARG A
329
65.708
62.956
32.431
1.00
31.12
N


ATOM
1587
NH2
ARG A
329
66.561
64.975
33.118
1.00
34.83
N


ATOM
1588
N
GLY A
330
67.733
64.908
25.452
1.00
32.13
N


ATOM
1589
CA
GLY A
330
68.978
64.419
24.893
1.00
29.42
C


ATOM
1590
C
GLY A
330
69.146
62.988
25.382
1.00
27.97
C


ATOM
1591
O
GLY A
330
68.986
62.718
26.569
1.00
26.61
O


ATOM
1592
N
GLN A
331
69.455
62.076
24.469
1.00
28.50
N


ATOM
1593
CA
GLN A
331
69.611
60.667
24.801
1.00
28.43
C


ATOM
1594
C
GLN A
331
70.586
60.394
25.947
1.00
28.88
C


ATOM
1595
O
GLN A
331
70.294
59.570
26.819
1.00
29.14
O


ATOM
1596
CB
GLN A
331
70.049
59.876
23.561
1.00
28.74
C


ATOM
1597
CG
GLN A
331
69.975
58.362
23.734
1.00
30.37
C


ATOM
1598
CD
GLN A
331
68.540
57.846
23.795
1.00
34.54
C


ATOM
1599
OE1
GLN A
331
68.288
56.727
24.250
1.00
34.07
O


ATOM
1600
NE2
GLN A
331
67.596
58.655
23.324
1.00
32.56
N


ATOM
1601
N
ALA A
332
71.733
61.073
25.951
1.00
26.91
N


ATOM
1602
CA
ALA A
332
72.732
60.857
26.999
1.00
27.04
C


ATOM
1603
C
ALA A
332
72.165
61.146
28.389
1.00
26.51
C


ATOM
1604
O
ALA A
332
72.235
60.304
29.289
1.00
24.75
O


ATOM
1605
CB
ALA A
332
73.981
61.725
26.743
1.00
26.35
C


ATOM
1606
N
THR A
333
71.602
62.337
28.555
1.00
25.80
N


ATOM
1607
CA
THR A
333
71.021
62.735
29.828
1.00
26.22
C


ATOM
1608
C
THR A
333
69.921
61.763
30.251
1.00
26.29
C


ATOM
1609
O
THR A
333
69.798
61.427
31.430
1.00
24.39
O


ATOM
1610
CB
THR A
333
70.421
64.145
29.740
1.00
27.31
C


ATOM
1611
OG1
THR A
333
71.440
65.071
29.336
1.00
28.44
O


ATOM
1612
CG2
THR A
333
69.863
64.566
31.094
1.00
27.55
C


ATOM
1613
N
ALA A
334
69.128
61.321
29.276
1.00
25.58
N


ATOM
1614
CA
ALA A
334
68.040
60.384
29.520
1.00
25.32
C


ATOM
1615
C
ALA A
334
68.570
59.079
30.125
1.00
24.79
C


ATOM
1616
O
ALA A
334
68.064
58.603
31.146
1.00
24.60
O


ATOM
1617
CB
ALA A
334
67.303
60.094
28.210
1.00
24.05
C


ATOM
1618
N
VAL A
335
69.588
58.506
29.491
1.00
24.43
N


ATOM
1619
CA
VAL A
335
70.181
57.256
29.964
1.00
24.60
C


ATOM
1620
C
VAL A
335
70.774
57.420
31.362
1.00
25.20
C


ATOM
1621
O
VAL A
335
70.484
56.635
32.271
1.00
26.11
O


ATOM
1622
CB
VAL A
335
71.288
56.765
28.995
1.00
26.29
C


ATOM
1623
CG1
VAL A
335
71.986
55.527
29.564
1.00
25.97
C


ATOM
1624
CG2
VAL A
335
70.678
56.442
27.640
1.00
24.78
C


ATOM
1625
N
ILE A
336
71.600
58.448
31.533
1.00
25.74
N


ATOM
1626
CA
ILE A
336
72.238
58.713
32.815
1.00
26.05
C


ATOM
1627
C
ILE A
336
71.213
58.842
33.945
1.00
27.20
C


ATOM
1628
O
ILE A
336
71.395
58.287
35.030
1.00
26.21
O


ATOM
1629
CB
ILE A
336
73.084
59.998
32.744
1.00
25.46
C


ATOM
1630
CG1
ILE A
336
74.275
59.769
31.806
1.00
24.75
C


ATOM
1631
CG2
ILE A
336
73.552
60.409
34.141
1.00
22.41
C


ATOM
1632
CD1
ILE A
336
75.078
61.022
31.519
1.00
26.47
C


ATOM
1633
N
ASP A
337
70.130
59.565
33.681
1.00
27.99
N


ATOM
1634
CA
ASP A
337
69.090
59.769
34.686
1.00
28.97
C


ATOM
1635
C
ASP A
337
68.318
58.476
35.001
1.00
29.22
C


ATOM
1636
O
ASP A
337
68.057
58.160
36.165
1.00
27.09
O


ATOM
1637
CB
ASP A
337
68.110
60.845
34.209
1.00
31.92
C


ATOM
1638
CG
ASP A
337
67.111
61.234
35.279
1.00
35.94
C


ATOM
1639
OD1
ASP A
337
66.026
61.755
34.937
1.00
39.65
O


ATOM
1640
OD2
ASP A
337
67.416
61.026
36.472
1.00
40.82
O


ATOM
1641
N
VAL A
338
67.950
57.739
33.956
1.00
27.65
N


ATOM
1642
CA
VAL A
338
67.205
56.502
34.133
1.00
26.39
C


ATOM
1643
C
VAL A
338
68.058
55.470
34.854
1.00
25.81
C


ATOM
1644
O
VAL A
338
67.575
54.780
35.748
1.00
25.37
O


ATOM
1645
CB
VAL A
338
66.720
55.930
32.771
1.00
24.93
C


ATOM
1646
CG1
VAL A
338
66.113
54.545
32.971
1.00
23.01
C


ATOM
1647
CG2
VAL A
338
65.677
56.870
32.155
1.00
23.63
C


ATOM
1648
N
VAL A
339
69.323
55.375
34.460
1.00
25.47
N


ATOM
1649
CA
VAL A
339
70.252
54.440
35.075
1.00
25.33
C


ATOM
1650
C
VAL A
339
70.413
54.711
36.572
1.00
27.56
C


ATOM
1651
O
VAL A
339
70.493
53.773
37.362
1.00
29.02
O


ATOM
1652
CB
VAL A
339
71.633
54.500
34.383
1.00
24.83
C


ATOM
1653
CG1
VAL A
339
72.701
53.830
35.246
1.00
23.64
C


ATOM
1654
CG2
VAL A
339
71.549
53.809
33.031
1.00
22.84
C


ATOM
1655
N
ALA A
340
70.458
55.982
36.962
1.00
27.28
N


ATOM
1656
CA
ALA A
340
70.596
56.330
38.374
1.00
28.29
C


ATOM
1657
C
ALA A
340
69.360
55.861
39.141
1.00
29.41
C


ATOM
1658
O
ALA A
340
69.461
55.348
40.260
1.00
29.34
O


ATOM
1659
CB
ALA A
340
70.775
57.835
38.536
1.00
25.77
C


ATOM
1660
N
GLU A
341
68.192
56.031
38.531
1.00
28.19
N


ATOM
1661
CA
GLU A
341
66.949
55.619
39.168
1.00
29.67
C


ATOM
1662
C
GLU A
341
66.878
54.093
39.245
1.00
28.17
C


ATOM
1663
O
GLU A
341
66.419
53.543
40.236
1.00
27.43
O


ATOM
1664
CB
GLU A
341
65.750
56.151
38.384
1.00
30.31
C


ATOM
1665
CG
GLU A
341
64.433
56.116
39.153
1.00
33.93
C


ATOM
1666
CD
GLU A
341
64.441
57.036
40.368
1.00
36.33
C


ATOM
1667
OE1
GLU A
341
65.031
58.137
40.294
1.00
37.90
O


ATOM
1668
OE2
GLU A
341
63.843
56.668
41.395
1.00
37.92
O


ATOM
1669
N
ARG A
342
67.335
53.420
38.192
1.00
28.17
N


ATOM
1670
CA
ARG A
342
67.328
51.959
38.140
1.00
27.23
C


ATOM
1671
C
ARG A
342
68.220
51.382
39.241
1.00
26.35
C


ATOM
1672
O
ARG A
342
67.861
50.394
39.875
1.00
27.18
O


ATOM
1673
CB
ARG A
342
67.799
51.481
36.756
1.00
26.16
C


ATOM
1674
CG
ARG A
342
67.736
49.961
36.513
1.00
25.81
C


ATOM
1675
CD
ARG A
342
68.988
49.223
37.006
1.00
22.94
C


ATOM
1676
NE
ARG A
342
70.230
49.706
36.405
1.00
23.37
N


ATOM
1677
CZ
ARG A
342
70.606
49.502
35.141
1.00
22.98
C


ATOM
1678
NH1
ARG A
342
69.837
48.816
34.304
1.00
22.05
N


ATOM
1679
NH2
ARG A
342
71.771
49.977
34.713
1.00
22.35
N


ATOM
1680
N
ASN A
343
69.372
52.005
39.472
1.00
26.04
N


ATOM
1681
CA
ASN A
343
70.288
51.542
40.510
1.00
27.90
C


ATOM
1682
C
ASN A
343
69.715
51.821
41.902
1.00
30.25
C


ATOM
1683
O
ASN A
343
69.891
51.030
42.827
1.00
31.34
O


ATOM
1684
CB
ASN A
343
71.662
52.202
40.353
1.00
25.88
C


ATOM
1685
CG
ASN A
343
72.379
51.755
39.086
1.00
28.08
C


ATOM
1686
OD1
ASN A
343
72.029
50.729
38.494
1.00
26.63
O


ATOM
1687
ND2
ASN A
343
73.396
52.510
38.674
1.00
26.34
N


ATOM
1688
N
LYS A
344
69.017
52.941
42.043
1.00
31.32
N


ATOM
1689
CA
LYS A
344
68.392
53.296
43.308
1.00
34.03
C


ATOM
1690
C
LYS A
344
67.296
52.260
43.561
1.00
33.69
C


ATOM
1691
O
LYS A
344
67.151
51.736
44.668
1.00
34.47
O


ATOM
1692
CB
LYS A
344
67.791
54.705
43.209
1.00
36.27
C


ATOM
1693
CG
LYS A
344
67.106
55.221
44.467
1.00
42.99
C


ATOM
1694
CD
LYS A
344
66.596
56.654
44.257
1.00
46.73
C


ATOM
1695
CE
LYS A
344
65.820
57.178
45.469
1.00
49.48
C


ATOM
1696
NZ
LYS A
344
66.664
57.318
46.702
1.00
53.65
N


ATOM
1697
N
TYR A
345
66.541
51.956
42.512
1.00
32.48
N


ATOM
1698
CA
TYR A
345
65.463
50.979
42.590
1.00
32.33
C


ATOM
1699
C
TYR A
345
66.008
49.599
42.989
1.00
32.68
C


ATOM
1700
O
TYR A
345
65.413
48.901
43.811
1.00
32.28
O


ATOM
1701
CB
TYR A
345
64.764
50.878
41.241
1.00
30.33
C


ATOM
1702
CG
TYR A
345
63.474
50.092
41.273
1.00
31.92
C


ATOM
1703
CD1
TYR A
345
62.291
50.685
41.702
1.00
32.27
C


ATOM
1704
CD2
TYR A
345
63.427
48.767
40.830
1.00
31.10
C


ATOM
1705
CE1
TYR A
345
61.090
49.988
41.681
1.00
32.84
C


ATOM
1706
CE2
TYR A
345
62.230
48.061
40.805
1.00
32.54
C


ATOM
1707
CZ
TYR A
345
61.066
48.683
41.228
1.00
33.59
C


ATOM
1708
OH
TYR A
345
59.869
48.022
41.152
1.00
35.30
O


ATOM
1709
N
PHE A
346
67.133
49.211
42.396
1.00
32.82
N


ATOM
1710
CA
PHE A
346
67.759
47.928
42.703
1.00
34.48
C


ATOM
1711
C
PHE A
346
68.103
47.840
44.193
1.00
35.77
C


ATOM
1712
O
PHE A
346
67.859
46.827
44.843
1.00
34.19
O


ATOM
1713
CB
PHE A
346
69.037
47.751
41.881
1.00
34.20
C


ATOM
1714
CG
PHE A
346
69.817
46.518
42.232
1.00
35.55
C


ATOM
1715
CD1
PHE A
346
69.302
45.254
41.964
1.00
34.50
C


ATOM
1716
CD2
PHE A
346
71.060
46.620
42.850
1.00
37.04
C


ATOM
1717
CE1
PHE A
346
70.010
44.107
42.304
1.00
35.77
C


ATOM
1718
CE2
PHE A
346
71.779
45.478
43.198
1.00
38.55
C


ATOM
1719
CZ
PHE A
346
71.250
44.217
42.923
1.00
38.73
C


ATOM
1720
N
GLU A
347
68.660
48.921
44.723
1.00
37.60
N


ATOM
1721
CA
GLU A
347
69.054
48.986
46.122
1.00
40.87
C


ATOM
1722
C
GLU A
347
67.875
48.954
47.091
1.00
40.71
C


ATOM
1723
O
GLU A
347
68.014
48.483
48.218
1.00
41.55
O


ATOM
1724
CB
GLU A
347
69.887
50.247
46.361
1.00
42.18
C


ATOM
1725
CG
GLU A
347
71.112
50.334
45.461
1.00
49.56
C


ATOM
1726
CD
GLU A
347
72.249
49.423
45.901
1.00
54.08
C


ATOM
1727
OE1
GLU A
347
71.994
48.244
46.240
1.00
57.12
O


ATOM
1728
OE2
GLU A
347
73.412
49.887
45.899
1.00
57.88
O


ATOM
1729
N
GLU A
348
66.717
49.446
46.656
1.00
39.71
N


ATOM
1730
CA
GLU A
348
65.543
49.464
47.523
1.00
39.97
C


ATOM
1731
C
GLU A
348
64.782
48.149
47.503
1.00
38.48
C


ATOM
1732
O
GLU A
348
64.283
47.705
48.529
1.00
38.26
O


ATOM
1733
CB
GLU A
348
64.543
50.550
47.100
1.00
41.21
C


ATOM
1734
CG
GLU A
348
65.120
51.879
46.664
1.00
44.97
C


ATOM
1735
CD
GLU A
348
64.044
52.828
46.141
1.00
45.86
C


ATOM
1736
OE1
GLU A
348
63.112
52.360
45.454
1.00
46.60
O


ATOM
1737
OE2
GLU A
348
64.135
54.043
46.405
1.00
48.18
O


ATOM
1738
N
THR A
349
64.696
47.536
46.327
1.00
37.21
N


ATOM
1739
CA
THR A
349
63.922
46.314
46.146
1.00
35.37
C


ATOM
1740
C
THR A
349
64.677
45.019
45.849
1.00
35.43
C


ATOM
1741
O
THR A
349
64.093
43.943
45.910
1.00
36.36
O


ATOM
1742
CB
THR A
349
62.906
46.507
45.004
1.00
35.82
C


ATOM
1743
OG1
THR A
349
63.613
46.564
43.755
1.00
33.52
O


ATOM
1744
CG2
THR A
349
62.116
47.812
45.190
1.00
34.32
C


ATOM
1745
N
GLY A
350
65.957
45.114
45.513
1.00
35.89
N


ATOM
1746
CA
GLY A
350
66.715
43.917
45.183
1.00
34.68
C


ATOM
1747
C
GLY A
350
66.415
43.442
43.766
1.00
33.95
C


ATOM
1748
O
GLY A
350
66.870
42.381
43.339
1.00
35.21
O


ATOM
1749
N
ILE A
351
65.639
44.231
43.029
1.00
33.01
N


ATOM
1750
CA
ILE A
351
65.283
43.885
41.654
1.00
30.90
C


ATOM
1751
C
ILE A
351
66.124
44.690
40.665
1.00
29.41
C


ATOM
1752
O
ILE A
351
66.117
45.911
40.699
1.00
27.96
O


ATOM
1753
CB
ILE A
351
63.795
44.197
41.356
1.00
33.21
C


ATOM
1754
CG1
ILE A
351
62.885
43.471
42.355
1.00
34.74
C


ATOM
1755
CG2
ILE A
351
63.455
43.779
39.930
1.00
32.48
C


ATOM
1756
CD1
ILE A
351
61.424
43.894
42.262
1.00
34.70
C


ATOM
1757
N
TYR A
352
66.842
44.005
39.785
1.00
28.99
N


ATOM
1758
CA
TYR A
352
67.655
44.685
38.787
1.00
28.73
C


ATOM
1759
C
TYR A
352
66.907
44.657
37.464
1.00
28.49
C


ATOM
1760
O
TYR A
352
66.651
43.588
36.921
1.00
27.67
O


ATOM
1761
CB
TYR A
352
69.004
43.991
38.593
1.00
27.77
C


ATOM
1762
CG
TYR A
352
69.899
44.726
37.617
1.00
27.14
C


ATOM
1763
CD1
TYR A
352
70.688
45.799
38.038
1.00
23.99
C


ATOM
1764
CD2
TYR A
352
69.925
44.376
36.267
1.00
26.25
C


ATOM
1765
CE1
TYR A
352
71.481
46.504
37.139
1.00
24.83
C


ATOM
1766
CE2
TYR A
352
70.715
45.076
35.358
1.00
26.68
C


ATOM
1767
CZ
TYR A
352
71.492
46.138
35.804
1.00
24.57
C


ATOM
1768
OH
TYR A
352
72.302
46.809
34.923
1.00
26.41
O


ATOM
1769
N
ILE A
353
66.554
45.831
36.948
1.00
28.02
N


ATOM
1770
CA
ILE A
353
65.843
45.897
35.681
1.00
26.70
C


ATOM
1771
C
ILE A
353
66.761
46.407
34.575
1.00
27.00
C


ATOM
1772
O
ILE A
353
67.247
47.536
34.631
1.00
27.67
O


ATOM
1773
CB
ILE A
353
64.620
46.826
35.780
1.00
28.56
C


ATOM
1774
CG1
ILE A
353
63.702
46.346
36.915
1.00
29.44
C


ATOM
1775
CG2
ILE A
353
63.875
46.840
34.443
1.00
28.04
C


ATOM
1776
CD1
ILE A
353
62.450
47.169
37.103
1.00
27.09
C


ATOM
1777
N
PRO A
354
67.020
45.574
33.556
1.00
26.94
N


ATOM
1778
CA
PRO A
354
67.892
45.999
32.456
1.00
25.14
C


ATOM
1779
C
PRO A
354
67.246
47.162
31.711
1.00
25.78
C


ATOM
1780
O
PRO A
354
66.020
47.210
31.578
1.00
24.81
O


ATOM
1781
CB
PRO A
354
67.988
44.748
31.582
1.00
23.53
C


ATOM
1782
CG
PRO A
354
67.734
43.614
32.558
1.00
24.17
C


ATOM
1783
CD
PRO A
354
66.612
44.167
33.392
1.00
25.08
C


ATOM
1784
N
VAL A
355
68.061
48.106
31.242
1.00
25.52
N


ATOM
1785
CA
VAL A
355
67.524
49.237
30.498
1.00
24.60
C


ATOM
1786
C
VAL A
355
68.152
49.287
29.124
1.00
24.64
C


ATOM
1787
O
VAL A
355
69.309
48.914
28.937
1.00
24.59
O


ATOM
1788
CB
VAL A
355
67.727
50.596
31.233
1.00
24.72
C


ATOM
1789
CG1
VAL A
355
66.987
50.566
32.560
1.00
23.24
C


ATOM
1790
CG2
VAL A
355
69.209
50.905
31.425
1.00
22.37
C


ATOM
1791
N
CYS A
356
67.365
49.746
28.163
1.00
24.56
N


ATOM
1792
CA
CYS A
356
67.794
49.819
26.783
1.00
24.50
C


ATOM
1793
C
CYS A
356
67.869
51.245
26.263
1.00
24.85
C


ATOM
1794
O
CYS A
356
66.901
51.998
26.368
1.00
25.28
O


ATOM
1795
CB
CYS A
356
66.816
49.018
25.919
1.00
24.42
C


ATOM
1796
SG
CYS A
356
67.077
49.153
24.147
1.00
27.02
S


ATOM
1797
N
SER A
357
69.017
51.614
25.704
1.00
24.06
N


ATOM
1798
CA
SER A
357
69.172
52.944
25.123
1.00
24.90
C


ATOM
1799
C
SER A
357
68.681
52.774
23.694
1.00
24.81
C


ATOM
1800
O
SER A
357
69.300
52.076
22.897
1.00
24.49
O


ATOM
1801
CB
SER A
357
70.629
53.394
25.110
1.00
23.83
C


ATOM
1802
OG
SER A
357
70.717
54.691
24.539
1.00
26.00
O


ATOM
1803
N
ASP A
358
67.562
53.414
23.389
1.00
25.07
N


ATOM
1804
CA
ASP A
358
66.927
53.308
22.085
1.00
26.86
C


ATOM
1805
C
ASP A
358
67.067
54.547
21.200
1.00
26.28
C


ATOM
1806
O
ASP A
358
66.510
55.598
21.504
1.00
25.81
O


ATOM
1807
CB
ASP A
358
65.442
52.986
22.309
1.00
26.49
C


ATOM
1808
CG
ASP A
358
64.672
52.770
21.021
1.00
26.81
C


ATOM
1809
OD1
ASP A
358
65.293
52.598
19.949
1.00
28.14
O


ATOM
1810
OD2
ASP A
358
63.425
52.757
21.099
1.00
25.32
O


ATOM
1811
N
GLY A
359
67.811
54.409
20.106
1.00
28.28
N


ATOM
1812
CA
GLY A
359
67.975
55.509
19.174
1.00
30.20
C


ATOM
1813
C
GLY A
359
69.098
56.486
19.460
1.00
33.11
C


ATOM
1814
O
GLY A
359
69.637
56.539
20.564
1.00
32.49
O


ATOM
1815
N
GLY A
360
69.456
57.260
18.442
1.00
34.01
N


ATOM
1816
CA
GLY A
360
70.504
58.243
18.602
1.00
36.30
C


ATOM
1817
C
GLY A
360
71.916
57.755
18.357
1.00
37.16
C


ATOM
1818
O
GLY A
360
72.849
58.538
18.482
1.00
39.18
O


ATOM
1819
N
ILE A
361
72.096
56.481
18.021
1.00
38.47
N


ATOM
1820
CA
ILE A
361
73.442
55.976
17.762
1.00
40.22
C


ATOM
1821
C
ILE A
361
73.856
56.399
16.359
1.00
42.51
C


ATOM
1822
O
ILE A
361
73.296
55.922
15.369
1.00
42.14
O


ATOM
1823
CB
ILE A
361
73.527
54.430
17.848
1.00
40.03
C


ATOM
1824
CG1
ILE A
361
73.133
53.945
19.247
1.00
38.70
C


ATOM
1825
CG2
ILE A
361
74.953
53.974
17.527
1.00
39.30
C


ATOM
1826
CD1
ILE A
361
74.077
54.379
20.352
1.00
38.35
C


ATOM
1827
N
VAL A
362
74.835
57.297
16.284
1.00
44.13
N


ATOM
1828
CA
VAL A
362
75.326
57.799
15.007
1.00
45.18
C


ATOM
1829
C
VAL A
362
76.688
57.200
14.659
1.00
46.18
C


ATOM
1830
O
VAL A
362
76.943
56.875
13.498
1.00
47.54
O


ATOM
1831
CB
VAL A
362
75.437
59.336
15.030
1.00
46.11
C


ATOM
1832
CG1
VAL A
362
75.853
59.856
13.653
1.00
47.64
C


ATOM
1833
CG2
VAL A
362
74.099
59.940
15.440
1.00
47.33
C


ATOM
1834
N
TYR A
363
77.552
57.052
15.665
1.00
44.63
N


ATOM
1835
CA
TYR A
363
78.889
56.482
15.473
1.00
42.52
C


ATOM
1836
C
TYR A
363
79.087
55.265
16.370
1.00
39.50
C


ATOM
1837
O
TYR A
363
78.395
55.109
17.373
1.00
38.80
O


ATOM
1838
CB
TYR A
363
79.960
57.519
15.803
1.00
44.72
C


ATOM
1839
CG
TYR A
363
79.838
58.794
15.010
1.00
48.91
C


ATOM
1840
CD1
TYR A
363
79.930
58.782
13.619
1.00
51.13
C


ATOM
1841
CD2
TYR A
363
79.639
60.016
15.649
1.00
50.12
C


ATOM
1842
CE1
TYR A
363
79.829
59.957
12.882
1.00
53.53
C


ATOM
1843
CE2
TYR A
363
79.538
61.199
14.921
1.00
52.91
C


ATOM
1844
CZ
TYR A
363
79.636
61.162
13.539
1.00
53.71
C


ATOM
1845
OH
TYR A
363
79.567
62.330
12.813
1.00
56.33
O


ATOM
1846
N
ASP A
364
80.040
54.409
16.024
1.00
37.74
N


ATOM
1847
CA
ASP A
364
80.289
53.221
16.831
1.00
37.31
C


ATOM
1848
C
ASP A
364
80.610
53.556
18.282
1.00
36.24
C


ATOM
1849
O
ASP A
364
80.175
52.852
19.192
1.00
37.36
O


ATOM
1850
CB
ASP A
364
81.441
52.389
16.259
1.00
39.54
C


ATOM
1851
CG
ASP A
364
81.104
51.746
14.926
1.00
41.10
C


ATOM
1852
OD1
ASP A
364
79.976
51.235
14.763
1.00
40.94
O


ATOM
1853
OD2
ASP A
364
81.985
51.738
14.042
1.00
44.42
O


ATOM
1854
N
TYR A
365
81.359
54.631
18.508
1.00
33.86
N


ATOM
1855
CA
TYR A
365
81.733
54.989
19.870
1.00
33.09
C


ATOM
1856
C
TYR A
365
80.544
55.418
20.733
1.00
31.64
C


ATOM
1857
O
TYR A
365
80.646
55.456
21.955
1.00
30.06
O


ATOM
1858
CB
TYR A
365
82.828
56.066
19.859
1.00
31.22
C


ATOM
1859
CG
TYR A
365
82.342
57.493
19.813
1.00
34.92
C


ATOM
1860
CD1
TYR A
365
82.131
58.216
20.987
1.00
35.27
C


ATOM
1861
CD2
TYR A
365
82.136
58.140
18.595
1.00
36.06
C


ATOM
1862
CE1
TYR A
365
81.735
59.549
20.948
1.00
37.45
C


ATOM
1863
CE2
TYR A
365
81.738
59.476
18.545
1.00
38.40
C


ATOM
1864
CZ
TYR A
365
81.543
60.173
19.724
1.00
38.62
C


ATOM
1865
OH
TYR A
365
81.174
61.500
19.676
1.00
43.03
O


ATOM
1866
N
HIS A
366
79.420
55.737
20.098
1.00
31.37
N


ATOM
1867
CA
HIS A
366
78.231
56.110
20.850
1.00
30.85
C


ATOM
1868
C
HIS A
366
77.743
54.859
21.571
1.00
28.97
C


ATOM
1869
O
HIS A
366
77.130
54.947
22.630
1.00
28.47
O


ATOM
1870
CB
HIS A
366
77.125
56.635
19.926
1.00
31.13
C


ATOM
1871
CG
HIS A
366
77.373
58.016
19.406
1.00
31.77
C


ATOM
1872
ND1
HIS A
366
78.311
58.862
19.957
1.00
33.13
N


ATOM
1873
CD2
HIS A
366
76.765
58.719
18.422
1.00
31.89
C


ATOM
1874
CE1
HIS A
366
78.267
60.028
19.339
1.00
31.00
C


ATOM
1875
NE2
HIS A
366
77.337
59.968
18.405
1.00
32.26
N


ATOM
1876
N
MET A
367
78.017
53.697
20.979
1.00
27.68
N


ATOM
1877
CA
MET A
367
77.633
52.419
21.580
1.00
28.37
C


ATOM
1878
C
MET A
367
78.372
52.283
22.909
1.00
26.83
C


ATOM
1879
O
MET A
367
77.774
51.998
23.938
1.00
27.33
O


ATOM
1880
CB
MET A
367
78.027
51.240
20.678
1.00
26.41
C


ATOM
1881
CG
MET A
367
77.301
51.164
19.333
1.00
29.28
C


ATOM
1882
SD
MET A
367
77.864
49.737
18.350
1.00
31.67
S


ATOM
1883
CE
MET A
367
76.804
49.861
16.903
1.00
31.17
C


ATOM
1884
N
THR A
368
79.686
52.485
22.868
1.00
27.26
N


ATOM
1885
CA
THR A
368
80.519
52.393
24.062
1.00
27.02
C


ATOM
1886
C
THR A
368
80.035
53.402
25.106
1.00
26.24
C


ATOM
1887
O
THR A
368
79.960
53.092
26.288
1.00
26.81
O


ATOM
1888
CB
THR A
368
81.998
52.667
23.713
1.00
27.29
C


ATOM
1889
OG1
THR A
368
82.350
51.907
22.548
1.00
28.57
O


ATOM
1890
CG2
THR A
368
82.912
52.252
24.861
1.00
26.87
C


ATOM
1891
N
LEU A
369
79.701
54.610
24.664
1.00
25.92
N


ATOM
1892
CA
LEU A
369
79.205
55.636
25.578
1.00
27.25
C


ATOM
1893
C
LEU A
369
77.913
55.206
26.263
1.00
25.90
C


ATOM
1894
O
LEU A
369
77.805
55.280
27.483
1.00
26.13
O


ATOM
1895
CB
LEU A
369
78.956
56.949
24.835
1.00
27.34
C


ATOM
1896
CG
LEU A
369
80.177
57.813
24.525
1.00
30.74
C


ATOM
1897
CD1
LEU A
369
79.731
59.030
23.718
1.00
30.74
C


ATOM
1898
CD2
LEU A
369
80.855
58.244
25.823
1.00
27.53
C


ATOM
1899
N
ALA A
370
76.946
54.755
25.464
1.00
25.24
N


ATOM
1900
CA
ALA A
370
75.644
54.313
25.966
1.00
25.58
C


ATOM
1901
C
ALA A
370
75.804
53.233
27.037
1.00
23.76
C


ATOM
1902
O
ALA A
370
75.192
53.294
28.099
1.00
24.01
O


ATOM
1903
CB
ALA A
370
74.792
53.787
24.809
1.00
20.78
C


ATOM
1904
N
LEU A
371
76.638
52.248
26.745
1.00
24.06
N


ATOM
1905
CA
LEU A
371
76.892
51.162
27.677
1.00
24.06
C


ATOM
1906
C
LEU A
371
77.599
51.698
28.926
1.00
24.64
C


ATOM
1907
O
LEU A
371
77.223
51.360
30.042
1.00
24.05
O


ATOM
1908
CB
LEU A
371
77.750
50.086
26.990
1.00
22.32
C


ATOM
1909
CG
LEU A
371
77.084
49.415
25.772
1.00
25.62
C


ATOM
1910
CD1
LEU A
371
78.104
48.572
25.004
1.00
24.75
C


ATOM
1911
CD2
LEU A
371
75.909
48.553
26.227
1.00
23.36
C


ATOM
1912
N
ALA A
372
78.607
52.549
28.732
1.00
23.99
N


ATOM
1913
CA
ALA A
372
79.367
53.109
29.844
1.00
24.54
C


ATOM
1914
C
ALA A
372
78.484
53.911
30.774
1.00
26.37
C


ATOM
1915
O
ALA A
372
78.699
53.920
31.984
1.00
26.64
O


ATOM
1916
CB
ALA A
372
80.505
53.989
29.329
1.00
23.23
C


ATOM
1917
N
MET A
373
77.496
54.598
30.207
1.00
26.85
N


ATOM
1918
CA
MET A
373
76.591
55.395
31.017
1.00
26.45
C


ATOM
1919
C
MET A
373
75.617
54.514
31.795
1.00
25.55
C


ATOM
1920
O
MET A
373
74.883
55.009
32.634
1.00
26.24
O


ATOM
1921
CB
MET A
373
75.834
56.402
30.145
1.00
25.35
C


ATOM
1922
CG
MET A
373
76.704
57.547
29.626
1.00
27.17
C


ATOM
1923
SD
MET A
373
75.865
58.517
28.344
1.00
27.74
S


ATOM
1924
CE
MET A
373
77.157
59.681
27.884
1.00
26.78
C


ATOM
1925
N
GLY A
374
75.603
53.212
31.518
1.00
25.87
N


ATOM
1926
CA
GLY A
374
74.725
52.327
32.269
1.00
24.01
C


ATOM
1927
C
GLY A
374
73.710
51.500
31.506
1.00
24.90
C


ATOM
1928
O
GLY A
374
73.120
50.581
32.073
1.00
26.82
O


ATOM
1929
N
ALA A
375
73.472
51.818
30.241
1.00
23.59
N


ATOM
1930
CA
ALA A
375
72.521
51.035
29.468
1.00
24.75
C


ATOM
1931
C
ALA A
375
73.061
49.611
29.345
1.00
25.43
C


ATOM
1932
O
ALA A
375
74.255
49.411
29.116
1.00
25.89
O


ATOM
1933
CB
ALA A
375
72.325
51.644
28.085
1.00
21.49
C


ATOM
1934
N
ASP A
376
72.182
48.627
29.506
1.00
25.62
N


ATOM
1935
CA
ASP A
376
72.571
47.221
29.406
1.00
26.07
C


ATOM
1936
C
ASP A
376
72.671
46.809
27.945
1.00
25.46
C


ATOM
1937
O
ASP A
376
73.531
46.017
27.573
1.00
25.47
O


ATOM
1938
CB
ASP A
376
71.559
46.355
30.147
1.00
24.89
C


ATOM
1939
CG
ASP A
376
71.472
46.713
31.616
1.00
25.22
C


ATOM
1940
OD1
ASP A
376
72.272
46.174
32.413
1.00
25.77
O


ATOM
1941
OD2
ASP A
376
70.616
47.549
31.971
1.00
25.29
O


ATOM
1942
N
PHE A
377
71.779
47.339
27.117
1.00
26.78
N


ATOM
1943
CA
PHE A
377
71.834
47.053
25.695
1.00
26.93
C


ATOM
1944
C
PHE A
377
71.331
48.236
24.876
1.00
26.74
C


ATOM
1945
O
PHE A
377
70.791
49.205
25.416
1.00
25.26
O


ATOM
1946
CB
PHE A
377
71.108
45.742
25.327
1.00
26.14
C


ATOM
1947
CG
PHE A
377
69.704
45.638
25.836
1.00
28.33
C


ATOM
1948
CD1
PHE A
377
69.451
45.223
27.141
1.00
28.91
C


ATOM
1949
CD2
PHE A
377
68.626
45.898
24.992
1.00
26.99
C


ATOM
1950
CE1
PHE A
377
68.137
45.064
27.597
1.00
29.14
C


ATOM
1951
CE2
PHE A
377
67.316
45.742
25.438
1.00
27.18
C


ATOM
1952
CZ
PHE A
377
67.072
45.323
26.741
1.00
28.12
C


ATOM
1953
N
ILE A
378
71.526
48.150
23.567
1.00
26.27
N


ATOM
1954
CA
ILE A
378
71.188
49.241
22.669
1.00
27.14
C


ATOM
1955
C
ILE A
378
70.242
48.824
21.556
1.00
27.25
C


ATOM
1956
O
ILE A
378
70.423
47.774
20.947
1.00
28.04
O


ATOM
1957
CB
ILE A
378
72.497
49.788
22.032
1.00
27.66
C


ATOM
1958
CG1
ILE A
378
73.491
50.146
23.137
1.00
28.26
C


ATOM
1959
CG2
ILE A
378
72.217
51.011
21.159
1.00
28.62
C


ATOM
1960
CD1
ILE A
378
74.915
50.248
22.644
1.00
30.77
C


ATOM
1961
N
MET A
379
69.226
49.641
21.301
1.00
26.60
N


ATOM
1962
CA
MET A
379
68.293
49.346
20.217
1.00
27.52
C


ATOM
1963
C
MET A
379
68.654
50.271
19.054
1.00
27.68
C


ATOM
1964
O
MET A
379
68.784
51.478
19.232
1.00
26.96
O


ATOM
1965
CB
MET A
379
66.838
49.581
20.645
1.00
26.96
C


ATOM
1966
CG
MET A
379
65.844
49.295
19.524
1.00
28.29
C


ATOM
1967
SD
MET A
379
64.114
49.244
20.007
1.00
26.79
S


ATOM
1968
CE
MET A
379
63.985
47.548
20.606
1.00
27.87
C


ATOM
1969
N
LEU A
380
68.829
49.701
17.868
1.00
29.02
N


ATOM
1970
CA
LEU A
380
69.181
50.503
16.706
1.00
29.48
C


ATOM
1971
C
LEU A
380
68.279
50.225
15.516
1.00
29.03
C


ATOM
1972
O
LEU A
380
67.880
49.086
15.275
1.00
29.34
O


ATOM
1973
CB
LEU A
380
70.642
50.258
16.301
1.00
29.79
C


ATOM
1974
CG
LEU A
380
71.722
50.470
17.368
1.00
30.01
C


ATOM
1975
CD1
LEU A
380
71.783
49.227
18.259
1.00
31.49
C


ATOM
1976
CD2
LEU A
380
73.079
50.693
16.714
1.00
30.65
C


ATOM
1977
N
GLY A
381
67.960
51.283
14.780
1.00
30.37
N


ATOM
1978
CA
GLY A
381
67.122
51.155
13.602
1.00
31.25
C


ATOM
1979
C
GLY A
381
67.941
51.401
12.348
1.00
30.92
C


ATOM
1980
O
GLY A
381
68.210
50.485
11.581
1.00
30.18
O


ATOM
1981
N
ARG A
382
68.351
52.646
12.147
1.00
33.69
N


ATOM
1982
CA
ARG A
382
69.142
53.014
10.977
1.00
36.36
C


ATOM
1983
C
ARG A
382
70.371
52.125
10.772
1.00
36.33
C


ATOM
1984
O
ARG A
382
70.645
51.681
9.656
1.00
35.82
O


ATOM
1985
CB
ARG A
382
69.585
54.472
11.084
1.00
38.87
C


ATOM
1986
CG
ARG A
382
70.584
54.858
10.023
1.00
45.32
C


ATOM
1987
CD
ARG A
382
71.228
56.211
10.282
1.00
50.37
C


ATOM
1988
NE
ARG A
382
72.434
56.333
9.470
1.00
54.70
N


ATOM
1989
CZ
ARG A
382
73.548
55.638
9.685
1.00
55.84
C


ATOM
1990
NH1
ARG A
382
73.614
54.780
10.700
1.00
56.30
N


ATOM
1991
NH2
ARG A
382
74.582
55.774
8.863
1.00
56.90
N


ATOM
1992
N
TYR A
383
71.109
51.877
11.851
1.00
35.02
N


ATOM
1993
CA
TYR A
383
72.311
51.044
11.808
1.00
33.31
C


ATOM
1994
C
TYR A
383
72.059
49.714
11.093
1.00
32.20
C


ATOM
1995
O
TYR A
383
72.818
49.323
10.209
1.00
32.03
O


ATOM
1996
CB
TYR A
383
72.808
50.781
13.237
1.00
31.93
C


ATOM
1997
CG
TYR A
383
74.023
49.884
13.333
1.00
30.42
C


ATOM
1998
CD1
TYR A
383
75.316
50.413
13.303
1.00
30.08
C


ATOM
1999
CD2
TYR A
383
73.879
48.501
13.445
1.00
29.35
C


ATOM
2000
CE1
TYR A
383
76.431
49.586
13.384
1.00
29.62
C


ATOM
2001
CE2
TYR A
383
74.983
47.665
13.527
1.00
27.30
C


ATOM
2002
CZ
TYR A
383
76.254
48.210
13.495
1.00
29.91
C


ATOM
2003
OH
TYR A
383
77.342
47.373
13.556
1.00
29.92
O


ATOM
2004
N
PHE A
384
70.988
49.029
11.477
1.00
30.96
N


ATOM
2005
CA
PHE A
384
70.635
47.741
10.884
1.00
32.01
C


ATOM
2006
C
PHE A
384
69.907
47.827
9.533
1.00
33.62
C


ATOM
2007
O
PHE A
384
69.951
46.886
8.744
1.00
33.74
O


ATOM
2008
CB
PHE A
384
69.773
46.939
11.862
1.00
30.96
C


ATOM
2009
CG
PHE A
384
70.526
46.421
13.063
1.00
32.53
C


ATOM
2010
CD1
PHE A
384
71.443
45.375
12.931
1.00
29.92
C


ATOM
2011
CD2
PHE A
384
70.301
46.963
14.330
1.00
28.33
C


ATOM
2012
CE1
PHE A
384
72.123
44.874
14.045
1.00
30.70
C


ATOM
2013
CE2
PHE A
384
70.971
46.471
15.444
1.00
30.80
C


ATOM
2014
CZ
PHE A
384
71.886
45.421
15.303
1.00
28.49
C


ATOM
2015
N
ALA A
385
69.234
48.943
9.269
1.00
35.08
N


ATOM
2016
CA
ALA A
385
68.504
49.104
8.010
1.00
36.64
C


ATOM
2017
C
ALA A
385
69.441
49.035
6.805
1.00
38.11
C


ATOM
2018
O
ALA A
385
69.051
48.586
5.731
1.00
38.07
O


ATOM
2019
CB
ALA A
385
67.752
50.429
8.009
1.00
35.59
C


ATOM
2020
N
ARG A
386
70.682
49.475
7.004
1.00
39.97
N


ATOM
2021
CA
ARG A
386
71.701
49.491
5.958
1.00
39.58
C


ATOM
2022
C
ARG A
386
72.150
48.109
5.488
1.00
40.10
C


ATOM
2023
O
ARG A
386
72.819
47.989
4.457
1.00
39.76
O


ATOM
2024
CB
ARG A
386
72.945
50.232
6.449
1.00
40.19
C


ATOM
2025
CG
ARG A
386
72.755
51.685
6.835
1.00
43.04
C


ATOM
2026
CA
ARG A
386
74.036
52.170
7.499
1.00
45.06
C


ATOM
2027
NE
ARG A
386
74.404
51.264
8.585
1.00
46.41
N


ATOM
2028
CZ
ARG A
386
75.644
51.055
9.015
1.00
45.80
C


ATOM
2029
NH1
ARG A
386
76.667
51.690
8.455
1.00
45.90
N


ATOM
2030
NH2
ARG A
386
75.860
50.190
9.996
1.00
44.95
N


ATOM
2031
N
PHE A
387
71.798
47.071
6.238
1.00
40.02
N


ATOM
2032
CA
PHE A
387
72.229
45.726
5.883
1.00
40.37
C


ATOM
2033
C
PHE A
387
71.346
44.966
4.892
1.00
41.94
C


ATOM
2034
O
PHE A
387
70.143
45.207
4.769
1.00
41.59
O


ATOM
2035
CB
PHE A
387
72.417
44.877
7.149
1.00
39.91
C


ATOM
2036
CG
PHE A
387
73.319
45.506
8.183
1.00
40.02
C


ATOM
2037
CD1
PHE A
387
74.411
46.283
7.801
1.00
39.37
C


ATOM
2038
CD2
PHE A
387
73.084
45.308
9.544
1.00
39.37
C


ATOM
2039
CE1
PHE A
387
75.255
46.855
8.755
1.00
40.23
C


ATOM
2040
CE2
PHE A
387
73.921
45.872
10.510
1.00
38.11
C


ATOM
2041
CZ
PHE A
387
75.009
46.648
10.117
1.00
39.23
C


ATOM
2042
N
GLU A
388
71.985
44.040
4.190
1.00
42.30
N


ATOM
2043
CA
GLU A
388
71.340
43.194
3.200
1.00
42.95
C


ATOM
2044
C
GLU A
388
70.103
42.530
3.784
1.00
41.98
C


ATOM
2045
O
GLU A
388
69.080
42.401
3.108
1.00
41.50
O


ATOM
2046
CB
GLU A
388
72.331
42.118
2.740
1.00
44.78
C


ATOM
2047
CG
GLU A
388
71.786
41.096
1.749
1.00
48.50
C


ATOM
2048
CD
GLU A
388
71.457
41.708
0.400
1.00
51.34
C


ATOM
2049
OE1
GLU A
388
72.306
42.458
−0.130
1.00
52.78
O


ATOM
2050
OE2
GLU A
388
70.359
41.435
−0.134
1.00
53.13
O


ATOM
2051
N
GLU A
389
70.200
42.128
5.049
1.00
40.73
N


ATOM
2052
CA
GLU A
389
69.107
41.441
5.722
1.00
39.64
C


ATOM
2053
C
GLU A
389
67.884
42.266
6.125
1.00
38.63
C


ATOM
2054
O
GLU A
389
66.879
41.699
6.541
1.00
38.65
O


ATOM
2055
CB
GLU A
389
69.648
40.678
6.937
1.00
39.65
C


ATOM
2056
CG
GLU A
389
70.631
39.577
6.567
1.00
39.31
C


ATOM
2057
CD
GLU A
389
72.088
39.993
6.699
1.00
39.13
C


ATOM
2058
OE1
GLU A
389
72.409
41.184
6.511
1.00
37.80
O


ATOM
2059
OE2
GLU A
389
72.924
39.112
6.982
1.00
38.72
O


ATOM
2060
N
SER A
390
67.951
43.589
6.020
1.00
38.90
N


ATOM
2061
CA
SER A
390
66.783
44.398
6.362
1.00
42.49
C


ATOM
2062
C
SER A
390
65.734
44.108
5.276
1.00
44.51
C


ATOM
2063
O
SER A
390
66.069
44.008
4.092
1.00
44.30
O


ATOM
2064
CB
SER A
390
67.130
45.886
6.393
1.00
41.33
C


ATOM
2065
OG
SER A
390
67.521
46.348
5.116
1.00
46.43
O


ATOM
2066
N
PRO A
391
64.454
43.985
5.669
1.00
45.30
N


ATOM
2067
CA
PRO A
391
63.317
43.691
4.785
1.00
47.36
C


ATOM
2068
C
PRO A
391
62.956
44.730
3.725
1.00
48.75
C


ATOM
2069
O
PRO A
391
61.909
44.625
3.089
1.00
50.35
O


ATOM
2070
CB
PRO A
391
62.176
43.478
5.775
1.00
46.19
C


ATOM
2071
CG
PRO A
391
62.473
44.525
6.804
1.00
44.91
C


ATOM
2072
CD
PRO A
391
63.975
44.374
7.010
1.00
44.19
C


ATOM
2073
N
THR A
392
63.806
45.727
3.529
1.00
49.99
N


ATOM
2074
CA
THR A
392
63.507
46.755
2.549
1.00
51.23
C


ATOM
2075
C
THR A
392
64.213
46.535
1.217
1.00
53.82
C


ATOM
2076
O
THR A
392
65.077
45.665
1.083
1.00
54.85
O


ATOM
2077
CB
THR A
392
63.863
48.152
3.084
1.00
49.99
C


ATOM
2078
OG1
THR A
392
65.261
48.209
3.375
1.00
50.17
O


ATOM
2079
CG2
THR A
392
63.070
48.450
4.351
1.00
49.74
C


ATOM
2080
N
ARG A
393
63.835
47.336
0.230
1.00
55.66
N


ATOM
2081
CA
ARG A
393
64.407
47.224
−1.098
1.00
58.14
C


ATOM
2082
C
ARG A
393
65.744
47.930
−1.238
1.00
58.48
C


ATOM
2083
O
ARG A
393
65.950
49.023
−0.709
1.00
57.12
O


ATOM
2084
CB
ARG A
393
63.419
47.766
−2.134
1.00
59.64
C


ATOM
2085
CG
ARG A
393
62.178
46.895
−2.315
1.00
62.55
C


ATOM
2086
CD
ARG A
393
61.092
47.637
−3.073
1.00
64.17
C


ATOM
2087
NE
ARG A
393
61.646
48.361
−4.210
1.00
65.75
N


ATOM
2088
CZ
ARG A
393
61.462
49.659
−4.423
1.00
67.27
C


ATOM
2089
NH1
ARG A
393
60.732
50.372
−3.576
1.00
66.89
N


ATOM
2090
NH2
ARG A
393
62.024
50.248
−5.472
1.00
68.47
N


ATOM
2091
N
LYS A
394
66.650
47.276
−1.957
1.00
59.95
N


ATOM
2092
CA
LYS A
394
67.979
47.805
−2.217
1.00
61.71
C


ATOM
2093
C
LYS A
394
67.835
48.647
−3.479
1.00
63.80
C


ATOM
2094
O
LYS A
394
67.576
48.116
−4.555
1.00
64.78
O


ATOM
2095
CB
LYS A
394
68.953
46.652
−2.456
1.00
59.47
C


ATOM
2096
CG
LYS A
394
70.408
47.017
−2.271
1.00
57.65
C


ATOM
2097
CD
LYS A
394
71.316
45.886
−2.715
1.00
56.24
C


ATOM
2098
CE
LYS A
394
71.039
44.606
−1.958
1.00
54.65
C


ATOM
2099
NZ
LYS A
394
71.894
43.500
−2.462
1.00
53.21
N


ATOM
2100
N
VAL A
395
67.994
49.959
−3.343
1.00
66.61
N


ATOM
2101
CA
VAL A
395
67.840
50.863
−4.474
1.00
69.32
C


ATOM
2102
C
VAL A
395
69.118
51.577
−4.896
1.00
71.12
C


ATOM
2103
O
VAL A
395
69.663
52.384
−4.145
1.00
71.80
O


ATOM
2104
CB
VAL A
395
66.775
51.935
−4.168
1.00
69.81
C


ATOM
2105
CG1
VAL A
395
66.653
52.901
−5.338
1.00
71.62
C


ATOM
2106
CG2
VAL A
395
65.438
51.270
−3.884
1.00
70.98
C


ATOM
2107
N
THR A
396
69.581
51.287
−6.109
1.00
73.05
N


ATOM
2108
CA
THR A
396
70.783
51.921
−6.644
1.00
74.05
C


ATOM
2109
C
THR A
396
70.409
53.303
−7.163
1.00
74.87
C


ATOM
2110
O
THR A
396
69.793
53.428
−8.222
1.00
75.03
O


ATOM
2111
CB
THR A
396
71.381
51.106
−7.804
1.00
74.00
C


ATOM
2112
OG1
THR A
396
71.715
49.791
−7.343
1.00
74.43
O


ATOM
2113
CG2
THR A
396
72.638
51.781
−8.336
1.00
74.35
C


ATOM
2114
N
ILE A
397
70.784
54.335
−6.415
1.00
75.83
N


ATOM
2115
CA
ILE A
397
70.472
55.710
−6.788
1.00
76.89
C


ATOM
2116
C
ILE A
397
71.681
56.521
−7.251
1.00
77.53
C


ATOM
2117
O
ILE A
397
72.537
56.897
−6.449
1.00
77.96
O


ATOM
2118
CB
ILE A
397
69.817
56.466
−5.612
1.00
77.21
C


ATOM
2119
CG1
ILE A
397
68.525
55.761
−5.196
1.00
77.37
C


ATOM
2120
CG2
ILE A
397
69.538
57.911
−6.010
1.00
76.96
C


ATOM
2121
CD1
ILE A
397
67.820
56.415
−4.025
1.00
78.15
C


ATOM
2122
N
ASN A
398
71.736
56.793
−8.551
1.00
78.03
N


ATOM
2123
CA
ASN A
398
72.814
57.583
−9.131
1.00
77.85
C


ATOM
2124
C
ASN A
398
74.200
57.051
−8.758
1.00
76.64
C


ATOM
2125
O
ASN A
398
75.036
57.787
−8.229
1.00
76.51
O


ATOM
2126
CB
ASN A
398
72.667
59.042
−8.679
1.00
79.57
C


ATOM
2127
CG
ASN A
398
73.387
60.019
−9.595
1.00
82.07
C


ATOM
2128
OD1
ASN A
398
74.617
60.007
−9.700
1.00
83.51
O


ATOM
2129
ND2
ASN A
398
72.618
60.874
−10.266
1.00
82.25
N


ATOM
2130
N
GLY A
399
74.434
55.768
−9.026
1.00
75.00
N


ATOM
2131
CA
GLY A
399
75.724
55.165
−8.730
1.00
72.65
C


ATOM
2132
C
GLY A
399
75.916
54.587
−7.336
1.00
71.38
C


ATOM
2133
O
GLY A
399
76.745
53.695
−7.143
1.00
71.58
O


ATOM
2134
N
SER A
400
75.163
55.087
−6.361
1.00
69.39
N


ATOM
2135
CA
SER A
400
75.283
54.609
−4.985
1.00
66.71
C


ATOM
2136
C
SER A
400
74.121
53.723
−4.565
1.00
64.95
C


ATOM
2137
O
SER A
400
72.958
54.084
−4.734
1.00
65.32
O


ATOM
2138
CB
SER A
400
75.381
55.794
−4.023
1.00
66.11
C


ATOM
2139
OG
SER A
400
76.546
56.557
−4.273
1.00
66.69
O


ATOM
2140
N
VAL A
401
74.440
52.561
−4.011
1.00
62.49
N


ATOM
2141
CA
VAL A
401
73.412
51.639
−3.557
1.00
60.52
C


ATOM
2142
C
VAL A
401
72.905
52.092
−2.190
1.00
60.36
C


ATOM
2143
O
VAL A
401
73.689
52.313
−1.261
1.00
60.61
O


ATOM
2144
CB
VAL A
401
73.960
50.203
−3.453
1.00
59.89
C


ATOM
2145
CG1
VAL A
401
72.869
49.261
−2.978
1.00
58.28
C


ATOM
2146
CG2
VAL A
401
74.496
49.758
−4.805
1.00
59.96
C


ATOM
2147
N
MET A
402
71.588
52.237
−2.079
1.00
58.65
N


ATOM
2148
CA
MET A
402
70.957
52.672
−0.841
1.00
56.16
C


ATOM
2149
C
MET A
402
69.885
51.671
−0.435
1.00
54.18
C


ATOM
2150
O
MET A
402
69.568
50.747
−1.186
1.00
53.12
O


ATOM
2151
CB
MET A
402
70.297
54.038
−1.038
1.00
58.26
C


ATOM
2152
CG
MET A
402
71.168
55.081
−1.713
1.00
59.17
C


ATOM
2153
SD
MET A
402
72.561
55.584
−0.705
1.00
63.98
S


ATOM
2154
CE
MET A
402
71.781
56.836
0.332
1.00
60.67
C


ATOM
2155
N
LYS A
403
69.340
51.856
0.764
1.00
51.25
N


ATOM
2156
CA
LYS A
403
68.267
51.007
1.267
1.00
48.15
C


ATOM
2157
C
LYS A
403
67.185
51.913
1.828
1.00
47.01
C


ATOM
2158
O
LYS A
403
67.473
52.981
2.369
1.00
46.14
O


ATOM
2159
CB
LYS A
403
68.760
50.049
2.357
1.00
47.38
C


ATOM
2160
CG
LYS A
403
69.675
48.948
1.850
1.00
46.96
C


ATOM
2161
CD
LYS A
403
69.389
47.602
2.514
1.00
46.69
C


ATOM
2162
CE
LYS A
403
68.052
47.027
2.054
1.00
45.74
C


ATOM
2163
NZ
LYS A
403
67.823
45.633
2.534
1.00
43.06
N


ATOM
2164
N
GLU A
404
65.937
51.491
1.683
1.00
46.11
N


ATOM
2165
CA
GLU A
404
64.817
52.276
2.171
1.00
46.13
C


ATOM
2166
C
GLU A
404
64.767
52.246
3.689
1.00
44.64
C


ATOM
2167
O
GLU A
404
65.107
51.243
4.316
1.00
43.82
O


ATOM
2168
CB
GLU A
404
63.506
51.725
1.616
1.00
47.95
C


ATOM
2169
CG
GLU A
404
63.453
51.663
0.101
1.00
52.21
C


ATOM
2170
CD
GLU A
404
62.145
51.099
−0.405
1.00
53.46
C


ATOM
2171
OE1
GLU A
404
61.875
49.900
−0.160
1.00
54.61
O


ATOM
2172
OE2
GLU A
404
61.386
51.860
−1.042
1.00
54.88
O


ATOM
2173
N
TYR A
405
64.336
53.354
4.272
1.00
43.31
N


ATOM
2174
CA
TYR A
405
64.228
53.454
5.714
1.00
42.00
C


ATOM
2175
C
TYR A
405
63.190
54.501
6.056
1.00
40.73
C


ATOM
2176
O
TYR A
405
63.323
55.662
5.688
1.00
41.74
O


ATOM
2177
CB
TYR A
405
65.577
53.837
6.328
1.00
41.52
C


ATOM
2178
CG
TYR A
405
65.571
53.885
7.839
1.00
40.73
C


ATOM
2179
CD1
TYR A
405
65.154
52.787
8.588
1.00
39.95
C


ATOM
2180
CD2
TYR A
405
66.002
55.020
8.521
1.00
40.92
C


ATOM
2181
CE1
TYR A
405
65.167
52.817
9.983
1.00
40.74
C


ATOM
2182
CE2
TYR A
405
66.019
55.061
9.913
1.00
40.89
C


ATOM
2183
CZ
TYR A
405
65.599
53.957
10.637
1.00
40.10
C


ATOM
2184
OH
TYR A
405
65.596
54.003
12.011
1.00
39.70
O


ATOM
2185
N
TRP A
406
62.150
54.082
6.760
1.00
39.11
N


ATOM
2186
CA
TRP A
406
61.091
54.993
7.153
1.00
37.83
C


ATOM
2187
C
TRP A
406
60.708
54.695
8.594
1.00
36.75
C


ATOM
2188
O
TRP A
406
60.862
53.566
9.057
1.00
36.18
O


ATOM
2189
CB
TRP A
406
59.887
54.829
6.209
1.00
34.87
C


ATOM
2190
CG
TRP A
406
59.258
53.464
6.225
1.00
32.13
C


ATOM
2191
CD1
TRP A
406
58.274
53.030
7.061
1.00
31.21
C


ATOM
2192
CD2
TRP A
406
59.574
52.357
5.371
1.00
31.79
C


ATOM
2193
NE1
TRP A
406
57.954
51.729
6.784
1.00
31.89
N


ATOM
2194
CE2
TRP A
406
58.736
51.287
5.752
1.00
31.65
C


ATOM
2195
CE3
TRP A
406
60.483
52.165
4.322
1.00
32.48
C


ATOM
2196
CZ2
TRP A
406
58.776
50.034
5.119
1.00
32.31
C


ATOM
2197
CZ3
TRP A
406
60.524
50.915
3.690
1.00
33.57
C


ATOM
2198
CH2
TRP A
406
59.674
49.869
4.094
1.00
32.43
C


ATOM
2199
N
GLY A
407
60.229
55.717
9.298
1.00
37.66
N


ATOM
2200
CA
GLY A
407
59.835
55.554
10.685
1.00
38.09
C


ATOM
2201
C
GLY A
407
58.446
54.963
10.858
1.00
39.18
C


ATOM
2202
O
GLY A
407
57.629
54.993
9.939
1.00
38.93
O


ATOM
2203
N
GLU A
408
58.183
54.419
12.042
1.00
39.46
N


ATOM
2204
CA
GLU A
408
56.888
53.822
12.350
1.00
40.78
C


ATOM
2205
C
GLU A
408
55.792
54.880
12.425
1.00
42.44
C


ATOM
2206
O
GLU A
408
54.607
54.563
12.370
1.00
43.17
O


ATOM
2207
CB
GLU A
408
56.963
53.062
13.674
1.00
39.22
C


ATOM
2208
CG
GLU A
408
57.763
51.777
13.589
1.00
37.81
C


ATOM
2209
CD
GLU A
408
57.106
50.743
12.681
1.00
37.71
C


ATOM
2210
OE1
GLU A
408
56.007
50.266
13.022
1.00
37.89
O


ATOM
2211
OE2
GLU A
408
57.685
50.408
11.628
1.00
37.24
O


ATOM
2212
N
GLY A
409
56.200
56.139
12.543
1.00
44.48
N


ATOM
2213
CA
GLY A
409
55.242
57.227
12.623
1.00
46.13
C


ATOM
2214
C
GLY A
409
54.866
57.805
11.269
1.00
47.54
C


ATOM
2215
O
GLY A
409
53.909
58.566
11.166
1.00
47.48
O


ATOM
2216
N
SER A
410
55.611
57.450
10.227
1.00
49.11
N


ATOM
2217
CA
SER A
410
55.316
57.956
8.893
1.00
51.17
C


ATOM
2218
C
SER A
410
54.028
57.319
8.381
1.00
53.44
C


ATOM
2219
O
SER A
410
53.676
56.205
8.777
1.00
52.20
O


ATOM
2220
CB
SER A
410
56.465
57.646
7.928
1.00
50.64
C


ATOM
2221
OG
SER A
410
56.489
56.273
7.580
1.00
52.23
O


ATOM
2222
N
SER A
411
53.328
58.033
7.503
1.00
55.87
N


ATOM
2223
CA
SER A
411
52.074
57.547
6.937
1.00
58.48
C


ATOM
2224
C
SER A
411
52.303
56.253
6.170
1.00
59.75
C


ATOM
2225
O
SER A
411
51.425
55.393
6.100
1.00
59.90
O


ATOM
2226
CB
SER A
411
51.481
58.605
6.006
1.00
59.49
C


ATOM
2227
OG
SER A
411
52.433
59.025
5.042
1.00
60.32
O


ATOM
2228
N
ARG A
412
53.498
56.122
5.605
1.00
61.10
N


ATOM
2229
CA
ARG A
412
53.867
54.939
4.841
1.00
62.63
C


ATOM
2230
C
ARG A
412
53.824
53.667
5.686
1.00
64.23
C


ATOM
2231
O
ARG A
412
54.057
52.572
5.177
1.00
63.68
O


ATOM
2232
CB
ARG A
412
55.273
55.114
4.254
1.00
60.98
C


ATOM
2233
CG
ARG A
412
55.772
53.904
3.483
1.00
59.74
C


ATOM
2234
CD
ARG A
412
57.137
54.136
2.871
1.00
58.42
C


ATOM
2235
NE
ARG A
412
57.566
52.982
2.086
1.00
57.23
N


ATOM
2236
CZ
ARG A
412
58.706
52.918
1.406
1.00
57.66
C


ATOM
2237
NH1
ARG A
412
59.547
53.944
1.409
1.00
56.64
N


ATOM
2238
NH2
ARG A
412
59.002
51.825
0.718
1.00
58.20
N


ATOM
2239
N
ALA A
413
53.514
53.806
6.972
1.00
67.55
N


ATOM
2240
CA
ALA A
413
53.480
52.643
7.851
1.00
70.19
C


ATOM
2241
C
ALA A
413
52.367
52.630
8.894
1.00
72.70
C


ATOM
2242
O
ALA A
413
51.812
51.573
9.189
1.00
72.87
O


ATOM
2243
CB
ALA A
413
54.828
52.496
8.548
1.00
70.18
C


ATOM
2244
N
ARG A
414
52.045
53.794
9.456
1.00
76.29
N


ATOM
2245
CA
ARG A
414
51.020
53.864
10.492
1.00
79.14
C


ATOM
2246
C
ARG A
414
49.605
53.528
10.021
1.00
80.91
C


ATOM
2247
O
ARG A
414
48.799
53.012
10.803
1.00
80.83
O


ATOM
2248
CB
ARG A
414
51.033
55.237
11.184
1.00
79.31
C


ATOM
2249
CG
ARG A
414
50.589
56.425
10.341
1.00
80.51
C


ATOM
2250
CD
ARG A
414
50.376
57.644
11.245
1.00
81.22
C


ATOM
2251
NE
ARG A
414
49.912
58.836
10.532
1.00
81.34
N


ATOM
2252
CZ
ARG A
414
50.676
59.603
9.757
1.00
81.51
C


ATOM
2253
NH1
ARG A
414
51.959
59.310
9.583
1.00
80.79
N


ATOM
2254
NH2
ARG A
414
50.158
60.671
9.161
1.00
80.72
N


ATOM
2255
N
ASN A
415
49.294
53.814
8.758
1.00
81.82
N


ATOM
2256
CA
ASN A
415
47.965
53.499
8.240
1.00
83.15
C


ATOM
2257
C
ASN A
415
47.967
52.029
7.797
1.00
83.41
C


ATOM
2258
O
ASN A
415
47.862
51.733
6.602
1.00
84.28
O


ATOM
2259
CB
ASN A
415
47.598
54.394
7.036
1.00
83.73
C


ATOM
2260
CG
ASN A
415
47.997
55.861
7.227
1.00
84.65
C


ATOM
2261
OD1
ASN A
415
47.436
56.589
8.076
1.00
84.65
O


ATOM
2262
ND2
ASN A
415
48.969
56.310
6.429
1.00
85.41
N


ATOM
2263
N
TRP A
416
48.101
51.116
8.758
1.00
82.63
N


ATOM
2264
CA
TRP A
416
48.118
49.682
8.465
1.00
82.02
C


ATOM
2265
C
TRP A
416
46.776
49.027
8.809
1.00
82.01
C


ATOM
2266
O
TRP A
416
46.228
49.228
9.896
1.00
82.27
O


ATOM
2267
CB
TRP A
416
49.268
48.998
9.236
1.00
79.66
C


ATOM
2268
CG
TRP A
416
48.850
47.849
10.126
1.00
77.46
C


ATOM
2269
CD1
TRP A
416
48.380
46.627
9.731
1.00
76.95
C


ATOM
2270
CD2
TRP A
416
48.806
47.849
11.560
1.00
76.39
C


ATOM
2271
NE1
TRP A
416
48.040
45.871
10.828
1.00
75.11
N


ATOM
2272
CE2
TRP A
416
48.290
46.595
11.963
1.00
75.43
C


ATOM
2273
CE3
TRP A
416
49.149
48.788
12.544
1.00
75.87
C


ATOM
2274
CZ2
TRP A
416
48.107
46.256
13.309
1.00
75.55
C


ATOM
2275
CZ3
TRP A
416
48.965
48.449
13.884
1.00
76.10
C


ATOM
2276
CH2
TRP A
416
48.448
47.193
14.251
1.00
75.60
C


ATOM
2277
N
PHE A
429
48.725
67.124
8.023
1.00
82.88
N


ATOM
2278
CA
PHE A
429
49.810
67.001
8.991
1.00
82.94
C


ATOM
2279
C
PHE A
429
50.394
65.588
8.957
1.00
82.92
C


ATOM
2280
O
PHE A
429
49.681
64.621
8.683
1.00
82.79
O


ATOM
2281
CB
PHE A
429
49.292
67.335
10.408
1.00
83.53
C


ATOM
2282
CG
PHE A
429
48.135
66.455
10.870
1.00
83.27
C


ATOM
2283
CD1
PHE A
429
48.310
65.082
11.041
1.00
82.47
C


ATOM
2284
CD2
PHE A
429
46.883
67.010
11.141
1.00
82.83
C


ATOM
2285
CE1
PHE A
429
47.263
64.261
11.473
1.00
81.70
C


ATOM
2286
CE2
PHE A
429
45.819
66.202
11.580
1.00
82.89
C


ATOM
2287
CZ
PHE A
429
46.014
64.819
11.745
1.00
82.38
C


ATOM
2288
N
GLU A
430
51.693
65.468
9.221
1.00
82.60
N


ATOM
2289
CA
GLU A
430
52.327
64.157
9.229
1.00
82.03
C


ATOM
2290
C
GLU A
430
53.060
63.870
10.528
1.00
81.40
C


ATOM
2291
O
GLU A
430
53.285
64.769
11.340
1.00
81.74
O


ATOM
2292
CB
GLU A
430
53.302
64.011
8.069
1.00
80.59
C


ATOM
2293
CG
GLU A
430
53.725
62.546
7.846
1.00
80.58
C


ATOM
2294
CD
GLU A
430
54.143
62.283
6.421
1.00
79.33
C


ATOM
2295
OE1
GLU A
430
55.063
62.985
5.936
1.00
79.26
O


ATOM
2296
OE2
GLU A
430
53.547
61.382
5.773
1.00
78.51
O


ATOM
2297
N
GLU A
431
53.456
62.614
10.712
1.00
79.43
N


ATOM
2298
CA
GLU A
431
54.133
62.214
11.941
1.00
77.44
C


ATOM
2299
C
GLU A
431
55.365
61.338
11.724
1.00
75.89
C


ATOM
2300
O
GLU A
431
55.739
60.568
12.606
1.00
75.77
O


ATOM
2301
CB
GLU A
431
53.129
61.482
12.841
1.00
76.96
C


ATOM
2302
CG
GLU A
431
51.677
61.970
12.631
1.00
76.64
C


ATOM
2303
CD
GLU A
431
50.767
61.647
13.795
1.00
77.02
C


ATOM
2304
OE1
GLU A
431
50.818
60.496
14.301
1.00
76.77
O


ATOM
2305
OE2
GLU A
431
49.984
62.546
14.214
1.00
77.41
O


ATOM
2306
N
GLY A
432
56.000
61.462
10.562
1.00
74.32
N


ATOM
2307
CA
GLY A
432
57.179
60.660
10.297
1.00
72.21
C


ATOM
2308
C
GLY A
432
57.936
61.058
9.047
1.00
70.77
C


ATOM
2309
O
GLY A
432
57.540
61.985
8.337
1.00
71.05
O


ATOM
2310
N
VAL A
433
59.032
60.352
8.776
1.00
68.86
N


ATOM
2311
CA
VAL A
433
59.855
60.629
7.603
1.00
66.42
C


ATOM
2312
C
VAL A
433
60.245
59.353
6.852
1.00
64.76
C


ATOM
2313
O
VAL A
433
60.353
58.275
7.442
1.00
63.75
O


ATOM
2314
CB
VAL A
433
61.139
61.397
7.998
1.00
66.53
C


ATOM
2315
CG1
VAL A
433
60.776
62.757
8.567
1.00
66.43
C


ATOM
2316
CG2
VAL A
433
61.928
60.600
9.016
1.00
66.47
C


ATOM
2317
N
ASP A
434
60.445
59.498
5.544
1.00
62.35
N


ATOM
2318
CA
ASP A
434
60.824
58.399
4.656
1.00
60.25
C


ATOM
2319
C
ASP A
434
62.173
58.780
4.052
1.00
58.31
C


ATOM
2320
O
ASP A
434
62.333
59.891
3.549
1.00
58.55
O


ATOM
2321
CB
ASP A
434
59.780
58.260
3.539
1.00
61.48
C


ATOM
2322
CG
ASP A
434
59.952
56.994
2.715
1.00
62.63
C


ATOM
2323
OD1
ASP A
434
61.091
56.500
2.578
1.00
65.25
O


ATOM
2324
OD2
ASP A
434
58.936
56.499
2.186
1.00
63.34
O


ATOM
2325
N
SER A
435
63.143
57.873
4.095
1.00
55.86
N


ATOM
2326
CA
SER A
435
64.459
58.182
3.548
1.00
53.85
C


ATOM
2327
C
SER A
435
65.260
56.977
3.069
1.00
51.23
C


ATOM
2328
O
SER A
435
64.753
55.859
2.996
1.00
50.16
O


ATOM
2329
CB
SER A
435
65.279
58.952
4.583
1.00
53.87
C


ATOM
2330
OG
SER A
435
65.363
58.220
5.792
1.00
56.33
O


ATOM
2331
N
TYR A
436
66.523
57.230
2.744
1.00
49.98
N


ATOM
2332
CA
TYR A
436
67.436
56.203
2.263
1.00
49.61
C


ATOM
2333
C
TYR A
436
68.712
56.158
3.104
1.00
48.71
C


ATOM
2334
O
TYR A
436
69.174
57.187
3.602
1.00
48.91
O


ATOM
2335
CB
TYR A
436
67.817
56.485
0.806
1.00
51.63
C


ATOM
2336
CG
TYR A
436
66.691
56.313
−0.188
1.00
52.47
C


ATOM
2337
CD1
TYR A
436
66.256
55.044
−0.562
1.00
52.86
C


ATOM
2338
CD2
TYR A
436
66.058
57.420
−0.752
1.00
54.05
C


ATOM
2339
CE1
TYR A
436
65.219
54.878
−1.475
1.00
55.19
C


ATOM
2340
CE2
TYR A
436
65.015
57.267
−1.668
1.00
55.67
C


ATOM
2341
CZ
TYR A
436
64.602
55.992
−2.023
1.00
55.33
C


ATOM
2342
OH
TYR A
436
63.569
55.825
−2.916
1.00
57.47
O


ATOM
2343
N
VAL A
437
69.272
54.963
3.263
1.00
45.78
N


ATOM
2344
CA
VAL A
437
70.514
54.794
4.008
1.00
44.47
C


ATOM
2345
C
VAL A
437
71.501
54.059
3.114
1.00
44.14
C


ATOM
2346
O
VAL A
437
71.120
53.167
2.357
1.00
43.85
O


ATOM
2347
CB
VAL A
437
70.318
53.984
5.316
1.00
43.82
C


ATOM
2348
CG1
VAL A
437
69.389
54.736
6.255
1.00
42.73
C


ATOM
2349
CG2
VAL A
437
69.778
52.598
5.004
1.00
41.37
C


ATOM
2350
N
PRO A
438
72.788
54.429
3.186
1.00
44.43
N


ATOM
2351
CA
PRO A
438
73.798
53.770
2.352
1.00
43.91
C


ATOM
2352
C
PRO A
438
73.930
52.285
2.654
1.00
43.14
C


ATOM
2353
O
PRO A
438
73.975
51.883
3.816
1.00
43.63
O


ATOM
2354
CB
PRO A
438
75.073
54.556
2.667
1.00
44.21
C


ATOM
2355
CG
PRO A
438
74.849
55.003
4.085
1.00
44.54
C


ATOM
2356
CD
PRO A
438
73.403
55.436
4.070
1.00
43.37
C


ATOM
2357
N
TYR A
439
73.971
51.480
1.597
1.00
42.30
N


ATOM
2358
CA
TYR A
439
74.103
50.034
1.713
1.00
41.24
C


ATOM
2359
C
TYR A
439
75.441
49.711
2.362
1.00
42.01
C


ATOM
2360
O
TYR A
439
76.477
50.233
1.956
1.00
41.44
O


ATOM
2361
CB
TYR A
439
74.025
49.391
0.323
1.00
39.97
C


ATOM
2362
CG
TYR A
439
74.174
47.884
0.302
1.00
37.05
C


ATOM
2363
CD1
TYR A
439
73.341
47.067
1.063
1.00
37.13
C


ATOM
2364
CD2
TYR A
439
75.134
47.273
−0.506
1.00
38.06
C


ATOM
2365
CE1
TYR A
439
73.458
45.675
1.019
1.00
37.56
C


ATOM
2366
CE2
TYR A
439
75.260
45.887
−0.557
1.00
36.89
C


ATOM
2367
CZ
TYR A
439
74.419
45.094
0.206
1.00
38.34
C


ATOM
2368
OH
TYR A
439
74.544
43.723
0.158
1.00
39.52
O


ATOM
2369
N
ALA A
440
75.415
48.841
3.366
1.00
42.74
N


ATOM
2370
CA
ALA A
440
76.632
48.473
4.078
1.00
42.66
C


ATOM
2371
C
ALA A
440
76.991
47.007
3.907
1.00
42.37
C


ATOM
2372
O
ALA A
440
77.982
46.540
4.462
1.00
43.02
O


ATOM
2373
CB
ALA A
440
76.480
48.799
5.561
1.00
42.72
C


ATOM
2374
N
GLY A
441
76.190
46.282
3.139
1.00
41.94
N


ATOM
2375
CA
GLY A
441
76.465
44.872
2.940
1.00
41.40
C


ATOM
2376
C
GLY A
441
75.788
44.014
3.991
1.00
42.16
C


ATOM
2377
O
GLY A
441
74.776
44.410
4.568
1.00
42.14
O


ATOM
2378
N
LYS A
442
76.351
42.838
4.246
1.00
42.68
N


ATOM
2379
CA
LYS A
442
75.799
41.909
5.225
1.00
42.67
C


ATOM
2380
C
LYS A
442
76.048
42.345
6.675
1.00
41.33
C


ATOM
2381
O
LYS A
442
77.086
42.924
7.000
1.00
39.63
O


ATOM
2382
CB
LYS A
442
76.384
40.515
4.990
1.00
45.23
C


ATOM
2383
CG
LYS A
442
76.063
39.949
3.612
1.00
49.35
C


ATOM
2384
CD
LYS A
442
74.990
38.864
3.670
1.00
51.07
C


ATOM
2385
CE
LYS A
442
75.563
37.563
4.226
1.00
54.09
C


ATOM
2386
NZ
LYS A
442
74.589
36.429
4.216
1.00
55.56
N


ATOM
2387
N
LEU A
443
75.078
42.055
7.534
1.00
40.11
N


ATOM
2388
CA
LEU A
443
75.140
42.395
8.951
1.00
38.38
C


ATOM
2389
C
LEU A
443
76.422
41.932
9.657
1.00
38.75
C


ATOM
2390
O
LEU A
443
77.085
42.717
10.329
1.00
36.60
O


ATOM
2391
CB
LEU A
443
73.917
41.805
9.659
1.00
35.66
C


ATOM
2392
CG
LEU A
443
73.769
41.987
11.173
1.00
34.22
C


ATOM
2393
CD1
LEU A
443
72.311
41.806
11.567
1.00
31.06
C


ATOM
2394
CD2
LEU A
443
74.660
40.991
11.904
1.00
33.38
C


ATOM
2395
N
LYS A
444
76.763
40.659
9.489
1.00
39.50
N


ATOM
2396
CA
LYS A
444
77.939
40.065
10.125
1.00
42.18
C


ATOM
2397
C
LYS A
444
79.232
40.890
10.156
1.00
41.66
C


ATOM
2398
O
LYS A
444
79.745
41.200
11.229
1.00
42.08
O


ATOM
2399
CB
LYS A
444
78.237
38.702
9.493
1.00
43.45
C


ATOM
2400
CG
LYS A
444
79.237
37.878
10.285
1.00
48.67
C


ATOM
2401
CD
LYS A
444
79.460
36.511
9.663
1.00
51.53
C


ATOM
2402
CE
LYS A
444
80.285
35.630
10.585
1.00
52.97
C


ATOM
2403
NZ
LYS A
444
81.600
36.254
10.907
1.00
53.80
N


ATOM
2404
N
ASP A
445
79.757
41.240
8.988
1.00
41.15
N


ATOM
2405
CA
ASP A
445
81.005
41.991
8.901
1.00
41.12
C


ATOM
2406
C
ASP A
445
80.951
43.355
9.567
1.00
40.48
C


ATOM
2407
O
ASP A
445
81.936
43.810
10.149
1.00
39.71
O


ATOM
2408
CB
ASP A
445
81.412
42.164
7.436
1.00
44.73
C


ATOM
2409
CG
ASP A
445
81.511
40.841
6.698
1.00
47.59
C


ATOM
2410
OD1
ASP A
445
82.364
40.008
7.077
1.00
48.96
O


ATOM
2411
OD2
ASP A
445
80.726
40.636
5.746
1.00
50.74
O


ATOM
2412
N
ASN A
446
79.802
44.012
9.471
1.00
38.11
N


ATOM
2413
CA
ASN A
446
79.637
45.332
10.058
1.00
37.61
C


ATOM
2414
C
ASN A
446
79.543
45.289
11.579
1.00
37.06
C


ATOM
2415
O
ASN A
446
80.122
46.136
12.261
1.00
35.82
O


ATOM
2416
CB
ASN A
446
78.405
46.000
9.469
1.00
38.33
C


ATOM
2417
CG
ASN A
446
78.605
46.388
8.023
1.00
39.42
C


ATOM
2418
OD1
ASN A
446
79.106
47.473
7.725
1.00
39.50
O


ATOM
2419
ND2
ASN A
446
78.232
45.493
7.112
1.00
38.24
N


ATOM
2420
N
VAL A
447
78.815
44.309
12.106
1.00
35.62
N


ATOM
2421
CA
VAL A
447
78.676
44.165
13.547
1.00
36.21
C


ATOM
2422
C
VAL A
447
80.030
43.786
14.160
1.00
36.80
C


ATOM
2423
O
VAL A
447
80.419
44.314
15.199
1.00
36.29
O


ATOM
2424
CB
VAL A
447
77.629
43.087
13.901
1.00
35.55
C


ATOM
2425
CG1
VAL A
447
77.741
42.707
15.373
1.00
34.78
C


ATOM
2426
CG2
VAL A
447
76.229
43.612
13.598
1.00
34.46
C


ATOM
2427
N
GLU A
448
80.746
42.876
13.505
1.00
37.04
N


ATOM
2428
CA
GLU A
448
82.048
42.451
13.994
1.00
38.35
C


ATOM
2429
C
GLU A
448
82.967
43.667
14.076
1.00
36.95
C


ATOM
2430
O
GLU A
448
83.655
43.864
15.075
1.00
35.90
O


ATOM
2431
CB
GLU A
448
82.656
41.392
13.062
1.00
40.48
C


ATOM
2432
CG
GLU A
448
83.949
40.772
13.586
1.00
45.60
C


ATOM
2433
CD
GLU A
448
84.553
39.739
12.634
1.00
50.26
C


ATOM
2434
OE1
GLU A
448
85.094
40.133
11.573
1.00
51.53
O


ATOM
2435
OE2
GLU A
448
84.482
38.529
12.950
1.00
52.94
O


ATOM
2436
N
ALA A
449
82.960
44.485
13.028
1.00
34.49
N


ATOM
2437
CA
ALA A
449
83.793
45.683
12.982
1.00
34.45
C


ATOM
2438
C
ALA A
449
83.417
46.670
14.089
1.00
33.89
C


ATOM
2439
O
ALA A
449
84.282
47.195
14.790
1.00
33.96
O


ATOM
2440
CB
ALA A
449
83.665
46.361
11.616
1.00
34.26
C


ATOM
2441
N
SER A
450
82.123
46.924
14.233
1.00
31.81
N


ATOM
2442
CA
SER A
450
81.638
47.841
15.252
1.00
32.08
C


ATOM
2443
C
SER A
450
82.023
47.380
16.657
1.00
31.86
C


ATOM
2444
O
SER A
450
82.531
48.166
17.463
1.00
29.55
O


ATOM
2445
CB
SER A
450
80.112
47.969
15.167
1.00
30.70
C


ATOM
2446
OG
SER A
450
79.724
48.753
14.056
1.00
31.66
O


ATOM
2447
N
LEU A
451
81.784
46.103
16.941
1.00
31.11
N


ATOM
2448
CA
LEU A
451
82.077
45.556
18.259
1.00
32.52
C


ATOM
2449
C
LEU A
451
83.565
45.413
18.559
1.00
33.63
C


ATOM
2450
O
LEU A
451
83.959
45.383
19.723
1.00
33.14
O


ATOM
2451
CB
LEU A
451
81.347
44.227
18.449
1.00
30.21
C


ATOM
2452
CG
LEU A
451
79.824
44.407
18.426
1.00
30.73
C


ATOM
2453
CD1
LEU A
451
79.143
43.096
18.766
1.00
27.89
C


ATOM
2454
CD2
LEU A
451
79.411
45.501
19.416
1.00
28.68
C


ATOM
2455
N
ASN A
452
84.392
45.331
17.521
1.00
35.18
N


ATOM
2456
CA
ASN A
452
85.831
45.251
17.732
1.00
35.86
C


ATOM
2457
C
ASN A
452
86.294
46.601
18.274
1.00
35.32
C


ATOM
2458
O
ASN A
452
87.176
46.665
19.134
1.00
34.79
O


ATOM
2459
CB
ASN A
452
86.581
44.941
16.429
1.00
37.41
C


ATOM
2460
CG
ASN A
452
86.632
43.459
16.125
1.00
41.69
C


ATOM
2461
OD1
ASN A
452
86.668
42.626
17.037
1.00
45.32
O


ATOM
2462
ND2
ASN A
452
86.656
43.117
14.841
1.00
44.05
N


ATOM
2463
N
LYS A
453
85.695
47.680
17.774
1.00
34.56
N


ATOM
2464
CA
LYS A
453
86.069
49.012
18.235
1.00
35.20
C


ATOM
2465
C
LYS A
453
85.568
49.255
19.651
1.00
32.43
C


ATOM
2466
O
LYS A
453
86.237
49.915
20.442
1.00
31.92
O


ATOM
2467
CB
LYS A
453
85.533
50.098
17.292
1.00
36.51
C


ATOM
2468
CG
LYS A
453
86.090
49.988
15.877
1.00
42.24
C


ATOM
2469
CD
LYS A
453
86.165
51.338
15.160
1.00
43.06
C


ATOM
2470
CE
LYS A
453
84.835
52.050
15.172
1.00
45.98
C


ATOM
2471
NZ
LYS A
453
84.889
53.331
14.419
1.00
46.25
N


ATOM
2472
N
VAL A
454
84.391
48.724
19.968
1.00
30.18
N


ATOM
2473
CA
VAL A
454
83.836
48.878
21.303
1.00
28.56
C


ATOM
2474
C
VAL A
454
84.741
48.143
22.295
1.00
29.40
C


ATOM
2475
O
VAL A
454
85.100
48.690
23.338
1.00
26.82
O


ATOM
2476
CB
VAL A
454
82.401
48.306
21.390
1.00
29.78
C


ATOM
2477
CG1
VAL A
454
81.943
48.247
22.855
1.00
26.04
C


ATOM
2478
CG2
VAL A
454
81.444
49.181
20.572
1.00
29.03
C


ATOM
2479
N
LYS A
455
85.111
46.910
21.953
1.00
28.71
N


ATOM
2480
CA
LYS A
455
85.984
46.095
22.799
1.00
30.25
C


ATOM
2481
C
LYS A
455
87.330
46.774
23.020
1.00
30.25
C


ATOM
2482
O
LYS A
455
87.864
46.779
24.125
1.00
29.71
O


ATOM
2483
CB
LYS A
455
86.225
44.725
22.159
1.00
29.78
C


ATOM
2484
CG
LYS A
455
85.048
43.776
22.199
1.00
31.31
C


ATOM
2485
CD
LYS A
455
85.354
42.555
21.340
1.00
34.36
C


ATOM
2486
CE
LYS A
455
84.234
41.536
21.385
1.00
38.66
C


ATOM
2487
NZ
LYS A
455
84.480
40.397
20.448
1.00
40.02
N


ATOM
2488
N
SER A
456
87.876
47.338
21.950
1.00
31.20
N


ATOM
2489
CA
SER A
456
89.159
48.020
22.012
1.00
32.66
C


ATOM
2490
C
SER A
456
89.063
49.232
22.939
1.00
32.37
C


ATOM
2491
O
SER A
456
89.938
49.461
23.786
1.00
32.02
O


ATOM
2492
CB
SER A
456
89.583
48.453
20.601
1.00
33.72
C


ATOM
2493
OG
SER A
456
90.866
49.044
20.615
1.00
36.70
O


ATOM
2494
N
THR A
457
87.994
50.009
22.776
1.00
29.64
N


ATOM
2495
CA
THR A
457
87.787
51.178
23.614
1.00
29.25
C


ATOM
2496
C
THR A
457
87.595
50.733
25.060
1.00
28.90
C


ATOM
2497
O
THR A
457
88.086
51.380
25.981
1.00
28.75
O


ATOM
2498
CB
THR A
457
86.561
51.982
23.158
1.00
29.05
C


ATOM
2499
OG1
THR A
457
86.757
52.393
21.805
1.00
32.49
O


ATOM
2500
CG2
THR A
457
86.369
53.216
24.022
1.00
26.06
C


ATOM
2501
N
MET A
458
86.884
49.625
25.259
1.00
28.56
N


ATOM
2502
CA
MET A
458
86.663
49.111
26.603
1.00
27.60
C


ATOM
2503
C
MET A
458
87.993
48.832
27.288
1.00
28.20
C


ATOM
2504
O
MET A
458
88.167
49.155
28.459
1.00
28.30
O


ATOM
2505
CB
MET A
458
85.792
47.853
26.560
1.00
27.08
C


ATOM
2506
CG
MET A
458
84.306
48.170
26.380
1.00
26.92
C


ATOM
2507
SD
MET A
458
83.227
46.746
26.210
1.00
28.93
S


ATOM
2508
CE
MET A
458
83.415
45.945
27.805
1.00
27.06
C


ATOM
2509
N
CYS A
459
88.944
48.252
26.561
1.00
29.24
N


ATOM
2510
CA
CYS A
459
90.254
47.982
27.141
1.00
30.30
C


ATOM
2511
C
CYS A
459
91.009
49.273
27.466
1.00
30.36
C


ATOM
2512
O
CYS A
459
91.818
49.303
28.397
1.00
28.82
O


ATOM
2513
CB
CYS A
459
91.092
47.100
26.212
1.00
32.96
C


ATOM
2514
SG
CYS A
459
90.670
45.337
26.352
1.00
36.19
S


ATOM
2515
N
ASN A
460
90.757
50.335
26.702
1.00
28.82
N


ATOM
2516
CA
ASN A
460
91.411
51.609
26.986
1.00
29.47
C


ATOM
2517
C
ASN A
460
90.884
52.087
28.334
1.00
28.59
C


ATOM
2518
O
ASN A
460
91.586
52.756
29.079
1.00
29.35
O


ATOM
2519
CB
ASN A
460
91.078
52.677
25.937
1.00
29.43
C


ATOM
2520
CG
ASN A
460
91.756
52.434
24.610
1.00
32.45
C


ATOM
2521
OD1
ASN A
460
91.097
52.161
23.612
1.00
33.79
O


ATOM
2522
ND2
ASN A
460
93.080
52.536
24.589
1.00
31.89
N


ATOM
2523
N
CYS A
461
89.636
51.735
28.633
1.00
28.48
N


ATOM
2524
CA
CYS A
461
88.993
52.143
29.878
1.00
27.53
C


ATOM
2525
C
CYS A
461
89.204
51.138
31.010
1.00
27.92
C


ATOM
2526
O
CYS A
461
88.633
51.289
32.086
1.00
27.95
O


ATOM
2527
CB
CYS A
461
87.486
52.355
29.646
1.00
29.51
C


ATOM
2528
SG
CYS A
461
87.070
53.620
28.389
1.00
32.81
S


ATOM
2529
N
GLY A
462
90.021
50.119
30.762
1.00
27.78
N


ATOM
2530
CA
GLY A
462
90.293
49.106
31.767
1.00
27.70
C


ATOM
2531
C
GLY A
462
89.133
48.163
32.052
1.00
28.72
C


ATOM
2532
O
GLY A
462
88.987
47.674
33.176
1.00
29.35
O


ATOM
2533
N
ALA A
463
88.315
47.881
31.043
1.00
27.30
N


ATOM
2534
CA
ALA A
463
87.163
47.012
31.248
1.00
27.53
C


ATOM
2535
C
ALA A
463
87.121
45.785
30.352
1.00
27.82
C


ATOM
2536
O
ALA A
463
87.288
45.886
29.139
1.00
27.55
O


ATOM
2537
CB
ALA A
463
85.879
47.820
31.069
1.00
26.38
C


ATOM
2538
N
LEU A
464
86.884
44.628
30.961
1.00
28.56
N


ATOM
2539
CA
LEU A
464
86.785
43.369
30.223
1.00
30.06
C


ATOM
2540
C
LEU A
464
85.330
42.963
30.014
1.00
29.07
C


ATOM
2541
O
LEU A
464
85.043
42.046
29.246
1.00
31.05
O


ATOM
2542
CB
LEU A
464
87.512
42.237
30.961
1.00
31.49
C


ATOM
2543
CG
LEU A
464
88.993
42.025
30.640
1.00
33.97
C


ATOM
2544
CD1
LEU A
464
89.150
41.723
29.158
1.00
36.04
C


ATOM
2545
CD2
LEU A
464
89.788
43.265
31.004
1.00
38.27
C


ATOM
2546
N
THR A
465
84.419
43.633
30.712
1.00
27.77
N


ATOM
2547
CA
THR A
465
82.996
43.338
30.595
1.00
27.41
C


ATOM
2548
C
THR A
465
82.197
44.630
30.674
1.00
27.20
C


ATOM
2549
O
THR A
465
82.709
45.664
31.107
1.00
26.83
O


ATOM
2550
CB
THR A
465
82.494
42.417
31.736
1.00
27.84
C


ATOM
2551
OG1
THR A
465
82.536
43.133
32.975
1.00
28.30
O


ATOM
2552
CG2
THR A
465
83.355
41.159
31.838
1.00
28.72
C


ATOM
2553
N
ILE A
466
80.936
44.567
30.260
1.00
25.31
N


ATOM
2554
CA
ILE A
466
80.085
45.743
30.298
1.00
25.03
C


ATOM
2555
C
ILE A
466
79.898
46.236
31.732
1.00
24.87
C


ATOM
2556
O
ILE A
466
79.985
47.430
31.993
1.00
27.04
O


ATOM
2557
CB
ILE A
466
78.724
45.456
29.629
1.00
25.22
C


ATOM
2558
CG1
ILE A
466
78.939
45.313
28.114
1.00
24.45
C


ATOM
2559
CG2
ILE A
466
77.726
46.565
29.944
1.00
22.53
C


ATOM
2560
CD1
ILE A
466
77.699
44.908
27.350
1.00
25.70
C


ATOM
2561
N
PRO A
467
79.638
45.327
32.684
1.00
25.57
N


ATOM
2562
CA
PRO A
467
79.468
45.805
34.058
1.00
25.31
C


ATOM
2563
C
PRO A
467
80.730
46.506
34.570
1.00
26.95
C


ATOM
2564
O
PRO A
467
80.649
47.499
35.292
1.00
27.35
O


ATOM
2565
CB
PRO A
467
79.149
44.525
34.828
1.00
25.79
C


ATOM
2566
CG
PRO A
467
78.393
43.723
33.811
1.00
24.45
C


ATOM
2567
CD
PRO A
467
79.258
43.909
32.577
1.00
23.17
C


ATOM
2568
N
GLN A
468
81.897
46.003
34.186
1.00
27.99
N


ATOM
2569
CA
GLN A
468
83.137
46.623
34.630
1.00
28.59
C


ATOM
2570
C
GLN A
468
83.320
47.995
33.976
1.00
29.85
C


ATOM
2571
O
GLN A
468
83.844
48.926
34.594
1.00
29.02
O


ATOM
2572
CB
GLN A
468
84.320
45.710
34.323
1.00
29.66
C


ATOM
2573
CG
GLN A
468
85.623
46.216
34.879
1.00
30.83
C


ATOM
2574
CD
GLN A
468
86.722
45.175
34.834
1.00
29.49
C


ATOM
2575
OE1
GLN A
468
86.806
44.380
33.900
1.00
27.39
O


ATOM
2576
NE2
GLN A
468
87.589
45.194
35.839
1.00
32.22
N


ATOM
2577
N
LEU A
469
82.872
48.124
32.729
1.00
28.18
N


ATOM
2578
CA
LEU A
469
82.961
49.395
32.025
1.00
26.94
C


ATOM
2579
C
LEU A
469
82.029
50.413
32.676
1.00
27.29
C


ATOM
2580
O
LEU A
469
82.379
51.587
32.815
1.00
26.46
O


ATOM
2581
CB
LEU A
469
82.566
49.232
30.554
1.00
27.22
C


ATOM
2582
CG
LEU A
469
82.343
50.536
29.777
1.00
28.28
C


ATOM
2583
CD1
LEU A
469
83.683
51.232
29.552
1.00
25.24
C


ATOM
2584
CD2
LEU A
469
81.657
50.238
28.438
1.00
27.64
C


ATOM
2585
N
GLN A
470
80.845
49.959
33.076
1.00
26.40
N


ATOM
2586
CA
GLN A
470
79.864
50.851
33.685
1.00
28.89
C


ATOM
2587
C
GLN A
470
80.344
51.351
35.038
1.00
29.84
C


ATOM
2588
O
GLN A
470
80.001
52.444
35.480
1.00
28.12
O


ATOM
2589
CB
GLN A
470
78.513
50.132
33.807
1.00
27.17
C


ATOM
2590
CG
GLN A
470
77.962
49.716
32.434
1.00
27.68
C


ATOM
2591
CD
GLN A
470
76.666
48.938
32.506
1.00
28.13
C


ATOM
2592
OE1
GLN A
470
76.449
48.166
33.432
1.00
28.58
O


ATOM
2593
NE2
GLN A
470
75.803
49.122
31.508
1.00
26.29
N


ATOM
2594
N
SER A
471
81.173
50.543
35.676
1.00
31.64
N


ATOM
2595
CA
SER A
471
81.712
50.880
36.976
1.00
31.86
C


ATOM
2596
C
SER A
471
82.949
51.783
36.887
1.00
32.13
C


ATOM
2597
O
SER A
471
83.081
52.742
37.646
1.00
32.18
O


ATOM
2598
CB
SER A
471
82.050
49.585
37.722
1.00
30.51
C


ATOM
2599
OG
SER A
471
82.831
49.842
38.870
1.00
33.39
O


ATOM
2600
N
LYS A
472
83.830
51.493
35.936
1.00
32.80
N


ATOM
2601
CA
LYS A
472
85.081
52.234
35.783
1.00
33.19
C


ATOM
2602
C
LYS A
472
85.148
53.388
34.781
1.00
32.28
C


ATOM
2603
O
LYS A
472
86.097
54.163
34.813
1.00
32.33
O


ATOM
2604
CB
LYS A
472
86.201
51.245
35.452
1.00
34.04
C


ATOM
2605
CG
LYS A
472
86.335
50.127
36.466
1.00
36.23
C


ATOM
2606
CD
LYS A
472
87.335
49.075
36.019
1.00
38.07
C


ATOM
2607
CE
LYS A
472
88.755
49.592
36.059
1.00
39.38
C


ATOM
2608
NZ
LYS A
472
89.723
48.517
35.698
1.00
41.01
N


ATOM
2609
N
ALA A
473
84.170
53.506
33.889
1.00
31.34
N


ATOM
2610
CA
ALA A
473
84.201
54.572
32.892
1.00
30.17
C


ATOM
2611
C
ALA A
473
84.324
55.987
33.461
1.00
30.11
C


ATOM
2612
O
ALA A
473
83.718
56.334
34.480
1.00
30.70
O


ATOM
2613
CB
ALA A
473
82.971
54.489
31.986
1.00
29.13
C


ATOM
2614
N
LYS A
474
85.136
56.788
32.781
1.00
30.05
N


ATOM
2615
CA
LYS A
474
85.362
58.184
33.129
1.00
29.85
C


ATOM
2616
C
LYS A
474
84.772
58.909
31.928
1.00
29.93
C


ATOM
2617
O
LYS A
474
85.302
58.833
30.816
1.00
29.14
O


ATOM
2618
CB
LYS A
474
86.862
58.441
33.277
1.00
28.50
C


ATOM
2619
CG
LYS A
474
87.460
57.684
34.471
1.00
28.70
C


ATOM
2620
CD
LYS A
474
88.943
57.375
34.279
1.00
27.54
C


ATOM
2621
CE
LYS A
474
89.803
58.620
34.334
1.00
29.17
C


ATOM
2622
NZ
LYS A
474
91.222
58.265
34.018
1.00
28.64
N


ATOM
2623
N
ILE A
475
83.660
59.597
32.150
1.00
29.12
N


ATOM
2624
CA
ILE A
475
82.968
60.254
31.056
1.00
29.85
C


ATOM
2625
C
ILE A
475
82.935
61.764
31.176
1.00
29.94
C


ATOM
2626
O
ILE A
475
82.444
62.314
32.166
1.00
30.35
O


ATOM
2627
CB
ILE A
475
81.524
59.703
30.943
1.00
29.86
C


ATOM
2628
CG1
ILE A
475
81.564
58.164
30.940
1.00
29.42
C


ATOM
2629
CG2
ILE A
475
80.867
60.213
29.666
1.00
29.91
C


ATOM
2630
CD1
ILE A
475
80.205
57.470
30.951
1.00
23.94
C


ATOM
2631
N
THR A
476
83.459
62.429
30.153
1.00
29.56
N


ATOM
2632
CA
THR A
476
83.511
63.881
30.141
1.00
29.14
C


ATOM
2633
C
THR A
476
82.686
64.506
29.042
1.00
28.15
C


ATOM
2634
O
THR A
476
82.582
63.986
27.932
1.00
26.60
O


ATOM
2635
CB
THR A
476
84.962
64.414
29.981
1.00
28.25
C


ATOM
2636
OG1
THR A
476
84.953
65.844
30.066
1.00
32.24
O


ATOM
2637
CG2
THR A
476
85.535
64.022
28.629
1.00
26.65
C


ATOM
2638
N
LEU A
477
82.105
65.644
29.381
1.00
29.09
N


ATOM
2639
CA
LEU A
477
81.312
66.424
28.456
1.00
32.22
C


ATOM
2640
C
LEU A
477
82.352
67.281
27.731
1.00
32.43
C


ATOM
2641
O
LEU A
477
83.395
67.592
28.304
1.00
32.10
O


ATOM
2642
CB
LEU A
477
80.352
67.312
29.256
1.00
33.05
C


ATOM
2643
CG
LEU A
477
79.239
68.097
28.566
1.00
35.08
C


ATOM
2644
CD1
LEU A
477
78.264
67.138
27.910
1.00
32.98
C


ATOM
2645
CD2
LEU A
477
78.526
68.966
29.604
1.00
35.36
C


ATOM
2646
N
VAL A
478
82.093
67.635
26.477
1.00
33.80
N


ATOM
2647
CA
VAL A
478
83.018
68.480
25.726
1.00
35.55
C


ATOM
2648
C
VAL A
478
82.280
69.767
25.365
1.00
35.88
C


ATOM
2649
O
VAL A
478
81.052
69.787
25.304
1.00
35.41
O


ATOM
2650
CB
VAL A
478
83.516
67.796
24.422
1.00
36.48
C


ATOM
2651
CG1
VAL A
478
83.960
66.370
24.718
1.00
37.57
C


ATOM
2652
CG2
VAL A
478
82.428
67.822
23.363
1.00
38.80
C


ATOM
2653
N
SER A
479
83.028
70.839
25.132
1.00
37.26
N


ATOM
2654
CA
SER A
479
82.432
72.127
24.794
1.00
39.38
C


ATOM
2655
C
SER A
479
81.806
72.119
23.406
1.00
40.82
C


ATOM
2656
O
SER A
479
82.200
71.341
22.537
1.00
41.28
O


ATOM
2657
CB
SER A
479
83.488
73.230
24.869
1.00
38.01
C


ATOM
2658
OG
SER A
479
84.515
72.999
23.924
1.00
38.36
O


ATOM
2659
N
SER A
480
80.825
72.990
23.203
1.00
44.34
N


ATOM
2660
CA
SER A
480
80.152
73.083
21.912
1.00
48.75
C


ATOM
2661
C
SER A
480
81.149
73.491
20.828
1.00
50.10
C


ATOM
2662
O
SER A
480
81.088
73.005
19.698
1.00
50.70
O


ATOM
2663
CB
SER A
480
79.017
74.104
21.986
1.00
49.74
C


ATOM
2664
OG
SER A
480
79.516
75.382
22.326
1.00
52.76
O


ATOM
2665
N
VAL A
481
82.074
74.377
21.187
1.00
52.36
N


ATOM
2666
CA
VAL A
481
83.096
74.856
20.262
1.00
54.26
C


ATOM
2667
C
VAL A
481
83.975
73.729
19.720
1.00
55.31
C


ATOM
2668
O
VAL A
481
84.319
73.721
18.537
1.00
55.24
O


ATOM
2669
CB
VAL A
481
84.017
75.901
20.937
1.00
54.94
C


ATOM
2670
CG1
VAL A
481
85.189
76.234
20.021
1.00
55.96
C


ATOM
2671
CG2
VAL A
481
83.229
77.162
21.256
1.00
55.59
C


ATOM
2672
N
SER A
482
84.343
72.788
20.586
1.00
56.16
N


ATOM
2673
CA
SER A
482
85.190
71.670
20.183
1.00
58.27
C


ATOM
2674
C
SER A
482
84.491
70.750
19.184
1.00
60.34
C


ATOM
2675
O
SER A
482
85.144
69.962
18.493
1.00
60.26
O


ATOM
2676
CB
SER A
482
85.620
70.855
21.408
1.00
57.59
C


ATOM
2677
OG
SER A
482
84.518
70.189
21.998
1.00
57.44
O


ATOM
2678
N
ILE A
483
83.166
70.851
19.107
1.00
61.66
N


ATOM
2679
CA
ILE A
483
82.395
70.016
18.192
1.00
64.37
C


ATOM
2680
C
ILE A
483
82.307
70.637
16.795
1.00
65.60
C


ATOM
2681
O
ILE A
483
82.290
71.886
16.692
1.00
65.96
O


ATOM
2682
CB
ILE A
483
80.959
69.786
18.728
1.00
64.32
C


ATOM
2683
CG1
ILE A
483
81.023
69.252
20.161
1.00
64.61
C


ATOM
2684
CG2
ILE A
483
80.215
68.796
17.835
1.00
64.26
C


ATOM
2685
CD1
ILE A
483
79.670
68.993
20.789
1.00
64.99
C


TER
2686

ILE A
483


HETATM
2687
K
K    A
900
52.942
60.264
29.342
0.75
35.52
K


HETATM
2688
P
IMP
602
67.729
55.171
15.018
1.00
32.01
P


HETATM
2689
O1P
IMP
602
67.318
55.116
13.589
1.00
35.06
O


HETATM
2690
O2P
IMP
602
68.541
53.958
15.324
1.00
37.34
O


HETATM
2691
O3P
IMP
602
68.509
56.460
15.351
1.00
34.23
O


HETATM
2692
O5*
IMP
602
66.513
55.208
16.042
1.00
32.49
O


HETATM
2693
C5*
IMP
602
65.484
54.230
15.900
1.00
28.06
C


HETATM
2694
C4*
IMP
602
64.416
54.369
16.948
1.00
29.30
C


HETATM
2695
O4*
IMP
602
63.654
55.545
16.512
1.00
28.92
O


HETATM
2696
C3*
IMP
602
63.350
53.301
17.112
1.00
27.97
C


HETATM
2697
O3*
IMP
602
63.765
52.190
17.882
1.00
29.87
O


HETATM
2698
C2*
IMP
602
62.219
54.048
17.747
1.00
28.37
C


HETATM
2699
O2*
IMP
602
62.308
54.094
19.151
1.00
28.77
O


HETATM
2700
C1*
IMP
602
62.341
55.422
17.066
1.00
29.44
C


HETATM
2701
N9
IMP
602
61.392
55.563
15.918
1.00
31.97
N


HETATM
2702
C8
IMP
602
60.890
54.644
15.016
1.00
32.78
C


HETATM
2703
N7
IMP
602
60.086
55.173
14.154
1.00
32.55
N


HETATM
2704
C5
IMP
602
60.027
56.497
14.463
1.00
34.42
C


HETATM
2705
C6
IMP
602
59.302
57.582
13.855
1.00
35.14
C


HETATM
2706
O6
IMP
602
58.555
57.521
12.883
1.00
36.42
O


HETATM
2707
N1
IMP
602
59.516
58.848
14.495
1.00
36.83
N


HETATM
2708
C2
IMP
602
60.355
59.011
15.609
1.00
38.21
C


HETATM
2709
N3
IMP
602
61.034
57.973
16.170
1.00
35.63
N


HETATM
2710
C4
IMP
602
60.832
56.774
15.563
1.00
34.37
C


HETATM
2711
O
HOH
1
63.019
58.881
18.340
1.00
44.26
O


HETATM
2712
O
HOH
2
52.277
57.766
28.053
1.00
120.54
O


HETATM
2713
O
HOH
3
66.605
47.974
38.976
1.00
25.54
O


HETATM
2714
O
HOH
4
59.386
45.205
36.943
1.00
29.43
O


HETATM
2715
O
HOH
5
79.662
41.845
29.507
1.00
22.13
O


HETATM
2716
O
HOH
6
65.938
60.529
24.679
1.00
31.17
O


HETATM
2717
O
HOH
7
74.980
45.671
32.871
1.00
30.42
O


HETATM
2718
O
HOH
8
57.548
58.753
28.347
1.00
28.92
O


HETATM
2719
O
HOH
9
70.703
54.421
21.919
1.00
26.74
O


HETATM
2720
O
HOH
10
70.985
53.252
14.290
1.00
27.12
O


HETATM
2721
O
HOH
11
45.680
44.301
11.265
1.00
103.96
O


HETATM
2722
O
HOH
12
77.744
53.946
34.272
1.00
32.08
O


HETATM
2723
O
HOH
13
58.727
51.272
23.006
1.00
27.53
O


HETATM
2724
O
HOH
14
62.326
38.666
34.100
1.00
27.41
O


HETATM
2725
O
HOH
15
56.691
78.735
34.475
1.00
29.79
O


HETATM
2726
O
HOH
16
88.368
53.773
33.242
1.00
29.09
O


HETATM
2727
O
HOH
17
72.567
38.252
33.805
1.00
32.29
O


HETATM
2728
O
HOH
18
87.198
55.495
31.179
1.00
28.25
O


HETATM
2729
O
HOH
19
49.308
44.270
21.126
1.00
33.03
O


HETATM
2730
O
HOH
20
78.730
48.078
37.343
1.00
33.84
O


HETATM
2731
O
HOH
21
73.616
57.426
36.203
1.00
27.28
O


HETATM
2732
O
HOH
22
56.311
77.113
37.092
1.00
34.13
O


HETATM
2733
O
HOH
23
74.197
59.875
37.788
1.00
40.63
O


HETATM
2734
O
HOH
24
64.449
41.371
7.872
1.00
35.33
O


HETATM
2735
O
HOH
25
76.108
43.846
30.984
1.00
26.68
O


HETATM
2736
O
HOH
26
70.175
33.467
27.535
1.00
36.79
O


HETATM
2737
O
HOH
27
84.289
53.139
21.052
1.00
32.01
O


HETATM
2738
O
HOH
28
56.502
57.506
38.867
1.00
42.20
O


HETATM
2739
O
HOH
29
48.256
54.233
36.924
1.00
41.83
O


HETATM
2740
O
HOH
30
75.042
38.867
31.153
1.00
33.27
O


HETATM
2741
O
HOH
31
69.348
62.804
21.515
1.00
38.19
O


HETATM
2742
O
HOH
32
92.355
40.593
20.080
1.00
59.23
O


HETATM
2743
O
HOH
33
59.908
50.926
20.187
1.00
37.89
O


HETATM
2744
O
HOH
34
53.040
51.707
38.077
1.00
33.13
O


HETATN
2745
O
HOH
35
58.612
45.227
6.010
1.00
41.56
O


HETATM
2746
O
HOH
36
69.127
67.876
32.847
1.00
41.45
O


HETATM
2747
O
HOH
37
63.999
56.486
20.273
1.00
37.87
O


HETATM
2748
O
HOH
38
52.165
53.830
25.868
1.00
36.90
O


HETATM
2749
O
HOH
39
65.226
36.648
34.797
1.00
33.52
O


HETATM
2750
O
HOH
40
67.969
38.369
46.331
1.00
38.33
O


HETATM
2751
O
HOH
41
76.432
41.259
32.168
1.00
31.45
O


HETATM
2752
O
HOH
42
58.931
42.035
5.988
1.00
51.68
O


HETATM
2753
O
HOH
43
58.873
38.279
34.683
1.00
31.39
O


HETATM
2754
O
HOH
44
91.268
41.892
34.973
1.00
45.58
O


HETATM
2755
O
HOH
45
87.214
67.124
30.708
1.00
29.61
O


HETATM
2756
O
HOH
46
61.767
50.507
18.007
1.00
29.58
O


HETATM
2757
O
HOH
47
53.679
55.874
20.408
1.00
48.69
O


HETATM
2758
O
HOH
48
56.278
41.477
37.489
1.00
44.57
O


HETATM
2759
O
HOH
49
59.791
59.574
31.027
1.00
52.11
O


HETATM
2760
O
HOH
50
62.820
39.505
6.099
1.00
44.52
O


HETATM
2761
O
HOH
51
49.843
43.256
7.770
1.00
52.85
O


HETATM
2762
O
HOH
52
58.407
35.678
26.960
1.00
39.42
O


HETATM
2763
O
HOH
53
59.608
51.214
9.860
1.00
33.11
O


HETATM
2764
O
HOH
54
59.577
51.575
16.371
1.00
31.46
O


HETATM
2765
O
HOH
55
74.077
50.717
36.341
1.00
43.49
O


HETATM
2766
O
HOH
56
79.182
38.296
17.383
1.00
40.40
O


HETATM
2767
O
HOH
57
75.288
70.156
31.710
1.00
40.54
O


HETATM
2768
O
HOH
58
64.697
73.440
32.795
1.00
34.94
O


HETATM
2769
O
HOH
59
66.251
37.651
16.856
1.00
33.53
O


HETATM
2770
O
HOH
60
63.282
31.611
25.681
1.00
44.64
O


HETATM
2771
O
HOH
61
71.430
55.918
41.920
1.00
36.49
O


HETATM
2772
O
HOH
62
65.638
58.677
21.385
1.00
35.26
O


HETATM
2773
O
HOH
63
55.080
46.995
17.425
1.00
53.19
O


HETATM
2774
O
HOH
64
50.562
31.766
16.460
1.00
43.10
O


HETATM
2775
O
HOH
65
74.644
37.157
10.791
1.00
39.58
O


HETATM
2776
O
HOH
66
62.315
61.756
37.610
1.00
36.98
O


HETATM
2777
O
HOH
67
73.617
64.778
30.740
1.00
42.65
O


HETATM
2778
O
HOH
68
55.753
71.270
16.210
1.00
37.70
O


HETATM
2779
O
HOH
69
60.894
73.990
38.995
1.00
52.68
O


HETATM
2780
O
HOH
70
54.230
73.527
38.967
1.00
53.01
O


HETATM
2781
O
HOH
71
85.347
49.247
39.609
1.00
46.03
O


HETATM
2782
O
HOH
72
90.366
44.868
34.983
1.00
60.08
O


HETATM
2783
O
HOH
73
74.553
34.802
40.308
1.00
42.36
O


HETATM
2784
O
HOH
74
92.253
47.877
34.577
1.00
48.24
O


HETATM
2785
O
HOH
75
62.333
64.301
35.516
1.00
42.55
O


HETATM
2786
O
HOH
76
75.293
38.619
8.177
1.00
42.95
O


HETATM
2787
O
HOH
77
74.834
47.737
35.645
1.00
45.47
O


HETATM
2788
O
HOH
78
43.248
43.725
23.511
1.00
41.40
O


HETATM
2789
O
HOH
79
92.749
48.847
23.299
1.00
48.74
O


HETATM
2790
O
HOH
80
81.622
38.388
24.165
1.00
48.40
O


HETATM
2791
O
HOH
81
69.535
35.845
7.684
1.00
44.93
O


HETATM
2792
O
HOH
82
66.021
28.568
15.079
1.00
43.38
O


HETATM
2793
O
HOH
83
63.363
58.444
43.595
1.00
60.19
O


HETATM
2794
O
HOH
84
50.760
46.222
35.814
1.00
40.54
O


HETATM
2795
O
HOH
85
73.050
33.188
26.343
1.00
59.24
O


HETATM
2796
O
HOH
86
60.595
29.978
22.680
1.00
52.27
O


HETATM
2797
O
HOH
87
69.555
45.175
46.108
1.00
47.35
O


HETATM
2798
O
HOH
88
91.680
50.881
35.482
1.00
58.01
O


HETATM
2799
O
HOH
89
54.754
33.372
37.626
1.00
47.38
O


HETATM
2800
O
HOH
90
70.270
53.925
17.757
1.00
43.71
O


HETATM
2801
O
HOH
91
86.174
38.632
29.884
1.00
51.68
O


HETATM
2802
O
HOH
92
50.223
32.982
11.986
1.00
53.26
O


HETATM
2803
O
HOH
93
69.797
32.727
38.335
1.00
48.52
O


HETATM
2804
O
HOH
94
45.294
44.791
32.974
1.00
45.93
O


HETATM
2805
O
HOH
95
50.957
50.719
21.814
1.00
47.04
O


HETATM
2806
O
HOH
96
67.427
59.503
38.921
1.00
51.20
O


HETATM
2807
O
HOH
97
45.814
48.859
27.359
1.00
52.57
O


HETATM
2808
O
HOH
98
67.272
72.374
31.829
1.00
43.34
O


HETATM
2809
O
HOH
99
81.547
54.867
13.482
1.00
56.22
O


HETATM
2810
O
HOH
100
73.436
41.135
42.320
1.00
51.99
O


HETATM
2811
O
HOH
101
45.438
41.435
12.889
1.00
51.81
O


HETATM
2812
O
HOH
102
72.135
31.364
23.780
1.00
49.13
O


HETATM
2813
O
HOH
103
64.895
66.481
39.105
1.00
64.76
O


HETATM
2814
O
HOH
104
67.577
69.286
38.086
1.00
45.89
O


HETATM
2815
O
HOH
105
69.612
68.635
35.879
1.00
63.93
O


HETATM
2816
O
HOH
106
72.031
67.254
32.046
1.00
48.47
O


HETATM
2817
O
HOH
107
72.305
61.345
21.016
1.00
44.10
O


HETATM
2818
O
HOH
108
74.756
62.694
19.263
1.00
48.65
O


HETATM
2819
O
HOH
109
95.910
46.347
27.675
1.00
53.29
O


HETATM
2820
O
HOH
110
94.046
48.897
25.977
1.00
51.23
O


HETATM
2821
O
HOH
111
97.282
43.405
26.308
1.00
55.88
O


HETATM
2822
O
HOH
112
96.131
51.037
25.453
1.00
43.15
O


HETATM
2823
O
HOH
113
79.236
36.729
24.882
1.00
50.87
O


HETATM
2824
O
HOH
114
79.234
40.387
31.965
1.00
38.53
O


HETATM
2825
O
HOH
115
81.670
39.064
21.018
1.00
60.16
O


HETATM
2826
O
HOH
116
60.063
41.314
40.014
1.00
53.39
O


HETATM
2827
O
HOH
117
68.407
44.274
48.786
1.00
58.93
O


HETATM
2828
O
HOH
118
73.852
38.881
40.464
1.00
54.08
O


HETATM
2829
O
HOH
119
66.435
34.694
36.949
1.00
50.41
O


HETATM
2830
O
HOH
120
68.667
31.549
25.842
1.00
64.44
O


HETATM
2831
O
HOH
121
65.857
31.082
26.881
1.00
40.73
O


HETATM
2832
O
HOH
122
62.672
33.363
29.890
1.00
48.58
O


HETATM
2833
O
HOH
123
61.493
33.436
27.087
1.00
48.36
O


HETATM
2834
O
HOH
124
69.854
28.735
27.500
1.00
61.68
O


HETATM
2835
O
HOH
125
64.874
31.147
29.825
1.00
60.07
O


HETATM
2836
O
HOH
126
71.711
32.640
30.005
1.00
47.37
O


HETATM
2837
O
HOH
127
52.466
50.282
19.032
1.00
52.65
O


HETATM
2838
O
HOH
128
49.739
53.604
24.073
1.00
61.02
O


HETATM
2839
O
HOH
129
48.481
31.684
25.480
1.00
54.44
O


HETATM
2840
O
HOH
130
65.224
61.485
37.955
1.00
47.75
O


HETATM
2841
O
HOH
131
72.681
36.196
7.328
1.00
60.10
O


HETATM
2842
O
HOH
132
54.600
53.590
40.349
1.00
61.76
O


HETATM
2843
O
HOH
133
55.212
44.260
39.797
1.00
54.33
O


HETATM
2844
O
HOH
134
58.628
61.370
13.634
1.00
55.77
O


HETATM
2845
O
HOH
135
78.074
50.966
38.251
1.00
55.68
O


HETATM
2846
O
HOH
136
76.140
52.648
36.261
1.00
34.66
O


HETATM
2847
O
HOH
137
66.486
54.699
47.835
1.00
67.66
O


HETATM
2848
O
HOH
138
74.079
55.395
38.640
1.00
55.76
O


HETATM
2849
O
HOH
139
72.037
53.724
43.983
1.00
49.73
O


HETATM
2850
O
HOH
140
89.745
53.305
35.869
1.00
47.56
O


HETATM
2851
O
HOH
141
66.701
41.042
2.783
1.00
58.40
O


HETATM
2852
O
HOH
142
92.676
53.997
36.233
1.00
50.74
O


HETATM
2853
O
HOH
143
70.897
57.476
14.491
1.00
45.37
O


HETATM
2854
O
HOH
144
68.797
43.869
0.416
1.00
57.30
O


HETATM
2855
O
HOH
145
63.760
40.147
3.283
1.00
60.15
O







CONECT
 202 2514


CONECT
1501 1502


CONECT
1502 1501 1503 1505


CONECT
1503 1502 1504


CONECT
1504 1503 1507


CONECT
1505 1502 1506


CONECT
1506 1505


CONECT
1507 1504


CONECT
2514  202


CONECT
2688 2689 2690 2691 2692


CONECT
2689 2688


CONECT
2690 2688


CONECT
2691 2688


CONECT
2692 2688 2693


CONECT
2693 2692 2694


CONECT
2694 2693 2695 2696


CONECT
2695 2694 2700


CONECT
2696 2694 2697 2698


CONECT
2697 2696


CONECT
2698 2696 2699 2700


CONECT
2699 2698


CONECT
2700 2695 2698 2701


CONECT
2701 2700 2702 2710


CONECT
2702 2701 2703


CONECT
2703 2702 2704


CONECT
2704 2703 2705 2710


CONECT
2705 2704 2706 2707


CONECT
2706 2705


CONECT
2707 2705 2708


CONECT
2708 2707 2709


CONECT
2709 2708 2710


CONECT
2710 2701 2704 2709


MASTER  521  0  3  14  18  0  0  6 2854  1  32  39


END


Figure 11


P-UC 5440


Page 1



















TABLE 3







HEADER
OXIDOREDUCTASE
08-AUG-02
1MEH








TITLE
INOSINE MONOPHOSPHATE DEHYDROGENASE (IMPDH) FROM









TITLE
  2
TRITRICHOMONAS FOETUS WITH IMP AND MOA BOUND








COMPND
MOL_ID: 1;









COMPND
  2
MOLECULE: INOSINE-5′-MONOPHOSPHATE DEHYDROGENASE;


COMPND
  3
CHAIN: A;


COMPND
  4
SYNONYM: IMP DEHYDROGENASE, IMPDH;


COMPND
  5
EC: 1.1.1.205;


COMPND
  6
ENGINEERED: YES








SOURCE
MOL_ID: 1;









SOURCE
  2
ORGANISM_SCIENTIFIC: TRITRICHOMONAS FOETUS;


SOURCE
  3
GENE: IMPDH;


SOURCE
  4
EXPRESSION_SYSTEM: ESCHERICHIA COLI;


SOURCE
  5
EXPRESSION_SYSTEM_COMMON: BACTERIA;


SOURCE
  6
EXPRESSION_SYSTEM_STRAIN: H712;


SOURCE
  7
EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;


SOURCE
  8
EXPRESSION_SYSTEM_PLASMID: PBACE








KEYWDS
ALPHA BETA BARREL


EXPDTA
X-RAY DIFFRACTION


AUTHOR
G. L. PROSISE, H. LUECKE









JRNL
AUTH
G. L. PROSISE, H. LUECKE


JRNL
TITL
CRYSTAL STRUCTURE OF T. FOETUS INOSINE


JRNL
TITL 2
MONOPHOSPHATE DEHYDROGENASE IN COMPLEX WITH


JRNL
TITL 3
SUBSTRATE, COFACTOR, AND ANALOGS:STRUCTURAL BASIS


JRNL
TITL 4
FOR THE RANDOM-IN ORDERED-OUT KINETIC MECHANISM


JRNL
REF
TO BE PUBLISHED


JRNL
REFN








REMARK
  1


REMARK
  2









REMARK
  2
RESOLUTION. 1.95 ANGSTROMS.


REMARK
  3


REMARK
  3
REFINEMENT.










REMARK
  3
PROGRAM
: CNS 1.1


REMARK
  3
AUTHORS
: BRUNGER, ADAMS, CLORE, DELANO, GROS, GROSSE-


REMARK
  3

: KUNSTLEVE, JIANG, KUSZEWSKI, NILGES, PANNU,


REMARK
  3

: READ, RICE, SIMONSON, WARREN


REMARK
  3









REMARK
  3
REFINEMENT TARGET : ENGH & HUBER


REMARK
  3


REMARK
  3
DATA USED IN REFINEMENT.











REMARK
  3
RESOLUTION RANGE HIGH
(ANGSTROMS)
: 1.95


REMARK
  3
RESOLUTION RANGE LOW
(ANGSTROMS)
: 19.98


REMARK
  3
DATA CUTOFF
(SIGMA(F))
: 0.000


REMARK
  3
OUTLIER CUTOFF HIGH
(RMS(ABS(F)))
: NULL











REMARK
  3
COMPLETENESS (WORKING+TEST)
(%)
: 98.6


REMARK
  3
NUMBER OF REFLECTIONS

: 44863


REMARK
  3









REMARK
  3
FIT TO DATA USED IN REFINEMENT.











REMARK
  3
CROSS-VALIDATION METHOD

: THROUGHOUT


REMARK
  3
FREE R VALUE TEST SET SELECTION

: RANDOM











REMARK
  3
R VALUE
(WORKING SET)
: 0.243











REMARK
  3
FREE R VALUE

: 0.272











REMARK
  3
FREE R VALUE TEST SET SIZE
(%)
: 5.100











REMARK
  3
FREE R VALUE TEST SET COUNT

: 2294


REMARK
  3
ESTIMATED ERROR OF FREE R VALUE

: 0.006









REMARK
  3



REMARK
  3
FIT IN THE HIGHEST RESOLUTION BIN.











REMARK
  3
TOTAL NUMBER OF BINS USED

: 6


REMARK
  3
BIN RESOLUTION RANGE HIGH
(A)
: 1.95


REMARK
  3
BIN RESOLUTION RANGE LOW
(A)
: 2.07


REMARK
  3
BIN COMPLETENESS (WORKING+TEST)
(%)
: 96.70











REMARK
  3
REFLECTIONS IN BIN
(WORKING SET)
: 6852


REMARK
  3
BIN R VALUE
(WORKING SET)
: 0.2630











REMARK
  3
BIN FREE R VALUE

: 0.2960











REMARK
  3
BIN FREE R VALUE TEST SET SIZE
(%)
: 4.60











REMARK
  3
BIN FREE R VALUE TEST SET COUNT

: 333


REMARK
  3
ESTIMATED ERROR OF BIN FREE R VALUE

: 0.016









REMARK
  3



REMARK
  3
NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.










REMARK
  3
PROTEIN ATOMS
: 2709


REMARK
  3
NUCLEIC ACID ATOMS
: 0


REMARK
  3
HETEROGEN ATOMS
: 47


REMARK
  3
SOLVENT ATOMS
: 193









REMARK
  3



REMARK
  3
B VALUES.











REMARK
  3
FROM WILSON PLOT
(A**2)
: 19.90


REMARK
  3
MEAN B VALUE
(OVERALL, A**2)
: 32.70









REMARK
  3
OVERALL ANISOTROPIC B VALUE.









REMARK
  3
B11 (A**2) : 0.00000


REMARK
  3
B22 (A**2) : 0.00000


REMARK
  3
B33 (A**2) : 0.00000


REMARK
  3
B12 (A**2) : 0.00000


REMARK
  3
B13 (A**2) : 0.00000


REMARK
  3
B23 (A**2) : 0.00000


REMARK
  3









REMARK
  3
ESTIMATED COORDINATE ERROR.











REMARK
  3
ESD FROM LUZZATI PLOT
(A)
: 0.25


REMARK
  3
ESD FROM SIGMAA
(A)
: 0.15


REMARK
  3
LOW RESOLUTION CUTOFF
(A)
: 5.00


REMARK
  3









REMARK
  3
CROSS-VALIDATED ESTIMATED COORDINATE ERROR.











REMARK
  3
ESD FROM C-V LUZZATI PLOT
(A)
: 0.29


REMARK
  3
ESD FROM C-V SIGMAA
(A)
: 0.18


REMARK
  3









REMARK
  3
RMS DEVIATIONS FROM IDEAL VALUES.











REMARK
  3
BOND LENGTHS
(A)
: 0.006


REMARK
  3
BOND ANGLES
(DEGREES)
: 1.20


REMARK
  3
DIHEDRAL ANGLES
(DEGREES)
: 22.30


REMARK
  3
IMPROPER ANGLES
(DEGREES)
: 0.70


REMARK
  3









REMARK
  3
ISOTROPIC THERMAL MODEL : RESTRAINED


REMARK
  3











REMARK
  3
ISOTROPIC THERMAL FACTOR RESTRAINTS.
 RMS
 SIGMA












REMARK
  3
MAIN-CHAIN BOND
(A**2)
: 0.810
; 1.500


REMARK
  3
MAIN-CHAIN ANGLE
(A**2)
: 1.440
; 2.000


REMARK
  3
SIDE-CHAIN BOND
(A**2)
: 1.060
; 2.000


REMARK
  3
SIDE-CHAIN ANGLE
(A**2)
: 1.700
; 2.500


REMARK
  3









REMARK
  3
BULK SOLVENT MODELING.










REMARK
  3
METHOD USED
: FLAT MODEL


REMARK
  3
KSOL
: 0.40


REMARK
  3
BSOL
: 48.93


REMARK
  3









REMARK
  3
NCS MODEL : NULL








REMARK
  3











REMARK
  3
NCS RESTRAINTS.
 RMS
 SIGMA/WEIGHT












REMARK
  3
GROUP 1 POSITIONAL
(A)
: NULL
; NULL


REMARK
  3
GROUP 1 B-FACTOR
(A**2)
: NULL
; NULL


REMARK
  3










REMARK
  3
PARAMETER FILE 1
: PROTEIN_REP.PARAM


REMARK
  3
PARAMETER FILE 2
: PARAM.GNSOL


REMARK
  3
PARAMETER FILE 3
: CIS_PEPTIDE.PARAM


REMARK
  3
PARAMETER FILE 4
: MPA.PAR


REMARK
  3
PARAMETER FILE 5
: IMP.PAR


REMARK
  3
PARAMETER FILE 6
: NULL


REMARK
  3
TOPOLOGY FILE 1
: PROTEIN.TOP


REMARK
  3
TOPOLOGY FILE 2
: IMP.TOP


REMARK
  3
TOPOLOGY FILE 3
: MPA.TOP


REMARK
  3
TOPOLOGY FILE 4
: K.TOP


REMARK
  3
TOPOLOGY FILE 5
: TOPH.GNSOL


REMARK
  3
TOPOLOGY FILE 6
: NULL


REMARK
  3









REMARK
  3
OTHER REFINEMENT REMARKS: NULL


REMARK
  4









REMARK
  4
1MEH COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998


REMARK
 100


REMARK
 100
THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-AUG-2002.


REMARK
 100
THE RCSB ID CODE IS RCSB016852.


REMARK
 200


REMARK
 200
EXPERIMENTAL DETAILS











REMARK
 200
EXPERIMENT TYPE

: X-RAY DIFFRACTION


REMARK
 200
DATE OF DATA COLLECTION

: 11-APR-2001











REMARK
 200
TEMPERATURE
(KELVIN)
: 100.0


REMARK
 200
PH

: 7.50


REMARK
 200
NUMBER OF CRYSTALS USED

: 1


REMARK
 200


REMARK
 200
SYNCHROTRON
(Y/N)
: Y











REMARK
 200
RADIATION SOURCE

: SSRL


REMARK
 200
BEAMLINE

: 9-1


REMARK
 200
X-RAY GENERATOR MODEL

: NULL











REMARK
 200
MONOCHROMATIC OR LAUE
(M/L)
: M


REMARK
 200
WAVELENGTH OR RANGE
(A)
: 0.97











REMARK
 200
MONOCHROMATOR

: NULL


REMARK
 200
OPTICS

: NULL


REMARK
 200


REMARK
 200
DETECTOR TYPE

: IMAGE PLATE


REMARK
 200
DETECTOR MANUFACTURER

: MARRESEARCH


REMARK
 200
INTENSITY-INTEGRATION SOFTWARE

: DENZO


REMARK
 200
DATA SCALING SOFTWARE

: SCALEPACK


REMARK
 200


REMARK
 200
NUMBER OF UNIQUE REFLECTIONS

: 44997











REMARK
 200
RESOLUTION RANGE HIGH
(A)
: 1.950


REMARK
 200
RESOLUTION RANGE LOW
(A)
: 20.000


REMARK
 200
REJECTION CRITERIA
(SIGMA(I))
: NULL


REMARK
 200









REMARK
 200
OVERALL.











REMARK
 200
COMPLETENESS FOR RANGE
(%)
: 99.0


REMARK
 200
DATA REDUNDANCY

: 5.400


REMARK
 200
R MERGE
(I)
: 0.05700


REMARK
 200
R SYM
(I)
: NULL











REMARK
 200
<I/SIGMA(I)> FOR THE DATA SET

: 25.9000


REMARK
 200









REMARK
 200
IN THE HIGHEST RESOLUTION SHELL.











REMARK
 200
HIGHEST RESOLUTION SHELL, RANGE HIGH
(A)
: 1.95


REMARK
 200
HIGHEST RESOLUTION SHELL, RANGE LOW
(A)
: 1.98











REMARK
 200
COMPLETENESS FOR SHELL
(%)
: 95.7


REMARK
 200
DATA REDUNDANCY IN SHELL

: NULL


REMARK
 200
R MERGE FOR SHELL
(I)
: 0.66000


REMARK
 200
R SYM FOR SHELL
(I)
: NULL


REMARK
 200
<I/SIGMA(I)> FOR SHELL

: 1.820


REMARK
 200









REMARK
 200
DIFFRACTION PROTOCOL: SINGLE WAVELENGTH


REMARK
 200
METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS


REMARK
 200
SOFTWARE USED: CNS


REMARK
 200
STARTING MODEL: PDB ENTRY 1AK5


REMARK
 200


REMARK
 200
REMARK: NULL


REMARK
 280


REMARK
 280
CRYSTAL


REMARK
 280
SOLVENT CONTENT, VS (%) : NULL


REMARK
 280
MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA) : NULL


REMARK
 280


REMARK
 280
CRYSTALLIZATION CONDITIONS: SODIUM MALONATE, TRIS, 2-









REMARK
 280
MERCAPTOETHANOL, EDTA, GLYCEROL


REMARK
 290









REMARK
 290
CRYSTALLOGRAPHIC SYMMETRY


REMARK
 290
SYMMETRY OPERATORS FOR SPACE GROUP: P 4 3 2


REMARK
 290










REMARK
 290
SYMOP
SYMMETRY


REMARK
 290
NNNMMM
OPERATOR


REMARK
 290
1555
X,Y,Z


REMARK
 290
2555
−X,−Y,Z


REMARK
 290
3555
−X,Y,−Z


REMARK
 290
4555
X,−Y,−Z


REMARK
 290
5555
Z,X,Y


REMARK
 290
6555
Z,−X,−Y


REMARK
 290
7555
−Z,−X,Y


REMARK
 290
8555
−Z,X,−Y


REMARK
 290
9555
Y,Z,X


REMARK
 290
10555
−Y,Z,−X


REMARK
 290
11555
Y,−Z,−X


REMARK
 290
12555
−Y,−Z,X


REMARK
 290
13555
Y,X,−Z


REMARK
 290
14555
−Y,−X,−Z


REMARK
 290
15555
Y,−X,Z


REMARK
 290
16555
−Y,X,Z


REMARK
 290
17555
X,Z,−Y


REMARK
 290
18555
−X,Z,Y


REMARK
 290
19555
−X,−Z,−Y


REMARK
 290
20555
X,−Z,Y


REMARK
 290
21555
Z,Y,−X


REMARK
 290
22555
Z,−Y,X


REMARK
 290
23555
−Z,Y,X


REMARK
 290
24555
−Z,−Y,−X


REMARK
 290










REMARK
 290
WHERE
NNN —> OPERATOR NUMBER


REMARK
 290

MMM —> TRANSLATION VECTOR


REMARK
 290









REMARK
 290
CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS


REMARK
 290
THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM


REMARK
 290
RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY


REMARK
 290
RELATED MOLECULES.















REMARK
 290
SMTRY1
 1
1.000000
0.000000
0.000000
0.00000



REMARK
 290
SMTRY2
 1
0.000000
1.000000
0.000000
0.00000


REMARK
 290
SMTRY3
 1
0.000000
0.000000
1.000000
0.00000


REMARK
 290
SMTRY1
 2
−1.000000
0.000000
0.000000
0.00000


REMARK
 290
SMTRY2
 2
0.000000
−1.000000
0.000000
0.00000


REMARK
 290
SMTRY3
 2
0.000000
0.000000
1.000000
0.00000


REMARK
 290
SMTRY1
 3
−1.000000
0.000000
0.000000
0.00000


REMARK
 290
SMTRY2
 3
0.000000
1.000000
0.000000
0.00000


REMARK
 290
SMTRY3
 3
0.000000
0.000000
−1.000000
0.00000


REMARK
 290
SMTRY1
 4
1.000000
0.000000
0.000000
0.00000


REMARK
 290
SMTRY2
 4
0.000000
−1.000000
0.000000
0.00000


REMARK
 290
SMTRY3
 4
0.000000
0.000000
−1.000000
0.00000


REMARK
 290
SMTRY1
 5
0.000000
0.000000
1.000000
0.00000


REMARK
 290
SMTRY2
 5
1.000000
0.000000
0.000000
0.00000


REMARK
 290
SMTRY3
 5
0.000000
1.000000
0.000000
0.00000


REMARK
 290
SMTRY1
 6
0.000000
0.000000
1.000000
0.00000


REMARK
 290
SMTRY2
 6
−1.000000
0.000000
0.000000
0.00000


REMARK
 290
SMTRY3
 6
0.000000
−1.000000
0.000000
0.00000


REMARK
 290
SMTRY1
 7
0.000000
0.000000
−1.000000
0.00000


REMARK
 290
SMTRY2
 7
−1.000000
0.000000
0.000000
0.00000


REMARK
 290
SMTRY3
 7
0.000000
1.000000
0.000000
0.00000


REMARK
 290
SMTRY1
 8
0.000000
0.000000
−1.000000
0.00000


REMARK
 290
SMTRY2
 8
1.000000
0.000000
0.000000
0.00000


REMARK
 290
SMTRY3
 8
0.000000
−1.000000
0.000000
0.00000


REMARK
 290
SMTRY1
 9
0.000000
1.000000
0.000000
0.00000


REMARK
 290
SMTRY2
 9
0.000000
0.000000
1.000000
0.00000


REMARK
 290
SMTRY3
 9
1.000000
0.000000
0.000000
0.00000


REMARK
 290
SMTRY1
10
0.000000
−1.000000
0.000000
0.00000


REMARK
 290
SMTRY2
10
0.000000
0.000000
1.000000
0.00000


REMARK
 290
SMTRY3
10
−1.000000
0.000000
0.000000
0.00000


REMARK
 290
SMTRY1
11
0.000000
1.000000
0.000000
0.00000


REMARK
 290
SMTRY2
11
0.000000
0.000000
−1.000000
0.00000


REMARK
 290
SMTRY3
11
−1.000000
0.000000
0.000000
0.00000


REMARK
 290
SMTRY1
12
0.000000
−1.000000
0.000000
0.00000


REMARK
 290
SMTRY2
12
0.000000
0.000000
−1.000000
0.00000


REMARK
 290
SMTRY3
12
1.000000
0.000000
0.000000
0.00000


REMARK
 290
SMTRY1
13
0.000000
1.000000
0.000000
0.00000


REMARK
 290
SMTRY2
13
1.000000
0.000000
0.000000
0.00000


REMARK
 290
SMTRY3
13
0.000000
0.000000
−1.000000
0.00000


REMARK
 290
SMTRY1
14
0.000000
−1.000000
0.000000
0.00000


REMARK
 290
SMTRY2
14
−1.000000
0.000000
0.000000
0.00000


REMARK
 290
SMTRY3
14
0.000000
0.000000
−1.000000
0.00000


REMARK
 290
SMTRY1
15
0.000000
1.000000
0.000000
0.00000


REMARK
 290
SMTRY2
15
−1.000000
0.000000
0.000000
0.00000


REMARK
 290
SMTRY3
15
0.000000
0.000000
1.000000
0.00000


REMARK
 290
SMTRY1
16
0.000000
−1.000000
0.000000
0.00000


REMARK
 290
SMTRY2
16
1.000000
0.000000
0.000000
0.00000


REMARK
 290
SMTRY3
16
0.000000
0.000000
1.000000
0.00000


REMARK
 290
SMTRY1
17
1.000000
0.000000
0.000000
0.00000


REMARK
 290
SMTRY2
17
0.000000
0.000000
1.000000
0.00000


REMARK
 290
SMTRY3
17
0.000000
−1.000000
0.000000
0.00000


REMARK
 290
SMTRY1
18
−1.000000
0.000000
0.000000
0.00000


REMARK
 290
SMTRY2
18
0.000000
0.000000
1.000000
0.00000


REMARK
 290
SMTRY3
18
0.000000
1.000000
0.000000
0.00000


REMARK
 290
SMTRY1
19
−1.000000
0.000000
0.000000
0.00000


REMARK
 290
SMTRY2
19
0.000000
0.000000
−1.000000
0.00000


REMARK
 290
SMTRY3
19
0.000000
−1.000000
0.000000
0.00000


REMARK
 290
SMTRY1
20
1.000000
0.000000
0.000000
0.00000


REMARK
 290
SMTRY2
20
0.000000
0.000000
−1.000000
0.00000


REMARK
 290
SMTRY3
20
0.000000
1.000000
0.000000
0.00000


REMARK
 290
SMTRY1
21
0.000000
0.000000
1.000000
0.00000


REMARK
 290
SMTRY2
21
0.000000
1.000000
0.000000
0.00000


REMARK
 290
SMTRY3
21
−1.000000
0.000000
0.000000
0.00000


REMARK
 290
SMTRY1
22
0.000000
0.000000
1.000000
0.00000


REMARK
 290
SMTRY2
22
0.000000
−1.000000
0.000000
0.00000


REMARK
 290
SMTRY3
22
1.000000
0.000000
0.000000
0.00000


REMARK
 290
SMTRY1
23
0.000000
0.000000
−1.000000
0.00000


REMARK
 290
SMTRY2
23
0.000000
1.000000
0.000000
0.00000


REMARK
 290
SMTRY3
23
1.000000
0.000000
0.000000
0.00000


REMARK
 290
SMTRY1
24
0.000000
0.000000
−1.000000
0.00000


REMARK
 290
SMTRY2
24
0.000000
−1.000000
0.000000
0.00000


REMARK
 290
SMTRY3
24
−1.000000
0.000000
0.000000
0.00000


REMARK
 290









REMARK
 290
REMARK: NULL


REMARK
 300


REMARK
 300
BIOMOLECULE: 1


REMARK
 300
THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT


REMARK
 300
WHICH CONSISTS OF 1 CHAIN(S). SEE REMARK 350 FOR


REMARK
 300
INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).


REMARK
 350


REMARK
 350
GENERATING THE BIOMOLECULE


REMARK
 350
COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN


REMARK
 350
BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE


REMARK
 350
MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS


REMARK
 350
GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND


REMARK
 350
CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.


REMARK
 350


REMARK
 350
BIOMOLECULE: 1


REMARK
 350
APPLY THE FOLLOWING TO CHAINS: A















REMARK
 350
BIOMT1
 1
1.000000
0.000000
0.000000
0.00000



REMARK
 350
BIOMT2
 1
0.000000
1.000000
0.000000
0.00000


REMARK
 350
BIOMT3
 1
0.000000
0.000000
1.000000
0.00000


REMARK
 350
BIOMT1
 2
−1.000000
0.000000
0.000000
153.48000


REMARK
 350
BIOMT2
 2
0.000000
−1.000000
0.000000
153.48000


REMARK
 350
BIOMT3
 2
0.000000
0.000000
1.000000
0.00000


REMARK
 350
BIOMT1
 3
0.000000
1.000000
0.000000
0.00000


REMARK
 350
BIOMT2
 3
−1.000000
0.000000
0.000000
153.48000


REMARK
 350
BIOMT3
 3
0.000000
0.000000
1.000000
0.00000


REMARK
 350
BIOMT1
 4
0.000000
−1.000000
0.000000
153.48000


REMARK
 350
BIOMT2
 4
1.000000
0.000000
0.000000
0.00000


REMARK
 350
BIOMT3
 4
0.000000
0.000000
1.000000
0.00000


REMARK
 465









REMARK
 465
MISSING RESIDUES


REMARK
 465
THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE


REMARK
 465
EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN


REMARK
 465
IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)


REMARK
 465












REMARK
 465
M
RES
C
SSSEQI











REMARK
 465
MET
A
 1


REMARK
 465
ASP
A
107


REMARK
 465
SER
A
108


REMARK
 465
ASN
A
109


REMARK
 465
VAL
A
110


REMARK
 465
LYS
A
111


REMARK
 465
PRO
A
112


REMARK
 465
ASP
A
113


REMARK
 465
GLN
A
114


REMARK
 465
THR
A
115


REMARK
 465
PHE
A
116


REMARK
 465
ALA
A
117


REMARK
 465
ASP
A
118


REMARK
 465
VAL
A
119


REMARK
 465
LEU
A
120


REMARK
 465
ALA
A
121


REMARK
 465
ILE
A
122


REMARK
 465
SER
A
123


REMARK
 465
GLN
A
124


REMARK
 465
ARG
A
125


REMARK
 465
THR
A
126


REMARK
 465
THR
A
127


REMARK
 465
HIS
A
128


REMARK
 465
ASN
A
129


REMARK
 465
THR
A
130


REMARK
 465
VAL
A
131


REMARK
 465
ALA
A
132


REMARK
 465
VAL
A
133


REMARK
 465
THR
A
134


REMARK
 465
ASP
A
135


REMARK
 465
ASP
A
136


REMARK
 465
GLY
A
137


REMARK
 465
THR
A
138


REMARK
 465
PRO
A
139


REMARK
 465
HIS
A
140


REMARK
 465
GLY
A
141


REMARK
 465
VAL
A
142


REMARK
 465
LEU
A
143


REMARK
 465
LEU
A
144


REMARK
 465
GLY
A
145


REMARK
 465
LEU
A
146


REMARK
 465
VAL
A
147


REMARK
 465
THR
A
148


REMARK
 465
GLN
A
149


REMARK
 465
ARG
A
150


REMARK
 465
ASP
A
151


REMARK
 465
TYR
A
152


REMARK
 465
PRO
A
153


REMARK
 465
ILE
A
154


REMARK
 465
ASP
A
155


REMARK
 465
LEU
A
156


REMARK
 465
THR
A
157


REMARK
 465
GLN
A
158


REMARK
 465
THR
A
159


REMARK
 465
GLU
A
160


REMARK
 465
THR
A
161


REMARK
 465
LYS
A
162


REMARK
 465
VAL
A
163


REMARK
 465
SER
A
164


REMARK
 465
ASP
A
165


REMARK
 465
MET
A
166


REMARK
 465
MET
A
167


REMARK
 465
THR
A
168


REMARK
 465
PRO
A
169


REMARK
 465
PHE
A
170


REMARK
 465
SER
A
171


REMARK
 465
LYS
A
172


REMARK
 465
LEU
A
173


REMARK
 465
VAL
A
174


REMARK
 465
THR
A
175


REMARK
 465
ALA
A
176


REMARK
 465
HIS
A
177


REMARK
 465
GLN
A
178


REMARK
 465
ASP
A
179


REMARK
 465
THR
A
180


REMARK
 465
LYS
A
181


REMARK
 465
LEU
A
182


REMARK
 465
SER
A
183


REMARK
 465
GLU
A
184


REMARK
 465
ALA
A
185


REMARK
 465
ASN
A
186


REMARK
 465
LYS
A
187


REMARK
 465
ILE
A
188


REMARK
 465
ILE
A
189


REMARK
 465
TRP
A
190


REMARK
 465
GLU
A
191


REMARK
 465
LYS
A
192


REMARK
 465
LYS
A
193


REMARK
 465
LEU
A
194


REMARK
 465
ASN
A
195


REMARK
 465
ALA
A
196


REMARK
 465
LEU
A
197


REMARK
 465
PRO
A
198


REMARK
 465
ILE
A
199


REMARK
 465
ILE
A
200


REMARK
 465
ASP
A
201


REMARK
 465
ASP
A
202


REMARK
 465
ASP
A
203


REMARK
 465
GLN
A
204


REMARK
 465
HIS
A
205


REMARK
 465
LEU
A
206


REMARK
 465
ARG
A
207


REMARK
 465
TYR
A
208


REMARK
 465
ILE
A
209


REMARK
 465
VAL
A
210


REMARK
 465
PHE
A
211


REMARK
 465
ARG
A
212


REMARK
 465
LYS
A
213


REMARK
 465
ASP
A
214


REMARK
 465
TYR
A
215


REMARK
 465
ASP
A
216


REMARK
 465
ARG
A
217


REMARK
 465
SER
A
218


REMARK
 465
GLN
A
219


REMARK
 465
VAL
A
220


REMARK
 465
CYS
A
221


REMARK
 465
GLN
A
417


REMARK
 465
ARG
A
418


REMARK
 465
TYR
A
419


REMARK
 465
ASP
A
420


REMARK
 465
LEU
A
421


REMARK
 465
GLY
A
422


REMARK
 465
GLY
A
423


REMARK
 465
LYS
A
424


REMARK
 465
GLN
A
425


REMARK
 465
LYS
A
426


REMARK
 465
LEU
A
427


REMARK
 465
SER
A
428


REMARK
 465
PHE
A
429


REMARK
 465
VAL
A
484


REMARK
 465
GLU
A
485


REMARK
 465
GLY
A
486


REMARK
 465
GLY
A
487


REMARK
 465
ALA
A
488


REMARK
 465
HIS
A
489


REMARK
 465
ASP
A
490


REMARK
 465
VAL
A
491


REMARK
 465
ILE
A
492


REMARK
 465
VAL
A
493


REMARK
 465
LYS
A
494


REMARK
 465
ASP
A
495


REMARK
 465
ARG
A
496


REMARK
 465
ILE
A
497


REMARK
 465
ASN
A
498


REMARK
 465
ASP
A
499


REMARK
 465
TYR
A
500


REMARK
 465
HIS
A
501


REMARK
 465
PRO
A
502


REMARK
 465
LYS
A
503


REMARK
 500









REMARK
 500
GEOMETRY AND STEREOCHEMISTRY


REMARK
 500
SUBTOPIC: COVALENT BOND LENGTHS


REMARK
 500


REMARK
 500
THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES


REMARK
 500
HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE


REMARK
 500
THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN


REMARK
 500
IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).


REMARK
 500


REMARK
 500
STANDARD TABLE:


REMARK
 500
FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3)


REMARK
 500


REMARK
 500
EXPECTED VALUES: ENGH AND HUBER, 1991


REMARK
 500
















REMARK
 500
M
RES
CSSEQI
ATM1
RES
CSSEQI
ATM2
DEVIATION


REMARK
 500

PRO
A 354
CG
PRO
A 354
CB
0.033


REMARK
 500

MET
A 373
CE
MET
A 373
SD
0.035


REMARK
 500









REMARK
 500
GEOMETRY AND STEREOCHEMISTRY


REMARK
 500
SUBTOPIC: COVALENT BOND ANGLES


REMARK
 500


REMARK
 500
THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES


REMARK
 500
HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE


REMARK
 500
THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN


REMARK
 500
IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).


REMARK
 500


REMARK
 500
STANDARD TABLE:


REMARK
 500
FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)


REMARK
 500


REMARK
 500
EXPECTED VALUES: ENGH AND HUBER, 1991


REMARK
 500

















REMARK
 500
M
RES
CSSEQI
ATM1

ATM2

ATM3



REMARK
 500

GLY
A  20
N
-
CA
-
C
ANGL. DEV. = −8.3 DEGREES


REMARK
 500

ILE
A  27
N
-
CA
-
C
ANGL. DEV. = −8.2 DEGREES


REMARK
 500

GLN
A  45
N
-
CA
-
C
ANGL. DEV. = −8.3 DEGREES


REMARK
 500

ILE
A  52
N
-
CA
-
C
ANGL. DEV. = −7.8 DEGREES


REMARK
 500

PRO
A  53
N
-
CA
-
C
ANGL. DEV. =  7.0 DEGREES


REMARK
 500

SER
A  63
N
-
CA
-
C
ANGL. DEV. =  8.6 DEGREES


REMARK
 500

PHE
A 266
N
-
CA
-
C
ANGL. DEV. = −8.1 DEGREES


REMARK
 500

LYS
A 394
N
-
CA
-
C
ANGL. DEV. = −7.7 DEGREES


REMARK
 500

LYS
A 472
N
-
CA
-
C
ANGL. DEV. =  7.3 DEGREES


REMARK
 500

LYS
A 474
N
-
CA
-
C
ANGL. DEV. = −8.1 DEGREES


REMARK
 500

LEU
A 477
N
-
CA
-
C
ANGL. DEV. = −7.0 DEGREES


REMARK
 900









REMARK
 900
RELATED ENTRIES










REMARK
 900
RELATED ID: 1AK5
RELATED DB: PDB









REMARK
 900
INOSINE MONOPHOSPHATE DEHYDROGENASE (IMPDH) FROM


REMARK
 900
TRITRICHOMONAS FOETUS










REMARK
 900
RELATED ID: 1ME7
RELATED DB: PDB









REMARK
 900
1ME7 CONTAINS THE SAME PROTEIN WITH RVP AND MOA BOUND










REMARK
 900
RELATED ID: 1ME8
RELATED DB: PDB









REMARK
 900
1ME8 CONTAINS THE SAME PROTEIN WITH RVP BOUND










REMARK
 900
RELATED ID: 1ME9
RELATED DB: PDB









REMARK
 900
1ME9 CONTAINS THE SAME PROTEIN WITH IMP BOUND










REMARK
 900
RELATED ID: 1MEI
RELATED DB: PDB









REMARK
 900
1MEI CONTAINS THE SAME PROTEIN WITH XMP AND MYCOPHENOLIC


REMARK
 900
ACID BOUND










REMARK
 900
RELATED ID: 1MEW
RELATED DB: PDB









REMARK
 900
1MEW CONTAINS THE SAME PROTEIN WITH XMP AND NAD BOUND
















DBREF
1MEH
A
1
503
SWS
P50097
IMDH_TRIFO
1
503















SEQADV
1MEH
CSO
A
319
SWS
P50097
CYS
319 MODIFIED RESIDUE























SEQRES
  1
A
503
MET
ALA
LYS
TYR
TYR
ASN
GLU
PRO
CYS
HIS
THR
PHE
ASN


SEQRES
  2
A
503
GLU
TYR
LEU
LEU
ILE
PRO
GLY
LEU
SER
THR
VAL
ASP
CYS


SEQRES
  3
A
503
ILE
PRO
SER
ASN
VAL
ASN
LEU
SER
THR
PRO
LEU
VAL
LYS


SEQRES
  4
A
503
PHE
GLN
LYS
GLY
GLN
GLN
SER
GLU
ILE
ASN
LEU
LYS
ILE


SEQRES
  5
A
503
PRO
LEU
VAL
SER
ALA
ILE
MET
GLN
SER
VAL
SER
GLY
GLU


SEQRES
  6
A
503
LYS
MET
ALA
ILE
ALA
LEU
ALA
ARG
GLU
GLY
GLY
ILE
SER


SEQRES
  7
A
503
PHE
ILE
PHE
GLY
SER
GLN
SER
ILE
GLU
SER
GLN
ALA
ALA


SEQRES
  8
A
503
MET
VAL
HIS
ALA
VAL
LYS
ASN
PHE
LYS
ALA
GLY
PHE
VAL


SEQRES
  9
A
503
VAL
SER
ASP
SER
ASN
VAL
LYS
PRO
ASP
GLN
THR
PHE
ALA


SEQRES
 10
A
503
ASP
VAL
LEU
ALA
ILE
SER
GLN
ARG
THR
THR
HIS
ASN
THR


SEQRES
 11
A
503
VAL
ALA
VAL
THR
ASP
ASP
GLY
THR
PRO
HIS
GLY
VAL
LEU


SEQRES
 12
A
503
LEU
GLY
LEU
VAL
THR
GLN
ARG
ASP
TYR
PRO
ILE
ASP
LEU


SEQRES
 13
A
503
THR
GLN
THR
GLU
THR
LYS
VAL
SER
ASP
MET
MET
THR
PRO


SEQRES
 14
A
503
PHE
SER
LYS
LEU
VAL
THR
ALA
HIS
GLN
ASP
THR
LYS
LEU


SEQRES
 15
A
503
SER
GLU
ALA
ASN
LYS
ILE
ILE
TRP
GLU
LYS
LYS
LEU
ASN


SEQRES
 16
A
503
ALA
LEU
PRO
ILE
ILE
ASP
ASP
ASP
GLN
HIS
LEU
ARG
TYR


SEQRES
 17
A
503
ILE
VAL
PHE
ARG
LYS
ASP
TYR
ASP
ARG
SER
GLN
VAL
CYS


SEQRES
 18
A
503
HIS
ASN
GLU
LEU
VAL
ASP
SER
GLN
LYS
ARG
TYR
LEU
VAL


SEQRES
 19
A
503
GLY
ALA
GLY
ILE
ASN
THR
ARG
ASP
PHE
ARG
GLU
ARG
VAL


SEQRES
 20
A
503
PRO
ALA
LEU
VAL
GLU
ALA
GLY
ALA
ASP
VAL
LEU
CYS
ILE


SEQRES
 21
A
503
ASP
SER
SER
ASP
GLY
PHE
SER
GLU
TRP
GLN
LYS
ILE
THR


SEQRES
 22
A
503
ILE
GLY
TRP
ILE
ARG
GLU
LYS
TYR
GLY
ASP
LYS
VAL
LYS


SEQRES
 23
A
503
VAL
GLY
ALA
GLY
ASN
ILE
VAL
ASP
GLY
GLU
GLY
PHE
ARG


SEQRES
 24
A
503
TYR
LEU
ALA
ASP
ALA
GLY
ALA
ASP
PHE
ILE
LYS
ILE
GLY


SEQRES
 25
A
503
ILE
GLY
GLY
GLY
SER
ILE
CSO
ILE
THR
ARG
GLU
GLN
LYS


SEQRES
 26
A
503
GLY
ILE
GLY
ARG
GLY
GLN
ALA
THR
ALA
VAL
ILE
ASP
VAL


SEQRES
 27
A
503
VAL
ALA
GLU
ARG
ASN
LYS
TYR
PHE
GLU
GLU
THR
GLY
ILE


SEQRES
 28
A
503
TYR
ILE
PRO
VAL
CYS
SER
ASP
GLY
GLY
ILE
VAL
TYR
ASP


SEQRES
 29
A
503
TYR
HIS
MET
THR
LEU
ALA
LEU
ALA
MET
GLY
ALA
ASP
PHE


SEQRES
 30
A
503
ILE
MET
LEU
GLY
ARG
TYR
PHE
ALA
ARG
PHE
GLU
GLU
SER


SEQRES
 31
A
503
PRO
THR
ARG
LYS
VAL
THR
ILE
ASN
GLY
SER
VAL
MET
LYS


SEQRES
 32
A
503
GLU
TYR
TRP
GLY
GLU
GLY
SER
SER
ARG
ALA
ARG
ASN
TRP


SEQRES
 33
A
503
GLN
ARG
TYR
ASP
LEU
GLY
GLY
LYS
GLN
LYS
LEU
SER
PHE


SEQRES
 34
A
503
GLU
GLU
GLY
VAL
ASP
SER
TYR
VAL
PRO
TYR
ALA
GLY
LYS


SEQRES
 35
A
503
LEU
LYS
ASP
ASN
VAL
GLU
ALA
SER
LEU
ASN
LYS
VAL
LYS


SEQRES
 36
A
503
SER
THR
MET
CYS
ASN
CYS
GLY
ALA
LEU
THR
ILE
PRO
GLN


SEQRES
 37
A
503
LEU
GLN
SER
LYS
ALA
LYS
ILE
THR
LEU
VAL
SER
SER
VAL


SEQRES
 38
A
503
SER
ILE
VAL
GLU
GLY
GLY
ALA
HIS
ASP
VAL
ILE
VAL
LYS


SEQRES
 39
A
503
ASP
ARG
ILE
ASN
ASP
TYR
HIS
PRO
LYS












MODRES
1MEH
CSO A
319
 CYS
S-HYDROXYCYSTEINE


HET
CSO
A 319

 7


HET
  K
A 900

 1


HET
IMP
 602

23


HET
MOA
 600

23









HETNAM
CSO
S-HYDROXYCYSTEINE


HETNAM
  K
POTASSIUM ION


HETNAM
IMP
INOSINIC ACID


HETNAM
MOA
MYCOPHENOLIC ACID


HETSYN
MOA
6-(1,3-DIHYDRO-7-HYDROXY-5-METHOXY-4-METHYL-1-










HETSYN
  2
MOA
OXOISOBENZOFURAN-6-YL)-4-METHYL-4-HEXANOIC ACID










FORMUL
  1
CSO
 C3 H7 N1 O3 S1


FORMUL
  2
  K
 K1 1+


FORMUL
  3
IMP
 C10 H13 N4 O8 P1


FORMUL
  4
MOA
 C17 H20 O6


FORMUL
  5
HOH
*193(H2 O1)



















HELIX
  1
1
THR
A
 11
ASN
A
 13
 5

 3



HELIX
  2
2
ILE
A
 27
VAL
A
 31
 5

 5


HELIX
  3
3
GLY
A
 64
GLU
A
 74
 1

11


HELIX
  4
4
SER
A
 85
ASN
A
 98
 1

14


HELIX
  5
5
ASP
A
242
GLY
A
254
 1

13


HELIX
  6
6
SER
A
267
GLY
A
282
 1

16


HELIX
  7
7
ASP
A
283
VAL
A
285
 5

 3


HELIX
  8
8
ASP
A
294
GLY
A
305
 1

12


HELIX
  9
9
GLY
A
316
ARG
A
322
 5

 7


HELIX
 10
10
GLY
A
330
GLY
A
350
 1

21


HELIX
 11
11
TYR
A
363
MET
A
373
 1

11


HELIX
 12
12
GLY
A
381
ARG
A
386
 1

 6


HELIX
 13
13
LYS
A
442
CYS
A
461
 1

20


HELIX
 14
14
THR
A
465
ALA
A
473
 1

 9
























SHEET
  1
A
2 TYR
A  15
LEU
A
 17
 0











SHEET
  2
A
2 ILE
A 475
LEU
A
477
−1
O
THR
A
476
N
LEU
A
 16


SHEET
  1
B
2 THR
A  35
PRO
A
 36
 0


SHEET
  2
B
2 ASN
A  49
LEU
A
 50
−1
O
LEU
A
 50
N
THR
A
 35


SHEET
  1
C
2 PHE
A  40
GLN
A
 41
 0


SHEET
  2
C
2 ILE
A 351
TYR
A
352
−1
O
TYR
A
352
N
PHE
A
 40


SHEET
  1
D
9 LEU
A  54
SER
A
 56
 0


SHEET
  2
D
9 ILE
A  77
ILE
A
 80
 1
O
ILE
A
 77
N
SER
A
 56


SHEET
  3
D
9 GLY
A 235
ILE
A
238
 1
O
GLY
A
237
N
ILE
A
 80


SHEET
  4
D
9 VAL
A 257
ILE
A
260
 1
O
CYS
A
259
N
ILE
A
238


SHEET
  5
D
9 VAL
A 287
ILE
A
292
 1
O
GLY
A
288
N
LEU
A
258


SHEET
  6
D
9 ILE
A 309
ILE
A
311
 1
O
LYS
A
310
N
ALA
A
289


SHEET
  7
D
9 VAL
A 355
ASP
A
358
 1
O
CYS
A
356
N
ILE
A
311


SHEET
  8
D
9 PHE
A 377
LEU
A
380
 1
O
MET
A
379
N
SER
A
357


SHEET
  9
D
9 LEU
A  54
SER
A
 56
 1
N
VAL
A
 55
O
ILE
A
378


SHEET
  1
E
3 LYS
A 394
ILE
A
397
 0


SHEET
  2
E
3 SER
A 400
TRP
A
406
−1
O
MET
A
402
N
VAL
A
395


SHEET
  3
E
3 ASP
A 434
PRO
A
438
−1
O
SER
A
435
N
TYR
A
405
















SSBOND
  1
CYS
A
 26
CYS
A
459




CISPEP
  1
GLY
A
290
ASN
A
291
0
1.32















CRYST1
 153.480
153.480
153.480
90.00
90.00
90.00
P 4 3 2
24











ORIGX1
1.000000
0.000000
0.000000
0.00000


ORIGX2
0.000000
1.000000
0.000000
0.00000


ORIGX3
0.000000
0.000000
1.000000
0.00000


SCALE1
0.006516
0.000000
0.000000
0.00000


SCALE2
0.000000
0.006516
0.000000
0.00000


SCALE3
0.000000
0.000000
0.006516
0.00000




















ATOM
  1
N
ALA
A
 2
54.528
74.306
36.657
1.00
34.86

N



ATOM
  2
CA
ALA
A
 2
55.364
73.391
35.830
1.00
34.91

C


ATOM
  3
C
ALA
A
 2
56.681
73.065
36.533
1.00
35.04

C


ATOM
  4
O
ALA
A
 2
57.152
73.829
37.373
1.00
34.42

O


ATOM
  5
CB
ALA
A
 2
55.650
74.032
34.477
1.00
34.75

C


ATOM
  6
N
LYS
A
 3
57.264
71.925
36.179
1.00
35.15

N


ATOM
  7
CA
LYS
A
 3
58.535
71.498
36.749
1.00
35.98

C


ATOM
  8
C
LYS
A
 3
59.629
71.674
35.700
1.00
35.70

C


ATOM
  9
O
LYS
A
 3
59.467
71.259
34.552
1.00
35.42

O


ATOM
 10
CB
LYS
A
 3
58.459
70.029
37.187
1.00
36.70

C


ATOM
 11
CG
LYS
A
 3
59.819
69.387
37.449
1.00
38.59

C


ATOM
 12
CD
LYS
A
 3
59.689
67.979
38.016
1.00
39.69

C


ATOM
 13
CE
LYS
A
 3
61.003
67.211
37.901
1.00
40.42

C


ATOM
 14
NZ
LYS
A
 3
62.157
67.940
38.510
1.00
40.89

N


ATOM
 15
N
TYR
A
 4
60.733
72.298
36.099
1.00
35.51

N


ATOM
 16
CA
TYR
A
 4
61.864
72.539
35.210
1.00
36.45

C


ATOM
 17
C
TYR
A
 4
63.081
71.752
35.695
1.00
37.94

C


ATOM
 18
O
TYR
A
 4
63.055
71.166
36.775
1.00
38.19

O


ATOM
 19
CB
TYR
A
 4
62.182
74.040
35.171
1.00
34.85

C


ATOM
 20
CG
TYR
A
 4
61.071
74.870
34.566
1.00
33.25

C


ATOM
 21
CD1
TYR
A
 4
60.904
74.944
33.182
1.00
32.63

C


ATOM
 22
CD2
TYR
A
 4
60.158
75.545
35.375
1.00
32.51

C


ATOM
 23
CE1
TYR
A
 4
59.850
75.670
32.618
1.00
31.87

C


ATOM
 24
CE2
TYR
A
 4
59.099
76.273
34.821
1.00
32.01

C


ATOM
 25
CZ
TYR
A
 4
58.953
76.328
33.445
1.00
31.47

C


ATOM
 26
OH
TYR
A
 4
57.900
77.024
32.896
1.00
31.76

O


ATOM
 27
N
TYR
A
 5
64.144
71.733
34.898
1.00
40.06

N


ATOM
 28
CA
TYR
A
 5
65.351
70.998
35.272
1.00
41.80

C


ATOM
 29
C
TYR
A
 5
66.588
71.888
35.355
1.00
42.70

C


ATOM
 30
O
TYR
A
 5
66.654
72.941
34.719
1.00
42.98

O


ATOM
 31
CB
TYR
A
 5
65.596
69.850
34.286
1.00
42.18

C


ATOM
 32
CG
TYR
A
 5
64.446
68.871
34.224
1.00
42.27

C


ATOM
 33
CD1
TYR
A
 5
63.238
69.225
33.630
1.00
42.61

C


ATOM
 34
CD2
TYR
A
 5
64.551
67.603
34.797
1.00
42.57

C


ATOM
 35
CE1
TYR
A
 5
62.160
68.347
33.611
1.00
42.81

C


ATOM
 36
CE2
TYR
A
 5
63.478
66.715
34.783
1.00
42.46

C


ATOM
 37
CZ
TYR
A
 5
62.285
67.096
34.188
1.00
42.90

C


ATOM
 38
OH
TYR
A
 5
61.211
66.234
34.173
1.00
42.71

O


ATOM
 39
N
ASN
A
 6
67.561
71.455
36.153
1.00
43.48

N


ATOM
 40
CA
ASN
A
 6
68.802
72.199
36.349
1.00
44.29

C


ATOM
 41
C
ASN
A
 6
69.702
72.229
35.117
1.00
44.03

C


ATOM
 42
O
ASN
A
 6
70.291
73.263
34.800
1.00
44.49

O


ATOM
 43
CB
ASN
A
 6
69.575
71.615
37.534
1.00
45.28

C


ATOM
 44
CG
ASN
A
 6
68.911
71.909
38.867
1.00
46.42

C


ATOM
 45
OD1
ASN
A
 6
69.164
71.229
39.863
1.00
47.16

O


ATOM
 46
ND2
ASN
A
 6
68.065
72.935
38.895
1.00
46.63

N


ATOM
 47
N
GLU
A
 7
69.812
71.102
34.421
1.00
43.48

N


ATOM
 48
CA
GLU
A
 7
70.659
71.039
33.233
1.00
42.70

C


ATOM
 49
C
GLU
A
 7
69.882
70.632
31.986
1.00
41.37

C


ATOM
 50
O
GLU
A
 7
68.858
69.955
32.073
1.00
40.86

O


ATOM
 51
CB
GLU
A
 7
71.803
70.041
33.446
1.00
44.08

C


ATOM
 52
CG
GLU
A
 7
72.774
70.384
34.577
1.00
45.95

C


ATOM
 53
CD
GLU
A
 7
73.516
71.695
34.358
1.00
46.95

C


ATOM
 54
OE1
GLU
A
 7
74.048
71.911
33.246
1.00
47.35

O


ATOM
 55
OE2
GLU
A
 7
73.575
72.507
35.307
1.00
48.10

O


ATOM
 56
N
PRO
A
 8
70.364
71.050
30.803
1.00
39.91

N


ATOM
 57
CA
PRO
A
 8
69.704
70.711
29.540
1.00
38.65

C


ATOM
 58
C
PRO
A
 8
70.048
69.265
29.203
1.00
37.69

C


ATOM
 59
O
PRO
A
 8
71.039
68.738
29.707
1.00
37.18

O


ATOM
 60
CB
PRO
A
 8
70.324
71.698
28.559
1.00
38.70

C


ATOM
 61
CG
PRO
A
 8
71.731
71.816
29.074
1.00
39.39

C


ATOM
 62
CD
PRO
A
 8
71.529
71.926
30.570
1.00
39.63

C


ATOM
 63
N
CYS
A
 9
69.235
68.616
28.372
1.00
36.47

N


ATOM
 64
CA
CYS
A
 9
69.517
67.235
28.005
1.00
35.60

C


ATOM
 65
C
CYS
A
 9
70.554
67.179
26.882
1.00
34.44

C


ATOM
 66
O
CYS
A
 9
70.712
68.138
26.116
1.00
34.18

O


ATOM
 67
CB
CYS
A
 9
68.226
66.497
27.617
1.00
36.20

C


ATOM
 68
SG
CYS
A
 9
67.191
67.270
26.369
1.00
39.57

S


ATOM
 69
N
HIS
A
 10
71.269
66.060
26.799
1.00
32.73

N


ATOM
 70
CA
HIS
A
 10
72.327
65.882
25.808
1.00
31.17

C


ATOM
 71
C
HIS
A
 10
72.184
64.600
24.990
1.00
30.48

C


ATOM
 72
O
HIS
A
 10
71.527
63.650
25.413
1.00
29.49

O


ATOM
 73
CB
HIS
A
 10
73.684
65.852
26.513
1.00
31.38

C


ATOM
 74
CG
HIS
A
 10
73.953
67.049
27.368
1.00
31.58

C


ATOM
 75
ND1
HIS
A
 10
74.340
68.264
26.847
1.00
32.08

N


ATOM
 76
CD2
HIS
A
 10
73.893
67.217
28.710
1.00
32.22

C


ATOM
 77
CE1
HIS
A
 10
74.511
69.129
27.832
1.00
31.71

C


ATOM
 78
NE2
HIS
A
 10
74.245
68.518
28.972
1.00
32.26

N


ATOM
 79
N
THR
A
 11
72.823
64.580
23.822
1.00
29.90

N


ATOM
 80
CA
THR
A
 11
72.796
63.417
22.936
1.00
29.38

C


ATOM
 81
C
THR
A
 11
74.134
62.681
23.054
1.00
28.79

C


ATOM
 82
O
THR
A
 11
75.057
63.175
23.699
1.00
28.16

O


ATOM
 83
CB
THR
A
 11
72.594
63.836
21.470
1.00
30.26

C


ATOM
 84
OG1
THR
A
 11
73.709
64.626
21.045
1.00
31.91

O


ATOM
 85
CG2
THR
A
 11
71.311
64.660
21.316
1.00
31.15

C


ATOM
 86
N
PHE
A
 12
74.240
61.510
22.433
1.00
28.35

N


ATOM
 87
CA
PHE
A
 12
75.474
60.730
22.493
1.00
28.54

C


ATOM
 88
C
PHE
A
 12
76.684
61.440
21.883
1.00
28.64

C


ATOM
 89
O
PHE
A
 12
77.813
61.252
22.340
1.00
27.98

O


ATOM
 90
CB
PHE
A
 12
75.282
59.367
21.816
1.00
27.87

C


ATOM
 91
CG
PHE
A
 12
74.379
58.428
22.578
1.00
27.50

C


ATOM
 92
CD1
PHE
A
 12
74.549
58.232
23.946
1.00
27.53

C


ATOM
 93
CD2
PHE
A
 12
73.374
57.724
21.923
1.00
27.61

C


ATOM
 94
CE1
PHE
A
 12
73.729
57.348
24.652
1.00
26.85

C


ATOM
 95
CE2
PHE
A
 12
72.549
56.834
22.621
1.00
27.24

C


ATOM
 96
CZ
PHE
A
 12
72.729
56.648
23.985
1.00
26.78

C


ATOM
 97
N
ASN
A
 13
76.449
62.246
20.851
1.00
28.52

N


ATOM
 98
CA
ASN
A
 13
77.527
62.988
20.191
1.00
29.04

C


ATOM
 99
C
ASN
A
 13
78.243
63.954
21.131
1.00
28.55

C


ATOM
 100
O
ASN
A
 13
79.339
64.428
20.829
1.00
28.82

O


ATOM
 101
CB
ASN
A
 13
76.969
63.792
19.016
1.00
30.99

C


ATOM
 102
CG
ASN
A
 13
76.995
63.027
17.716
1.00
32.29

C


ATOM
 103
OD1
ASN
A
 13
76.291
63.379
16.772
1.00
34.44

O


ATOM
 104
ND2
ASN
A
 13
77.823
61.990
17.647
1.00
32.33

N


ATOM
 105
N
GLU
A
 14
77.625
64.255
22.265
1.00
27.53

N


ATOM
 106
CA
GLU
A
 14
78.218
65.190
23.212
1.00
27.62

C


ATOM
 107
C
GLU
A
 14
79.093
64.530
24.278
1.00
26.94

C


ATOM
 108
O
GLU
A
 14
79.548
65.199
25.203
1.00
27.17

O


ATOM
 109
CB
GLU
A
 14
77.114
66.003
23.890
1.00
28.36

C


ATOM
 110
CG
GLU
A
 14
76.224
66.769
22.912
1.00
29.57

C


ATOM
 111
CD
GLU
A
 14
75.134
67.557
23.608
1.00
30.53

C


ATOM
 112
OE1
GLU
A
 14
75.468
68.455
24.411
1.00
31.64

O


ATOM
 113
OE2
GLU
A
 14
73.941
67.281
23.352
1.00
31.42

O


ATOM
 114
N
TYR
A
 15
79.343
63.231
24.140
1.00
26.43

N


ATOM
 115
CA
TYR
A
 15
80.150
62.509
25.123
1.00
26.24

C


ATOM
 116
C
TYR
A
 15
81.325
61.721
24.555
1.00
26.03

C


ATOM
 117
O
TYR
A
 15
81.325
61.315
23.393
1.00
25.65

O


ATOM
 118
CB
TYR
A
 15
79.264
61.538
25.909
1.00
26.61

C


ATOM
 119
CG
TYR
A
 15
78.257
62.197
26.818
1.00
27.62

C


ATOM
 120
CD1
TYR
A
 15
78.604
62.578
28.112
1.00
28.33

C


ATOM
 121
CD2
TYR
A
 15
76.954
62.447
26.383
1.00
28.22

C


ATOM
 122
CE1
TYR
A
 15
77.682
63.188
28.958
1.00
29.62

C


ATOM
 123
CE2
TYR
A
 15
76.023
63.063
27.222
1.00
29.03

C


ATOM
 124
CZ
TYR
A
 15
76.395
63.429
28.505
1.00
29.97

C


ATOM
 125
OH
TYR
A
 15
75.495
64.057
29.335
1.00
31.38

O


ATOM
 126
N
LEU
A
 16
82.323
61.509
25.408
1.00
26.11

N


ATOM
 127
CA
LEU
A
 16
83.507
60.730
25.071
1.00
26.06

C


ATOM
 128
C
LEU
A
 16
83.925
59.997
26.336
1.00
25.29

C


ATOM
 129
O
LEU
A
 16
83.606
60.430
27.444
1.00
24.34

O


ATOM
 130
CB
LEU
A
 16
84.660
61.628
24.607
1.00
26.91

C


ATOM
 131
CG
LEU
A
 16
84.570
62.300
23.233
1.00
28.35

C


ATOM
 132
CD1
LEU
A
 16
85.820
63.150
23.016
1.00
27.97

C


ATOM
 133
CD2
LEU
A
 16
84.452
61.246
22.134
1.00
28.15

C


ATOM
 134
N
LEU
A
 17
84.634
58.889
26.165
1.00
24.72

N


ATOM
 135
CA
LEU
A
 17
85.119
58.097
27.290
1.00
24.73

C


ATOM
 136
C
LEU
A
 17
86.592
58.405
27.558
1.00
24.51

C


ATOM
 137
O
LEU
A
 17
87.386
58.553
26.626
1.00
24.84

O


ATOM
 138
CB
LEU
A
 17
84.970
56.603
26.983
1.00
24.74

C


ATOM
 139
CG
LEU
A
 17
83.551
56.029
26.964
1.00
25.01

C


ATOM
 140
CD1
LEU
A
 17
83.526
54.730
26.166
1.00
25.67

C


ATOM
 141
CD2
LEU
A
 17
83.086
55.796
28.391
1.00
25.40

C


ATOM
 142
N
ILE
A
 18
86.950
58.512
28.831
1.00
24.38

N


ATOM
 143
CA
ILE
A
 18
88.330
58.770
29.219
1.00
24.63

C


ATOM
 144
C
ILE
A
 18
88.900
57.408
29.613
1.00
24.85

C


ATOM
 145
O
ILE
A
 18
88.315
56.694
30.429
1.00
25.12

O


ATOM
 146
CB
ILE
A
 18
88.395
59.765
30.406
1.00
25.11

C


ATOM
 147
CG1
ILE
A
 18
87.927
61.147
29.926
1.00
25.53

C


ATOM
 148
CG2
ILE
A
 18
89.820
59.838
30.972
1.00
24.64

C


ATOM
 149
CD1
ILE
A
 18
87.909
62.211
31.010
1.00
27.24

C


ATOM
 150
N
PRO
A
 19
90.039
57.020
29.023
1.00
25.20

N


ATOM
 151
CA
PRO
A
 19
90.652
55.723
29.332
1.00
25.63

C


ATOM
 152
C
PRO
A
 19
90.914
55.433
30.805
1.00
25.58

C


ATOM
 153
O
PRO
A
 19
91.147
56.339
31.602
1.00
25.92

O


ATOM
 154
CB
PRO
A
 19
91.949
55.746
28.520
1.00
25.89

C


ATOM
 155
CG
PRO
A
 19
91.597
56.623
27.346
1.00
26.34

C


ATOM
 156
CD
PRO
A
 19
90.828
57.744
28.009
1.00
25.19

C


ATOM
 157
N
GLY
A
 20
90.847
54.150
31.149
1.00
25.25

N


ATOM
 158
CA
GLY
A
 20
91.121
53.705
32.505
1.00
25.27

C


ATOM
 159
C
GLY
A
 20
92.328
52.800
32.362
1.00
25.31

C


ATOM
 160
O
GLY
A
 20
92.926
52.766
31.293
1.00
24.89

O


ATOM
 161
N
LEU
A
 21
92.701
52.067
33.402
1.00
25.69

N


ATOM
 162
CA
LEU
A
 21
93.858
51.184
33.293
1.00
26.65

C


ATOM
 163
C
LEU
A
 21
93.558
49.946
32.453
1.00
26.91

C


ATOM
 164
O
LEU
A
 21
92.641
49.185
32.761
1.00
26.58

O


ATOM
 165
CB
LEU
A
 21
94.341
50.752
34.685
1.00
26.99

C


ATOM
 166
CG
LEU
A
 21
95.498
49.739
34.720
1.00
27.71

C


ATOM
 167
CD1
LEU
A
 21
96.721
50.297
34.003
1.00
27.95

C


ATOM
 168
CD2
LEU
A
 21
95.838
49.412
36.174
1.00
28.33

C


ATOM
 169
N
SER
A
 22
94.328
49.756
31.383
1.00
27.24

N


ATOM
 170
CA
SER
A
 22
94.165
48.593
30.516
1.00
28.46

C


ATOM
 171
C
SER
A
 22
95.145
47.515
30.977
1.00
29.50

C


ATOM
 172
O
SER
A
 22
96.353
47.747
31.011
1.00
28.90

O


ATOM
 173
CB
SER
A
 22
94.468
48.952
29.060
1.00
28.09

C


ATOM
 174
OG
SER
A
 22
93.577
49.931
28.573
1.00
27.34

O


ATOM
 175
N
THR
A
 23
94.621
46.342
31.323
1.00
30.24

N


ATOM
 176
CA
THR
A
 23
95.448
45.231
31.790
1.00
31.35

C


ATOM
 177
C
THR
A
 23
95.902
44.337
30.642
1.00
31.61

C


ATOM
 178
O
THR
A
 23
95.257
44.283
29.595
1.00
32.12

O


ATOM
 179
CB
THR
A
 23
94.682
44.369
32.810
1.00
31.67

C


ATOM
 180
OG1
THR
A
 23
93.384
44.061
32.286
1.00
33.18

O


ATOM
 181
CG2
THR
A
 23
94.532
45.105
34.126
1.00
32.36

C


ATOM
 182
N
VAL
A
 24
97.011
43.628
30.842
1.00
32.54

N


ATOM
 183
CA
VAL
A
 24
97.537
42.746
29.805
1.00
33.28

C


ATOM
 184
C
VAL
A
 24
96.516
41.691
29.378
1.00
34.33

C


ATOM
 185
O
VAL
A
 24
96.585
41.166
28.269
1.00
34.00

O


ATOM
 186
CB
VAL
A
 24
98.837
42.025
30.267
1.00
33.25

C


ATOM
 187
CG1
VAL
A
 24
99.934
43.049
30.552
1.00
32.51

C


ATOM
 188
CG2
VAL
A
 24
98.563
41.185
31.499
1.00
33.40

C


ATOM
 189
N
ASP
A
 25
95.563
41.392
30.253
1.00
36.01

N


ATOM
 190
CA
ASP
A
 25
94.552
40.389
29.945
1.00
38.28

C


ATOM
 191
C
ASP
A
 25
93.382
40.901
29.106
1.00
38.45

C


ATOM
 192
O
ASP
A
 25
92.550
40.114
28.668
1.00
38.94

O


ATOM
 193
CB
ASP
A
 25
94.023
39.761
31.241
1.00
40.34

C


ATOM
 194
CG
ASP
A
 25
93.159
40.713
32.048
1.00
42.35

C


ATOM
 195
OD1
ASP
A
 25
91.955
40.834
31.745
1.00
44.31

O


ATOM
 196
OD2
ASP
A
 25
93.684
41.348
32.985
1.00
44.56

O


ATOM
 197
N
CYS
A
 26
93.311
42.206
28.860
1.00
38.57

N


ATOM
 198
CA
CYS
A
 26
92.195
42.714
28.070
1.00
38.08

C


ATOM
 199
C
CYS
A
 26
92.480
42.930
26.597
1.00
38.07

C


ATOM
 200
O
CYS
A
 26
93.094
43.923
26.204
1.00
38.02

O


ATOM
 201
CB
CYS
A
 26
91.652
44.026
28.639
1.00
37.39

C


ATOM
 202
SG
CYS
A
 26
89.947
44.430
28.092
1.00
36.98

S


ATOM
 203
N
ILE
A
 27
92.025
41.982
25.789
1.00
37.71

N


ATOM
 204
CA
ILE
A
 27
92.144
42.070
24.347
1.00
37.96

C


ATOM
 205
C
ILE
A
 27
90.721
41.819
23.871
1.00
37.64

C


ATOM
 206
O
ILE
A
 27
89.965
41.100
24.526
1.00
37.26

O


ATOM
 207
CB
ILE
A
 27
93.099
40.999
23.765
1.00
38.64

C


ATOM
 208
CG1
ILE
A
 27
92.780
39.627
24.361
1.00
38.53

C


ATOM
 209
CG2
ILE
A
 27
94.548
41.407
24.020
1.00
38.05

C


ATOM
 210
CD1
ILE
A
 27
93.629
38.504
23.789
1.00
39.94

C


ATOM
 211
N
PRO
A
 28
90.329
42.424
22.742
1.00
37.48

N


ATOM
 212
CA
PRO
A
 28
88.985
42.267
22.185
1.00
37.27

C


ATOM
 213
C
PRO
A
 28
88.399
40.862
22.281
1.00
37.00

C


ATOM
 214
O
PRO
A
 28
87.245
40.696
22.675
1.00
36.24

O


ATOM
 215
CB
PRO
A
 28
89.165
42.726
20.741
1.00
37.74

C


ATOM
 216
CG
PRO
A
 28
90.147
43.838
20.892
1.00
37.23

C


ATOM
 217
CD
PRO
A
 28
91.165
43.259
21.858
1.00
37.69

C


ATOM
 218
N
SER
A
 29
89.195
39.854
21.934
1.00
36.71

N


ATOM
 219
CA
SER
A
 29
88.724
38.473
21.960
1.00
36.44

C


ATOM
 220
C
SER
A
 29
88.358
37.934
23.340
1.00
35.69

C


ATOM
 221
O
SER
A
 29
87.608
36.964
23.444
1.00
35.87

O


ATOM
 222
CB
SER
A
 29
89.747
37.543
21.291
1.00
37.16

C


ATOM
 223
OG
SER
A
 29
91.019
37.620
21.907
1.00
38.53

O


ATOM
 224
N
ASN
A
 30
88.874
38.547
24.400
1.00
34.53

N


ATOM
 225
CA
ASN
A
 30
88.541
38.084
25.744
1.00
33.29

C


ATOM
 226
C
ASN
A
 30
87.358
38.850
26.342
1.00
31.44

C


ATOM
 227
O
ASN
A
 30
86.903
38.526
27.436
1.00
31.19

O


ATOM
 228
CB
ASN
A
 30
89.747
38.195
26.686
1.00
35.35

C


ATOM
 229
CG
ASN
A
 30
90.819
37.158
26.396
1.00
37.30

C


ATOM
 230
OD1
ASN
A
 30
90.517
36.011
26.061
1.00
38.46

O


ATOM
 231
ND2
ASN
A
 30
92.078
37.552
26.544
1.00
37.96

N


ATOM
 232
N
VAL
A
 31
86.861
39.858
25.628
1.00
28.79

N


ATOM
 233
CA
VAL
A
 31
85.730
40.645
26.119
1.00
27.05

C


ATOM
 234
C
VAL
A
 31
84.408
39.897
25.955
1.00
26.82

C


ATOM
 235
O
VAL
A
 31
84.095
39.394
24.880
1.00
26.06

O


ATOM
 236
CB
VAL
A
 31
85.637
42.011
25.400
1.00
26.53

C


ATOM
 237
CG1
VAL
A
 31
84.345
42.724
25.797
1.00
25.95

C


ATOM
 238
CG2
VAL
A
 31
86.845
42.873
25.773
1.00
24.71

C


ATOM
 239
N
ASN
A
 32
83.645
39.835
27.041
1.00
26.34

N


ATOM
 240
CA
ASN
A
 32
82.355
39.140
27.082
1.00
26.00

C


ATOM
 241
C
ASN
A
 32
81.227
40.164
26.965
1.00
25.15

C


ATOM
 242
O
ASN
A
 32
81.080
41.016
27.842
1.00
25.29

O


ATOM
 243
CB
ASN
A
 32
82.240
38.396
28.420
1.00
26.75

C


ATOM
 244
CG
ASN
A
 32
80.958
37.583
28.549
1.00
28.49

C


ATOM
 245
OD1
ASN
A
 32
79.957
37.851
27.884
1.00
28.21

O


ATOM
 246
ND2
ASN
A
 32
80.984
36.591
29.434
1.00
29.77

N


ATOM
 247
N
LEU
A
 33
80.429
40.079
25.901
1.00
24.40

N


ATOM
 248
CA
LEU
A
 33
79.329
41.024
25.700
1.00
24.28

C


ATOM
 249
C
LEU
A
 33
77.947
40.492
26.094
1.00
23.96

C


ATOM
 250
O
LEU
A
 33
76.922
41.024
25.664
1.00
23.48

O


ATOM
 251
CB
LEU
A
 33
79.300
41.511
24.242
1.00
24.79

C


ATOM
 252
CG
LEU
A
 33
80.520
42.316
23.774
1.00
25.38

C


ATOM
 253
CD1
LEU
A
 33
80.321
42.761
22.333
1.00
25.52

C


ATOM
 254
CD2
LEU
A
 33
80.721
43.529
24.675
1.00
25.70

C


ATOM
 255
N
SER
A
 34
77.920
39.445
26.913
1.00
23.29

N


ATOM
 256
CA
SER
A
 34
76.653
38.882
27.375
1.00
23.29

C


ATOM
 257
C
SER
A
 34
75.916
39.961
28.168
1.00
22.23

C


ATOM
 258
O
SER
A
 34
76.544
40.817
28.780
1.00
22.07

O


ATOM
 259
CB
SER
A
 34
76.909
37.670
28.278
1.00
23.70

C


ATOM
 260
OG
SER
A
 34
75.698
37.216
28.861
1.00
27.20

O


ATOM
 261
N
THR
A
 35
74.588
39.923
28.170
1.00
21.87

N


ATOM
 262
CA
THR
A
 35
73.822
40.925
28.902
1.00
20.75

C


ATOM
 263
C
THR
A
 35
72.396
40.419
29.149
1.00
20.94

C


ATOM
 264
O
THR
A
 35
71.826
39.699
28.320
1.00
21.27

O


ATOM
 265
CB
THR
A
 35
73.814
42.277
28.112
1.00
21.38

C


ATOM
 266
OG1
THR
A
 35
73.523
43.368
29.001
1.00
21.23

O


ATOM
 267
CG2
THR
A
 35
72.786
42.239
26.991
1.00
20.66

C


ATOM
 268
N
PRO
A
 36
71.801
40.786
30.296
1.00
20.32

N


ATOM
 269
CA
PRO
A
 36
70.440
40.354
30.636
1.00
20.69

C


ATOM
 270
C
PRO
A
 36
69.338
41.049
29.841
1.00
20.70

C


ATOM
 271
O
PRO
A
 36
69.404
42.251
29.581
1.00
21.51

O


ATOM
 272
CB
PRO
A
 36
70.350
40.662
32.128
1.00
19.89

C


ATOM
 273
CG
PRO
A
 36
71.153
41.919
32.239
1.00
19.69

C


ATOM
 274
CD
PRO
A
 36
72.372
41.614
31.377
1.00
20.06

C


ATOM
 275
N
LEU
A
 37
68.317
40.285
29.471
1.00
21.00

N


ATOM
 276
CA
LEU
A
 37
67.197
40.830
28.718
1.00
21.84

C


ATOM
 277
C
LEU
A
 37
65.980
41.072
29.609
1.00
21.93

C


ATOM
 278
O
LEU
A
 37
65.257
42.049
29.416
1.00
21.26

O


ATOM
 279
CB
LEU
A
 37
66.798
39.882
27.582
1.00
22.24

C


ATOM
 280
CG
LEU
A
 37
65.696
40.404
26.650
1.00
22.01

C


ATOM
 281
CD1
LEU
A
 37
66.269
41.525
25.787
1.00
22.09

C


ATOM
 282
CD2
LEU
A
 37
65.164
39.289
25.777
1.00
22.26

C


ATOM
 283
N
VAL
A
 38
65.758
40.193
30.585
1.00
21.79

N


ATOM
 284
CA
VAL
A
 38
64.598
40.328
31.466
1.00
22.14

C


ATOM
 285
C
VAL
A
 38
64.950
40.384
32.950
1.00
22.71

C


ATOM
 286
O
VAL
A
 38
65.973
39.846
33.386
1.00
22.81

O


ATOM
 287
CB
VAL
A
 38
63.577
39.188
31.216
1.00
22.25

C


ATOM
 288
CG1
VAL
A
 38
63.064
39.267
29.776
1.00
22.95

C


ATOM
 289
CG2
VAL
A
 38
64.220
37.832
31.469
1.00
22.56

C


ATOM
 290
N
LYS
A
 39
64.081
41.032
33.719
1.00
22.22

N


ATOM
 291
CA
LYS
A
 39
64.296
41.230
35.144
1.00
22.61

C


ATOM
 292
C
LYS
A
 39
64.525
39.970
35.972
1.00
22.81

C


ATOM
 293
O
LYS
A
 39
64.018
38.892
35.655
1.00
22.94

O


ATOM
 294
CB
LYS
A
 39
63.130
42.019
35.750
1.00
22.84

C


ATOM
 295
CG
LYS
A
 39
61.814
41.259
35.802
1.00
23.34

C


ATOM
 296
CD
LYS
A
 39
60.751
42.061
36.548
1.00
25.09

C


ATOM
 297
CE
LYS
A
 39
59.425
41.313
36.606
1.00
25.38

C


ATOM
 298
NZ
LYS
A
 39
58.393
42.105
37.328
1.00
26.79

N


ATOM
 299
N
PHE
A
 40
65.297
40.140
37.041
1.00
23.12

N


ATOM
 300
CA
PHE
A
 40
65.620
39.065
37.973
1.00
24.28

C


ATOM
 301
C
PHE
A
 40
65.900
39.689
39.342
1.00
25.44

C


ATOM
 302
O
PHE
A
 40
66.044
40.914
39.456
1.00
26.48

O


ATOM
 303
CB
PHE
A
 40
66.848
38.272
37.492
1.00
22.73

C


ATOM
 304
CG
PHE
A
 40
68.061
39.123
37.217
1.00
22.77

C


ATOM
 305
CD1
PHE
A
 40
68.251
39.709
35.965
1.00
22.17

C


ATOM
 306
CD2
PHE
A
 40
69.011
39.347
38.212
1.00
22.45

C


ATOM
 307
CE1
PHE
A
 40
69.369
40.504
35.709
1.00
22.24

C


ATOM
 308
CE2
PHE
A
 40
70.133
40.139
37.971
1.00
22.30

C


ATOM
 309
CZ
PHE
A
 40
70.313
40.721
36.713
1.00
23.25

C


ATOM
 310
N
GLN
A
 41
65.968
38.850
40.373
1.00
25.99

N


ATOM
 311
CA
GLN
A
 41
66.233
39.300
41.741
1.00
27.32

C


ATOM
 312
C
GLN
A
 41
67.722
39.323
42.021
1.00
26.58

C


ATOM
 313
O
GLN
A
 41
68.494
38.644
41.350
1.00
26.05

O


ATOM
 314
CB
GLN
A
 41
65.580
38.360
42.767
1.00
28.63

C


ATOM
 315
CG
GLN
A
 41
64.073
38.418
42.811
1.00
32.62

C


ATOM
 316
CD
GLN
A
 41
63.568
39.766
43.273
1.00
34.57

C


ATOM
 317
OE1
GLN
A
 41
63.767
40.164
44.429
1.00
37.98

O


ATOM
 318
NE2
GLN
A
 41
62.915
40.485
42.375
1.00
35.13

N


ATOM
 319
N
LYS
A
 42
68.112
40.091
43.035
1.00
26.17

N


ATOM
 320
CA
LYS
A
 42
69.511
40.189
43.432
1.00
26.88

C


ATOM
 321
C
LYS
A
 42
70.104
38.790
43.624
1.00
26.18

C


ATOM
 322
O
LYS
A
 42
69.506
37.936
44.284
1.00
25.24

O


ATOM
 323
CB
LYS
A
 42
69.620
40.984
44.738
1.00
28.70

C


ATOM
 324
CG
LYS
A
 42
71.020
41.076
45.320
1.00
30.39

C


ATOM
 325
CD
LYS
A
 42
71.018
41.936
46.581
1.00
32.90

C


ATOM
 326
CE
LYS
A
 42
72.414
42.059
47.174
1.00
34.17

C


ATOM
 327
NZ
LYS
A
 42
72.429
42.982
48.349
1.00
36.34

N


ATOM
 328
N
GLY
A
 43
71.271
38.561
43.031
1.00
25.61

N


ATOM
 329
CA
GLY
A
 43
71.929
37.272
43.157
1.00
25.50

C


ATOM
 330
C
GLY
A
 43
71.574
36.267
42.079
1.00
24.98

C


ATOM
 331
O
GLY
A
 43
72.260
35.260
41.916
1.00
25.00

O


ATOM
 332
N
GLN
A
 44
70.500
36.523
41.343
1.00
24.55

N


ATOM
 333
CA
GLN
A
 44
70.092
35.606
40.287
1.00
24.65

C


ATOM
 334
C
GLN
A
 44
70.707
36.017
38.961
1.00
25.02

C


ATOM
 335
O
GLN
A
 44
71.394
37.029
38.868
1.00
24.74

O


ATOM
 336
CB
GLN
A
 44
68.569
35.610
40.117
1.00
24.79

C


ATOM
 337
CG
GLN
A
 44
67.766
35.374
41.390
1.00
24.46

C


ATOM
 338
CD
GLN
A
 44
66.270
35.328
41.124
1.00
25.55

C


ATOM
 339
OE1
GLN
A
 44
65.758
36.043
40.255
1.00
24.07

O


ATOM
 340
NE2
GLN
A
 44
65.557
34.499
41.884
1.00
24.73

N


ATOM
 341
N
GLN
A
 45
70.452
35.208
37.942
1.00
25.65

N


ATOM
 342
CA
GLN
A
 45
70.894
35.490
36.584
1.00
26.47

C


ATOM
 343
C
GLN
A
 45
69.584
35.679
35.834
1.00
25.54

C


ATOM
 344
O
GLN
A
 45
68.559
35.137
36.242
1.00
24.56

O


ATOM
 345
CB
GLN
A
 45
71.650
34.298
35.982
1.00
28.94

C


ATOM
 346
CG
GLN
A
 45
73.051
34.092
36.532
1.00
31.95

C


ATOM
 347
CD
GLN
A
 45
73.946
35.287
36.280
1.00
34.21

C


ATOM
 348
OE1
GLN
A
 45
74.117
35.716
35.137
1.00
36.26

O


ATOM
 349
NE2
GLN
A
 45
74.525
35.834
37.348
1.00
35.09

N


ATOM
 350
N
SER
A
 46
69.597
36.458
34.759
1.00
24.88

N


ATOM
 351
CA
SER
A
 46
68.379
36.643
33.986
1.00
24.59

C


ATOM
 352
C
SER
A
 46
68.038
35.329
33.287
1.00
25.11

C


ATOM
 353
O
SER
A
 46
68.937
34.576
32.907
1.00
24.15

O


ATOM
 354
CB
SER
A
 46
68.567
37.732
32.931
1.00
23.51

C


ATOM
 355
OG
SER
A
 46
67.375
37.895
32.188
1.00
22.66

O


ATOM
 356
N
GLU
A
 47
66.747
35.052
33.122
1.00
26.17

N


ATOM
 357
CA
GLU
A
 47
66.318
33.831
32.443
1.00
27.54

C


ATOM
 358
C
GLU
A
 47
66.708
33.896
30.970
1.00
27.30

C


ATOM
 359
O
GLU
A
 47
66.831
32.871
30.303
1.00
27.84

O


ATOM
 360
CB
GLU
A
 47
64.803
33.649
32.564
1.00
29.20

C


ATOM
 361
CG
GLU
A
 47
64.330
33.359
33.977
1.00
32.39

C


ATOM
 362
CD
GLU
A
 47
62.821
33.411
34.104
1.00
34.34

C


ATOM
 363
OE1
GLU
A
 47
62.145
32.508
33.566
1.00
35.91

O


ATOM
 364
OE2
GLU
A
 47
62.314
34.363
34.735
1.00
35.54

O


ATOM
 365
N
ILE
A
 48
66.890
35.109
30.458
1.00
26.04

N


ATOM
 366
CA
ILE
A
 48
67.284
35.284
29.063
1.00
25.89

C


ATOM
 367
C
ILE
A
 48
68.454
36.254
28.971
1.00
25.55

C


ATOM
 368
O
ILE
A
 48
68.353
37.409
29.387
1.00
25.22

O


ATOM
 369
CB
ILE
A
 48
66.133
35.844
28.193
1.00
26.14

C


ATOM
 370
CG1
ILE
A
 48
64.913
34.921
28.255
1.00
27.04

C


ATOM
 371
CG2
ILE
A
 48
66.604
35.977
26.747
1.00
25.69

C


ATOM
 372
CD1
ILE
A
 48
63.686
35.502
27.561
1.00
28.89

C


ATOM
 373
N
ASN
A
 49
69.567
35.775
28.431
1.00
24.84

N


ATOM
 374
CA
ASN
A
 49
70.750
36.603
28.277
1.00
24.41

C


ATOM
 375
C
ASN
A
 49
71.148
36.668
26.813
1.00
24.16

C


ATOM
 376
O
ASN
A
 49
71.297
35.637
26.157
1.00
24.28

O


ATOM
 377
CB
ASN
A
 49
71.914
36.030
29.095
1.00
24.39

C


ATOM
 378
CG
ASN
A
 49
71.693
36.157
30.592
1.00
25.36

C


ATOM
 379
OD1
ASN
A
 49
71.883
37.227
31.175
1.00
23.83

O


ATOM
 380
ND2
ASN
A
 49
71.273
35.065
31.219
1.00
25.54

N


ATOM
 381
N
LEU
A
 50
71.298
37.879
26.292
1.00
23.32

N


ATOM
 382
CA
LEU
A
 50
71.724
38.045
24.909
1.00
23.00

C


ATOM
 383
C
LEU
A
 50
73.222
37.769
24.916
1.00
23.10

C


ATOM
 384
O
LEU
A
 50
73.873
37.953
25.945
1.00
22.63

O


ATOM
 385
CB
LEU
A
 50
71.492
39.484
24.442
1.00
22.34

C


ATOM
 386
CG
LEU
A
 50
70.087
40.075
24.569
1.00
22.93

C


ATOM
 387
CD1
LEU
A
 50
70.100
41.515
24.045
1.00
23.23

C


ATOM
 388
CD2
LEU
A
 50
69.093
39.221
23.787
1.00
23.68

C


ATOM
 389
N
LYS
A
 51
73.769
37.322
23.788
1.00
23.53

N


ATOM
 390
CA
LYS
A
 51
75.201
37.074
23.707
1.00
24.58

C


ATOM
 391
C
LYS
A
 51
75.900
38.353
23.240
1.00
24.53

C


ATOM
 392
O
LYS
A
 51
77.099
38.525
23.448
1.00
24.51

O


ATOM
 393
CB
LYS
A
 51
75.492
35.878
22.789
1.00
26.26

C


ATOM
 394
CG
LYS
A
 51
75.057
34.561
23.438
1.00
27.65

C


ATOM
 395
CD
LYS
A
 51
75.469
33.337
22.639
1.00
29.52

C


ATOM
 396
CE
LYS
A
 51
74.978
32.065
23.324
1.00
30.43

C


ATOM
 397
NZ
LYS
A
 51
75.354
30.839
22.555
1.00
32.78

N


ATOM
 398
N
ILE
A
 52
75.139
39.240
22.596
1.00
23.97

N


ATOM
 399
CA
ILE
A
 52
75.641
40.555
22.192
1.00
23.86

C


ATOM
 400
C
ILE
A
 52
74.496
41.505
22.570
1.00
23.49

C


ATOM
 401
O
ILE
A
 52
73.322
41.143
22.469
1.00
24.41

O


ATOM
 402
CB
ILE
A
 52
75.985
40.667
20.678
1.00
24.09

C


ATOM
 403
CG1
ILE
A
 52
74.760
40.365
19.815
1.00
24.55

C


ATOM
 404
CG2
ILE
A
 52
77.174
39.749
20.352
1.00
24.63

C


ATOM
 405
CD1
ILE
A
 52
74.985
40.668
18.337
1.00
25.99

C


ATOM
 406
N
PRO
A
 53
74.821
42.722
23.019
1.00
22.93

N


ATOM
 407
CA
PRO
A
 53
73.827
43.720
23.437
1.00
22.98

C


ATOM
 408
C
PRO
A
 53
73.051
44.482
22.363
1.00
23.03

C


ATOM
 409
O
PRO
A
 53
72.673
45.631
22.586
1.00
23.64

O


ATOM
 410
CB
PRO
A
 53
74.654
44.657
24.305
1.00
22.57

C


ATOM
 411
CG
PRO
A
 53
75.944
44.714
23.542
1.00
23.54

C


ATOM
 412
CD
PRO
A
 53
76.190
43.246
23.194
1.00
23.09

C


ATOM
 413
N
LEU
A
 54
72.798
43.853
21.220
1.00
22.71

N


ATOM
 414
CA
LEU
A
 54
72.073
44.521
20.138
1.00
23.22

C


ATOM
 415
C
LEU
A
 54
70.760
43.834
19.777
1.00
22.95

C


ATOM
 416
O
LEU
A
 54
70.715
42.615
19.596
1.00
22.05

O


ATOM
 417
CB
LEU
A
 54
72.940
44.589
18.870
1.00
23.59

C


ATOM
 418
CG
LEU
A
 54
74.366
45.141
18.963
1.00
23.98

C


ATOM
 419
CD1
LEU
A
 54
75.015
45.095
17.583
1.00
24.50

C


ATOM
 420
CD2
LEU
A
 54
74.343
46.567
19.494
1.00
24.21

C


ATOM
 421
N
VAL
A
 55
69.695
44.625
19.675
1.00
22.53

N


ATOM
 422
CA
VAL
A
 55
68.392
44.104
19.284
1.00
22.49

C


ATOM
 423
C
VAL
A
 55
67.871
45.017
18.170
1.00
22.61

C


ATOM
 424
O
VAL
A
 55
68.116
46.229
18.183
1.00
22.47

O


ATOM
 425
CB
VAL
A
 55
67.387
44.060
20.475
1.00
22.79

C


ATOM
 426
CG1
VAL
A
 55
68.032
43.361
21.673
1.00
22.48

C


ATOM
 427
CG2
VAL
A
 55
66.924
45.452
20.845
1.00
22.85

C


ATOM
 428
N
SER
A
 56
67.180
44.438
17.193
1.00
22.42

N


ATOM
 429
CA
SER
A
 56
66.665
45.232
16.080
1.00
22.42

C


ATOM
 430
C
SER
A
 56
65.300
45.823
16.410
1.00
22.63

C


ATOM
 431
O
SER
A
 56
64.485
45.200
17.094
1.00
23.01

O


ATOM
 432
CB
SER
A
 56
66.611
44.389
14.794
1.00
22.36

C


ATOM
 433
OG
SER
A
 56
65.832
43.220
14.959
1.00
23.60

O


ATOM
 434
N
ALA
A
 57
65.076
47.039
15.921
1.00
22.62

N


ATOM
 435
CA
ALA
A
 57
63.853
47.799
16.163
1.00
22.97

C


ATOM
 436
C
ALA
A
 57
62.557
47.117
15.730
1.00
23.76

C


ATOM
 437
O
ALA
A
 57
62.533
46.338
14.781
1.00
24.23

O


ATOM
 438
CB
ALA
A
 57
63.971
49.174
15.496
1.00
21.89

C


ATOM
 439
N
ILE
A
 58
61.480
47.430
16.444
1.00
24.06

N


ATOM
 440
CA
ILE
A
 58
60.161
46.860
16.174
1.00
24.95

C


ATOM
 441
C
ILE
A
 58
59.552
47.647
15.016
1.00
25.14

C


ATOM
 442
O
ILE
A
 58
58.567
48.369
15.189
1.00
25.13

O


ATOM
 443
CB
ILE
A
 58
59.259
46.984
17.427
1.00
25.04

C


ATOM
 444
CG1
ILE
A
 58
60.035
46.504
18.661
1.00
25.04

C


ATOM
 445
CG2
ILE
A
 58
57.992
46.149
17.260
1.00
25.28

C


ATOM
 446
CD1
ILE
A
 58
59.239
46.529
19.950
1.00
24.84

C


ATOM
 447
N
MET
A
 59
60.143
47.483
13.834
1.00
25.33

N


ATOM
 448
CA
MET
A
 59
59.716
48.220
12.647
1.00
25.63

C


ATOM
 449
C
MET
A
 59
59.521
47.358
11.398
1.00
25.77

C


ATOM
 450
O
MET
A
 59
60.257
46.397
11.171
1.00
25.17

O


ATOM
 451
CB
MET
A
 59
60.750
49.310
12.354
1.00
25.44

C


ATOM
 452
CG
MET
A
 59
61.021
50.234
13.540
1.00
24.70

C


ATOM
 453
SD
MET
A
 59
62.394
51.382
13.288
1.00
24.28

S


ATOM
 454
CE
MET
A
 59
61.721
52.448
11.981
1.00
24.30

C


ATOM
 455
N
GLN
A
 60
58.533
47.724
10.585
1.00
26.54

N


ATOM
 456
CA
GLN
A
 60
58.234
47.005
9.345
1.00
27.32

C


ATOM
 457
C
GLN
A
 60
59.464
46.961
8.443
1.00
27.38

C


ATOM
 458
O
GLN
A
 60
59.719
45.963
7.771
1.00
27.43

O


ATOM
 459
CB
GLN
A
 60
57.109
47.701
8.564
1.00
27.95

C


ATOM
 460
CG
GLN
A
 60
55.838
47.994
9.337
1.00
29.68

C


ATOM
 461
CD
GLN
A
 60
54.802
48.717
8.482
1.00
31.25

C


ATOM
 462
OE1
GLN
A
 60
55.149
49.525
7.616
1.00
31.26

O


ATOM
 463
NE2
GLN
A
 60
53.526
48.442
8.735
1.00
31.01

N


ATOM
 464
N
SER
A
 61
60.220
48.053
8.427
1.00
27.19

N


ATOM
 465
CA
SER
A
 61
61.398
48.145
7.573
1.00
27.60

C


ATOM
 466
C
SER
A
 61
62.682
47.598
8.193
1.00
27.60

C


ATOM
 467
O
SER
A
 61
63.773
47.818
7.662
1.00
28.23

O


ATOM
 468
CB
SER
A
 61
61.620
49.602
7.152
1.00
27.83

C


ATOM
 469
OG
SER
A
 61
61.955
50.422
8.261
1.00
29.04

O


ATOM
 470
N
VAL
A
 62
62.560
46.867
9.296
1.00
26.86

N


ATOM
 471
CA
VAL
A
 62
63.745
46.337
9.957
1.00
26.42

C


ATOM
 472
C
VAL
A
 62
63.665
44.883
10.402
1.00
26.63

C


ATOM
 473
O
VAL
A
 62
64.432
44.045
9.938
1.00
27.23

O


ATOM
 474
CB
VAL
A
 62
64.098
47.181
11.210
1.00
26.30

C


ATOM
 475
CG1
VAL
A
 62
65.342
46.618
11.893
1.00
25.75

C


ATOM
 476
CG2
VAL
A
 62
64.310
48.631
10.820
1.00
25.78

C


ATOM
 477
N
SER
A
 63
62.725
44.585
11.291
1.00
26.87

N


ATOM
 478
CA
SER
A
 63
62.621
43.248
11.849
1.00
26.97

C


ATOM
 479
C
SER
A
 63
61.630
42.252
11.253
1.00
27.37

C


ATOM
 480
O
SER
A
 63
60.534
42.048
11.778
1.00
26.24

O


ATOM
 481
CB
SER
A
 63
62.394
43.364
13.359
1.00
27.27

C


ATOM
 482
OG
SER
A
 63
63.447
44.106
13.965
1.00
27.97

O


ATOM
 483
N
GLY
A
 64
62.049
41.627
10.158
1.00
27.73

N


ATOM
 484
CA
GLY
A
 64
61.248
40.610
9.507
1.00
28.60

C


ATOM
 485
C
GLY
A
 64
61.899
39.284
9.859
1.00
29.32

C


ATOM
 486
O
GLY
A
 64
62.870
39.257
10.623
1.00
28.30

O


ATOM
 487
N
GLU
A
 65
61.387
38.190
9.304
1.00
29.97

N


ATOM
 488
CA
GLU
A
 65
61.912
36.855
9.584
1.00
31.24

C


ATOM
 489
C
GLU
A
 65
63.413
36.688
9.339
1.00
30.93

C


ATOM
 490
O
GLU
A
 65
64.131
36.167
10.188
1.00
30.06

O


ATOM
 491
CB
GLU
A
 65
61.147
35.811
8.760
1.00
33.66

C


ATOM
 492
CG
GLU
A
 65
60.983
36.196
7.292
1.00
37.41

C


ATOM
 493
CD
GLU
A
 65
59.788
37.106
7.051
1.00
39.43

C


ATOM
 494
OE1
GLU
A
 65
58.650
36.587
7.069
1.00
41.83

O


ATOM
 495
OE2
GLU
A
 65
59.978
38.331
6.846
1.00
40.38

O


ATOM
 496
N
LYS
A
 66
63.884
37.123
8.176
1.00
30.29

N


ATOM
 497
CA
LYS
A
 66
65.295
36.996
7.837
1.00
30.29

C


ATOM
 498
C
LYS
A
 66
66.221
37.768
8.781
1.00
29.26

C


ATOM
 499
O
LYS
A
 66
67.294
37.284
9.140
1.00
28.41

O


ATOM
 500
CB
LYS
A
 66
65.528
37.423
6.380
1.00
31.58

C


ATOM
 501
CG
LYS
A
 66
64.731
38.637
5.917
1.00
33.89

C


ATOM
 502
CD
LYS
A
 66
63.214
38.395
5.941
1.00
34.74

C


ATOM
 503
CE
LYS
A
 66
62.489
39.441
5.136
1.00
35.36

C


ATOM
 504
NZ
LYS
A
 66
62.985
39.417
3.718
1.00
34.63

N


ATOM
 505
N
MET
A
 67
65.807
38.962
9.185
1.00
28.14

N


ATOM
 506
CA
MET
A
 67
66.606
39.765
10.104
1.00
26.95

C


ATOM
 507
C
MET
A
 67
66.722
39.019
11.433
1.00
26.58

C


ATOM
 508
O
MET
A
 67
67.812
38.889
11.997
1.00
25.12

O


ATOM
 509
CB
MET
A
 67
65.939
41.125
10.327
1.00
27.01

C


ATOM
 510
CG
MET
A
 67
66.628
42.020
11.347
1.00
25.99

C


ATOM
 511
SD
MET
A
 67
68.293
42.472
10.859
1.00
26.26

S


ATOM
 512
CE
MET
A
 67
67.950
43.550
9.432
1.00
25.77

C


ATOM
 513
N
ALA
A
 68
65.587
38.513
11.910
1.00
26.72

N


ATOM
 514
CA
ALA
A
 68
65.524
37.791
13.174
1.00
26.82

C


ATOM
 515
C
ALA
A
 68
66.457
36.590
13.203
1.00
27.20

C


ATOM
 516
O
ALA
A
 68
67.092
36.315
14.217
1.00
27.21

O


ATOM
 517
CB
ALA
A
 68
64.092
37.350
13.452
1.00
26.91

C


ATOM
 518
N
ILE
A
 69
66.532
35.867
12.092
1.00
27.20

N


ATOM
 519
CA
ILE
A
 69
67.403
34.702
12.011
1.00
27.15

C


ATOM
 520
C
ILE
A
 69
68.870
35.125
11.980
1.00
26.50

C


ATOM
 521
O
ILE
A
 69
69.700
34.568
12.695
1.00
27.23

O


ATOM
 522
CB
ILE
A
 69
67.089
33.867
10.747
1.00
27.71

C


ATOM
 523
CG1
ILE
A
 69
65.692
33.250
10.870
1.00
28.00

C


ATOM
 524
CG2
ILE
A
 69
68.144
32.787
10.558
1.00
27.79

C


ATOM
 525
CD1
ILE
A
 69
65.121
32.737
9.547
1.00
29.43

C


ATOM
 526
N
ALA
A
 70
69.184
36.116
11.154
1.00
25.73

N


ATOM
 527
CA
ALA
A
 70
70.556
36.592
11.029
1.00
25.41

C


ATOM
 528
C
ALA
A
 70
71.109
37.181
12.325
1.00
25.00

C


ATOM
 529
O
ALA
A
 70
72.260
36.936
12.683
1.00
24.51

O


ATOM
 530
CB
ALA
A
 70
70.645
37.627
9.914
1.00
25.47

C


ATOM
 531
N
LEU
A
 71
70.292
37.961
13.025
1.00
24.62

N


ATOM
 532
CA
LEU
A
 71
70.736
38.580
14.266
1.00
24.36

C


ATOM
 533
C
LEU
A
 71
70.878
37.541
15.372
1.00
24.81

C


ATOM
 534
O
LEU
A
 71
71.850
37.562
16.121
1.00
25.09

O


ATOM
 535
CB
LEU
A
 71
69.759
39.680
14.690
1.00
23.62

C


ATOM
 536
CG
LEU
A
 71
70.116
40.466
15.960
1.00
23.09

C


ATOM
 537
CD1
LEU
A
 71
71.583
40.872
15.932
1.00
22.51

C


ATOM
 538
CD2
LEU
A
 71
69.220
41.701
16.053
1.00
22.83

C


ATOM
 539
N
ALA
A
 72
69.916
36.629
15.471
1.00
25.59

N


ATOM
 540
CA
ALA
A
 72
69.982
35.583
16.490
1.00
26.49

C


ATOM
 541
C
ALA
A
 72
71.246
34.742
16.284
1.00
27.18

C


ATOM
 542
O
ALA
A
 72
71.868
34.287
17.249
1.00
26.99

O


ATOM
 543
CB
ALA
A
 72
68.739
34.699
16.421
1.00
26.25

C


ATOM
 544
N
ARG
A
 73
71.624
34.540
15.025
1.00
27.93

N


ATOM
 545
CA
ARG
A
 73
72.822
33.765
14.707
1.00
28.79

C


ATOM
 546
C
ARG
A
 73
74.084
34.417
15.267
1.00
28.77

C


ATOM
 547
O
ARG
A
 73
75.058
33.729
15.573
1.00
28.68

O


ATOM
 548
CB
ARG
A
 73
72.965
33.596
13.191
1.00
30.52

C


ATOM
 549
CG
ARG
A
 73
72.054
32.535
12.601
1.00
31.89

C


ATOM
 550
CD
ARG
A
 73
72.198
32.469
11.089
1.00
33.48

C


ATOM
 551
NE
ARG
A
 73
71.517
31.303
10.534
1.00
35.10

N


ATOM
 552
CZ
ARG
A
 73
71.257
31.135
9.241
1.00
36.83

C


ATOM
 553
NH1
ARG
A
 73
71.618
32.061
8.360
1.00
37.07

N


ATOM
 554
NH2
ARG
A
 73
70.642
30.034
8.825
1.00
37.30

N


ATOM
 555
N
GLU
A
 74
74.064
35.741
15.401
1.00
28.39

N


ATOM
 556
CA
GLU
A
 74
75.210
36.470
15.933
1.00
28.09

C


ATOM
 557
C
GLU
A
 74
75.100
36.720
17.444
1.00
27.22

C


ATOM
 558
O
GLU
A
 74
75.977
37.342
18.034
1.00
27.15

O


ATOM
 559
CB
GLU
A
 74
75.378
37.804
15.195
1.00
30.01

C


ATOM
 560
CG
GLU
A
 74
75.546
37.668
13.679
1.00
32.33

C


ATOM
 561
CD
GLU
A
 74
76.686
36.741
13.283
1.00
33.71

C


ATOM
 562
OE1
GLU
A
 74
77.836
36.984
13.704
1.00
36.00

O


ATOM
 563
OE2
GLU
A
 74
76.431
35.768
12.543
1.00
35.10

O


ATOM
 564
N
GLY
A
 75
74.021
36.251
18.066
1.00
26.36

N


ATOM
 565
CA
GLY
A
 75
73.872
36.427
19.504
1.00
25.20

C


ATOM
 566
C
GLY
A
 75
72.872
37.461
19.993
1.00
24.86

C


ATOM
 567
O
GLY
A
 75
72.677
37.607
21.200
1.00
24.26

O


ATOM
 568
N
GLY
A
 76
72.238
38.179
19.070
1.00
24.23

N


ATOM
 569
CA
GLY
A
 76
71.266
39.186
19.464
1.00
24.11

C


ATOM
 570
C
GLY
A
 76
69.848
38.706
19.237
1.00
23.43

C


ATOM
 571
O
GLY
A
 76
69.627
37.531
18.963
1.00
23.27

O


ATOM
 572
N
ILE
A
 77
68.876
39.604
19.346
1.00
23.31

N


ATOM
 573
CA
ILE
A
 77
67.494
39.205
19.127
1.00
22.63

C


ATOM
 574
C
ILE
A
 77
66.718
40.293
18.391
1.00
23.12

C


ATOM
 575
O
ILE
A
 77
66.984
41.487
18.563
1.00
22.23

O


ATOM
 576
CB
ILE
A
 77
66.797
38.873
20.470
1.00
22.89

C


ATOM
 577
CG1
ILE
A
 77
65.535
38.044
20.212
1.00
22.47

C


ATOM
 578
CG2
ILE
A
 77
66.465
40.163
21.230
1.00
22.43

C


ATOM
 579
CD1
ILE
A
 77
64.847
37.547
21.474
1.00
21.82

C


ATOM
 580
N
SER
A
 78
65.771
39.873
17.556
1.00
23.10

N


ATOM
 581
CA
SER
A
 78
64.942
40.813
16.809
1.00
23.37

C


ATOM
 582
C
SER
A
 78
63.526
40.796
17.362
1.00
23.52

C


ATOM
 583
O
SER
A
 78
63.044
39.762
17.820
1.00
24.10

O


ATOM
 584
CB
SER
A
 78
64.877
40.434
15.321
1.00
23.20

C


ATOM
 585
OG
SER
A
 78
66.125
40.583
14.671
1.00
24.07

O


ATOM
 586
N
PHE
A
 79
62.863
41.944
17.328
1.00
23.99

N


ATOM
 587
CA
PHE
A
 79
61.483
42.020
17.777
1.00
24.76

C


ATOM
 588
C
PHE
A
 79
60.617
42.208
16.534
1.00
24.96

C


ATOM
 589
O
PHE
A
 79
60.474
43.321
16.031
1.00
24.87

O


ATOM
 590
CB
PHE
A
 79
61.284
43.183
18.760
1.00
24.45

C


ATOM
 591
CG
PHE
A
 79
61.820
42.905
20.137
1.00
24.94

C


ATOM
 592
CD1
PHE
A
 79
63.161
43.126
20.438
1.00
25.40

C


ATOM
 593
CD2
PHE
A
 79
60.993
42.367
21.121
1.00
25.21

C


ATOM
 594
CE1
PHE
A
 79
63.674
42.812
21.699
1.00
25.47

C


ATOM
 595
CE2
PHE
A
 79
61.496
42.050
22.382
1.00
25.32

C


ATOM
 596
CZ
PHE
A
 79
62.839
42.272
22.670
1.00
24.97

C


ATOM
 597
N
ILE
A
 80
60.060
41.108
16.033
1.00
25.49

N


ATOM
 598
CA
ILE
A
 80
59.212
41.134
14.837
1.00
25.86

C


ATOM
 599
C
ILE
A
 80
58.160
42.236
14.964
1.00
25.66

C


ATOM
 600
O
ILE
A
 80
57.435
42.294
15.961
1.00
24.99

O


ATOM
 601
CB
ILE
A
 80
58.496
39.775
14.634
1.00
26.44

C


ATOM
 602
CG1
ILE
A
 80
59.527
38.640
14.575
1.00
26.91

C


ATOM
 603
CG2
ILE
A
 80
57.658
39.810
13.353
1.00
26.85

C


ATOM
 604
CD1
ILE
A
 80
60.497
38.729
13.410
1.00
27.62

C


ATOM
 605
N
PHE
A
 81
58.064
43.101
13.955
1.00
25.74

N


ATOM
 606
CA
PHE
A
 81
57.107
44.202
14.020
1.00
26.34

C


ATOM
 607
C
PHE
A
 81
55.665
43.759
14.221
1.00
26.79

C


ATOM
 608
O
PHE
A
 81
55.234
42.737
13.688
1.00
26.54

O


ATOM
 609
CB
PHE
A
 81
57.221
45.123
12.787
1.00
27.27

C


ATOM
 610
CG
PHE
A
 81
56.931
44.453
11.470
1.00
27.76

C


ATOM
 611
CD1
PHE
A
 81
57.864
43.610
10.877
1.00
27.97

C


ATOM
 612
CD2
PHE
A
 81
55.733
44.706
10.801
1.00
28.39

C


ATOM
 613
CE1
PHE
A
 81
57.614
43.027
9.631
1.00
28.62

C


ATOM
 614
CE2
PHE
A
 81
55.471
44.129
9.553
1.00
28.30

C


ATOM
 615
CZ
PHE
A
 81
56.414
43.290
8.969
1.00
28.84

C


ATOM
 616
N
GLY
A
 82
54.930
44.540
15.009
1.00
27.50

N


ATOM
 617
CA
GLY
A
 82
53.543
44.230
15.303
1.00
28.54

C


ATOM
 618
C
GLY
A
 82
52.553
45.047
14.496
1.00
29.14

C


ATOM
 619
O
GLY
A
 82
51.342
44.898
14.661
1.00
28.33

O


ATOM
 620
N
SER
A
 83
53.068
45.914
13.629
1.00
29.58

N


ATOM
 621
CA
SER
A
 83
52.222
46.746
12.780
1.00
30.10

C


ATOM
 622
C
SER
A
 83
51.858
45.966
11.515
1.00
30.82

C


ATOM
 623
O
SER
A
 83
52.172
46.368
10.393
1.00
30.41

O


ATOM
 624
CB
SER
A
 83
52.947
48.046
12.423
1.00
29.96

C


ATOM
 625
OG
SER
A
 83
54.228
47.778
11.889
1.00
29.80

O


ATOM
 626
N
GLN
A
 84
51.202
44.832
11.732
1.00
31.40

N


ATOM
 627
CA
GLN
A
 84
50.752
43.941
10.674
1.00
31.71

C


ATOM
 628
C
GLN
A
 84
49.694
43.059
11.328
1.00
32.16

C


ATOM
 629
O
GLN
A
 84
49.489
43.140
12.543
1.00
32.26

O


ATOM
 630
CB
GLN
A
 84
51.915
43.093
10.147
1.00
31.73

C


ATOM
 631
CG
GLN
A
 84
52.525
42.130
11.165
1.00
31.03

C


ATOM
 632
CD
GLN
A
 84
53.658
41.307
10.579
1.00
31.51

C


ATOM
 633
OE1
GLN
A
 84
53.500
40.679
9.532
1.00
31.44

O


ATOM
 634
NE2
GLN
A
 84
54.809
41.299
11.255
1.00
30.10

N


ATOM
 635
N
SER
A
 85
49.021
42.221
10.547
1.00
32.25

N


ATOM
 636
CA
SER
A
 85
47.986
41.365
11.115
1.00
32.76

C


ATOM
 637
C
SER
A
 85
48.568
40.370
12.113
1.00
33.10

C


ATOM
 638
O
SER
A
 85
49.736
39.988
12.020
1.00
33.02

O


ATOM
 639
CB
SER
A
 85
47.243
40.604
10.010
1.00
32.36

C


ATOM
 640
OG
SER
A
 85
48.034
39.553
9.489
1.00
32.58

O


ATOM
 641
N
ILE
A
 86
47.741
39.965
13.072
1.00
33.27

N


ATOM
 642
CA
ILE
A
 86
48.138
39.005
14.092
1.00
33.73

C


ATOM
 643
C
ILE
A
 86
48.637
37.732
13.412
1.00
34.65

C


ATOM
 644
O
ILE
A
 86
49.670
37.167
13.785
1.00
34.09

O


ATOM
 645
CB
ILE
A
 86
46.935
38.662
15.008
1.00
33.67

C


ATOM
 646
CG1
ILE
A
 86
46.553
39.889
15.842
1.00
33.78

C


ATOM
 647
CG2
ILE
A
 86
47.267
37.479
15.898
1.00
33.45

C


ATOM
 648
CD1
ILE
A
 86
45.321
39.696
16.704
1.00
34.30

C


ATOM
 649
N
GLU
A
 87
47.896
37.297
12.397
1.00
34.81

N


ATOM
 650
CA
GLU
A
 87
48.235
36.093
11.650
1.00
35.57

C


ATOM
 651
C
GLU
A
 87
49.582
36.220
10.946
1.00
34.64

C


ATOM
 652
O
GLU
A
 87
50.399
35.301
10.975
1.00
34.19

O


ATOM
 653
CB
GLU
A
 87
47.143
35.800
10.617
1.00
37.45

C


ATOM
 654
CG
GLU
A
 87
45.768
35.485
11.210
1.00
40.12

C


ATOM
 655
CD
GLU
A
 87
45.205
36.609
12.076
1.00
42.17

C


ATOM
 656
OE1
GLU
A
 87
45.205
37.779
11.629
1.00
42.59

O


ATOM
 657
OE2
GLU
A
 87
44.751
36.316
13.206
1.00
43.96

O


ATOM
 658
N
SER
A
 88
49.806
37.365
10.313
1.00
34.00

N


ATOM
 659
CA
SER
A
 88
51.045
37.619
9.592
1.00
34.14

C


ATOM
 660
C
SER
A
 88
52.264
37.630
10.523
1.00
33.33

C


ATOM
 661
O
SER
A
 88
53.291
37.015
10.225
1.00
33.84

O


ATOM
 662
CB
SER
A
 88
50.941
38.955
8.850
1.00
34.56

C


ATOM
 663
OG
SER
A
 88
52.106
39.207
8.086
1.00
37.63

O


ATOM
 664
N
GLN
A
 89
52.148
38.329
11.647
1.00
32.36

N


ATOM
 665
CA
GLN
A
 89
53.247
38.416
12.609
1.00
31.38

C


ATOM
 666
C
GLN
A
 89
53.538
37.064
13.255
1.00
31.34

C


ATOM
 667
O
GLN
A
 89
54.697
36.688
13.433
1.00
30.83

O


ATOM
 668
CB
GLN
A
 89
52.923
39.448
13.696
1.00
30.40

C


ATOM
 669
CG
GLN
A
 89
53.986
39.546
14.786
1.00
29.25

C


ATOM
 670
CD
GLN
A
 89
53.629
40.544
15.877
1.00
28.00

C


ATOM
 671
OE1
GLN
A
 89
52.470
40.658
16.275
1.00
26.78

O


ATOM
 672
NE2
GLN
A
 89
54.632
41.258
16.378
1.00
26.79

N


ATOM
 673
N
ALA
A
 90
52.486
36.333
13.608
1.00
31.60

N


ATOM
 674
CA
ALA
A
 90
52.654
35.022
14.225
1.00
31.80

C


ATOM
 675
C
ALA
A
 90
53.379
34.079
13.265
1.00
32.05

C


ATOM
 676
O
ALA
A
 90
54.178
33.245
13.686
1.00
32.08

O


ATOM
 677
CB
ALA
A
 90
51.297
34.447
14.613
1.00
31.91

C


ATOM
 678
N
ALA
A
 91
53.105
34.224
11.971
1.00
32.10

N


ATOM
 679
CA
ALA
A
 91
53.738
33.386
10.958
1.00
32.03

C


ATOM
 680
C
ALA
A
 91
55.248
33.614
10.934
1.00
32.05

C


ATOM
 681
O
ALA
A
 91
56.026
32.666
10.818
1.00
31.83

O


ATOM
 682
CB
ALA
A
 91
53.137
33.678
9.578
1.00
32.23

C


ATOM
 683
N
MET
A
 92
55.664
34.873
11.038
1.00
31.86

N


ATOM
 684
CA
MET
A
 92
57.090
35.190
11.037
1.00
31.76

C


ATOM
 685
C
MET
A
 92
57.762
34.598
12.270
1.00
31.37

C


ATOM
 686
O
MET
A
 92
58.860
34.053
12.185
1.00
31.68

O


ATOM
 687
CB
MET
A
 92
57.311
36.702
11.024
1.00
31.76

C


ATOM
 688
CG
MET
A
 92
56.857
37.392
9.759
1.00
32.23

C


ATOM
 689
SD
MET
A
 92
57.284
39.134
9.784
1.00
32.24

S


ATOM
 690
CE
MET
A
 92
56.701
39.656
8.159
1.00
32.37

C


ATOM
 691
N
VAL
A
 93
57.100
34.718
13.418
1.00
31.37

N


ATOM
 692
CA
VAL
A
 93
57.639
34.185
14.667
1.00
30.84

C


ATOM
 693
C
VAL
A
 93
57.828
32.678
14.526
1.00
31.49

C


ATOM
 694
O
VAL
A
 93
58.901
32.142
14.805
1.00
31.13

O


ATOM
 695
CB
VAL
A
 93
56.686
34.472
15.849
1.00
30.30

C


ATOM
 696
CG1
VAL
A
 93
57.131
33.699
17.086
1.00
29.35

C


ATOM
 697
CG2
VAL
A
 93
56.662
35.971
16.138
1.00
29.04

C


ATOM
 698
N
HIS
A
 94
56.775
32.003
14.076
1.00
32.42

N


ATOM
 699
CA
HIS
A
 94
56.812
30.557
13.884
1.00
33.18

C


ATOM
 700
C
HIS
A
 94
57.929
30.173
12.909
1.00
32.93

C


ATOM
 701
O
HIS
A
 94
58.667
29.217
13.147
1.00
33.48

O


ATOM
 702
CB
HIS
A
 94
55.447
30.078
13.369
1.00
34.65

C


ATOM
 703
CG
HIS
A
 94
55.280
28.591
13.374
1.00
35.98

C


ATOM
 704
ND1
HIS
A
 94
55.796
27.778
12.388
1.00
36.93

N


ATOM
 705
CD2
HIS
A
 94
54.656
27.768
14.251
1.00
36.50

C


ATOM
 706
CE1
HIS
A
 94
55.497
26.519
12.657
1.00
36.90

C


ATOM
 707
NE2
HIS
A
 94
54.806
26.486
13.782
1.00
37.15

N


ATOM
 708
N
ALA
A
 95
58.067
30.928
11.823
1.00
32.80

N


ATOM
 709
CA
ALA
A
 95
59.109
30.649
10.834
1.00
32.63

C


ATOM
 710
C
ALA
A
 95
60.507
30.700
11.453
1.00
32.64

C


ATOM
 711
O
ALA
A
 95
61.383
29.903
11.107
1.00
32.76

O


ATOM
 712
CB
ALA
A
 95
59.019
31.641
9.677
1.00
32.50

C


ATOM
 713
N
VAL
A
 96
60.721
31.642
12.365
1.00
32.04

N


ATOM
 714
CA
VAL
A
 96
62.023
31.770
13.011
1.00
31.47

C


ATOM
 715
C
VAL
A
 96
62.262
30.620
13.981
1.00
31.55

C


ATOM
 716
O
VAL
A
 96
63.329
30.007
13.976
1.00
31.64

O


ATOM
 717
CB
VAL
A
 96
62.142
33.105
13.783
1.00
30.96

C


ATOM
 718
CG1
VAL
A
 96
63.479
33.176
14.508
1.00
30.67

C


ATOM
 719
CG2
VAL
A
 96
62.009
34.266
12.824
1.00
31.22

C


ATOM
 720
N
LYS
A
 97
61.261
30.327
14.805
1.00
32.04

N


ATOM
 721
CA
LYS
A
 97
61.358
29.256
15.792
1.00
33.20

C


ATOM
 722
C
LYS
A
 97
61.543
27.872
15.169
1.00
34.86

C


ATOM
 723
O
LYS
A
 97
62.171
26.999
15.767
1.00
34.76

O


ATOM
 724
CB
LYS
A
 97
60.108
29.240
16.681
1.00
32.12

C


ATOM
 725
CG
LYS
A
 97
59.868
30.523
17.477
1.00
31.22

C


ATOM
 726
CD
LYS
A
 97
61.064
30.874
18.360
1.00
29.75

C


ATOM
 727
CE
LYS
A
 97
61.404
29.751
19.333
1.00
29.19

C


ATOM
 728
NZ
LYS
A
 97
62.616
30.076
20.141
1.00
29.12

N


ATOM
 729
N
ASN
A
 98
61.000
27.671
13.972
1.00
36.75

N


ATOM
 730
CA
ASN
A
 98
61.108
26.375
13.308
1.00
39.34

C


ATOM
 731
C
ASN
A
 98
61.978
26.386
12.055
1.00
40.41

C


ATOM
 732
O
ASN
A
 98
61.781
25.571
11.150
1.00
40.41

O


ATOM
 733
CB
ASN
A
 98
59.711
25.850
12.955
1.00
40.86

C


ATOM
 734
CG
ASN
A
 98
58.870
25.553
14.185
1.00
42.24

C


ATOM
 735
OD1
ASN
A
 98
58.468
26.461
14.912
1.00
44.16

O


ATOM
 736
ND2
ASN
A
 98
58.605
24.275
14.427
1.00
43.29

N


ATOM
 737
N
PHE
A
 99
62.950
27.293
12.010
1.00
41.32

N


ATOM
 738
CA
PHE
A
 99
63.837
27.410
10.854
1.00
42.37

C


ATOM
 739
C
PHE
A
 99
64.779
26.225
10.654
1.00
43.23

C


ATOM
 740
O
PHE
A
 99
65.086
25.860
9.519
1.00
43.09

O


ATOM
 741
CB
PHE
A
 99
64.680
28.682
10.957
1.00
42.31

C


ATOM
 742
CG
PHE
A
 99
65.533
28.941
9.746
1.00
42.53

C


ATOM
 743
CD1
PHE
A
 99
64.955
29.335
8.544
1.00
42.50

C


ATOM
 744
CD2
PHE
A
 99
66.913
28.780
9.803
1.00
42.81

C


ATOM
 745
CE1
PHE
A
 99
65.742
29.566
7.414
1.00
42.79

C


ATOM
 746
CE2
PHE
A
 99
67.707
29.009
8.681
1.00
42.73

C


ATOM
 747
CZ
PHE
A
 99
67.120
29.403
7.485
1.00
42.71

C


ATOM
 748
N
LYS
A
100
65.246
25.639
11.752
1.00
44.14

N


ATOM
 749
CA
LYS
A
100
66.173
24.512
11.678
1.00
45.76

C


ATOM
 750
C
LYS
A
100
65.520
23.178
11.337
1.00
47.12

C


ATOM
 751
O
LYS
A
100
66.214
22.185
11.130
1.00
47.59

O


ATOM
 752
CB
LYS
A
100
66.941
24.372
12.996
1.00
45.30

C


ATOM
 753
CG
LYS
A
100
67.867
25.541
13.304
1.00
44.67

C


ATOM
 754
CD
LYS
A
100
68.619
25.319
14.604
1.00
44.01

C


ATOM
 755
CE
LYS
A
100
69.645
26.417
14.840
1.00
43.17

C


ATOM
 756
NZ
LYS
A
100
70.359
26.229
16.128
1.00
42.38

N


ATOM
 757
N
ALA
A
101
64.193
23.152
11.279
1.00
48.59

N


ATOM
 758
CA
ALA
A
101
63.472
21.924
10.960
1.00
50.30

C


ATOM
 759
C
ALA
A
101
63.843
21.416
9.570
1.00
51.59

C


ATOM
 760
O
ALA
A
101
64.125
22.202
8.666
1.00
51.58

O


ATOM
 761
CB
ALA
A
101
61.967
22.162
11.043
1.00
49.96

C


ATOM
 762
N
GLY
A
102
63.846
20.095
9.410
1.00
53.11

N


ATOM
 763
CA
GLY
A
102
64.175
19.504
8.126
1.00
54.99

C


ATOM
 764
C
GLY
A
102
62.909
19.190
7.356
1.00
56.36

C


ATOM
 765
O
GLY
A
102
62.401
20.035
6.617
1.00
56.47

O


ATOM
 766
N
PHE
A
103
62.396
17.975
7.524
1.00
57.72

N


ATOM
 767
CA
PHE
A
103
61.167
17.580
6.848
1.00
59.15

C


ATOM
 768
C
PHE
A
103
59.987
18.171
7.609
1.00
59.91

C


ATOM
 769
O
PHE
A
103
59.771
17.853
8.779
1.00
60.20

O


ATOM
 770
CB
PHE
A
103
61.036
16.054
6.797
1.00
59.55

C


ATOM
 771
CG
PHE
A
103
62.114
15.377
5.996
1.00
59.88

C


ATOM
 772
CD1
PHE
A
103
63.409
15.269
6.495
1.00
60.13

C


ATOM
 773
CD2
PHE
A
103
61.835
14.854
4.739
1.00
59.99

C


ATOM
 774
CE1
PHE
A
103
64.411
14.649
5.753
1.00
60.20

C


ATOM
 775
CE2
PHE
A
103
62.830
14.232
3.988
1.00
60.34

C


ATOM
 776
CZ
PHE
A
103
64.122
14.130
4.497
1.00
60.26

C


ATOM
 777
N
VAL
A
104
59.229
19.035
6.942
1.00
60.70

N


ATOM
 778
CA
VAL
A
104
58.078
19.673
7.566
1.00
61.34

C


ATOM
 779
C
VAL
A
104
56.764
19.239
6.924
1.00
61.90

C


ATOM
 780
O
VAL
A
104
56.666
19.111
5.702
1.00
61.92

O


ATOM
 781
CB
VAL
A
104
58.185
21.212
7.479
1.00
61.42

C


ATOM
 782
CG1
VAL
A
104
56.991
21.858
8.169
1.00
61.56

C


ATOM
 783
CG2
VAL
A
104
59.485
21.679
8.118
1.00
61.49

C


ATOM
 784
N
VAL
A
105
55.757
19.014
7.761
1.00
62.35

N


ATOM
 785
CA
VAL
A
105
54.440
18.604
7.292
1.00
62.87

C


ATOM
 786
C
VAL
A
105
53.715
19.808
6.697
1.00
63.08

C


ATOM
 787
O
VAL
A
105
53.411
20.771
7.403
1.00
63.17

O


ATOM
 788
CB
VAL
A
105
53.591
18.034
8.450
1.00
62.93

C


ATOM
 789
CG1
VAL
A
105
52.234
17.585
7.931
1.00
63.00

C


ATOM
 790
CG2
VAL
A
105
54.324
16.876
9.109
1.00
62.99

C


ATOM
 791
N
SER
A
106
53.445
19.751
5.397
1.00
63.19

N


ATOM
 792
CA
SER
A
106
52.759
20.839
4.710
1.00
63.34

C


ATOM
 793
C
SER
A
106
51.372
21.071
5.298
1.00
63.37

C


ATOM
 794
O
SER
A
106
51.163
22.011
6.065
1.00
63.55

O


ATOM
 795
CB
SER
A
106
52.638
20.527
3.217
1.00
63.52

C


ATOM
 796
OG
SER
A
106
51.969
21.570
2.530
1.00
63.46

O


ATOM
 797
N
HIS
A
222
78.549
29.753
16.811
1.00
46.50

N


ATOM
 798
CA
HIS
A
222
79.214
29.762
18.111
1.00
46.34

C


ATOM
 799
C
HIS
A
222
78.515
30.714
19.076
1.00
45.23

C


ATOM
 800
O
HIS
A
222
78.376
30.423
20.263
1.00
45.39

O


ATOM
 801
CB
HIS
A
222
80.679
30.185
17.962
1.00
47.77

C


ATOM
 802
CG
HIS
A
222
81.512
29.225
17.170
1.00
49.66

C


ATOM
 803
ND1
HIS
A
222
81.651
27.897
17.515
1.00
50.29

N


ATOM
 804
CD2
HIS
A
222
82.269
29.406
16.061
1.00
50.09

C


ATOM
 805
CE1
HIS
A
222
82.457
27.302
16.653
1.00
50.69

C


ATOM
 806
NE2
HIS
A
222
82.847
28.195
15.761
1.00
50.78

N


ATOM
 807
N
ASN
A
223
78.079
31.857
18.560
1.00
43.45

N


ATOM
 808
CA
ASN
A
223
77.402
32.843
19.386
1.00
41.69

C


ATOM
 809
C
ASN
A
223
75.906
32.910
19.120
1.00
39.79

C


ATOM
 810
O
ASN
A
223
75.266
33.908
19.444
1.00
38.70

O


ATOM
 811
CB
ASN
A
223
78.024
34.225
19.171
1.00
43.26

C


ATOM
 812
CG
ASN
A
223
79.314
34.408
19.946
1.00
44.91

C


ATOM
 813
OD1
ASN
A
223
79.305
34.509
21.177
1.00
45.63

O


ATOM
 814
ND2
ASN
A
223
80.433
34.446
19.232
1.00
45.69

N


ATOM
 815
N
GLU
A
224
75.345
31.852
18.537
1.00
37.33

N


ATOM
 816
CA
GLU
A
224
73.915
31.836
18.254
1.00
35.82

C


ATOM
 817
C
GLU
A
224
73.110
31.935
19.540
1.00
33.98

C


ATOM
 818
O
GLU
A
224
73.464
31.338
20.555
1.00
34.05

O


ATOM
 819
CB
GLU
A
224
73.508
30.560
17.499
1.00
36.85

C


ATOM
 820
CG
GLU
A
224
73.919
29.250
18.173
1.00
38.61

C


ATOM
 821
CD
GLU
A
224
73.188
28.035
17.613
1.00
39.59

C


ATOM
 822
OE1
GLU
A
224
72.843
28.032
16.411
1.00
40.09

O


ATOM
 823
OE2
GLU
A
224
72.967
27.072
18.377
1.00
40.45

O


ATOM
 824
N
LEU
A
225
72.032
32.707
19.496
1.00
32.23

N


ATOM
 825
CA
LEU
A
225
71.162
32.869
20.651
1.00
31.01

C


ATOM
 826
C
LEU
A
225
69.988
31.928
20.443
1.00
30.52

C


ATOM
 827
O
LEU
A
225
69.142
32.164
19.578
1.00
29.48

O


ATOM
 828
CB
LEU
A
225
70.660
34.311
20.750
1.00
30.04

C


ATOM
 829
CG
LEU
A
225
69.753
34.608
21.947
1.00
29.97

C


ATOM
 830
CD1
LEU
A
225
70.505
34.321
23.250
1.00
29.58

C


ATOM
 831
CD2
LEU
A
225
69.294
36.056
21.899
1.00
28.91

C


ATOM
 832
N
VAL
A
226
69.938
30.863
21.238
1.00
30.37

N


ATOM
 833
CA
VAL
A
226
68.874
29.875
21.107
1.00
30.90

C


ATOM
 834
C
VAL
A
226
68.249
29.459
22.436
1.00
31.48

C


ATOM
 835
O
VAL
A
226
68.767
29.782
23.512
1.00
31.51

O


ATOM
 836
CB
VAL
A
226
69.405
28.604
20.414
1.00
30.86

C


ATOM
 837
CG1
VAL
A
226
69.837
28.924
18.997
1.00
30.18

C


ATOM
 838
CG2
VAL
A
226
70.579
28.040
21.209
1.00
31.20

C


ATOM
 839
N
ASP
A
227
67.130
28.743
22.352
1.00
31.82

N


ATOM
 840
CA
ASP
A
227
66.446
28.257
23.543
1.00
32.90

C


ATOM
 841
C
ASP
A
227
66.961
26.857
23.874
1.00
34.23

C


ATOM
 842
O
ASP
A
227
67.891
26.365
23.231
1.00
34.23

O


ATOM
 843
CB
ASP
A
227
64.921
28.225
23.339
1.00
32.40

C


ATOM
 844
CG
ASP
A
227
64.486
27.355
22.158
1.00
32.01

C


ATOM
 845
OD1
ASP
A
227
65.177
26.369
21.829
1.00
31.77

O


ATOM
 846
OD2
ASP
A
227
63.426
27.652
21.569
1.00
31.75

O


ATOM
 847
N
SER
A
228
66.354
26.219
24.871
1.00
35.88

N


ATOM
 848
CA
SER
A
228
66.767
24.881
25.289
1.00
37.61

C


ATOM
 849
C
SER
A
228
66.675
23.846
24.169
1.00
38.35

C


ATOM
 850
O
SER
A
228
67.330
22.805
24.227
1.00
38.93

O


ATOM
 851
CB
SER
A
228
65.927
24.421
26.486
1.00
37.87

C


ATOM
 852
OG
SER
A
228
64.547
24.377
26.159
1.00
39.04

O


ATOM
 853
N
GLN
A
229
65.868
24.135
23.152
1.00
39.18

N


ATOM
 854
CA
GLN
A
229
65.698
23.227
22.021
1.00
39.80

C


ATOM
 855
C
GLN
A
229
66.566
23.622
20.828
1.00
39.23

C


ATOM
 856
O
GLN
A
229
66.348
23.151
19.712
1.00
39.37

O


ATOM
 857
CB
GLN
A
229
64.232
23.192
21.584
1.00
41.24

C


ATOM
 858
CG
GLN
A
229
63.250
22.883
22.703
1.00
43.62

C


ATOM
 859
CD
GLN
A
229
61.819
22.778
22.207
1.00
45.00

C


ATOM
 860
OE1
GLN
A
229
60.871
22.836
22.992
1.00
45.95

O


ATOM
 861
NE2
GLN
A
229
61.656
22.613
20.898
1.00
46.15

N


ATOM
 862
N
LYS
A
230
67.544
24.492
21.065
1.00
38.50

N


ATOM
 863
CA
LYS
A
230
68.451
24.949
20.013
1.00
37.74

C


ATOM
 864
C
LYS
A
230
67.765
25.765
18.920
1.00
36.23

C


ATOM
 865
O
LYS
A
230
68.303
25.921
17.824
1.00
36.06

O


ATOM
 866
CB
LYS
A
230
69.176
23.756
19.376
1.00
39.35

C


ATOM
 867
CG
LYS
A
230
70.046
22.964
20.342
1.00
41.26

C


ATOM
 868
CD
LYS
A
230
71.113
23.843
20.984
1.00
43.12

C


ATOM
 869
CE
LYS
A
230
71.938
23.060
21.997
1.00
44.34

C


ATOM
 870
NZ
LYS
A
230
72.907
23.933
22.723
1.00
45.01

N


ATOM
 871
N
ARG
A
231
66.579
26.283
19.217
1.00
34.84

N


ATOM
 872
CA
ARG
A
231
65.844
27.099
18.257
1.00
34.03

C


ATOM
 873
C
ARG
A
231
66.203
28.565
18.499
1.00
32.95

C


ATOM
 874
O
ARG
A
231
66.289
29.001
19.646
1.00
31.96

O


ATOM
 875
CB
ARG
A
231
64.335
26.910
18.442
1.00
34.65

C


ATOM
 876
CG
ARG
A
231
63.864
25.460
18.369
1.00
35.93

C


ATOM
 877
CD
ARG
A
231
62.362
25.367
18.593
1.00
36.99

C


ATOM
 878
NE
ARG
A
231
61.977
25.904
19.897
1.00
38.07

N


ATOM
 879
CZ
ARG
A
231
60.720
26.085
20.292
1.00
39.08

C


ATOM
 880
NH1
ARG
A
231
59.716
25.774
19.484
1.00
39.24

N


ATOM
 881
NH2
ARG
A
231
60.467
26.582
21.498
1.00
40.03

N


ATOM
 882
N
TYR
A
232
66.414
29.320
17.424
1.00
31.73

N


ATOM
 883
CA
TYR
A
232
66.754
30.733
17.548
1.00
30.36

C


ATOM
 884
C
TYR
A
232
65.701
31.473
18.364
1.00
29.68

C


ATOM
 885
O
TYR
A
232
64.504
31.206
18.237
1.00
28.90

O


ATOM
 886
CB
TYR
A
232
66.843
31.393
16.172
1.00
31.11

C


ATOM
 887
CG
TYR
A
232
67.909
30.824
15.268
1.00
31.38

C


ATOM
 888
CD1
TYR
A
232
69.246
30.798
15.661
1.00
31.61

C


ATOM
 889
CD2
TYR
A
232
67.582
30.320
14.013
1.00
31.87

C


ATOM
 890
CE1
TYR
A
232
70.233
30.279
14.820
1.00
32.53

C


ATOM
 891
CE2
TYR
A
232
68.557
29.801
13.167
1.00
32.60

C


ATOM
 892
CZ
TYR
A
232
69.877
29.784
13.576
1.00
32.81

C


ATOM
 893
OH
TYR
A
232
70.838
29.280
12.730
1.00
34.16

O


ATOM
 894
N
LEU
A
233
66.148
32.401
19.205
1.00
28.53

N


ATOM
 895
CA
LEU
A
233
65.218
33.185
20.003
1.00
28.15

C


ATOM
 896
C
LEU
A
233
64.666
34.306
19.136
1.00
27.30

C


ATOM
 897
O
LEU
A
233
65.333
34.783
18.216
1.00
27.41

O


ATOM
 898
CB
LEU
A
233
65.913
33.801
21.224
1.00
28.49

C


ATOM
 899
CG
LEU
A
233
66.443
32.883
22.328
1.00
29.33

C


ATOM
 900
CD1
LEU
A
233
66.808
33.738
23.535
1.00
29.80

C


ATOM
 901
CD2
LEU
A
233
65.396
31.855
22.724
1.00
28.86

C


ATOM
 902
N
VAL
A
234
63.444
34.725
19.431
1.00
26.70

N


ATOM
 903
CA
VAL
A
234
62.830
35.804
18.684
1.00
26.26

C


ATOM
 904
C
VAL
A
234
61.821
36.512
19.564
1.00
25.94

C


ATOM
 905
O
VAL
A
234
61.172
35.892
20.407
1.00
26.26

O


ATOM
 906
CB
VAL
A
234
62.120
35.288
17.407
1.00
26.74

C


ATOM
 907
CG1
VAL
A
234
60.919
34.429
17.782
1.00
25.97

C


ATOM
 908
CG2
VAL
A
234
61.693
36.466
16.543
1.00
25.98

C


ATOM
 909
N
GLY
A
235
61.711
37.821
19.378
1.00
25.83

N


ATOM
 910
CA
GLY
A
235
60.766
38.599
20.152
1.00
25.73

C


ATOM
 911
C
GLY
A
235
59.698
39.117
19.215
1.00
25.81

C


ATOM
 912
O
GLY
A
235
59.823
38.976
17.999
1.00
26.03

O


ATOM
 913
N
ALA
A
236
58.655
39.724
19.771
1.00
25.58

N


ATOM
 914
CA
ALA
A
236
57.567
40.255
18.962
1.00
24.80

C


ATOM
 915
C
ALA
A
236
56.956
41.480
19.628
1.00
24.47

C


ATOM
 916
O
ALA
A
236
56.724
41.494
20.838
1.00
23.49

O


ATOM
 917
CB
ALA
A
236
56.500
39.183
18.759
1.00
24.63

C


ATOM
 918
N
GLY
A
237
56.694
42.509
18.832
1.00
23.78

N


ATOM
 919
CA
GLY
A
237
56.104
43.711
19.381
1.00
23.62

C


ATOM
 920
C
GLY
A
237
54.597
43.582
19.482
1.00
24.13

C


ATOM
 921
O
GLY
A
237
53.968
42.900
18.671
1.00
23.90

O


ATOM
 922
N
ILE
A
238
54.015
44.210
20.497
1.00
24.19

N


ATOM
 923
CA
ILE
A
238
52.570
44.188
20.654
1.00
24.84

C


ATOM
 924
C
ILE
A
238
52.113
45.610
20.932
1.00
25.64

C


ATOM
 925
O
ILE
A
238
52.931
46.496
21.196
1.00
24.88

O


ATOM
 926
CB
ILE
A
238
52.110
43.274
21.816
1.00
24.90

C


ATOM
 927
CG1
ILE
A
238
52.669
43.782
23.147
1.00
24.94

C


ATOM
 928
CG2
ILE
A
238
52.537
41.841
21.550
1.00
24.38

C


ATOM
 929
CD1
ILE
A
238
52.192
42.969
24.360
1.00
25.52

C


ATOM
 930
N
ASN
A
239
50.807
45.831
20.854
1.00
26.34

N


ATOM
 931
CA
ASN
A
239
50.251
47.147
21.116
1.00
27.12

C


ATOM
 932
C
ASN
A
239
49.239
47.032
22.248
1.00
27.64

C


ATOM
 933
O
ASN
A
239
48.820
45.932
22.610
1.00
27.63

O


ATOM
 934
CB
ASN
A
239
49.598
47.715
19.849
1.00
27.57

C


ATOM
 935
CG
ASN
A
239
48.478
46.841
19.325
1.00
27.88

C


ATOM
 936
OD1
ASN
A
239
47.419
46.731
19.941
1.00
28.35

O


ATOM
 937
ND2
ASN
A
239
48.708
46.211
18.181
1.00
28.71

N


ATOM
 938
N
THR
A
240
48.858
48.172
22.808
1.00
28.33

N


ATOM
 939
CA
THR
A
240
47.916
48.210
23.916
1.00
29.57

C


ATOM
 940
C
THR
A
240
46.456
48.037
23.496
1.00
31.11

C


ATOM
 941
O
THR
A
240
45.553
48.160
24.324
1.00
31.21

O


ATOM
 942
CB
THR
A
240
48.056
49.538
24.686
1.00
29.04

C


ATOM
 943
OG1
THR
A
240
47.813
50.632
23.792
1.00
29.08

O


ATOM
 944
CG2
THR
A
240
49.468
49.678
25.262
1.00
27.94

C


ATOM
 945
N
ARG
A
241
46.217
47.736
22.223
1.00
32.81

N


ATOM
 946
CA
ARG
A
241
44.843
47.584
21.749
1.00
34.67

C


ATOM
 947
C
ARG
A
241
44.326
46.161
21.532
1.00
34.16

C


ATOM
 948
O
ARG
A
241
43.360
45.752
22.174
1.00
34.43

O


ATOM
 949
CB
ARG
A
241
44.635
48.395
20.464
1.00
36.65

C


ATOM
 950
CG
ARG
A
241
43.247
48.215
19.851
1.00
39.95

C


ATOM
 951
CD
ARG
A
241
42.994
49.151
18.671
1.00
42.38

C


ATOM
 952
NE
ARG
A
241
42.483
50.457
19.088
1.00
45.23

N


ATOM
 953
CZ
ARG
A
241
43.212
51.418
19.648
1.00
46.14

C


ATOM
 954
NH1
ARG
A
241
44.509
51.238
19.870
1.00
47.33

N


ATOM
 955
NH2
ARG
A
241
42.642
52.566
19.990
1.00
46.48

N


ATOM
 956
N
ASP
A
242
44.955
45.408
20.636
1.00
33.84

N


ATOM
 957
CA
ASP
A
242
44.493
44.050
20.349
1.00
33.74

C


ATOM
 958
C
ASP
A
242
45.275
42.926
21.026
1.00
33.27

C


ATOM
 959
O
ASP
A
242
45.270
41.796
20.547
1.00
33.34

O


ATOM
 960
CB
ASP
A
242
44.483
43.803
18.830
1.00
33.77

C


ATOM
 961
CG
ASP
A
242
45.874
43.869
18.206
1.00
33.91

C


ATOM
 962
OD1
ASP
A
242
46.869
43.553
18.891
1.00
34.63

O


ATOM
 963
OD2
ASP
A
242
45.975
44.220
17.012
1.00
34.44

O


ATOM
 964
N
PHE
A
243
45.929
43.228
22.143
1.00
33.23

N


ATOM
 965
CA
PHE
A
243
46.725
42.228
22.854
1.00
33.10

C


ATOM
 966
C
PHE
A
243
45.977
40.971
23.305
1.00
33.10

C


ATOM
 967
O
PHE
A
243
46.553
39.883
23.330
1.00
32.90

O


ATOM
 968
CB
PHE
A
243
47.428
42.878
24.056
1.00
32.51

C


ATOM
 969
CG
PHE
A
243
46.494
43.438
25.089
1.00
31.55

C


ATOM
 970
CD1
PHE
A
243
45.956
42.620
26.078
1.00
31.75

C


ATOM
 971
CD2
PHE
A
243
46.155
44.785
25.077
1.00
31.51

C


ATOM
 972
CE1
PHE
A
243
45.095
43.136
27.041
1.00
31.53

C


ATOM
 973
CE2
PHE
A
243
45.293
45.314
26.037
1.00
31.87

C


ATOM
 974
CZ
PHE
A
243
44.763
44.487
27.022
1.00
32.20

C


ATOM
 975
N
ARG
A
244
44.703
41.104
23.660
1.00
33.75

N


ATOM
 976
CA
ARG
A
244
43.937
39.942
24.105
1.00
34.29

C


ATOM
 977
C
ARG
A
244
43.920
38.850
23.042
1.00
34.39

C


ATOM
 978
O
ARG
A
244
43.801
37.666
23.355
1.00
34.22

O


ATOM
 979
CB
ARG
A
244
42.507
40.347
24.478
1.00
34.64

C


ATOM
 980
CG
ARG
A
244
42.444
41.300
25.662
1.00
35.99

C


ATOM
 981
CD
ARG
A
244
41.012
41.616
26.074
1.00
36.99

C


ATOM
 982
NE
ARG
A
244
40.968
42.595
27.157
1.00
37.44

N


ATOM
 983
CZ
ARG
A
244
41.260
43.884
27.012
1.00
38.60

C


ATOM
 984
NH1
ARG
A
244
41.616
44.361
25.825
1.00
38.28

N


ATOM
 985
NH2
ARG
A
244
41.200
44.699
28.058
1.00
39.02

N


ATOM
 986
N
GLU
A
245
44.048
39.247
21.782
1.00
34.77

N


ATOM
 987
CA
GLU
A
245
44.066
38.281
20.693
1.00
35.05

C


ATOM
 988
C
GLU
A
245
45.473
38.075
20.138
1.00
34.00

C


ATOM
 989
O
GLU
A
245
45.853
36.955
19.803
1.00
33.63

O


ATOM
 990
CB
GLU
A
245
43.128
38.725
19.561
1.00
36.92

C


ATOM
 991
CG
GLU
A
245
41.643
38.667
19.921
1.00
40.34

C


ATOM
 992
CD
GLU
A
245
41.188
39.805
20.829
1.00
42.35

C


ATOM
 993
OE1
GLU
A
245
40.089
39.688
21.415
1.00
44.16

O


ATOM
 994
OE2
GLU
A
245
41.912
40.821
20.949
1.00
43.70

O


ATOM
 995
N
ARG
A
246
46.249
39.151
20.051
1.00
32.70

N


ATOM
 996
CA
ARG
A
246
47.605
39.060
19.512
1.00
31.63

C


ATOM
 997
C
ARG
A
246
48.569
38.278
20.403
1.00
31.12

C


ATOM
 998
O
ARG
A
246
49.349
37.467
19.908
1.00
30.59

O


ATOM
 999
CB
ARG
A
246
48.167
40.464
19.251
1.00
31.59

C


ATOM
1000
CG
ARG
A
246
49.547
40.475
18.593
1.00
31.32

C


ATOM
1001
CD
ARG
A
246
50.027
41.901
18.325
1.00
31.90

C


ATOM
1002
NE
ARG
A
246
49.162
42.624
17.392
1.00
32.03

N


ATOM
1003
CZ
ARG
A
246
49.171
42.461
16.072
1.00
31.59

C


ATOM
1004
NH1
ARG
A
246
50.004
41.597
15.506
1.00
31.30

N


ATOM
1005
NH2
ARG
A
246
48.348
43.171
15.315
1.00
32.08

N


ATOM
1006
N
VAL
A
247
48.514
38.511
21.712
1.00
30.54

N


ATOM
1007
CA
VAL
A
247
49.411
37.822
22.638
1.00
30.81

C


ATOM
1008
C
VAL
A
247
49.299
36.296
22.600
1.00
31.06

C


ATOM
1009
O
VAL
A
247
50.304
35.603
22.439
1.00
31.19

O


ATOM
1010
CB
VAL
A
247
49.215
38.339
24.087
1.00
30.61

C


ATOM
1011
CG1
VAL
A
247
49.955
37.460
25.070
1.00
29.27

C


ATOM
1012
CG2
VAL
A
247
49.742
39.772
24.189
1.00
30.03

C


ATOM
1013
N
PRO
A
248
48.080
35.749
22.754
1.00
31.23

N


ATOM
1014
CA
PRO
A
248
47.944
34.289
22.717
1.00
31.12

C


ATOM
1015
C
PRO
A
248
48.504
33.704
21.420
1.00
30.88

C


ATOM
1016
O
PRO
A
248
49.142
32.650
21.421
1.00
30.83

O


ATOM
1017
CB
PRO
A
248
46.434
34.084
22.846
1.00
31.29

C


ATOM
1018
CG
PRO
A
248
46.026
35.237
23.719
1.00
30.86

C


ATOM
1019
CD
PRO
A
248
46.802
36.388
23.118
1.00
30.24

C


ATOM
1020
N
ALA
A
249
48.272
34.402
20.313
1.00
31.01

N


ATOM
1021
CA
ALA
A
249
48.751
33.953
19.012
1.00
30.71

C


ATOM
1022
C
ALA
A
249
50.277
33.926
18.960
1.00
30.92

C


ATOM
1023
O
ALA
A
249
50.871
32.989
18.421
1.00
30.39

O


ATOM
1024
CB
ALA
A
249
48.211
34.859
17.919
1.00
31.05

C


ATOM
1025
N
LEU
A
250
50.909
34.957
19.516
1.00
30.74

N


ATOM
1026
CA
LEU
A
250
52.367
35.035
19.521
1.00
30.84

C


ATOM
1027
C
LEU
A
250
52.952
33.987
20.459
1.00
31.45

C


ATOM
1028
O
LEU
A
250
53.995
33.403
20.172
1.00
31.01

O


ATOM
1029
CB
LEU
A
250
52.827
36.437
19.935
1.00
30.44

C


ATOM
1030
CG
LEU
A
250
52.442
37.553
18.952
1.00
30.49

C


ATOM
1031
CD1
LEU
A
250
52.899
38.901
19.491
1.00
29.78

C


ATOM
1032
CD2
LEU
A
250
53.071
37.279
17.590
1.00
29.75

C


ATOM
1033
N
VAL
A
251
52.275
33.752
21.579
1.00
32.58

N


ATOM
1034
CA
VAL
A
251
52.724
32.755
22.546
1.00
33.79

C


ATOM
1035
C
VAL
A
251
52.683
31.378
21.884
1.00
34.44

C


ATOM
1036
O
VAL
A
251
53.632
30.598
21.987
1.00
34.16

O


ATOM
1037
CB
VAL
A
251
51.818
32.742
23.799
1.00
34.18

C


ATOM
1038
CG1
VAL
A
251
52.183
31.569
24.703
1.00
35.25

C


ATOM
1039
CG2
VAL
A
251
51.965
34.055
24.554
1.00
35.24

C


ATOM
1040
N
GLU
A
252
51.580
31.094
21.196
1.00
34.83

N


ATOM
1041
CA
GLU
A
252
51.411
29.818
20.509
1.00
35.52

C


ATOM
1042
C
GLU
A
252
52.488
29.645
19.442
1.00
34.61

C


ATOM
1043
O
GLU
A
252
53.032
28.557
19.277
1.00
34.77

O


ATOM
1044
CB
GLU
A
252
50.031
29.742
19.845
1.00
37.32

C


ATOM
1045
CG
GLU
A
252
49.752
28.398
19.162
1.00
40.99

C


ATOM
1046
CD
GLU
A
252
48.561
28.429
18.203
1.00
43.11

C


ATOM
1047
OE1
GLU
A
252
48.090
27.335
17.814
1.00
44.94

O


ATOM
1048
OE2
GLU
A
252
48.102
29.532
17.823
1.00
44.42

O


ATOM
1049
N
ALA
A
253
52.784
30.723
18.719
1.00
33.41

N


ATOM
1050
CA
ALA
A
253
53.793
30.691
17.663
1.00
32.41

C


ATOM
1051
C
ALA
A
253
55.198
30.428
18.201
1.00
31.93

C


ATOM
1052
O
ALA
A
253
56.104
30.078
17.441
1.00
31.99

O


ATOM
1053
CB
ALA
A
253
53.773
31.999
16.884
1.00
32.46

C


ATOM
1054
N
GLY
A
254
55.384
30.613
19.504
1.00
30.81

N


ATOM
1055
CA
GLY
A
254
56.684
30.366
20.098
1.00
29.67

C


ATOM
1056
C
GLY
A
254
57.527
31.587
20.431
1.00
28.80

C


ATOM
1057
O
GLY
A
254
58.723
31.452
20.686
1.00
28.19

O


ATOM
1058
N
ALA
A
255
56.929
32.775
20.429
1.00
28.28

N


ATOM
1059
CA
ALA
A
255
57.690
33.984
20.752
1.00
27.64

C


ATOM
1060
C
ALA
A
255
58.349
33.807
22.112
1.00
27.07

C


ATOM
1061
O
ALA
A
255
57.721
33.341
23.059
1.00
27.00

O


ATOM
1062
CB
ALA
A
255
56.776
35.203
20.769
1.00
27.72

C


ATOM
1063
N
ASP
A
256
59.617
34.183
22.205
1.00
26.96

N


ATOM
1064
CA
ASP
A
256
60.368
34.049
23.446
1.00
26.98

C


ATOM
1065
C
ASP
A
256
60.197
35.244
24.380
1.00
26.65

C


ATOM
1066
O
ASP
A
256
60.354
35.124
25.594
1.00
26.61

O


ATOM
1067
CB
ASP
A
256
61.845
33.848
23.117
1.00
27.66

C


ATOM
1068
CG
ASP
A
256
62.085
32.590
22.312
1.00
28.65

C


ATOM
1069
OD1
ASP
A
256
62.063
31.497
22.908
1.00
29.35

O


ATOM
1070
OD2
ASP
A
256
62.275
32.690
21.081
1.00
29.48

O


ATOM
1071
N
VAL
A
257
59.873
36.397
23.808
1.00
25.89

N


ATOM
1072
CA
VAL
A
257
59.683
37.608
24.594
1.00
25.16

C


ATOM
1073
C
VAL
A
257
58.841
38.589
23.786
1.00
24.93

C


ATOM
1074
O
VAL
A
257
58.880
38.581
22.556
1.00
24.52

O


ATOM
1075
CB
VAL
A
257
61.053
38.255
24.950
1.00
25.36

C


ATOM
1076
CG1
VAL
A
257
61.850
38.514
23.684
1.00
26.06

C


ATOM
1077
CG2
VAL
A
257
60.847
39.550
25.725
1.00
24.98

C


ATOM
1078
N
LEU
A
258
58.072
39.415
24.487
1.00
24.27

N


ATOM
1079
CA
LEU
A
258
57.220
40.413
23.851
1.00
24.81

C


ATOM
1080
C
LEU
A
258
57.652
41.801
24.319
1.00
25.12

C


ATOM
1081
O
LEU
A
258
58.377
41.936
25.304
1.00
25.19

O


ATOM
1082
CB
LEU
A
258
55.758
40.200
24.253
1.00
24.78

C


ATOM
1083
CG
LEU
A
258
55.165
38.798
24.097
1.00
25.27

C


ATOM
1084
CD1
LEU
A
258
53.738
38.804
24.625
1.00
26.64

C


ATOM
1085
CD2
LEU
A
258
55.201
38.367
22.636
1.00
25.42

C


ATOM
1086
N
CYS
A
259
57.202
42.829
23.612
1.00
24.79

N


ATOM
1087
CA
CYS
A
259
57.518
44.195
23.999
1.00
25.27

C


ATOM
1088
C
CYS
A
259
56.447
45.139
23.486
1.00
25.48

C


ATOM
1089
O
CYS
A
259
56.146
45.150
22.297
1.00
25.28

O


ATOM
1090
CB
CYS
A
259
58.883
44.628
23.448
1.00
25.05

C


ATOM
1091
SG
CYS
A
259
59.397
46.260
24.055
1.00
24.98

S


ATOM
1092
N
ILE
A
260
55.864
45.920
24.389
1.00
26.39

N


ATOM
1093
CA
ILE
A
260
54.846
46.884
23.996
1.00
27.80

C


ATOM
1094
C
ILE
A
260
55.571
48.017
23.275
1.00
29.01

C


ATOM
1095
O
ILE
A
260
56.492
48.627
23.816
1.00
29.15

O


ATOM
1096
CB
ILE
A
260
54.108
47.462
25.210
1.00
27.85

C


ATOM
1097
CG1
ILE
A
260
53.585
46.325
26.088
1.00
27.74

C


ATOM
1098
CG2
ILE
A
260
52.943
48.340
24.734
1.00
27.65

C


ATOM
1099
CD1
ILE
A
260
52.992
46.796
27.406
1.00
29.12

C


ATOM
1100
N
ASP
A
261
55.136
48.287
22.054
1.00
30.05

N


ATOM
1101
CA
ASP
A
261
55.726
49.307
21.195
1.00
31.69

C


ATOM
1102
C
ASP
A
261
54.914
50.611
21.272
1.00
31.11

C


ATOM
1103
O
ASP
A
261
53.747
50.624
20.901
1.00
31.52

O


ATOM
1104
CB
ASP
A
261
55.760
48.721
19.773
1.00
33.20

C


ATOM
1105
CG
ASP
A
261
56.363
49.653
18.746
1.00
35.95

C


ATOM
1106
OD1
ASP
A
261
57.279
50.427
19.080
1.00
37.14

O


ATOM
1107
OD2
ASP
A
261
55.925
49.586
17.576
1.00
37.53

O


ATOM
1108
N
SER
A
262
55.524
51.692
21.769
1.00
30.51

N


ATOM
1109
CA
SER
A
262
54.829
52.985
21.896
1.00
30.28

C


ATOM
1110
C
SER
A
262
55.742
54.207
22.054
1.00
29.74

C


ATOM
1111
O
SER
A
262
56.801
54.123
22.673
1.00
29.61

O


ATOM
1112
CB
SER
A
262
53.863
52.937
23.087
1.00
31.07

C


ATOM
1113
OG
SER
A
262
53.352
54.226
23.389
1.00
31.39

O


ATOM
1114
N
SER
A
263
55.313
55.350
21.515
1.00
29.06

N


ATOM
1115
CA
SER
A
263
56.093
56.585
21.608
1.00
28.10

C


ATOM
1116
C
SER
A
263
56.027
57.203
23.005
1.00
27.79

C


ATOM
1117
O
SER
A
263
56.822
58.079
23.345
1.00
28.25

O


ATOM
1118
CB
SER
A
263
55.611
57.615
20.574
1.00
28.95

C


ATOM
1119
OG
SER
A
263
54.300
58.073
20.857
1.00
29.45

O


ATOM
1120
N
ASP
A
264
55.073
56.749
23.809
1.00
26.48

N


ATOM
1121
CA
ASP
A
264
54.923
57.245
25.173
1.00
25.78

C


ATOM
1122
C
ASP
A
264
54.400
56.107
26.043
1.00
25.45

C


ATOM
1123
O
ASP
A
264
53.191
55.891
26.144
1.00
25.07

O


ATOM
1124
CB
ASP
A
264
53.959
58.440
25.202
1.00
25.30

C


ATOM
1125
CG
ASP
A
264
53.616
58.900
26.619
1.00
24.43

C


ATOM
1126
OD1
ASP
A
264
54.333
58.559
27.586
1.00
23.75

O


ATOM
1127
OD2
ASP
A
264
52.618
59.629
26.760
1.00
24.33

O


ATOM
1128
N
GLY
A
265
55.331
55.378
26.652
1.00
24.58

N


ATOM
1129
CA
GLY
A
265
54.985
54.253
27.500
1.00
24.14

C


ATOM
1130
C
GLY
A
265
54.505
54.603
28.896
1.00
24.38

C


ATOM
1131
O
GLY
A
265
54.105
53.718
29.655
1.00
23.84

O


ATOM
1132
N
PHE
A
266
54.554
55.884
29.250
1.00
24.38

N


ATOM
1133
CA
PHE
A
266
54.095
56.321
30.562
1.00
24.40

C


ATOM
1134
C
PHE
A
266
52.584
56.429
30.382
1.00
24.85

C


ATOM
1135
O
PHE
A
266
52.035
57.523
30.275
1.00
23.66

O


ATOM
1136
CB
PHE
A
266
54.700
57.685
30.902
1.00
24.77

C


ATOM
1137
CG
PHE
A
266
54.758
57.987
32.383
1.00
25.09

C


ATOM
1138
CD1
PHE
A
266
54.030
57.233
33.302
1.00
24.80

C


ATOM
1139
CD2
PHE
A
266
55.530
59.047
32.851
1.00
24.88

C


ATOM
1140
CE1
PHE
A
266
54.071
57.533
34.665
1.00
25.40

C


ATOM
1141
CE2
PHE
A
266
55.580
59.360
34.210
1.00
24.97

C


ATOM
1142
CZ
PHE
A
266
54.849
58.601
35.121
1.00
25.68

C


ATOM
1143
N
SER
A
267
51.924
55.274
30.348
1.00
25.48

N


ATOM
1144
CA
SER
A
267
50.486
55.203
30.112
1.00
26.23

C


ATOM
1145
C
SER
A
267
49.777
54.078
30.855
1.00
26.64

C


ATOM
1146
O
SER
A
267
50.306
52.971
30.983
1.00
25.99

O


ATOM
1147
CB
SER
A
267
50.241
55.016
28.616
1.00
26.26

C


ATOM
1148
OG
SER
A
267
48.898
54.647
28.356
1.00
28.51

O


ATOM
1149
N
GLU
A
268
48.567
54.363
31.321
1.00
27.32

N


ATOM
1150
CA
GLU
A
268
47.776
53.363
32.021
1.00
28.41

C


ATOM
1151
C
GLU
A
268
47.486
52.195
31.089
1.00
28.35

C


ATOM
1152
O
GLU
A
268
47.276
51.070
31.544
1.00
27.34

O


ATOM
1153
CB
GLU
A
268
46.454
53.964
32.513
1.00
30.40

C


ATOM
1154
CG
GLU
A
268
46.594
54.834
33.754
1.00
33.77

C


ATOM
1155
CD
GLU
A
268
45.255
55.298
34.320
1.00
35.87

C


ATOM
1156
OE1
GLU
A
268
45.246
55.792
35.471
1.00
37.72

O


ATOM
1157
OE2
GLU
A
268
44.221
55.177
33.623
1.00
35.03

O


ATOM
1158
N
TRP
A
269
47.471
52.464
29.785
1.00
28.35

N


ATOM
1159
CA
TRP
A
269
47.204
51.417
28.806
1.00
29.40

C


ATOM
1160
C
TRP
A
269
48.275
50.332
28.857
1.00
29.06

C


ATOM
1161
O
TRP
A
269
47.976
49.154
28.653
1.00
29.12

O


ATOM
1162
CB
TRP
A
269
47.121
51.995
27.388
1.00
30.30

C


ATOM
1163
CG
TRP
A
269
45.916
52.861
27.150
1.00
32.00

C


ATOM
1164
CD1
TRP
A
269
45.908
54.202
26.892
1.00
32.39

C


ATOM
1165
CD2
TRP
A
269
44.543
52.443
27.146
1.00
32.75

C


ATOM
1166
NE1
TRP
A
269
44.617
54.644
26.727
1.00
33.20

N


ATOM
1167
CE2
TRP
A
269
43.760
53.586
26.877
1.00
33.15

C


ATOM
1168
CE3
TRP
A
269
43.899
51.212
27.343
1.00
33.57

C


ATOM
1169
CZ2
TRP
A
269
42.363
53.539
26.798
1.00
33.93

C


ATOM
1170
CZ3
TRP
A
269
42.507
51.164
27.266
1.00
34.42

C


ATOM
1171
CH2
TRP
A
269
41.757
52.323
26.994
1.00
34.51

C


ATOM
1172
N
GLN
A
270
49.519
50.726
29.122
1.00
28.51

N


ATOM
1173
CA
GLN
A
270
50.610
49.755
29.209
1.00
28.61

C


ATOM
1174
C
GLN
A
270
50.460
48.941
30.490
1.00
28.10

C


ATOM
1175
O
GLN
A
270
50.699
47.736
30.499
1.00
28.60

O


ATOM
1176
CB
GLN
A
270
51.977
50.457
29.205
1.00
28.36

C


ATOM
1177
CG
GLN
A
270
52.238
51.315
27.977
1.00
28.23

C


ATOM
1178
CD
GLN
A
270
53.519
50.943
27.244
1.00
28.01

C


ATOM
1179
OE1
GLN
A
270
54.445
50.374
27.825
1.00
27.19

O


ATOM
1180
NE2
GLN
A
270
53.581
51.282
25.963
1.00
26.48

N


ATOM
1181
N
LYS
A
271
50.072
49.604
31.575
1.00
28.37

N


ATOM
1182
CA
LYS
A
271
49.878
48.915
32.846
1.00
28.70

C


ATOM
1183
C
LYS
A
271
48.784
47.858
32.671
1.00
27.88

C


ATOM
1184
O
LYS
A
271
48.917
46.734
33.144
1.00
27.93

O


ATOM
1185
CB
LYS
A
271
49.476
49.912
33.941
1.00
29.92

C


ATOM
1186
CG
LYS
A
271
49.092
49.260
35.266
1.00
32.48

C


ATOM
1187
CD
LYS
A
271
48.701
50.309
36.300
1.00
34.72

C


ATOM
1188
CE
LYS
A
271
48.207
49.671
37.590
1.00
36.23

C


ATOM
1189
NZ
LYS
A
271
49.269
48.881
38.274
1.00
38.61

N


ATOM
1190
N
ILE
A
272
47.712
48.231
31.979
1.00
27.39

N


ATOM
1191
CA
ILE
A
272
46.592
47.326
31.726
1.00
27.48

C


ATOM
1192
C
ILE
A
272
47.036
46.124
30.902
1.00
26.99

C


ATOM
1193
O
ILE
A
272
46.668
44.989
31.195
1.00
27.02

O


ATOM
1194
CB
ILE
A
272
45.447
48.057
30.978
1.00
27.22

C


ATOM
1195
CG1
ILE
A
272
44.786
49.064
31.922
1.00
27.67

C


ATOM
1196
CG2
ILE
A
272
44.422
47.046
30.447
1.00
27.76

C


ATOM
1197
CD1
ILE
A
272
43.836
50.030
31.231
1.00
27.85

C


ATOM
1198
N
THR
A
273
47.831
46.377
29.868
1.00
26.65

N


ATOM
1199
CA
THR
A
273
48.322
45.306
29.010
1.00
26.53

C


ATOM
1200
C
THR
A
273
49.202
44.331
29.792
1.00
26.14

C


ATOM
1201
O
THR
A
273
49.041
43.114
29.694
1.00
25.79

O


ATOM
1202
CB
THR
A
273
49.120
45.878
27.824
1.00
26.74

C


ATOM
1203
OG1
THR
A
273
48.270
46.744
27.059
1.00
27.53

O


ATOM
1204
CG2
THR
A
273
49.626
44.752
26.928
1.00
27.26

C


ATOM
1205
N
ILE
A
274
50.134
44.863
30.571
1.00
26.20

N


ATOM
1206
CA
ILE
A
274
51.010
44.003
31.357
1.00
26.20

C


ATOM
1207
C
ILE
A
274
50.175
43.230
32.377
1.00
26.66

C


ATOM
1208
O
ILE
A
274
50.411
42.045
32.616
1.00
26.11

O


ATOM
1209
CB
ILE
A
274
52.080
44.821
32.096
1.00
25.86

C


ATOM
1210
CG1
ILE
A
274
52.942
45.581
31.082
1.00
26.16

C


ATOM
1211
CG2
ILE
A
274
52.950
43.895
32.945
1.00
25.61

C


ATOM
1212
CD1
ILE
A
274
53.895
46.583
31.715
1.00
27.00

C


ATOM
1213
N
GLY
A
275
49.194
43.908
32.966
1.00
26.98

N


ATOM
1214
CA
GLY
A
275
48.335
43.266
33.949
1.00
28.29

C


ATOM
1215
C
GLY
A
275
47.599
42.064
33.382
1.00
28.55

C


ATOM
1216
O
GLY
A
275
47.537
41.009
34.015
1.00
28.98

O


ATOM
1217
N
TRP
A
276
47.041
42.222
32.187
1.00
28.87

N


ATOM
1218
CA
TRP
A
276
46.312
41.145
31.526
1.00
28.90

C


ATOM
1219
C
TRP
A
276
47.246
39.963
31.270
1.00
29.40

C


ATOM
1220
O
TRP
A
276
46.864
38.802
31.453
1.00
29.24

O


ATOM
1221
CB
TRP
A
276
45.735
41.633
30.197
1.00
29.68

C


ATOM
1222
CG
TRP
A
276
44.847
40.631
29.531
1.00
30.48

C


ATOM
1223
CD1
TRP
A
276
43.513
40.429
29.766
1.00
30.71

C


ATOM
1224
CD2
TRP
A
276
45.230
39.673
28.539
1.00
30.72

C


ATOM
1225
NE1
TRP
A
276
43.043
39.405
28.977
1.00
30.48

N


ATOM
1226
CE2
TRP
A
276
44.075
38.922
28.214
1.00
31.35

C


ATOM
1227
CE3
TRP
A
276
46.437
39.373
27.891
1.00
31.18

C


ATOM
1228
CZ2
TRP
A
276
44.092
37.890
27.268
1.00
31.27

C


ATOM
1229
CZ3
TRP
A
276
46.455
38.344
26.951
1.00
31.86

C


ATOM
1230
CH2
TRP
A
276
45.287
37.616
26.649
1.00
31.77

C


ATOM
1231
N
ILE
A
277
48.472
40.256
30.844
1.00
28.84

N


ATOM
1232
CA
ILE
A
277
49.440
39.197
30.585
1.00
28.97

C


ATOM
1233
C
ILE
A
277
49.774
38.442
31.878
1.00
29.36

C


ATOM
1234
O
ILE
A
277
49.822
37.213
31.886
1.00
28.83

O


ATOM
1235
CB
ILE
A
277
50.740
39.765
29.950
1.00
28.28

C


ATOM
1236
CG1
ILE
A
277
50.442
40.296
28.542
1.00
28.37

C


ATOM
1237
CG2
ILE
A
277
51.802
38.678
29.867
1.00
28.02

C


ATOM
1238
CD1
ILE
A
277
51.604
41.054
27.890
1.00
27.79

C


ATOM
1239
N
ARG
A
278
49.988
39.174
32.969
1.00
30.21

N


ATOM
1240
CA
ARG
A
278
50.312
38.551
34.254
1.00
31.53

C


ATOM
1241
C
ARG
A
278
49.173
37.683
34.776
1.00
33.21

C


ATOM
1242
O
ARG
A
278
49.400
36.609
35.334
1.00
33.46

O


ATOM
1243
CB
ARG
A
278
50.643
39.616
35.304
1.00
30.82

C


ATOM
1244
CG
ARG
A
278
51.957
40.335
35.071
1.00
30.23

C


ATOM
1245
CD
ARG
A
278
53.143
39.393
35.206
1.00
29.99

C


ATOM
1246
NE
ARG
A
278
54.382
40.066
34.832
1.00
28.97

N


ATOM
1247
CZ
ARG
A
278
55.148
39.711
33.806
1.00
28.64

C


ATOM
1248
NH1
ARG
A
278
54.812
38.677
33.044
1.00
26.58

N


ATOM
1249
NH2
ARG
A
278
56.243
40.409
33.530
1.00
27.89

N


ATOM
1250
N
GLU
A
279
47.949
38.168
34.597
1.00
34.74

N


ATOM
1251
CA
GLU
A
279
46.754
37.466
35.043
1.00
36.51

C


ATOM
1252
C
GLU
A
279
46.553
36.166
34.268
1.00
36.74

C


ATOM
1253
O
GLU
A
279
46.101
35.162
34.819
1.00
36.85

O


ATOM
1254
CB
GLU
A
279
45.541
38.384
34.859
1.00
38.13

C


ATOM
1255
CG
GLU
A
279
44.204
37.819
35.314
1.00
41.43

C


ATOM
1256
CD
GLU
A
279
43.065
38.828
35.182
1.00
43.32

C


ATOM
1257
OE1
GLU
A
279
41.902
38.449
35.442
1.00
44.56

O


ATOM
1258
OE2
GLU
A
279
43.327
40.002
34.823
1.00
44.56

O


ATOM
1259
N
LYS
A
280
46.915
36.183
32.991
1.00
36.37

N


ATOM
1260
CA
LYS
A
280
46.742
35.019
32.133
1.00
36.81

C


ATOM
1261
C
LYS
A
280
47.941
34.071
32.107
1.00
36.04

C


ATOM
1262
O
LYS
A
280
47.773
32.854
32.038
1.00
35.58

O


ATOM
1263
CB
LYS
A
280
46.433
35.495
30.710
1.00
38.33

C


ATOM
1264
CG
LYS
A
280
45.519
34.591
29.895
1.00
40.96

C


ATOM
1265
CD
LYS
A
280
46.185
33.281
29.512
1.00
42.35

C


ATOM
1266
CE
LYS
A
280
45.280
32.456
28.601
1.00
42.90

C


ATOM
1267
NZ
LYS
A
280
44.954
33.184
27.341
1.00
42.89

N


ATOM
1268
N
TYR
A
281
49.146
34.627
32.185
1.00
34.52

N


ATOM
1269
CA
TYR
A
281
50.362
33.826
32.100
1.00
33.39

C


ATOM
1270
C
TYR
A
281
51.328
33.919
33.274
1.00
33.09

C


ATOM
1271
O
TYR
A
281
52.334
33.214
33.297
1.00
33.09

O


ATOM
1272
CB
TYR
A
281
51.124
34.209
30.834
1.00
32.75

C


ATOM
1273
CG
TYR
A
281
50.356
34.016
29.549
1.00
32.31

C


ATOM
1274
CD1
TYR
A
281
50.221
32.752
28.976
1.00
32.30

C


ATOM
1275
CD2
TYR
A
281
49.785
35.103
28.889
1.00
32.48

C


ATOM
1276
CE1
TYR
A
281
49.541
32.577
27.774
1.00
32.47

C


ATOM
1277
CE2
TYR
A
281
49.104
34.939
27.691
1.00
32.55

C


ATOM
1278
CZ
TYR
A
281
48.987
33.674
27.138
1.00
32.49

C


ATOM
1279
OH
TYR
A
281
48.328
33.512
25.941
1.00
33.37

O


ATOM
1280
N
GLY
A
282
51.043
34.780
34.240
1.00
32.83

N


ATOM
1281
CA
GLY
A
282
51.961
34.919
35.355
1.00
32.77

C


ATOM
1282
C
GLY
A
282
53.284
35.449
34.826
1.00
33.10

C


ATOM
1283
O
GLY
A
282
53.305
36.220
33.863
1.00
32.17

O


ATOM
1284
N
ASP
A
283
54.391
35.041
35.436
1.00
33.13

N


ATOM
1285
CA
ASP
A
283
55.699
35.501
34.986
1.00
33.88

C


ATOM
1286
C
ASP
A
283
56.322
34.574
33.945
1.00
33.49

C


ATOM
1287
O
ASP
A
283
57.519
34.647
33.674
1.00
34.01

O


ATOM
1288
CB
ASP
A
283
56.637
35.665
36.184
1.00
34.83

C


ATOM
1289
CG
ASP
A
283
56.242
36.833
37.072
1.00
36.88

C


ATOM
1290
OD1
ASP
A
283
56.206
37.978
36.569
1.00
38.24

O


ATOM
1291
OD2
ASP
A
283
55.965
36.615
38.270
1.00
38.21

O


ATOM
1292
N
LYS
A
284
55.504
33.711
33.352
1.00
33.24

N


ATOM
1293
CA
LYS
A
284
55.985
32.773
32.342
1.00
33.02

C


ATOM
1294
C
LYS
A
284
56.118
33.426
30.968
1.00
32.02

C


ATOM
1295
O
LYS
A
284
56.838
32.931
30.105
1.00
32.97

O


ATOM
1296
CB
LYS
A
284
55.058
31.551
32.275
1.00
34.39

C


ATOM
1297
CG
LYS
A
284
55.260
30.568
33.433
1.00
36.82

C


ATOM
1298
CD
LYS
A
284
55.284
31.281
34.783
1.00
38.42

C


ATOM
1299
CE
LYS
A
284
55.742
30.359
35.910
1.00
39.93

C


ATOM
1300
NZ
LYS
A
284
56.028
31.120
37.168
1.00
39.68

N


ATOM
1301
N
VAL
A
285
55.410
34.530
30.761
1.00
29.89

N


ATOM
1302
CA
VAL
A
285
55.510
35.259
29.502
1.00
28.50

C


ATOM
1303
C
VAL
A
285
56.233
36.566
29.813
1.00
27.10

C


ATOM
1304
O
VAL
A
285
55.816
37.326
30.691
1.00
27.10

O


ATOM
1305
CB
VAL
A
285
54.122
35.559
28.895
1.00
28.58

C


ATOM
1306
CG1
VAL
A
285
54.259
36.563
27.748
1.00
27.74

C


ATOM
1307
CG2
VAL
A
285
53.502
34.264
28.375
1.00
28.28

C


ATOM
1308
N
LYS
A
286
57.327
36.815
29.101
1.00
25.90

N


ATOM
1309
CA
LYS
A
286
58.125
38.014
29.317
1.00
24.52

C


ATOM
1310
C
LYS
A
286
57.671
39.148
28.410
1.00
24.47

C


ATOM
1311
O
LYS
A
286
57.419
38.944
27.222
1.00
24.28

O


ATOM
1312
CB
LYS
A
286
59.601
37.697
29.076
1.00
25.16

C


ATOM
1313
CG
LYS
A
286
60.112
36.510
29.893
1.00
24.27

C


ATOM
1314
CD
LYS
A
286
59.926
36.746
31.388
1.00
24.81

C


ATOM
1315
CE
LYS
A
286
60.396
35.544
32.204
1.00
25.83

C


ATOM
1316
NZ
LYS
A
286
60.194
35.749
33.670
1.00
24.86

N


ATOM
1317
N
VAL
A
287
57.574
40.347
28.972
1.00
24.27

N


ATOM
1318
CA
VAL
A
287
57.120
41.495
28.202
1.00
24.13

C


ATOM
1319
C
VAL
A
287
57.779
42.813
28.597
1.00
23.84

C


ATOM
1320
O
VAL
A
287
57.687
43.255
29.743
1.00
23.87

O


ATOM
1321
CB
VAL
A
287
55.573
41.644
28.308
1.00
24.31

C


ATOM
1322
CG1
VAL
A
287
55.146
41.662
29.769
1.00
25.02

C


ATOM
1323
CG2
VAL
A
287
55.114
42.923
27.609
1.00
24.49

C


ATOM
1324
N
GLY
A
288
58.456
43.428
27.634
1.00
23.20

N


ATOM
1325
CA
GLY
A
288
59.097
44.707
27.882
1.00
22.85

C


ATOM
1326
C
GLY
A
288
58.077
45.801
27.643
1.00
22.44

C


ATOM
1327
O
GLY
A
288
57.018
45.548
27.063
1.00
22.27

O


ATOM
1328
N
ALA
A
289
58.383
47.014
28.088
1.00
22.59

N


ATOM
1329
CA
ALA
A
289
57.468
48.139
27.922
1.00
23.01

C


ATOM
1330
C
ALA
A
289
58.248
49.422
27.682
1.00
23.15

C


ATOM
1331
O
ALA
A
289
59.438
49.498
27.976
1.00
23.72

O


ATOM
1332
CB
ALA
A
289
56.573
48.287
29.168
1.00
23.19

C


ATOM
1333
N
GLY
A
290
57.565
50.427
27.144
1.00
23.69

N


ATOM
1334
CA
GLY
A
290
58.205
51.698
26.856
1.00
23.22

C


ATOM
1335
C
GLY
A
290
57.432
52.435
25.775
1.00
23.29

C


ATOM
1336
O
GLY
A
290
56.397
51.945
25.320
1.00
22.89

O


ATOM
1337
N
ASN
A
291
57.937
53.582
25.324
1.00
22.88

N


ATOM
1338
CA
ASN
A
291
59.199
54.155
25.787
1.00
22.55

C


ATOM
1339
C
ASN
A
291
59.028
55.263
26.817
1.00
22.60

C


ATOM
1340
O
ASN
A
291
58.024
55.974
26.817
1.00
22.43

O


ATOM
1341
CB
ASN
A
291
59.977
54.727
24.592
1.00
22.24

C


ATOM
1342
CG
ASN
A
291
60.565
53.651
23.708
1.00
22.60

C


ATOM
1343
OD1
ASN
A
291
60.148
52.493
23.758
1.00
21.74

O


ATOM
1344
ND2
ASN
A
291
61.538
54.029
22.884
1.00
21.50

N


ATOM
1345
N
ILE
A
292
60.028
55.404
27.685
1.00
22.32

N


ATOM
1346
CA
ILE
A
292
60.031
56.448
28.702
1.00
22.58

C


ATOM
1347
C
ILE
A
292
61.391
57.144
28.669
1.00
22.53

C


ATOM
1348
O
ILE
A
292
62.327
56.651
28.033
1.00
22.76

O


ATOM
1349
CB
ILE
A
292
59.722
55.879
30.123
1.00
22.99

C


ATOM
1350
CG1
ILE
A
292
60.591
54.655
30.437
1.00
22.90

C


ATOM
1351
CG2
ILE
A
292
58.243
55.506
30.208
1.00
23.43

C


ATOM
1352
CD1
ILE
A
292
62.040
54.972
30.767
1.00
23.93

C


ATOM
1353
N
VAL
A
293
61.502
58.296
29.322
1.00
22.08

N


ATOM
1354
CA
VAL
A
293
62.765
59.028
29.320
1.00
22.29

C


ATOM
1355
C
VAL
A
293
63.201
59.555
30.678
1.00
22.70

C


ATOM
1356
O
VAL
A
293
64.187
60.282
30.766
1.00
22.85

O


ATOM
1357
CB
VAL
A
293
62.720
60.228
28.346
1.00
22.95

C


ATOM
1358
CG1
VAL
A
293
62.595
59.730
26.906
1.00
22.15

C


ATOM
1359
CG2
VAL
A
293
61.550
61.148
28.706
1.00
22.40

C


ATOM
1360
N
ASP
A
294
62.474
59.209
31.736
1.00
22.82

N


ATOM
1361
CA
ASP
A
294
62.851
59.680
33.060
1.00
23.34

C


ATOM
1362
C
ASP
A
294
62.532
58.660
34.145
1.00
23.54

C


ATOM
1363
O
ASP
A
294
61.897
57.634
33.880
1.00
23.02

O


ATOM
1364
CB
ASP
A
294
62.181
61.040
33.365
1.00
23.61

C


ATOM
1365
CG
ASP
A
294
60.680
60.934
33.635
1.00
24.61

C


ATOM
1366
OD1
ASP
A
294
60.057
59.898
33.323
1.00
25.36

O


ATOM
1367
OD2
ASP
A
294
60.115
61.921
34.158
1.00
24.53

O


ATOM
1368
N
GLY
A
295
62.991
58.943
35.359
1.00
23.57

N


ATOM
1369
CA
GLY
A
295
62.762
58.043
36.474
1.00
24.71

C


ATOM
1370
C
GLY
A
295
61.300
57.752
36.756
1.00
24.99

C


ATOM
1371
O
GLY
A
295
60.943
56.611
37.038
1.00
24.55

O


ATOM
1372
N
GLU
A
296
60.455
58.777
36.692
1.00
25.66

N


ATOM
1373
CA
GLU
A
296
59.022
58.603
36.943
1.00
26.31

C


ATOM
1374
C
GLU
A
296
58.413
57.575
36.001
1.00
25.52

C


ATOM
1375
O
GLU
A
296
57.635
56.715
36.421
1.00
24.66

O


ATOM
1376
CB
GLU
A
296
58.269
59.924
36.759
1.00
28.85

C


ATOM
1377
CG
GLU
A
296
58.342
60.889
37.927
1.00
33.07

C


ATOM
1378
CD
GLU
A
296
57.642
62.208
37.621
1.00
36.15

C


ATOM
1379
OE1
GLU
A
296
56.485
62.181
37.130
1.00
37.36

O


ATOM
1380
OE2
GLU
A
296
58.250
63.272
37.871
1.00
38.01

O


ATOM
1381
N
GLY
A
297
58.750
57.687
34.721
1.00
25.01

N


ATOM
1382
CA
GLY
A
297
58.227
56.761
33.733
1.00
24.76

C


ATOM
1383
C
GLY
A
297
58.735
55.353
33.981
1.00
24.56

C


ATOM
1384
O
GLY
A
297
57.976
54.384
33.891
1.00
24.54

O


ATOM
1385
N
PHE
A
298
60.026
55.238
34.279
1.00
23.53

N


ATOM
1386
CA
PHE
A
298
60.628
53.938
34.559
1.00
23.73

C


ATOM
1387
C
PHE
A
298
59.904
53.288
35.737
1.00
23.95

C


ATOM
1388
O
PHE
A
298
59.470
52.140
35.659
1.00
23.92

O


ATOM
1389
CB
PHE
A
298
62.107
54.091
34.926
1.00
22.70

C


ATOM
1390
CG
PHE
A
298
62.710
52.844
35.510
1.00
22.74

C


ATOM
1391
CD1
PHE
A
298
63.206
51.841
34.685
1.00
22.49

C


ATOM
1392
CD2
PHE
A
298
62.702
52.636
36.885
1.00
22.82

C


ATOM
1393
CE1
PHE
A
298
63.680
50.645
35.223
1.00
22.80

C


ATOM
1394
CE2
PHE
A
298
63.171
51.447
37.433
1.00
22.71

C


ATOM
1395
CZ
PHE
A
298
63.659
50.448
36.599
1.00
22.47

C


ATOM
1396
N
ARG
A
299
59.800
54.043
36.829
1.00
24.49

N


ATOM
1397
CA
ARG
A
299
59.158
53.588
38.062
1.00
25.88

C


ATOM
1398
C
ARG
A
299
57.736
53.090
37.833
1.00
25.06

C


ATOM
1399
O
ARG
A
299
57.323
52.074
38.402
1.00
24.51

O


ATOM
1400
CB
ARG
A
299
59.154
54.735
39.080
1.00
28.63

C


ATOM
1401
CG
ARG
A
299
58.300
54.510
40.313
1.00
32.44

C


ATOM
1402
CD
ARG
A
299
59.044
53.764
41.400
1.00
35.12

C


ATOM
1403
NE
ARG
A
299
60.302
54.414
41.772
1.00
37.30

N


ATOM
1404
CZ
ARG
A
299
61.032
54.061
42.827
1.00
37.36

C


ATOM
1405
NH1
ARG
A
299
60.620
53.077
43.614
1.00
37.31

N


ATOM
1406
NH2
ARG
A
299
62.186
54.665
43.079
1.00
37.90

N


ATOM
1407
N
TYR
A
300
56.987
53.804
36.998
1.00
23.80

N


ATOM
1408
CA
TYR
A
300
55.615
53.413
36.717
1.00
23.18

C


ATOM
1409
C
TYR
A
300
55.549
52.050
36.022
1.00
22.98

C


ATOM
1410
O
TYR
A
300
54.760
51.189
36.405
1.00
22.25

O


ATOM
1411
CB
TYR
A
300
54.929
54.460
35.837
1.00
23.21

C


ATOM
1412
CG
TYR
A
300
53.474
54.153
35.573
1.00
23.56

C


ATOM
1413
CD1
TYR
A
300
52.505
54.362
36.560
1.00
24.05

C


ATOM
1414
CD2
TYR
A
300
53.066
53.632
34.349
1.00
23.81

C


ATOM
1415
CE1
TYR
A
300
51.164
54.059
36.325
1.00
24.38

C


ATOM
1416
CE2
TYR
A
300
51.734
53.325
34.105
1.00
24.00

C


ATOM
1417
CZ
TYR
A
300
50.790
53.540
35.094
1.00
23.95

C


ATOM
1418
OH
TYR
A
300
49.474
53.239
34.845
1.00
24.48

O


ATOM
1419
N
LEU
A
301
56.372
51.857
34.996
1.00
21.97

N


ATOM
1420
CA
LEU
A
301
56.366
50.592
34.274
1.00
22.14

C


ATOM
1421
C
LEU
A
301
56.991
49.463
35.102
1.00
22.14

C


ATOM
1422
O
LEU
A
301
56.625
48.298
34.947
1.00
22.36

O


ATOM
1423
CB
LEU
A
301
57.081
50.741
32.920
1.00
21.32

C


ATOM
1424
CG
LEU
A
301
56.381
51.668
31.909
1.00
21.51

C


ATOM
1425
CD1
LEU
A
301
57.204
51.757
30.618
1.00
21.05

C


ATOM
1426
CD2
LEU
A
301
54.972
51.136
31.607
1.00
21.05

C


ATOM
1427
N
ALA
A
302
57.925
49.808
35.984
1.00
22.39

N


ATOM
1428
CA
ALA
A
302
58.559
48.799
36.833
1.00
23.49

C


ATOM
1429
C
ALA
A
302
57.500
48.240
37.790
1.00
24.06

C


ATOM
1430
O
ALA
A
302
57.357
47.022
37.937
1.00
23.67

O


ATOM
1431
CB
ALA
A
302
59.708
49.415
37.625
1.00
22.59

C


ATOM
1432
N
ASP
A
303
56.760
49.138
38.432
1.00
24.53

N


ATOM
1433
CA
ASP
A
303
55.709
48.734
39.360
1.00
26.12

C


ATOM
1434
C
ASP
A
303
54.589
48.010
38.614
1.00
26.16

C


ATOM
1435
O
ASP
A
303
53.891
47.179
39.194
1.00
26.12

O


ATOM
1436
CB
ASP
A
303
55.121
49.948
40.094
1.00
27.14

C


ATOM
1437
CG
ASP
A
303
56.086
50.560
41.103
1.00
28.94

C


ATOM
1438
OD1
ASP
A
303
56.998
49.856
41.586
1.00
30.42

O


ATOM
1439
OD2
ASP
A
303
55.916
51.751
41.432
1.00
30.69

O


ATOM
1440
N
ALA
A
304
54.416
48.333
37.332
1.00
25.47

N


ATOM
1441
CA
ALA
A
304
53.386
47.695
36.517
1.00
25.15

C


ATOM
1442
C
ALA
A
304
53.755
46.246
36.196
1.00
25.19

C


ATOM
1443
O
ALA
A
304
52.895
45.451
35.811
1.00
24.86

O


ATOM
1444
CB
ALA
A
304
53.172
48.472
35.233
1.00
24.93

C


ATOM
1445
N
GLY
A
305
55.035
45.909
36.337
1.00
24.65

N


ATOM
1446
CA
GLY
A
305
55.461
44.540
36.086
1.00
24.64

C


ATOM
1447
C
GLY
A
305
56.306
44.266
34.851
1.00
24.36

C


ATOM
1448
O
GLY
A
305
56.597
43.107
34.547
1.00
24.74

O


ATOM
1449
N
ALA
A
306
56.711
45.311
34.140
1.00
23.62

N


ATOM
1450
CA
ALA
A
306
57.521
45.136
32.935
1.00
23.66

C


ATOM
1451
C
ALA
A
306
58.803
44.351
33.214
1.00
23.20

C


ATOM
1452
O
ALA
A
306
59.430
44.532
34.256
1.00
23.66

O


ATOM
1453
CB
ALA
A
306
57.866
46.499
32.336
1.00
22.87

C


ATOM
1454
N
ASP
A
307
59.188
43.490
32.274
1.00
23.16

N


ATOM
1455
CA
ASP
A
307
60.398
42.679
32.406
1.00
22.69

C


ATOM
1456
C
ASP
A
307
61.659
43.439
31.998
1.00
22.59

C


ATOM
1457
O
ASP
A
307
62.764
43.098
32.415
1.00
22.56

O


ATOM
1458
CB
ASP
A
307
60.243
41.391
31.601
1.00
23.45

C


ATOM
1459
CG
ASP
A
307
59.292
40.424
32.267
1.00
23.60

C


ATOM
1460
OD1
ASP
A
307
59.626
39.963
33.375
1.00
24.19

O


ATOM
1461
OD2
ASP
A
307
58.217
40.144
31.705
1.00
23.04

O


ATOM
1462
N
PHE
A
308
61.482
44.453
31.159
1.00
22.02

N


ATOM
1463
CA
PHE
A
308
62.571
45.334
30.756
1.00
21.84

C


ATOM
1464
C
PHE
A
308
61.903
46.608
30.264
1.00
21.93

C


ATOM
1465
O
PHE
A
308
60.755
46.587
29.809
1.00
20.69

O


ATOM
1466
CB
PHE
A
308
63.505
44.695
29.700
1.00
21.68

C


ATOM
1467
CG
PHE
A
308
62.928
44.596
28.312
1.00
22.97

C


ATOM
1468
CD1
PHE
A
308
62.892
45.707
27.470
1.00
23.01

C


ATOM
1469
CD2
PHE
A
308
62.487
43.369
27.820
1.00
22.89

C


ATOM
1470
CE1
PHE
A
308
62.431
45.596
26.153
1.00
23.45

C


ATOM
1471
CE2
PHE
A
308
62.023
43.245
26.504
1.00
23.97

C


ATOM
1472
CZ
PHE
A
308
61.998
44.362
25.669
1.00
23.35

C


ATOM
1473
N
ILE
A
309
62.609
47.724
30.381
1.00
20.99

N


ATOM
1474
CA
ILE
A
309
62.040
49.001
29.994
1.00
21.61

C


ATOM
1475
C
ILE
A
309
62.877
49.704
28.929
1.00
21.29

C


ATOM
1476
O
ILE
A
309
64.096
49.835
29.071
1.00
20.03

O


ATOM
1477
CB
ILE
A
309
61.866
49.881
31.264
1.00
21.66

C


ATOM
1478
CG1
ILE
A
309
60.841
49.204
32.189
1.00
22.00

C


ATOM
1479
CG2
ILE
A
309
61.444
51.298
30.886
1.00
20.92

C


ATOM
1480
CD1
ILE
A
309
60.725
49.797
33.575
1.00
22.70

C


ATOM
1481
N
LYS
A
310
62.212
50.132
27.854
1.00
21.58

N


ATOM
1482
CA
LYS
A
310
62.884
50.809
26.745
1.00
21.98

C


ATOM
1483
C
LYS
A
310
62.919
52.317
26.942
1.00
21.74

C


ATOM
1484
O
LYS
A
310
61.907
52.942
27.271
1.00
21.19

O


ATOM
1485
CB
LYS
A
310
62.211
50.489
25.404
1.00
23.35

C


ATOM
1486
CG
LYS
A
310
62.440
49.071
24.915
1.00
26.33

C


ATOM
1487
CD
LYS
A
310
62.448
48.987
23.377
1.00
24.86

C


ATOM
1488
CE
LYS
A
310
61.072
49.221
22.764
1.00
26.09

C


ATOM
1489
NZ
LYS
A
310
60.922
50.568
22.124
1.00
25.19

N


ATOM
1490
N
ILE
A
311
64.093
52.890
26.704
1.00
20.80

N


ATOM
1491
CA
ILE
A
311
64.330
54.319
26.888
1.00
20.47

C


ATOM
1492
C
ILE
A
311
64.496
55.076
25.578
1.00
20.59

C


ATOM
1493
O
ILE
A
311
65.258
54.658
24.707
1.00
20.84

O


ATOM
1494
CB
ILE
A
311
65.625
54.543
27.695
1.00
19.79

C


ATOM
1495
CG1
ILE
A
311
65.544
53.813
29.039
1.00
19.38

C


ATOM
1496
CG2
ILE
A
311
65.876
56.037
27.885
1.00
19.52

C


ATOM
1497
CD1
ILE
A
311
66.917
53.602
29.686
1.00
19.29

C


ATOM
1498
N
GLY
A
312
63.796
56.197
25.444
1.00
21.35

N


ATOM
1499
CA
GLY
A
312
63.962
56.992
24.247
1.00
22.14

C


ATOM
1500
C
GLY
A
312
62.738
57.526
23.542
1.00
22.59

C


ATOM
1501
O
GLY
A
312
61.877
56.771
23.106
1.00
22.49

O


ATOM
1502
N
ILE
A
313
62.670
58.847
23.430
1.00
23.41

N


ATOM
1503
CA
ILE
A
313
61.577
59.497
22.725
1.00
24.56

C


ATOM
1504
C
ILE
A
313
62.156
60.654
21.912
1.00
25.54

C


ATOM
1505
O
ILE
A
313
62.786
61.553
22.467
1.00
24.97

O


ATOM
1506
CB
ILE
A
313
60.505
60.047
23.692
1.00
24.81

C


ATOM
1507
CG1
ILE
A
313
59.855
58.896
24.471
1.00
24.74

C


ATOM
1508
CG2
ILE
A
313
59.447
60.804
22.904
1.00
25.11

C


ATOM
1509
CD1
ILE
A
313
58.854
59.350
25.526
1.00
25.63

C


ATOM
1510
N
GLY
A
314
61.962
60.609
20.596
1.00
27.37

N


ATOM
1511
CA
GLY
A
314
62.451
61.673
19.729
1.00
29.50

C


ATOM
1512
C
GLY
A
314
63.927
61.641
19.369
1.00
31.01

C


ATOM
1513
O
GLY
A
314
64.422
62.554
18.706
1.00
32.03

O


ATOM
1514
N
GLY
A
315
64.636
60.598
19.791
1.00
31.66

N


ATOM
1515
CA
GLY
A
315
66.056
60.505
19.490
1.00
32.68

C


ATOM
1516
C
GLY
A
315
66.396
59.643
18.285
1.00
33.40

C


ATOM
1517
O
GLY
A
315
67.553
59.576
17.876
1.00
33.37

O


ATOM
1518
N
GLY
A
316
65.396
58.985
17.710
1.00
34.10

N


ATOM
1519
CA
GLY
A
316
65.644
58.137
16.555
1.00
35.23

C


ATOM
1520
C
GLY
A
316
66.065
58.913
15.319
1.00
36.50

C


ATOM
1521
O
GLY
A
316
65.677
60.070
15.141
1.00
36.03

O


ATOM
1522
N
SER
A
317
66.857
58.276
14.460
1.00
37.55

N


ATOM
1523
CA
SER
A
317
67.337
58.911
13.236
1.00
39.31

C


ATOM
1524
C
SER
A
317
66.171
59.337
12.356
1.00
40.68

C


ATOM
1525
O
SER
A
317
66.295
60.251
11.543
1.00
40.52

O


ATOM
1526
CB
SER
A
317
68.240
57.951
12.453
1.00
38.70

C


ATOM
1527
OG
SER
A
317
67.512
56.826
11.980
1.00
38.86

O


ATOM
1528
N
ILE
A
318
65.040
58.663
12.522
1.00
42.85

N


ATOM
1529
CA
ILE
A
318
63.842
58.960
11.751
1.00
45.43

C


ATOM
1530
C
ILE
A
318
63.419
60.410
11.977
1.00
47.03

C


ATOM
1531
O
ILE
A
318
62.896
61.062
11.074
1.00
47.28

O


ATOM
1532
CB
ILE
A
318
62.667
58.043
12.165
1.00
45.77

C


ATOM
1533
CG1
ILE
A
318
63.127
56.586
12.239
1.00
46.41

C


ATOM
1534
CG2
ILE
A
318
61.541
58.171
11.171
1.00
46.37

C


ATOM
1535
CD1
ILE
A
318
63.984
56.265
13.459
1.00
46.06

C


HETATM
1536
N
CSO
A
319
63.652
60.907
13.188
1.00
48.82

N


HETATM
1537
CA
CSO
A
319
63.290
62.276
13.544
1.00
51.09

C


HETATM
1538
CB
CSO
A
319
63.435
62.481
15.053
1.00
50.48

C


HETATM
1539
SG
CSO
A
319
62.220
61.534
16.020
1.00
49.21

S


HETATM
1540
C
CSO
A
319
64.088
63.347
12.809
1.00
52.89

C


HETATM
1541
O
CSO
A
319
63.690
64.513
12.782
1.00
53.33

O


HETATM
1542
OD
CSO
A
319
60.509
62.125
15.865
1.00
49.59

O


ATOM
1543
N
ILE
A
320
65.210
62.955
12.215
1.00
54.92

N


ATOM
1544
CA
ILE
A
320
66.048
63.899
11.484
1.00
56.96

C


ATOM
1545
C
ILE
A
320
65.262
64.568
10.360
1.00
58.10

C


ATOM
1546
O
ILE
A
320
65.443
65.756
10.083
1.00
58.63

O


ATOM
1547
CB
ILE
A
320
67.279
63.197
10.873
1.00
57.26

C


ATOM
1548
CG1
ILE
A
320
68.121
62.562
11.983
1.00
57.57

C


ATOM
1549
CG2
ILE
A
320
68.113
64.201
10.089
1.00
57.46

C


ATOM
1550
CD1
ILE
A
320
69.282
61.731
11.473
1.00
57.71

C


ATOM
1551
N
THR
A
321
64.389
63.801
9.714
1.00
59.12

N


ATOM
1552
CA
THR
A
321
63.583
64.323
8.618
1.00
60.34

C


ATOM
1553
C
THR
A
321
62.103
64.387
8.985
1.00
60.84

C


ATOM
1554
O
THR
A
321
61.257
63.773
8.330
1.00
61.34

O


ATOM
1555
CB
THR
A
321
63.755
63.464
7.352
1.00
60.65

C


ATOM
1556
OG1
THR
A
321
63.414
62.105
7.647
1.00
61.41

O


ATOM
1557
CG2
THR
A
321
65.195
63.524
6.860
1.00
60.98

C


ATOM
1558
N
ARG
A
322
61.806
65.138
10.040
1.00
61.12

N


ATOM
1559
CA
ARG
A
322
60.441
65.314
10.523
1.00
61.24

C


ATOM
1560
C
ARG
A
322
60.445
66.385
11.606
1.00
60.69

C


ATOM
1561
O
ARG
A
322
61.501
66.723
12.145
1.00
60.84

O


ATOM
1562
CB
ARG
A
322
59.901
63.994
11.080
1.00
62.07

C


ATOM
1563
CG
ARG
A
322
58.509
64.074
11.698
1.00
63.32

C


ATOM
1564
CD
ARG
A
322
57.518
64.813
10.804
1.00
64.42

C


ATOM
1565
NE
ARG
A
322
57.486
64.287
9.442
1.00
65.37

N


ATOM
1566
CZ
ARG
A
322
56.737
64.792
8.466
1.00
65.78

C


ATOM
1567
NH1
ARG
A
322
55.955
65.838
8.702
1.00
65.97

N


ATOM
1568
NH2
ARG
A
322
56.774
64.258
7.253
1.00
65.94

N


ATOM
1569
N
GLU
A
323
59.272
66.925
11.919
1.00
59.94

N


ATOM
1570
CA
GLU
A
323
59.174
67.960
12.940
1.00
59.06

C


ATOM
1571
C
GLU
A
323
58.885
67.393
14.325
1.00
57.87

C


ATOM
1572
O
GLU
A
323
58.236
66.355
14.466
1.00
57.61

O


ATOM
1573
CB
GLU
A
323
58.096
68.981
12.570
1.00
59.76

C


ATOM
1574
CG
GLU
A
323
57.938
70.098
13.597
1.00
60.62

C


ATOM
1575
CD
GLU
A
323
59.243
70.833
13.897
1.00
61.14

C


ATOM
1576
OE1
GLU
A
323
59.296
71.537
14.928
1.00
61.68

O


ATOM
1577
OE2
GLU
A
323
60.211
70.719
13.113
1.00
61.24

O


ATOM
1578
N
GLN
A
324
59.379
68.091
15.343
1.00
56.34

N


ATOM
1579
CA
GLN
A
324
59.192
67.685
16.729
1.00
54.78

C


ATOM
1580
C
GLN
A
324
57.726
67.648
17.141
1.00
53.18

C


ATOM
1581
O
GLN
A
324
56.947
68.537
16.794
1.00
53.10

O


ATOM
1582
CB
GLN
A
324
59.956
68.634
17.658
1.00
55.79

C


ATOM
1583
CG
GLN
A
324
61.319
68.127
18.094
1.00
56.75

C


ATOM
1584
CD
GLN
A
324
61.220
66.843
18.891
1.00
57.57

C


ATOM
1585
OE1
GLN
A
324
60.430
66.746
19.830
1.00
58.20

O


ATOM
1586
NE2
GLN
A
324
62.025
65.849
18.524
1.00
58.36

N


ATOM
1587
N
LYS
A
325
57.357
66.607
17.880
1.00
50.98

N


ATOM
1588
CA
LYS
A
325
55.992
66.461
18.367
1.00
48.78

C


ATOM
1589
C
LYS
A
325
55.860
67.276
19.651
1.00
46.62

C


ATOM
1590
O
LYS
A
325
54.757
67.518
20.140
1.00
47.07

O


ATOM
1591
CB
LYS
A
325
55.680
64.987
18.648
1.00
49.79

C


ATOM
1592
CG
LYS
A
325
54.374
64.759
19.405
1.00
50.84

C


ATOM
1593
CD
LYS
A
325
54.094
63.274
19.607
1.00
51.53

C


ATOM
1594
CE
LYS
A
325
53.023
63.046
20.668
1.00
51.83

C


ATOM
1595
NZ
LYS
A
325
51.726
63.694
20.333
1.00
52.33

N


ATOM
1596
N
GLY
A
326
56.997
67.701
20.193
1.00
43.50

N


ATOM
1597
CA
GLY
A
326
56.973
68.490
21.409
1.00
40.48

C


ATOM
1598
C
GLY
A
326
57.413
67.734
22.648
1.00
38.13

C


ATOM
1599
O
GLY
A
326
57.736
68.347
23.664
1.00
37.44

O


ATOM
1600
N
ILE
A
327
57.422
66.405
22.569
1.00
36.05

N


ATOM
1601
CA
ILE
A
327
57.836
65.579
23.696
1.00
34.00

C


ATOM
1602
C
ILE
A
327
59.153
64.882
23.381
1.00
32.98

C


ATOM
1603
O
ILE
A
327
59.400
64.481
22.244
1.00
32.36

O


ATOM
1604
CB
ILE
A
327
56.776
64.498
24.037
1.00
34.45

C


ATOM
1605
CG1
ILE
A
327
56.576
63.557
22.845
1.00
34.20

C


ATOM
1606
CG2
ILE
A
327
55.453
65.165
24.413
1.00
34.27

C


ATOM
1607
CD1
ILE
A
327
55.626
62.390
23.132
1.00
35.32

C


ATOM
1608
N
GLY
A
328
60.001
64.741
24.390
1.00
31.07

N


ATOM
1609
CA
GLY
A
328
61.268
64.078
24.166
1.00
29.89

C


ATOM
1610
C
GLY
A
328
62.337
64.489
25.151
1.00
28.34

C


ATOM
1611
O
GLY
A
328
62.082
65.254
26.080
1.00
27.64

O


ATOM
1612
N
ARG
A
329
63.545
63.980
24.930
1.00
26.67

N


ATOM
1613
CA
ARG
A
329
64.669
64.283
25.797
1.00
25.93

C


ATOM
1614
C
ARG
A
329
65.940
63.749
25.142
1.00
24.65

C


ATOM
1615
O
ARG
A
329
65.904
62.714
24.485
1.00
24.97

O


ATOM
1616
CB
ARG
A
329
64.458
63.605
27.154
1.00
25.47

C


ATOM
1617
CG
ARG
A
329
65.375
64.095
28.248
1.00
25.11

C


ATOM
1618
CD
ARG
A
329
65.056
63.413
29.568
1.00
24.72

C


ATOM
1619
NE
ARG
A
329
65.626
64.149
30.692
1.00
24.50

N


ATOM
1620
CZ
ARG
A
329
65.577
63.743
31.955
1.00
25.99

C


ATOM
1621
NH1
ARG
A
329
64.986
62.595
32.267
1.00
24.83

N


ATOM
1622
NH2
ARG
A
329
66.104
64.497
32.909
1.00
26.04

N


ATOM
1623
N
GLY
A
330
67.054
64.458
25.304
1.00
24.47

N


ATOM
1624
CA
GLY
A
330
68.305
63.977
24.737
1.00
24.08

C


ATOM
1625
C
GLY
A
330
68.487
62.533
25.182
1.00
24.18

C


ATOM
1626
O
GLY
A
330
68.292
62.222
26.358
1.00
22.92

O


ATOM
1627
N
GLN
A
331
68.857
61.655
24.254
1.00
24.04

N


ATOM
1628
CA
GLN
A
331
69.022
60.230
24.551
1.00
24.22

C


ATOM
1629
C
GLN
A
331
70.004
59.909
25.679
1.00
24.49

C


ATOM
1630
O
GLN
A
331
69.737
59.033
26.503
1.00
24.57

O


ATOM
1631
CB
GLN
A
331
69.445
59.470
23.286
1.00
24.17

C


ATOM
1632
CG
GLN
A
331
69.411
57.946
23.436
1.00
24.47

C


ATOM
1633
CD
GLN
A
331
67.988
57.392
23.540
1.00
25.33

C


ATOM
1634
OE1
GLN
A
331
67.777
56.262
23.989
1.00
25.75

O


ATOM
1635
NE2
GLN
A
331
67.013
58.183
23.112
1.00
24.22

N


ATOM
1636
N
ALA
A
332
71.139
60.602
25.713
1.00
23.98

N


ATOM
1637
CA
ALA
A
332
72.138
60.355
26.746
1.00
23.64

C


ATOM
1638
C
ALA
A
332
71.576
60.692
28.124
1.00
23.77

C


ATOM
1639
O
ALA
A
332
71.673
59.892
29.058
1.00
22.81

O


ATOM
1640
CB
ALA
A
332
73.403
61.176
26.470
1.00
23.79

C


ATOM
1641
N
THR
A
333
70.982
61.875
28.245
1.00
23.32

N


ATOM
1642
CA
THR
A
333
70.401
62.302
29.510
1.00
23.16

C


ATOM
1643
C
THR
A
333
69.294
61.345
29.954
1.00
23.11

C


ATOM
1644
O
THR
A
333
69.163
61.040
31.144
1.00
22.07

O


ATOM
1645
CB
THR
A
333
69.814
63.717
29.398
1.00
23.96

C


ATOM
1646
OG1
THR
A
333
70.838
64.619
28.960
1.00
25.42

O


ATOM
1647
CG2
THR
A
333
69.273
64.179
30.749
1.00
24.50

C


ATOM
1648
N
ALA
A
334
68.497
60.884
28.995
1.00
22.70

N


ATOM
1649
CA
ALA
A
334
67.407
59.959
29.292
1.00
23.13

C


ATOM
1650
C
ALA
A
334
67.949
58.654
29.886
1.00
22.44

C


ATOM
1651
O
ALA
A
334
67.456
58.175
30.907
1.00
22.81

O


ATOM
1652
CB
ALA
A
334
66.602
59.671
28.020
1.00
22.10

C


ATOM
1653
N
VAL
A
335
68.965
58.085
29.251
1.00
22.20

N


ATOM
1654
CA
VAL
A
335
69.556
56.840
29.737
1.00
21.98

C


ATOM
1655
C
VAL
A
335
70.150
57.026
31.134
1.00
22.34

C


ATOM
1656
O
VAL
A
335
69.869
56.249
32.047
1.00
22.57

O


ATOM
1657
CB
VAL
A
335
70.656
56.334
28.765
1.00
23.03

C


ATOM
1658
CG1
VAL
A
335
71.411
55.152
29.378
1.00
22.63

C


ATOM
1659
CG2
VAL
A
335
70.015
55.917
27.440
1.00
22.29

C


ATOM
1660
N
ILE
A
336
70.952
58.071
31.302
1.00
22.70

N


ATOM
1661
CA
ILE
A
336
71.588
58.352
32.583
1.00
23.12

C


ATOM
1662
C
ILE
A
336
70.569
58.499
33.710
1.00
23.63

C


ATOM
1663
O
ILE
A
336
70.751
57.941
34.796
1.00
23.32

O


ATOM
1664
CB
ILE
A
336
72.437
59.636
32.498
1.00
23.30

C


ATOM
1665
CG1
ILE
A
336
73.614
59.406
31.545
1.00
23.03

C


ATOM
1666
CG2
ILE
A
336
72.929
60.044
33.888
1.00
23.03

C


ATOM
1667
CD1
ILE
A
336
74.395
60.668
31.215
1.00
23.69

C


ATOM
1668
N
ASP
A
337
69.500
59.248
33.449
1.00
24.24

N


ATOM
1669
CA
ASP
A
337
68.457
59.471
34.447
1.00
24.71

C


ATOM
1670
C
ASP
A
337
67.713
58.179
34.777
1.00
24.54

C


ATOM
1671
O
ASP
A
337
67.506
57.849
35.947
1.00
24.97

O


ATOM
1672
CB
ASP
A
337
67.446
60.505
33.948
1.00
25.62

C


ATOM
1673
CG
ASP
A
337
66.441
60.891
35.016
1.00
27.13

C


ATOM
1674
OD1
ASP
A
337
65.279
61.195
34.679
1.00
27.55

O


ATOM
1675
OD2
ASP
A
337
66.821
60.902
36.202
1.00
29.34

O


ATOM
1676
N
VAL
A
338
67.293
57.455
33.743
1.00
23.33

N


ATOM
1677
CA
VAL
A
338
66.569
56.206
33.953
1.00
22.60

C


ATOM
1678
C
VAL
A
338
67.430
55.171
34.672
1.00
22.27

C


ATOM
1679
O
VAL
A
338
66.948
54.471
35.557
1.00
21.72

O


ATOM
1680
CB
VAL
A
338
66.075
55.611
32.615
1.00
22.51

C


ATOM
1681
CG1
VAL
A
338
65.518
54.204
32.839
1.00
21.86

C


ATOM
1682
CG2
VAL
A
338
64.985
56.514
32.023
1.00
21.22

C


ATOM
1683
N
VAL
A
339
68.700
55.078
34.284
1.00
22.03

N


ATOM
1684
CA
VAL
A
339
69.622
54.129
34.903
1.00
21.70

C


ATOM
1685
C
VAL
A
339
69.776
54.432
36.398
1.00
22.15

C


ATOM
1686
O
VAL
A
339
69.853
53.520
37.219
1.00
21.73

O


ATOM
1687
CB
VAL
A
339
71.015
54.174
34.214
1.00
21.11

C


ATOM
1688
CG1
VAL
A
339
72.079
53.494
35.099
1.00
20.90

C


ATOM
1689
CG2
VAL
A
339
70.936
53.465
32.855
1.00
20.61

C


ATOM
1690
N
ALA
A
340
69.821
55.712
36.749
1.00
21.99

N


ATOM
1691
CA
ALA
A
340
69.957
56.085
38.155
1.00
23.22

C


ATOM
1692
C
ALA
A
340
68.717
55.623
38.928
1.00
22.99

C


ATOM
1693
O
ALA
A
340
68.818
55.112
40.048
1.00
23.73

O


ATOM
1694
CB
ALA
A
340
70.140
57.599
38.283
1.00
23.33

C


ATOM
1695
N
GLU
A
341
67.549
55.788
38.320
1.00
22.81

N


ATOM
1696
CA
GLU
A
341
66.298
55.376
38.955
1.00
23.25

C


ATOM
1697
C
GLU
A
341
66.234
53.851
39.047
1.00
22.89

C


ATOM
1698
O
GLU
A
341
65.740
53.296
40.029
1.00
22.02

O


ATOM
1699
CB
GLU
A
341
65.103
55.885
38.146
1.00
23.80

C


ATOM
1700
CG
GLU
A
341
63.786
55.897
38.910
1.00
26.95

C


ATOM
1701
CD
GLU
A
341
63.827
56.810
40.130
1.00
29.07

C


ATOM
1702
OE1
GLU
A
341
64.433
57.902
40.052
1.00
30.17

O


ATOM
1703
OE2
GLU
A
341
63.240
56.441
41.165
1.00
30.84

O


ATOM
1704
N
ARG
A
342
66.736
53.179
38.014
1.00
22.30

N


ATOM
1705
CA
ARG
A
342
66.737
51.722
37.979
1.00
22.47

C


ATOM
1706
C
ARG
A
342
67.639
51.169
39.084
1.00
22.30

C


ATOM
1707
O
ARG
A
342
67.303
50.182
39.732
1.00
22.02

O


ATOM
1708
CB
ARG
A
342
67.205
51.233
36.598
1.00
22.21

C


ATOM
1709
CG
ARG
A
342
67.165
49.717
36.393
1.00
21.30

C


ATOM
1710
CD
ARG
A
342
68.428
49.027
36.910
1.00
21.14

C


ATOM
1711
NE
ARG
A
342
69.657
49.497
36.266
1.00
21.04

N


ATOM
1712
CZ
ARG
A
342
70.024
49.221
35.012
1.00
21.58

C


ATOM
1713
NH1
ARG
A
342
69.260
48.468
34.227
1.00
20.91

N


ATOM
1714
NH2
ARG
A
342
71.175
49.686
34.543
1.00
21.45

N


ATOM
1715
N
ASN
A
343
68.780
51.813
39.304
1.00
22.59

N


ATOM
1716
CA
ASN
A
343
69.697
51.356
40.343
1.00
23.77

C


ATOM
1717
C
ASN
A
343
69.096
51.613
41.721
1.00
24.38

C


ATOM
1718
O
ASN
A
343
69.274
50.816
42.643
1.00
23.51

O


ATOM
1719
CB
ASN
A
343
71.060
52.046
40.201
1.00
23.94

C


ATOM
1720
CG
ASN
A
343
71.798
51.608
38.948
1.00
24.43

C


ATOM
1721
OD1
ASN
A
343
71.500
50.554
38.386
1.00
24.77

O


ATOM
1722
ND2
ASN
A
343
72.775
52.404
38.513
1.00
24.50

N


ATOM
1723
N
LYS
A
344
68.368
52.718
41.849
1.00
24.94

N


ATOM
1724
CA
LYS
A
344
67.717
53.063
43.104
1.00
26.62

C


ATOM
1725
C
LYS
A
344
66.626
52.029
43.368
1.00
26.38

C


ATOM
1726
O
LYS
A
344
66.461
51.551
44.492
1.00
26.78

O


ATOM
1727
CB
LYS
A
344
67.106
54.465
43.008
1.00
29.24

C


ATOM
1728
CG
LYS
A
344
66.398
54.943
44.267
1.00
32.28

C


ATOM
1729
CD
LYS
A
344
65.866
56.358
44.078
1.00
34.61

C


ATOM
1730
CE
LYS
A
344
65.196
56.878
45.343
1.00
36.69

C


ATOM
1731
NZ
LYS
A
344
66.161
57.002
46.475
1.00
38.80

N


ATOM
1732
N
TYR
A
345
65.888
51.681
42.318
1.00
25.59

N


ATOM
1733
CA
TYR
A
345
64.811
50.702
42.412
1.00
25.49

C


ATOM
1734
C
TYR
A
345
65.366
49.339
42.841
1.00
25.79

C


ATOM
1735
O
TYR
A
345
64.746
48.627
43.635
1.00
24.45

O


ATOM
1736
CB
TYR
A
345
64.117
50.566
41.057
1.00
25.37

C


ATOM
1737
CG
TYR
A
345
62.815
49.801
41.089
1.00
25.96

C


ATOM
1738
CD1
TYR
A
345
61.626
50.427
41.460
1.00
26.32

C


ATOM
1739
CD2
TYR
A
345
62.764
48.459
40.713
1.00
26.30

C


ATOM
1740
CE1
TYR
A
345
60.415
49.738
41.446
1.00
27.08

C


ATOM
1741
CE2
TYR
A
345
61.558
47.759
40.697
1.00
27.11

C


ATOM
1742
CZ
TYR
A
345
60.391
48.406
41.061
1.00
27.19

C


ATOM
1743
OH
TYR
A
345
59.195
47.735
41.008
1.00
28.86

O


ATOM
1744
N
PHE
A
346
66.530
48.983
42.305
1.00
26.33

N


ATOM
1745
CA
PHE
A
346
67.181
47.713
42.632
1.00
27.73

C


ATOM
1746
C
PHE
A
346
67.537
47.684
44.118
1.00
28.91

C


ATOM
1747
O
PHE
A
346
67.337
46.679
44.798
1.00
28.66

O


ATOM
1748
CB
PHE
A
346
68.450
47.540
41.793
1.00
27.70

C


ATOM
1749
CG
PHE
A
346
69.269
46.331
42.163
1.00
27.99

C


ATOM
1750
CD1
PHE
A
346
68.773
45.047
41.959
1.00
27.87

C


ATOM
1751
CD2
PHE
A
346
70.536
46.480
42.723
1.00
28.85

C


ATOM
1752
CE1
PHE
A
346
69.526
43.923
42.304
1.00
27.89

C


ATOM
1753
CE2
PHE
A
346
71.303
45.361
43.076
1.00
29.71

C


ATOM
1754
CZ
PHE
A
346
70.793
44.080
42.864
1.00
29.06

C


ATOM
1755
N
GLU
A
347
68.059
48.798
44.616
1.00
30.12

N


ATOM
1756
CA
GLU
A
347
68.430
48.897
46.021
1.00
32.28

C


ATOM
1757
C
GLU
A
347
67.227
48.820
46.958
1.00
31.98

C


ATOM
1758
O
GLU
A
347
67.329
48.280
48.056
1.00
31.99

O


ATOM
1759
CB
GLU
A
347
69.189
50.200
46.280
1.00
33.95

C


ATOM
1760
CG
GLU
A
347
70.645
50.150
45.853
1.00
38.56

C


ATOM
1761
CD
GLU
A
347
71.454
51.319
46.386
1.00
41.08

C


ATOM
1762
OE1
GLU
A
347
71.294
51.673
47.576
1.00
42.98

O


ATOM
1763
OE2
GLU
A
347
72.265
51.875
45.619
1.00
43.56

O


ATOM
1764
N
GLU
A
348
66.091
49.352
46.522
1.00
31.64

N


ATOM
1765
CA
GLU
A
348
64.888
49.347
47.348
1.00
31.87

C


ATOM
1766
C
GLU
A
348
64.124
48.031
47.330
1.00
30.98

C


ATOM
1767
O
GLU
A
348
63.576
47.617
48.350
1.00
31.10

O


ATOM
1768
CB
GLU
A
348
63.911
50.439
46.897
1.00
33.10

C


ATOM
1769
CG
GLU
A
348
64.506
51.812
46.664
1.00
35.32

C


ATOM
1770
CD
GLU
A
348
63.494
52.779
46.059
1.00
36.44

C


ATOM
1771
OE1
GLU
A
348
62.716
52.358
45.178
1.00
37.22

O


ATOM
1772
OE2
GLU
A
348
63.481
53.961
46.454
1.00
38.05

O


ATOM
1773
N
THR
A
349
64.079
47.381
46.171
1.00
29.37

N


ATOM
1774
CA
THR
A
349
63.316
46.147
46.016
1.00
28.42

C


ATOM
1775
C
THR
A
349
64.107
44.864
45.790
1.00
28.26

C


ATOM
1776
O
THR
A
349
63.563
43.775
45.928
1.00
28.54

O


ATOM
1777
CB
THR
A
349
62.347
46.267
44.829
1.00
28.53

C


ATOM
1778
OG1
THR
A
349
63.106
46.331
43.611
1.00
26.68

O


ATOM
1779
CG2
THR
A
349
61.489
47.525
44.956
1.00
27.99

C


ATOM
1780
N
GLY
A
350
65.375
44.982
45.423
1.00
27.91

N


ATOM
1781
CA
GLY
A
350
66.153
43.789
45.148
1.00
27.45

C


ATOM
1782
C
GLY
A
350
65.860
43.276
43.743
1.00
26.56

C


ATOM
1783
O
GLY
A
350
66.367
42.235
43.339
1.00
27.60

O


ATOM
1784
N
ILE
A
351
65.034
44.005
42.995
1.00
25.92

N


ATOM
1785
CA
ILE
A
351
64.687
43.614
41.625
1.00
24.44

C


ATOM
1786
C
ILE
A
351
65.530
44.395
40.619
1.00
23.82

C


ATOM
1787
O
ILE
A
351
65.557
45.627
40.649
1.00
22.61

O


ATOM
1788
CB
ILE
A
351
63.203
43.913
41.299
1.00
25.48

C


ATOM
1789
CG1
ILE
A
351
62.281
43.222
42.310
1.00
25.99

C


ATOM
1790
CG2
ILE
A
351
62.880
43.449
39.873
1.00
25.21

C


ATOM
1791
CD1
ILE
A
351
60.810
43.615
42.169
1.00
26.39

C


ATOM
1792
N
TYR
A
352
66.214
43.683
39.728
1.00
23.12

N


ATOM
1793
CA
TYR
A
352
67.024
44.339
38.708
1.00
22.28

C


ATOM
1794
C
TYR
A
352
66.274
44.290
37.389
1.00
22.46

C


ATOM
1795
O
TYR
A
352
66.033
43.210
36.845
1.00
21.68

O


ATOM
1796
CB
TYR
A
352
68.375
43.647
38.518
1.00
22.40

C


ATOM
1797
CG
TYR
A
352
69.269
44.375
37.526
1.00
22.27

C


ATOM
1798
CD1
TYR
A
352
70.058
45.451
37.932
1.00
22.07

C


ATOM
1799
CD2
TYR
A
352
69.296
44.012
36.176
1.00
22.89

C


ATOM
1800
CE1
TYR
A
352
70.852
46.151
37.028
1.00
22.81

C


ATOM
1801
CE2
TYR
A
352
70.094
44.714
35.252
1.00
22.60

C


ATOM
1802
CZ
TYR
A
352
70.868
45.779
35.691
1.00
22.45

C


ATOM
1803
OH
TYR
A
352
71.676
46.468
34.814
1.00
22.10

O


ATOM
1804
N
ILE
A
353
65.912
45.462
36.876
1.00
22.15

N


ATOM
1805
CA
ILE
A
353
65.196
45.556
35.610
1.00
22.13

C


ATOM
1806
C
ILE
A
353
66.119
46.052
34.495
1.00
21.86

C


ATOM
1807
O
ILE
A
353
66.603
47.188
34.531
1.00
21.86

O


ATOM
1808
CB
ILE
A
353
63.996
46.523
35.721
1.00
23.05

C


ATOM
1809
CG1
ILE
A
353
63.036
46.030
36.817
1.00
23.41

C


ATOM
1810
CG2
ILE
A
353
63.278
46.614
34.374
1.00
21.86

C


ATOM
1811
CD1
ILE
A
353
61.863
46.936
37.063
1.00
24.85

C


ATOM
1812
N
PRO
A
354
66.388
45.201
33.495
1.00
21.74

N


ATOM
1813
CA
PRO
A
354
67.263
45.626
32.397
1.00
21.25

C


ATOM
1814
C
PRO
A
354
66.608
46.780
31.649
1.00
21.17

C


ATOM
1815
O
PRO
A
354
65.385
46.825
31.534
1.00
21.72

O


ATOM
1816
CB
PRO
A
354
67.360
44.373
31.524
1.00
21.72

C


ATOM
1817
CG
PRO
A
354
67.181
43.240
32.529
1.00
20.93

C


ATOM
1818
CD
PRO
A
354
66.051
43.769
33.382
1.00
21.57

C


ATOM
1819
N
VAL
A
355
67.406
47.722
31.159
1.00
20.15

N


ATOM
1820
CA
VAL
A
355
66.841
48.829
30.396
1.00
19.73

C


ATOM
1821
C
VAL
A
355
67.482
48.842
29.022
1.00
19.50

C


ATOM
1822
O
VAL
A
355
68.629
48.430
28.851
1.00
19.88

O


ATOM
1823
CB
VAL
A
355
67.032
50.206
31.094
1.00
18.66

C


ATOM
1824
CG1
VAL
A
355
66.254
50.226
32.394
1.00
18.46

C


ATOM
1825
CG2
VAL
A
355
68.514
50.497
31.333
1.00
18.65

C


ATOM
1826
N
CYS
A
356
66.723
49.312
28.043
1.00
19.68

N


ATOM
1827
CA
CYS
A
356
67.185
49.346
26.666
1.00
20.26

C


ATOM
1828
C
CYS
A
356
67.273
50.761
26.110
1.00
20.70

C


ATOM
1829
O
CYS
A
356
66.297
51.509
26.161
1.00
20.96

O


ATOM
1830
CB
CYS
A
356
66.228
48.522
25.796
1.00
20.28

C


ATOM
1831
SG
CYS
A
356
66.486
48.701
24.007
1.00
22.73

S


ATOM
1832
N
SER
A
357
68.440
51.129
25.586
1.00
20.27

N


ATOM
1833
CA
SER
A
357
68.597
52.447
24.981
1.00
20.16

C


ATOM
1834
C
SER
A
357
68.088
52.277
23.553
1.00
20.30

C


ATOM
1835
O
SER
A
357
68.713
51.599
22.734
1.00
19.54

O


ATOM
1836
CB
SER
A
357
70.061
52.882
24.962
1.00
20.20

C


ATOM
1837
OG
SER
A
357
70.163
54.193
24.432
1.00
20.16

O


ATOM
1838
N
ASP
A
358
66.951
52.899
23.262
1.00
20.12

N


ATOM
1839
CA
ASP
A
358
66.327
52.767
21.955
1.00
21.37

C


ATOM
1840
C
ASP
A
358
66.441
54.009
21.070
1.00
21.92

C


ATOM
1841
O
ASP
A
358
65.862
55.057
21.367
1.00
22.18

O


ATOM
1842
CB
ASP
A
358
64.855
52.370
22.166
1.00
20.81

C


ATOM
1843
CG
ASP
A
358
64.081
52.214
20.867
1.00
22.08

C


ATOM
1844
OD1
ASP
A
358
64.703
52.059
19.791
1.00
21.34

O


ATOM
1845
OD2
ASP
A
358
62.834
52.229
20.937
1.00
20.69

O


ATOM
1846
N
GLY
A
359
67.204
53.875
19.986
1.00
22.92

N


ATOM
1847
CA
GLY
A
359
67.381
54.964
19.040
1.00
23.74

C


ATOM
1848
C
GLY
A
359
68.538
55.905
19.328
1.00
25.08

C


ATOM
1849
O
GLY
A
359
69.078
55.928
20.431
1.00
24.78

O


ATOM
1850
N
GLY
A
360
68.932
56.678
18.323
1.00
25.97

N


ATOM
1851
CA
GLY
A
360
70.007
57.633
18.517
1.00
27.86

C


ATOM
1852
C
GLY
A
360
71.419
57.132
18.287
1.00
28.88

C


ATOM
1853
O
GLY
A
360
72.367
57.904
18.417
1.00
29.93

O


ATOM
1854
N
ILE
A
361
71.581
55.855
17.961
1.00
29.68

N


ATOM
1855
CA
ILE
A
361
72.918
55.329
17.706
1.00
30.57

C


ATOM
1856
C
ILE
A
361
73.309
55.719
16.282
1.00
31.81

C


ATOM
1857
O
ILE
A
361
72.765
55.196
15.310
1.00
31.75

O


ATOM
1858
CB
ILE
A
361
72.971
53.789
17.838
1.00
30.18

C


ATOM
1859
CG1
ILE
A
361
72.603
53.368
19.266
1.00
29.88

C


ATOM
1860
CG2
ILE
A
361
74.366
53.282
17.481
1.00
30.01

C


ATOM
1861
CD1
ILE
A
361
73.605
53.792
20.328
1.00
28.84

C


ATOM
1862
N
VAL
A
362
74.249
56.648
16.167
1.00
32.99

N


ATOM
1863
CA
VAL
A
362
74.699
57.110
14.862
1.00
33.95

C


ATOM
1864
C
VAL
A
362
76.028
56.463
14.483
1.00
34.24

C


ATOM
1865
O
VAL
A
362
76.203
56.015
13.351
1.00
35.04

O


ATOM
1866
CB
VAL
A
362
74.851
58.646
14.854
1.00
34.42

C


ATOM
1867
CG1
VAL
A
362
75.233
59.131
13.462
1.00
34.82

C


ATOM
1868
CG2
VAL
A
362
73.555
59.292
15.304
1.00
34.82

C


ATOM
1869
N
TYR
A
363
76.953
56.404
15.438
1.00
33.91

N


ATOM
1870
CA
TYR
A
363
78.271
55.813
15.210
1.00
33.19

C


ATOM
1871
C
TYR
A
363
78.507
54.649
16.163
1.00
31.86

C


ATOM
1872
O
TYR
A
363
77.862
54.561
17.207
1.00
31.05

O


ATOM
1873
CB
TYR
A
363
79.350
56.877
15.411
1.00
34.45

C


ATOM
1874
CG
TYR
A
363
79.142
58.094
14.544
1.00
36.04

C


ATOM
1875
CD1
TYR
A
363
79.242
58.008
13.154
1.00
37.00

C


ATOM
1876
CD2
TYR
A
363
78.796
59.323
15.105
1.00
36.77

C


ATOM
1877
CE1
TYR
A
363
78.998
59.114
12.344
1.00
38.19

C


ATOM
1878
CE2
TYR
A
363
78.548
60.435
14.304
1.00
37.90

C


ATOM
1879
CZ
TYR
A
363
78.649
60.323
12.926
1.00
38.55

C


ATOM
1880
OH
TYR
A
363
78.390
61.415
12.130
1.00
40.47

O


ATOM
1881
N
ASP
A
364
79.432
53.760
15.813
1.00
30.55

N


ATOM
1882
CA
ASP
A
364
79.717
52.610
16.668
1.00
29.67

C


ATOM
1883
C
ASP
A
364
80.055
52.987
18.108
1.00
28.54

C


ATOM
1884
O
ASP
A
364
79.621
52.316
19.043
1.00
28.30

O


ATOM
1885
CB
ASP
A
364
80.871
51.772
16.109
1.00
30.75

C


ATOM
1886
CG
ASP
A
364
80.511
51.052
14.819
1.00
31.62

C


ATOM
1887
OD1
ASP
A
364
79.346
50.634
14.647
1.00
31.07

O


ATOM
1888
OD2
ASP
A
364
81.413
50.887
13.981
1.00
33.54

O


ATOM
1889
N
TYR
A
365
80.828
54.054
18.293
1.00
26.82

N


ATOM
1890
CA
TYR
A
365
81.214
54.449
19.642
1.00
26.01

C


ATOM
1891
C
TYR
A
365
80.021
54.874
20.499
1.00
25.10

C


ATOM
1892
O
TYR
A
365
80.117
54.925
21.723
1.00
24.73

O


ATOM
1893
CB
TYR
A
365
82.295
55.541
19.588
1.00
25.94

C


ATOM
1894
CG
TYR
A
365
81.804
56.962
19.451
1.00
26.33

C


ATOM
1895
CD1
TYR
A
365
81.582
57.751
20.578
1.00
25.79

C


ATOM
1896
CD2
TYR
A
365
81.624
57.542
18.193
1.00
26.48

C


ATOM
1897
CE1
TYR
A
365
81.203
59.086
20.459
1.00
27.08

C


ATOM
1898
CE2
TYR
A
365
81.242
58.876
18.063
1.00
27.27

C


ATOM
1899
CZ
TYR
A
365
81.036
59.640
19.198
1.00
27.74

C


ATOM
1900
OH
TYR
A
365
80.675
60.962
19.074
1.00
29.07

O


ATOM
1901
N
HIS
A
366
78.892
55.164
19.858
1.00
24.53

N


ATOM
1902
CA
HIS
A
366
77.685
55.534
20.591
1.00
24.28

C


ATOM
1903
C
HIS
A
366
77.190
54.300
21.339
1.00
23.77

C


ATOM
1904
O
HIS
A
366
76.569
54.411
22.399
1.00
23.59

O


ATOM
1905
CB
HIS
A
366
76.589
56.017
19.641
1.00
24.35

C


ATOM
1906
CG
HIS
A
366
76.799
57.409
19.134
1.00
25.11

C


ATOM
1907
ND1
HIS
A
366
77.870
58.187
19.517
1.00
25.78

N


ATOM
1908
CD2
HIS
A
366
76.059
58.173
18.295
1.00
25.31

C


ATOM
1909
CE1
HIS
A
366
77.779
59.372
18.938
1.00
25.96

C


ATOM
1910
NE2
HIS
A
366
76.690
59.389
18.191
1.00
25.85

N


ATOM
1911
N
MET
A
367
77.463
53.129
20.773
1.00
23.23

N


ATOM
1912
CA
MET
A
367
77.062
51.863
21.388
1.00
23.44

C


ATOM
1913
C
MET
A
367
77.785
51.715
22.721
1.00
22.42

C


ATOM
1914
O
MET
A
367
77.180
51.385
23.735
1.00
21.74

O


ATOM
1915
CB
MET
A
367
77.437
50.672
20.494
1.00
23.55

C


ATOM
1916
CG
MET
A
367
76.680
50.582
19.169
1.00
25.18

C


ATOM
1917
SD
MET
A
367
77.253
49.158
18.204
1.00
26.50

S


ATOM
1918
CE
MET
A
367
76.270
49.323
16.707
1.00
25.76

C


ATOM
1919
N
THR
A
368
79.093
51.941
22.698
1.00
22.22

N


ATOM
1920
CA
THR
A
368
79.915
51.835
23.898
1.00
22.15

C


ATOM
1921
C
THR
A
368
79.445
52.838
24.952
1.00
21.97

C


ATOM
1922
O
THR
A
368
79.380
52.517
26.137
1.00
22.10

O


ATOM
1923
CB
THR
A
368
81.392
52.097
23.560
1.00
22.55

C


ATOM
1924
OG1
THR
A
368
81.735
51.369
22.373
1.00
22.22

O


ATOM
1925
CG2
THR
A
368
82.294
51.645
24.702
1.00
21.82

C


ATOM
1926
N
LEU
A
369
79.117
54.052
24.517
1.00
21.48

N


ATOM
1927
CA
LEU
A
369
78.640
55.087
25.431
1.00
21.65

C


ATOM
1928
C
LEU
A
369
77.318
54.693
26.096
1.00
21.14

C


ATOM
1929
O
LEU
A
369
77.163
54.833
27.306
1.00
20.89

O


ATOM
1930
CB
LEU
A
369
78.446
56.416
24.689
1.00
22.45

C


ATOM
1931
CG
LEU
A
369
79.697
57.209
24.300
1.00
24.02

C


ATOM
1932
CD1
LEU
A
369
79.301
58.381
23.400
1.00
23.76

C


ATOM
1933
CD2
LEU
A
369
80.397
57.710
25.567
1.00
23.98

C


ATOM
1934
N
ALA
A
370
76.371
54.211
25.296
1.00
20.39

N


ATOM
1935
CA
ALA
A
370
75.065
53.806
25.810
1.00
20.84

C


ATOM
1936
C
ALA
A
370
75.242
52.732
26.877
1.00
20.22

C


ATOM
1937
O
ALA
A
370
74.635
52.793
27.945
1.00
20.03

O


ATOM
1938
CB
ALA
A
370
74.194
53.279
24.675
1.00
20.37

C


ATOM
1939
N
LEU
A
371
76.078
51.748
26.576
1.00
20.36

N


ATOM
1940
CA
LEU
A
371
76.343
50.669
27.516
1.00
20.12

C


ATOM
1941
C
LEU
A
371
77.032
51.209
28.773
1.00
20.41

C


ATOM
1942
O
LEU
A
371
76.656
50.853
29.887
1.00
19.69

O


ATOM
1943
CB
LEU
A
371
77.222
49.602
26.854
1.00
19.81

C


ATOM
1944
CG
LEU
A
371
76.580
48.882
25.656
1.00
20.61

C


ATOM
1945
CD1
LEU
A
371
77.592
47.954
24.999
1.00
21.12

C


ATOM
1946
CD2
LEU
A
371
75.364
48.092
26.127
1.00
20.77

C


ATOM
1947
N
ALA
A
372
78.036
52.064
28.588
1.00
20.08

N


ATOM
1948
CA
ALA
A
372
78.772
52.640
29.712
1.00
20.58

C


ATOM
1949
C
ALA
A
372
77.868
53.444
30.641
1.00
21.51

C


ATOM
1950
O
ALA
A
372
78.064
53.450
31.858
1.00
21.21

O


ATOM
1951
CB
ALA
A
372
79.909
53.525
29.199
1.00
20.25

C


ATOM
1952
N
MET
A
373
76.883
54.126
30.065
1.00
21.00

N


ATOM
1953
CA
MET
A
373
75.947
54.923
30.852
1.00
21.56

C


ATOM
1954
C
MET
A
373
74.960
54.065
31.641
1.00
21.75

C


ATOM
1955
O
MET
A
373
74.187
54.588
32.449
1.00
21.78

O


ATOM
1956
CB
MET
A
373
75.192
55.892
29.944
1.00
21.91

C


ATOM
1957
CG
MET
A
373
76.082
56.987
29.370
1.00
22.56

C


ATOM
1958
SD
MET
A
373
75.243
57.985
28.132
1.00
24.61

S


ATOM
1959
CE
MET
A
373
76.595
59.086
27.591
1.00
23.75

C


ATOM
1960
N
GLY
A
374
74.970
52.754
31.405
1.00
21.29

N


ATOM
1961
CA
GLY
A
374
74.078
51.884
32.157
1.00
20.54

C


ATOM
1962
C
GLY
A
374
73.062
51.058
31.390
1.00
20.55

C


ATOM
1963
O
GLY
A
374
72.444
50.164
31.961
1.00
20.60

O


ATOM
1964
N
ALA
A
375
72.864
51.345
30.108
1.00
20.21

N


ATOM
1965
CA
ALA
A
375
71.910
50.562
29.332
1.00
20.36

C


ATOM
1966
C
ALA
A
375
72.448
49.140
29.228
1.00
20.12

C


ATOM
1967
O
ALA
A
375
73.644
48.943
29.011
1.00
19.79

O


ATOM
1968
CB
ALA
A
375
71.731
51.166
27.932
1.00
20.49

C


ATOM
1969
N
ASP
A
376
71.573
48.151
29.399
1.00
20.05

N


ATOM
1970
CA
ASP
A
376
71.976
46.744
29.308
1.00
20.54

C


ATOM
1971
C
ASP
A
376
72.074
46.303
27.854
1.00
20.62

C


ATOM
1972
O
ASP
A
376
72.933
45.498
27.491
1.00
20.67

O


ATOM
1973
CB
ASP
A
376
70.978
45.874
30.069
1.00
20.75

C


ATOM
1974
CG
ASP
A
376
70.900
46.253
31.530
1.00
21.21

C


ATOM
1975
OD1
ASP
A
376
71.732
45.757
32.319
1.00
21.97

O


ATOM
1976
OD2
ASP
A
376
70.027
47.073
31.882
1.00
21.23

O


ATOM
1977
N
PHE
A
377
71.173
46.813
27.022
1.00
21.26

N


ATOM
1978
CA
PHE
A
377
71.220
46.501
25.604
1.00
21.16

C


ATOM
1979
C
PHE
A
377
70.726
47.683
24.788
1.00
21.44

C


ATOM
1980
O
PHE
A
377
70.186
48.647
25.336
1.00
21.24

O


ATOM
1981
CB
PHE
A
377
70.467
45.204
25.252
1.00
21.17

C


ATOM
1982
CG
PHE
A
377
69.056
45.135
25.758
1.00
22.60

C


ATOM
1983
CD1
PHE
A
377
68.791
44.771
27.077
1.00
23.03

C


ATOM
1984
CD2
PHE
A
377
67.987
45.371
24.900
1.00
21.57

C


ATOM
1985
CE1
PHE
A
377
67.478
44.638
27.531
1.00
22.95

C


ATOM
1986
CE2
PHE
A
377
66.669
45.240
25.345
1.00
22.51

C


ATOM
1987
CZ
PHE
A
377
66.416
44.872
26.663
1.00
22.95

C


ATOM
1988
N
ILE
A
378
70.931
47.600
23.480
1.00
20.98

N


ATOM
1989
CA
ILE
A
378
70.607
48.683
22.567
1.00
21.02

C


ATOM
1990
C
ILE
A
378
69.669
48.272
21.439
1.00
20.93

C


ATOM
1991
O
ILE
A
378
69.847
47.222
20.833
1.00
20.57

O


ATOM
1992
CB
ILE
A
378
71.923
49.220
21.936
1.00
21.28

C


ATOM
1993
CG1
ILE
A
378
72.914
49.588
23.046
1.00
21.93

C


ATOM
1994
CG2
ILE
A
378
71.643
50.439
21.056
1.00
21.62

C


ATOM
1995
CD1
ILE
A
378
74.341
49.772
22.558
1.00
22.57

C


ATOM
1996
N
MET
A
379
68.669
49.105
21.166
1.00
20.84

N


ATOM
1997
CA
MET
A
379
67.743
48.831
20.073
1.00
21.55

C


ATOM
1998
C
MET
A
379
68.084
49.794
18.941
1.00
21.65

C


ATOM
1999
O
MET
A
379
68.230
50.998
19.164
1.00
21.66

O


ATOM
2000
CB
MET
A
379
66.284
49.028
20.503
1.00
21.25

C


ATOM
2001
CG
MET
A
379
65.303
48.766
19.356
1.00
21.22

C


ATOM
2002
SD
MET
A
379
63.576
48.745
19.833
1.00
22.14

S


ATOM
2003
CE
MET
A
379
63.437
47.038
20.433
1.00
22.39

C


ATOM
2004
N
LEU
A
380
68.226
49.262
17.731
1.00
22.48

N


ATOM
2005
CA
LEU
A
380
68.575
50.092
16.584
1.00
22.61

C


ATOM
2006
C
LEU
A
380
67.703
49.788
15.373
1.00
22.97

C


ATOM
2007
O
LEU
A
380
67.342
48.634
15.128
1.00
22.62

O


ATOM
2008
CB
LEU
A
380
70.041
49.875
16.192
1.00
23.11

C


ATOM
2009
CG
LEU
A
380
71.131
49.897
17.270
1.00
23.70

C


ATOM
2010
CD1
LEU
A
380
71.193
48.542
17.966
1.00
23.80

C


ATOM
2011
CD2
LEU
A
380
72.476
50.200
16.625
1.00
23.63

C


ATOM
2012
N
GLY
A
381
67.382
50.830
14.614
1.00
22.74

N


ATOM
2013
CA
GLY
A
381
66.576
50.655
13.419
1.00
24.26

C


ATOM
2014
C
GLY
A
381
67.414
50.872
12.172
1.00
24.94

C


ATOM
2015
O
GLY
A
381
67.648
49.946
11.397
1.00
25.50

O


ATOM
2016
N
ARG
A
382
67.882
52.103
11.992
1.00
26.09

N


ATOM
2017
CA
ARG
A
382
68.694
52.477
10.836
1.00
27.52

C


ATOM
2018
C
ARG
A
382
69.891
51.551
10.630
1.00
27.04

C


ATOM
2019
O
ARG
A
382
70.180
51.130
9.507
1.00
26.49

O


ATOM
2020
CB
ARG
A
382
69.199
53.911
10.998
1.00
29.77

C


ATOM
2021
CG
ARG
A
382
69.830
54.488
9.737
1.00
34.03

C


ATOM
2022
CD
ARG
A
382
70.702
55.699
10.034
1.00
37.28

C


ATOM
2023
NE
ARG
A
382
72.102
55.327
10.247
1.00
41.27

N


ATOM
2024
CZ
ARG
A
382
72.554
54.651
11.300
1.00
42.49

C


ATOM
2025
NH1
ARG
A
382
71.723
54.267
12.255
1.00
44.24

N


ATOM
2026
NH2
ARG
A
382
73.842
54.354
11.396
1.00
44.03

N


ATOM
2027
N
TYR
A
383
70.589
51.248
11.721
1.00
26.34

N


ATOM
2028
CA
TYR
A
383
71.763
50.380
11.679
1.00
25.33

C


ATOM
2029
C
TYR
A
383
71.493
49.062
10.948
1.00
24.88

C


ATOM
2030
O
TYR
A
383
72.280
48.639
10.096
1.00
24.77

O


ATOM
2031
CB
TYR
A
383
72.233
50.075
13.105
1.00
24.87

C


ATOM
2032
CG
TYR
A
383
73.466
49.203
13.179
1.00
24.53

C


ATOM
2033
CD1
TYR
A
383
74.742
49.754
13.066
1.00
24.66

C


ATOM
2034
CD2
TYR
A
383
73.356
47.823
13.354
1.00
24.92

C


ATOM
2035
CE1
TYR
A
383
75.882
48.952
13.126
1.00
24.58

C


ATOM
2036
CE2
TYR
A
383
74.491
47.008
13.413
1.00
24.77

C


ATOM
2037
CZ
TYR
A
383
75.748
47.581
13.299
1.00
25.09

C


ATOM
2038
OH
TYR
A
383
76.867
46.782
13.350
1.00
24.41

O


ATOM
2039
N
PHE
A
384
70.383
48.416
11.291
1.00
24.06

N


ATOM
2040
CA
PHE
A
384
70.015
47.136
10.694
1.00
23.93

C


ATOM
2041
C
PHE
A
384
69.289
47.263
9.357
1.00
24.44

C


ATOM
2042
O
PHE
A
384
69.320
46.338
8.542
1.00
24.13

O


ATOM
2043
CB
PHE
A
384
69.139
46.334
11.663
1.00
23.18

C


ATOM
2044
CG
PHE
A
384
69.869
45.847
12.889
1.00
22.86

C


ATOM
2045
CD1
PHE
A
384
70.813
44.828
12.795
1.00
22.67

C


ATOM
2046
CD2
PHE
A
384
69.606
46.407
14.139
1.00
22.33

C


ATOM
2047
CE1
PHE
A
384
71.487
44.369
13.929
1.00
22.64

C


ATOM
2048
CE2
PHE
A
384
70.272
45.958
15.281
1.00
21.84

C


ATOM
2049
CZ
PHE
A
384
71.216
44.936
15.176
1.00
22.26

C


ATOM
2050
N
ALA
A
385
68.629
48.395
9.138
1.00
24.36

N


ATOM
2051
CA
ALA
A
385
67.904
48.612
7.889
1.00
26.01

C


ATOM
2052
C
ALA
A
385
68.839
48.544
6.679
1.00
26.76

C


ATOM
2053
O
ALA
A
385
68.424
48.166
5.588
1.00
27.26

O


ATOM
2054
CB
ALA
A
385
67.193
49.964
7.927
1.00
25.65

C


ATOM
2055
N
ARG
A
386
70.102
48.908
6.891
1.00
28.04

N


ATOM
2056
CA
ARG
A
386
71.119
48.915
5.837
1.00
28.74

C


ATOM
2057
C
ARG
A
386
71.531
47.529
5.344
1.00
28.88

C


ATOM
2058
O
ARG
A
386
72.116
47.401
4.267
1.00
29.00

O


ATOM
2059
CB
ARG
A
386
72.390
49.612
6.331
1.00
29.46

C


ATOM
2060
CG
ARG
A
386
72.241
51.044
6.813
1.00
31.77

C


ATOM
2061
CD
ARG
A
386
73.547
51.470
7.482
1.00
32.99

C


ATOM
2062
NE
ARG
A
386
73.922
50.500
8.508
1.00
34.12

N


ATOM
2063
CZ
ARG
A
386
75.170
50.218
8.871
1.00
34.01

C


ATOM
2064
NH1
ARG
A
386
76.197
50.830
8.294
1.00
33.31

N


ATOM
2065
NH2
ARG
A
386
75.388
49.313
9.813
1.00
34.05

N


ATOM
2066
N
PHE
A
387
71.239
46.495
6.127
1.00
28.95

N


ATOM
2067
CA
PHE
A
387
71.649
45.146
5.763
1.00
28.84

C


ATOM
2068
C
PHE
A
387
70.775
44.388
4.777
1.00
29.75

C


ATOM
2069
O
PHE
A
387
69.581
44.642
4.641
1.00
29.59

O


ATOM
2070
CB
PHE
A
387
71.833
44.289
7.021
1.00
28.17

C


ATOM
2071
CG
PHE
A
387
72.742
44.904
8.050
1.00
28.00

C


ATOM
2072
CD1
PHE
A
387
73.851
45.655
7.663
1.00
27.77

C


ATOM
2073
CD2
PHE
A
387
72.499
44.723
9.408
1.00
27.53

C


ATOM
2074
CE1
PHE
A
387
74.703
46.218
8.617
1.00
27.95

C


ATOM
2075
CE2
PHE
A
387
73.346
45.282
10.370
1.00
26.97

C


ATOM
2076
CZ
PHE
A
387
74.445
46.029
9.976
1.00
27.00

C


ATOM
2077
N
GLU
A
388
71.412
43.441
4.100
1.00
30.90

N


ATOM
2078
CA
GLU
A
388
70.773
42.585
3.112
1.00
32.08

C


ATOM
2079
C
GLU
A
388
69.544
41.898
3.691
1.00
31.92

C


ATOM
2080
O
GLU
A
388
68.539
41.713
3.001
1.00
31.55

O


ATOM
2081
CB
GLU
A
388
71.778
41.529
2.647
1.00
33.36

C


ATOM
2082
CG
GLU
A
388
71.235
40.528
1.647
1.00
37.10

C


ATOM
2083
CD
GLU
A
388
70.777
41.189
0.367
1.00
38.82

C


ATOM
2084
OE1
GLU
A
388
71.594
41.898
−0.258
1.00
40.61

O


ATOM
2085
OE2
GLU
A
388
69.604
41.000
−0.015
1.00
41.01

O


ATOM
2086
N
GLU
A
389
69.626
41.532
4.967
1.00
31.81

N


ATOM
2087
CA
GLU
A
389
68.534
40.837
5.633
1.00
31.88

C


ATOM
2088
C
GLU
A
389
67.315
41.667
6.027
1.00
31.91

C


ATOM
2089
O
GLU
A
389
66.307
41.103
6.442
1.00
31.96

O


ATOM
2090
CB
GLU
A
389
69.064
40.090
6.863
1.00
31.96

C


ATOM
2091
CG
GLU
A
389
70.092
39.016
6.523
1.00
31.96

C


ATOM
2092
CD
GLU
A
389
71.527
39.515
6.568
1.00
31.52

C


ATOM
2093
OE1
GLU
A
389
71.764
40.735
6.447
1.00
32.44

O


ATOM
2094
OE2
GLU
A
389
72.431
38.676
6.715
1.00
32.19

O


ATOM
2095
N
SER
A
390
67.385
42.991
5.920
1.00
32.24

N


ATOM
2096
CA
SER
A
390
66.215
43.792
6.270
1.00
33.25

C


ATOM
2097
C
SER
A
390
65.147
43.453
5.218
1.00
34.01

C


ATOM
2098
O
SER
A
390
65.474
43.169
4.064
1.00
33.38

O


ATOM
2099
CB
SER
A
390
66.544
45.290
6.264
1.00
33.16

C


ATOM
2100
OG
SER
A
390
66.764
45.776
4.954
1.00
34.84

O


ATOM
2101
N
PRO
A
391
63.860
43.484
5.604
1.00
34.79

N


ATOM
2102
CA
PRO
A
391
62.737
43.165
4.713
1.00
35.94

C


ATOM
2103
C
PRO
A
391
62.322
44.209
3.681
1.00
37.25

C


ATOM
2104
O
PRO
A
391
61.208
44.153
3.167
1.00
38.09

O


ATOM
2105
CB
PRO
A
391
61.611
42.883
5.697
1.00
35.46

C


ATOM
2106
CG
PRO
A
391
61.850
43.944
6.725
1.00
34.53

C


ATOM
2107
CD
PRO
A
391
63.363
43.892
6.933
1.00
34.40

C


ATOM
2108
N
THR
A
392
63.196
45.157
3.373
1.00
38.30

N


ATOM
2109
CA
THR
A
392
62.849
46.185
2.403
1.00
39.78

C


ATOM
2110
C
THR
A
392
63.551
45.958
1.072
1.00
41.04

C


ATOM
2111
O
THR
A
392
64.460
45.131
0.969
1.00
40.81

O


ATOM
2112
CB
THR
A
392
63.210
47.581
2.920
1.00
39.64

C


ATOM
2113
OG1
THR
A
392
64.629
47.674
3.085
1.00
40.34

O


ATOM
2114
CG2
THR
A
392
62.528
47.844
4.259
1.00
39.79

C


ATOM
2115
N
ARG
A
393
63.122
46.697
0.055
1.00
42.49

N


ATOM
2116
CA
ARG
A
393
63.707
46.566
−1.271
1.00
44.24

C


ATOM
2117
C
ARG
A
393
65.072
47.214
−1.372
1.00
44.65

C


ATOM
2118
O
ARG
A
393
65.306
48.298
−0.834
1.00
44.87

O


ATOM
2119
CB
ARG
A
393
62.806
47.196
−2.337
1.00
45.06

C


ATOM
2120
CG
ARG
A
393
61.425
46.587
−2.464
1.00
46.87

C


ATOM
2121
CD
ARG
A
393
60.966
46.622
−3.919
1.00
48.41

C


ATOM
2122
NE
ARG
A
393
61.374
47.850
−4.597
1.00
49.42

N


ATOM
2123
CZ
ARG
A
393
60.971
49.068
−4.253
1.00
49.97

C


ATOM
2124
NH1
ARG
A
393
60.138
49.231
−3.233
1.00
50.58

N


ATOM
2125
NH2
ARG
A
393
61.410
50.125
−4.925
1.00
50.50

N


ATOM
2126
N
LYS
A
394
65.973
46.535
−2.069
1.00
45.28

N


ATOM
2127
CA
LYS
A
394
67.309
47.056
−2.296
1.00
46.21

C


ATOM
2128
C
LYS
A
394
67.171
47.833
−3.598
1.00
46.79

C


ATOM
2129
O
LYS
A
394
66.911
47.242
−4.645
1.00
47.04

O


ATOM
2130
CB
LYS
A
394
68.304
45.913
−2.478
1.00
45.89

C


ATOM
2131
CG
LYS
A
394
69.744
46.366
−2.558
1.00
46.14

C


ATOM
2132
CD
LYS
A
394
70.649
45.254
−3.055
1.00
46.46

C


ATOM
2133
CE
LYS
A
394
70.618
44.049
−2.140
1.00
46.54

C


ATOM
2134
NZ
LYS
A
394
71.498
42.968
−2.658
1.00
46.60

N


ATOM
2135
N
VAL
A
395
67.316
49.151
−3.533
1.00
47.31

N


ATOM
2136
CA
VAL
A
395
67.183
49.977
−4.726
1.00
48.01

C


ATOM
2137
C
VAL
A
395
68.489
50.671
−5.078
1.00
48.58

C


ATOM
2138
O
VAL
A
395
69.209
51.136
−4.197
1.00
48.67

O


ATOM
2139
CB
VAL
A
395
66.086
51.049
−4.543
1.00
48.06

C


ATOM
2140
CG1
VAL
A
395
64.757
50.379
−4.223
1.00
48.03

C


ATOM
2141
CG2
VAL
A
395
66.473
52.014
−3.435
1.00
47.99

C


ATOM
2142
N
THR
A
396
68.792
50.736
−6.370
1.00
49.08

N


ATOM
2143
CA
THR
A
396
70.014
51.380
−6.831
1.00
49.73

C


ATOM
2144
C
THR
A
396
69.691
52.708
−7.493
1.00
50.27

C


ATOM
2145
O
THR
A
396
69.007
52.759
−8.516
1.00
50.30

O


ATOM
2146
CB
THR
A
396
70.770
50.497
−7.835
1.00
49.70

C


ATOM
2147
OG1
THR
A
396
71.053
49.228
−7.234
1.00
49.67

O


ATOM
2148
CG2
THR
A
396
72.080
51.159
−8.240
1.00
49.85

C


ATOM
2149
N
ILE
A
397
70.192
53.784
−6.899
1.00
50.84

N


ATOM
2150
CA
ILE
A
397
69.953
55.122
−7.416
1.00
51.13

C


ATOM
2151
C
ILE
A
397
71.261
55.795
−7.821
1.00
51.21

C


ATOM
2152
O
ILE
A
397
72.043
56.214
−6.967
1.00
51.47

O


ATOM
2153
CB
ILE
A
397
69.260
56.001
−6.358
1.00
51.32

C


ATOM
2154
CG1
ILE
A
397
68.033
55.276
−5.800
1.00
51.51

C


ATOM
2155
CG2
ILE
A
397
68.855
57.333
−6.977
1.00
51.27

C


ATOM
2156
CD1
ILE
A
397
67.325
56.029
−4.691
1.00
51.49

C


ATOM
2157
N
ASN
A
398
71.497
55.889
−9.126
1.00
51.17

N


ATOM
2158
CA
ASN
A
398
72.702
56.528
−9.644
1.00
50.97

C


ATOM
2159
C
ASN
A
398
73.987
55.852
−9.174
1.00
50.29

C


ATOM
2160
O
ASN
A
398
74.930
56.525
−8.758
1.00
50.58

O


ATOM
2161
CB
ASN
A
398
72.730
58.000
−9.228
1.00
51.92

C


ATOM
2162
CG
ASN
A
398
71.476
58.742
−9.635
1.00
52.91

C


ATOM
2163
OD1
ASN
A
398
71.150
58.827
−10.819
1.00
53.63

O


ATOM
2164
ND2
ASN
A
398
70.761
59.284
−8.654
1.00
53.34

N


ATOM
2165
N
GLY
A
399
74.021
54.526
−9.238
1.00
49.43

N


ATOM
2166
CA
GLY
A
399
75.209
53.801
−8.824
1.00
48.10

C


ATOM
2167
C
GLY
A
399
75.308
53.532
−7.334
1.00
47.22

C


ATOM
2168
O
GLY
A
399
76.228
52.844
−6.887
1.00
47.45

O


ATOM
2169
N
SER
A
400
74.374
54.073
−6.559
1.00
45.83

N


ATOM
2170
CA
SER
A
400
74.387
53.864
−5.115
1.00
44.44

C


ATOM
2171
C
SER
A
400
73.287
52.916
−4.674
1.00
43.04

C


ATOM
2172
O
SER
A
400
72.100
53.221
−4.793
1.00
42.88

O


ATOM
2173
CB
SER
A
400
74.243
55.195
−4.373
1.00
44.67

C


ATOM
2174
OG
SER
A
400
75.455
55.926
−4.407
1.00
45.51

O


ATOM
2175
N
VAL
A
401
73.692
51.757
−4.167
1.00
41.55

N


ATOM
2176
CA
VAL
A
401
72.739
50.768
−3.697
1.00
40.15

C


ATOM
2177
C
VAL
A
401
72.251
51.225
−2.328
1.00
39.84

C


ATOM
2178
O
VAL
A
401
73.046
51.445
−1.413
1.00
39.36

O


ATOM
2179
CB
VAL
A
401
73.395
49.375
−3.599
1.00
39.80

C


ATOM
2180
CG1
VAL
A
401
72.386
48.348
−3.117
1.00
38.64

C


ATOM
2181
CG2
VAL
A
401
73.944
48.971
−4.966
1.00
39.24

C


ATOM
2182
N
MET
A
402
70.938
51.387
−2.206
1.00
39.55

N


ATOM
2183
CA
MET
A
402
70.329
51.837
−0.961
1.00
39.09

C


ATOM
2184
C
MET
A
402
69.240
50.864
−0.539
1.00
38.02

C


ATOM
2185
O
MET
A
402
68.872
49.962
−1.289
1.00
37.68

O


ATOM
2186
CB
MET
A
402
69.683
53.213
−1.148
1.00
40.51

C


ATOM
2187
CG
MET
A
402
70.529
54.244
−1.882
1.00
42.23

C


ATOM
2188
SD
MET
A
402
71.952
54.787
−0.942
1.00
45.56

S


ATOM
2189
CE
MET
A
402
71.204
56.039
0.120
1.00
43.68

C


ATOM
2190
N
LYS
A
403
68.734
51.059
0.673
1.00
36.46

N


ATOM
2191
CA
LYS
A
403
67.649
50.250
1.199
1.00
35.41

C


ATOM
2192
C
LYS
A
403
66.641
51.227
1.785
1.00
34.75

C


ATOM
2193
O
LYS
A
403
67.016
52.298
2.265
1.00
34.48

O


ATOM
2194
CB
LYS
A
403
68.153
49.275
2.266
1.00
35.62

C


ATOM
2195
CG
LYS
A
403
69.086
48.205
1.710
1.00
35.12

C


ATOM
2196
CD
LYS
A
403
68.847
46.848
2.346
1.00
35.57

C


ATOM
2197
CE
LYS
A
403
67.466
46.315
2.009
1.00
35.05

C


ATOM
2198
NZ
LYS
A
403
67.242
44.936
2.521
1.00
33.99

N


ATOM
2199
N
GLU
A
404
65.364
50.869
1.727
1.00
34.23

N


ATOM
2200
CA
GLU
A
404
64.305
51.734
2.235
1.00
34.40

C


ATOM
2201
C
GLU
A
404
64.259
51.735
3.754
1.00
33.56

C


ATOM
2202
O
GLU
A
404
64.590
50.740
4.394
1.00
33.40

O


ATOM
2203
CB
GLU
A
404
62.947
51.268
1.718
1.00
35.68

C


ATOM
2204
CG
GLU
A
404
62.879
51.034
0.225
1.00
38.04

C


ATOM
2205
CD
GLU
A
404
61.547
50.453
−0.193
1.00
39.70

C


ATOM
2206
OE1
GLU
A
404
61.264
49.284
0.159
1.00
40.89

O


ATOM
2207
OE2
GLU
A
404
60.778
51.171
−0.864
1.00
40.74

O


ATOM
2208
N
TYR
A
405
63.833
52.855
4.325
1.00
32.74

N


ATOM
2209
CA
TYR
A
405
63.714
52.975
5.770
1.00
32.04

C


ATOM
2210
C
TYR
A
405
62.665
54.027
6.092
1.00
31.67

C


ATOM
2211
O
TYR
A
405
62.782
55.179
5.677
1.00
32.05

O


ATOM
2212
CB
TYR
A
405
65.059
53.365
6.392
1.00
31.13

C


ATOM
2213
CG
TYR
A
405
65.049
53.387
7.905
1.00
30.72

C


ATOM
2214
CD1
TYR
A
405
64.643
52.269
8.636
1.00
29.79

C


ATOM
2215
CD2
TYR
A
405
65.451
54.523
8.607
1.00
29.90

C


ATOM
2216
CE1
TYR
A
405
64.638
52.282
10.033
1.00
30.48

C


ATOM
2217
CE2
TYR
A
405
65.449
54.546
10.001
1.00
30.64

C


ATOM
2218
CZ
TYR
A
405
65.041
53.423
10.707
1.00
30.22

C


ATOM
2219
OH
TYR
A
405
65.029
53.448
12.085
1.00
30.03

O


ATOM
2220
N
TRP
A
406
61.632
53.627
6.822
1.00
31.08

N


ATOM
2221
CA
TRP
A
406
60.574
54.555
7.186
1.00
30.89

C


ATOM
2222
C
TRP
A
406
60.134
54.345
8.629
1.00
31.03

C


ATOM
2223
O
TRP
A
406
60.190
53.231
9.150
1.00
30.22

O


ATOM
2224
CB
TRP
A
406
59.384
54.401
6.227
1.00
29.70

C


ATOM
2225
CG
TRP
A
406
58.715
53.059
6.267
1.00
28.77

C


ATOM
2226
CD1
TRP
A
406
57.695
52.675
7.090
1.00
28.91

C


ATOM
2227
CD2
TRP
A
406
59.018
51.924
5.448
1.00
28.70

C


ATOM
2228
NE1
TRP
A
406
57.342
51.374
6.833
1.00
29.02

N


ATOM
2229
CE2
TRP
A
406
58.139
50.887
5.831
1.00
28.47

C


ATOM
2230
CE3
TRP
A
406
59.947
51.681
4.426
1.00
28.73

C


ATOM
2231
CZ2
TRP
A
406
58.158
49.624
5.228
1.00
28.64

C


ATOM
2232
CZ3
TRP
A
406
59.967
50.423
3.825
1.00
29.12

C


ATOM
2233
CH2
TRP
A
406
59.075
49.411
4.231
1.00
29.01

C


ATOM
2234
N
GLY
A
407
59.708
55.428
9.270
1.00
31.77

N


ATOM
2235
CA
GLY
A
407
59.270
55.349
10.652
1.00
32.35

C


ATOM
2236
C
GLY
A
407
57.927
54.665
10.816
1.00
32.51

C


ATOM
2237
O
GLY
A
407
57.124
54.619
9.887
1.00
32.50

O


ATOM
2238
N
GLU
A
408
57.685
54.125
12.005
1.00
32.68

N


ATOM
2239
CA
GLU
A
408
56.428
53.450
12.296
1.00
32.74

C


ATOM
2240
C
GLU
A
408
55.302
54.465
12.443
1.00
33.30

C


ATOM
2241
O
GLU
A
408
54.127
54.106
12.447
1.00
33.00

O


ATOM
2242
CB
GLU
A
408
56.562
52.625
13.576
1.00
32.42

C


ATOM
2243
CG
GLU
A
408
57.342
51.343
13.382
1.00
32.27

C


ATOM
2244
CD
GLU
A
408
56.618
50.373
12.460
1.00
32.10

C


ATOM
2245
OE1
GLU
A
408
55.511
49.930
12.824
1.00
31.95

O


ATOM
2246
OE2
GLU
A
408
57.149
50.059
11.376
1.00
31.80

O


ATOM
2247
N
GLY
A
409
55.670
55.736
12.563
1.00
34.53

N


ATOM
2248
CA
GLY
A
409
54.677
56.784
12.702
1.00
36.36

C


ATOM
2249
C
GLY
A
409
54.250
57.358
11.362
1.00
37.80

C


ATOM
2250
O
GLY
A
409
53.313
58.148
11.291
1.00
37.85

O


ATOM
2251
N
SER
A
410
54.934
56.965
10.293
1.00
39.37

N


ATOM
2252
CA
SER
A
410
54.598
57.462
8.963
1.00
41.45

C


ATOM
2253
C
SER
A
410
53.291
56.839
8.485
1.00
43.20

C


ATOM
2254
O
SER
A
410
52.945
55.723
8.876
1.00
42.83

O


ATOM
2255
CB
SER
A
410
55.715
57.135
7.971
1.00
40.60

C


ATOM
2256
OG
SER
A
410
55.795
55.740
7.738
1.00
40.47

O


ATOM
2257
N
SER
A
411
52.564
57.566
7.642
1.00
45.39

N


ATOM
2258
CA
SER
A
411
51.300
57.065
7.120
1.00
47.54

C


ATOM
2259
C
SER
A
411
51.556
55.777
6.347
1.00
48.82

C


ATOM
2260
O
SER
A
411
50.699
54.897
6.287
1.00
48.87

O


ATOM
2261
CB
SER
A
411
50.642
58.113
6.212
1.00
47.83

C


ATOM
2262
OG
SER
A
411
51.518
58.534
5.180
1.00
48.13

O


ATOM
2263
N
ARG
A
412
52.750
55.669
5.770
1.00
50.57

N


ATOM
2264
CA
ARG
A
412
53.125
54.483
5.009
1.00
52.38

C


ATOM
2265
C
ARG
A
412
53.169
53.244
5.895
1.00
53.64

C


ATOM
2266
O
ARG
A
412
52.940
52.130
5.426
1.00
53.63

O


ATOM
2267
CB
ARG
A
412
54.495
54.677
4.351
1.00
52.24

C


ATOM
2268
CG
ARG
A
412
55.008
53.420
3.652
1.00
52.42

C


ATOM
2269
CD
ARG
A
412
56.351
53.628
2.971
1.00
52.24

C


ATOM
2270
NE
ARG
A
412
56.789
52.412
2.286
1.00
52.01

N


ATOM
2271
CZ
ARG
A
412
57.920
52.298
1.596
1.00
52.09

C


ATOM
2272
NH1
ARG
A
412
58.747
53.329
1.487
1.00
51.74

N


ATOM
2273
NH2
ARG
A
412
58.226
51.145
1.014
1.00
52.05

N


ATOM
2274
N
ALA
A
413
53.465
53.445
7.176
1.00
55.35

N


ATOM
2275
CA
ALA
A
413
53.555
52.344
8.128
1.00
57.35

C


ATOM
2276
C
ALA
A
413
52.196
51.934
8.682
1.00
58.87

C


ATOM
2277
O
ALA
A
413
51.760
50.799
8.501
1.00
58.87

O


ATOM
2278
CB
ALA
A
413
54.483
52.725
9.278
1.00
56.92

C


ATOM
2279
N
ARG
A
414
51.532
52.858
9.368
1.00
61.25

N


ATOM
2280
CA
ARG
A
414
50.232
52.558
9.945
1.00
63.66

C


ATOM
2281
C
ARG
A
414
49.102
52.862
8.968
1.00
64.89

C


ATOM
2282
O
ARG
A
414
48.824
54.018
8.648
1.00
65.40

O


ATOM
2283
CB
ARG
A
414
50.040
53.330
11.259
1.00
64.13

C


ATOM
2284
CG
ARG
A
414
50.007
54.843
11.139
1.00
65.06

C


ATOM
2285
CD
ARG
A
414
49.833
55.477
12.511
1.00
65.70

C


ATOM
2286
NE
ARG
A
414
49.344
56.850
12.427
1.00
66.48

N


ATOM
2287
CZ
ARG
A
414
49.075
57.614
13.481
1.00
66.77

C


ATOM
2288
NH1
ARG
A
414
49.250
57.143
14.709
1.00
66.88

N


ATOM
2289
NH2
ARG
A
414
48.615
58.846
13.311
1.00
67.02

N


ATOM
2290
N
ASN
A
415
48.467
51.799
8.486
1.00
66.35

N


ATOM
2291
CA
ASN
A
415
47.361
51.907
7.542
1.00
67.56

C


ATOM
2292
C
ASN
A
415
46.837
50.495
7.276
1.00
67.89

C


ATOM
2293
O
ASN
A
415
46.002
50.282
6.397
1.00
68.21

O


ATOM
2294
CB
ASN
A
415
47.840
52.552
6.233
1.00
68.15

C


ATOM
2295
CG
ASN
A
415
46.701
53.155
5.418
1.00
68.99

C


ATOM
2296
OD1
ASN
A
415
45.788
52.454
4.978
1.00
69.44

O


ATOM
2297
ND2
ASN
A
415
46.756
54.466
5.215
1.00
69.28

N


ATOM
2298
N
TRP
A
416
47.343
49.534
8.045
1.00
68.11

N


ATOM
2299
CA
TRP
A
416
46.932
48.140
7.915
1.00
68.12

C


ATOM
2300
C
TRP
A
416
45.656
47.901
8.719
1.00
68.17

C


ATOM
2301
O
TRP
A
416
44.616
47.529
8.171
1.00
68.31

O


ATOM
2302
CB
TRP
A
416
48.040
47.209
8.424
1.00
68.13

C


ATOM
2303
CG
TRP
A
416
48.339
47.382
9.886
1.00
67.91

C


ATOM
2304
CD1
TRP
A
416
49.047
48.397
10.465
1.00
67.92

C


ATOM
2305
CD2
TRP
A
416
47.868
46.558
10.960
1.00
67.76

C


ATOM
2306
NE1
TRP
A
416
49.040
48.259
11.834
1.00
67.80

N


ATOM
2307
CE2
TRP
A
416
48.323
47.139
12.164
1.00
67.78

C


ATOM
2308
CE3
TRP
A
416
47.101
45.388
11.021
1.00
67.62

C


ATOM
2309
CZ2
TRP
A
416
48.036
46.588
13.419
1.00
67.74

C


ATOM
2310
CZ3
TRP
A
416
46.815
44.839
12.268
1.00
67.75

C


ATOM
2311
CH2
TRP
A
416
47.282
45.441
13.450
1.00
67.77

C


ATOM
2312
N
GLU
A
430
49.118
63.275
11.644
1.00
73.03

N


ATOM
2313
CA
GLU
A
430
50.037
62.232
12.086
1.00
72.84

C


ATOM
2314
C
GLU
A
430
51.464
62.554
11.659
1.00
72.49

C


ATOM
2315
O
GLU
A
430
51.709
63.560
10.992
1.00
72.57

O


ATOM
2316
CB
GLU
A
430
49.622
60.882
11.499
1.00
73.23

C


ATOM
2317
CG
GLU
A
430
49.699
60.809
9.981
1.00
73.60

C


ATOM
2318
CD
GLU
A
430
49.250
59.466
9.439
1.00
73.90

C


ATOM
2319
OE1
GLU
A
430
49.840
58.437
9.831
1.00
73.94

O


ATOM
2320
OE2
GLU
A
430
48.308
59.439
8.619
1.00
74.25

O


ATOM
2321
N
GLU
A
431
52.403
61.695
12.046
1.00
71.87

N


ATOM
2322
CA
GLU
A
431
53.803
61.891
11.692
1.00
71.10

C


ATOM
2323
C
GLU
A
431
54.066
61.249
10.333
1.00
70.43

C


ATOM
2324
O
GLU
A
431
53.136
60.792
9.666
1.00
70.43

O


ATOM
2325
CB
GLU
A
431
54.714
61.254
12.744
1.00
71.29

C


ATOM
2326
CG
GLU
A
431
56.138
61.783
12.716
1.00
71.71

C


ATOM
2327
CD
GLU
A
431
57.111
60.917
13.493
1.00
71.87

C


ATOM
2328
OE1
GLU
A
431
56.854
60.632
14.684
1.00
72.06

O


ATOM
2329
OE2
GLU
A
431
58.141
60.528
12.907
1.00
71.88

O


ATOM
2330
N
GLY
A
432
55.331
61.211
9.926
1.00
69.40

N


ATOM
2331
CA
GLY
A
432
55.667
60.614
8.647
1.00
67.99

C


ATOM
2332
C
GLY
A
432
57.101
60.847
8.215
1.00
66.90

C


ATOM
2333
O
GLY
A
432
57.524
61.987
8.030
1.00
67.35

O


ATOM
2334
N
VAL
A
433
57.853
59.763
8.054
1.00
65.49

N


ATOM
2335
CA
VAL
A
433
59.246
59.851
7.631
1.00
63.66

C


ATOM
2336
C
VAL
A
433
59.611
58.651
6.760
1.00
62.12

C


ATOM
2337
O
VAL
A
433
59.537
57.503
7.200
1.00
61.66

O


ATOM
2338
CB
VAL
A
433
60.198
59.891
8.840
1.00
64.04

C


ATOM
2339
CG1
VAL
A
433
61.624
60.100
8.366
1.00
64.18

C


ATOM
2340
CG2
VAL
A
433
59.784
60.994
9.797
1.00
64.08

C


ATOM
2341
N
ASP
A
434
60.008
58.930
5.522
1.00
60.25

N


ATOM
2342
CA
ASP
A
434
60.377
57.892
4.566
1.00
58.26

C


ATOM
2343
C
ASP
A
434
61.718
58.280
3.947
1.00
56.78

C


ATOM
2344
O
ASP
A
434
61.881
59.405
3.475
1.00
56.70

O


ATOM
2345
CB
ASP
A
434
59.311
57.805
3.470
1.00
58.76

C


ATOM
2346
CG
ASP
A
434
59.280
56.456
2.783
1.00
58.92

C


ATOM
2347
OD1
ASP
A
434
60.357
55.902
2.487
1.00
59.73

O


ATOM
2348
OD2
ASP
A
434
58.168
55.955
2.525
1.00
59.23

O


ATOM
2349
N
SER
A
435
62.676
57.359
3.944
1.00
54.66

N


ATOM
2350
CA
SER
A
435
63.988
57.664
3.382
1.00
52.26

C


ATOM
2351
C
SER
A
435
64.779
56.437
2.938
1.00
50.24

C


ATOM
2352
O
SER
A
435
64.263
55.319
2.913
1.00
49.77

O


ATOM
2353
CB
SER
A
435
64.815
58.454
4.400
1.00
52.83

C


ATOM
2354
OG
SER
A
435
65.010
57.701
5.586
1.00
53.50

O


ATOM
2355
N
TYR
A
436
66.040
56.668
2.586
1.00
47.86

N


ATOM
2356
CA
TYR
A
436
66.935
55.609
2.140
1.00
45.83

C


ATOM
2357
C
TYR
A
436
68.198
55.593
2.993
1.00
43.91

C


ATOM
2358
O
TYR
A
436
68.622
56.626
3.513
1.00
43.83

O


ATOM
2359
CB
TYR
A
436
67.333
55.825
0.677
1.00
46.59

C


ATOM
2360
CG
TYR
A
436
66.196
55.715
−0.312
1.00
47.13

C


ATOM
2361
CD1
TYR
A
436
65.599
54.485
−0.585
1.00
47.53

C


ATOM
2362
CD2
TYR
A
436
65.713
56.843
−0.974
1.00
47.79

C


ATOM
2363
CE1
TYR
A
436
64.547
54.380
−1.493
1.00
48.14

C


ATOM
2364
CE2
TYR
A
436
64.661
56.751
−1.882
1.00
48.43

C


ATOM
2365
CZ
TYR
A
436
64.083
55.517
−2.136
1.00
48.48

C


ATOM
2366
OH
TYR
A
436
63.036
55.424
−3.024
1.00
49.29

O


ATOM
2367
N
VAL
A
437
68.786
54.412
3.140
1.00
41.44

N


ATOM
2368
CA
VAL
A
437
70.018
54.251
3.901
1.00
39.25

C


ATOM
2369
C
VAL
A
437
70.997
53.500
3.010
1.00
37.73

C


ATOM
2370
O
VAL
A
437
70.604
52.608
2.261
1.00
37.14

O


ATOM
2371
CB
VAL
A
437
69.786
53.455
5.209
1.00
38.97

C


ATOM
2372
CG1
VAL
A
437
68.841
54.225
6.119
1.00
39.50

C


ATOM
2373
CG2
VAL
A
437
69.221
52.084
4.901
1.00
38.52

C


ATOM
2374
N
PRO
A
438
72.289
53.852
3.075
1.00
37.00

N


ATOM
2375
CA
PRO
A
438
73.280
53.169
2.239
1.00
35.94

C


ATOM
2376
C
PRO
A
438
73.390
51.682
2.547
1.00
34.96

C


ATOM
2377
O
PRO
A
438
73.442
51.282
3.710
1.00
34.43

O


ATOM
2378
CB
PRO
A
438
74.569
53.929
2.543
1.00
36.50

C


ATOM
2379
CG
PRO
A
438
74.377
54.345
3.981
1.00
37.42

C


ATOM
2380
CD
PRO
A
438
72.935
54.813
3.988
1.00
37.02

C


ATOM
2381
N
TYR
A
439
73.412
50.872
1.492
1.00
33.53

N


ATOM
2382
CA
TYR
A
439
73.526
49.423
1.619
1.00
32.47

C


ATOM
2383
C
TYR
A
439
74.858
49.089
2.284
1.00
31.86

C


ATOM
2384
O
TYR
A
439
75.881
49.681
1.959
1.00
31.19

O


ATOM
2385
CB
TYR
A
439
73.459
48.778
0.232
1.00
31.92

C


ATOM
2386
CG
TYR
A
439
73.590
47.273
0.230
1.00
31.72

C


ATOM
2387
CD1
TYR
A
439
72.683
46.476
0.925
1.00
31.68

C


ATOM
2388
CD2
TYR
A
439
74.601
46.643
−0.497
1.00
31.71

C


ATOM
2389
CE1
TYR
A
439
72.775
45.087
0.896
1.00
32.18

C


ATOM
2390
CE2
TYR
A
439
74.702
45.254
−0.533
1.00
32.39

C


ATOM
2391
CZ
TYR
A
439
73.784
44.484
0.165
1.00
32.74

C


ATOM
2392
OH
TYR
A
439
73.863
43.112
0.124
1.00
34.28

O


ATOM
2393
N
ALA
A
440
74.847
48.133
3.208
1.00
31.96

N


ATOM
2394
CA
ALA
A
440
76.070
47.765
3.913
1.00
32.22

C


ATOM
2395
C
ALA
A
440
76.429
46.297
3.758
1.00
32.05

C


ATOM
2396
O
ALA
A
440
77.465
45.856
4.244
1.00
32.90

O


ATOM
2397
CB
ALA
A
440
75.938
48.115
5.396
1.00
31.52

C


ATOM
2398
N
GLY
A
441
75.577
45.538
3.080
1.00
32.08

N


ATOM
2399
CA
GLY
A
441
75.857
44.127
2.899
1.00
32.00

C


ATOM
2400
C
GLY
A
441
75.250
43.262
3.991
1.00
32.35

C


ATOM
2401
O
GLY
A
441
74.248
43.639
4.602
1.00
31.44

O


ATOM
2402
N
LYS
A
442
75.867
42.106
4.231
1.00
32.08

N


ATOM
2403
CA
LYS
A
442
75.411
41.147
5.235
1.00
32.60

C


ATOM
2404
C
LYS
A
442
75.531
41.671
6.664
1.00
31.49

C


ATOM
2405
O
LYS
A
442
76.495
42.350
7.012
1.00
31.52

O


ATOM
2406
CB
LYS
A
442
76.216
39.848
5.129
1.00
34.46

C


ATOM
2407
CG
LYS
A
442
76.072
39.097
3.814
1.00
37.78

C


ATOM
2408
CD
LYS
A
442
74.734
38.377
3.714
1.00
39.58

C


ATOM
2409
CE
LYS
A
442
74.725
37.415
2.527
1.00
41.54

C


ATOM
2410
NZ
LYS
A
442
73.453
36.640
2.425
1.00
42.55

N


ATOM
2411
N
LEU
A
443
74.548
41.332
7.491
1.00
30.52

N


ATOM
2412
CA
LEU
A
443
74.538
41.751
8.887
1.00
29.23

C


ATOM
2413
C
LEU
A
443
75.790
41.271
9.624
1.00
29.23

C


ATOM
2414
O
LEU
A
443
76.430
42.040
10.343
1.00
28.36

O


ATOM
2415
CB
LEU
A
443
73.281
41.208
9.582
1.00
28.43

C


ATOM
2416
CG
LEU
A
443
73.124
41.454
11.087
1.00
28.11

C


ATOM
2417
CD1
LEU
A
443
71.648
41.409
11.471
1.00
27.84

C


ATOM
2418
CD2
LEU
A
443
73.920
40.408
11.863
1.00
28.16

C


ATOM
2419
N
LYS
A
444
76.136
40.003
9.423
1.00
29.23

N


ATOM
2420
CA
LYS
A
444
77.282
39.382
10.083
1.00
30.71

C


ATOM
2421
C
LYS
A
444
78.583
40.179
10.103
1.00
30.91

C


ATOM
2422
O
LYS
A
444
79.124
40.453
11.174
1.00
30.45

O


ATOM
2423
CB
LYS
A
444
77.562
38.002
9.477
1.00
31.85

C


ATOM
2424
CG
LYS
A
444
78.712
37.262
10.164
1.00
34.22

C


ATOM
2425
CD
LYS
A
444
78.908
35.868
9.587
1.00
36.27

C


ATOM
2426
CE
LYS
A
444
80.016
35.126
10.314
1.00
37.68

C


ATOM
2427
NZ
LYS
A
444
81.325
35.828
10.197
1.00
38.57

N


ATOM
2428
N
ASP
A
445
79.087
40.542
8.927
1.00
30.82

N


ATOM
2429
CA
ASP
A
445
80.344
41.280
8.829
1.00
31.15

C


ATOM
2430
C
ASP
A
445
80.303
42.662
9.462
1.00
30.19

C


ATOM
2431
O
ASP
A
445
81.296
43.125
10.022
1.00
29.83

O


ATOM
2432
CB
ASP
A
445
80.757
41.412
7.363
1.00
33.63

C


ATOM
2433
CG
ASP
A
445
80.781
40.079
6.650
1.00
35.59

C


ATOM
2434
OD1
ASP
A
445
81.474
39.158
7.136
1.00
36.48

O


ATOM
2435
OD2
ASP
A
445
80.102
39.953
5.610
1.00
37.86

O


ATOM
2436
N
ASN
A
446
79.157
43.321
9.366
1.00
28.50

N


ATOM
2437
CA
ASN
A
446
79.005
44.657
9.922
1.00
28.18

C


ATOM
2438
C
ASN
A
446
78.957
44.660
11.450
1.00
27.76

C


ATOM
2439
O
ASN
A
446
79.575
45.506
12.092
1.00
27.67

O


ATOM
2440
CB
ASN
A
446
77.750
45.306
9.347
1.00
28.54

C


ATOM
2441
CG
ASN
A
446
77.938
45.755
7.909
1.00
28.71

C


ATOM
2442
OD1
ASN
A
446
78.508
46.815
7.652
1.00
29.83

O


ATOM
2443
ND2
ASN
A
446
77.473
44.945
6.967
1.00
27.87

N


ATOM
2444
N
VAL
A
447
78.222
43.714
12.023
1.00
27.34

N


ATOM
2445
CA
VAL
A
447
78.105
43.600
13.474
1.00
27.67

C


ATOM
2446
C
VAL
A
447
79.461
43.220
14.071
1.00
28.37

C


ATOM
2447
O
VAL
A
447
79.878
43.770
15.088
1.00
28.42

O


ATOM
2448
CB
VAL
A
447
77.043
42.542
13.850
1.00
27.28

C


ATOM
2449
CG1
VAL
A
447
77.154
42.172
15.324
1.00
26.67

C


ATOM
2450
CG2
VAL
A
447
75.657
43.091
13.553
1.00
26.56

C


ATOM
2451
N
GLU
A
448
80.151
42.287
13.426
1.00
28.89

N


ATOM
2452
CA
GLU
A
448
81.464
41.861
13.897
1.00
30.04

C


ATOM
2453
C
GLU
A
448
82.412
43.061
13.971
1.00
29.13

C


ATOM
2454
O
GLU
A
448
83.127
43.239
14.960
1.00
28.39

O


ATOM
2455
CB
GLU
A
448
82.029
40.790
12.959
1.00
32.21

C


ATOM
2456
CG
GLU
A
448
83.451
40.343
13.273
1.00
35.95

C


ATOM
2457
CD
GLU
A
448
83.912
39.210
12.365
1.00
38.46

C


ATOM
2458
OE1
GLU
A
448
83.834
39.364
11.124
1.00
40.14

O


ATOM
2459
OE2
GLU
A
448
84.351
38.163
12.890
1.00
40.41

O


ATOM
2460
N
ALA
A
449
82.404
43.889
12.930
1.00
27.90

N


ATOM
2461
CA
ALA
A
449
83.265
45.069
12.893
1.00
27.67

C


ATOM
2462
C
ALA
A
449
82.870
46.080
13.974
1.00
27.21

C


ATOM
2463
O
ALA
A
449
83.725
46.612
14.685
1.00
26.68

O


ATOM
2464
CB
ALA
A
449
83.203
45.722
11.513
1.00
28.18

C


ATOM
2465
N
SER
A
450
81.573
46.343
14.097
1.00
26.17

N


ATOM
2466
CA
SER
A
450
81.090
47.279
15.105
1.00
26.52

C


ATOM
2467
C
SER
A
450
81.487
46.829
16.511
1.00
26.58

C


ATOM
2468
O
SER
A
450
82.062
47.603
17.281
1.00
26.69

O


ATOM
2469
CB
SER
A
450
79.562
47.408
15.032
1.00
26.11

C


ATOM
2470
OG
SER
A
450
79.154
48.048
13.833
1.00
25.91

O


ATOM
2471
N
LEU
A
451
81.186
45.575
16.839
1.00
25.76

N


ATOM
2472
CA
LEU
A
451
81.490
45.045
18.163
1.00
26.02

C


ATOM
2473
C
LEU
A
451
82.986
44.910
18.450
1.00
26.55

C


ATOM
2474
O
LEU
A
451
83.404
44.961
19.611
1.00
25.99

O


ATOM
2475
CB
LEU
A
451
80.767
43.709
18.372
1.00
25.37

C


ATOM
2476
CG
LEU
A
451
79.238
43.840
18.305
1.00
25.01

C


ATOM
2477
CD1
LEU
A
451
78.586
42.524
18.693
1.00
24.99

C


ATOM
2478
CD2
LEU
A
451
78.773
44.962
19.232
1.00
25.24

C


ATOM
2479
N
ASN
A
452
83.796
44.747
17.407
1.00
26.96

N


ATOM
2480
CA
ASN
A
452
85.240
44.661
17.618
1.00
28.17

C


ATOM
2481
C
ASN
A
452
85.722
46.016
18.133
1.00
27.59

C


ATOM
2482
O
ASN
A
452
86.624
46.094
18.968
1.00
26.76

O


ATOM
2483
CB
ASN
A
452
85.977
44.310
16.320
1.00
30.23

C


ATOM
2484
CG
ASN
A
452
86.089
42.815
16.099
1.00
33.77

C


ATOM
2485
OD1
ASN
A
452
86.244
42.048
17.050
1.00
36.57

O


ATOM
2486
ND2
ASN
A
452
86.034
42.393
14.839
1.00
35.31

N


ATOM
2487
N
LYS
A
453
85.104
47.081
17.632
1.00
27.29

N


ATOM
2488
CA
LYS
A
453
85.453
48.435
18.043
1.00
27.38

C


ATOM
2489
C
LYS
A
453
84.962
48.684
19.465
1.00
26.33

C


ATOM
2490
O
LYS
A
453
85.654
49.305
20.267
1.00
25.74

O


ATOM
2491
CB
LYS
A
453
84.835
49.453
17.076
1.00
29.18

C


ATOM
2492
CG
LYS
A
453
85.374
49.322
15.651
1.00
31.57

C


ATOM
2493
CD
LYS
A
453
84.545
50.103
14.637
1.00
33.43

C


ATOM
2494
CE
LYS
A
453
84.630
51.604
14.856
1.00
34.79

C


ATOM
2495
NZ
LYS
A
453
83.781
52.334
13.861
1.00
35.78

N


ATOM
2496
N
VAL
A
454
83.764
48.197
19.772
1.00
25.19

N


ATOM
2497
CA
VAL
A
454
83.200
48.351
21.104
1.00
24.18

C


ATOM
2498
C
VAL
A
454
84.108
47.638
22.114
1.00
24.77

C


ATOM
2499
O
VAL
A
454
84.455
48.194
23.159
1.00
23.53

O


ATOM
2500
CB
VAL
A
454
81.770
47.741
21.180
1.00
24.45

C


ATOM
2501
CG1
VAL
A
454
81.293
47.691
22.627
1.00
23.62

C


ATOM
2502
CG2
VAL
A
454
80.800
48.574
20.338
1.00
23.76

C


ATOM
2503
N
LYS
A
455
84.501
46.409
21.791
1.00
24.44

N


ATOM
2504
CA
LYS
A
455
85.355
45.634
22.683
1.00
24.98

C


ATOM
2505
C
LYS
A
455
86.728
46.266
22.878
1.00
25.10

C


ATOM
2506
O
LYS
A
455
87.273
46.254
23.984
1.00
24.49

O


ATOM
2507
CB
LYS
A
455
85.477
44.194
22.168
1.00
25.62

C


ATOM
2508
CG
LYS
A
455
84.136
43.465
22.213
1.00
27.11

C


ATOM
2509
CD
LYS
A
455
84.249
41.968
21.985
1.00
28.53

C


ATOM
2510
CE
LYS
A
455
84.339
41.611
20.517
1.00
29.62

C


ATOM
2511
NZ
LYS
A
455
84.059
40.156
20.315
1.00
30.79

N


ATOM
2512
N
SER
A
456
87.282
46.831
21.810
1.00
24.87

N


ATOM
2513
CA
SER
A
456
88.583
47.478
21.895
1.00
26.04

C


ATOM
2514
C
SER
A
456
88.477
48.690
22.831
1.00
25.43

C


ATOM
2515
O
SER
A
456
89.337
48.908
23.689
1.00
25.09

O


ATOM
2516
CB
SER
A
456
89.046
47.920
20.501
1.00
27.09

C


ATOM
2517
OG
SER
A
456
90.355
48.454
20.559
1.00
30.80

O


ATOM
2518
N
THR
A
457
87.414
49.471
22.671
1.00
24.22

N


ATOM
2519
CA
THR
A
457
87.214
50.640
23.520
1.00
24.20

C


ATOM
2520
C
THR
A
457
86.999
50.197
24.968
1.00
23.77

C


ATOM
2521
O
THR
A
457
87.484
50.835
25.900
1.00
23.17

O


ATOM
2522
CB
THR
A
457
86.013
51.470
23.035
1.00
24.69

C


ATOM
2523
OG1
THR
A
457
86.268
51.918
21.699
1.00
25.52

O


ATOM
2524
CG2
THR
A
457
85.791
52.680
23.934
1.00
24.52

C


ATOM
2525
N
MET
A
458
86.285
49.092
25.155
1.00
23.48

N


ATOM
2526
CA
MET
A
458
86.054
48.582
26.500
1.00
23.69

C


ATOM
2527
C
MET
A
458
87.395
48.265
27.160
1.00
23.66

C


ATOM
2528
O
MET
A
458
87.582
48.522
28.351
1.00
23.57

O


ATOM
2529
CB
MET
A
458
85.157
47.339
26.453
1.00
22.39

C


ATOM
2530
CG
MET
A
458
83.680
47.680
26.256
1.00
22.53

C


ATOM
2531
SD
MET
A
458
82.608
46.247
26.043
1.00
23.32

S


ATOM
2532
CE
MET
A
458
82.688
45.515
27.705
1.00
22.32

C


ATOM
2533
N
CYS
A
459
88.332
47.716
26.393
1.00
24.05

N


ATOM
2534
CA
CYS
A
459
89.649
47.413
26.947
1.00
25.56

C


ATOM
2535
C
CYS
A
459
90.409
48.701
27.281
1.00
25.13

C


ATOM
2536
O
CYS
A
459
91.214
48.725
28.215
1.00
24.61

O


ATOM
2537
CB
CYS
A
459
90.465
46.548
25.985
1.00
28.49

C


ATOM
2538
SG
CYS
A
459
90.054
44.772
26.089
1.00
33.40

S


ATOM
2539
N
ASN
A
460
90.160
49.766
26.519
1.00
24.08

N


ATOM
2540
CA
ASN
A
460
90.804
51.047
26.793
1.00
24.35

C


ATOM
2541
C
ASN
A
460
90.302
51.515
28.155
1.00
24.02

C


ATOM
2542
O
ASN
A
460
91.029
52.148
28.915
1.00
23.20

O


ATOM
2543
CB
ASN
A
460
90.412
52.110
25.759
1.00
24.60

C


ATOM
2544
CG
ASN
A
460
91.081
51.909
24.415
1.00
25.78

C


ATOM
2545
OD1
ASN
A
460
90.405
51.787
23.399
1.00
27.02

O


ATOM
2546
ND2
ASN
A
460
92.410
51.889
24.399
1.00
24.46

N


ATOM
2547
N
CYS
A
461
89.042
51.205
28.448
1.00
23.87

N


ATOM
2548
CA
CYS
A
461
88.422
51.611
29.704
1.00
24.41

C


ATOM
2549
C
CYS
A
461
88.660
50.633
30.848
1.00
24.32

C


ATOM
2550
O
CYS
A
461
88.180
50.852
31.958
1.00
25.56

O


ATOM
2551
CB
CYS
A
461
86.918
51.806
29.496
1.00
24.60

C


ATOM
2552
SG
CYS
A
461
86.525
53.116
28.308
1.00
26.96

S


ATOM
2553
N
GLY
A
462
89.389
49.556
30.570
1.00
24.32

N


ATOM
2554
CA
GLY
A
462
89.685
48.558
31.587
1.00
24.60

C


ATOM
2555
C
GLY
A
462
88.547
47.600
31.907
1.00
25.06

C


ATOM
2556
O
GLY
A
462
88.465
47.076
33.024
1.00
24.53

O


ATOM
2557
N
ALA
A
463
87.682
47.343
30.929
1.00
24.46

N


ATOM
2558
CA
ALA
A
463
86.539
46.463
31.147
1.00
24.56

C


ATOM
2559
C
ALA
A
463
86.489
45.254
30.234
1.00
24.52

C


ATOM
2560
O
ALA
A
463
86.647
45.372
29.018
1.00
24.90

O


ATOM
2561
CB
ALA
A
463
85.246
47.257
31.000
1.00
24.47

C


ATOM
2562
N
LEU
A
464
86.246
44.092
30.834
1.00
24.58

N


ATOM
2563
CA
LEU
A
464
86.139
42.840
30.096
1.00
24.71

C


ATOM
2564
C
LEU
A
464
84.683
42.423
29.927
1.00
23.91

C


ATOM
2565
O
LEU
A
464
84.387
41.458
29.224
1.00
24.47

O


ATOM
2566
CB
LEU
A
464
86.887
41.720
30.823
1.00
25.91

C


ATOM
2567
CG
LEU
A
464
88.397
41.634
30.616
1.00
27.36

C


ATOM
2568
CD1
LEU
A
464
88.947
40.476
31.448
1.00
28.44

C


ATOM
2569
CD2
LEU
A
464
88.702
41.420
29.147
1.00
27.33

C


ATOM
2570
N
THR
A
465
83.782
43.131
30.596
1.00
22.92

N


ATOM
2571
CA
THR
A
465
82.354
42.831
30.512
1.00
22.25

C


ATOM
2572
C
THR
A
465
81.568
44.129
30.548
1.00
21.44

C


ATOM
2573
O
THR
A
465
82.104
45.177
30.891
1.00
20.34

O


ATOM
2574
CB
THR
A
465
81.862
41.981
31.699
1.00
22.45

C


ATOM
2575
OG1
THR
A
465
81.932
42.762
32.899
1.00
22.22

O


ATOM
2576
CG2
THR
A
465
82.710
40.726
31.858
1.00
22.79

C


ATOM
2577
N
ILE
A
466
80.288
44.052
30.214
1.00
21.19

N


ATOM
2578
CA
ILE
A
466
79.447
45.236
30.230
1.00
20.76

C


ATOM
2579
C
ILE
A
466
79.254
45.736
31.666
1.00
20.40

C


ATOM
2580
O
ILE
A
466
79.358
46.929
31.927
1.00
19.90

O


ATOM
2581
CB
ILE
A
466
78.098
44.944
29.530
1.00
21.19

C


ATOM
2582
CG1
ILE
A
466
78.356
44.780
28.022
1.00
21.38

C


ATOM
2583
CG2
ILE
A
466
77.100
46.073
29.792
1.00
21.25

C


ATOM
2584
CD1
ILE
A
466
77.152
44.290
27.219
1.00
22.58

C


ATOM
2585
N
PRO
A
467
78.995
44.828
32.626
1.00
20.68

N


ATOM
2586
CA
PRO
A
467
78.822
45.333
33.991
1.00
20.34

C


ATOM
2587
C
PRO
A
467
80.094
46.009
34.510
1.00
21.02

C


ATOM
2588
O
PRO
A
467
80.025
47.006
35.216
1.00
21.23

O


ATOM
2589
CB
PRO
A
467
78.461
44.076
34.782
1.00
20.94

C


ATOM
2590
CG
PRO
A
467
77.717
43.250
33.750
1.00
20.39

C


ATOM
2591
CD
PRO
A
467
78.606
43.411
32.538
1.00
19.76

C


ATOM
2592
N
GLN
A
468
81.259
45.475
34.160
1.00
21.22

N


ATOM
2593
CA
GLN
A
468
82.491
46.093
34.627
1.00
21.96

C


ATOM
2594
C
GLN
A
468
82.648
47.477
33.992
1.00
22.09

C


ATOM
2595
O
GLN
A
468
83.108
48.412
34.644
1.00
22.10

O


ATOM
2596
CB
GLN
A
468
83.709
45.217
34.308
1.00
22.23

C


ATOM
2597
CG
GLN
A
468
85.015
45.839
34.780
1.00
22.84

C


ATOM
2598
CD
GLN
A
468
86.211
44.908
34.692
1.00
22.48

C


ATOM
2599
OE1
GLN
A
468
86.355
44.141
33.740
1.00
22.48

O


ATOM
2600
NE2
GLN
A
468
87.097
44.997
35.683
1.00
22.38

N


ATOM
2601
N
LEU
A
469
82.264
47.603
32.722
1.00
21.64

N


ATOM
2602
CA
LEU
A
469
82.344
48.886
32.027
1.00
21.89

C


ATOM
2603
C
LEU
A
469
81.434
49.905
32.714
1.00
22.01

C


ATOM
2604
O
LEU
A
469
81.818
51.051
32.925
1.00
21.53

O


ATOM
2605
CB
LEU
A
469
81.904
48.735
30.564
1.00
21.51

C


ATOM
2606
CG
LEU
A
469
81.761
50.027
29.745
1.00
22.03

C


ATOM
2607
CD1
LEU
A
469
83.134
50.627
29.484
1.00
21.95

C


ATOM
2608
CD2
LEU
A
469
81.056
49.727
28.414
1.00
22.12

C


ATOM
2609
N
GLN
A
470
80.225
49.473
33.058
1.00
22.00

N


ATOM
2610
CA
GLN
A
470
79.254
50.349
33.696
1.00
23.44

C


ATOM
2611
C
GLN
A
470
79.743
50.838
35.055
1.00
24.51

C


ATOM
2612
O
GLN
A
470
79.377
51.922
35.513
1.00
25.02

O


ATOM
2613
CB
GLN
A
470
77.917
49.612
33.817
1.00
23.09

C


ATOM
2614
CG
GLN
A
470
77.402
49.156
32.439
1.00
23.12

C


ATOM
2615
CD
GLN
A
470
76.092
48.397
32.492
1.00
22.83

C


ATOM
2616
OE1
GLN
A
470
75.855
47.613
33.406
1.00
23.32

O


ATOM
2617
NE2
GLN
A
470
75.242
48.610
31.488
1.00
21.97

N


ATOM
2618
N
SER
A
471
80.590
50.039
35.687
1.00
25.04

N


ATOM
2619
CA
SER
A
471
81.139
50.391
36.983
1.00
26.85

C


ATOM
2620
C
SER
A
471
82.378
51.284
36.863
1.00
27.29

C


ATOM
2621
O
SER
A
471
82.530
52.246
37.614
1.00
27.87

O


ATOM
2622
CB
SER
A
471
81.500
49.115
37.749
1.00
27.07

C


ATOM
2623
OG
SER
A
471
82.193
49.422
38.943
1.00
30.83

O


ATOM
2624
N
LYS
A
472
83.244
50.981
35.900
1.00
27.53

N


ATOM
2625
CA
LYS
A
472
84.496
51.723
35.732
1.00
28.78

C


ATOM
2626
C
LYS
A
472
84.519
52.903
34.768
1.00
27.72

C


ATOM
2627
O
LYS
A
472
85.421
53.733
34.840
1.00
27.66

O


ATOM
2628
CB
LYS
A
472
85.604
50.752
35.316
1.00
29.70

C


ATOM
2629
CG
LYS
A
472
85.789
49.598
36.274
1.00
33.23

C


ATOM
2630
CD
LYS
A
472
86.819
48.602
35.768
1.00
33.84

C


ATOM
2631
CE
LYS
A
472
88.218
49.184
35.759
1.00
34.76

C


ATOM
2632
NZ
LYS
A
472
89.209
48.107
35.470
1.00
34.52

N


ATOM
2633
N
ALA
A
473
83.548
52.976
33.865
1.00
26.96

N


ATOM
2634
CA
ALA
A
473
83.522
54.045
32.870
1.00
26.73

C


ATOM
2635
C
ALA
A
473
83.663
55.472
33.395
1.00
26.34

C


ATOM
2636
O
ALA
A
473
83.045
55.853
34.389
1.00
26.04

O


ATOM
2637
CB
ALA
A
473
82.250
53.936
32.023
1.00
26.80

C


ATOM
2638
N
LYS
A
474
84.502
56.248
32.713
1.00
26.28

N


ATOM
2639
CA
LYS
A
474
84.712
57.656
33.034
1.00
26.69

C


ATOM
2640
C
LYS
A
474
84.166
58.376
31.807
1.00
26.49

C


ATOM
2641
O
LYS
A
474
84.724
58.278
30.712
1.00
25.96

O


ATOM
2642
CB
LYS
A
474
86.202
57.955
33.241
1.00
27.26

C


ATOM
2643
CG
LYS
A
474
86.777
57.279
34.485
1.00
28.54

C


ATOM
2644
CD
LYS
A
474
88.207
57.724
34.778
1.00
30.16

C


ATOM
2645
CE
LYS
A
474
89.177
57.220
33.745
1.00
30.74

C


ATOM
2646
NZ
LYS
A
474
90.571
57.651
34.057
1.00
30.36

N


ATOM
2647
N
ILE
A
475
83.067
59.095
31.995
1.00
26.72

N


ATOM
2648
CA
ILE
A
475
82.403
59.763
30.885
1.00
27.59

C


ATOM
2649
C
ILE
A
475
82.413
61.281
30.960
1.00
28.14

C


ATOM
2650
O
ILE
A
475
81.900
61.871
31.910
1.00
28.29

O


ATOM
2651
CB
ILE
A
475
80.943
59.278
30.794
1.00
27.25

C


ATOM
2652
CG1
ILE
A
475
80.919
57.743
30.797
1.00
27.67

C


ATOM
2653
CG2
ILE
A
475
80.281
59.832
29.537
1.00
27.73

C


ATOM
2654
CD1
ILE
A
475
79.522
57.134
30.885
1.00
26.56

C


ATOM
2655
N
THR
A
476
82.982
61.912
29.941
1.00
28.53

N


ATOM
2656
CA
THR
A
476
83.045
63.364
29.916
1.00
29.40

C


ATOM
2657
C
THR
A
476
82.184
63.974
28.820
1.00
29.85

C


ATOM
2658
O
THR
A
476
82.029
63.407
27.734
1.00
28.69

O


ATOM
2659
CB
THR
A
476
84.488
63.865
29.722
1.00
29.27

C


ATOM
2660
OG1
THR
A
476
84.501
65.293
29.813
1.00
30.19

O


ATOM
2661
CG2
THR
A
476
85.027
63.445
28.353
1.00
28.75

C


ATOM
2662
N
LEU
A
477
81.615
65.133
29.126
1.00
30.92

N


ATOM
2663
CA
LEU
A
477
80.791
65.863
28.176
1.00
33.43

C


ATOM
2664
C
LEU
A
477
81.792
66.681
27.363
1.00
34.68

C


ATOM
2665
O
LEU
A
477
82.829
67.084
27.887
1.00
34.58

O


ATOM
2666
CB
LEU
A
477
79.831
66.795
28.925
1.00
34.07

C


ATOM
2667
CG
LEU
A
477
78.671
67.452
28.173
1.00
35.06

C


ATOM
2668
CD1
LEU
A
477
77.683
66.393
27.716
1.00
34.39

C


ATOM
2669
CD2
LEU
A
477
77.975
68.449
29.094
1.00
35.94

C


ATOM
2670
N
VAL
A
478
81.497
66.910
26.089
1.00
36.01

N


ATOM
2671
CA
VAL
A
478
82.388
67.688
25.234
1.00
37.55

C


ATOM
2672
C
VAL
A
478
81.741
69.041
24.929
1.00
38.64

C


ATOM
2673
O
VAL
A
478
80.517
69.151
24.884
1.00
37.96

O


ATOM
2674
CB
VAL
A
478
82.681
66.929
23.919
1.00
37.92

C


ATOM
2675
CG1
VAL
A
478
83.612
67.732
23.046
1.00
38.33

C


ATOM
2676
CG2
VAL
A
478
83.308
65.577
24.234
1.00
38.01

C


ATOM
2677
N
SER
A
479
82.559
70.073
24.733
1.00
40.23

N


ATOM
2678
CA
SER
A
479
82.034
71.408
24.452
1.00
42.03

C


ATOM
2679
C
SER
A
479
81.414
71.483
23.062
1.00
43.58

C


ATOM
2680
O
SER
A
479
81.868
70.818
22.130
1.00
43.18

O


ATOM
2681
CB
SER
A
479
83.139
72.465
24.572
1.00
41.76

C


ATOM
2682
OG
SER
A
479
84.069
72.363
23.508
1.00
41.31

O


ATOM
2683
N
SER
A
480
80.373
72.299
22.930
1.00
45.81

N


ATOM
2684
CA
SER
A
480
79.688
72.465
21.653
1.00
48.45

C


ATOM
2685
C
SER
A
480
80.615
73.067
20.602
1.00
49.80

C


ATOM
2686
O
SER
A
480
80.426
72.859
19.402
1.00
50.06

O


ATOM
2687
CB
SER
A
480
78.450
73.352
21.830
1.00
48.66

C


ATOM
2688
OG
SER
A
480
78.778
74.574
22.468
1.00
50.04

O


ATOM
2689
N
VAL
A
481
81.622
73.805
21.062
1.00
51.44

N


ATOM
2690
CA
VAL
A
481
82.584
74.442
20.168
1.00
53.08

C


ATOM
2691
C
VAL
A
481
83.452
73.408
19.462
1.00
53.99

C


ATOM
2692
O
VAL
A
481
83.755
73.544
18.277
1.00
54.37

O


ATOM
2693
CB
VAL
A
481
83.515
75.402
20.936
1.00
53.14

C


ATOM
2694
CG1
VAL
A
481
84.397
76.161
19.958
1.00
53.54

C


ATOM
2695
CG2
VAL
A
481
82.698
76.363
21.775
1.00
53.62

C


ATOM
2696
N
SER
A
482
83.858
72.379
20.199
1.00
55.12

N


ATOM
2697
CA
SER
A
482
84.695
71.324
19.642
1.00
56.25

C


ATOM
2698
C
SER
A
482
83.890
70.412
18.722
1.00
57.11

C


ATOM
2699
O
SER
A
482
84.454
69.577
18.012
1.00
57.33

O


ATOM
2700
CB
SER
A
482
85.319
70.499
20.767
1.00
56.17

C


ATOM
2701
OG
SER
A
482
84.315
69.924
21.581
1.00
56.14

O


ATOM
2702
N
ILE
A
483
82.571
70.572
18.742
1.00
57.97

N


ATOM
2703
CA
ILE
A
483
81.693
69.769
17.899
1.00
58.92

C


ATOM
2704
C
ILE
A
483
81.319
70.545
16.639
1.00
59.33

C


ATOM
2705
O
ILE
A
483
81.588
70.028
15.535
1.00
59.84

O


ATOM
2706
CB
ILE
A
483
80.399
69.375
18.645
1.00
59.00

C


ATOM
2707
CG1
ILE
A
483
80.744
68.544
19.883
1.00
59.10

C


ATOM
2708
CG2
ILE
A
483
79.485
68.585
17.716
1.00
59.45

C


ATOM
2709
CD1
ILE
A
483
79.543
68.155
20.718
1.00
59.17

C


TER
2710

ILE
A
483


HETATM
2711
K
   K
A
900
52.243
59.799
29.172
0.75
29.54

K


HETATM
2712
P
IMP

602
67.273
54.643
14.906
1.00
25.76

P


HETATM
2713
O1P
IMP

602
66.861
54.580
13.478
1.00
26.22

O


HETATM
2714
O2P
IMP

602
68.037
53.408
15.254
1.00
26.63

O


HETATM
2715
O3P
IMP

602
68.090
55.908
15.218
1.00
25.72

O


HETATM
2716
O5*
IMP

602
66.048
54.751
15.914
1.00
25.69

O


HETATM
2717
C5*
IMP

602
65.054
53.735
15.819
1.00
23.90

C


HETATM
2718
C4*
IMP

602
63.955
53.909
16.822
1.00
23.17

C


HETATM
2719
O4*
IMP

602
63.226
55.091
16.335
1.00
22.32

O


HETATM
2720
C3*
IMP

602
62.855
52.875
16.958
1.00
22.53

C


HETATM
2721
O3*
IMP

602
63.229
51.710
17.687
1.00
21.85

O


HETATM
2722
C2*
IMP

602
61.776
53.670
17.629
1.00
22.98

C


HETATM
2723
O2*
IMP

602
61.948
53.736
19.029
1.00
22.76

O


HETATM
2724
C1*
IMP

602
61.928
55.030
16.924
1.00
23.55

C


HETATM
2725
N9
IMP

602
60.928
55.202
15.816
1.00
24.16

N


HETATM
2726
C8
IMP

602
60.310
54.298
14.971
1.00
25.51

C


HETATM
2727
N7
IMP

602
59.490
54.866
14.137
1.00
25.39

N


HETATM
2728
C5
IMP

602
59.548
56.197
14.417
1.00
25.42

C


HETATM
2729
C6
IMP

602
58.866
57.320
13.831
1.00
26.39

C


HETATM
2730
O6
IMP

602
58.049
57.295
12.909
1.00
27.34

O


HETATM
2731
N1
IMP

602
59.213
58.576
14.425
1.00
26.64

N


HETATM
2732
C2
IMP

602
60.131
58.702
15.478
1.00
26.89

C


HETATM
2733
N3
IMP

602
60.765
57.630
16.021
1.00
25.55

N


HETATM
2734
C4
IMP

602
60.437
56.438
15.458
1.00
25.01

C


HETATM
2735
C1
MOA

600
59.312
58.341
19.371
1.00
30.41

C


HETATM
2736
C2
MOA

600
54.700
56.341
16.455
1.00
32.49

C


HETATM
2737
C3
MOA

600
53.578
55.627
16.198
1.00
33.53

C


HETATM
2738
C4
MOA

600
52.262
56.261
16.628
1.00
34.60

C


HETATM
2739
C5
MOA

600
51.704
55.529
17.856
1.00
35.56

C


HETATM
2740
C6
MOA

600
52.413
55.880
19.153
1.00
36.42

C


HETATM
2741
C7
MOA

600
58.717
53.456
19.827
1.00
29.24

C


HETATM
2742
C8
MOA

600
55.639
53.144
18.309
1.00
29.52

C


HETATM
2743
C9
MOA

600
53.564
54.254
15.513
1.00
33.79

C


HETATM
2744
C10
MOA

600
59.889
56.364
20.539
1.00
29.78

C


HETATM
2745
C11
MOA

600
58.905
56.011
19.445
1.00
29.43

C


HETATM
2746
C12
MOA

600
58.347
54.721
19.086
1.00
29.74

C


HETATM
2747
C13
MOA

600
57.416
54.689
17.974
1.00
30.13

C


HETATM
2748
C14
MOA

600
57.077
55.910
17.275
1.00
30.94

C


HETATM
2749
C15
MOA

600
57.655
57.164
17.672
1.00
30.68

C


HETATM
2750
C16
MOA

600
58.569
57.183
18.763
1.00
30.24

C


HETATM
2751
C17
MOA

600
56.107
55.881
16.099
1.00
32.03

C


HETATM
2752
O1
MOA

600
59.306
59.497
19.082
1.00
30.18

O


HETATM
2753
O2
MOA

600
60.036
57.818
20.365
1.00
29.58

O


HETATM
2754
O3
MOA

600
56.876
53.479
17.608
1.00
30.38

O


HETATM
2755
O4
MOA

600
57.314
58.318
16.987
1.00
32.33

O


HETATM
2756
O5
MOA

600
52.401
57.074
19.536
1.00
37.48

O


HETATM
2757
O6
MOA

600
52.985
54.959
19.780
1.00
35.87

O


HETATM
2758
O
HOH

 1
59.924
29.679
22.414
1.00
50.51

O


HETATM
2759
O
HOH

 2
79.013
41.426
29.423
1.00
18.90

O


HETATM
2760
O
HOH

 3
58.751
44.934
36.922
1.00
19.77

O


HETATM
2761
O
HOH

 4
70.195
53.954
21.764
1.00
22.57

O


HETATM
2762
O
HOH

 5
65.251
60.127
24.411
1.00
21.78

O


HETATM
2763
O
HOH

 6
75.493
43.370
30.924
1.00
20.48

O


HETATM
2764
O
HOH

 7
56.253
78.397
34.291
1.00
25.40

O


HETATM
2765
O
HOH

 8
66.025
47.704
38.822
1.00
22.86

O


HETATM
2766
O
HOH

 9
56.894
58.199
28.230
1.00
22.26

O


HETATM
2767
O
HOH

 10
70.506
52.801
14.222
1.00
25.03

O


HETATM
2768
O
HOH

 11
63.871
40.741
7.794
1.00
24.61

O


HETATM
2769
O
HOH

 12
60.616
40.963
2.773
1.00
57.79

O


HETATM
2770
O
HOH

 13
72.961
57.112
35.993
1.00
22.52

O


HETATM
2771
O
HOH

 14
74.407
45.323
32.761
1.00
26.87

O


HETATM
2772
O
HOH

 15
86.443
54.944
31.105
1.00
24.24

O


HETATM
2773
O
HOH

 16
64.957
58.145
21.206
1.00
26.57

O


HETATM
2774
O
HOH

 17
58.226
37.978
34.604
1.00
28.06

O


HETATM
2775
O
HOH

 18
65.737
37.023
16.608
1.00
23.81

O


HETATM
2776
O
HOH

 19
71.973
37.555
33.842
1.00
27.82

O


HETATM
2777
O
HOH

 20
61.772
38.247
34.046
1.00
22.62

O


HETATM
2778
O
HOH

 21
52.301
52.152
19.306
1.00
49.95

O


HETATM
2779
O
HOH

 22
87.828
53.279
33.165
1.00
28.88

O


HETATM
2780
O
HOH

 23
81.359
62.610
21.058
1.00
27.37

O


HETATM
2781
O
HOH

 24
75.817
40.774
32.087
1.00
26.13

O


HETATM
2782
O
HOH

 25
58.057
34.952
27.087
1.00
28.97

O


HETATM
2783
O
HOH

 26
83.688
52.415
20.816
1.00
30.28

O


HETATM
2784
O
HOH

 27
77.149
53.162
34.368
1.00
29.69

O


HETATM
2785
O
HOH

 28
56.074
56.906
38.662
1.00
37.23

O


HETATM
2786
O
HOH

 29
49.870
31.480
16.451
1.00
33.88

O


HETATM
2787
O
HOH

 30
73.925
34.558
39.925
1.00
28.68

O


HETATM
2788
O
HOH

 31
78.589
39.852
31.836
1.00
26.69

O


HETATM
2789
O
HOH

 32
59.193
50.825
9.635
1.00
30.48

O


HETATM
2790
O
HOH

 33
48.757
43.664
20.942
1.00
29.46

O


HETATM
2791
O
HOH

 34
63.470
55.921
20.034
1.00
28.45

O


HETATM
2792
O
HOH

 35
64.748
36.350
34.843
1.00
29.99

O


HETATM
2793
O
HOH

 36
74.476
38.378
31.025
1.00
30.13

O


HETATM
2794
O
HOH

 37
51.517
53.493
25.810
1.00
33.48

O


HETATM
2795
O
HOH

 38
67.426
38.071
46.103
1.00
30.22

O


HETATM
2796
O
HOH

 39
73.458
50.410
36.144
1.00
28.96

O


HETATM
2797
O
HOH

 40
48.967
53.101
24.116
1.00
49.76

O


HETATM
2798
O
HOH

 41
70.826
32.483
29.970
1.00
39.88

O


HETATM
2799
O
HOH

 42
61.107
50.022
17.672
1.00
23.40

O


HETATM
2800
O
HOH

 43
73.974
36.418
10.780
1.00
31.43

O


HETATM
2801
O
HOH

 44
50.211
45.778
35.694
1.00
31.02

O


HETATM
2802
O
HOH

 45
63.973
35.222
38.133
1.00
49.08

O


HETATM
2803
O
HOH

 46
52.459
51.210
38.008
1.00
33.23

O


HETATM
2804
O
HOH

 47
68.639
62.467
21.428
1.00
33.95

O


HETATM
2805
O
HOH

 48
69.432
33.097
27.354
1.00
32.47

O


HETATM
2806
O
HOH

 49
74.578
37.941
8.159
1.00
32.47

O


HETATM
2807
O
HOH

 50
58.916
51.450
16.416
1.00
29.63

O


HETATM
2808
O
HOH

 51
69.598
53.385
17.586
1.00
29.79

O


HETATM
2809
O
HOH

 52
47.572
53.766
36.762
1.00
39.69

O


HETATM
2810
O
HOH

 53
84.793
48.751
39.168
1.00
43.51

O


HETATM
2811
O
HOH

 54
59.544
49.841
20.045
1.00
33.31

O


HETATM
2812
O
HOH

 55
64.161
25.507
14.641
1.00
30.60

O


HETATM
2813
O
HOH

 56
55.066
70.757
16.127
1.00
32.83

O


HETATM
2814
O
HOH

 57
74.182
47.486
35.548
1.00
31.59

O


HETATM
2815
O
HOH

 58
62.583
34.645
41.460
1.00
39.46

O


HETATM
2816
O
HOH

 59
51.561
30.405
13.105
1.00
57.09

O


HETATM
2817
O
HOH

 60
47.880
31.075
25.095
1.00
39.60

O


HETATM
2818
O
HOH

 61
53.997
32.961
37.361
1.00
38.91

O


HETATM
2819
O
HOH

 62
84.739
38.545
32.721
1.00
34.80

O


HETATM
2820
O
HOH

 63
70.499
56.677
14.512
1.00
31.54

O


HETATM
2821
O
HOH

 64
96.766
42.780
26.087
1.00
48.54

O


HETATM
2822
O
HOH

 65
48.178
56.536
26.666
1.00
44.06

O


HETATM
2823
O
HOH

 66
55.822
40.800
37.347
1.00
41.31

O


HETATM
2824
O
HOH

 67
62.651
58.499
18.259
1.00
30.38

O


HETATM
2825
O
HOH

 68
78.584
37.867
17.336
1.00
35.48

O


HETATM
2826
O
HOH

 69
73.741
59.595
37.699
1.00
46.66

O


HETATM
2827
O
HOH

 70
61.930
61.268
37.149
1.00
35.16

O


HETATM
2828
O
HOH

 71
64.600
31.307
29.524
1.00
40.08

O


HETATM
2829
O
HOH

 72
68.630
35.309
7.689
1.00
35.28

O


HETATM
2830
O
HOH

 73
74.821
69.567
31.440
1.00
45.20

O


HETATM
2831
O
HOH

 74
60.851
32.866
26.981
1.00
36.07

O


HETATM
2832
O
HOH

 75
78.209
47.346
37.269
1.00
42.78

O


HETATM
2833
O
HOH

 76
78.477
34.764
30.567
1.00
40.04

O


HETATM
2834
O
HOH

 77
71.498
30.722
23.744
1.00
35.11

O


HETATM
2835
O
HOH

 78
64.709
27.584
26.706
1.00
39.53

O


HETATM
2836
O
HOH

 79
58.218
44.875
5.808
1.00
39.15

O


HETATM
2837
O
HOH

 80
91.925
40.314
20.235
1.00
47.22

O


HETATM
2838
O
HOH

 81
65.374
28.271
14.859
1.00
33.66

O


HETATM
2839
O
HOH

 82
86.254
46.969
13.548
1.00
42.09

O


HETATM
2840
O
HOH

 83
86.599
66.411
30.817
1.00
28.92

O


HETATM
2841
O
HOH

 84
62.054
33.096
29.810
1.00
43.30

O


HETATM
2842
O
HOH

 85
95.032
45.638
27.312
1.00
44.01

O


HETATM
2843
O
HOH

 86
50.747
50.260
21.915
1.00
33.76

O


HETATM
2844
O
HOH

 87
64.754
61.086
37.994
1.00
43.01

O


HETATM
2845
O
HOH

 88
70.920
55.587
41.621
1.00
30.53

O


HETATM
2846
O
HOH

 89
87.356
35.892
30.913
1.00
54.42

O


HETATM
2847
O
HOH

 90
58.062
50.894
22.714
1.00
36.70

O


HETATM
2848
O
HOH

 91
66.375
33.870
36.838
1.00
36.70

O


HETATM
2849
O
HOH

 92
80.489
54.081
12.959
1.00
34.92

O


HETATM
2850
O
HOH

 93
49.688
32.577
11.671
1.00
44.86

O


HETATM
2851
O
HOH

 94
59.901
34.059
37.276
1.00
46.67

O


HETATM
2852
O
HOH

 95
60.124
37.261
37.104
1.00
40.44

O


HETATM
2853
O
HOH

 96
68.062
43.325
0.440
1.00
40.55

O


HETATM
2854
O
HOH

 97
92.043
48.470
23.328
1.00
41.20

O


HETATM
2855
O
HOH

 98
91.696
47.559
34.606
1.00
36.60

O


HETATM
2856
O
HOH

 99
72.456
40.842
41.613
1.00
38.50

O


HETATM
2857
O
HOH

100
56.000
31.198
23.572
1.00
40.79

O


HETATM
2858
O
HOH

101
49.154
42.288
7.689
1.00
40.98

O


HETATM
2859
O
HOH

102
73.470
34.115
8.839
1.00
54.10

O


HETATM
2860
O
HOH

103
61.679
22.463
5.705
1.00
52.66

O


HETATM
2861
O
HOH

104
77.579
33.064
16.137
1.00
47.51

O


HETATM
2862
O
HOH

105
44.253
34.815
19.536
1.00
42.37

O


HETATM
2863
O
HOH

106
45.451
48.437
27.057
1.00
38.64

O


HETATM
2864
O
HOH

107
59.592
41.005
40.036
1.00
41.25

O


HETATM
2865
O
HOH

108
72.057
60.543
20.606
1.00
36.69

O


HETATM
2866
O
HOH

109
55.706
47.432
14.991
1.00
42.24

O


HETATM
2867
O
HOH

110
62.531
31.016
25.446
1.00
42.66

O


HETATM
2868
O
HOH

111
73.718
48.291
39.771
1.00
53.04

O


HETATM
2869
O
HOH

112
83.522
36.024
30.729
1.00
43.33

O


HETATM
2870
O
HOH

113
45.028
41.039
12.802
1.00
37.34

O


HETATM
2871
O
HOH

114
69.524
61.101
18.831
1.00
49.35

O


HETATM
2872
O
HOH

115
44.452
44.556
32.827
1.00
42.61

O


HETATM
2873
O
HOH

116
54.399
50.470
15.469
1.00
48.43

O


HETATM
2874
O
HOH

117
61.680
63.886
35.352
1.00
38.29

O


HETATM
2875
O
HOH

118
77.475
37.083
32.225
1.00
42.79

O


HETATM
2876
O
HOH

119
53.086
57.730
38.200
1.00
44.72

O


HETATM
2877
O
HOH

120
79.877
44.361
4.154
1.00
44.06

O


HETATM
2878
O
HOH

121
57.773
49.349
44.295
1.00
43.42

O


HETATM
2879
O
HOH

122
81.021
37.925
24.041
1.00
40.18

O


HETATM
2880
O
HOH

123
92.237
46.682
19.335
1.00
49.83

O


HETATM
2881
O
HOH

124
80.220
47.967
11.064
1.00
40.72

O


HETATM
2882
O
HOH

125
73.280
38.459
40.030
1.00
48.09

O


HETATM
2883
O
HOH

126
75.038
35.191
27.031
1.00
35.93

O


HETATM
2884
O
HOH

127
54.075
73.213
39.117
1.00
50.72

O


HETATM
2885
O
HOH

128
53.079
51.663
12.707
1.00
36.75

O


HETATM
2886
O
HOH

129
60.212
50.703
45.884
1.00
49.07

O


HETATM
2887
O
HOH

130
85.493
38.286
29.721
1.00
45.03

O


HETATM
2888
O
HOH

131
72.246
32.952
26.073
1.00
44.35

O


HETATM
2889
O
HOH

132
74.333
61.925
18.775
1.00
48.91

O


HETATM
2890
O
HOH

133
78.475
36.361
24.540
1.00
37.31

O


HETATM
2891
O
HOH

134
70.535
25.345
24.416
1.00
53.34

O


HETATM
2892
O
HOH

135
81.081
38.943
20.640
1.00
56.12

O


HETATM
2893
O
HOH

136
60.987
73.452
38.941
1.00
44.96

O


HETATM
2894
O
HOH

137
72.007
45.634
46.667
1.00
47.04

O


HETATM
2895
O
HOH

138
54.881
54.255
40.087
1.00
47.22

O


HETATM
2896
O
HOH

139
64.127
73.162
32.500
1.00
39.03

O


HETATM
2897
O
HOH

140
91.015
51.135
35.563
1.00
54.84

O


HETATM
2898
O
HOH

141
44.237
42.950
15.139
1.00
48.61

O


HETATM
2899
O
HOH

142
84.958
38.682
22.430
1.00
41.83

O


HETATM
2900
O
HOH

143
58.380
41.590
5.816
1.00
48.19

O


HETATM
2901
O
HOH

144
83.941
42.401
9.407
1.00
45.78

O


HETATM
2902
O
HOH

145
48.035
32.860
14.382
1.00
49.29

O


HETATM
2903
O
HOH

146
62.470
25.629
24.500
1.00
47.15

O


HETATM
2904
O
HOH

147
65.188
30.631
26.633
1.00
37.87

O


HETATM
2905
O
HOH

148
77.128
50.319
38.016
1.00
50.84

O


HETATM
2906
O
HOH

149
42.757
43.332
23.225
1.00
33.93

O


HETATM
2907
O
HOH

150
58.953
59.302
30.126
1.00
39.39

O


HETATM
2908
O
HOH

151
55.806
76.784
37.029
1.00
43.89

O


HETATM
2909
O
HOH

152
90.603
36.990
30.793
1.00
49.14

O


HETATM
2910
O
HOH

153
73.243
28.912
13.776
1.00
44.78

O


HETATM
2911
O
HOH

154
67.670
43.878
49.116
1.00
67.50

O


HETATM
2912
O
HOH

155
65.834
40.753
2.745
1.00
47.30

O


HETATM
2913
O
HOH

156
73.843
26.459
21.225
1.00
51.06

O


HETATM
2914
O
HOH

157
47.543
41.292
37.139
1.00
43.81

O


HETATM
2915
O
HOH

158
68.949
44.995
46.463
1.00
50.27

O


HETATM
2916
O
HOH

159
65.492
48.526
5.504
1.00
49.51

O


HETATM
2917
O
HOH

160
61.797
59.722
40.006
1.00
48.68

O


HETATM
2918
O
HOH

161
55.273
30.697
8.635
1.00
52.97

O


HETATM
2919
O
HOH

162
50.769
46.331
39.662
1.00
54.24

O


HETATM
2920
O
HOH

163
55.705
37.312
5.362
1.00
48.34

O


HETATM
2921
O
HOH

164
71.788
35.831
6.649
1.00
44.94

O


HETATM
2922
O
HOH

165
56.757
27.304
17.057
1.00
47.57

O


HETATM
2923
O
HOH

166
65.426
40.295
46.540
1.00
43.83

O


HETATM
2924
O
HOH

167
55.456
40.561
4.913
1.00
53.90

O


HETATM
2925
O
HOH

168
66.954
59.058
38.463
1.00
50.46

O


HETATM
2926
O
HOH

169
71.615
66.882
31.700
1.00
48.78

O


HETATM
2927
O
HOH

170
73.024
64.238
30.477
1.00
52.09

O


HETATM
2928
O
HOH

171
64.066
49.499
51.024
1.00
64.01

O


HETATM
2929
O
HOH

172
53.222
41.567
6.859
1.00
49.28

O


HETATM
2930
O
HOH

173
70.234
41.586
−4.830
1.00
59.58

O


HETATM
2931
O
HOH

174
66.709
49.280
−8.054
1.00
53.26

O


HETATM
2932
O
HOH

175
61.589
53.016
−3.167
1.00
53.96

O


HETATM
2933
O
HOH

176
66.692
71.708
31.475
1.00
48.45

O


HETATM
2934
O
HOH

177
71.233
53.697
43.927
1.00
52.05

O


HETATM
2935
O
HOH

178
72.743
64.308
17.573
1.00
54.16

O


HETATM
2936
O
HOH

179
89.336
53.769
35.871
1.00
53.70

O


HETATM
2937
O
HOH

180
54.353
46.276
17.782
1.00
54.59

O


HETATM
2938
O
HOH

181
68.022
31.001
25.937
1.00
44.50

O


HETATM
2939
O
HOH

182
52.980
29.445
10.465
1.00
50.22

O


HETATM
2940
O
HOH

183
56.686
28.215
9.903
1.00
56.33

O


HETATM
2941
O
HOH

184
77.977
49.876
10.573
1.00
53.98

O


HETATM
2942
O
HOH

185
82.562
49.900
11.756
1.00
57.59

O


HETATM
2943
O
HOH

186
81.326
47.021
8.192
1.00
51.32

O


HETATM
2944
O
HOH

187
76.430
51.542
−3.718
1.00
42.16

O


HETATM
2945
O
HOH

188
75.167
53.201
−1.226
1.00
44.07

O


HETATM
2946
O
HOH

189
62.348
54.827
1.013
1.00
51.43

O


HETATM
2947
O
HOH

190
59.995
64.398
17.439
1.00
60.65

O


HETATM
2948
O
HOH

191
97.267
51.029
39.970
1.00
58.50

O


HETATM
2949
O
HOH

192
97.537
47.953
39.149
1.00
64.57

O


HETATM
2950
O
HOH

193
93.132
47.026
37.250
1.00
46.96

O












CONECT
 202
2538





CONECT
1536
1537


CONECT
1537
1536
1538
1540


CONECT
1538
1537
1539


CONECT
1539
1538
1542


CONECT
1540
1537
1541


CONECT
1541
1540


CONECT
1542
1539


CONECT
2538
 202


CONECT
2712
2713
2714
2715
2716


CONECT
2713
2712


CONECT
2714
2712


CONECT
2715
2712


CONECT
2716
2712
2717


CONECT
2717
2716
2718


CONECT
2718
2717
2719
2720


CONECT
2719
2718
2724


CONECT
2720
2718
2721
2722


CONECT
2721
2720


CONECT
2722
2720
2723
2724


CONECT
2723
2722


CONECT
2724
2719
2722
2725


CONECT
2725
2724
2726
2734


CONECT
2726
2725
2727


CONECT
2727
2726
2728


CONECT
2728
2727
2729
2734


CONECT
2729
2728
2730
2731


CONECT
2730
2729


CONECT
2731
2729
2732


CONECT
2732
2731
2733


CONECT
2733
2732
2734


CONECT
2734
2725
2728
2733


CONECT
2735
2750
2752
2753


CONECT
2736
2737
2751


CONECT
2737
2736
2738
2743


CONECT
2738
2737
2739


CONECT
2739
2738
2740


CONECT
2740
2739
2756
2757


CONECT
2741
2746


CONECT
2742
2754


CONECT
2743
2737


CONECT
2744
2745
2753


CONECT
2745
2744
2746
2750


CONECT
2746
2741
2745
2747


CONECT
2747
2746
2748
2754


CONECT
2748
2747
2749
2751


CONECT
2749
2748
2750
2755


CONECT
2750
2735
2745
2749


CONECT
2751
2736
2748


CONECT
2752
2735


CONECT
2753
2735
2744


CONECT
2754
2742
2747


CONECT
2755
2749


CONECT
2756
2740


CONECT
2757
2740









MASTER
520
0  4  14  18  0  0  6 2949  1  55  39







END


FIG. 12


P-UC 5440


Page 69


6876


62


TABLE 3



















TABLE 4







HEADER
OXIDOREDUCTASE
08-AUG-02
1MEI








TITLE
INOSINE MONOPHOSPHATE DEHYDROGENASE (IMPDH) FROM









TITLE
2
TRITRICHOMONAS FOETUS WITH XMP AND MYCOPHENOLIC ACID BOUND


COMPND

MOL_ID: 1;


COMPND
2
MOLECULE: INOSINE-5′-MONOPHOSPHATE DEHYDROGENASE;


COMPND
3
CHAIN: A;


COMPND
4
SYNONYM: IMP DEHYDROGENASE, IMPDH;


COMPND
S
EC: 1.1.1.205;


COMPND
6
ENGINEERED: YES


SOURCE

MOL ID: 1;


SOURCE
2
ORGANISM_SCIENTIFIC: TRITRICHOMONAS FOETUS;


SOURCE
3
GENE: IMPDH;


SOURCE
4
EXPRESSION_SYSTEM: ESCHERICHIA COLI;


SOURCE
5
EXPRESSION_SYSTEM_COMMON: BACTERIA;


SOURCE
6
EXPRESSION_SYSTEM_STRAIN: H712;


SOURCE
7
EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;


SOURCE
8
EXPRESSION_SYSTEM_PLASMID: PBACE


KEYWDS

ALPHA BETA BARREL


EXPDTA

X-RAY DIFFRACTION


AUTHOR

G. L. PROSISE, H. LUECKE










JRNL
AUTH

G. L. PROSISE, H. LUECKE


JRNL
TITL

CRYSTAL STRUCTURE OF T. FOETUS INOSINE


JRNL
TITL
2
MONOPHOSPHATE DEHYDROGENASE IN COMPLEX WITH


JRNL
TITL
3
SUBSTRATE, COFACTOR, AND ANALOGS:STRUCTURAL BASIS


JRNL
TITL
4
FOR THE RANDOM-IN ORDERED-OUT KINETIC MECHANISM


JRNL
REF

TO BE PUBLISHED


JRNL
REFN









REMARK
1



REMARK
2


REMARK
2
RESOLUTION. 2.20 ANGSTROMS.


REMARK
3


REMARK
3
REFINEMENT.












REMARK
3

PROGRAM
:
CNS 1.1


REMARK
3

AUTHORS
:
BRUNGER, ADAMS, CLORE, DELANO, GROS, GROSSE-


REMARK
3


:
KUNSTLEVE, JIANG, KUSZEWSKI, NILGES, PANNU,


REMARK
3


:
READ, RICE, SIMONSON, WARREN


REMARK
3









REMARK
3
REFINEMENT TARGET : ENGH & HUBER


REMARK
3


REMARK
3
DATA USED IN REFINEMENT.













REMARK
3

RESOLUTION RANGE HIGH
(ANGSTROMS)
:
2.20


REMARK
3

RESOLUTION RANGE LOW
(ANGSTROMS)
:
33.06


REMARK
3

DATA CUTOFF
(SIGMA(F))
:
0.000


REMARK
3

OUTLIER CUTOFF HIGH
(RMS(ABS(F)))
:
NULL













REMARK
3

COMPLETENESS (WORKING+TEST)
(%)
:
99.5


REMARK
3

NUMBER OF REFLECTIONS

:
32648


REMARK
3









REMARK
3
FIT TO DATA USED IN REFINEMENT.












REMARK
3

CROSS-VALIDATION METHOD
:
THROUGHOUT


REMARK
3

FREE R VALUE TEST SET SELECTION
:
RANDOM













REMARK
3

R VALUE
(WORKING SET)
:
0.227


REMARK
3

FREE R VALUE

:
0.257













REMARK
3

FREE R VALUE TEST SET SIZE
(%)
:
5.200


REMARK
3

FREE R VALUE TEST SET COUNT

:
1709












REMARK
3

ESTIMATED ERROR OF FREE R VALUE
:
0.006


REMARK
3









REMARK
3
FIT IN THE HIGHEST RESOLUTION BIN.













REMARK
3

TOTAL NUMBER OF BINS USED

:
6


REMARK
3

BIN RESOLUTION RANGE HIGH
(A)
:
2.20


REMARK
3

BIN RESOLUTION RANGE LOW
(A)
:
2.34













REMARK
3

BIN COMPLETENESS (WORKING+TEST)
(%)
:
96.60













REMARK
3

REFLECTIONS IN BIN
(WORKING SET)
:
4936


REMARK
3

BIN R VALUE
(WORKING SET)
:
0.2710


REMARK
3

BIN FREE R VALUE

:
0.2930













REMARK
3

BIN FREE R VALUE TEST SET SIZE
(%)
:
5.00


REMARK
3

BIN FREE R VALUE TEST SET COUNT

:
259












REMARK
3

ESTIMATED ERROR OF BINFREE R VALUE
:
0.018


REMARK
3









REMARK
3
NUMBER OF NON-HYDROGEN ATOMS USED INREFINEMENT.












REMARK
3

PROTEIN ATOMS
:
2690


REMARK
3

NUCLEIC ACID ATOMS
:
0


REMARK
3

HETEROGEN ATOMS
:
48


REMARK
3

SOLVENT ATOMS
:
180


REMARK
3









REMARK
3
B VALUES.













REMARK
3

FROM WILSON PLOT
(A**2)
:
27.40


REMARK
3

MEAN B VALUE
(OVERALL, A**2)
:
37.30










REMARK
3

OVERALL ANISOTROPIC B VALUE.













REMARK
3

B11
(A**2)
:
0.00000


REMARK
3

B22
(A**2)
:
0.00000


REMARK
3

B33
(A**2)
:
0.00000


REMARK
3

B12
(A**2)
:
0.00000


REMARK
3

B13
(A**2)
:
0.00000


REMARK
3

B23
(A**2)
:
0.00000


REMARK
3









REMARK
3
ESTIMATED COORDINATE ERROR.













REMARK
3

ESD FROM LUZZATI PLOT
(A)
:
0.27


REMARK
3

ESD FROM SIGMAA
(A)
:
0.23


REMARK
3

LOW RESOLUTION CUTOFF
(A)
:
5.00


REMARK
3









REMARK
3
CROSS-VALIDATED ESTIMATED COORDINATEERROR.













REMARK
3

ESD FROM C-V LUZZATI PLOT
(A)
:
0.32


REMARK
3

ESD FROM C-V SIGMAA
(A)
:
0.28


REMARK
3









REMARK
3
RMS DEVIATIONS FROM IDEAL VALUES.













REMARK
3

BOND LENGTHS
(A)
:
0.006


REMARK
3

BOND ANGLES
(DEGREES)
:
1.20


REMARK
3

DIHEDRAL ANGLES
(DEGREES)
:
22.50


REMARK
3

IMPROPER ANGLES
(DEGREES)
:
0.68


REMARK
3









REMARK
3
ISOTROPIC THERMAL MODEL : RESTRAINED


REMARK
3











REMARK
3
ISOTROPIC THERMAL FACTOR RESTRAINTS.
RMS
SIGMA















REMARK
3

MAIN-CHAIN BOND
(A**2)
:
1.230
;
1.500


REMARK
3

MAIN-CHAIN ANGLE
(A**2)
:
2.190
;
2.000


REMARK
3

SIDE-CHAIN BOND
(A**2)
:
1.610
;
2.000


REMARK
3

SIDE-CHAIN ANGLE
(A**2)
:
2.520
;
2.500


REMARK
3









REMARK
3
BULK SOLVENT MODELING.












REMARK
3

METHOD USED
:
FLAT MODEL


REMARK
3

KSOL
:
0.34


REMARK
3

BSOL
:
35.45


REMARK
3









REMARK
3
NCS MODEL : NULL


REMARK
3












REMARK
3

NCS RESTRAINTS.
RMS
SIGMA/WEIGHT
















REMARK
3

GROUP 1
POSITIONAL
(A)
:
NULL
;
NULL


REMARK
3

GROUP 2
B-FACTOR
(A**2)
:
NULL
;
NULL


REMARK
3












REMARK
3

PARAMETER FILE 1
:
PROTEIN_REP.PARAM


REMARK
3

PARAMETER FILE 2
:
PARAM.GNSOL


REMARK
3

PARAMETER FILE 3
:
CIS_PEPTIDE.PARAM


REMARK
3

PARAMETER FILE 4
:
MPA.PAR


REMARK
3

PARAMETER FILE 5
:
XMP.PAR


REMARK
3

PARAMETER FILE 6
:
NULL


REMARK
3

TOPOLOGY FILE 1
:
PROTEIN.TOP


REMARK
3

TOPOLOGY FILE 2
:
XMP.TOP


REMARK
3

TOPOLOGY FILE 3
:
MPA.TOP


REMARK
3

TOPOLOGY FILE 4
:
K.TOP


REMARK
3

TOPOLOGY FILE 5
:
TOPH.GNSOL


REMARK
3

TOPOLOGY FILE 6
:
NULL


REMARK
3










REMARK
3

OTHER REFINEMENT REMARKS: NULL


REMARK
4









REMARK
4
1MEI COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998


REMARK
100


REMARK
100
THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-AUG-2002.


REMARK
100
THE RCSB ID CODE IS RCSB016853.


REMARK
200


REMARK
200
EXPERIMENTAL DETAILS













REMARK
200

EXPERIMENT TYPE

:
X-RAY DIFFRACTION


REMARK
200

DATE OF DATA COLLECTION

:
11-APR-2001


REMARK
200

TEMPERATURE
(KELVIN)
:
100.0


REMARK
200

PH

:
7.50


REMARK
200

NUMBER OF CRYSTALS USED

:
1


REMARK
200


REMARK
200

SYNCHROTRON
(Y/N)
:
Y


REMARK
200

RADIATION SOURCE

:
SSRL


REMARK
200

BEAMLINE

:
9-1


REMARK
200

X-RAY GENERATOR MODEL

:
NULL


REMARK
200

MONOCHROMATIC OR LAUE
(M/L)
:
M


REMARK
200

WAVELENGTH OR RANGE
(A)
:
0.97


REMARK
200

MONOCHROMATOR

:
NULL


REMARK
200

OPTICS

:
NULL


REMARK
200


REMARK
200

DETECTOR TYPE

:
IMAGE PLATE


REMARK
200

DETECTOR MANUFACTURER

:
MARRESEARCH












REMARK
200

INTENSITY-INTEGRATION SOFTWARE
:
DENZO


REMARK
200

DATA SCALING SOFTWARE
:
SCALEPACK


REMARK
200


REMARK
200

NUMBER OF UNIQUE REFLECTIONS
:
32815













REMARK
200

RESOLUTION RANGE HIGH
(A)
:
2.200


REMARK
200

RESOLUTION RANGE LOW
(A)
:
99.000


REMARK
200

REJECTION CRITERIA
(SIGMA(I))
:
NULL


REMARK
200









REMARK
200
OVERALL.













REMARK
200

COMPLETENESS FOR RANGE
(%)
:
99.5


REMARK
200

DATA REDUNDANCY

:
4.700


REMARK
200

R MERGE
(I)
:
0.06600


REMARK
200

R SYM
(I)
:
NULL












REMARK
200

<I/SIGMA(I)> FOR THE DATA SET
:
21.4000


REMARK
200









REMARK
200
IN THE HIGHEST RESOLUTION SHELL.













REMARK
200

HIGHEST RESOLUTION SHELL, RANGE HIGH
(A)
:
2.20


REMARK
200

HIGHEST RESOLUTION SHELL, RANGE LOW
(A)
:
2.24













REMARK
200

COMPLETENESS FOR SHELL
(%)
:
98.7


REMARK
200

DATA REDUNDANCY IN SHELL

:
NULL


REMARK
200

R MERGE FOR SHELL
(I)
:
0.50000


REMARK
200

R SYM FOR SHELL
(I)
:
NULL


REMARK
200

<I/SIGMA(I)> FOR SHELL

:
2.900


REMARK
200









REMARK
200
DIFFRACTION PROTOCOL: SINGLE WAVELENGTH


REMARK
200
METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS


REMARK
200
SOFTWARE USED: CNS


REMARK
200
STARTING MODEL: PDB ENTRY 1AK5


REMARK
200


REMARK
200
REMARK: NULL


REMARK
280


REMARK
280
CRYSTAL












REMARK
280
SOLVENT CONTENT, VS
(%)
:
NULL












REMARK
280
MATTHEWS COEFFICIENT, VM
(ANGSTROMS**3/DA)
:
NULL


REMARK
280









REMARK
280
CRYSTALLIZATION CONDITIONS: SODIUM MALONATE, TRIS, 2-










REMARK
280

MERCAPTOETHANOL, EDTA, GLYCEROL


REMARK
290









REMARK
290
CRYSTALLOGRAPHIC SYMMETRY


REMARK
290
SYMMETRY OPERATORS FOR SPACE GROUP: P 4 3 2


REMARK
290











REMARK
290

SYMOP
SYMMETRY


REMARK
290

NNNMMM
OPERATOR


REMARK
290

 1555
X, Y, Z


REMARK
290

 2555
−X, −Y, Z


REMARK
290

 3555
−X, Y, −Z


REMARK
290

 4555
X, −Y, −Z


REMARK
290

 5555
Z, X, Y


REMARK
290

 6555
Z, −X, −Y


REMARK
290

 7555
−Z, −X, Y


REMARK
290

 8555
−Z, X, −Y


REMARK
290

 9555
Y, Z, X


REMARK
290

10555
−Y, Z, −X


REMARK
290

11555
Y, −Z, −X


REMARK
290

12555
−Y, −Z, X


REMARK
290

13555
Y, X, −Z


REMARK
290

14555
−Y, −X, −Z


REMARK
290

15555
Y, −X, Z


REMARK
290

16555
−Y, X, Z


REMARK
290

17555
X, Z, −Y


REMARK
290

18555
X, Z, Y


REMARK
290

19555
−X, −Z, −Y


REMARK
290

20555
X, −Z, Y


REMARK
290

21555
Z, Y, −X


REMARK
290

22555
Z, −Y, X


REMARK
290

23555
−Z, Y, X


REMARK
290

24555
−Z, −Y, −X


REMARK
290











REMARK
290

WHERE
NNN −> OPERATOR NUMBER


REMARK
290


MMM −> TRANSLATION VECTOR


REMARK
290









REMARK
290
CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS


REMARK
290
THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM


REMARK
290
RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY


REMARK
290
RELATED MOLECULES.















REMARK
290

SMTRY1
1
1.000000
0.000000
0.000000
0.00000


REMARK
290

SMTRY2
1
0.000000
1.000000
0.000000
0.00000


REMARK
290

SMTRY3
1
0.000000
0.000000
1.000000
0.00000


REMARK
290

SMTRY1
2
−1.000000
0.000000
0.000000
0.00000


REMARK
290

SMTRY2
2
0.000000
−1.000000
0.000000
0.00000


REMARK
290

SMTRY3
2
0.000000
0.000000
1.000000
0.00000


REMARK
290

SMTRY1
3
−1.000000
0.000000
0.000000
0.00000


REMARK
290

SMTRY2
3
0.000000
1.000000
0.000000
0.00000


REMARK
290

SMTRY3
3
0.000000
0.000000
−1.000000
0.00000


REMARK
290

SMTRY1
4
1.000000
0.000000
0.000000
0.00000


REMARK
290

SMTRY2
4
0.000000
−1.000000
0.000000
0.00000


REMARK
290

SMTRY3
4
0.000000
0.000000
−1.000000
0.00000


REMARK
290

SMTRY1
5
0.000000
0.000000
1.000000
0.00000


REMARK
290

SMTRY2
5
1.000000
0.000000
0.000000
0.00000


REMARK
290

SMTRY3
5
0.000000
1.000000
0.000000
0.00000


REMARK
290

SMTRY1
6
0.000000
0.000000
1.000000
0.00000


REMARK
290

SMTRY2
6
−1.000000
0.000000
0.000000
0.00000


REMARK
290

SMTRY3
6
0.000000
−1.000000
0.000000
0.00000


REMARK
290

SMTRY1
7
0.000000
0.000000
−1.000000
0.00000


REMARK
290

SMTRY2
7
−1.000000
0.000000
0.000000
0.00000


REMARK
290

SMTRY3
7
0.000000
1.000000
0.000000
0.00000


REMARK
290

SMTRY1
8
0.000000
0.000000
−1.000000
0.00000


REMARK
290

SMTRY2
8
1.000000
0.000000
0.000000
0.00000


REMARK
290

SMTRY3
8
0.000000
−1.000000
0.000000
0.00000


REMARK
290

SMTRY1
9
0.000000
1.000000
0.000000
0.00000


REMARK
290

SMTRY2
9
0.000000
0.000000
1.000000
0.00000


REMARK
290

SMTRY3
9
1.000000
0.000000
0.000000
0.00000


REMARK
290

SMTRY1
10
0.000000
−1.000000
0.000000
0.00000


REMARK
290

SMTRY2
10
0.000000
0.000000
1.000000
0.00000


REMARK
290

SMTRY3
10
−1.000000
0.000000
0.000000
0.00000


REMARK
290

SMTRY1
11
0.000000
1.000000
0.000000
0.00000


REMARK
290

SMTRY2
11
0.000000
0.000000
−1.000000
0.00000


REMARK
290

SMTRY3
11
−1.000000
0.000000
0.000000
0.00000


REMARK
290

SMTRY1
12
0.000000
−1.000000
0.000000
0.00000


REMARK
290

SMTRY2
12
0.000000
0.000000
−1.000000
0.00000


REMARK
290

SMTRY3
12
1.000000
0.000000
0.000000
0.00000


REMARK
290

SMTRY1
13
0.000000
1.000000
0.000000
0.00000


REMARK
290

SMTRY2
13
1.000000
0.000000
0.000000
0.00000


REMARK
290

SMTRY3
13
0.000000
0.000000
−1.000000
0.00000


REMARK
290

SMTRY1
14
0.000000
−1.000000
0.000000
0.00000


REMARK
290

SMTRY2
14
−1.000000
0.000000
0.000000
0.00000


REMARK
290

SMTRY3
14
0.000000
0.000000
−1.000000
0.00000


REMARK
290

SMTRY1
15
0.000000
1.000000
0.000000
0.00000


REMARK
290

SMTRY2
15
−1.000000
0.000000
0.000000
0.00000


REMARK
290

SMTRY3
15
0.000000
0.000000
1.000000
0.00000


REMARK
290

SMTRY1
16
0.000000
−1.000000
0.000000
0.00000


REMARK
290

SMTRY2
16
1.000000
0.000000
0.000000
0.00000


REMARK
290

SMTRY3
16
0.000000
0.000000
1.000000
0.00000


REMARK
290

SMTRY1
17
1.000000
0.000000
0.000000
0.00000


REMARK
290

SMTRY2
17
0.000000
0.000000
1.000000
0.00000


REMARK
290

SMTRY3
17
0.000000
−1.000000
0.000000
0.00000


REMARK
290

SMTRY1
18
−1.000000
0.000000
0.000000
0.00000


REMARK
290

SMTRY2
18
0.000000
0.000000
1.000000
0.00000


REMARK
290

SMTRY3
18
0.000000
1.000000
0.000000
0.00000


REMARK
290

SMTRY1
19
−1.000000
0.000000
0.000000
0.00000


REMARK
290

SMTRY2
19
0.000000
0.000000
−1.000000
0.00000


REMARK
290

SMTRY3
19
0.000000
−1.000000
0.000000
0.00000


REMARK
290

SMTRY1
20
1.000000
0.000000
0.000000
0.00000


REMARK
290

SMTRY2
20
0.000000
0.000000
−1.000000
0.00000


REMARK
290

SMTRY3
20
0.000000
1.000000
0.000000
0.00000


REMARK
290

SMTRY1
21
0.000000
0.000000
1.000000
0.00000


REMARK
290

SMTRY2
21
0.000000
1.000000
0.000000
0.00000


REMARK
290

SMTRY3
21
−1.000000
0.000000
0.000000
0.00000


REMARK
290

SMTRY1
22
0.000000
0.000000
1.000000
0.00000


REMARK
290

SMTRY2
22
0.000000
−1.000000
0.000000
0.00000


REMARK
290

SMTRY3
22
1.000000
0.000000
0.000000
0.00000


REMARK
290

SMTRY1
23
0.000000
0.000000
−1.000000
0.00000


REMARK
290

SMTRY2
23
0.000000
1.000000
0.000000
0.00000


REMARK
290

SMTRY3
23
1.000000
0.000000
0.000000
0.00000


REMARK
290

SMTRY1
24
0.000000
0.000000
−1.000000
0.00000


REMARK
290

SMTRY2
24
0.000000
−1.000000
0.000000
0.00000


REMARK
290

SMTRY3
24
−1.000000
0.000000
0.000000
0.00000


REMARK
290









REMARK
290
REMARK: NULL


REMARK
300


REMARK
300
BIOMOLECULE: 1


REMARK
300
THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT


REMARK
300
WHICH CONSISTS OF 1 CHAIN(S). SEE REMARK 350 FOR


REMARK
300
INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).


REMARK
350


REMARK
350
GENERATING THE BIOMOLECULE


REMARK
350
COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN


REMARK
350
BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE


REMARK
350
MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS


REMARK
350
GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND


REMARK
350
CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.


REMARK
350


REMARK
350
BIOMOLECULE: 1


REMARK
350
APPLY THE FOLLOWING TO CHAINS: A















REMARK
350

BIOMT1
1
1.000000
0.000000
0.000000
0.00000


REMARK
350

BIOMT2
1
0.000000
1.000000
0.000000
0.00000


REMARK
350

BIOMT3
1
0.000000
0.000000
1.000000
0.00000


REMARK
350

BIOMT1
2
−1.000000
0.000000
0.000000
155.07000


REMARK
350

BIOMT2
2
0.000000
−1.000000
0.000000
155.07000


REMARK
350

BIOMT3
2
0.000000
0.000000
1.000000
0.00000


REMARK
350

BIOMT1
3
0.000000
1.000000
0.000000
0.00000


REMARK
350

BIOMT2
3
−1.000000
0.000000
0.000000
155.07000


REMARK
350

BIOMT3
3
0.000000
0.000000
1.000000
0.00000


REMARK
350

BIOMT1
4
0.000000
−1.000000
0.000000
155.07000


REMARK
350

BIOMT2
4
1.000000
0.000000
0.000000
0.00000


REMARK
350

BIOMT3
4
0.000000
0.000000
1.000000
0.00000


REMARK
375









REMARK
375
SPECIAL POSITION


REMARK
375
THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS


REMARK
375
OF A SYMMETRY RELATEDATOM AND ARE ASSUMED TO BE ON SPECIAL


REMARK
375
POSITIONS.


REMARK
375












REMARK
375
ATOM
RES
CSSEQI



REMARK
375

HOH
131
LIES ON A SPECIAL POSITION.


REMARK
465









REMARK
465
MISSING RESIDUES


REMARK
465
THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE


REMARK
465
EXPERIMENT. (M = MODEL NUMBER; RES = RESIDUE NAME; C = CHAIN


REMARK
465
IDENTIFIER; SSSEQ = SEQUENCE NUMBER; I = INSERTION CODE.)


REMARK
465














REMARK
465

M
RES
C
SSSEQI



REMARK
465

MET
A
1


REMARK
465

GLY
A
102


REMARK
465

PHE
A
103


REMARK
465

VAL
A
104


REMARK
465

VAL
A
105


REMARK
465

SER
A
106


REMARK
465

ASP
A
107


REMARK
465

SER
A
108


REMARK
465

ASN
A
109


REMARK
465

VAL
A
110


REMARK
465

LYS
A
111


REMARK
465

PRO
A
112


REMARK
465

ASP
A
113


REMARK
465

GLN
A
114


REMARK
465

THR
A
115


REMARK
465

PHE
A
116


REMARK
465

ALA
A
117


REMARK
465

ASP
A
118


REMARK
465

VAL
A
119


REMARK
465

LEU
A
120


REMARK
465

ALA
A
121


REMARK
465

ILE
A
122


REMARK
465

SER
A
123


REMARK
465

GLN
A
124


REMARK
465

ARG
A
125


REMARK
465

THR
A
126


REMARK
465

THR
A
127


REMARK
465

HIS
A
128


REMARK
465

ASN
A
129


REMARK
465

THR
A
130


REMARK
465

VAL
A
131


REMARK
465

ALA
A
132


REMARK
465

VAL
A
133


REMARK
465

THR
A
134


REMARK
465

ASP
A
135


REMARK
465

ASP
A
136


REMARK
465

GLY
A
137


REMARK
465

THR
A
138


REMARK
465

PRO
A
139


REMARK
465

HIS
A
140


REMARK
465

GLY
A
141


REMARK
465

VAL
A
142


REMARK
465

LEU
A
143


REMARK
465

LEU
A
144


REMARK
465

GLY
A
145


REMARK
465

LEU
A
146


REMARK
465

VAL
A
147


REMARK
465

THR
A
148


REMARK
465

GLN
A
149


REMARK
465

ARG
A
150


REMARK
465

ASP
A
151


REMARK
465

TYR
A
152


REMARK
465

PRO
A
153


REMARK
465

ILE
A
154


REMARK
465

ASP
A
155


REMARK
465

LEU
A
156


REMARK
465

THR
A
157


REMARK
465

GLN
A
158


REMARK
465

THR
A
159


REMARK
465

GLU
A
160


REMARK
465

THR
A
161


REMARK
465

LYS
A
162


REMARK
465

VAL
A
163


REMARK
465

SER
A
164


REMARK
465

ASP
A
165


REMARK
465

MET
A
166


REMARK
465

MET
A
167


REMARK
465

THR
A
168


REMARK
465

PRO
A
169


REMARK
465

PHE
A
170


REMARK
465

SER
A
171


REMARK
465

LYS
A
172


REMARK
465

LEU
A
173


REMARK
465

VAL
A
174


REMARK
465

THR
A
175


REMARK
465

ALA
A
176


REMARK
465

HIS
A
177


REMARK
465

GLN
A
178


REMARK
465

ASP
A
179


REMARK
465

THR
A
180


REMARK
465

LYS
A
181


REMARK
465

LEU
A
182


REMARK
465

SER
A
183


REMARK
465

GLU
A
184


REMARK
465

ALA
A
185


REMARK
465

ASN
A
186


REMARK
465

LYS
A
187


REMARK
465

ILE
A
188


REMARK
465

ILE
A
189


REMARK
465

TRP
A
190


REMARK
465

GLU
A
191


REMARK
465

LYS
A
192


REMARK
465

LYS
A
193


REMARK
465

LEU
A
194


REMARK
465

ASN
A
195


REMARK
465

ALA
A
196


REMARK
465

LEU
A
197


REMARK
465

PRO
A
198


REMARK
465

ILE
A
199


REMARK
465

ILE
A
200


REMARK
465

ASP
A
201


REMARK
465

ASP
A
202


REMARK
465

ASP
A
203


REMARK
465

GLN
A
204


REMARK
465

HIS
A
205


REMARK
465

LEU
A
206


REMARK
465

ARG
A
207


REMARK
465

TYR
A
208


REMARK
465

ILE
A
209


REMARK
465

VAL
A
210


REMARK
465

PHE
A
211


REMARK
465

ARG
A
212


REMARK
465

LYS
A
213


REMARK
465

ASP
A
214


REMARK
465

TYR
A
215


REMARK
465

ASP
A
216


REMARK
465

ARG
A
217


REMARK
465

SER
A
218


REMARK
465

GLN
A
219


REMARK
465

VAL
A
220


REMARK
465

CYS
A
221


REMARK
465

GLN
A
417


REMARK
465

ARG
A
418


REMARK
465

TYR
A
419


REMARK
465

ASP
A
420


REMARK
465

LEU
A
421


REMARK
465

GLY
A
422


REMARK
465

GLY
A
423


REMARK
465

LYS
A
424


REMARK
465

GLN
A
425


REMARK
465

LYS
A
426


REMARK
465

LEU
A
427


REMARK
465

VAL
A
484


REMARK
465

GLU
A
485


REMARK
465

GLY
A
486


REMARK
465

GLY
A
487


REMARK
465

ALA
A
488


REMARK
465

HIS
A
489


REMARK
465

ASP
A
490


REMARK
465

VAL
A
491


REMARK
465

ILE
A
492


REMARK
465

VAL
A
493


REMARK
465

LYS
A
494


REMARK
465

ASP
A
495


REMARK
465

ARG
A
496


REMARK
465

ILE
A
497


REMARK
465

ASN
A
498


REMARK
465

ASP
A
499


REMARK
465

TYR
A
500


REMARK
465

HIS
A
501


REMARK
465

PRO
A
502


REMARK
465

LYS
A
503


REMARK
500









REMARK
500
GEOMETRY AND STEREOCHEMISTRY


REMARK
500
SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT


REMARK
500


REMARK
500
THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.


REMARK
500


















REMARK
500
ATM1
RES
C
SSEQI
ATM2
RES
C
SSEQI




REMARK
500
0
GLYA
20
K
K
A
900

2.12


REMARK
500









REMARK
500
GEOMETRY AND STEREOCHEMISTRY


REMARK
500
SUBTOPIC: COVALENT BOND LENGTHS


REMARK
500


REMARK
500
THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES


REMARK
500
HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE


REMARK
500
THAN 6*RMSD (M = MODEL NUMBER; RES = RESIDUE NAME; C = CHAIN


REMARK
500
IDENTIFIER; SSEQ = SEQUENCE NUMBER; I = INSERTION CODE)


REMARK
500


REMARK
500
STANDARD TABLE:


REMARK
500
FORMAT: (10X, 13, 1X, 2(A3, 1X, A1, I4, A1, 1X, A4, 3X), F6.3).


REMARK
500


REMARK
500
EXPECTED VALUES: ENGH AND HUBER, 1991


REMARK
500

















REMARK
500
M
RES
CSSEQI
ATM1
RES
CSSEQI
ATM2
DEVIATION



















REMARK
500

MET
A
379
CE
MET
A
379
SD
0.037


REMARK
500









REMARK
500
GEOMETRY AND STEREOCHEMISTRY


REMARK
500
SUBTOPIC: COVALENT BOND ANGLES


REMARK
500


REMARK
500
THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES


REMARK
500
HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE


REMARK
500
THAN 6*RMSD (M = MODEL NUMBER; RES = RESIDUE NAME; C = CHAIN


REMARK
500
IDENTIFIER; SSEQ = SEQUENCE NUMBER; I = INSERTION CODE).


REMARK
500


REMARK
500
STANDARD TABLE:


REMARK
500
FORMAT: (10X, I3, 1X, A3, 1X, A1, I4, A1, 3(1X, A4, 2X), 12X, F5.1)


REMARK
500


REMARK
500
EXPECTED VALUES: ENGH AND HUBER, 1991


REMARK
500














REMARK
500
M
RES
CSSEQI
ATM1
ATM2
ATM3



















REMARK
500

ILE
A
27
N
-
CA
-
C
ANGL. DEV. =
−7.8 DEGREES


REMARK
500

GLN
A
45
N
-
CA
-
C
ANGL. DEV. =
−7.7 DEGREES


REMARK
500

SER
A
63
N
-
CA
-
C
ANGL. DEV. =
  8.3 DEGREES


REMARK
500

PHE
A
266
N
-
CA
-
C
ANGL. DEV. =
−7.2 DEGREES


REMARK
500

GLY
A
312
N
-
CA
-
C
ANGL. DEV. =
  7.6 DEGREES


REMARK
500

THR
A
349
N
-
CA
-
C
ANGL. DEV. =
  7.3 DEGREES


REMARK
500

PRO
A
391
N
-
CA
-
C
ANGL. DEV. =
  7.3 DEGREES


REMARK
500

LYS
A
394
N
-
CA
-
C
ANGL. DEV. =
−7.8 DEGREES


REMARK
500

LYS
A
472
N
-
CA
-
C
ANGL. DEV. =
  8.3 DEGREES


REMARK
500

LYS
A
474
N
-
CA
-
C
ANGL. DEV. =
−8.6 DEGREES


REMARK
500

LEU
A
477
N
-
CA
-
C
ANGL. DEV. =
−7.6 DEGREES


REMARK
500









REMARK
500
GEOMETRY AND STEREOCHEMISTRY


REMARK
500
SUBTOPIC: TORSION ANGLES


REMARK
500


REMARK
500
TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:


REMARK
500
(M = MODEL NUMBER; RES = RESIDUE NAME; C = CHAIN IDENTIFIER;


REMARK
500
SSEQ = SEQUENCE NUMBER; I = INSERTION CODE).


REMARK
500


REMARK
500
STANDARD TABLE:


REMARK
500
FORMAT: (10X, I3, 1X, A3, 1X, A1, I4, A1, 4X, F7.2, 3X, F7.2)


REMARK
500














REMARK
500
M
RES
CSSEQI
PSI
PHI
















REMARK
500

GLN
A
324
−106.74
−152.50



REMARK
900









REMARK
900
RELATED ENTRIES










REMARK
900
RELATED ID: 1AK5
RELATED DB: PDB









REMARK
900
INOSINE MONOPHOSPHATE DEHYDROGENASE (IMPDH) FROM


REMARK
900
TRITRICHOMONAS FOETUS










REMARK
900
RELATED ID: 1ME7
RELATED DB: PDB









REMARK
900
1ME7 CONTAINS THE SAME PROTEIN WITH RVP AND MOA BOUND










REMARK
900
RELATED ID: 1ME8
RELATED DB: PDB









REMARK
900
1ME8 CONTAINS THE SAME PROTEIN WITH RVP BOUND










REMARK
900
RELATED ID: 1ME9
RELATED DB: PDB









REMARK
900
1ME9 CONTAINS THE SAME PROTEIN WITH IMP BOUND










REMARK
900
RELATED ID: 1MEH
RELATED DB: PDB









REMARK
900
1MEH CONTAINS THE SAME PROTEIN WITH IMP AND MOA BOUND










REMARK
900
RELATED ID: 1MEW
RELATED DB: PDB









REMARK
900
1MEW CONTAINS THE SAME PROTEIN WITH XMP AND NAD BOUND
















DBREF
1MEI
A
1
503
SWS
P50097
IMDH_TRIFO
1
503























SEQRES
1
A
503
MET
ALA
LYS
TYR
TYR
ASN
GLU
PRO
CYS
HIS
THR
PHE
ASN


SEQRES
2
A
503
GLU
TYR
LEU
LEU
ILE
PRO
GLY
LEU
SER
THR
VAL
ASP
CYS


SEQRES
3
A
503
ILE
PRO
SER
ASN
VAL
ASN
LEU
SER
THR
PRO
LEU
VAL
LYS


SEQRES
4
A
503
PHE
GLN
LYS
GLY
GLN
GLN
SER
GLU
ILE
ASN
LEU
LYS
ILE


SEQRES
5
A
503
PRO
LEU
VAL
SER
ALA
ILE
MET
GLN
SER
VAL
SER
GLY
GLU


SEQRES
6
A
503
LYS
MET
ALA
ILE
ALA
LEU
ALA
ARG
GLU
GLY
GLY
ILE
SER


SEQRES
7
A
503
PHE
ILE
PHE
GLY
SER
GLN
SER
ILE
GLU
SER
GLN
ALA
ALA


SEQRES
8
A
503
MET
VAL
HIS
ALA
VAL
LYS
ASN
PHE
LYS
ALA
GLY
PHE
VAL


SEQRES
9
A
503
VAL
SER
ASP
SER
ASN
VAL
LYS
PRO
ASP
GLN
THR
PHE
ALA


SEQRES
10
A
503
ASP
VAL
LEU
ALA
ILE
SER
GLN
ARO
THR
THR
HIS
ASN
THR


SEQRES
11
A
503
VAL
ALA
VAL
THR
ASP
ASP
GLY
THR
PRO
HIS
GLY
VAL
LEU


SEQRES
12
A
503
LEU
GLY
LEU
VAL
THR
GLN
ARG
ASP
TYR
PRO
ILE
ASP
LEU


SEQRES
13
A
503
THR
GLN
THR
GLU
THR
LYS
VAL
SER
ASP
MET
MET
THR
PRO


SEQRES
14
A
503
PHE
SER
LYS
LEU
VAL
THR
ALA
HIS
GLN
ASP
THR
LYS
LEU


SEQRES
15
A
503
SER
GLU
ALA
ASN
LYS
ILE
ILE
TRP
GLU
LYS
LYS
LEU
ASN


SEQRES
16
A
503
ALA
LEU
PRO
ILE
ILE
ASP
ASP
ASP
GLN
HIS
LEU
ARG
TYR


SEQRES
17
A
503
ILE
VAL
PHE
ARG
LYS
ASP
TYR
ASP
ARG
SER
GLN
VAL
CYS


SEQRES
18
A
503
HIS
ASN
GLU
LEU
VAL
ASP
SER
GLN
LYS
ARG
TYR
LEU
VAL


SEQRES
19
A
503
GLY
ALA
GLY
ILE
ASN
THR
ARG
ASP
PHE
ARG
GLU
ARG
VAL


SEQRES
20
A
503
PRO
ALA
LEU
VAL
GLU
ALA
GLY
ALA
ASP
VAL
LEU
CYS
ILE


SEQRES
21
A
503
ASP
SER
SER
ASP
GLY
PHE
SER
GLU
TRP
GLN
LYS
ILE
THR


SEQRES
22
A
503
ILE
GLY
TRP
ILE
ARG
GLU
LYS
TYR
GLY
ASP
LYS
VAL
LYS


SEQRES
23
A
503
VAL
GLY
ALA
GLY
ASN
ILE
VAL
ASP
GLY
GLU
GLY
PHE
ARG


SEQRES
24
A
503
TYR
LEU
ALA
ASP
ALA
GLY
ALA
ASP
PHE
ILE
LYS
ILE
GLY


SEQRES
25
A
503
ILE
GLY
GLY
GLY
SER
ILE
CYS
ILE
THR
ARO
GLU
GLN
LYS


SEQRES
26
A
503
GLY
ILE
GLY
ARG
GLY
GLN
ALA
THR
ALA
VAL
ILE
ASP
VAL


SEQRES
27
A
503
VAL
ALA
GLU
ARG
ASN
LYS
TYR
PHE
GLU
GLU
THR
GLY
ILE


SEQRES
28
A
503
TYR
ILE
PRO
VAL
CYS
SER
ASP
GLY
GLY
ILE
VAL
TYR
ASP


SEQRES
29
A
503
TYR
HIS
MET
THR
LEU
ALA
LEU
ALA
MET
GLY
ALA
ASP
PHE


SEQRES
30
A
503
ILE
MET
LEU
GLY
ARG
TYR
PHE
ALA
ARG
PHE
GLU
GIU
SER


SEQRES
31
A
503
PRO
THR
ARG
LYS
VAL
THR
ILE
ASN
GLY
SER
VAL
MET
LYS


SEQRES
32
A
503
GLU
TYR
TRP
GLY
GLU
GLY
SER
SER
ARG
ALA
ARG
ASN
TRP


SEQRES
33
A
503
GLN
ARG
TYR
ASP
LEU
GLY
GLY
LYS
GLN
LYS
LEU
SER
PHE


SEQRES
34
A
503
GLU
GLU
GLY
VAL
ASP
SER
TYR
VAL
PRO
TYR
ALA
GLY
LYS


SEQRES
35
A
503
LEU
LYS
ASP
ASN
VAL
GLU
ALA
SER
LEU
ASN
LYS
VAL
LYS


SEQRES
36
A
503
SER
THR
MET
CYS
ASN
CYS
GLY
ALA
LEU
THR
ILE
PRO
GLN


SEQRES
37
A
503
LEU
GLN
SER
LYS
ALA
LYS
ILE
THR
LEU
VAL
SER
SER
VAL


SEQRES
38
A
503
SER
ILE
VAL
GLU
GLY
GLY
ALA
HIS
ASP
VAL
ILE
VAL
LYS


SEQRES
39
A
503
ASP
ARG
ILE
ASN
ASP
TYR
HIS
PRO
LYS













HET
K
A
900

1



HET
XMP

602
24


HET
MOA

600
23










HETNAM

K
POTASSIUM ION


HETNAM

XMP
XANTHOSINE-5′-MONOPHOSPHATE


HETNAM

MOA
MYCOPHENOLIC ACID


HETSYN

XMP
5--MONOPHOSPHATE-9-BETA-D-RIBOFURANOSYL XANTHINE


HETSYN

MOA
6-(1,3-DIHYDRO-7-HYDROXY-5-METHOXY-4-METHYL-1-


HETSYN
2
MOA
OXOISOBENZOFURAN-6-YL)-4-METHYL-4-HEXANOIC ACID















FORMUL
2
K
 K1
1+






FORMUL
3
XMP
 C10
H14
N4
O9
P1
1+


FORMUL
4
MOA
 C17
H20
O6










FORMUL
5
HOH
*180(H2 01)


















HELIX
1
1
THR
A
 11
ASN
A
 13
5

3


HELIX
2
2
ILE
A
 27
VAL
A
 31
5

5


HELIX
3
3
GLY
A
 64
GLU
A
 74
1

11


HELIX
4
4
SER
A
 85
ASN
A
 98
1

14


HELIX
5
5
ASP
A
242
GLY
A
254
1

13


HELIX
6
6
SER
A
267
GLY
A
282
1

16


HELIX
7
7
ASP
A
283
VAL
A
285
5

3


HELIX
8
8
ASP
A
294
GLY
A
305
1

12


HELIX
9
9
GLY
A
330
GLY
A
350
1

21


HELIX
10 
10 
TYR
A
363
MET
A
373
1

11


HELIX
11 
11 
GLY
A
381
ARG
A
386
1

6


HELIX
12 
12 
SER
A
410
ASN
A
415
1

6


HELIX
13 
13 
LYS
A
442
CYS
A
461
1

20


HELIX
14 
14 
THR
A
465
ALA
A
473
1

9

























SHEET
1
A
2 TYR
A
 15
ILE
A
 18
0











SHEET
2
A
2 LYS
A
474
LEU
A
477
−1
O
LYS
A
474
N
ILE
A
 18


SHEET
1
B
2 THR
A
 35
PRO
A
 36
0


SHEET
2
B
2 ASN
A
 49
LEU
A
 50
−1
O
LEU
A
 50
N
THR
A
 35


SHEET
1
C
2 PHE
A
 40
GLN
A
 41
0


SHEET
2
C
2 ILE
A
351
TYR
A
352
−1
O
TYR
A
352
N
PHE
A
 40


SHEET
1
D
9 LEU
A
 54
SER
A
 56
0


SHEET
2
D
9 ILE
A
 77
ILE
A
 80
1
O
ILE
A
 77
N
SER
A
 56


SHEET
3
D
9 GLY
A
235
ILE
A
238
1
O
GLY
A
237
N
ILE
A
 80


SHEET
4
D
9 VAL
A
257
ILE
A
260
1
O
CYS
A
259
N
ILE
A
238


SHEET
5
D
9 VAL
A
287
ILE
A
292
1
O
GLY
A
288
N
LEU
A
258


SHEET
6
D
9 PHE
A
308
ILE
A
311
1
O
LYS
A
310
N
ALA
A
289


SHEET
7
D
9 VAL
A
355
ASP
A
358
1
O
CYS
A
356
N
ILE
A
311


SHEET
8
D
9 PHE
A
377
LEU
A
380
1
O
PHE
A
377
N
SER
A
357


SHEET
9
D
9 LEU
A
 54
SER
A
 56
1
N
VAL
A
 55
O
ILE
A
378


SHEET
1
E
3 LYS
A
394
ILE
A
397
0


SHEET
2
E
3 SER
A
400
TRP
A
406
−1
O
MET
A
402
N
VAL
A
395


SHEET
3
E
3 ASP
A
434
PRO
A
438
−1
O
SER
A
435
N
TYR
A
405

















SSBOND
1
CYS
A
 26
CYS
A
459





CISPEP
1
GLY
A
290
ASN
A
291
0
0.82
















CRYST1
155.070
155.070
155.070
90.00
90.00
90.00
P 4 3 2
24














ORIGX1
1.000000
0.000000
0.000000

0.00000



ORIGX2
0.000000
1.000000
0.000000

0.00000


ORIGX3
0.000000
0.000000
1.000000

0.00000


SCALE1
0.006449
0.000000
0.000000

0.00000


SCALE2
0.000000
0.006449
0.000000

0.00000


SCALE3
0.000000
0.000000
0.006449

0.00000


















ATOM
1
N
ALA
A
2
55.246
75.030
36.667
1.00
28.12
N


ATOM
2
CA
ALA
A
2
56.014
73.998
35.916
1.00
26.83
C


ATOM
3
C
ALA
A
2
57.303
73.637
36.651
1.00
27.59
C


ATOM
4
O
ALA
A
2
57.744
74.364
37.542
1.00
26.06
O


ATOM
S
CB
ALA
A
2
56.331
74.512
34.522
1.00
27.30
C


ATOM
6
N
LYS
A
3
57.901
72.510
36.272
1.00
27.55
N


ATOM
7
CA
LYS
A
3
59.139
72.052
36.891
1.00
28.66
C


ATOM
8
C
LYS
A
3
60.304
72.241
35.923
1.00
28.28
C


ATOM
9
O
LYS
A
3
60.213
71.877
34.751
1.00
28.88
O


ATOM
10
CB
LYS
A
3
59.022
70.571
37.276
1.00
30.08
C


ATOM
11
CG
LYS
A
3
60.256
70.001
37.985
1.00
34.20
C


ATOM
12
CD
LYS
A
3
60.835
68.809
37.222
1.00
37.41
C


ATOM
13
CE
LYS
A
3
61.981
68.154
37.977
1.00
38.58
C


ATOM
14
NZ
LYS
A
3
63.081
69.118
38.256
1.00
40.73
N


ATOM
15
N
TYR
A
4
61.396
72.809
36.424
1.00
27.63
N


ATOM
16
CA
TYR
A
4
62.589
73.060
35.617
1.00
27.84
C


ATOM
17
C
TYR
A
4
63.789
72.257
36.120
1.00
29.05
C


ATOM
18
O
TYR
A
4
63.729
71.620
37.168
1.00
28.98
O


ATOM
19
CB
TYR
A
4
62.906
74.559
35.635
1.00
26.14
C


ATOM
20
CG
TYR
A
4
61.816
75.386
34.994
1.00
26.21
C


ATOM
21
CD1
TYR
A
4
61.746
75.528
33.607
1.00
24.20
C


ATOM
22
CD2
TYR
A
4
60.819
75.981
35.769
1.00
26.83
C


ATOM
23
CE1
TYR
A
4
60.707
76.243
33.007
1.00
24.96
C


ATOM
24
CE2
TYR
A
4
59.773
76.699
35.177
1.00
26.60
C


ATOM
25
CZ
TYR
A
4
59.726
76.824
33.799
1.00
25.65
C


ATOM
26
OH
TYR
A
4
58.698
77.523
33.215
1.00
25.82
O


ATOM
27
N
TYR
A
5
64.880
72.288
35.362
1.00
30.21
N


ATOM
28
CA
TYR
A
5
66.082
71.556
35.732
1.00
31.29
C


ATOM
29
C
TYR
A
5
67.275
72.487
35.860
1.00
32.27
C


ATOM
30
O
TYR
A
5
67.313
73.551
35.241
1.00
33.48
O


ATOM
31
CB
TYR
A
5
66.370
70.467
34.700
1.00
30.15
C


ATOM
32
CG
TYR
A
5
65.246
69.467
34.568
1.00
30.45
C


ATOM
33
CD1
TYR
A
5
64.076
69.789
33.876
1.00
30.10
C


ATOM
34
CD2
TYR
A
5
65.338
68.203
35.158
1.00
29.26
C


ATOM
35
CE1
TYR
A
5
63.028
68.879
33.775
1.00
30.02
C


ATOM
36
CE2
TYR
A
5
64.298
67.289
35.064
1.00
29.82
C


ATOM
37
CZ
TYR
A
5
63.147
67.632
34.372
1.00
30.16
C


ATOM
38
OH
TYR
A
5
62.122
66.728
34.277
1.00
29.57
O


ATOM
39
N
ASN
A
6
68.249
72.079
36.667
1.00
33.12
N


ATOM
40
CA
ASN
A
6
69.445
72.880
36.903
1.00
34.04
C


ATOM
41
C
ASN
A
6
70.421
72.883
35.732
1.00
33.43
C


ATOM
42
O
ASN
A
6
71.190
73.827
35.569
1.00
34.04
O


ATOM
43
CB
ASN
A
6
70.158
72.380
38.162
1.00
36.54
C


ATOM
44
CG
ASN
A
6
69.322
72.563
39.417
1.00
40.37
C


ATOM
45
OD1
ASN
A
6
69.335
71.716
40.315
1.00
42.93
O


ATOM
46
ND2
ASN
A
6
68.597
73.679
39.493
1.00
41.40
N


ATOM
47
N
GLU
A
7
70.388
71.839
34.912
1.00
32.19
N


ATOM
48
CA
GLU
A
7
71.301
71.749
33.774
1.00
30.55
C


ATOM
49
C
GLU
A
7
70.588
71.404
32.477
1.00
28.37
C


ATOM
50
O
GLU
A
7
69.563
70.724
32.483
1.00
27.97
O


ATOM
51
CB
GLU
A
7
72.365
70.671
34.030
1.00
32.84
C


ATOM
52
CG
GLU
A
7
73.323
70.926
35.203
1.00
36.46
C


ATOM
53
CD
GLU
A
7
74.235
72.121
34.978
1.00
38.59
C


ATOM
54
OE1
GLU
A
7
74.649
72.348
33.821
1.00
39.18
O


ATOM
55
OE2
GLU
A
7
74.552
72.828
35.961
1.00
41.76
O


ATOM
56
N
PRO
A
8
71.125
71.868
31.339
1.00
26.18
N


ATOM
57
CA
PRO
A
8
70.484
71.549
30.062
1.00
25.74
C


ATOM
58
C
PRO
A
8
70.830
70.098
29.736
1.00
25.66
C


ATOM
59
O
PRO
A
8
71.796
69.561
30.281
1.00
25.70
O


ATOM
60
CB
PRO
A
8
71.140
72.530
29.094
1.00
25.89
C


ATOM
61
CG
PRO
A
8
72.531
72.678
29.661
1.00
24.82
C


ATOM
62
CD
PRO
A
8
72.270
72.780
31.149
1.00
25.95
C


ATOM
63
N
CYS
A
9
70.053
69.457
28.869
1.00
25.32
N


ATOM
64
CA
CYS
A
9
70.342
68.074
28.501
1.00
25.12
C


ATOM
65
C
CYS
A
9
71.405
68.030
27.396
1.00
24.58
C


ATOM
66
O
CYS
A
9
71.599
69.009
26.674
1.00
24.57
O


ATOM
67
CB
CYS
A
9
69.058
67.354
28.064
1.00
25.98
C


ATOM
68
SG
CYS
A
9
68.140
68.110
26.701
1.00
28.89
S


ATOM
69
N
HIS
A
10
72.087
66.895
27.267
1.00
23.82
N


ATOM
70
CA
HIS
A
10
73.159
66.735
26.284
1.00
22.97
C


ATOM
71
C
HIS
A
10
73.016
65.458
25.450
1.00
23.29
C


ATOM
72
O
HIS
A
10
72.389
64.491
25.886
1.00
22.16
O


ATOM
73
CB
HIS
A
10
74.505
66.695
27.013
1.00
23.38
C


ATOM
74
CG
HIS
A
10
74.767
67.892
27.874
1.00
24.01
C


ATOM
75
ND1
HIS
A
10
75.212
69.094
27.364
1.00
23.71
N


ATOM
76
CD2
HIS
A
10
74.645
68.071
29.211
1.00
23.36
C


ATOM
77
CE1
HIS
A
10
75.353
69.962
28.351
1.00
22.56
C


ATOM
78
NE2
HIS
A
10
75.015
69.366
29.481
1.00
23.59
N


ATOM
79
N
THR
A
11
73.605
65.462
24.255
1.00
23.11
N


ATOM
80
CA
THR
A
11
73.573
64.300
23.362
1.00
23.58
C


ATOM
81
C
THR
A
11
74.920
63.571
23.464
1.00
23.26
C


ATOM
82
O
THR
A
11
75.858
64.093
24.061
1.00
22.66
O


ATOM
83
CB
THR
A
11
73.360
64.719
21.889
1.00
24.09
C


ATOM
84
OG1
THR
A
11
74.439
65.562
21.475
1.00
25.91
O


ATOM
85
CG2
THR
A
11
72.049
65.480
21.727
1.00
25.24
C


ATOM
86
N
PHE
A
12
75.017
62.377
22.881
1.00
23.30
N


ATOM
87
CA
PHE
A
12
76.262
61.609
22.931
1.00
24.87
C


ATOM
88
C
PHE
A
12
77.458
62.328
22.304
1.00
26.16
C


ATOM
89
O
PHE
A
12
78.596
62.112
22.713
1.00
26.04
O


ATOM
90
CB
PHE
A
12
76.096
60.243
22.249
1.00
23.25
C


ATOM
91
CG
PHE
A
12
75.216
59.284
23.004
1.00
23.37
C


ATOM
92
CD1
PHE
A
12
75.362
59.119
24.377
1.00
22.09
C


ATOM
93
CD2
PHE
A
12
74.253
58.537
22.337
1.00
22.79
C


ATOM
94
CE1
PHE
A
12
74.560
58.223
25.078
1.00
23.40
C


ATOM
95
CE2
PHE
A
12
73.443
57.634
23.027
1.00
24.01
C


ATOM
96
CZ
PHE
A
12
73.596
57.476
24.399
1.00
22.98
C


ATOM
97
N
ASN
A
13
77.202
63.173
21.310
1.00
26.96
N


ATOM
98
CA
ASN
A
13
78.273
63.905
20.637
1.00
28.09
C


ATOM
99
C
ASN
A
13
78.998
64.901
21.533
1.00
26.75
C


ATOM
100
O
ASN
A
13
80.044
65.420
21.152
1.00
27.23
O


ATOM
101
CB
ASN
A
13
77.734
64.663
19.417
1.00
31.04
C


ATOM
102
CG
ASN
A
13
77.622
63.787
18.183
1.00
36.11
C


ATOM
103
OD1
ASN
A
13
78.522
63.000
17.883
1.00
39.98
O


ATOM
104
ND2
ASN
A
13
76.526
63.934
17.448
1.00
38.57
N


ATOM
105
N
GLU
A
14
78.445
65.178
22.710
1.00
25.07
N


ATOM
106
CA
GLU
A
14
79.060
66.136
23.621
1.00
25.01
C


ATOM
107
C
GLU
A
14
79.976
65.483
24.650
1.00
25.17
C


ATOM
108
O
GLU
A
14
80.464
66.148
25.563
1.00
26.57
O


ATOM
109
CB
GLU
A
14
77.976
66.937
24.348
1.00
25.02
C


ATOM
110
CG
GLU
A
14
77.000
67.638
23.420
1.00
25.34
C


ATOM
111
CD
GLU
A
14
75.926
68.401
24.169
1.00
25.36
C


ATOM
112
OE1
GLU
A
14
76.272
69.314
24.947
1.00
25.19
O


ATOM
113
OE2
GLU
A
14
74.734
68.083
23.978
1.00
26.80
O


ATOM
114
N
TYR
A
15
80.229
64.189
24.499
1.00
24.38
N


ATOM
115
CA
TYR
A
15
81.067
63.487
25.455
1.00
23.13
C


ATOM
116
C
TYR
A
15
82.248
62.754
24.856
1.00
23.75
C


ATOM
117
O
TYR
A
15
82.230
62.360
23.691
1.00
24.15
O


ATOM
118
CB
TYR
A
15
80.224
62.478
26.238
1.00
22.70
C


ATOM
119
CG
TYR
A
15
79.201
63.097
27.153
1.00
23.45
C


ATOM
120
CD1
TYR
A
15
79.519
63.416
28.474
1.00
23.71
C


ATOM
121
CD2
TYR
A
15
77.909
63.361
26.702
1.00
24.00
C


ATOM
122
CE1
TYR
A
15
78.571
63.977
29.326
1.00
25.23
C


ATOM
123
CE2
TYR
A
15
76.954
63.927
27.544
1.00
25.30
C


ATOM
124
CZ
TYR
A
15
77.288
64.231
28.851
1.00
25.69
C


ATOM
125
OH
TYR
A
15
76.342
64.793
29.680
1.00
29.22
O


ATOM
126
N
LEU
A
16
83.273
62.570
25.681
1.00
24.09
N


ATOM
127
CA
LEU
A
16
84.470
61.830
25.301
1.00
24.11
C


ATOM
128
C
LEU
A
16
84.866
61.010
26.519
1.00
23.10
C


ATOM
129
O
LEU
A
16
84.525
61.360
27.649
1.00
22.07
O


ATOM
130
CB
LEU
A
16
85.625
62.767
24.922
1.00
24.98
C


ATOM
131
CG
LEU
A
16
85.590
63.480
23.569
1.00
26.50
C


ATOM
132
CD1
LEU
A
16
86.770
64.421
23.467
1.00
28.14
C


ATOM
133
CD2
LEU
A
16
85.635
62.471
22.444
1.00
28.66
C


ATOM
134
N
LEU
A
17
85.572
59.913
26.279
1.00
23.04
N


ATOM
135
CA
LEU
A
17
86.047
59.040
27.346
1.00
23.77
C


ATOM
136
C
LEU
A
17
87.512
59.362
27.630
1.00
23.70
C


ATOM
137
O
LEU
A
17
88.301
59.540
26.706
1.00
23.54
O


ATOM
138
CB
LEU
A
17
85.929
57.569
26.923
1.00
22.71
C


ATOM
139
CG
LEU
A
17
84.511
56.990
26.882
1.00
23.40
C


ATOM
140
CD1
LEU
A
17
84.480
55.739
26.022
1.00
23.07
C


ATOM
141
CD2
LEU
A
17
84.047
56.698
28.301
1.00
21.29
C


ATOM
142
N
ILE
A
18
87.860
59.456
28.909
1.00
24.51
N


ATOM
143
CA
ILE
A
18
89.236
59.720
29.313
1.00
24.55
C


ATOM
144
C
ILE
A
18
89.803
58.357
29.705
1.00
24.94
C


ATOM
145
O
ILE
A
18
89.236
57.670
30.545
1.00
25.77
O


ATOM
146
CB
ILE
A
18
89.279
60.687
30.509
1.00
24.40
C


ATOM
147
CG1
ILE
A
18
88.798
62.071
30.054
1.00
25.23
C


ATOM
148
CG2
ILE
A
18
90.696
60.750
31.089
1.00
24.00
C


ATOM
149
CD1
ILE
A
18
88.754
63.115
31.149
1.00
26.14
C


ATOM
150
N
PRO
A
19
90.921
57.942
29.089
1.00
24.65
N


ATOM
151
CA
PRO
A
19
91.519
56.640
29.402
1.00
26.08
C


ATOM
152
C
PRO
A
19
91.842
56.372
30.868
1.00
26.01
C


ATOM
153
O
PRO
A
19
92.120
57.288
31.646
1.00
25.83
O


ATOM
154
CB
PRO
A
19
92.787
56.610
28.533
1.00
26.14
C


ATOM
155
CG
PRO
A
19
92.431
57.503
27.375
1.00
26.01
C


ATOM
156
CD
PRO
A
19
91.708
58.646
28.061
1.00
24.66
C


ATOM
157
N
GLY
A
20
91.792
55.092
31.221
1.00
25.78
N


ATOM
158
CA
GLY
A
20
92.118
54.654
32.564
1.00
25.89
C


ATOM
159
C
GLY
A
20
93.331
53.748
32.425
1.00
26.31
C


ATOM
160
O
GLY
A
20
93.940
53.671
31.353
1.00
26.09
O


ATOM
161
N
LEU
A
21
93.692
53.052
33.492
1.00
27.91
N


ATOM
162
CA
LEU
A
21
94.842
52.161
33.436
1.00
28.51
C


ATOM
163
C
LEU
A
21
94.522
50.917
32.626
1.00
28.22
C


ATOM
164
O
LEU
A
21
93.599
50.178
32.950
1.00
28.84
O


ATOM
165
CB
LEU
A
21
95.281
51.748
34.850
1.00
28.54
C


ATOM
166
CG
LEU
A
21
96.424
50.721
34.929
1.00
28.79
C


ATOM
167
CD1
LEU
A
21
97.661
51.272
34.230
1.00
25.50
C


ATOM
168
CD2
LEU
A
21
96.726
50.390
36.394
1.00
28.73
C


ATOM
169
N
SER
A
22
95.284
50.697
31.562
1.00
29.18
N


ATOM
170
CA
SER
A
22
95.099
49.525
30.725
1.00
30.50
C


ATOM
171
C
SER
A
22
96.101
48.467
31.171
1.00
32.47
C


ATOM
172
O
SER
A
22
97.310
48.684
31.107
1.00
31.83
O


ATOM
173
CB
SER
A
22
95.340
49.874
29.259
1.00
30.15
C


ATOM
174
OG
SER
A
22
94.432
50.858
28.813
1.00
31.65
O


ATOM
175
N
THR
A
23
95.595
47.327
31.630
1.00
35.11
N


ATOM
176
CA
THR
A
23
96.451
46.237
32.090
1.00
36.70
C


ATOM
177
C
THR
A
23
96.864
45.327
30.941
1.00
37.53
C


ATOM
178
O
THR
A
23
96.241
45.331
29.879
1.00
38.20
O


ATOM
179
CB
THR
A
23
95.741
45.392
33.155
1.00
37.23
C


ATOM
180
OG1
THR
A
23
94.462
44.985
32.660
1.00
40.43
O


ATOM
181
CG2
THR
A
23
95.552
46.191
34.429
1.00
37.20
C


ATOM
182
N
VAL
A
24
97.919
44.547
31.159
1.00
38.34
N


ATOM
183
CA
VAL
A
24
98.425
43.636
30.135
1.00
38.85
C


ATOM
184
C
VAL
A
24
97.396
42.605
29.666
1.00
39.73
C


ATOM
185
O
VAL
A
24
97.401
42.203
28.499
1.00
39.77
O


ATOM
186
CB
VAL
A
24
99.700
42.886
30.625
1.00
39.23
C


ATOM
187
CG1
VAL
A
24
100.851
43.871
30.800
1.00
38.15
C


ATOM
188
CG2
VAL
A
24
99.418
42.167
31.938
1.00
38.35
C


ATOM
189
N
ASP
A
25
96.506
42.186
30.560
1.00
40.55
N


ATOM
190
CA
ASP
A
25
95.503
41.195
30.186
1.00
43.23
C


ATOM
191
C
ASP
A
25
94.328
41.733
29.370
1.00
42.88
C


ATOM
192
O
ASP
A
25
93.485
40.951
28.933
1.00
43.24
O


ATOM
193
CB
ASP
A
25
94.956
40.476
31.425
1.00
45.78
C


ATOM
194
CG
ASP
A
25
94.301
41.421
32.405
1.00
48.75
C


ATOM
195
OD1
ASP
A
25
93.333
41.010
33.083
1.00
49.75
O


ATOM
196
OD2
ASP
A
25
94.764
42.574
32.503
1.00
50.54
O


ATOM
197
N
CYS
A
26
94.257
43.045
29.150
1.00
42.32
N


ATOM
198
CA
CYS
A
26
93.137
43.581
28.377
1.00
41.35
C


ATOM
199
C
CYS
A
26
93.440
43.763
26.903
1.00
41.34
C


ATOM
200
O
CYS
A
26
94.067
44.738
26.496
1.00
41.54
O


ATOM
201
CB
CYS
A
26
92.640
44.924
28.943
1.00
39.84
C


ATOM
202
SG
CYS
A
26
90.919
45.372
28.462
1.00
36.85
S


ATOM
203
N
ILE
A
27
92.992
42.802
26.108
1.00
42.52
N


ATOM
204
CA
ILE
A
27
93.142
42.857
24.664
1.00
43.62
C


ATOM
205
C
ILE
A
27
91.725
42.630
24.152
1.00
44.10
C


ATOM
206
O
ILE
A
27
90.935
41.930
24.789
1.00
43.64
O


ATOM
207
CB
ILE
A
27
94.086
41.748
24.125
1.00
45.23
C


ATOM
208
CG1
ILE
A
27
93.613
40.374
24.601
1.00
45.47
C


ATOM
209
CG2
ILE
A
27
95.519
42.019
24.579
1.00
44.91
C


ATOM
210
CD1
ILE
A
27
94.479
39.224
24.114
1.00
47.61
C


ATOM
211
N
PRO
A
28
91.377
43.235
23.010
1.00
44.56
N


ATOM
212
CA
PRO
A
28
90.041
43.090
22.429
1.00
44.54
C


ATOM
213
C
PRO
A
28
89.474
41.673
22.450
1.00
44.69
C


ATOM
214
O
PRO
A
28
88.312
41.471
22.801
1.00
44.73
O


ATOM
215
CB
PRO
A
28
90.233
43.625
21.016
1.00
45.21
C


ATOM
216
CG
PRO
A
28
91.205
44.738
21.239
1.00
44.60
C


ATOM
217
CD
PRO
A
28
92.221
44.104
22.170
1.00
44.85
C


ATOM
218
N
SER
A
29
90.292
40.692
22.082
1.00
44.42
N


ATOM
219
CA
SER
A
29
89.835
39.307
22.048
1.00
43.86
C


ATOM
220
C
SER
A
29
89.390
38.767
23.405
1.00
42.44
C


ATOM
221
O
SER
A
29
88.605
37.821
23.468
1.00
43.23
O


ATOM
222
CB
SER
A
29
90.926
38.400
21.455
1.00
45.84
C


ATOM
223
OG
SER
A
29
92.107
38.401
22.241
1.00
48.98
O


ATOM
224
N
ASN
A
30
89.878
39.357
24.491
1.00
40.37
N


ATOM
225
CA
ASN
A
30
89.489
38.892
25.819
1.00
39.43
C


ATOM
226
C
ASN
A
30
88.330
39.695
26.417
1.00
37.05
C


ATOM
227
O
ASN
A
30
87.912
39.442
27.548
1.00
36.90
O


ATOM
228
CB
ASN
A
30
90.677
38.942
26.788
1.00
41.28
C


ATOM
229
CG
ASN
A
30
91.830
38.061
26.348
1.00
44.29
C


ATOM
230
OD1
ASN
A
30
91.638
37.064
25.648
1.00
45.64
O


ATOM
231
ND2
ASN
A
30
93.040
38.417
26.773
1.00
44.79
N


ATOM
232
N
VAL
A
31
87.817
40.666
25.668
1.00
34.05
N


ATOM
233
CA
VAL
A
31
86.716
41.478
26.169
1.00
31.36
C


ATOM
234
C
VAL
A
31
85.404
40.711
26.051
1.00
30.32
C


ATOM
235
O
VAL
A
31
85.090
40.149
25.005
1.00
28.53
O


ATOM
236
CB
VAL
A
31
86.615
42.823
25.404
1.00
31.14
C


ATOM
237
CG1
VAL
A
31
85.429
43.641
25.919
1.00
29.88
C


ATOM
238
CG2
VAL
A
31
87.910
43.612
25.579
1.00
29.52
C


ATOM
239
N
ASN
A
32
84.653
40.680
27.144
1.00
29.79
N


ATOM
240
CA
ASN
A
32
83.369
39.987
27.195
1.00
30.76
C


ATOM
241
C
ASN
A
32
82.246
41.013
27.030
1.00
30.01
C


ATOM
242
O
ASN
A
32
82.095
41.908
27.860
1.00
29.60
O


ATOM
243
CB
ASN
A
32
83.244
39.266
28.541
1.00
32.62
C


ATOM
244
CG
ASN
A
32
81.916
38.549
28.716
1.00
34.80
C


ATOM
245
OD1
ASN
A
32
81.640
38.004
29.786
1.00
38.96
O


ATOM
246
ND2
ASN
A
32
81.093
38.538
27.676
1.00
32.90
N


ATOM
247
N
LEU
A
33
81.458
40.872
25.964
1.00
29.61
N


ATOM
248
CA
LEU
A
33
80.361
41.798
25.677
1.00
29.44
C


ATOM
249
C
LEU
A
33
78.961
41.292
26.050
1.00
29.73
C


ATOM
250
O
LEU
A
33
77.955
41.805
25.555
1.00
29.64
O


ATOM
251
CB
LEU
A
33
80.397
42.176
24.191
1.00
30.47
C


ATOM
252
CG
LEU
A
33
80.910
43.558
23.761
1.00
31.37
C


ATOM
253
CD1
LEU
A
33
81.975
44.091
24.699
1.00
30.40
C


ATOM
254
CD2
LEU
A
33
81.439
43.446
22.350
1.00
31.39
C


ATOM
255
N
SER
A
34
78.892
40.289
26.920
1.00
28.68
N


ATOM
256
CA
SER
A
34
77.605
39.752
27.360
1.00
28.45
C


ATOM
257
C
SER
A
34
76.885
40.800
28.197
1.00
26.82
C


ATOM
258
O
SER
A
34
77.521
41.633
28.840
1.00
27.22
O


ATOM
259
CB
SER
A
34
77.812
38.502
28.216
1.00
28.51
C


ATOM
260
OG
SER
A
34
78.504
37.518
27.477
1.00
35.24
O


ATOM
261
N
THR
A
35
75.561
40.750
28.209
1.00
24.82
N


ATOM
262
CA
THR
A
35
74.795
41.709
28.982
1.00
23.94
C


ATOM
263
C
THR
A
35
73.380
41.170
29.201
1.00
24.11
C


ATOM
264
O
THR
A
35
72.834
40.470
28.349
1.00
25.00
O


ATOM
265
CB
THR
A
35
74.752
43.084
28.251
1.00
24.28
C


ATOM
266
OG1
THR
A
35
74.409
44.117
29.181
1.00
24.41
O


ATOM
267
CG2
THR
A
35
73.728
43.069
27.126
1.00
21.95
C


ATOM
268
N
PRO
A
36
72.776
41.478
30.358
1.00
23.32
N


ATOM
269
CA
PRO
A
36
71.419
41.023
30.687
1.00
22.99
C


ATOM
270
C
PRO
A
36
70.304
41.697
29.881
1.00
24.25
C


ATOM
271
O
PRO
A
36
70.321
42.912
29.670
1.00
23.91
O


ATOM
272
CB
PRO
A
36
71.309
41.328
32.177
1.00
22.91
C


ATOM
273
CG
PRO
A
36
72.159
42.567
32.321
1.00
22.08
C


ATOM
274
CD
PRO
A
36
73.370
42.236
31.475
1.00
22.10
C


ATOM
275
N
LEU
A
37
69.329
40.900
29.447
1.00
24.03
N


ATOM
276
CA
LEU
A
37
68.201
41.407
28.677
1.00
24.03
C


ATOM
277
C
LEU
A
37
66.974
41.670
29.552
1.00
24.86
C


ATOM
278
O
LEU
A
37
66.293
42.684
29.385
1.00
25.14
O


ATOM
279
CB
LEU
A
37
67.825
40.420
27.567
1.00
24.13
C


ATOM
280
CG
LEU
A
37
66.707
40.862
26.614
1.00
25.46
C


ATOM
281
CD1
LEU
A
37
67.191
42.043
25.759
1.00
24.90
C


ATOM
282
CD2
LEU
A
37
66.306
39.698
25.708
1.00
25.09
C


ATOM
283
N
VAL
A
38
66.691
40.767
30.487
1.00
24.24
N


ATOM
284
CA
VAL
A
38
65.525
40.920
31.347
1.00
24.00
C


ATOM
285
C
VAL
A
38
65.889
40.950
32.820
1.00
25.63
C


ATOM
286
O
VAL
A
38
66.942
40.454
33.215
1.00
26.92
O


ATOM
287
CB
VAL
A
38
64.488
39.802
31.074
1.00
24.41
C


ATOM
288
CG1
VAL
A
38
64.014
39.890
29.623
1.00
21.19
C


ATOM
289
CG2
VAL
A
38
65.100
38.427
31.349
1.00
23.21
C


ATOM
290
N
LYS
A
39
65.003
41.527
33.629
1.00
25.88
N


ATOM
291
CA
LYS
A
39
65.240
41.686
35.060
1.00
27.51
C


ATOM
292
C
LYS
A
39
65.422
40.413
35.869
1.00
28.51
C


ATOM
293
O
LYS
A
39
64.916
39.351
35.513
1.00
29.00
O


ATOM
294
CB
LYS
A
39
64.121
42.513
35.697
1.00
27.27
C


ATOM
295
CG
LYS
A
39
62.754
41.843
35.661
1.00
28.27
C


ATOM
296
CD
LYS
A
39
61.751
42.595
36.514
1.00
27.78
C


ATOM
297
CE
LYS
A
39
60.369
41.943
36.448
1.00
29.12
C


ATOM
298
NZ
LYS
A
39
59.401
42.617
37.361
1.00
28.02
N


ATOM
299
N
PHE
A
40
66.152
40.556
36.973
1.00
28.42
N


ATOM
300
CA
PHE
A
40
66.439
39.470
37.893
1.00
29.14
C


ATOM
301
C
PHE
A
40
66.668
40.063
39.278
1.00
30.30
C


ATOM
302
O
PHE
A
40
66.794
41.278
39.421
1.00
30.54
O


ATOM
303
CB
PHE
A
40
67.687
38.697
37.449
1.00
28.10
C


ATOM
304
CG
PHE
A
40
68.913
39.558
37.251
1.00
27.25
C


ATOM
305
CD1
PHE
A
40
69.163
40.167
36.023
1.00
25.59
C


ATOM
306
CD2
PHE
A
40
69.824
39.743
38.287
1.00
25.17
C


ATOM
307
CE1
PHE
A
40
70.304
40.944
35.830
1.00
25.72
C


ATOM
308
CE2
PHE
A
40
70.968
40.518
38.106
1.00
25.52
C


ATOM
309
CZ
PHE
A
40
71.211
41.120
36.873
1.00
26.27
C


ATOM
310
N
GLN
A
41
66.713
39.200
40.291
1.00
31.34
N


ATOM
311
CA
GLN
A
41
66.927
39.622
41.672
1.00
33.56
C


ATOM
312
C
GLN
A
41
68.408
39.585
41.998
1.00
32.76
C


ATOM
313
O
GLN
A
41
69.183
38.929
41.305
1.00
32.65
O


ATOM
314
CB
GLN
A
41
66.190
38.685
42.641
1.00
36.73
C


ATOM
315
CG
GLN
A
41
64.681
38.719
42.523
1.00
42.60
C


ATOM
316
CD
GLN
A
41
64.087
40.002
43.073
1.00
45.09
C


ATOM
317
OE1
GLN
A
41
62.956
40.359
42.749
1.00
48.80
O


ATOM
318
NE2
GLN
A
41
64.842
40.693
43.921
1.00
48.01
N


ATOM
319
N
LYS
A
42
68.798
40.280
43.061
1.00
32.91
N


ATOM
320
CA
LYS
A
42
70.191
40.291
43.471
1.00
34.34
C


ATOM
321
C
LYS
A
42
70.670
38.865
43.747
1.00
34.29
C


ATOM
322
O
LYS
A
42
69.934
38.055
44.311
1.00
32.99
O


ATOM
323
CB
LYS
A
42
70.382
41.129
44.731
1.00
35.20
C


ATOM
324
CG
LYS
A
42
71.849
41.328
45.053
1.00
39.21
C


ATOM
325
CD
LYS
A
42
72.079
42.234
46.244
1.00
42.37
C


ATOM
326
CE
LYS
A
42
71.760
41.547
47.549
1.00
42.56
C


ATOM
327
NZ
LYS
A
42
72.329
42.327
48.680
1.00
43.58
N


ATOM
328
N
GLY
A
43
71.902
38.568
43.345
1.00
34.17
N


ATOM
329
CA
GLY
A
43
72.457
37.244
43.565
1.00
34.57
C


ATOM
330
C
GLY
A
43
72.186
36.277
42.431
1.00
34.77
C


ATOM
331
O
GLY
A
43
72.784
35.202
42.361
1.00
34.67
O


ATOM
332
N
GLN
A
44
71.282
36.655
41.538
1.00
35.36
N


ATOM
333
CA
GLN
A
44
70.942
35.810
40.403
1.00
36.05
C


ATOM
334
C
GLN
A
44
71.551
36.364
39.123
1.00
35.80
C


ATOM
335
O
GLN
A
44
72.230
37.390
39.138
1.00
35.18
O


ATOM
336
CB
GLN
A
44
69.422
35.740
40.228
1.00
38.46
C


ATOM
337
CG
GLN
A
44
68.644
35.556
41.517
1.00
42.54
C


ATOM
338
CD
GLN
A
44
67.145
35.481
41.281
1.00
44.54
C


ATOM
339
OE1
GLN
A
44
66.583
36.271
40.517
1.00
46.34
O


ATOM
340
NE2
GLN
A
44
66.487
34.539
41.945
1.00
44.29
N


ATOM
341
N
GLN
A
45
71.299
35.664
38.022
1.00
35.96
N


ATOM
342
CA
GLN
A
45
71.759
36.055
36.695
1.00
36.42
C


ATOM
343
C
GLN
A
45
70.469
36.221
35.907
1.00
35.19
C


ATOM
344
O
GLN
A
45
69.435
35.682
36.293
1.00
35.44
O


ATOM
345
CB
GLN
A
45
72.586
34.943
36.039
1.00
39.65
C


ATOM
346
CG
GLN
A
45
73.865
34.569
36.763
1.00
44.40
C


ATOM
347
CD
GLN
A
45
74.951
35.614
36.610
1.00
47.78
C


ATOM
348
OE1
GLN
A
45
75.471
35.834
35.510
1.00
50.39
O


ATOM
349
NE2
GLN
A
45
75.303
36.266
37.714
1.00
48.43
N


ATOM
350
N
SER
A
46
70.519
36.967
34.812
1.00
32.83
N


ATOM
351
CA
SER
A
46
69.333
37.154
33.995
1.00
32.14
C


ATOM
352
C
SER
A
46
69.040
35.856
33.244
1.00
32.13
C


ATOM
353
O
SER
A
46
69.962
35.137
32.864
1.00
32.53
O


ATOM
354
CB
SER
A
46
69.554
38.289
32.996
1.00
29.54
C


ATOM
355
OG
SER
A
46
68.415
38.451
32.179
1.00
28.47
O


ATOM
356
N
GLU
A
47
67.762
35.562
33.032
1.00
32.14
N


ATOM
357
CA
GLU
A
47
67.364
34.355
32.318
1.00
32.15
C


ATOM
358
C
GLU
A
47
67.768
34.441
30.856
1.00
31.61
C


ATOM
359
O
GLU
A
47
67.865
33.424
30.169
1.00
30.42
O


ATOM
360
CB
GLU
A
47
65.853
34.154
32.418
1.00
34.33
C


ATOM
361
CG
GLU
A
47
65.358
33.856
33.823
1.00
37.88
C


ATOM
362
CD
GLU
A
47
63.844
33.834
33.905
1.00
41.09
C


ATOM
363
OE1
GLU
A
47
63.226
32.981
33.231
1.00
43.20
O


ATOM
364
OE2
GLU
A
47
63.271
34.671
34.639
1.00
43.10
O


ATOM
365
N
ILE
A
48
67.978
35.663
30.373
1.00
30.37
N


ATOM
366
CA
ILE
A
48
68.392
35.871
28.990
1.00
29.07
C


ATOM
367
C
ILE
A
48
69.551
36.863
28.923
1.00
28.22
C


ATOM
368
O
ILE
A
48
69.434
38.010
29.354
1.00
27.33
O


ATOM
369
CB
ILE
A
48
67.241
36.415
28.113
1.00
29.02
C


ATOM
370
CG1
ILE
A
48
66.068
35.430
28.102
1.00
29.85
C


ATOM
371
CG2
ILE
A
48
67.744
36.639
26.687
1.00
28.61
C


ATOM
372
CD1
ILE
A
48
64.865
35.915
27.302
1.00
29.38
C


ATOM
373
N
ASN
A
49
70.676
36.412
28.388
1.00
27.92
N


ATOM
374
CA
ASN
A
49
71.839
37.271
28.258
1.00
28.26
C


ATOM
375
C
ASN
A
49
72.251
37.351
26.798
1.00
28.80
C


ATOM
376
O
ASN
A
49
72.436
36.328
26.143
1.00
30.14
O


ATOM
377
CB
ASN
A
49
72.997
36.726
29.101
1.00
27.34
C


ATOM
378
CG
ASN
A
49
72.738
36.847
30.592
1.00
27.92
C


ATOM
379
OD1
ASN
A
49
72.899
37.914
31.176
1.00
26.65
O


ATOM
380
ND2
ASN
A
49
72.317
35.752
31.211
1.00
27.88
N


ATOM
381
N
LEU
A
50
72.367
38.569
26.281
1.00
28.12
N


ATOM
382
CA
LEU
A
50
72.795
38.760
24.899
1.00
27.11
C


ATOM
383
C
LEU
A
50
74.302
38.496
24.876
1.00
26.67
C


ATOM
384
O
LEU
A
50
74.964
38.644
25.900
1.00
25.35
O


ATOM
385
CB
LEU
A
50
72.530
40.203
24.454
1.00
26.25
C


ATOM
386
CG
LEU
A
50
71.098
40.734
24.549
1.00
27.50
C


ATOM
387
CD1
LEU
A
50
71.071
42.216
24.160
1.00
25.93
C


ATOM
388
CD2
LEU
A
50
70.190
39.917
23.632
1.00
27.40
C


ATOM
389
N
LYS
A
51
74.837
38.100
23.723
1.00
27.96
N


ATOM
390
CA
LYS
A
51
76.275
37.859
23.585
1.00
29.04
C


ATOM
391
C
LYS
A
51
76.941
39.189
23.217
1.00
27.91
C


ATOM
392
O
LYS
A
51
78.128
39.397
23.472
1.00
28.86
O


ATOM
393
CB
LYS
A
51
76.564
36.813
22.496
1.00
30.79
C


ATOM
394
CG
LYS
A
51
76.813
35.389
23.004
1.00
33.79
C


ATOM
395
CD
LYS
A
51
75.558
34.739
23.541
1.00
36.94
C


ATOM
396
CE
LYS
A
51
75.836
33.339
24.093
1.00
39.15
C


ATOM
397
NZ
LYS
A
51
76.304
32.377
23.060
1.00
40.17
N


ATOM
398
N
ILE
A
52
76.163
40.070
22.590
1.00
26.85
N


ATOM
399
CA
ILE
A
52
76.608
41.411
22.216
1.00
24.81
C


ATOM
400
C
ILE
A
52
75.442
42.326
22.590
1.00
25.02
C


ATOM
401
O
ILE
A
52
74.276
41.961
22.425
1.00
24.33
O


ATOM
402
CB
ILE
A
52
76.950
41.540
20.700
1.00
25.62
C


ATOM
403
CG1
ILE
A
52
75.738
41.178
19.833
1.00
25.04
C


ATOM
404
CG2
ILE
A
52
78.159
40.654
20.370
1.00
25.34
C


ATOM
405
CD1
ILE
A
52
75.946
41.460
18.351
1.00
22.84
C


ATOM
406
N
PRO
A
53
75.742
43.527
23.102
1.00
24.40
N


ATOM
407
CA
PRO
A
53
74.732
44.502
23.526
1.00
25.22
C


ATOM
408
C
PRO
A
53
73.979
45.272
22.439
1.00
25.38
C


ATOM
409
O
PRO
A
53
73.644
46.438
22.638
1.00
25.66
O


ATOM
410
CB
PRO
A
53
75.535
45.432
24.426
1.00
23.34
C


ATOM
411
CG
PRO
A
53
76.829
45.526
23.670
1.00
24.00
C


ATOM
412
CD
PRO
A
53
77.101
44.079
23.267
1.00
23.34
C


ATOM
413
N
LEU
A
54
73.705
44.633
21.304
1.00
25.11
N


ATOM
414
CA
LEU
A
54
72.982
45.306
20.229
1.00
24.78
C


ATOM
415
C
LEU
A
54
71.670
44.607
19.883
1.00
25.72
C


ATOM
416
O
LEU
A
54
71.613
43.375
19.783
1.00
25.86
O


ATOM
417
CB
LEU
A
54
73.842
45.382
18.965
1.00
24.66
C


ATOM
418
CG
LEU
A
54
75.270
45.925
19.050
1.00
24.20
C


ATOM
419
CD1
LEU
A
54
75.865
45.913
17.660
1.00
22.76
C


ATOM
420
CD2
LEU
A
54
75.288
47.333
19.636
1.00
23.83
C


ATOM
421
N
VAL
A
55
70.613
45.396
19.721
1.00
24.79
N


ATOM
422
CA
VAL
A
55
69.315
44.866
19.335
1.00
25.45
C


ATOM
423
C
VAL
A
55
68.803
45.777
18.220
1.00
26.67
C


ATOM
424
O
VAL
A
55
69.044
46.988
18.252
1.00
26.82
O


ATOM
425
CB
VAL
A
55
68.298
44.846
20.519
1.00
24.52
C


ATOM
426
CG1
VAL
A
55
68.889
44.086
21.698
1.00
23.68
C


ATOM
427
CG2
VAL
A
55
67.906
46.263
20.922
1.00
25.10
C


ATOM
428
N
SER
A
56
68.132
45.197
17.225
1.00
26.09
N


ATOM
429
CA
SER
A
56
67.603
45.980
16.111
1.00
26.11
C


ATOM
430
C
SER
A
56
66.219
46.532
16.453
1.00
25.25
C


ATOM
431
O
SER
A
56
65.418
45.877
17.121
1.00
25.67
O


ATOM
432
CB
SER
A
56
67.565
45.135
14.825
1.00
26.43
C


ATOM
433
OG
SER
A
56
66.749
43.988
14.965
1.00
27.47
O


ATOM
434
N
ALA
A
57
65.957
47.751
15.996
1.00
24.68
N


ATOM
435
CA
ALA
A
57
64.710
48.458
16.270
1.00
25.05
C


ATOM
436
C
ALA
A
57
63.407
47.783
15.820
1.00
25.91
C


ATOM
437
O
ALA
A
57
63.375
47.019
14.853
1.00
25.61
O


ATOM
438
CB
ALA
A
57
64.797
49.868
15.691
1.00
22.75
C


ATOM
439
N
ILE
A
58
62.335
48.091
16.544
1.00
25.97
N


ATOM
440
CA
ILE
A
58
61.002
47.555
16.276
1.00
27.20
C


ATOM
441
C
ILE
A
58
60.400
48.361
15.124
1.00
27.24
C


ATOM
442
O
ILE
A
58
59.417
49.088
15.297
1.00
28.19
O


ATOM
443
CB
ILE
A
58
60.114
47.696
17.535
1.00
26.40
C


ATOM
444
CG1
ILE
A
58
60.929
47.293
18.773
1.00
26.10
C


ATOM
445
CG2
ILE
A
58
58.869
46.829
17.403
1.00
25.39
C


ATOM
446
CD1
ILE
A
58
60.144
47.268
20.061
1.00
25.45
C


ATOM
447
N
MET
A
59
60.998
48.213
13.945
1.00
27.31
N


ATOM
448
CA
MET
A
59
60.581
48.965
12.768
1.00
27.85
C


ATOM
449
C
MET
A
59
60.419
48.127
11.501
1.00
28.29
C


ATOM
450
O
MET
A
59
61.177
47.185
11.261
1.00
27.17
O


ATOM
451
CB
MET
A
59
61.604
50.072
12.503
1.00
27.11
C


ATOM
452
CG
MET
A
59
61.908
50.946
13.711
1.00
26.18
C


ATOM
453
SD
MET
A
59
63.235
52.128
13.373
1.00
28.54
S


ATOM
454
CE
MET
A
59
62.471
53.130
12.107
1.00
25.89
C


ATOM
455
N
GLN
A
60
59.444
48.505
10.679
1.00
29.33
N


ATOM
456
CA
GLN
A
60
59.163
47.806
9.428
1.00
30.56
C


ATOM
457
C
GLN
A
60
60.372
47.772
8.503
1.00
30.93
C


ATOM
458
O
GLN
A
60
60.576
46.800
7.783
1.00
31.46
O


ATOM
459
CB
GLN
A
60
58.006
48.479
8.674
1.00
31.20
C


ATOM
460
CG
GLN
A
60
56.741
48.712
9.491
1.00
32.68
C


ATOM
461
CD
GLN
A
60
55.654
49.395
8.680
1.00
33.85
C


ATOM
462
OE1
GLN
A
60
55.941
50.208
7.802
1.00
36.50
O


ATOM
463
NE2
GLN
A
60
54.401
49.079
8.979
1.00
34.24
N


ATOM
464
N
SER
A
61
61.171
48.834
8.519
1.00
30.66
N


ATOM
465
CA
SER
A
61
62.332
48.906
7.639
1.00
31.00
C


ATOM
466
C
SER
A
61
63.619
48.359
8.241
1.00
30.65
C


ATOM
467
O
SER
A
61
64.695
48.514
7.659
1.00
30.72
O


ATOM
468
CB
SER
A
61
62.553
50.353
7.185
1.00
30.89
C


ATOM
469
OG
SER
A
61
62.658
51.225
8.292
1.00
34.36
O


ATOM
470
N
VAL
A
62
63.512
47.698
9.388
1.00
30.00
N


ATOM
471
CA
VAL
A
62
64.696
47.165
10.039
1.00
29.68
C


ATOM
472
C
VAL
A
62
64.642
45.696
10.449
1.00
30.05
C


ATOM
473
O
VAL
A
62
65.413
44.880
9.948
1.00
30.69
O


ATOM
474
CB
VAL
A
62
65.046
47.997
11.306
1.00
29.93
C


ATOM
475
CG1
VAL
A
62
66.287
47.418
11.989
1.00
30.22
C


ATOM
476
CG2
VAL
A
62
65.280
49.460
10.926
1.00
29.24
C


ATOM
477
N
SER
A
63
63.729
45.364
11.354
1.00
30.78
N


ATOM
478
CA
SER
A
63
63.641
44.011
11.889
1.00
31.26
C


ATOM
479
C
SER
A
63
62.664
43.019
11.267
1.00
32.02
C


ATOM
480
O
SER
A
63
61.535
42.842
11.741
1.00
30.32
O


ATOM
481
CB
SER
A
63
63.389
44.091
13.400
1.00
30.76
C


ATOM
482
OG
SER
A
63
64.420
44.825
14.051
1.00
29.40
O


ATOM
483
N
GLY
A
64
63.122
42.361
10.211
1.00
32.88
N


ATOM
484
CA
GLY
A
64
62.320
41.352
9.553
1.00
33.87
C


ATOM
485
C
GLY
A
64
62.916
40.005
9.925
1.00
35.96
C


ATOM
486
O
GLY
A
64
63.761
39.932
10.823
1.00
33.92
O


ATOM
487
N
GLU
A
65
62.501
38.949
9.226
1.00
37.32
N


ATOM
488
CA
GLU
A
65
62.980
37.596
9.493
1.00
39.14
C


ATOM
489
C
GLU
A
65
64.487
37.461
9.320
1.00
37.65
C


ATOM
490
O
GLU
A
65
65.175
36.945
10.198
1.00
36.98
O


ATOM
491
CB
GLU
A
65
62.298
36.591
8.559
1.00
42.54
C


ATOM
492
CG
GLU
A
65
60.841
36.885
8.260
1.00
48.99
C


ATOM
493
CD
GLU
A
65
60.245
35.884
7.283
1.00
53.35
C


ATOM
494
OE1
GLU
A
65
60.872
35.654
6.224
1.00
55.95
O


ATOM
495
OE2
GLU
A
65
59.155
35.333
7.568
1.00
54.54
O


ATOM
496
N
LYS
A
66
64.991
37.914
8.177
1.00
37.01
N


ATOM
497
CA
LYS
A
66
66.416
37.820
7.883
1.00
36.92
C


ATOM
498
C
LYS
A
66
67.290
38.597
8.859
1.00
34.95
C


ATOM
499
O
LYS
A
66
68.373
38.140
9.228
1.00
33.49
O


ATOM
500
CB
LYS
A
66
66.691
38.282
6.448
1.00
38.53
C


ATOM
501
CG
LYS
A
66
66.185
37.309
5.397
1.00
43.00
C


ATOM
502
CD
LYS
A
66
66.517
37.777
3.987
1.00
47.32
C


ATOM
503
CE
LYS
A
66
66.060
36.759
2.944
1.00
48.73
C


ATOM
504
NZ
LYS
A
66
66.276
37.246
1.549
1.00
49.84
N


ATOM
505
N
MET
A
67
66.826
39.772
9.272
1.00
33.11
N


ATOM
506
CA
MET
A
67
67.582
40.584
10.218
1.00
32.25
C


ATOM
507
C
MET
A
67
67.696
39.825
11.536
1.00
32.26
C


ATOM
508
O
MET
A
67
68.780
39.717
12.106
1.00
32.78
O


ATOM
509
CB
MET
A
67
66.882
41.927
10.452
1.00
31.65
C


ATOM
510
CG
MET
A
67
67.589
42.843
11.447
1.00
30.85
C


ATOM
511
SD
MET
A
67
69.259
43.315
10.933
1.00
30.60
S


ATOM
512
CE
MET
A
67
68.905
44.374
9.529
1.00
28.51
C


ATOM
513
N
ALA
A
68
66.573
39.286
12.003
1.00
30.79
N


ATOM
514
CA
ALA
A
68
66.535
38.548
13.261
1.00
30.85
C


ATOM
515
C
ALA
A
68
67.495
37.355
13.281
1.00
31.53
C


ATOM
516
O
ALA
A
68
68.158
37.099
14.286
1.00
31.47
O


ATOM
517
CB
ALA
A
68
65.114
38.089
13.542
1.00
29.40
C


ATOM
518
N
ILE
A
69
67.573
36.632
12.169
1.00
31.56
N


ATOM
519
CA
ILE
A
69
68.466
35.484
12.067
1.00
31.71
C


ATOM
520
C
ILE
A
69
69.923
35.952
12.011
1.00
31.13
C


ATOM
521
O
ILE
A
69
70.778
35.446
12.734
1.00
31.74
O


ATOM
522
CB
ILE
A
69
68.137
34.645
10.801
1.00
33.02
C


ATOM
523
CG1
ILE
A
69
66.787
33.942
10.983
1.00
34.17
C


ATOM
524
CG2
ILE
A
69
69.236
33.629
10.535
1.00
32.75
C


ATOM
525
CD1
ILE
A
69
66.173
33.422
9.680
1.00
34.42
C


ATOM
526
N
ALA
A
70
70.194
36.933
12.255
1.00
30.92
N


ATOM
527
CA
ALA
A
70
71.540
37.468
11.000
1.00
29.65
C


ATOM
528
C
ALA
A
70
72.102
38.049
12.298
1.00
29.11
C


ATOM
529
O
ALA
A
70
73.278
37.866
12.602
1.00
28.78
O


ATOM
530
CB
ALA
A
70
71.550
38.529
9.914
1.00
30.07
C


ATOM
531
N
LEU
A
71
71.263
38.752
13.055
1.00
28.45
N


ATOM
532
CA
LEU
A
71
71.701
39.357
14.308
1.00
28.31
C


ATOM
533
C
LEU
A
71
71.845
38.324
15.420
1.00
29.00
C


ATOM
534
O
LEU
A
71
72.796
38.377
16.198
1.00
28.61
O


ATOM
535
CB
LEU
A
71
70.726
40.453
14.742
1.00
26.49
C


ATOM
536
CG
LEU
A
71
71.090
41.270
15.992
1.00
26.53
C


ATOM
537
CD1
LEU
A
71
72.561
41.711
15.941
1.00
24.18
C


ATOM
538
CD2
LEU
A
71
70.168
42.487
16.073
1.00
24.70
C


ATOM
539
N
ALA
A
72
70.899
37.392
15.502
1.00
29.36
N


ATOM
540
CA
ALA
A
72
70.966
36.355
16.526
1.00
29.89
C


ATOM
541
C
ALA
A
72
72.251
35.553
16.336
1.00
30.74
C


ATOM
542
O
ALA
A
72
72.890
35.147
17.308
1.00
29.87
O


ATOM
543
CB
ALA
A
72
69.747
35.429
16.435
1.00
28.97
C


ATOM
544
N
ARG
A
73
72.623
35.330
15.077
1.00
31.36
N


ATOM
545
CA
ARG
A
73
73.832
34.580
14.761
1.00
33.37
C


ATOM
546
C
ARG
A
73
75.082
35.242
15.321
1.00
33.97
C


ATOM
547
O
ARG
A
73
76.062
34.562
15.616
1.00
34.69
O


ATOM
548
CB
ARG
A
73
73.988
34.414
13.247
1.00
34.83
C


ATOM
549
CG
ARG
A
73
73.071
33.373
12.630
1.00
37.24
C


ATOM
550
CD
ARG
A
73
73.289
33.268
11.124
1.00
40.12
C


ATOM
551
NE
ARG
A
73
72.462
32.222
10.531
1.00
43.25
N


ATOM
552
CZ
ARG
A
73
72.258
32.069
9.225
1.00
45.18
C


ATOM
553
NH1
ARG
A
73
72.821
32.899
8.354
1.00
44.94
N


ATOM
554
NH2
ARG
A
73
71.484
31.083
8.789
1.00
45.96
N


ATOM
555
N
GLU
A
74
75.050
36.566
15.463
1.00
33.85
N


ATOM
556
CA
GLU
A
74
76.198
37.293
15.995
1.00
33.08
C


ATOM
557
C
GLU
A
74
76.089
37.514
17.501
1.00
31.63
C


ATOM
558
O
GLU
A
74
77.011
38.037
18.119
1.00
32.56
O


ATOM
559
CB
GLU
A
74
76.367
38.642
15.286
1.00
34.18
C


ATOM
560
CG
GLU
A
74
76.569
38.544
13.779
1.00
37.13
C


ATOM
561
CD
GLU
A
74
77.709
37.611
13.384
1.00
39.95
C


ATOM
562
OE1
GLU
A
74
78.834
37.775
13.909
1.00
41.16
O


ATOM
563
OE2
GLU
A
74
77.478
36.718
12.539
1.00
40.45
O


ATOM
564
N
GLY
A
75
74.964
37.127
18.095
1.00
30.42
N


ATOM
565
CA
GLY
A
75
74.820
37.284
19.533
1.00
29.77
C


ATOM
566
C
GLY
A
75
73.815
38.310
20.019
1.00
29.50
C


ATOM
567
O
GLY
A
75
73.598
38.439
21.222
1.00
29.13
O


ATOM
568
N
GLY
A
76
73.212
39.051
19.096
1.00
29.23
N


ATOM
569
CA
GLY
A
76
72.226
40.042
19.483
1.00
28.60
C


ATOM
570
C
GLY
A
76
70.831
39.498
19.245
1.00
28.37
C


ATOM
571
O
GLY
A
76
70.668
38.304
18.976
1.00
26.97
O


ATOM
572
N
ILE
A
77
69.823
40.361
19.345
1.00
27.56
N


ATOM
573
CA
ILE
A
77
68.445
39.937
19.122
1.00
27.52
C


ATOM
574
C
ILE
A
77
67.643
41.025
18.409
1.00
28.94
C


ATOM
575
O
ILE
A
77
67.905
42.221
18.572
1.00
28.96
O


ATOM
576
CB
ILE
A
77
67.750
39.578
20.455
1.00
26.85
C


ATOM
577
CG1
ILE
A
77
66.524
38.704
20.183
1.00
27.10
C


ATOM
578
CG2
ILE
A
77
67.332
40.852
21.205
1.00
24.72
C


ATOM
579
CD1
ILE
A
77
65.800
38.268
21.443
1.00
24.29
C


ATOM
580
N
SER
A
78
66.674
40.602
17.605
1.00
28.99
N


ATOM
581
CA
SER
A
78
65.824
41.529
16.872
1.00
28.68
C


ATOM
582
C
SER
A
78
64.409
41.496
17.423
1.00
28.78
C


ATOM
583
O
SER
A
78
63.950
40.469
17.913
1.00
30.10
O


ATOM
584
CB
SER
A
78
65.775
41.160
15.387
1.00
27.58
C


ATOM
585
OG
SER
A
78
67.004
41.415
14.743
1.00
27.37
O


ATOM
586
N
PHE
A
79
63.727
42.632
17.357
1.00
28.40
N


ATOM
587
CA
PHE
A
79
62.350
42.710
17.807
1.00
28.34
C


ATOM
588
C
PHE
A
79
61.494
42.893
16.558
1.00
28.91
C


ATOM
589
O
PHE
A
79
61.360
44.004
16.048
1.00
29.07
O


ATOM
590
CB
PHE
A
79
62.150
43.885
18.778
1.00
26.91
C


ATOM
591
CG
PHE
A
79
62.715
43.635
20.155
1.00
27.54
C


ATOM
592
CD1
PHE
A
79
64.067
43.839
20.421
1.00
28.32
C


ATOM
593
CD2
PHE
A
79
61.902
43.146
21.175
1.00
27.29
C


ATOM
594
CE1
PHE
A
79
64.601
43.555
21.685
1.00
28.62
C


ATOM
595
CE2
PHE
A
79
62.426
42.861
22.436
1.00
27.31
C


ATOM
596
CZ
PHE
A
79
63.775
43.065
22.691
1.00
27.27
C


ATOM
597
N
ILE
A
80
60.947
41.789
16.053
1.00
28.75
N


ATOM
598
CA
ILE
A
80
60.102
41.815
14.861
1.00
29.29
C


ATOM
599
C
ILE
A
80
59.054
42.919
15.011
1.00
29.89
C


ATOM
600
O
ILE
A
80
58.319
42.950
16.000
1.00
30.34
O


ATOM
601
CB
ILE
A
80
59.384
40.450
14.657
1.00
29.92
C


ATOM
602
CG1
ILE
A
80
60.416
39.326
14.516
1.00
30.32
C


ATOM
603
CG2
ILE
A
80
58.499
40.498
13.414
1.00
29.91
C


ATOM
604
CD1
ILE
A
80
61.356
39.496
13.341
1.00
30.51
C


ATOM
605
N
PHE
A
81
58.981
43.821
14.035
1.00
30.13
N


ATOM
606
CA
PHE
A
81
58.027
44.922
14.120
1.00
31.72
C


ATOM
607
C
PHE
A
81
56.579
44.473
14.289
1.00
31.73
C


ATOM
608
O
PHE
A
81
56.136
43.510
13.661
1.00
32.24
O


ATOM
609
CB
PHE
A
81
58.150
45.861
12.905
1.00
32.72
C


ATOM
610
CG
PHE
A
81
57.886
45.203
11.573
1.00
34.52
C


ATOM
611
CD1
PHE
A
81
58.857
44.422
10.959
1.00
34.19
C


ATOM
612
CD2
PHE
A
81
56.673
45.396
10.918
1.00
35.24
C


ATOM
613
CE1
PHE
A
81
58.625
43.844
9.708
1.00
34.16
C


ATOM
614
CE2
PHE
A
81
56.432
44.823
9.668
1.00
35.18
C


ATOM
615
CZ
PHE
A
81
57.410
44.048
9.064
1.00
34.69
C


ATOM
616
N
GLY
A
82
55.851
45.179
15.152
1.00
31.39
N


ATOM
617
CA
GLY
A
82
54.462
44.851
15.401
1.00
32.43
C


ATOM
618
C
GLY
A
82
53.490
45.673
14.574
1.00
33.20
C


ATOM
619
O
GLY
A
82
52.277
45.505
14.688
1.00
33.41
O


ATOM
620
N
SER
A
83
54.012
46.567
13.741
1.00
33.11
N


ATOM
621
CA
SER
A
83
53.156
47.392
12.900
1.00
34.17
C


ATOM
622
C
SER
A
83
52.759
46.625
11.640
1.00
34.38
C


ATOM
623
O
SER
A
83
53.044
47.038
10.517
1.00
34.03
O


ATOM
624
CB
SER
A
83
53.867
48.697
12.534
1.00
33.42
C


ATOM
625
OG
SER
A
83
55.143
48.439
11.990
1.00
34.18
O


ATOM
626
N
GLN
A
84
52.110
45.487
11.855
1.00
35.41
N


ATOM
627
CA
GLN
A
84
51.640
44.625
10.780
1.00
36.62
C


ATOM
628
C
GLN
A
84
50.585
43.711
11.397
1.00
37.53
C


ATOM
629
O
GLN
A
84
50.373
43.741
12.611
1.00
36.60
O


ATOM
630
CB
GLN
A
84
52.794
43.797
10.201
1.00
37.29
C


ATOM
631
CG
GLN
A
84
53.412
42.805
11.174
1.00
37.90
C


ATOM
632
CD
GLN
A
84
54.568
42.035
10.563
1.00
39.55
C


ATOM
633
OE1
GLN
A
84
54.427
41.416
9.510
1.00
41.11
O


ATOM
634
NE2
GLN
A
84
55.720
42.065
11.228
1.00
39.70
N


ATOM
635
N
SER
A
85
49.921
42.908
10.571
1.00
38.61
N


ATOM
636
CA
SER
A
85
48.888
42.013
11.079
1.00
40.37
C


ATOM
637
C
SER
A
85
49.485
41.050
12.092
1.00
40.61
C


ATOM
638
O
SER
A
85
50.655
40.678
11.993
1.00
40.59
O


ATOM
639
CB
SER
A
85
48.249
41.211
9.943
1.00
40.55
C


ATOM
640
OG
SER
A
85
49.115
40.182
9.501
1.00
41.70
O


ATOM
641
N
ILE
A
86
48.667
40.657
13.063
1.00
40.88
N


ATOM
642
CA
ILE
A
86
49.079
39.732
14.108
1.00
41.21
C


ATOM
643
C
ILE
A
86
49.589
38.424
13.508
1.00
42.63
C


ATOM
644
O
ILE
A
86
50.578
37.858
13.977
1.00
42.00
O


ATOM
645
CB
ILE
A
86
47.899
39.429
15.061
1.00
40.49
C


ATOM
646
CG1
ILE
A
86
47.454
40.722
15.750
1.00
39.68
C


ATOM
647
CG2
ILE
A
86
48.299
38.366
16.079
1.00
39.80
C


ATOM
648
CD1
ILE
A
86
46.272
40.558
16.686
1.00
38.99
C


ATOM
649
N
GLU
A
87
48.918
37.952
12.462
1.00
43.90
N


ATOM
650
CA
GLU
A
87
49.314
36.709
11.814
1.00
45.61
C


ATOM
651
C
GLU
A
87
50.604
36.839
11.009
1.00
44.76
C


ATOM
652
O
GLU
A
87
51.355
35.874
10.879
1.00
45.04
O


ATOM
653
CB
GLU
A
87
48.177
36.173
10.924
1.00
47.51
C


ATOM
654
CG
GLU
A
87
47.243
37.229
10.324
1.00
51.63
C


ATOM
655
CD
GLU
A
87
46.341
37.895
11.362
1.00
53.09
C


ATOM
656
OE1
GLU
A
87
45.804
37.180
12.238
1.00
54.09
O


ATOM
657
OE2
GLU
A
87
46.156
39.131
11.290
1.00
53.94
O


ATOM
658
N
SER
A
88
50.865
38.025
10.470
1.00
44.57
N


ATOM
659
CA
SER
A
88
52.091
38.246
9.704
1.00
44.09
C


ATOM
660
C
SER
A
88
53.295
38.287
10.643
1.00
42.16
C


ATOM
661
O
SER
A
88
54.343
37.720
10.346
1.00
41.66
O


ATOM
662
CB
SER
A
88
52.017
39.560
8.925
1.00
45.33
C


ATOM
663
OG
SER
A
88
51.076
39.473
7.875
1.00
49.27
O


ATOM
664
N
GLN
A
89
53.137
38.966
11.774
1.00
40.30
N


ATOM
665
CA
GLN
A
89
54.214
39.070
12.750
1.00
39.20
C


ATOM
666
C
GLN
A
89
54.529
37.696
13.336
1.00
38.78
C


ATOM
667
O
GLN
A
89
55.695
37.325
13.477
1.00
38.47
O


ATOM
668
CB
GLN
A
89
53.827
40.046
13.867
1.00
37.90
C


ATOM
669
CG
GLN
A
89
54.856
40.158
14.984
1.00
36.29
C


ATOM
670
CD
GLN
A
89
54.484
41.196
16.025
1.00
35.77
C


ATOM
671
OE1
GLN
A
89
53.314
41.342
16.381
1.00
34.41
O


ATOM
672
NE2
GLN
A
89
55.483
41.910
16.534
1.00
34.88
N


ATOM
673
N
ALA
A
90
53.487
36.940
13.668
1.00
38.89
N


ATOM
674
CA
ALA
A
90
53.665
35.606
14.236
1.00
38.52
C


ATOM
675
C
ALA
A
90
54.416
34.706
13.258
1.00
37.75
C


ATOM
676
O
ALA
A
90
55.284
33.932
13.658
1.00
37.34
O


ATOM
677
CB
ALA
A
90
52.310
34.996
14.580
1.00
38.78
C


ATOM
678
N
ALA
A
91
54.086
34.815
11.976
1.00
37.31
N


ATOM
679
CA
ALA
A
91
54.751
34.007
10.960
1.00
37.66
C


ATOM
680
C
ALA
A
91
56.259
34.272
10.972
1.00
37.59
C


ATOM
681
O
ALA
A
91
57.061
33.339
10.934
1.00
37.08
O


ATOM
682
CB
ALA
A
91
54.170
34.312
9.582
1.00
36.97
C


ATOM
683
N
MET
A
92
56.644
35.544
11.023
1.00
38.21
N


ATOM
684
CA
MET
A
92
58.063
35.898
11.052
1.00
38.30
C


ATOM
685
C
MET
A
92
58.747
35.311
12.282
1.00
37.53
C


ATOM
686
O
MET
A
92
59.841
34.756
12.188
1.00
37.70
O


ATOM
687
CB
MET
A
92
58.242
37.418
11.054
1.00
39.02
C


ATOM
688
CG
MET
A
92
57.888
38.093
9.747
1.00
39.39
C


ATOM
689
SD
MET
A
92
58.282
39.850
9.772
1.00
39.06
S


ATOM
690
CE
MET
A
92
57.340
40.410
8.355
1.00
38.06
C


ATOM
691
N
VAL
A
93
58.099
35.443
13.436
1.00
37.33
N


ATOM
692
CA
VAL
A
93
58.647
34.919
14.679
1.00
37.59
C


ATOM
693
C
VAL
A
93
58.822
33.416
14.558
1.00
38.75
C


ATOM
694
O
VAL
A
93
59.865
32.871
14.915
1.00
39.48
O


ATOM
695
CB
VAL
A
93
57.718
35.218
15.877
1.00
37.43
C


ATOM
696
CG1
VAL
A
93
58.182
34.447
17.106
1.00
35.94
C


ATOM
697
CG2
VAL
A
93
57.705
36.711
16.162
1.00
36.07
C


ATOM
698
N
HIS
A
94
57.795
32.749
14.042
1.00
40.16
N


ATOM
699
CA
HIS
A
94
57.833
31.301
13.875
1.00
40.66
C


ATOM
700
C
HIS
A
94
58.930
30.881
12.898
1.00
40.13
C


ATOM
701
O
HIS
A
94
59.624
29.888
13.122
1.00
40.44
O


ATOM
702
CB
HIS
A
94
56.466
30.797
13.395
1.00
42.53
C


ATOM
703
CG
HIS
A
94
56.400
29.312
13.209
1.00
43.62
C


ATOM
704
ND1
HIS
A
94
56.844
28.683
12.065
1.00
44.37
N


ATOM
705
CD2
HIS
A
94
55.961
28.331
14.033
1.00
43.39
C


ATOM
706
CE1
HIS
A
94
56.680
27.379
12.191
1.00
44.17
C


ATOM
707
NE2
HIS
A
94
56.146
27.139
13.376
1.00
44.00
N


ATOM
708
N
ALA
A
95
59.092
31.642
11.821
1.00
39.31
N


ATOM
709
CA
ALA
A
95
60.111
31.335
10.825
1.00
38.23
C


ATOM
710
C
ALA
A
95
61.516
31.408
11.425
1.00
38.43
C


ATOM
711
O
ALA
A
95
62.399
30.637
11.055
1.00
38.01
O


ATOM
712
CB
ALA
A
95
59.996
32.298
9.647
1.00
37.20
C


ATOM
713
N
VAL
A
96
61.720
32.341
12.350
1.00
38.46
N


ATOM
714
CA
VAL
A
96
63.019
32.504
12.992
1.00
37.77
C


ATOM
715
C
VAL
A
96
63.293
31.366
13.973
1.00
38.35
C


ATOM
716
O
VAL
A
96
64.383
30.794
13.983
1.00
37.59
O


ATOM
717
CB
VAL
A
96
63.103
33.858
13.748
1.00
37.72
C


ATOM
718
CG1
VAL
A
96
64.417
33.959
14.509
1.00
36.02
C


ATOM
719
CG2
VAL
A
96
62.985
35.009
12.757
1.00
36.81
C


ATOM
720
N
LYS
A
97
62.295
31.040
14.787
1.00
38.94
N


ATOM
721
CA
LYS
A
97
62.426
29.978
15.777
1.00
40.76
C


ATOM
722
C
LYS
A
97
62.607
28.599
15.145
1.00
42.67
C


ATOM
723
O
LYS
A
97
63.211
27.710
15.747
1.00
43.04
O


ATOM
724
CB
LYS
A
97
61.199
29.955
16.697
1.00
39.98
C


ATOM
725
CG
LYS
A
97
60.989
31.227
17.516
1.00
39.03
C


ATOM
726
CD
LYS
A
97
62.189
31.543
18.411
1.00
37.55
C


ATOM
727
CE
LYS
A
97
62.416
30.474
19.472
1.00
36.48
C


ATOM
728
NZ
LYS
A
97
63.663
30.739
20.249
1.00
34.18
N


ATOM
729
N
ASN
A
98
62.091
28.425
13.933
1.00
44.43
N


ATOM
730
CA
ASN
A
98
62.190
27.142
13.247
1.00
46.61
C


ATOM
731
C
ASN
A
98
63.069
27.188
12.005
1.00
46.93
C


ATOM
732
O
ASN
A
98
62.847
26.431
11.059
1.00
48.02
O


ATOM
733
CB
ASN
A
98
60.790
26.656
12.866
1.00
48.75
C


ATOM
734
CG
ASN
A
98
59.921
26.378
14.078
1.00
51.25
C


ATOM
735
OD1
ASN
A
98
58.697
26.390
13.992
1.00
53.69
O


ATOM
736
ND2
ASN
A
98
60.555
26.114
15.214
1.00
53.55
N


ATOM
737
N
PHE
A
99
64.073
28.060
12.007
1.00
46.26
N


ATOM
738
CA
PHE
A
99
64.958
28.182
10.855
1.00
46.28
C


ATOM
739
C
PHE
A
99
65.891
26.987
10.674
1.00
46.62
C


ATOM
740
O
PHE
A
99
66.232
26.634
9.548
1.00
46.35
O


ATOM
741
CB
PHE
A
99
65.799
29.459
10.952
1.00
45.12
C


ATOM
742
CG
PHE
A
99
66.577
29.765
9.699
1.00
44.39
C


ATOM
743
CD1
PHE
A
99
65.918
30.122
8.526
1.00
44.53
C


ATOM
744
CD2
PHE
A
99
67.964
29.690
9.689
1.00
43.94
C


ATOM
745
CE1
PHE
A
99
66.630
30.401
7.362
1.00
44.09
C


ATOM
746
CE2
PHE
A
99
68.685
29.966
8.529
1.00
43.84
C


ATOM
747
CZ
PHE
A
99
68.018
30.323
7.365
1.00
44.07
C


ATOM
748
N
LYS
A
100
66.303
26.368
11.775
1.00
47.68
N


ATOM
749
CA
LYS
A
100
67.214
25.226
11.708
1.00
49.23
C


ATOM
750
C
LYS
A
100
66.519
23.882
11.499
1.00
50.54
C


ATOM
751
O
LYS
A
100
67.165
22.834
11.564
1.00
50.71
O


ATOM
752
CB
LYS
A
100
68.059
25.146
12.980
1.00
48.77
C


ATOM
753
CG
LYS
A
100
68.932
26.364
13.239
1.00
47.96
C


ATOM
754
CD
LYS
A
100
69.709
26.180
14.526
1.00
46.23
C


ATOM
755
CE
LYS
A
100
70.672
27.320
14.777
1.00
44.66
C


ATOM
756
NZ
LYS
A
100
71.462
27.057
16.006
1.00
43.46
N


ATOM
757
N
ALA
A
101
65.212
23.909
11.253
1.00
51.61
N


ATOM
758
CA
ALA
A
101
64.447
22.683
11.040
1.00
52.22
C


ATOM
759
C
ALA
A
101
64.975
21.911
9.835
1.00
52.77
C


ATOM
760
O
ALA
A
101
64.961
22.412
8.711
1.00
53.93
O


ATOM
761
CB
ALA
A
101
62.974
23.011
10.840
1.00
52.31
C


ATOM
762
N
HIS
A
222
80.602
29.634
17.602
1.00
62.86
N


ATOM
763
CA
HIS
A
222
79.850
30.811
17.181
1.00
61.95
C


ATOM
764
C
HIS
A
222
79.347
31.556
18.415
1.00
60.27
C


ATOM
765
O
HIS
A
222
79.357
31.019
19.526
1.00
60.09
O


ATOM
766
CB
HIS
A
222
78.642
30.402
16.323
1.00
64.41
C


ATOM
767
CG
HIS
A
222
78.978
29.493
15.179
1.00
67.13
C


ATOM
768
ND1
HIS
A
222
78.014
28.948
14.357
1.00
68.00
N


ATOM
769
CD2
HIS
A
222
80.165
29.019
14.729
1.00
68.21
C


ATOM
770
CE1
HIS
A
222
78.591
28.177
13.452
1.00
68.36
C


ATOM
771
NE2
HIS
A
222
79.896
28.202
13.656
1.00
68.83
N


ATOM
772
N
ASN
A
223
78.915
32.796
18.220
1.00
57.17
N


ATOM
773
CA
ASN
A
223
78.378
33.583
19.319
1.00
53.95
C


ATOM
774
C
ASN
A
223
76.882
33.737
19.113
1.00
50.53
C


ATOM
775
O
ASN
A
223
76.293
34.746
19.493
1.00
48.94
O


ATOM
776
CB
ASN
A
223
79.039
34.960
19.388
1.00
55.72
C


ATOM
777
CG
ASN
A
223
80.463
34.895
19.899
1.00
57.65
C


ATOM
778
OD1
ASN
A
223
81.380
34.504
19.173
1.00
59.28
O


ATOM
779
ND2
ASN
A
223
80.654
35.262
21.161
1.00
57.30
N


ATOM
780
N
GLU
A
224
76.275
32.723
18.505
1.00
46.60
N


ATOM
781
CA
GLU
A
224
74.843
32.740
18.248
1.00
43.68
C


ATOM
782
C
GLU
A
224
74.057
32.795
19.548
1.00
40.12
C


ATOM
783
O
GLU
A
224
74.438
32.179
20.542
1.00
38.99
O


ATOM
784
CB
GLU
A
224
74.419
31.502
17.449
1.00
44.21
C


ATOM
785
CG
GLU
A
224
74.834
30.176
18.074
1.00
46.74
C


ATOM
786
CD
GLU
A
224
74.123
28.981
17.454
1.00
47.84
C


ATOM
787
OE1
GLU
A
224
73.924
28.977
16.221
1.00
48.39
O


ATOM
788
OE2
GLU
A
224
73.775
28.041
18.199
1.00
48.26
O


ATOM
789
N
LEU
A
225
72.962
33.546
19.527
1.00
37.30
N


ATOM
790
CA
LEU
A
225
72.089
33.681
20.681
1.00
35.11
C


ATOM
791
C
LEU
A
225
70.932
32.704
20.479
1.00
34.44
C


ATOM
792
O
LEU
A
225
70.088
32.901
19.603
1.00
33.50
O


ATOM
793
CB
LEU
A
225
71.561
35.116
20.775
1.00
33.83
C


ATOM
794
CG
LEU
A
225
70.675
35.448
21.979
1.00
34.33
C


ATOM
795
CD1
LEU
A
225
71.450
35.194
23.274
1.00
34.23
C


ATOM
796
CD2
LEU
A
225
70.220
36.899
21.899
1.00
33.89
C


ATOM
797
N
VAL
A
226
70.893
31.653
21.292
1.00
34.99
N


ATOM
798
CA
VAL
A
226
69.853
30.635
21.169
1.00
35.64
C


ATOM
799
C
VAL
A
226
69.235
30.197
22.491
1.00
37.35
C


ATOM
800
O
VAL
A
226
69.744
30.516
23.566
1.00
38.20
O


ATOM
801
CB
VAL
A
226
70.412
29.372
20.488
1.00
34.80
C


ATOM
802
CG1
VAL
A
226
70.890
29.701
19.086
1.00
33.57
C


ATOM
803
CG2
VAL
A
226
71.557
28.805
21.325
1.00
34.39
C


ATOM
804
N
ASP
A
227
68.128
29.462
22.397
1.00
38.54
N


ATOM
805
CA
ASP
A
227
67.453
28.938
23.575
1.00
39.28
C


ATOM
806
C
ASP
A
227
67.986
27.529
23.842
1.00
40.76
C


ATOM
807
O
ASP
A
227
68.841
27.032
23.103
1.00
39.48
O


ATOM
808
CB
ASP
A
227
65.929
28.897
23.374
1.00
39.13
C


ATOM
809
CG
ASP
A
227
65.510
28.134
22.123
1.00
39.09
C


ATOM
810
OD1
ASP
A
227
66.196
27.164
21.740
1.00
39.60
O


ATOM
811
OD2
ASP
A
227
64.472
28.498
21.529
1.00
38.30
O


ATOM
812
N
SER
A
228
67.478
26.888
24.891
1.00
43.19
N


ATOM
813
CA
SER
A
228
67.918
25.544
25.262
1.00
45.34
C


ATOM
814
C
SER
A
228
67.723
24.504
24.157
1.00
46.69
C


ATOM
815
O
SER
A
228
68.239
23.388
24.255
1.00
47.84
O


ATOM
816
CB
SER
A
228
67.202
25.088
26.537
1.00
45.27
C


ATOM
817
OG
SER
A
228
65.796
25.143
26.379
1.00
46.27
O


ATOM
818
N
GLN
A
229
66.988
24.868
23.110
1.00
47.37
N


ATOM
819
CA
GLN
A
229
66.746
23.962
21.990
1.00
47.48
C


ATOM
820
C
GLN
A
229
67.631
24.320
20.797
1.00
47.27
C


ATOM
821
O
GLN
A
229
67.433
23.812
19.691
1.00
46.74
O


ATOM
822
CB
GLN
A
229
65.272
24.014
21.573
1.00
48.89
C


ATOM
823
CG
GLN
A
229
64.301
23.525
22.639
1.00
50.86
C


ATOM
824
CD
GLN
A
229
62.849
23.622
22.197
1.00
53.57
C


ATOM
825
OE1
GLN
A
229
62.439
22.989
21.221
1.00
54.79
O


ATOM
826
NE2
GLN
A
229
62.063
24.421
22.913
1.00
54.30
N


ATOM
827
N
LYS
A
230
68.603
25.200
21.032
1.00
46.64
N


ATOM
828
CA
LYS
A
230
69.534
25.642
19.994
1.00
45.65
C


ATOM
829
C
LYS
A
230
68.876
26.513
18.925
1.00
43.41
C


ATOM
830
O
LYS
A
230
69.462
26.758
17.870
1.00
43.63
O


ATOM
831
CB
LYS
A
230
70.199
24.434
19.324
1.00
48.29
C


ATOM
832
CG
LYS
A
230
70.961
23.521
20.277
1.00
52.07
C


ATOM
833
CD
LYS
A
230
72.156
24.222
20.911
1.00
55.27
C


ATOM
834
CE
LYS
A
230
72.890
23.286
21.871
1.00
57.57
C


ATOM
835
NZ
LYS
A
230
74.090
23.919
22.492
1.00
58.56
N


ATOM
836
N
ARG
A
231
67.663
26.982
19.197
1.00
41.68
N


ATOM
837
CA
ARG
A
231
66.947
27.829
18.246
1.00
40.28
C


ATOM
838
C
ARG
A
231
67.277
29.302
18.488
1.00
38.35
C


ATOM
839
O
ARG
A
231
67.386
29.739
19.634
1.00
36.97
O


ATOM
840
CB
ARG
A
231
65.438
27.626
18.386
1.00
41.68
C


ATOM
841
CG
ARG
A
231
64.972
26.186
18.232
1.00
43.64
C


ATOM
842
CD
ARG
A
231
63.472
26.084
18.443
1.00
45.03
C


ATOM
843
NE
ARG
A
231
63.077
26.614
19.746
1.00
46.86
N


ATOM
844
CZ
ARG
A
231
61.817
26.753
20.150
1.00
48.34
C


ATOM
845
NH1
ARG
A
231
60.814
26.402
19.354
1.00
48.72
N


ATOM
846
NH2
ARG
A
231
61.559
27.248
21.355
1.00
49.43
N


ATOM
847
N
TYR
A
232
67.431
30.061
17.406
1.00
36.49
N


ATOM
848
CA
TYR
A
232
67.742
31.483
17.510
1.00
34.28
C


ATOM
849
C
TYR
A
232
66.713
32.225
18.352
1.00
33.16
C


ATOM
850
O
TYR
A
232
65.514
31.959
18.265
1.00
33.82
O


ATOM
851
CS
TYR
A
232
67.791
32.131
16.127
1.00
33.26
C


ATOM
852
CG
TYR
A
232
68.892
31.630
15.232
1.00
32.73
C


ATOM
853
CD1
TYR
A
232
70.213
31.584
15.672
1.00
32.85
C


ATOM
854
CD2
TYR
A
232
68.614
31.215
13.932
1.00
33.54
C


ATOM
855
CE1
TYR
A
232
71.237
31.131
14.830
1.00
33.51
C


ATOM
856
CE2
TYR
A
232
69.620
30.764
13.087
1.00
33.65
C


ATOM
857
CZ
TYR
A
232
70.927
30.724
13.540
1.00
33.53
C


ATOM
858
OH
TYR
A
232
71.910
30.270
12.695
1.00
34.70
O


ATOM
859
N
LEU
A
233
67.186
33.151
19.177
1.00
32.10
N


ATOM
860
CA
LEU
A
233
66.290
33.942
20.008
1.00
31.00
C


ATOM
861
C
LEU
A
233
65.707
35.036
19.132
1.00
29.82
C


ATOM
862
O
LEU
A
233
66.346
35.479
18.175
1.00
29.69
O


ATOM
863
CB
LEU
A
233
67.051
34.571
21.180
1.00
30.50
C


ATOM
864
CG
LEU
A
233
66.828
33.952
22.564
1.00
32.28
C


ATOM
865
CD1
LEU
A
233
66.898
32.442
22.480
1.00
31.52
C


ATOM
866
CD2
LEU
A
233
67.867
34.488
23.542
1.00
30.57
C


ATOM
867
N
VAL
A
234
64.491
35.461
19.446
1.00
28.87
N


ATOM
868
CA
VAL
A
234
63.855
36.517
18.675
1.00
28.85
C


ATOM
869
C
VAL
A
234
62.872
37.272
19.552
1.00
29.58
C


ATOM
870
O
VAL
A
234
62.257
36.699
20.454
1.00
29.60
O


ATOM
871
CB
VAL
A
234
63.113
35.952
17.431
1.00
28.52
C


ATOM
872
CG1
VAL
A
234
61.924
35.100
17.861
1.00
27.33
C


ATOM
873
CG2
VAL
A
234
62.669
37.091
16.533
1.00
26.42
C


ATOM
874
N
GLY
A
235
62.752
38.571
19.299
1.00
29.15
N


ATOM
875
CA
GLY
A
235
61.835
39.387
20.065
1.00
29.25
C


ATOM
876
C
GLY
A
235
60.701
39.852
19.178
1.00
30.00
C


ATOM
877
O
GLY
A
235
60.745
39.678
17.955
1.00
29.63
O


ATOM
878
N
ALA
A
236
59.680
40.444
19.786
1.00
29.18
N


ATOM
879
CA
ALA
A
236
58.545
40.932
19.023
1.00
29.42
C


ATOM
880
C
ALA
A
236
57.930
42.156
19.681
1.00
28.94
C


ATOM
881
O
ALA
A
236
57.700
42.175
20.887
1.00
30.25
O


ATOM
882
CB
ALA
A
236
57.502
39.828
18.880
1.00
30.04
C


ATOM
883
N
GLY
A
237
57.675
43.185
18.885
1.00
28.85
N


ATOM
884
CA
GLY
A
237
57.072
44.386
19.426
1.00
29.68
C


ATOM
885
C
GLY
A
237
55.565
44.232
19.522
1.00
30.66
C


ATOM
886
O
GLY
A
237
54.957
43.541
18.700
1.00
31.29
O


ATOM
887
N
ILE
A
238
54.969
44.850
20.540
1.00
30.86
N


ATOM
888
CA
ILE
A
238
53.524
44.811
20.734
1.00
31.71
C


ATOM
889
C
ILE
A
238
53.038
46.228
21.055
1.00
32.48
C


ATOM
890
O
ILE
A
238
53.834
47.106
21.385
1.00
31.88
O


ATOM
891
CB
ILE
A
238
53.107
43.869
21.901
1.00
32.49
C


ATOM
892
CG1
ILE
A
238
53.631
44.409
23.233
1.00
32.43
C


ATOM
893
CG2
ILE
A
238
53.626
42.458
21.652
1.00
31.98
C


ATOM
894
CD1
ILE
A
238
53.098
43.658
24.452
1.00
31.48
C


ATOM
895
N
ASN
A
239
51.732
46.451
20.946
1.00
32.65
N


ATOM
896
CA
ASN
A
239
51.171
47.761
21.232
1.00
33.12
C


ATOM
897
C
ASN
A
239
50.172
47.661
22.375
1.00
34.35
C


ATOM
898
O
ASN
A
239
49.801
46.559
22.798
1.00
34.32
O


ATOM
899
CB
ASN
A
239
50.508
48.344
19.977
1.00
33.45
C


ATOM
900
CG
ASN
A
239
49.374
47.478
19.450
1.00
33.90
C


ATOM
901
OD1
ASN
A
239
48.333
47.342
20.090
1.00
33.39
O


ATOM
902
ND2
ASN
A
239
49.576
46.889
18.278
1.00
33.29
N


ATOM
903
N
THR
A
240
49.743
48.810
22.883
1.00
35.36
N


ATOM
904
CA
THR
A
240
48.799
48.847
23.993
1.00
35.80
C


ATOM
905
C
THR
A
240
47.337
48.691
23.576
1.00
37.42
C


ATOM
906
O
THR
A
240
46.444
48.870
24.401
1.00
36.13
O


ATOM
907
CB
THR
A
240
48.923
50.162
24.770
1.00
34.93
C


ATOM
908
OG1
THR
A
240
48.776
51.257
23.859
1.00
34.76
O


ATOM
909
CG2
THR
A
240
50.273
50.252
25.467
1.00
33.70
C


ATOM
910
N
ARG
A
241
47.086
48.349
22.313
1.00
39.17
N


ATOM
911
CA
ARG
A
241
45.707
48.208
21.853
1.00
42.57
C


ATOM
912
C
ARG
A
241
45.212
46.785
21.603
1.00
42.28
C


ATOM
913
O
ARG
A
241
44.262
46.347
22.247
1.00
43.14
O


ATOM
914
CB
ARG
A
241
45.484
49.058
20.598
1.00
45.89
C


ATOM
915
CG
ARG
A
241
45.948
50.498
20.767
1.00
51.37
C


ATOM
916
CD
ARG
A
241
45.095
51.484
19.983
1.00
56.20
C


ATOM
917
NE
ARG
A
241
45.628
52.843
20.084
1.00
60.59
N


ATOM
918
CZ
ARG
A
241
44.928
53.947
19.834
1.00
62.98
C


ATOM
919
NH1
ARG
A
241
43.654
53.862
19.468
1.00
63.64
N


ATOM
920
NH2
ARG
A
241
45.505
55.138
19.945
1.00
64.03
N


ATOM
921
N
ASP
A
242
45.843
46.063
20.682
1.00
41.72
N


ATOM
922
CA
ASP
A
242
45.410
44.698
20.373
1.00
42.47
C


ATOM
923
C
ASP
A
242
46.241
43.591
21.030
1.00
41.62
C


ATOM
924
O
ASP
A
242
46.326
42.488
20.501
1.00
41.70
O


ATOM
925
CS
ASP
A
242
45.403
44.478
18.853
1.00
42.18
C


ATOM
926
CG
ASP
A
242
46.799
44.528
18.240
1.00
44.11
C


ATOM
927
OD1
ASP
A
242
47.791
44.451
18.998
1.00
43.54
O


ATOM
928
OD2
ASP
A
242
46.903
44.631
16.995
1.00
42.81
O


ATOM
929
N
PHE
A
243
46.830
43.876
22.186
1.00
41.52
N


ATOM
930
CA
PHE
A
243
47.668
42.897
22.878
1.00
41.20
C


ATOM
931
C
PHE
A
243
46.966
41.623
23.352
1.00
42.11
C


ATOM
932
O
PHE
A
243
47.603
40.573
23.467
1.00
42.24
O


ATOM
933
CB
PHE
A
243
48.387
43.565
24.058
1.00
38.57
C


ATOM
934
CG
PHE
A
243
47.465
44.128
25.095
1.00
37.00
C


ATOM
935
CD1
PHE
A
243
46.983
43.327
26.123
1.00
36.77
C


ATOM
936
CD2
PHE
A
243
47.083
45.464
25.051
1.00
36.43
C


ATOM
937
CE1
PHE
A
243
46.136
43.847
27.096
1.00
35.68
C


ATOM
938
CE2
PHE
A
243
46.237
45.996
26.017
1.00
36.27
C


ATOM
939
CZ
PHE
A
243
45.762
45.185
27.044
1.00
36.83
C


ATOM
940
N
ARG
A
244
45.666
41.702
23.623
1.00
43.08
N


ATOM
941
CA
ARG
A
244
44.926
40.526
24.078
1.00
43.54
C


ATOM
942
C
ARG
A
244
44.890
39.447
22.996
1.00
43.52
C


ATOM
943
O
ARG
A
244
44.803
38.257
23.297
1.00
43.24
O


ATOM
944
CB
ARG
A
244
43.502
40.914
24.498
1.00
43.28
C


ATOM
945
CG
ARG
A
244
43.455
41.843
25.705
1.00
43.47
C


ATOM
946
CD
ARG
A
244
42.029
42.095
26.172
1.00
44.74
C


ATOM
947
NE
ARG
A
244
41.971
43.071
27.259
1.00
45.31
N


ATOM
948
CZ
ARG
A
244
42.192
44.376
27.110
1.00
46.31
C


ATOM
949
NH1
ARG
A
244
42.485
44.872
25.914
1.00
44.51
N


ATOM
950
NH2
ARG
A
244
42.123
45.188
28.159
1.00
44.79
N


ATOM
951
N
GLU
A
245
44.960
39.867
21.736
1.00
44.04
N


ATOM
952
CA
GLU
A
245
44.959
38.928
20.618
1.00
44.49
C


ATOM
953
C
GLU
A
245
46.371
38.707
20.078
1.00
43.54
C


ATOM
954
O
GLU
A
245
46.720
37.601
19.665
1.00
43.64
O


ATOM
955
CB
GLU
A
245
44.067
39.439
19.479
1.00
47.18
C


ATOM
956
CG
GLU
A
245
42.599
39.036
19.570
1.00
51.54
C


ATOM
957
CD
GLU
A
245
41.917
39.551
20.822
1.00
54.39
C


ATOM
958
OE1
GLU
A
245
41.972
40.777
21.070
1.00
56.74
O


ATOM
959
OE2
GLU
A
245
41.320
38.730
21.555
1.00
56.12
O


ATOM
960
N
ARG
A
246
47.183
39.761
20.088
1.00
41.72
N


ATOM
961
CA
ARG
A
246
48.547
39.679
19.569
1.00
40.10
C


ATOM
962
C
ARG
A
246
49.529
38.897
20.449
1.00
38.51
C


ATOM
963
O
ARG
A
246
50.305
38.087
19.943
1.00
37.50
O


ATOM
964
CD
ARG
A
246
49.093
41.091
19.314
1.00
39.02
C


ATOM
965
CG
ARG
A
246
50.417
41.125
18.558
1.00
38.76
C


ATOM
966
CD
ARG
A
246
50.877
42.560
18.333
1.00
39.34
C


ATOM
967
NE
ARG
A
246
49.978
43.314
17.460
1.00
37.43
N


ATOM
968
CZ
ARG
A
246
49.985
43.242
16.132
1.00
38.30
C


ATOM
969
NH1
ARG
A
246
50.847
42.450
15.507
1.00
37.21
N


ATOM
970
NH2
ARG
A
246
49.129
43.967
15.422
1.00
39.33
N


ATOM
971
N
VAL
A
247
49.502
39.137
21.756
1.00
37.24
N


ATOM
972
CA
VAL
A
247
50.414
38.440
22.657
1.00
37.34
C


ATOM
973
C
VAL
A
247
50.303
36.918
22.523
1.00
38.18
C


ATOM
974
O
VAL
A
247
51.292
36.251
22.209
1.00
38.12
O


ATOM
975
CD
VAL
A
247
50.185
38.872
24.129
1.00
36.77
C


ATOM
976
CG1
VAL
A
247
51.023
38.026
25.070
1.00
35.70
C


ATOM
977
CG2
VAL
A
247
50.550
40.343
24.293
1.00
37.03
C


ATOM
978
N
PRO
A
248
49.100
36.347
22.747
1.00
38.57
N


ATOM
979
CA
PRO
A
248
48.934
34.892
22.631
1.00
38.12
C


ATOM
980
C
PRO
A
248
49.506
34.329
21.333
1.00
37.59
C


ATOM
981
O
PRO
A
248
50.166
33.293
21.336
1.00
37.87
O


ATOM
982
CB
PRO
A
248
47.422
34.714
22.729
1.00
38.80
C


ATOM
983
CG
PRO
A
248
47.039
35.791
23.701
1.00
38.59
C


ATOM
984
CD
PRO
A
248
47.840
36.979
23.188
1.00
38.38
C


ATOM
985
N
ALA
A
249
49.256
35.016
20.224
1.00
37.30
N


ATOM
986
CA
ALA
A
249
49.763
34.573
18.932
1.00
38.37
C


ATOM
987
C
ALA
A
249
51.292
34.588
18.923
1.00
39.52
C


ATOM
988
O
ALA
A
249
51.931
33.682
18.379
1.00
38.98
O


ATOM
989
CB
ALA
A
249
49.228
35.471
17.826
1.00
38.41
C


ATOM
990
N
LEU
A
250
51.872
35.625
19.526
1.00
39.58
N


ATOM
991
CA
LEU
A
250
53.322
35.761
19.587
1.00
39.74
C


ATOM
992
C
LEU
A
250
53.935
34.682
20.475
1.00
39.38
C


ATOM
993
O
LEU
A
250
54.951
34.082
20.123
1.00
38.34
O


ATOM
994
CB
LEU
A
250
53.695
37.163
20.092
1.00
39.96
C


ATOM
995
CG
LEU
A
250
54.043
38.222
19.029
1.00
40.83
C


ATOM
996
CD1
LEU
A
250
53.463
37.859
17.678
1.00
39.28
C


ATOM
997
CD2
LEU
A
250
53.540
39.582
19.487
1.00
39.93
C


ATOM
998
N
VAL
A
251
53.310
34.434
21.620
1.00
39.76
N


ATOM
999
CA
VAL
A
251
53.793
33.409
22.537
1.00
41.50
C


ATOM
1000
C
VAL
A
251
53.714
32.055
21.845
1.00
42.53
C


ATOM
1001
O
VAL
A
251
54.690
31.303
21.810
1.00
42.76
O


ATOM
1002
CB
VAL
A
251
52.940
33.354
23.818
1.00
41.62
C


ATOM
1003
CG1
VAL
A
251
53.352
32.161
24.671
1.00
41.89
C


ATOM
1004
CG2
VAL
A
251
53.104
34.644
24.600
1.00
41.93
C


ATOM
1005
N
GLU
A
252
52.541
31.756
21.293
1.00
43.62
N


ATOM
1006
CA
GLU
A
252
52.317
30.500
20.590
1.00
43.74
C


ATOM
1007
C
GLU
A
252
53.332
30.314
19.465
1.00
41.50
C


ATOM
1008
O
GLU
A
252
53.789
29.203
19.215
1.00
41.39
O


ATOM
1009
CB
GLU
A
252
50.893
30.456
20.020
1.00
46.53
C


ATOM
1010
CG
GLU
A
252
49.920
29.576
20.810
1.00
51.69
C


ATOM
1011
CD
GLU
A
252
49.586
30.124
22.193
1.00
54.01
C


ATOM
1012
OE1
GLU
A
252
48.841
31.128
22.279
1.00
53.93
O


ATOM
1013
OE2
GLU
A
252
50.070
29.545
23.194
1.00
55.79
O


ATOM
1014
N
ALA
A
253
53.682
31.404
18.788
1.00
38.82
N


ATOM
1015
CA
ALA
A
253
54.651
31.343
17.698
1.00
36.89
C


ATOM
1016
C
ALA
A
253
56.078
31.102
18.212
1.00
36.24
C


ATOM
1017
O
ALA
A
253
56.968
30.739
17.441
1.00
35.13
O


ATOM
1018
CB
ALA
A
253
54.596
32.622
16.881
1.00
35.91
C


ATOM
1019
N
GLY
A
254
56.292
31.313
19.510
1.00
35.29
N


ATOM
1020
CA
GLY
A
254
57.609
31.085
20.086
1.00
35.95
C


ATOM
1021
C
GLY
A
254
58.480
32.301
20.380
1.00
35.64
C


ATOM
1022
O
GLY
A
254
59.684
32.159
20.578
1.00
35.66
O


ATOM
1023
N
ALA
A
255
57.895
33.493
20.410
1.00
35.20
N


ATOM
1024
CA
ALA
A
255
58.675
34.694
20.697
1.00
33.82
C


ATOM
1025
C
ALA
A
255
59.321
34.554
22.074
1.00
32.75
C


ATOM
1026
O
ALA
A
255
58.653
34.196
23.045
1.00
32.02
O


ATOM
1027
CB
ALA
A
255
57.779
35.922
20.657
1.00
33.94
C


ATOM
1028
N
ASP
A
256
60.621
34.834
22.156
1.00
31.67
N


ATOM
1029
CA
ASP
A
256
61.351
34.723
23.418
1.00
32.02
C


ATOM
1030
C
ASP
A
256
61.145
35.912
24.355
1.00
31.11
C


ATOM
1031
O
ASP
A
256
61.234
35.777
25.574
1.00
30.14
O


ATOM
1032
CB
ASP
A
256
62.841
34.541
23.139
1.00
33.02
C


ATOM
1033
CG
ASP
A
256
63.129
33.275
22.362
1.00
34.81
C


ATOM
1034
OD1
ASP
A
256
63.114
32.188
22.979
1.00
36.54
O


ATOM
1035
OD2
ASP
A
256
63.350
33.365
21.135
1.00
33.32
O


ATOM
1036
N
VAL
A
257
60.871
37.077
23.784
1.00
30.39
N


ATOM
1037
CA
VAL
A
257
60.660
38.271
24.589
1.00
29.66
C


ATOM
1038
C
VAL
A
257
59.823
39.270
23.808
1.00
29.38
C


ATOM
1039
O
VAL
A
257
59.879
39.308
22.582
1.00
28.28
O


ATOM
1040
CB
VAL
A
257
62.012
38.911
24.988
1.00
29.16
C


ATOM
1041
CG1
VAL
A
257
62.829
39.194
23.747
1.00
29.29
C


ATOM
1042
CG2
VAL
A
257
61.782
40.177
25.798
1.00
28.00
C


ATOM
1043
N
LEU
A
258
59.038
40.065
24.523
1.00
28.75
N


ATOM
1044
CA
LEU
A
258
58.187
41.059
23.886
1.00
29.85
C


ATOM
1045
C
LEU
A
258
58.608
42.453
24.344
1.00
29.91
C


ATOM
1046
O
LEU
A
258
59.381
42.597
25.293
1.00
30.16
O


ATOM
1047
CB
LEU
A
258
56.720
40.823
24.265
1.00
28.53
C


ATOM
1048
CG
LEU
A
258
56.167
39.402
24.111
1.00
29.86
C


ATOM
1049
CD1
LEU
A
258
54.713
39.397
24.543
1.00
30.36
C


ATOM
1050
CD2
LEU
A
258
56.296
38.921
22.670
1.00
28.79
C


ATOM
1051
N
CYS
A
259
58.104
43.477
23.663
1.00
29.40
N


ATOM
1052
CA
CYS
A
259
58.416
44.850
24.034
1.00
28.72
C


ATOM
1053
C
CYS
A
259
57.344
45.795
23.530
1.00
27.77
C


ATOM
1054
O
CYS
A
259
57.043
45.820
22.337
1.00
27.16
O


ATOM
1055
CB
CYS
A
259
59.772
45.285
23.465
1.00
28.20
C


ATOM
1056
SG
CYS
A
259
60.305
46.904
24.092
1.00
28.27
S


ATOM
1057
N
ILE
A
260
56.766
46.564
24.446
1.00
28.22
N


ATOM
1058
CA
ILE
A
260
55.744
47.533
24.083
1.00
29.67
C


ATOM
1059
C
ILE
A
260
56.463
48.683
23.373
1.00
31.98
C


ATOM
1060
O
ILE
A
260
57.365
49.308
23.927
1.00
31.74
O


ATOM
1061
CB
ILE
A
260
55.010
48.056
25.325
1.00
28.89
C


ATOM
1062
CG1
ILE
A
260
54.391
46.877
26.086
1.00
28.30
C


ATOM
1063
CG2
ILE
A
260
53.926
49.045
24.912
1.00
26.45
C


ATOM
1064
CD1
ILE
A
260
53.791
47.257
27.423
1.00
26.77
C


ATOM
1065
N
ASP
A
261
56.045
48.936
22.139
1.00
33.17
N


ATOM
1066
CA
ASP
A
261
56.625
49.951
21.267
1.00
35.06
C


ATOM
1067
C
ASP
A
261
55.836
51.272
21.315
1.00
35.12
C


ATOM
1068
O
ASP
A
261
54.712
51.338
20.820
1.00
36.56
O


ATOM
1069
CB
ASP
A
261
56.647
49.349
19.852
1.00
36.45
C


ATOM
1070
CG
ASP
A
261
57.248
50.264
18.819
1.00
38.72
C


ATOM
1071
OD1
ASP
A
261
58.086
51.109
19.176
1.00
41.12
O


ATOM
1072
OD2
ASP
A
261
56.892
50.118
17.630
1.00
41.11
O


ATOM
1073
N
SER
A
262
56.420
52.321
21.902
1.00
33.61
N


ATOM
1074
CA
SER
A
262
55.729
53.610
22.003
1.00
33.31
C


ATOM
1075
C
SER
A
262
56.640
54.837
22.141
1.00
32.60
C


ATOM
1076
O
SER
A
262
57.725
54.751
22.711
1.00
32.55
O


ATOM
1077
CB
SER
A
262
54.755
53.566
23.185
1.00
34.17
C


ATOM
1078
OG
SER
A
262
54.108
54.811
23.367
1.00
33.91
O


ATOM
1079
N
SER
A
263
56.185
55.986
21.638
1.00
31.57
N


ATOM
1080
CA
SER
A
263
56.976
57.216
21.715
1.00
31.90
C


ATOM
1081
C
SER
A
263
56.966
57.806
23.119
1.00
31.13
C


ATOM
1082
O
SER
A
263
57.846
58.585
23.483
1.00
32.42
O


ATOM
1083
CB
SER
A
263
56.471
58.265
20.709
1.00
32.36
C


ATOM
1084
OG
SER
A
263
55.175
58.741
21.027
1.00
34.74
O


ATOM
1085
N
ASP
A
264
55.963
57.441
23.905
1.00
29.11
N


ATOM
1086
CA
ASP
A
264
55.864
57.918
25.279
1.00
27.37
C


ATOM
1087
C
ASP
A
264
55.321
56.786
26.142
1.00
26.83
C


ATOM
1088
O
ASP
A
264
54.107
56.594
26.249
1.00
26.56
O


ATOM
1089
CB
ASP
A
264
54.960
59.156
25.351
1.00
26.62
C


ATOM
1090
CG
ASP
A
264
54.591
59.538
26.778
1.00
25.32
C


ATOM
1091
OD1
ASP
A
264
55.309
59.148
27.725
1.00
23.54
O


ATOM
1092
OD2
ASP
A
264
53.578
60.243
26.949
1.00
25.29
O


ATOM
1093
N
GLY
A
265
56.239
56.036
26.744
1.00
25.91
N


ATOM
1094
CA
GLY
A
265
55.868
54.908
27.581
1.00
26.10
C


ATOM
1095
C
GLY
A
265
55.421
55.273
28.981
1.00
26.66
C


ATOM
1096
O
GLY
A
265
55.005
54.404
29.750
1.00
26.18
O


ATOM
1097
N
PHE
A
266
55.514
56.551
29.328
1.00
26.34
N


ATOM
1098
CA
PHE
A
266
55.082
56.982
30.650
1.00
26.68
C


ATOM
1099
C
PHE
A
266
53.564
57.071
30.531
1.00
27.63
C


ATOM
1100
O
PHE
A
266
52.988
58.150
30.606
1.00
26.70
O


ATOM
1101
CB
PHE
A
266
55.677
58.352
30.984
1.00
25.83
C


ATOM
1102
CG
PHE
A
266
55.781
58.634
32.462
1.00
26.28
C


ATOM
1103
CD1
PHE
A
266
55.018
57.915
33.386
1.00
25.02
C


ATOM
1104
CD2
PHE
A
266
56.618
59.647
32.927
1.00
25.66
C


ATOM
1105
CE1
PHE
A
266
55.083
58.201
34.745
1.00
23.88
C


ATOM
1106
CE2
PHE
A
266
56.694
59.946
34.290
1.00
24.67
C


ATOM
1107
CZ
PHE
A
266
55.923
59.221
35.202
1.00
26.34
C


ATOM
1108
N
SER
A
267
52.924
55.917
30.338
1.00
29.46
N


ATOM
1109
CA
SER
A
267
51.477
55.855
30.154
1.00
30.33
C


ATOM
1110
C
SER
A
267
50.777
54.748
30.930
1.00
31.43
C


ATOM
1111
O
SER
A
267
51.302
53.642
31.087
1.00
29.64
O


ATOM
1112
CB
SER
A
267
51.160
55.677
28.670
1.00
30.83
C


ATOM
1113
OG
SER
A
267
49.775
55.456
28.462
1.00
33.50
O


ATOM
1114
N
GLU
A
268
49.572
55.053
31.394
1.00
32.18
N


ATOM
1115
CA
GLU
A
268
48.783
54.087
32.135
1.00
33.83
C


ATOM
1116
C
GLU
A
268
48.483
52.896
31.227
1.00
33.76
C


ATOM
1117
O
GLU
A
268
48.289
51.778
31.699
1.00
34.08
O


ATOM
1118
CB
GLU
A
268
47.481
54.729
32.621
1.00
35.26
C


ATOM
1119
CG
GLU
A
268
46.691
53.851
33.573
1.00
39.14
C


ATOM
1120
CD
GLU
A
268
45.494
54.561
34.188
1.00
41.79
C


ATOM
1121
OE1
GLU
A
268
44.761
53.901
34.961
1.00
43.08
O


ATOM
1122
OE2
GLU
A
268
45.286
55.767
33.908
1.00
41.44
O


ATOM
1123
N
TRP
A
269
48.458
53.133
29.920
1.00
33.42
N


ATOM
1124
CA
TRP
A
269
48.190
52.058
28.972
1.00
34.58
C


ATOM
1125
C
TRP
A
269
49.255
50.963
29.027
1.00
34.05
C


ATOM
1126
O
TRP
A
269
48.942
49.784
28.846
1.00
33.83
O


ATOM
1127
CB
TRP
A
269
48.087
52.602
27.543
1.00
36.69
C


ATOM
1128
CG
TRP
A
269
46.919
53.508
27.340
1.00
40.80
C


ATOM
1129
CD1
TRP
A
269
46.944
54.869
27.236
1.00
41.67
C


ATOM
1130
CD2
TRP
A
269
45.540
53.126
27.268
1.00
42.61
C


ATOM
1131
NE1
TRP
A
269
45.667
55.359
27.106
1.00
43.36
N


ATOM
1132
CE2
TRP
A
269
44.785
54.311
27.123
1.00
43.31
C


ATOM
1133
CE3
TRP
A
269
44.868
51.896
27.315
1.00
43.67
C


ATOM
1134
CZ2
TRP
A
269
43.390
54.305
27.024
1.00
44.76
C


ATOM
1135
CZ3
TRP
A
269
43.480
51.888
27.216
1.00
44.62
C


ATOM
1136
CH2
TRP
A
269
42.757
53.087
27.072
1.00
45.35
C


ATOM
1137
N
GLN
A
270
50.510
51.344
29.257
1.00
32.55
N


ATOM
1138
CA
GLN
A
270
51.582
50.354
29.343
1.00
32.29
C


ATOM
1139
C
GLN
A
270
51.421
49.566
30.641
1.00
31.72
C


ATOM
1140
O
GLN
A
270
51.685
48.368
30.686
1.00
31.18
O


ATOM
1141
CB
GLN
A
270
52.961
51.025
29.314
1.00
31.01
C


ATOM
1142
CG
GLN
A
270
53.207
51.882
28.083
1.00
30.60
C


ATOM
1143
CD
GLN
A
270
54.489
51.525
27.357
1.00
30.06
C


ATOM
1144
OE1
GLN
A
270
55.390
50.904
27.923
1.00
29.84
O


ATOM
1145
NE2
GLN
A
270
54.584
51.932
26.100
1.00
28.50
N


ATOM
1146
N
LYS
A
271
50.991
50.246
31.698
1.00
32.14
N


ATOM
1147
CA
LYS
A
271
50.782
49.575
32.971
1.00
33.59
C


ATOM
1148
C
LYS
A
271
49.694
48.514
32.793
1.00
33.87
C


ATOM
1149
O
LYS
A
271
49.838
47.378
33.246
1.00
33.86
O


ATOM
1150
CB
LYS
A
271
50.355
50.568
34.051
1.00
33.76
C


ATOM
1151
CG
LYS
A
271
50.063
49.894
35.384
1.00
35.01
C


ATOM
1152
CD
LYS
A
271
49.834
50.893
36.498
1.00
36.09
C


ATOM
1153
CE
LYS
A
271
49.709
50.170
37.835
1.00
38.50
C


ATOM
1154
NZ
LYS
A
271
49.561
51.103
38.991
1.00
41.38
N


ATOM
1155
N
ILE
A
272
48.612
48.895
32.121
1.00
33.39
N


ATOM
1156
CA
ILE
A
272
47.501
47.987
31.873
1.00
34.07
C


ATOM
1157
C
ILE
A
272
47.957
46.798
31.034
1.00
33.99
C


ATOM
1158
O
ILE
A
272
47.635
45.653
31.345
1.00
34.22
O


ATOM
1159
CB
ILE
A
272
46.341
48.713
31.145
1.00
33.73
C


ATOM
1160
CG1
ILE
A
272
45.735
49.768
32.074
1.00
34.18
C


ATOM
1161
CG2
ILE
A
272
45.281
47.710
30.707
1.00
33.44
C


ATOM
1162
CD1
ILE
A
272
44.704
50.668
31.413
1.00
34.51
C


ATOM
1163
N
THR
A
273
48.715
47.072
29.977
1.00
33.02
N


ATOM
1164
CA
THR
A
273
49.205
46.013
29.104
1.00
33.58
C


ATOM
1165
C
THR
A
273
50.099
45.011
29.835
1.00
34.00
C


ATOM
1166
O
THR
A
273
49.921
43.800
29.697
1.00
33.77
O


ATOM
1167
CE
THR
A
273
49.986
46.595
27.911
1.00
33.70
C


ATOM
1168
OG1
THR
A
273
49.114
47.426
27.135
1.00
35.34
O


ATOM
1169
CG2
THR
A
273
50.521
45.480
27.025
1.00
32.30
C


ATOM
1170
N
ILE
A
274
51.065
45.512
30.599
1.00
33.72
N


ATOM
1171
CA
ILE
A
274
51.969
44.640
31.340
1.00
33.64
C


ATOM
1172
C
ILE
A
274
51.176
43.843
32.375
1.00
34.72
C


ATOM
1173
O
ILE
A
274
51.414
42.650
32.571
1.00
33.85
O


ATOM
1174
CB
ILE
A
274
53.060
45.451
32.071
1.00
33.60
C


ATOM
1175
CG1
ILE
A
274
53.927
46.194
31.051
1.00
33.18
C


ATOM
1176
CG2
ILE
A
274
53.906
44.521
32.950
1.00
33.23
C


ATOM
1177
CD1
ILE
A
274
54.987
47.089
31.674
1.00
33.18
C


ATOM
1178
N
GLY
A
275
50.231
44.513
33.030
1.00
34.87
N


ATOM
1179
CA
GLY
A
275
49.412
43.860
34.036
1.00
36.02
C


ATOM
1180
C
GLY
A
275
48.617
42.686
33.492
1.00
36.38
C


ATOM
1181
O
GLY
A
275
48.494
41.655
34.147
1.00
37.56
O


ATOM
1182
N
TRP
A
276
48.075
42.846
32.292
1.00
36.26
N


ATOM
1183
CA
TRP
A
276
47.292
41.796
31.656
1.00
36.36
C


ATOM
1184
C
TRP
A
276
48.193
40.601
31.366
1.00
37.31
C


ATOM
1185
O
TRP
A
276
47.788
39.448
31.531
1.00
37.11
O


ATOM
1186
CB
TRP
A
276
46.701
42.307
30.344
1.00
35.76
C


ATOM
1187
CG
TRP
A
276
45.824
41.316
29.656
1.00
36.30
C


ATOM
1188
CD1
TRP
A
276
44.483
41.132
29.850
1.00
35.72
C


ATOM
1189
CD2
TRP
A
276
46.222
40.359
28.665
1.00
35.75
C


ATOM
1190
NE1
TRP
A
276
44.023
40.121
29.038
1.00
35.15
N


ATOM
1191
CE2
TRP
A
276
45.067
39.629
28.301
1.00
35.45
C


ATOM
1192
CE3
TRP
A
276
47.443
40.047
28.050
1.00
35.85
C


ATOM
1193
CZ2
TRP
A
276
45.094
38.607
27.347
1.00
35.33
C


ATOM
1194
CZ3
TRP
A
276
47.471
39.027
27.098
1.00
36.37
C


ATOM
1195
CN2
TRP
A
276
46.300
38.320
26.758
1.00
36.25
C


ATOM
1196
N
ILE
A
277
49.415
40.885
30.926
1.00
36.56
N


ATOM
1197
CA
ILE
A
277
50.370
39.834
30.607
1.00
36.06
C


ATOM
1198
C
ILE
A
277
50.757
39.048
31.857
1.00
37.15
C


ATOM
1199
O
ILE
A
277
50.865
37.824
31.821
1.00
36.69
O


ATOM
1200
CE
ILE
A
277
51.636
40.424
29.942
1.00
34.92
C


ATOM
1201
CG1
ILE
A
277
51.282
40.963
28.550
1.00
34.03
C


ATOM
1202
CG2
ILE
A
277
52.724
39.363
29.837
1.00
34.16
C


ATOM
1203
CD1
ILE
A
277
52.412
41.698
27.863
1.00
32.67
C


ATOM
1204
N
ARG
A
278
50.955
39.756
32.962
1.00
38.15
N


ATOM
1205
CA
ARG
A
278
51.328
39.124
34.220
1.00
40.72
C


ATOM
1206
C
ARG
A
278
50.198
38.278
34.802
1.00
42.31
C


ATOM
1207
O
ARG
A
278
50.445
37.273
35.468
1.00
42.76
O


ATOM
1208
CB
ARG
A
278
51.743
40.189
35.234
1.00
39.40
C


ATOM
1209
CG
ARG
A
278
53.054
40.864
34.911
1.00
38.26
C


ATOM
1220
CD
ARG
A
278
54.240
39.956
35.206
1.00
37.49
C


ATOM
1211
NE
ARG
A
278
55.493
40.590
34.802
1.00
35.79
N


ATOM
1212
CZ
ARG
A
278
56.192
40.250
33.725
1.00
34.09
C


ATOM
1213
NH1
ARG
A
278
55.774
39.267
32.938
1.00
33.23
N


ATOM
1214
NH2
ARG
A
278
57.298
40.913
33.420
1.00
33.05
N


ATOM
1215
N
GLU
A
279
48.962
38.692
34.543
1.00
44.10
N


ATOM
1216
CA
GLU
A
279
47.785
37.989
35.039
1.00
46.28
C


ATOM
1217
C
GLU
A
279
47.513
36.691
34.282
1.00
45.72
C


ATOM
1218
O
GLU
A
279
46.944
35.752
34.832
1.00
46.12
O


ATOM
1219
CB
GLU
A
279
46.561
38.903
34.944
1.00
48.80
C


ATOM
1220
CG
GLU
A
279
45.260
38.276
35.411
1.00
54.66
C


ATOM
1221
CD
GLU
A
279
44.101
39.259
35.381
1.00
58.25
C


ATOM
1222
OE1
GLU
A
279
43.781
39.778
34.285
1.00
60.30
O


ATOM
1223
OE2
GLU
A
279
43.511
39.515
36.455
1.00
59.99
O


ATOM
1224
N
LYS
A
280
47.927
36.638
33.022
1.00
44.85
N


ATOM
1225
CA
LYS
A
280
47.704
35.454
32.207
1.00
44.61
C


ATOM
1226
C
LYS
A
280
48.924
34.556
32.057
1.00
43.52
C


ATOM
1227
O
LYS
A
280
48.787
33.361
31.808
1.00
44.19
O


ATOM
1228
CB
LYS
A
280
47.212
35.867
30.817
1.00
46.41
C


ATOM
1229
CG
LYS
A
280
47.082
34.709
29.834
1.00
48.70
C


ATOM
1230
CD
LYS
A
280
46.383
35.138
28.550
1.00
50.95
C


ATOM
1231
CE
LYS
A
280
46.292
33.987
27.556
1.00
51.64
C


ATOM
1232
NZ
LYS
A
280
45.625
32.794
28.148
1.00
53.00
N


ATOM
1233
N
TYR
A
281
50.115
35.122
32.217
1.00
41.82
N


ATOM
1234
CA
TYR
A
281
51.338
34.353
32.050
1.00
39.15
C


ATOM
1235
C
TYR
A
281
52.317
34.435
33.216
1.00
38.62
C


ATOM
1236
O
TYR
A
281
53.355
33.773
33.198
1.00
37.75
O


ATOM
1237
CB
TYR
A
281
52.059
34.816
30.787
1.00
38.77
C


ATOM
1238
CG
TYR
A
281
51.280
34.655
29.503
1.00
37.82
C


ATOM
1239
CD1
TYR
A
281
51.167
33.409
28.882
1.00
37.09
C


ATOM
1240
CD2
TYR
A
281
50.693
35.757
28.882
1.00
36.24
C


ATOM
1241
CE1
TYR
A
281
50.498
33.267
27.670
1.00
36.51
C


ATOM
1242
CE2
TYR
A
281
50.019
35.625
27.674
1.00
37.22
C


ATOM
1243
CZ
TYR
A
281
49.928
34.378
27.071
1.00
37.04
C


ATOM
1244
OH
TYR
A
281
49.284
34.247
25.863
1.00
38.46
O


ATOM
1245
N
GLY
A
282
52.002
35.236
34.225
1.00
38.46
N


ATOM
1246
CA
GLY
A
282
52.926
35.370
35.337
1.00
39.34
C


ATOM
1247
C
GLY
A
282
54.249
35.931
34.829
1.00
40.34
C


ATOM
1248
O
GLY
A
282
54.262
36.760
33.919
1.00
38.99
O


ATOM
1249
N
ASP
A
283
55.360
35.479
35.402
1.00
42.07
N


ATOM
1250
CA
ASP
A
283
56.682
35.945
34.990
1.00
44.04
C


ATOM
1251
C
ASP
A
283
57.306
35.069
33.905
1.00
44.08
C


ATOM
1252
O
ASP
A
283
58.510
35.130
33.674
1.00
44.67
O


ATOM
1253
CB
ASP
A
283
57.629
35.994
36.193
1.00
45.90
C


ATOM
1254
CG
ASP
A
283
57.267
37.087
37.180
1.00
49.98
C


ATOM
1255
OD1
ASP
A
283
57.233
38.274
36.777
1.00
51.56
O


ATOM
1256
OD2
ASP
A
283
57.023
36.760
38.363
1.00
52.17
O


ATOM
1257
N
LYS
A
284
56.493
34.260
33.236
1.00
44.69
N


ATOM
1258
CA
LYS
A
284
57.000
33.373
32.191
1.00
45.15
C


ATOM
1259
C
LYS
A
284
57.172
34.086
30.854
1.00
43.68
C


ATOM
1260
O
LYS
A
284
57.955
33.664
30.001
1.00
44.14
O


ATOM
1261
CB
LYS
A
284
56.064
32.171
32.024
1.00
48.63
C


ATOM
1262
CG
LYS
A
284
56.003
31.260
33.249
1.00
53.02
C


ATOM
1263
CD
LYS
A
284
57.377
30.674
33.572
1.00
56.22
C


ATOM
1264
CE
LYS
A
284
57.326
29.736
34.772
1.00
58.58
C


ATOM
1265
NZ
LYS
A
284
58.679
29.181
35.089
1.00
60.63
N


ATOM
1266
N
VAL
A
285
56.425
35.164
30.669
1.00
40.25
N


ATOM
1267
CA
VAL
A
285
56.514
35.937
29.446
1.00
37.27
C


ATOM
1268
C
VAL
A
285
57.225
37.243
29.773
1.00
35.62
C


ATOM
1269
O
VAL
A
285
56.792
37.997
30.641
1.00
35.11
O


ATOM
1270
CB
VAL
A
285
55.114
36.213
28.874
1.00
37.07
C


ATOM
1271
CG1
VAL
A
285
55.205
37.182
27.706
1.00
35.98
C


ATOM
1272
CG2
VAL
A
285
54.489
34.897
28.418
1.00
37.05
C


ATOM
1273
N
LYS
A
286
58.331
37.494
29.084
1.00
34.12
N


ATOM
1274
CA
LYS
A
286
59.117
38.699
29.311
1.00
31.70
C


ATOM
1275
C
LYS
A
286
58.643
39.823
28.404
1.00
30.65
C


ATOM
1276
O
LYS
A
286
58.443
39.625
27.206
1.00
29.79
O


ATOM
1277
CB
LYS
A
286
60.599
38.411
29.059
1.00
30.46
C


ATOM
1278
CG
LYS
A
286
61.135
37.224
29.847
1.00
30.11
C


ATOM
1279
CD
LYS
A
286
60.902
37.387
31.344
1.00
29.65
C


ATOM
1280
CE
LYS
A
286
61.427
36.183
32.118
1.00
29.40
C


ATOM
1281
NZ
LYS
A
286
61.201
36.319
33.591
1.00
30.72
N


ATOM
1282
N
VAL
A
287
58.469
41.005
28.983
1.00
28.78
N


ATOM
1283
CA
VAL
A
287
58.004
42.154
28.224
1.00
27.93
C


ATOM
1284
C
VAL
A
287
58.722
43.442
28.617
1.00
27.40
C


ATOM
1285
O
VAL
A
287
58.733
43.838
29.784
1.00
26.80
O


ATOM
1286
CB
VAL
A
287
56.463
42.338
28.400
1.00
27.55
C


ATOM
1287
CG1
VAL
A
287
56.102
42.398
29.876
1.00
28.57
C


ATOM
1288
CG2
VAL
A
287
56.002
43.603
27.704
1.00
28.04
C


ATOM
1289
N
GLY
A
288
59.340
44.081
27.630
1.00
28.27
N


ATOM
1290
CA
GLY
A
288
60.031
45.336
27.873
1.00
27.27
C


ATOM
1291
C
GLY
A
288
59.038
46.459
27.644
1.00
27.80
C


ATOM
1292
O
GLY
A
288
58.042
46.263
26.944
1.00
28.16
O


ATOM
1293
N
ALA
A
289
59.293
47.627
28.230
1.00
27.53
N


ATOM
1294
CA
ALA
A
289
58.396
48.771
28.085
1.00
28.35
C


ATOM
1295
C
ALA
A
289
59.171
50.063
27.815
1.00
29.42
C


ATOM
1296
O
ALA
A
289
60.386
50.120
28.021
1.00
29.84
O


ATOM
1297
CB
ALA
A
289
57.543
48.923
29.346
1.00
28.05
C


ATOM
1298
N
GLY
A
290
58.461
51.096
27.364
1.00
28.77
N


ATOM
1299
CA
GLY
A
290
59.096
52.371
27.063
1.00
28.22
C


ATOM
1300
C
GLY
A
290
58.395
53.070
25.905
1.00
28.36
C


ATOM
1301
O
GLY
A
290
57.369
52.588
25.433
1.00
27.76
O


ATOM
1302
N
ASN
A
291
58.942
54.184
25.418
1.00
26.86
N


ATOM
1303
CA
ASN
A
291
60.186
54.766
25.919
1.00
25.60
C


ATOM
1304
C
ASN
A
291
59.985
55.857
26.969
1.00
25.05
C


ATOM
1305
O
ASN
A
291
58.963
56.536
26.987
1.00
25.04
O


ATOM
1306
CB
ASN
A
291
60.973
55.357
24.748
1.00
24.30
C


ATOM
1307
CG
ASN
A
291
61.485
54.298
23.793
1.00
24.09
C


ATOM
1308
OD1
ASN
A
291
60.978
53.180
23.761
1.00
25.26
O


ATOM
1309
ND2
ASN
A
291
62.492
54.651
23.001
1.00
20.96
N


ATOM
1310
N
ILE
A
292
60.965
56.010
27.852
1.00
23.64
N


ATOM
1311
CA
ILE
A
292
60.923
57.054
28.867
1.00
23.62
C


ATOM
1312
C
ILE
A
292
62.290
57.733
28.846
1.00
24.18
C


ATOM
1313
O
ILE
A
292
63.219
57.230
28.200
1.00
24.40
O


ATOM
1314
CB
ILE
A
292
60.583
56.498
30.289
1.00
24.12
C


ATOM
1315
CG1
ILE
A
292
61.395
55.238
30.599
1.00
23.86
C


ATOM
1316
CG2
ILE
A
292
59.093
56.210
30.383
1.00
24.23
C


ATOM
1317
CD1
ILE
A
292
62.865
55.491
30.874
1.00
24.33
C


ATOM
1318
N
VAL
A
293
62.420
58.870
29.528
1.00
22.80
N


ATOM
1319
CA
VAL
A
293
63.686
59.597
29.526
1.00
22.92
C


ATOM
1320
C
VAL
A
293
64.146
60.119
30.876
1.00
23.26
C


ATOM
1321
O
VAL
A
293
65.142
60.840
30.951
1.00
23.53
O


ATOM
1322
CB
VAL
A
293
63.635
60.805
28.561
1.00
22.53
C


ATOM
1323
CG1
VAL
A
293
63.492
60.330
27.122
1.00
21.53
C


ATOM
1324
CG2
VAL
A
293
62.474
61.717
28.943
1.00
21.31
C


ATOM
1325
N
ASP
A
294
63.430
59.779
31.942
1.00
23.20
N


ATOM
1326
CA
ASP
A
294
63.824
60.241
33.269
1.00
23.65
C


ATOM
1327
C
ASP
A
294
63.528
59.203
34.352
1.00
24.09
C


ATOM
1328
O
ASP
A
294
62.885
58.188
34.096
1.00
24.41
O


ATOM
1329
CB
ASP
A
294
63.122
61.570
33.597
1.00
23.02
C


ATOM
1330
CG
ASP
A
294
61.620
61.418
33.778
1.00
24.10
C


ATOM
1331
OD1
ASP
A
294
61.064
60.375
33.376
1.00
26.12
O


ATOM
1332
OD2
ASP
A
294
60.990
62.354
34.312
1.00
25.00
O


ATOM
1333
N
GLY
A
295
64.006
59.467
35.561
1.00
25.18
N


ATOM
1334
CA
GLY
A
295
63.793
58.553
36.669
1.00
25.72
C


ATOM
1335
C
GLY
A
295
62.339
58.246
36.987
1.00
26.61
C


ATOM
1336
O
GLY
A
295
62.016
57.105
37.326
1.00
25.47
O


ATOM
1337
N
GLU
A
296
61.463
59.249
36.894
1.00
27.36
N


ATOM
1338
CA
GLU
A
296
60.042
59.049
37.184
1.00
28.17
C


ATOM
1339
C
GLU
A
296
59.417
58.064
36.214
1.00
26.97
C


ATOM
1340
O
GLU
A
296
58.684
57.166
36.620
1.00
26.88
O


ATOM
1341
CB
GLU
A
296
59.261
60.367
37.103
1.00
31.11
C


ATOM
1342
CG
GLU
A
296
59.579
61.376
38.182
1.00
37.71
C


ATOM
1343
CD
GLU
A
296
58.622
62.567
38.160
1.00
43.64
C


ATOM
1344
OE1
GLU
A
296
58.943
63.589
38.808
1.00
45.94
O


ATOM
1345
OE2
GLU
A
296
57.550
62.482
37.503
1.00
44.55
O


ATOM
1346
N
GLY
A
297
59.695
58.251
34.928
1.00
26.28
N


ATOM
1347
CA
GLY
A
297
59.151
57.363
33.917
1.00
26.08
C


ATOM
1348
C
GLY
A
297
59.661
55.944
34.094
1.00
25.81
C


ATOM
1349
O
GLY
A
297
58.910
54.984
33.932
1.00
26.85
O


ATOM
1350
N
PHE
A
298
60.945
55.813
34.415
1.00
25.29
N


ATOM
1351
CA
PHE
A
298
61.554
54.506
34.639
1.00
25.86
C


ATOM
1352
C
PHE
A
298
60.856
53.815
35.805
1.00
26.44
C


ATOM
1353
O
PHE
A
298
60.461
52.656
35.712
1.00
26.85
O


ATOM
1354
CB
PHE
A
298
63.040
54.655
34.988
1.00
25.61
C


ATOM
1355
CG
PHE
A
298
63.640
53.410
35.585
1.00
25.67
C


ATOM
1356
CD1
PHE
A
298
64.139
52.398
34.771
1.00
24.15
C


ATOM
1357
CD2
PHE
A
298
63.627
53.214
36.964
1.00
24.54
C


ATOM
1358
CE1
PHE
A
298
64.611
51.202
35.325
1.00
24.57
C


ATOM
1359
CE2
PHE
A
298
64.093
52.025
37.524
1.00
24.83
C


ATOM
1360
CZ
PHE
A
298
64.584
51.017
36.701
1.00
23.36
C


ATOM
1361
N
ARG
A
299
60.733
54.553
36.905
1.00
27.12
N


ATOM
1362
CA
ARG
A
299
60.110
54.089
38.143
1.00
29.07
C


ATOM
1363
C
ARG
A
299
58.680
53.603
37.910
1.00
29.11
C


ATOM
1364
O
ARG
A
299
58.275
52.554
38.420
1.00
28.93
O


ATOM
1365
CB
ARG
A
299
60.136
55.235
39.162
1.00
30.82
C


ATOM
1366
CG
ARG
A
299
59.233
55.085
40.370
1.00
35.20
C


ATOM
1367
CD
ARG
A
299
59.914
54.374
41.518
1.00
38.25
C


ATOM
1368
NE
ARG
A
299
61.166
55.010
41.934
1.00
39.66
N


ATOM
1369
CZ
ARG
A
299
61.900
54.581
42.959
1.00
40.55
C


ATOM
1370
NH1
ARG
A
299
61.497
53.533
43.662
1.00
39.93
N


ATOM
1371
NH2
ARG
A
299
63.045
55.173
43.270
1.00
40.75
N


ATOM
1372
N
TYR
A
300
57.912
54.363
37.139
1.00
28.00
N


ATOM
1373
CA
TYR
A
300
56.542
53.973
36.853
1.00
27.38
C


ATOM
1374
C
TYR
A
300
56.486
52.639
36.113
1.00
27.60
C


ATOM
1375
O
TYR
A
300
55.658
51.793
36.424
1.00
27.82
O


ATOM
1376
CB
TYR
A
300
55.841
55.033
36.006
1.00
25.95
C


ATOM
1377
CG
TYR
A
300
54.385
54.714
35.739
1.00
25.23
C


ATOM
1378
CD1
TYR
A
300
53.410
54.933
36.716
1.00
24.39
C


ATOM
1379
CD2
TYR
A
300
53.984
54.183
34.516
1.00
24.30
C


ATOM
1380
CE1
TYR
A
300
52.069
54.631
36.477
1.00
23.68
C


ATOM
1381
CE2
TYR
A
300
52.650
53.875
34.268
1.00
25.86
C


ATOM
1382
CZ
TYR
A
300
51.698
54.104
35.252
1.00
24.81
C


ATOM
1383
OH
TYR
A
300
50.379
53.810
34.995
1.00
24.58
O


ATOM
1384
N
LEU
A
301
57.355
52.454
35.124
1.00
27.28
N


ATOM
1385
CA
LEU
A
301
57.339
51.210
34.369
1.00
27.52
C


ATOM
1386
C
LEU
A
301
57.922
50.044
35.168
1.00
27.98
C


ATOM
1387
O
LEU
A
301
57.539
48.896
34.968
1.00
28.58
O


ATOM
1388
CB
LEU
A
301
58.078
51.386
33.036
1.00
25.33
C


ATOM
1389
CG
LEU
A
301
57.369
52.305
32.024
1.00
25.53
C


ATOM
1390
CD1
LEU
A
301
58.189
52.409
30.741
1.00
20.77
C


ATOM
1391
CD2
LEU
A
301
55.979
51.756
31.714
1.00
23.64
C


ATOM
1392
N
ALA
A
302
58.837
50.340
36.081
1.00
28.68
N


ATOM
1393
CA
ALA
A
302
59.437
49.301
36.911
1.00
29.55
C


ATOM
1394
C
ALA
A
302
58.365
A8.740
37.852
1.00
29.73
C


ATOM
1395
O
ALA
A
302
58.159
47.528
37.925
1.00
29.99
O


ATOM
1396
CB
ALA
A
302
60.607
49.877
37.714
1.00
27.04
C


ATOM
1397
N
ASP
A
303
57.679
49.624
38.565
1.00
30.56
N


ATOM
1398
CA
ASP
A
303
56.625
49.193
39.474
1.00
31.48
C


ATOM
1399
C
ASP
A
303
55.527
48.474
38.704
1.00
32.09
C


ATOM
1400
O
ASP
A
303
54.836
47.620
39.256
1.00
33.91
O


ATOM
1401
CB
ASP
A
303
56.013
50.381
40.218
1.00
31.91
C


ATOM
1402
CG
ASP
A
303
56.947
50.968
41.254
1.00
33.42
C


ATOM
1403
OD1
ASP
A
303
57.869
50.253
41.701
1.00
34.40
O


ATOM
1404
OD2
ASP
A
303
56.743
52.139
41.639
1.00
34.93
O


ATOM
1405
N
ALA
A
304
55.358
48.828
37.434
1.00
31.62
N


ATOM
1406
CA
ALA
A
304
54.336
48.198
36.605
1.00
30.73
C


ATOM
1407
C
ALA
A
304
54.723
46.759
36.239
1.00
30.76
C


ATOM
1408
O
ALA
A
304
53.873
45.969
35.823
1.00
30.18
O


ATOM
1409
CB
ALA
A
304
54.103
49.020
35.346
1.00
30.45
C


ATOM
1410
N
GLY
A
305
56.007
46.425
36.379
1.00
29.89
N


ATOM
1411
CA
GLY
A
305
56.452
45.069
36.086
1.00
28.06
C


ATOM
1412
C
GLY
A
305
57.299
44.817
34.850
1.00
28.84
C


ATOM
1413
O
GLY
A
305
57.596
43.661
34.535
1.00
28.23
O


ATOM
1414
N
ALA
A
306
57.695
45.873
34.144
1.00
28.22
N


ATOM
1415
CA
ALA
A
306
58.510
45.719
32.937
1.00
27.85
C


ATOM
1416
C
ALA
A
306
59.772
44.889
33.206
1.00
27.06
C


ATOM
1417
O
ALA
A
306
60.378
45.010
34.270
1.00
26.25
O


ATOM
1418
CB
ALA
A
306
58.896
47.094
32.399
1.00
28.08
C


ATOM
1419
N
ASP
A
307
60.157
44.049
32.244
1.00
27.17
N


ATOM
1420
CA
ASP
A
307
61.350
43.201
32.374
1.00
27.07
C


ATOM
1421
C
ASP
A
307
62.618
43.950
31.946
1.00
27.21
C


ATOM
1422
O
ASP
A
307
63.737
43.546
32.259
1.00
27.56
O


ATOM
1423
CB
ASP
A
307
61.178
41.918
31.553
1.00
26.85
C


ATOM
1424
CG
ASP
A
307
60.190
40.954
32.187
1.00
29.12
C


ATOM
1425
OD1
ASP
A
307
60.488
40.450
33.290
1.00
29.15
O


ATOM
1426
OD2
ASP
A
307
59.116
40.709
31.592
1.00
29.54
O


ATOM
1427
N
PHE
A
308
62.424
45.021
31.189
1.00
26.81
N


ATOM
1428
CA
PHE
A
308
63.507
45.896
30.771
1.00
26.08
C


ATOM
1429
C
PHE
A
308
62.823
47.180
30.314
1.00
26.24
C


ATOM
1430
O
PHE
A
308
61.677
47.158
29.871
1.00
25.83
O


ATOM
1431
CB
PHE
A
308
64.416
45.245
29.703
1.00
25.02
C


ATOM
1432
CG
PHE
A
308
63.879
45.264
28.291
1.00
24.83
C


ATOM
1433
CD1
PHE
A
308
63.847
46.447
27.552
1.00
24.91
C


ATOM
1434
CD2
PHE
A
308
63.492
44.076
27.671
1.00
24.33
C


ATOM
1435
CE1
PHE
A
308
63.443
46.449
26.210
1.00
24.84
C


ATOM
1436
CE2
PHE
A
308
63.085
44.062
26.330
1.00
25.69
C


ATOM
1437
CZ
PHE
A
308
63.062
45.255
25.597
1.00
25.81
C


ATOM
1438
N
ILE
A
309
63.503
48.305
30.484
1.00
25.90
N


ATOM
1439
CA
ILE
A
309
62.928
49.591
30.130
1.00
25.03
C


ATOM
1440
C
ILE
A
309
63.754
50.294
29.053
1.00
24.57
C


ATOM
1441
O
ILE
A
309
64.976
50.407
29.160
1.00
24.32
O


ATOM
1442
CB
ILE
A
309
62.784
50.445
31.414
1.00
25.42
C


ATOM
1443
CG1
ILE
A
309
61.756
49.763
32.331
1.00
22.98
C


ATOM
1444
CG2
ILE
A
309
62.390
51.891
31.072
1.00
24.21
C


ATOM
1445
CD1
ILE
A
309
61.674
50.320
33.740
1.00
22.68
C


ATOM
1446
N
LYS
A
310
63.068
50.750
28.009
1.00
24.43
N


ATOM
1447
CA
LYS
A
310
63.713
51.396
26.877
1.00
24.50
C


ATOM
1448
C
LYS
A
310
63.785
52.921
27.042
1.00
24.35
C


ATOM
1449
O
LYS
A
310
62.786
53.583
27.334
1.00
23.81
O


ATOM
1450
CB
LYS
A
310
62.970
51.000
25.598
1.00
24.83
C


ATOM
1451
CG
LYS
A
310
63.793
51.071
24.336
1.00
24.74
C


ATOM
1452
CD
LYS
A
310
63.473
49.906
23.401
1.00
24.26
C


ATOM
1453
CE
LYS
A
310
62.069
49.994
22.836
1.00
24.22
C


ATOM
1454
NZ
LYS
A
310
61.904
51.272
22.092
1.00
23.28
N


ATOM
1455
N
ILE
A
311
64.986
53.459
26.851
1.00
23.88
N


ATOM
1456
CA
ILE
A
311
65.252
54.890
27.009
1.00
23.05
C


ATOM
1457
C
ILE
A
311
65.399
55.641
25.693
1.00
23.48
C


ATOM
1458
O
ILE
A
311
66.113
55.194
24.792
1.00
22.99
O


ATOM
1459
CB
ILE
A
311
66.562
55.118
27.804
1.00
21.85
C


ATOM
1460
CG1
ILE
A
311
66.503
54.367
29.137
1.00
19.66
C


ATOM
1461
CG2
ILE
A
311
66.782
56.619
28.037
1.00
19.08
C


ATOM
1462
CD1
ILE
A
311
67.858
54.239
29.821
1.00
19.70
C


ATOM
1463
N
GLY
A
312
64.730
56.785
25.582
1.00
23.63
N


ATOM
1464
CA
GLY
A
312
64.871
57.569
24.374
1.00
24.66
C


ATOM
1465
C
GLY
A
312
63.644
58.103
23.669
1.00
26.40
C


ATOM
1466
O
GLY
A
312
62.771
57.350
23.240
1.00
25.18
O


ATOM
1467
N
ILE
A
313
63.595
59.426
23.553
1.00
28.70
N


ATOM
1468
CA
ILE
A
313
62.527
60.128
22.854
1.00
31.54
C


ATOM
1469
C
ILE
A
313
63.184
61.309
22.152
1.00
35.25
C


ATOM
1470
O
ILE
A
313
63.698
62.216
22.811
1.00
33.97
O


ATOM
1471
CB
ILE
A
313
61.450
60.678
23.812
1.00
30.50
C


ATOM
1472
CG1
ILE
A
313
60.739
59.528
24.529
1.00
29.70
C


ATOM
1473
CG2
ILE
A
313
60.438
61.498
23.021
1.00
30.02
C


ATOM
1474
CD1
ILE
A
313
59.794
59.984
25.624
1.00
27.55
C


ATOM
1475
N
GLY
A
314
63.190
61.283
20.823
1.00
40.22
N


ATOM
1476
CA
GLY
A
314
63.780
62.372
20.065
1.00
47.64
C


ATOM
1477
C
GLY
A
314
65.152
62.121
19.458
1.00
53.44
C


ATOM
1478
O
GLY
A
314
65.474
62.660
18.392
1.00
54.62
O


ATOM
1479
N
GLY
A
315
65.965
61.306
20.125
1.00
57.31
N


ATOM
1480
CA
GLY
A
315
67.304
61.024
19.632
1.00
62.24
C


ATOM
1481
C
GLY
A
315
67.422
60.395
18.251
1.00
65.54
C


ATOM
1482
O
GLY
A
315
68.347
60.724
17.509
1.00
66.23
O


ATOM
1483
N
GLY
A
316
66.499
59.497
17.906
1.00
68.35
N


ATOM
1484
CA
GLY
A
316
66.534
58.826
16.611
1.00
71.80
C


ATOM
1485
C
GLY
A
316
66.996
59.648
15.415
1.00
74.31
C


ATOM
1486
O
GLY
A
316
66.889
60.875
15.413
1.00
74.26
O


ATOM
1487
N
SER
A
317
67.505
58.968
14.388
1.00
76.73
N


ATOM
1488
CA
SER
A
317
67.989
59.635
13.178
1.00
79.34
C


ATOM
1489
C
SER
A
317
66.831
60.196
12.357
1.00
81.34
C


ATOM
1490
O
SER
A
317
66.887
61.330
11.879
1.00
81.51
O


ATOM
1491
CB
SER
A
317
68.799
58.663
12.314
1.00
79.01
C


ATOM
1492
OG
SER
A
317
67.969
57.683
11.719
1.00
78.20
O


ATOM
1493
N
ILE
A
318
65.789
59.387
12.189
1.00
83.77
N


ATOM
1494
CA
ILE
A
318
64.602
59.797
11.444
1.00
86.14
C


ATOM
1495
C
ILE
A
318
63.663
60.558
12.371
1.00
87.68
C


ATOM
1496
O
ILE
A
318
62.441
60.481
12.236
1.00
87.87
O


ATOM
1497
CS
ILE
A
318
63.845
58.575
10.866
1.00
85.84
C


ATOM
1498
CG1
ILE
A
318
64.062
57.346
11.756
1.00
85.74
C


ATOM
1499
CG2
ILE
A
318
64.323
58.291
9.448
1.00
86.18
C


ATOM
1500
CD1
ILE
A
318
63.713
57.544
13.210
1.00
84.97
C


ATOM
1501
N
CYS
A
319
64.250
61.293
13.312
1.00
89.77
N


ATOM
1502
CA
CYS
A
319
63.484
62.064
14.282
1.00
91.80
C


ATOM
1503
C
CYS
A
319
63.660
63.571
14.135
1.00
92.66
C


ATOM
1504
O
CYS
A
319
64.776
64.090
14.207
1.00
92.78
O


ATOM
1505
CS
CYS
A
319
63.878
61.660
15.703
1.00
92.28
C


ATOM
1506
SG
CYS
A
319
63.009
62.593
16.985
1.00
94.56
S


ATOM
1507
N
ILE
A
320
62.545
64.268
13.937
1.00
93.64
N


ATOM
1508
CA
ILE
A
320
62.552
65.720
13.800
1.00
94.66
C


ATOM
1509
C
ILE
A
320
61.771
66.290
14.988
1.00
94.85
C


ATOM
1510
O
ILE
A
320
60.809
67.041
14.814
1.00
95.16
O


ATOM
1511
CB
ILE
A
320
61.876
66.165
12.473
1.00
95.15
C


ATOM
1512
CG1
ILE
A
320
62.418
65.339
11.299
1.00
95.39
C


ATOM
1513
CG2
ILE
A
320
62.132
67.649
12.226
1.00
94.99
C


ATOM
1514
CD1
ILE
A
320
63.920
65.452
11.086
1.00
95.47
C


ATOM
1515
N
THR
A
321
62.200
65.913
16.193
1.00
94.85
N


ATOM
1516
CA
THR
A
321
61.572
66.338
17.446
1.00
94.56
C


ATOM
1517
C
THR
A
321
60.932
67.723
17.389
1.00
94.12
C


ATOM
1518
O
THR
A
321
59.744
67.876
17.683
1.00
93.67
O


ATOM
1519
CS
THR
A
321
62.590
66.322
18.606
1.00
94.80
C


ATOM
1520
OG1
THR
A
321
63.228
65.040
18.664
1.00
94.77
O


ATOM
1521
CG2
THR
A
321
61.891
66.588
19.931
1.00
94.58
C


ATOM
1522
N
ARG
A
322
61.721
68.730
17.022
1.00
93.60
N


ATOM
1523
CA
ARG
A
322
61.208
70.091
16.926
1.00
92.93
C


ATOM
1524
C
ARG
A
322
59.929
70.126
16.098
1.00
91.61
C


ATOM
1525
O
ARG
A
322
58.860
70.457
16.611
1.00
91.89
O


ATOM
1526
CS
ARG
A
322
62.250
71.025
16.301
1.00
93.99
C


ATOM
1527
CG
ARG
A
322
63.301
71.546
17.274
1.00
95.47
C


ATOM
1528
CD
ARG
A
322
64.337
70.495
17.640
1.00
96.98
C


ATOM
1529
NE
ARG
A
322
65.319
71.030
18.583
1.00
98.14
N


ATOM
1530
CZ
ARG
A
322
66.530
70.517
18.784
1.00
98.80
C


ATOM
1531
NH1
ARG
A
322
66.925
69.448
18.105
1.00
98.87
N


ATOM
1532
NH2
ARG
A
322
67.348
71.079
19.663
1.00
99.15
N


ATOM
1533
N
GLU
A
323
60.036
69.778
14.820
1.00
89.52
N


ATOM
1534
CA
GLU
A
323
58.871
69.778
13.946
1.00
87.37
C


ATOM
1535
C
GLU
A
323
57.958
68.588
14.247
1.00
84.86
C


ATOM
1536
O
GLU
A
323
57.628
67.795
13.361
1.00
84.93
O


ATOM
1537
CS
GLU
A
323
59.311
69.757
12.478
1.00
88.77
C


ATOM
1538
CG
GLU
A
323
58.163
69.856
11.473
1.00
90.52
C


ATOM
1539
CD
GLU
A
323
57.281
71.080
11.689
1.00
91.42
C


ATOM
1540
OE1
GLU
A
323
56.303
71.245
10.927
1.00
91.57
O


ATOM
1541
OE2
GLU
A
323
57.560
71.875
12.615
1.00
91.76
O


ATOM
1542
N
GLN
A
324
57.553
68.473
15.509
1.00
81.41
N


ATOM
1543
CA
GLN
A
324
56.676
67.393
15.944
1.00
77.43
C


ATOM
1544
C
GLN
A
324
55.848
67.831
17.153
1.00
73.46
C


ATOM
1545
O
GLN
A
324
54.919
68.630
17.018
1.00
73.89
O


ATOM
1546
CS
GLN
A
324
57.503
66.146
16.289
1.00
79.24
C


ATOM
1547
CG
GLN
A
324
56.677
64.923
16.679
1.00
81.03
C


ATOM
1548
CD
GLN
A
324
55.595
64.599
15.665
1.00
82.58
C


ATOM
1549
OE1
GLN
A
324
55.867
64.472
14.471
1.00
83.19
O


ATOM
1550
NE2
GLN
A
324
54.359
64.463
16.137
1.00
83.06
N


ATOM
1551
N
LYS
A
325
56.191
67.312
18.329
1.00
67.65
N


ATOM
1552
CA
LYS
A
325
55.476
67.644
19.556
1.00
61.35
C


ATOM
1553
C
LYS
A
325
56.326
68.484
20.492
1.00
56.32
C


ATOM
1554
O
LYS
A
325
55.807
69.147
21.391
1.00
55.43
O


ATOM
1555
CB
LYS
A
325
55.056
66.375
20.299
1.00
62.67
C


ATOM
1556
CG
LYS
A
325
53.889
65.612
19.697
1.00
63.57
C


ATOM
1557
CD
LYS
A
325
53.512
64.469
20.624
1.00
64.06
C


ATOM
1558
CE
LYS
A
325
52.278
63.738
20.158
1.00
64.95
C


ATOM
1559
NZ
LYS
A
325
51.932
62.638
21.100
1.00
65.54
N


ATOM
1560
N
GLY
A
326
57.636
68.444
20.292
1.00
50.41
N


ATOM
1561
CA
GLY
A
326
58.515
69.204
21.152
1.00
44.73
C


ATOM
1562
C
GLY
A
326
58.777
68.502
22.473
1.00
41.12
C


ATOM
1563
O
GLY
A
326
59.036
69.151
23.484
1.00
38.92
O


ATOM
1564
N
ILE
A
327
58.684
67.174
22.474
1.00
37.83
N


ATOM
1565
CA
ILE
A
327
58.954
66.403
23.680
1.00
34.93
C


ATOM
1566
C
ILE
A
327
60.248
65.627
23.449
1.00
32.50
C


ATOM
1567
O
ILE
A
327
60.556
65.229
22.329
1.00
30.63
O


ATOM
1568
CB
ILE
A
327
57.807
65.406
24.022
1.00
35.16
C


ATOM
1569
CG1
ILE
A
327
57.684
64.340
22.936
1.00
35.16
C


ATOM
1570
CG2
ILE
A
327
56.485
66.157
24.169
1.00
36.07
C


ATOM
1571
CD1
ILE
A
327
56.624
63.273
23.233
1.00
37.60
C


ATOM
1572
N
GLY
A
328
61.018
65.429
24.507
1.00
30.83
N


ATOM
1573
CA
GLY
A
328
62.257
64.695
24.351
1.00
30.46
C


ATOM
1574
C
GLY
A
328
63.331
65.116
25.326
1.00
28.07
C


ATOM
1575
O
GLY
A
328
63.087
65.907
26.241
1.00
26.85
O


ATOM
1576
N
ARG
A
329
64.531
64.587
25.121
1.00
27.11
N


ATOM
1577
CA
ARG
A
329
65.650
64.897
25.991
1.00
25.00
C


ATOM
1578
C
ARG
A
329
66.912
64.341
25.355
1.00
24.52
C


ATOM
1579
O
ARG
A
329
66.866
63.282
24.728
1.00
24.57
O


ATOM
1580
CB
ARG
A
329
65.426
64.243
27.356
1.00
25.02
C


ATOM
1581
CG
ARG
A
329
66.250
64.828
28.486
1.00
23.52
C


ATOM
1582
CD
ARG
A
329
66.101
63.994
29.745
1.00
23.12
C


ATOM
1583
NE
ARG
A
329
66.454
64.757
30.935
1.00
23.07
N


ATOM
1584
CZ
ARG
A
329
66.352
64.300
32.177
1.00
24.79
C


ATOM
1585
NH1
ARG
A
329
65.909
63.067
32.402
1.00
25.05
N


ATOM
1586
NH2
ARG
A
329
66.670
65.086
33.198
1.00
23.95
N


ATOM
1587
N
GLY
A
330
68.031
65.053
25.502
1.00
22.80
N


ATOM
1588
CA
GLY
A
330
69.281
64.560
24.952
1.00
21.71
C


ATOM
1589
C
GLY
A
330
69.466
63.134
25.449
1.00
22.12
C


ATOM
1590
O
GLY
A
330
69.269
62.856
26.635
1.00
21.20
O


ATOM
1591
N
GLN
A
331
69.844
62.230
24.552
1.00
22.96
N


ATOM
1592
CA
GLN
A
331
70.005
60.824
24.900
1.00
23.04
C


ATOM
1593
C
GLN
A
331
70.969
60.550
26.054
1.00
23.91
C


ATOM
1594
O
GLN
A
331
70.689
59.699
26.901
1.00
24.69
O


ATOM
1595
CB
GLN
A
331
70.440
60.023
23.670
1.00
23.45
C


ATOM
1596
CG
GLN
A
331
70.322
58.504
23.848
1.00
23.57
C


ATOM
1597
CD
GLN
A
331
68.876
58.025
23.890
1.00
26.07
C


ATOM
1598
OE1
GLN
A
331
68.595
56.889
24.278
1.00
28.19
O


ATOM
1599
NE2
GLN
A
331
67.954
58.887
23.483
1.00
23.86
N


ATOM
1600
N
ALA
A
332
72.098
61.256
26.096
1.00
22.41
N


ATOM
1601
CA
ALA
A
332
73.068
61.042
27.169
1.00
22.13
C


ATOM
1602
C
ALA
A
332
72.460
61.375
28.529
1.00
21.81
C


ATOM
1603
O
ALA
A
332
72.528
60.581
29.472
1.00
20.89
O


ATOM
1604
CB
ALA
A
332
74.326
61.886
26.928
1.00
21.50
C


ATOM
1605
N
THR
A
333
71.857
62.553
28.626
1.00
20.86
N


ATOM
1606
CA
THR
A
333
71.239
62.979
29.867
1.00
21.05
C


ATOM
1607
C
THR
A
333
70.148
61.998
30.276
1.00
22.50
C


ATOM
1608
O
THR
A
333
70.013
61.668
31.456
1.00
22.49
O


ATOM
1609
CB
THR
A
333
70.622
64.384
29.730
1.00
20.97
C


ATOM
1610
CG1
THR
A
333
71.643
65.308
29.334
1.00
19.27
O


ATOM
1611
CG2
THR
A
333
70.023
64.839
31.069
1.00
20.51
C


ATOM
1612
N
ALA
A
334
69.378
61.529
29.297
1.00
21.69
N


ATOM
1613
CA
ALA
A
334
68.299
60.583
29.568
1.00
22.09
C


ATOM
1614
C
ALA
A
334
68.835
59.278
30.163
1.00
21.26
C


ATOM
1615
O
ALA
A
334
68.314
58.780
31.160
1.00
22.26
O


ATOM
1616
CB
ALA
A
334
67.521
60.290
28.281
1.00
20.13
C


ATOM
1617
N
VAL
A
335
69.866
58.721
29.539
1.00
22.35
N


ATOM
1618
CA
VAL
A
335
70.458
57.469
30.010
1.00
22.27
C


ATOM
1619
C
VAL
A
335
71.061
57.628
31.404
1.00
22.75
C


ATOM
1620
O
VAL
A
335
70.810
56.814
32.298
1.00
24.25
O


ATOM
1621
CB
VAL
A
335
71.561
56.965
29.041
1.00
22.72
C


ATOM
1622
CG1
VAL
A
335
72.273
55.739
29.639
1.00
23.71
C


ATOM
1623
CG2
VAL
A
335
70.945
56.602
27.702
1.00
21.59
C


ATOM
1624
N
ILE
A
336
71.848
58.680
31.590
1.00
22.45
N


ATOM
1625
CA
ILE
A
336
72.489
58.930
32.876
1.00
22.52
C


ATOM
1626
C
ILE
A
336
71.465
59.051
34.004
1.00
23.41
C


ATOM
1627
O
ILE
A
336
71.662
58.518
35.095
1.00
22.49
O


ATOM
1628
CB
ILE
A
336
73.349
60.217
32.817
1.00
21.60
C


ATOM
1629
CG1
ILE
A
336
74.548
59.985
31.890
1.00
19.73
C


ATOM
1630
CG2
ILE
A
336
73.804
60.623
34.220
1.00
18.66
C


ATOM
1631
CD1
ILE
A
336
75.364
61.233
31.615
1.00
21.73
C


ATOM
1632
N
ASP
A
337
70.364
59.742
33.730
1.00
24.43
N


ATOM
1633
CA
ASP
A
337
69.319
59.938
34.729
1.00
24.42
C


ATOM
1634
C
ASP
A
337
68.550
58.646
35.026
1.00
24.54
C


ATOM
1635
O
ASP
A
337
68.294
58.317
36.186
1.00
23.43
O


ATOM
1636
CS
ASP
A
337
68.364
61.038
34.260
1.00
25.94
C


ATOM
1637
CG
ASP
A
337
67.298
61.359
35.285
1.00
28.42
C


ATOM
1638
OD1
ASP
A
337
67.631
61.405
36.483
1.00
31.45
O


ATOM
1639
OD2
ASP
A
337
66.131
61.578
34.897
1.00
29.42
O


ATOM
1640
N
VAL
A
338
68.187
57.912
33.980
1.00
24.02
N


ATOM
1641
CA
VAL
A
338
67.457
56.664
34.161
1.00
23.68
C


ATOM
1642
C
VAL
A
338
68.326
55.622
34.868
1.00
24.05
C


ATOM
1643
O
VAL
A
338
67.842
54.896
35.735
1.00
23.76
O


ATOM
1644
CB
VAL
A
338
66.956
56.110
32.800
1.00
24.17
C


ATOM
1645
CG1
VAL
A
338
66.387
54.704
32.973
1.00
22.42
C


ATOM
1646
CG2
VAL
A
338
65.882
57.046
32.228
1.00
21.26
C


ATOM
1647
N
VAL
A
339
69.607
55.562
34.505
1.00
23.11
N


ATOM
1648
CA
VAL
A
339
70.533
54.614
35.117
1.00
23.44
C


ATOM
1649
C
VAL
A
339
70.680
54.852
36.624
1.00
24.25
C


ATOM
1650
O
VAL
A
339
70.759
53.898
37.397
1.00
25.77
O


ATOM
1651
CB
VAL
A
339
71.930
54.683
34.444
1.00
23.37
C


ATOM
1652
CG1
VAL
A
339
72.970
53.969
35.290
1.00
21.96
C


ATOM
1653
CG2
VAL
A
339
71.866
54.039
33.067
1.00
21.79
C


ATOM
1654
N
ALA
A
340
70.719
56.114
37.043
1.00
23.85
N


ATOM
1655
CA
ALA
A
340
70.844
56.428
38.464
1.00
24.36
C


ATOM
1656
C
ALA
A
340
69.579
55.983
39.200
1.00
24.66
C


ATOM
1657
O
ALA
A
340
69.645
55.467
40.315
1.00
24.46
O


ATOM
1658
CB
ALA
A
340
71.068
57.923
38.661
1.00
22.34
C


ATOM
1659
N
GLU
A
341
68.426
56.179
38.571
1.00
24.16
N


ATOM
1660
CA
GLU
A
341
67.170
55.784
39.188
1.00
25.70
C


ATOM
1661
C
GLU
A
341
67.116
54.261
39.261
1.00
25.09
C


ATOM
1662
O
GLU
A
341
66.681
53.701
40.258
1.00
24.84
O


ATOM
1663
CB
GLU
A
341
65.980
56.309
38.375
1.00
26.08
C


ATOM
1664
CG
GLU
A
341
64.630
56.199
39.082
1.00
27.72
C


ATOM
1665
CD
GLU
A
341
64.541
57.095
40.311
1.00
31.11
C


ATOM
1666
OE2
GLU
A
341
65.068
58.227
40.269
1.00
32.05
O


ATOM
1667
OE2
GLU
A
341
63.929
56.680
41.315
1.00
31.72
O


ATOM
1668
N
ARG
A
342
67.558
53.601
38.195
1.00
25.02
N


ATOM
1669
CA
ARG
A
342
67.567
52.141
38.137
1.00
25.81
C


ATOM
1670
C
ARG
A
342
68.459
51.563
39.241
1.00
25.77
C


ATOM
1671
O
ARG
A
342
68.101
50.572
39.869
1.00
25.65
O


ATOM
1672
CB
ARG
A
342
68.045
51.676
36.752
1.00
24.80
C


ATOM
1673
CG
ARG
A
342
67.994
50.162
36.495
1.00
24.72
C


ATOM
1674
CD
ARG
A
342
69.246
49.441
37.015
1.00
23.36
C


ATOM
1675
NE
ARG
A
342
70.486
49.936
36.413
1.00
22.99
N


ATOM
1676
CZ
ARG
A
342
70.856
49.729
35.149
1.00
23.14
C


ATOM
1677
NH1
ARG
A
342
70.086
49.028
34.325
1.00
23.28
N


ATOM
1678
NH2
ARG
A
342
72.002
50.227
34.701
1.00
22.15
N


ATOM
1679
N
ASN
A
343
69.609
52.189
39.481
1.00
25.74
N


ATOM
1680
CA
ASN
A
343
70.524
51.722
40.519
1.00
26.49
C


ATOM
1681
C
ASN
A
343
69.928
51.972
41.899
1.00
28.14
C


ATOM
1682
O
ASN
A
343
70.119
51.191
42.826
1.00
28.20
O


ATOM
1683
CB
ASN
A
343
71.880
52.418
40.396
1.00
24.99
C


ATOM
1684
CO
ASN
A
343
72.642
51.980
39.163
1.00
26.53
C


ATOM
1685
OD1
ASN
A
343
72.333
50.943
38.572
1.00
25.64
O


ATOM
1686
ND2
ASN
A
343
73.650
52.756
38.774
1.00
24.62
N


ATOM
1687
N
LYS
A
344
69.198
53.071
42.026
1.00
29.38
N


ATOM
1688
CA
LYS
A
344
68.545
53.410
43.276
1.00
30.78
C


ATOM
1689
C
LYS
A
344
67.447
52.373
43.508
1.00
30.83
C


ATOM
1690
O
LYS
A
344
67.280
51.861
44.612
1.00
31.06
O


ATOM
1691
CB
LYS
A
344
67.947
54.810
43.172
1.00
33.74
C


ATOM
1692
CG
LYS
A
344
67.298
55.335
44.437
1.00
38.78
C


ATOM
1693
CD
LYS
A
344
66.906
56.799
44.255
1.00
41.30
C


ATOM
1694
CE
LYS
A
344
66.250
57.364
45.501
1.00
43.10
C


ATOM
1695
NZ
LYS
A
344
65.928
58.810
45.325
1.00
46.21
N


ATOM
1696
N
TYR
A
345
66.715
52.054
42.448
1.00
29.99
N


ATOM
1697
CA
TYR
A
345
65.640
51.076
42.516
1.00
30.40
C


ATOM
1698
C
TYR
A
345
66.174
49.696
42.921
1.00
31.13
C


ATOM
1699
O
TYR
A
345
65.538
48.977
43.693
1.00
31.45
O


ATOM
1700
CB
TYR
A
345
64.950
50.968
41.162
1.00
29.11
C


ATOM
1701
CG
TYR
A
345
63.630
50.231
41.196
1.00
29.15
C


ATOM
1702
CD1
TYR
A
345
62.465
50.880
41.597
1.00
29.67
C


ATOM
1703
CD2
TYR
A
345
63.539
48.896
40.802
1.00
28.37
C


ATOM
1704
CE1
TYR
A
345
61.243
50.226
41.597
1.00
29.42
C


ATOM
1705
CE2
TYR
A
345
62.318
48.230
40.800
1.00
29.73
C


ATOM
1706
CZ
TYR
A
345
61.175
48.905
41.196
1.00
30.08
C


ATOM
1707
OH
TYR
A
345
59.954
48.279
41.163
1.00
31.23
O


ATOM
1708
N
PHE
A
346
67.334
49.328
42.387
1.00
31.61
N


ATOM
1709
CA
PHE
A
346
67.949
48.040
42.705
1.00
32.63
C


ATOM
1710
C
PHE
A
346
68.288
47.958
44.194
1.00
33.80
C


ATOM
1711
O
PHE
A
346
68.060
46.932
44.837
1.00
33.23
O


ATOM
1712
CB
PHE
A
346
69.223
47.836
41.877
1.00
32.13
C


ATOM
1713
CG
PHE
A
346
69.961
46.567
42.204
1.00
33.47
C


ATOM
1714
CD1
PHE
A
346
69.380
45.326
41.969
1.00
33.38
C


ATOM
1715
CD2
PHE
A
346
71.235
46.613
42.763
1.00
35.61
C


ATOM
1716
CE1
PHE
A
346
70.050
44.151
42.284
1.00
33.75
C


ATOM
1717
CE2
PHE
A
346
71.917
45.440
43.084
1.00
36.22
C


ATOM
1718
CZ
PHE
A
346
71.320
44.206
42.842
1.00
35.99
C


ATOM
1719
N
GLU
A
347
68.826
49.045
44.737
1.00
34.63
N


ATOM
1720
CA
GLU
A
347
69.187
49.090
46.148
1.00
37.31
C


ATOM
1721
C
GLU
A
347
67.980
48.990
47.074
1.00
37.23
C


ATOM
1722
O
GLU
A
347
68.068
48.393
48.144
1.00
38.77
O


ATOM
1723
CB
GLU
A
347
69.953
50.377
46.468
1.00
37.91
C


ATOM
1724
CG
GLU
A
347
71.349
50.441
45.877
1.00
43.97
C


ATOM
1725
CD
GLU
A
347
72.215
49.262
46.296
1.00
47.61
C


ATOM
1726
OE1
GLU
A
347
72.231
48.923
47.501
1.00
50.24
O


ATOM
1727
OE2
GLU
A
347
72.889
48.675
45.420
1.00
50.39
O


ATOM
1728
N
GLU
A
348
66.858
49.571
46.664
1.00
36.75
N


ATOM
1729
CA
GLU
A
348
65.652
49.556
47.482
1.00
36.89
C


ATOM
1730
C
GLU
A
348
64.901
48.230
47.444
1.00
36.67
C


ATOM
1731
O
GLU
A
348
64.376
47.780
48.460
1.00
37.48
O


ATOM
1732
CB
GLU
A
348
64.672
50.643
47.022
1.00
37.65
C


ATOM
1733
CG
GLU
A
348
65.295
51.969
46.635
1.00
40.22
C


ATOM
1734
CD
GLU
A
348
64.265
52.960
46.108
1.00
40.32
C


ATOM
1735
OE1
GLU
A
348
63.309
52.526
45.434
1.00
41.11
O


ATOM
1736
OE2
GLU
A
348
64.417
54.174
46.356
1.00
41.33
O


ATOM
1737
N
THR
A
349
64.856
47.610
46.268
1.00
35.60
N


ATOM
1738
CA
THR
A
349
64.096
46.382
46.075
1.00
33.65
C


ATOM
1739
C
THR
A
349
64.859
45.094
45.759
1.00
33.57
C


ATOM
1740
O
THR
A
349
64.282
44.006
45.807
1.00
33.25
O


ATOM
1741
CB
THR
A
349
63.071
46.588
44.950
1.00
33.39
C


ATOM
1742
OG1
THR
A
349
63.763
46.710
43.700
1.00
32.24
O


ATOM
1743
CG2
THR
A
349
62.265
47.863
45.187
1.00
33.01
C


ATOM
1744
N
GLY
A
350
66.138
45.205
45.425
1.00
32.80
N


ATOM
1745
CA
GLY
A
350
66.903
44.018
45.085
1.00
31.46
C


ATOM
1746
C
GLY
A
350
66.608
43.556
43.666
1.00
29.99
C


ATOM
1747
O
GLY
A
350
67.073
42.503
43.232
1.00
30.31
O


ATOM
1748
N
ILE
A
351
65.832
44.346
42.933
1.00
28.63
N


ATOM
1749
CA
ILE
A
351
65.482
44.001
41.557
1.00
27.69
C


ATOM
1750
C
ILE
A
351
66.327
44.807
40.575
1.00
27.05
C


ATOM
1751
O
ILE
A
351
66.315
46.036
40.612
1.00
24.50
O


ATOM
1752
CB
ILE
A
351
64.004
44.315
41.253
1.00
29.37
C


ATOM
1753
CG1
ILE
A
351
63.092
43.640
42.281
1.00
31.00
C


ATOM
1754
CG2
ILE
A
351
63.662
43.862
39.841
1.00
28.85
C


ATOM
1755
CD1
ILE
A
351
61.625
44.051
42.154
1.00
32.57
C


ATOM
1756
N
TYR
A
352
67.060
44.121
39.702
1.00
26.80
N


ATOM
1757
CA
TYR
A
352
67.879
44.811
38.715
1.00
26.62
C


ATOM
1758
C
TYR
A
352
67.142
44.808
37.385
1.00
26.67
C


ATOM
1759
O
TYR
A
352
66.899
43.751
36.804
1.00
26.28
O


ATOM
1760
CB
TYR
A
352
69.240
44.130
38.527
1.00
25.22
C


ATOM
1761
CG
TYR
A
352
70.153
44.886
37.578
1.00
24.08
C


ATOM
1762
CD1
TYR
A
352
70.961
45.931
38.035
1.00
22.64
C


ATOM
1763
CD2
TYR
A
352
70.185
44.580
36.218
1.00
23.85
C


ATOM
1764
CE1
TYR
A
352
71.780
46.647
37.161
1.00
21.59
C


ATOM
1765
CE2
TYR
A
352
70.998
45.294
35.334
1.00
22.91
C


ATOM
1766
CZ
TYR
A
352
71.793
46.321
35.814
1.00
21.43
C


ATOM
1767
OH
TYR
A
352
72.621
47.001
34.951
1.00
22.44
O


ATOM
1768
N
ILE
A
353
66.782
45.992
36.906
1.00
26.51
N


ATOM
1769
CA
ILE
A
353
66.085
46.094
35.635
1.00
26.58
C


ATOM
1770
C
ILE
A
353
67.019
46.605
34.542
1.00
26.72
C


ATOM
1771
O
ILE
A
353
67.517
47.730
34.612
1.00
26.19
O


ATOM
1772
CB
ILE
A
353
64.882
47.042
35.735
1.00
27.79
C


ATOM
1773
CG1
ILE
A
353
63.948
46.566
36.855
1.00
28.55
C


ATOM
1774
CG2
ILE
A
353
64.147
47.086
34.399
1.00
27.23
C


ATOM
1775
CD1
ILE
A
353
62.751
47.446
37.089
1.00
27.39
C


ATOM
1776
N
PRO
A
354
67.290
45.770
33.526
1.00
25.87
N


ATOM
1777
CA
PRO
A
354
68.174
46.189
32.435
1.00
24.49
C


ATOM
1778
C
PRO
A
354
67.530
47.347
31.680
1.00
24.47
C


ATOM
1779
O
PRO
A
354
66.312
47.368
31.503
1.00
24.18
O


ATOM
1780
CB
PRO
A
354
68.273
44.935
31.568
1.00
23.91
C


ATOM
1781
CG
PRO
A
354
68.077
43.813
32.561
1.00
24.60
C


ATOM
1782
CD
PRO
A
354
66.947
44.341
33.409
1.00
25.26
C


ATOM
1783
N
VAL
A
355
68.333
48.317
31.250
1.00
23.40
N


ATOM
1784
CA
VAL
A
355
67.783
49.433
30.495
1.00
22.64
C


ATOM
1785
C
VAL
A
355
68.418
49.464
29.119
1.00
22.19
C


ATOM
1786
O
VAL
A
355
69.576
49.090
28.944
1.00
21.72
O


ATOM
1787
CB
VAL
A
355
67.989
50.805
31.211
1.00
23.23
C


ATOM
1788
CG1
VAL
A
355
67.314
50.773
32.582
1.00
20.89
C


ATOM
1789
CG2
VAL
A
355
69.478
51.144
31.325
1.00
20.18
C


ATOM
1790
N
CYS
A
356
67.640
49.905
28.141
1.00
21.94
N


ATOM
1791
CA
CYS
A
356
68.100
49.965
26.769
1.00
22.63
C


ATOM
1792
C
CYS
A
356
68.172
51.393
26.251
1.00
23.07
C


ATOM
1793
O
CYS
A
356
67.192
52.131
26.330
1.00
24.45
O


ATOM
1794
CB
CYS
A
356
67.148
49.152
25.887
1.00
22.81
C


ATOM
1795
SG
CYS
A
356
67.367
49.360
24.113
1.00
23.52
5


ATOM
1796
N
SER
A
357
69.332
51.784
25.732
1.00
23.41
N


ATOM
1797
CA
SER
A
357
69.480
53.118
25.158
1.00
23.70
C


ATOM
1798
C
SER
A
357
69.024
52.967
23.712
1.00
23.48
C


ATOM
1799
O
SER
A
357
69.703
52.339
22.902
1.00
23.03
O


ATOM
1800
CB
SER
A
357
70.933
53.587
25.186
1.00
23.53
C


ATOM
1801
OG
SER
A
357
71.039
54.865
24.579
1.00
23.13
O


ATOM
1802
N
ASP
A
358
67.871
53.550
23.406
1.00
23.76
N


ATOM
1803
CA
ASP
A
358
67.269
53.465
22.080
1.00
24.67
C


ATOM
1804
C
ASP
A
358
67.363
54.754
21.268
1.00
25.27
C


ATOM
1805
O
ASP
A
358
66.749
55.762
21.608
1.00
24.49
O


ATOM
1806
CB
ASP
A
358
65.799
53.040
22.238
1.00
24.63
C


ATOM
1807
CG
ASP
A
358
65.060
52.947
20.922
1.00
24.23
C


ATOM
1808
OD1
ASP
A
358
65.706
52.780
19.869
1.00
24.31
O


ATOM
1809
OD2
ASP
A
358
63.818
53.024
20.952
1.00
23.07
O


ATOM
1810
N
GLY
A
359
68.144
54.711
20.192
1.00
26.85
N


ATOM
1811
CA
GLY
A
359
68.284
55.870
19.332
1.00
28.13
C


ATOM
1812
C
GLY
A
359
69.370
56.852
19.717
1.00
30.06
C


ATOM
1813
O
GLY
A
359
69.890
56.829
20.832
1.00
30.69
O


ATOM
1814
N
GLY
A
360
69.722
57.717
18.775
1.00
32.24
N


ATOM
1815
CA
GLY
A
360
70.740
58.714
19.037
1.00
34.39
C


ATOM
1816
C
GLY
A
360
72.159
58.243
18.804
1.00
34.76
C


ATOM
1817
O
GLY
A
360
73.099
58.981
19.085
1.00
37.37
O


ATOM
1818
N
ILE
A
361
72.328
57.019
18.315
1.00
36.00
N


ATOM
1819
CA
ILE
A
361
73.664
56.496
18.046
1.00
37.27
C


ATOM
1820
C
ILE
A
361
74.052
56.893
16.627
1.00
39.44
C


ATOM
1821
O
ILE
A
361
73.479
56.392
15.657
1.00
39.25
O


ATOM
1822
CB
ILE
A
361
73.715
54.949
18.144
1.00
36.74
C


ATOM
1823
CG1
ILE
A
361
73.421
54.490
19.580
1.00
36.41
C


ATOM
1824
CG2
ILE
A
361
75.081
54.442
17.679
1.00
35.82
C


ATOM
1825
CD1
ILE
A
361
74.512
54.788
20.589
1.00
33.92
C


ATOM
1826
N
VAL
A
362
75.024
57.793
16.508
1.00
41.13
N


ATOM
1827
CA
VAL
A
362
75.479
58.248
15.201
1.00
42.28
C


ATOM
1828
C
VAL
A
362
76.807
57.608
14.801
1.00
42.57
C


ATOM
1829
O
VAL
A
362
76.993
57.249
13.640
1.00
44.09
O


ATOM
1830
CB
VAL
A
362
75.630
59.781
15.167
1.00
43.37
C


ATOM
1831
CG1
VAL
A
362
76.025
60.236
13.762
1.00
44.64
C


ATOM
1832
CG2
VAL
A
362
74.324
60.438
15.592
1.00
43.73
C


ATOM
1833
N
TYR
A
363
77.722
57.459
15.760
1.00
41.34
N


ATOM
1834
CA
TYR
A
363
79.032
56.857
15.495
1.00
39.51
C


ATOM
1835
C
TYR
A
363
79.287
55.654
16.396
1.00
37.48
C


ATOM
1836
O
TYR
A
363
78.654
55.512
17.440
1.00
37.25
O


ATOM
1837
CB
TYR
A
363
80.236
57.887
15.728
1.00
42.87
C


ATOM
1838
CG
TYR
A
363
79.974
59.140
14.896
1.00
45.48
C


ATOM
1839
CD1
TYR
A
363
80.011
59.093
13.504
1.00
47.49
C


ATOM
1840
CD2
TYR
A
363
79.779
60.374
15.509
1.00
46.57
C


ATOM
1841
CE1
TYR
A
363
79.858
60.246
12.742
1.00
49.35
C


ATOM
1842
CE2
TYR
A
363
79.625
61.531
14.759
1.00
48.79
C


ATOM
1843
CZ
TYR
A
363
79.666
61.461
13.377
2.00
49.83
C


ATOM
1844
OH
TYR
A
363
79.519
62.610
12.629
1.00
52.64
O


ATOM
1845
N
ASP
A
364
80.223
54.793
16.007
1.00
35.17
N


ATOM
1846
CA
ASP
A
364
80.523
53.619
16.821
1.00
34.10
C


ATOM
1847
C
ASP
A
364
80.846
53.973
18.271
1.00
32.20
C


ATOM
1848
O
ASP
A
364
80.387
53.298
19.191
1.00
33.00
O


ATOM
1849
CB
ASP
A
364
81.696
52.815
16.240
1.00
36.21
C


ATOM
1850
CG
ASP
A
364
81.321
52.031
14.991
1.00
36.90
C


ATOM
1851
OD1
ASP
A
364
80.170
51.566
14.885
1.00
36.58
O


ATOM
1852
OD2
ASP
A
364
82.194
51.860
14.118
1.00
38.57
O


ATOM
1853
N
TYR
A
365
81.621
55.033
18.485
1.00
30.02
N


ATOM
1854
CA
TYR
A
365
81.994
55.401
19.848
1.00
28.95
C


ATOM
1855
C
TYR
A
365
80.802
55.809
20.709
1.00
27.94
C


ATOM
1856
O
TYR
A
365
80.899
55.825
21.931
1.00
26.36
O


ATOM
1857
CB
TYR
A
365
83.081
56.489
19.843
1.00
28.15
C


ATOM
1858
CG
TYR
A
365
82.607
57.921
19.696
1.00
29.09
C


ATOM
1859
CD1
TYR
A
365
82.405
58.729
20.816
1.00
28.03
C


ATOM
1860
CD2
TYR
A
365
82.421
58.487
18.437
1.00
29.60
C


ATOM
1861
CE1
TYR
A
365
82.039
60.073
20.681
1.00
29.32
C


ATOM
1862
CE2
TYR
A
365
82.055
59.830
18.291
1.00
30.03
C


ATOM
1863
CZ
TYR
A
365
81.868
60.613
19.414
1.00
30.20
C


ATOM
1864
OH
TYR
A
365
81.519
61.936
19.259
1.00
32.66
O


ATOM
1865
N
HIS
A
366
79.674
56.126
20.074
1.00
28.10
N


ATOM
1866
CA
HIS
A
366
78.478
56.477
20.829
1.00
27.17
C


ATOM
1867
C
HIS
A
366
77.995
55.216
21.548
1.00
25.93
C


ATOM
1868
O
HIS
A
366
77.380
55.301
22.609
1.00
24.73
O


ATOM
1869
CB
HIS
A
366
77.371
57.003
19.909
1.00
28.22
C


ATOM
1870
CG
HIS
A
366
77.616
58.387
19.394
1.00
29.65
C


ATOM
1871
ND1
HIS
A
366
78.642
59.184
19.856
1.00
31.11
N


ATOM
1872
CD2
HIS
A
366
76.947
59.129
18.481
1.00
30.20
C


ATOM
1873
CE1
HIS
A
366
78.593
60.357
19.252
1.00
29.57
C


ATOM
1874
NE2
HIS
A
366
77.574
60.350
18.412
1.00
31.07
N


ATOM
1875
N
MET
A
367
78.275
54.051
20.960
1.00
24.23
N


ATOM
1876
CA
MET
A
367
77.892
52.773
21.569
1.00
24.28
C


ATOM
1877
C
MET
A
367
78.634
52.627
22.892
1.00
22.96
C


ATOM
1878
O
MET
A
367
78.036
52.342
23.924
1.00
23.44
O


ATOM
1879
CB
MET
A
367
78.273
51.595
20.666
1.00
24.50
C


ATOM
1880
CG
MET
A
367
77.537
51.530
19.332
1.00
26.42
C


ATOM
1881
SD
MET
A
367
78.087
50.102
18.355
1.00
29.45
5


ATOM
1882
CE
MET
A
367
77.053
50.267
16.894
1.00
28.05
C


ATOM
1883
N
THR
A
368
79.947
52.827
22.853
1.00
23.22
N


ATOM
1884
CA
THR
A
368
80.764
52.719
24.058
1.00
23.72
C


ATOM
1885
C
THR
A
368
80.266
53.711
25.110
1.00
22.92
C


ATOM
1886
O
THR
A
368
80.180
53.379
26.290
1.00
23.78
O


ATOM
1887
CB
THR
A
368
82.249
53.005
23.748
1.00
24.12
C


ATOM
1888
OG1
THR
A
368
82.625
52.305
22.554
1.00
24.48
O


ATOM
1889
CG2
THR
A
368
83.138
52.537
24.902
1.00
23.20
C


ATOM
1890
N
LEU
A
369
79.939
54.929
24.680
1.00
22.01
N


ATOM
1891
CA
LEU
A
369
79.435
55.947
25.602
1.00
22.78
C


ATOM
1892
C
LEU
A
369
78.125
55.525
26.253
1.00
22.41
C


ATOM
1893
O
LEU
A
369
77.958
55.659
27.464
1.00
23.15
O


ATOM
1894
CB
LEU
A
369
79.217
57.280
24.882
1.00
21.96
C


ATOM
1895
CG
LEU
A
369
80.456
58.127
24.604
1.00
23.46
C


ATOM
1896
CD1
LEU
A
369
80.050
59.369
23.807
1.00
22.62
C


ATOM
1897
CD2
LEU
A
369
81.114
58.520
25.929
1.00
21.25
C


ATOM
1898
N
ALA
A
370
77.197
55.016
25.445
1.00
21.89
N


ATOM
1899
CA
ALA
A
370
75.898
54.592
25.956
1.00
22.53
C


ATOM
1900
C
ALA
A
370
76.069
53.503
27.013
1.00
21.32
C


ATOM
1901
O
ALA
A
370
75.411
53.524
28.047
1.00
22.46
O


ATOM
1902
CB
ALA
A
370
75.018
54.087
24.805
1.00
20.75
C


ATOM
1903
N
LEU
A
371
76.959
52.555
26.751
1.00
21.38
N


ATOM
1904
CA
LEU
A
371
77.205
51.470
27.693
1.00
21.60
C


ATOM
1905
C
LEU
A
371
77.899
52.010
28.950
1.00
22.18
C


ATOM
1906
O
LEU
A
371
77.494
51.700
30.063
1.00
22.86
O


ATOM
1907
CB
LEU
A
371
78.062
50.384
27.029
1.00
20.20
C


ATOM
1908
CG
LEU
A
371
77.444
49.692
25.806
1.00
21.57
C


ATOM
1909
CD1
LEU
A
371
78.482
48.784
25.147
1.00
23.83
C


ATOM
1910
CD2
LEU
A
371
76.220
48.884
26.228
1.00
21.62
C


ATOM
1911
N
ALA
A
372
78.932
52.835
28.763
1.00
22.30
N


ATOM
1912
CA
ALA
A
372
79.675
53.407
29.883
1.00
22.28
C


ATOM
1913
C
ALA
A
372
78.768
54.196
30.814
1.00
23.49
C


ATOM
1914
O
ALA
A
372
78.979
54.225
32.027
1.00
22.49
O


ATOM
1915
CB
ALA
A
372
80.794
54.305
29.369
1.00
21.55
C


ATOM
1916
N
MET
A
373
77.763
54.848
30.242
1.00
23.46
N


ATOM
1917
CA
MET
A
373
76.837
55.631
31.043
1.00
23.37
C


ATOM
1918
C
MET
A
373
75.850
54.762
31.830
1.00
22.64
C


ATOM
1919
O
MET
A
373
75.111
55.269
32.662
1.00
22.93
O


ATOM
1920
CB
MET
A
373
76.100
56.639
30.150
1.00
23.08
C


ATOM
1921
CG
MET
A
373
77.007
57.763
29.640
1.00
23.17
C


ATOM
1922
SD
MET
A
373
76.206
58.901
28.474
1.00
23.90
S


ATOM
1923
CE
MET
A
373
77.545
60.031
28.102
1.00
22.19
C


ATOM
1924
N
GLY
A
374
75.842
53.457
31.577
1.00
23.01
N


ATOM
1925
CA
GLY
A
374
74.952
52.579
32.322
1.00
22.40
C


ATOM
1926
C
GLY
A
374
73.945
51.751
31.540
1.00
23.47
C


ATOM
1927
O
GLY
A
374
73.316
50.853
32.106
1.00
24.05
O


ATOM
1928
N
ALA
A
375
73.764
52.041
30.257
1.00
22.06
N


ATOM
1929
CA
ALA
A
375
72.826
51.264
29.460
1.00
23.47
C


ATOM
1930
C
ALA
A
375
73.365
49.840
29.331
1.00
23.69
C


ATOM
1931
O
ALA
A
375
74.549
49.641
29.065
1.00
25.05
O


ATOM
1932
CB
ALA
A
375
72.655
51.887
28.082
1.00
20.67
C


ATOM
1933
N
ASP
A
376
72.497
48.854
29.528
1.00
24.20
N


ATOM
1934
CA
ASP
A
376
72.895
47.453
29.431
1.00
24.16
C


ATOM
1935
C
ASP
A
376
73.021
47.053
27.968
1.00
23.81
C


ATOM
1936
O
ASP
A
376
73.937
46.324
27.596
1.00
23.82
O


ATOM
1937
CB
ASP
A
376
71.878
46.579
30.159
1.00
24.02
C


ATOM
1938
CG
ASP
A
376
71.763
46.939
31.632
1.00
24.67
C


ATOM
1939
OD1
ASP
A
376
72.561
46.418
32.444
1.00
24.99
O


ATOM
1940
OD2
ASP
A
376
70.889
47.764
31.977
1.00
24.71
O


ATOM
1941
N
PHE
A
377
72.094
47.521
27.139
1.00
23.81
N


ATOM
1942
CA
PHE
A
377
72.164
47.245
25.712
1.00
23.63
C


ATOM
1943
C
PHE
A
377
71.667
48.440
24.905
1.00
23.27
C


ATOM
1944
O
PHE
A
377
71.132
49.398
25.462
1.00
22.71
O


ATOM
1945
CB
PHE
A
377
71.427
45.942
25.320
1.00
22.50
C


ATOM
1946
CG
PHE
A
377
70.013
45.838
25.817
1.00
23.64
C


ATOM
1947
CD1
PHE
A
377
69.748
45.464
27.132
1.00
25.15
C


ATOM
1948
CD2
PHE
A
377
68.941
46.055
24.953
1.00
22.89
C


ATOM
1949
CE1
PHE
A
377
68.428
45.300
27.579
1.00
25.01
C


ATOM
1950
CE2
PHE
A
377
67.626
45.895
25.387
1.00
23.60
C


ATOM
1951
CZ
PHE
A
377
67.369
45.516
26.702
1.00
24.96
C


ATOM
1952
N
ILE
A
378
71.857
48.376
23.592
1.00
22.99
N


ATOM
1953
CA
ILE
A
378
71.512
49.470
22.698
1.00
23.32
C


ATOM
1954
C
ILE
A
378
70.573
49.043
21.573
1.00
24.13
C


ATOM
1955
O
ILE
A
378
70.760
47.983
20.978
1.00
24.04
O


ATOM
1956
CB
ILE
A
378
72.815
50.030
22.061
1.00
24.07
C


ATOM
1957
CG1
ILE
A
378
73.807
50.406
23.163
1.00
25.55
C


ATOM
1958
CG2
ILE
A
378
72.521
51.232
21.176
1.00
23.97
C


ATOM
1959
CD1
ILE
A
378
75.242
50.486
22.665
1.00
25.45
C


ATOM
1960
N
MET
A
379
69.565
49.866
21.285
1.00
23.06
N


ATOM
1961
CA
MET
A
379
68.643
49.566
20.195
1.00
23.94
C


ATOM
1962
C
MET
A
379
68.968
50.516
19.045
1.00
24.07
C


ATOM
1963
O
MET
A
379
69.061
51.725
19.237
1.00
23.67
O


ATOM
1964
CB
MET
A
379
67.179
49.746
20.621
1.00
23.89
C


ATOM
1965
CG
MET
A
379
66.206
49.546
19.461
1.00
23.47
C


ATOM
1966
SD
MET
A
379
64.466
49.424
19.913
1.00
23.78
S


ATOM
1967
CE
MET
A
379
64.375
47.682
20.458
1.00
23.21
C


ATOM
1968
N
LEU
A
380
69.136
49.961
17.851
1.00
24.45
N


ATOM
1969
CA
LEU
A
380
69.476
50.758
16.682
1.00
25.64
C


ATOM
1970
C
LEU
A
380
68.561
50.484
15.502
1.00
25.46
C


ATOM
1971
O
LEU
A
380
68.162
49.346
15.265
1.00
24.86
O


ATOM
1972
CB
LEU
A
380
70.922
50.477
16.259
1.00
26.84
C


ATOM
1973
CG
LEU
A
380
72.033
50.818
17.255
1.00
28.40
C


ATOM
1974
CD1
LEU
A
380
73.394
50.462
16.689
1.00
28.92
C


ATOM
1975
CD2
LEU
A
380
71.977
52.299
17.546
1.00
31.59
C


ATOM
1976
N
GLY
A
381
68.238
51.539
14.764
1.00
26.35
N


ATOM
1977
CA
GLY
A
381
67.398
51.397
13.587
1.00
27.38
C


ATOM
1978
C
GLY
A
381
68.230
51.618
12.335
1.00
27.51
C


ATOM
1979
O
GLY
A
381
68.535
50.679
11.604
1.00
27.02
O


ATOM
1980
N
ARG
A
382
68.611
52.870
12.108
1.00
29.52
N


ATOM
1981
CA
ARG
A
382
69.412
53.264
10.947
1.00
32.19
C


ATOM
1982
C
ARG
A
382
70.626
52.353
10.722
1.00
30.92
C


ATOM
1983
O
ARG
A
382
70.878
51.899
9.608
1.00
30.21
O


ATOM
1984
CB
ARG
A
382
69.895
54.707
11.125
1.00
35.86
C


ATOM
1985
CO
ARG
A
382
69.994
55.497
9.834
1.00
42.94
C


ATOM
1986
CD
ARG
A
382
70.799
56.793
9.990
1.00
48.04
C


ATOM
1987
NE
ARG
A
382
72.237
56.531
10.060
1.00
52.92
N


ATOM
1988
CZ
ARG
A
382
72.883
56.136
11.156
1.00
55.81
C


ATOM
1989
NH1
ARG
A
382
72.228
55.961
12.296
1.00
57.30
N


ATOM
1990
NH2
ARG
A
382
74.187
55.896
11.106
1.00
56.34
N


ATOM
1991
N
TYR
A
383
71.376
52.105
11.791
1.00
29.98
N


ATOM
1992
CA
TYR
A
383
72.569
51.261
11.748
1.00
28.39
C


ATOM
1993
C
TYR
A
383
72.324
49.926
11.034
1.00
28.21
C


ATOM
1994
O
TYR
A
383
73.084
49.543
10.143
1.00
27.77
O


ATOM
1995
CB
TYR
A
383
73.059
51.000
13.179
1.00
26.48
C


ATOM
1996
CG
TYR
A
383
74.301
50.137
13.276
1.00
25.37
C


ATOM
1997
CD1
TYR
A
383
75.578
50.703
13.240
1.00
24.67
C


ATOM
1998
CD2
TYR
A
383
74.196
48.752
13.397
1.00
24.26
C


ATOM
1999
CE1
TYR
A
383
76.716
49.910
13.322
1.00
24.73
C


ATOM
2000
CE2
TYR
A
383
75.320
47.951
13.479
1.00
23.84
C


ATOM
2001
CZ
TYR
A
383
76.578
48.530
13.440
1.00
25.89
C


ATOM
2002
OH
TYR
A
383
77.689
47.722
13.511
1.00
25.39
O


ATOM
2003
N
PHE
A
384
71.263
49.228
11.428
1.00
27.07
N


ATOM
2004
CA
PHE
A
384
70.922
47.931
10.843
1.00
28.18
C


ATOM
2005
C
PHE
A
384
70.200
48.007
9.493
1.00
28.50
C


ATOM
2006
O
PHE
A
384
70.278
47.076
8.696
1.00
29.39
O


ATOM
2007
CB
PHE
A
384
70.068
47.122
11.827
1.00
25.94
C


ATOM
2008
CG
PHE
A
384
70.832
46.611
13.025
1.00
26.50
C


ATOM
2009
CG
PHE
A
384
71.790
45.610
12.882
1.00
25.77
C


ATOM
2010
CD2
PHE
A
384
70.595
47.133
14.295
1.00
25.04
C


ATOM
2011
CE1
PHE
A
384
72.502
45.135
13.983
1.00
25.85
C


ATOM
2012
CE2
PHE
A
384
71.300
46.666
15.402
1.00
26.26
C


ATOM
2013
CZ
PHE
A
384
72.258
45.663
15.246
1.00
25.10
C


ATOM
2014
N
ALA
A
385
69.493
49.105
9.244
1.00
29.51
N


ATOM
2015
CA
ALA
A
385
68.758
49.281
7.996
1.00
29.99
C


ATOM
2016
C
ALA
A
385
69.686
49.249
6.780
1.00
31.15
C


ATOM
2017
O
ALA
A
385
69.275
48.868
5.685
1.00
31.07
O


ATOM
2018
CB
ALA
A
385
67.993
50.600
8.033
1.00
29.53
C


ATOM
2019
N
ARG
A
386
70.939
49.647
6.989
1.00
32.12
N


ATOM
2020
CA
ARG
A
386
71.949
49.686
5.936
1.00
32.14
C


ATOM
2021
C
ARG
A
386
72.391
48.308
5.453
1.00
32.91
C


ATOM
2022
O
ARG
A
386
72.983
48.180
4.380
1.00
33.24
O


ATOM
2023
CB
ARG
A
386
73.204
50.405
6.434
1.00
32.61
C


ATOM
2024
CG
ARG
A
386
73.039
51.825
6.908
1.00
33.83
C


ATOM
2025
CD
ARG
A
386
74.356
52.269
7.538
1.00
36.13
C


ATOM
2026
NE
ARG
A
386
74.740
51.371
8.628
1.00
36.98
N


ATOM
2027
CZ
ARG
A
386
75.990
51.156
9.027
1.00
37.29
C


ATOM
2028
NH1
ARG
A
386
77.004
51.772
8.429
1.00
36.98
N


ATOM
2029
NH2
ARG
A
386
76.227
50.318
10.027
1.00
36.19
N


ATOM
2030
N
PHE
A
387
72.126
47.279
6.248
1.00
33.19
N


ATOM
2031
CA
PHE
A
387
72.565
45.941
5.890
1.00
33.56
C


ATOM
2032
C
PHE
A
387
71.710
45.194
4.872
1.00
35.13
C


ATOM
2033
O
PHE
A
387
70.511
45.448
4.711
1.00
34.37
O


ATOM
2034
CB
PHE
A
387
72.725
45.085
7.155
1.00
32.86
C


ATOM
2035
CG
PHE
A
387
73.621
45.701
8.200
1.00
32.36
C


ATOM
2036
CD1
PHE
A
387
74.756
46.417
7.832
1.00
31.61
C


ATOM
2037
CD2
PHE
A
387
73.331
45.563
9.553
1.00
31.75
C


ATOM
2038
CE1
PHE
A
387
75.586
46.991
8.797
1.00
32.70
C


ATOM
2039
CE2
PHE
A
387
74.156
46.132
10.529
1.00
31.49
C


ATOM
2040
CZ
PHE
A
387
75.284
46.848
10.151
1.00
30.49
C


ATOM
2041
N
GLU
A
388
72.364
44.265
4.186
1.00
35.81
N


ATOM
2042
CA
GLU
A
388
71.731
43.428
3.181
1.00
36.15
C


ATOM
2043
C
GLU
A
388
70.509
42.735
3.770
1.00
34.62
C


ATOM
2044
O
GLU
A
388
69.494
42.577
3.098
1.00
33.35
O


ATOM
2045
CB
GLU
A
388
72.730
42.374
2.689
1.00
38.38
C


ATOM
2046
CG
GLU
A
388
72.130
41.319
1.771
1.00
42.94
C


ATOM
2047
CD
GLU
A
388
71.780
41.870
0.404
1.00
45.98
C


ATOM
2048
OE1
GLU
A
388
70.997
41.216
−0.324
1.00
48.50
O


ATOM
2049
OE2
GLU
A
388
72.297
42.954
0.054
1.00
47.51
O


ATOM
2050
N
GLU
A
389
70.609
42.343
5.038
1.00
33.73
N


ATOM
2051
CA
GLU
A
389
69.526
41.639
5.706
1.00
33.32
C


ATOM
2052
C
GLU
A
389
68.295
42.448
6.115
1.00
33.33
C


ATOM
2053
O
GLU
A
389
67.313
41.864
6.563
1.00
33.97
O


ATOM
2054
CB
GLU
A
389
70.067
40.883
6.924
1.00
33.42
C


ATOM
2055
CG
GLU
A
389
71.099
39.827
6.575
1.00
33.24
C


ATOM
2056
CD
GLU
A
389
72.525
40.343
6.656
1.00
34.22
C


ATOM
2057
OE1
GLU
A
389
72.736
41.563
6.511
1.00
33.67
O


ATOM
2058
OE2
GLU
A
389
73.441
39.519
6.854
1.00
34.50
O


ATOM
2059
N
SER
A
390
68.328
43.772
5.986
1.00
33.75
N


ATOM
2060
CA
SER
A
390
67.145
44.558
6.341
1.00
35.12
C


ATOM
2061
C
SER
A
390
66.106
44.264
5.252
1.00
36.23
C


ATOM
2062
O
SER
A
390
66.462
44.028
4.097
1.00
35.59
O


ATOM
2063
CB
SER
A
390
67.456
46.055
6.397
1.00
33.40
C


ATOM
2064
OG
SER
A
390
67.716
46.575
5.112
1.00
35.26
O


ATOM
2065
N
PRO
A
391
64.811
44.290
5.608
1.00
37.69
N


ATOM
2066
CA
PRO
A
391
63.704
44.012
4.686
1.00
39.43
C


ATOM
2067
C
PRO
A
391
63.332
45.059
3.635
1.00
40.72
C


ATOM
2068
O
PRO
A
391
62.291
44.938
2.991
1.00
41.37
O


ATOM
2069
CB
PRO
A
391
62.548
43.729
5.639
1.00
39.02
C


ATOM
2070
CG
PRO
A
391
62.797
44.733
6.725
1.00
38.46
C


ATOM
2071
CD
PRO
A
391
64.300
44.637
6.949
1.00
36.88
C


ATOM
2072
N
THR
A
392
64.167
46.071
3.443
1.00
41.57
N


ATOM
2073
CA
THR
A
392
63.844
47.103
2.469
1.00
42.35
C


ATOM
2074
C
THR
A
392
64.520
46.929
1.114
1.00
44.91
C


ATOM
2075
O
THR
A
392
65.399
46.084
0.938
1.00
45.02
O


ATOM
2076
CB
THR
A
392
64.178
48.502
3.011
1.00
41.05
C


ATOM
2077
OG1
THR
A
392
65.579
48.587
3.293
1.00
39.97
O


ATOM
2078
CG2
THR
A
392
63.383
48.778
4.281
1.00
39.92
C


ATOM
2079
N
ARG
A
393
64.094
47.747
0.159
1.00
47.45
N


ATOM
2080
CA
ARG
A
393
64.623
47.703
1.195
1.00
50.03
C


ATOM
2081
C
ARG
A
393
65.990
48.355
1.317
1.00
50.45
C


ATOM
2082
O
ARG
A
393
66.243
49.419
−0.751
1.00
50.27
O


ATOM
2083
CB
ARG
A
393
63.640
48.380
−2.163
1.00
51.81
C


ATOM
2084
CG
ARG
A
393
62.377
47.565
−2.431
1.00
54.92
C


ATOM
2085
CD
ARG
A
393
61.284
48.366
−3.146
1.00
57.32
C


ATOM
2086
NE
ARG
A
393
61.775
49.068
−4.328
1.00
59.58
N


ATOM
2087
CZ
ARG
A
393
62.024
50.375
−4.370
1.00
61.26
C


ATOM
2088
NH1
ARG
A
393
61.823
51.125
−3.295
1.00
61.47
N


ATOM
2089
NH2
ARG
A
393
62.481
50.934
−5.484
1.00
62.64
N


ATOM
2090
N
LYS
A
394
66.872
47.690
−2.053
1.00
50.90
N


ATOM
2091
CA
LYS
A
394
68.213
48.191
−2.299
1.00
51.87
C


ATOM
2092
C
LYS
A
394
68.046
49.050
−3.545
1.00
53.29
C


ATOM
2093
O
LYS
A
394
67.637
48.551
−4.590
1.00
53.60
O


ATOM
2094
CB
LYS
A
394
69.158
47.023
−2.579
1.00
51.11
C


ATOM
2095
CG
LYS
A
394
70.618
47.333
−2.352
1.00
50.68
C


ATOM
2096
CD
LYS
A
394
71.508
46.184
−2.795
1.00
49.41
C


ATOM
2097
CE
LYS
A
394
71.231
44.910
−2.025
1.00
48.96
C


ATOM
2098
NZ
LYS
A
394
72.139
43.816
−2.476
1.00
47.88
N


ATOM
2099
N
VAL
A
395
68.343
50.340
−3.435
1.00
55.26
N


ATOM
2100
CA
VAL
A
395
68.183
51.253
−4.562
1.00
57.43
C


ATOM
2101
C
VAL
A
395
69.475
51.939
−4.979
1.00
58.81
C


ATOM
2102
O
VAL
A
395
70.207
52.463
−4.145
1.00
59.36
O


ATOM
2103
CB
VAL
A
395
67.141
52.344
−4.238
1.00
57.67
C


ATOM
2104
CG1
VAL
A
395
67.047
53.339
−5.388
1.00
58.68
C


ATOM
2105
CG2
VAL
A
395
65.789
51.703
−3.974
1.00
57.82
C


ATOM
2106
N
THR
A
396
69.740
51.946
−6.281
1.00
60.52
N


ATOM
2107
CA
THR
A
396
70.942
52.577
−6.813
1.00
62.17
C


ATOM
2108
C
THR
A
396
70.648
53.995
−7.284
1.00
63.08
C


ATOM
2109
O
THR
A
396
69.919
54.197
−8.255
1.00
63.34
O


ATOM
2110
CB
THR
A
396
71.514
51.781
−7.998
1.00
62.45
C


ATOM
2111
OG1
THR
A
396
71.837
50.454
−7.569
1.00
63.27
O


ATOM
2112
CG2
THR
A
396
72.772
52.452
−8.529
1.00
63.24
C


ATOM
2113
N
ILE
A
397
71.222
54.970
−6.586
1.00
64.02
N


ATOM
2114
CA
ILE
A
397
71.035
56.376
−6.918
1.00
65.04
C


ATOM
2115
C
ILE
A
397
72.365
56.980
−7.362
1.00
65.43
C


ATOM
2116
O
ILE
A
397
73.287
57.134
−6.559
1.00
65.88
O


ATOM
2117
CB
ILE
A
397
70.509
57.168
−5.701
1.00
65.43
C


ATOM
2118
CG1
ILE
A
397
69.229
56.516
−5.171
1.00
65.85
C


ATOM
2119
CG2
ILE
A
397
70.230
58.608
−6.099
1.00
65.50
C


ATOM
2120
CD1
ILE
A
397
68.688
57.167
−3.914
1.00
66.46
C


ATOM
2121
N
ASN
A
398
72.450
57.319
−8.644
1.00
65.44
N


ATOM
2122
CA
ASN
A
398
73.652
57.900
−9.238
1.00
65.13
C


ATOM
2123
C
ASN
A
398
74.959
57.251
−8.770
1.00
63.59
C


ATOM
2124
O
ASN
A
398
75.819
57.911
−8.186
1.00
63.13
O


ATOM
2125
CB
ASN
A
398
73.703
59.417
−8.988
1.00
67.26
C


ATOM
2126
CG
ASN
A
398
73.838
59.773
−7.515
1.00
69.20
C


ATOM
2127
OD1
ASN
A
398
72.906
59.598
−6.730
1.00
70.21
O


ATOM
2128
ND2
ASN
A
398
75.009
60.278
−7.135
1.00
69.87
N


ATOM
2129
N
GLY
A
399
75.097
55.954
−9.031
1.00
61.70
N


ATOM
2130
CA
GLY
A
399
76.306
55.242
−8.653
1.00
59.47
C


ATOM
2131
C
GLY
A
399
76.406
54.789
−7.207
1.00
57.89
C


ATOM
2132
O
GLY
A
399
77.324
54.047
−6.850
1.00
57.93
O


ATOM
2133
N
SER
A
400
75.477
55.232
−6.368
1.00
55.71
N


ATOM
2134
CA
SER
A
400
75.495
54.850
−4.960
1.00
52.89
C


ATOM
2135
C
SER
A
400
74.343
53.929
−4.604
1.00
50.55
C


ATOM
2136
O
SER
A
400
73.182
54.249
−4.841
1.00
50.80
O


ATOM
2137
CB
SER
A
400
75.445
56.090
−4.067
1.00
52.32
C


ATOM
2138
OG
SER
A
400
76.657
56.816
−4.147
1.00
53.54
O


ATOM
2139
N
VAL
A
401
74.672
52.778
−4.033
1.00
48.12
N


ATOM
2140
CA
VAL
A
401
73.655
51.824
−3.629
1.00
46.03
C


ATOM
2141
C
VAL
A
401
73.166
52.225
−2.237
1.00
45.54
C


ATOM
2142
O
VAL
A
401
73.959
52.368
−1.302
1.00
44.42
O


ATOM
2143
CB
VAL
A
401
74.224
50.397
−3.605
1.00
45.67
C


ATOM
2144
CG1
VAL
A
401
73.149
49.412
−3.178
1.00
44.59
C


ATOM
2145
CG2
VAL
A
401
74.768
50.041
−4.985
1.00
44.66
C


ATOM
2146
N
MET
A
402
71.856
52.418
−2.118
1.00
44.66
N


ATOM
2147
CA
MET
A
402
71.236
52.829
−0.863
1.00
43.40
C


ATOM
2148
C
MET
A
402
70.154
51.846
−0.434
1.00
42.35
C


ATOM
2149
O
MET
A
402
69.786
50.933
−1.175
1.00
41.19
O


ATOM
2150
CB
MET
A
402
70.580
54.208
−1.020
1.00
45.15
C


ATOM
2151
CG
MET
A
402
71.414
55.261
−1.728
1.00
45.44
C


ATOM
2152
SD
MET
A
402
72.814
55.813
−0.761
1.00
50.48
S


ATOM
2153
CE
MET
A
402
72.042
57.060
0.274
1.00
47.04
C


ATOM
2154
N
LYS
A
403
69.646
52.045
0.776
1.00
40.23
N


ATOM
2155
CA
LYS
A
403
68.575
51.217
1.297
1.00
38.93
C


ATOM
2156
C
LYS
A
403
67.506
52.157
1.827
1.00
38.85
C


ATOM
2157
O
LYS
A
403
67.805
53.246
2.325
1.00
37.82
O


ATOM
2158
CB
LYS
A
403
69.071
50.295
2.414
1.00
38.52
C


ATOM
2159
CG
LYS
A
403
70.049
49.234
1.944
1.00
38.14
C


ATOM
2160
CD
LYS
A
403
69.733
47.871
2.535
1.00
38.41
C


ATOM
2161
CE
LYS
A
403
68.425
47.321
1.989
1.00
38.28
C


ATOM
2162
NZ
LYS
A
403
68.123
45.957
2.514
1.00
36.94
N


ATOM
2163
N
GLU
A
404
66.255
51.746
1.697
1.00
39.27
N


ATOM
2164
CA
GLU
A
404
65.159
52.567
2.169
1.00
39.45
C


ATOM
2165
C
GLU
A
404
65.108
52.518
3.682
1.00
38.83
C


ATOM
2166
O
GLU
A
404
65.459
51.509
4.297
1.00
37.69
O


ATOM
2167
CB
GLU
A
404
63.840
52.060
1.609
1.00
41.56
C


ATOM
2168
CG
GLU
A
404
63.763
52.059
0.103
1.00
45.30
C


ATOM
2169
CD
GLU
A
404
62.435
51.539
−0.384
1.00
46.12
C


ATOM
2170
OE1
GLU
A
404
62.155
50.338
−0.167
1.00
47.85
O


ATOM
2171
OE2
GLU
A
404
61.673
52.334
−0.971
1.00
47.62
O


ATOM
2172
N
TYR
A
405
64.665
53.616
4.275
1.00
38.06
N


ATOM
2173
CA
TYR
A
405
64.550
53.700
5.717
1.00
37.61
C


ATOM
2174
C
TYR
A
405
63.512
54.746
6.066
1.00
36.92
C


ATOM
2175
O
TYR
A
405
63.619
55.899
5.658
1.00
37.99
O


ATOM
2176
CB
TYR
A
405
65.892
54.078
6.335
1.00
37.41
C


ATOM
2177
CG
TYR
A
405
65.857
54.147
7.842
1.00
37.40
C


ATOM
2178
CD1
TYR
A
405
65.593
53.013
8.603
1.00
36.23
C


ATOM
2179
CD2
TYR
A
405
66.084
55.349
8.507
1.00
38.07
C


ATOM
2180
CE1
TYR
A
405
65.557
53.072
9.990
1.00
36.68
C


ATOM
2181
CE2
TYR
A
405
66.049
55.417
9.892
1.00
38.81
C


ATOM
2182
CZ
TYR
A
405
65.784
54.274
10.627
1.00
36.81
C


ATOM
2183
OH
TYR
A
405
65.736
54.345
11.999
1.00
37.95
O


ATOM
2184
N
TRP
A
406
62.498
54.336
6.813
1.00
35.74
N


ATOM
2185
CA
TRP
A
406
61.450
55.256
7.214
1.00
34.25
C


ATOM
2186
C
TRP
A
406
61.075
54.979
8.661
1.00
34.05
C


ATOM
2187
O
TRP
A
406
61.165
53.841
9.126
1.00
33.82
O


ATOM
2188
CB
TRP
A
406
60.232
55.113
6.281
1.00
32.23
C


ATOM
2189
CG
TRP
A
406
59.577
53.763
6.285
1.00
29.53
C


ATOM
2190
CD1
TRP
A
406
58.605
53.327
7.138
1.00
29.14
C


ATOM
2191
CD2
TRP
A
406
59.874
52.659
5.419
1.00
29.51
C


ATOM
2192
NE1
TRP
A
406
58.280
52.023
6.860
1.00
28.25
N


ATOM
2193
CE2
TRP
A
406
59.045
51.586
5.811
1.00
28.80
C


ATOM
2194
CE3
TRP
A
406
60.764
52.472
4.350
1.00
30.06
C


ATOM
2195
CZ2
TRP
A
406
59.077
50.337
5.173
1.00
29.23
C


ATOM
2196
CZ3
TRP
A
406
60.797
51.230
3.713
1.00
30.49
C


ATOM
2197
CH2
TRP
A
406
59.956
50.178
4.131
1.00
30.09
C


ATOM
2198
N
GLY
A
407
60.682
56.030
9.372
1.00
33.97
N


ATOM
2199
CA
GLY
A
407
60.300
55.883
10.763
1.00
35.09
C


ATOM
2200
C
GLY
A
407
58.921
55.270
10.912
1.00
35.29
C


ATOM
2201
O
GLY
A
407
58.124
55.281
9.978
1.00
34.78
O


ATOM
2202
N
GLU
A
408
58.640
54.723
12.090
1.00
35.40
N


ATOM
2203
CA
GLU
A
408
57.347
54.112
12.356
1.00
35.13
C


ATOM
2204
C
GLU
A
408
56.273
55.189
12.468
1.00
36.19
C


ATOM
2205
O
GLU
A
408
55.081
54.899
12.408
1.00
35.83
O


ATOM
2206
CB
GLU
A
408
57.414
53.295
13.647
1.00
33.46
C


ATOM
2207
CG
GLU
A
408
58.193
51.999
13.498
1.00
32.80
C


ATOM
2208
CD
GLU
A
408
57.499
51.006
12.569
1.00
31.60
C


ATOM
2209
OE1
GLU
A
408
56.402
50.534
12.918
1.00
29.78
O


ATOM
2210
OE2
GLU
A
408
58.047
50.701
11.490
1.00
31.44
O


ATOM
2211
N
GLY
A
409
56.709
56.436
12.619
1.00
37.77
N


ATOM
2212
CA
GLY
A
409
55.773
57.539
12.734
1.00
39.49
C


ATOM
2213
C
GLY
A
409
55.400
58.156
11.397
1.00
40.71
C


ATOM
2214
O
GLY
A
409
54.482
58.970
11.323
1.00
40.61
O


ATOM
2215
N
SER
A
410
56.109
57.782
10.338
1.00
42.27
N


ATOM
2216
CA
SER
A
410
55.813
58.318
9.013
1.00
44.24
C


ATOM
2217
C
SER
A
410
54.485
57.742
8.526
1.00
45.74
C


ATOM
2218
O
SER
A
410
54.065
56.672
8.968
1.00
44.79
O


ATOM
2219
CB
SER
A
410
56.917
57.952
8.017
1.00
43.45
C


ATOM
2220
OG
SER
A
410
56.832
56.587
7.641
1.00
44.08
O


ATOM
2221
N
SER
A
411
53.828
58.457
7.618
1.00
48.17
N


ATOM
2222
CA
SER
A
411
52.556
57.998
7.081
1.00
50.72
C


ATOM
2223
C
SER
A
411
52.777
56.708
6.301
1.00
51.98
C


ATOM
2224
O
SER
A
411
51.885
55.865
6.205
1.00
51.95
O


ATOM
2225
CB
SER
A
411
51.947
59.064
6.170
1.00
51.02
C


ATOM
2226
OG
SER
A
411
52.832
59.393
5.116
1.00
52.23
O


ATOM
2227
N
ARG
A
412
53.978
56.555
5.754
1.00
53.68
N


ATOM
2228
CA
ARG
A
412
54.323
55.363
4.989
1.00
55.96
C


ATOM
2229
C
ARG
A
412
54.226
54.083
5.819
1.00
58.17
C


ATOM
2230
O
ARG
A
412
54.018
53.000
5.275
1.00
57.86
O


ATOM
2231
CB
ARG
A
412
55.741
55.491
4.419
1.00
54.66
C


ATOM
2232
CG
ARG
A
412
56.208
54.242
3.687
1.00
53.34
C


ATOM
2233
CD
ARG
A
412
57.550
54.426
3.003
1.00
51.73
C


ATOM
2234
NE
ARG
A
412
57.933
53.211
2.288
1.00
50.66
N


ATOM
2235
CZ
ARG
A
412
59.023
53.086
1.539
1.00
51.11
C


ATOM
2236
NH1
ARG
A
412
59.860
54.108
1.396
1.00
50.38
N


ATOM
2237
NH2
ARG
A
412
59.276
51.935
0.929
1.00
51.44
N


ATOM
2238
N
ALA
A
413
54.374
54.212
7.134
1.00
61.58
N


ATOM
2239
CA
ALA
A
413
54.321
53.057
8.031
1.00
64.71
C


ATOM
2240
C
ALA
A
413
52.976
52.880
8.733
1.00
67.35
C


ATOM
2241
O
ALA
A
413
52.495
51.757
8.877
1.00
66.86
O


ATOM
2242
CB
ALA
A
413
55.436
53.165
9.067
1.00
63.82
C


ATOM
2243
N
ARG
A
414
52.386
53.987
9.179
1.00
71.43
N


ATOM
2244
CA
ARG
A
414
51.102
53.948
9.874
1.00
75.31
C


ATOM
2245
C
ARG
A
414
49.999
53.373
8.991
1.00
77.02
C


ATOM
2246
O
ARG
A
414
49.031
52.789
9.485
1.00
77.08
O


ATOM
2247
CB
ARG
A
414
50.683
55.353
10.322
1.00
76.52
C


ATOM
2248
CG
ARG
A
414
51.456
55.939
11.491
1.00
78.03
C


ATOM
2249
CD
ARG
A
414
50.703
57.153
12.026
1.00
80.11
C


ATOM
2250
NE
ARG
A
414
51.381
57.807
13.142
1.00
81.88
N


ATOM
2251
CZ
ARG
A
414
50.844
58.779
13.874
1.00
82.61
C


ATOM
2252
NH1
ARG
A
414
49.617
59.210
13.612
1.00
83.27
N


ATOM
2253
NH2
ARG
A
414
51.532
59.325
14.867
1.00
83.16
N


ATOM
2254
N
ASN
A
415
50.154
53.546
7.683
1.00
78.97
N


ATOM
2255
CA
ASN
A
415
49.170
53.058
6.725
1.00
81.09
C


ATOM
2256
C
ASN
A
415
49.252
51.540
6.520
1.00
81.85
C


ATOM
2257
O
ASN
A
415
49.489
51.069
5.403
1.00
81.77
O


ATOM
2258
CB
ASN
A
415
49.356
53.774
5.380
1.00
82.25
C


ATOM
2259
CG
ASN
A
415
48.070
53.845
4.568
1.00
83.78
C


ATOM
2260
OD1
ASN
A
415
47.434
52.825
4.295
1.00
84.64
O


ATOM
2261
ND2
ASN
A
415
47.681
55.055
4.181
1.00
84.44
N


ATOM
2262
N
TRP
A
416
49.055
50.778
7.598
1.00
82.26
N


ATOM
2263
CA
TRP
A
416
49.095
49.316
7.519
1.00
82.50
C


ATOM
2264
C
TRP
A
416
47.758
48.722
7.927
1.00
82.72
C


ATOM
2265
O
TRP
A
416
47.554
47.515
7.823
1.00
83.08
O


ATOM
2266
CE
TRP
A
416
50.209
48.732
8.412
1.00
82.13
C


ATOM
2267
CG
TRP
A
416
49.928
48.742
9.894
1.00
81.82
C


ATOM
2268
CD1
TRP
A
416
50.244
49.730
10.781
1.00
82.00
C


ATOM
2269
CD2
TRP
A
416
49.273
47.714
10.659
1.00
81.56
C


ATOM
2270
NE1
TRP
A
416
49.830
49.385
12.048
1.00
81.96
N


ATOM
2271
CE2
TRP
A
416
49.230
48.154
12.001
1.00
81.69
C


ATOM
2272
CE3
TRP
A
416
48.716
46.467
10.339
1.00
81.07
C


ATOM
2273
CZ2
TRP
A
416
48.652
47.390
13.026
1.00
81.58
C


ATOM
2274
CZ3
TRP
A
416
48.140
45.706
11.359
1.00
80.88
C


ATOM
2275
CH2
TRP
A
416
48.113
46.173
12.685
1.00
81.28
C


ATOM
2276
N
SER
A
428
47.786
65.086
7.718
1.00
95.79
N


ATOM
2277
CA
SER
A
428
48.357
66.353
7.278
1.00
95.93
C


ATOM
2278
C
SER
A
428
49.676
66.643
7.988
1.00
96.13
C


ATOM
2279
O
SER
A
428
50.268
67.709
7.812
1.00
96.06
O


ATOM
2280
CE
SER
A
428
47.367
67.497
7.532
1.00
95.59
C


ATOM
2281
OG
SER
A
428
47.047
67.610
8.907
1.00
95.03
O


ATOM
2282
N
PHE
A
429
50.134
65.687
8.789
1.00
96.33
N


ATOM
2283
CA
PHE
A
429
51.384
65.837
9.525
1.00
96.45
C


ATOM
2284
C
PHE
A
429
52.185
64.541
9.412
1.00
95.70
C


ATOM
2285
O
PHE
A
429
51.867
63.685
8.586
1.00
95.85
O


ATOM
2286
CB
PHE
A
429
51.091
66.156
10.995
1.00
97.56
C


ATOM
2287
CG
PHE
A
429
52.269
66.717
11.741
1.00
98.75
C


ATOM
2288
CD1
PHE
A
429
52.886
67.889
11.311
1.00
99.16
C


ATOM
2289
CD2
PHE
A
429
52.771
66.069
12.866
1.00
99.35
C


ATOM
2290
CE1
PHE
A
429
53.987
68.410
11.989
1.00
99.58
C


ATOM
2291
CE2
PHE
A
429
53.872
66.581
13.553
1.00
99.81
C


ATOM
2292
CZ
PHE
A
429
54.481
67.754
13.113
1.00
99.76
C


ATOM
2293
N
GLU
A
430
53.222
64.395
10.235
1.00
94.58
N


ATOM
2294
CA
GLU
A
430
54.047
63.191
10.205
1.00
93.27
C


ATOM
2295
C
GLU
A
430
55.093
63.181
11.320
1.00
91.79
C


ATOM
2296
O
GLU
A
430
55.884
64.115
11.453
1.00
91.62
O


ATOM
2297
CB
GLU
A
430
54.728
63.065
8.841
1.00
94.00
C


ATOM
2298
CG
GLU
A
430
55.300
61.691
8.559
1.00
94.70
C


ATOM
2299
CD
GLU
A
430
55.471
61.436
7.076
1.00
95.05
C


ATOM
2300
OE1
GLU
A
430
54.459
61.503
6.346
1.00
95.03
O


ATOM
2301
OE2
GLU
A
430
56.612
61.168
6.642
1.00
95.48
O


ATOM
2302
N
GLU
A
431
55.092
62.110
12.110
1.00
89.87
N


ATOM
2303
CA
GLU
A
431
56.014
61.960
13.234
1.00
87.81
C


ATOM
2304
C
GLU
A
431
57.423
61.519
12.843
1.00
85.39
C


ATOM
2305
O
GLU
A
431
58.356
61.618
13.643
1.00
85.00
O


ATOM
2306
CB
GLU
A
43L
55.437
60.973
14.257
1.00
89.03
C


ATOM
2307
CG
GLU
A
431
54.235
61.494
15.044
1.00
90.63
C


ATOM
2308
CD
GLU
A
431
53.091
61.955
14.153
1.00
91.93
C


ATOM
2309
OE1
GLU
A
431
52.602
61.144
13.336
1.00
92.15
O


ATOM
2310
OE2
GLU
A
431
52.678
63.130
14.274
1.00
92.38
O


ATOM
2311
N
GLY
A
432
57.577
61.031
11.618
1.00
82.69
N


ATOM
2312
CA
GLY
A
432
58.885
60.587
11.170
1.00
79.01
C


ATOM
2313
C
GLY
A
432
59.146
60.936
9.720
1.00
76.48
C


ATOM
2314
O
GLY
A
432
58.345
61.623
9.087
1.00
76.66
O


ATOM
2315
N
VAL
A
433
60.269
60.464
9.190
1.00
73.56
N


ATOM
2316
CA
VAL
A
433
60.615
60.739
7.803
1.00
70.14
C


ATOM
2317
C
VAL
A
433
60.915
59.466
7.014
1.00
67.42
C


ATOM
2318
O
VAL
A
433
61.128
58.399
7.588
1.00
67.04
O


ATOM
2319
CE
VAL
A
433
61.827
61.699
7.710
1.00
70.47
C


ATOM
2320
CG1
VAL
A
433
61.451
63.062
8.272
1.00
70.12
C


ATOM
2321
CG2
VAL
A
433
63.010
61.124
8.465
1.00
70.31
C


ATOM
2322
N
ASP
A
434
60.913
59.598
5.691
1.00
63.84
N


ATOM
2323
CA
ASP
A
434
61.173
58.491
4.778
1.00
60.33
C


ATOM
2324
C
ASP
A
434
62.386
58.864
3.930
1.00
58.07
C


ATOM
2325
O
ASP
A
434
62.300
59.737
3.066
1.00
57.72
O


ATOM
2326
CB
ASP
A
434
59.937
58.261
3.899
1.00
60.27
C


ATOM
2327
CG
ASP
A
434
60.115
57.123
2.914
1.00
60.71
C


ATOM
2328
OD1
ASP
A
434
60.683
56.081
3.297
1.00
61.60
O


ATOM
2329
OD2
ASP
A
434
59.669
57.261
1.756
1.00
60.76
O


ATOM
2330
N
SER
A
435
63.516
58.207
4.181
1.00
55.22
N


ATOM
2331
CA
SER
A
435
64.741
58.509
3.448
1.00
52.53
C


ATOM
2332
C
SER
A
435
65.566
57.297
3.028
1.00
49.99
C


ATOM
2333
O
SER
A
435
65.072
56.172
2.970
1.00
49.04
O


ATOM
2334
CB
SER
A
435
65.620
59.437
4.284
1.00
53.18
C


ATOM
2335
OG
SER
A
435
65.947
58.820
5.515
1.00
54.44
O


ATOM
2336
N
TYR
A
436
66.838
57.550
2.740
1.00
47.61
N


ATOM
2337
CA
TYR
A
436
67.765
56.513
2.307
1.00
45.82
C


ATOM
2338
C
TYR
A
436
69.026
56.466
3.168
1.00
44.39
C


ATOM
2339
O
TYR
A
436
69.481
57.490
3.685
1.00
44.28
O


ATOM
2340
CB
TYR
A
436
68.184
56.764
0.858
1.00
46.81
C


ATOM
2341
CG
TYR
A
436
67.075
56.643
−0.159
1.00
47.16
C


ATOM
2342
CD1
TYR
A
436
66.584
55.396
−0.537
1.00
47.36
C


ATOM
2343
CD2
TYR
A
436
66.527
57.778
−0.754
1.00
48.36
C


ATOM
2344
CE1
TYR
A
436
65.575
55.279
−1.485
1.00
49.05
C


ATOM
2345
CE2
TYR
A
436
65.515
57.674
−1.706
1.00
49.53
C


ATOM
2346
CZ
TYR
A
436
65.046
56.422
−2.066
1.00
49.47
C


ATOM
2347
OH
TYR
A
436
64.050
56.312
−3.007
1.00
51.33
O


ATOM
2348
N
VAL
A
437
69.585
55.269
3.318
1.00
41.45
N


ATOM
2349
CA
VAL
A
437
70.817
55.089
4.072
1.00
38.90
C


ATOM
2350
C
VAL
A
437
71.765
54.336
3.151
1.00
38.06
C


ATOM
2351
O
VAL
A
437
71.334
53.496
2.366
1.00
37.46
O


ATOM
2352
CB
VAL
A
437
70.600
54.275
5.370
1.00
38.21
C


ATOM
2353
CG1
VAL
A
437
69.639
55.014
6.286
1.00
38.54
C


ATOM
2354
CG2
VAL
A
437
70.086
52.884
5.042
1.00
36.53
C


ATOM
2355
N
PRO
A
438
73.071
54.635
3.226
1.00
37.64
N


ATOM
2356
CA
PRO
A
438
74.049
53.958
2.371
1.00
36.86
C


ATOM
2357
C
PRO
A
438
74.220
52.474
2.674
1.00
36.29
C


ATOM
2358
O
PRO
A
438
74.336
52.069
3.834
1.00
36.41
O


ATOM
2359
CB
PRO
A
438
75.327
54.764
2.608
1.00
36.76
C


ATOM
2360
CG
PRO
A
438
75.175
55.210
4.026
1.00
37.68
C


ATOM
2361
CD
PRO
A
438
73.725
55.641
4.080
1.00
37.02
C


ATOM
2362
N
TYR
A
439
74.223
51.671
1.613
1.00
35.21
N


ATOM
2363
CA
TYR
A
439
74.381
50.227
1.717
1.00
34.92
C


ATOM
2364
C
TYR
A
439
75.744
49.913
2.328
1.00
34.83
C


ATOM
2365
O
TYR
A
439
76.768
50.436
1.888
1.00
35.17
O


ATOM
2366
CB
TYR
A
439
74.267
49.599
0.325
1.00
34.07
C


ATOM
2367
CG
TYR
A
439
74.418
48.098
0.299
1.00
33.14
C


ATOM
2368
CD1
TYR
A
439
73.561
47.279
1.029
1.00
32.78
C


ATOM
2369
CD2
TYR
A
439
75.407
47.494
−0.478
1.00
34.43
C


ATOM
2370
CE1
TYR
A
439
73.682
45.892
0.984
1.00
34.47
C


ATOM
2371
CE2
TYR
A
439
75.536
46.110
−0.529
1.00
34.40
C


ATOM
2372
CZ
TYR
A
439
74.670
45.317
0.202
1.00
34.68
C


ATOM
2373
OH
TYR
A
439
74.791
43.949
0.148
1.00
36.73
O


ATOM
2374
N
ALA
A
440
75.752
49.051
3.337
1.00
34.57
N


ATOM
2375
CA
ALA
A
440
76.990
48.696
4.019
1.00
34.81
C


ATOM
2376
C
ALA
A
440
77.361
47.225
3.860
1.00
34.72
C


ATOM
2377
O
ALA
A
440
78.375
46.776
4.390
1.00
34.93
O


ATOM
2378
CE
ALA
A
440
76.874
49.047
5.502
1.00
33.67
C


ATOM
2379
N
GLY
A
441
76.542
46.474
3.134
1.00
34.47
N


ATOM
2380
CA
GLY
A
441
76.833
45.066
2.945
1.00
34.40
C


ATOM
2381
C
GLY
A
441
76.172
44.203
4.003
1.00
34.97
C


ATOM
2382
O
GLY
A
441
75.144
44.581
4.567
1.00
35.10
O


ATOM
2383
N
LYS
A
442
76.763
43.043
4.276
1.00
35.43
N


ATOM
2384
CA
LYS
A
442
76.226
42.110
5.265
1.00
35.71
C


ATOM
2385
C
LYS
A
442
76.421
42.615
6.694
1.00
34.74
C


ATOM
2386
O
LYS
A
442
77.415
43.272
7.005
1.00
33.81
O


ATOM
2387
CB
LYS
A
442
76.909
40.745
5.132
1.00
37.45
C


ATOM
2388
CG
LYS
A
442
76.860
40.138
3.739
1.00
41.47
C


ATOM
2389
CD
LYS
A
442
75.891
38.966
3.666
1.00
44.08
C


ATOM
2390
CE
LYS
A
442
74.461
39.409
3.914
1.00
47.03
C


ATOM
2391
NZ
LYS
A
442
73.508
38.265
3.826
1.00
49.47
N


ATOM
2392
N
LEU
A
443
75.466
42.282
7.555
1.00
33.84
N


ATOM
2393
CA
LEU
A
443
75.497
42.663
8.962
1.00
33.05
C


ATOM
2394
C
LEU
A
443
76.769
42.197
9.681
1.00
33.87
C


ATOM
2395
O
LEU
A
443
77.401
42.968
10.398
1.00
32.69
O


ATOM
2396
CE
LEU
A
443
74.265
42.084
9.672
1.00
31.90
C


ATOM
2397
CG
LEU
A
443
74.104
42.252
11.190
1.00
31.99
C


ATOM
2398
CD1
LEU
A
443
72.651
42.031
11.568
1.00
31.10
C


ATOM
2399
CD2
LEU
A
443
75.001
41.274
11.935
1.00
31.47
C


ATOM
2400
N
LYS
A
444
77.135
40.934
9.481
1.00
34.24
N


ATOM
2401
CA
LYS
A
444
78.304
40.344
10.134
1.00
36.18
C


ATOM
2402
C
LYS
A
444
79.587
41.182
10.174
1.00
35.95
C


ATOM
2403
O
LYS
A
444
80.089
41.499
11.252
1.00
36.11
O


ATOM
2404
CE
LYS
A
444
78.621
38.981
9.510
1.00
37.74
C


ATOM
2405
CG
LYS
A
444
79.746
38.236
10.219
1.00
41.26
C


ATOM
2406
CD
LYS
A
444
79.871
36.804
9.720
1.00
44.01
C


ATOM
2407
CE
LYS
A
444
80.857
36.013
10.560
1.00
44.57
C


ATOM
2408
NZ
LYS
A
444
82.223
36.599
10.490
1.00
46.17
N


ATOM
2409
N
ASP
A
445
80.113
41.530
9.005
1.00
35.90
N


ATOM
2410
CA
ASP
A
445
81.347
42.301
8.904
1.00
36.42
C


ATOM
2411
C
ASP
A
445
81.273
43.666
9.569
1.00
35.53
C


ATOM
2412
O
ASP
A
445
82.241
44.125
10.172
1.00
35.05
O


ATOM
2413
CB
ASP
A
445
81.733
42.490
7.433
1.00
39.61
C


ATOM
2414
CG
ASP
A
445
81.951
41.172
6.713
1.00
42.27
C


ATOM
2415
OD1
ASP
A
445
82.810
40.383
7.163
1.00
43.65
O


ATOM
2416
OD2
ASP
A
445
81.262
40.927
5.700
1.00
45.22
O


ATOM
2417
N
ASN
A
446
80.126
44.317
9.447
1.00
34.05
N


ATOM
2418
CA
ASN
A
446
79.945
45.639
10.027
1.00
33.14
C


ATOM
2419
C
ASN
A
446
79.862
45.596
11.547
1.00
32.11
C


ATOM
2420
O
ASN
A
446
80.506
46.394
12.227
1.00
31.82
O


ATOM
2421
CB
ASN
A
446
78.693
46.281
9.439
1.00
34.11
C


ATOM
2422
CG
ASN
A
446
78.853
46.608
7.969
1.00
35.94
C


ATOM
2423
OD1
ASN
A
446
79.391
47.659
7.612
1.00
37.15
O


ATOM
2424
ND2
ASN
A
446
78.406
45.698
7.104
1.00
33.70
N


ATOM
2425
N
VAL
A
447
79.071
44.669
12.078
1.00
31.18
N


ATOM
2426
CA
VAL
A
447
78.929
44.533
13.523
1.00
30.87
C


ATOM
2427
C
VAL
A
447
80.273
44.161
14.154
1.00
31.57
C


ATOM
2428
O
VAL
A
447
80.621
44.637
15.233
1.00
31.53
O


ATOM
2429
CB
VAL
A
447
77.883
43.454
13.882
1.00
30.26
C


ATOM
2430
CG1
VAL
A
447
77.995
43.087
15.354
1.00
29.78
C


ATOM
2431
CG2
VAL
A
447
76.490
43.969
13.581
1.00
29.08
C


ATOM
2432
N
GLU
A
448
81.030
43.313
13.468
1.00
31.62
N


ATOM
2433
CA
GLU
A
448
82.326
42.887
13.971
1.00
33.06
C


ATOM
2434
C
GLU
A
448
83.279
44.082
14.049
1.00
31.22
C


ATOM
2435
O
GLU
A
448
83.975
44.257
15.042
1.00
29.89
O


ATOM
2436
CB
GLU
A
448
82.900
41.790
13.066
1.00
35.76
C


ATOM
2437
CG
GLU
A
448
84.250
41.240
13.503
1.00
41.89
C


ATOM
2438
CD
GLU
A
448
84.719
40.085
12.623
1.00
46.86
C


ATOM
2439
OE1
GLU
A
448
84.030
39.037
12.596
1.00
49.61
O


ATOM
2440
OE2
GLU
A
448
85.770
40.228
11.957
1.00
47.95
O


ATOM
2441
N
ALA
A
449
83.302
44.904
13.004
1.00
29.89
N


ATOM
2442
CA
ALA
A
449
84.167
46.083
12.982
1.00
29.27
C


ATOM
2443
C
ALA
A
449
83.764
47.074
14.075
1.00
28.76
C


ATOM
2444
O
ALA
A
449
84.619
47.677
14.725
1.00
28.88
O


ATOM
2445
CB
ALA
A
449
84.099
46.764
11.616
1.00
28.30
C


ATOM
2446
N
SER
A
450
82.460
47.243
14.267
1.00
27.76
N


ATOM
2447
CA
SER
A
450
81.947
48.157
15.282
1.00
27.63
C


ATOM
2448
C
SER
A
450
82.321
47.712
16.691
1.00
27.22
C


ATOM
2449
O
SER
A
450
82.815
48.507
17.490
1.00
26.61
O


ATOM
2450
CB
SER
A
450
80.421
48.272
15.182
1.00
27.03
C


ATOM
2451
OG
SER
A
450
80.037
49.038
14.053
1.00
28.56
O


ATOM
2452
N
LEU
A
451
82.086
46.437
16.989
1.00
26.98
N


ATOM
2453
CA
LEU
A
451
82.378
45.906
18.310
1.00
27.66
C


ATOM
2454
C
LEU
A
451
83.870
45.755
18.598
1.00
29.12
C


ATOM
2455
O
LEU
A
451
84.270
45.719
19.758
1.00
28.46
O


ATOM
2456
CB
LEU
A
451
81.638
44.580
18.522
1.00
26.68
C


ATOM
2457
CG
LEU
A
451
80.112
44.754
18.493
1.00
26.86
C


ATOM
2458
CD1
LEU
A
451
79.422
43.455
18.852
1.00
24.50
C


ATOM
2459
CD2
LEU
A
451
79.704
45.860
19.461
1.00
26.58
C


ATOM
2460
N
ASN
A
452
84.697
45.671
17.559
1.00
30.10
N


ATOM
2461
CA
ASN
A
452
86.132
45.577
17.795
1.00
31.68
C


ATOM
2462
C
ASN
A
452
86.595
46.926
18.323
1.00
31.06
C


ATOM
2463
O
ASN
A
452
87.470
46.999
19.187
1.00
30.69
O


ATOM
2464
CB
ASN
A
452
86.907
45.230
16.519
1.00
33.39
C


ATOM
2465
CG
ASN
A
452
86.881
43.747
16.208
1.00
37.58
C


ATOM
2466
OD1
ASN
A
452
86.800
42.908
17.113
1.00
40.20
O


ATOM
2467
ND2
ASN
A
452
86.969
43.411
14.925
1.00
39.30
N


ATOM
2468
N
LYS
A
453
86.000
47.996
17.805
1.00
30.67
N


ATOM
2469
CA
LYS
A
453
86.358
49.334
18.256
1.00
31.02
C


ATOM
2470
C
LYS
A
453
85.863
49.550
19.680
1.00
28.53
C


ATOM
2471
O
LYS
A
453
86.549
50.170
20.489
1.00
28.63
O


ATOM
2472
CB
LYS
A
453
85.779
50.407
17.326
1.00
32.56
C


ATOM
2473
CG
LYS
A
453
86.475
50.454
15.974
1.00
38.18
C


ATOM
2474
CD
LYS
A
453
86.326
51.813
15.290
1.00
40.85
C


ATOM
2475
CE
LYS
A
453
84.888
52.108
14.928
1.00
43.86
C


ATOM
2476
NZ
LYS
A
453
84.745
53.424
14.236
1.00
45.10
N


ATOM
2477
N
VAL
A
454
84.674
49.041
19.982
1.00
26.35
N


ATOM
2478
CA
VAL
A
454
84.121
49.168
21.321
1.00
25.14
C


ATOM
2479
C
VAL
A
454
85.037
48.436
22.305
1.00
25.64
C


ATOM
2480
O
VAL
A
454
85.395
48.980
23.352
1.00
24.53
O


ATOM
2481
CB
VAL
A
454
82.700
48.566
21.409
1.00
25.38
C


ATOM
2482
CG1
VAL
A
454
82.241
48.504
22.869
1.00
24.56
C


ATOM
2483
CG2
VAL
A
454
81.725
49.413
20.589
1.00
24.60
C


ATOM
2484
N
LYS
A
455
85.419
47.208
21.956
1.00
25.47
N


ATOM
2485
CA
LYS
A
455
86.290
46.393
22.805
1.00
26.49
C


ATOM
2486
C
LYS
A
455
87.634
47.073
23.053
1.00
27.06
C


ATOM
2487
O
LYS
A
455
88.162
47.051
24.165
1.00
26.76
O


ATOM
2488
CB
LYS
A
455
86.534
45.030
22.157
1.00
26.81
C


ATOM
2489
CG
LYS
A
455
85.335
44.099
22.139
1.00
27.88
C


ATOM
2490
CD
LYS
A
455
85.653
42.889
21.279
1.00
29.25
C


ATOM
2491
CE
LYS
A
455
84.558
41.857
21.344
1.00
32.72
C


ATOM
2492
NZ
LYS
A
455
84.871
40.695
20.464
1.00
33.72
N


ATOM
2493
N
SER
A
456
88.185
47.664
22.000
1.00
26.88
N


ATOM
2494
CA
SER
A
456
89.463
48.355
22.084
1.00
28.22
C


ATOM
2495
C
SER
A
456
89.356
49.563
23.021
1.00
27.71
C


ATOM
2496
O
SER
A
456
90.221
49.788
23.868
1.00
27.11
O


ATOM
2497
CB
SER
A
456
89.896
48.801
20.684
1.00
29.36
C


ATOM
2498
OG
SER
A
456
91.173
49.401
20.715
1.00
32.57
O


ATOM
2499
N
THR
A
457
88.289
50.339
22.866
1.00
26.02
N


ATOM
2500
CA
THR
A
457
88.083
51.502
23.713
1.00
25.29
C


ATOM
2501
C
THR
A
457
87.905
51.052
25.159
1.00
24.88
C


ATOM
2502
O
THR
A
457
88.407
51.692
26.083
1.00
25.60
O


ATOM
2503
CB
THR
A
457
86.847
52.297
23.269
1.00
24.46
C


ATOM
2504
OG1
THR
A
457
87.013
52.689
21.904
1.00
26.98
O


ATOM
2505
CG2
THR
A
457
86.677
53.541
24.113
1.00
21.68
C


ATOM
2506
N
MET
A
458
87.192
49.948
25.355
1.00
24.86
N


ATOM
2507
CA
MET
A
458
86.977
49.430
26.697
1.00
23.62
C


ATOM
2508
C
MET
A
458
88.314
49.140
27.363
1.00
24.86
C


ATOM
2509
O
MET
A
458
88.496
49.424
28.545
1.00
25.51
O


ATOM
2510
CB
MET
A
458
86.097
48.179
26.653
1.00
23.91
C


ATOM
2511
CG
MET
A
458
84.603
48.501
26.525
1.00
23.56
C


ATOM
2512
SD
MET
A
458
83.557
47.082
26.176
1.00
24.90
S


ATOM
2513
CE
MET
A
458
83.569
46.235
27.743
1.00
23.81
C


ATOM
2514
N
CYS
A
459
89.268
48.599
26.613
1.00
26.31
N


ATOM
2515
CA
CYS
A
459
90.567
48.321
27.213
1.00
27.49
C


ATOM
2516
C
GYS
A
459
91.294
49.613
27.561
1.00
27.38
C


ATOM
2517
O
CYS
A
459
92.055
49.655
28.528
1.00
27.52
O


ATOM
2518
CB
CYS
A
459
91.418
47.440
26.300
1.00
29.11
C


ATOM
2519
SG
CYS
A
459
90.985
45.676
26.452
1.00
33.31
S


ATOM
2520
N
ASN
A
460
91.052
50.665
26.780
1.00
26.76
N


ATOM
2521
CA
ASN
A
460
91.659
51.966
27.053
1.00
26.30
C


ATOM
2522
C
ASN
A
460
91.112
52.452
28.387
1.00
25.18
C


ATOM
2523
O
ASN
A
460
91.780
53.177
29.110
1.00
25.85
O


ATOM
2524
CB
ASN
A
460
91.284
52.996
25.983
1.00
26.49
C


ATOM
2525
CG
ASN
A
460
91.974
52.753
24.662
1.00
27.93
C


ATOM
2526
OD1
ASN
A
460
91.321
52.628
23.629
1.00
30.37
O


ATOM
2527
ND2
ASN
A
460
93.301
52.698
24.683
1.00
27.47
N


ATOM
2528
N
CYS
A
461
89.886
52.049
28.704
1.00
24.75
N


ATOM
2529
CA
CYS
A
461
89.245
52.468
29.946
1.00
24.35
C


ATOM
2530
C
GYS
A
461
89.471
51.485
31.093
1.00
24.59
C


ATOM
2531
O
CYS
A
461
88.929
51.663
32.179
1.00
24.19
O


ATOM
2532
CB
CYS
A
461
87.738
52.665
29.716
1.00
25.37
C


ATOM
2533
SG
CYS
A
461
87.342
53.931
28.465
1.00
26.44
S


ATOM
2534
N
GLY
A
462
90.266
50.449
30.839
1.00
25.17
N


ATOM
2535
CA
GLY
A
462
90.562
49.454
31.857
1.00
24.26
C


ATOM
2536
C
GLY
A
462
89.424
48.490
32.136
1.00
25.01
C


ATOM
2537
O
GLY
A
462
89.300
47.970
33.250
1.00
25.14
O


ATOM
2538
N
ALA
A
463
88.601
48.228
31.127
1.00
23.44
N


ATOM
2539
CA
ALA
A
463
87.462
47.339
31.302
1.00
23.93
C


ATOM
2540
C
ALA
A
463
87.479
46.110
30.397
1.00
24.29
C


ATOM
2541
O
ALA
A
463
87.688
46.216
29.185
1.00
23.39
O


ATOM
2542
CB
ALA
A
463
86.169
48.122
31.085
1.00
21.46
C


ATOM
2543
N
LEU
A
464
87.245
44.950
31.002
1.00
24.49
N


ATOM
2544
CA
LEU
A
464
87.195
43.686
30.275
1.00
26.40
C


ATOM
2545
C
LEU
A
464
85.749
43.260
30.066
1.00
25.77
C


ATOM
2546
O
LEU
A
464
85.476
42.351
29.287
1.00
27.45
O


ATOM
2547
CB
LEU
A
464
87.936
42.582
31.039
1.00
27.85
C


ATOM
2548
CG
LEU
A
464
89.448
42.499
30.823
1.00
29.66
C


ATOM
2549
CD1
LEU
A
464
90.024
41.335
31.630
1.00
31.06
C


ATOM
2550
CD2
LEU
A
464
89.730
42.304
29.349
1.00
30.29
C


ATOM
2551
N
THR
A
465
84.829
43.909
30.775
1.00
25.23
N


ATOM
2552
CA
THR
A
465
83.406
43.603
30.656
1.00
24.98
C


ATOM
2553
C
THR
A
465
82.589
44.893
30.684
1.00
25.79
C


ATOM
2554
O
THR
A
465
83.096
45.955
31.057
1.00
24.88
O


ATOM
2555
CB
THR
A
465
82.913
42.719
31.812
1.00
25.00
C


ATOM
2556
OG1
THR
A
465
82.998
43.458
33.035
1.00
24.92
O


ATOM
2557
CG2
THR
A
465
83.757
41.447
31.921
1.00
24.20
C


ATOM
2558
N
ILE
A
466
81.323
44.801
30.293
1.00
24.73
N


ATOM
2559
CA
ILE
A
466
80.470
45.977
30.294
1.00
24.59
C


ATOM
2560
C
ILE
A
466
80.269
46.503
31.717
1.00
24.91
C


ATOM
2561
O
ILE
A
466
80.359
47.702
31.952
1.00
26.03
O


ATOM
2562
CB
ILE
A
466
79.117
45.672
29.616
1.00
24.22
C


ATOM
2563
CG1
ILE
A
466
79.340
45.548
28.104
1.00
22.81
C


ATOM
2564
CG2
ILE
A
466
78.095
46.761
29.931
1.00
20.91
C


ATOM
2565
CD1
ILE
A
466
78.132
45.051
27.344
1.00
23.02
C


ATOM
2566
N
PRO
A
467
79.997
45.614
32.688
1.00
25.66
N


ATOM
2567
CA
PRO
A
467
79.811
46.107
34.058
1.00
25.52
C


ATOM
2568
C
PRO
A
467
81.057
46.840
34.566
1.00
26.38
C


ATOM
2569
O
PRO
A
467
80.967
47.837
35.284
1.00
25.66
O


ATOM
2570
CB
PRO
A
467
79.525
44.829
34.846
1.00
25.82
C


ATOM
2571
CG
PRO
A
467
78.798
43.980
33.829
1.00
25.19
C


ATOM
2572
CD
PRO
A
467
79.658
44.181
32.596
1.00
24.50
C


ATOM
2573
N
GLN
A
468
82.225
46.346
34.183
1.00
26.53
N


ATOM
2574
CA
GLN
A
468
83.464
46.968
34.609
1.00
27.70
C


ATOM
2575
C
GLN
A
468
83.626
48.344
33.954
1.00
28.31
C


ATOM
2576
O
GLN
A
468
84.153
49.279
34.567
1.00
27.56
O


ATOM
2577
CB
GLN
A
468
84.631
46.052
34.265
1.00
29.61
C


ATOM
2578
CG
GLN
A
468
85.932
46.460
34.882
1.00
32.72
C


ATOM
2579
CD
GLN
A
468
86.925
45.320
34.922
1.00
32.87
C


ATOM
2580
OE2
GLN
A
468
87.034
44.540
33.977
1.00
30.31
O


ATOM
2581
NE2
GLN
A
468
87.670
45.231
36.015
1.00
35.10
N


ATOM
2582
N
LEU
A
469
83.156
48.468
32.713
1.00
27.10
N


ATOM
2583
CA
LEU
A
469
83.222
49.734
31.994
1.00
26.38
C


ATOM
2584
C
LEU
A
469
82.286
50.742
32.656
1.00
25.76
C


ATOM
2585
O
LEU
A
469
82.641
51.904
32.840
1.00
24.62
O


ATOM
2586
CE
LEU
A
469
82.809
49.547
30.530
1.00
26.12
C


ATOM
2587
CG
LEU
A
469
82.606
50.848
29.742
1.00
26.70
C


ATOM
2588
CD1
LEU
A
469
83.947
51.530
29.499
1.00
24.80
C


ATOM
2589
CD2
LEU
A
469
81.920
50.538
28.421
1.00
26.30
C


ATOM
2590
N
GLN
A
470
81.092
50.285
33.018
1.00
24.81
N


ATOM
2591
CA
GLN
A
470
80.101
51.148
33.652
1.00
26.06
C


ATOM
2592
C
GLN
A
470
80.595
51.643
35.004
1.00
27.46
C


ATOM
2593
O
GLN
A
470
80.229
52.723
35.473
1.00
27.35
O


ATOM
2594
CB
GLN
A
470
78.779
50.383
33.798
1.00
25.66
C


ATOM
2595
CG
GLN
A
470
78.145
50.108
32.437
1.00
26.19
C


ATOM
2596
CD
GLN
A
470
76.907
49.240
32.484
1.00
27.08
C


ATOM
2597
OE1
GLN
A
470
76.089
49.270
31.561
1.00
28.25
O


ATOM
2598
NE2
GLN
A
470
76.768
48.452
33.537
1.00
24.83
N


ATOM
2599
N
SER
A
471
81.464
50.855
35.611
1.00
27.91
N


ATOM
2600
CA
SER
A
471
82.008
51.194
36.909
1.00
29.16
C


ATOM
2601
C
SER
A
471
83.245
52.094
36.831
1.00
28.62
C


ATOM
2602
O
SER
A
471
83.387
53.028
37.618
1.00
29.46
O


ATOM
2603
CB
SER
A
471
82.346
49.901
37.660
1.00
28.43
C


ATOM
2604
OG
SER
A
471
82.917
50.183
38.920
1.00
33.24
O


ATOM
2605
N
LYS
A
472
84.116
51.832
35.863
1.00
28.60
N


ATOM
2606
CA
LYS
A
472
85.368
52.578
35.732
1.00
28.32
C


ATOM
2607
C
LYS
A
472
85.459
53.725
34.728
1.00
27.50
C


ATOM
2608
O
LYS
A
472
86.386
54.526
34.803
1.00
26.62
O


ATOM
2609
CE
LYS
A
472
86.499
51.591
35.437
1.00
28.80
C


ATOM
2610
CG
LYS
A
472
86.598
50.469
36.445
1.00
29.70
C


ATOM
2611
CD
LYS
A
472
87.547
49.371
35.990
1.00
32.26
C


ATOM
2612
CE
LYS
A
472
88.992
49.826
35.994
1.00
33.68
C


ATOM
2613
NZ
LYS
A
472
89.910
48.692
35.671
1.00
34.81
N


ATOM
2614
N
ALA
A
473
84.523
53.811
33.789
1.00
26.86
N


ATOM
2615
CA
ALA
A
473
84.586
54.866
32.784
1.00
26.51
C


ATOM
2616
C
ALA
A
473
84.672
56.284
33.351
1.00
26.27
C


ATOM
2617
O
ALA
A
473
83.986
56.637
34.313
1.00
26.64
O


ATOM
2618
CE
ALA
A
473
83.394
54.760
31.831
1.00
26.47
C


ATOM
2619
N
LYS
A
474
85.544
57.080
32.742
1.00
25.53
N


ATOM
2620
CA
LYS
A
474
85.746
58.476
33.110
1.00
25.18
C


ATOM
2621
C
LYS
A
474
85.178
59.222
31.911
1.00
25.48
C


ATOM
2622
O
LYS
A
474
85.742
59.190
30.816
1.00
25.05
O


ATOM
2623
CE
LYS
A
474
87.237
58.749
33.293
1.00
23.52
C


ATOM
2624
CG
LYS
A
474
87.842
57.916
34.425
1.00
25.87
C


ATOM
2625
CD
LYS
A
474
89.333
57.657
34.217
1.00
24.85
C


ATOM
2626
CE
LYS
A
474
90.152
58.924
34.356
1.00
25.06
C


ATOM
2627
NZ
LYS
A
474
91.582
58.631
34.061
1.00
25.87
N


ATOM
2628
N
ILE
A
475
84.044
59.881
32.118
1.00
25.73
N


ATOM
2629
CA
ILE
A
475
83.361
60.558
31.025
1.00
25.74
C


ATOM
2630
C
ILE
A
475
83.328
62.069
31.166
1.00
25.52
C


ATOM
2631
O
ILE
A
475
82.858
62.598
32.173
1.00
25.22
O


ATOM
2632
CE
ILE
A
475
81.912
60.020
30.906
1.00
26.10
C


ATOM
2633
CG1
ILE
A
475
81.934
58.482
30.888
1.00
25.99
C


ATOM
2634
CG2
ILE
A
475
81.254
60.550
29.639
1.00
27.00
C


ATOM
2635
CD1
ILE
A
475
80.559
57.819
30.973
1.00
22.84
C


ATOM
2636
N
THR
A
476
83.833
62.766
30.154
1.00
25.28
N


ATOM
2637
CA
THR
A
476
83.839
64.220
30.199
1.00
24.69
C


ATOM
2638
C
THR
A
476
82.968
64.853
29.137
1.00
24.58
C


ATOM
2639
O
THR
A
476
82.822
64.340
28.026
1.00
23.13
O


ATOM
2640
CB
THR
A
476
85.254
64.819
30.029
1.00
24.42
C


ATOM
2641
OG1
THR
A
476
85.179
66.245
30.177
1.00
24.64
O


ATOM
2642
CG2
THR
A
476
85.817
64.506
28.641
1.00
21.62
C


ATOM
2643
N
LEU
A
477
82.392
65.985
29.504
1.00
25.11
N


ATOM
2644
CA
LEU
A
477
81.568
66.751
28.599
1.00
26.78
C


ATOM
2645
C
LEU
A
477
82.580
67.571
27.798
1.00
26.72
C


ATOM
2646
O
LEU
A
477
83.672
67.855
28.290
1.00
26.01
O


ATOM
2647
CB
LEU
A
477
80.645
67.668
29.405
1.00
27.13
C


ATOM
2648
CG
LEU
A
477
79.566
68.443
28.661
1.00
28.34
C


ATOM
2649
CD1
LEU
A
477
78.598
67.476
27.985
1.00
27.41
C


ATOM
2650
CD2
LEU
A
477
78.838
69.331
29.653
1.00
29.11
C


ATOM
2651
N
VAL
A
478
82.221
67.924
26.569
1.00
27.82
N


ATOM
2652
CA
VAL
A
478
83.075
68.708
25.678
1.00
28.66
C


ATOM
2653
C
VAL
A
478
82.407
70.062
25.415
1.00
29.15
C


ATOM
2654
O
VAL
A
478
81.186
70.143
25.327
1.00
28.79
O


ATOM
2655
CB
VAL
A
478
83.275
67.964
24.342
1.00
30.20
C


ATOM
2656
CG1
VAL
A
478
83.918
68.870
23.326
1.00
33.41
C


ATOM
2657
CG2
VAL
A
478
84.133
66.731
24.563
1.00
30.57
C


ATOM
2658
N
SER
A
479
83.200
71.121
25.288
1.00
29.64
N


ATOM
2659
CA
SER
A
479
82.645
72.455
25.054
1.00
31.24
C


ATOM
2660
C
SER
A
479
82.016
72.595
23.675
1.00
32.88
C


ATOM
2661
O
SER
A
479
82.376
71.878
22.745
1.00
32.90
O


ATOM
2662
CB
SER
A
479
83.731
73.523
25.208
1.00
28.66
C


ATOM
2663
OG
SER
A
479
84.669
73.432
24.151
1.00
29.51
O


ATOM
2664
N
SER
A
480
81.075
73.528
23.556
1.00
36.21
N


ATOM
2665
CA
SER
A
480
80.389
73.798
22.290
1.00
40.17
C


ATOM
2666
C
SER
A
480
81.393
74.060
21.172
1.00
41.93
C


ATOM
2667
O
SER
A
480
81.303
73.479
20.091
1.00
42.38
O


ATOM
2668
CB
SER
A
480
79.487
75.026
22.429
1.00
40.09
C


ATOM
2669
OG
SER
A
480
78.558
74.864
23.482
1.00
42.83
O


ATOM
2670
N
VAL
A
481
82.346
74.948
21.447
1.00
44.79
N


ATOM
2671
CA
VAL
A
481
83.377
75.316
20.483
1.00
47.03
C


ATOM
2672
C
VAL
A
481
84.169
74.125
19.958
1.00
48.55
C


ATOM
2673
O
VAL
A
481
84.514
74.083
18.778
1.00
49.15
O


ATOM
2674
CB
VAL
A
481
84.368
76.327
21.091
1.00
46.95
C


ATOM
2675
CG1
VAL
A
481
85.504
76.593
20.111
1.00
47.91
C


ATOM
2676
CG2
VAL
A
481
83.646
77.625
21.420
1.00
47.48
C


ATOM
2677
N
SER
A
482
84.466
73.168
20.832
1.00
50.46
N


ATOM
2678
CA
SER
A
482
85.219
71.982
20.438
1.00
52.74
C


ATOM
2679
C
SER
A
482
84.505
71.250
19.312
1.00
54.09
C


ATOM
2680
O
SER
A
482
85.131
70.520
18.543
1.00
54.30
O


ATOM
2681
CB
SER
A
482
85.381
71.022
21.620
1.00
52.72
C


ATOM
2682
OG
SER
A
482
86.013
71.650
22.718
1.00
55.18
O


ATOM
2683
N
ILE
A
483
83.193
71.446
19.222
1.00
55.12
N


ATOM
2684
CA
ILE
A
483
82.391
70.791
18.194
1.00
56.51
C


ATOM
2685
C
ILE
A
483
82.101
71.737
17.026
1.00
56.96
C


ATOM
2686
O
ILE
A
483
82.516
71.404
15.895
1.00
58.03
O


ATOM
2687
CB
ILE
A
483
81.063
70.276
18.792
1.00
56.37
C


ATOM
2688
CG1
ILE
A
483
81.355
69.431
20.037
1.00
56.23
C


ATOM
2689
CG2
ILE
A
483
80.304
69.450
17.763
1.00
56.35
C


ATOM
2690
CD1
ILE
A
483
80.121
69.014
20.813
1.00
56.41
C


TER
2691

ILE
A
483


















HETATM
2692
K
K
A
900
94.574
53.191
29.387
0.75
33.20
K


HETATM
2693
P
XMP

602
68.081
55.369
14.890
1.00
29.26
P


HETATM
2694
O1P
XMP

602
67.684
55.295
13.481
1.00
30.18
O


HETATM
2695
O2P
XMP

602
68.902
54.234
15.354
1.00
31.70
O


HETATM
2696
O5′
XMP

602
66.787
55.392
15.717
1.00
28.83
O


HETATM
2697
O3P
XMP

602
68.651
56.672
15.275
1.00
30.39
O


HETATM
2698
C5′
XMP

602
65.796
54.347
15.863
1.00
26.57
C


HETATM
2699
C4′
XMP

602
64.756
54.593
16.960
1.00
26.90
C


HETATM
2700
O4′
XMP

602
63.943
55.732
16.688
1.00
27.02
O


HETATM
2701
C1′
XMP

602
62.618
55.681
17.180
1.00
27.81
C


HETATM
2702
W9
XMP

602
61.690
55.9S3
16.031
1.00
28.12
N


HETATM
2703
C4
XMP

602
61.248
57.183
15.601
1.00
28.78
C


HETATM
2704
N3
XMP

602
61.556
58.444
16.121
1.00
29.01
N


HETATM
2705
N1
XMP

602
60.086
59.258
14.353
1.00
29.05
N


HETATM
2706
C2
XMP

602
60.942
59.481
15.459
1.00
30.77
C


HETATM
2707
O2
XMP

602
61.128
60.639
15.829
1.00
31.42
O


HETATM
2708
C6
XMP

602
59.764
57.989
13.811
1.00
27.88
C


HETATM
2709
O6
XMP

602
59.015
57.875
12.853
1.00
28.97
O


HETATM
2710
C5
XMP

602
60.406
56.909
14.506
1.00
28.31
C


HETATM
2711
N7
XMP

602
60.325
55.573
14.268
1.00
27.77
N


HETATM
2712
C8
XMP

602
61.076
55.082
15.166
1.00
27.54
C


HETATM
2713
C2′
XMP

602
62.604
54.298
17.878
1.00
26.62
C


HETATM
2714
O2′
XMP

602
62.808
54.554
19.261
1.00
26.73
O


HETATM
2715
C3′
XMP

602
63.705
53.537
17.141
1.00
26.75
C


HETATM
2716
O3′
XMP

602
64.161
52.438
17.926
1.00
26.88
O


HETATM
2717
C1
MOA

600
60.161
58.910
19.598
1.00
39.69
C


HETATM
2718
C2
MOA

600
55.659
56.950
16.499
1.00
41.87
C


HETATM
2719
C3
MOA

600
54.526
56.264
16.209
1.00
42.80
C


HETATM
2720
C4
MOA

600
53.214
56.947
16.563
1.00
43.33
C


HETATM
2721
C5
MOA

600
52.615
56.311
17.824
1.00
44.46
C


HETATM
2722
C6
MOA

600
53.260
56.803
19.110
1.00
45.19
C


HETATM
2723
C7
MOA

600
59.586
54.022
20.007
1.00
38.55
C


HETATM
2724
C8
MOA

600
56.536
53.702
18.367
1.00
39.77
C


HETATM
272S
C9
MOA

600
54.498
54.877
15.549
1.00
42.56
C


HETATM
2726
C10
MOA

600
60.713
56.925
20.765
1.00
38.97
C


HETATM
2727
C11
MOA

600
59.765
56.576
19.638
1.00
38.97
C


HETATM
2728
C12
MOA

600
59.227
55.285
19.257
1.00
38.94
C


HETATM
2729
C13
MOA

600
58.328
55.252
18.116
1.00
38.60
C


HETATM
2730
C14
MOA

600
58.002
56.474
17.412
1.00
39.76
C


HETATM
2731
C15
MOA

600
58.558
57.736
17.831
1.00
39.72
C


HETATM
2732
C16
MOA

600
59.443
57.754
18.951
1.00
39.74
C


HETATM
2733
C17
MOA

600
57.066
56.441
16.206
1.00
41.19
C


HETATM
2734
O1
MOA

600
60.164
60.070
19.326
1.00
40.10
O


HETATM
2735
O2
MOA

600
60.857
58.377
20.607
1.00
39.52
O


HETATM
2736
O3
MOA

600
57.806
54.039
17.729
1.00
38.84
O


HETATM
2737
O4
MOA

600
58.226
58.894
17.131
1.00
41.40
O


HETATM
2738
O5
MOA

600
53.221
58.031
19.364
1.00
46.62
O


HETATM
2739
O6
MOA

600
53.815
55.961
19.854
1.00
44.12
O


HETATM
2740
O
HOH

1
61.376
37.927
37.348
1.00
48.46
O


HETATM
2741
O
HOH

2
66.118
60.676
24.768
1.00
20.39
O


NETATM
2742
O
HOH

3
57.906
58.970
28.360
1.00
26.84
O


HETATM
2743
O
HOH

4
66.772
48.007
38.757
1.00
2S.49
O


HETATM
2744
O
HOH

5
87.612
55.755
31.226
1.00
23.33
O


NETATM
2745
O
HOH

6
79.992
42.156
29.537
1.00
21.25
O


HETATM
2746
O
HOH

7
59.636
45.401
36.922
1.00
29.33
O


NETATM
2747
O
HOH

8
71.079
54.650
21.993
1.00
25.95
O


HETATM
2748
O
HOH

9
75.154
45.933
32.815
1.00
29.51
O


HETATM
2749
O
HOH

10
84.715
43.023
9.513
1.00
52.28
O


NETATM
2750
O
HOH

11
78.040
54.255
34.365
1.00
26.73
O


HETATM
2751
O
HOH

12
56.541
77.341
37.146
1.00
29.92
O


NETATM
2752
O
HOH

13
71.260
53.575
14.099
1.00
27.29
O


HETATM
2753
O
HOH

14
76.501
44.082
31.079
1.00
23.02
O


HETATM
2754
O
HOH

15
56.998
79.001
34.463
1.00
24.15
O


HETATM
2755
O
HOH

16
73.891
57.573
36.189
1.00
25.33
O


HETATM
2756
O
HOH

17
79.049
48.291
37.245
1.00
34.20
O


HETATM
2757
O
HOH

18
84.628
53.459
21.080
1.00
24.55
O


HETATM
2758
O
HOH

19
60.274
50.551
20.190
1.00
29.66
O


HETATM
2759
O
HOH

20
88.720
54.039
33.349
1.00
25.23
O


HETATM
2760
O
HOH

21
72.841
38.348
33.765
1.00
30.16
O


HETATM
2761
O
HOH

22
66.292
58.791
21.349
1.00
29.06
O


HETATM
2762
O
HOH

23
67.212
67.480
30.959
1.00
23.37
O


HETATM
2763
O
HOH

24
64.926
73.569
32.978
1.00
27.92
O


HETATM
2764
O
HOH

25
74.543
60.063
37.886
1.00
37.97
O


HETATM
2765
O
HOH

26
70.536
33.662
27.436
1.00
32.78
O


HETATM
2766
O
HOH

27
49.672
44.473
20.960
1.00
32.61
O


HETATM
2767
O
HOH

28
82.525
67.407
31.912
1.00
36.84
O


HETATM
2768
O
HOH

29
62.576
38.739
33.869
1.00
27.93
O


HETATM
2769
O
HOH

30
65.657
36.916
34.650
1.00
31.90
O


HETATM
2770
O
HOH

31
77.268
36.846
6.578
1.00
54.28
O


HETATM
2771
O
HOH

32
53.069
53.133
19.199
1.00
50.49
O


HETATM
2772
O
HOH

33
76.732
41.427
32.285
1.00
26.63
O


HETATM
2773
O
HOH

34
59.082
42.334
5.797
1.00
52.93
O


HETATM
2774
O
HOH

35
75.506
39.010
8.246
1.00
30.82
O


HETATM
2775
O
HOH

36
69.343
68.054
32.924
1.00
32.47
O


HETATM
2776
O
HOH

37
64.457
56.749
20.210
1.00
32.67
O


HETATM
2777
O
HOH

38
62.747
61.776
37.438
1.00
35.12
O


HETATM
2778
O
HOH

39
73.816
64.979
30.707
1.00
34.05
O


HETATM
2779
O
HOH

40
64.885
41.594
7.798
1.00
30.67
O


HETATM
2780
O
HOH

41
87.291
69.760
24.178
1.00
33.68
O


HETATM
2781
O
HOH

42
63.521
39.537
6.109
1.00
44.37
O


HETATM
2782
O
HOH

43
65.271
63.920
35.809
1.00
34.06
O


HETATM
2783
O
HOH

44
56.965
57.545
38.806
1.00
37.58
O


HETATM
2784
O
HOH

45
79.547
40.499
32.022
1.00
37.32
O


HETATM
2785
O
HOH

46
60.019
51.355
9.831
1.00
30.80
O


HETATM
2786
O
HOH

47
61.960
50.701
17.845
1.00
28.12
O


HETATM
2787
O
HOH

48
74.307
50.935
36.302
1.00
32.12
O


HETATM
2788
O
HOH

49
48.640
54.380
36.947
1.00
38.70
O


HETATM
2789
O
HOH

50
53.284
51.835
37.998
1.00
35.47
O


HETATM
2790
O
HOH

51
51.464
58.781
25.814
1.00
42.15
O


HETATM
2791
O
HOH

52
66.312
31.378
26.604
1.00
42.30
O


HETATM
2792
O
HOH

53
51.114
46.450
35.768
1.00
39.78
O


HETATM
2793
O
HOH

54
72.161
53.847
44.046
1.00
49.25
O


HETATM
2794
O
HOH

55
68.174
38.435
46.467
1.00
39.10
O


HETATM
2795
O
HOH

56
62.329
64.325
35.245
1.00
31.82
O


HETATM
2796
O
HOH

57
56.533
41.432
37.289
1.00
42.75
O


HETATM
2797
O
HOH

58
60.631
39.846
6.689
1.00
42.47
O


HETATM
2798
O
HOH

59
54.566
73.818
39.035
1.00
35.31
O


HETATM
2799
O
HOH

60
60.006
59.911
30.562
1.00
39.12
O


HETATM
2800
O
HOH

61
93.037
49.413
23.367
1.00
39.58
O


HETATM
2801
O
HOH

62
78.413
51.159
38.006
1.00
44.41
O


HETATM
2802
O
HOH

63
66.743
37.946
16.658
1.00
31.22
O


HETATM
2803
O
HOH

64
61.454
73.868
39.323
1.00
45.74
O


HETATM
2804
O
HOH

65
52.424
53.998
25.927
1.00
36.17
O


HETATM
2805
O
HOH

66
59.056
45.472
5.839
1.00
44.80
O


HETATM
2806
O
HOH

67
71.714
56.136
41.913
1.00
33.23
O


HETATM
2807
O
HOH

68
92.961
54.326
36.232
1.00
47.69
O


HETATM
2808
O
HOH

69
82.193
63.483
21.263
1.00
31.53
O


HETATM
2809
O
HOH

70
80.771
49.496
10.878
1.00
59.85
O


HETATM
2810
O
HOH

71
50.884
32.054
16.328
1.00
46.83
O


HETATM
2811
O
HOH

72
43.572
44.049
23.478
1.00
40.54
O


HETATM
2812
O
HOH

73
79.532
38.613
17.574
1.00
40.24
O


HETATM
2813
O
HOH

74
94.403
49.046
26.001
1.00
45.47
O


HETATM
2814
O
HOH

75
59.694
51.808
16.401
1.00
31.05
O


HETATM
2815
O
HOH

76
72.250
67.511
32.157
1.00
37.70
O


HETATM
2816
O
HOH

77
62.657
53.868
−3.472
1.00
54.27
O


HETATM
2817
O
HOH

78
51.622
50.791
21.993
1.00
42.86
O


HETATM
2818
O
HOH

79
92.002
50.835
35.387
1.00
48.05
O


HETATM
2819
O
HOH

80
59.267
38.498
34.638
1.00
33.40
O


HETATM
2820
O
HOH

81
90.144
53.498
35.941
1.00
39.87
O


HETATM
2821
O
HOH

82
78.700
70.970
25.462
1.00
45.50
O


HETATM
2822
O
HOH

83
75.528
70.617
31.893
1.00
36.82
O


HETATM
2823
O
HOH

84
58.864
51.527
22.923
1.00
41.16
O


HETATM
2824
O
HOH

85
85.509
49.375
39.516
1.00
46.27
O


HETATM
2825
O
HOH

86
75.401
39.056
31.150
1.00
35.14
O


HETATM
2826
O
HOH

87
75.010
37.307
10.676
1.00
38.37
O


HETATM
2827
O
HOH

88
91.471
42.227
35.142
1.00
46.93
O


HETATM
2828
O
HOH

89
49.032
57.262
26.680
1.00
45.04
O


HETATM
2829
O
HOH

90
58.819
35.855
26.787
1.00
33.51
O


HETATM
2830
O
HOH

91
66.610
35.147
36.987
1.00
41.70
O


HETATM
2831
O
HOH

92
66.423
29.073
14.771
1.00
36.38
O


HETATM
2832
O
HOH

93
50.205
43.386
7.840
1.00
48.37
O


HETATM
2833
O
HOH

94
69.770
36.084
7.610
1.00
43.71
O


HETATM
2834
O
HOH

95
56.434
31.334
8.824
1.00
51.14
O


HETATM
2835
O
HOH

96
68.525
59.191
7.595
1.00
57.38
O


HETATM
2836
O
HOH

97
68.856
74.797
33.274
1.00
45.02
O


HETATM
2837
O
HOH

98
45.466
44.918
32.864
1.00
44.79
O


HETATM
2838
O
HOH

99
73.439
40.590
41.918
1.00
43.45
O


HETATM
2839
O
HOH

100
82.331
76.466
24.096
1.00
49.31
O


HETATM
2840
O
HOH

101
63.989
58.544
43.317
1.00
49.06
O


HETATM
2841
O
HOH

102
52.822
30.334
14.629
1.00
50.72
O


HETATM
2842
O
HOH

103
69.162
44.078
0.587
1.00
44.93
O


HETATM
2843
O
HOH

104
57.966
65.984
38.109
1.00
50.45
O


HETATM
2844
O
HOH

105
61.009
30.223
22.762
1.00
54.86
O


HETATM
2845
O
HOH

106
92.696
40.912
20.325
1.00
51.59
O


HETATM
2846
O
HOH

107
83.364
55.951
16.129
1.00
38.90
O


HETATM
2847
O
HOH

108
80.747
50.654
40.836
1.00
49.94
O


HETATM
2848
O
HOH

109
55.067
32.734
36.953
1.00
52.02
O


HETATM
2849
O
HOH

110
61.338
24.112
16.927
1.00
75.61
O


HETATM
2850
O
HOH

111
55.363
51.236
15.584
1.00
50.23
O


HETATM
2851
O
HOH

112
86.105
39.380
22.608
1.00
43.92
O


HETATM
2852
O
HOH

113
65.590
61.745
38.398
1.00
44.21
O


HETATM
2853
O
HOH

114
76.005
54.691
−0.953
1.00
60.80
O


HETATM
2854
O
HOH

115
63.472
78.599
34.826
1.00
49.03
O


HETATM
2855
O
HOH

116
56.584
48.288
14.849
1.00
40.92
O


HETATM
2856
O
HOH

117
74.848
29.487
24.069
1.00
48.29
O


HETATM
2857
O
HOH

118
60.786
51.033
45.907
1.00
58.58
O


HETATM
2858
O
HOH

119
63.463
59.191
18.549
1.00
40.51
O


HETATM
2859
O
HOH

120
64.003
26.220
24.484
1.00
50.15
O


HETATM
2860
O
HOH

121
58.655
37.671
5.381
1.00
53.24
O


HETATM
2861
O
HOH

122
63.615
31.933
25.497
1.00
40.97
O


HETATM
2862
O
HOH

123
65.616
76.381
33.672
1.00
46.89
O


HETATM
2863
O
HOH

124
55.158
44.415
39.591
1.00
56.77
O


HETATM
2864
O
HOH

125
75.132
48.039
35.838
1.00
43.66
O


HETATM
2865
O
HOH

126
65.816
28.316
26.676
1.00
42.04
O


HETATM
2866
O
HOH

127
54.208
52.470
12.608
1.00
47.30
O


HETATM
2867
O
HOH

128
53.242
30.460
11.276
1.00
68.84
O


HETATM
2868
O
HOH

129
60.726
33.090
34.181
1.00
47.71
O


HETATM
2869
O
HOH

130
64.010
40.397
3.202
1.00
52.21
O


HETATM
2870
O
HOH

131
77.504
52.228
0.017
1.00
50.80
O


HETATM
2871
O
HOH

132
69.804
61.883
38.293
1.00
46.95
O


HETATM
2872
O
HOH

133
45.792
41.736
13.068
1.00
47.40
O


HETATM
2873
O
HOH

134
50.939
33.262
11.744
1.00
43.38
O


HETATM
2874
O
HOH

135
76.312
35.442
27.267
1.00
53.79
O


HETATM
2875
O
HOH

136
62.510
56.249
46.266
1.00
55.19
O


HETATM
2876
O
HOH

137
73.706
35.590
8.247
1.00
48.59
O


HETATM
2877
O
HOH

138
66.547
78.277
31.624
1.00
74.03
O


HETATM
2878
O
HOH

139
64.392
81.457
33.669
1.00
49.54
O


HETATM
2879
O
HOH

140
61.558
64.657
38.228
1.00
56.05
O


HETATM
2880
O
HOH

141
96.215
46.485
27.601
1.00
49.93
O


HETATM
2881
O
HOH

142
61.787
33.565
27.109
1.00
49.84
O


HETATM
2882
O
HOH

143
52.202
49.654
40.025
1.00
57.52
O


HETATM
2883
O
HOH

144
65.216
31.604
29.511
1.00
59.80
O


HETATM
2884
O
HOH

145
69.153
31.657
25.777
1.00
57.79
O


HETATM
2885
O
HOH

146
60.092
41.511
39.950
1.00
50.45
O


HETATM
2886
O
HOH

147
74.800
33.112
28.850
1.00
67.42
O


HETATM
2887
O
HOH

148
62.654
33.516
30.073
1.00
62.16
O


HETATM
2888
O
HOH

149
71.897
32.924
29.976
1.00
50.48
O


HETATM
2889
O
HOH

150
56.804
34.357
25.133
1.00
46.97
O


HETATM
2890
O
HOH

151
73.224
33.332
26.044
1.00
49.98
O


HETATM
2891
O
HOH

152
62.549
28.935
25.883
1.00
63.89
O


HETATM
2892
O
HOH

153
72.526
31.533
23.597
1.00
46.02
O


HETATM
2893
O
HOH

154
55.400
54.063
40.193
1.00
51.55
O


HETATM
2894
O
HOH

155
56.260
50.851
2.415
1.00
59.29
O


HETATM
2895
O
HOH

156
59.029
24.830
22.198
1.00
60.82
O


HETATM
2896
O
HOH

157
65.228
26.246
14.456
1.00
42.42
O


HETATM
2897
O
HOH

158
74.086
29.603
13.669
1.00
44.88
O


HETATM
2898
O
HOH

159
71.012
57.900
14.425
1.00
49.16
O


HETATM
2899
O
HOH

160
76.443
52.766
36.176
1.00
32.86
O


HETATM
2900
O
HOH

161
74.501
55.579
38.525
1.00
43.80
O


HETATM
2901
O
HOH

162
68.390
53.333
47.198
1.00
57.30
O


HETATM
2902
O
HOH

163
66.068
54.957
48.273
1.00
52.03
O


HETATM
2903
O
HOH

164
90.274
44.981
34.515
1.00
42.74
O


HETATM
2904
O
HOH

165
92.357
46.800
32.648
1.00
50.13
O


HETATM
2905
O
HOH

166
87.411
55.494
37.249
1.00
49.75
O


HETATM
2906
O
HOH

167
65.234
66.995
39.283
1.00
56.66
O


HETATM
2907
O
HOH

168
75.023
62.880
19.374
1.00
43.60
O


HETATM
2908
O
HOH

169
49.785
54.078
24.384
1.00
56.06
O


HETATM
2909
O
HOH

170
93.198
47.611
19.693
1.00
57.65
O


HETATM
2910
O
HOH

171
69.700
45.410
46.557
1.00
42.35
O


HETATM
2911
O
HOH

172
66.820
41.422
2.567
1.00
50.29
O


HETATM
2912
O
HOH

173
87.119
47.913
13.662
1.00
52.23
O


HETATM
2913
O
HOH

174
72.571
61.611
21.232
1.00
34.11
O


HETATM
2914
O
HOH

175
81.561
38.698
24.061
1.00
46.29
O


HETATM
2915
O
HOH

176
70.615
32.679
38.298
1.00
45.72
O


HETATM
2916
O
HOH

177
53.945
58.607
38.141
1.00
50.80
O


HETATM
2917
O
HOH

178
69.562
62.885
21.604
1.00
28.51
O


HETATM
2918
O
HOH

179
69.716
68.855
36.042
1.00
48.11
O


HETATM
2919
O
HOH

180
67.633
69.270
38.272
1.00
45.15
O













CONECT
202
2519






CONECT
2519
202


CONECT
2693
2694
2695
2696
2697


CONECT
2694
2693


CONECT
2695
2693


CONECT
2696
2693
2698


CONECT
2697
2693


CONECT
2698
2696
2699


CONECT
2699
2698
2700
2715


CONECT
2700
2699
2701


CONECT
2701
2700
2702
2713


CONECT
2702
2701
2703
2712


CONECT
2703
2702
2704
2710


CONECT
2704
2703
2706


CONECT
2705
2706
2708


CONECT
2706
2704
2705
2707


CONECT
2707
2706


CONECT
2708
2705
2709
2710


CONECT
2709
2708


CONECT
2710
2703
2708
2711


CONECT
2711
2710
2712


CONECT
2712
2702
2711


CONECT
2713
2701
2714
2715


CONECT
2714
2713


CONECT
2715
2699
2713
2716


CONECT
2716
2715


CONECT
2717
2732
2734
2735


CONECT
2718
2719
2733


CONECT
2719
2718
2720
2725


CONECT
2720
2719
2721


CONECT
2721
2720
2722


CONECT
2722
2721
2738
2739


CONECT
2723
2728


CONECT
2724
2736


CONECT
2725
2719


CONECT
2726
2727
2735


CONECT
2727
2726
2728
2732


CONECT
2728
2723
2727
2729


CONECT
2729
2728
2730
2736


CONECT
2730
2729
2731
2733


CONECT
2731
2730
2732
2737


CONECT
2732
2717
2727
2731


CONECT
2733
2718
2730


CONECT
2734
2717


CONECT
2735
2717
2726


CONECT
2736
2724
2729


CONECT
2737
2731


CONECT
2738
2722


CONECT
2739
2722




















MASTER
550
0
3
14
18
0
0
6
2918
1
49
39



END


FIG. 13


P-UC 5440


Page 21


















TABLE 5







HEADER
OXIDOREDUCTASE
08-AUG-02 1MEW








TITLE
INOSINE MONOPHOSPHATE DEHYDROGENASE (IMPDH) FROM









TITLE
2
TRITRICHOMONAS FOETUS WITH XMP AND NAD BOUND


COMPND

MOL_ID: 1;


COMPND
2
MOLECULE: INOSINE-5′-MONOPHOSPHATE DEHYDROGENASE;


COMPND
3
CHAIN: A;


COMPND
4
SYNONYM: IMP DEHYDROGENASE, IMPDH;


COMPND
5
EC: 1.1.1.205;


COMPND
6
ENGINEERED: YES


SOURCE

MOL_ID: 1;


SOURCE
2
ORGANISM_SCIENTIFIC: TRITRICHOMONAS FOETUS;


SOURCE
3
GENE: IMPDH;


SOURCE
4
EXPRESSION_SYSTEM: ESCHERICHIA COLI;


SOURCE
5
EXPRESSION_SYSTEM_COMMON: BACTERIA;


SOURCE
6
EXPRESSION_SYSTEM_STRAIN: H712;


SOURCE
7
EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;


SOURCE
8
EXPRESSION_SYSTEM_PLASMID: PEACE


KEYWDS

ALPHA BETA BARREL


EXPDTA

X-RAY DIFFRACTION


AUTHOR

G.L. PROSISE, H. LUECKE











JRNL

AUTH

G.L. PROSISE, H. LUECKE


JRNL

TITL

CRYSTAL STRUCTURE OF T. FOETUS INOSINE


JRNL

TITL
2
MONOPHOSPHATE DEHYDROGENASE IN COMPLEX WITH


JRNL

TITL
3
SUBSTRATE, COFACTOR, AND ANALOGS: STRUCTURAL BASIS


JRNL

TITL
4
FOR THE RANDOM-IN ORDERED-OUT KINETIC MECHANISM


JRNL

REF

TO BE PUBLISHED


JRNL

REFN









REMARK
1



REMARK
2


REMARK
2
RESOLUTION. 2.15 ANGSTROMS.


REMARK
3


REMARK
3
REFINEMENT.










REMARK
3
PROGRAM
: CNS 1.1


REMARK
3
AUTHORS
: BRUNGER, ADAMS, CLORE, DELANO, GROS, GROSSE-


REMARK
3

: KUNSTLEVE, JIANG, KUSZEWSKI, NILGES, PANNU,


REMARK
3

: READ, RICE, SIMONSON, WARREN


REMARK
3









REMARK
3
REFINEMENT TARGET : ENGH & HUBER


REMARK
3


REMARK
3
DATA USED IN REFINEMENT.










REMARK
3
RESOLUTION RANGE HIGH (ANGSTROMS)
: 2.15


REMARK
3
RESOLUTION RANGE LOW (ANGSTROMS)
: 29.61


REMARK
3
DATA CUTOFF (SIGMA(F))
: 0.000


REMARK
3
OUTLIER CUTOFF HIGH (RMS(ABS(F)))
: NULL


REMARK
3
COMPLETENESS (WORKING+TEST) (%)
: 98.3


REMARK
3
NUMBER OF REFLECTIONS
: 33857


REMARK
3


REMARK
3
FIT TO DATA USED IN REFINEMENT.


REMARK
3
CROSS-VALIDATION METHOD
: THROUGHOUT


REMARK
3
FREE R VALUE TEST SET SELECTION
: RANDOM


REMARK
3
R VALUE (WORKING SET)
: 0.224


REMARK
3
FREE R VALUE
: 0.246


REMARK
3
FREE R VALUE TEST SET SIZE (%)
: 5.200


REMARK
3
FREE R VALUE TEST SET COUNT
: 1768


REMARK
3
ESTIMATED ERROR OF FREE R VALUE
: 0.006


REMARK
3


REMARK
3
FIT IN THE HIGHEST RESOLUTION BIN.


REMARK
3
TOTAL NUMBER OF BINS USED
: 6


REMARK
3
BIN RESOLUTION RANGE HIGH (A)
: 2.15


REMARK
3
BIN RESOLUTION RANGE LOW (A)
: 2.28


REMARK
3
BIN COMPLETENESS (WORKING+TEST) (%)
: 95.80


REMARK
3
REFLECTIONS IN BIN (WORKING SET)
: 5092


REMARK
3
BIN R VALUE (WORKING SET)
: 0.2580


REMARK
3
BIN FREE R VALUE
: 0.2840


REMARK
3
BIN FREE R VALUE TEST SET SIZE (%)
: 5.00


REMARK
3
BIN FREE R VALUE TEST SET COUNT
: 270


REMARK
3
ESTIMATED ERROR OF BIN FREE R VALUE
: 0.017


REMARK
3









REMARK
3
NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.










REMARK
3
PROTEIN ATOMS
: 2635


REMARK
3
NUCLEIC ACID ATOMS
: 0


REMARK
3
HETEROGEN ATOMS
: 69


REMARK
3
SOLVENT ATOMS
: 164


REMARK
3


REMARK
3
B VALUES.


REMARK
3
FROM WILSON PLOT (A**2)
: 28.80


REMARK
3
MEAN B VALUE (OVERALL, A**2)
: 36.10


REMARK
3
OVERALL ANISOTROPIC B VALUE.










REMARK
3
B11 (A**2)
: 0.00000


REMARK
3
B22 (A**2)
: 0.00000


REMARK
3
B33 (A**2)
: 0.00000


REMARK
3
B12 (A**2)
: 0.00000


REMARK
3
B13 (A**2)
: 0.00000


REMARK
3
B23 (A**2)
: 0.00000


REMARK
3










REMARK
3
ESTIMATED COORDINATE ERROR.



REMARK
3
ESD FROM LUZZATI PLOT
(A) : 0.26


REMARK
3
ESD FROM SIGMAA
(A) : 0.22


REMARK
3
LOW RESOLUTION CUTOFF
(A) : 5.00


REMARK
3









REMARK
3
CROSS-VALIDATED ESTIMATED COORDINATE ERROR.










REMARK
3
ESO FROM C-V LUZZATI PLOT
(A) : 0.30


REMARK
3
ESD FROM C-V SIGMAA
(A) : 0.28


REMARK
3


REMARK
3
RMS DEVIATIONS FROM IDEAL VALUES.


REMARK
3
BOND LENGTHS
   (A) : 0.006


REMARK
3
BOND ANGLES
(DEGREES) : 1.20


REMARK
3
DIHEDRAL ANGLES
(DEGREES) : 22.90


REMARK
3
IMPROPER ANGLES
(DEGREES) : 0.77


REMARK
3


REMARK
3
ISOTROPIC THERMAL MODEL : RESTRAINED


REMARK
3











REMARK
3
ISOTROPIC THERMAL FACTOR RESTRAINTS.
RMS
SIGMA


REMARK
3
MAIN-CHAIN BOND
(A**2) : 0.780 ;
1.500


REMARK
3
MAIN-CHAIN ANGLE
(A**2) : 1.410 ;
2.000


REMARK
3
SIDE-CHAIN BOND
(A**2) : 0.900 ;
2.000


REMARK
3
SIDE-CHAIN ANGLE
(A**2) : 1.480 ;
2.500


REMARK
3










REMARK
3
BULK SOLVENT MODELING.



REMARK
3
METHOD USED
: FLAT MODEL


REMARK
3
KSOL
: 0.38


REMARK
3
ESOL
: 41.94


REMARK
3


REMARK
3
NCS MODEL
: NULL


REMARK
3











REMARK
3
NCS RESTRAINTS.
RMS
SIGMA/WEIGHT


REMARK
3
GROUP 1 POSITIONAL (A)
: NULL ;
NULL


REMARK
3
GROUP 1 B-FACTOR (A**2)
: NULL ;
NULL










REMARK
3




REMARK
3
PARAMETER FILE 1
: PROTEIN_REP.PARAM


REMARK
3
PARAMETER FILE 2
: PARAM.GNSOL


REMARK
3
PARAMETER FILE 3
: CIS_PEPTIDE.PARAM


REMARK
3
PARAMETER FILE 4
: XMPG.PAR


REMARK
3
PARAMETER FILE 5
: NAD_PROD.PAR


REMARK
3
PARAMETER FILE 6
: NULL


REMARK
3
TOPOLOGY FILE 1
: PROTEIN.TOP


REMARK
3
TOPOLOGY FILE 2
: XMPG.TOP


REMARK
3
TOPOLOGY FILE 3
: NAD_PROD.TOP


REMARK
3
TOPOLOGY FILE 4
: ION.TOP


REMARK
3
TOPOLOGY FILE 5
: TOPH.GNSOL


REMARK
3
TOPOLOGY FILE 6
: NULL


REMARK
3









REMARK
3
OTHER REF INEMENT REMARKS: NULL


REMARK
4


REMARK
4
1MEW COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998


REMARK
100


REMARK
100
THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-AUG-2002.


REMARK
100
THE RCSB ID CODE IS RCSB016859.


REMARK
200


REMARK
200
EXPERIMENTAL DETAILS










REMARK
200
EXPERIMENT TYPE
: X-RAY DIFFRACTION


REMARK
200
DATE OF DATA COLLECTION
: 01-NOV-2000


REMARK
200
TEMPERATURE (KELVIN)
: 100.0


REMARK
200
PH
: 7.50


REMARK
200
NUMBER OF CRYSTALS USED
: 1


REMARK
200


REMARK
200
SYNCHROTRON (Y/N)
: Y


REMARK
200
RADIATION SOURCE
: ALS


REMARK
200
BEAMLINE
: 5.0.2


REMARK
200
X-RAY GENERATOR MODEL
: NULL


REMARK
200
MONOCHROMATIC OR LAUE (M/L)
: M


REMARK
200
WAVELENGTH OR RANGE (A)
: 1.00


REMARK
200
MONOCHROMATOR
: NULL


REMARK
200
OPTICS
: NULL


REMARK
200


REMARK
200
DETECTOR TYPE
: CCD


REMARK
200
DETECTOR MANUFACTURER
: ADSC QUANTUM 4


REMARK
200
INTENSITY-INTEGRATION SOFTWARE
: DENZO


REMARK
200
DATA SCALING SOFTWARE
: SCALEPACK


REMARK
200


REMARK
200
NUMBER OF UNIQUE REFLECTIONS
: 33857


REMARK
200
RESOLUTION RANGE HIGH (A)
: 2.150


REMARK
200
RESOLUTION RANGE LOW (A)
: 50.000


REMARK
200
REJECTION CRITERIA (SIGMA(I))
: 0.000


REMARK
200


REMARK
200
OVERALL.


REMARK
200
COMPLETENESS FOR RANGE (%)
: 98.4


REMARK
200
DATA REDUNDANCY
: 5.400


REMARK
200
R MERGE (I)
: 0.08000


REMARK
200
R SYM (I)
: NULL


REMARK
200
<I/SIGMA(I)> FOR THE DATA SET
: 19.0000


REMARK
200


REMARK
200
IN THE HIGHEST RESOLUTION SHELL.


REMARK
200
HIGHEST RESOLUTION SHELL, RANGE HIGH
(A) : 2.15


REMARK
200
HIGHEST RESOLUTION SHELL, RANGE LOW
(A) : 2.19


REMARK
200
COMPLETENESS FOR SHELL (%)
: 95.9


REMARK
200
DATA REDUNDANCY IN SHELL
: NULL


REMARK
200
R MERGE FOR SHELL (I)
: 0.58000


REMARK
200
R SYM FOR SHELL (I)
: NULL


REMARK
200
<I/SIGMA(I)> FOR SHELL
: 2.200


REMARK
200









REMARK
200
DIFFRACTION PROTOCOL: SINGLE WAVELENGTH


REMARK
200
METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS


REMARK
200
SOFTWARE USED: CNS


REMARK
200
STARTING MODEL: PDB ENTRY 1AK5


REMARK
200


REMARK
200
REMARK: NULL


REMARK
280


REMARK
280
CRYSTAL


REMARK
280
SOLVENT CONTENT, VS (%) : NULL


REMARK
280
MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA) : NULL


REMARK
280


REMARK
280
CRYSTALLIZATION CONDITIONS: SODIUM MALONATE, TRIS, 2-


REMARK
280
MERCAPTOETHANOL, EDTA, GLYCEROL


REMARK
290


REMARK
290
CRYSTALLOGRAPHIC SYMMETRY


REMARK
290
SYMMETRY OPERATORS FOR SPACE GROUP: P 4 3 2


REMARK
290











REMARK
290

SYMOP
SYMMETRY


REMARK
290

NNNMMM
OPERATOR


REMARK
290

1555
X, Y, Z


REMARK
290

2555
X, −Y, Z


REMARK
290

3555
−X, Y, −Z


REMARK
290

4555
X, −Y, −Z


REMARK
290

5555
Z, X, Y


REMARK
290

6555
Z, −X, −Y


REMARK
290

7555
−Z, −X, Y


REMARK
290

8555
−Z, X, −Y


REMARK
290

9555
Y, Z, X


REMARK
290

10555
−Y, Z, −X


REMARK
290

11555
Y, −Z, −X


REMARK
290

12555
−Y, −Z, X


REMARK
290

13555
Y, X, −Z


REMARK
290

14555
−Y, −X, −Z


REMARK
290

15555
Y, −X, Z


REMARK
290

16555
−Y, X, Z


REMARK
290

17555
X, Z, −Y


REMARK
290

18555
−X, Z, Y


REMARK
290

19555
−X, −Z, −Y


REMARK
290

20555
X, −Z, Y


REMARK
290

21555
Z, Y, −X


REMARK
290

22555
Z, −Y, X


REMARK
290

23555
−Z, Y, X


REMARK
290

24555
−Z, −Y, −X


REMARK
290










REMARK
290
WHERE
NNN -> OPERATOR NUMBER


REMARK
290

MMM -> TRANSLATION VECTOR


REMARK
290









REMARK
290
CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS


REMARK
290
THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM


REMARK
290
RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY


REMARK
290
RELATED MOLECULES.














REMARK
290
SMTRY1
1
1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY2
1
0.000000
1.000000
0.000000
0.00000


REMARK
290
SMTRY3
1
0.000000
0.000000
1.000000
0.00000


REMARK
290
SMTRY1
2
−1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY2
2
0.000000
−1.000000
0.000000
0.00000


REMARK
290
SMTRY3
2
0.000000
0.000000
1.000000
0.00000


REMARK
290
SMTRY1
3
−1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY2
3
0.000000
1.000000
0.000000
0.00000


REMARK
290
SMTRY3
3
0.000000
0.000000
−1.000000
0.00000


REMARK
290
SMTRY1
4
1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY2
4
0.000000
−1.000000
0.000000
0.00000


REMARK
290
SMTRY3
4
0.000000
0.000000
−1.000000
0.00000


REMARK
290
SMTRY1
5
0.000000
0.000000
1.000000
0.00000


REMARK
290
SMTRY2
5
1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY3
5
0.000000
1.000000
0.000000
0.00000


REMARK
290
SMTRY1
6
0.000000
0.000000
1.000000
0.00000


REMARK
290
SMTRY2
6
−1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY3
6
0.000000
−1.000000
0.000000
0.00000


REMARK
290
SMTRY1
7
0.000000
0.000000
−1.000000
0.00000


REMARK
290
SMTRY2
7
−1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY3
7
0.000000
1.000000
0.000000
0.00000


REMARK
290
SMTRY1
8
0.000000
0.000000
−1.000000
0.00000


REMARK
290
SMTRY2
8
1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY3
8
0.000000
−1.000000
0.000000
0.00000


REMARK
290
SMTRY1
9
0.000000
1.000000
0.000000
0.00000


REMARK
290
SMTRY2
9
0.000000
0.000000
1.000000
0.00000


REMARK
290
SMTRY3
9
1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY1
10
0.000000
−1.000000
0.000000
0.00000


REMARK
290
SMTRY2
10
0.000000
0.000000
1.000000
0.00000


REMARK
290
SMTRY3
10
−1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY1
11
0.000000
1.000000
0.000000
0.00000


REMARK
290
SMTRY2
11
0.000000
0.000000
−1.000000
0.00000


REMARK
290
SMTRY3
11
−1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY1
12
0.000000
−1.000000
0.000000
0.00000


REMARK
290
SMTRY2
12
0.000000
0.000000
−1.000000
0.00000


REMARK
290
SMTRY3
12
1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY1
13
0.000000
1.000000
0.000000
0.00000


REMARK
290
SMTRY2
13
1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY3
13
0.000000
0.000000
−1.000000
0.00000


REMARK
290
SMTRY1
14
0.000000
−1.000000
0.000000
0.00000


REMARK
290
SMTRY2
14
−1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY3
14
0.000000
0.000000
−1.000000
0.00000


REMARK
290
SMTRY1
15
0.000000
1.000000
0.000000
0.00000


REMARK
290
SMTRY2
15
−1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY3
15
0.000000
0.000000
1.000000
0.00000


REMARK
290
SMTRY1
16
0.000000
−1.000000
0.000000
0.00000


REMARK
290
SMTRY2
16
1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY3
16
0.000000
0.000000
1.000000
0.00000


REMARK
290
SMTRY1
17
1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY2
17
0.000000
0.000000
1.000000
0.00000


REMARK
290
SMTRY3
17
0.000000
−1.000000
0.000000
0.00000


REMARK
290
SMTRY1
18
−1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY2
18
0.000000
0.000000
1.000000
0.00000


REMARK
290
SMTRY3
18
0.000000
1.000000
0.000000
0.00000


REMARK
290
SMTRY1
19
−1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY2
19
0.000000
0.000000
−1.000000
0.00000


REMARK
290
SMTRY3
19
0.000000
−1.000000
0.000000
0.00000


REMARK
290
SMTRY1
20
1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY2
20
0.000000
0.000000
−1.000000
0.00000


REMARK
290
SMTRY3
20
0.000000
1.000000
0.000000
0.00000


REMARK
290
SMTRY1
21
0.000000
0.000000
1.000000
0.00000


REMARK
290
SMTRY2
21
0.000000
1.000000
0.000000
0.00000


REMARK
290
SMTRY3
21
−1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY1
22
0.000000
0.000000
1.000000
0.00000


REMARK
290
SMTRY2
22
0.000000
−1.000000
0.000000
0.00000


REMARK
290
SMTRY3
22
1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY1
23
0.000000
0.000000
−1.000000
0.00000


REMARK
290
SMTRY2
23
0.000000
1.000000
0.000000
0.00000


REMARK
290
SMTRY3
23
1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY1
24
0.000000
0.000000
−1.000000
0.00000


REMARK
290
SMTRY2
24
0.000000
−1.000000
0.000000
0.00000


REMARK
290
SMTRY3
24
−1.000000
0.000000
0.000000
0.00000









REMARK
290



REMARK
290
REMARK: NULL


REMARK
300


REMARK
300
BIOMOLECULE: 1


REMARK
300
THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT


REMARK
300
WHICH CONSISTS OF 1 CHAIN(S). SEE REMARK 350 FOR


REMARK
300
INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).


REMARK
350


REMARK
350
GENERATING THE BIOMOLECULE


REMARK
350
COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN


REMARK
350
BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE


REMARK
350
MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS


REMARK
350
GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND


REMARK
350
CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.


REMARK
350


REMARK
350
BIOMOLECULE: 1


REMARK
350
APPLY THE FOLLOWING TO CHAINS: A














REMARK
350
BIOMT1
1
1.000000
0.000000
0.000000
0.00000


REMARK
350
BIOMT2
1
0.000000
1.000000
0.000000
0.00000


REMARK
350
BIOMT3
1
0.000000
0.000000
1.000000
0.00000


REMARK
350
BIOMT1
2
−1.000000
0.000000
0.000000
153.82700


REMARK
350
BIOMT2
2
0.000000
−1.000000
0.000000
153.82700


REMARK
350
BIOMT3
2
0.000000
0.000000
1.000000
0.00000


REMARK
350
BIOMT1
3
0.000000
1.000000
0.000000
0.00000


REMARK
350
BIOMT2
3
−1.000000
0.000000
0.000000
153.82700


REMARK
350
BIOMT3
3
0.000000
0.000000
1.000000
0.00000


REMARK
350
BIOMT1
4
0.000000
−1.000000
0.000000
153.82700


REMARK
350
BIOMT2 4
1.000000
0.000000
0.000000
0.00000


REMARK
350
BIOMT3 4
0.000000
0.000000
1.000000
0.00000









REMARK
465



REMARK
465
MISSING RESIDUES


REMARK
465
THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE


REMARK
465
EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN


REMARK
465
IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)


REMARK
465


REMARK
465
M RES C SSSEQI










REMARK
465
MET A
 


REMARK
465
GLY A
102


REMARK
465
PHE A
103


REMARK
465
VAL A
104


REMARK
465
VAL A
105


REMARK
465
SER A
106


REMARK
465
ASP A
107


REMARK
465
SER A
108


REMARK
465
ASN A
109


REMARK
465
VAL A
110


REMARK
465
LYS A
111


REMARK
465
PRO A
112


REMARK
465
ASP A
113


REMARK
465
GLN A
114


REMARK
465
THR A
115


REMARK
465
PHE A
116


REMARK
465
ALA A
117


REMARK
465
ASP A
118


REMARK
465
VAL A
119


REMARK
465
LEU A
120


REMARK
465
ALA A
121


REMARK
465
ILE A
122


REMARK
465
SER A
123


REMARK
465
GLN A
124


REMARK
465
ARG A
125


REMARK
465
THR A
126


REMARK
465
THR A
127


REMARK
465
HIS A
128


REMARK
465
ASN A
129


REMARK
465
THR A
130


REMARK
465
VAL A
131


REMARK
465
ALA A
132


REMARK
465
VAL A
133


REMARK
465
THR A
134


REMARK
465
ASP A
135


REMARK
465
ASP A
136


REMARK
465
GLY A
137


REMARK
465
THR A
138


REMARK
465
PRO A
139


REMARK
465
HIS A
140


REMARK
465
GLY A
141


REMARK
465
VAL A
142


REMARK
465
LEU A
143


REMARK
465
LEU A
144


REMARK
46S
GLY A
145


REMARK
465
LEU A
146


REMARK
465
VAL A
147


REMARK
465
THR A
148


REMARK
465
GLN A
149


REMARK
465
ARG A
150


REMARK
465
ASP A
151


REMARK
465
TYR A
152


REMARK
465
PRO A
153


REMARK
465
ILE A
154


REMARK
465
ASP A
155


REMARK
465
LEU A
156


REMARK
465
THR A
157


REMARK
465
GLN A
158


REMARK
465
THR A
159


REMARK
465
GLU A
160


REMARK
465
THR A
161


REMARK
465
LYS A
162


REMARK
465
VAL A
163


REMARK
465
SER A
164


REMARK
465
ASP A
165


REMARK
465
MET A
166


REMARK
465
MET A
167


REMARK
465
THR A
168


REMARK
465
PRO A
169


REMARK
465
PHE A
170


REMARK
465
SER A
171


REMARK
465
LYS A
172


REMARK
465
LEU A
173


REMARK
465
VAL A
174


REMARK
465
THR A
175


REMARK
465
ALA A
176


REMARK
465
HIS A
177


REMARK
465
GLN A
178


REMARK
465
ASP A
179


REMARK
465
THR A
180


REMARK
465
LYS A
181


REMARK
465
LEU A
182


REMARK
465
SER A
183


REMARK
465
GLU A
184


REMARK
465
ALA A
185


REMARK
465
ASN A
186


REMARK
465
LYS A
187


REMARK
465
ILE A
188


REMARK
465
ILE A
189


REMARK
465
TRP A
190


REMARK
465
GLU A
191


REMARK
465
LYS A
192


REMARK
465
LYS A
193


REMARK
465
LEU A
194


REMARK
465
ASM A
195


REMARK
465
ALA A
196


REMARK
465
LEU A
197


REMARK
465
PRO A
198


REMARK
465
ILE A
199


REMARK
465
ILE A
200


REMARK
465
ASP A
201


REMARK
465
ASP A
202


REMARK
465
ASP A
203


REMARK
465
GLN A
204


REMARK
465
HIS A
205


REMARK
465
LEU A
206


REMARK
465
ARG A
207


REMARK
465
TYR A
208


REMARK
465
ILE A
209


REMARK
465
VAL A
210


REMARK
465
PHE A
211


REMARK
465
ARG A
212


REMARK
465
LYS A
213


REMARK
465
ASP A
214


REMARK
465
TYR A
215


REMARK
465
ASP A
216


REMARK
465
ARG A
217


REMARK
465
SER A
218


REMARK
465
GLN A
219


REMARK
465
VAL A
220


REMARK
465
CYS A
221


REMARK
465
ILE A
318


REMARK
465
CYS A
319


REMARK
465
ILE A
320


REMARK
465
THR A
321


REMARK
465
GLN A
417


REMARK
465
ARG A
418


REMARK
465
TYR A
419


REMARK
465
ASP A
420


REMARK
465
LEU A
421


REMARK
465
GLY A
422


REMARK
465
GLY A
423


REMARK
465
LYS A
424


REMARK
465
GLN A
425


REMARK
465
LYS A
426


REMARK
465
LEU A
427


REMARK
465
SER A
428


REMARK
465
PHE A
429


REMARK
465
GLU A
430


REMARK
465
VAL A
484


REMARK
465
GLU A
485


REMARK
465
GLY A
486


REMARK
465
GLY A
487


REMARK
465
ALA A
488


REMARK
465
HIS A
489


REMARK
465
ASP A
490


REMARK
465
VAL A
491


REMARK
465
ILE A
492


REMARK
465
VAL A
493


REMARK
465
LYS A
494


REMARK
465
ASP A
495


REMARK
465
ARG A
496


REMARK
465
ILE A
497


REMARK
465
ASN A
498


REMARK
465
ASP A
499


REMARK
465
TYR A
500


REMARK
465
HIS A
501


REMARK
465
PRO A
502


REMARK
465
LYS A
503









REMARK
500



REMARK
500
GEOMETRY AND STEREOCHEMISTRY


REMARK
500
SUBTOPIC: COVALENT BOND LENGTHS


REMARK
500


REMARK
500
THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWIMG RESIDUES


REMARK
500
HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE


REMARK
500
THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN


REMARK
500
IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).


REMARK
500


REMARK
500
STANDARD TABLE:


REMARK
500
FORMAT: (10X, I3, 1X, 2 (A3, 1X, A1, I4, A1, 1X, A4, 3X), F6.3)


REMARK
500


REMARK
500
EXPECTED VALUES: ENGH AND HUBER, 1991


REMARK
500















REMARK
500
M RES
CSSEQI
ATM1
RES
CSSEQI
ATM2
DEVIATION


REMARK
500
VAL A
 62
CB
VAL A
 62
CA
 0.036


REMARK
500
MET A
 92
CE
MET A
 92
SD
−0.071


REMARK
500
MET A
458
CE
MET A
458 SD
 0.037









REMARK
500



REMARK
500
GEOMETRY AND STEREOCHEMISTRY


REMARK
500
SUBTOPIC: COVALENT BOND ANGLES


REMARK
500


REMARK
500
THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES


REMARK
500
HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE


REMARK
500
THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN


REMARK
500
IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).


REMARK
500


REMARK
500
STANDARD TABLE:


REMARK
500
FORMAT: (10X, I3, 1X, A3, 1X, A1, I4, A1, 3(1X, A4, 2X), 12X, F5.1).


REMARK
500


REMARK
500
EXPECTED VALUES: ENGH AND HUBER, 1991


REMARK
500












REMARK
500
M RES
CSSEQI
ATM1  ATM2  ATM3



REMARK
500
GLY A
 20
N - CA - C
ANGL. DEV. = −7.9 DEGREES


REMARK
500
ILE A
 27
N - CA - C
ANGL. DEV. = −9.5 DEGREES


REMARK
500
PHE A
266
N - CA - C
ANGL. DEV. = −7.5 DEGREES


REMARK
500
GLY A
312
N - CA - C
ANGL. DEV. =  7.8 DEGREES


REMARK
500
LYS A
472
N - CA - C
ANGL. DEV. =  8.0 DEGREES


REMARK
500
LYS A
474
N - CA - C
ANGL. DEV. = −8.4 DEGREES


REMARK
500
LEU A
477
N - CA - C
ANGL. DEV. = −8.5 DEGREES









REMARK
900



REMARK
900
RELATED ENTRIES


REMARK
900
RELATED ID: 1AK5 RELATED DB: PDB


REMARK
900
INOSINE MONOPHOSPHATE DEHYDROGENASE (IMPDH) FROM.


REMARK
900
TRITRICHOMONAS FOETUS


REMARK
900
RELATED ID: 1ME7 RELATED DB: PDB


REMARK
900
1ME7 CONTAINS THE SAME PROTEIN WITH RVP AND MOA BOUND


REMARK
900
RELATED ID: 1ME8 RELATED DB: PDB


REMARK
900
1ME8 CONTAINS THE SAME PROTEIN WITH RVP BOUND


REMARK
900
RELATED ID: 1ME9 RELATED DB: PDB


REMARK
900
1ME9 CONTAINS THE SAME PROTEIN WITH IMP BOUND


REMARK
900
RELATED ID: 1MEH RELATED DB: PDB


REMARK
900
1MEH CONTAINS THE SAME PROTEIN WITH IMP AND MOA BOUND


REMARK
900
RELATED ID: 1MEI RELATED DB: PDB


REMARK
900
1MEI CONTAINS THE SAME PROTEIN WITH XMP AND MYCOPHENOLIC


REMARK
900
ACID BOUND


DBREF

1MEW A  1  503  SWS   P50097   IMDH_TRIFO   1  503























SEQRES
1
A
503
MET
ALA
LYS
TYR
TYR
ASN
GLU
PRO
CYS
HIS
THR
PHE
ASN


SEQRES
2
A
503
GLU
TYR
LEU
LEU
ILE
PRO
GLY
LEU
SER
THR
VAL
ASP
CYS


SEQRES
3
A
503
ILE
PRO
SER
ASN
VAL
ASN
LEU
SER
THR
PRO
LEU
VAL
LYS


SEQRES
4
A
503
PHE
GLN
LYS
GLY
GLN
GLN
SER
GLU
ILE
ASN
LEU
LYS
ILE


SEQRES
5
A
503
PRO
LEU
VAL
SER
ALA
ILE
MET
GLN
SER
VAL
SER
GLY
GLU


SEQRES
6
A
503
LYS
MET
ALA
ILE
ALA
LEU
ALA
ARG
GLU
GLY
GLY
ILE
SER


SEQRES
7
A
503
PHE
ILE
PHE
GLY
SER
GLN
SER
ILE
GLU
SER
GLN
ALA
ALA


SEQRES
8
A
503
MET
VAL
HIS
ALA
VAL
LYS
ASN
PHE
LYS
ALA
GLY
PHE
VAL


SEQRES
9
A
503
VAL
SER
ASP
SER
ASN
VAL
LYS
PRO
ASP
GLN
THR
PHE
ALA


SEQRES
10
A
503
ASP
VAL
LEU
ALA
ILE
SER
GLN
ARG
THR
THR
HIS
ASN
THR


SEQRES
11
A
503
VAL
ALA
VAL
THR
ASP
ASP
GLY
THR
PRO
HIS
GLY
VAL
LEU


SEQRES
12
A
503
LEU
GLY
LEU
VAL
THR
GLN
ARG
ASP
TYR
PRO
ILE
ASP
LEU


SEQRES
13
A
503
THR
GLN
THR
GLU
THR
LYS
VAL
SER
ASP
MET
MET
THR
PRO


SEQRES
14
A
503
PHE
SER
LYS
LEU
VAL
THR
ALA
HIS
GLN
ASP
THR
LYS
LEU


SEQRES
15
A
503
SER
GLU
ALA
ASN
LYS
ILE
ILE
TRP
GLN
LYS
LYS
LEU
ASN


SEQRES
16
A
503
ALA
LEU
PRO
ILE
ILE
ASP
ASP
ASP
GLN
HIS
LEU
ARG
TYR


SEQRES
17
A
503
ILE
VAL
PHE
ARG
LYS
ASP
TYR
ASP
ARG
SER
GLN
VAL
CYS


SEQRES
18
A
503
HIS
ASN
GLU
LEU
VAL
ASP
SER
GLN
LYS
ARO
TYR
LEU
VAL


SEQRES
19
A
503
GLY
ALA
GLY
ILE
ASN
THR
ARG
ASP
PHE
ARG
GLU
ARO
VAL


SEQRES
20
A
503
PRO
ALA
LEU
VAL
GLU
ALA
GLY
ALA
ASP
VAL
LEU
CYS
ILE


SEQRES
21
A
503
ASP
SER
SER
ASP
GLY
PHE
SER
GLU
TRP
GLN
LYS
ILE
THR


SEQRES
22
A
503
ILE
GLY
TRP
ILE
ARG
GLU
LYS
TYR
GLY
ASP
LYS
VAL
LYS


SEQRES
23
A
503
VAL
GLY
ALA
GLY
ASN
ILE
VAL
ASP
GLY
GLU
GLY
PHE
ARG


SEQRES
24
A
503
TYR
LEU
ALA
ASP
ALA
GLY
ALA
ASP
PHE
ILE
LYS
ILE
GLY


SEQRES
25
A
503
ILE
GLY
GLY
GLY
SER
ILE
CYS
ILE
THR
ARG
GLU
GLN
LYS


SEQRES
26
A
503
GLY
ILE
GLY
ARG
GLY
GLN
ALA
THR
ALA
VAL
ILE
ASP
VAL


SEQRES
27
A
503
VAL
ALA
GLU
ARG
ASN
LYS
TYR
PHE
GLU
GLU
THR
GLY
ILE


SEQRES
28
A
503
TYR
ILE
PRO
VAL
CYS
SER
ASP
GLY
GLY
ILE
VAL
TYR
ASP


SEQRES
29
A
503
TYR
HIS
MET
THR
LEU
ALA
LEU
ALA
MET
GLY
ALA
ASP
PHE


SEQRES
30
A
503
ILE
MET
LEU
GLY
ARG
TYR
PHE
ALA
ARG
PHE
GLU
GLU
SER


SEQRES
31
A
503
PRO
THR
ARG
LYS
VAL
THR
ILE
ASN
GLY
SER
VAL
MET
LYS


SEQRES
32
A
503
GLU
TYR
TRP
GLY
GLU
GLY
SER
SER
ARG
ALA
ARG
ASN
TRP


SEQRES
33
A
503
GLN
ARG
TYR
ASP
LEU
GLY
GLY
LYS
GLN
LYS
LEU
SER
PHE


SEQRES
34
A
503
GLU
GLU
GLY
VAL
ASP
SER
TYR
VAL
PRO
TYR
ALA
GLY
LYS


SEQRES
35
A
503
LEU
LYS
ASP
ASN
VAL
GLU
ALA
SER
LEU
ASN
LYS
VAL
LYS


SEQRES
36
A
503
SER
THR
MET
CYS
ASN
CYS
GLY
ALA
LEU
THR
ILE
PRO
GLN


SEQRES
37
A
503
LEU
GLN
SER
LYS
ALA
LYS
ILE
THR
LEU
VAL
SER
SER
VAL


SEQRES
38
A
503
SER
ILE
VAL
GLU
GLY
GLY
ALA
HIS
ASP
VAL
ILE
VAL
LYS


SEQRES
39
A
503
ASP
ARG
ILE
ASN
ASP
TYR
HIS
PRO
LYS












HET

K
A
900
 1


HET

XMP

602
24


HET

NAD

987
44









HETNAM

K POTASSIUM ION


HETNAM

XMP XANTHOSINE-5′-MONOPHOSPHATE


HETNAM

NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE


HETSYN

XMP 5--MONOPHOSPHATE-9-BETA-D-RIBOFURANOSYL XANTHINE










FORMUL
2
K
K1 1+


FORMUL
3
XMP
C10 H14 N4 O9 P1 1+


FORMUL
4
NAD
C21 H27 N7 O14 P2


FORMUL
5
HOH
*164 (H2 O1)


















HELIX
1
 1
THR A
11
ASN A
13
5



3


HELIX
2
 2
ILE A
27
VAL A
31
5



5


HELIX
3
 3
GLY A
64
GLU A
74
1



11


HELIX
4
 4
SER A
85
ASN A
98
1



14


HELIX
5
 5
ASP A
242
GLY A
254
1



13


HELIX
6
 6
SER A
267
GLY A
282
1



16


HELIX
7
 7
ASP A
283
VAL A
285
5



3


HELIX
8
 8
ASP A
294
GLY A
305
1



12


HELIX
9
 9
GLY A
330
GLY A
350
1



21


HELIX
10
10
TYR A
363
MET A
373
1



11


HELIX
11
11
GLY A
381
ARG A
386
1



6


HELIX
12
12
LYS A
442
CYS A
461
1



20


HELIX
13
13
THR A
465
ALA A
473
1



9


SHEET
1
A 2
TYR A
15
LEU A
17
0


SHEET
2
A 2
ILE A
475
LEU A
477
−1
O THR A
476
N LEU A
16


SHEET
1
B 2
THR A
35
PRO A
36
0


SHEET
2
B 2
ASN A
49
LEU A
50
−1
O LEU A
50
N THR A
35


SHEET
1
C 2
PHE A
40
GLN A
41
0


SHEET
2
C 2
ILE A
351
TYR A
352
−1
O TYR A
352
N PHE A
40


SHEET
1
D 9
LEU A
54
SER A
56
0


SHEET
2
D 9
ILE A
77
ILE A
80
1
O ILE A
77
N SER A
56


SHEET
3
D 9
GLY A
235
ILE A
238
1
O GLY A
237
N ILE A
80


SHEET
4
D 9
VAL A
257
ILE A
260
1
O CYS A
259
N ILE A
238


SHEET
5
D 9
VAL A
287
ILE A
292
1
O GLY A
288
N LEU A
258


SHEET
6
D 9
PHE A
308
ILE A
311
1
O LYS A
310
N ALA A
289


SHEET
7
D 9
VAL A
355
ASP A
358
1
O CYS A
356
N ILE A
311


SHEET
8
D 9
PHE A
377
LEU A
380
1
O MET A
379
N SER A
357


SHEET
9
D 9
LEU A
54
SER A
56
1
N VAL A
55
O ILE A
378


SHEET
1
E 3
LYS A
394
ILE A
397
0


SHEET
2
E 3
SER A
400
TRP A
406
−1
O MET A
402
N VAL A
395


SHEET
3
E 3
ASP A
434
PRO A
438
−1
O SER A
435
N TYR A
405













SSBOND
1
CYS A
 26
CYS A
459



CISPEP
1
GLY A
290
ASN A
291
0    1.02









CRYST1

153.827 153.827 153.827 90.00 90.00 90.00 P 4 3 2  24












ORIGX1

1.000000
0.000000
0.000000
0.00000


ORIGX2

0.000000
1.000000
0.000000
0.00000


ORIGX3

0.000000
0.000000
1.000000
0.00000


SCALE1

0.006501
0.000000
0.000000
0.00000


SCALE2

0.000000
0.006501
0.000000
0.00000


SCALE3

0.000000
0.000000
0.006501
0.00000

















ATOM
1
N
ALA A
2
54.794
74.512
36.618
1.00
30.12
N


ATOM
2
CA
ALA A
2
55.518
73.408
35.927
1.00
29.62
C


ATOM
3
C
ALA A
2
56.825
73.048
36.643
1.00
30.02
C


ATOM
4
O
ALA A
2
57.295
73.782
37.518
1.00
28.78
O


ATOM
5
CE
ALA A
2
55.807
73.811
34.492
1.00
29.41
C


ATOM
6
N
LYS A
3
57.397
71.908
36.261
1.00
29.90
N


ATOM
7
CA
LYS A
3
58.649
71.435
36.834
1.00
30.45
C


ATOM
8
C
LYS A
3
59.766
71.663
35.818
1.00
30.17
C


ATOM
9
O
LYS A
3
59.626
71.311
34.648
1.00
29.92
O


ATOM
10
CB
LYS A
3
58.564
69.938
37.150
1.00
31.27
C


ATOM
11
CG
LYS A
3
59.840
69.374
37.767
1.00
33.74
C


ATOM
12
CD
LYS A
3
59.988
67.882
37.515
1.00
35.82
C


ATOM
13
CE
LYS A
3
61.209
67.325
38.235
1.00
37.03
C


ATOM
14
NZ
LYS A
3
62.422
68.153
38.000
1.00
37.77
N


ATOM
15
N
TYR A
4
60.868
72.249
36.273
1.00
30.13
N


ATOM
16
CA
TYR A
4
62.022
72.523
35.421
1.00
30.22
C


ATOM
17
C
TYR A
4
63.218
71.738
35.939
1.00
30.80
C


ATOM
18
O
TYR A
4
63.151
71.131
37.003
1.00
31.54
O


ATOM
19
CB
TYR A
4
62.333
74.023
35.429
1.00
29.07
C


ATOM
20
CG
TYR A
4
61.238
74.845
34.800
1.00
28.39
C


ATOM
21
CD1
TYR A
4
61.148
74.974
33.417
1.00
27.65
C


ATOM
22
CD2
TYR A
4
60.260
75.464
35.588
1.00
28.22
C


ATOM
23
CE1
TYR A
4
60.106
75.701
32.827
1.00
27.89
C


ATOM
24
CE2
TYR A
4
59.213
76.192
35.007
1.00
27.42
C


ATOM
25
CZ
TYR A
4
59.145
76.304
33.629
1.00
27.38
C


ATOM
26
OH
TYR A
4
58.116
77.005
33.045
1.00
27.02
O


ATOM
27
N
TYR A
5
64.313
71.749
35.190
1.00
31.44
N


ATOM
28
CA
TYR A
5
65.508
71.016
35.597
1.00
32.16
C


ATOM
29
C
TYR A
5
66.719
71.930
35.741
1.00
32.66
C


ATOM
30
O
TYR A
5
66.779
73.005
35.142
1.00
32.67
O


ATOM
31
CB
TYRA
5
65.806
69.894
34.594
1.00
31.56
C


ATOM
32
CG
TYR A
5
64.679
68.891
34.466
1.00
31.13
C


ATOM
33
CD1
TYR A
5
63.511
69.212
33.777
1.00
30.96
C


ATOM
34
CD2
TYR A
5
64.763
67.634
35.073
1.00
31.04
C


ATOM
35
CE1
TYR A
5
62.453
68.311
33.694
1.00
30.92
C


ATOM
36
CE2
TYR A
5
63.713
66.726
34.997
1.00
30.33
C


ATOM
37
CZ
TYR A
5
62.559
67.071
34.307
1.00
31.08
C


ATOM
38
OH
TYR A
5
61.504
66.189
34.242
1.00
30.49
O


ATOM
39
N
ASN A
6
67.681
71.495
36.545
1.00
33.45
N


ATOM
40
CA
ASN A
6
68.889
72.271
36.796
1.00
34.17
C


ATOM
41
C
ASN A
6
69.829
72.350
35.596
1.00
33.77
C


ATOM
42
O
ASN A
6
70.505
73.357
35.404
1.00
34.57
O


ATOM
43
CB
ASN A
6
69.635
71.684
37.997
1.00
36.09
C


ATOM
44
CG
ASN A
6
68.893
71.902
39.311
1.00
38.01
C


ATOM
45
OD1
ASN A
6
69.083
71.156
40.276
1.00
39.34
O


ATOM
46
ND2
ASN A
6
68.054
72.936
39.356
1.00
38.72
N


ATOM
47
N
GLU A
7
69.868
71.296
34.786
1.00
32.81
N


ATOM
48
CA
GLU A
7
70.752
71.262
33.623
1.00
31.44
C


ATOM
49
C
GLU A
7
70.016
70.880
32.351
1.00
30.04
C


ATOM
50
O
GLU A
7
69.016
70.166
32.393
1.00
29.37
O


ATOM
51
CB
GLU A
7
71.870
70.238
33.840
1.00
32.95
C


ATOM
52
CG
GLU A
7
72.811
70.511
35.009
1.00
34.80
C


ATOM
53
CD
GLU A
7
73.665
71.758
34.814
1.00
36.26
C


ATOM
54
OE1
GLU A
7
74.098
72.025
33.667
1.00
37.11
O


ATOM
55
OE2
GLU A
7
73.919
72.463
35.816
1.00
37.12
O


ATOM
56
N
PRO A
8
70.505
71.353
31.193
1.00
28.73
N


ATOM
57
CA
PRO A
8
69.854
71.015
29.925
1.00
27.94
C


ATOM
58
C
PRO A
8
70.216
69.567
29.597
1.00
27.17
C


ATOM
59
O
PRO A
8
71.198
69.043
30.127
1.00
26.26
O


ATOM
60
CB
PRO A
8
70.481
72.004
28.945
1.00
27.85
C


ATOM
61
CG
PRO A
8
71.873
72.153
29.484
1.00
27.96
C


ATOM
62
CD
PRO A
8
71.641
72.268
30.975
1.00
28.51
C


ATOM
63
N
CYS A
9
69.432
68.918
28.742
1.00
26.44
N


ATOM
64
CA
CYS A
9
69.730
67.539
28.375
1.00
26.06
C


ATOM
65
C
CYS A
9
70.788
67.503
27.266
1.00
25.59
C


ATOM
66
O
CYS A
9
70.978
68.484
26.546
1.00
25.32
O


ATOM
67
CB
CYS A
9
68.452
66.801
27.950
1.00
26.04
C


ATOM
68
SG
CYS A
9
67.458
67.585
26.659
1.00
27.03
S


ATOM
69
N
HIS A
10
71.478
66.373
27.146
1.00
25.08
N


ATOM
70
CA
HIS A
10
72.545
66.203
26.163
1.00
24.94
C


ATOM
71
C
HIS A
10
72.398
64.914
25.351
1.00
25.14
C


ATOM
72
O
HIS A
10
71.761
63.957
25.789
1.00
24.67
O


ATOM
73
CB
HIS A
10
73.900
66.172
26.875
1.00
25.17
C


ATOM
74
CG
HIS A
10
74.154
67.356
27.755
1.00
25.33
C


ATOM
75
ND1
HIS A
10
74.603
68.565
27.269
1.00
25.05
N


ATOM
76
CD2
HIS A
10
74.016
67.517
29.092
1.00
25.00
C


ATOM
77
CE1
HIS A
10
74.731
69.419
28.267
1.00
24.83
C


ATOM
78
NE2
HIS A
10
74.381
68.807
29.385
1.00
25.63
N


ATOM
79
N
THR A
11
73.012
64.905
24.174
1.00
25.28
N


ATOM
80
CA
THR A
11
72.988
63.760
23.268
1.00
26.09
C


ATOM
81
C
THR A
11
74.336
63.045
23.334
1.00
25.82
C


ATOM
82
O
THR A
11
75.309
63.600
23.852
1.00
25.75
O


ATOM
83
CB
THR A
11
72.759
64.210
21.814
1.00
26.08
C


ATOM
84
OG1
THR A
11
73.768
65.160
21.456
1.00
27.99
O


ATOM
85
CG2
THR A
11
71.401
64.859
21.655
1.00
26.96
C


ATOM
86
N
PHE A
12
74.391
61.825
22.803
1.00
26.03
N


ATOM
87
CA
PHE A
12
75.618
61.028
22.798
1.00
26.92
C


ATOM
88
C
PHE A
12
76.820
61.750
22.185
1.00
27.61
C


ATOM
89
O
PHE A
12
77.957
61.556
22.625
1.00
27.79
O


ATOM
90
CB
PHE A
12
75.400
59.710
22.050
1.00
26.64
C


ATOM
91
CG
PHE A
12
74.493
58.740
22.763
1.00
26.79
C


ATOM
92
CD1
PHE A
12
74.631
58.510
24.131
1.00
26.53
C


ATOM
93
CD2
PHE A
12
73.533
58.023
22.056
1.00
26.50
C


ATOM
94
CE1
PHE A
12
73.826
57.577
24.787
1.00
26.96
C


ATOM
95
CE2
PHE A
12
72.723
57.085
22.700
1.00
27.06
C


ATOM
96
CZ
PHE A
12
72.870
56.861
24.072
1.00
26.55
C


ATOM
97
N
ASN A
13
76.567
62.569
21.167
1.00
28.01
N


ATOM
98
CA
ASN A
13
77.614
63.330
20.484
1.00
28.79
C


ATOM
99
C
ASN A
13
78.353
64.309
21.392
1.00
28.20
C


ATOM
100
O
ASN A
13
79.409
64.822
21.027
1.00
28.50
O


ATOM
101
CB
ASN A
13
77.013
64.115
19.316
1.00
30.83
C


ATOM
102
CG
ASN A
13
76.925
63.299
18.041
1.00
33.42
C


ATOM
103
OD1
ASN A
13
76.014
63.490
17.235
1.00
35.66
O


ATOM
104
ND2
ASN A
13
77.883
62.400
17.838
1.00
34.84
N


ATOM
105
N
GLU A
14
77.799
64.580
22.568
1.00
27.32
N


ATOM
106
CA
GLU A
14
78.422
65.520
23.494
1.00
26.81
C


ATOM
107
C
GLU A
14
79.333
64.863
24.528
1.00
26.48
C


ATOM
108
O
GLU A
14
79.794
65.524
25.462
1.00
26.71
O


ATOM
109
CB
GLU A
14
77.342
66.330
24.215
1.00
26.50
C


ATOM
110
CG
GLU A
14
76.448
67.124
23.283
1.00
26.18
C


ATOM
111
CD
GLU A
14
75.339
67.860
24.014
1.00
25.91
C


ATOM
112
OE1
GLU A
14
75.643
68.736
24.848
1.00
25.89
O


ATOM
113
OE2
GLU A
14
74.158
67.559
23.750
1.00
25.85
O


ATOM
114
N
TYR A
15
79.610
63.576
24.363
1.00
25.89
N


ATOM
115
CA
TYR A
15
80.454
62.880
25.325
1.00
25.89
C


ATOM
116
C
TYR A
15
81.647
62.145
24.733
1.00
25.92
C


ATOM
117
O
TYR A
15
81.652
61.758
23.562
1.00
25.82
O


ATOM
118
CB
TYR A
15
79.616
61.876
26.122
1.00
25.79
C


ATOM
119
CG
TYR A
15
78.551
62.505
26.986
1.00
26.02
C


ATOM
120
CD1
TYR A
15
78.814
62.856
28.310
1.00
25.94
C


ATOM
121
CD2
TYR A
15
77.276
62.757
26.475
1.00
25.51
C


ATOM
122
CE1
TYR A
15
77.831
63.440
29.107
1.00
26.32
C


ATOM
123
CE2
TYR A
15
76.296
63.339
27.256
1.00
25.69
C


ATOM
124
CZ
TYR A
15
76.574
63.678
28.567
1.00
26.16
C


ATOM
125
OH
TYR A
15
75.595
64.268
29.328
1.00
27.92
O


ATOM
126
N
LEU A
16
82.659
61.958
25.571
1.00
25.68
N


ATOM
127
CA
LEU A
16
83.857
61.221
25.201
1.00
25.59
C


ATOM
128
C
LEU A
16
84.240
60.398
26.421
1.00
25.18
C


ATOM
129
O
LEU A
16
83.879
60.741
27.545
1.00
23.99
O


ATOM
130
CB
LEU A
16
85.011
62.163
24.835
1.00
25.74
C


ATOM
131
CG
LEU A
16
84.924
62.928
23.513
1.00
26.58
C


ATOM
132
CD1
LEU A
16
86.164
63.782
23.349
1.00
26.64
C


ATOM
133
CD2
LEU A
16
84.802
61.955
22.355
1.00
26.82
C


ATOM
134
N
LEU A
17
84.955
59.304
26.193
1.00
25.52
N


ATOM
135
CA
LEU A
17
85.403
58.444
27.281
1.00
25.75
C


ATOM
136
C
LEU A
17
86.873
58.726
27.569
1.00
25.91
C


ATOM
137
O
LEU A
17
87.685
58.859
26.649
1.00
26.05
O


ATOM
138
CB
LEU A
17
85.236
56.973
26.898
1.00
25.70
C


ATOM
139
CG
LEU A
17
83.811
56.418
26.904
1.00
25.75
C


ATOM
140
CD1
LEU A
17
83.715
55.203
25.988
1.00
25.70
C


ATOM
141
CD2
LEU A
17
83.422
56.062
28.330
1.00
24.96
C


ATOM
142
N
ILE A
18
87.207
58.841
28.848
1.00
26.13
N


ATOM
143
CA
ILE A
18
88.584
59.070
29.247
1.00
26.23
C


ATOM
144
C
ILE A
18
89.125
57.707
29.665
1.00
26.76
C


ATOM
145
O
ILE A
18
88.568
57.054
30.547
1.00
26.89
O


ATOM
146
CB
ILE A
18
88.657
60.077
30.408
1.00
26.10
C


ATOM
147
CG1
ILE A
18
88.213
61.457
29.896
1.00
25.77
C


ATOM
148
CG2
ILE A
18
90.078
60.122
30.983
1.00
25.02
C


ATOM
149
CD1
ILE A
18
88.079
62.511
30.963
1.00
27.03
C


ATOM
150
N
PRO A
19
90.209
57.251
29.016
1.00
27.09
N


ATOM
151
CA
PRO A
19
90.821
55.949
29.319
1.00
27.41
C


ATOM
152
C
PRO A
19
91.121
55.680
30.792
1.00
27.03
C


ATOM
153
O
PRO A
19
91.403
56.595
31.562
1.00
27.37
O


ATOM
154
CB
PRO A
19
92.098
55.960
28.477
1.00
27.80
C


ATOM
155
CG
PRO A
19
91.703
56.803
27.280
1.00
27.76
C


ATOM
156
CD
PRO A
19
90.949
57.944
27.944
1.00
27.42
C


ATOM
157
N
GLY A
20
91.040
54.410
31.169
1.00
26.77
N


ATOM
158
CA
GLY A
20
91.346
54.000
32.528
1.00
26.84
C


ATOM
159
C
GLY A
20
92.544
53.079
32.388
1.00
27.02
C


ATOM
160
O
GLY A
20
93.130
53.018
31.314
1.00
26.32
O


ATOM
161
N
LEU A
21
92.919
52.360
33.437
1.00
27.85
N


ATOM
162
CA
LEU A
21
94.070
51.468
33.333
1.00
28.67
C


ATOM
163
C
LEU A
21
93.765
50.236
32.500
1.00
29.29
C


ATOM
164
O
LEU A
21
92.834
49.491
32.795
1.00
29.57
O


ATOM
165
CB
LEU A
21
94.549
51.022
34.724
1.00
28.50
C


ATOM
166
CG
LEU A
21
95.732
50.038
34.732
1.00
28.54
C


ATOM
167
CD1
LEU A
21
96.928
50.654
34.003
1.00
27.17
C


ATOM
168
CD2
LEU A
21
96.101
49.681
36.175
1.00
28.26
C


ATOM
169
N
SER A
22
94.552
50.032
31.449
1.00
30.33
N


ATOM
170
CA
SER A
22
94.392
48.867
30.592
1.00
31.39
C


ATOM
171
C
SER A
22
95.419
47.829
31.039
1.00
32.61
C


ATOM
172
O
SER A
22
96.626
48.063
30.930
1.00
32.22
O


ATOM
173
CB
SER A
22
94.650
49.233
29.131
1.00
31.24
C


ATOM
174
OG
SER A
22
93.690
50.152
28.652
1.00
31.78
O


ATOM
175
N
THR A
23
94.941
46.693
31.547
1.00
33.62
N


ATOM
176
CA
THR A
23
95.821
45.620
32.007
1.00
34.86
C


ATOM
177
C
THR A
23
96.222
44.737
30.834
1.00
35.59
C


ATOM
178
O
THR A
23
95.573
44.757
29.786
1.00
35.63
O


ATOM
179
CB
THR A
23
95.132
44.727
33.059
1.00
35.00
C


ATOM
180
OG1
THR A
23
93.945
44.160
32.493
1.00
36.07
O


ATOM
181
CG2
THR A
23
94.766
45.533
34.295
1.00
35.01
C


ATOM
182
N
VAL A
24
97.287
43.958
31.015
1.00
36.20
N


ATOM
183
CA
VAL A
24
97.767
43.070
29.962
1.00
37.31
C


ATOM
184
C
VAL A
24
96.717
42.041
29.553
1.00
38.42
C


ATOM
185
O
VAL A
24
96.757
41.520
28.439
1.00
38.33
O


ATOM
186
CB
VAL A
24
99.053
42.308
30.388
1.00
37.05
C


ATOM
187
CG1
VAL A
24
100.194
43.295
30.612
1.00
36.36
C


ATOM
188
CG2
VAL A
24
98.786
41.485
31.642
1.00
36.49
C


ATOM
189
N
ASP A
25
95.773
41.749
30.441
1.00
39.90
N


ATOM
190
CA
ASP A
25
94.753
40.772
30.101
1.00
41.78
C


ATOM
191
C
ASP A
25
93.581
41.335
29.298
1.00
41.86
C


ATOM
192
O
ASP A
25
92.762
40.570
28.794
1.00
42.34
O


ATOM
193
CB
ASP A
25
94.251
40.050
31.362
1.00
43.81
C


ATOM
194
CG
ASP A
25
93.534
40.968
32.323
1.00
45.75
C


ATOM
195
OD1
ASP A
25
92.406
41.397
32.011
1.00
47.52
O


ATOM
196
OD2
ASP A
25
94.099
41.261
33.400
1.00
48.02
O


ATOM
197
N
CYS A
26
93.485
42.656
29.151
1.00
41.52
N


ATOM
198
CA
CYS A
26
92.374
43.173
28.363
1.00
41.49
C


ATOM
199
C
CYS A
26
92.701
43.323
26.898
1.00
41.58
C


ATOM
200
O
CYS A
26
93.229
44.343
26.456
1.00
41.10
O


ATOM
201
CB
CYS A
26
91.854
44.522
28.856
1.00
40.64
C


ATOM
202
SG
CYS A
26
90.147
44.844
28.259
1.00
40.94
S


ATOM
203
N
ILE A
27
92.379
42.281
26.151
1.00
42.19
N


ATOM
204
CA
ILE A
27
92.563
42.280
24.721
1.00
42.85
C


ATOM
205
C
ILE A
27
91.140
42.075
24.226
1.00
43.07
C


ATOM
206
O
ILE A
27
90.327
41.450
24.911
1.00
42.66
O


ATOM
207
CB
ILE A
27
93.491
41.125
24.265
1.00
43.47
C


ATOM
208
CG1
ILE A
27
93.134
39.831
25.002
1.00
43.91
C


ATOM
209
CG2
ILE A
27
94.940
41.501
24.523
1.00
43.28
C


ATOM
210
CD1
ILE A
27
94.064
38.662
24.686
1.00
44.36
C


ATOM
211
N
PRO A
28
90.809
42.628
23.052
1.00
43.47
N


ATOM
212
CA
PRO A
28
89.476
42.516
22.456
1.00
43.48
C


ATOM
213
C
PRO A
28
88.861
41.117
22.465
1.00
43.56
C


ATOM
214
O
PRO A
28
87.685
40.956
22.797
1.00
43.47
O


ATOM
215
CB
PRO A
28
89.696
43.049
21.044
1.00
44.02
C


ATOM
216
CG
PRO A
28
90.692
44.142
21.277
1.00
43.69
C


ATOM
217
CD
PRO A
28
91.680
43.481
22.220
1.00
43.81
C


ATOM
218
N
SER A
29
89.654
40.109
22.116
1.00
43.37
N


ATOM
219
CA
SER A
29
89.152
38.739
22.065
1.00
43.09
C


ATOM
220
C
SER A
29
88.731
38.182
23.422
1.00
42.29
C


ATOM
221
O
SER A
29
88.027
37.176
23.493
1.00
42.98
O


ATOM
222
CB
SER A
29
90.192
37.810
21.414
1.00
43.86
C


ATOM
223
OG
SER A
29
91.393
37.743
22.165
1.00
45.20
O


ATOM
224
N
ASN A
30
89.154
38.828
24.500
1.00
41.03
N


ATOM
225
CA
ASN A
30
88.780
38.362
25.829
1.00
39.63
C


ATOM
226
C
ASN A
30
87.608
39.158
26.410
1.00
37.78
C


ATOM
227
O
ASN A
30
87.194
38.931
27.545
1.00
37.59
O


ATOM
228
CB
ASN A
30
89.986
38.429
26.765
1.00
41.20
C


ATOM
229
CG
ASN A
30
90.922
37.244
26.591
1.00
42.75
C


ATOM
230
OD1
ASN A
30
91.261
36.864
25.468
1.00
43.71
O


ATOM
231
ND2
ASN A
30
91.345
36.656
27.704
1.00
43.38
N


ATOM
232
N
VAL A
31
87.072
40.088
25.627
1.00
35.31
N


ATOM
233
CA
VAL A
31
85.948
40.894
26.087
1.00
33.17
C


ATOM
234
C
VAL A
31
84.636
40.127
25.953
1.00
32.15.
C


ATOM
235
O
VAL A
31
84.319
39.593
24.892
1.00
31.40
O


ATOM
236
CB
VAL A
31
85.847
42.227
25.302
1.00
32.76
C


ATOM
237
CG1
VAL A
31
84.590
42.989
25.715
1.00
31.80
C


ATOM
238
CG2
VAL A
31
87.088
43.074
25.570
1.00
32.13
C


ATOM
239
N
ASN A
32
83.887
40.075
27.047
1.00
30.94
N


ATOM
240
CA
ASN A
32
82.604
39.383
27.088
1.00
30.49
C


ATOM
241
C
ASN A
32
81.503
40.434
26.951
1.00
29.50
C


ATOM
242
O
ASN A
32
81.363
41.307
27.804
1.00
29.55
O


ATOM
243
CB
ASN A
32
82.474
38.633
28.421
1.00
30.56
C


ATOM
244
CG
ASN A
32
81.174
37.862
28.542
1.00
31.78
C


ATOM
245
OD1
ASN A
32
80.279
37.978
27.705
1.00
31.47
O


ATOM
246
ND2
ASN A
32
81.062
37.068
29.604
1.00
32.67
N


ATOM
247
N
LEU A
33
80.728
40.343
25.875
1.00
28.85
N


ATOM
248
CA
LEU A
33
79.647
41.290
25.591
1.00
28.13
C


ATOM
249
C
LEU A
33
78.259
40.780
25.983
1.00
27.84
C


ATOM
250
O
LEU A
33
77.240
41.298
25.524
1.00
28.25
O


ATOM
251
CB
LEU A
33
79.662
41.637
24.101
1.00
27.87
C


ATOM
252
CG
LEU A
33
80.228
42.982
23.621
1.00
28.18
C


ATOM
253
CD1
LEU A
33
81.299
43.515
24.546
1.00
27.71
C


ATOM
254
CD2
LEU A
33
80.757
42.799
22.215
1.00
27.10
C


ATOM
255
N
SER A
34
78.223
39.762
26.828
1.00
27.39
N


ATOM
256
CA
SER A
34
76.963
39.183
27.291
1.00
27.16
C


ATOM
257
C
SER A
34
76.204
40.218
28.129
1.00
26.24
C


ATOM
258
O
SER A
34
76.814
41.063
28.774
1.00
25.91
O


ATOM
259
CB
SER A
34
77.263
37.930
28.124
1.00
27.60
C


ATOM
260
OG
SER A
34
76.102
37.434
28.756
1.00
30.45
O


ATOM
261
N
THR A
35
74.877
40.157
28.124
1.00
25.86
N


ATOM
262
CA
THR A
35
74.095
41.125
28.885
1.00
24.92
C


ATOM
263
C
THR A
35
72.687
40.592
29.158
1.00
24.89
C


ATOM
264
O
THR A
35
72.115
39.865
28.344
1.00
25.03
O


ATOM
265
CB
THR A
35
74.021
42.485
28.121
1.00
25.02
C


ATOM
266
OG1
THR A
35
73.744
43.549
29.040
1.00
25.25
O


ATOM
267
CG2
THR A
35
72.931
42.456
27.070
1.00
24.69
C


ATOM
268
N
PRO A
36
72.109
40.948
30.314
1.00
24.52
N


ATOM
269
CA
PRO A
36
70.761
40.485
30.665
1.00
24.57
C


ATOM
270
C
PRO A
36
69.651
41.167
29.867
1.00
25.00
C


ATOM
271
O
PRO A
36
69.697
42.375
29.631
1.00
25.19
O


ATOM
272
CB
PRO A
36
70.672
40.797
32.155
1.00
24.46
C


ATOM
273
CG
PRO A
36
71.479
42.072
32.264
1.00
24.23
C


ATOM
274
CD
PRO A
36
72.684
41.786
31.383
1.00
24.01
C


ATOM
275
N
LEU A
37
68.651
40.393
29.456
1.00
24.96
N


ATOM
276
CA
LEU A
37
67.535
40.946
28.705
1.00
25.21
C


ATOM
277
C
LEU A
37
66.308
41.179
29.593
1.00
25.43
C


ATOM
278
O
LEU A
37
65.599
42.175
29.426
1.00
25.20
O


ATOM
279
CB
LEU A
37
67.156
40.017
27.546
1.00
24.90
C


ATOM
280
CG
LEU A
37
66.049
40.506
26.599
1.00
25.00
C


ATOM
281
CD1
LEU A
37
66.593
41.629
25.709
1.00
24.59
C


ATOM
282
CD2
LEU A
37
65.550
39.351
25.729
1.00
24.58
C


ATOM
283
N
VAL A
38
66.061
40.274
30.539
1.00
25.54
N


ATOM
284
CA
VAL A
38
64.896
40.397
31.415
1.00
25.63
C


ATOM
285
C
VAL A
38
65.241
40.442
32.904
1.00
26.35
C


ATOM
286
O
VAL A
38
66.268
39.919
33.335
1.00
26.41
O


ATOM
287
CB
VAL A
38
63.885
39.262
31.136
1.00
25.83
C


ATOM
288
CG1
VAL A
38
63.410
39.357
29.679
1.00
25.31
C


ATOM
289
CG2
VAL A
38
64.523
37.895
31.398
1.00
24.98
C


ATOM
290
N
LYS A
39
64.368
41.074
33.682
1.00
26.62
N


ATOM
291
CA
LYS A
39
64.588
41.251
35.113
1.00
27.40
C


ATOM
292
C
LYS A
39
64.768
39.986
35.943
1.00
27.98
C


ATOM
293
O
LYS A
39
64.220
38.926
35.625
1.00
28.34
O


ATOM
294
CB
LYS A
39
63.453
42.085
35.722
1.00
27.32
C


ATOM
295
CG
LYS A
39
62.098
41.400
35.710
1.00
27.27
C


ATOM
296
CD
LYS A
39
61.075
42.203
36.491
1.00
27.48
C


ATOM
297
CE
LYS A
39
59.703
41.538
36.465
1.00
27.05
C


ATOM
298
NZ
LYS A
39
58.735
42.262
37.335
1.00
26.75
N


ATOM
299
N
PHE A
40
65.539
40.133
37.017
1.00
28.20
N


ATOM
300
CA
PHE A
40
65.828
39.057
37.958
1.00
29.34
C


ATOM
301
C
PHE A
40
66.082
39.682
39.337
1.00
30.13
C


ATOM
302
O
PHE A
40
66.226
40.899
39.447
1.00
30.16
O


ATOM
303
CB
PHE A
40
67.058
38.258
37.501
1.00
28.35
C


ATOM
304
CG
PHE A
40
68.264
39.110
37.197
1.00
27.78
C


ATOM
305
CD1
PHE A
40
68.448
39.650
35.924
1.00
26.96
C


ATOM
306
CD2
PHE A
40
69.209
39.379
38.183
1.00
27.28
C


ATOM
307
CE1
PHE A
40
69.553
40.442
35.635
1.00
26.45
C


ATOM
308
CE2
PHE A
40
70.325
40.174
37.907
1.00
27.06
C


ATOM
309
CZ
PHE A
40
70.497
40.706
36.628
1.00
27.14
C


ATOM
310
N
GLN A
41
66.130
38.851
40.379
1.00
31.29
N


ATOM
311
CA
GLN A
41
66.358
39.317
41.754
1.00
32.59
C


ATOM
312
C
GLN A
41
67.851
39.354
42.054
1.00
32.23
C


ATOM
313
O
GLN A
41
68.637
38.714
41.362
1.00
31.49
O


ATOM
314
CB
GLN A
41
65.698
38.365
42.759
1.00
34.28
C


ATOM
315
CG
GLN A
41
64.249
38.045
42.486
1.00
37.74
C


ATOM
316
CD
GLN A
41
63.310
39.092
43.041
1.00
40.33
C


ATOM
317
OE1
GLN A
41
63.397
40.277
42.694
1.00
41.23
O


ATOM
318
NE2
GLN A
41
62.397
38.662
43.916
1.00
41.92
N


ATOM
319
N
LYS A
42
68.245
40.084
43.095
1.00
32.61
N


ATOM
320
CA
LYS A
42
69.659
40.152
43.442
1.00
33.23
C


ATOM
321
C
LYS A
42
70.235
38.768
43.716
1.00
33.05
C


ATOM
322
O
LYS A
42
69.609
37.943
44.384
1.00
32.65
O


ATOM
323
CB
LYS A
42
69.898
41.024
44.672
1.00
34.37


ATOM
324
CG
LYS A
42
71.380
41.106
45.002
1.00
36.49
C


ATOM
325
CD
LYS A
42
71.712
42.108
46.093
1.00
38.56
C


ATOM
326
CE
LYS A
42
71.361
41.595
47.463
1.00
38.86
C


ATOM
327
NZ
LYS A
42
71.973
42.474
48.502
1.00
40.12
N


ATOM
328
N
GLY A
43
71.432
38.518
43.198
1.00
32.94
N


ATOM
329
CA
GLY A
43
72.064
37.231
43.414
1.00
32.98
C


ATOM
330
C
GLY A
43
71.847
36.234
42.297
1.00
32.97
C


ATOM
331
O
GLY A
43
72.611
35.279
42.170
1.00
32.75
O


ATOM
332
N
GLN A
44
70.815
36.430
41.483
1.00
33.23
N


ATOM
333
CA
GLN A
44
70.580
35.498
40.388
1.00
33.79
C


ATOM
334
C
GLN A
44
70.996
36.029
39.023
1.00
33.69
C


ATOM
335
O
GLN A
44
71.505
37.139
38.906
1.00
33.63
O


ATOM
336
CB
GLN A
44
69.113
35.039
40.362
1.00
34.55
C


ATOM
337
CG
GLN A
44
68.093
36.090
40.695
1.00
35.61
C


ATOM
338
CD
GLN A
44
66.677
35.538
40.781
1.00
35.93
C


ATOM
339
OE1
GLN A
44
66.382
34.665
41.599
1.00
37.13
O


ATOM
340
NE2
GLN A
44
65.793
36.051
39.938
1.00
35.37
N


ATOM
341
N
GLN A
45
70.803
35.204
37.999
1.00
33.77
N


ATOM
342
CA
GLN A
45
71.135
35.560
36.623
1.00
33.60
C


ATOM
343
C
GLN A
45
69.832
35.752
35.874
1.00
32.34
C


ATOM
344
O
GLN A
45
68.794
35.245
36.287
1.00
31.56
O


ATOM
345
CB
GLN A
45
71.921
34.432
35.938
1.00
35.04
C


ATOM
346
CG
GLN A
45
73.297
34.165
36.516
1.00
37.78
C


ATOM
347
CD
GLN A
45
74.285
35.267
36.191
1.00
39.44
C


ATOM
348
OE1
GLN A
45
74.613
35.497
35.022
1.00
40.59
O


ATOM
349
NE2
GLN A
45
74.767
35.959
37.225
1.00
39.68
N


ATOM
350
N
SER A
46
69.889
36.483
34.771
1.00
31.43
N


ATOM
351
CA
SER A
46
68.701
36.703
33.969
1.00
31.01
C


ATOM
352
C
SER A
46
68.396
35.419
33.211
1.00
30.99
C


ATOM
353
O
SER A
46
69.312
34.730
32.766
1.00
31.11
O


ATOM
354
CB
SER A
46
68.931
37.833
32.964
1.00
30.11
C


ATOM
355
OG
SER A
46
67.752
38.074
32.219
1.00
28.77
O


ATOM
356
N
GLU A
47
67.113
35.100
33.068
1.00
31.10
N


ATOM
357
CA
GLU A
47
66.708
33.905
32.337
1.00
31.53
C


ATOM
358
C
GLU A
47
67.119
34.002
30.877
1.00
31.11
C


ATOM
359
O
GLU A
47
67.311
32.985
30.215
1.00
31.30
O


ATOM
360
CB
GLU A
47
65.198
33.710
32.427
1.00
32.16
C


ATOM
361
CG
GLU A
47
64.717
33.337
33.814
1.00
34.70
C


ATOM
362
CD
GLU A
47
63.211
33.402
33.933
1.00
36.22
C


ATOM
363
OE1
GLU A
47
62.524
32.650
33.208
1.00
37.59
O


ATOM
364
OE2
GLU A
47
62.715
34.211
34.747
1.00
37.82
O


ATOM
365
N
ILE A
48
67.233
35.226
30.367
1.00
30.49
N


ATOM
366
CA
ILE A
48
67.643
35.431
28.981
1.00
29.71
C


ATOM
367
C
ILE A
48
68.791
36.432
28.911
1.00
29.44
C


ATOM
368
O
ILE A
48
68.670
37.575
29.356
1.00
29.08
O


ATOM
369
CB
ILE A
48
66.488
35.962
28.099
1.00
30.08
C


ATOM
370
CG1
ILE A
48
65.281
35.021
28.171
1.00
30.16
C


ATOM
371
CG2
ILE A
48
66.967
36.091
26.653
1.00
29.55
C


ATOM
372
CD1
ILE A
48
64.082
35.489
27.348
1.00
29.84
C


ATOM
373
N
ASN A
49
69.905
35.988
28.347
1.00
28.86
N


ATOM
374
CA
ASN A
49
71.085
36.820
28.198
1.00
29.07
C


ATOM
375
C
ASN A
49
71.483
36.882
26.730
1.00
28.95
C


ATOM
376
O
ASN A
49
71.609
35.852
26.067
1.00
29.13
O


ATOM
377
CB
ASN A
49
72.245
36.245
29.021
1.00
28.75
C


ATOM
378
CG
ASN A
49
72.023
36.385
30.515
1.00
28.90
C


ATOM
379
OD1
ASN A
49
72.210
37.459
31.084
1.00
28.55
O


ATOM
380
ND2
ASN A
49
71.609
35.302
31.155
1.00
29.52
N


ATOM
381
N
LEU A
50
71.658
38.094
26.220
1.00
28.25
N


ATOM
382
CA
LEU A
50
72.071
38.273
24.834
1.00
27.70
C


ATOM
383
C
LEU A
50
73.568
37.994
24.791
1.00
27.62
C


ATOM
384
O
LEU A
50
74.252
38.178
25.793
1.00
27.10
O


ATOM
385
CB
LEU A
50
71.814
39.718
24.389
1.00
26.87
C


ATOM
386
CG
LEU A
50
70.381
40.241
24.527
1.00
27.52
C


ATOM
387
CD1
LEU A
50
70.339
41.740
24.227
1.00
27.19
C


ATOM
388
CD2
LEU A
50
69.467
39.465
23.588
1.00
27.05
C


ATOM
389
N
LYS A
51
74.073
37.541
23.646
1.00
28.04
N


ATOM
390
CA
LYS A
51
75.507
37.286
23.493
1.00
28.80
C


ATOM
391
C
LYS A
51
76.182
38.622
23.166
1.00
27.80
C


ATOM
392
O
LYS A
51
77.351
38.834
23.481
1.00
28.10
O


ATOM
393
CB
LYS A
51
75.772
36.277
22.364
1.00
30.63
C


ATOM
394
CG
LYS A
51
76.038
34.848
22.827
1.00
32.96
C


ATOM
395
CD
LYS A
51
74.829
34.217
23.460
1.00
34.61
C


ATOM
396
CE
LYS A
51
75.131
32.788
23.913
1.00
35.94
C


ATOM
397
NZ
LYS A
51
75.513
31.887
22.788
1.00
36.84
N


ATOM
398
N
ILE A
52
75.431
39.508
22.518
1.00
26.90
N


ATOM
399
CA
ILE A
52
75.899
40.848
22.177
1.00
26.16
C


ATOM
400
C
ILE A
52
74.759
41.798
22.556
1.00
26.14
C


ATOM
401
O
ILE A
52
73.583
41.452
22.430
1.00
26.42
O


ATOM
402
CB
ILE A
52
76.247
40.989
20.671
1.00
25.90
C


ATOM
403
CG1
ILE A
52
75.041
40.634
19.803
1.00
25.37
C


ATOM
404
CG2
ILE A
52
77.443
40.086
20.329
1.00
25.95
C


ATOM
405
CD1
ILE A
52
75.244
40.975
18.331
1.00
24.51
C


ATOM
406
N
PRO A
53
75.093
43.011
23.016
1.00
25.79
N


ATOM
407
CA
PRO A
53
74.090
43.999
23.431
1.00
25.66
C


ATOM
408
C
PRO A
53
73.334
44.765
22.345
1.00
25.90
C


ATOM
409
O
PRO A
53
73.041
45.947
22.521
1.00
26.17
O


ATOM
410
CB
PRO A
53
74.900
44.929
24.319
1.00
24.87
C


ATOM
411
CG
PRO A
53
76.207
44.999
23.568
1.00
25.16
C


ATOM
412
CD
PRO A
53
76.459
43.553
23.167
1.00
25.11
C


ATOM
413
N
LEU A
54
73.002
44.101
21.241
1.00
25.97
N


ATOM
414
CA
LEU A
54
72.285
44.767
20.157
1.00
25.81
C


ATOM
415
C
LEU A
54
70.975
44.072
19.799
1.00
26.02
C


ATOM
416
O
LEU A
54
70.931
42.847
19.653
1.00
26.13
O


ATOM
417
CB
LEU A
54
73.160
44.839
18.897
1.00
25.47
C


ATOM
418
CG
LEU A
54
74.556
45.459
19.009
1.00
26.34
C


ATOM
419
CD1
LEU A
54
75.216
45.494
17.627
1.00
26.06
C


ATOM
420
CD2
LEU A
54
74.458
46.863
19.591
1.00
26.01
C


ATOM
421
N
VAL A
55
69.911
44.858
19.668
1.00
25.53
N


ATOM
422
CA
VAL A
55
68.614
44.325
19.277
1.00
25.73
C


ATOM
423
C
VAL A
55
68.078
45.236
18.172
1.00
26.28
C


ATOM
424
O
VAL A
55
68.287
46.455
18.207
1.00
26.42
O


ATOM
425
CB
VAL A
55
67.612
44.265
20.477
1.00
25.52
C


ATOM
426
CG1
VAL A
55
68.262
43.550
21.654
1.00
24.72
C


ATOM
427
CG2
VAL A
55
67.139
45.656
20.868
1.00
24.62
C


ATOM
428
N
SER A
56
67.418
44.652
17.174
1.00
26.19
N


ATOM
429
CA
SER A
56
66.884
45.447
16.073
1.00
25.97
C


ATOM
430
C
SER A
56
65.508
46.017
16.417
1.00
25.83
C


ATOM
431
O
SER A
56
64.700
45.373
17.089
1.00
25.99
O


ATOM
432
CB
SER A
56
66.831
44.610
14.788
1.00
25.77
C


ATOM
433
OG
SER A
56
66.050
43.446
14.965
1.00
26.05
O


ATOM
434
N
ALA A
57
65.264
47.238
15.957
1.00
25.89
N


ATOM
435
CA
ALA A
57
64.024
47.966
16.218
1.00
26.47
C


ATOM
436
C
ALA A
57
62.721
47.300
15.756
1.00
27.16
C


ATOM
437
O
ALA A
57
62.692
46.554
14.779
1.00
27.22
O


ATOM
438
CB
ALA A
57
64.133
49.358
15.619
1.00
25.66
C


ATOM
439
N
ILE A
58
61.643
47.594
16.478
1.00
27.68
N


ATOM
440
CA
ILE A
58
60.316
47.056
16.184
1.00
28.41
C


ATOM
441
C
ILE A
58
59.737
47.863
15.021
1.00
28.86
C


ATOM
442
O
ILE A
58
58.795
48.644
15.194
1.00
29.04
O


ATOM
443
CB
ILE A
58
59.388
47.204
17.414
1.00
27.86
C


ATOM
444
CG1
ILE A
58
60.156
46.808
18.683
1.00
27.40
C


ATOM
445
CG2
ILE A
58
58.145
46.335
17.239
1.00
27.81
C


ATOM
446
CD1
ILE A
58
59.338
46.846
19.959
1.00
26.01
C


ATOM
447
N
MET A
59
60.304
47.659
13.836
1.00
29.07
N


ATOM
448
CA
MET A
59
59.896
48.407
12.652
1.00
29.93
C


ATOM
449
C
MET A
59
59.747
47.546
11.400
1.00
30.41
C


ATOM
450
O
MET A
59
60.510
46.605
11.185
1.00
29.96
O


ATOM
451
CB
MET A
59
60.922
49.507
12.379
1.00
29.62
C


ATOM
452
CG
MET A
59
61.172
50.439
13.556
1.00
29.09
C


ATOM
453
SD
MET A
59
62.564
51.543
13.248
1.00
29.35
S


ATOM
454
CE
MET A
59
61.850
52.630
12.008
1.00
28.25
C


ATOM
455
N
GLN A
60
58.766
47.901
10.575
1.00
31.54
N


ATOM
456
CA
GLN A
60
58.476
47.186
9.331
1.00
32.53
C


ATOM
457
C
GLN A
60
59.685
47.152
8.411
1.00
32.76
C


ATOM
458
O
GLN A
60
59.904
46.173
7.707
1.00
32.70
O


ATOM
459
CB
GLN A
60
57.334
47.862
8.565
1.00
32.88
C


ATOM
460
CG
GLN A
60
56.084
48.176
9.362
1.00
34.01
C


ATOM
461
CD
GLN A
60
55.010
48.821
8.497
1.00
34.77
C


ATOM
462
OE1
GLN A
60
55.313
49.611
7.603
1.00
35.73
O


ATOM
463
NE2
GLN A
60
53.749
48.497
8.767
1.00
35.22
N


ATOM
464
N
SER A
61
60.463
48.232
8.418
1.00
33.31
N


ATOM
465
CA
SER A
61
61.629
48.334
7.552
1.00
33.30
C


ATOM
466
C
SER A
61
62.931
47.752
8.099
1.00
33.20
C


ATOM
467
O
SER A
61
63.988
47.933
7.492
1.00
33.61
O


ATOM
468
CB
SER A
61
61.853
49.799
7.143
1.00
33.43
C


ATOM
469
OG
SER A
61
62.047
50.635
8.271
1.00
35.07
O


ATOM
470
N
VAL A
62
62.875
47.052
9.227
1.00
32.70
N


ATOM
471
CA
VAL A
62
64.101
46.475
9.764
1.00
32.55
C


ATOM
472
C
VAL A
62
63.999
45.079
10.358
1.00
32.60
C


ATOM
473
O
VAL A
62
64.800
44.213
10.026
1.00
33.59
O


ATOM
474
CB
VAL A
62
64.789
47.432
10.810
1.00
32.46
C


ATOM
475
CG1
VAL A
62
63.860
48.545
11.206
1.00
32.31
C


ATOM
476
CG2
VAL A
62
65.245
46.655
12.041
1.00
31.54
C


ATOM
477
N
SER A
63
63.017
44.838
11.215
1.00
33.04
N


ATOM
478
CA
SER A
63
62.924
43.531
11.845
1.00
32.74
C


ATOM
479
C
SER A
63
61.986
42.510
11.214
1.00
33.02
C


ATOM
480
O
SER A
63
60.871
42.283
11.692
1.00
32.02
O


ATOM
481
CB
SER A
63
62.600
43.700
13.331
1.00
32.70
C


ATOM
482
OG
SER A
63
63.666
44.356
14.005
1.00
31.78
O


ATOM
483
N
GLY A
64
62.467
41.894
10.138
1.00
33.46
N


ATOM
484
CA
GLY A
64
61.717
40.857
9.454
1.00
33.96
C


ATOM
485
C
GLY A
64
62.338
39.518
9.829
1.00
34.68
C


ATOM
486
O
GLY A
64
63.160
39.455
10.749
1.00
33.86
O


ATOM
487
N
GLU A
65
61.961
38.453
9.123
1.00
35.46
N


ATOM
488
CA
GLU A
65
62.482
37.113
9.394
1.00
36.69
C


ATOM
489
C
GLU A
65
63.987
36.993
9.207
1.00
36.64
C


ATOM
490
O
GLU A
65
64.694
36.532
10.101
1.00
36.51
O


ATOM
491
CB
GLU A
65
61.809
36.077
8.489
1.00
38.32
C


ATOM
492
CG
GLU A
65
60.441
35.608
8.946
1.00
41.08
C


ATOM
493
CD
GLU A
65
59.808
34.623
7.964
1.00
42.59
C


ATOM
494
OE1
GLU A
65
60.483
33.631
7.595
1.00
43.43
O


ATOM
495
OE2
GLU A
65
58.639
34.844
7.568
1.00
42.90
O


ATOM
496
N
LYS A
66
64.470
37.386
8.033
1.00
36.50
N


ATOM
497
CA
LYS A
66
65.891
37.293
7.734
1.00
36.67
C


ATOM
498
C
LYS A
66
66.729
38.082
8.734
1.00
35.70
C


ATOM
499
O
LYS A
66
67.803
37.639
9.137
1.00
35.10
O


ATOM
500
CB
LYS A
66
66.164
37.775
6.304
1.00
37.83
C


ATOM
501
CG
LYS A
66
65.512
36.899
5.242
1.00
40.02
C


ATOM
502
CD
LYS A
66
65.935
37.299
3.828
1.00
42.33
C


ATOM
503
CE
LYS A
66
65.202
36.465
2.776
1.00
43.21
C


ATOM
504
NZ
LYS A
66
65.582
36.849
1.381
1.00
44.57
N


ATOM
505
N
MET A
67
66.231
39.247
9.134
1.00
34.61
N


ATOM
506
CA
MET A
67
66.938
40.068
10.105
1.00
33.55
C


ATOM
507
C
MET A
67
67.023
39.306
11.427
1.00
32.84
C


ATOM
508
O
MET A
67
68.104
39.148
11.995
1.00
32.24
O


ATOM
509
CB
MET A
67
66.204
41.394
10.322
1.00
33.32
C


ATOM
510
CG
MET A
67
66.868
42.316
11.338
1.00
32.81
C


ATOM
511
SD
MET A
67
68.526
42.816
10.844
1.00
32.40
S


ATOM
512
CE
MET A
67
68.141
43.942
9.476
1.00
31.53
C


ATOM
513
N
ALA A
68
65.877
38.825
11.899
1.00
31.91
N


ATOM
514
CA
ALA A
68
65.811
38.093
13.156
1.00
31.69
C


ATOM
515
C
ALA A
68
66.789
36.928
13.183
1.00
31.70
C


ATOM
516
O
ALA A
68
67.459
36.686
14.190
1.00
31.79
O


ATOM
517
CB
ALA A
68
64.389
37.592
13.394
1.00
31.52
C


ATOM
518
N
ILE A
69
66.866
36.203
12.073
1.00
31.40
N


ATOM
519
CA
ILE A
69
67.766
35.061
11.969
1.00
31.19
C


ATOM
520
C
ILE A
69
69.226
35.511
11.942
1.00
30.56
C


ATOM
521
O
ILE A
69
70.059
34.992
12.686
1.00
30.98
O


ATOM
522
CB
ILE A
69
67.452
34.234
10.691
1.00
31.73
C


ATOM
523
CG1
ILE A
69
66.083
33.563
10.836
1.00
32.13
C


ATOM
524
CG2
ILE A
69
68.529
33.184
10.459
1.00
32.02
C


ATOM
525
CD1
ILE A
69
65.529
33.009
9.536
1.00
32.48
C


ATOM
526
N
ALA A
70
69.526
36.484
11.088
1.00
29.80
N


ATOM
527
CA
ALA A
70
70.882
36.998
10.953
1.00
29.27
C


ATOM
528
C
ALA A
70
71.425
37.592
12.249
1.00
28.89
C


ATOM
529
O
ALA A
70
72.589
37.391
12.583
1.00
28.35
O


ATOM
530
CB
ALA A
70
70.932
38.041
9.847
1.00
29.17
C


ATOM
531
N
LEU A
71
70.585
38.324
12.979
1.00
28.72
N


ATOM
532
CA
LEU A
71
71.027
38.937
14.224
1.00
28.35
C


ATOM
533
C
LEU A
71
71.187
37.890
15.316
1.00
28.41
C


ATOM
534
O
LEU A
71
72.158
37.913
16.064
1.00
27.56
O


ATOM
535
CE
LEU A
71
70.044
40.021
14.669
1.00
27.97
C


ATOM
536
CG
LEU A
71
70.409
40.792
15.945
1.00
27.65
C


ATOM
537
CD1
LEU A
71
71.861
41.254
15.890
1.00
26.83
C


ATOM
538
CD2
LEU A
71
69.476
41.990
16.092
1.00
27.34
C


ATOM
539
N
ALA A
72
70.235
36.967
15.398
1.00
29.11
N


ATOM
540
CA
ALA A
72
70.302
35.911
16.400
1.00
30.05
C


ATOM
541
C
ALA A
72
71.587
35.109
16.211
1.00
30.73
C


ATOM
542
O
ALA A
72
72.212
34.688
17.187
1.00
30.22
O


ATOM
543
CB
ALA A
72
69.081
34.992
16.288
1.00
29.99
C


ATOM
544
N
ARG A
73
71.980
34.900
14.955
1.00
31.51
N


ATOM
545
CA
ARG A
73
73.203
34.152
14.659
1.00
32.60
C


ATOM
546
C
ARG A
73
74.432
34.827
15.253
1.00
32.59
C


ATOM
547
O
ARG A
73
75.402
34.161
15.602
1.00
32.71
O


ATOM
548
CB
ARG A
73
73.392
34.000
13.147
1.00
33.56
C


ATOM
549
CG
ARG A
73
72.540
32.910
12.528
1.00
35.32
C


ATOM
550
CD
ARG A
73
72.697
32.866
11.022
1.00
36.95
C


ATOM
551
NE
ARG A
73
71.978
31.732
10.448
1.00
39.16
N


ATOM
552
CZ
ARG A
73
71.740
31.572
9.149
1.00
39.97
C


ATOM
553
NH1
ARG A
73
72.161
32.476
8.274
1.00
39.65
N


ATOM
554
NH2
ARG A
73
71.075
30.505
8.726
1.00
40.71
N


ATOM
555
N
GLU A
74
74.384
36.151
15.368
1.00
32.40
N


ATOM
556
CA
GLU A
74
75.498
36.908
15.920
1.00
32.28
C


ATOM
557
C
GLU A
74
75.397
37.091
17.430
1.00
31.45
C


ATOM
558
O
GLU A
74
76.299
37.642
18.047
1.00
31.66
O


ATOM
559
CE
GLU A
74
75.595
38.274
15.235
1.00
33.47
C


ATOM
560
CG
GLU A
74
75.967
38.197
13.759
1.00
35.41
C


ATOM
561
CD
GLU A
74
77.306
37.510
13.524
1.00
37.04
C


ATOM
562
OE1
GLU A
74
78.337
38.018
14.017
1.00
37.82
O


ATOM
563
OE2
GLU A
74
77.325
36.458
12.846
1.00
38.54
O


ATOM
564
N
GLY A
75
74.295
36.646
18.026
1.00
30.81
N


ATOM
565
CA
GLY A
75
74.152
36.774
19.467
1.00
30.19
C


ATOM
566
C
GLY A
75
73.133
37.780
19.966
1.00
29.59
C


ATOM
567
O
GLY A
75
72.909
37.888
21.176
1.00
28.90
O


ATOM
568
N
GLY A
76
72.524
38.522
19.044
1.00
29.15
N


ATOM
569
CA
GLY A
76
71.526
39.504
19.427
1.00
28.52
C


ATOM
570
C
GLY A
76
70.124
38.968
19.194
1.00
28.42
C


ATOM
571
O
GLY A
76
69.949
37.769
18.970
1.00
28.19
O


ATOM
572
N
ILE A
77
69.124
39.846
19.250
1.00
27.85
N


ATOM
573
CA
ILE A
77
67.744
39.435
19.026
1.00
27.34
C


ATOM
574
C
ILE A
77
66.963
40.538
18.315
1.00
27.73
C


ATOM
575
O
ILE A
77
67.228
41.730
18.507
1.00
27.71
O


ATOM
576
CB
ILE A
77
67.043
39.089
20.363
1.00
26.95
C


ATOM
577
CG1
ILE A
77
65.811
38.217
20.097
1.00
26.86
C


ATOM
578
CG2
ILE A
77
66.642
40.370
21.099
1.00
26.54
C


ATOM
579
CD1
ILE A
77
65.128
37.709
21.362
1.00
25.58
C


ATOM
580
N
SER A
78
66.010
40.135
17.481
1.00
27.61
N


ATOM
581
CA
SER A
78
65.176
41.083
16.752
1.00
27.42
C


ATOM
582
C
SER A
78
63.763
41.054
17.313
1.00
27.91
C


ATOM
583
O
SER A
78
63.317
40.045
17.858
1.00
27.91
O


ATOM
584
CE
SER A
78
65.104
40.721
15.264
1.00
26.86
C


ATOM
585
OG
SER A
78
66.353
40.859
14.618
1.00
26.59
O


ATOM
586
N
PHE A
79
63.056
42.166
17.180
1.00
28.37
N


ATOM
587
CA
PHE A
79
61.681
42.228
17.634
1.00
28.70
C


ATOM
588
C
PHE A
79
60.796
42.394
16.403
1.00
29.22
C


ATOM
589
O
PHE A
79
60.599
43.505
15.920
1.00
29.28
O


ATOM
590
CB
PHE A
79
61.489
43.389
18.620
1.00
28.26
C


ATOM
591
CG
PHE A
79
62.076
43.121
19.980
1.00
28.13
C


ATOM
592
CD1
PHE A
79
63.421
43.363
20.234
1.00
28.01
C


ATOM
593
CD2
PHE A
79
61.291
42.574
20.995
1.00
28.23
C


ATOM
594
CE1
PHE A
79
63.981
43.063
21.479
1.00
28.23
C


ATOM
595
CE2
PHE A
79
61.840
42.270
22.244
1.00
27.87
C


ATOM
596
CZ
PHE A
79
63.185
42.514
22.485
1.00
27.96
C


ATOM
597
N
ILE A
80
60.286
41.279
15.880
1.00
30.20
N


ATOM
598
CA
ILE A
80
59.426
41.316
14.697
1.00
30.73
C


ATOM
599
C
ILE A
80
58.372
42.393
14.884
1.00
31.00
C


ATOM
600
O
ILE A
80
57.661
42.407
15.892
1.00
30.84
O


ATOM
601
CE
ILE A
80
58.730
39.948
14.441
1.00
31.03
C


ATOM
602
CG1
ILE A
80
59.673
39.001
13.696
1.00
31.69
C


ATOM
603
CG2
ILE A
80
57.508
40.137
13.549
1.00
30.82
C


ATOM
604
CD1
ILE A
80
60.976
38.770
14.361
1.00
32.86
C


ATOM
605
N
PHE A
81
58.277
43.299
13.914
1.00
31.46
N


ATOM
606
CA
PHE A
81
57.318
44.387
14.010
1.00
32.33
C


ATOM
607
C
PHE A
81
55.884
43.903
14.193
1.00
32.76
C


ATOM
608
O
PHE A
81
55.464
42.908
13.595
1.00
32.74
O


ATOM
609
CB
PHE A
81
57.417
45.316
12.788
1.00
32.73
C


ATOM
610
CG
PHE A
81
57.167
44.635
11.470
1.00
33.07
C


ATOM
611
CD1
PHE A
81
58.155
43.859
10.872
1.00
33.23
C


ATOM
612
CD2
PHE A
81
55.949
44.796
10.812
1.00
33.18
C


ATOM
613
CE1
PHE A
81
57.937
43.251
9.629
1.00
33.42
C


ATOM
614
CE2
PHE A
81
55.717
44.194
9.571
1.00
33.24
C


ATOM
615
CZ
PHE A
81
56.716
43.420
8.979
1.00
33.26
C


ATOM
616
N
GLY A
82
55.143
44.615
15.035
1.00
33.07
N


ATOM
617
CA
GLY A
82
53.763
44.260
15.303
1.00
34.00
C


ATOM
618
C
GLY A
82
52.780
45.069
14.481
1.00
34.67
C


ATOM
619
O
GLY A
82
51.567
44.884
14.600
1.00
34.70
O


ATOM
620
N
SER A
83
53.300
45.971
13.651
1.00
35.05
N


ATOM
621
CA
SER A
83
52.459
46.795
12.791
1.00
35.41
C


ATOM
622
C
SER A
83
52.095
45.999
11.538
1.00
36.15
C


ATOM
623
O
SER A
83
52.438
46.367
10.411
1.00
36.11
O


ATOM
624
CB
SER A
83
53.185
48.085
12.409
1.00
35.00
C


ATOM
625
OG
SER A
83
54.407
47.807
11.755
1.00
34.80
O


ATOM
626
N
GLN A
84
51.411
44.884
11.766
1.00
36.71
N


ATOM
627
CA
GLN A
84
50.952
43.993
10.714
1.00
37.15
C


ATOM
628
C
GLN A
84
49.907
43.107
11.386
1.00
37.55
C


ATOM
629
O
GLN A
84
49.734
43.173
12.605
1.00
37.38
O


ATOM
630
CB
GLN A
84
52.115
43.157
10.165
1.00
37.55
C


ATOM
631
CG
GLN A
84
52.783
42.238
11.179
1.00
37.88
C


ATOM
632
CD
GLN A
84
53.907
41.426
10.569
1.00
38.47
C


ATOM
633
OE1
GLN A
84
53.730
40.791
9.530
1.00
39.45
O


ATOM
634
NE2
GLN A
84
55.072
41.435
11.214
1.00
38.16
N


ATOM
635
N
SER A
85
49.208
42.286
10.610
1.00
37.98
N


ATOM
636
CA
SER A
85
48.177
41.427
11.183
1.00
38.63
C


ATOM
637
C
SER A
85
48.755
40.456
12.205
1.00
39.17
C


ATOM
638
O
SER A
85
49.922
40.068
12.119
1.00
39.21
O


ATOM
639
CB
SER A
85
47.471
40.625
10.089
1.00
38.43
C


ATOM
640
OG
SER A
85
48.237
39.491
9.726
1.00
38.74
O


ATOM
641
N
ILE A
86
47.928
40.059
13.167
1.00
39.52
N


ATOM
642
CA
ILE A
86
48.348
39.116
14.192
1.00
40.46
C


ATOM
643
C
ILE A
86
48.837
37.827
13.533
1.00
41.43
C


ATOM
644
O
ILE A
86
49.832
37.239
13.959
1.00
41.37
O


ATOM
645
CB
ILE A
86
47.179
38.792
15.155
1.00
40.12
C


ATOM
646
CG1
ILE A
86
46.847
40.034
15.993
1.00
40.13
C


ATOM
647
CG2
ILE A
86
47.533
37.605
16.043
1.00
39.47
C


ATOM
648
CD1
ILE A
86
45.631
39.878
16.891
1.00
39.39
C


ATOM
649
N
GLU A
87
48.139
37.403
12.480
1.00
42.20
N


ATOM
650
CA
GLU A
87
48.497
36.182
11.768
1.00
42.84
C


ATOM
651
C
GLU A
87
49.845
36.280
11.057
1.00
42.23
C


ATOM
652
O
GLU A
87
50.633
35.337
11.089
1.00
42.25
O


ATOM
653
CB
GLU A
87
47.405
35.809
10.755
1.00
44.28
C


ATOM
654
CG
GLU A
87
46.291
36.848
10.587
1.00
46.83
C


ATOM
655
CD
GLU A
87
45.454
37.041
11.847
1.00
47.87
C


ATOM
656
OE1
GLU A
87
44.982
36.030
12.416
1.00
48.85
O


ATOM
657
OE2
GLU A
87
45.261
38.206
12.264
1.00
48.52
O


ATOM
658
N
SER A
88
50.108
37.415
10.416
1.00
41.90
N


ATOM
659
CA
SER A
88
51.372
37.617
9.710
1.00
41.64
C


ATOM
660
C
SER A
88
52.563
37.665
10.665
1.00
40.67
C


ATOM
661
O
SER A
88
53.596
37.048
10.409
1.00
40.52
O


ATOM
662
CB
SER A
88
51.337
38.916
8.902
1.00
42.19
C


ATOM
663
OG
SER A
88
50.359
38.853
7.882
1.00
44.49
O


ATOM
664
N
GLN A
89
52.423
38.405
11.759
1.00
39.75
N


ATOM
665
CA
GLN A
89
53.507
38.518
12.729
1.00
39.13
C


ATOM
666
C
GLN A
89
53.805
37.160
13.353
1.00
38.91
C


ATOM
667
O
GLN A
89
54.964
36.754
13.453
1.00
38.76
O


ATOM
668
CE
GLN A
89
53.151
39.534
13.821
1.00
38.26
C


ATOM
669
CG
GLN A
89
54.226
39.689
14.888
1.00
37.37
C


ATOM
670
CD
GLN A
89
53.860
40.714
15.946
1.00
36.90
C


ATOM
671
OE1
GLN A
89
52.692
40.870
16.299
1.00
36.35
O


ATOM
672
NE2
GLN A
89
54.863
41.407
16.470
1.00
36.22
N


ATOM
673
N
ALA A
90
52.753
36.457
13.762
1.00
39.14
N


ATOM
674
CA
ALA A
90
52.902
35.140
14.370
1.00
39.24
C


ATOM
675
C
ALA A
90
53.587
34.185
13.395
1.00
39.46
C


ATOM
676
O
ALA A
90
54.404
33.354
13.798
1.00
39.52
O


ATOM
677
CB
ALA A
90
51.537
34.593
14.774
1.00
39.44
C


ATOM
678
N
ALA A
91
53.260
34.312
12.112
1.00
39.32
N


ATOM
679
CA
ALA A
91
53.856
33.456
11.093
1.00
39.50
C


ATOM
680
C
ALA A
91
55.357
33.724
10.984
1.00
39.72
C


ATOM
681
O
ALA A
91
56.154
32.793
10.840
1.00
39.86
O


ATOM
682
CE
ALA A
91
53.177
33.689
9.745
1.00
39.16
C


ATOM
683
N
MET A
92
55.741
34.995
11.045
1.00
39.61
N


ATOM
684
CA
MET A
92
57.151
35.352
10.967
1.00
39.71
C


ATOM
685
C
MET A
92
57.889
34.791
12.173
1.00
39.19
C


ATOM
686
O
MET A
92
58.990
34.258
12.041
1.00
39.13
O


ATOM
687
CB
MET A
92
57.326
36.871
10.918
1.00
40.44
C


ATOM
688
CG
MET A
92
56.931
37.495
9.598
1.00
41.57
C


ATOM
689
SD
MET A
92
57.352
39.245
9.523
1.00
42.86
S


ATOM
690
CE
MET A
92
59.055
39.148
9.746
1.00
43.00
C


ATOM
691
N
VAL A
93
57.277
34.917
13.348
1.00
38.70
N


ATOM
692
CA
VAL A
93
57.871
34.413
14.581
1.00
38.24
C


ATOM
693
C
VAL A
93
58.066
32.909
14.452
1.00
38.82
C


ATOM
694
O
VAL A
93
59.139
32.381
14.744
1.00
38.41
O


ATOM
695
CB
VAL A
93
56.962
34.708
15.800
1.00
37.90
C


ATOM
696
CG1
VAL A
93
57.400
33.883
17.003
1.00
37.53
C


ATOM
697
CG2
VAL A
93
57.011
36.185
16.133
1.00
37.21
C


ATOM
698
N
HIS A
94
57.018
32.226
14.001
1.00
39.48
N


ATOM
699
CA
HIS A
94
57.061
30.778
13.828
1.00
40.12
C


ATOM
700
C
HIS A
94
58.181
30.377
12.866
1.00
39.88
C


ATOM
701
O
HIS A
94
58.927
29.434
13.127
1.00
39.95
O


ATOM
702
CE
HIS A
94
55.722
30.274
13.288
1.00
41.19
C


ATOM
703
CG
HIS A
94
55.595
28.785
13.294
1.00
42.21
C


ATOM
704
ND1
HIS A
94
55.385
28.062
14.448
1.00
42.90
N


ATOM
705
CD2
HIS A
94
55.676
27.879
12.291
1.00
42.67
C


ATOM
706
CE1
HIS A
94
55.340
26.775
14.156
1.00
42.91
C


ATOM
707
NE2
HIS A
94
55.515
26.637
12.854
1.00
43.21
N


ATOM
708
N
ALA A
95
58.294
31.104
11.759
1.00
39.52
N


ATOM
709
CA
ALA A
95
59.318
30.828
10.757
1.00
39.41
C


ATOM
710
C
ALA A
95
60.732
30.903
11.336
1.00
39.70
C


ATOM
711
O
ALA A
95
61.600
30.104
10.979
1.00
39.80
O


ATOM
712
CE
ALA A
95
59.181
31.800
9.599
1.00
39.04
C


ATOM
713
N
VAL A
96
60.968
31.868
12.221
1.00
39.80.
N


ATOM
714
CA
VAL A
96
62.280
32.022
12.834
1.00
39.46
C


ATOM
715
C
VAL A
96
62.540
30.876
13.807
1.00
40.06
C


ATOM
716
O
VAL A
96
63.640
30.322
13.851
1.00
40.00
O


ATOM
717
CE
VAL A
96
62.392
33.367
13.593
1.00
39.16
C


ATOM
718
CG1
VAL A
96
63.723
33.449
14.326
1.00
38.41
C


ATOM
719
CG2
VAL A
96
62.264
34.522
12.617
1.00
38.80
C


ATOM
720
N
LYS A
97
61.518
30.516
14.574
1.00
40.40
N


ATOM
721
CA
LYS A
97
61.641
29.442
15.550
1.00
41.60
C


ATOM
722
C
LYS A
97
61.861
28.063
14.927
1.00
42.73
C


ATOM
723
O
LYS A
97
62.472
27.193
15.548
1.00
42.73
O


ATOM
724
CB
LYS A
97
60.398
29.405
16.448
1.00
40.87
C


ATOM
725
CG
LYS A
97
60.165
30.681
17.242
1.00
39.77
C


ATOM
726
CD
LYS A
97
61.374
31.020
18.112
1.00
38.88
C


ATOM
727
CE
LYS A
97
61.645
29.938
19.146
1.00
38.08
C


ATOM
728
NZ
LYS A
97
62.859
30.238
19.957
1.00
37.01
N


ATOM
729
N
ASN A
98
61.373
27.867
13.705
1.00
44.37
N


ATOM
730
CA
ASN A
98
61.509
26.579
13.024
1.00
46.53
C


ATOM
731
C
ASN A
98
62.485
26.602
11.854
1.00
47.31
C


ATOM
732
O
ASN A
98
62.519
25.664
11.056
1.00
47.58
O


ATOM
733
CB
ASN A
98
60.146
26.112
12.506
1.00
47.72
C


ATOM
734
CG
ASN A
98
59.160
25.828
13.621
1.00
49.35
C


ATOM
735
OD1
ASN A
98
57.953
25.977
13.439
1.00
50.61
O


ATOM
736
ND2
ASN A
98
59.664
25.403
14.778
1.00
49.87
N


ATOM
737
N
PHE A
99
63.284
27.659
11.751
1.00
48.16
N


ATOM
738
CA
PHE A
99
64.227
27.782
10.644
1.00
48.79
C


ATOM
739
C
PHE A
99
65.234
26.636
10.519
1.00
49.62
C


ATOM
740
O
PHE A
99
65.528
26.189
9.412
1.00
49.73
O


ATOM
741
CB
PHE A
99
64.988
29.107
10.741
1.00
48.15
C


ATOM
742
CG
PHE A
99
65.802
29.425
9.518
1.00
47.62
C


ATOM
743
CD1
PHE A
99
65.179
29.755
8.319
1.00
47.45
C


ATOM
744
CD2
PHE A
99
67.192
29.383
9.559
1.00
47.46
C


ATOM
745
CE1
PHE A
99
65.928
30.038
7.177
1.00
47.25
C


ATOM
746
CE2
PHE A
99
67.950
29.663
8.425
1.00
47.37
C


ATOM
747
CZ
PHE A
99
67.317
29.992
7.231
1.00
47.38
C


ATOM
748
N
LYS A
100
65.752
26.160
11.648
1.00
50.63
N


ATOM
749
CA
LYS A
100
66.751
25.092
11.644
1.00
51.74
C


ATOM
750
C
LYS A
100
66.180
23.677
11.537
1.00
52.59
C


ATOM
751
O
LYS A
100
66.768
22.722
12.045
1.00
53.01
O


ATOM
752
CB
LYS A
100
67.625
25.215
12.896
1.00
51.65
C


ATOM
753
CG
LYS A
100
68.234
26.604
13.048
1.00
51.70
C


ATOM
754
CD
LYS A
100
68.860
26.837
14.417
1.00
51.72
C


ATOM
755
CE
LYS A
100
70.214
26.175
14.552
1.00
51.52
C


ATOM
756
NZ
LYS A
100
70.846
26.548
15.844
1.00
51.13
N


ATOM
757
N
ALA A
101
65.041
23.543
10.864
1.00
53.24
N


ATOM
758
CA
ALA A
101
64.402
22.241
10.691
1.00
53.65
C


ATOM
759
C
ALA A
101
64.609
21.717
9.270
1.00
53.86
C


ATOM
760
O
ALA A
101
64.007
22.218
8.317
1.00
53.99
O


ATOM
761
CB
ALA A
101
62.908
22.347
10.997
1.00
53.63
C


ATOM
762
N
HIS A
222
79.084
30.118
16.803
1.00
56.10
N


ATOM
763
CA
HIS A
222
79.441
29.875
18.198
1.00
56.03
C


ATOM
764
C
HIS A
222
78.777
30.884
19.132
1.00
54.99
C


ATOM
765
O
HIS A
222
78.609
30.624
20.326
1.00
54.92
O


ATOM
766
CB
HIS A
222
80.964
29.929
18.373
1.00
57.63
C


ATOM
767
CG
HIS A
222
81.692
28.829
17.662
1.00
59.44
C


ATOM
768
ND1
HIS A
222
81.472
27.495
17.935
1.00
60.05
N


ATOM
769
CD2
HIS A
222
82.619
28.863
16.675
1.00
60.20
C


ATOM
770
CE1
HIS A
222
82.231
26.755
17.145
1.00
60.69
C


ATOM
771
NE2
HIS A
222
82.937
27.560
16.370
1.00
60.70
N


ATOM
772
N
ASN A
223
78.399
32.036
18.588
1.00
53.33
N


ATOM
773
CA
ASN A
223
77.749
33.058
19.391
1.00
51.76
C


ATOM
774
C
ASN A
223
76.279
33.236
19.049
1.00
49.93
C


ATOM
775
O
ASN A
223
75.713
34.298
19.289
1.00
49.49
O


ATOM
776
CB
ASN A
223
78.473
34.399
19.249
1.00
52.87
C


ATOM
777
CO
ASN A
223
79.779
34.438
20.020
1.00
53.79
C


ATOM
778
OD1
ASN A
223
80.743
33.748
19.676
1.00
54.29
O


ATOM
779
ND2
ASN A
223
79.815
35.244
21.078
1.00
54.20
N


ATOM
780
N
GLU A
224
75.657
32.201
18.490
1.00
47.90
N


ATOM
781
CA
GLU A
224
74.243
32.288
18.148
1.00
46.08
C


ATOM
782
C
GLU A
224
73.406
32.282
19.418
1.00
43.99
C


ATOM
783
O
GLU A
224
73.720
31.581
20.379
1.00
42.95
O


ATOM
784
CB
GLU A
224
73.816
31.127
17.239
1.00
46.94
C


ATOM
785
CG
GLU A
224
74.134
29.736
17.778
1.00
48.84
C


ATOM
786
CD
GLU A
224
73.590
28.616
16.896
1.00
49.60
C


ATOM
787
OE1
GLU A
224
73.641
28.749
15.651
1.00
50.06
O


ATOM
788
OE2
GLU A
224
73.126
27.594
17.452
1.00
49.95
O


ATOM
789
N
LEU A
225
72.350
33.086
19.418
1.00
42.15
N


ATOM
790
CA
LEU A
225
71.453
33.175
20.558
1.00
40.63
C


ATOM
791
C
LEU A
225
70.303
32.200
20.332
1.00
39.80
C


ATOM
792
O
LEU A
225
69.475
32.407
19.445
1.00
39.10
O


ATOM
793
CB
LEU A
225
70.915
34.600
20.692
1.00
39.95
C


ATOM
794
CG
LEU A
225
70.043
34.870
21.920
1.00
39.53
C


ATOM
795
CD1
LEU A
225
70.866
34.649
23.180
1.00
39.09
C


ATOM
796
CD2
LEU A
225
69.509
36.292
21.871
1.00
38.92
C


ATOM
797
N
VAL A
226
70.255
31.143
21.138
1.00
39.41
N


ATOM
798
CA
VAL A
226
69.216
30.121
21.005
1.00
39.48
C


ATOM
799
C
VAL A
226
68.609
29.668
22.334
1.00
39.55
C


ATOM
800
O
VAL A
226
69.121
29.985
23.409
1.00
39.03
O


ATOM
801
CE
VAL A
226
69.772
28.859
20.301
1.00
39.18
C


ATOM
802
CG1
VAL A
226
70.195
29.185
18.873
1.00
38.53
C


ATOM
803
CG2
VAL A
226
70.951
28.313
21.092
1.00
39.07
C


ATOM
804
N
ASP A
227
67.506
28.926
22.245
1.00
40.09
N


ATOM
805
CA
ASP A
227
66.848
28.399
23.431
1.00
40.34
C


ATOM
806
C
ASP A
227
67.377
26.996
23.720
1.00
41.22
C


ATOM
807
O
ASP A
227
68.309
26.530
23.058
1.00
40.82
O


ATOM
808
CB
ASP A
227
65.324
28.359
23.253
1.00
40.17
C


ATOM
809
CG
ASP A
227
64.883
27.591
22.013
1.00
39.66
C


ATOM
810
OD1
ASP A
227
65.540
26.598
21.635
1.00
39.52
O


ATOM
811
OD2
ASP A
227
63.851
27.975
21.424
1.00
39.07
O


ATOM
812
N
SER A
228
66.778
26.328
24.705
1.00
42.36
N


ATOM
813
CA
SER A
228
67.190
24.979
25.098
1.00
43.39
C


ATOM
814
C
SER A
228
67.033
23.945
23.981
1.00
44.03
C


ATOM
815
O
SER A
228
67.660
22.884
24.022
1.00
44.51
O


ATOM
816
CE
SER A
228
66.398
24.526
26.328
1.00
43.24
C


ATOM
817
OG
SER A
228
65.008
24.504
26.053
1.00
43.57
O


ATOM
818
N
GLN A
229
66.199
24.255
22.993
1.00
44.53
N


ATOM
819
CA
GLN A
229
65.970
23.361
21.861
1.00
45.10
C


ATOM
820
C
GLN A
229
66.852
23.748
20.676
1.00
44.98
C


ATOM
821
O
GLN A
229
66.675
23.241
19.568
1.00
44.97
O


ATOM
822
CB
GLN A
229
64.497
23.407
21.431
1.00
45.98
C


ATOM
823
CG
GLN A
229
63.517
22.870
22.464
1.00
47.38
C


ATOM
824
CD
GLN A
229
62.069
22.994
22.014
1.00
48.68
C


ATOM
825
OE1
GLN A
229
61.684
22.476
20.962
1.00
49.59
O


ATOM
826
NE2
GLN A
229
61.259
23.683
22.810
1.00
49.07
N


ATOM
827
N
LYS A
230
67.793
24.657
20.919
1.00
44.98
N


ATOM
828
CA
LYS A
230
68.717
25.136
19.893
1.00
44.38
C


ATOM
829
C
LYS A
230
68.072
25.967
18.788
1.00
43.28
C


ATOM
830
O
LYS A
230
68.639
26.116
17.708
1.00
43.52
O


ATOM
831
CB
LYS A
230
69.486
23.961
19.274
1.00
45.73
C


ATOM
832
CG
LYS A
230
70.609
23.431
20.158
1.00
47.31
C


ATOM
833
CD
LYS A
230
71.619
24.538
20.461
1.00
49.00
C


ATOM
834
CE
LYS A
230
72.772
24.046
21.334
1.00
50.10
C


ATOM
835
NZ
LYS A
230
73.732
25.151
21.659
1.00
50.80
N


ATOM
836
N
ARG A
231
66.891
26.512
19.054
1.00
42.16
N


ATOM
837
CA
ARG A
231
66.206
27.344
18.068
1.00
41.22
C


ATOM
838
C
ARG A
231
66.596
28.797
18.324
1.00
40.06
C


ATOM
839
O
ARG A
231
66.782
29.199
19.474
1.00
39.86
O


ATOM
840
CB
ARG A
231
64.687
27.189
18.194
1.00
42.00
C


ATOM
841
CG
ARG A
231
64.195
25.742
18.119
1.00
43.23
C


ATOM
842
CD
ARG A
231
62.693
25.651
18.341
1.00
44.06
C


ATOM
843
NE
ARG A
231
62.304
26.202
19.636
1.00
45.39
N


ATOM
844
CZ
ARG A
231
61.047
26.309
20.058
1.00
46.06
C


ATOM
845
NH1
ARG A
231
60.047
25.900
19.287
1.00
46.08
N


ATOM
846
NH2
ARG A
231
60.787
26.833
21.251
1.00
46.43
N


ATOM
847
N
TYR A
232
66.730
29.578
17.256
1.00
38.48
N


ATOM
848
CA
TYR A
232
67.093
30.985
17.390
1.00
37.00
C


ATOM
849
C
TYR A
232
66.068
31.733
18.236
1.00
35.83
C


ATOM
850
O
TYR A
232
64.867
31.475
18.154
1.00
35.57
O


ATOM
851
CB
TYR A
232
67.183
31.656
16.015
1.00
37.19
C


ATOM
852
CG
TYR A
232
68.311
31.153
15.143
1.00
37.51
C


ATOM
853
CD1
TYR A
232
69.633
31.195
15.585
1.00
37.61
C


ATOM
854
CD2
TYR A
232
68.058
30.636
13.872
1.00
37.62
C


ATOM
855
CE1
TYR A
232
70.679
30.730
14.782
1.00
37.95
C


ATOM
856
CE2
TYR A
232
69.097
30.171
13.060
1.00
37.82
C


ATOM
857
CZ
TYR A
232
70.400
30.219
13.521
1.00
38.06
C


ATOM
858
OH
TYR A
232
71.422
29.752
12.729
1.00
38.65
O


ATOM
859
N
LEU A
233
66.547
32.654
19.061
1.00
34.40
N


ATOM
860
CA
LEU A
233
65.653
33.447
19.887
1.00
33.28
C


ATOM
861
C
LEU A
233
65.058
34.541
19.015
1.00
32.48
C


ATOM
862
O
LEU A
233
65.681
34.992
18.053
1.00
32.36
O


ATOM
863
CB
LEU A
233
66.418
34.080
21.057
1.00
33.73
C


ATOM
864
CG
LEU A
233
66.128
33.504
22.449
1.00
34.07
C


ATOM
865
CD1
LEU A
233
66.374
32.010
22.441
1.00
33.66
C


ATOM
866
CD2
LEU A
233
66.994
34.190
23.496
1.00
34.12
C


ATOM
867
N
VAL A
234
63.842
34.958
19.335
1.00
31.40
N


ATOM
868
CA
VAL A
234
63.210
36.020
18.574
1.00
30.69
C


ATOM
869
C
VAL A
234
62.213
36.752
19.447
1.00
30.26
C


ATOM
870
O
VAL A
234
61.584
36.156
20.319
1.00
30.27
O


ATOM
871
CB
VAL A
234
62.488
35.479
17.321
1.00
30.52
C


ATOM
872
CG1
VAL A
234
61.272
34.654
17.719
1.00
30.18
C


ATOM
873
CG2
VAL A
234
62.083
36.636
16.434
1.00
30.21
C


ATOM
874
N
GLY A
235
62.087
38.052
19.218
1.00
30.07
N


ATOM
875
CA
GLY A
235
61.158
38.851
19.987
1.00
29.43
C


ATOM
876
C
GLY A
235
60.039
39.341
19.095
1.00
29.31
C


ATOM
877
O
GLY A
235
60.105
39.201
17.874
1.00
29.17
O


ATOM
878
N
ALA A
236
59.011
39.922
19.699
1.00
28.71
N


ATOM
879
CA
ALA A
236
57.888
40.420
18.929
1.00
28.71
C


ATOM
880
C
ALA A
236
57.267
41.637
19.600
1.00
28.78
C


ATOM
881
O
ALA A
236
57.035
41.643
20.809
1.00
28.79
O


ATOM
882
CB
ALA A
236
56.846
39.320
18.768
1.00
28.81
C


ATOM
883
N
GLY A
237
57.007
42.670
18.809
1.00
28.64
N


ATOM
884
CA
GLY A
237
56.405
43.866
19.355
1.00
28.99
C


ATOM
885
C
GLY A
237
54.902
43.715
19.462
1.00
29.51
C


ATOM
886
O
GLY A
237
54.284
43.014
18.657
1.00
29.85
O


ATOM
887
N
ILE A
238
54.311
44.352
20.467
1.00
29.44
N


ATOM
888
CA
ILE A
238
52.866
44.301
20.649
1.00
29.75
C


ATOM
889
C
ILE A
238
52.370
45.707
20.959
1.00
30.10
C


ATOM
890
O
ILE A
238
53.150
46.580
21.332
1.00
29.88
O


ATOM
891
CE
ILE A
238
52.449
43.359
21.814
1.00
29.59
C


ATOM
892
CG1
ILE A
238
52.950
43.912
23.151
1.00
29.43
C


ATOM
893
CG2
ILE A
238
53.001
41.964
21.578
1.00
29.87
C


ATOM
894
CD1
ILE A
238
52.438
43.149
24.376
1.00
28.69
C


ATOM
895
N
ASN A
239
51.072
45.925
20.789
1.00
30.32
N


ATOM
896
CA
ASN A
239
50.488
47.224
21.067
1.00
30.41
C


ATOM
897
C
ASN A
239
49.515
47.095
22.233
1.00
30.69
C


ATOM
898
O
ASN A
239
49.107
45.992
22.599
1.00
30.13
O


ATOM
899
CB
ASN A
239
49.774
47.760
19.822
1.00
30.86
C


ATOM
900
CG
ASN A
239
48.606
46.892
19.397
1.00
30.89
C


ATOM
901
OD1
ASN A
239
47.610
46.785
20.108
1.00
30.90
O


ATOM
902
ND2
ASN A
239
48.724
46.269
18.231
1.00
31.26
N


ATOM
903
N
THR A
240
49.144
48.226
22.816
1.00
31.46
N


ATOM
904
CA
THR A
240
48.236
48.229
23.953
1.00
32.48
C


ATOM
905
C
THR A
240
46.760
48.143
23.557
1.00
33.71
C


ATOM
906
O
THR A
240
45.885
48.393
24.383
1.00
33.65
O


ATOM
907
CB
THR A
240
48.448
49.491
24.792
1.00
32.03
C


ATOM
908
OG1
THR A
240
48.264
50.635
23.957
1.00
31.61
O


ATOM
909
CG2
THR A
240
49.862
49.526
25.366
1.00
31.27
C


ATOM
910
N
ARG A
241
46.484
47.782
22.305
1.00
34.92
N


ATOM
911
CA
ARG A
241
45.100
47.680
21.837
1.00
36.67
C


ATOM
912
C
ARG A
241
44.578
46.259
21.614
1.00
36.73
C


ATOM
913
O
ARG A
241
43.619
45.848
22.262
1.00
36.77
O


ATOM
914
CB
ARG A
241
44.909
48.494
20.552
1.00
37.87
C


ATOM
915
CG
ARG A
241
44.891
50.010
20.755
1.00
40.48
C


ATOM
916
CD
ARG A
241
44.875
50.729
19.409
1.00
42.72
C


ATOM
917
NE
ARG A
241
44.876
52.188
19.522
1.00
44.49
N


ATOM
918
CZ
ARG A
241
43.818
52.916
19.866
1.00
45.58
C


ATOM
919
NE1
ARG A
241
42.661
52.325
20.140
1.00
46.47
N


ATOM
920
NH2
ARG A
241
43.909
54.239
19.912
1.00
45.69
N


ATOM
921
N
ASP A
242
45.202
45.505
20.713
1.00
36.96
N


ATOM
922
CA
ASP A
242
44.732
44.148
20.424
1.00
37.70
C


ATOM
923
C
ASP A
242
45.537
43.008
21.051
1.00
37.72
C


ATOM
924
O
ASP A
242
45.525
41.888
20.540
1.00
38.14
O


ATOM
925
CB
ASP A
242
44.663
43.927
18.904
1.00
37.89
C


ATOM
926
CG
ASP A
242
46.025
44.024
18.225
1.00
38.50
C


ATOM
927
OD1
ASP A
242
47.055
43.712
18.866
1.00
38.41
O


ATOM
928
OD2
ASP A
242
46.066
44.394
17.029
1.00
38.58
O


ATOM
929
N
PHE A
243
46.210
43.287
22.163
1.00
37.60
N


ATOM
930
CA
PHE A
243
47.043
42.293
22.838
1.00
37.44
C


ATOM
931
C
PHE A
243
46.355
41.022
23.339
1.00
37.84
C


ATOM
932
O
PHE A
243
46.992
39.970
23.425
1.00
37.47
O


ATOM
933
CB
PHE A
243
47.796
42.957
23.996
1.00
36.54
C


ATOM
934
CG
PHE A
243
46.903
43.587
25.022
1.00
35.45
C


ATOM
935
CD1
PHE A
243
46.382
42.833
26.066
1.00
35.41
C


ATOM
936
CD2
PHE A
243
46.594
44.940
24.955
1.00
35.12
C


ATOM
937
CE1
PHE A
243
45.566
43.416
27.033
1.00
34.98
C


ATOM
938
CE2
PHE A
243
45.780
45.534
25.916
1.00
35.22
C


ATOM
939
CZ
PHE A
243
45.265
44.769
26.959
1.00
35.05
C


ATOM
940
N
ARG A
244
45.072
41.114
23.675
1.00
38.36
N


ATOM
941
CA
ARG A
244
44.337
39.949
24.163
1.00
38.96
C


ATOM
942
C
ARG A
244
44.291
38.857
23.099
1.00
39.31
C


ATOM
943
O
ARG A
244
44.140
37.676
23.413
1.00
39.37
O


ATOM
944
CB
ARG A
244
42.913
40.340
24.579
1.00
38.87
C


ATOM
945
CG
ARG A
244
42.863
41.345
25.722
1.00
38.92
C


ATOM
946
CD
ARG A
244
41.440
41.607
26.189
1.00
38.85
C


ATOM
947
NE
ARG A
244
41.389
42.595
27.267
1.00
39.27
N


ATOM
948
CZ
ARG A
244
41.572
43.902
27.095
1.00
39.54
C


ATOM
949
NH1
ARG A
244
41.816
44.388
25.885
1.00
39.23
N


ATOM
950
NH2
ARG A
244
41.510
44.725
28.135
1.00
39.60
N


ATOM
951
N
GLU A
245
44.422
39.257
21.839
1.00
39.62
N


ATOM
952
CA
GLU A
245
44.413
38.300
20.742
1.00
39.94
C


ATOM
953
C
GLU A
245
45.822
38.091
20.183
1.00
39.41
C


ATOM
954
O
GLU A
245
46.214
36.965
19.873
1.00
39.17
O


ATOM
955
CB
GLU.A
245
43.477
38.772
19.618
1.00
41.18
C


ATOM
956
CG
GLU A
245
41.987
38.670
19.955
1.00
43.82
C


ATOM
957
CD
GLU A
245
41.479
39.800
20.848
1.00
45.62
C


ATOM
958
OE1
GLU A
245
40.433
39.604
21.510
1.00
46.25
O


ATOM
959
OE2
GLU A
245
42.105
40.889
20.881
1.00
46.89
O


ATOM
960
N
ARG A
246
46.584
39.177
20.067
1.00
38.53
N


ATOM
961
CA
ARG A
246
47.940
39.103
19.528
1.00
37.66
C


ATOM
962
C
ARG A
246
48.908
38.320
20.415
1.00
37.14
C


ATOM
963
O
ARG A
246
49.651
37.469
19.931
1.00
37.14
O


ATOM
964
CB
ARG A
246
48.490
40.516
19.287
1.00
36.94
C


ATOM
965
CG
ARG A
246
49.819
40.546
18.536
1.00
36.46
C


ATOM
966
CD
ARG A
246
50.278
41.970
18.276
1.00
35.96
C


ATOM
967
NE
ARG A
246
49.341
42.724
17.441
1.00
35.46
N


ATOM
968
CZ
ARG A
246
49.311
42.687
16.111
1.00
35.16
C


ATOM
969
NH1
ARG A
246
50.170
41.932
15.441
1.00
34.77
N


ATOM
970
NH2
ARG A
246
48.421
43.417
15.448
1.00
35.59
N


ATOM
971
N
VAL A
247
48.896
38.599
21.714
1.00
36.70
N


ATOM
972
CA
VAL A
247
49.802
37.919
22.630
1.00
36.48
C


ATOM
973
C
VAL A
247
49.701
36.389
22.572
1.00
36.82
C


ATOM
974
O
VAL A
247
50.702
35.710
22.328
1.00
36.60
O


ATOM
975
CB
VAL A
247
49.589
38.404
24.087
1.00
35.99
C


ATOM
976
CG1
VAL A
247
50.425
37.578
25.042
1.00
35.65
C


ATOM
977
CG2
VAL A
247
49.969
39.877
24.202
1.00
35.85
C


ATOM
978
N
PRO A
248
48.497
35.824
22.800
1.00
36.88
N


ATOM
979
CA
PRO A
248
48.355
34.363
22.756
1.00
36.60
C


ATOM
980
C
PRO A
248
48.891
33.775
21.453
1.00
36.20
C


ATOM
981
O
PRO A
248
49.538
32.729
21.450
1.00
36.15
O


ATOM
982
CB
PRO A
248
46.850
34.163
22.920
1.00
36.98
C


ATOM
983
CG
PRO A
248
46.469
35.306
23.823
1.00
36.81
C


ATOM
984
CD
PRO A
248
47.223
36.459
23.192
1.00
36.48
C


ATOM
985
N
ALA A
249
48.626
34.465
20.349
1.00
36.16
N


ATOM
986
CA
ALA A
249
49.087
34.025
19.042
1.00
36.32
C


ATOM
987
C
ALA A
249
50.613
34.043
19.000
1.00
36.64
C


ATOM
988
O
ALA A
249
51.242
33.137
18.444
1.00
36.51
O


ATOM
989
CB
ALA A
249
48.517
34.931
17.959
1.00
36.44
C


ATOM
990
N
LEU A
250
51.206
35.076
19.596
1.00
36.66
N


ATOM
991
CA
LEU A
250
52.660
35.202
19.629
1.00
36.66
C


ATOM
992
C
LEU A
250
53.284
34.148
20.540
1.00
36.79
C


ATOM
993
O
LEU A
250
54.328
33.586
20.222
1.00
36.30
O


ATOM
994
CB
LEU A
250
53.062
36.610
20.090
1.00
36.33
C


ATOM
995
CG
LEU A
250
53.366
37.679
19.026
1.00
36.54
C


ATOM
996
CD1
LEU A
250
52.849
37.266
17.658
1.00
36.13
C


ATOM
997
CD2
LEU A
250
52.757
39.002
19.461
1.00
35.88
C


ATOM
998
N
VAL A
251
52.644
33.878
21.671
1.00
37.78
N


ATOM
999
CA
VAL A
251
53.166
32.875
22.593
1.00
39.09
C


ATOM
1000
C
VAL A
251
53.103
31.507
21.928
1.00
39.91
C


ATOM
1001
O
VAL A
251
54.069
30.745
21.961
1.00
40.18
O


ATOM
1002
CB
VAL A
251
52.358
32.829
23.907
1.00
38.94
C


ATOM
1003
CG1
VAL A
251
52.815
31.651
24.761
1.00
39.25
C


ATOM
1004
CG2
VAL A
251
52.545
34.126
24.674
1.00
39.03
C


ATOM
1005
N
GLU A
252
51.963
31.200
21.317
1.00
40.90
N


ATOM
1006
CA
GLU A
252
51.794
29.918
20.642
1.00
41.65
C


ATOM
1007
C
GLU A
252
52.801
29.762
19.504
1.00
40.64
C


ATOM
1008
O
GLU A
252
53.293
28.666
19.251
1.00
40.83
O


ATOM
1009
CB
GLU A
252
50.370
29.784
20.095
1.00
43.45
C


ATOM
1010
CG
GLU A
252
49.477
28.839
20.889
1.00
46.51
C


ATOM
1011
CD
GLU A
252
49.239
29.298
22.318
1.00
48.31
C


ATOM
1012
OE1
GLU A
252
48.600
30.359
22.512
1.00
49.25
O


ATOM
1013
OE2
GLU A
252
49.691
28.589
23.249
1.00
49.10
O


ATOM
1014
N
ALA A
253
53.103
30.864
18.822
1.00
39.42
N


ATOM
1015
CA
ALA A
253
54.051
30.844
17.714
1.00
38.09
C


ATOM
1016
C
ALA A
253
55.488
30.617
18.189
1.00
37.51
C


ATOM
1017
O
ALA A
253
56.377
30.344
17.380
1.00
37.32
O


ATOM
1018
CB
ALA A
253
53.961
32.137
16.931
1.00
37.90
C


ATOM
1019
N
GLY A
254
55.715
30.740
19.495
1.00
36.62
N


ATOM
1020
CA
GLY A
254
57.048
30.521
20.033
1.00
35.88
C


ATOM
1021
C
GLY A
254
57.879
31.754
20.366
1.00
35.36
C


ATOM
1022
O
GLY A
254
59.072
31.632
20.651
1.00
34.95
O


ATOM
1023
N
ALA A
255
57.270
32.938
20.330
1.00
34.50
N


ATOM
1024
CA
ALA A
255
57.994
34.166
20.649
1.00
33.48
C


ATOM
1025
C
ALA A
255
58.659
34.025
22.019
1.00
32.88
C


ATOM
1026
O
ALA A
255
58.016
33.663
23.000
1.00
32.47
O


ATOM
1027
CB
ALA A
255
57.039
35.352
20.644
1.00
33.55
C


ATOM
1028
N
ASP A
256
59.954
34.309
22.079
1.00
32.31
N


ATOM
1029
CA
ASP A
256
60.703
34.185
23.323
1.00
31.81
C


ATOM
1030
C
ASP A
256
60.518
35.367
24.266
1.00
31.12
C


ATOM
1031
O
ASP A
256
60.649
35.232
25.481
1.00
30.65
O


ATOM
1032
CB
ASP A
256
62.181
33.994
22.999
1.00
31.98
C


ATOM
1033
CG
ASP A
256
62.425
32.745
22.182
1.00
32.65
C


ATOM
1034
OD1
ASP A
256
62.295
31.643
22.749
1.00
33.20
O


ATOM
1035
OD2
ASP A
256
62.725
32.860
20.975
1.00
32.82
O


ATOM
1036
N
VAL A
257
60.211
36.526
23.700
1.00
30.48
N


ATOM
1037
CA
VAL A
257
60.007
37.722
24.500
1.00
29.85
C


ATOM
1038
C
VAL A
257
59.153
38.696
23.708
1.00
29.52
C


ATOM
1039
O
VAL A
257
59.158
38.683
22.477
1.00
29.18
O


ATOM
1040
CB
VAL A
257
61.359
38.398
24.867
1.00
29.74
C


ATOM
1041
CG1
VAL A
257
62.118
38.768
23.603
1.00
29.96
C


ATOM
1042
CG2
VAL A
257
61.116
39.636
25.721
1.00
29.25
C


ATOM
1043
N
LEU A
258
58.410
39.530
24.422
1.00
28.83
N


ATOM
1044
CA
LEU A
258
57.556
40.513
23.785
1.00
28.70
C


ATOM
1045
C
LEU A
258
57.993
41.899
24.238
1.00
28.49
C


ATOM
1046
O
LEU A
258
58.752
42.041
25.198
1.00
28.65
O


ATOM
1047
CB
LEU A
258
56.094
40.289
24.189
1.00
28.62
C


ATOM
1048
CG
LEU A
258
55.534
38.871
24.065
1.00
29.10
C


ATOM
1049
CD1
LEU A
258
54.122
38.855
24.605
1.00
29.34
C


ATOM
1050
CD2
LEU A
258
55.573
38.407
22.610
1.00
29.01
C


ATOM
1051
N
CYS A
259
57.527
42.920
23.535
1.00
27.96
N


ATOM
1052
CA
CYS A
259
57.840
44.286
23.914
1.00
27.94
C


ATOM
1053
C
CYS A
259
56.759
45.216
23.403
1.00
27.70
C


ATOM
1054
O
CYS A
259
56.475
45.257
22.209
1.00
27.35
O


ATOM
1055
CB
CYS A
259
59.198
44.730
23.358
1.00
27.38
C


ATOM
1056
SG
CYS A
259
59.725
46.331
24.021
1.00
26.82
S


ATOM
1057
N
ILE A
260
56.143
45.950
24.320
1.00
28.21
N


ATOM
1058
CA
ILE A
260
55.108
46.898
23.943
1.00
28.49
C


ATOM
1059
C
ILE A
260
55.815
48.001
23.168
1.00
29.26
C


ATOM
1060
O
ILE A
260
56.769
48.615
23.657
1.00
28.86
O


ATOM
1061
CB
ILE A
260
54.421
47.483
25.182
1.00
28.21
C


ATOM
1062
CG1
ILE A
260
53.792
46.346
25.994
1.00
27.85
C


ATOM
1063
CG2
ILE A
260
53.373
48.510
24.761
1.00
27.76
C


ATOM
1064
CD1
ILE A
260
53.275
46.763
27.351
1.00
27.51
C


ATOM
1065
N
ASP A
261
55.344
48.233
21.951
1.00
29.87
N


ATOM
1066
CA
ASP A
261
55.920
49.224
21.062
1.00
30.69
C


ATOM
1067
C
ASP A
261
55.160
50.552
21.108
1.00
31.35
C


ATOM
1068
O
ASP A
261
54.046
50.659
20.597
1.00
31.90
O


ATOM
1069
CB
ASP A
261
55.934
48.632
19.651
1.00
31.21
C


ATOM
1070
CG
ASP A
261
56.417
49.603
18.599
1.00
31.62
C


ATOM
1071
OD1
ASP A
261
57.220
50.508
18.913
1.00
31.79
O


ATOM
1072
OD2
ASP A
261
55.997
49.438
17.437
1.00
32.40
O


ATOM
1073
N
SER A
262
55.767
51.562
21.727
1.00
31.57
N


ATOM
1074
CA
SER A
262
55.136
52.876
21.843
1.00
32.25
C


ATOM
1075
C
SER A
262
56.162
53.984
22.056
1.00
32.15
C


ATOM
1076
O
SER A
262
57.250
53.730
22.574
1.00
32.40
O


ATOM
1077
CB
SER A
262
54.146
52.871
23.012
1.00
32.42
C


ATOM
1078
OG
SER A
262
53.637
54.171
23.261
1.00
33.43
O


ATOM
1079
N
SER A
263
55.818
55.212
21.665
1.00
31.88
N


ATOM
1080
CA
SER A
263
56.734
56.331
21.847
1.00
31.98
C


ATOM
1081
C
SER A
263
56.658
56.839
23.280
1.00
31.45
C


ATOM
1082
O
SER A
263
57.683
57.118
23.898
1.00
32.24
O


ATOM
1083
CB
SER A
263
56.433
57.465
20.859
1.00
32.64
C


ATOM
1084
OG
SER A
263
55.121
57.971
20.999
1.00
35.89
O


ATOM
1085
N
ASP A
264
55.447
56.941
23.814
1.00
30.33
N


ATOM
1086
CA
ASP A
264
55.253
57.394
25.189
1.00
29.38
C


ATOM
1087
C
ASP A
264
54.694
56.241
26.026
1.00
28.76
C


ATOM
1088
O
ASP A
264
53.481
56.036
26.093
1.00
28.66
O


ATOM
1089
CB
ASP A
264
54.298
58.597
25.215
1.00
29.24
C


ATOM
1090
CG
ASP A
264
53.927
59.037
26.632
1.00
29.06
C


ATOM
1091
OD1
ASP A
264
54.618
58.666
27.606
1.00
28.24
O


ATOM
1092
OD2
ASP A
264
52.935
59.780
26.763
1.00
28.61
O


ATOM
1093
N
GLY A
265
55.594
55.497
26.664
1.00
27.72
N


ATOM
1094
CA
GLY A
265
55.194
54.358
27.474
1.00
26.80
C


ATOM
1095
C
GLY A
265
54.724
54.700
28.874
1.00
26.32
C


ATOM
1096
O
GLY A
265
54.304
53.815
29.622
1.00
25.26
O


ATOM
1097
N
PHE A
266
54.800
55.978
29.238
1.00
26.32
N


ATOM
1098
CA
PHE A
266
54.358
56.418
30.555
1.00
26.48
C


ATOM
1099
C
PHE A
266
52.841
56.551
30.402
1.00
27.26
C


ATOM
1100
O
PHE A
266
52.277
57.642
30.427
1.00
26.89
O


ATOM
1101
CB
PHE A
266
55.000
57.764
30.903
1.00
26.26
C


ATOM
1102
CG
PHE A
266
55.074
58.045
32.388
1.00
26.33
C


ATOM
1103
CD1
PHE A
266
54.336
57.289
33.301
1.00
25.12
C


ATOM
1104
CD2
PHE A
266
55.866
59.089
32.867
1.00
25.66
C


ATOM
1105
CE1
PHE A
266
54.385
57.569
34.664
1.00
25.49
C


ATOM
1106
CE2
PHE A
266
55.922
59.378
34.228
1.00
24.95
C


ATOM
1107
CZ
PHE A
266
55.179
58.617
35.131
1.00
25.18
C


ATOM
1108
N
SER A
267
52.195
55.403
30.239
1.00
28.41
N


ATOM
1109
CA
SER A
267
50.764
55.334
30.010
1.00
29.17
C


ATOM
1110
C
SER A
267
50.084
54.224
30.791
1.00
29.72
C


ATOM
1111
O
SER A
267
50.659
53.155
31.012
1.00
29.22
O


ATOM
1112
CB
SER A
267
50.515
55.112
28.521
1.00
29.55
C


ATOM
1113
OG
SER A
267
49.162
54.792
28.269
1.00
31.97
O


ATOM
1114
N
GLU A
268
48.844
54.482
31.188
1.00
30.02
N


ATOM
1115
CA
GLU A
268
48.072
53.506
31.927
1.00
31.13
C


ATOM
1116
C
GLU A
268
47.767
52.325
31.005
1.00
31.03
C


ATOM
1117
O
GLU A
268
47.618
51.195
31.462
1.00
30.56
O


ATOM
1118
CE
GLU A
268
46.775
54.139
32.437
1.00
32.14
C


ATOM
1119
CG
GLU A
268
45.961
53.213
33.322
1.00
34.23
C


ATOM
1120
CD
GLU A
268
44.724
53.872
33.902
1.00
35.72
C


ATOM
1121
OE1
GLU A
268
43.933
53.148
34.551
1.00
36.93
O


ATOM
1122
OE2
GLU A
268
44.542
55.099
33.717
1.00
35.59
O


ATOM
1123
N
TRP A
269
47.688
52.592
29.703
1.00
31.57
N


ATOM
1124
CA
TRP A
269
47.414
51.539
28.730
1.00
32.18
C


ATOM
1125
C
TRP A
269
48.488
50.453
28.800
1.00
32.07
C


ATOM
1126
O
TRP A
269
48.194
49.266
28.661
1.00
32.37
O


ATOM
1127
CB
TRP A
269
47.347
52.109
27.309
1.00
32.84
C


ATOM
1128
CG
TRP A
269
46.211
53.064
27.085
1.00
34.12
C


ATOM
1129
CD1
TRP A
269
46.306
54.401
26.827
1.00
34.63
C


ATOM
1130
CD2
TRP A
269
44.807
52.761
27.114
1.00
34.88
C


ATOM
1132
NE1
TRP A
269
45.051
54.950
26.694
1.00
35.25
N


ATOM
1132
CE2
TRP A
269
44.114
53.966
26.866
1.00
34.78
C


ATOM
1133
CE3
TRP A
269
44.068
51.587
27.325
1.00
35.27
C


ATOM
1134
CZ2
TRP A
269
42.717
54.035
26.823
1.00
35.56
C


ATOM
1135
CZ3
TRP A
269
42.675
51.655
27.284
1.00
35.55
C


ATOM
1136
CH2
TRP A
269
42.017
52.872
27.035
1.00
35.57
C


ATOM
1137
N
GLN A
270
49.736
50.855
29.013
1.00
31.69
N


ATOM
1138
CA
GLN A
270
50.808
49.875
29.114
1.00
31.74
C


ATOM
1139
C
GLN A
270
50.720
49.115
30.430
1.00
31.80
C


ATOM
1140
O
GLN A
270
51.002
47.916
30.480
1.00
32.05
O


ATOM
1141
CB
GLN A
270
52.179
50.544
28.965
1.00
30.95
C


ATOM
1142
CG
GLN A
270
52.461
50.929
27.526
1.00
30.42
C


ATOM
1143
CD
GLN A
270
53.936
50.960
27.191
1.00
29.71
C


ATOM
1144
OE1
GLN A
270
54.755
50.317
27.851
1.00
28.19
O


ATOM
1145
NE2
GLN A
270
54.278
51.691
26.141
1.00
28.75
N


ATOM
1146
N
LYS A
271
50.325
49.803
31.495
1.00
31.92
N


ATOM
1147
CA
LYS A
271
50.192
49.138
32.781
1.00
32.22
C


ATOM
1148
C
LYS A
271
49.114
48.065
32.643
1.00
31.72
C


ATOM
1149
O
LYS A
271
49.265
46.949
33.135
1.00
31.50
O


ATOM
1150
CB
LYS A
271
49.795
50.131
33.872
1.00
32.96
C


ATOM
1151
CG
LYS A
271
49.476
49.448
35.190
1.00
34.60
C


ATOM
1152
CD
LYS A
271
49.184
50.433
36.301
1.00
36.08
C


ATOM
1153
CE
LYS A
271
48.928
49.688
37.605
1.00
37.48
C


ATOM
1154
NZ
LYS A
271
48.792
50.615
38.769
1.00
39.24
N


ATOM
1155
N
ILE A
272
48.031
48.421
31.959
1.00
31.65
N


ATOM
1156
CA
ILE A
272
46.919
47.511
31.733
1.00
31.59
C


ATOM
1157
C
ILE A
272
47.351
46.309
30.904
1.00
31.68
C


ATOM
1158
O
ILE A
272
46.967
45.182
31.203
1.00
31.84
O


ATOM
1159
CB
ThE A
272
45.751
48.232
31.025
1.00
31.59
C


ATOM
1160
CG1
ILE A
272
45.058
49.167
32.018
1.00
30.96
C


ATOM
1161
CG2
ILE A
272
44.761
47.214
30.452
1.00
31.15
C


ATOM
1162
CD1
ILE A
272
44.109
50.157
31.367
1.00
30.73
C


ATOM
1163
N
THR A
273
48.151
46.548
29.869
1.00
31.76
N


ATOM
1164
CA
THR A
273
48.634
45.465
29.015
1.00
31.96
C


ATOM
1165
C
THR A
273
49.536
44.497
29.788
1.00
32.26
C


ATOM
1166
O
THR A
273
49.374
43.280
29.695
1.00
32.32
O


ATOM
1167
CB
THR A
273
49.406
46.020
27.806
1.00
32.10
C


ATOM
1168
OG1
THR A
273
48.522
46.813
27.004
1.00
32.10
O


ATOM
1169
CG2
THR A
273
49.970
44.890
26.960
1.00
32.28
C


ATOM
1170
N
ILE A
274
50.487
45.030
30.548
1.00
32.22
N


ATOM
1171
CA
ILE A
274
51.377
44.176
31.328
1.00
32.21
C


ATOM
1172
C
ILE A
274
50.558
43.401
32.366
1.00
32.57
C


ATOM
1173
O
ILE A
274
50.783
42.212
32.590
1.00
32.28
O


ATOM
1174
CB
ILE A
274
52.445
44.999
32.071
1.00
31.88
C


ATOM
1175
CG1
ILE A
274
53.279
45.802
31.070
1.00
31.35
C


ATOM
1176
CG2
ILE A
274
53.332
44.068
32.899
1.00
31.40
C


ATOM
1177
CD1
ILE A
274
54.276
46.749
31.724
1.00
31.35
C


ATOM
1178
N
GLY A
275
49.610
44.089
32.994
1.00
32.79
N


ATOM
1179
CA
GLY A
275
48.772
43.454
33.994
1.00
33.65
C


ATOM
1180
C
GLY A
275
47.998
42.274
33.438
1.00
33.76
C


ATOM
1181
O
GLY A
275
47.845
41.251
34.103
1.00
34.32
O


ATOM
1182
N
TRP A
276
47.505
42.412
32.214
1.00
33.77
N


ATOM
1183
CA
TRP A
276
46.752
41.341
31.580
1.00
34.23
C


ATOM
1184
C
TRP A
276
47.677
40.152
31.331
1.00
34.65
C


ATOM
1185
O
TRP A
276
47.293
39.001
31.536
1.00
34.89
O


ATOM
1186
CB
TRP A
276
46.163
41.821
30.253
1.00
34.33
C


ATOM
1187
CG
TRP A
276
45.278
40.809
29.591
1.00
34.90
C


ATOM
1188
CD1
TRP A
276
43.932
40.639
29.784
1.00
34.76
C


ATOM
1189
CD2
TRP A
276
45.675
39.817
28.635
1.00
34.98
C


ATOM
1190
NE1
TRP A
276
43.469
39.604
29.003
1.00
34.35
N


ATOM
1191
CE2
TRP A
276
44.516
39.082
28.289
1.00
34.87
C


ATOM
1192
CE3
TRP A
276
46.898
39.476
28.038
1.00
35.16
C


ATOM
1193
CZ2
TRP A
276
44.545
38.026
27.368
1.00
35.33
C


ATOM
1194
CZ3
TRP A
276
46.927
38.425
27.122
1.00
35.14
C


ATOM
1195
CH2
TRP A
276
45.755
37.713
26.797
1.00
35.58
C


ATOM
1196
N
ILE A
277
48.900
40.435
30.890
1.00
34.66
N


ATOM
1197
CA
ILE A
277
49.868
39.381
30.620
1.00
34.37
C


ATOM
1198
C
ILE A
277
50.227
38.622
31.900
1.00
35.02
C


ATOM
1199
O
ILE A
277
50.350
37.399
31.891
1.00
34.44
O


ATOM
1200
CE
ILE A
277
51.146
39.961
29.972
1.00
33.65
C


ATOM
1201
CG1
ILE A
277
50.802
40.550
28.604
1.00
33.07
C


ATOM
1202
CG2
ILE A
277
52.206
38.877
29.823
1.00
32.69
C


ATOM
1203
CD1
ILE A
277
51.952
41.268
27.926
1.00
32.85
C


ATOM
1204
N
ARG A
278
50.390
39.346
33.001
1.00
36.08
N


ATOM
1205
CA
ARG A
278
50.722
38.713
34.275
1.00
37.93
C


ATOM
1206
C
ARG A
278
49.570
37.835
34.757
1.00
39.10
C


ATOM
1207
O
ARG A
278
49.778
36.704
35.192
1.00
39.55
O


ATOM
1208
CB
ARG A
278
51.037
39.774
35.334
1.00
37.11
C


ATOM
1209
CG
ARG A
278
52.342
40.499
35.106
1.00
36.58
C


ATOM
1210
CD
ARG A
278
53.533
39.574
35.306
1.00
36.31
C


ATOM
1211
NE
ARG A
278
54.770
40.224
34.883
1.00
35.73
N


ATOM
1212
CZ
ARG A
278
55.478
39.861
33.819
1.00
35.12
C


ATOM
1213
NH1
ARG A
278
55.079
38.840
33.072
1.00
33.98
N


ATOM
1214
NH2
ARG A
278
56.569
40.539
33.487
1.00
34.31
N


ATOM
1215
N
GLU A
279
48.356
38.367
34.669
1.00
40.86
N


ATOM
1216
CA
GLU A
279
47.157
37.654
35.089
1.00
42.25
C


ATOM
1217
C
GLU A
279
46.961
36.339
34.331
1.00
42.65
C


ATOM
1218
O
GLU A
279
46.500
35.352
34.900
1.00
42.50
O


ATOM
1219
CB
GLU A
279
45.931
38.556
34.894
1.00
43.71
C


ATOM
1220
CG
GLU A
279
44.582
37.864
35.074
1.00
46.30
C


ATOM
1221
CD
GLU A
279
43.398
38.825
34.946
1.00
48.03
C


ATOM
1222
OE1
GLU A
279
43.314
39.555
33.928
1.00
48.89
O


ATOM
1223
OE2
GLU A
279
42.544
38.844
35.863
1.00
48.40
O


ATOM
1224
N
LYS A
280
47.324
36.319
33.055
1.00
42.53
N


ATOM
1225
CA
LYS A
280
47.144
35.116
32.255
1.00
42.83
C


ATOM
1226
C
LYS A
280
48.356
34.188
32.182
1.00
42.50
C


ATOM
1227
O
LYS A
280
48.201
32.975
32.047
1.00
42.55
O


ATOM
1228
CB
LYS A
280
46.723
35.499
30.834
1.00
43.85
C


ATOM
1229
CG
LYS A
280
46.229
34.321
30.008
1.00
45.53
C


ATOM
1230
CD
LYS A
280
45.821
34.743
28.602
1.00
46.52
C


ATOM
1231
CE
LYS A
280
45.103
33.612
27.871
1.00
46.76
C


ATOM
1232
NZ
LYS A
280
45.916
32.367
27.837
1.00
47.35
N


ATOM
1233
N
TYR A
281
49.557
34.749
32.287
1.00
41.56
N


ATOM
1234
CA
TYR A
281
50.771
33.949
32.172
1.00
40.39
C


ATOM
1235
C
TYR A
281
51.738
34.039
33.341
1.00
40.00
C


ATOM
1236
O
TYR A
281
52.746
33.335
33.360
1.00
39.98
O


ATOM
1237
CB
TYR A
281
51.530
34.355
30.910
1.00
40.02
C


ATOM
1238
CG
TYR A
281
50.757
34.204
29.625
1.00
39.56
C


ATOM
1239
CD1
TYR A
281
50.552
32.949
29.056
1.00
39.41
C


ATOM
1240
CD2
TYR A
281
50.255
35.322
28.957
1.00
39.51
C


ATOM
1241
CE1
TYR A
281
49.873
32.809
27.853
1.00
39.24
C


ATOM
1242
CE2
TYR A
281
49.571
35.193
27.752
1.00
39.30
C


ATOM
1243
CZ
TYR A
281
49.386
33.933
27.206
1.00
39.40
C


ATOM
1244
OH
TYR A
281
48.722
33.794
26.012
1.00
39.81
O


ATOM
1245
N
GLY A
282
51.444
34.892
34.313
1.00
39.64
N


ATOM
1246
CA
GLY A
282
52.365
35.045
35.422
1.00
39.49
C


ATOM
1247
C
GLY A
282
53.673
35.588
34.863
1.00
39.77
C


ATOM
1248
O
GLY A
282
53.665
36.379
33.916
1.00
39.23
O


ATOM
1249
N
ASP A
283
54.796
35.156
35.427
1.00
39.96
N


ATOM
1250
CA
ASP A
283
56.105
35.611
34.968
1.00
40.22
C


ATOM
1251
C
ASP A
283
56.709
34.682
33.916
1.00
39.77
C


ATOM
1252
O
ASP A
283
57.905
34.745
33.638
1.00
40.01
O


ATOM
1253
CB
ASP A
283
57.063
35.737
36.157
1.00
41.08
C


ATOM
1254
CG
ASP A
283
56.660
36.845
37.118
1.00
42.76
C


ATOM
1255
OD1
ASP A
283
56.621
38.024
36.696
1.00
43.36
O


ATOM
1256
OD2
ASP A
283
56.381
36.541
38.300
1.00
43.92
O


ATOM
1257
N
LYS A
284
55.882
33.825
33.328
1.00
39.38
N


ATOM
1258
CA
LYS A
284
56.354
32.887
32.314
1.00
39.05
C


ATOM
1259
C
LYS A
284
56.482
33.538
30.937
1.00
37.99
C


ATOM
1260
O
LYS A
284
57.178
33.026
30.061
1.00
38.55
O


ATOM
1261
CB
LYS A
284
55.416
31.678
32.234
1.00
40.57
C


ATOM
1262
CG
LYS A
284
55.327
30.866
33.526
1.00
42.45
C


ATOM
1263
CD
LYS A
284
56.686
30.300
33.930
1.00
44.18
C


ATOM
1264
CE
LYS A
284
56.559
29.340
35.112
1.00
45.45
C


ATOM
1265
NZ
LYS A
284
57.886
28.778
35.524
1.00
46.66
N


ATOM
1266
N
VAL A
285
55.793
34.655
30.741
1.00
36.07
N


ATOM
1267
CA
VAL A
285
55.863
35.383
29.482
1.00
34.18
C


ATOM
1268
C
VAL A
285
56.556
36.709
29.781
1.00
33.12
C


ATOM
1269
O
VAL A
285
56.094
37.486
30.619
1.00
32.87
O


ATOM
1270
CB
VAL A
285
54.453
35.630
28.899
1.00
33.89
C


ATOM
1271
CG1
VAL A
285
54.520
36.625
27.749
1.00
33.39
C


ATOM
1272
CG2
VAL A
285
53.868
34.311
28.408
1.00
33.56
C


ATOM
1273
N
LYS A
286
57.676
36.951
29.108
1.00
32.14
N


ATOM
1274
CA
LYSA
286
58.457
38.171
29.313
1.00
31.09
C


ATOM
1275
C
LYS A
286
57.988
39.305
28.407
1.00
30.39
C


ATOM
1276
O
LYS A
286
57.751
39.107
27.216
1.00
29.75
O


ATOM
1277
CB
LYS A
286
59.943
37.885
29.067
1.00
31.10
C


ATOM
1278
CG
LYS A
286
60.484
36.696
29.857
1.00
31.07
C


ATOM
1279
CD
LYS A
286
60.260
36.865
31.357
1.00
31.03
C


ATOM
1280
CE
LYS A
286
60.845
35.697
32.145
1.00
31.38
C


ATOM
1281
NZ
LYS A
286
60.578
35.811
33.619
1.00
31.84
N


ATOM
1282
N
VAL A
287
57.858
40.498
28.980
1.00
29.67
N


ATOM
1283
CA
VAL A
287
57.402
41.649
28.218
1.00
28.82
C


ATOM
1284
C
VAL A
287
58.123
42.952
28.571
1.00
28.35
C


ATOM
1285
O
VAL A
287
58.116
43.395
29.723
1.00
28.33
O


ATOM
1286
CB
VAL A
287
55.870
41.843
28.397
1.00
29.01
C


ATOM
1287
CG1
VAL A
287
55.514
41.886
29.873
1.00
29.59
C


ATOM
1288
CG2
VAL A
287
55.417
43.120
27.721
1.00
28.72
C


ATOM
1289
N
GLY A
288
58.754
43.555
27.568
1.00
27.62
N


ATOM
1290
CA
GLY A
288
59.441
44.817
27.771
1.00
26.79
C


ATOM
1291
C
GLY A
288
58.434
45.938
27.573
1.00
26.65
C


ATOM
1292
O
GLY A
288
57.403
45.737
26.922
1.00
26.44
O


ATOM
1293
N
ALA A
289
58.721
47.112
28.128
1.00
26.17
N


ATOM
1294
CA
ALA A
289
57.820
48.255
28.012
1.00
26.19
C


ATOM
1295
C
ALA A
289
58.591
49.543
27.741
1.00
26.50
C


ATOM
1296
O
ALA A
289
59.810
49.593
27.900
1.00
26.69
O


ATOM
1297
CB
ALA A
289
56.994
48.401
29.291
1.00
26.59
C


ATOM
1298
N
GLY A
290
57.871
50.584
27.331
1.00
26.15
N


ATOM
1299
CA
GLY A
290
58.502
51.856
27.037
1.00
25.55
C


ATOM
1300
C
GLY A
290
57.745
52.567
25.930
1.00
25.64
C


ATOM
1301
O
GLY A
290
56.726
52.059
25.470
1.00
25.93
O


ATOM
1302
N
ASN A
291
58.246
53.712
25.468
1.00
24.68
N


ATOM
1303
CA
ASN A
291
59.491
54.295
25.961
1.00
24.17
C


ATOM
1304
C
ASN A
291
59.309
55.373
27.022
1.00
23.88
C


ATOM
1305
O
ASN A
291
58.278
56.041
27.078
1.00
24.05
O


ATOM
1306
CB
ASN A
291
60.279
54.883
24.788
1.00
23.44
C


ATOM
1307
CG
ASN A
291
60.771
53.819
23.840
1.00
24.01
C


ATOM
1308
OD1
ASN A
291
60.266
52.695
23.849
1.00
24.09
O


ATOM
1309
ND2
ASN A
291
61.756
54.162
23.012
1.00
22.58
N


ATOM
1310
N
ILE A
292
60.323
55.522
27.867
1.00
23.43
N


ATOM
1311
CA
ILE A
292
60.329
56.541
28.906
1.00
23.67
C


ATOM
1312
C
ILE A
292
61.706
57.220
28.861
1.00
23.76
C


ATOM
1313
O
ILE A
292
62.642
56.688
28.247
1.00
23.31
O


ATOM
1314
CB
ILE A
292
60.033
55.936
30.324
1.00
23.51
C


ATOM
1315
CG1
ILE A
292
60.898
54.703
30.594
1.00
23.67
C


ATOM
1316
CG2
ILE A
292
58.561
55.563
30.426
1.00
23.40
C


ATOM
1317
CD1
ILE A
292
62.342
55.009
30.958
1.00
23.64
C


ATOM
1318
N
VAL A
293
61.823
58.393
29.481
1.00
23.36
N


ATOM
1319
CA
VAL A
293
63.084
59.137
29.478
1.00
23.68
C


ATOM
1320
C
VAL A
293
63.490
59.686
30.844
1.00
24.18
C


ATOM
1321
O
VAL A
293
64.459
60.439
30.946
1.00
24.31
O


ATOM
1322
CB
VAL A
293
63.033
60.329
28.480
1.00
23.27
C


ATOM
1323
CG1
VAL A
293
62.966
59.815
27.047
1.00
22.91
C


ATOM
1324
CG2
VAL A
293
61.823
61.209
28.776
1.00
22.79
C


ATOM
1325
N
ASP A
294
62.750
59.328
31.889
1.00
24.54
N


ATOM
1326
CA
ASP A
294
63.095
59.794
33.227
1.00
25.28
C


ATOM
1327
C
ASP A
294
62.808
58.743
34.300
1.00
25.54
C


ATOM
1328
O
ASP A
294
62.245
57.688
34.013
1.00
25.69
O


ATOM
1329
CB
ASP A
294
62.372
61.120
33.544
1.00
24.98
C


ATOM
1330
CG
ASP A
294
60.862
60.962
33.726
1.00
25.49
C


ATOM
1331
OD1
ASP A
294
60.290
59.921
33.347
1.00
26.22
O


ATOM
1332
OD2
ASP A
294
60.238
61.911
34.244
1.00
25.60
O


ATOM
1333
N
GLY A
295
63.221
59.031
35.531
1.00
26.27
N


ATOM
1334
CA
GLY A
295
63.008
58.106
36.628
1.00
26.98
C


ATOM
1335
C
GLY A
295
61.553
57.787
36.914
1.00
27.45
C


ATOM
1336
O
GLY A
295
61.216
56.643
37.216
1.00
27.19
O


ATOM
1337
N
GLU A
296
60.686
58.793
36.829
1.00
28.15
N


ATOM
1338
CA
GLU A
296
59.263
58.582
37.084
1.00
29.28
C


ATOM
1339
C
GLU A
296
58.669
57.578
36.110
1.00
28.28
C


ATOM
1340
O
GLU A
296
57.908
56.705
36.508
1.00
28.87
O


ATOM
1341
CB
GLU A
296
58.477
59.889
36.959
1.00
31.29
C


ATOM
1342
CG
GLU A
296
58.771
60.920
38.014
1.00
35.34
C


ATOM
1343
CD
GLU A
296
57.900
62.166
37.866
1.00
38.57
C


ATOM
1344
OE1
GLU A
296
58.213
63.169
38.544
1.00
40.66
O


ATOM
1345
OE2
GLU A
296
56.910
62.148
37.081
1.00
39.48
O


ATOM
1346
N
GLY A
297
58.996
57.728
34.830
1.00
27.39
N


ATOM
1347
CA
GLY A
297
58.482
56.819
33.821
1.00
26.83
C


ATOM
1348
C
GLY A
297
58.997
55.406
34.032
1.00
26.40
C


ATOM
1349
O
GLY A
297
58.261
54.436
33.850
1.00
26.39
O


ATOM
1350
N
PHE A
298
60.270
55.292
34.399
1.00
25.90
N


ATOM
1351
CA
PHE A
298
60.886
53.992
34.667
1.00
25.89
C


ATOM
1352
C
PHE A
298
60.156
53.324
35.825
1.00
26.26
C


ATOM
1353
O
PHE A
298
59.741
52.173
35.736
1.00
26.46
O


ATOM
1354
CB
PHE A
298
62.356
54.158
35.073
1.00
24.63
C


ATOM
1355
CG
PHE A
298
62.973
52.900
35.625
1.00
24.52
C


ATOM
1356
CD1
PHE A
298
63.510
51.935
34.774
1.00
24.45
C


ATOM
1357
CD2
PHE A
298
62.948
52.642
36.993
1.00
24.69
C


ATOM
1358
CE1
PHE A
298
64.004
50.729
35.283
1.00
24.11
C


ATOM
1359
CE2
PHE A
298
63.438
51.441
37.506
1.00
24.45
C


ATOM
1360
CZ
PHE A
298
63.965
50.485
36.648
1.00
24.01
C


ATOM
1361
N
ARG A
299
60.038
54.071
36.917
1.00
26.97
N


ATOM
1362
CA
ARG A
299
59.392
53.627
38.148
1.00
27.76
C


ATOM
1363
C
ARG A
299
57.979
53.112
37.896
1.00
27.50
C


ATOM
1364
O
ARG A
299
57.575
52.073
38.432
1.00
27.02
O


ATOM
1365
CB
ARG A
299
59.368
54.798
39.134
1.00
29.28
C


ATOM
1366
CG
ARG A
299
58.488
54.625
40.354
1.00
32.58
C


ATOM
1367
CD
ARG A
299
59.185
53.881
41.472
1.00
34.72
C


ATOM
1368
NE
ARG A
299
60.450
54.500
41.869
1.00
36.94
N


ATOM
1369
CZ
ARG A
299
61.175
54.093
42.911
1.00
37.49
C


ATOM
1370
NH1
ARG A
299
60.748
53.081
43.656
1.00
37.79
N


ATOM
1371
NH2
ARG A
299
62.336
54.671
43.191
1.00
37.51
N


ATOM
1372
N
TYR A
300
57.228
53.840
37.076
1.00
26.42
N


ATOM
1373
CA
TYR A
300
55.867
53.448
36.764
1.00
26.07
C


ATOM
1374
C
TYR A
300
55.807
52.106
36.028
1.00
25.82
C


ATOM
1375
O
TYR A
300
54.967
51.263
36.332
1.00
25.66
O


ATOM
1376
CB
TYR A
300
55.194
54.517
35.905
1.00
26.47
C


ATOM
1377
CG
TYR A
300
53.740
54.220
35.612
1.00
26.10
C


ATOM
1378
CD1
TYR A
300
52.755
54.430
36.583
1.00
25.70
C


ATOM
1379
CD2
TYR A
300
53.349
53.726
34.367
1.00
25.87
C


ATOM
1380
CE1
TYR A
300
51.413
54.157
36.318
1.00
25.69
C


ATOM
1381
CE2
TYR A
300
52.013
53.450
34.092
1.00
26.08
C


ATOM
1382
CZ
TYR A
300
51.052
53.671
35.069
1.00
26.05
C


ATOM
1383
OH
TYR A
300
49.729
53.428
34.780
1.00
26.67
O


ATOM
1384
N
LEU A
301
56.687
51.912
35.054
1.00
24.94
N


ATOM
1385
CA
LEU A
301
56.686
50.667
34.297
1.00
24.79
C


ATOM
1386
C
LEU A
301
57.290
49.516
35.104
1.00
25.13
C


ATOM
1387
O
LEU A
301
56.933
48.356
34.910
1.00
24.72
O


ATOM
1388
CD
LEU A
301
57.422
50.860
32.965
1.00
23.46
C


ATOM
1389
CG
LEU A
301
56.676
51.797
31.998
1.00
22.90
C


ATOM
1390
CD1
LEU A
301
57.460
51.938
30.687
1.00
21.27
C


ATOM
1391
CD2
LEU A
301
55.273
51.237
31.726
1.00
22.01
C


ATOM
1392
N
ALA A
302
58.194
49.844
36.020
1.00
25.45
N


ATOM
1393
CA
ALA A
302
58.803
48.828
36.867
1.00
26.43
C


ATOM
1394
C
ALA A
302
57.718
48.269
37.802
1.00
27.00
C


ATOM
1395
O
ALA A
302
57.551
47.053
37.912
1.00
26.60
O


ATOM
1396
CD
ALA A
302
59.944
49.433
37.676
1.00
25.79
C


ATOM
1397
N
ASP A
303
56.976
49.163
38.456
1.00
27.78
N


ATOM
1398
CA
ASP A
303
55.911
48.748
39.366
1.00
28.82
C


ATOM
1399
C
ASP A
303
54.817
48.007
38.606
1.00
29.16
C


ATOM
1400
O
ASP A
303
54.177
47.115
39.157
1.00
30.06
O


ATOM
1401
CD
ASP A
303
55.287
49.948
40.100
1.00
29.58
C


ATOM
1402
CG
ASP A
303
56.218
50.565
41.138
1.00
31.14
C


ATOM
1403
OD1
ASP A
303
57.081
49.848
41.693
1.00
31.95
O


ATOM
1404
OD2
ASP A
303
56.070
51.774
41.417
1.00
32.16
O


ATOM
1405
N
ALA A
304
54.594
48.382
37.348
1.00
28.83
N


ATOM
1406
CA
ALA A
304
53.581
47.721
36.531
1.00
28.20
C


ATOM
1407
C
ALA A
304
54.008
46.288
36.197
1.00
28.33
C


ATOM
1408
O
ALA A
304
53.179
45.461
35.818
1.00
28.02
O


ATOM
1409
CD
ALA A
304
53.343
48.499
35.260
1.00
27.85
C


ATOM
1410
N
GLY A
305
55.303
46.001
36.316
1.00
28.12
N


ATOM
1411
CA
GLY A
305
55.777
44.649
36.051
1.00
27.69
C


ATOM
1412
C
GLY A
305
56.626
44.386
34.820
1.00
27.36
C


ATOM
1413
O
GLY A
305
56.891
43.228
34.486
1.00
27.45
O


ATOM
1414
N
ALA A
306
57.064
45.439
34.141
1.00
26.93
N


ATOM
1415
CA
ALA A
306
57.884
45.268
32.945
1.00
26.72
C


ATOM
1416
C
ALA A
306
59.144
44.438
33.220
1.00
26.12
C


ATOM
1417
O
ALA A
306
59.759
44.557
34.277
1.00
26.19
O


ATOM
1418
CB
ALA A
306
58.271
46.642
32.382
1.00
26.69
C


ATOM
1419
N
ASP A
307
59.521
43.595
32.263
1.00
26.12
N


ATOM
1420
CA
ASP A
307
60.716
42.763
32.392
1.00
25.75
C


ATOM
1421
C
ASP A
307
61.976
43.541
31.989
1.00
25.56
C


ATOM
1422
O
ASP A
307
63.084
43.221
32.414
1.00
25.02
O


ATOM
1423
CD
ASP A
307
60.550
41.494
31.556
1.00
25.88
C


ATOM
1424
CG
ASP A
307
59.605
40.503
32.210
1.00
26.34
C


ATOM
1425
OD1
ASP A
307
59.941
40.031
33.316
1.00
25.65
O


ATOM
1426
OD2
ASP A
307
58.532
40.208
31.639
1.00
26.39
O


ATOM
1427
N
PHE A
308
61.791
44.553
31.148
1.00
25.21
N


ATOM
1428
CA
PHE A
308
62.872
45.435
30.739
1.00
25.37
C


ATOM
1429
C
PHE A
308
62.207
46.715
30.251
1.00
25.54
C


ATOM
1430
O
PHE A
308
61.096
46.689
29.718
1.00
26.05
O


ATOM
1431
CD
PHE A
308
63.803
44.781
29.692
1.00
24.85
C


ATOM
1432
CG
PHE A
308
63.254
44.722
28.286
1.00
25.59
C


ATOM
1433
CD1
PHE A
308
63.202
45.866
27.488
1.00
25.36
C


ATOM
1434
CD2
PHE A
308
62.863
43.499
27.730
1.00
25.52
C


ATOM
1435
CE1
PHE A
308
62.776
45.789
26.158
1.00
25.87
C


ATOM
1436
CE2
PHE A
308
62.435
43.413
26.397
1.00
25.33
C


ATOM
1437
CZ
PHE A
308
62.393
44.558
25.611
1.00
25.03
C


ATOM
1438
N
ILE A
309
62.860
47.844
30.490
1.00
25.29
N


ATOM
1439
CA
ILE A
309
62.293
49.126
30.118
1.00
25.21
C


ATOM
1440
C
ILE A
309
63.119
49.820
29.041
1.00
24.80
C


ATOM
1441
O
ILE A
309
64.338
49.945
29.152
1.00
24.39
O


ATOM
1442
CD
ILE A
309
62.124
50.001
31.390
1.00
25.06
C


ATOM
1443
CG1
ILE A
309
61.045
49.356
32.280
1.00
24.71
C


ATOM
1444
CG2
ILE A
309
61.743
51.429
31.018
1.00
24.45
C


ATOM
1445
CD1
ILE A
309
60.990
49.849
33.715
1.00
23.70
C


ATOM
1446
N
LYS A
310
62.430
50.249
27.988
1.00
24.64
N


ATOM
1447
CA
LYS A
310
63.066
50.895
26.850
1.00
24.86
C


ATOM
1448
C
LYS A
310
63.134
52.416
27.024
1.00
24.46
C


ATOM
1449
O
LYS A
310
62.146
53.060
27.373
1.00
24.21
O


ATOM
1450
CD
LYS A
310
62.311
50.509
25.574
1.00
25.07
C


ATOM
1451
CG
LYS A
310
63.177
50.404
24.340
1.00
25.07
C


ATOM
1452
CD
LYS A
310
62.769
49.218
23.461
1.00
25.06
C


ATOM
1453
CE
LYS A
310
61.376
49.398
22.850
1.00
25.52
C


ATOM
1454
NZ
LYS A
310
61.267
50.678
22.090
1.00
25.01
N


ATOM
1455
N
ILE A
311
64.316
52.971
26.768
1.00
24.00
N


ATOM
1456
CA
ILE A
311
64.571
54.401
26.925
1.00
23.52
C


ATOM
1457
C
ILE A
311
64.715
55.166
25.613
1.00
23.91
C


ATOM
1458
O
ILE A
311
65.486
54.776
24.737
1.00
23.10
O


ATOM
1459
CB
ILE A
311
65.883
54.643
27.715
1.00
22.79
C


ATOM
1460
CG1
ILE A
311
65.828
53.933
29.070
1.00
22.26
C


ATOM
1461
CG2
ILE A
311
66.121
56.146
27.878
1.00
21.49
C


ATOM
1462
CD1
ILE A
311
67.200
53.802
29.751
1.00
21.78
C


ATOM
1463
N
GLY A
312
63.991
56.270
25.484
1.00
24.94
N


ATOM
1464
CA
GLY A
312
64.137
57.058
24.280
1.00
26.52
C


ATOM
1465
C
GLY A
312
62.921
57.644
23.599
1.00
28.07
C


ATOM
1466
O
GLY A
312
62.052
56.925
23.108
1.00
27.43
O


ATOM
1467
N
ILE A
313
62.876
58.971
23.575
1.00
30.06
N


ATOM
1468
CA
ILE A
313
61.819
59.715
22.907
1.00
32.43
C


ATOM
1469
C
ILE A
313
62.497
60.917
22.262
1.00
34.74
C


ATOM
1470
O
ILE A
313
63.031
61.788
22.954
1.00
33.88
O


ATOM
1471
CB
ILE A
313
60.745
60.229
23.881
1.00
32.08
C


ATOM
1472
CG1
ILE A
313
60.029
59.055
24.554
1.00
31.93
C


ATOM
1473
CG2
ILE A
313
59.735
61.071
23.117
1.00
32.14
C


ATOM
1474
CD1
ILE A
313
58.970
59.481
25.560
1.00
31.83
C


ATOM
1475
N
GLY A
314
62.484
60.959
20.935
1.00
37.68
N


ATOM
1476
CA
GLY A
314
63.115
62.065
20.241
1.00
41.68
C


ATOM
1477
C
GLY A
314
64.614
61.848
20.205
1.00
44.77
C


ATOM
1478
O
GLY A
314
65.380
62.540
20.898
1.00
45.22
O


ATOM
1479
N
GLY A
315
65.025
60.864
19.406
1.00
46.78
N


ATOM
1480
CA
GLY A
315
66.432
60.539
19.265
1.00
49.14
C


ATOM
1481
C
GLY A
315
66.702
59.826
17.952
1.00
50.80
C


ATOM
1482
O
GLY A
315
67.732
60.057
17.310
1.00
51.20
O


ATOM
1483
N
GLY A
316
65.774
58.962
17.547
1.00
52.08
N


ATOM
1484
CA
GLY A
316
65.934
58.224
16.304
1.00
53.45
C


ATOM
1485
C
GLY A
316
66.265
59.085
15.092
1.00
54.43
C


ATOM
1486
O
GLY A
316
66.109
60.310
15.124
1.00
54.52
O


ATOM
1487
N
SER A
317
66.718
58.437
14.019
1.00
55.17
N


ATOM
1488
CA
SER A
317
67.086
59.120
12.776
1.00
55.85
C


ATOM
1489
C
SER A
317
66.116
60.238
12.410
1.00
56.05
C


ATOM
1490
O
SER A
317
66.224
60.838
11.338
1.00
56.24
O


ATOM
1491
CB
SER A
317
67.152
58.117
11.618
1.00
56.06
C


ATOM
1492
OG
SER A
317
68.116
57.109
11.864
1.00
56.47
O


ATOM
1493
N
ARG A
322
60.666
65.002
18.046
1.00
69.94
N


ATOM
1494
CA
ARG A
322
60.632
66.036
19.075
1.00
69.88
C


ATOM
1495
C
ARG A
322
60.442
67.421
18.458
1.00
69.25
C


ATOM
1496
O
ARG A
322
59.992
68.357
19.123
1.00
69.33
O


ATOM
1497
CB
ARG A
322
61.922
65.990
19.904
1.00
70.76
C


ATOM
1498
CG
ARG A
322
63.200
66.013
19.077
1.00
72.26
C


ATOM
1499
CD
ARG A
322
64.412
65.622
19.916
1.00
73.59
C


ATOM
1500
NE
ARG A
322
65.616
65.472
19.098
1.00
75.09
N


ATOM
1501
CZ
ARG A
322
66.295
66.483
18.561
1.00
75.74
C


ATOM
1502
NH1
ARG A
322
65.893
67.733
18.757
1.00
75.89
N


ATOM
1503
NH2
ARG A
322
67.372
66.241
17.818
1.00
75.84
N


ATOM
1504
N
GLU A
323
60.786
67.544
17.180
1.00
68.34
N


ATOM
1505
CA
GLU A
323
60.638
68.805
16.466
1.00
66.98
C


ATOM
1506
C
GLU A
323
59.314
68.796
15.706
1.00
65.40
C


ATOM
1507
O
GLU A
323
59.205
69.339
14.603
1.00
65.33
O


ATOM
1508
CB
GLU A
323
61.805
69.003
15.495
1.00
68.07
C


ATOM
1509
CG
GLU A
323
63.168
69.072
16.178
1.00
69.20
C


ATOM
1510
CD
GLU A
323
64.322
69.148
15.188
1.00
70.01
C


ATOM
1511
OE1
GLU A
323
64.371
70.116
14.393
1.00
70.24
O


ATOM
1512
OE2
GLU A
323
65.181
68.238
15.209
1.00
70.24
O


ATOM
1513
N
GLN A
324
58.311
68.163
16.311
1.00
63.21
N


ATOM
1514
CA
GLN A
324
56.982
68.075
15.722
1.00
60.76
C


ATOM
1515
C
GLN A
324
55.916
68.047
16.814
1.00
58.40
C


ATOM
1516
O
GLN A
324
54.859
68.662
16.679
1.00
58.63
O


ATOM
1517
CB
GLN A
324
56.861
66.821
14.852
1.00
61.63
C


ATOM
1518
CG
GLN A
324
55.533
66.714
14.120
1.00
62.44
C


ATOM
1519
CD
GLN A
324
55.341
67.814
13.085
1.00
63.06
C


ATOM
1520
OE1
GLN A
324
55.567
68.996
13.363
1.00
63.40
O


ATOM
1521
NE2
GLN A
324
54.910
67.431
11.887
1.00
63.02
N


ATOM
1522
N
LYS A
325
56.193
67.329
17.897
1.00
55.16
N


ATOM
1523
CA
LYS A
325
55.246
67.250
19.001
1.00
51.62
C


ATOM
1524
C
LYS A
325
55.822
67.983
20.207
1.00
48.73
C


ATOM
1525
O
LYS A
325
55.092
68.412
21.099
1.00
48.29
O


ATOM
1526
CB
LYS A
325
54.962
65.789
19.347
1.00
52.41
C


ATOM
1527
CG
LYS A
325
53.645
65.576
20.063
1.00
52.70
C


ATOM
1528
CD
LYS A
325
53.291
64.104
20.115
1.00
53.01
C


ATOM
1529
CE
LYS A
325
51.906
63.905
20.678
1.00
53.28
C


ATOM
1530
NZ
LYS A
325
51.527
62.469
20.681
1.00
54.05
N


ATOM
1531
N
GLY A
326
57.141
68.124
20.225
1.00
45.49
N


ATOM
1532
CA
GLY A
326
57.789
68.832
21.311
1.00
42.06
C


ATOM
1533
C
GLY A
326
58.097
68.028
22.558
1.00
39.58
C


ATOM
1534
O
GLY A
326
58.407
68.613
23.591
1.00
38.74
O


ATOM
1535
N
ILE A
327
58.002
66.703
22.478
1.00
37.33
N


ATOM
1536
CA
ILE A
327
58.302
65.861
23.629
1.00
35.54
C


ATOM
1537
C
ILE A
327
59.598
65.096
23.385
1.00
34.11
C


ATOM
1538
O
ILE A
327
59.911
64.723
22.256
1.00
33.94
O


ATOM
1539
CB
ILE A
327
57.165
64.836
23.936
1.00
35.64
C


ATOM
1540
CG1
ILE A
327
57.042
63.815
22.807
1.00
35.72
C


ATOM
1541
CG2
ILE A
327
55.837
65.563
24.130
1.00
35.90
C


ATOM
1542
CD1
ILE A
327
56.106
62.650
23.131
1.00
36.15
C


ATOM
1543
N
GLY A
328
60.357
64.869
24.447
1.00
32.52
N


ATOM
1544
CA
GLY A
328
61.599
64.142
24.295
1.00
30.76
C


ATOM
1545
C
GLY A
328
62.680
64.581
25.260
1.00
29.34
C


ATOM
1546
O
GLY A
328
62.447
65.403
26.153
1.00
27.81
O


ATOM
1547
N
ARG A
329
63.874
64.030
25.066
1.00
27.97
N


ATOM
1548
CA
ARG A
329
65.008
64.343
25.919
1.00
27.02
C


ATOM
1549
C
ARG A
329
66.265
63.793
25.272
1.00
26.17
C


ATOM
1550
O
ARG A
329
66.222
62.730
24.657
1.00
26.57
O


ATOM
1551
CB
ARG A
329
64.813
63.691
27.295
1.00
26.66
C


ATOM
1552
CG
ARG A
329
65.752
64.198
28.374
1.00
25.97
C


ATOM
1553
CD
ARG A
329
65.514
63.470
29.688
1.00
26.09
C


ATOM
1554
NE
ARG A
329
65.797
64.324
30.835
1.00
26.17
N


ATOM
1555
CZ
ARG A
329
65.626
63.964
32.103
1.00
27.08
C


ATOM
1556
NH1
ARG A
329
65.177
62.752
32.408
1.00
26.65
N


ATOM
1557
NH2
ARG A
329
65.884
64.829
33.072
1.00
27.28
N


ATOM
1558
N
GLY A
330
67.377
64.513
25.396
1.00
25.55
N


ATOM
1559
CA
GLY A
330
68.625
64.021
24.837
1.00
24.59
C


ATOM
1560
C
GLY A
330
68.797
62.587
25.311
1.00
24.12
C


ATOM
1561
O
GLY A
330
68.580
62.287
26.482
1.00
23.28
O


ATOM
1562
N
GLN A
331
69.180
61.698
24.404
1.00
24.45
N


ATOM
1563
CA
GLN A
331
69.332
60.286
24.729
1.00
24.31
C


ATOM
1564
C
GLN A
331
70.295
60.017
25.883
1.00
24.63
C


ATOM
1565
O
GLN A
331
70.000
59.191
26.751
1.00
24.51
O


ATOM
1566
CB
GLN A
331
69.772
59.505
23.486
1.00
24.66
C


ATOM
1567
CG
GLN A
331
69.635
57.989
23.627
1.00
25.35
C


ATOM
1568
CD
GLN A
331
68.181
57.536
23.753
1.00
26.40
C


ATOM
1569
OE1
GLN A
331
67.905
56.422
24.197
1.00
27.18
O


ATOM
1570
NE2
GLN A
331
67.251
58.395
23.351
1.00
25.73
N


ATOM
1571
N
ALA A
332
71.435
60.713
25.904
1.00
23.94
N


ATOM
1572
CA
ALA A
332
72.420
60.515
26.964
1.00
23.57
C


ATOM
1573
C
ALA A
332
71.833
60.835
28.338
1.00
23.62
C


ATOM
1574
O
ALA A
332
71.955
60.044
29.278
1.00
23.57
O


ATOM
1575
CB
ALA A
332
73.669
61.375
26.702
1.00
23.41
C


ATOM
1576
N
THR A
333
71.192
61.993
28.451
1.00
23.21
N


ATOM
1577
CA
THR A
333
70.584
62.403
29.707
1.00
22.90
C


ATOM
1578
C
THR A
333
69.500
61.408
30.105
1.00
23.18
C


ATOM
1579
O
THR A
333
69.380
61.031
31.273
1.00
22.90
O


ATOM
1580
CB
THR A
333
69.967
63.814
29.590
1.00
22.97
C


ATOM
1581
OG1
THR A
333
70.992
64.751
29.222
1.00
22.52
O


ATOM
1582
CG2
THR A
333
69.349
64.240
30.922
1.00
21.69
C


ATOM
1583
N
ALA A
334
68.717
60.977
29.123
1.00
23.07
N


ATOM
1584
CA
ALA A
334
67.648
60.018
29.373
1.00
23.70
C


ATOM
1585
C
ALA A
334
68.206
58.718
29.963
1.00
23.40
C


ATOM
1586
O
ALA A
334
67.717
58.223
30.977
1.00
23.84
O


ATOM
1587
CB
ALA A
334
66.890
59.731
28.070
1.00
23.17
C


ATOM
1588
N
VAL A
335
69.231
58.168
29.324
1.00
23.69
N


ATOM
1589
CA
VAL A
335
69.842
56.933
29.797
1.00
24.02
C


ATOM
1590
C
VAL A
335
70.430
57.107
31.194
1.00
24.09
C


ATOM
1591
O
VAL A
335
70.147
56.316
32.100
1.00
24.31
O


ATOM
1592
CB
VAL A
335
70.955
56.459
28.837
1.00
24.63
C


ATOM
1593
CG1
VAL A
335
71.682
55.254
29.431
1.00
25.02
C


ATOM
1594
CG2
VAL A
335
70.348
56.090
27.487
1.00
24.84
C


ATOM
1595
N
ILE A
336
71.240
58.147
31.371
1.00
24.11
N


ATOM
1596
CA
ILE A
336
71.867
58.416
32.661
1.00
23.87
C


ATOM
1597
C
ILE A
336
70.851
58.544
33.801
1.00
24.46
C


ATOM
1598
O
ILE A
336
71.039
57.963
34.874
1.00
23.73
O


ATOM
1599
CB
ILE A
336
72.725
59.701
32.607
1.00
23.25
C


ATOM
1600
CG1
ILE A
336
73.913
59.495
31.660
1.00
22.68
C


ATOM
1601
CG2
ILE A
336
73.234
60.055
34.008
1.00
22.89
C


ATOM
1602
CD1
ILE A
336
74.743
60.756
31.431
1.00
22.49
C


ATOM
1603
N
ASP A
337
69.775
59.296
33.572
1.00
24.98
N


ATOM
1604
CA
ASP A
337
68.759
59.479
34.606
1.00
25.52
C


ATOM
1605
C
ASP A
337
67.938
58.219
34.875
1.00
24.84
C


ATOM
1606
O
ASP A
337
67.629
57.907
36.024
1.00
24.56
O


ATOM
1607
CB
ASP A
337
67.818
60.637
34.245
1.00
27.31
C


ATOM
1608
CG
ASP A
337
68.502
62.000
34.327
1.00
30.71
C


ATOM
1609
OD1
ASP A
337
69.614
62.096
34.913
1.00
32.05
O


ATOM
1610
OD2
ASP A
337
67.918
62.983
33.815
1.00
31.24
O


ATOM
1611
N
VAL A
338
67.569
57.501
33.822
1.00
24.57
N


ATOM
1612
CA
VAL A
338
66.787
56.280
34.006
1.00
23.99
C


ATOM
1613
C
VAL A
338
67.631
55.230
34.735
1.00
23.85
C


ATOM
1614
O
VAL A
338
67.139
54.547
35.627
1.00
23.32
O


ATOM
1615
CB
VAL A
338
66.288
55.716
32.646
1.00
23.60
C


ATOM
1616
CG1
VAL A
338
65.631
54.347
32.848
1.00
23.15
C


ATOM
1617
CG2
VAL A
338
65.280
56.690
32.019
1.00
22.47
C


ATOM
1618
N
VAL A
339
68.906
55.126
34.362
1.00
23.84.
N


ATOM
1619
CA
VAL A
339
69.816
54.165
34.981
1.00
24.21
C


ATOM
1620
C
VAL A
339
69.980
54.429
36.480
1.00
25.13
C


ATOM
1621
O
VAL A
339
70.043
53.493
37.278
1.00
25.49
O


ATOM
1622
CB
VAL A
339
71.215
54.195
34.289
1.00
23.92
C


ATOM
1623
CG1
VAL A
339
72.270
53.502
35.158
1.00
23.40
C


ATOM
1624
CG2
VAL A
339
71.134
53.503
32.940
1.00
23.43
C


ATOM
1625
N
ALA A
340
70.053
55.700
36.866
1.00
25.88
N


ATOM
1626
CA
ALA A
340
70.202
56.042
38.278
1.00
26.36
C


ATOM
1627
C
ALA A
340
68.959
55.600
39.051
1.00
26.83
C


ATOM
1628
O
ALA A
340
69.053
55.132
40.185
1.00
26.86
O


ATOM
1629
CB
ALA A
340
70.419
57.540
38.437
1.00
26.17
C


ATOM
1630
N
GLU A
341
67.796
55.750
38.429
1.00
27.07
N


ATOM
1631
CA
GLU A
341
66.542
55.358
39.061
1.00
27.92
C


ATOM
1632
C
GLU A
341
66.472
53.834
39.131
1.00
27.70
C


ATOM
1633
O
GLU A
341
66.016
53.273
40.124
1.00
27.73
O


ATOM
1634
CB
GLU A
341
65.358
55.898
38.256
1.00
28.93
C


ATOM
1635
CG
GLU A
341
64.004
55.796
38.960
1.00
30.89
C


ATOM
1636
CD
GLU A
341
63.955
56.592
40.258
1.00
32.66
C


ATOM
1637
OE1
GLU A
341
64.480
57.727
40.299
1.00
34.48
O


ATOM
1638
OE2
GLU A
341
63.380
56.090
41.240
1.00
34.06
O


ATOM
1639
N
ARG A
342
66.926
53.173
38.067
1.00
27.14
N


ATOM
1640
CA
ARG A
342
66.928
51.714
37.999
1.00
26.71
C


ATOM
1641
C
ARG A
342
67.821
51.149
39.103
1.00
26.54
C


ATOM
1642
O
ARG A
342
67.497
50.130
39.716
1.00
26.18
O


ATOM
1643
CB
ARG A
342
67.426
51.254
36.618
1.00
25.95
C


ATOM
1644
CG
ARG A
342
67.409
49.739
36.373
1.00
24.78
C


ATOM
1645
CD
ARG A
342
68.642
49.033
36.940
1.00
23.69
C


ATOM
1646
NE
ARG A
342
69.905
49.458
36.335
1.00
23.29
N


ATOM
1647
CZ
ARG A
342
70.262
49.229
35.070
1.00
23.19
C


ATOM
1648
NH1
ARG A
342
69.453
48.574
34.247
1.00
22.48
N


ATOM
1649
NH2
ARG A
342
71.442
49.648
34.626
1.00
22.80
N


ATOM
1650
N
ASN A
343
68.943
51.815
39.354
1.00
26.63
N


ATOM
1651
CA
ASN A
343
69.866
51.363
40.389
1.00
27.25
C


ATOM
1652
C
ASN A
343
69.271
51.619
41.770
1.00
28.00
C


ATOM
1653
O
ASN A
343
69.415
50.804
42.680
1.00
27.55
O


ATOM
1654
CB
ASN A
343
71.222
52.055
40.238
1.00
26.44
C


ATOM
1655
CG
ASN A
343
71.979
51.575
39.008
1.00
26.67
C


ATOM
1656
OD1
ASN A
343
71.660
50.523
38.445
1.00
26.42
O


ATOM
1657
ND2
ASN A
343
72.995
52.330
38.595
1.00
25.68
N


ATOM
1658
N
LYS A
344
68.585
52.748
41.913
1.00
28.63
N


ATOM
1659
CA
LYS A
344
67.937
53.089
43.168
1.00
30.19
C


ATOM
1660
C
LYS A
344
66.852
52.044
43.419
1.00
30.06
C


ATOM
1661
O
LYS A
344
66.702
51.536
44.530
1.00
30.48
O


ATOM
1662
CB
LYS A
344
67.308
54.481
43.073
1.00
31.64
C


ATOM
1663
CG
LYS A
344
66.560
54.917
44.323
1.00
34.82
C


ATOM
1664
CD
LYS A
344
65.887
56.276
44.143
1.00
36.84
C


ATOM
1665
CE
LYS A
344
66.890
57.354
43.756
1.00
38.89
C


ATOM
1666
NZ
LYS A
344
66.248
58.707
43.638
1.00
41.17
N


ATOM
1667
N
TYR A
345
66.107
51.723
42.367
1.00
29.84
N


ATOM
1668
CA
TYR A
345
65.032
50.743
42.443
1.00
30.10
C


ATOM
1669
C
TYR A
345
65.576
49.370
42.854
1.00
30.60
C


ATOM
1670
O
TYR A
345
64.960
48.665
43.654
1.00
30.17
O


ATOM
1671
CB
TYR A
345
64.334
50.635
41.088
1.00
29.60
C


ATOM
1672
CG
TYR A
345
63.051
49.828
41.103
1.00
30.01
C


ATOM
1673
CD1
TYR A
345
61.847
50.407
41.508
1.00
29.92
C


ATOM
1674
CD2
TYR A
345
63.032
48.499
40.675
1.00
29.79
C


ATOM
1675
CE1
TYR A
345
60.658
49.690
41.476
1.00
30.21
C


ATOM
1676
CE2
TYR A
345
61.843
47.770
40.641
1.00
30.08
C


ATOM
1677
CZ
TYR A
345
60.662
48.376
41.040
1.00
30.51
C


ATOM
1678
OH
TYR A
345
59.479
47.685
40.978
1.00
31.68
O


ATOM
1679
N
PHE A
346
66.726
48.996
42.298
1.00
31.26
N


ATOM
1680
CA
PHE A
346
67.351
47.717
42.619
1.00
32.37
C


ATOM
1681
C
PHE A
346
67.722
47.651
44.102
1.00
33.09
C


ATOM
1682
O
PHE A
346
67.528
46.630
44.754
1.00
32.99
O


ATOM
1683
CB
PHE A
346
68.613
47.509
41.781
1.00
32.81
C


ATOM
1684
CG
PHE A
346
69.374
46.269
42.141
1.00
33.53
C


ATOM
1685
CD1
PHE A
346
68.841
45.011
41.881
1.00
33.63
C


ATOM
1686
CD2
PHE A
346
70.608
46.357
42.777
1.00
34.62
C


ATOM
1687
CE1
PHE A
346
69.519
43.858
42.246
1.00
34.10
C


ATOM
1688
CE2
PHE A
346
71.301
45.206
43.152
1.00
35.41
C


ATOM
1689
CZ
PHE A
346
70.750
43.950
42.883
1.00
35.25
C


ATOM
1690
N
GLU A
347
68.260
48.745
44.626
1.00
33.99
N


ATOM
1691
CA
GLU A
347
68.646
48.803
46.026
1.00
35.45
C


ATOM
1692
C
GLU A
347
67.435
48.732
46.958
1.00
35.29
C


ATOM
1693
O
GLU A
347
67.540
48.231
48.075
1.00
35.27
O


ATOM
1694
CB
GLU A
347
69.429
50.088
46.312
1.00
36.72
C


ATOM
1695
CG
GLU A
347
70.769
50.204
45.594
1.00
40.50
C


ATOM
1696
CD
GLU A
347
71.714
49.039
45.888
1.00
42.72
C


ATOM
1697
OE1
GLU A
347
71.826
48.625
47.069
1.00
44.09
O


ATOM
1698
OE2
GLU A
347
72.360
48.544
44.935
1.00
44.09
O


ATOM
1699
N
GLU A
348
66.287
49.225
46.504
1.00
35.07
N


ATOM
1700
CA
GLU A
348
65.089
49.221
47.337
1.00
35.42
C


ATOM
1701
C
GLU A
348
64.306
47.914
47.303
1.00
34.55
C


ATOM
1702
O
GLU A
348
63.739
47.502
48.309
1.00
34.49
O


ATOM
1703
CB
GLU A
348
64.127
50.339
46.915
1.00
37.00
C


ATOM
1704
CG
GLU A
348
64.759
51.699
46.683
1.00
39.47
C


ATOM
1705
CD
GLU A
348
63.750
52.738
46.194
1.00
40.68
C


ATOM
1706
OE1
GLU A
348
62.928
52.416
45.308
1.00
41.24
O


ATOM
1707
OE2
GLU A
348
63.788
53.883
46.690
1.00
41.95
O


ATOM
1708
N
THR A
349
64.281
47.266
46.143
1.00
33.77
N


ATOM
1709
CA
THR A
349
63.501
46.049
45.957
1.00
32.68
C


ATOM
1710
C
THR A
349
64.277
44.756
45.706
1.00
32.25
C


ATOM
1711
O
THR A
349
63.717
43.670
45.813
1.00
32.24
O


ATOM
1712
CB
THR A
349
62.534
46.231
44.770
1.00
32.69
C


ATOM
1713
OG1
THR A
349
63.296
46.372
43.562
1.00
32.06
O


ATOM
1714
CG2
THR A
349
61.678
47.481
44.959
1.00
32.19
C


ATOM
1715
N
GLY A
350
65.554
44.867
45.363
1.00
31.82
N


ATOM
1716
CA
GLY A
350
66.335
43.678
45.072
1.00
30.66
C


ATOM
1717
C
GLY A
350
66.068
43.202
43.648
1.00
29.93
C


ATOM
1718
O
GLY A
350
66.557
42.157
43.220
1.00
30.20
O


ATOM
1719
N
ILE A
351
65.287
43.978
42.906
1.00
28.99
N


ATOM
1720
CA
ILE A
351
64.950
43.633
41.529
1.00
27.61
C


ATOM
1721
C
ILE A
351
65.773
44.447
40.538
1.00
26.84
C


ATOM
1722
O
ILE A
351
65.744
45.675
40.558
1.00
26.06
O


ATOM
1723
CB
ILE A
351
63.459
43.901
41.239
1.00
27.81
C


ATOM
1724
CG1
ILE A
351
62.588
43.128
42.233
1.00
27.74
C


ATOM
1725
CG2
ILE A
351
63.123
43.498
39.802
1.00
27.06
C


ATOM
1726
CD1
ILE A
351
61.150
43.611
42.277
1.00
27.83
C


ATOM
1727
N
TYR A
352
66.518
43.757
39.681
1.00
26.12
N


ATOM
1728
CA
TYR A
352
67.323
44.431
38.675
1.00
25.65
C


ATOM
1729
C
TYR A
352
66.570
44.364
37.358
1.00
25.14
C


ATOM
1730
O
TYR A
352
66.344
43.279
36.829
1.00
25.00
O


ATOM
1731
CB
TYR A
352
68.682
43.754
38.490
1.00
24.90
C


ATOM
1732
CG
TYR A
352
69.562
44.497
37.502
1.00
24.91
C


ATOM
1733
CD1
TYR A
352
70.365
45.561
37.915
1.00
24.55
C


ATOM
1734
CD2
TYR A
352
69.574
44.150
36.152
1.00
24.86
C


ATOM
1735
CE1
TYR A
352
71.161
46.258
37.010
1.00
25.05
C


ATOM
1736
CE2
TYR A
352
70.371
44.843
35.234
1.00
24.70
C


ATOM
1737
CZ
TYR A
352
71.161
45.892
35.670
1.00
24.84
C


ATOM
1738
OH
TYR A
352
71.976
46.555
34.783
1.00
24.66
O


ATOM
1739
N
ILE A
353
66.181
45.522
36.835
1.00
25.14
N


ATOM
1740
CA
ILE A
353
65.455
45.581
35.574
1.00
24.39
C


ATOM
1741
C
ILE A
353
66.364
46.094
34.467
1.00
24.46
C


ATOM
1742
O
ILE A
353
66.838
47.229
34.519
1.00
24.61
O


ATOM
1743
CB
ILE A
353
64.234
46.515
35.678
1.00
25.03
C


ATOM
1744
CG1
ILE A
353
63.298
46.017
36.786
1.00
24.96
C


ATOM
1745
CG2
ILE A
353
63.499
46.567
34.336
1.00
24.60
C


ATOM
1746
CD1
ILE A
353
62.097
46.889
37.009
1.00
25.74
C


ATOM
1747
N
PRO A
354
66.635
45.256
33.453
1.00
24.02
N


ATOM
1748
CA
PRO A
354
67.504
45.700
32.356
1.00
23.55
C


ATOM
1749
C
PRO A
354
66.849
46.858
31.617
1.00
23.06
C


ATOM
1750
O
PRO A
354
65.627
46.896
31.491
1.00
23.02
O


ATOM
1751
CB
PRO A
354
67.619
44.454
31.470
1.00
23.02
C


ATOM
1752
CG
PRO A
354
67.455
43.318
32.455
1.00
23.37
C


ATOM
1753
CD
PRO A
354
66.323
43.819
33.334
1.00
23.29
C


ATOM
1754
N
VAL A
355
67.652
47.807
31.142
1.00
22.63
N


ATOM
1755
CA
VAL A
355
67.107
48.929
30.398
1.00
22.20
C


ATOM
1756
C
VAL A
355
67.732
48.959
29.011
1.00
22.50
C


ATOM
1757
O
VAL A
355
68.885
48.573
28.817
1.00
22.33
O


ATOM
1758
CB
VAL A
355
67.318
50.296
31.134
1.00
21.96
C


ATOM
1759
CG1
VAL A
355
66.618
50.258
32.483
1.00
20.76
C


ATOM
1760
CG2
VAL A
355
68.806
50.617
31.293
1.00
20.60
C


ATOM
1761
N
CYS A
356
66.950
49.408
28.044
1.00
23.02
N


ATOM
1762
CA
CYS A
356
67.394
49.457
26.667
1.00
23.36
C


ATOM
1763
C
CYS A
356
67.484
50.882
26.130
1.00
23.39
C


ATOM
1764
O
CYS A
356
66.510
51.633
26.191
1.00
22.96
O


ATOM
1765
CB
CYS A
356
66.422
48.643
25.801
1.00
23.63
C


ATOM
1766
SG
CYS A
356
66.671
48.801
24.017
1.00
24.61
S


ATOM
1767
N
SER A
357
68.657
51.255
25.621
1.00
23.18
N


ATOM
1768
CA
SER A
357
68.819
52.577
25.033
1.00
23.61
C


ATOM
1769
C
SER A
357
68.312
52.425
23.601
1.00
23.62
C


ATOM
1770
O
SER A
357
68.930
51.746
22.783
1.00
23.43
O


ATOM
1771
CB
SER A
357
70.283
53.013
25.027
1.00
23.25
C


ATOM
1772
OG
SER A
357
70.387
54.322
24.490
1.00
23.60
O


ATOM
1773
N
ASP A
358
67.177
53.051
23.315
1.00
24.07
N


ATOM
1774
CA
ASP A
358
66.554
52.951
21.998
1.00
25.02
C


ATOM
1775
C
ASP A
358
66.654
54.226
21.164
1.00
25.69
C


ATOM
1776
O
ASP A
358
66.047
55.244
21.494
1.00
24.92
O


ATOM
1777
CB
ASP A
358
65.081
52.549
22.182
1.00
24.37
C


ATOM
1778
CG
ASP A
358
64.336
52.369
20.867
1.00
24.57
C


ATOM
1779
OD1
ASP A
358
64.978
52.209
19.804
1.00
24.40
O


ATOM
1780
OD2
ASP A
358
63.088
52.369
20.909
1.00
24.16
O


ATOM
1781
N
GLY A
359
67.427
54.151
20.083
1.00
27.42
N


ATOM
1782
CA
GLY A
359
67.585
55.281
19.186
1.00
29.54
C


ATOM
1783
C
GLY A
359
68.670
56.272
19.559
1.00
31.70
C


ATOM
1784
O
GLY A
359
69.235
56.224
20.652
1.00
32.10
O


ATOM
1785
N
GLY A
360
68.975
57.171
18.631
1.00
33.51
N


ATOM
1786
CA
GLY A
360
69.983
58.183
18.883
1.00
35.62
C


ATOM
1787
C
GLY A
360
71.415
57.733
18.679
1.00
36.94
C


ATOM
1788
O
GLY A
360
72.343
58.451
19.049
1.00
37.99
O


ATOM
1789
N
ILE A
361
71.611
56.552
18.105
1.00
38.04
N


ATOM
1790
CA
ILE A
361
72.962
56.069
17.871
1.00
39.16
C


ATOM
1791
C
ILE A
361
73.376
56.307
16.426
1.00
40.31
C


ATOM
1792
O
ILE A
361
72.908
55.631
15.502
1.00
40.46
O


ATOM
1793
CB
ILE A
361
73.100
54.572
18.249
1.00
39.05
C


ATOM
1794
CG1
ILE A
361
73.124
54.459
19.783
1.00
39.14
C


ATOM
1795
CG2
ILE A
361
74.344
53.961
17.601
1.00
38.66
C


ATOM
1796
CD1
ILE A
361
73.769
53.223
20.332
1.00
38.76
C


ATOM
1797
N
VAL A
362
74.257
57.288
16.244
1.00
41.02
N


ATOM
1798
CA
VAL A
362
74.746
57.655
14.924
1.00
41.61
C


ATOM
1799
C
VAL A
362
76.048
56.942
14.566
1.00
41.66
C


ATOM
1800
O
VAL A
362
76.193
56.430
13.455
1.00
42.31
O


ATOM
1801
CB
VAL A
362
74.973
59.179
14.829
1.00
42.09
C


ATOM
1802
CG1
VAL A
362
75.272
59.577
13.386
1.00
42.28
C


ATOM
1803
CG2
VAL A
362
73.751
59.916
15.347
1.00
42.45
C


ATOM
1804
N
TYR A
363
76.987
56.902
15.510
1.00
41.20
N


ATOM
1805
CA
TYR A
363
78.282
56.260
15.283
1.00
40.38
C


ATOM
1806
C
TYR A
363
78.523
55.080
16.219
1.00
39.29
C


ATOM
1807
O
TYR A
363
77.904
54.985
17.278
1.00
38.90
O


ATOM
1808
CB
TYR A
363
79.396
57.293
15.454
1.00
41.48
C


ATOM
1809
CG
TYR A
363
79.233
58.478
14.535
1.00
43.32
C


ATOM
1810
CD1
TYR A
363
79.265
58.315
13.150
1.00
44.27
C


ATOM
1811
CD2
TYR A
363
79.001
59.755
15.045
1.00
44.05
C


ATOM
1812
CE1
TYR A
363
79.067
59.392
12.293
1.00
45.45
C


ATOM
1813
CE2
TYR A
363
78.801
60.841
14.197
1.00
45.25
C


ATOM
1814
CZ
TYR A
363
78.836
60.652
12.822
1.00
45.68
C


ATOM
1815
OH
TYR A
363
78.647
61.719
11.972
1.00
47.00
O


ATOM
1816
N
ASP A
364
79.425
54.182
15.828
1.00
37.99
N


ATOM
1817
CA
ASP A
364
79.731
53.016
16.649
1.00
36.91
C


ATOM
1818
C
ASP A
364
80.088
53.368
18.089
1.00
35.76
C


ATOM
1819
O
ASP A
364
79.629
52.701
19.018
1.00
35.85
O


ATOM
1820
CB
ASP A
364
80.892
52.202
16.062
1.00
37.35
C


ATOM
1821
CG
ASP A
364
80.504
51.412
14.824
1.00
37.70
C


ATOM
1822
OD1
ASP A
364
79.312
51.080
14.647
1.00
37.53
O


ATOM
1823
OD2
ASP A
364
81.417
51.102
14.033
1.00
38.32
O


ATOM
1824
N
TYR A
365
80.898
54.407
18.283
1.00
34.01
N


ATOM
1825
CA
TYR A
365
81.304
54.771
19.638
1.00
33.07
C


ATOM
1826
C
TYR A
365
80.131
55.199
20.524
1.00
31.99
C


ATOM
1827
O
TYR A
365
80.255
55.228
21.745
1.00
31.66
O


ATOM
1828
CB
TYR A
365
82.413
55.840
19.609
1.00
32.88
C


ATOM
1829
CG
TYR A
365
81.962
57.282
19.513
1.00
33.91
C


ATOM
1830
CD1
TYR A
365
81.650
58.015
20.660
1.00
33.73
C


ATOM
1831
CD2
TYR A
365
81.883
57.927
18.278
1.00
34.01
C


ATOM
1832
CE1
TYR A
365
81.275
59.357
20.578
1.00
34.76
C


ATOM
1833
CE2
TYR A
365
81.507
59.268
18.184
1.00
34.68
C


ATOM
1834
CZ
TYR A
365
81.206
59.977
19.335
1.00
34.89
C


ATOM
1835
OH
TYR A
365
80.841
61.302
19.239
1.00
35.48
O


ATOM
1836
N
HIS A
366
78.995
55.519
19.912
1.00
31.15
N


ATOM
1837
CA
HIS A
366
77.807
55.886
20.680
1.00
30.50
C


ATOM
1838
C
HIS A
366
77.305
54.640
21.411
1.00
29.58
C


ATOM
1839
O
HIS A
366
76.639
54.742
22.439
1.00
28.57
O


ATOM
1840
CB
HIS A
366
76.694
56.411
19.767
1.00
31.15
C


ATOM
1841
CG
HIS A
366
76.918
57.806
19.275
1.00
32.03
C


ATOM
1842
ND1
HIS A
366
77.928
58.613
19.753
1.00
32.57
N


ATOM
1843
CD2
HIS A
366
76.227
58.557
18.383
1.00
32.25
C


ATOM
1844
CE1
HIS A
366
77.848
59.800
19.179
1.00
32.26
C


ATOM
1845
NE2
HIS A
366
76.824
59.793
18.346
1.00
32.44
N


ATOM
1846
N
MET A
367
77.618
53.466
20.861
1.00
28.34
N


ATOM
1847
CA
MET A
367
77.215
52.201
21.475
1.00
27.90
C


ATOM
1848
C
MET A
367
77.951
52.050
22.801
1.00
26.79
C


ATOM
1849
O
MET A
367
77.350
51.752
23.829
1.00
26.19
O


ATOM
1850
CB
MET A
367
77.573
51.008
20.577
1.00
27.81
C


ATOM
1851
CG
MET A
367
76.771
50.894
19.285
1.00
28.28
C


ATOM
1852
SD
MET A
367
77.371
49.505
18.270
1.00
29.89
S


ATOM
1853
CE
MET A
367
76.390
49.722
16.782
1.00
29.69
C


ATOM
1854
N
THR A
368
79.262
52.256
22.758
1.00
26.73
N


ATOM
1855
CA
THR A
368
80.095
52.142
23.945
1.00
26.43
C


ATOM
1856
C
THR A
368
79.609
53.141
24.993
1.00
26.11
C


ATOM
1857
O
THR A
368
79.501
52.804
26.168
1.00
26.83
O


ATOM
1858
CB
THR A
368
81.572
52.399
23.592
1.00
26.81
C


ATOM
1859
OG1
THR A
368
81.911
51.638
22.424
1.00
26.87
O


ATOM
1860
CG2
THR A
368
82.480
51.975
24.738
1.00
26.28
C


ATOM
1861
N
LEU A
369
79.302
54.362
24.565
1.00
25.06
N


ATOM
1862
CA
LEU A
369
78.801
55.380
25.482
1.00
24.58
C


ATOM
1863
C
LEU A
369
77.494
54.938
26.142
1.00
23.99
C


ATOM
1864
O
LEU A
369
77.352
55.015
27.360
1.00
23.70
O


ATOM
1865
CB
LEU A
369
78.567
56.706
24.744
1.00
24.31
C


ATOM
1866
CG
LEU A
369
79.799
57.572
24.453
1.00
25.45
C


ATOM
1867
CD1
LEU A
369
79.369
58.829
23.700
1.00
24.63
C


ATOM
1868
CD2
LEU A
369
80.494
57.952
25.770
1.00
24.55
C


ATOM
1869
N
ALA A
370
76.544
54.478
25.330
1.00
23.02
N


ATOM
1870
CA
ALA A
370
75.250
54.031
25.833
1.00
22.95
C


ATOM
1871
C
ALA A
370
75.427
52.936
26.885
1.00
22.49
C


ATOM
1872
O
ALA A
370
74.777
52.951
27.930
1.00
22.45
O


ATOM
1873
CB
ALA A
370
74.380
53.519
24.674
1.00
21.80
C


ATOM
1874
N
LEU A
371
76.311
51.987
26.604
1.00
22.45
N


ATOM
1875
CA
LEU A
371
76.561
50.902
27.539
1.00
22.46
C


ATOM
1876
C
LEU A
371
77.268
51.435
28.793
1.00
22.58
C


ATOM
1877
O
LEU A
371
76.910
51.071
29.912
1.00
22.70
O


ATOM
1878
CB
LEU A
371
77.407
49.810
26.863
1.00
22.22
C


ATOM
1879
CG
LEU A
371
76.777
49.111
25.644
1.00
23.05
C


ATOM
1880
CD1
LEU A
371
77.821
48.224
24.960
1.00
23.28
C


ATOM
1881
CD2
LEU A
371
75.570
48.278
26.074
1.00
22.74
C


ATOM
1882
N
ALA A
372
78.259
52.306
28.607
1.00
22.30
N


ATOM
1883
CA
ALA A
372
79.001
52.863
29.736
1.00
22.69
C


ATOM
1884
C
ALA A
372
78.100
53..669
30.663
1.00
23.09
C


ATOM
1885
O
ALA A
372
78.320
53.705
31.874
1.00
22.83
O


ATOM
1886
CB
ALA A
372
80.140
53.738
29.236
1.00
22.43
C


ATOM
1887
N
MET A
373
77.087
54.316
30.091
1.00
23.19
N


ATOM
1888
CA
MET A
373
76.159
55.113
30.883
1.00
23.33
C


ATOM
1889
C
MET A
373
75.140
54.272
31.654
1.00
23.50
C


ATOM
1890
O
MET A
373
74.361
54.813
32.431
1.00
23.61
O


ATOM
1891
CB
MET A
373
75.437
56.127
29.992
1.00
23.33
C


ATOM
1892
CG
MET A
373
76.355
57.212
29.437
1.00
23.20
C


ATOM
1893
SD
MET A
373
75.548
58.296
28.242
1.00
24.70
S


ATOM
1894
CE
MET A
373
76.895
59.426
27.833
1.00
23.13
C


ATOM
1895
N
GLY A
374
75.135
52.956
31.437
1.00
23.73
N


ATOM
1896
CA
GLY A
374
74.210
52.108
32.174
1.00
23.47
C


ATOM
1897
C
GLY A
374
73.258
51.222
31.386
1.00
23.98
C


ATOM
1898
O
GLY A
374
72.709
50.266
31.941
1.00
24.30
O


ATOM
1899
N
ALA A
375
73.034
51.533
30.113
1.00
23.43
N


ATOM
1900
CA
ALA A
375
72.147
50.713
29.296
1.00
24.14
C


ATOM
1901
C
ALA A
375
72.716
49.298
29.212
1.00
24.24
C


ATOM
1902
O
ALA A
375
73.916
49.118
29.022
1.00
24.62
O


ATOM
1903
CB
ALA A
375
72.010
51.302
27.898
1.00
22.91
C


ATOM
1904
N
ASP A
376
71.848
48.304
29.369
1.00
24.28
N


ATOM
1905
CA
ASP A
376
72.248
46.905
29.301
1.00
24.39
C


ATOM
1906
C
ASP A
376
72.343
46.495
27.839
1.00
24.24
C


ATOM
1907
O
ASP A
376
73.206
45.708
27.455
1.00
24.28
O


ATOM
1908
CB
ASP A
376
71.227
46.042
30.040
1.00
24.71
C


ATOM
1909
CG
ASP A
376
71.144
46.385
31.518
1.00
25.23
C


ATOM
1910
OD1
ASP A
376
71.931
45.821
32.307
1.00
25.91
O


ATOM
1911
OD2
ASP A
376
70.304
47.234
31.890
1.00
25.50
O


ATOM
1912
N
PHE A
377
71.432
47.011
27.025
1.00
24.62
N


ATOM
1913
CA
PHE A
377
71.472
46.728
25.604
1.00
25.19
C


ATOM
1914
C
PHE A
377
70.944
47.899
24.795
1.00
25.15
C


ATOM
1915
O
PHE A
377
70.363
48.838
25.341
1.00
25.14
O


ATOM
1916
CB
PHE A
377
70.754
45.413
25.240
1.00
24.88
C


ATOM
1917
CG
PHE A
377
69.354
45.301
25.750
1.00
25.68
C


ATOM
1918
CD1
PHE A
377
69.105
44.892
27.056
1.00
25.76
C


ATOM
1919
CD2
PHE A
377
68.274
45.533
24.901
1.00
25.64
C


ATOM
1920
CE1
PHE A
377
67.795
44.709
27.512
1.00
25.70
C


ATOM
1921
CE2
PHE A
377
66.961
45.353
25.346
1.00
25.63
C


ATOM
1922
CZ
PHE A
377
66.724
44.939
26.653
1.00
26.08
C


ATOM
1923
N
ILE A
378
71.159
47.827
23.488
1.00
25.27
N


ATOM
1924
CA
ILE A
378
70.802
48.895
22.575
1.00
25.00
C


ATOM
1925
C
ILE A
378
69.858
48.454
21.466
1.00
25.29
C


ATOM
1926
O
ILE A
378
70.023
47.379
20.895
1.00
25.10
O


ATOM
1927
CB
ILE A
378
72.099
49.445
21.936
1.00
25.25
C


ATOM
1928
CG1
ILE A
378
73.083
49.820
23.043
1.00
24.86
C


ATOM
1929
CG2
ILE A
378
71.802
50.659
21.052
1.00
25.15
C


ATOM
1930
CD1
ILE A
378
74.499
49.981
22.560
1.00
26.24
C


ATOM
1931
N
MET A
379
68.859
49.285
21.177
1.00
25.26
N


ATOM
1932
CA
MET A
379
67.922
48.996
20.101
1.00
25.45
C


ATOM
1933
C
MET A
379
68.271
49.957
18.968
1.00
25.68
C


ATOM
1934
O
MET A
379
68.464
51.147
19.199
1.00
25.94
O


ATOM
1935
CB
MET A
379
66.467
49.208
20.546
1.00
25.00
C


ATOM
1936
CG
MET A
379
65.466
48.982
19.413
1.00
24.97
C


ATOM
1937
SD
MET A
379
63.735
48.885
19.881
1.00
24.78
S


ATOM
1938
CE
MET A
379
63.630
47.182
20.459
1.00
24.64
C


ATOM
1939
N
LEU A
380
68.367
49.443
17.747
1.00
26.01
N


ATOM
1940
CA
LEU A
380
68.712
50.287
16.606
1.00
26.36
C


ATOM
1941
C
LEU A
380
67.836
49.997
15.398
1.00
26.33
C


ATOM
1942
O
LEU A
380
67.452
48.852
15.160
1.00
25.51
O


ATOM
1943
CB
LEU A
380
70.183
50.090
16.208
1.00
26.63
C


ATOM
1944
CG
LEU A
380
71.270
50.303
17.268
1.00
27.60
C


ATOM
1945
CD1
LEU A
380
71.391
49.039
18.110
1.00
28.42
C


ATOM
1946
CD2
LED A
380
72.609
50.595
16.608
1.00
27.51
C


ATOM
1947
N
GLY A
381
67.529
51.048
14.644
1.00
26.78
N


ATOM
1948
CA
GLY A
381
66.720
50.907
13.446
1.00
27.90
C


ATOM
1949
C
GLY A
381
67.566
51.146
12.206
1.00
28.83
C


ATOM
1950
O
GLY A
381
67.879
50.215
11.465
1.00
28.61
O


ATOM
1951
N
ARG A
382
67.950
52.399
11.991
1.00
30.04
N


ATOM
1952
CA
ARG A
382
68.766
52.775
10.837
1.00
31.91
C


ATOM
1953
C
ARG A
382
69.988
51.873
10.639
1.00
31.42
C


ATOM
1954
O
ARG A
382
70.278
51.442
9.522
1.00
31.49
O


ATOM
1955
CB
ARG A
382
69.220
54.232
10.971
1.00
34.20
C


ATOM
1956
CG
ARG A
382
70.290
54.630
9.964
1.00
38.29
C


ATOM
1957
CD
ARG A
382
70.947
55.962
10.312
1.00
41.29
C


ATOM
1958
NE
ARG A
382
72.287
56.062
9.729
1.00
44.45
N


ATOM
1959
CZ
ARG A
382
72.542
56.128
8.423
1.00
45.83
C


ATOM
1960
NH1
ARG A
382
71.545
56.111
7.544
1.00
46.63
N


ATOM
1961
NH2
ARG A
382
73.796
56.202
7.994
1.00
46.53
N


ATOM
1962
N
TYR A
383
70.700
51.596
11.727
1.00
30.70
N


ATOM
1963
CA
TYR A
383
71.892
50.753
11.692
1.00
29.42
C


ATOM
1964
C
TYR A
383
71.652
49.421
10.978
1.00
29.27
C


ATOM
1965
O
TYR A
383
72.448
49.013
10.128
1.00
29.04
O


ATOM
1966
CB
TYR A
383
72.380
50.487
13.124
1.00
28.61
C


ATOM
1967
CG
TYR A
383
73.607
49.602
13.223
1.00
27.85
C


ATOM
1968
CD1
TYR A
383
74.894
50.134
13.107
1.00
27.60
C


ATOM
1969
CD2
TYR A
383
73.479
48.228
13.419
1.00
27.75
C


ATOM
1970
CE1
TYR A
383
76.020
49.317
13.185
1.00
27.67
C


ATOM
1971
CE2
TYR A
383
74.592
47.403
13.495
1.00
27.39
C


ATOM
1972
CZ
TYR A
383
75.859
47.948
13.377
1.00
27.90
C


ATOM
1973
OH
TYR A
383
76.958
47.118
13.438
1.00
27.45
O


ATOM
1974
N
PHE A
384
70.560
48.747
11.327
1.00
28.44
N


ATOM
1975
CA
PHE A
384
70.232
47.454
10.733
1.00
28.47
C


ATOM
1976
C
PHE A
384
69.521
47.555
9.381
1.00
28.91
C


ATOM
1977
O
PHE A
384
69.627
46.650
8.555
1.00
28.72
O


ATOM
1978
CB
PHE A
384
69.375
46.636
11.705
1.00
27.39
C


ATOM
1979
CG
PHE A
384
70.132
46.130
12.906
1.00
26.72
C


ATOM
1980
CD1
PHE A
384
71.098
45.132
12.768
1.00
25.87
C


ATOM
1981
CD2
PHE A
384
69.886
46.656
14.173
1.00
25.64
C


ATOM
1982
CE1
PHE A
384
71.807
44.664
13.868
1.00
25.34
C


ATOM
1983
CE2
PHE A
384
70.591
46.193
15.285
1.00
25.24
C


ATOM
1984
CZ
PHE A
384
71.554
45.195
15.134
1.00
24.96
C


ATOM
1985
N
ALA A
385
68.804
48.653
9.158
1.00
29.46
N


ATOM
1986
CA
ALA A
385
68.081
48.852
7.905
1.00
30.43
C


ATOM
1987
C
ALA A
385
69.024
48.849
6.701
1.00
31.20
C


ATOM
1988
O
ALA A
385
68.626
48.506
5.592
1.00
31.54
O


ATOM
1989
CB
ALA A
385
67.299
50.166
7.958
1.00
29.86
C


ATOM
1990
N
ARG A
386
70.278
49.226
6.934
1.00
32.25
N


ATOM
1991
CA
ARG A
386
71.291
49.281
5.883
1.00
32.76
C


ATOM
1992
C
ARG A
386
71.725
47.907
5.381
1.00
33.11
C


ATOM
1993
O
ARG A
386
72.310
47.794
4.305
1.00
32.93
O


ATOM
1994
CB
ARG A
386
72.542
49.995
6.392
1.00
33.15
C


ATOM
1995
CG
ARG A
386
72.363
51.434
6.832
1.00
34.37
C


ATOM
1996
CD
ARG A
386
73.645
51.881
7.510
1.00
34.93
C


ATOM
1997
NE
ARG A
386
74.002
50.939
8.567
1.00
36.03
N


ATOM
1998
CZ
ARG A
386
75.245
50.652
8.938
1.00
36.05
C


ATOM
1999
NH1
ARG A
386
76.278
51.233
8.338
1.00
35.62
N


ATOM
2000
NH2
ARG A
386
75.451
49.774
9.910
1.00
35.65
N


ATOM
2001
N
PHE A
387
71.447
46.867
6.158
1.00
33.64
N


ATOM
2002
CA
PHE A
387
71.875
45.525
5.787
1.00
34.50
C


ATOM
2003
C
PHE A
387
71.012
44.785
4.768
1.00
35.58
C


ATOM
2004
O
PHE A
387
69.818
45.037
4.623
1.00
35.41
O


ATOM
2005
CB
PHE A
387
72.040
44.665
7.046
1.00
33.89
C


ATOM
2006
CG
PHE A
387
72.940
45.276
8.091
1.00
33.56
C


ATOM
2007
CD1
PHE A
387
74.033
46.058
7.722
1.00
33.59
C


ATOM
2008
CD2
PHE A
387
72.707
45.050
9.444
1.00
33.20
C


ATOM
2009
CE1
PHE A
387
74.881
46.607
8.689
1.00
33.28
C


ATOM
2010
CE2
PHE A
387
73.547
45.592
10.417
1.00
32.86
C


ATOM
2011
CZ
PHE A
387
74.636
46.372
10.040
1.00
33.10
C


ATOM
2012
N
GLU A
388
71.647
43.859
4.064
1.00
37.23
N


ATOM
2013
CA
GLU A
388
70.979
43.061
3.048
1.00
38.92
C


ATOM
2014
C
GLU A
388
69.769
42.341
3.632
1.00
38.75
C


ATOM
2015
O
GLU A
388
68.737
42.209
2.972
1.00
38.22
O


ATOM
2016
CB
GLU A
388
71.957
42.034
2.473
1.00
40.97
C


ATOM
2Q17
CG
GLU A
388
71.424
41.264
1.272
1.00
44.75
C


ATOM
2018
CD
GLU A
388
72.279
40.056
0.934
1.00
47.13
C


ATOM
2019
OE1
GLU A
388
72.425
39.172
1.808
1.00
48.77
O


ATOM
2020
OE2
GLU A
388
72.803
39.985
−0.202
1.00
48.96
O


ATOM
2021
N
GLU A
389
69.899
41.886
4.876
1.00
38.62
N


ATOM
2022
CA
GLU A
389
68.823
41.159
5.534
1.00
38.62
C


ATOM
2023
C
GLU A
389
67.615
41.987
5.964
1.00
38.96
C


ATOM
2024
O
GLU A
389
66.621
41.424
6.413
1.00
39.16
O


ATOM
2025
CB
GLU A
389
69.369
40.375
6.732
1.00
37.80
C


ATOM
2026
CG
GLU A
389
70.398
39.320
6.347
1.00
36.96
C


ATOM
2027
CD
GLU A
389
71.834
39.798
6.504
1.00
36.79
C


ATOM
2028
OE1
GLU A
389
72.100
41.004
6.310
1.00
36.41
O


ATOM
2029
OE2
GLU A
389
72.704
38.958
6.808
1.00
35.78
O


ATOM
2030
N
SER A
390
67.679
43.310
5.843
1.00
39.56
N


ATOM
2031
CA
SER A
390
66.515
44.105
6.216
1.00
40.72
C


ATOM
2032
C
SER A
390
65.467
43.815
5.138
1.00
41.70
C


ATOM
2033
O
SER A
390
65.807
43.599
3.973
1.00
41.48
O


ATOM
2034
CB
SER A
390
66.844
45.598
6.278
1.00
40.08
C


ATOM
2035
OG
SER A
390
67.105
46.130
5.000
1.00
40.77
O


ATOM
2036
N
PRO A
391
64.181
43.804
5.515
1.00
42.67
N


ATOM
2037
CA
PRO A
391
63.073
43.523
4.595
1.00
43.86
C


ATOM
2038
C
PRO A
391
62.716
44.593
3.567
1.00
44.88
C


ATOM
2039
O
PRO A
391
61.651
44.530
2.959
1.00
45.36
O


ATOM
2040
CB
PRO A
391
61.917
43.245
5.550
1.00
43.53
C


ATOM
2041
CG
PRO A
391
62.172
44.253
6.634
1.00
42.86
C


ATOM
2042
CD
PRO A
391
63.672
44.149
6.858
1.00
42.43
C


ATOM
2043
N
THR A
392
63.588
45.570
3.361
1.00
46.16
N


ATOM
2044
CA
THR A
392
63.280
46.619
2.402
1.00
47.44
C


ATOM
2045
C
THR A
392
63.962
46.419
1.057
1.00
48.73
C


ATOM
2046
O
THR A
392
64.940
45.680
0.939
1.00
48.53
O


ATOM
2047
CB
THR A
392
63.646
48.010
2.955
1.00
47.37
C


ATOM
2048
OG1
THR A
392
65.056
48.081
3.190
1.00
47.28
O


ATOM
2049
CG2
THR A
392
62.901
48.266
4.264
1.00
47.46
C


ATOM
2050
N
ARG A
393
63.430
47.085
0.041
1.00
50.37
N


ATOM
2051
CA
ARG A
393
63.966
46.980
−1.305
1.00
52.41
C


ATOM
2052
C
ARG A
393
65.285
47.716
−1.481
1.00
52.98
C


ATOM
2053
O
ARG A
393
65.459
48.846
−1.020
1.00
52.98
O


ATOM
2054
CB
ARG A
393
62.936
47.494
−2.318
1.00
53.44
C


ATOM
2055
CG
ARG A
393
61.734
46.567
−2.475
1.00
54.94
C


ATOM
2056
CD
ARG A
393
60.591
47.199
−3.269
1.00
56.14
C


ATOM
2057
NE
ARG A
393
61.022
47.742
−4.554
1.00
57.05
N


ATOM
2058
CZ
ARG A
393
61.422
48.997
−4.739
1.00
57.73
C


ATOM
2059
NH1
ARG A
393
61.444
49.848
−3.720
1.00
58.03
N


ATOM
2060
NH2
ARG A
393
61.803
49.402
−5.943
1.00
58.01
N


ATOM
2061
N
LYS A
394
66.220
47.046
−2.141
1.00
53.68
N


ATOM
2062
CA
LYS A
394
67.526
47.616
−2.417
1.00
54.28
C


ATOM
2063
C
LYS A
394
67.338
48.454
−3.674
1.00
54.83
C


ATOM
2064
O
LYS A
394
66.910
47.943
−4.704
1.00
54.68
O


ATOM
2065
CB
LYS A
394
68.532
46.495
−2.670
1.00
53.95
C


ATOM
2066
CG
LYS A
394
69.979
46.924
−2.607
1.00
53.65
C


ATOM
2067
CD
LYS A
394
70.900
45.769
−2.961
1.00
53.38
C


ATOM
2068
CE
LYS A
394
70.731
44.601
−2.009
1.00
52.92
C


ATOM
2069
NZ
LYS A
394
71.581
43.452
−2.415
1.00
52.51
N


ATOM
2070
N
VAL A
395
67.640
49.742
−3.585
1.00
55.84
N


ATOM
2071
CA
VAL A
395
67.471
50.629
−4.724
1.00
57.03
C


ATOM
2072
C
VAL A
395
68.749
51.379
−5.052
1.00
57.77
C


ATOM
2073
O
VAL A
395
69.439
51.859
−4.159
1.00
58.06
O


ATOM
2074
CB
VAL A
395
66.352
51.653
−4.457
1.00
57.18
C


ATOM
2075
CG1
VAL A
395
66.227
52.612
−5.632
1.00
57.63
C


ATOM
2076
CG2
VAL A
395
65.036
50.926
−4.220
1.00
57.44
C


ATOM
2077
N
THR A
396
69.055
51.480
−6.340
1.00
58.78
N


ATOM
2078
CA
THR A
396
70.255
52.176
−6.786
1.00
59.74
C


ATOM
2079
C
THR A
396
69.940
53.611
−7.189
1.00
60.37
C


ATOM
2080
O
THR A
396
69.146
53.851
−8.096
1.00
60.74
O


ATOM
2081
CB
THR A
396
70.900
51.466
−7.989
1.00
59.62
C


ATOM
2082
OG1
THR A
396
71.197
50.110
−7.639
1.00
59.68
O


ATOM
2083
CG2
THR A
396
72.184
52.173
−8.394
1.00
59.73
C


ATOM
2084
N
ILE A
397
70.565
54.559
−6.502
1.00
61.02
N


ATOM
2085
CA
ILE A
397
70.366
55.974
−6.783
1.00
61.57
C


ATOM
2086
C
ILE A
397
71.659
56.562
−7.342
1.00
61.67
C


ATOM
2087
O
ILE A
397
72.589
56.872
−6.595
1.00
61.90
O


ATOM
2088
CB
ILE A
397
69.962
56.744
−5.506
1.00
61.92
C


ATOM
2089
CG1
ILE A
397
68.655
56.173
−4.950
1.00
62.18
C


ATOM
2090
CG2
ILE A
397
69.792
58.223
−5.817
1.00
62.12
C


ATOM
2091
CD1
ILE A
397
68.171
56.858
−3.689
1.00
62.37
C


ATOM
2092
N
ASN A
398
71.700
56.708
−8.663
1.00
61.56
N


ATOM
2093
CA
ASN A
398
72.856
57.247
−9.375
1.00
61.04
C


ATOM
2094
C
ASN A
398
74.211
56.789
−8.831
1.00
60.11
C


ATOM
2095
O
ASN A
398
74.960
57.570
−8.239
1.00
60.00
O


ATOM
2096
CB
ASN A
398
72.795
58.784
−9.415
1.00
62.12
C


ATOM
2097
CG
ASN A
398
72.965
59.425
−8.047
1.00
62.95
C


ATOM
2098
OD1
ASN A
398
72.154
59.222
−7.145
1.00
63.58
O


ATOM
2099
ND2
ASN A
398
74.026
60.216
−7.892
1.00
63.27
N


ATOM
2100
N
GLY A
399
74.516
55.512
−9.039
1.00
58.84
N


ATOM
2101
CA
GLY A
399
75.786
54.965
−8.593
1.00
57.27
C


ATOM
2102
C
GLY A
399
75.861
54.494
−7.153
1.00
56.12
C


ATOM
2103
O
GLY A
399
76.847
53.867
−6.761
1.00
56.17
O


ATOM
2104
N
SER A
400
74.835
54.788
−6.359
1.00
54.73
N


ATOM
2105
CA
SER A
400
74.832
54.379
−4.957
1.00
52.89
C


ATOM
2106
C
SER A
400
73.686
53.444
−4.603
1.00
51.55
C


ATOM
2107
O
SER A
400
72.517
53.775
−4.785
1.00
51.45
O


ATOM
2108
CB
SER A
400
74.779
55.608
−4.047
1.00
52.78
C


ATOM
2109
OG
SER A
400
75.979
56.353
−4.134
1.00
52.96
O


ATOM
2110
N
VAL A
401
74.030
52.268
−4.094
1.00
50.01
N


ATOM
2111
CA
VAL A
401
73.025
51.298
−3.697
1.00
48.59
C


ATOM
2112
C
VAL A
401
72.507
51.704
−2.320
1.00
48.17
C


ATOM
2113
O
VAL A
401
73.275
51.816
−1.360
1.00
47.91
O


ATOM
2114
CB
VAL A
401
73.620
49.883
−3.637
1.00
48.31
C


ATOM
2115
CG1
VAL A
401
72.563
48.892
−3.182
1.00
47.71
C


ATOM
2116
CG2
VAL A
401
74.167
49.499
−5.007
1.00
47.95
C


ATOM
2117
N
MET A
402
71.202
51.941
−2.238
1.00
47.38
N


ATOM
2118
CA
MET A
402
70.566
52.360
−0.998
1.00
46.51
C


ATOM
2119
C
MET A
402
69.492
51.365
−0.589
1.00
45.72
C


ATOM
2120
O
MET A
402
69.161
50.440
−1.333
1.00
45.52
O


ATOM
2121
CB
MET A
402
69.893
53.724
−1.179
1.00
47.39
C


ATOM
2122
CG
MET A
402
70.722
54.785
−1.882
1.00
47.80
C


ATOM
2123
SD
MET A
402
72.046
55.436
−0.875
1.00
49.53
S


ATOM
2124
CE
MET A
402
71.130
56.502
0.246
1.00
48.12
C


ATOM
2125
N
LYS A
403
68.953
51.568
0.606
1.00
44.48
N


ATOM
2126
CA
LYS A
403
67.879
50.735
1.118
1.00
43.18
C


ATOM
2127
C
LYS A
403
66.843
51.671
1.713
1.00
42.91
C


ATOM
2128
O
LYS A
403
67.178
52.736
2.232
1.00
42.51
O


ATOM
2129
CB
LYS A
403
68.387
49.759
2.180
1.00
42.62
C


ATOM
2130
CG
LYS A
403
69.316
48.691
1.632
1.00
41.97
C


ATOM
2131
CD
LYS A
403
69.087
47.352
2.306
1.00
41.27
C


ATOM
2132
CE
LYS A
403
67.729
46.777
1.941
1.00
40.54
C


ATOM
2133
NZ
LYS A
403
67.534
45.407
2.492
1.00
39.50
N


ATOM
2134
N
GLU A
404
65.580
51.280
1.622
1.00
42.89
N


ATOM
2135
CA
GLU A
404
64.500
52.097
2.146
1.00
42.99
C


ATOM
2136
C
GLU A
404
64.451
52.019
3.661
1.00
42.20
C


ATOM
2137
O
GLU A
404
64.760
50.987
4.254
1.00
41.68
O


ATOM
2138
CB
GLU A
404
63.166
51.623
1.580
1.00
44.40
C


ATOM
2139
CG
GLU A
404
63.131
51.559
0.071
1.00
46.68
C


ATOM
2140
CD
GLU A
404
61.810
51.042
−0.446
1.00
48.00
C


ATOM
2141
OE1
GLU A
404
61.485
49.856
−0.191
1.00
49.02
O


ATOM
2142
OE2
GLU A
404
61.095
51.827
−1.101
1.00
49.09
O


ATOM
2143
N
TYR A
405
64.061
53.124
4.284
1.00
41.51
N


ATOM
2144
CA
TYR A
405
63.949
53.180
5.729
1.00
40.50
C


ATOM
2145
C
TYR A
405
62.918
54.221
6.123
1.00
40.07
C


ATOM
2146
O
TYR A
405
63.100
55.416
5.882
1.00
40.71
O


ATOM
2147
CB
TYR A
405
65.294
53.524
6.365
1.00
40.22
C


ATOM
2148
CG
TYR A
405
65.231
53.579
7.872
1.00
40.08
C


ATOM
2149
CD1
TYR A
405
64.847
52.463
8.611
1.00
39.84
C


ATOM
2150
CD2
TYR A
405
65.539
54.750
8.561
1.00
40.31
C


ATOM
2151
CE1
TYR A
405
64.771
52.508
9.998
1.00
39.70
C


ATOM
2152
CE2
TYR A
405
65.466
54.807
9.949
1.00
40.16
C


ATOM
2153
CZ
TYR A
405
65.080
53.681
10.659
1.00
39.81
C


ATOM
2154
OH
TYR A
405
64.990
53.734
12.027
1.00
39.77
O


ATOM
2155
N
TRP A
406
61.830
53.764
6.729
1.00
38.92
N


ATOM
2156
CA
TRP A
406
60.773
54.666
7.153
1.00
38.11
C


ATOM
2157
C
TRP A
406
60.373
54.354
8.588
1.00
38.26
C


ATOM
2158
O
TRP A
406
60.439
53.202
9.026
1.00
37.61
O


ATOM
2159
CB
TRP A
406
59.565
54.545
6.212
1.00
36.65
C


ATOM
2160
CG
TRP A
406
58.932
53.186
6.184
1.00
35.15
C


ATOM
2161
CD1
TRP A
406
57.972
52.715
7.028
1.00
34.75
C


ATOM
2162
CD2
TRP A
406
59.246
52.111
5.293
1.00
34.82
C


ATOM
2163
NE1
TRP A
406
57.667
51.414
6.722
1.00
34.33
N


ATOM
2164
CE2
TRP A
406
58.437
51.015
5.661
1.00
34.71
C


ATOM
2165
CE3
TRP A
406
60.135
51.965
4.218
1.00
34.73
C


ATOM
2166
CZ2
TRP A
406
58.488
49.784
4.994
1.00
34.60
C


ATOM
2167
CZ3
TRP A
406
60.186
50.740
3.551
1.00
34.68
C


ATOM
2168
CH2
TRP A
406
59.366
49.666
3.946
1.00
34.70
C


ATOM
2169
N
GLY A
407
59.978
55.392
9.316
1.00
38.58
N


ATOM
2170
CA
GLY A
407
59.571
55.221
10.695
1.00
39.46
C


ATOM
2171
C
GLY A
407
58.182
54.625
10.820
1.00
40.35
C


ATOM
2172
O
GLY A
407
57.402
54.627
9.867
1.00
40.02
O


ATOM
2173
N
GLU A
408
57.878
54.102
12.003
1.00
41.35
N


ATOM
2174
CA
GLU A
408
56.578
53.506
12.271
1.00
42.48
C


ATOM
2175
C
GLU A
408
55.513
54.585
12.394
1.00
43.53
C


ATOM
2176
O
GLU A
408
54.320
54.302
12.334
1.00
43.54
O


ATOM
2177
CB
GLU A
408
56.641
52.682
13.555
1.00
42.13
C


ATOM
2178
CG
GLU A
408
57.446
51.408
13.410
1.00
41.70
C


ATOM
2179
CD
GLU A
408
56.789
50.416
12.464
1.00
41.39
C


ATOM
2180
OE1
GLU A
408
55.688
49.927
12.785
1.00
41.50
O


ATOM
2181
OE2
GLU A
408
57.370
50.126
11.401
1.00
40.96
O


ATOM
2182
N
GLY A
409
55.954
55.827
12.562
1.00
45.08
N


ATOM
2183
CA
GLY A
409
55.022
56.932
12.681
1.00
47.32
C


ATOM
2184
C
GLY A
409
54.711
57.588
11.345
1.00
48.91
C


ATOM
2185
O
GLY A
409
53.891
58.502
11.274
1.00
48.67
O


ATOM
2186
N
SER A
410
55.365
57.130
10.281
1.00
50.68
N


ATOM
2187
CA
SER A
410
55.132
57.699
8.958
1.00
52.76
C


ATOM
2188
C
SER A
410
53.849
57.131
8.373
1.00
54.23
C


ATOM
2189
O
SER A
410
53.454
56.008
8.689
1.00
53.75
O


ATOM
2190
CB
SER A
410
56.301
57.394
8.015
1.00
52.65
C


ATOM
2191
OG
SER A
410
56.325
56.026
7.646
1.00
53.09
O


ATOM
2192
N
SER A
411
53.200
57.918
7.520
1.00
56.27
N


ATOM
2193
CA
SER A
411
51.960
57.493
6.889
1.00
58.56
C


ATOM
2194
C
SER A
411
52.188
56.213
6.088
1.00
60.08
C


ATOM
2195
O
SER A
411
51.270
55.406
5.916
1.00
60.54
O


ATOM
2196
CB
SER A
411
51.430
58.600
5.973
1.00
58.70
C


ATOM
2197
OG
SER A
411
52.376
58.934
4.974
1.00
59.09
O


ATOM
2198
N
ARG A
412
53.418
56.027
5.612
1.00
61.61
N


ATOM
2199
CA
ARG A
412
53.770
54.844
4.831
1.00
63.31
C


ATOM
2200
C
ARG A
412
53.527
53.549
5.609
1.00
64.68
C


ATOM
2201
O
ARG A
412
53.565
52.457
5.043
1.00
64.66
O


ATOM
2202
CB
ARG A
412
55.236
54.921
4.385
1.00
62.76
C


ATOM
2203
CG
ARG A
412
55.694
53.712
3.581
1.00
62.41
C


ATOM
2204
CD
ARG A
412
57.020
53.948
2.877
1.00
61.98
C


ATOM
2205
NE
ARG A
412
57.408
52.776
2.097
1.00
61.77
N


ATOM
2206
CZ
ARG A
412
58.493
52.701
1.332
1.00
62.01
C


ATOM
2207
NH1
ARG A
412
59.321
53.736
1.229
1.00
61.70
N


ATOM
2208
NH2
ARG A
412
58.751
51.581
0.669
1.00
62.05
N


ATOM
2209
N
ALA A
413
53.273
53.681
6.908
1.00
66.59
N


ATOM
2210
CA
ALA A
413
53.016
52.532
7.770
1.00
68.37
C


ATOM
2211
C
ALA A
413
51.774
52.795
8.617
1.00
69.80
C


ATOM
2212
O
ALA A
413
50.907
53.587
8.232
1.00
70.13
O


ATOM
2213
CB
ALA A
413
54.222
52.279
8.672
1.00
68.21
C


ATOM
2214
N
ARG A
414
51.697
52.124
9.767
1.00
71.35
N


ATOM
2215
CA
ARG A
414
50.586
52.267
10.715
1.00
72.93
C


ATOM
2216
C
ARG A
414
49.190
52.288
10.097
1.00
73.77
C


ATOM
2217
O
ARG A
414
48.213
52.609
10.774
1.00
73.88
O


ATOM
2218
CB
ARG A
414
50.783
53.530
11.570
1.00
73.43
C


ATOM
2219
CG
ARG A
414
51.031
54.815
10.779
1.00
74.17
C


ATOM
2220
CD
ARG A
414
51.446
55.967
11.688
1.00
74.85
C


ATOM
2221
NE
ARG A
414
50.307
56.638
12.308
1.00
75.54
N


ATOM
2222
CZ
ARG A
414
49.508
57.492
11.675
1.00
75.93
C


ATOM
2223
NH1
ARG A
414
49.724
57.784
10.398
1.00
76.05
N


ATOM
2224
NH2
ARG A
414
48.495
58.059
12.319
1.00
76.11
N


ATOM
2225
N
ASN A
415
49.098
51.936
8.819
1.00
74.50
N


ATOM
2226
CA
ASN A
415
47.818
51.923
8.124
1.00
75.19
C


ATOM
2227
C
ASN A
415
47.577
50.540
7.515
1.00
75.37
C


ATOM
2228
O
ASN A
415
47.344
50.406
6.311
1.00
75.45
O


ATOM
2229
CB
ASN A
415
47.809
52.996
7.028
1.00
75.72
C


ATOM
2230
CG
ASN A
415
46.402
53.424
6.634
1.00
76.17
C


ATOM
2231
OD1
ASN A
415
46.214
54.171
5.671
1.00
76.40
O


ATOM
2232
ND2
ASN A
415
45.406
52.958
7.385
1.00
76.16
N


ATOM
2233
N
TRP A
416
47.644
49.516
8.361
1.00
75.41
N


ATOM
2234
CA
TRP A
416
47.437
48.136
7.931
1.00
75.40
C


ATOM
2235
C
TRP A
416
46.062
47.625
8.366
1.00
75.38
C


ATOM
2236
O
TRP A
416
45.571
47.959
9.448
1.00
75.34
O


ATOM
2237
CB
TRP A
416
48.532
47.232
8.515
1.00
75.24
C


ATOM
2238
CG
TRP A
416
48.733
47.426
9.990
1.00
74.99
C


ATOM
2239
CD1
TRP A
416
49.406
48.449
10.599
1.00
74.96
C


ATOM
2240
CD2
TRP A
416
48.190
46.620
11.044
1.00
74.76
C


ATOM
2241
NE1
TRP A
416
49.311
48.333
11.966
1.00
74.83
N


ATOM
2242
CE2
TRP A
416
48.570
47.220
12.267
1.00
74.77
C


ATOM
2243
CE3
TRP A
416
47.415
45.453
11.075
1.00
74.57
C


ATOM
2244
CZ2
TRP A
416
48.200
46.691
13.510
1.00
74.66
C


ATOM
2245
CZ3
TRP A
416
47.047
44.927
12.313
1.00
74.66
C


ATOM
2246
CH2
TRP A
416
47.442
45.549
13.513
1.00
74.65
C


ATOM
2247
N
GLU A
431
54.518
61.394
12.341
1.00
65.44
N


ATOM
2248
CA
GLU A
431
55.528
61.368
13.394
1.00
65.56
C


ATOM
2249
C
GLU A
431
56.862
60.844
12.879
1.00
64.74
C


ATOM
2250
O
GLU A
431
57.864
60.865
13.595
1.00
64.65
O


ATOM
2251
CB
GLU A
431
55.072
60.484
14.557
1.00
66.48
C


ATOM
2252
CG
GLU A
431
53.806
60.944
15.256
1.00
68.09
C


ATOM
2253
CD
GLU A
431
53.483
60.087
16.469
1.00
69.15
C


ATOM
2254
OE1
GLU A
431
53.319
58.854
16.306
1.00
69.66
O


ATOM
2255
OE2
GLU A
431
53.397
60.647
17.586
1.00
69.60
O


ATOM
2256
N
GLY A
432
56.873
60.368
11.641
1.00
63.84
N


ATOM
2257
CA
GLY A
432
58.100
59.842
11.080
1.00
62.59
C


ATOM
2258
C
GLY A
432
58.315
60.225
9.633
1.00
61.80
C


ATOM
2259
O
GLY A
432
57.421
60.765
8.977
1.00
61.75
O


ATOM
2260
N
VAL A
433
59.513
59.938
9.135
1.00
60.79
N


ATOM
2261
CA
VAL A
433
59.867
60.246
7.758
1.00
59.34
C


ATOM
2262
C
VAL A
433
60.128
58.968
6.964
1.00
58.28
C


ATOM
2263
O
VAL A
433
60.193
57.874
7.527
1.00
58.02
O


ATOM
2264
CB
VAL A
433
61.124
61.149
7.700
1.00
59.34
C


ATOM
2265
CG1
VAL A
433
60.851
62.462
8.413
1.00
59.24
C


ATOM
2266
CG2
VAL A
433
62.309
60.442
8.336
1.00
59.25
C


ATOM
2267
N
ASP A
434
60.263
59.122
5.651
1.00
56.94
N


ATOM
2268
CA
ASP A
434
60.528
58.010
4.747
1.00
55.49
C


ATOM
2269
C
ASP A
434
61.778
58.380
3.957
1.00
54.43
C


ATOM
2270
O
ASP A
434
61.777
59.359
3.210
1.00
54.60
O


ATOM
2271
CB
ASP A
434
59.333
57.808
3.809
1.00
55.70
C


ATOM
2272
CG
ASP A
434
59.529
56.653
2.849
1.00
55.96
C


ATOM
2273
OD1
ASP A
434
59.987
55.578
3.288
1.00
56.51
O


ATOM
2274
OD2
ASP A
434
59.212
56.812
1.652
1.00
56.42
O


ATOM
2275
N
SER A
435
62.845
57.602
4.119
1.00
52.71
N


ATOM
2276
CA
SER A
435
64.099
57.908
3.440
1.00
50.99
C


ATOM
2277
C
SER A
435
64.910
56.705
2.962
1.00
49.63
C


ATOM
2278
O
SER A
435
64.416
55.581
2.891
1.00
48.99
O


ATOM
2279
CB
SER A
435
64.971
58.757
4.366
1.00
51.10
C


ATOM
2280
OG
SER A
435
65.160
58.097
5.608
1.00
50.72
O


ATOM
2281
N
TYR A
436
66.172
56.970
2.640
1.00
48.33
N


ATOM
2282
CA
TYR A
436
67.091
55.947
2.163
1.00
47.20
C


ATOM
2283
C
TYR A
436
68.375
55.936
2.984
1.00
45.70
C


ATOM
2284
O
TYR A
436
68.863
56.987
3.400
1.00
45.68
O


ATOM
2285
CB
TYR A
436
67.452
56.211
0.699
1.00
48.21
C


ATOM
2286
CG
TYR A
436
66.289
56.130
−0.260
1.00
49.01
C


ATOM
2287
CD1
TYR A
436
65.771
54.895
−0.656
1.00
49.13
C


ATOM
2288
CD2
TYR A
436
65.701
57.288
−0.769
1.00
49.35
C


ATOM
2289
CE1
TYR A
436
64.694
54.816
−1.538
1.00
49.77
C


ATOM
2290
CE2
TYR A
436
64.622
57.221
−1.650
1.00
49.98
C


ATOM
2291
CZ
TYR A
436
64.125
55.982
−2.029
1.00
49.99
C


ATOM
2292
OH
TYR A
436
63.054
55.911
−2.891
1.00
50.64
O


ATOM
2293
N
VAL A
437
68.913
54.743
3.214
1.00
43.68
N


ATOM
2294
CA
VAL A
437
70.164
54.591
3.944
1.00
41.96
C


ATOM
2295
C
VAL A
437
71.139
53.869
3.025
1.00
40.88
C


ATOM
2296
O
VAL A
437
70.741
53.013
2.238
1.00
40.43
O


ATOM
2297
CB
VAL A
437
69.992
53.765
5.245
1.00
41.57
C


ATOM
2298
CG1
VAL A
437
69.165
54.547
6.252
1.00
41.59
C


ATOM
2299
CG2
VAL A
437
69.341
52.433
4.936
1.00
41.15
C


ATOM
2300
N
PRO A
438
72.431
54.210
3.107
1.00
40.34
N


ATOM
2301
CA
PRO A
438
73.428
53.559
2.252
1.00
39.68
C


ATOM
2302
C
PRO A
438
73.553
52.068
2.546
1.00
39.03
C


ATOM
2303
O
PRO A
438
73.591
51.656
3.708
1.00
38.81
O


ATOM
2304
CB
PRO A
438
74.706
54.329
2.570
1.00
39.92
C


ATOM
2305
CG
PRO A
438
74.512
54.693
4.014
1.00
40.33
C


ATOM
2306
CD
PRO A
438
73.072
55.149
4.043
1.00
40.10
C


ATOM
2307
N
TYR A
439
73.606
51.267
1.486
1.00
38.09
N


ATOM
2308
CA
TYR A
439
73.736
49.821
1.614
1.00
37.58
C


ATOM
2309
C
TYR A
439
75.059
49.499
2.299
1.00
37.43
C


ATOM
2310
O
TYR A
439
76.098
50.048
1.948
1.00
37.52
O


ATOM
2311
CB
TYR A
439
73.688
49.170
0.229
1.00
36.98
C


ATOM
2312
CG
TYR A
439
73.817
47.666
0.237
1.00
36.27
C


ATOM
2313
CD1
TYR A
439
72.869
46.871
0.870
1.00
36.31
C


ATOM
2314
CD2
TYR A
439
74.879
47.034
−0.414
1.00
36.64
C


ATOM
2315
CE1
TYR A
439
72.970
45.479
0.856
1.00
36.58
C


ATOM
2316
CE2
TYR A
439
74.989
45.646
−0.434
1.00
36.33
C


ATOM
2317
CZ
TYR A
439
74.030
44.877
0.202
1.00
36.46
C


ATOM
2318
OH
TYR A
439
74.134
43.506
0.187
1.00
37.16
O


ATOM
2319
N
ALA A
440
75.024
48.598
3.272
1.00
37.46
N


ATOM
2320
CA
ALA A
440
76.236
48.251
4.002
1.00
37.42
C


ATOM
2321
C
ALA A
440
76.672
46.809
3.794
1.00
37.20
C


ATOM
2322
O
ALA A
440
77.760
46.424
4.213
1.00
37.15
O


ATOM
2323
CB
ALA A
440
76.033
48.523
5.494
1.00
37.18
C


ATOM
2324
N
GLY A
441
75.828
46.016
3.145
1.00
37.04
N


ATOM
2325
CA
GLY A
441
76.169
44.624
2.926
1.00
37.04
C


ATOM
2326
C
GLY A
441
75.475
43.746
3.950
1.00
37.28
C


ATOM
2327
O
GLY A
441
74.415
44.107
4.456
1.00
37.10
O


ATOM
2328
N
LYS A
442
76.067
42.598
4.265
1.00
37.56
N


ATOM
2329
CA
LYS A
442
75.469
41.687
5.232
1.00
37.84
C


ATOM
2330
C
LYS A
442
75.707
42.113
6.677
1.00
37.14
C


ATOM
2331
O
LYS A
442
76.746
42.683
7.013
1.00
36.64
O


ATOM
2332
CB
LYS A
442
75.995
40.266
5.017
1.00
39.16
C


ATOM
2333
CG
LYS A
442
75.839
39.789
3.584
1.00
41.53
C


ATOM
2334
CD
LYS A
442
75.692
38.280
3.495
1.00
43.26
C


ATOM
2335
CE
LYS A
442
74.316
37.842
3.976
1.00
44.48
C


ATOM
2336
NZ
LYS A
442
74.126
36.365
3.858
1.00
45.91
N


ATOM
2337
N
LEU A
443
74.724
41.823
7.524
1.00
36.39
N


ATOM
2338
CA
LEU A
443
74.774
42.161
8.940
1.00
35.72
C


ATOM
2339
C
LEU A
443
76.055
41.701
9.645
1.00
35.73
C


ATOM
2340
O
LEU A
443
76.723
42.493
10.314
1.00
35.02
O


ATOM
2341
CB
LEU A
443
73.545
41.571
9.640
1.00
34.56
C


ATOM
2342
CG
LEU A
443
73.386
41.723
11.157
1.00
34.09
C


ATOM
2343
CD1
LEU A
443
71.921
41.572
11.526
1.00
33.35
C


ATOM
2344
CD2
LEU A
443
74.234
40.685
11.883
1.00
33.47
C


ATOM
2345
N
LYS A
444
76.396
40.428
9.479
1.00
35.89
N


ATOM
2346
CA
LYS A
444
77.572
39.840
10.116
1.00
36.54
C


ATOM
2347
C
LYS A
444
78.837
40.702
10.158
1.00
36.30
C


ATOM
2348
O
LYS A
444
79.285
41.100
11.232
1.00
36.27
O


ATOM
2349
CB
LYS A
444
77.910
38.500
9.455
1.00
37.62
C


ATOM
2350
CG
LYS A
444
78.998
37.715
10.180
1.00
39.34
C


ATOM
2351
CD
LYS A
444
79.322
36.415
9.452
1.00
40.97
C


ATOM
2352
CE
LYS A
444
80.227
35.523
10.285
1.00
41.64
C


ATOM
2353
NZ
LYS A
444
81.483
36.221
10.689
1.00
42.46
N


ATOM
2354
N
ASP A
445
79.406
40.985
8.991
1.00
35.80
N


ATOM
2355
CA
ASP A
445
80.638
41.762
8.892
1.00
35.72
C


ATOM
2356
C
ASP A
445
80.567
43.135
9.546
1.00
34.60
C


ATOM
2357
O
ASP A
445
81.541
43.593
10.148
1.00
34.07
O


ATOM
2358
CB
ASP A
445
81.033
41.918
7.421
1.00
37.61
C


ATOM
2359
CG
ASP A
445
81.167
40.580
6.711
1.00
39.41
C


ATOM
2360
OD1
ASP A
445
82.084
39.804
7.066
1.00
39.74
O


ATOM
2361
OD2
ASP A
445
80.343
40.301
5.810
1.00
40.68
O


ATOM
2362
N
ASN A
446
79.420
43.792
9.415
1.00
33.16
N


ATOM
2363
CA
ASN A
446
79.231
45.117
9.991
1.00
32.29
C


ATOM
2364
C
ASN A
446
79.121
45.054
11.508
1.00
31.85
C


ATOM
2365
O
ASN A
446
79.757
45.833
12.217
1.00
31.32
O


ATOM
2366
CB
ASN A
446
77.983
45.759
9.398
1.00
32.15
C


ATOM
2367
CG
ASN A
446
78.181
46.173
7.956
1.00
32.29
C


ATOM
2368
OD1
ASN A
446
78.690
47.264
7.678
1.00
32.36
O


ATOM
2369
ND2
ASN A
446
77.797
45.300
7.029
1.00
30.94
N


ATOM
2370
N
VAL A
447
78.318
44.120
12.004
1.00
31.23
N


ATOM
2371
CA
VAL A
447
78.151
43.965
13.436
1.00
31.20
C


ATOM
2372
C
VAL A
447
79.477
43.588
14.104
1.00
31.65
C


ATOM
2373
O
VAL A
447
79.819
44.124
15.156
1.00
31.22
O


ATOM
2374
CB
VAL A
447
77.088
42.889
13.763
1.00
30.72
C


ATOM
2375
CG1
VAL A
447
77.151
42.519
15.235
1.00
30.21
C


ATOM
2376
CG2
VAL A
447
75.705
43.416
13.424
1.00
30.13
C


ATOM
2377
N
GLU A
448
80.228
42.679
13.490
1.00
31.79
N


ATOM
2378
CA
GLU A
448
81.493
42.260
14.071
1.00
32.87
C


ATOM
2379
C
GLU A
448
82.509
43.398
14.062
1.00
32.19
C


ATOM
2380
O
GLU A
448
83.329
43.506
14.970
1.00
31.93
O


ATOM
2381
CB
GLU A
448
82.037
41.021
13.339
1.00
34.51
C


ATOM
2382
CG
GLU A
448
81.008
39.886
13.264
1.00
37.38
C


ATOM
2383
CD
GLU A
448
81.609
38.522
12.933
1.00
39.91
C


ATOM
2384
OE1
GLU A
448
82.543
38.447
12.098
1.00
41.39
O


ATOM
2385
OE2
GLU A
448
81.129
37.514
13.501
1.00
40.50
O


ATOM
2386
N
ALA A
449
82.448
44.254
13.049
1.00
31.62
N


ATOM
2387
CA
ALA A
449
83.366
45.385
12.978
1.00
30.96
C


ATOM
2388
C
ALA A
449
82.995
46.398
14.063
1.00
30.59
C


ATOM
2389
O
ALA A
449
83.866
46.907
14.775
1.00
29.96
O


ATOM
2390
CB
ALA A
449
83.304
46.040
11.600
1.00
31.10
C


ATOM
2391
N
SER A
450
81.701
46.686
14.187
1.00
30.07
N


ATOM
2392
CA
SER A
450
81.222
47.625
15.197
1.00
29.77
C


ATOM
2393
C
SER A
450
81.589
47.160
16.606
1.00
29.70
C


ATOM
2394
O
SER A
450
82.085
47.943
17.419
1.00
29.34
O


ATOM
2395
CB
SER A
450
79.699
47.779
15.117
1.00
29.51
C


ATOM
2396
OG
SER A
450
79.306
48.434
13.931
1.00
29.55
O


ATOM
2397
N
LEU A
451
81.341
45.884
16.886
1.00
29.59
N


ATOM
2398
CA
LEU A
451
81.624
45.321
18.202
1.00
29.99
C


ATOM
2399
C
LEU A
451
83.111
45.175
18.505
1.00
30.55
C


ATOM
2400
O
LEU A
451
83.509
45.213
19.670
1.00
30.21
O


ATOM
2401
CB
LEU A
451
80.902
43.981
18.372
1.00
28.74
C


ATOM
2402
CG
LEU A
451
79.374
44.128
18.335
1.00
28.52
C


ATOM
2403
CD1
LEU A
451
78.726
42.808
18.674
1.00
27.60
C


ATOM
2404
CD2
LEU A
451
78.924
45.215
19.319
1.00
27.59
C


ATOM
2405
N
ASN A
452
83.933
45.012
17.471
1.00
31.38
N


ATOM
2406
CA
ASN A
452
85.372
44.923
17.694
1.00
32.50
C


ATOM
2407
C
ASNA
452
85.838
46.287
18.185
1.00
32.25
C


ATOM
2408
O
ASN A
452
86.751
46.390
19.005
1.00
32.13
O


ATOM
2409
CB
ASN A
452
86.130
44.568
16.411
1.00
33.77
C


ATOM
2410
CG
ASN A
452
86.149
43.079
16.140
1.00
36.12
C


ATOM
2411
OD1
ASN A
452
86.254
42.263
17.066
1.00
37.33
O


ATOM
2412
ND2
ASN A
452
86.069
42.712
14.866
1.00
37.13
N


ATOM
2413
N
LYS A
453
85.203
47.335
17.674
1.00
31.85
N


ATOM
2414
CA
LYS A
453
85.547
48.693
18.067
1.00
32.30
C


ATOM
2415
C
LYS A
453
85.137
48.922
19.519
1.00
31.23
C


ATOM
2416
O
LYS A
453
85.888
49.497
20.303
1.00
30.82
O


ATOM
2417
CB
LYS A
453
84.838
49.694
17.157
1.00
33.75
C


ATOM
2418
CG
LYS A
453
85.166
51.143
17.450
1.00
36.50
C


ATOM
2419
CD
LYS A
453
84.539
52.063
16.406
1.00
39.06
C


ATOM
2420
CE
LYS A
453
85.055
51.754
14.999
1.00
39.28
C


ATOM
2421
NZ
LYS A
453
84.355
52.589
13.978
1.00
40.79
N


ATOM
2422
N
VAL A
454
83.937
48.462
19.864
1.00
30.16
N


ATOM
2423
CA
VAL A
454
83.418
48.591
21.215
1.00
29.31
C


ATOM
2424
C
VAL A
454
84.334
47.848
22.189
1.00
29.13
C


ATOM
2425
O
VAL A
454
84.696
48.372
23.243
1.00
28.31
O


ATOM
2426
CB
VAL A
454
81.984
48.012
21.314
1.00
29.18
C


ATOM
2427
CG1
VAL A
454
81.506
48.019
22.765
1.00
28.54
C


ATOM
2428
CG2
VAL A
454
81.038
48.830
20.444
1.00
28.30
C


ATOM
2429
N
LYS A
455
84.705
46.623
21.824
1.00
28.92
N


ATOM
2430
CA
LYS A
455
85.581
45.804
22.656
1.00
28.73
C


ATOM
2431
C
LYS A
455
86.919
46.498
22.855
1.00
28.34
C


ATOM
2432
O
LYS A
455
87.462
46.522
23.954
1.00
28.12
O


ATOM
2433
CB
LYS A
455
85.822
44.440
22.006
1.00
28.84
C


ATOM
2434
CG
LYS A
455
84.620
43.517
21.976
1.00
29.31
C


ATOM
2435
CD
LYS A
455
84.971
42.252
21.200
1.00
29.86
C


ATOM
2436
CE
LYS A
455
83.802
41.296
21.114
1.00
31.18
C


ATOM
2437
NZ
LYS A
455
84.174
40.040
20.399
1.00
31.56
N


ATOM
2438
N
SER A
456
87.448
47.057
21.774
1.00
28.04
N


ATOM
2439
CA
SER A
456
88.720
47.754
21.834
1.00
28.45
C


ATOM
2440
C
SER A
456
88.631
48.936
22.802
1.00
27.62
C


ATOM
2441
O
SER A
456
89.497
49.121
23.658
1.00
27.05
O


ATOM
2442
CB
SER A
456
89.114
48.237
20.434
1.00
28.94
C


ATOM
2443
OG
SER A
456
90.336
48.950
20.475
1.00
31.01
O


ATOM
2444
N
THR A
457
87.578
49.733
22.662
1.00
26.61
N


ATOM
2445
CA
THR A
457
87.377
50.885
23.528
1.00
26.30
C


ATOM
2446
C
THR A
457
87.186
50.444
24.978
1.00
25.88
C


ATOM
2447
O
THR A
457
87.697
51.080
25.896
1.00
25.21
O


ATOM
2448
CE
THR A
457
86.157
51.706
23.070
1.00
26.38
C


ATOM
2449
OG1
THR A
457
86.378
52.139
21.727
1.00
27.27
O


ATOM
2450
CG2
THR A
457
85.949
52.926
23.961
1.00
25.15
C


ATOM
2451
N
MET A
458
86.456
49.353
25.184
1.00
25.53
N


ATOM
2452
CA
MET A
458
86.244
48.857
26.535
1.00
26.03
C


ATOM
2453
C
MET A
458
87.578
48.547
27.201
1.00
26.68
C


ATOM
2454
O
MET A
458
87.768
48.826
28.383
1.00
26.93
O


ATOM
2455
CE
MET A
458
85.340
47.623
26.521
1.00
25.33
C


ATOM
2456
CG
MET A
458
83.876
47.976
26.285
1.00
24.43
C


ATOM
2457
SD
MET A
458
82.816
46.551
26.067
1.00
25.53
S


ATOM
2458
CE
MET A
458
82.942
45.769
27.715
1.00
24.14
C


ATOM
2459
N
CYS A
459
88.507
47.977
26.445
1.00
27.44
N


ATOM
2460
CA
CYS A
459
89.819
47.682
27.000
1.00
28.79
C


ATOM
2461
C
CYS A
459
90.578
48.968
27.351
1.00
28.24
C


ATOM
2462
O
CYS A
459
91.338
48.996
28.322
1.00
27.71
O


ATOM
2463
CE
CYS A
459
90.628
46.819
26.030
1.00
31.37
C


ATOM
2464
SG
CYS A
459
90.257
45.047
26.230
1.00
35.38
S


ATOM
2465
N
ASN A
460
90.375
50.030
26.569
1.00
27.55
N


ATOM
2466
CA
ASN A
460
91.028
51.309
26.855
1.00
27.53
C


ATOM
2467
C
ASN A
460
90.504
51.804
28.202
1.00
27.21
C


ATOM
2468
O
ASN A
460
91.202
52.496
28.938
1.00
26.69
O


ATOM
2469
CB
ASN A
460
90.696
52.362
25.787
1.00
27.94
C


ATOM
2470
CG
ASN A
460
91.419
52.122
24.471
1.00
29.27
C


ATOM
2471
OD1
ASN A
460
90.796
52.061
23.409
1.00
29.42
O


ATOM
2472
ND2
ASN A
460
92.741
51.998
24.533
1.00
29.31
N


ATOM
2473
N
CYS A
461
89.261
51.441
28.512
1.00
26.99
N


ATOM
2474
CA
CYS A
461
88.632
51.855
29.755
1.00
26.90
C


ATOM
2475
C
CYS A
461
88.865
50.838
30.871
1.00
26.66
C


ATOM
2476
O
CYS A
461
88.367
51.003
31.976
1.00
26.77
O


ATOM
2477
CE
CYS A
461
87.126
52.063
29.538
1.00
27.30
C


ATOM
2478
SG
CYS A
461
86.714
53.341
28.304
1.00
27.83
S


ATOM
2479
N
GLY A
462
89.627
49.793
30.570
1.00
26.92
N


ATOM
2480
CA
GLY A
462
89.919
48.768
31.557
1.00
26.65
C


ATOM
2481
C
GLY A
462
88.758
47.842
31.881
1.00
26.78
C


ATOM
2482
O
GLY A
462
88.659
47.347
33.001
1.00
26.85
O


ATOM
2483
N
ALA A
463
87.882
47.592
30.913
1.00
26.47
N


ATOM
2484
CA
ALA A
463
86.731
46.725
31.155
1.00
26.74
C


ATOM
2485
C
ALA A
463
86.700
45.507
30.249
1.00
26.80
C


ATOM
2486
O
ALA A
463
86.898
45.616
29.034
1.00
26.39
O


ATOM
2487
CB
ALA A
463
85.433
47.515
30.991
1.00
26.14
C


ATOM
2488
N
LEU A
464
86.444
44.349
30.850
1.00
27.16
N


ATOM
2489
CA
LEU A
464
86.356
43.101
30.105
1.00
27.87
C


ATOM
2490
C
LEU A
464
84.901
42.683
29.943
1.00
27.47
C


ATOM
2491
O
LEU A
464
84.604
41.722
29.239
1.00
28.26
O


ATOM
2492
CB
LEU A
464
87.138
41.984
30.806
1.00
28.54
C


ATOM
2493
CG
LEU A
464
88.634
41.869
30.492
1.00
29.79
C


ATOM
2494
CD1
LEU A
464
88.827
41.779
28.983
1.00
29.98
C


ATOM
2495
CD2
LEU A
464
89.388
43.078
31.039
1.00
31.57
C


ATOM
2496
N
THR A
465
83.997
43.398
30.606
1.00
26.65
N


ATOM
2497
CA
THR A
465
82.573
43.096
30.515
1.00
25.99
C


ATOM
2498
C
THR A
465
81.786
44.391
30.567
1.00
25.84
C


ATOM
2499
O
THR A
465
82.318
45.435
30.945
1.00
25.20
O


ATOM
2500
CB
THR A
465
82.077
42.229
31.688
1.00
25.98
C


ATOM
2501
OG1
THR A
465
82.139
42.991
32.899
1.00
25.86
O


ATOM
2502
CG2
THR A
465
82.921
40.975
31.827
1.00
26.08
C


ATOM
2503
N
ILE A
466
80.514
44.316
30.197
1.00
25.29
N


ATOM
2504
CA
ILE A
466
79.666
45.495
30.229
1.00
25.21
C


ATOM
2505
C
ILE A
466
79.470
45.999
31.650
1.00
25.01
C


ATOM
2506
O
ILE A
466
79.569
47.197
31.902
1.00
25.19
O


ATOM
2507
CB
ILE A
466
78.316
45.208
29.531
1.00
25.13
C


ATOM
2508
CG1
ILE A
466
78.565
45.033
28.025
1.00
25.57
C


ATOM
2509
CG2
ILE A
466
77.323
46.336
29.809
1.00
24.41
C


ATOM
2510
CD1
ILE A
466
77.351
44.586
27.223
1.00
26.34
C


ATOM
2511
N
PRO A
467
79.197
45.095
32.610
1.00
25.04
N


ATOM
2512
CA
PRO A
467
79.023
45.598
33.975
1.00
24.53
C


ATOM
2513
C
PRO A
467
80.303
46.274
34.464
1.00
24.42
C


ATOM
2514
O
PRO A
467
80.256
47.287
35.155
1.00
24.23
O


ATOM
2515
CB
PRO A
467
78.686
44.333
34.767
1.00
24.74
C


ATOM
2516
CG
PRO A
467
77.936
43.508
33.754
1.00
24.43
C


ATOM
2517
CD
PRO A
467
78.817
43.672
32.527
1.00
24.58
C


ATOM
2518
N
GLN A
468
81.455
45.723
34.105
1.00
24.65
N


ATOM
2519
CA
GLN A
468
82.702
46.335
34.536
1.00
25.05
C


ATOM
2520
C
GLN A
468
82.883
47.705
33.873
1.00
25.35
C


ATOM
2521
O
GLN A
468
83.447
48.621
34.471
1.00
25.30
O


ATOM
2522
CB
GLN A
468
83.890
45.430
34.219
1.00
24.93
C


ATOM
2523
CG
GLN A
468
85.207
46.019
34.668
1.00
25.22
C


ATOM
2524
CD
GLN A
468
86.347
45.017
34.648
1.00
25.10
C


ATOM
2525
OE1
GLN A
468
86.493
44.234
33.707
1.00
24.05
O


ATOM
2526
NE2
GLN A
468
87.176
45.054
35.686
1.00
25.09
N


ATOM
2527
N
LEU A
469
82.400
47.840
32.639
1.00
25.06
N


ATOM
2528
CA
LEU A
469
82.488
49.108
31.919
1.00
24.83
C


ATOM
2529
C
LEU A
469
81.609
50.150
32.617
1.00
25.01
C


ATOM
2530
O
LEU A
469
82.023
51.292
32.838
1.00
24.50
O


ATOM
2531
CB
LEU A
469
82.010
48.932
30.476
1.00
24.41
C


ATOM
2532
CG
LEU A
469
81.852
50.214
29.655
1.00
24.56
C


ATOM
2533
CD1
LEU A
469
83.223
50.807
29.360
1.00
24.30
C


ATOM
2534
CD2
LEU A
469
81.112
49.906
28.358
1.00
24.10
C


ATOM
2535
N
GLN A
470
80.395
49.741
32.966
1.00
25.06.
N


ATOM
2536
CA
GLN A
470
79.441
50.622
33.629
1.00
25.82
C


ATOM
2537
C
GLN A
470
79.966
51.100
34.981
1.00
26.53
C


ATOM
2538
O
GLN A
470
79.627
52.184
35.467
1.00
26.74
O


ATOM
2539
CB
GLN A
470
78.102
49.886
33.775
1.00
25.24
C


ATOM
2540
CG
GLN A
470
77.455
49.646
32.406
1.00
25.04
C


ATOM
2541
CD
GLN A
470
76.245
48.731
32.421
1.00
25.22
C


ATOM
2542
OE1
GLN A
470
75.453
48.722
31.469
1.00
25.47
O


ATOM
2543
NE2
GLN A
470
76.099
47.948
33.479
1.00
24.84
N


ATOM
2544
N
SER A
471
80.829
50.291
35.572
1.00
27.02
N


ATOM
2545
CA
SER A
471
81.404
50.617
36.860
1.00
27.70
C


ATOM
2546
C
SER A
471
82.654
51.505
36.756
1.00
27.93
C


ATOM
2547
O
SER A
471
82.805
52.458
37.517
1.00
28.18
O


ATOM
2548
CB
SER A
471
81.741
49.316
37.596
1.00
27.39
C


ATOM
2549
OG
SER A
471
82.515
49.569
38.748
1.00
29.07
O


ATOM
2550
N
LYS A
472
83.522
51.208
35.794
1.00
28.02
N


ATOM
2551
CA
LYS A
472
84.785
51.935
35.630
1.00
28.71
C


ATOM
2552
C
LYS A
472
84.851
53.106
34.647
1.00
28.19
C


ATOM
2553
O
LYS A
472
85.796
53.891
34.696
1.00
28.07
O


ATOM
2554
CB
LYS A
472
85.883
50.938
35.257
1.00
29.32
C


ATOM
2555
CG
LYS A
472
86.050
49.816
36.267
1.00
31.72
C


ATOM
2556
CD
LYS A
472
87.050
48.764
35.805
1.00
32.09
C


ATOM
2557
CE
LYS A
472
88.459
49.308
35.753
1.00
32.85
C


ATOM
2558
NZ
LYS A
472
89.418
48.212
35.419
1.00
33.48
N


ATOM
2559
N
ALA A
473
83.868
53.223
33.760
1.00
27.53
N


ATOM
2560
CA
ALA A
473
83.875
54.283
32.758
1.00
27.01
C


ATOM
2561
C
ALA A
473
83.977
55.698
33.313
1.00
26.91
C


ATOM
2562
O
ALA A
473
83.341
56.049
34.309
1.00
26.92
O


ATOM
2563
CB
ALA A
473
82.635
54.169
31.859
1.00
27.23
C


ATOM
2564
N
LYS A
474
84.803
56.499
32.649
1.00
26.59
N


ATOM
2565
CA
LYS A
474
85.012
57.898
32.999
1.00
26.15
C


ATOM
2566
C
LYS A
474
84.444
58.636
31.791
1.00
26.08
C


ATOM
2567
O
LYS A
474
84.973
58.545
30.684
1.00
25.63
O


ATOM
2568
CB
LYS A
474
86.504
58.161
33.190
1.00
25.22
C


ATOM
2569
CG
LYS A
474
87.062
57.433
34.414
1.00
25.03
C


ATOM
2570
CD
LYS A
474
88.530
57.064
34.245
1.00
24.53
C


ATOM
2571
CE
LYS A
474
89.433
58.274
34.298
1.00
24.54
C


ATOM
2572
NZ
LYS A
474
90.837
57.870
33.996
1.00
23.96
N


ATOM
2573
N
ILE A
475
83.348
59.350
32.011
1.00
26.24
N


ATOM
2574
CA
ILE A
475
82.652
60.025
30.926
1.00
26.16
C


ATOM
2575
C
ILE A
475
82.601
61.527
31.073
1.00
26.07
C


ATOM
2576
O
ILE A
475
82.064
62.045
32.049
1.00
26.61
O


ATOM
2577
CB
ILE A
475
81.206
59.489
30.821
1.00
26.31
C


ATOM
2578
CG1
ILE A
475
81.230
57.954
30.784
1.00
26.16
C


ATOM
2579
CG2
ILE A
475
80.526
60.042
29.572
1.00
26.65
C


ATOM
2580
CD1
ILE A
475
79.853
57.299
30.764
1.00
24.83
C


ATOM
2581
N
THR A
476
83.156
62.228
30.093
1.00
25.67
N


ATOM
2582
CA
THR A
476
83.158
63.677
30.136
1.00
25.52
C


ATOM
2583
C
THR A
476
82.290
64.288
29.056
1.00
25.76
C


ATOM
2584
O
THR A
476
82.160
63.752
27.951
1.00
25.51
O


ATOM
2585
CB
THR A
476
84.581
64.261
29.977
1.00
25.15
C


ATOM
2586
OG1
THR A
476
84.519
65.689
30.093
1.00
24.81
O


ATOM
2587
CG2
THR A
476
85.168
63.897
28.616
1.00
24.56
C


ATOM
2588
N
LEU A
477
81.686
65.414
29.401
1.00
26.07
N


ATOM
2589
CA
LEU A
477
80.869
66.159
28.467
1.00
27.01
C


ATOM
2590
C
LEU A
477
81.908
66.963
27.677
1.00
27.30
C


ATOM
2591
O
LEU A
477
82.996
67.239
28.183
1.00
26.31
O


ATOM
2592
CB
LEU A
477
79.929
67.103
29.225
1.00
27.31
C


ATOM
2593
CG
LEU A
477
78.834
67.808
28.421
1.00
28.63
C


ATOM
2594
CD1
LEU A
477
77.822
66.782
27.915
1.00
28.11
C


ATOM
2595
CD2
LEU A
477
78.148
68.842
29.303
1.00
28.70
C


ATOM
2596
N
VAL A
478
81.577
67.317
26.443
1.00
27.88
N


ATOM
2597
CA
VAL A
478
82.472
68.085
25.590
1.00
29.05
C


ATOM
2598
C
VAL A
478
81.802
69.428
25.295
1.00
29.61
C


ATOM
2599
O
VAL A
478
80.581
69.504
25.177
1.00
29.56
O


ATOM
2600
CB
VAL A
478
82.737
67.322
24.269
1.00
29.48
C


ATOM
2601
CG1
VAL A
478
83.643
68.125
23.368
1.00
30.38
C


ATOM
2602
CG2
VAL A
478
83.370
65.970
24.579
1.00
29.54
C


ATOM
2603
N
SER A
479
82.596
70.484
25.183
1.00
30.34
N


ATOM
2604
CA
SER A
479
82.058
71.819
24.916
1.00
31.62
C


ATOM
2605
C
SER A
479
81.402
71.940
23.545
1.00
32.67
C


ATOM
2606
O
SER A
479
81.770
71.232
22.609
1.00
31.95
O


ATOM
2607
CB
SER A
479
83.168
72.866
25.021
1.00
30.68
C


ATOM
2608
OG
SER A
479
84.085
72.730
23.949
1.00
30.46
O


ATOM
2609
N
SER A
480
80.442
72.858
23.437
1.00
34.86
N


ATOM
2610
CA
SER A
480
79.729
73.110
22.183
1.00
37.33
C


ATOM
2611
C
SER A
480
80.703
73.371
21.041
1.00
38.47
C


ATOM
2612
O
SER A
480
80.561
72.816
19.951
1.00
38.60
O


ATOM
2613
CB
SER A
480
78.813
74.331
22.317
1.00
37.61
C


ATOM
2614
OG
SER A
480
77.888
74.175
23.373
1.00
39.26
O


ATOM
2615
N
VAL A
481
81.685
74.229
21.302
1.00
40.19
N


ATOM
2616
CA
VAL A
481
82.694
74.592
20.311
1.00
42.19
C


ATOM
2617
C
VAL A
481
83.561
73.422
19.843
1.00
43.43
C


ATOM
2618
O
VAL A
481
83.944
73.364
18.676
1.00
43.73
O


ATOM
2619
CB
VAL A
481
83.617
75.716
20.848
1.00
42.42
C


ATOM
2620
CG1
VAL A
481
84.833
75.879
19.941
1.00
42.66
C


ATOM
2621
CG2
VAL A
481
82.844
77.029
20.917
1.00
42.27
C


ATOM
2622
N
SER A
482
83.879
72.499
20.744
1.00
44.59
N


ATOM
2623
CA
SER A
482
84.697
71.346
20.378
1.00
46.25
C


ATOM
2624
C
SER A
482
84.013
70.517
19.293
1.00
47.04
C


ATOM
2625
O
SER A
482
84.670
69.773
18.556
1.00
47.14
O


ATOM
2626
CB
SER A
482
84.943
70.448
21.594
1.00
46.49
C


ATOM
2627
OG
SER A
482
85.710
71.107
22.583
1.00
48.50
O


ATOM
2628
N
ILE A
483
82.693
70.638
19.204
1.00
47.71
N


ATOM
2629
CA
ILE A
483
81.934
69.876
18.219
1.00
48.77
C


ATOM
2630
C
ILE A
483
81.656
70.687
16.952
1.00
49.17
C


ATOM
2631
O
ILE A
483
81.552
71.931
17.042
1.00
49.53
O


ATOM
2632
CB
ILE A
483
80.597
69.387
18.833
1.00
48.86
C


ATOM
2633
CG1
ILE A
483
80.886
68.549
20.081
1.00
48.85
C


ATOM
2634
CG2
ILE A
483
79.818
68.552
17.822
1.00
49.17
C


ATOM
2635
CD1
ILE A
483
79.650
68.141
20.845
1.00
49.07
C


TER
2636

ILE A
483


HETATM
2637
K
K A
900
52.558
59.979
29.204
0.75
33.19
K


HETATM
2638
P
XMP
602
67.402
54.842
14.904
1.00
30.34
P


HETATM
2639
O1P
XMP
602
67.002
54.789
13.486
1.00
30.72
O


HETATM
2640
O2P
XMP
602
68.190
53.690
15.379
1.00
30.78
O


HETATM
2641
O5′
XMP
602
66.075
54.823
15.699
1.00
29.65
O


HETATM
2642
O3P
XMP
602
67.954
56.140
15.323
1.00
30.68
O


HETATM
2643
C5′
XMP
602
65.078
53.767
15.814
1.00
29.12
C


HETATM
2644
C4′
XMP
602
63.985
54.002
16.886
1.00
29.15
C


HETATM
2645
O4′
XMP
602
63.144
55.124
16.601
1.00
29.44
O


HETATM
2646
C1′
XMP
602
61.803
55.041
17.060
1.00
29.86
C


HETATM
2647
N9
XMP
602
60.863
55.346
15.925
1.00
30.85
N


HETATM
2648
C4
XMP
602
60.396
56.585
15.533
1.00
31.77
C


HETATM
2649
N3
XMP
602
60.681
57.809
16.083
1.00
32.09
N


HETATM
2650
N1
XMP
602
59.202
58.646
14.358
1.00
32.72
N


HETATM
2651
C2
XMP
602
60.053
58.836
15.454
1.00
33.14
C


HETATM
2652
O2
XMP
602
60.229
59.983
15.858
1.00
33.63
O


HETATM
2653
C6
XMP
602
58.897
57.407
13.781
1.00
32.30
C


HETATM
2654
O6
XMP
602
58.148
57.308
12.825
1.00
33.30
O


HETATM
2655
C5
XMP
602
59.556
56.336
14.439
1.00
32.02
C


HETATM
2656
N7
XMP
602
59.498
55.005
14.154
1.00
31.42
N


HETATM
2657
C8
XMP
602
60.263
54.494
15.036
1.00
31.18
C


HETATM
2658
C2′
XMP
602
61.788
53.653
17.733
1.00
29.10
C


HETATM
2659
O2′
XMP
602
61.947
53.880
19.132
1.00
29.07
O


HETATM
2660
C3′
XMP
602
62.943
52.927
17.024
1.00
28.77
C


HETATM
2661
O3′
XMP
602
63.388
51.798
17.768
1.00
28.12
O


HETATM
2662
AP
NAD
987
50.634
53.888
20.452
1.00
70.18
P


HETATM
2663
AO1
NAD
987
49.686
52.811
20.084
1.00
70.10
O


HETATM
2664
AO2
NAD
987
51.622
53.619
21.519
1.00
70.18
O


HETATM
2665
AO5*
NAD
987
49.807
55.222
20.825
1.00
70.73
O


HETATM
2666
AC5*
NAD
987
48.836
55.190
21.879
1.00
71.96
C


HETATM
2667
AC4*
NAD
987
48.158
56.575
22.018
1.00
72.40
C


HETATM
2668
AO4*
NAD
987
47.053
56.406
22.993
1.00
72.62
O


HETATM
2669
AC3*
NAD
987
47.458
56.986
20.719
1.00
72.81
C


HETATM
2670
AO3*
NAD
987
48.185
56.491
19.587
1.00
73.24
O


HETATM
2671
AC2*
NAD
987
46.117
56.309
20.794
1.00
72.87
C


HETATM
2672
AO2*
NAD
987
46.258
54.925
20.444
1.00
72.72
O


HETATM
2673
AC1*
NAD
987
45.766
56.439
22.272
1.00
72.67
C


HETATM
2674
AN9
NAD
987
44.784
55.412
22.731
1.00
72.51
N


HETATM
2675
AC8
NAD
987
43.460
55.583
22.865
1.00
72.46
C


HETATM
2676
AN7
NAD
987
42.908
54.431
23.274
1.00
72.16
N


HETATM
2677
AC5
NAD
987
43.880
53.538
23.399
1.00
72.08
C


HETATM
2678
AC6
NAD
987
43.920
52.200
23.781
1.00
72.01
C


HETATM
2679
AN6
NAD
987
42.803
51.558
24.105
1.00
72.25
N


HETATM
2680
AN1
NAD
987
45.108
51.553
23.810
1.00
71.86
N


HETATM
2681
AC2
NAD
987
46.241
52.179
23.476
1.00
71.78
C


HETATM
2682
AN3
NAD
987
46.228
53.462
23.105
1.00
71.90
N


HETATM
2683
AC4
NAD
987
45.069
54.157
23.059
1.00
72.20
C


HETATM
2684
O3
NAD
987
51.412
54.316
19.101
1.00
69.74
O


HETATM
2685
NP
NAD
987
52.634
55.383
19.126
1.00
69.12
P


HETATM
2686
NO1
NAD
987
53.103
55.572
20.519
1.00
68.69
O


HETATM
2687
NO2
NAD
987
52.250
56.578
18.341
1.00
69.23
O


HETATM
2688
NO5*
NAD
987
53.807
54.613
18.343
1.00
69.13
O


HETATM
2689
NC5*
NAD
987
53.538
53.954
17.101
1.00
68.98
C


HETATM
2690
NC4*
NAD
987
54.844
53.577
16.381
1.00
68.78
C


HETATM
2691
NO4*
NAD
987
55.536
54.846
16.049
1.00
68.83
O


HETATM
2692
NC3*
NAD
987
55.787
52.849
17.333
1.00
68.59
C


HETATM
2693
NO3*
NAD
987
56.629
51.948
16.611
1.00
68.69
O


HETATM
2694
NC2*
NAD
987
56.615
53.936
17.951
1.00
68.50
C


HETATM
2695
NO2*
NAD
987
57.896
53.435
18.333
1.00
68.13
O


HETATM
2696
NC1*
NAD
987
56.784
54.933
16.818
1.00
68.70
C


HETATM
2697
NN1
NAD
987
57.133
56.318
17.254
1.00
69.08
N


HETATM
2698
NC2
NAD
987
58.217
56.537
18.152
1.00
69.28
C


HETATM
2699
NC3
NAD
987
58.549
57.847
18.538
1.00
69.57
C


HETATM
2700
NC7
NAD
987
59.715
58.103
19.514
1.00
69.91
C


HETATM
2701
NO7
NAD
987
60.134
59.245
19.712
1.00
70.20
O


HETATM
2702
NN7
NAD
987
60.220
57.016
20.103
1.00
69.78
N


HETATM
2703
NC4
NAD
987
57.806
58.929
18.030
1.00
69.34
C


HETATM
2704
NC5
NAD
987
56.734
58.723
17.144
1.00
69.28
C


HETATM
2705
NC6
NAD
987
56.393
57.421
16.753
1.00
69.10
C


HETATM
2706
O
HOH
1
80.159
44.885
4.169
1.00
45.58
O


HETATM
2707
O
HOH
2
70.459
54.183
21.914
1.00
24.31
O


HETATM
2708
O
HOH
3
57.313
58.461
28.306
1.00
24.50
O


HETATM
2709
O
NOH
4
65.571
60.118
24.639
1.00
23.07
O


HETATM
2710
O
HOH
5
40.291
38.852
28.760
1.00
49.15
O


HETATM
2711
O
HOH
6
66.287
47.668
38.747
1.00
21.93
O


HETATM
2712
O
HOH
7
86.808
55.200
31.125
1.00
27.24
O


HETATM
2713
O
HOH
8
79.324
41.691
29.401
1.00
21.83
O


HETATM
2714
O
HOH
9
69.419
61.415
38.396
1.00
44.68
O


HETATM
2715
O
HOH
10
58.291
50.786
22.925
1.00
24.55
O


HETATM
2716
O
HOH
11
70.499
53.076
14.172
1.00
25.36
O


HETATM
2717
O
HOH
12
75.758
43.567
30.918
1.00
21.79
O


HETATH
2718
O
HOH
13
88.069
53.459
33.173
1.00
26.13
O


HETATM
2719
O
HOH
14
67.647
38.078
46.052
1.00
35.25
O


HETATM
2720
O
HOH
15
72.291
37.808
33.719
1.00
27.23
O


HETATM
2721
O
HOH
16
56.445
78.452
34.278
1.00
24.45
O


HETATM
2722
O
HOH
17
58.982
44.997
36.851
1.00
25.40
O


HETATM
2723
O
HOH
18
51.923
53.605
25.905
1.00
30.95
O


HETATM
2724
O
HOH
19
58.261
35.282
26.925
1.00
32.59
O


HETATM
2725
O
NON
20
78.214
47.801
37.366
1.00
36.04
O


HETATM
2726
O
HOH
21
77.272
53.707
34.316
1.00
27.76
O


HETATM
2727
O
HOH
22
47.841
54.106
36.571
1.00
37.78
O


HETATM
2728
O
HOH
23
64.271
41.030
7.745
1.00
31.98
O


HETATM
2729
O
HOH
24
73.286
57.144
36.094
1.00
24.02
O


HETATM
2730
O
HOH
25
67.036
59.452
38.278
1.00
48.34
O


HETATM
2731
O
HOH
26
56.058
41.046
37.332
1.00
41.47
O


HETATM
2732
O
HOH
27
59.588
50.684
20.017
1.00
32.62
O


HETATM
2733
O
HOH
28
68.814
67.431
32.848
1.00
28.56
O


HETATM
2734
O
HOH
29
81.923
66.876
31.746
1.00
32.25
O


HETATM
2735
O
HOH
30
61.989
38.331
33.948
1.00
24.11
O


HETATM
2736
O
HOH
31
69.891
33.131
27.256
1.00
33.89
O


HETATM
2737
O
HOH
32
60.032
39.147
6.730
1.00
39.28
O


HETATM
2738
O
HOH
33
61.745
63.891
35.416
1.00
31.28
O


HETATM
2739
O
HOH
34
48.981
43.802
20.915
1.00
29.86
O


HETATM
2740
O
HOH
35
69.168
35.704
7.655
1.00
35.67
O


HETATM
2741
O
NOH
36
76.202
65.130
31.664
1.00
44.93
O


HETATM
2742
O
HOH
37
69.263
32.519
38.368
1.00
38.37
O


HETATM
2743
O
HOH
38
65.179
36.434
34.852
1.00
29.61
O


HETATM
2744
O
HOH
39
59.293
59.263
30.587
1.00
36.96
O


HETATM
2745
O
NOH
40
49.423
42.410
7.845
1.00
53.80
O


HETATM
2746
O
HOH
41
64.358
73.055
32.790
1.00
26.48
O


HETATM
2747
O
HOH
42
71.857
63.707
34.068
1.00
60.77
O


HETATM
2748
O
HOH
43
56.071
57.344
38.813
1.00
42.44
O


HETATM
2749
O
HOH
44
63.542
56.163
20.268
1.00
36.97
O


HETATM
2750
O
HOH
45
61.356
50.051
17.813
1.00
26.22
O


HETATM
2751
O
HOH
46
92.220
40.526
20.299
1.00
49.10
O


HETATM
2752
O
HOH
47
71.972
61.198
21.121
1.00
35.90
O


HETATM
2753
O
HOH
48
83.870
52.797
20.905
1.00
29.24
O


HETATM
2754
O
HOH
49
56.116
76.920
37.019
1.00
36.67
O


HETATM
2755
O
HOH
50
50.418
45.939
35.861
1.00
36.94
O


HETATM
2756
O
HOH
51
81.571
63.014
21.227
1.00
32.08
O


HETATM
2757
O
HOH
52
66.576
33.997
36.818
1.00
42.85
O


HETATM
2758
O
HOH
53
59.306
51.362
16.242
1.00
31.71
O


HETATM
2759
O
HOH
54
58.726
37.969
34.720
1.00
37.12
O


HETATM
2760
O
HOH
55
59.306
53.739
20.688
1.00
31.48
O


HETATM
2761
O
HOH
56
52.755
51.235
37.729
1.00
38.98
O


HETATM
2762
O
HOH
57
77.948
70.194
25.195
1.00
40.94
O


HETATM
2763
O
HOH
58
42.877
43.465
23.430
1.00
37.12
O


HETATM
2764
O
HOH
59
74.941
70.159
31.554
1.00
37.95
O


HETATM
2765
O
HOH
60
62.836
39.227
5.777
1.00
41.89
O


HETATM
2766
O
HOH
61
63.043
31.312
25.273
1.00
42.37
O


HETATM
2767
O
HOH
62
73.944
59.700
37.703
1.00
39.09
O


HETATM
2768
O
HOH
63
45.718
48.708
27.281
1.00
38.46
O


HETATM
2769
O
HOH
64
65.979
37.356
16.650
1.00
29.39
O


HETATM
2770
O
HOH
65
74.924
38.483
8.198
1.00
36.88
O


HETATM
2771
O
HOH
66
72.792
32.939
26.042
1.00
49.82
O


HETATM
2772
O
HOH
67
71.174
32.495
29.960
1.00
43.86
O


HETATM
2773
O
HOH
68
86.835
69.123
23.909
1.00
40.67
O


HETATM
2774
O
HOH
69
51.919
29.585
14.737
1.00
50.08
O


HETATM
2775
O
HOH
70
74.502
36.683
10.729
1.00
38.28
O


HETATM
2776
O
HOH
71
74.398
47.611
35.605
1.00
39.16
O


HETATM
2777
O
HOH
72
73.613
50.462
36.144
1.00
32.41
O


HETATM
2778
O
HOH
73
54.489
46.459
17.581
1.00
46.38
O


HETATM
2779
O
HOH
74
73.145
64.449
30.898
1.00
37.64
O


HETATM
2780
O
HOH
75
69.890
53.682
17.707
1.00
40.51
O


HETATM
2781
O
HOH
76
44.394
42.781
15.412
1.00
49.08
O


HETATM
2782
O
HOH
77
59.413
50.782
9.634
1.00
33.53
O


HETATM
2783
O
HOH
78
68.121
74.231
33.089
1.00
42.30
O


HETATM
2784
O
HOH
79
58.561
44.690
5.902
1.00
40.98
O


HETATM
2785
O
HOH
80
65.000
31.161
29.173
1.00
52.37
O


HETATM
2786
O
HOH
81
74.095
34.670
40.190
1.00
36.19
O


HETATM
2787
O
HOH
82
78.806
36.429
24.680
1.00
48.73
O


HETATM
2788
O
HOH
83
72.866
40.403
41.762
1.00
43.72
O


HETATM
2789
O
HOH
84
71.162
55.709
41.847
1.00
30.47
O


HETATM
2790
O
HOH
85
50.170
31.463
16.442
1.00
46.81
O


HETATM
2791
O
HOH
86
55.811
30.709
8.794
1.00
49.33
O


HETATM
2792
O
HOH
87
61.016
73.187
39.258
1.00
46.28
O


HETATM
2793
O
HOH
88
83.287
41.191
17.129
1.00
48.85
O


HETATM
2794
O
HOH
89
85.733
38.892
22.703
1.00
43.02
O


HETATM
2795
O
HOH
90
67.617
53.275
46.890
1.00
44.36
O


HETATM
2796
O
HOH
91
76.440
36.363
6.407
1.00
60.32
O


HETATM
2797
O
HOH
92
74.688
38.584
30.945
1.00
34.79
O


HETATM
2798
O
HOH
93
57.076
65.531
38.139
1.00
47.34
O


HETATM
2799
O
HOH
94
78.761
38.342
17.426
1.00
41.15
O


HETATM
2800
O
HOH
95
61.259
33.096
26.930
1.00
44.33
O


HETATM
2801
O
HOH
96
65.482
28.592
14.900
1.00
41.37
O


HETATM
2802
O
HOH
97
93.557
52.441
21.951
1.00
58.36
O


HETATM
2803
O
HOH
98
52.048
50.238
18.507
1.00
50.58
O


HETATM
2804
O
HOH
99
69.144
44.907
46.298
1.00
41.41
O


HETATM
2805
O
HOH
100
92.572
46.733
19.480
1.00
53.29
O


HETATM
2806
O
HOH
101
60.394
50.886
46.427
1.00
58.13
O


HETATM
2807
O
HOH
102
60.206
29.776
22.560
1.00
51.85
O


HETATM
2808
O
HOH
103
55.550
45.667
5.832
1.00
54.36
O


HETATM
2809
O
HOH
104
66.124
45.356
49.309
1.00
55.34
O


HETATM
2810
O
HOH
105
42.594
47.628
27.697
1.00
57.72
O


HETATM
2811
O
HOH
106
78.097
71.838
27.740
1.00
51.84
O


HETATM
2812
O
HOH
107
74.276
62.445
19.161
1.00
40.85
O


HETATM
2813
O
HOH
108
47.828
41.389
36.858
1.00
50.41
O


HETATM
2814
O
HOH
109
71.642
67.017
32.073
1.00
37.86
O


HETATM
2815
O
HOH
110
74.696
67.506
33.229
1.00
57.41
O


HETATM
2816
O
HOH
111
75.703
52.363
36.244
1.00
30.66
O


HETATM
2817
O
HOH
112
73.719
66.099
18.701
1.00
56.53
O


HETATM
2818
O
HOH
113
51.821
45.822
7.467
1.00
52.27
O


HETATM
2819
O
HOH
114
81.307
38.594
20.656
1.00
70.73
O


HETATM
2820
O
HOH
115
81.169
38.251
23.961
1.00
41.30
O


HETATM
2821
O
NOH
116
45.113
41.184
12.778
1.00
63.00
O


HETATM
2822
O
HOH
117
68.809
39.136
48.780
1.00
38.97
O


HETATM
2823
O
HOH
118
62.055
33.092
29.952
1.00
52.24
O


HETATM
2824
O
HOH
119
51.760
31.011
12.019
1.00
58.64
O


HETATM
2825
O
HOH
120
59.767
32.566
33.591
1.00
52.66
O


HETATM
2826
O
HOH
121
56.985
32.023
26.849
1.00
57.15
O


HETATM
2827
O
HOH
122
60.737
40.820
44.361
1.00
56.30
O


HETATM
2828
O
HOH
123
64.564
25.631
14.455
1.00
43.27
O


HETATM
2829
O
HOH
124
49.818
53.007
23.891
1.00
49.86
O


HETATM
2830
O
HOH
125
50.978
50.308
21.539
1.00
35.65
O


HETATM
2831
O
HOH
126
67.755
31.430
25.861
1.00
55.46
O


HETATM
2832
O
HOH
127
48.199
31.294
25.210
1.00
54.24
O


HETATM
2833
O
HOH
128
73.604
54.433
12.696
1.00
61.45
O


HETATM
2834
O
HOH
129
70.275
57.346
14.361
1.00
41.07
O


HETATM
2835
O
HOH
130
74.635
45.539
32.754
1.00
32.00
O


HETATM
2836
O
HOH
131
75.089
72.613
28.286
1.00
49.39
O


HETATM
2837
O
HOH
132
86.853
66.678
30.930
1.00
25.20
O


HETATM
2838
O
HOH
133
78.835
40.047
31.875
1.00
31.20
O


HETATM
2839
O
HOH
134
62.167
61.367
37.551
1.00
30.60
O


HETATM
2840
O
HOH
135
65.184
28.026
26.437
1.00
48.57
O


HETATM
2841
O
HOH
136
76.047
40.918
32.141
1.00
34.64
O


HETATM
2842
O
HOH
137
59.729
41.105
39.908
1.00
47.69
O


HETATM
2843
O
HOH
138
70.728
75.819
32.304
1.00
53.80
O


HETATM
2844
O
HOH
139
81.807
75.821
23.632
1.00
51.16
O


HETATM
2845
O
HOH
140
79.607
73.914
25.874
1.00
49.38
O


HETATM
2846
O
HOH
141
44.883
44.348
32.806
1.00
49.33
O


HETATM
2847
O
HOH
142
74.170
42.608
43.856
1.00
52.82
O


HETATM
2848
O
HOH
143
53.514
41.420
6.894
1.00
48.12
O


HETATM
2849
O
HOH
144
76.967
51.935
3.952
1.00
54.45
O


HETATM
2850
O
HOH
145
82.602
55.478
15.958
1.00
37.47
O


HETATM
2851
O
HOH
146
58.199
49.374
44.387
1.00
54.43
O


HETATM
2852
O
HOH
147
53.891
73.194
38.807
1.00
45.80
O


HETATM
2853
O
HOH
148
48.842
61.463
23.357
1.00
44.65
O


HETATM
2854
O
HOH
149
49.731
59.561
25.854
1.00
55.20
O


HETATM
2855
O
HOH
150
51.048
56.764
24.880
1.00
58.92
O


HETATM
2856
O
HOH
151
52.529
57.301
22.316
1.00
49.02
O


HETATM
2857
O
HOH
152
46.169
58.096
27.292
1.00
44.50
O


HETATM
2858
O
HOH
153
40.023
51.519
24.080
1.00
57.09
O


HETATM
2859
O
HOH
154
70.783
28.023
10.528
1.00
65.20
O


HETATM
2860
O
HOH
155
55.358
44.178
39.610
1.00
55.31
O


HETATM
2861
O
HOH
156
50.499
52.835
39.274
1.00
56.09
O


HETATM
2862
O
HOH
157
51.427
49.112
39.630
1.00
50.88
O


HETATM
2863
O
HOH
158
54.238
33.150
37.602
1.00
49.72
O


HETATM
2864
O
HOH
159
62.155
53.228
3.383
1.00
55.20
O


HETATM
2865
O
HOH
160
65.352
58.405
21.237
1.00
40.73
O


HETATM
2866
O
HOH
161
55.476
50.398
2.549
1.00
58.50
O


HETATM
2867
O
HOH
162
73.645
34.699
8.566
1.00
52.83
O


HETATM
2868
O
HOH
163
71.990
36.204
6.534
1.00
56.54
O


HETATM
2869
O
HOH
164
70.553
26.585
7.610
1.00
59.27
O








CONECT
 202 2464


CONECT
2464  202


CONECT
2638 2639 2640 2641 2642


CONECT
2639 2638


CONECT
2640 2638


CONECT
2641 2638 2643


CONECT
2642 2638


CONECT
2643 2641 2644


CONECT
2644 2643 2645 2660


CONECT
2645 2644 2646


CONECT
2646 2645 2647 2658


CONECT
2647 2646 2648 2657


CONECT
2648 2647 2649 2655


CONECT
2649 2648 2651


CONECT
2650 2651 2653


CONECT
2651 2649 2650 2652


CONECT
2652 2651


CONECT
2653 2650 2654 2655


CONECT
2654 2653


CONECT
2655 2648 2653 2656


CONECT
2656 2655 2657


CONECT
2657 2647 2656


CONECT
2658 2646 2659 2660


CONECT
2659 2658


CONECT
2660 2644 2658 2661


CONECT
2661 2660


CONECT
2662 2663 2664 2665 2684


CONECT
2663 2662


CONECT
2664 2662


CONECT
2665 2662 2666


CONECT
2666 2665 2667


CONECT
2667 2666 2668 2669


CONECT
2668 2667 2673


CONECT
2669 2667 2670 2671


CONECT
2670 2669


CONECT
2671 2669 2672 2673


CONECT
2672 2671


CONECT
2673 2668 2671 2674


CONECT
2674 2673 2675 2683


CONECT
2675 2674 2676


CONECT
2676 2675 2677


CONECT
2677 2676 2678 2683


CONECT
2678 2677 2679 2680


CONECT
2679 2678


CONECT
2680 2678 2681


CONECT
2681 2680 2682


CONECT
2682 2681 2683


CONECT
2683 2674 2677 2682


CONECT
2684 2662 2685


CONECT
2685 2684 2686 2687 2688


CONECT
2686 2685


CONECT
2687 2685


CONECT
2688 2685 2689


CONECT
2689 2688 2690


CONECT
2690 2689 2691 2692


CONECT
2691 2690 2696


CONECT
2692 2690 2693 2694


CONECT
2693 2692


CONECT
2694 2692 2695 2696


CONECT
2695 2694


CONECT
2696 2691 2694 2697


CONECT
2697 2696 2698 2705


CONECT
2698 2697 2699


CONECT
2699 2698 2700 2703


CONECT
2700 2699 2701 2702


CONECT
2701 2700


CONECT
2702 2700


CONECT
2703 2699 2704


CONECT
2704 2703 2705


CONECT
2705 2697 2704








MASTER
527   0   3   13   18   0   0   6  2868   1  70  39


END


FIG. 14


P-UC 5440


Page 36



















TABLE 6







HEADER

OXIDOREDUCTASE
08-AUG-02 1ME7









TITLE

INOSINE MONOPHOSPHATE DEHYDROGENASE (IMPDH) FROM


TITLE
2
TRITRICHOMONAS FOETUS WITH RVP AND MOA BOUND


COMPND

MOL_ID: 1;


COMPND
2
MOLECULE: INOSINE-5′-MONOPHOSPHATE DEHYDROGENASE;


COMPND
3
CHAIN: A;


COMPND
4
SYNONYM: IMP DEHYDROGENASE, IMPDH;


COMPND
5
EC: 1.1.1.205;


COMPND
6
ENGINEERED: YES


SOURCE

MOL_ID: 1;


SOURCE
2
ORGANISM_SCIENTIFIC: TRITRICHOMONAS FOETUS;


SOURCE
3
GENE: IMPDH;


SOURCE
4
EXPRESSION_SYSTEM: ESCHERICHIA COLI;


SOURCE
5
EXPRESSION_SYSTEM_COMMON: BACTERIA;


SOURCE
6
EXPRESSION_SYSTEM_STRAIN: H712;


SOURCE
7
EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;


SOURCE
8
EXPRESSION_SYSTEM_PLASMID: PBACE


KEYWDS

ALPHA BETA BARREL


EXPDTA

X-RAY DIFFRACTION


AUTHOR

G.L.PROSISE,J.WU,H.LUECKE


JRNL

AUTH G.L.PROSISE,J.WU,H.LUECKE


JRNL

TITL CRYSTAL STRUCTURE OF T. FOETUS INOSINE


JRNL

TITL 2 MONOPHOSPHATE DEHYDROGENASE IN COMPLEX WITH THE


JRNL

TITL 3 INHIBITOR RIBAVIRIN REVEALS A CATALYSIS-DEPENDENT


JRNL

TITL 4 ION BINDING SITE


JRNL

REF TO BE PUBLISHED


JRNL

REFN


REMARK
1


REMARK
2


REMARK
2
RESOLUTION. 2.15 ANGSTROMS.


REMARK
3


REMARK
3
REFINEMENT.










REMARK
3
PROGRAM
: CNS 1.1


REMARK
3
AUTHORS
: BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-


REMARK
3

: KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,


REMARK
3

: READ,RICE,SIMONSON,WARREN


REMARK
3









REMARK
3
REFINEMENT TARGET : ENGH & HUBER


REMARK
3


REMARK
3
DATA USED IN REFINEMENT.










REMARK
3
RESOLUTION RANGE HIGH (ANGSTROMS)
: 2.15


REMARK
3
RESOLUTION RANGE LOW (ANGSTROMS)
: 49.04


REMARK
3
DATA CUTOFF (SIGMA(F))
: 0.000


REMARK
3
OUTLIER CUTOFF HIGH (RMS(ABS(F)))
: NULL


REMARK
3
COMPLETENESS (WORKING+TEST) (%)
: 94.0


REMARK
3
NUMBER OF REFLECTIONS
: 32980


REMARK
3


REMARK
3
FIT TO DATA USED IN REFINEMENT.


REMARK
3
CROSS-VALIDATION METHOD
: THROUGHOUT


REMARK
3
FREE R VALUE TEST SET SELECTION
: RANDOM


REMARK
3
R VALUE (WORKING SET)
: 0.233


REMARK
3
FREE R VALUE
: 0.264


REMARK
3
FREE R VALUE TEST SET SIZE (%)
: 5.200


REMARK
3
FREE R VALUE TEST SET COUNT
: 1712


REMARK
3
ESTIMATED ERROR OF FREE R VALUE
: 0.006


REMARK
3


REMARK
3
FIT IN THE HIGHEST RESOLUTION BIN.


REMARK
3
TOTAL NUMBER OF BINS USED
: 6


REMARK
3
BIN RESOLUTION RANGE HIGH (A)
: 2.15


REMARK
3
BIN RESOLUTION RANGE LOW (A)
: 2.28


REMARK
3
BIN COMPLETENESS (WORKING+TEST) (%)
: 77.30


REMARK
3
REFLECTIONS IN BIN (WORKING SET)
: 4218


REMARK
3
BIN R VALUE (WORKING SET)
: 0.2880


REMARK
3
BIN FREE R VALUE
: 0.3290


REMARK
3
BIN FREE R VALUE TEST SET SIZE (%)
: 4.80


REMARK
3
BIN FREE R VALUE TEST SET COUNT
: 215


REMARK
3
ESTIMATED ERROR OF BIN FREE R VALUE
: 0.023


REMARK
3









REMARK
3
NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.










REMARK
3
PROTEIN ATOMS
: 2782


REMARK
3
NUCLEIC ACID ATOMS
: 0


REMARK
3
HETEROGEN ATOMS
: 46


REMARK
3
SOLVENT ATOMS
: 120


REMARK
3


REMARK
3
B VALUES.










REMARK
3
FROM WILSON PLOT (A**2)
: 33.10


REMARK
3
MEAN B VALUE (OVERALL, A**2)
: 44.70


REMARK
3
OVERALL ANISOTROPIC B VALUE.


REMARK
3
B11 (A**2) : 0.00000


REMARK
3
B22 (A**2) : 0.00000


REMARK
3
B33 (A**2) : 0.00000


REMARK
3
B12 (A**2) : 0.00000


REMARK
3
B13 (A**2) : 0.00000


REMARK
3
B23 (A**2) : 0.00000


REMARK
3


REMARK
3
ESTIMATED COORDINATE ERROR.


REMARK
3
ESD FROM LUZZATI PLOT
(A) : 0.29


REMARK
3
ESD FROM SIGMAA
(A) : 0.25


REMARK
3
LOW RESOLUTION CUTOFF
(A) : 5.00


REMARK
3


REMARK
3
CROSS-VALIDATED ESTIMATED COORDINATE ERROR.


REMARK
3
ESD FROM C-V LUZZATI PLOT
(A) : 0.35


REMARK
3
ESD FROM C-V SIGMAA
(A) : 0.28


REMARK
3


REMARK
3
RMS DEVIATIONS FROM IDEAL VALUES.


REMARK
3
BOND LENGTHS (A)
: 0.006


REMARK
3
BOND ANGLES (DEGREES)
: 1.20


REMARK
3
DIHEDRAL ANGLES (DEGREES)
: 22.50


REMARK
3
IMPROPER ANGLES (DEGREES)
: 0.71


REMARK
3


REMARK
3
ISOTROPIC THERMAL MODEL : RESTRAINED


REMARK
3












REMARK
3
ISOTROPIC THERMAL FACTOR RESTRAINTS.

RMS
SIGMA


REMARK
3
MAIN-CHAIN BOND
(A**2)
: 1.190
; 1.500


REMARK
3
MAIN-CHAIN ANGLE
(A**2)
: 2.070
; 2.000


REMARK
3
SIDE-CHAIN BOND
(A**2)
: 1.630
; 2.000


REMARK
3
SIDE-CHAIN ANGLE
(A**2)
: 2.500
; 2.500


REMARK
3


REMARK
3
BULK SOLVENT MODELING.


REMARK
3
METHOD USED
: FLAT MODEL


REMARK
3
KSOL
: 0.36


REMARK
3
BSOL
: 41.54


REMARK
3


REMARK
3
NCS MODEL : NULL


REMARK
3


REMARK
3
NCS RESTRAINTS.

RMS
SIGMA/WEIGHT


REMARK
3
GROUP 1 POSITIONAL
(A)
: NULL
; NULL


REMARK
3
GROUP 1 B-FACTOR
(A**2)
: NULL
; NULL


REMARK
3










REMARK
3
PARAMETER FILE 1
: PROTEIN_REP.PARAM


REMARK
3
PARAMETER FILE 2
: PARAM.GNSOL


REMARK
3
PARAMETER FILE 3
: CIS_PEPTIDE.PARAM


REMARK
3
PARAMETER FILE 4
: RMP_MPA.PAR


REMARK
3
PARAMETER FILE 5
: ION.PARAM


REMARK
3
PARAMETER FILE 6
: NULL


REMARK
3
TOPOLOGY FILE 1
: PROTEIN.TOP


REMARK
3
TOPOLOGY FILE 2
: RMP.TOP


REMARK
3
TOPOLOGY FILE 3
: MPA.TOP


REMARK
3
TOPOLOGY FILE 4
: ION.TOP


REMARK
3
TOPOLOGY FILE 5
: TOPH.GNSOL


REMARK
3
TOPOLOGY FILE 6
: NULL


REMARK
3









REMARK
3
OTHER REFINEMENT REMARKS: NULL


REMARK
4


REMARK
4
1ME7 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998


REMARK
100


REMARK
100
THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-AUG-2002.


REMARK
100
THE RCSB ID CODE IS RCSB016849.


REMARK
200


REMARK
200
EXPERIMENTAL DETAILS










REMARK
200
EXPERIMENT TYPE
: X-RAY DIFFRACTION


REMARK
200
DATE OF DATA COLLECTION
: 12-JUN-2001


REMARK
200
TEMPERATURE (KELVIN)
: 100.0


REMARK
200
PH
: 7.50


REMARK
200
NUMBER OF CRYSTALS USED
: 1


REMARK
200


REMARK
200
SYNCHROTRON (Y/N)
: Y


REMARK
200
RADIATION SOURCE
: SSRL


REMARK
200
BEAMLINE
: 9-1


REMARK
200
X-RAY GENERATOR MODEL
: NULL


REMARK
200
MONOCHROMATIC OR LAUE (M/L)
: M


REMARK
200
WAVELENGTH OR RANGE (A)
: 0.97


REMARK
200
MONOCHROMATOR
: NULL


REMARK
200
OPTICS
: NULL


REMARK
200


REMARK
200
DETECTOR TYPE
: IMAGE PLATE


REMARK
200
DETECTOR MANUFACTURER
: MARRESEARCH


REMARK
200
INTENSITY-INTEGRATION SOFTWARE
: DENZO


REMARK
200
DATA SCALING SOFTWARE
: SCALEPACK


REMARK
200


REMARK
200
NUMBER OF UNIQUE REFLECTIONS
: 33143


REMARK
200
RESOLUTION RANGE HIGH (A)
: 2.150


REMARK
200
RESOLUTION RANGE LOW (A)
: 50.000


REMARK
200
REJECTION CRITERIA (SIGMA(I))
: 0.000


REMARK
200


REMARK
200
OVERALL.


REMARK
200
COMPLETENESS FOR RANGE (%)
: 94.0


REMARK
200
DATA REDUNDANCY
: 5.300


REMARK
200
R MERGE (I)
: 0.07200


REMARK
200
R SYM (I)
: NULL


REMARK
200
<I/SIGMA(I)> FOR THE DATA SET
: 2.0500


REMARK
200


REMARK
200
IN THE HIGHEST RESOLUTION SHELL.


REMARK
200
HIGHEST RESOLUTION SHELL, RANGE HIGH (A)
: 2.2.5


REMARK
200
HIGHEST RESOLUTION SHELL, RANGE LOW (A)
: 2.19


REMARK
200
COMPLETENESS FOR SHELL (%)
: 79.5


REMARK
200
DATA REDUNDANCY IN SHELL
: NULL


REMARK
200
R MERGE FOR SHELL (I)
: 0.49100


REMARK
200
R SYM FOR SHELL (I)
: NULL


REMARK
200
<I/SIGMA(I)> FOR SHELL
: 2.050


REMARK
200


REMARK
200
DIFFRACTION PROTOCOL: SINGLE WAVELENGTH









REMARK
200
METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS


REMARK
200
SOFTWARE USED: CNS


REMARK
200
STARTING MODEL: PDB ENTRY 1AK5


REMARK
200


REMARK
200
REMARK: NULL


REMARK
280


REMARK
280
CRYSTAL


REMARK
280
SOLVENT CONTENT, VS (%): NULL


REMARK
280
MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL


REMARK
280


REMARK
280
CRYSTALLIZATION CONDITIONS: SODIUM MALONATE, TRIS, 2-


REMARK
280
MERCAPTOETHANOL, EDTA, GLYCEROL


REMARK
290


REMARK
290
CRYSTALLOGRAPHIC SYMMETRY


REMARK
290
SYMMETRY OPERATORS FOR SPACE GROUP: P 4 3 2


REMARK
290










REMARK
290
SYMOP
SYMMETRY


REMARK
290
NNNMMM
OPERATOR


REMARK
290
1555
X,Y,Z


REMARK
290
2555
−X,−Y,Z


REMARK
290
3555
−X,Y,−Z


REMARK
290
4555
X,−Y,−Z


REMARK
290
5555
Z,X,Y


REMARK
290
6555
Z,−X,−Y


REMARK
290
7555
−Z,−X,Y


REMARK
290
8555
−Z,X,−Y


REMARK
290
9555
Y,Z,X


REMARK
290
10555
−Y,Z,−X


REMARK
290
11555
Y,Z,−X


REMARK
290
12555
−Y,−Z,X


REMARK
290
13555
Y,X,Z


REMARK
290
14555
−Y,−X,−Z


REMARK
290
15555
Y,−X,Z


REMARK
290
16555
−Y,X,Z


REMARK
290
17555
X,Z,−Y


REMARK
290
18555
−X,Z,Y


REMARK
290
19555
−X,−Z,−Y


REMARK
290
20555
X,−Z,Y


REMARK
290
21555
Z,Y,−X


REMARK
290
22555
Z,−Y,X


REMARK
290
23555
−Z,Y,X


REMARK
290
24555
−Z,−Y,−X


REMARK
290










REMARK
290
WHERE NNN −>
OPERATOR NUMBER


REMARK
290
MMM −>
TRANSLATION VECTOR


REMARK
290









REMARK
290
CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS


REMARK
290
THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM


REMARK
290
RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY


REMARK
290
RELATED MOLECULES.














REMARK
290
SMTRY1
1
1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY2
1
0.000000
1.000000
0.000000
0.00000


REMARK
290
SMTRY3
1
0.000000
0.000000
1.000000
0.00000


REMARK
290
SMTRY1
2
−1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY2
2
0.000000
−1.000000
0.000000
0.00000


REMARK
290
SMTRY3
2
0.000000
0.000000
1.000000
0.00000


REMARK
290
SMTRY1
3
−1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY2
3
0.000000
1.000000
0.000000
0.00000


REMARK
290
SMTRY3
3
0.000000
0.000000
−1.000000
0.00000


REMARK
290
SMTRY1
4
1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY2
4
0.000000
−1.000000
0.000000
0.00000


REMARK
290
SMTRY3
4
0.000000
0.000000
−1.000000
0.00000


REMARK
290
SMTRY1
5
0.000000
0.000000
1.000000
0.00000


REMARK
290
SMTRY2
5
1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY3
5
0.000000
1.000000
0.000000
0.00000


REMARK
290
SMTRY1
6
0.000000
0.000000
1.000000
0.00000


REMARK
290
SMTRY2
6
−1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY3
6
0.000000
−1.000000
0.000000
0.00000


REMARK
290
SMTRY1
7
0.000000
0.000000
−1.000000
0.00000


REMARK
290
SMTRY2
7
−1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY3
7
0.000000
1.000000
0.000000
0.00000


REMARK
290
SMTRY1
8
0.000000
0.000000
−1.000000
0.00000


REMARK
290
SMTRY2
8
1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY3
8
0.000000
−1.000000
0.000000
0.00000


REMARK
290
SMTRY1
9
0.000000
1.000000
0.000000
0.00000


REMARK
290
SMTRY2
9
0.000000
0.000000
1.000000
0.00000


REMARK
290
SMTRY3
9
1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY1
10
0.000000
−1.000000
0.000000
0.00000


REMARK
290
SMTRY2
10
0.000000
0.000000
1.000000
0.00000


REMARK
290
SMTRY3
10
−1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY1
11
0.000000
1.000000
0.000000
0.00000


REMARK
290
SMTRY2
11
0.000000
0.000000
−1.000000
0.00000


REMARK
290
SMTRY3
11
−1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY1
12
0.000000
−1.000000
0.000000
0.00000


REMARK
290
SMTRY2
12
0.000000
0.000000
−1.000000
0.00000


REMARK
290
SMTRY3
12
1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY1
13
0.000000
1.000000
0.000000
0.00000


REMARK
290
SMTRY2
13
1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY3
13
0.000000
0.000000
−1.000000
0.00000


REMARK
290
SMTRY1
14
0.000000
−1.000000
0.000000
0.00000


REMARK
290
SMTRY2
14
−1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY3
14
0.000000
0.000000
−1.000000
0.00000


REMARK
290
SMTRY1
15
0.000000
1.000000
0.000000
0.00000


REMARK
290
SMTRY2
15
−1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY3
15
0.000000
0.000000
1.000000
0.00000


REMARK
290
SMTRY1
16
0.000000
−1.000000
0.000000
0.00000


REMARK
290
SMTRY2
16
1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY3
16
0.000000
0.000000
1.000000
0.00000


REMARK
290
SMTRY1
17
1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY2
17
0.000000
0.000000
1.000000
0.00000


REMARK
290
SMTRY3
17
0.000000
−1.000000.
0.000000
0.00000


REMARK
290
SMTRY1
18
−1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY2
18
0.000000
0.000000
1.000000
0.00000


REMARK
290
SMTRY3
18
0.000000
1.000000
0.000000
0.00000


REMARK
290
SMTRY1
19
−1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY2
19
0.000000
0.000000
−1.000000
0.00000


REMARK
290
SMTRY3
19
0.000000
−2.000000
0.000000
0.00000


REMARK
290
SMTRY1
20
1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY2
20
0.000000
0.000000
−1.000000
0.00000


REMARK
290
SMTRY3
20
0.000000
1.000000
0.000000
0.00000


REMARK
290
SMTRY1
21
0.000000
0.000000
1.000000
0.00000


REMARK
290
SMTRY2
21
0.000000
1.000000
0.000000
0.00000


REMARK
290
SMTRY3
21
−1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY1
22
0.000000
0.000000
1.000000
0.00000


REMARK
290
SMTRY2
22
0.000000
−1.000000
0.000000
0.00000


REMARK
290
SMTRY3
22
1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY1
23
0.000000
0.000000
−1.000000
0.00000


REMARK
290
SMTRY2
23
0.000000
1.000000
0.000000
0.00000


REMARK
290
SMTRY3
23
1.000000
0.000000
0.000000
0.00000


REMARK
290
SMTRY1
24
0.000000
0.000000
−1.000000
0.00000


REMARK
290
SMTRY2
24
0.000000
−1.000000
0.000000
0.00000


REMARK
290
SMTRY3
24
−1.000000
0.000000
0.000000
0.00000


REMARK
290









REMARK
290
REMARK: NULL


REMARK
300


REMARK
300
BIOMOLECULE: 1


REMARK
300
THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT


REMARK
300
WHICH CONSISTS OF 1 CHAIN(S). SEE REMARK 350 FOR


REMARK
300
INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).


REMARK
350


REMARK
350
GENERATING THE BIOMOLECULE


REMARK
350
COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN


REMARK
350
BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE


REMARK
350
MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS


REMARK
350
GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND


REMARK
350
CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.


REMARK
350


REMARK
350
BIOMOLECULE: 1


REMARK
350
APPLY THE FOLLOWING TO CHAINS: A














REMARK
350
BIOMT1
1
1.000000
0.000000
0.000000
0.00000


REMARK
350
BIOMT2
1
0.000000
1.000000
0.000000
0.00000


REMARK
350
BIOMT3
1
0.000000
0.000000
1.000000
0.00000


REMARK
350
BIOMT1
2
−1.000000
0.000000
0.000000
155.06800


REMARK
350
BIOMT2
2
0.000000
−1.000000
0.000000
155.06800


REMARK
350
BIOMT3
2
0.000000
0.000000
1.000000
0.00000


REMARK
350
BIOMT1
3
0.000000
1.000000
0.000000
0.00000


REMARK
350
BIOMT2
3
−1.000000
0.000000
0.000000
155.06800


REMARK
350
BIOMT3
3
0.000000
0.000000
1.000000
0.00000


REMARK
350
BIOMT1
4
0.000000
−1.000000
0.000000
155.06800


REMARK
350
BIOMT2
4
1.000000
0.000000
0.000000
0.00000


REMARK
350
BIOMT3
4
0.000000
0.000000
1.000000
0.00000


REMARK
465









REMARK
465
MISSING RESIDUES


REMARK
465
THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE


REMARK
465
EXPERIMENT. (M = MODEL NUMBER; RES = RESIDUE NAME; C = CHAIN


REMARK
465
IDENTIFIER; SSSEQ = SEQUENCE NUMBER; I = INSERTION CODE.)


REMARK
465


REMARK
465
M RES C SSSEQI












REMARK
465
MET
A
1



REMARK
465
SER
A
108


REMARK
465
ASN
A
109


REMARK
465
VAL
A
110


REMARK
465
LYS
A
111


REMARK
465
PRO
A
112


REMARK
465
ASP
A
113


REMARK
465
GLN
A
114


REMARK
465
THR
A
115


REMARK
465
PHE
A
116


REMARK
465
ALA
A
117


REMARK
465
ASP
A
118


REMARK
465
VAL
A
119


REMARK
465
LEU
A
120


REMARK
465
ALA
A
121


REMARK
465
ILE
A
122


REMARK
465
SER
A
123


REMARK
465
GLN
A
124


REMARK
465
ARG
A
125


REMARK
465
THR
A
126


REMARK
465
THR
A
127


REMARK
465
HIS
A
128


REMARK
465
ASN
A
129


REMARK
465
THR
A
130


REMARK
465
VAL
A
131


REMARK
465
ALA
A
132


REMARK
465
VAL
A
133


REMARK
465
THR
A
134


REMARK
465
ASP
A
135


REMARK
465
ASP
A
136


REMARK
465
GLY
A
137


REMARK
465
THR
A
138


REMARK
465
PRO
A
139


REMARK
465
HIS
A
140


REMARK
465
GLY
A
141


REMARK
465
VAL
A
142


REMARK
465
LEU
A
143


REMARK
465
LEU
A
144


REMARK
465
GLY
A
145


REMARK
465
LEU
A
146


REMARK
465
VAL
A
147


REMARK
465
THR
A
148


REMARK
465
GLN
A
149


REMARK
465
ARG
A
150


REMARK
465
ASP
A
151


REMARK
465
TYR
A
152


REMARK
465
PRO
A
153


REMARK
465
ILE
A
154


REMARK
465
ASP
A
155


REMARK
465
LEU
A
156


REMARK
465
THR
A
157


REMARK
465
GLN
A
158


REMARK
465
THR
A
159


REMARK
465
GLU
A
160


REMARK
465
THR
A
161


REMARK
465
LYS
A
162


REMARK
465
VAL
A
163


REMARK
465
SER
A
164


REMARK
465
ASP
A
165


REMARK
465
MET
A
166


REMARK
465
MET
A
167


REMARK
465
THR
A
168


REMARK
465
PRO
A
169


REMARK
465
PHE
A
170


REMARK
465
SER
A
171


REMARK
465
LYS
A
172


REMARK
465
LEU
A
173


REMARK
465
VAL
A
174


REMARK
465
THR
A
175


REMARK
465
ALA
A
176


REMARK
465
HIS
A
177


REMARK
465
GLN
A
178


REMARK
465
ASP
A
179


REMARK
465
THR
A
180


REMARK
465
LYS
A
181


REMARK
465
LEU
A
182


REMARK
465
SER
A
183


REMARK
465
GLU
A
184


REMARK
465
ALA
A
185


REMARK
465
ASN
A
186


REMARK
465
LYS
A
187


REMARK
465
ILE
A
188


REMARK
465
ILE
A
189


REMARK
465
TRP
A
190


REMARK
465
GLU
A
191


REMARK
465
LYS
A
192


REMARK
465
LYS
A
193


REMARK
465
LEU
A
194


REMARK
465
ASN
A
195


REMARK
465
ALA
A
196


REMARK
465
LEU
A
197


REMARK
465
PRO
A
198


REMARK
465
ILE
A
199


REMARK
465
ILE
A
200


REMARK
465
ASP
A
201


REMARK
465
ASP
A
202


REMARK
465
ASP
A
203


REMARK
465
GLN
A
204


REMARK
465
HIS
A
205


REMARK
465
LEU
A
206


REMARK
465
ARG
A
207


REMARK
465
TYR
A
208


REMARK
465
ILE
A
209


REMARK
465
VAL
A
210


REMARK
465
PHE
A
211


REMARK
465
ARG
A
212


REMARK
465
LYS
A
213


REMARK
465
ASP
A
214


REMARK
465
TYR
A
215


REMARK
465
ASP
A
216


REMARK
465
ARG
A
217


REMARK
465
SER
A
218


REMARK
465
GLN
A
219


REMARK
465
GLN
A
417


REMARK
465
ARG
A
418


REMARK
465
TYR
A
419


REMARK
465
ASP
A
420


REMARK
465
LEU
A
421


REMARK
465
GLY
A
422


REMARK
465
GLY
A
423


REMARK
465
LYS
A
424


REMARK
465
GLN
A
425


REMARK
465
LYS
A
426


REMARK
465
LEU
A
427


REMARK
465
SER
A
428


REMARK
465
PHE
A
429


REMARK
465
GLU
A
430


REMARK
465
VAL
A
493


REMARK
465
LYS
A
494


REMARK
465
ASP
A
495


REMARK
465
ARG
A
496


REMARK
465
ILE
A
497


REMARK
465
ASN
A
498


REMARK
465
ASP
A
499


REMARK
465
TYR
A
500


REMARK
465
HIS
A
502


REMARK
465
PRO
A
502


REMARK
465
LYS
A
503


REMARK
500









REMARK
500
GEOMETRY AND STEREOCHEMISTRY


REMARK
500
SUBTOPIC: COVALENT BOND LENGTHS


REMARK
500


REMARK
500
THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES


REMARK
500
HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE


REMARK
500
THAN 6*RMSD (M = MODEL NUMBER; RES = RESIDUE NAME; C = CHAIN


REMARK
500
IDENTIFIER; SSEQ = SEQUENCE NUMBER; I = INSERTION CODE).


REMARK
500


REMARK
500
STANDARD TABLE:


REMARK
500
FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3)


REMARK
500


REMARK
500
EXPECTED VALUES: ENGH AND HUBER, 1991


REMARK
500













REMARK
500
M RES CSSEQI
ATM1
RES CSSEQI
ATM2
DEVIATION


REMARK
500
ASP A 107
OD2
ASP A 107
CG
0.080


REMARK
500
MET A 373
CE
MET A 373
SD
0.038


REMARK
500









REMARK
500
GEOMETRY AND STEREOCHEMISTRY.


REMARK
500
SUBTOPIC: COVALENT BOND ANGLES


REMARK
500


REMARK
500
THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES


REMARK
500
HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE


REMARK
500
THAN 6*RMSD (M = MODEL NUMBER; RES = RESIDUE NAME; C = CHAIN


REMARK
500
IDENTIFIER; SSEQ = SEQUENCE NUMBER; I = INSERTION CODE).


REMARK
500


REMARK
500
STANDARD TABLE:


REMARK
500
FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)


REMARK
500


REMARK
500
EXPECTED VALUES: ENGH AND HUBER, 1991


REMARK
500













REMARK
500
M RES CSSEQI
ATM1
ATM2
ATM3



REMARK
500
GLY A 20
N −
CA −
C ANGL. DEV. = −7.6 DEGREES


REMARK
500
ILE A 27
N −
CA −
C ANGL. DEV. = −7.8 DEGREES


REMARK
500
ILE A 52
N −
CA −
C ANGL. DEV. = −7.9 DEGREES


REMARK
500
SER A 63
N −
CA −
C ANGL. DEV. = 8.1 DEGREES


REMARK
500
GLY A 64
N −
CA −
C ANGL. DEV. = −7.5 DEGREES


REMARK
500
GLY A 305
N −
CA −
C ANGL. DEV. = 7.5 DEGREES


REMARK
500
SER A 357
N −
CA −
C ANGL. DEV. = −7.4 DEGREES


REMARK
500
LYS A 444
N −
CA −
C ANGL. DEV. = 7.7 DEGREES


REMARK
500
LYS A 472
N −
CA −
C ANGL. DEV. = 7.6 DEGREES


REMARK
500
LYS A 474
N −
CA −
C ANGL. DEV. = −9.1 DEGREES


REMARK
500
LEU A 477
N −
CA −
C ANGL. DEV. = −8.2 DEGREES


REMARK
900









REMARK
900
RELATED ENTRIES


REMARK
900
RELATED ID: 1AK5  RELATED DB: PDB


REMARK
900
INOSINE MONOPHOSPHATE DEHYDROGENASE (IMPDH) FROM


REMARK
900
TRITRICHOMONAS FOETUS


REMARK
900
RELATED ID: 1ME8  RELATED DB: PDB


REMARK
900
1ME8 CONTAINS THE SAME PROTEIN WITH RVP BOUND


REMARK
900
RELATED ID: 1ME9  RELATED DB: PDB


REMARK
900
1ME9 CONTAINS THE SAME PROTEIN WITH IMP BOUND


REMARK
900
RELATED ID: 1MEH  RELATED DB: PDB


REMARK
900
1MEH CONTAINS THE SAME PROTEIN WITH IMP AND MOA BOUND


REMARK
900
RELATED ID: 1MEI  RELATED DB: PDB


REMARK
900
1MEI CONTAINS THE SAME PROTEIN WITH XMP AND MYCOPHENOLIC


REMARK
900
ACID BOUND


REMARK
900
RELATED ID: 1MEW  RELATED DB: PDB


REMARK
900
1MEW CONTAINS THE SAME PROTEIN WITH XMP AND NAD BOUND


DBREF
1ME7
A  1  503  SWS  P50097  IMDH_TRIFO   1  503























SEQRES
1
A
503
MET
ALA
LYS
TYR
TYR
ASN
GLU
PRO
CYS
HIS
THR
PHE
ASN


SEQRES
2
A
503
GLU
TYR
LEU
LEU
ILE
PRO
GLY
LEU
SER
THR
VAL
ASP
CYS


SEQRES
3
A
503
ILE
PRO
SER
ASN
VAL
ASN
LEU
SER
THR
PRO
LEU
VAL
LYS


SEQRES
4
A
503
PHE
GLN
LYS
GLY
GLN
GLN
SER
GLU
ILE
ASN
LEU
LYS
ILE


SEQRES
5
A
503
PRO
LEU
VAL
SER
ALA
ILE
MET
GLN
SER
VAL
SER
GLY
GLU


SEQRES
6
A
503
LYS
MET
ALA
ILE
ALA
LEU
ALA
ARG
GLU
GLY
GLY
ILE
SER


SEQRES
7
A
503
PHE
ILE
PHE
GLY
SER
GLN
SER
ILE
GLU
SER
GLN
ALA
ALA


SEQRES
8
A
503
MET
VAL
HIS
ALA
VAL
LYS
ASN
PHE
LYS
ALA
GLY
PHE
VAL


SEQRES
9
A
503
VAL
SER
ASP
SER
ASN
VAL
LYS
PRO
ASP
GLN
THR
PHE
ALA


SEQRES
10
A
503
ASP
VAL
LEU
ALA
ILE
SER
GLN
ARG
THR
THR
HIS
ASN
THR


SEQRES
11
A
503
VAL
ALA
VAL
THR
ASP
ASP
GLY
THR
PRO
HIS
GLY
VAL
LEU


SEQRES
12
A
503
LEU
GLY
LEU
VAL
THR
GLN
ARG
ASP
TYR
PRO
ILE
ASP
LEU


SEQRES
13
A
503
THR
GLN
THR
GLU
THR
LYS
VAL
SER
ASP
MET
MET
THR
PRO


SEQRES
14
A
503
PHE
SER
LYS
LEU
VAL
THR
ALA
HIS
GLN
ASP
THR
LYS
LEU


SEQRES
15
A
503
SER
GLU
ALA
ASN
LYS
ILE
ILE
TRP
GLU
LYS
LYS
LEU
ASN


SEQRES
16
A
503
ALA
LEU
PRO
ILE
ILE
ASP
ASP
ASP
GLN
HIS
LEU
ARG
TYR


SEQRES
17
A
503
ILE
VAL
PHE
ARG
LYS
ASP
TYR
ASP
ARG
SER
GLN
VAL
CYS


SEQRES
18
A
503
HIS
ASN
GLU
LEU
VAL
ASP
SER
GLN
LYS
ARG
TYR
LEU
VAL


SEQRES
19
A
503
GLY
ALA
GLY
ILE
ASN
THR
ARG
ASP
PHE
ARG
GLU
ARG
VAL


SEQRES
20
A
503
PRO
ALA
LEU
VAL
GLU
ALA
GLY
ALA
ASP
VAL
LEU
CYS
ILE


SEQRES
21
A
503
ASP
SER
SER
ASP
GLY
PHE
SER
GLU
TRP
GLN
LYS
ILE
THR


SEQRES
22
A
503
ILE
GLY
TRP
ILE
ARG
GLU
LYS
TYR
GLY
ASP
LYS
VAL
LYS


SEQRES
23
A
503
VAL
GLY
ALA
GLY
ASN
ILE
VAL
ASP
GLY
GLU
GLY
PHE
ARG


SEQRES
24
A
503
TYR
LEU
ALA
ASP
ALA
GLY
ALA
ASP
PHE
ILE
LYS
ILE
GLY


SEQRES
25
A
503
ILE
GLY
GLY
GLY
SER
ILE
CYS
ILE
THR
ARG
GLU
GLN
LYS


SEQRES
26
A
503
GLY
ILE
GLY
ARG
GLY
GLN
ALA
THR
ALA
VAL
ILE
ASP
VAL


SEQRES
27
A
503
VAL
ALA
GLU
ARG
ASN
LYS
TYR
PHE
GLU
GLU
THR
GLY
ILE


SEQRES
28
A
503
TYR
ILE
PRO
VAL
CYS
SER
ASP
GLY
GLY
ILE
VAL
TYR
ASP


SEQRES
29
A
503
TYR
HIS
MET
THR
LEU
ALA
LEU
ALA
MET
GLY
ALA
ASP
PHE


SEQRES
30
A
503
ILE
MET
LEU
GLY
ARG
TYR
PHE
ALA
ARG
PHE
GLU
GLU
SER


SEQRES
31
A
503
PRO
THR
ARG
LYS
VAL
THR
ILE
ASN
GLY
SER
VAL
MET
LYS


SEQRES
32
A
503
GLU
TYR
TRP
GLY
GLU
GLY
SER
SER
ARG
ALA
ARG
ASN
TRP


SEQRES
33
A
503
GLN
ARG
TYR
ASP
LEU
GLY
GLY
LYS
GLN
LYS
LEU
SER
PHE


SEQRES
34
A
503
GLU
GLU
GLY
VAL
ASP
SER
TYR
VAL
PRO
TYR
ALA
GLY
LYS


SEQRES
35
A
503
LEU
LYS
ASP
ASN
VAL
GLU
ALA
SER
LEU
ASN
LYS
VAL
LYS


SEQRES
36
A
503
SER
THR
MET
CYS
ASN
CYS
GLY
ALA
LEU
THR
ILE
PRO
GLN


SEQRES
37
A
503
LEU
GLN
SER
LYS
ALA
LYS
ILE
THR
LEU
VAL
SER
SER
VAL


SEQRES
38
A
503
SER
ILE
VAL
GLU
GLY
GLY
ALA
HIS
ASP
VAL
ILE
VAL
LYS


SEQRES
39
A
503
ASP
ARG
ILE
ASN
ASP
TYR
HIS
PRO
LYS


HET
NA

901

 1


HET
K
A
900

 1


HET
RVP

602

21


RET
MOA

600

23









HETNAM

NA SODIUM ION


HETNAM

K POTASSIUM ION


HETNAN

RVP RIBAVIRIN MONOPHOSPHATE


HETNAN

MOA MYCOPHENOLIC ACID


HETSYN

MOA 6-(1,3-DIHYDRO-7-HYDROXY-5-METHOXY-4-METHYL-1-


HETSYN
2
MOA OXOISOBENZOFURAN-6-YL)-4-METHYL-4-HEXANOIC ACID










FORMUL
2
NA
NA1 1+


FORMUL
3
K
K1 1+


FORMUL
4
RVP
C8 H13 N4 O8 P1


FORMUL
5
MOA
C17 H20 O6


FORMUL
6
HON
*120 (H2 O1)


























HELIX
1
1
THR
A
11
ASN
A
13
5








3



HELIX
2
2
ILE
A
27
VAL
A
31
5








5


HELIX
3
3
GLY
A
64
GLU
A
74
1








11


HELIX
4
4
SER
A
85
ASN
A
98
1








14


HELIX
5
5
ASP
A
242
ALA
A
253
1








12


HELIX
6
6
SER
A
267
GLY
A
282
1








16


HELIX
7
7
ASP
A
283
VAL
A
285
5








3


HELIX
8
8
ASP
A
294
ALA
A
304
1








11


HELIX
9
9
GLY
A
330
GLY
A
350
1








21


HELIX
10
10
TYR
A
363
MET
A
373
1








11


HELIX
11
11
GLY
A
381
ARG
A
386
1








6


HELIX
12
12
LYS
A
442
CYS
A
461
1








20


HELIX
13
13
THR
A
465
ALA
A
473
1








9


SHEET
1
A
2
TYR
A
15
ILE
A
18
0


SHEET
2
A
2
LYS
A
474
LEU
A
477
−1
O
LYS
A
474
N
ILE
A
18


SHEET
1
B
2
THR
A
35
PRO
A
36
0


SHEET
2
B
2
ASN
A
49
LEU
A
50
−1
O
LEU
A
50
N
THR
A
35


SHEET
1
C
2
PHE
A
40
GLN
A
41
0


SHEET
2
C
2
ILE
A
351
TYR
A
352
−1
O
TYR
A
352
N
PHE
A
40


SHEET
1
D
9
LEU
A
54
SER
A
56
0


SHEET
2
D
9
ILE
A
77
ILE
A
80
1
O
ILE
A
77
N
SER
A
56


SHEET
3
D
9
GLY
A
235
ILE
A
238
1
O
GLY
A
237
N
ILE
A
80


SHEET
4
D
9
VAL
A
257
ILE
A
260
1
O
CYS
A
259
N
ILE
A
238


SHEET
5
D
9
VAL
A
287
ILE
A
292
1
O
GLY
A
288
N
LEU
A
258


SHEET
6
D
9
PHE
A
308
ILE
A
311
1
O
LYS
A
310
N
ALA
A
289


SHEET
7
D
9
VAL
A
355
ASP
A
358
1
O
CYS
A
356
N
ILE
A
311


SHEET
8
D
9
PHE
A
377
LEU
A
380
1
O
MET
A
379
N
SER
A
357


SHEET
9
D
9
LEU
A
54
SER
A
56
1
N
VAL
A
55
O
ILE
A
378


SHEET
1
E
3
LYS
A
394
ILE
A
397
0


SHEET
2
E
3
SER
A
400
TRP
A
406
−1
O
MET
A
402
N
VAL
A
395


SHEET
3
E
3
ASP
A
434
PRO
A
438
−1
O
SER
A
435
N
TYR
A
405

















SSBOND
1
CYS
A
26
CYS
A
459





CISPEP
1
GLY
A
290
ASN
A
291
0
1.08















CRYST1
155.068
155.068
155.068
90.00
90.00
90.00
P 4 3 2
24













ORIGX1

1.000000
0.000000
0.000000
0.00000



ORIGX2

0.000000
1.000000
0.000000
0.00000


ORIGX3

0.000000
0.000000
1.000000
0.00000


SCALE1

0.006449
0.000000
0.000000
0.00000


SCALE2

0.000000
0.006449
0.000000
0.00000


SCALE3

0.000000
0.000000
0.006449
0.00000


















ATOM
1
N
ALA
A
2
55.337
75.180
36.704
1.00
34.41
N


ATOM
2
CA
ALA
A
2
56.037
74.068
35.999
1.00
33.40
C


ATOM
3
C
ALA
A
2
57.330
73.693
36.728
1.00
33.89
C


ATOM
4
O
ALA
A
2
57.769
74.397
37.640
1.00
32.06
O


ATOM
5
CB
ALA
A
2
56.344
74.482
34.569
1.00
33.59
C


ATOM
6
N
LYS
A
3
57.931
72.578
36.328
1.00
33.85
N


ATOM
7
CA
LYS
A
3
59.175
72.132
36.943
1.00
35.52
C


ATOM
8
C
LYS
A
3
60.319
72.311
35.953
1.00
34.41
C


ATOM
9
O
LYS
A
3
60.214
71.899
34.800
1.00
34.80
O


ATOM
10
CB
LYS
A
3
59.086
70.654
37.343
1.00
38.16
C


ATOM
11
CG
LYS
A
3
60.364
70.140
38.018
1.00
42.91
C


ATOM
12
CD
LYS
A
3
60.512
68.625
37.892
1.00
46.63
C


ATOM
13
CE
LYS
A
3
61.851
68.159
38.443
1.00
48.14
C


ATOM
14
NZ
LYS
A
3
62.983
68.796
37.717
1.00
49.64
N


ATOM
15
N
TYR
A
4
61.410
72.915
36.413
1.00
33.82
N


ATOM
16
CA
TYR
A
4
62.582
73.157
35.576
1.00
34.00
C


ATOM
17
C
TYR
A
4
63.792
72.378
36.094
1.00
35.31
C


ATOM
18
O
TYR
A
4
63.748
71.806
37.179
1.00
35.23
O


ATOM
19
CB
TYR
A
4
62.886
74.661
35.548
1.00
32.00
C


ATOM
20
CG
TYR
A
4
61.771
75.471
34.930
1.00
31.34
C


ATOM
21
CD1
TYR
A
4
61.659
75.598
33.546
1.00
30.66
C


ATOM
22
CD2
TYR
A
4
60.793
76.070
35.726
1.00
32.52
C


ATOM
23
CE1
TYR
A
4
60.593
76.303
32.969
1.00
29.90
C


ATOM
24
CE2
TYR
A
4
59.726
76.776
35.158
1.00
30.38
C


ATOM
25
CZ
TYR
A
4
59.635
76.884
33.784
1.00
29.87
C


ATOM
26
OH
TYR
A
4
58.582
77.565
33.222
1.00
31.29
O


ATOM
27
N
TYR
A
5
64.867
72.351
35.314
1.00
36.84
N


ATOM
28
CA
TYR
A
5
66.072
71.630
35.708
1.00
38.47
C


ATOM
29
C
TYR
A
5
67.273
72.559
35.843
1.00
39.48
C


ATOM
30
O
TYR
A
5
67.312
73.636
35.243
1.00
39.29
O


ATOM
31
CB
TYR
A
5
66.377
70.519
34.698
1.00
37.98
C


ATOM
32
CG
TYR
A
5
65.243
69.530
34.551
1.00
38.25
C


ATOM
33
CD1
TYR
A
5
64.068
69.884
33.884
1.00
38.19
C


ATOM
34
CD2
TYR
A
5
65.320
68.258
35.128
1.00
37.95
C


ATOM
35
CE1
TYR
A
5
62.995
69.002
33.796
1.00
38.93
C


ATOM
36
CE2
TYR
A
5
64.251
67.363
35.050
1.00
38.15
C


ATOM
37
CZ
TYR
A
5
63.091
67.744
34.383
1.00
39.68
C


ATOM
38
OH
TYR
A
5
62.028
66.879
34.309
1.00
38.51
O


ATOM
39
N
ASN
A
6
68.249
72.136
36.641
1.00
40.42
N


ATOM
40
CA
ASN
A
6
69.450
72.931
36.876
1.00
41.21
C


ATOM
41
C
ASN
A
6
70.427
72.917
35.706
1.00
40.26
C


ATOM
42
O
ASN
A
6
71.205
73.851
35.543
1.00
40.88
O


ATOM
43
CB
ASN
A
6
70.164
72.432
38.134
1.00
44.17
C


ATOM
44
CG
ASN
A
6
69.365
72.682
39.400
1.00
48.00
C


ATOM
45
OD1
ASN
A
6
69.468
71.926
40.371
1.00
49.62
O


ATOM
46
ND2
ASN
A
6
68.574
73.757
39.405
1.00
49.76
N


ATOM
47
N
GLU
A
7
70.388
71.868
34.892
1.00
38.65
N


ATOM
48
CA
GLU
A
7
71.304
71.760
33.754
1.00
37.25
C


ATOM
49
C
GLU
A
7
70.606
71.443
32.441
1.00
34.73
C


ATOM
50
O
GLU
A
7
69.592
70.750
32.417
1.00
34.20
O


ATOM
51
CB
GLU
A
7
72.340
70.656
34.004
1.00
38.95
C


ATOM
52
CG
GLU
A
7
73.284
70.878
35.186
1.00
43.43
C


ATOM
53
CD
GLU
A
7
74.155
72.110
35.020
1.00
45.61
C


ATOM
54
OE1
GLU
A
7
74.568
72.401
33.874
1.00
45.97
O


ATOM
55
OE2
GLU
A
7
74.438
72.779
36.040
1.00
49.17
O


ATOM
56
N
PRO
A
8
71.140
71.952
31.326
1.00
32.47
N


ATOM
57
CA
PRO
A
8
70.498
71.644
30.048
1.00
31.28
C


ATOM
58
C
PRO
A
8
70.855
70.188
29.731
1.00
31.10
C


ATOM
59
O
PRO
A
8
71.830
69.667
30.271
1.00
30.11
O


ATOM
60
CB
PRO
A
8
71.160
72.627
29.089
1.00
31.56
C


ATOM
61
CG
PRO
A
8
72.558
72.782
29.675
1.00
30.51
C


ATOM
62
CD
PRO
A
8
72.273
72.883
31.153
1.00
32.79
C


ATOM
63
N
CYS
A
9
70.077
69.522
28.882
1.00
30.22
N


ATOM
64
CA
CYS
A
9
70.389
68.137
28.531
1.00
29.58
C


ATOM
65
C
CYS
A
9
71.493
68.098
27.462
1.00
28.36
C


ATOM
66
O
CYS
A
9
71.727
69.096
26.772
1.00
26.35
O


ATOM
67
CB
CYS
A
9
69.124
67.414
28.046
1.00
31.88
C


ATOM
68
SG
CYS
A
9
68.260
68.177
26.653
1.00
38.35
S


ATOM
69
N
HIS
A
10
72.169
66.955
27.343
1.00
27.89
N


ATOM
70
CA
HIS
A
10
73.271
66.765
26.391
1.00
27.84
C


ATOM
71
C
HIS
A
10
73.107
65.471
25.593
1.00
28.16
C


ATOM
72
O
HIS
A
10
72.470
64.524
26.066
1.00
27.35
O


ATOM
73
CB
HIS
A
10
74.610
66.693
27.142
1.00
29.04
C


ATOM
74
CG
HIS
A
10
74.871
67.865
28.034
1.00
30.87
C


ATOM
75
ND1
HIS
A
10
75.329
69.075
27.560
1.00
30.98
N


ATOM
76
CD2
HIS
A
10
74.695
68.025
29.368
1.00
31.03
C


ATOM
77
CE1
HIS
A
10
75.423
69.931
28.563
1.00
30.39
C


ATOM
78
NE2
HIS
A
10
75.045
69.318
29.670
1.00
31.86
N


ATOM
79
N
THR
A
11
73.690
65.440
24.393
1.00
28.34
N


ATOM
80
CA
THR
A
11
73.642
64.268
23.505
1.00
30.45
C


ATOM
81
C
THR
A
11
75.019
63.582
23.511
1.00
29.54
C


ATOM
82
O
THR
A
11
75.994
64.158
23.987
1.00
29.40
O


ATOM
83
CE
THR
A
11
73.324
64.667
22.038
1.00
31.33
C


ATOM
84
OG1
THR
A
11
74.374
65.507
21.537
1.00
35.21
O


ATOM
85
CG2
THR
A
11
72.016
65.425
21.947
1.00
32.48
C


ATOM
86
N
PHE
A
12
75.095
62.368
22.964
1.00
30.67
N


ATOM
87
CA
PHE
A
12
76.349
61.606
22.916
1.00
32.58
C


ATOM
88
C
PHE
A
12
77.534
62.334
22.291
1.00
32.84
C


ATOM
89
O
PHE
A
12
78.664
62.178
22.745
1.00
32.45
O


ATOM
90
CB
PHE
A
12
76.155
60.280
22.167
1.00
32.22
C


ATOM
91
CG
PHE
A
12
75.231
59.318
22.859
1.00
32.84
C


ATOM
92
CD1
PHE
A
12
75.383
59.038
24.213
1.00
32.67
C


ATOM
93
CD2
PHE
A
12
74.217
58.682
22.152
1.00
32.52
C


ATOM
94
CE1
PHE
A
12
74.535
58.137
24.854
1.00
33.67
C


ATOM
95
CE2
PHE
A
12
73.364
57.777
22.783
1.00
32.40
C


ATOM
96
CZ
PHE
A
12
73.522
57.505
24.133
1.00
32.01
C


ATOM
97
N
ASN
A
13
77.280
63.111
21.242
1.00
34.83
N


ATOM
98
CA
ASN
A
13
78.341
63.850
20.564
1.00
35.40
C


ATOM
99
C
ASN
A
13
79.075
64.842
21.460
1.00
34.57
C


ATOM
100
O
ASN
A
13
80.147
65.319
21.096
1.00
34.83
O


ATOM
101
CE
ASN
A
13
77.783
64.602
19.349
1.00
39.42
C


ATOM
102
CG
ASN
A
13
77.635
63.714
18.130
1.00
44.49
C


ATOM
103
OD1
ASN
A
13
78.553
62.970
17.773
1.00
47.75
O


ATOM
104
ND2
ASN
A
13
76.482
63.796
17.473
1.00
48.05
N


ATOM
105
N
GLU
A
14
78.501
65.153
22.621
1.00
33.44
N


ATOM
106
CA
GLU
A
14
79.108
66.100
23.553
1.00
33.47
C


ATOM
107
C
GLU
A
14
80.050
65.462
24.572
1.00
33.77
C


ATOM
108
O
GLU
A
14
80.608
66.157
25.418
1.00
34.50
O


ATOM
109
CE
GLU
A
14
78.018
66.868
24.307
1.00
32.95
C


ATOM
110
CG
GLU
A
14
77.087
67.648
23.406
1.00
33.19
C


ATOM
111
CD
GLU
A
14
76.050
68.434
24.175
1.00
32.32
C


ATOM
112
OE1
GLU
A
14
76.433
69.350
24.936
1.00
32.77
O


ATOM
113
OE2
GLU
A
14
74.852
68.131
24.016
1.00
31.82
O


ATOM
114
N
TYR
A
15
80.230
64.148
24.496
1.00
32.50
N


ATOM
115
CA
TYR
A
15
81.093
63.463
25.444
1.00
31.35
C


ATOM
116
C
TYR
A
15
82.280
62.747
24.829
1.00
32.01
C


ATOM
117
O
TYR
A
15
82.283
62.403
23.649
1.00
32.05
O


ATOM
118
CB
TYR
A
15
80.286
62.435
26.236
1.00
30.88
C


ATOM
119
CG
TYR
A
15
79.251
63.028
27.153
1.00
31.45
C


ATOM
120
CD1
TYR
A
15
79.571
63.380
28.462
1.00
31.97
C


ATOM
121
CD2
TYR
A
15
77.947
63.241
26.710
1.00
31.39
C


ATOM
122
CE1
TYR
A
15
78.614
63.928
29.314
1.00
33.72
C


ATOM
123
CE2
TYR
A
15
76.986
63.790
27.549
1.00
33.18
C


ATOM
124
CZ
TYR
A
15
77.321
64.129
28.846
1.00
32.92
C


ATOM
125
ON
TYR
A
15
76.363
64.677
29.669
1.00
36.12
O


ATOM
126
N
LEU
A
16
83.290
62.523
25.661
1.00
32.48
N


ATOM
127
CA
LEU
A
16
84.479
61.779
25.263
1.00
31.96
C


ATOM
128
C
LEU
A
16
84.859
60.959
26.486
1.00
30.88
C


ATOM
129
O
LEU
A
16
84.541
61.336
27.609
1.00
29.12
O


ATOM
130
CB
LEU
A
16
85.641
62.711
24.888
1.00
31.45
C


ATOM
131
CG
LEU
A
16
85.562
63.515
23.583
1.00
33.88
C


ATOM
132
CD1
LEU
A
16
86.829
64.331
23.436
1.00
34.99
C


ATOM
133
CD2
LEU
A
16
85.406
62.591
22.383
1.00
33.78
C


ATOM
134
N
LEU A
17
85.521
59.830
26.261
1.00
31.45
N


ATOM
135
CA
LEU
A
17
85.977
58.966
27.347
1.00
32.43
C


ATOM
136
C
LEU
A
17
87.454
59.276
27.617
1.00
32.04
C


ATOM
137
O
LEU
A
17
88.245
59.410
26.678
1.00
32.62
O


ATOM
138
CB
LEU
A
17
85.840
57.489
26.944
1.00
31.23
C


ATOM
139
CG
LEU
A
17
84.423
56.919
26.852
1.00
32.03
C


ATOM
140
CD1
LEU
A
17
84.389
55.730
25.898
1.00
30.72
C


ATOM
141
CD2
LEU
A
17
83.943
56.532
28.243
1.00
29.59
C


ATOM
142
N
ILE
A
18
87.809
59.410
28.893
1.00
31.01
N


ATOM
143
CA
ILE
A
18
89.190
59.664
29.287
1.00
30.55
C


ATOM
144
C
ILE
A
18
89.743
58.306
29.717
1.00
30.47
C


ATOM
145
O
ILE
A
18
89.188
57.659
30.598
1.00
30.46
O


ATOM
146
CB
ILE
A
18
89.273
60.651
30.471
1.00
30.96
C


ATOM
147
CG1
ILE
A
18
88.794
62.035
30.026
1.00
31.21
C


ATOM
148
CG2
ILE
A
18
90.712
60.731
30.989
1.00
29.69
C


ATOM
149
CD1
ILE
A
18
88.792
63.066
31.139
1.00
32.55
C


ATOM
150
N
PRO
A
19
90.842
57.857
29.095
1.00
30.24
N


ATOM
151
CA
PRO
A
19
91.439
56.562
29.428
1.00
32.18
C


ATOM
152
C
PRO
A
19
91.766
56.336
30.903
1.00
31.60
C


ATOM
153
O
PRO
A
19
91.999
57.282
31.662
1.00
31.91
O


ATOM
154
CB
PRO
A
19
92.697
56.517
28.552
1.00
31.40
C


ATOM
155
CG
PRO
A
19
92.326
57.403
27.384
1.00
31.65
C


ATOM
156
CD
PRO
A
19
91.634
58.550
28.065
1.00
30.73
C


ATOM
157
N
GLY
A
20
91.757
55.062
31.285
1.00
31.52
N


ATOM
158
CA
GLY
A
20
92.092
54.655
32.638
1.00
31.25
C


ATOM
159
C
GLY
A
20
93.307
53.755
32.485
1.00
31.86
C


ATOM
160
O
GLY
A
20
93.903
53.696
31.403
1.00
30.12
O


ATOM
161
N
LEU
A
21
93.677
53.040
33.539
1.00
32.96
N


ATOM
162
CA
LEU
A
21
94.840
52.163
33.458
1.00
34.19
C


ATOM
163
C
LEU
A
21
94.525
50.904
32.669
1.00
33.97
C


ATOM
164
O
LEU
A
21
93.619
50.151
33.020
1.00
34.45
O


ATOM
165
CB
LEU
A
21
95.330
51.770
34.863
1.00
34.37
C


ATOM
166
CG
LEU
A
21
96.489
50.759
34.904
1.00
34.20
C


ATOM
167
CD1
LEU
A
21
97.700
51.336
34.182
1.00
30.55
C


ATOM
168
CD2
LEU
A
21
96.838
50.420
36.355
1.00
34.84
C


ATOM
169
N
SER
A
22
95.269
50.688
31.592
1.00
34.75
N


ATOM
170
CA
SER
A
22
95.079
49.502
30.774
1.00
36.74
C


ATOM
171
C
SER
A
22
96.083
48.451
31.233
1.00
38.35
C


ATOM
172
O
SER
A
22
97.294
48.668
31.165
1.00
36.70
O


ATOM
173
CB
SER
A
22
95.313
49.827
29.300
1.00
36.32
C


ATOM
174
OG
SER
A
22
94.402
50.807
28.845
1.00
37.15
O


ATOM
175
N
THR
A
23
95.575
47.318
31.706
1.00
40.20
N


ATOM
176
CA
THR
A
23
96.429
46.235
32.183
1.00
42.51
C


ATOM
177
C
THR
A
23
96.838
45.318
31.036
1.00
43.43
C


ATOM
178
O
THR
A
23
96.204
45.321
29.980
1.00
44.38
O


ATOM
179
CB
THR
A
23
95.711
45.414
33.258
1.00
42.79
C


ATOM
180
OG1
THR
A
23
94.456
44.957
32.744
1.00
45.13
O


ATOM
181
CG2
THR
A
23
95.461
46.263
34.492
1.00
43.22
C


ATOM
182
N
VAL
A
24
97.897
44.535
31.241
1.00
43.96
N


ATOM
183
CA
VAL
A
24
98.383
43.632
30.198
1.00
45.09
C


ATOM
184
C
VAL
A
24
97.369
42.587
29.737
1.00
45.87.
C


ATOM
185
O
VAL
A
24
97.391
42.175
28.576
1.00
45.20
O


ATOM
186
CB
VAL
A
24
99.678
42.894
30.632
1.00
45.95
C


ATOM
187
CG1
VAL
A
24
100.823
43.893
30.783
1.00
45.49
C


ATOM
188
CG2
VAL
A
24
99.442
42.134
31.933
1.00
45.36
C


ATOM
189
N
ASP
A
25
96.479
42.159
30.628
1.00
47.13
N


ATOM
190
CA
ASP
A
25
95.489
41.159
30.244
1.00
50.41
C


ATOM
191
C
ASP
A
25
94.326
41.710
29.421
1.00
50.20
C


ATOM
192
O
ASP
A
25
93.519
40.940
28.909
1.00
50.81
O


ATOM
193
CB
ASP
A
25
94.936
40.430
31.479
1.00
52.89
C


ATOM
194
CG
ASP
A
25
94.232
41.361
32.446
1.00
56.19
C


ATOM
195
OD1
ASP
A
25
93.566
40.864
33.381
1.00
58.03
O


ATOM
196
OD2
ASP
A
25
94.345
42.590
32.281
1.00
59.03
O


ATOM
197
N
CYS
A
26
94.234
43.030
29.270
1.00
49.99
N


ATOM
198
CA
CYS
A
26
93.124
43.581
28.497
1.00
48.97
C


ATOM
199
C
CYS
A
26
93.408
43.743
27.018
1.00
49.15
C


ATOM
200
O
CYS
A
26
93.939
44.764
26.581
1.00
48.97
O


ATOM
201
CB
CYS
A
26
92.660
44.937
29.047
1.00
47.43
C


ATOM
202
SG
CYS
A
26
90.937
45.377
28.585
1.00
43.74
S


ATOM
203
N
ILE
A
27
93.054
42.722
26.250
1.00
49.92
N


ATOM
204
CA
ILE
A
27
93.204
42.774
24.810
1.00
50.73
C


ATOM
205
C
ILE
A
27
91.781
42.593
24.300
1.00
50.66
C


ATOM
206
O
ILE
A
27
90.960
41.941
24.953
1.00
50.24
O


ATOM
207
CB
ILE
A
27
94.111
41.644
24.271
1.00
52.78
C


ATOM
208
CG1
ILE
A
27
93.547
40.280
24.661
1.00
53.35
C


ATOM
209
CG2
ILE
A
27
95.530
41.814
24.810
1.00
52.47
C


ATOM
210
CD1
ILE
A
27
94.339
39.120
24.094
1.00
56.96
C


ATOM
211
N
PRO
A
28
91.460
43.188
23.145
1.00
50.63
N


ATOM
212
CA
PRO
A
28
90.126
43.096
22.548
1.00
50.44
C


ATOM
213
C
PRO
A
28
89.496
41.705
22.535
1.00
50.71
C


ATOM
214
O
PRO
A
28
88.329
41.545
22.895
1.00
50.80
O


ATOM
215
CB
PRO
A
28
90.349
43.653
21.148
1.00
50.84
C


ATOM
216
CG
PRO
A
28
91.336
44.746
21.407
1.00
50.51
C


ATOM
217
CD
PRO
A
28
92.325
44.085
22.356
1.00
50.67
C


ATOM
218
N
SER
A
29
90.265
40.700
22.131
1.00
50.62
N


ATOM
219
CA
SER
A
29
89.745
39.340
22.060
1.00
49.43
C


ATOM
220
C
SER
A
29
89.327
38.758
23.409
1.00
48.35
C


ATOM
221
O
SER
A
29
88.575
37.786
23.456
1.00
49.06
O


ATOM
222
CB
SER
A
29
90.767
38.416
21.383
1.00
51.07
C


ATOM
223
OG
SER
A
29
91.969
38.322
22.126
1.00
53.31
O


ATOM
224
N
ASN
A
30
89.801
39.335
24.508
1.00
45.87
N


ATOM
225
CA
ASN
A
30
89.414
38.824
25.819
1.00
44.49
C


ATOM
226
C
ASN
A
30
88.238
39.593
26.433
1.00
42.49
C


ATOM
227
O
ASN
A
30
87.765
39.248
27.518
1.00
42.16
O


ATOM
228
CB
ASN
A
30
90.594
38.854
26.793
1.00
46.85
C


ATOM
229
CG
ASN
A
30
91.698
37.892
26.404
1.00
50.18
C


ATOM
230
OD1
ASN
A
30
91.443
36.831
25.828
1.00
52.17
O


ATOM
231
ND2
ASN
A
30
92.936
38.250
26.734
1.00
51.10
N


ATOM
232
N
VAL
A
31
87.768
40.632
25.746
1.00
38.75
N


ATOM
233
CA
VAL
A
31
86.651
41.422
26.258
1.00
36.68
C


ATOM
234
C
VAL
A
31
85.333
40.660
26.097
1.00
35.73
C


ATOM
235
O
VAL
A
31
85.033
40.127
25.034
1.00
33.64
O


ATOM
236
CB
VAL
A
31
86.558
42.802
25.538
1.00
36.09
C


ATOM
237
CG1
VAL
A
31
85.357
43.593
26.053
1.00
34.31
C


ATOM
238
CG2
VAL
A
31
87.839
43.598
25.782
1.00
35.58
C


ATOM
239
N
ASN
A
32
84.564
40.589
27.174
1.00
35.18
N


ATOM
240
CA
ASN
A
32
83.284
39.894
27.152
1.00
35.95
C


ATOM
241
C
ASN
A
32
82.173
40.938
27.055
1.00
35.44
C


ATOM
242
O
ASN
A
32
82.050
41.802
27.918
1.00
36.50
O


ATOM
243
CB
ASN
A
32
83.150
39.041
28.423
1.00
36.77
C


ATOM
244
CG
ASN
A
32
81.740
38.509
28.644
1.00
38.35
C


ATOM
245
OD1
ASN
A
32
80.908
38.499
27.739
1.00
37.24
O


ATOM
246
ND2
ASN
A
32
81.475
38.050
29.863
1.00
40.73
N


ATOM
247
N
LEU
A
33
81.373
40.863
25.995
1.00
34.92
N


ATOM
248
CA
LEU
A
33
80.291
41.822
25.799
1.00
34.68
C


ATOM
249
C
LEU
A
33
78.908
41.292
26.161
1.00
34.77
C


ATOM
250
O
LEU
A
33
77.900
41.799
25.663
1.00
35.47
O


ATOM
251
CB
LEU
A
33
80.282
42.329
24.348
1.00
34.75
C


ATOM
252
CG
LEU
A
33
81.474
43.173
23.894
1.00
35.98
C


ATOM
253
CD1
LEU
A
33
81.283
43.601
22.451
1.00
35.27
C


ATOM
254
CD2
LEU
A
33
81.621
44.392
24.799
1.00
35.37
C


ATOM
255
N
SER
A
34
78.851
40.275
27.016
1.00
33.98
N


ATOM
256
CA
SER
A
34
77.566
39.724
27.449
1.00
34.88
C


ATOM
257
C
SER
A
34
76.841
40.762
28.301
1.00
34.25
C


ATOM
258
O
SER
A
34
77.472
41.554
28.998
1.00
33.82
O


ATOM
259
CB
SER
A
34
77.770
38.456
28.284
1.00
35.12
C


ATOM
260
OG
SER
A
34
78.323
37.420
27.491
1.00
42.00
O


ATOM
261
N
THR
A
35
75.516
40.748
28.263
1.00
32.80
N


ATOM
262
CA
THR
A
35
74.754
41.708
29.034
1.00
31.26
C


ATOM
263
C
THR
A
35
73.342
41.170
29.282
1.00
31.11
C


ATOM
264
O
THR
A
35
72.798
40.424
28.466
1.00
31.76
O


ATOM
265
CB
THR
A
35
74.706
43.068
28.280
1.00
31.41
C


ATOM
266
OG1
THR
A
35
74.416
44.123
29.202
1.00
30.49
O


ATOM
267
CG2
THR
A
35
73.644
43.043
27.184
1.00
30.33
C


ATOM
268
N
PRO
A
36
72.736
41.530
30.422
1.00
29.74
N


ATOM
269
CA
PRO
A
36
71.385
41.070
30.758
1.00
30.21
C


ATOM
270
C
PRO
A
36
70.264
41.741
29.958
1.00
31.22
C


ATOM
271
O
PRO
A
36
70.291
42.953
29.713
1.00
31.11
O


ATOM
272
CB
PRO
A
36
71.284
41.366
32.253
1.00
30.05
C


ATOM
273
CG
PRO
A
36
72.114
42.613
32.397
1.00
27.96
C


ATOM
274
CD
PRO
A
36
73.322
42.310
31.529
1.00
28.83
C


ATOM
275
N
LEU
A
37
69.276
40.943
29.566
1.00
30.99
N


ATOM
276
CA
LEU
A
37
68.142
41.438
28.805
1.00
31.62
C


ATOM
277
C
LEU
A
37
66.910
41.656
29.683
1.00
32.81
C


ATOM
278
O
LEU
A
37
66.165
42.618
29.485
1.00
34.25
O


ATOM
279
CB
LEU
A
37
67.788
40.459
27.681
1.00
31.89
C


ATOM
280
CG
LEU
A
37
66.642
40.913
26.764
1.00
32.36
C


ATOM
281
CD1
LEU
A
37
67.124
42.073
25.888
1.00
31.95
C


ATOM
282
CD2
LEU
A
37
66.175
39.757
25.892
1.00
31.83
C


ATOM
283
N
VAL
A
38
66.691
40.774
30.655
1.00
32.12
N


ATOM
284
CA
VAL
A
38
65.521
40.901
31.517
1.00
31.54
C


ATOM
285
C
VAL
A
38
65.869
40.922
33.004
1.00
32.49
C


ATOM
286
O
VAL
A
38
66.867
40.344
33.427
1.00
33.79
O


ATOM
287
CE
VAL
A
38
64.486
39.772
31.219
1.00
31.66
C


ATOM
288
CG1
VAL
A
38
64.026
39.872
29.765
1.00
28.94
C


ATOM
289
CG2
VAL
A
38
65.093
38.398
31.482
1.00
29.49
C


ATOM
290
N
LYE
A
39
65.025
41.584
33.789
1.00
31.86
N


ATOM
291
CA
LYS
A
39
65.246
41.742
35.219
1.00
33.55
C


ATOM
292
C
LYE
A
39
65.423
40.464
36.025
1.00
34.23
C


ATOM
293
O
LYE
A
39
64.893
39.415
35.678
1.00
34.30
O


ATOM
294
CB
LYS
A
39
64.112
42.560
35.842
1.00
34.12
C


ATOM
295
CG
LYS
A
39
62.743
41.886
35.791
1.00
34.26
C


ATOM
296
CD
LYS
A
39
61.727
42.681
36.588
1.00
34.93
C


ATOM
297
CE
LYS
A
39
60.368
41.981
36.614
1.00
35.16
C


ATOM
298
NZ
LYS
A
39
59.412
42.684
37.515
1.00
34.58
N


ATOM
299
N
PHE
A
40
66.175
40.592
37.114
1.00
34.89
N


ATOM
300
CA
PHE
A
40
66.454
39.499
38.032
1.00
36.02
C


ATOM
301
C
PHE
A
40
66.698
40.089
39.416
1.00
37.46
C


ATOM
302
O
PHE
A
40
66.849
41.303
39.562
1.00
38.06
O


ATOM
303
CB
PHE
A
40
67.687
38.699
37.582
1.00
34.23
C


ATOM
304
CG
PHE
A
40
68.926
39.535
37.376
1.00
33.77
C


ATOM
305
CD1
PHE
A
40
69.178
40.142
36.145
1.00
32.47
C


ATOM
306
CD2
PHE
A
40
69.844
39.704
38.405
1.00
31.36
C


ATOM
307
CE1
PHE
A
40
70.326
40.899
35.945
1.00
31.93
C


ATOM
308
CE2
PHE
A
40
70.998
40.460
38.218
1.00
31.43
C


ATOM
309
CZ
PHE
A
40
71.241
41.060
36.984
1.00
31.40
C


ATOM
310
N
GLN
A
41
66.728
39.227
40.427
1.00
38.80
N


ATOM
311
CA
GLN
A
41
66.954
39.653
41.800
1.00
40.40
C


ATOM
312
C
GLN
A
41
68.439
39.656
42.110
1.00
39.88
C


ATOM
313
O
GLN
A
41
69.238
39.044
41.402
1.00
39.75
O


ATOM
314
CB
GLN
A
41
66.256
38.705
42.790
1.00
44.12
C


ATOM
315
CG
GLN
A
41
64.735
38.752
42.795
1.00
49.04
C


ATOM
316
CD
GLN
A
41
64.188
40.059
43.352
1.00
51.98
C


ATOM
317
OE1
GLN
A
41
64.464
40.433
44.501
1.00
54.77
O


ATOM
318
NE2
GLN
A
41
63.406
40.761
42.541
1.00
52.25
N


ATOM
319
N
LYS
A
42
68.798
40.353
43.179
1.00
39.91
N


ATOM
320
CA
LYS
A
42
70.178
40.423
43.627
1.00
41.35
C


ATOM
321
C
LYS
A
42
70.701
38.997
43.872
1.00
41.68
C


ATOM
322
O
LYE
A
42
69.993
38.157
44.428
1.00
40.20
O


ATOM
323
CE
LYS
A
42
70.236
41.226
44.921
1.00
42.49
C


ATOM
324
CG
LYS
A
42
71.606
41.323
45.551
1.00
45.67
C


ATOM
325
CD
LYE
A
42
71.501
42.014
46.902
1.00
47.42
C


ATOM
326
CE
LYS
A
42
72.844
42.067
47.605
1.00
48.87
C


ATOM
327
NZ
LYS
A
42
72.721
42.779
48.906
1.00
52.09
N


ATOM
328
N
GLY
A
43
71.929
38.728
43.442
1.00
41.55
N


ATOM
329
CA
GLY
A
43
72.511
37.412
43.644
1.00
40.73
C


ATOM
330
C
GLY
A
43
72.226
36.425
42.532
1.00
40.52
C


ATOM
331
O
GLY
A
43
72.807
35.341
42.496
1.00
40.95
O


ATOM
332
N
GLN
A
44
71.330
36.788
41.625
1.00
40.46
N


ATOM
333
CA
GLN
A
44
70.992
35.912
40.511
1.00
41.27
C


ATOM
334
C
GLN
A
44
71.591
36.440
39.211
1.00
41.60
C


ATOM
335
O
GLN
A
44
72.292
37.450
39.196
1.00
40.78
O


ATOM
336
CE
GLN
A
44
69.471
35.822
40.342
1.00
42.42
C


ATOM
337
CG
GLN
A
44
68.688
35.691
41.637
1.00
45.60
C


ATOM
338
CD
GLN
A
44
67.186
35.582
41.402
1.00
47.33
C


ATOM
339
OE1
GLN
A
44
66.621
36.293
40.565
1.00
48.58
O


ATOM
340
NE2
GLN
A
44
66.533
34.703
42.149
1.00
46.68
N


ATOM
341
N
GLN
A
45
71.308
35.726
38.127
1.00
42.62
N


ATOM
342
CA
GLN
A
45
71.741
36.089
36.784
1.00
43.67
C


ATOM
343
C
GLN
A
45
70.443
36.216
35.999
1.00
41.83
C


ATOM
344
O
GLN
A
45
69.439
35.611
36.367
1.00
40.98
O


ATOM
345
CB
GLN
A
45
72.593
34.981
36.153
1.00
46.80
C


ATOM
346
CG
GLN
A
45
73.929
34.741
36.833
1.00
52.13
C


ATOM
347
CD
GLN
A
45
74.909
35.872
36.601
1.00
54.67
C


ATOM
348
OE1
GLN
A
45
75.420
36.047
35.489
1.00
57.71
O


ATOM
349
NE2
GLN
A
45
75.175
36.653
37.647
1.00
54.39
N


ATOM
350
N
SER
A
46
70.458
36.999
34.928
1.00
39.93
N


ATOM
351
CA
SER
A
46
69.268
37.162
34.110
1.00
38.73
C


ATOM
352
C
SER
A
46
69.005
35.868
33.347
1.00
39.01
C


ATOM
353
O
SER
A
46
69.942
35.211
32.906
1.00
39.13
O


ATOM
354
CB
SER
A
46
69.464
38.304
33.113
1.00
36.60
C


ATOM
355
OG
SER
A
46
68.330
38.437
32.280
1.00
35.88
O


ATOM
356
N
GLU
A
47
67.733
35.511
33.190
1.00
39.22
N


ATOM
357
CA
GLU
A
47
67.363
34.297
32.463
1.00
39.59
C


ATOM
358
C
GLU
A
47
67.762
34.400
31.000
1.O0
38.86
C


ATOM
359
O
GLU
A
47
67.904
33.385
30.316
1.00
38.01
O


ATOM
360
CB
GLU
A
47
65.857
34.057
32.563
1.00
41.44
C


ATOM
361
CG
GLU
A
47
65.365
33.806
33.978
1.00
44.53
C


ATOM
362
CD
GLU
A
47
63.853
33.843
34.073
1.00
47.63
C


ATOM
363
OE1
GLU
A
47
63.197
32.987
33.436
1.00
49.95
O


ATOM
364
OE2
GLU
A
47
63.321
34.732
34.777
1.00
49.50
O


ATOM
365
N
ILE
A
48
67.920
35.631
30.514
1.00
37.02
N


ATOM
366
CA
ILE
A
48
68.318
35.856
29.126
1.00
35.30
C


ATOM
367
C
ILE
A
48
69.474
36.854
29.055
1.00
34.82
C


ATOM
368
O
ILE
A
48
69.372
37.982
29.538
1.00
34.21
O


ATOM
369
CB
ILE
A
48
67.144
36.400
28.273
1.00
35.95
C


ATOM
370
CG1
ILE
A
48
65.958
35.434
28.328
1.00
37.12
C


ATOM
371
CG2
ILE
A
48
67.595
36.583
26.836
1.00
34.56
C


ATOM
372
CD1
ILE
A
48
64.768
35.879
27.509
1.00
37.86
C


ATOM
373
N
ASN
A
49
70.579
36.426
28.462
1.00
34.10
N


ATOM
374
CA
ASN
A
49
71.739
37.285
28.323
1.00
34.92
C


ATOM
375
C
ASN
A
49
72.160
37.365
26.866
1.00
35.76
C


ATOM
376
O
ASN
A
49
72.383
36.341
26.218
1.00
36.32
O


ATOM
377
CB
ASN
A
49
72.903
36.752
29.169
1.00
35.35
C


ATOM
378
CG
ASN
A
49
72.634
36.856
30.660
1.00
37.43
C


ATOM
379
OD1
ASN
A
49
72.802
37.917
31.263
1.00
34.90
O


ATOM
380
ND2
ASN
A
49
72.193
35.755
31.258
1.00
36.59
N


ATOM
381
N
LEU
A
50
72.242
38.582
26.342
1.00
34.27
N


ATOM
382
CA
LEU
A
50
72.682
38.770
24.965
1.00
33.47
C


ATOM
383
C
LEU
A
50
74.184
38.504
24.991
1.00
33.03
C


ATOM
384
O
LEU
A
50
74.809
38.633
26.040
1.00
31.70
O


ATOM
385
CE
LEU
A
50
72.444
40.213
24.522
1.00
33.25
C


ATOM
386
CG
LEU
A
50
71.041
40.784
24.715
1.00
33.75
C


ATOM
387
CD1
LEU
A
50
71.050
42.270
24.362
1.00
33.97
C


ATOM
388
CD2
LEU
A
50
70.054
40.019
23.846
1.00
35.15
C


ATOM
389
N
LYS
A
51
74.766
38.132
23.855
1.00
33.34
N


ATOM
390
CA
LYS
A
51
76.208
37.902
23.815
1.00
33.66
C


ATOM
391
C
LYS
A
51
76.902
39.177
23.335
1.00
32.95
C


ATOM
392
O
LYS
A
51
78.109
39.359
23.532
1.00
32.77
O


ATOM
393
CE
LYS
A
51
76.531
36.680
22.946
1.00
34.82
C


ATOM
394
CG
LYS
A
51
75.984
35.408
23.593
1.00
37.49
C


ATOM
395
CD
LYE
A
51
76.413
34.136
22.897
1.00
39.84
C


ATOM
396
CE
LYS
A
51
75.893
32.920
23.663
1.00
40.88
C


ATOM
397
NZ
LYE
A
51
76.295
31.643
22.997
1.00
43.33
N


ATOM
398
N
ILE
A
52
76.119
40.054
22.708
1.00
31.66
N


ATOM
399
CA
ILE
A
52
76.585
41.370
22.274
1.00
31.00
C


ATOM
400
C
ILE
A
52
75.425
42.297
22.651
1.00
31.49
C


ATOM
401
O
ILE
A
52
74.257
41.937
22.498
1.00
31.89
O


ATOM
402
CB
ILE
A
52
76.912
41.454
20.750
1.00
31.40
C


ATOM
403
CG1
ILE
A
52
75.685
41.121
19.892
1.00
31.59
C


ATOM
404
CG2
ILE
A
52
78.089
40.538
20.432
1.00
31.15
C


ATOM
405
CD1
ILE
A
52
75.900
41.415
18.400
1.00
29.50
C


ATOM
406
N
PRO
A
53
75.733
43.499
23.1.54
1.00
31.49
N


ATOM
407
CA
PRO
A
53
74.731
44.482
23.579
1.00
31.87
C


ATOM
408
C
PRO
A
53
73.958
45.252
22.506
1.00
32.48
C


ATOM
409
O
PRO
A
53
73.645
46.428
22.698
1.00
33.45
O


ATOM
410
CB
PRO
A
53
75.544
45.412
24.468
1.00
31.07
C


ATOM
411
CG
PRO
A
53
76.853
45.479
23.713
1.00
31.12
C


ATOM
412
CD
PRO
A
53
77.101
44.034
23.325
1.00
30.40
C


ATOM
413
N
LEU
A
54
73.630
44.602
21.395
1.00
31.62
N


ATOM
414
CA
LEU
A
54
72.901
45.279
20.331
1.00
30.89
C


ATOM
415
C
LEU
A
54
71.582
44.592
19.986
1.00
31.85
C


ATOM
416
O
LEU
A
54
71.524
43.365
19.872
1.00
32.82
O


ATOM
417
CB
LEU
A
54
73.767
45.347
19.069
1.00
29.66
C


ATOM
418
CG
LEU
A
54
75.192
45.900
19.182
1.00
30.68
C


ATOM
419
CD1
LEU
A
54
75.876
45.810
17.824
1.00
29.65
C


ATOM
420
CD2
LEU
A
54
75.162
47.347
19.678
1.00
30.19
C


ATOM
421
N
VAL
A
55
70.519
45.377
19.840
1.00
31.15
N


ATOM
422
CA
VAL
A
55
69.230
44.830
19.441
1.00
30.86
C


ATOM
423
C
VAL
A
55
68.692
45.737
18.333
1.00
32.57
C


ATOM
424
O
VAL
A
55
68.876
46.956
18.385
1.00
33.70
O


ATOM
425
CB
VAL
A
55
68.214
44.757
20.618
1.00
29.59
C


ATOM
426
CG1
VAL
A
55
68.833
44.009
21.786
1.00
28.25
C


ATOM
427
CG2
VAL
A
55
67.750
46.146
21.025
1.00
29.12
C


ATOM
428
N
SER
A
56
68.058
45.144
17.322
1.00
32.00
N


ATOM
429
CA
SER
A
56
67.511
45.914
16.207
1.00
31.93
C


ATOM
430
C
SER
A
56
66.134
46.469
16.556
1.00
31.63
C


ATOM
431
O
SER
A
56
65.324
45.812
17.214
1.00
31.90
O


ATOM
432
CB
SER
A
56
67.459
45.056
14.929
1.00
31.63
C


ATOM
433
OG
SER
A
56
66.668
43.895
15.102
1.00
31.84
O


ATOM
434
N
ALA
A
57
65.891
47.697
16.115
1.00
31.38
N


ATOM
435
CA
ALA
A
57
64.654
48.419
16.395
1.00
31.55
C


ATOM
436
C
ALA
A
57
63.361
47.756
15.907
1.00
32.70
C


ATOM
437
O
ALA
A
57
63.351
47.012
14.922
1.00
33.02
O


ATOM
438
CB
ALA
A
57
64.764
49.833
15.836
1.00
29.58
C


ATOM
439
N
ILE
A
58
62.277
48.047
16.620
1.00
32.44
N


ATOM
440
CA
ILE
A
58
60.950
47.511
16.328
1.00
33.86
C


ATOM
441
C
ILE
A
58
60.380
48.325
15.173
1.00
34.14
C


ATOM
442
O
ILE
A
58
59.463
49.129
15.359
1.00
34.72
O


ATOM
443
CB
ILE
A
58
60.032
47.654
17.578
1.00
32.65
C


ATOM
444
CG1
ILE
A
58
60.827
47.277
18.835
1.00
33.43
C


ATOM
445
CG2
ILE
A
58
58.800
46.759
17.444
1.00
30.11
C


ATOM
446
CD1
ILE
A
58
60.068
47.428
20.135
1.00
31.89
C


ATOM
447
N
MET
A
59
60.931
48.111
13.982
1.00
34.79
N


ATOM
448
CA
MET
A
59
60.523
48.870
12.803
1.00
35.21
C


ATOM
449
C
MET
A
59
60.363
48.024
11.545
1.00
36.00
C


ATOM
450
O
MET
A
59
61.151
47.107
11.287
1.00
34.61
O


ATOM
451
CB
MET
A
59
61.554
49.971
12.525
1.00
35.03
C


ATOM
452
CG
MET
A
59
61.851
50.887
13.706
1.00
34.37
C


ATOM
453
SD
MET
A
59
63.181
52.051
13.323
1.00
35.17
S


ATOM
454
CE
MET
A
59
62.401
53.057
12.081
1.00
35.07
C


ATOM
455
N
GLN
A
60
59.353
48.366
10.748
1.00
37.49
N


ATOM
456
CA
GLN
A
60
59.063
47.649
9.509
1.00
39.05
C


ATOM
457
C
GLN
A
60
60.275
47.600
8.594
1.00
38.95
C


ATOM
458
O
GLN
A
60
60.506
46.603
7.915
1.00
39.70
O


ATOM
459
CB
GLN
A
60
57.927
48.329
8.738
1.00
39.93
C


ATOM
460
CG
GLN
A
60
56.671
48.629
9.532
1.00
41.07
C


ATOM
461
CD
GLN
A
60
55.609
49.290
8.665
1.00
42.66
C


ATOM
462
OE1
GLN
A
60
55.930
50.010
7.717
1.00
42.94
O


ATOM
463
NE2
GLN
A
60
54.342
49.058
8.992
1.00
42.62
N


ATOM
464
N
SER
A
61
61.046
48.683
8.578
1.00
39.09
N


ATOM
465
CA
SER
A
61
62.215
48.770
7.705
1.00
38.98
C


ATOM
466
C
SER
A
61
63.506
48.217
8.296
1.00
38.63
C


ATOM
467
O
SER
A
61
64.577
48.352
7.694
1.00
38.93
O


ATOM
468
CB
SER
A
61
62.436
50.228
7.280
1.00
39.27
C


ATOM
469
OG
SER
A
61
62.568
51.078
8.409
1.00
42.11
O


ATOM
470
N
VAL
A
62
63.407
47.578
9.457
1.00
37.45
N


ATOM
471
CA
VAL
A
62
64.593
47.048
10.112
1.00
36.30
C


ATOM
472
C
VAL
A
62
64.535
45.590
10.53.6
1.00
37.04
C


ATOM
473
O
VAL
A
62
65.304
44.765
10.050
1.00
38.38
O


ATOM
474
CB
VAL
A
62
64.939
47.869
11.382
1.00
36.10
C


ATOM
475
CG1
VAL
A
62
66.168
47.274
12.069
1.00
34.59
C


ATOM
476
CG2
VAL
A
62
65.175
49.330
11.016
1.00
35.17
C


ATOM
477
N
SER
A
63
63.621
45.275
11.444
1.00
37.88
N


ATOM
478
CA
SER
A
63
63.540
43.929
11.982
1.00
38.55
C


ATOM
479
C
SER
A
63
62.557
42.938
11.368
1.00
39.50
C


ATOM
480
O
SER
A
63
61.454
42.727
11.879
1.00
37.63
O


ATOM
481
CB
SER
A
63
63.319
44.013
13.495
1.00
38.61
C


ATOM
482
OG
SER
A
63
64.401
44.694
14.120
1.00
36.71
O


ATOM
483
N
GLY
A
64
62.991
42.329
10.268
1.00
39.83
N


ATOM
484
CA
GLY
A
64
62.201
41.317
9.597
1.00
41.35
C


ATOM
485
C
GLY
A
64
62.814
39.992
10.023
1.00
43.17
C


ATOM
486
O
GLY
A
64
63.710
39.973
10.874
1.00
39.88
O


ATOM
487
N
GLU
A
65
62.373
38.884
9.432
1.00
44.98
N


ATOM
488
CA
GLU
A
65
62.913
37.593
9.832
1.00
47.09
C


ATOM
489
C
GLU
A
65
64.384
37.401
9.484
1.00
45.97
C


ATOM
490
O
GLU
A
65
65.129
36.825
10.274
1.00
45.63
O


ATOM
491
CB
GLU
A
65
62.069
36.447
9.259
1.00
50.39
C


ATOM
492
CG
GLU
A
65
62.087
36.305
7.758
1.00
56.03
C


ATOM
493
CD
GLU
A
65
61.206
35.158
7.297
1.00
60.65
C


ATOM
494
OE1
GLU
A
65
59.968
35.256
7.478
1.00
62.24
O


ATOM
495
OE2
GLU
A
65
61.752
34.158
6.768
1.00
61.62
O


ATOM
496
N
LYS
A
66
64.814
37.885
8.322
1.00
45.39
N


ATOM
497
CA
LYS
A
66
66.216
37.740
7.941
1.00
45.57
C


ATOM
498
C
LYS
A
66
67.118
38.490
8.917
1.00
43.76
C


ATOM
499
O
LYS
A
66
68.197
38.014
9.275
1.00
43.26
O


ATOM
500
CB
LYS
A
66
66.452
38.255
6.518
1.00
48.10
C


ATOM
501
CG
LYS
A
66
66.051
37.272
5.426
1.00
53.08
C


ATOM
502
CD
LYS
A
66
66.353
37.827
4.032
1.00
56.63
C


ATOM
503
CE
LYS
A
66
65.933
36.847
2.937
1.00
58.88
C


ATOM
504
NZ
LYS
A
66
66.138
37.403
1.561
1.00
59.62
N


ATOM
505
N
MET
A
67
66.671
39.665
9.347
1.00
41.61
N


ATOM
506
CA
MET
A
67
67.440
40.468
10.290
1.00
40.17
C


ATOM
507
C
MET
A
67
67.552
39.730
11.625
1.00
39.71
C


ATOM
508
O
MET
A
67
68.638
39.619
12.199
1.00
38.59
O


ATOM
509
CB
MET
A
67
66.761
41.822
10.507
1.00
39.65
C


ATOM
510
CG
MET
A
67
67.451
42.722
11.525
1.00
38.90
C


ATOM
511
SD
MET
A
67
69.110
43.219
11.014
1.00
38.59
S


ATOM
512
CE
MET
A
67
68.730
44.370
9.680
1.00
37.11
C


ATOM
513
N
ALA
A
68
66.422
39.217
12.102
1.00
38.12
N


ATOM
514
CA
ALA
A
68
66.370
38.505
13.371
1.00
38.12
C


ATOM
515
C
ALA
A
68
67.314
37.306
13.407
1.00
38.48
C


ATOM
516
O
ALA
A
68
67.919
37.009
14.437
1.00
38.33
O


ATOM
517
CB
ALA
A
68
64.947
38.064
13.652
1.00
37.40
C


ATOM
518
N
ILE
A
69
67.435
36.622
12.275
1.00
38.50
N


ATOM
519
CA
ILE
A
69
68.308
35.461
12.163
1.00
38.32
C


ATOM
520
C
ILE
A
69
69.774
35.896
12.129
1.00
37.75
C


ATOM
521
O
ILE
A
69
70.601
35.383
12.883
1.00
38.40
O


ATOM
522
CB
ILE
A
69
67.981
34.656
10.874
1.00
40.02
C


ATOM
523
CG1
ILE
A
69
66.603
33.998
11.006
1.00
40.60
C


ATOM
524
CG2
ILE
A
69
69.042
33.599
10.625
1.00
38.98
C


ATOM
525
CD1
ILE
A
69
66.013
33.545
9.678
1.00
41.31
C


ATOM
526
N
ALA
A
70
70.084
36.847
11.254
1.00
37.08
N


ATOM
527
CA
ALA
A
70
71.442
37.348
11.109
1.00
36.18
C


ATOM
528
C
ALA
A
70
72.000
37.959
12.392
1.00
36.22
C


ATOM
529
O
ALA
A
70
73.182
37.796
12.695
1.00
36.51
O


ATOM
530
CB
ALA
A
70
71.499
38.366
9.987
1.00
36.62
C


ATOM
531
N
LEU
A
71
71.155
38.661
13.142
1.00
35.64
N


ATOM
532
CA
LEU
A
71
71.593
39.293
14.381
1.00
35.41
C


ATOM
533
C
LEU
A
71
71.752
38.281
15.511
1.00
35.81
C


ATOM
534
O
LEU
A
71
72.707
38.353
16.282
1.00
34.47
O


ATOM
535
CB
LEU
A
71
70.617
40.400
14.792
1.00
33.24
C


ATOM
536
CG
LEU
A
71
70.921
41.215
16.061
1.00
33.66
C


ATOM
537
CD1
LEU
A
71
72.391
41.629
16.110
1.00
31.27
C


ATOM
538
CD2
LEU
A
71
70.021
42.451
16.083
1.00
31.14
C


ATOM
539
N
ALA
A
72
70.822
37.337
15.608
1.00
37.05
N


ATOM
540
CA
ALA
A
72
70.906
36.317
16.648
1.00
38.69
C


ATOM
541
C
ALA
A
72
72.166
35.476
16.445
1.00
40.01
C


ATOM
542
O
ALA
A
72
72.756
34.988
17.411
1.00
39.86
O


ATOM
543
CB
ALA
A
72
69.665
35.422
16.620
1.00
37.80
C


ATOM
544
N
ARG
A
73
72.570
35.304
15.188
1.00
40.95
N


ATOM
545
CA
ARG
A
73
73.761
34.525
14.874
1.00
43.10
C


ATOM
546
C
ARG
A
73
75.004
35.169
15.464
1.00
43.29
C


ATOM
547
O
ARG
A
73
75.963
34.477
15.807
1.00
42.95
O


ATOM
548
CB
ARG
A
73
73.940
34.384
13.359
1.00
45.58
C


ATOM
549
CG
ARG
A
73
73.014
33.367
12.707
1.00
49.18
C


ATOM
550
CD
ARG
A
73
73.285
33.246
11.210
1.00
52.08
C


ATOM
551
NE
ARG
A
73
72.430
32.238
10.591
1.00
55.80
N


ATOM
552
CZ
ARG
A
73
72.264
32.093
9.278
1.00
58.09
C


ATOM
553
NH1
ARG
A
73
72.897
32.895
8.427
1.00
58.20
N


ATOM
554
NH2
ARG
A
73
71.460
31.144
8.813
1.00
58.98
N


ATOM
555
N
GLU
A
74
74.976
36.495
15.585
1.00
42.49
N


ATOM
556
CA
GLU
A
74
76.103
37.239
16.129
1.00
41.53
C


ATOM
557
C
GLU
A
74
75.987
37.478
17.631
1.00
39.63
C


ATOM
558
O
GLU
A
74
76.896
38.031
18.242
1.00
40.05
O


ATOM
559
CB
GLU
A
74
76.255
38.577
15.401
1.00
42.87
C


ATOM
560
CG
GLU
A
74
76.467
38.458
13.892
1.00
45.91
C


ATOM
561
CD
GLU
A
74
77.673
37.595
13.522
1.00
49.55
C


ATOM
562
OE1
GLU
A
74
78.768
37.813
14.094
1.00
50.07
O


ATOM
563
OE2
GLU
A
74
77.524
36.704
12.653
1.00
50.61
O


ATOM
564
N
GLY
A
75
74.869
37.074
18.229
1.00
38.37
N


ATOM
565
CA
GLY
A
75
74.716
37.250
19.664
1.00
38.10
C


ATOM
566
C
GLY
A
75
73.715
38.287
20.132
1.00
38.30
C


ATOM
567
O
GLY
A
75
73.517
38.458
21.337
1.00
39.24
O


ATOM
568
N
GLY
A
76
73.092
38.987
19.192
1.00
37.09
N


ATOM
569
CA
GLY
A
76
72.107
39.990
19.549
1.00
36.51
C


ATOM
570
C
GLY
A
76
70.708
39.449
19.312
1.00
36.82
C


ATOM
571
O
GLY
A
76
70.546
38.266
18.989
1.00
36.23
O


ATOM
572
N
ILE
A
77
69.698
40.298
19.477
1.00
35.24
N


ATOM
573
CA
ILE
A
77
68.316
39.875
19.259
1.00
34.74
C


ATOM
574
C
ILE
A
77
67.536
40.962
18.518
1.00
35.14
C


ATOM
575
O
ILE
A
77
67.837
42.159
18.634
1.00
34.83
O


ATOM
576
CB
ILE
A
77
67.609
39.552
20.602
1.00
33.95
C


ATOM
577
CG1
ILE
A
77
66.389
38.655
20.350
1.00
34.82
C


ATOM
578
CG2
ILE
A
77
67.179
40.850
21.305
1.00
33.35
C


ATOM
579
CD1
ILE
A
77
65.636
38.255
21.619
1.00
31.17
C


ATOM
580
N
SER
A
78
66.543
40.539
17.744
1.00
34.83
N


ATOM
581
CA
SER
A
78
65.711
41.467
16.993
1.00
33.97
C


ATOM
582
C
SER
A
78
64.300
41.484
17.547
1.00
34.42
C


ATOM
583
O
SER
A
78
63.817
40.484
18.074
1.00
35.04
0


ATOM
584
CB
SER
A
78
65.645
41.068
15.513
1.00
32.74
C


ATOM
585
OG
SER
A
78
66.870
41.295
14.848
1.00
30.88
O


ATOM
586
N
PHE
A
79
63.641
42.629
17.439
1.00
34.58
N


ATOM
587
CA
PHE
A
79
62.270
42.740
17.891
1.00
35.16
C


ATOM
588
C
PHE
A
79
61.405
42.906
16.646
1.00
35.89
C


ATOM
589
O
PHE
A
79
61.253
44.011
16.126
1.00
36.16
O


ATOM
590
CB
PHE
A
79
62.094
43.929
18.846
1.00
33.75
C


ATOM
591
CG
PHE
A
79
62.664
43.688
20.219
1.00
34.30
C


ATOM
592
CD1
PHE
A
79
64.016
43.911
20.481
1.00
35.61
C


ATOM
593
CD2
PHE
A
79
61.862
43.182
21.238
1.00
33.96
C


ATOM
594
CE1
PHE
A
79
64.559
43.626
21.745
1.00
35.47
C


ATOM
595
CE2
PHE
A
79
62.395
42.893
22.503
1.00
33.04
C


ATOM
596
CZ
PHE
A
79
63.741
43.115
22.755
1.00
33.81
C


ATOM
597
N
ILE
A
80
60.869
41.790
16.158
1.00
35.40
N


ATOM
598
CA
ILE
A
80
60.011
41.791
14.977
1.00
35.16
C


ATOM
599
C
ILE
A
80
58.951
42.878
15.136
1.00
35.68
C


ATOM
600
O
ILE
A
80
58.241
42.916
16.149
1.00
35.60
O


ATOM
601
CB
ILE
A
80
59.317
40.417
14.802
1.00
35.87
C


ATOM
602
CG1
ILE
A
80
60.373
39.319
14.621
1.00
35.71
C


ATOM
603
CG2
ILE
A
80
58.381
40.446
13.592
1.00
35.14
C


ATOM
604
CD1
ILE
A
80
61.235
39.494
13.386
1.00
34.65
C


ATOM
605
N
PHE
A
81
58.838
43.754
14.140
1.00
35.48
N


ATOM
606
CA
PHE
A
81
57.879
44.848
14.221
1.00
37.39
C


ATOM
607
C
PHE
A
81
56.427
44.423
14.437
1.00
37.98
C


ATOM
608
O
PHE
A
81
55.953
43.440
13.863
1.00
38.21
O


ATOM
609
CB
PHE
A
81
57.989
45.773
12.990
1.00
38.37
C


ATOM
610
CG
PHE
A
81
57.733
45.093
11.666
1.00
39.29
C


ATOM
611
CD1
PHE
A
81
58.693
44.272
11.089
1.00
39.25
C


ATOM
612
CD2
PHE
A
81
56.543
45.315
10.978
1.00
39.78
C


ATOM
613
CE1
PHE
A
81
58.476
43.681
9.838
1.00
39.50
C


ATOM
614
CE2
PHE
A
81
56.313
44.731
9.729
1.00
40.29
C


ATOM
615
CZ
PHE
A
81
57.284
43.911
9.158
1.00
39.87
C


ATOM
616
N
GLY
A
82
55.730
45.178
15.281
1.00
38.14
N


ATOM
617
CA
GLY
A
82
54.341
44.878
15.570
1.00
39.76
C


ATOM
618
C
GLY
A
82
53.374
45.678
14.720
1.00
40.57
C


ATOM
619
O
GLY
A
82
52.158
45.550
14.869
1.00
41.33
O


ATOM
620
N
SER
A
83
53.909
46.504
13.826
1.00
40.23
N


ATOM
621
CA
SER
A
83
53.076
47.313
12.945
1.00
41.14
C


ATOM
622
C
SER
A
83
52.678
46.522
11.698
1.00
41.79
C


ATOM
623
O
SER
A
83
52.958
46.920
10.566
1.00
40.82
O


ATOM
624
CB
SER
A
83
53.816
48.590
12.549
1.00
40.01
C


ATOM
625
OG
SER
A
83
55.077
48.281
11.989
1.00
42.73
O


ATOM
626
N
GLN
A
84
52.034
45.385
11.934
1.00
42.84
N


ATOM
627
CA
GLN
A
84
51.552
44.502
10.879
1.00
43.52
C


ATOM
628
C
GLN
A
84
50.500
43.599
11.524
1.00
44.66
C


ATOM
629
O
GLN
A
84
50.323
43.632
12.742
1.00
44.23
O


ATOM
630
CB
GLN
A
84
52.699
43.665
10.310
1.00
43.55
C


ATOM
631
CG
GLN
A
84
53.361
42.741
11.318
1.00
43.62
C


ATOM
632
CD
GLN
A
84
54.467
41.917
10.694
1.00
45.55
C


ATOM
633
OE1
GLN
A
84
54.266
41.275
9.662
1.00
46.16
O


ATOM
634
NE2
GLN
A
84
55.646
41.926
11.319
1.00
44.86
N


ATOM
635
N
SER
A
85
49.807
42.798
10.720
1.00
46.26
N


ATOM
636
CA
SER
A
85
48.774
41.912
11.249
1.00
47.95
C


ATOM
637
C
SER
A
85
49.364
40.964
12.283
1.00
48.90
C


ATOM
638
O
SER
A
85
50.554
40.648
12.239
1.00
48.83
O


ATOM
639
CB
SER
A
85
48.135
41.087
10.128
1.00
47.83
C


ATOM
640
OG
SER
A
85
48.937
39.965
9.804
1.00
48.77
O


ATOM
641
N
ILE
A
86
48.520
40.517
13.209
1.00
49.03
N


ATOM
642
CA
ILE
A
86
48.934
39.593
14.256
1.00
50.14
C


ATOM
643
C
ILE
A
86
49.416
38.281
13.636
1.00
51.13
C


ATOM
644
O
ILE
A
86
50.425
37.715
14.059
1.00
50.51
O


ATOM
645
CB
ILE
A
86
47.764
39.305
15.222
1.00
49.46
C


ATOM
646
CG1
ILE
A
86
47.346
40.605
15.919
1.00
49.50
C


ATOM
647
CG2
ILE
A
86
48.162
38.236
16.227
1.00
48.57
C


ATOM
648
CD1
ILE
A
86
46.160
40.463
16.864
1.00
49.15
C


ATOM
649
N
GLU
A
87
48.689
37.811
12.626
1.00
52.14
N


ATOM
650
CA
GLU
A
87
49.028
36.573
11.930
1.00
53.33
C


ATOM
651
C
GLU
A
87
50.377
36.714
11.227
1.00
52.06
C


ATOM
652
O
GLU
A
87
51.197
35.795
11.228
1.00
51.76
O


ATOM
653
CB
GLU
A
87
47.956
36.237
10.881
1.00
55.49
C


ATOM
654
CG
GLU
A
87
46.545
35.978
11.430
1.00
59.83
C


ATOM
655
CD
GLU
A
87
45.948
37.179
12.164
1.00
62.66
C


ATOM
656
OE1
GLU
A
87
45.934
38.298
11.594
1.00
63.16
O


ATOM
657
OE2
GLU
A
87
45.484
36.998
13.314
1.00
64.49
O


ATOM
658
N
SER
A
88
50.594
37.876
10.623
1.00
51.42
N


ATOM
659
CA
SER
A
88
51.828
38.149
9.895
1.00
51.37
C


ATOM
660
C
SER
A
88
53.048
38.223
10.818
1.00
49.76
C


ATOM
661
O
SER
A
88
54.098
37.651
10.522
1.00
48.93
O


ATOM
662
CB
SER
A
88
51.683
39.459
9.116
1.00
52.05
C


ATOM
663
OG
SER
A
88
52.784
39.661
8.253
1.00
54.78
O


ATOM
664
N
GLN
A
89
52.909
38.927
11.935
1.00
48.17
N


ATOM
665
CA
GLN
A
89
54.010
39.051
12.878
1.00
47.23
C


ATOM
666
C
GLN
A
89
54.338
37.692
13.493
1.00
47.15
C


ATOM
667
O
GLN
A
89
55.507
37.333
13.636
1.00
47.13
O


ATOM
668
CB
GLN
A
89
53.663
40.060
13.980
1.00
45.26
C


ATOM
669
CG
GLN
A
89
54.718
40.149
15.081
1.00
43.42
C


ATOM
670
CD
GLN
A
89
54.405
41.207
16.127
1.00
42.17
C


ATOM
671
OE1
GLN
A
89
53.243
41.438
16.470
1.00
40.51
O


ATOM
672
NE2
GLN
A
89
55.447
41.840
16.658
1.00
40.16
N


ATOM
673
N
ALA
A
90
53.305
36.934
13.848
1.00
47.23
N


ATOM
674
CA
ALA
A
90
53.498
35.616
14.445
1.00
47.19
C


ATOM
675
C
ALA
A
90
54.224
34.678
13.486
1.00
47.12
C


ATOM
676
O
ALA
A
90
55.065
33.881
13.903
1.00
48.12
O


ATOM
677
CB
ALA
A
90
52.154
35.022
14.848
1.00
47.65
C


ATOM
678
N
ALA
A
91
53.909
34.774
12.199
1.00
46.68
N


ATOM
679
CA
ALA
A
91
54.560
33.924
11.211
1.00
47.00
C


ATOM
680
C
ALA
A
92
56.064
34.212
11.175
1.00
47.22
C


ATOM
681
O
ALA
A
91
56.877
33.291
11.081
1.00
47.71
O


ATOM
682
CB
ALA
A
91
53.940
34.142
9.828
1.00
46.18
C


ATOM
683
N
MET
A
92
56.439
35.486
11.249
1.00
47.06
N


ATOM
684
CA
MET
A
92
57.856
35.840
11.237
1.00
46.89
C


ATOM
685
C
MET
A
92
58.568
35.257
12.451
1.00
46.53
C


ATOM
686
O
MET
A
92
59.684
34.753
12.340
1.00
47.29
O


ATOM
687
CB
MET
A
92
58.041
37.357
11.222
1.00
46.77
C


ATOM
688
CG
MET
A
92
57.871
37.987
9.863
1.00
46.28
C


ATOM
689
SD
MET
A
92
58.254
39.733
9.915
1.00
45.24
S


ATOM
690
CE
MET
A
92
56.986
40.381
8.852
1.00
46.35
C


ATOM
691
N
VAL
A
93
57.925
35.333
13.611
1.00
46.27
N


ATOM
692
CA
VAL
A
93
58.511
34.796
14.829
1.00
46.01
C


ATOM
693
C
VAL
A
93
58.675
33.290
14.682
1.00
47.76
C


ATOM
694
O
VAL
A
93
59.715
32.733
15.037
1.00
48.37
O


ATOM
695
CB
VAL
A
93
57.624
35.090
16.057
1.00
44.88
C


ATOM
696
CG1
VAL
A
93
58.080
34.254
17.251
1.00
43.31
C


ATOM
697
CG2
VAL
A
93
57.692
36.568
16.394
1.00
43.70
C


ATOM
698
N
HIS
A
94
57.642
32.637
14.153
1.00
49.11
N


ATOM
699
CA
HIS
A
94
57.668
31.189
13.955
1.00
49.55
C


ATOM
700
C
HIS
A
94
58.818
30.791
13.035
1.00
48.88
C


ATOM
701
O
HIS
A
94
59.572
29.862
13.330
1.00
49.22
O


ATOM
702
CB
HIS
A
94
56.344
30.703
13.349
1.00
51.41
C


ATOM
703
CG
HIS
A
94
56.256
29.213
13.221
1.00
53.19
C


ATOM
704
ND1
HIS
A
94
55.924
28.394
14.278
1.00
53.72
N


ATOM
705
CD2
HIS
A
94
56.520
28.391
12.176
1.00
54.01
C


ATOM
706
CE1
HIS
A
94
55.989
27.131
13.893
1.00
53.86
C


ATOM
707
NE2
HIS
A
94
56.351
27.102
12.622
1.00
54.56
N


ATOM
708
N
ALA
A
95
58.952
31.502
11.921
1.00
48.06
N


ATOM
709
CA
ALA
A
95
60.006
31.219
10.956
1.00
47.57
C


ATOM
710
C
ALA
A
95
61.405
31.321
11.567
1.00
48.34
C


ATOM
711
O
ALA
A
95
62.294
30.538
11.233
1.00
48.18
O


ATOM
712
CB
ALA
A
95
59.887
32.162
9.770
1.00
46.85
C


ATOM
713
N
VAL
A
96
61.604
32.289
12.458
1.00
48.08
N


ATOM
714
CA
VAL
A
96
62.906
32.463
13.087
1.00
47.54
C


ATOM
715
C
VAL
A
96
63.165
31.344
14.086
1.00
48.02
C


ATOM
716
O
VAL
A
96
64.276
30.815
14.164
1.00
47.17
O


ATOM
717
CB
VAL
A
96
63.003
33.826
13.815
1.00
47.26
C


ATOM
718
CG1
VAL
A
96
64.336
33.945
14.537
1.00
46.34
C


ATOM
719
CG2
VAL
A
96
62.856
34.952
12.813
1.00
47.02
C


ATOM
720
N
LYS
A
97
62.133
30.979
14.840
1.00
48.62
N


ATOM
721
CA
LYS
A
97
62.252
29.924
15.837
1.00
50.60
C


ATOM
722
C
LYS
A
97
62.459
28.546
15.209
1.00
52.32
C


ATOM
723
O
LYS
A
97
63.068
27.670
15.823
1.00
52.87
O


ATOM
724
CB
LYS
A
97
61.010
29.899
16.742
1.00
49.44
C


ATOM
725
CG
LYS
A
97
60.791
31.169
17.564
1.00
47.42
C


ATOM
726
CD
LYS
A
97
61.988
31.489
18.467
1.00
45.88
C


ATOM
727
CE
LYS
A
97
62.191
30.440
19.557
1.00
44.36
C


ATOM
728
NZ
LYS
A
97
63.433
30.692
20.354
1.00
42.11
N


ATOM
729
N
ASN
A
98
61.962
28.354
13.991
1.00
54.75
N


ATOM
730
CA
ASN
A
98
62.108
27.066
13.315
1.00
58.07
C


ATOM
731
C
ASN
A
98
63.004
27.120
12.085
1.00
59.49
C


ATOM
732
O
ASN
A
98
62.799
26.361
11.138
1.00
60.40
O


ATOM
733
CB
ASN
A
98
60.738
26.515
12.899
1.00
58.95
C


ATOM
734
CG
ASN
A
98
59.882
26.119
14.082
1.00
61.39
C


ATOM
735
OD1
ASN
A
98
59.420
26.970
14.845
1.00
62.44
O


ATOM
736
ND2
ASN
A
98
59.668
24.816
14.248
1.00
62.55
N


ATOM
737
N
PHE
A
99
64.000
27.999
12.092
1.00
61.00
N


ATOM
738
CA
PHE
A
99
64.889
28.117
10.942
1.00
62.73
C


ATOM
739
C
PHE
A
99
65.827
26.926
10.774
1.00
64.62
C


ATOM
740
O
PHE
A
99
66.150
26.544
9.650
1.00
64.73
O


ATOM
741
CB
PHE
A
99
65.719
29.398
11.028
1.00
61.76
C


ATOM
742
CG
PHE
A
99
66.492
29.703
9.772
1.00
61.06
C


ATOM
743
CD1
PHE
A
99
65.827
29.971
8.579
1.00
60.96
C


ATOM
744
CD2
PHE
A
99
67.881
29.727
9.780
1.00
60.81
C


ATOM
745
CE1
PHE
A
99
66.537
30.258
7.412
1.00
60.52
C


ATOM
746
CE2
PHE
A
99
68.599
30.012
8.620
1.00
60.86
C


ATOM
747
CZ
PHE
A
99
67.924
30.279
7.434
1.00
60.69
C


ATOM
748
N
LYS
A
100
66.267
26.340
11.883
1.00
67.08
N


ATOM
749
CA
LYS
A
100
67.178
25.199
11.820
1.00
70.33
C


ATOM
750
C
LYS
A
100
66.462
23.871
11.582
1.00
72.95
C


ATOM
751
O
LYS
A
100
66.988
22.809
11.914
1.00
72.97
O


ATOM
752
CB
LYS
A
100
68.006
25.108
13.104
1.00
69.54
C


ATOM
753
CG
LYS
A
100
68.932
26.288
13.333
1.00
68.73
C


ATOM
754
CD
LYS
A
100
69.765
26.088
14.586
1.00
68.36
C


ATOM
755
CE
LYS
A
100
70.750
27.227
14.791
1.00
67.27
C


ATOM
756
NZ
LYS
A
100
71.581
27.006
16.000
1.00
66.23
N


ATOM
757
N
ALA
A
101
65.269
23.937
10.999
1.00
76.17
N


ATOM
758
CA
ALA
A
101
64.486
22.739
10.717
1.00
79.28
C


ATOM
759
C
ALA
A
101
64.671
22.262
9.275
1.00
81.72
C


ATOM
760
O
ALA
A
101
65.159
21.154
9.043
1.00
81.99
O


ATOM
761
CB
ALA
A
101
63.011
23.002
10.996
1.00
79.19
C


ATOM
762
N
GLY
A
102
64.280
23.092
8.310
1.00
84.33
N


ATOM
763
CA
GLY
A
102
64.420
22.707
6.915
1.00
87.56
C


ATOM
764
C
GLY
A
102
63.773
23.645
5.910
1.00
89.81
C


ATOM
765
O
GLY
A
102
62.728
24.243
6.179
1.00
90.05
O


ATOM
766
N
PHE
A
103
64.402
23.760
4.741
1.00
91.88
N


ATOM
767
CA
PHE
A
103
63.930
24.618
3.653
1.00
93.97
C


ATOM
768
C
PHE
A
103
62.785
23.976
2.864
1.00
95.19
C


ATOM
769
O
PHE
A
103
61.854
24.661
2.427
1.00
95.10
0


ATOM
770
CB
PHE
A
103
65.107
24.933
2.714
1.00
94.40
C


ATOM
771
CG
PHE
A
103
64.716
25.637
1.439
1.00
95.36
C


ATOM
772
CD1
PHE
A
103
64.030
24.961
0.430
1.00
95.96
C


ATOM
773
CD2
PHE
A
103
65.052
26.973
1.238
1.00
95.68
C


ATOM
774
CE1
PHE
A
103
63.682
25.603
0.758
1.00
96.63
C


ATOM
775
CE2
PHE
A
103
64.710
27.627
0.054
1.00
96.41
C


ATOM
776
CZ
PHE
A
103
64.024
26.940
0.947
1.00
96.90
C


ATOM
777
N
VAL
A
104
62.867
22.660
2.685
1.00
96.51
N


ATOM
778
CA
VAL
A
104
61.864
21.904
1.941
1.00
97.40
C


ATOM
779
C
VAL
A
104
60.668
21.484
2.796
1.00
98.06
C


ATOM
780
O
VAL
A
104
60.475
21.986
3.905
1.00
98.29
O


ATOM
781
CB
VAL
A
104
62.494
20.639
1.318
1.00
97.53
C


ATOM
782
CG1
VAL
A
104
63.604
21.035
0.358
1.00
97.83
C


ATOM
783
CG2
VAL
A
104
63.043
19.733
2.415
1.00
97.17
C


ATOM
784
N
VAL
A
105
59.869
20.562
2.265
1.00
98.68
N


ATOM
785
CA
VAL
A
105
58.690
20.055
2.960
1.00
99.19
C


ATOM
786
C
VAL
A
105
58.840
18.556
3.223
1.00
99.69
C


ATOM
787
O
VAL
A
105
59.955
18.034
3.251
1.00
99.86
O


ATOM
788
CB
VAL
A
105
57.408
20.294
2.130
1.00
99.21
C


ATOM
789
CG1
VAL
A
105
57.207
21.786
1.904
1.00
98.66
C


ATOM
790
CG2
VAL
A
105
57.505
19.562
0.798
1.00
99.13
C


ATOM
791
N
SER
A
106
57.720
17.864
3.411
1.00
100.19
N


ATOM
792
CA
SER
A
106
57.748
16.427
3.674
1.00
100.80
C


ATOM
793
C
SER
A
106
57.538
15.604
2.401
1.00
101.31
C


ATOM
794
O
SER
A
106
56.616
14.788
2.323
1.00
101.42
O


ATOM
795
CB
SER
A
106
56.678
16.063
4.707
1.00
100.69
C


ATOM
796
OG
SER
A
106
55.384
16.412
4.245
1.00
100.34
O


ATOM
797
N
ASP
A
107
58.402
15.816
1.412
1.00
101.66
N


ATOM
798
CA
ASP
A
107
58.312
15.101
0.142
1.00
101.66
C


ATOM
799
C
ASP
A
107
59.084
13.785
0.184
1.00
101.55
C


ATOM
800
O
ASP
A
107
59.050
13.003
0.767
1.00
101.37
O


ATOM
801
CB
ASP
A
107
58.848
15.976
0.997
1.00
101.95
C


ATOM
802
CG
ASP
A
107
60.326
16.302
0.843
1.00
102.22
C


ATOM
803
OD1
ASP
A
107
60.742
16.916
0.140
1.00
102.16
O


ATOM
804
OD2
ASP
A
107
61.126
15.891
1.821
1.00
102.12
O


ATOM
805
N
VAL
A
220
77.129
27.310
12.363
1.00
82.99
N


ATOM
806
CA
VAL
A
220
78.036
26.953
13.450
1.00
82.93
C


ATOM
807
C
VAL
A
220
78.735
28.199
13.998
1.00
82.11
C


ATOM
808
O
VAL
A
220
79.965
28.283
14.018
1.00
82.35
O


ATOM
809
CB
VAL
A
220
79.103
25.942
12.967
1.00
83.59
C


ATOM
810
CG1
VAL
A
220
79.931
25.443
14.152
1.00
83.61
C


ATOM
811
CG2
VAL
A
220
78.424
24.777
12.252
1.00
84.13
C


ATOM
812
N
CYS
A
221
77.936
29.165
14.43.9
1.00
80.94
N


ATOM
813
CA
CYS
A
221
78.454
30.414
14.989
1.00
79.61
C


ATOM
814
C
CYS
A
221
78.548
30.290
16.509
1.00
78.38
C


ATOM
815
O
CYS
A
221
77.557
29.996
17.176
1.00
78.27
O


ATOM
816
CB
CYS
A
221
77.526
31.568
14.602
1.00
80.09
C


ATOM
817
SG
CYS
A
221
77.159
31.648
12.823
1.00
80.23
S


ATOM
818
N
HIS
A
222
79.739
30.518
17.054
1.00
76.79
N


ATOM
819
CA
HIS
A
222
79.949
30.395
18.493
1.00
74.99
C


ATOM
820
C
HIS
A
222
79.364
31.496
19.366
1.00
72.24
C


ATOM
821
O
HIS
A
222
79.359
31.376
20.592
1.00
72.13
O


ATOM
822
CB
HIS
A
222
81.442
30.238
18.799
1.00
77.56
C


ATOM
823
CG
HIS
A
222
81.952
28.846
18.586
1.00
80.75
C


ATOM
824
ND1
HIS
A
222
81.352
27.741
19.155
1.00
81.58
N


ATOM
825
CD2
HIS
A
222
83.003
28.377
17.872
1.00
81.49
C


ATOM
826
CE1
HIS
A
222
82.011
26.653
18.799
1.00
82.43
C


ATOM
827
NE2
HIS
A
222
83.017
27.011
18.021
1.00
82.72
N


ATOM
828
N
ASN
A
223
78.875
32.565
18.751
1.00
68.37
N


ATOM
829
CA
ASN
A
223
78.282
33.643
19.526
1.00
64.96
C


ATOM
830
C
ASN
A
223
76.793
33.775
19.261
1.00
61.91
C


ATOM
831
O
ASN
A
223
76.185
34.788
19.599
1.00
60.48
O


ATOM
832
CB
ASN
A
223
78.984
34.968
19.237
1.00
65.81
C


ATOM
833
CG
ASN
A
223
80.285
35.107
19.998
1.00
66.63
C


ATOM
834
OD1
ASN
A
223
80.302
35.069
21.229
1.00
65.69
O


ATOM
835
ND2
ASN
A
223
81.385
35.266
19.270
1.00
67.36
N


ATOM
836
N
GLU
A
224
76.206
32.746
18.660
1.00
58.19
N


ATOM
837
CA
GLU
A
224
74.780
32.774
18.371
1.00
55.64
C


ATOM
838
C
GLU
A
224
73.972
32.796
19.657
1.00
51.83
C


ATOM
839
O
GLU
A
224
74.341
32.166
20.646
1.00
50.93
O


ATOM
840
CB
GLU
A
224
74.367
31.560
17.534
1.00
56.74
C


ATOM
841
CG
GLU
A
224
74.747
30.220
18.136
1.00
59.42
C


ATOM
842
CD
GLU
A
224
74.114
29.053
17.398
1.00
60.69
C


ATOM
843
OE1
GLU
A
224
74.019
29.115
16.149
1.00
61.36
O


ATOM
844
OE2
GLU
A
224
73.722
28.073
18.069
1.00
60.59
O


ATOM
845
N
LEU
A
225
72.871
33.536
19.634
1.00
48.65
N


ATOM
846
CA
LEU
A
225
71.991
33.641
20.785
1.00
46.12
C


ATOM
847
C
LEU
A
225
70.843
32.660
20.571
1.00
44.98
C


ATOM
848
O
LEU
A
225
70.031
32.832
19.660
1.00
42.50
O


ATOM
849
CB
LEU
A
225
71.456
35.071
20.904
1.00
45.35
C


ATOM
850
CG
LEU
A
225
70.635
35.402
22.151
1.00
46.02
C


ATOM
851
CD1
LEU
A
225
71.483
35.146
23.389
1.00
46.56
C


ATOM
852
CD2
LEU
A
225
70.174
36.851
22.107
1.00
45.65
C


ATOM
853
N
VAL
A
226
70.778
31.634
21.415
1.00
45.11
N


ATOM
854
CA
VAL
A
226
69.740
30.612
21.293
1.00
45.18
C


ATOM
855
C
VAL
A
226
69.138
30.162
22.623
1.00
46.10
C


ATOM
856
O
VAL
A
226
69.664
30.461
23.698
1.00
46.22
O


ATOM
857
CB
VAL
A
226
70.294
29.355
20.598
1.00
44.37
C


ATOM
858
CG1
VAL
A
226
70.698
29.674
19.170
1.00
42.78
C


ATOM
859
CG2
VAL
A
226
71.478
28.826
21.383
1.00
43.24
C


ATOM
860
N
ASP
A
227
68.026
29.435
22.535
1.00
46.56
N


ATOM
861
CA
ASP
A
227
67.366
28.912
23.721
1.00
47.21
C


ATOM
862
C
ASP
A
227
67.910
27.516
24.017
1.00
48.24
C


ATOM
863
O
ASP
A
227
68.808
27.034
23.325
1.00
47.45
O


ATOM
864
CB
ASP
A
227
65.848
28.854
23.523
1.00
46.83
C


ATOM
865
CG
ASP
A
227
65.445
28.110
22.264
1.00
46.84
C


ATOM
866
OD1
ASP
A
227
66.094
27.099
21.924
1.00
47.01
O


ATOM
867
OD2
ASP
A
227
64.460
28.529
21.620
1.00
46.98
O


ATOM
868
N
SER
A
228
67.357
26.875
25.043
1.00
50.32
N


ATOM
869
CA
SER
A
228
67.782
25.541
25.456
1.00
52.29
C


ATOM
870
C
SER
A
228
67.580
24.487
24.366
1.00
53.54
C


ATOM
871
O
SER
A
228
68.129
23.386
24.448
1.00
54.15
O


ATOM
872
CB
SER
A
228
67.031
25.127
26.723
1.00
51.85
C


ATOM
873
OG
SER
A
228
65.636
25.099
26.492
1.00
52.33
O


ATOM
874
N
GLN
A
229
66.793
24.832
23.352
1.00
54.18
N


ATOM
875
CA
GLN
A
229
66.526
23.934
22.237
1.00
54.92
C


ATOM
876
C
GLN
A
229
67.418
24.282
21.049
1.00
55.01
C


ATOM
877
O
GLN
A
229
67.224
23.772
19.942
1.00
55.05
O


ATOM
878
CB
GLN
A
229
65.058
24.038
21.818
1.00
56.21
C


ATOM
879
CG
GLN
A
229
64.088
23.265
22.691
1.00
58.02
C


ATOM
880
CD
GLN
A
229
62.641
23.613
22.386
1.00
60.19
C


ATOM
881
OE1
GLN
A
229
62.130
24.637
22.845
1.00
60.85
O


ATOM
882
NE2
GLN
A
229
61.976
22.770
21.597
1.00
61.03
N


ATOM
883
N
LYS
A
230
68.392
25.157
21.287
1.00
54.58
N


ATOM
884
CA
LYS
A
230
69.328
25.596
20.255
1.00
53.47
C


ATOM
885
C
LYS
A
230
68.684
26.418
19.137
1.00
51.87
C


ATOM
886
O
LYS
A
230
69.257
26.554
18.055
1.00
51.62
O


ATOM
887
CB
LYS
A
230
70.057
24.390
19.652
1.00
55.91
C


ATOM
888
CG
LYS
A
230
70.846
23.572
20.669
1.00
58.78
C


ATOM
889
CD
LYS
A
230
71.977
24.381
21.305
1.00
61.46
C


ATOM
890
CE
LYS
A
230
73.062
24.738
20.290
1.00
62.75
C


ATOM
891
NZ
LYS
A
230
74.211
25.454
20.926
1.00
63.92
N


ATOM
892
N
ARG
A
231
67.501
26.970
19.395
1.00
50.44
N


ATOM
893
CA
ARG
A
231
66.816
27.796
18.400
1.00
48.86
C


ATOM
894
C
ARG
A
231
67.179
29.261
18.644
1.00
47.36
C


ATOM
895
O
ARG
A
231
67.351
29.679
19.789
1.00
45.45
O


ATOM
896
CB
ARG
A
231
65.296
27.637
18.512
1.00
50.40
C


ATOM
897
CG
ARG
A
231
64.794
26.199
18.451
1.00
51.58
C


ATOM
898
CD
ARG
A
231
63.779
25.952
19.553
1.00
53.03
C


ATOM
899
NE
ARG
A
231
62.461
26.504
19.257
1.00
55.50
N


ATOM
900
CZ
ARG
A
231
61.573
26.852
20.186
1.00
56.77
C


ATOM
901
NH1
ARG
A
231
61.869
26.716
21.471
1.00
57.45
N


ATOM
902
NH2
ARG
A
231
60.379
27.317
19.833
1.00
57.86
N


ATOM
903
N
TYR
A
232
67.294
30.034
17.567
1.00
45.64
N


ATOM
904
CA
TYR
A
232
67.623
31.450
17.671
1.00
43.85
C


ATOM
905
C
TYR
A
232
66.581
32.200
18.497
1.00
42.80
C


ATOM
906
O
TYR
A
232
65.376
31.965
18.361
1.00
41.87
O


ATOM
907
CB
TYR
A
232
67.692
32.093
16.286
1.00
43.80
C


ATOM
908
CG
TYR
A
232
68.821
31.603
15.423
1.00
44.82
C


ATOM
909
CD1
TYR
A
232
70.142
31.650
15.871
1.00
45.02
C


ATOM
910
CD2
TYR
A
232
68.573
31.094
14.151
1.00
45.58
C


ATOM
911
CE1
TYR
A
232
71.193
31.197
15.066
1.00
46.46
C


ATOM
912
CE2
TYR
A
232
69.610
30.642
13.341
1.00
46.70
C


ATOM
913
CZ
TYR
A
232
70.915
30.694
13.803
1.00
46.56
C


ATOM
914
OH
TYR
A
232
71.932
30.237
12.998
1.00
47.52
O


ATOM
915
N
LEU
A
233
67.044
33.097
19.358
1.00
41.20
N


ATOM
916
CA
LEU
A
233
66.119
33.882
20.160
1.00
40.26
C


ATOM
917
C
LEU
A
233
65.573
34.990
19.275
1.00
39.17
C


ATOM
918
O
LEU
A
233
66.231
35.428
18.328
1.00
39.41
O


ATOM
919
CB
LEU
A
233
66.816
34.493
21.380
1.00
39.71
C


ATOM
920
CG
LEU
A
233
67.335
33.532
22.453
1.00
40.47
C


ATOM
921
CD1
LEU
A
233
67.794
34.339
23.661
1.00
40.88
C


ATOM
922
CD2
LEU
A
233
66.243
32.562
22.870
1.00
39.44
C


ATOM
923
N
VAL
A
234
64.360
35.432
19.572
1.00
37.75
N


ATOM
924
CA
VAL
A
234
63.756
36.498
18.799
1.00
37.14
C


ATOM
925
C
VAL
A
234
62.766
37.241
19.681
1.00
37.43
C


ATOM
926
O
VAL
A
234
62.157
36.653
20.575
1.00
37.88
O


ATOM
927
CB
VAL
A
234
63.032
35.946
17.544
1.00
36.92
C


ATOM
928
CG1
VAL
A
234
61.826
35.102
17.954
1.00
34.91
C


ATOM
929
CG2
VAL
A
234
62.619
37.096
16.638
1.00
35.20
C


ATOM
930
N
GLY
A
235
62.631
38.540
19.444
1.00
36.87
N


ATOM
931
CA
GLY
A
235
61.703
39.335
20.223
1.00
36.91
C


ATOM
932
C
GLY
A
235
60.596
39.828
19.318
1.00
36.80
C


ATOM
933
O
GLY
A
235
60.670
39.654
18.098
1.00
37.13
O


ATOM
934
N
ALA
A
236
59.572
40.440
19.903
1.00
35.88
N


ATOM
935
CA
ALA
A
236
58.465
40.958
19.116
1.00
35.95
C


ATOM
936
C
ALA
A
236
57.824
42.165
19.791
1.00
35.70
C


ATOM
937
O
ALA
A
236
57.559
42.153
20.995
1.00
37.71
O


ATOM
938
CB
ALA
A
236
57.423
39.860
18.893
1.00
36.04
C


ATOM
939
N
GLY
A
237
57.578
43.212
19.012
1.00
35.37
N


ATOM
940
CA
GLY
A
237
56.961
44.401
19.564
1.00
36.75
C


ATOM
941
C
GLY
A
237
55.459
44.243
19.696
1.00
38.21
C


ATOM
942
O
GLY
A
237
54.837
43.542
18.895
1.00
39.76
O


ATOM
943
N
ILE
A
238
54.876
44.870
20.715
1.00
36.81
N


ATOM
944
CA
ILE
A
238
53.437
44.818
20.926
1.00
37.17
C


ATOM
945
C
ILE
A
238
52.933
46.227
21.232
1.00
37.51
C


ATOM
946
O
ILE
A
238
53.713
47.111
21.591
1.00
36.78
O


ATOM
947
CB
ILE
A
238
53.043
43.883
22.107
1.00
38.27
C


ATOM
948
CG1
ILE
A
238
53.568
44.449
23.432
1.00
38.61
C


ATOM
949
CG2
ILE
A
238
53.588
42.485
21.872
1.00
36.69
C


ATOM
950
CD1
ILE
A
238
53.046
43.710
24.665
1.00
38.14
C


ATOM
951
N
ASN
A
239
51.631
46.442
21.074
1.00
37.56
N


ATOM
952
CA
ASN
A
239
51.048
47.746
21.351
1.00
37.15
C


ATOM
953
C
ASN
A
239
50.037
47.630
22.484
1.00
38.42
C


ATOM
954
O
ASN
A
239
49.644
46.526
22.873
1.00
37.39
O


ATOM
955
CB
ASN
A
239
50.388
48.312
20.090
1.00
37.73
C


ATOM
956
CG
ASN
A
239
49.255
47.439
19.575
1.00
38.01
C


ATOM
957
OD1
ASN
A
239
48.224
47.300
20.228
1.00
37.30
O


ATOM
958
ND2
ASN
A
239
49.446
46.846
18.402
1.00
37.32
N


ATOM
959
N
THR
A
240
49.629
48.776
23.018
1.00
39.33
N


ATOM
960
CA
THR
A
240
48.678
48.832
24.121
1.00
40.33
C


ATOM
961
C
THR
A
240
47.219
48.678
23.672
1.00
42.53
C


ATOM
962
O
THR
A
240
46.299
48.869
24.468
1.00
41.92
O


ATOM
963
CB
THR
A
240
48.812
50.168
24.870
1.00
39.24
C


ATOM
964
OG1
THR
A
240
48.634
51.242
23.940
1.00
39.26
O


ATOM
965
CG2
THR
A
240
50.192
50.293
25.514
1.00
37.80
C


ATOM
966
N
ARG
A
241
47.010
48.319
22.409
1.00
44.79
N


ATOM
967
CA
ARG
A
241
45.659
48.177
21.876
1.00
48.48
C


ATOM
968
C
ARG
A
241
45.165
46.738
21.739
1.00
48.69
C


ATOM
969
O
ARG
A
241
44.291
46.305
22.487
1.00
48.51
O


ATOM
970
CB
ARG
A
241
45.565
48.862
20.509
1.00
51.38
C


ATOM
971
CG
ARG
A
241
45.987
50.327
20.508
1.00
56.77
C


ATOM
972
CD
ARG
A
241
44.854
51.258
20.917
1.00
60.32
C


ATOM
973
NE
ARG
A
241
43.743
51.209
19.965
1.00
63.77
N


ATOM
974
CZ
ARG
A
241
42.827
52.166
19.829
1.00
65.29
C


ATOM
975
NH1
ARG
A
241
42.885
53.260
20.583
1.00
65.45
N


ATOM
976
NH2
ARG
A
241
41.850
52.030
18.939
1.00
65.16
N


ATOM
977
N
ASP
A
242
45.724
46.006
20.781
1.00
48.65
N


ATOM
978
CA
ASP
A
242
45.304
44.632
20.523
1.00
50.20
C


ATOM
979
C
ASP
A
242
46.142
43.558
21.206
1.00
50.06
C


ATOM
980
O
ASP
A
242
46.237
42.442
20.702
1.00
51.04
O


ATOM
981
CB
ASP
A
242
45.306
44.362
19.013
1.00
49.94
C


ATOM
982
CG
ASP
A
242
46.696
44.458
18.404
1.00
51.08
C


ATOM
983
OD1
ASP
A
242
47.683
44.268
19.146
1.00
50.09
O


ATOM
984
0D2
ASP
A
242
46.804
44.708
17.181
1.00
51.20
O


ATOM
985
N
PHE
A
243
46.732
43.879
22.353
1.00
49.77
N


ATOM
986
CA
PHE
A
243
47.579
42.924
23.065
1.00
49.06
C


ATOM
987
C
PHE
A
243
46.889
41.647
23.549
1.00
49.87
C


ATOM
988
O
PHE
A
243
47.539
40.609
23.694
1.00
49.78
O


ATOM
989
CB
PHE
A
243
48.274
43.617
24.242
1.00
45.99
C


ATOM
990
CG
PHE
A
243
47.334
44.151
25.279
1.00
44.15
C


ATOM
991
CD1
PHE
A
243
46.841
43.323
26.283
1.00
43.69
C


ATOM
992
CD2
PHE
A
243
46.956
45.490
25.268
1.00
43.83
C


ATOM
993
CE1
PHE
A
243
45.989
43.821
27.266
1.00
42.27
C


ATOM
994
CE2
PHE
A
243
46.103
46.001
26.247
1.00
43.52
C


ATOM
995
CZ
PHE
A
243
45.619
45.163
27.249
1.00
43.49
C


ATOM
996
N
ARG
A
244
45.583
41.714
23.796
1.00
50.68
N


ATOM
997
CA
ARG
A
244
44.852
40.537
24.260
1.00
51.51
C


ATOM
998
C
ARG
A
244
44.820
39.453
23.187
1.00
51.28
C


ATOM
999
O
ARG
A
244
44.697
38.268
23.494
1.00
51.51
O


ATOM
1000
CB
ARG
A
244
43.423
40.915
24.682
1.00
52.01
C


ATOM
1001
CG
ARG
A
244
43.368
41.841
25.899
1.00
52.37
C


ATOM
1002
CD
ARG
A
244
41.939
42.089
26.374
1.00
53.17
C


ATOM
1003
NE
ARG
A
244
41.895
43.054
27.473
1.00
54.20
N


ATOM
1004
CZ
ARG
A
244
42.125
44.359
27.337
1.00
55.49
C


ATOM
1005
NH1
ARG
A
244
42.408
44.870
26.144
1.00
54.46
N


ATOM
1006
NH2
ARG
A
244
42.089
45.154
28.399
1.00
55.06
N


ATOM
1007
N
GLU
A
245
44.935
39.859
21.928
1.00
50.95
N


ATOM
1008
CA
GLU
A
245
44.940
38.906
20.826
1.00
51.31
C


ATOM
1009
C
GLU
A
245
46.362
38.666
20.335
1.00
50.29
C


ATOM
1010
O
GLU
A
245
46.770
37.526
20.107
1.00
50.46
O


ATOM
1011
CB
GLU
A
245
44.095
39.415
19.653
1.00
53.93
C


ATOM
1012
CG
GLU
A
245
42.588
39.248
19.813
1.00
58.44
C


ATOM
1013
CD
GLU
A
245
42.012
40.073
20.950
1.00
61.81
C


ATOM
1014
OE1
GLU
A
245
42.234
41.309
20.972
1.00
63.52
O


ATOM
1015
OE2
GLU
A
245
41.329
39.484
21.818
1.00
63.32
O


ATOM
1016
N
ARG
A
246
47.117
39.749
20.181
1.00
48.30
N


ATOM
1017
CA
ARG
A
246
48.489
39.671
19.689
1.00
46.47
C


ATOM
1018
C
ARG
A
246
49.447
38.897
20.599
1.00
45.04
C


ATOM
1019
O
ARG
A
246
50.187
38.036
20.132
1.00
44.61
O


ATOM
1020
CB
ARG
A
246
49.029
41.085
19.442
1.00
45.89
C


ATOM
1021
CG
ARG
A
246
50.345
41.127
18.681
1.00
45.20
C


ATOM
1022
CD
ARG
A
246
50.833
42.556
18.513
1.00
44.73
C


ATOM
1023
NE
ARG
A
246
49.950
43.359
17.671
1.00
43.18
N


ATOM
1024
CZ
ARG
A
246
49.880
43.265
16.347
1.00
42.54
C


ATOM
1025
NH1
ARG
A
246
50.644
42.402
15.694
1.00
41.20
N


ATOM
1026
NH2
ARG
A
246
49.042
44.040
15.673
1.00
44.27
N


ATOM
1027
N
VAL
A
247
49.435
39.193
21.894
1.00
44.31
N


ATOM
1028
CA
VAL
A
247
50.335
38.509
22.819
1.00
44.71
C


ATOM
1029
C
VAL
A
247
50.238
36.976
22.757
1.00
45.57
C


ATOM
1030
O
VAL
A
247
51.245
36.296
22.530
1.00
45.24
O


ATOM
1031
CB
VAL
A
247
50.101
38.984
24.274
1.00
43.46
C


ATOM
1032
CG1
VAL
A
247
50.894
38.123
25.244
1.00
43.08
C


ATOM
1033
CG2
VAL
A
247
50.512
40.444
24.410
1.00
43.85
C


ATOM
1034
N
PRO
A
248
49.027
36.411
22.959
1.00
45.51
N


ATOM
1035
CA
PRO
A
248
48.879
34.952
22.912
1.00
44.41
C


ATOM
1036
C
PRO
A
248
49.439
34.367
21.624
1.00
44.05
C


ATOM
1037
O
PRO
A
248
50.118
33.348
21.641
1.00
44.00
O


ATOM
1038
CB
PRO
A
248
47.369
34.755
23.030
1.00
45.34
C


ATOM
1039
CG
PRO
A
248
46.956
35.899
23.898
1.00
45.42
C


ATOM
1040
CD
PRO
A
248
47.741
37.052
23.297
1.00
44.89
C


ATOM
1041
N
ALA
A
249
49.162
35.028
20.508
1.00
43.48
N


ATOM
1042
CA
ALA
A
249
49.639
34.565
19.215
1.00
43.34
C


ATOM
1043
C
ALA
A
249
51.167
34.583
19.129
1.00
44.16
C


ATOM
1044
O
ALA
A
249
51.774
33.705
18.504
1.00
43.00
O


ATOM
1045
CB
ALA
A
249
49.040
35.421
18.111
1.00
42.95
C


ATOM
1046
N
LEU
A
250
51.786
35.582
19.755
1.00
43.64
N


ATOM
1047
CA
LEU
A
250
53.238
35.692
19.729
1.00
43.74
C


ATOM
1048
C
LEU
A
250
53.862
34.647
20.643
1.00
43.57
C


ATOM
1049
O
LEU
A
250
54.897
34.069
20.322
1.00
41.77
O


ATOM
1050
CB
LEU
A
250
53.677
37.110
20.125
1.00
43.33
C


ATOM
1051
CG
LEU
A
250
53.303
38.171
19.078
1.00
43.68
C


ATOM
1052
CD1
LEU
A
250
53.687
39.554
19.563
1.00
43.65
C


ATOM
1053
CD2
LEU
A
250
54.001
37.858
17.761
1.00
42.84
C


ATOM
1054
N
VAL
A
251
53.223
34.398
21.778
1.00
44.52
N


ATOM
1055
CA
VAL
A
251
53.721
33.398
22.708
1.00
47.01
C


ATOM
1056
C
VAL
A
251
53.668
32.020
22.049
1.00
48.22
C


ATOM
1057
O
VAL
A
251
54.659
31.289
22.047
1.00
48.12
O


ATOM
1058
CB
VAL
A
251
52.883
33.364
23.993
1.00
47.37
C


ATOM
1059
CG1
VAL
A
251
53.327
32.206
24.870
1.00
48.76
C


ATOM
1060
CG2
VAL
A
251
53.031
34.678
24.739
1.00
48.75
C


ATOM
1061
N
GLU
A
252
52.512
31.676
21.483
1.00
49.02
N


ATOM
1062
CA
GLU
A
252
52.341
30.383
20.821
1.00
50.45
C


ATOM
1063
C
GLU
A
252
53.372
30.211
19.712
1.00
48.80
C


ATOM
1064
O
GLU
A
252
53.859
29.109
19.476
1.00
48.65
O


ATOM
1065
CB
GLU
A
252
50.945
30.253
20.195
1.00
53.26
C


ATOM
1066
CG
GLU
A
252
49.795
30.809
21.010
1.00
58.83
C


ATOM
1067
CD
GLU
A
252
49.648
30.175
22.379
1.00
62.50
C


ATOM
1068
OE1
GLU
A
252
48.721
30.596
23.108
1.00
64.11
O


ATOM
1069
OE2
GLU
A
252
50.444
29.267
22.727
1.00
64.32
O


ATOM
1070
N
ALA
A
253
53.688
31.303
19.022
1.00
47.24
N


ATOM
1071
CA
ALA
A
253
54.658
31.270
17.933
1.00
45.47
C


ATOM
1072
C
ALA
A
253
56.075
31.044
18.457
1.00
44.43
C


ATOM
1073
O
ALA
A
253
56.988
30.749
17.686
1.00
43.74
O


ATOM
1074
CB
ALA
A
253
54.591
32.563
17.131
1.00
45.15
C


ATOM
1075
N
GLY
A
254
56.253
31.184
19.769
1.00
43.76
N


ATOM
1076
CA
GLY
A
254
57.562
30.968
20.366
1.00
43.81
C


ATOM
1077
C
GLY
A
254
58.415
32.207
20.610
1.00
43.78
C


ATOM
1078
O
GLY
A
254
59.635
32.103
20.751
1.00
43.49
O


ATOM
1079
N
ALA
A
255
57.793
33.381
20.658
1.00
42.53
N


ATOM
1080
CA
ALA
A
255
58.540
34.611
20.902
1.00
40.96
C


ATOM
1081
C
ALA
A
255
59.227
34.506
22.263
1.00
39.56
C


ATOM
1082
O
ALA
A
255
58.595
34.154
23.260
1.00
40.08
O


ATOM
1083
CB
ALA
A
255
57.603
35.805
20.871
1.00
40.32
C


ATOM
1084
N
ASP
A
256
60.520
34.812
22.307
1.00
38.45
N


ATOM
1085
CA
ASP
A
256
61.274
34.723
23.557
1.00
38.35
C


ATOM
1086
C
ASP
A
256
61.088
35.928
24.478
1.00
37.56
C


ATOM
1087
O
ASP
A
256
61.159
35.802
25.700
1.00
36.65
O


ATOM
1088
CB
ASP
A
256
62.752
34.522
23.247
1.00
38.22
C


ATOM
1089
CG
ASP
A
256
63.007
33.235
22.497
1.00
40.05
C


ATOM
1090
OD1
ASP
A
256
62.884
32.161
23.123
1.00
42.66
O


ATOM
1091
OD2
ASP
A
256
63.313
33.292
21.286
1.00
37.79
O


ATOM
1092
N
VAL
A
257
60.847
37.093
23.890
1.00
36.57
N


ATOM
1093
CA
VAL
A
257
60.647
38.302
24.676
1.00
35.73
C


ATOM
1094
C
VAL
A
257
59.773
39.278
23.903
1.00
35.41
C


ATOM
1095
O
VAL
A
257
59.755
39.265
22.678
1.00
36.12
O


ATOM
1096
CB
VAL
A
257
61.999
38.979
25.019
1.00
34.09
C


ATOM
1097
CG1
VAL
A
257
62.725
39.352
23.746
1.00
33.95
C


ATOM
1098
CG2
VAL
A
257
61.771
40.206
25.889
1.00
33.54
C


ATOM
1099
N
LEU
A
258
59.040
40.113
24.626
1.00
34.36
N


ATOM
1100
CA
LEU
A
258
58.173
41.095
23.993
1.00
35.77
C


ATOM
1101
C
LEU
A
258
58.597
42.498
24.423
1.00
35.65
C


ATOM
1102
O
LEU
A
258
59.376
42.661
25.359
1.00
36.03
O


ATOM
1103
CB
LEU
A
258
56.713
40.857
24.402
1.00
34.23
C


ATOM
1104
CG
LEU
A
258
56.155
39.441
24.206
1.00
35.31
C


ATOM
1105
CD1
LEU
A
258
54.719
39.402
24.682
1.00
38.42
C


ATOM
1106
CD2
LEU
A
258
56.245
39.027
22.747
1.00
34.36
C


ATOM
1107
N
CYS
A
259
58.100
43.509
23.721
1.00
36.29
N


ATOM
1108
CA
CYS
A
259
58.403
44.886
24.080
1.00
34.94
C


ATOM
1109
C
CYS
A
259
57.318
45.825
23.576
1.00
34.40
C


ATOM
1110
O
CYS
A
259
57.033
45.867
22.377
1.00
33.93
O


ATOM
1111
CB
CYS
A
259
59.756
45.329
23.512
1.00
34.49
C


ATOM
1112
SG
CYS
A
259
60.296
46.925
24.191
1.00
34.45
S


ATOM
1113
N
ILE
A
260
56.712
46.568
24.496
1.00
34.72
N


ATOM
1114
CA
ILE
A
260
55.682
47.526
24.126
1.00
36.19
C


ATOM
1115
C
ILE
A
260
56.391
48.632
23.350
1.00
37.93
C


ATOM
1116
O
ILE
A
260
57.355
49.223
23.829
1.00
37.54
O


ATOM
1117
CB
ILE
A
260
55.003
48.122
25.364
1.00
35.39
C


ATOM
1118
CG1
ILE
A
260
54.471
46.988
26.247
1.00
34.45
C


ATOM
1119
CG2
ILE
A
260
53.868
49.052
24.937
1.00
34.98
C


ATOM
1120
CD1
ILE
A
260
53.866
47.456
27.556
1.00
32.91
C


ATOM
1121
N
ASP
A
261
55.905
48.886
22.143
1.00
39.60
N


ATOM
1122
CA
ASP
A
261
56.472
49.873
21.236
1.00
40.88
C


ATOM
1123
C
ASP
A
261
55.700
51.197
21.318
1.00
41.39
C


ATOM
1124
O
ASP
A
261
54.549
51.275
20.887
1.00
42.16
O


ATOM
1125
CB
ASP
A
261
56.422
49.266
19.826
1.00
42.12
C


ATOM
1126
CG
ASP
A
261
56.977
50.179
18.756
1.00
43.34
C


ATOM
1127
OD1
ASP
A
261
57.842
51.025
19.061
1.00
43.64
O


ATOM
1128
OD2
ASP
A
261
56.553
50.025
17.591
1.00
42.92
O


ATOM
1129
N
SER
A
262
56.328
52.232
21.881
1.00
40.43
N


ATOM
1130
CA
SER
A
262
55.673
53.535
22.030
1.00
39.93
C


ATOM
1131
C
SER
A
262
56.679
54.678
22.197
1.00
39.85
C


ATOM
1132
O
SER
A
262
57.777
54.464
22.711
1.00
40.98
O


ATOM
1133
CB
SER
A
262
54.733
53.492
23.242
1.00
40.30
C


ATOM
1134
OG
SER
A
262
54.167
54.761
23.518
1.00
40.02
O


ATOM
1135
N
SER
A
263
56.305
55.888
21.778
1.00
38.66
N


ATOM
2136
CA
SER
A
263
57.202
57.040
22.904
1.00
39.38
C


ATOM
1137
C
SER
A
263
57.161
57.641
23.302
1.00
38.48
C


ATOM
1138
O
SER
A
263
58.107
58.300
23.733
1.00
40.33
O


ATOM
1139
CE
SER
A
263
56.867
58.121
20.869
1.00
38.57
C


ATOM
1140
OG
SER
A
263
55.566
58.644
21.047
1.00
45.09
O


ATOM
1141
N
ASP
A
264
56.057
57.425
24.005
1.00
35.74
N


ATOM
1142
CA
ASP
A
264
55.913
57.920
25.366
1.00
33.57
C


ATOM
1143
C
ASP
A
264
55.358
56.776
26.217
1.00
33.27
C


ATOM
1144
O
ASP
A
264
54.144
56.587
26.313
1.00
32.17
O


ATOM
1145
CB
ASP
A
264
54.975
59.136
25.399
1.00
32.37
C


ATOM
1146
CG
ASP
A
264
54.581
59.537
26.812
1.00
32.47
C


ATOM
1147
OD1
ASP
A
264
55.252
59.113
27.781
1.00
30.31
O


ATOM
1148
OD2
ASP
A
264
53.598
60.287
26.957
1.00
32.93
O


ATOM
1149
N
GLY
A
265
56.265
56.014
26.822
1.00
32.50
N


ATOM
1150
CA
GLY
A
265
55.872
54.888
27.649
1.00
32.54
C


ATOM
1151
C
GLY
A
265
55.400
55.262
29.039
1.00
32.72
C


ATOM
1152
O
GLY
A
265
54.959
54.397
29.799
1.00
33.52
O


ATOM
1153
N
PHE
A
266
55.502
56.539
29.390
1.00
31.81
N


ATOM
1154
CA
PHE
A
266
55.057
56.985
30.705
1.00
32.42
C


ATOM
1155
C
PHE
A
266
53.540
57.082
30.577
1.00
33.52
C


ATOM
1156
O
PHE
A
266
52.967
58.166
30.582
1.00
31.71
O


ATOM
1157
CS
PHE
A
266
55.664
58.352
31.043
1.00
30.79
C


ATOM
1158
CG
PHE
A
266
55.742
58.641
32.525
1.00
32.48
C


ATOM
1159
CD1
PHE
A
266
55.019
57.877
33.450
1.00
31.15
C


ATOM
1160
CD2
PHE
A
266
56.534
59.690
32.997
1.00
31.72
C


ATOM
1161
CE1
PHE
A
266
55.085
58.153
34.823
1.00
31.90
C


ATOM
1162
CE2
PHE
A
266
56.611
59.976
34.361
1.00
31.70
C


ATOM
1163
CZ
PHE
A
266
55.883
59.206
35.281
1.00
32.01
C


ATOM
1164
N
SER
A
267
52.896
55.922
30.468
1.00
35.51
N


ATOM
1165
CA
SER
A
267
51.455
55.859
30.272
1.00
35.95
C


ATOM
1166
C
SER
A
267
50.735
54.762
31.045
1.00
36.73
C


ATOM
1167
O
SER
A
267
51.233
53.644
31.187
1.00
34.99
O


ATOM
1168
CE
SER
A
267
51.169
55.671
28.785
1.00
36.57
C


ATOM
1169
OG
SER
A
267
49.795
55.428
28.553
1.00
40.30
O


ATOM
1170
N
GLU
A
268
49.543
55.089
31.523
1.00
37.27
N


ATOM
1171
CA
GLU
A
268
48.736
54.133
32.252
1.00
38.55
C


ATOM
1172
C
GLU
A
268
48.437
52.945
31.331
1.00
38.48
C


ATOM
1173
O
GLU
A
268
48.204
51.830
31.797
1.00
38.40
O


ATOM
1174
CB
GLU
A
268
47.436
54.793
32.719
1.00
39.99
C


ATOM
1175
CG
GLU
A
268
46.601
53.903
33.614
1.00
44.01
C


ATOM
1176
CD
GLU
A
268
45.427
54.627
34.254
1.00
46.54
C


ATOM
1177
OE1
GLU
A
268
44.703
53.969
35.037
1.00
48.88
O


ATOM
1178
OE2
GLU
A
268
45.230
55.836
33.983
1.00
44.63
O


ATOM
1179
N
TRP
A
269
48.453
53.184
30.022
1.00
38.21
N


ATOM
1180
CA
TRP
A
269
48.198
52.114
29.061
1.00
39.86
C


ATOM
1181
C
TRP
A
269
49.267
51.024
29.131
1.00
39.35
C


ATOM
1182
O
TRP
A
269
48.967
49.849
28.917
1.00
40.08
O


ATOM
1183
CE
TRP
A
269
48.129
52.657
27.630
1.00
41.72
C


ATOM
1184
CG
TRP
A
269
46.968
53.561
27.393
1.00
46.52
C


ATOM
1185
CD1
TRP
A
269
47.004
54.914
27.207
1.00
46.39
C


ATOM
1186
CD2
TRP
A
269
45.585
53.186
27.347
1.00
47.71
C


ATOM
1187
NE1
TRP
A
269
45.731
55.404
27.049
1.00
47.84
N


ATOM
1188
CE2
TRP
A
269
44.841
54.366
27.130
1.00
48.66
C


ATOM
1189
CE3
TRP
A
269
44.903
51.969
27.470
1.00
49.25
C


ATOM
1190
CZ2
TRP
A
269
43.445
54.364
27.032
1.00
49.71
C


ATOM
1191
CZ3
TRP
A
269
43.513
51.966
27.373
1.00
49.48
C


ATOM
1192
CH2
TRP
A
269
42.802
53.158
27.156
1.00
50.26
C


ATOM
1193
N
GLN
A
270
50.512
51.401
29.411
1.00
37.64
N


ATOM
1194
CA
GLN
A
270
51.575
50.401
29.506
1.00
37.63
C


ATOM
1195
C
GLN
A
270
51.402
49.609
30.803
1.00
37.10
C


ATOM
1196
O
GLN
A
270
51.661
48.410
30.838
1.00
37.39
O


ATOM
1197
CB
GLN
A
270
52.972
51.053
29.461
1.00
35.59
C


ATOM
1198
CG
GLN
A
270
53.233
51.888
28.205
1.00
34.03
C


ATOM
1199
CD
GLN
A
270
54.518
51.520
27.470
1.00
33.74
C


ATOM
1200
OE1
GLN
A
270
55.417
50.883
28.024
1.00
31.90
O


ATOM
1201
NE2
GLN
A
270
54.615
51.943
26.217
1.00
31.81
N


ATOM
1202
N
LYS
A
271
50.955
50.276
31.864
1.00
37.76
N


ATOM
1203
CA
LYS
A
271
50.737
49.592
33.135
1.00
39.58
C


ATOM
1204
C
LYS
A
271
49.646
48.532
32.968
1.00
39.28
C


ATOM
1205
O
LYS
A
271
49.780
47.412
33.455
1.00
39.33
O


ATOM
1206
CB
LYS
A
271
50.320
50.574
34.228
1.00
41.44
C


ATOM
1207
CG
LYS
A
271
50.086
49.901
35.578
1.00
43.95
C


ATOM
1208
CD
LYS
A
271
49.844
50.909
36.688
1.00
46.05
C


ATOM
1209
CE
LYS
A
271
49.756
50.209
38.044
1.00
48.90
C


ATOM
1210
NZ
LYS
A
271
49.762
51.161
39.201
1.00
50.93
N


ATOM
1211
N
ILE
A
272
48.574
48.896
32.269
1.00
38.91
N


ATOM
1212
CA
ILE
A
272
47.462
47.984
32.029
1.00
39.12
C


ATOM
1213
C
ILE
A
272
47.926
46.793
31.198
1.00
39.33
C


ATOM
1214
O
ILE
A
272
47.616
45.654
31.517
1.00
40.20
O


ATOM
1215
CB
ILE
A
272
46.297
48.701
31.300
1.00
38.48
C


ATOM
1216
CG1
ILE
A
272
45.626
49.687
32.257
1.00
38.00
C


ATOM
1217
CG2
ILE
A
272
45.286
47.682
30.781
1.00
38.67
C


ATOM
1218
CD1
ILE
A
272
44.609
50.606
31.596
1.00
39.18
C


ATOM
1219
N
THR
A
273
48.685
47.061
30.143
1.00
38.73
N


ATOM
1220
CA
THR
A
273
49.184
45.999
29.287
1.00
38.01
C


ATOM
1221
C
THR
A
273
50.089
45.016
30.030
1.00
39.07
C


ATOM
1222
O
THR
A
273
49.935
43.802
29.896
1.00
38.49
O


ATOM
1223
CB
THR
A
273
49.959
46.577
28.091
1.00
37.70
C


ATOM
1224
OG1
THR
A
273
49.086
47.409
27.316
1.00
37.99
O


ATOM
1225
CG2
THR
A
273
50.494
45.458
27.212
1.00
36.21
C


ATOM
1226
N
ILE
A
274
51.045
45.537
30.797
1.00
38.89
N


ATOM
1227
CA
ILE
A
274
51.958
44.681
31.547
1.00
38.36
C


ATOM
1228
C
ILE
A
274
51.168
43.894
32.586
1.00
39.27
C


ATOM
1229
O
ILE
A
274
51.452
42.726
32.847
1.00
37.60
O


ATOM
1230
CB
ILE
A
274
53.040
45.507
32.277
1.00
38.10
C


ATOM
1231
CG1
ILE
A
274
53.911
46.250
31.259
1.00
38.10
C


ATOM
1232
CG2
ILE
A
274
53.887
44.588
33.163
1.00
37.28
C


ATOM
1233
CD1
ILE
A
274
54.879
47.247
31.888
1.00
37.22
C


ATOM
1234
N
GLY
A
275
50.177
44.547
33.182
1.00
39.95
N


ATOM
1235
CA
GLY
A
275
49.361
43.884
34.183
1.00
41.68
C


ATOM
1236
C
GLY
A
275
48.607
42.702
33.600
1.00
41.85
C


ATOM
1237
O
GLY
A
275
48.576
41.622
34.187
1.00
42.65
O


ATOM
1238
N
TRP
A
276
48.002
42.904
32.437
1.00
41.82
N


ATOM
1239
CA
TRP
A
276
47.242
41.847
31.785
1.00
42.57
C


ATOM
1240
C
TRP
A
276
48.144
40.658
31.487
1.00
43.64
C


ATOM
1241
O
TRP
A
276
47.707
39.505
31.545
1.00
42.42
O


ATOM
1242
CB
TRP
A
276
46.641
42.356
30.479
1.00
42.84
C


ATOM
1243
CG
TRP
A
276
45.770
41.356
29.809
1.00
43.77
C


ATOM
1244
CD1
TRP
A
276
44.431
41.168
30.008
1.00
44.10
C


ATOM
1245
CD2
TRP
A
276
46.170
40.390
28.829
1.00
44.12
C


ATOM
1246
NE1
TRP
A
276
43.972
40.146
29.209
1.00
43.95
N


ATOM
1247
CE2
TRP
A
276
45.018
39.651
28.475
1.00
44.37
C


ATOM
1248
CE3
TRP
A
276
47.391
40.077
28.216
1.00
44.62
C


ATOM
1249
CZ2
TRP
A
276
45.049
38.620
27.533
1.00
44.03
C


ATOM
1250
CZ3
TRP
A
276
47.424
39.049
27.278
1.00
44.60
C


ATOM
1251
CH2
TRP
A
276
46.256
38.333
26.946
1.00
44.88
C


ATOM
1252
N
ILE
A
277
49.401
40.945
31.159
1.00
43.10
N


ATOM
1253
CA
ILE
A
277
50.366
39.899
30.849
1.00
43.16
C


ATOM
1254
C
ILE
A
277
50.781
39.127
32.101
1.00
44.32
C


ATOM
1255
O
ILE
A
277
50.872
37.901
32.079
1.00
43.89
O


ATOM
1256
CB
ILE
A
277
51.619
40.490
30.160
1.00
42.16
C


ATOM
1257
CG1
ILE
A
277
51.249
40.985
28.759
1.00
40.86
C


ATOM
1258
CG2
ILE
A
277
52.724
39.444
30.084
1.00
41.70
C


ATOM
1259
CD1
ILE
A
277
52.370
41.677
28.027
1.00
39.92
C


ATOM
1260
N
ARG
A
278
51.029
39.845
33.190
1.00
45.51
N


ATOM
1261
CA
ARG
A
278
51.427
39.217
34.445
1.00
47.63
C


ATOM
1262
C
ARG
A
278
50.313
38.350
35.026
1.00
49.58
C


ATOM
1263
O
ARG
A
278
50.570
37.299
35.617
1.00
49.82
O


ATOM
1264
CB
ARG
A
278
51.815
40.287
35.466
1.00
46.39
C


ATOM
1265
CG
ARG
A
278
53.125
40.967
35.172
1.00
44.78
C


ATOM
1266
CD
ARG
A
278
54.320
40.087
35.522
1.00
43.71
C


ATOM
1267
NE
ARG
A
278
55.551
40.701
35.032
1.00
42.04
N


ATOM
1268
CZ
ARG
A
278
56.199
40.311
33.942
1.00
40.35
C


ATOM
1269
NH1
ARG
A
278
55.751
39.287
33.229
1.00
38.71
N


ATOM
1270
NH2
ARG
A
278
57.272
40.976
33.536
1.00
39.83
N


ATOM
1271
N
GLU
A
279
49.077
38.801
34.853
1.00
51.53
N


ATOM
1272
CA
GLU
A
279
47.908
38.094
35.359
1.00
53.86
C


ATOM
1273
C
GLU
A
279
47.596
36.819
34.575
1.00
53.60
C


ATOM
1274
O
GLU
A
279
47.070
35.854
35.127
1.00
53.73
O


ATOM
1275
CB
GLU
A
279
46.703
39.048
35.343
1.00
56.33
C


ATOM
1276
CG
GLU
A
279
45.337
38.391
35.440
1.00
61.52
C


ATOM
1277
CD
GLU
A
279
44.917
37.730
34.137
1.00
64.89
C


ATOM
1278
OE1
GLU
A
279
44.882
38.429
33.096
1.00
66.72
O


ATOM
1279
OE2
GLU
A
279
44.623
36.512
34.154
1.00
66.94
O


ATOM
1280
N
LYS
A
280
47.942
36.813
33.294
1.00
53.24
N


ATOM
1281
CA
LYS
A
280
47.672
35.671
32.432
1.00
53.14
C


ATOM
1282
C
LYS
A
280
48.863
34.724
32.294
1.00
52.81
C


ATOM
1283
O
LYE
A
280
48.685
33.537
32.029
1.00
52.92
O


ATOM
1284
CE
LYS
A
280
47.250
36.182
31.049
1.00
55.15
C


ATOM
1285
CG
LYS
A
280
46.435
35.209
30.199
1.00
57.74
C


ATOM
1286
CD
LYS
A
280
47.296
34.157
29.519
1.00
59.91
C


ATOM
1287
CE
LYS
A
280
46.441
33.170
28.715
1.00
61.61
C


ATOM
1288
NZ
LYS
A
280
45.645
33.828
27.634
1.00
61.74
N


ATOM
1289
N
TYR
A
281
50.074
35.241
32.490
1.00
51.29
N


ATOM
1290
CA
TYR
A
281
51.273
34.426
32.338
1.00
47.99
C


ATOM
1291
C
TYR
A
281
52.260
34.496
33.494
1.00
46.98
C


ATOM
1292
O
TYR
A
281
53.268
33.794
33.485
1.00
46.65
O


ATOM
1293
CB
TYR
A
281
52.016
34.835
31.066
1.00
47.79
C


ATOM
1294
CG
TYR
A
281
51.239
34.703
29.778
1.00
46.17
C


ATOM
1295
CD1
TYR
A
281
51.086
33.465
29.154
1.00
46.76
C


ATOM
1296
CD2
TYR
A
281
50.699
35.828
29.153
1.00
45.95
C


ATOM
1297
CE1
TYR
A
281
50.420
33.353
27.930
1.00
46.42
C


ATOM
1298
CE2
TYR
A
281
50.032
35.729
27.939
1.00
45.43
C


ATOM
1299
CZ
TYR
A
281
49.897
34.492
27.330
1.00
46.84
C


ATOM
1300
OH
TYR
A
281
49.255
34.401
26.118
1.00
47.66
O


ATOM
1301
N
GLY
A
282
51.990
35.336
34.484
1.00
46.78
N


ATOM
1302
CA
GLY
A
282
52.926
35.458
35.588
1.00
46.99
C


ATOM
1303
C
GLY
A
282
54.252
35.993
35.064
1.00
48.06
C


ATOM
1304
O
GLY
A
282
54.270
36.784
34.122
1.00
45.90
O


ATOM
1305
N
ASP
A
283
55.362
35.566
35.660
1.00
49.43
N


ATOM
1306
CA
ASP
A
283
56.682
36.019
35.223
1.00
50.90
C


ATOM
1307
C
ASP
A
283
57.290
35.115
34.146
1.00
50.49
C


ATOM
1308
O
ASP
A
283
58.501
35.117
33.940
1.00
51.46
O


ATOM
1309
CB
ASP
A
283
57.637
36.099
36.418
1.00
52.54
C


ATOM
1310
CG
ASP
A
283
57.266
37.208
37.395
1.00
56.76
C


ATOM
1311
OD1
ASP
A
283
57.213
38.387
36.974
1.00
57.47
O


ATOM
1312
OD2
ASP
A
283
57.034
36.903
38.587
1.00
57.67
O


ATOM
1313
N
LYS
A
284
56.452
34.354
33.450
1.00
50.15
N


ATOM
1314
CA
LYS
A
284
56.935
33.443
32.412
1.00
50.38
C


ATOM
1315
C
LYS
A
284
57.073
34.116
31.052
1.00
48.98
C


ATOM
1316
O
LYS
A
284
57.780
33.632
30.168
1.00
48.72
O


ATOM
1317
CB
LYS
A
284
56.003
32.229
32.297
1.00
53.78
C


ATOM
1318
CG
LYS
A
284
56.138
31.226
33.449
1.00
58.18
C


ATOM
1319
CD
LYS
A
284
55.845
31.868
34.802
1.00
60.71
C


ATOM
1320
CE
LYS
A
284
56.104
30.899
35.950
1.00
63.62
C


ATOM
1321
NZ
LYS
A
284
55.874
31.551
37.276
1.00
64.97
N


ATOM
1322
N
VAL
A
285
56.374
35.227
30.880
1.00
46.54
N


ATOM
1323
CA
VAL
A
285
56.445
35.969
29.634
1.00
43.33
C


ATOM
1324
C
VAL
A
285
57.170
37.270
29.950
1.00
41.39
C


ATOM
1325
O
VAL
A
285
56.759
38.019
30.840
1.00
40.81
O


ATOM
1326
CB
VAL
A
285
55.039
36.252
29.086
1.00
43.01
C


ATOM
1327
CG1
VAL
A
285
55.122
37.183
27.887
1.00
42.67
C


ATOM
1328
CG2
VAL
A
285
54.380
34.936
28.690
1.00
42.46
C


ATOM
1329
N
LYS
A
286
58.261
37.520
29.234
1.00
38.50
N


ATOM
1330
CA
LYS
A
286
59.060
38.720
29.451
1.00
36.37
C


ATOM
1331
C
LYS
A
286
58.594
39.861
28.556
1.00
34.87
C


ATOM
1332
O
LYS
A
286
58.383
39.680
27.359
1.00
34.64
O


ATOM
1333
CB
LYS
A
286
60.541
38.417
29.193
1.00
34.83
C


ATOM
1334
CG
LYS
A
286
61.077
37.232
29.993
1.00
35.06
C


ATOM
1335
CD
LYS
A
286
60.840
37.401
31.495
1.00
34.44
C


ATOM
1336
CE
LYS
A
286
61.373
36.207
32.282
1.00
35.15
C


ATOM
1337
NZ
LYS
A
286
61.155
36.341
33.759
1.00
35.87
N


ATOM
1338
N
VAL
A
287
58.437
41.042
29.139
1.00
33.15
N


ATOM
1339
CA
VAL
A
287
57.979
42.185
28.367
1.00
33.28
C


ATOM
1340
C
VAL
A
287
58.706
43.480
28.730
1.00
32.69
C


ATOM
1341
O
VAL
A
287
58.745
43.886
29.892
1.00
32.80
O


ATOM
1342
CB
VAL
A
287
56.437
42.379
28.543
1.00
32.82
C


ATOM
1343
CG1
VAL
A
287
56.083
42.447
30.020
1.00
32.50
C


ATOM
1344
CG2
VAL
A
287
55.978
43.644
27.843
1.00
34.03
C


ATOM
1345
N
GLY
A
288
59.295
44.113
27.722
1.00
33.35
N


ATOM
1346
CA
GLY
A
288
59.983
45.373
27.935
1.00
32.17
C


ATOM
1347
C
GLY
A
288
58.966
46.477
27.731
1.00
32.40
C


ATOM
1348
O
GLY
A
288
57.953
46.263
27.056
1.00
33.04
O


ATOM
1349
N
ALA
A
289
59.221
47.646
28.309
1.00
31.58
N


ATOM
1350
CA
ALA
A
289
58.309
48.783
28.190
1.00
32.03
C


ATOM
1351
C
ALA
A
289
59.088
50.084
27.944
1.00
33.08
C


ATOM
1352
O
ALA
A
289
60.304
50.126
28.138
1.00
32.71
O


ATOM
1353
CB
ALA
A
289
57.463
48.899
29.464
1.00
31.09
C


ATOM
1354
N
GLY
A
290
58.384
51.135
27.519
1.00
32.95
N


ATOM
1355
CA
GLY
A
290
59.027
52.415
27.242
1.00
33.02
C


ATOM
1356
C
GLY
A
290
58.397
53.107
26.039
1.00
33.75
C


ATOM
1357
O
GLY
A
290
57.396
52.622
25.517
1.00
34.16
O


ATOM
1358
N
ASN
A
291
58.975
54.210
25.560
1.00
32.53
N


ATOM
1359
CA
ASN
A
291
60.199
54.804
26.095
1.00
31.60
C


ATOM
1360
C
ASN
A
291
59.964
55.899
27.134
1.00
31.33
C


ATOM
1361
O
ASN
A
291
58.936
56.577
27.123
1.00
30.56
O


ATOM
1362
CB
ASN
A
291
61.019
55.405
24.943
1.00
30.32
C


ATOM
1363
CG
ASN
A
291
61.501
54.354
23.958
1.00
31.30
C


ATOM
1364
OD1
ASN
A
291
60.981
53.240
23.923
1.00
31.67
O


ATOM
1365
ND2
ASN
A
291
62.495
54.708
23.147
1.00
28.26
N


ATOM
1366
N
ILE
A
292
60.933
56.052
28.033
1.00
30.09
N


ATOM
1367
CA
ILE
A
292
60.904
57.090
29.053
1.00
30.04
C


ATOM
1368
C
ILE
A
292
62.276
57.774
29.013
1.00
30.43
C


ATOM
1369
O
ILE
A
292
63.205
57.266
28.375
1.00
30.27
O


ATOM
1370
CB
ILE
A
292
60.583
56.526
30.484
1.00
29.76
C


ATOM
1371
CG1
ILE
A
292
61.381
55.253
30.787
1.00
30.31
C


ATOM
1372
CG2
ILE
A
292
59.105
56.229
30.588
1.00
30.24
C


ATOM
1373
CD1
ILE
A
292
62.856
55.473
31.028
1.00
29.06
C


ATOM
1374
N
VAL
A
293
62.409
58.924
29.668
1.00
30.29
N


ATOM
1375
CA
VAL
A
293
63.680
59.640
29.641
1.00
29.96
C


ATOM
1376
C
VAL
A
293
64.153
60.149
30.991
1.00
30.54
C


ATOM
1377
O
VAL
A
293
65.175
60.829
31.068
1.00
30.92
O


ATOM
1378
CB
VAL
A
293
63.612
60.839
28.680
1.00
29.70
C


ATOM
1379
CG1
VAL
A
293
63.492
60.351
27.238
1.00
27.77
C


ATOM
1380
CG2
VAL
A
293
62.418
61.717
29.045
1.00
28.93
C


ATOM
1381
N
ASP
A
294
63.414
59.841
32.053
1.00
29.98
N


ATOM
1382
CA
ASP
A
294
63.822
60.282
33.384
1.00
30.26
C


ATOM
1383
C
ASP
A
294
63.503
59.249
34.465
1.00
29.51
C


ATOM
1384
O
ASP
A
294
62.859
58.237
34.201
1.00
28.45
O


ATOM
1385
CB
ASP
A
294
63.184
61.645
33.733
1.00
29.22
C


ATOM
1386
CG
ASP
A
294
61.667
61.579
33.893
1.00
30.83
C


ATOM
1387
OD1
ASP
A
294
61.069
60.517
33.634
1.00
30.38
O


ATOM
1388
OD2
ASP
A
294
61.065
62.609
34.277
1.00
31.14
O


ATOM
1389
N
GLY
A
295
63.970
59.516
35.680
1.00
30.57
N


ATOM
1390
CA
GLY
A
295
63.739
58.613
36.793
1.00
32.07
C


ATOM
1391
C
GLY
A
295
62.278
58.313
37.065
1.00
33.84
C


ATOM
1392
O
GLY
A
295
61.928
57.165
37.359
1.00
33.24
O


ATOM
1393
N
GLU
A
296
61.426
59.337
36.986
1.00
35.06
N


ATOM
1394
CA
GLU
A
296
59.986
59.172
37.221
1.00
36.02
C


ATOM
1395
C
GLU
A
296
59.400
58.100
36.315
1.00
34.20
C


ATOM
1396
O
GLU
A
296
58.739
57.179
36.775
1.00
34.47
O


ATOM
1397
CB
GLU
A
296
59.222
60.473
36.938
1.00
39.08
C


ATOM
1398
CG
GLU
A
296
59.026
61.420
38.101
1.00
44.63
C


ATOM
1399
CD
GLU
A
296
57.731
62.229
37.955
1.00
49.36
C


ATOM
1400
OE1
GLU
A
296
57.490
62.820
36.868
1.00
49.76
O


ATOM
1401
OE2
GLU
A
296
56.946
62.266
38.930
1.00
52.97
O


ATOM
1402
N
GLY
A
297
59.634
58.251
35.015
1.00
34.02
N


ATOM
1403
CA
GLY
A
297
59.120
57.307
34.040
1.00
32.68
C


ATOM
1404
C
GLY
A
297
59.651
55.901
34.239
1.00
32.72
C


ATOM
1405
O
GLY
A
297
58.912
54.930
34.091
1.00
33.28
O


ATOM
1406
N
PHE
A
298
60.937
55.791
34.558
1.00
31.86
N


ATOM
1407
CA
PHE
A
298
61.557
54.490
34.793
1.00
32.60
C


ATOM
1408
C
PHE
A
298
60.832
53.804
35.946
1.00
33.15
C


ATOM
1409
O
PHE
A
298
60.382
52.668
35.829
1.00
33.25
O


ATOM
1410
CB
PHE
A
298
63.029
54.656
35.183
1.00
30.95
C


ATOM
1411
CG
PHE
A
298
63.635
53.414
35.773
1.00
31.63
C


ATOM
1412
CD1
PHE
A
298
64.151
52.414
34.953
1.00
31.00
C


ATOM
1413
CD2
PHE
A
298
63.622
53.209
37.149
1.00
31.36
C


ATOM
1414
CE1
PHE
A
298
64.641
51.221
35.498
1.00
30.09
C


ATOM
1415
CE2
PHE
A
298
64.108
52.023
37.701
1.00
30.73
C


ATOM
1416
CZ
PHE
A
298
64.616
51.028
36.871
1.00
30.06
C


ATOM
1417
N
ARG
A
299
60.743
54.528
37.057
1.00
33.22
N


ATOM
1418
CA
ARG
A
299
60.111
54.074
38.291
1.00
34.33
C


ATOM
1419
C
ARG
A
299
58.671
53.593
38.074
1.00
34.12
C


ATOM
1420
O
ARG
A
299
58.252
52.577
38.635
1.00
32.73
O


ATOM
1421
CB
ARG
A
299
60.161
55.228
39.300
1.00
35.94
C


ATOM
1422
CG
ARG
A
299
59.224
55.130
40.491
1.00
41.25
C


ATOM
1423
CD
ARG
A
299
59.892
54.483
41.682
1.00
42.59
C


ATOM
1424
NE
ARG
A
299
61.160
55.121
42.041
1.00
44.25
N


ATOM
1425
CZ
ARG
A
299
61.927
54.709
43.050
1.00
44.43
C


ATOM
1426
NH1
ARG
A
299
61.544
53.677
43.791
1.00
42.61
N


ATOM
1427
NH2
ARG
A
299
63.085
55.304
43.304
1.00
44.39
N


ATOM
1428
N
TYR
A
300
57.920
54.318
37.255
1.00
32.22
N


ATOM
1429
CA
TYR
A
300
56.540
53.948
36.981
1.00
32.60
C


ATOM
1430
C
TYR
A
300
56.453
52.607
36.251
1.00
33.71
C


ATOM
1431
O
TYR
A
300
55.643
51.750
36.606
1.00
34.20
O


ATOM
1432
CB
TYR
A
300
55.855
55.027
36.143
1.00
32.42
C


ATOM
1433
CG
TYR
A
300
54.398
54.736
35.864
1.00
32.17
C


ATOM
1434
CD1
TYR
A
300
53.418
54.973
36.828
1.00
31.34
C


ATOM
1435
CD2
TYR
A
300
54.002
54.216
34.637
1.00
30.83
C


ATOM
1436
CE1
TYR
A
300
52.073
54.700
36.568
1.00
30.71
C


ATOM
1437
CE2
TYR
A
300
52.670
53.942
34.369
1.00
32.95
C


ATOM
1438
CZ
TYR
A
300
51.712
54.186
35.334
1.00
31.71
C


ATOM
1439
OH
TYR
A
300
50.396
53.929
35.041
1.00
31.68
O


ATOM
1440
N
LEU
A
301
57.275
52.429
35.222
1.00
32.89
N


ATOM
1441
CA
LEU
A
301
57.257
51.180
34.477
1.00
32.98
C


ATOM
1442
C
LEU
A
301
57.881
50.045
35.304
1.00
33.13
C


ATOM
1443
O
LEU
A
301
57.547
48.878
35.114
1.00
33.27
O


ATOM
1444
CB
LEU
A
301
57.992
51.349
33.140
1.00
31.76
C


ATOM
1445
CG
LEU
A
301
57.342
52.341
32.160
1.00
31.64
C


ATOM
1446
CD1
LEU
A
301
58.174
52.459
30.891
1.00
29.55
C


ATOM
1447
CD2
LEU
A
301
55.928
51.870
31.823
1.00
30.86
C


ATOM
1448
N
ALA
A
302
58.780
50.390
36.220
1.00
32.34
N


ATOM
1449
CA
ALA
A
302
59.418
49.385
37.066
1.00
34.28
C


ATOM
1450
C
ALA
A
302
58.355
48.806
38.008
1.00
34.11
C


ATOM
1451
O
ALA
A
302
58.169
47.590
38.082
1.00
34.00
O


ATOM
1452
CB
ALA
A
302
60.563
50.012
37.866
1.00
31.06
C


ATOM
1453
N
ASP
A
303
57.652
49.686
38.711
1.0.0
34.91
N


ATOM
1454
CA
ASP
A
303
56.595
49.262
39.618
1.00
35.64
C


ATOM
1455
C
ASP
A
303
55.485
48.552
38.846
1.00
36.85
C


ATOM
1456
O
ASP
A
303
54.761
47.737
39.408
1.00
37.85
O


ATOM
1457
CB
ASP
A
303
56.008
50.458
40.365
1.00
35.88
C


ATOM
1458
CG
ASP
A
303
56.956
51.022
41.398
1.00
38.13
C


ATOM
1459
OD1
ASP
A
303
57.843
50.276
41.863
1.00
40.12
O


ATOM
1460
OD2
ASP
A
303
56.800
52.205
41.764
1.00
40.53
O


ATOM
1461
N
ALA
A
304
55.356
48.859
37.557
1.00
36.62
N


ATOM
1462
CA
ALA
A
304
54.331
48.233
36.725
1.00
36.26
C


ATOM
1463
C
ALA
A
304
54.719
46.802
36.343
1.00
36.18
C


ATOM
1464
O
ALA
A
304
53.876
46.035
35.868
1.00
35.97
O


ATOM
1465
CB
ALA
A
304
54.095
49.063
35.466
1.00
35.66
C


ATOM
1466
N
GLY
A
305
55.994
46.454
36.519
1.00
35.62
N


ATOM
1467
CA
GLY
A
305
56.440
45.102
36.212
1.00
33.54
C


ATOM
1468
C
GLY
A
305
57.266
44.840
34.964
1.00
34.83
C


ATOM
1469
O
GLY
A
305
57.559
43.678
34.654
1.00
34.47
O


ATOM
1470
N
ALA
A
306
57.648
45.890
34.239
1.00
34.51
N


ATOM
1471
CA
ALA
A
306
58.448
45.718
33.022
1.00
34.01
C


ATOM
1472
C
ALA
A
306
59.718
44.902
33.304
1.00
33.98
C


ATOM
1473
O
ALA
A
306
60.302
45.017
34.378
1.00
33.26
O


ATOM
1474
CB
ALA
A
306
58.825
47.084
32.450
1.00
33.19
C


ATOM
1475
N
ASP
A
307
60.137
44.085
32.339
1.00
34.27
N


ATOM
1476
CA
ASP
A
307
61.341
43.257
32.489
1.00
35.04
C


ATOM
1477
C
ASP
A
307
62.605
44.014
32.075
1.00
34.78
C


ATOM
1478
O
ASP
A
307
63.716
43.658
32.462
1.00
35.12
O


ATOM
1479
CE
ASP
A
307
61.191
41.967
31.684
1.00
34.06
C


ATOM
1480
CG
ASP
A
307
60.205
41.010
32.322
1.00
35.84
C


ATOM
1481
OD1
ASP
A
307
60.511
40.519
33.429
1.00
33.94
O


ATOM
1482
OD2
ASP
A
307
59.127
40.764
31.733
1.00
35.52
O


ATOM
1483
N
PHE
A
308
62.418
45.042
31.255
1.00
33.72
N


ATOM
1484
CA
PHE
A
308
63.499
45.920
30.838
1.00
32.62
C


ATOM
1485
C
PHE
A
308
62.811
47.210
30.396
1.00
32.76
C


ATOM
1486
O
PHE
A
308
61.660
47.194
29.961
1.00
32.31
O


ATOM
1487
CE
PHE
A
308
64.389
45.282
29.751
1.00
30.88
C


ATOM
1488
CG
PHE
A
308
63.833
45.325
28.351
1.00
31.29
C


ATOM
1489
CD1
PHE
A
308
63.823
46.514
27.622
1.00
30.95
C


ATOM
1490
CD2
PHE
A
308
63.399
44.152
27.729
1.00
31.69
C


ATOM
1491
CE1
PHE
A
308
63.396
46.536
26.289
1.00
31.24
C


ATOM
1492
CE2
PHE
A
308
62.968
44.158
26.393
1.00
32.80
C


ATOM
1493
CZ
PHE
A
308
62.968
45.356
25.671
1.00
33.19
C


ATOM
1494
N
ILE
A
309
63.499
48.330
30.558
1.00
32.53
N


ATOM
1495
CA
ILE
A
309
62.919
49.618
30.221
1.00
31.47
C


ATOM
1496
C
ILE
A
309
63.723
50.323
29.138
1.00
31.48
C


ATOM
1497
O
ILE
A
309
64.952
50.428
29.228
1.00
29.64
O


ATOM
1498
CB
ILE
A
309
62.809
50.477
31.502
1.00
31.63
C


ATOM
1499
CG1
ILE
A
309
61.767
49.835
32.431
1.00
29.83
C


ATOM
1500
CG2
ILE
A
309
62.467
51.924
31.160
1.00
30.76
C


ATOM
1501
CD1
ILE
A
309
61.696
50.434
33.823
1.00
30.01
C


ATOM
1502
N
LYS
A
310
63.016
50.794
28.109
1.00
30.52
N


ATOM
1503
CA
LYS
A
310
63.649
51.456
26.977
1.00
30.74
C


ATOM
1504
C
LYS
A
310
63.730
52.975
27.166
1.00
30.46
C


ATOM
1505
O
LYS
A
310
62.746
53.630
27.515
1.00
30.84
O


ATOM
1506
CE
LYS
A
310
62.899
51.092
25.693
1.00
30.85
C


ATOM
1507
CG
LYS
A
310
63.787
50.985
24.461
1.00
30.94
C


ATOM
1508
CD
LYS
A
310
63.396
49.797
23.572
1.00
29.84
C


ATOM
1509
CE
LYS
A
310
62.017
49.979
22.964
1.00
28.94
C


ATOM
1510
NZ
LYS
A
310
61.928
51.268
22.219
1.00
28.29
N


ATOM
1511
N
ILE
A
311
64.917
53.517
26.920
1.00
29.41
N


ATOM
1512
CA
ILE
A
311
65.197
54.943
27.097
1.00
29.44
C


ATOM
1513
C
ILE
A
311
65.362
55.711
25.796
1.00
29.18
C


ATOM
1514
O
ILE
A
311
66.100
55.288
24.908
1.00
28.56
O


ATOM
1515
CB
ILE
A
311
66.517
55.158
27.887
1.00
28.45
C


ATOM
1516
CG1
ILE
A
311
66.498
54.353
29.186
1.00
27.16
C


ATOM
1517
CG2
ILE
A
311
66.721
56.653
28.178
1.00
25.82
C


ATOM
1518
CD1
ILE
A
311
67.864
54.280
29.857
1.00
27.18
C


ATOM
1519
N
GLY
A
312
64.690
56.852
25.692
1.00
30.57
N


ATOM
1520
CA
GLY
A
312
64.856
57.660
24.502
1.00
30.97
C


ATOM
1521
C
GLY
A
312
63.637
58.202
23.798
1.00
33.02
C


ATOM
1522
O
GLY
A
312
62.739
57.460
23.412
1.00
32.51
O


ATOM
1523
N
ILE
A
313
63.622
59.519
23.631
1.00
35.45
N


ATOM
1524
CA
ILE
A
313
62.558
60.210
22.920
1.00
37.38
C


ATOM
1525
C
ILE
A
313
63.194
61.380
22.181
1.00
40.19
C


ATOM
1526
O
ILE
A
313
63.759
62.280
22.807
1.00
39.32
O


ATOM
1527
CE
ILE
A
313
61.484
60.766
23.865
1.00
36.69
C


ATOM
1528
CG1
ILE
A
313
60.825
59.625
24.646
1.00
37.09
C


ATOM
1529
CG2
ILE
A
313
60.437
61.517
23.053
1.00
36.17
C


ATOM
1530
CD1
ILE
A
313
59.810
60.097
25.666
1.00
34.32
C


ATOM
1531
N
GLY
A
314
63.121
61.350
20.853
1.00
43.35
N


ATOM
1532
CA
GLY
A
314
63.682
62.424
20.055
1.00
47.92
C


ATOM
1533
C
GLY
A
314
65.013
62.127
19.386
1.00
51.41
C


ATOM
1534
O
GLY
A
314
65.318
62.690
18.333
1.00
52.28
O


ATOM
1535
N
GLY
A
315
65.804
61.244
19.990
1.00
53.66
N


ATOM
1536
CA
GLY
A
315
67.109
60.902
19.443
1.00
55.96
C


ATOM
1537
C
GLY
A
315
67.151
60.218
18.085
1.00
57.72
C


ATOM
1538
O
GLY
A
315
68.050
60.499
17.288
1.00
58.05
O


ATOM
1539
N
GLY
A
316
66.202
59.320
17.818
1.00
58.68
N


ATOM
1540
CA
GLY
A
316
66.174
58.615
16.542
1.00
60.38
C


ATOM
1541
C
GLY
A
316
66.578
59.446
15.330
1.00
61.63
C


ATOM
1542
O
GLY
A
316
66.212
60.617
15.216
1.00
61.39
O


ATOM
1543
N
SER
A
317
67.328
58.838
14.415
1.00
63.21
N


ATOM
1544
CA
SER
A
317
67.786
59.529
13.211
1.00
64.85
C


ATOM
1545
C
SER
A
317
66.626
59.987
12.331
1.00
66.57
C


ATOM
1546
O
SER
A
317
66.711
61.022
11.667
1.00
66.58
O


ATOM
1547
CB
SER
A
317
68.714
58.621
12.395
1.00
64.42
C


ATOM
1548
OG
SER
A
317
68.001
57.556
11.787
1.00
62.55
O


ATOM
1549
N
ILE
A
318
65.547
59.212
12.324
1.00
68.56
N


ATOM
1550
CA
ILE
A
318
64.376
59.542
11.517
1.00
71.22
C


ATOM
1551
C
ILE
A
318
63.259
60.192
12.327
1.00
72.91
C


ATOM
1552
O
ILE
A
318
62.098
60.185
11.913
1.00
73.31
O


ATOM
1553
CB
ILE
A
318
63.815
58.286
10.805
1.00
71.18
C


ATOM
1554
CG1
ILE
A
318
63.983
57.051
11.698
1.00
71.48
C


ATOM
1555
CG2
ILE
A
318
64.529
58.080
9.475
1.00
70.96
C


ATOM
1556
CD1
ILE
A
318
63.326
57.162
13.049
1.00
70.32
C


ATOM
1557
N
CYS
A
319
63.617
60.755
13.478
1.00
75.09
N


ATOM
1558
CA
CYS
A
319
62.651
61.417
14.350
1.00
77.73
C


ATOM
1559
C
CYS
A
319
62.958
62.911
14.448
1.00
78.61
C


ATOM
1560
O
CYS
A
319
64.091
63.300
14.731
1.00
78.56
O


ATOM
1561
CB
CYS
A
319
62.686
60.789
15.746
1.00
78.48
C


ATOM
1562
SG
CYS
A
319
61.465
61.464
16.899
1.00
81.82
S


ATOM
1563
N
ILE
A
320
61.947
63.743
14.214
1.00
79.90
N


ATOM
1564
CA
ILE
A
320
62.123
65.194
14.271
1.00
81.47
C


ATOM
1565
C
ILE
A
320
61.255
65.828
15.362
1.00
82.10
C


ATOM
1566
O
ILE
A
320
60.147
66.298
15.096
1.00
82.35
O


ATOM
1567
CB
ILE
A
320
61.776
65.850
12.911
1.00
81.84
C


ATOM
1568
CG1
ILE
A
320
62.556
65.162
11.787
1.00
82.02
C


ATOM
1569
CG2
ILE
A
320
62.121
67.340
12.946
1.00
82.15
C


ATOM
1570
CD1
ILE
A
320
62.212
65.669
10.396
1.00
82.11
C


ATOM
1571
N
THR
A
321
61.775
65.841
16.587
1.00
82.35
N


ATOM
1572
CA
THR
A
321
61.072
66.403
17.738
1.00
82.60
C


ATOM
1573
C
THR
A
321
60.461
67.782
17.469
1.00
82.30
C


ATOM
1574
O
THR
A
321
59.253
67.975
17.619
1.00
81.76
O


ATOM
1575
CB
THR
A
321
62.019
66.527
18.949
1.00
82.94
C


ATOM
1576
OG1
THR
A
321
62.607
65.250
19.232
1.00
83.54
O


ATOM
1577
CG2
THR
A
321
61.257
67.016
20.167
1.00
82.53
C


ATOM
1578
N
ARG
A
322
61.306
68.735
17.083
1.00
82.27
N


ATOM
1579
CA
ARG
A
322
60.863
70.099
16.800
1.00
82.39
C


ATOM
1580
C
ARG
A
322
59.651
70.172
15.878
1.00
81.93
C


ATOM
1581
O
ARG
A
322
58.611
70.714
16.254
1.00
81.88
O


ATOM
1582
CB
ARG
A
322
62.005
70.915
16.191
1.00
83.09
C


ATOM
1583
CG
ARG
A
322
63.009
71.456
17.199
1.00
83.95
C


ATOM
1584
CD
ARG
A
322
63.963
72.423
16.516
1.00
84.72
C


ATOM
1585
NE
ARG
A
322
64.729
73.227
17.464
1.00
85.49
N


ATOM
1586
CZ
ARG
A
322
65.543
74.218
17.108
1.00
85.83
C


ATOM
1587
NH1
ARG
A
322
65.696
74.526
15.824
1.00
85.76
N


ATOM
1588
NH2
ARG
A
322
66.203
74.903
18.032
1.00
85.80
N


ATOM
1589
N
GLU
A
323
59.791
69.634
14.668
1.00
81.06
N


ATOM
1590
CA
GLU
A
323
58.699
69.643
13.697
1.00
80.15
C


ATOM
1591
C
GLU
A
323
57.547
68.739
14.131
1.00
78.66
C


ATOM
1592
O
GLU
A
323
56.713
68.343
13.313
1.00
78.92
O


ATOM
1593
CB
GLU
A
323
59.205
69.192
12.324
1.00
81.16
C


ATOM
1594
CG
GLU
A
323
60.194
70.145
11.677
1.00
83.13
C


ATOM
1595
CD
GLU
A
323
60.632
69.676
10.302
1.00
84.05
C


ATOM
1596
OE1
GLU
A
323
61.266
68.602
10.212
1.00
84.52
O


ATOM
1597
OE2
GLU
A
323
60.337
70.381
9.312
1.00
84.85
O


ATOM
1598
N
GLN
A
324
57.500
68.420
15.421
1.00
76.17
N


ATOM
1599
CA
GLN
A
324
56.451
67.559
15.947
1.00
73.65
C


ATOM
1600
C
GLN
A
324
55.768
68.105
17.202
1.00
70.58
C


ATOM
1601
O
GLN
A
324
55.066
69.117
17.147
1.00
70.75
O


ATOM
1602
CB
GLN
A
324
57.019
66.160
16.218
1.00
76.03
C


ATOM
1603
CG
GLN
A
324
57.091
65.267
14.980
1.00
78.70
C


ATOM
1604
CD
GLN
A
324
58.247
64.274
15.029
1.00
80.71
C


ATOM
1605
OE1
GLN
A
324
58.488
63.623
16.050
1.00
81.60
O


ATOM
1606
NE2
GLN
A
324
58.964
64.150
13.913
1.00
81.50
N


ATOM
1607
N
LYS
A
325
55.987
67.439
18.331
1.00
66.07
N


ATOM
1608
CA
LYS
A
325
55.358
67.823
19.588
1.00
61.45
C


ATOM
1609
C
LYS
A
325
56.260
68.589
20.549
1.00
57.60
C


ATOM
1610
O
LYS
A
325
55.778
69.239
21.479
1.00
56.87
O


ATOM
1611
CB
LYS
A
325
54.817
66.566
20.274
1.00
62.25
C


ATOM
1612
CG
LYS
A
325
53.832
65.795
19.402
1.00
63.17
C


ATOM
1613
CD
LYS
A
325
53.889
64.295
19.660
1.00
63.20
C


ATOM
1614
CE
LYS
A
325
53.295
63.928
20.999
1.00
62.14
C


ATOM
1615
NZ
LYS
A
325
51.844
64.232
21.055
1.00
62.08
N


ATOM
1616
N
GLY
A
326
57.566
68.515
20.335
1.00
52.89
N


ATOM
1617
CA
GLY
A
326
58.468
69.220
21.222
1.00
48.72
C


ATOM
1618
C
GLY
A
326
58.716
68.493
22.534
1.00
45.75
C


ATOM
1619
O
GLY
A
326
58.952
69.129
23.557
1.00
44.02
O


ATOM
1620
N
ILE
A
327
58.639
67.164
22.510
1.00
42.92
N


ATOM
1621
CA
ILE
A
327
58.901
66.362
23.698
1.00
41.83
C


ATOM
1622
C
ILE
A
327
60.222
65.632
23.463
1.00
40.05
C


ATOM
1623
O
ILE
A
327
60.573
65.316
22.329
1.00
39.48
O


ATOM
1624
CB
ILE
A
327
57.777
65.310
23.974
1.00
42.64
C


ATOM
1625
CG1
ILE
A
327
57.577
64.408
22.754
1.00
44.04
C


ATOM
1626
CG2
ILE
A
327
56.470
66.012
24.333
1.00
42.95
C


ATOM
1627
CD1
ILE
A
327
56.582
63.261
22.982
1.00
46.03
C


ATOM
1628
N
GLY
A
328
60.964
65.374
24.528
1.00
38.80
N


ATOM
1629
CA
GLY
A
328
62.223
64.681
24.360
1.00
37.90
C


ATOM
1630
C
GLY
A
328
63.289
65.133
25.334
1.00
36.87
C


ATOM
1631
O
GLY
A
328
63.041
65.973
26.206
1.00
35.37
O


ATOM
1632
N
ARG
A
329
64.484
64.573
25.175
1.00
34.44
N


ATOM
1633
CA
ARG
A
329
65.602
64.901
26.042
1.00
32.91
C


ATOM
1634
C
ARG
A
329
66.872
64.373
25.389
1.00
32.38
C


ATOM
1635
O
ARG
A
329
66.826
63.365
24.689
1.00
32.32
O


ATOM
1636
CS
ARG
A
329
65.395
64.239
27.410
1.00
32.23
C


ATOM
1637
CG
ARG
A
329
66.233
64.822
28.530
1.00
31.22
C


ATOM
1638
CD
ARG
A
329
66.062
64.023
29.813
1.00
31.90
C


ATOM
1639
NE
ARG
A
329
66.413
64.807
30.991
1.00
30.70
N


ATOM
1640
CZ
ARG
A
329
66.373
64.344
32.235
1.00
33.01
C


ATOM
1641
NH1
ARG
A
329
66.002
63.093
32.469
1.00
32.08
N


ATOM
1642
NH2
ARG
A
329
66.692
65.139
33.249
1.00
32.28
N


ATOM
1643
N
GLY
A
330
67.999
65.058
25.592
1.00
31.61
N


ATOM
1644
CA
GLY
A
330
69.245
64.582
25.012
1.00
29.56
C


ATOM
1645
C
GLY
A
330
69.431
63.148
25.481
1.00
29.63
C


ATOM
1646
O
GLY
A
330
69.267
62.861
26.666
1.00
29.00
O


ATOM
1647
N
GLN
A
331
69.775
62.253
24.563
1.00
29.35
N


ATOM
1648
CA
GLN
A
331
69.936
60.839
24.880
1.00
29.79
C


ATOM
1649
C
GLN
A
331
70.913
60.538
26.021
1.00
30.69
C


ATOM
1650
O
GLN
A
331
70.644
59.654
26.840
1.00
30.62
O


ATOM
1651
CB
GLN
A
331
70.348
60.057
23.625
1.00
29.75
C


ATOM
1652
CG
GLN
A
331
70.254
58.531
23.781
1.00
31.50
C


ATOM
1653
CD
GLN
A
331
68.822
58.039
23.959
1.00
33.75
C


ATOM
1654
OE1
GLN
A
331
68.590
56.903
24.387
1.00
35.72
O


ATOM
1655
NE2
GLN
A
331
67.858
58.885
23.623
1.00
30.84
N


ATOM
1656
N
ALA
A
332
72.039
61.254
26.078
1.00
28.60
N


ATOM
1657
CA
ALA
A
332
73.017
61.020
27.142
1.00
29.13
C


ATOM
1658
C
ALA
A
332
72.422
61.330
28.513
1.00
28.73
C


ATOM
1659
O
ALA
A
332
72.495
60.513
29.437
1.00
28.92
O


ATOM
1660
CB
ALA
A
332
74.281
61.873
26.912
1.00
29.21
C


ATOM
1661
N
THR
A
333
71.833
62.513
28.639
1.00
26.69
N


ATOM
1662
CA
THR
A
333
71.229
62.933
29.893
1.00
27.66
C


ATOM
1663
C
THR
A
333
70.126
61.968
30.321
1.00
27.96
C


ATOM
1664
O
THR
A
333
70.017
61.619
31.496
1.00
27.38
O


ATOM
1665
CB
THR
A
333
70.643
64.347
29.770
1.00
28.02
C


ATOM
1666
0G1
THR
A
333
71.681
65.249
29.359
1.00
27.47
O


ATOM
1667
CG2
THR
A
333
70.066
64.804
31.121
1.00
28.00
C


ATOM
1668
N
ALA
A
334
69.317
61.534
29.361
1.00
27.55
N


ATOM
1669
CA
ALA
A
334
68.236
60.596
29.642
1.00
27.85
C


ATOM
1670
C
ALA
A
334
68.795
59.294
30.219
1.00
27.98
C


ATOM
1671
O
ALA
A
334
68.318
58.792
31.238
1.00
28.76
O


ATOM
1672
CB
ALA
A
334
67.448
60.309
28.362
1.00
26.67
C


ATOM
1673
N
VAL
A
335
69.809
58.745
29.562
1.00
29.11
N


ATOM
1674
CA
VAL
A
335
70.416
57.499
30.011
1.00
29.37
C


ATOM
1675
C
VAL
A
335
71.009
57.652
31.411
1.00
29.55
C


ATOM
1676
O
VAL
A
335
70.721
56.856
32.311
1.00
28.49
O


ATOM
1677
CB
VAL
A
335
71.524
57.039
29.033
1.00
30.52
C


ATOM
1678
CG1
VAL
A
335
72.291
55.859
29.622
1.00
31.70
C


ATOM
1679
CG2
VAL
A
335
70.904
56.644
27.701
1.00
30.54
C


ATOM
1680
N
ILE
A
336
71.823
58.686
31.592
1.00
29.23
N


ATOM
1681
CA
ILE
A
336
72.464
58.938
32.878
1.00
28.94
C


ATOM
1682
C
ILE
A
336
71.450
59.063
34.013
1.00
30.36
C


ATOM
1683
O
ILE
A
336
71.652
58.525
35.109
1.00
28.57
O


ATOM
1684
CS
ILE
A
336
73.325
60.216
32.813
1.00
28.69
C


ATOM
1685
CG1
ILE
A
336
74.531
59.974
31.898
1.00
27.72
C


ATOM
1686
CG2
ILE
A
336
73.768
60.630
34.211
1.00
24.85
C


ATOM
1687
CD1
ILE
A
336
75.352
61.229
31.609
1.00
29.74
C


ATOM
1688
N
ASP
A
337
70.351
59.761
33.743
1.00
30.78
N


ATOM
1689
CA
ASP
A
337
69.312
59.964
34.746
1.00
30.67
C


ATOM
1690
C
ASP
A
337
68.563
58.662
35.065
1.00
30.77
C


ATOM
1691
O
ASP
A
337
68.358
58.320
36.229
1.00
29.22
O


ATOM
1692
CB
ASP
A
337
68.325
61.018
34.250
1.00
33.77
C


ATOM
1693
CG
ASP
A
337
67.287
61.373
35.285
1.00
35.46
C


ATOM
1694
OD1
ASP
A
337
66.180
61.806
34.897
1.00
36.96
O


ATOM
1695
OD2
ASP
A
337
67.581
61.228
36.488
1.00
38.65
O


ATOM
1696
N
VAL
A
338
68.152
57.941
34.027
1.00
30.12
N


ATOM
1697
CA
VAL
A
338
67.427
56.693
34.217
1.00
29.17
C


ATOM
1698
C
VAL
A
338
68.289
55.663
34.935
1.00
30.19
C


ATOM
1699
O
VAL
A
338
67.808
54.963
35.829
1.00
29.30
O


ATOM
1700
CB
VAL
A
338
66.947
56.103
32.865
1.00
29.20
C


ATOM
1701
CG1
VAL
A
338
66.423
54.683
33.068
1.00
26.29
C


ATOM
1702
CG2
VAL
A
338
65.845
56.986
32.277
1.00
27.28
C


ATOM
1703
N
VAL
A
339
69.556
55.572
34.535
1.00
28.08
N


ATOM
1704
CA
VAL
A
339
70.489
54.636
35.147
1.00
29.13
C


ATOM
1705
C
VAL
A
339
70.653
54.889
36.648
1.00
30.51
C


ATOM
1706
O
VAL
A
339
70.731
53.943
37.432
1.00
31.60
O


ATOM
1707
CB
VAL
A
339
71.874
54.710
34.457
1.00
29.06
C


ATOM
1708
CG1
VAL
A
339
72.931
54.010
35.302
1.00
27.64
C


ATOM
1709
CG2
VAL
A
339
71.789
54.062
33.070
1.00
27.50
C


ATOM
1710
N
ALA
A
340
70.708
56.158
37.048
1.00
30.84
N


ATOM
1711
CA
ALA
A
340
70.851
56.490
38.463
1.00
31.17
C


ATOM
1712
C
ALA
A
340
69.610
56.014
39.211
1.00
31.63
C


ATOM
1713
O
ALA
A
340
69.701
55.469
40.313
1.00
32.08
O


ATOM
1714
CB
ALA
A
340
71.028
57.999
38.644
1.00
30.25
C


ATOM
1715
N
GLU
A
341
68.448
56.215
38.601
1.00
31.19
N


ATOM
1716
CA
GLU
A
341
67.196
55.810
39.225
1.00
31.45
C


ATOM
1717
C
GLU
A
341
67.138
54.290
39.301
1.00
31.09
C


ATOM
1718
O
GLU
A
341
66.702
53.730
40.305
1.00
30.16
O


ATOM
1719
CB
GLU
A
341
66.006
56.334
38.419
1.00
31.78
C


ATOM
1720
CG
GLU
A
341
64.668
56.257
39.149
1.00
34.04
C


ATOM
1721
CD
GLU
A
341
64.611
57.177
40.362
1.00
37.16
C


ATOM
1722
OE1
GLU
A
341
65.211
58.273
40.313
1.00
38.31
O


ATOM
1723
OE2
GLU
A
341
63.954
56.816
41.358
1.00
37.63
O


ATOM
1724
N
ARG
A
342
67.578
53.634
38.232
1.00
30.40
N


ATOM
1725
CA
ARG
A
342
67.585
52.177
38.170
1.00
31.42
C


ATOM
1726
C
ARG
A
342
68.469
51.616
39.286
1.00
31.57
C


ATOM
1727
O
ARG
A
342
68.099
50.646
39.937
1.00
32.09
O


ATOM
1728
CB
ARG
A
342
68.086
51.709
36.791
1.00
31.10
C


ATOM
1729
CG
ARG
A
342
68.037
50.192
36.542
1.00
28.82
C


ATOM
1730
CD
ARG
A
342
69.284
49.477
37.069
1.00
28.26
C


ATOM
1731
NE
ARG
A
342
70.531
49.919
36.441
1.00
26.03
N


ATOM
1732
CZ
ARG
A
342
70.871
49.696
35.172
1.00
26.57
C


ATOM
1733
NH1
ARG
A
342
70.060
49.035
34.360
1.00
25.10
N


ATOM
1734
NH2
ARG
A
342
72.043
50.120
34.714
1.00
26.92
N


ATOM
1735
N
ASN
A
343
69.626
52.236
39.508
1.00
31.96
N


ATOM
1736
CA
ASN
A
343
70.537
51.788
40.557
1.00
33.03
C


ATOM
1737
C
ASN
A
343
69.943
52.031
41.946
1.00
34.72
C


ATOM
1738
O
ASN
A
343
70.122
51.220
42.854
1.00
35.11
O


ATOM
1739
CB
ASN
A
343
71.898
52.478
40.418
1.00
31.35
C


ATOM
1740
CG
ASN
A
343
72.651
52.020
39.176
1.00
32.01
C


ATOM
1741
OD1
ASN
A
343
72.335
50.976
38.604
1.00
31.68
O


ATOM
1742
ND2
ASN
A
343
73.657
52.786
38.765
1.00
29.30
N


ATOM
1743
N
LYS
A
344
69.229
53.141
42.107
1.00
36.02
N


ATOM
1744
CA
LYS
A
344
68.587
53.446
43.378
1.00
38.22
C


ATOM
1745
C
LYS
A
344
67.512
52.384
43.615
1.00
37.85
C


ATOM
1746
O
LYS
A
344
67.392
51.834
44.709
1.00
39.02
O


ATOM
1747
CB
LYS
A
344
67.942
54.837
43.338
1.00
40.96
C


ATOM
1748
CG
LYS
A
344
67.139
55.177
44.589
1.00
46.89
C


ATOM
1749
CD
LYS
A
344
66.252
56.412
44.393
1.00
51.33
C


ATOM
1750
CE
LYS
A
344
67.040
57.709
44.454
1.00
54.56
C


ATOM
1751
NZ
LYS
A
344
67.416
58.052
45.862
1.00
58.14
N


ATOM
1752
N
TYR
A
345
66.744
52.092
42.573
1.00
37.18
N


ATOM
1753
CA
TYR
A
345
65.679
51.098
42.639
1.00
36.37
C


ATOM
1754
C
TYR
A
345
66.223
49.722
43.031
1.00
37.15
C


ATOM
1755
O
TYR
A
345
65.615
49.009
43.827
1.00
36.61
O


ATOM
1756
CB
TYR
A
345
64.987
50.991
41.287
1.00
35.78
C


ATOM
1757
CG
TYR
A
345
63.677
50.235
41.321
1.00
37.12
C


ATOM
1758
CD1
TYR
A
345
62.506
50.863
41.736
1.00
36.58
C


ATOM
1759
CD2
TYR
A
345
63.600
48.905
40.906
1.00
35.92
C


ATOM
1760
CE1
TYR
A
345
61.294
50.196
41.731
1.00
37.36
C


ATOM
1761
CE2
TYR
A
345
62.385
48.223
40.897
1.00
37.19
C


ATOM
1762
CZ
TYR
A
345
61.238
48.880
41.309
1.00
37.67
C


ATOM
1763
OH
TYR
A
345
60.025
48.240
41.280
1.00
39.76
O


ATOM
1764
N
PHE
A
346
67.359
49.346
42.452
1.00
37.41
N


ATOM
1765
CA
PHE
A
346
67.986
48.064
42.759
1.00
38.71
C


ATOM
1766
C
PHE
A
346
68.354
47.996
44.244
1.00
39.07
C


ATOM
1767
O
PHE
A
346
68.162
46.969
44.889
1.00
38.25
O


ATOM
1768
CB
PHE
A
346
69.251
47.869
41.915
1.00
37.92
C


ATOM
1769
CG
PHE
A
346
70.018
46.621
42.252
1.00
39.35
C


ATOM
1770
CD1
PHE
A
346
69.484
45.362
41.984
1.00
38.94
C


ATOM
1771
CD2
PHE
A
346
71.277
46.703
42.841
1.00
41.21
C


ATOM
1772
CE1
PHE
A
346
70.190
44.203
42.294
1.00
39.83
C


ATOM
1773
CE2
PHE
A
346
71.997
45.545
43.159
1.00
41.80
C


ATOM
1774
CZ
PHE
A
346
71.449
44.292
42.883
1.00
41.67
C


ATOM
1775
N
GLU
A
347
68.877
49.096
44.778
1.00
40.05
N


ATOM
1776
CA
GLU
A
347
69.269
49.150
46.183
1.00
42.73
C


ATOM
1777
C
GLU
A
347
68.091
49.066
47.147
1.00
42.82
C


ATOM
1778
O
GLU
A
347
68.227
48.534
48.249
1.00
43.20
O


ATOM
1779
CB
GLU
A
347
70.061
50.429
46.472
1.00
43.65
C


ATOM
1780
CG
GLU
A
347
71.410
50.480
45.778
1.00
50.82
C


ATOM
1781
CD
GLU
A
347
72.321
49.322
46.176
1.00
54.96
C


ATOM
1782
OE1
GLU
A
347
73.405
49.177
45.565
1.00
57.64
O


ATOM
1783
OE2
GLU
A
347
71.961
48.556
47.101
1.00
57.77
O


ATOM
1784
N
GLU
A
348
66.940
49.582
46.731
1.00
41.38
N


ATOM
1785
CA
GLU
A
348
65.760
49.574
47.580
1.00
42.21
C


ATOM
1786
C
GLU
A
348
64.987
48.265
47.522
1.00
41.45
C


ATOM
1787
O
GLU
A
348
64.437
47.821
48.526
1.00
41.84
O


ATOM
1788
CB
GLU
A
348
64.800
50.705
47.178
1.00
43.87
C


ATOM
1789
CG
GLU
A
348
65.481
52.020
46.833
1.00
47.35
C


ATOM
1790
CD
GLU
A
348
64.505
53.097
46.375
1.00
49.04
C


ATOM
1791
OE1
GLU
A
348
63.565
52.781
45.611
1.00
47.83
O


ATOM
1792
OE2
GLU
A
348
64.694
54.268
46.773
1.00
51.17
O


ATOM
1793
N
THR
A
349
64.954
47.645
46.349
1.00
40.08
N


ATOM
1794
CA
THR
A
349
64.171
46.432
46.159
1.00
37.91
C


ATOM
1795
C
THR
A
349
64.910
45.133
45.859
1.00
37.79
C


ATOM
1796
O
THR
A
349
64.306
44.062
45.895
1.00
37.84
O


ATOM
1797
CB
THR
A
349
63.173
46.639
45.020
1.00
37.46
C


ATOM
1798
OG1
THR
A
349
63.894
46.724
43.784
1.00
37.27
O


ATOM
1799
CG2
THR
A
349
62.387
47.933
45.223
1.00
36.70
C


ATOM
1800
N
GLY
A
350
66.197
45.216
45.550
1.00
37.03
N


ATOM
1801
CA
GLY
A
350
66.940
44.014
45.215
1.00
36.78
C


ATOM
1802
C
GLY
A
350
66.646
43.568
43.787
1.00
36.94
C


ATOM
1803
O
GLY
A
350
67.115
42.520
43.340
1.00
37.38
O


ATOM
1804
N
ILE
A
351
65.863
44.362
43.061
1.00
34.88
N


ATOM
1805
CA
ILE
A
351
65.515
44.027
41.683
1.00
33.79
C


ATOM
1806
C
ILE
A
351
66.368
44.835
40.708
1.00
32.41
C


ATOM
1807
O
ILE
A
351
66.378
46.061
40.765
1.00
31.22
O


ATOM
1808
CB
ILE
A
351
64.043
44.357
41.381
1.00
36.04
C


ATOM
1809
CG1
ILE
A
351
63.125
43.668
42.391
1.00
36.61
C


ATOM
1810
CG2
ILE
A
351
63.706
43.948
39.948
1.00
35.73
C


ATOM
1811
CD1
ILE
A
351
61.686
44.165
42.331
1.00
37.65
C


ATOM
1812
N
TYR
A
352
67.078
44.153
39.817
1.00
32.08
N


ATOM
1813
CA
TYR
A
352
67.904
44.843
38.835
1.00
32.62
C


ATOM
1814
C
TYR
A
352
67.177
44.844
37.493
1.00
33.29
C


ATOM
1815
O
TYR
A
352
66.953
43.791
36.904
1.00
33.54
O


ATOM
1816
CB
TYR
A
352
69.264
44.158
38.666
1.00
31.31
C


ATOM
1817
CG
TYR
A
352
70.174
44.889
37.695
1.00
30.97
C


ATOM
1818
CD1
TYR
A
352
70.998
45.930
38.128
1.00
29.66
C


ATOM
1819
CD2
TYR
A
352
70.171
44.575
36.336
1.00
30.63
C


ATOM
1820
CE1
TYR
A
352
71.794
46.638
37.237
1.00
28.10
C


ATOM
1821
CE2
TYR
A
352
70.966
45.280
35.434
1.00
30.54
C


ATOM
1822
CZ
TYR
A
352
71.775
46.309
35.895
1.00
29.18
C


ATOM
1823
OH
TYR
A
352
72.580
46.996
35.019
1.00
31.65
O


ATOM
1824
N
ILE
A
353
66.811
46.027
37.010
1.00
32.84
N


ATOM
1825
CA
ILE
A
353
66.113
46.119
35.735
1.00
31.85
C


ATOM
1826
C
ILE
A
353
67.028
46.626
34.634
1.00
31.84
C


ATOM
1827
O
ILE
A
353
67.506
47.760
34.679
1.00
32.46
O


ATOM
1828
CB
ILE
A
353
64.900
47.048
35.835
1.00
32.61
C


ATOM
1829
CG1
ILE
A
353
63.962
46.536
36.936
1.00
34.08
C


ATOM
1830
CG2
ILE
A
353
64.181
47.105
34.487
1.00
33.22
C


ATOM
1831
CD1
ILE
A
353
62.793
47.431
37.244
1.00
32.45
C


ATOM
1832
N
PRO
A
354
67.303
45.779
33.634
1.00
30.90
N


ATOM
1833
CA
PRO
A
354
68.177
46.197
32.533
1.00
29.68
C


ATOM
1834
C
PRO
A
354
67.528
47.344
31.763
1.00
29.05
C


ATOM
1835
O
PRO
A
354
66.308
47.368
31.600
1.00
28.14
O


ATOM
1836
CB
PRO
A
354
68.293
44.934
31.679
1.00
28.34
C


ATOM
1837
CG
PRO
A
354
68.051
43.808
32.680
1.00
29.10
C


ATOM
1838
CD
PRO
A
354
66.921
44.360
33.506
1.00
29.33
C


ATOM
1839
N
VAL
A
355
68.330
48.302
31.301
1.00
28.33
N


ATOM
1840
CA
VAL
A
355
67.771
49.404
30.529
1.00
27.79
C


ATOM
1841
C
VAL
A
355
68.406
49.446
29.151
1.00
27.36
C


ATOM
1842
O
VAL
A
355
69.552
49.044
28.958
1.00
26.70
O


ATOM
1843
CB
VAL
A
355
67.931
50.788
31.246
1.00
28.56
C


ATOM
1844
CG1
VAL
A
355
67.191
50.759
32.584
1.00
27.11
C


ATOM
1845
CG2
VAL
A
355
69.406
51.147
31.427
1.00
24.91
C


ATOM
1846
N
CYS
A
356
67.640
49.941
28.193
1.00
26.85
N


ATOM
1847
CA
CYS
A
356
68.075
50.008
26.813
1.00
27.44
C


ATOM
1848
C
CYS
A
356
68.148
51.436
26.298
1.00
27.62
C


ATOM
1849
O
CYS
A
356
67.170
52.177
26.385
1.00
28.60
O


ATOM
1850
CB
CYS
A
356
67.099
49.198
25.945
1.00
28.37
C


ATOM
1851
SG
CYS
A
356
67.313
49.376
24.155
1.00
31.02
S


ATOM
1852
N
SER
A
357
69.305
51.826
25.770
1.00
27.52
N


ATOM
1853
CA
SER
A
357
69.455
53.160
25.196
1.00
28.11
C


ATOM
1854
C
SER
A
357
68.975
52.992
23.756
1.00
28.62
C


ATOM
1855
O
SEP
A
357
69.628
52.323
22.948
1.00
28.65
O


ATOM
1856
CB
SER
A
357
70.916
53.610
25.210
1.00
27.16
C


ATOM
1857
OG
SER
A
357
71.045
54.894
24.615
1.00
28.40
O


ATOM
1858
N
ASP
A
358
67.831
53.594
23.451
1.00
29.11
N


ATOM
1859
CA
ASP
A
358
67.215
53.487
22.124
1.00
30.39
C


ATOM
1860
C
ASP
A
358
67.269
54.773
21.294
1.00
30.74
C


ATOM
1861
O
ASP
A
358
66.604
55.758
21.608
1.00
29.70
O


ATOM
1862
CB
ASP
A
358
65.762
53.019
22.305
1.00
29.62
C


ATOM
1863
CG
ASP
A
358
64.978
52.960
21.007
1.00
30.36
C


ATOM
1864
OD1
ASP
A
358
65.580
52.835
19.920
1.00
31.20
O


ATOM
1865
OD2
ASP
A
358
63.734
53.022
21.086
1.00
30.14
O


ATOM
1866
N
GLY
A
359
68.081
54.751
20.240
1.00
33.56
N


ATOM
1867
CA
GLY
A
359
68.193
55.899
19.357
1.00
35.42
C


ATOM
1868
C
GLY
A
359
69.310
56.878
19.659
1.00
38.10
C


ATOM
1869
O
GLY
A
359
69.854
56.901
20.761
1.00
39.07
O


ATOM
1870
N
GLY
A
360
69.662
57.681
18.659
1.00
40.00
N


ATOM
1871
CA
GLY
A
360
70.706
58.673
18.831
1.00
41.21
C


ATOM
1872
C
GLY
A
360
72.123
58.198
18.581
1.00
41.96
C


ATOM
1873
O
GLY
A
360
73.055
58.987
18.695
1.00
44.15
O


ATOM
1874
N
ILE
A
361
72.305
56.923
18.256
1.00
42.76
N


ATOM
1875
CA
ILE
A
361
73.646
56.410
17.996
1.00
43.52
C


ATOM
1876
C
ILE
A
361
74.052
56.802
16.581
1.00
44.42
C


ATOM
1877
O
ILE
A
361
73.470
56.322
15.609
1.00
44.27
O


ATOM
1878
CB
ILE
A
361
73.714
54.862
18.107
1.00
43.69
C


ATOM
1879
CG1
ILE
A
361
73.392
54.412
19.538
1.00
43.46
C


ATOM
1880
CG2
ILE
A
361
75.095
54.366
17.685
1.00
42.46
C


ATOM
1881
CD1
ILE
A
361
74.429
54.792
20.565
1.00
42.32
C


ATOM
1882
N
VAL
A
362
75.049
57.675
16.469
1.00
45.42
N


ATOM
1883
CA
VAL
A
362
75.529
58.118
15.166
1.00
45.68
C


ATOM
1884
C
VAL
A
362
76.851
57.440
14.820
1.00
45.91
C


ATOM
1885
O
VAL
A
362
77.035
56.969
13.696
1.00
46.38
O


ATOM
1886
CB
VAL
A
362
75.723
59.643
15.135
1.00
46.35
C


ATOM
1887
CG1
VAL
A
362
76.105
60.091
13.727
1.00
48.19
C


ATOM
1888
CG2
VAL
A
362
74.444
60.333
15.572
1.00
46.73
C


ATOM
1889
N
TYR
A
363
77.761
57.379
15.792
1.00
44.38
N


ATOM
1890
CA
TYR
A
363
79.067
56.759
15.589
1.00
43.12
C


ATOM
1891
C
TYR
A
363
79.278
55.547
16.491
1.00
41.17
C


ATOM
1892
O
TYR
A
363
78.599
55.387
17.501
1.00
40.86
O


ATOM
1893
CB
TYR
A
363
80.176
57.771
15.862
1.00
46.18
C


ATOM
1894
CG
TYR
A
363
80.072
59.040
15.052
1.00
49.95
C


ATOM
1895
CD1
TYR
A
363
80.052
59.001
13.659
1.00
52.89
C


ATOM
1896
CD2
TYR
A
363
80.012
60.283
15.677
1.00
51.68
C


ATOM
1897
CE1
TYR
A
363
79.978
60.171
12.905
1.00
55.23
C


ATOM
1898
CE2
TYR
A
363
79.938
61.462
14.934
1.00
54.25
C


ATOM
1899
CZ
TYR
A
363
79.924
61.397
13.549
1.00
55.42
C


ATOM
1900
OH
TYR
A
363
79-.872
62.556
12.803
1.00
58.12
O


ATOM
1901
N
ASP
A
364
80.231
54.695
16.134
1.00
39.35
N


ATOM
1902
CA
ASP
A
364
80.507
53.523
16.953
1.00
38.37
C


ATOM
1903
C
ASP
A
364
80.828
53.907
18.396
1.00
36.34
C


ATOM
1904
O
ASP
A
364
80.378
53.245
19.331
1.00
37.10
O


ATOM
1905
CB
ASP
A
364
81.681
52.712
16.386
1.00
40.35
C


ATOM
1906
CG
ASP
A
364
81.347
52.031
15.068
1.00
41.28
C


ATOM
1907
OD1
ASP
A
364
80.207
51.547
14.912
1.00
39.82
O


ATOM
1908
OD2
ASP
A
364
82.236
51.964
14.197
1.00
42.22
O


ATOM
1909
N
TYR
A
365
81.594
54.978
18.587
1.00
33.88
N


ATOM
1910
CA
TYR
A
365
81.959
55.375
19.945
1.00
33.29
C


ATOM
1911
C
TYR
A
365
80.754
55.781
20.792
1.00
31.98
C


ATOM
1912
O
TYR
A
365
80.827
55.776
22.016
1.00
30.93
O


ATOM
1913
CB
TYR
A
365
83.031
56.477
19.926
1.00
32.04
C


ATOM
1914
CG
TYR
A
365
82.536
57.903
19.814
1.00
35.20
C


ATOM
1915
CD1
TYR
A
365
82.298
58.677
20.954
1.00
34.49
C


ATOM
1916
CD2
TYR
A
365
82.362
58.501
18.567
1.00
35.46
C


ATOM
1917
CE1
TYR
A
365
81.905
60.016
20.849
1.00
36.12
C


ATOM
1918
CE2
TYR
A
365
81.971
59.837
18.452
1.00
37.53
C


ATOM
1919
CZ
TYR
A
365
81.744
60.586
19.594
1.00
37.51
C


ATOM
1920
OH
TYR
A
365
81.351
61.901
19.461
1.00
40.00
O


ATOM
1921
N
HIS
A
366
79.641
56.119
20.143
1.00
31.70
N


ATOM
1922
CA
HIS
A
366
78.434
56.467
20.882
1.00
32.08
C


ATOM
1923
C
HIS
A
366
77.938
55.198
21.591
1.00
30.99
C


ATOM
1924
O
HIS
A
366
77.289
55.278
22.635
1.00
30.53
O


ATOM
1925
CB
HIS
A
366
77.336
57.002
19.947
1.00
32.20
C


ATOM
1926
CG
HIS
A
366
77.597
58.378
19.422
1.00
33.31
C


ATOM
1927
ND1
HIS
A
366
78.598
59.190
19.914
1.00
34.60
N


ATOM
1928
CD2
HIS
A
366
76.948
59.110
18.485
1.00
33.99
C


ATOM
1929
CE1
HIS
A
366
78.552
60.362
19.305
1.00
32.63
C


ATOM
1930
NE2
HIS
A
366
77.560
60.339
18.434
1.00
35.91
N


ATOM
1931
N
MET
A
367
78.244
54.031
21.017
1.00
30.17
N


ATOM
1932
CA
MET
A
367
77.853
52.748
21.619
1.00
30.37
C


ATOM
1933
C
MET
A
367
78.588
52.573
22.953
1.00
29.75
C


ATOM
1934
O
MET
A
367
77.997
52.214
23.967
1.00
31.07
O


ATOM
1935
CE
MET
A
367
78.232
51.567
20.711
1.00
30.58
C


ATOM
1936
CG
MET
A
367
77.477
51.457
19.385
1.00
31.52
C


ATOM
1937
SD
MET
A
367
78.053
50.007
18.447
1.00
35.95
S


ATOM
1938
CE
MET
A
367
77.121
50.189
16.917
1.00
34.32
C


ATOM
1939
N
THR
A
368
79.894
52.810
22.928
1.00
29.18
N


ATOM
1940
CA
THR
A
368
80.726
52.688
24.118
1.00
29.61
C


ATOM
1941
C
THR
A
368
80.241
53.682
25.165
1.00
28.28
C


ATOM
1942
O
THR
A
368
80.163
53.354
26.343
1.00
29.90
O


ATOM
1943
CB
THR
A
368
82.196
52.974
23.775
1.00
29.95
C


ATOM
1944
OG1
THR
A
368
82.548
52.222
22.606
1.00
31.91
O


ATOM
1945
CG2
THR
A
368
83.113
52.574
24.928
1.00
28.50
C


ATOM
1946
N
LEU
A
369
79.916
54.895
24.729
1.00
28.13
N


ATOM
1947
CA
LEU
A
369
79.418
55.925
25.639
1.00
29.19
C


ATOM
1948
C
LEU
A
369
78.117
55.493
26.321
1.00
28.58
C


ATOM
1949
O
LEU
A
369
77.978
55.619
27.535
1.00
28.56
O


ATOM
1950
CB
LEU
A
369
79.165
57.245
24.890
1.00
29.00
C


ATOM
1951
CG
LEU
A
369
80.362
58.150
24.593
1.00
30.35
C


ATOM
1952
CD1
LEU
A
369
79.877
59.404
23.866
1.00
30.34
C


ATOM
1953
CD2
LEU
A
369
81.064
58.528
25.898
1.00
28.91
C


ATOM
1954
N
ALA
A
370
77.172
54.990
25.529
1.00
28.37
N


ATOM
1955
CA
ALA
A
370
75.880
54.560
26.052
1.00
28.93
C


ATOM
1956
C
ALA
A
370
76.052
53.464
27.103
1.00
27.87
C


ATOM
1957
O
ALA
A
370
75.424
53.500
28.152
1.00
28.49
O


ATOM
1958
CB
ALA
A
370
74.987
54.064
24.911
1.00
26.15
C


ATOM
1959
N
LEU
A
371
76.905
52.491
26.813
1.00
27.99
N


ATOM
1960
CA
LEU
A
371
77.146
51.401
27.746
1.00
28.20
C


ATOM
1961
C
LEU
A
371
77.852
51.935
28.995
1.00
28.01
C


ATOM
1962
O
LEU
A
371
77.475
51.599
30.111
1.00
27.43
O


ATOM
1963
CE
LEU
A
371
77.992
50.309
27.069
1.00
27.75
C


ATOM
1964
CG
LEU
A
371
77.347
49.632
25.844
1.00
29.75
C


ATOM
1965
CD1
LEU
A
371
78.370
48.736
25.140
1.00
31.88
C


ATOM
1966
CD2
LEU
A
371
76.140
48.815
26.272
1.00
29.40
C


ATOM
1967
N
ALA
A
372
78.863
52.783
28.803
1.00
27.59
N


ATOM
1968
CA
ALA
A
372
79.608
53.346
29.923
1.00
27.55
C


ATOM
1969
C
ALA
A
372
78.710
54.146
30.845
1.00
28.89
C


ATOM
1970
O
ALA
A
372
78.913
54.158
32.063
1.00
28.91
O


ATOM
1971
CB
ALA
A
372
80.746
54.226
29.423
1.00
25.48
C


ATOM
1972
N
MET
A
373
77.723
54.828
30.271
1.00
28.54
N


ATOM
1973
CA
MET
A
373
76.813
55.616
31.090
1.00
28.48
C


ATOM
1974
C
MET
A
373
75.815
54.738
31.853
1.00
28.37
C


ATOM
1975
O
MET
A
373
75.048
55.238
32.665
1.00
28.46
O


ATOM
1976
CE
MET
A
373
76.084
56.655
30.229
1.00
26.76
C


ATOM
1977
CG
MET
A
373
76.992
57.775
29.722
1.00
26.55
C


ATOM
1978
SD
MET
A
373
76.204
58.784
28.435
1.00
29.55
S


ATOM
1979
CE
MET
A
373
77.549
59.940
27.986
1.00
27.96
C


ATOM
1980
N
GLY
A
374
75.825
53.430
31.606
1.00
28.86
N


ATOM
1981
CA
GLY
A
374
74.917
52.563
32.344
1.00
27.32
C


ATOM
1982
C
GLY
A
374
73.906
51.744
31.563
1.00
28.78
C


ATOM
1983
O
GLY
A
374
73.257
50.862
32.133
1.00
29.86
O


ATOM
1984
N
ALA
A
375
73.746
52.023
30.274
1.00
27.82
N


ATOM
1985
CA
ALA
A
375
72.812
51.249
29.472
1.00
28.98
C


ATOM
1986
C
ALA
A
375
73.363
49.829
29.355
1.00
29.41
C


ATOM
1987
O
ALA
A
375
74.552
49.641
29.099
1.00
30.88
O


ATOM
1988
CB
ALA
A
375
72.657
51.866
28.086
1.00
26.18
C


ATOM
1989
N
ASP
A
376
72.500
48.837
29.545
1.00
29.72
N


ATOM
1990
CA
ASP
A
376
72.900
47.435
29.457
1.00
30.17
C


ATOM
1992
C
ASP
A
376
72.997
47.034
27.994
1.00
30.68
C


ATOM
1992
O
ASP
A
376
73.896
46.293
27.597
1.00
30.02
O


ATOM
1993
CB
ASP
A
376
71.882
46.568
30.187
1.00
30.75
C


ATOM
1994
CG
ASP
A
376
71.780
46.924
31.658
1.00
31.02
C


ATOM
1995
OD1
ASP
A
376
72.596
46.409
32.455
1.00
29.99
O


ATOM
1996
OD2
ASP
A
376
70.895
47.733
32.013
1.00
31.49
O


ATOM
1997
N
PHE
A
377
72.058
47.513
27.189
1.00
30.61
N


ATOM
1998
CA
PHE
A
377
72.106
47.236
25.767
1.00
30.87
C


ATOM
1999
C
PHE
A
377
71.603
48.425
24.954
1.00
30.14
C


ATOM
2000
O
PHE
A
377
71.047
49.388
25.498
1.00
29.61
O


ATOM
2001
CB
PHE
A
377
71.374
45.922
25.396
1.00
29.78
C


ATOM
2002
CG
PHE
A
377
69.955
45.827
25.881
1.00
31.57
C


ATOM
2003
CD1
PHE
A
377
69.673
45.401
27.178
1.00
31.78
C


ATOM
2004
CD2
PHE
A
377
68.894
46.099
25.020
1.00
31.27
C


ATOM
2005
CE1
PHE
A
377
68.349
45.242
27.610
1.00
32.32
C


ATOM
2006
CE2
PHE
A
377
67.569
45.945
25.436
1.00
32.45
C


ATOM
2007
CZ
PHE
A
377
67.295
45.514
26.735
1.00
32.96
C


ATOM
2008
N
ILE
A
378
71.820
48.354
23.648
1.00
30.17
N


ATOM
2009
CA
ILE
A
378
71.473
49.436
22.742
1.00
30.04
C


ATOM
2010
C
ILE
A
378
70.520
49.007
21.627
1.00
30.86
C


ATOM
2011
O
ILE
A
378
70.693
47.939
21.038
1.00
31.49
O


ATOM
2012
CB
ILE
A
378
72.772
49.974
22.099
1.00
31.01
C


ATOM
2013
CG1
ILE
A
378
73.760
50.360
23.201
1.00
32.35
C


ATOM
2014
CG2
ILE
A
378
72.482
51.174
21.191
1.00
31.58
C


ATOM
2015
CD1
ILE
A
378
75.178
50.566
22.694
1.00
34.75
C


ATOM
2016
N
MET
A
379
69.511
49.829
21.349
1.00
29.83
N


ATOM
2017
CA
MET
A
379
68.581
49.531
20.265
1.00
30.54
C


ATOM
2018
C
MET
A
379
68.913
50.461
19.095
1.00
30.14
C


ATOM
2019
O
MET
A
379
69.010
51.669
19.268
1.00
29.93
O


ATOM
2020
CS
MET
A
379
67.122
49.749
20.694
1.00
30.89
C


ATOM
2021
CG
MET
A
379
66.139
49.547
19.538
1.00
31.32
C


ATOM
2022
SD
MET
A
379
64.386
49.460
19.961
1.00
31.78
S


ATOM
2023
CE
MET
A
379
64.246
47.743
20.461
1.00
30.99
C


ATOM
2024
N
LEU
A
380
69.090
49.901
17.906
1.00
30.34
N


ATOM
2025
CA
LEU
A
380
69.416
50.720
16.746
1.00
31.69
C


ATOM
2026
C
LEU
A
380
68.521
50.429
15.553
1.00
31.86
C


ATOM
2027
O
LEU
A
380
68.100
49.293
15.343
1.00
31.20
O


ATOM
2028
CB
LEU
A
380
70.879
50.514
16.331
1.00
31.86
C


ATOM
2029
CG
LEU
A
380
71.975
50.752
17.373
1.00
33.23
C


ATOM
2030
CD1
LEU
A
380
72.067
49.532
18.2821
1.00
34.47
C


ATOM
2031
CD2
LEU
A
380
73.319
50.966
16.679
1.00
33.89
C


ATOM
2032
N
GLY
A
381
68.241
51.469
14.775
1.00
32.46
N


ATOM
2033
CA
GLY
A
381
67.414
51.321
13.589
1.00
33.27
C


ATOM
2034
C
GLY
A
381
68.237
51.561
12.338
1.00
34.20
C


ATOM
2035
O
GLY
A
381
68.519
50.635
11.580
1.00
34.83
O


ATOM
2036
N
ARG
A
382
68.630
52.813
12.132
1.00
35.93
N


ATOM
2037
CA
ARG
A
382
69.431
53.220
10.978
1.00
37.19
C


ATOM
2038
C
ARG
A
382
70.643
52.297
10.765
1.00
36.78
C


ATOM
2039
O
ARG
A
382
70.879
51.801
9.660
1.00
35.86
O


ATOM
2040
CB
ARG
A
382
69.905
54.666
11.181
1.00
39.94
C


ATOM
2041
CG
ARG
A
382
70.739
55.238
10.039
1.00
45.52
C


ATOM
2042
CD
ARG
A
382
71.468
56.513
10.466
1.00
49.66
C


ATOM
2043
NE
ARG
A
382
72.418
56.259
11.552
1.00
53.52
N


ATOM
2044
CZ
ARG
A
382
73.540
55.552
11.423
1.00
54.96
C


ATOM
2045
NH1
ARG
A
382
73.871
55.023
10.249
1.00
54.91
N


ATOM
2046
NH2
ARG
A
382
74.327
55.359
12.478
1.00
54.92
N


ATOM
2047
N
TYR
A
383
71.405
52.080
11.834
1.00
35.43
N


ATOM
2048
CA
TYR
A
383
72.595
51.230
11.798
1.00
34.40
C


ATOM
2049
C
TYR
A
383
72.324
49.893
11.108
1.00
34.58
C


ATOM
2050
O
TYR
A
383
73.082
49.480
10.229
1.00
35.55
O


ATOM
2051
CB
TYR
A
383
73.091
50.975
13.230
1.00
32.13
C


ATOM
2052
CG
TYR
A
383
74.315
50.090
13.328
1.00
32.06
C


ATOM
2053
CD1
TYR
A
383
75.603
50.628
13.275
1.00
31.61
C


ATOM
2054
CD2
TYR
A
383
74.185
48.711
13.476
1.00
31.52
C


ATOM
2055
CE1
TYR
A
383
76.728
49.811
13.370
1.00
32.15
C


ATOM
2056
CE2
TYR
A
383
75.293
47.889
13.569
1.00
30.67
C


ATOM
2057
CZ
TYR
A
383
76.564
48.440
13.516
1.00
33.10
C


ATOM
2058
OH
TYR
A
383
77.662
47.610
13.604
1.00
30.90
O


ATOM
2059
N
PHE
A
384
71.242
49.227
11.505
1.00
32.76
N


ATOM
2060
CA
PHE
A
384
70.877
47.929
10.936
1.00
34.01
C


ATOM
2061
C
PHE
A
384
70.164
47.997
9.574
1.00
34.71
C


ATOM
2062
O
PHE
A
384
70.249
47.058
8.782
1.00
35.23
O


ATOM
2063
CB
PHE
A
384
70.004
47.150
11.930
1.00
32.49
C


ATOM
2064
CG
PHE
A
384
70.764
46.603
13.115
1.00
33.56
C


ATOM
2065
CD1
PHE
A
384
71.737
45.618
12.944
1.00
32.15
C


ATOM
2066
CD2
PHE
A
384
70.510
47.076
14.401
1.00
31.87
C


ATOM
2067
CE1
PHE
A
384
72.447
45.113
14.037
1.00
32.91
C


ATOM
2068
CE2
PHE
A
384
71.211
46.579
15.497
1.00
32.18
C


ATOM
2069
CZ
PHE
A
384
72.181
45.596
15.317
1.00
31.64
C


ATOM
2070
N
ALA
A
385
69.465
49.096
9.305
1.00
35.43
N


ATOM
2071
CA
ALA
A
385
68.750
49.250
8.036
2.00
36.93
C


ATOM
2072
C
ALA
A
385
69.702
49.171
6.842
1.00
37.68
C


ATOM
2073
O
ALA
A
385
69.335
48.678
5.776
1.00
37.47
O


ATOM
2074
CB
ALA
A
385
67.999
50.585
8.014
1.00
35.75
C


ATOM
2075
N
ARG
A
386
70.926
49.658
7.038
1.00
38.60
N


ATOM
2076
CA
ARG
A
386
71.956
49.672
6.001
1.00
38.80
C


ATOM
2077
C
ARG
A
386
72.388
48.285
5.532
1.00
39.38
C


ATOM
2078
O
ARG
A
386
73.027
48.151
4.482
1.00
39.24
O


ATOM
2079
CB
ARG
A
386
73.213
50.392
6.506
1.00
38.96
C


ATOM
2080
CG
ARG
A
386
73.057
51.842
6.915
1.00
41.08
C


ATOM
2081
CD
ARG
A
386
74.373
52.314
7.530
1.00
43.49
C


ATOM
2082
NE
ARG
A
386
74.784
51.422
8.616
1.00
45.03
N


ATOM
2083
CZ
ARG
A
386
76.045
51.162
8.950
1.00
45.42
C


ATOM
2084
NH1
ARG
A
386
77.049
51.724
8.284
1.00
44.14
N


ATOM
2085
NH2
ARG
A
386
76.301
50.330
9.954
1.00
44.38
N


ATOM
2086
N
PHE
A
387
72.057
47.256
6.302
1.00
40.14
N


ATOM
2087
CA
PHE
A
387
72.483
45.911
5.950
1.00
41.48
C


ATOM
2088
C
PHE
A
387
71.620
45.137
4.954
1.00
43.09
C


ATOM
2089
O
PHE
A
387
70.412
45.350
4.827
1.00
43.30
O


ATOM
2090
CB
PHE
A
387
72.658
45.066
7.218
1.00
41.15
C


ATOM
2091
CG
PHE
A
387
73.559
45.690
8.255
1.00
41.44
C


ATOM
2092
CD1
PHE
A
387
74.665
46.450
7.878
1.00
40.93
C


ATOM
2093
CD2
PHE
A
387
73.312
45.496
9.614
1.00
40.05
C


ATOM
2094
CE1
PHE
A
387
75.512
47.007
8.837
1.00
40.83
C


ATOM
2095
CE2
PHE
A
387
74.154
46.048
10.583
1.00
39.34
C


ATOM
2096
CZ
PHE
A
387
75.254
46.804
10.196
1.00
39.79
C


ATOM
2097
N
GLU
A
388
72.284
44.222
4.261
1.00
44.03
N


ATOM
2098
CA
GLU
A
388
71.673
43.348
3.274
1.00
45.03
C


ATOM
2099
C
GLU
A
388
70.445
42.655
3.850
1.00
44.35
C


ATOM
2100
O
GLU
A
388
69.431
42.507
3.171
1.00
43.66
O


ATOM
2101
CB
GLU
A
388
72.700
42.297
2.846
1.00
46.61
C


ATOM
2102
CG
GLU
A
388
72.210
41.252
1.853
1.00
50.47
C


ATOM
2103
CD
GLU
A
388
71.843
41.854
0.516
1.00
52.73
C


ATOM
2104
OE1
GLU
A
388
72.569
42.769
0.063
1.00
54.19
O


ATOM
2105
OE2
GLU
A
388
70.842
41.407
−0.089
1.00
54.15
O


ATOM
2106
N
GLU
A
389
70.535
42.250
5.114
1.00
43.43
N


ATOM
2107
CA
GLU
A
389
69.442
41.540
5.762
1.00
42.71
C


ATOM
2108
C
GLU
A
389
68.218
42.345
6.187
1.00
42.10
C


ATOM
2109
O
GLU
A
389
67.249
41.765
6.663
1.00
41.97
O


ATOM
2110
CB
GLU
A
389
69.973
40.738
6.955
1.00
41.76
C


ATOM
2111
CG
GLU
A
389
71.002
39.695
6.563
1.00
42.42
C


ATOM
2112
CD
GLU
A
389
72.429
40.180
6.750
1.00
43.40
C


ATOM
2113
OE1
GLU
A
389
72.688
41.387
6.567
1.00
42.57
O


ATOM
2114
OE2
GLU
A
389
73.297
39.344
7.074
1.00
43.26
O


ATOM
2115
N
SER
A
390
68.245
43.666
6.041
1.00
43.01
N


ATOM
2116
CA
SER
A
390
67.065
44.446
6.399
1.00
45.54
C


ATOM
2117
C
SER
A
390
66.047
44.174
5.280
1.00
47.27
C


ATOM
2118
O
SER
A
390
66.422
44.044
4.112
1.00
46.75
O


ATOM
2119
CB
SER
A
390
67.387
45.938
6.492
1.00
44.44
C


ATOM
2120
OG
SER
A
390
67.730
46.469
5.230
1.00
47.93
O


ATOM
2121
N
PRO
A
391
64.750
44.096
5.625
1.00
48.64
N


ATOM
2122
CA
PRO
A
391
63.649
43.825
4.690
1.00
50.18
C


ATOM
2123
C
PRO
A
391
63.348
44.842
3.587
1.00
51.58
C


ATOM
2124
O
PRO
A
391
62.530
44.575
2.707
1.00
53.10
O


ATOM
2125
CB
PRO
A
391
62.459
43.632
5.626
1.00
49.90
C


ATOM
2126
CG
PRO
A
391
62.741
44.643
6.698
1.00
48.60
C


ATOM
2127
CD
PRO
A
391
64.223
44.439
6.962
1.00
47.30
C


ATOM
2128
N
THR
A
392
63.996
45.998
3.623
1.00
52.18
N


ATOM
2129
CA
THR
A
392
63.737
47.020
2.620
1.00
52.69
C


ATOM
2130
C
THR
A
392
64.409
46.724
1.287
1.00
54.68
C


ATOM
2131
O
THR
A
392
65.163
45.759
1.158
1.00
54.94
O


ATOM
2132
CB
THR
A
392
64.186
48.403
3.114
1.00
51.72
C


ATOM
2133
OG1
THR
A
392
65.610
48.421
3.263
1.00
50.10
O


ATOM
2134
CG2
THR
A
392
63.528
48.719
4.455
1.00
50.74
C


ATOM
2135
N
ARG
A
393
64.132
47.565
0.295
1.00
56.32
N


ATOM
2136
CA
ARG
A
393
64.699
47.376
−1.032
1.00
58.34
C


ATOM
2137
C
ARG
A
393
66.023
48.088
−1.244
1.00
58.35
C


ATOM
2138
O
ARG
A
393
66.223
49.219
−0.800
1.00
57.31
O


ATOM
2139
CB
ARG
A
393
63.701
47.818
−2.112
1.00
60.27
C


ATOM
2140
CG
ARG
A
393
62.463
46.928
−2.205
1.00
63.46
C


ATOM
2141
CD
ARG
A
393
61.561
47.293
−3.386
1.00
65.10
C


ATOM
2142
NE
ARG
A
393
61.125
48.684
−3.338
1.00
66.35
N


ATOM
2143
CZ
ARG
A
393
61.584
49.639
−4.139
1.00
67.03
C


ATOM
2144
NH1
ARG
A
393
62.495
49.355
−5.063
1.00
67.37
N


ATOM
2145
NH2
ARG
A
393
61.144
50.883
−4.006
1.00
67.53
N


ATOM
2146
N
LYS
A
394
66.927
47.394
−1.925
1.00
59.11
N


ATOM
2147
CA
LYS
A
394
68.241
47.922
−2.248
1.00
59.88
C


ATOM
2148
C
LYS
A
394
68.034
48.693
−3.542
1.00
60.73
C


ATOM
2149
O
LYS
A
394
67.680
48.106
−4.562
1.00
61.24
O


ATOM
2150
CB
LYS
A
394
69.218
46.768
−2.479
1.00
59.07
C


ATOM
2151
CG
LYS
A
394
70.646
47.055
−2.060
1.00
58.59
C


ATOM
2152
CD
LYS
A
394
71.590
45.945
−2.504
1.00
58.08
C


ATOM
2153
CE
LYS
A
394
71.164
44.582
−1.990
1.00
57.63
C


ATOM
2154
NZ
LYS
A
394
72.088
43.519
−2.476
1.00
57.79
N


ATOM
2155
N
VAL
A
395
68.234
50.005
−3.503
1.00
62.13
N


ATOM
2156
CA
VAL
A
395
68.048
50.827
−4.692
1.00
63.84
C


ATOM
2157
C
VAL
A
395
69.326
51.564
−5.069
1.00
65.15
C


ATOM
2158
O
VAL
A
395
69.995
52.143
−4.215
1.00
65.50
O


ATOM
2159
CB
VAL
A
395
66.917
51.859
−4.483
1.00
63.69
C


ATOM
2160
CG1
VAL
A
395
65.642
51.147
−4.064
1.00
63.82
C


ATOM
2161
CG2
VAL
A
395
67.323
52.884
−3.438
1.00
63.76
C


ATOM
2162
N
THR
A
396
69.666
51.537
−6.354
1.00
66.43
N


ATOM
2163
CA
THR
A
396
70.869
52.209
−6.829
1.00
67.58
C


ATOM
2164
C
THR
A
396
70.552
53.613
−7.319
1.00
68.48
C


ATOM
2165
O
THR
A
396
69.742
53.799
−8.227
1.00
68.56
O


ATOM
2166
CB
THR
A
396
71.535
51.427
−7.971
1.00
67.68
C


ATOM
2167
OG1
THR
A
396
71.919
50.130
−7.500
1.00
68.09
O


ATOM
2168
CG2
THR
A
396
72.773
52.162
−8.464
1.00
68.17
C


ATOM
2169
N
ILE
A
397
71.198
54.599
−6.707
1.00
69.55
N


ATOM
2170
CA
ILE
A
397
70.999
55.996
−7.066
1.00
70.46
C


ATOM
2171
C
ILE
A
397
72.322
56.609
−7.518
1.00
71.03
C


ATOM
2172
O
ILE
A
397
73.224
56.826
−6.708
1.00
71.53
O


ATOM
2173
CB
ILE
A
397
70.453
56.791
−5.867
1.00
70.76
C


ATOM
2174
CG1
ILE
A
397
69.148
56.154
−5.384
1.00
71.18
C


ATOM
2175
CG2
ILE
A
397
70.231
58.246
−6.259
1.00
70.80
C


ATOM
2176
CD1
ILE
A
397
68.542
56.832
−4.175
1.00
71.99
C


ATOM
2177
N
ASN
A
398
72.425
56.879
−8.817
1.00
71.45
N


ATOM
2178
CA
ASN
A
398
73.624
57.464
−9.417
1.00
71.04
C


ATOM
2179
C
ASN
A
398
74.940
56.865
−8.914
1.00
69.90
C


ATOM
2180
O
ASN
A
398
75.802
57.574
−8.389
1.00
69.77
O


ATOM
2181
CB
ASN
A
398
73.630
58.989
−9.218
1.00
72.89
C


ATOM
2182
CG
ASN
A
398
73.544
59.397
−7.755
1.00
74.87
C


ATOM
2183
OD1
ASN
A
398
74.421
59.071
−6.949
1.00
76.25
O


ATOM
2184
ND2
ASN
A
398
72.483
60.119
−7.406
1.00
75.32
N


ATOM
2185
N
GLY
A
399
75.088
55.554
−9.082
1.00
68.28
N


ATOM
2186
CA
GLY
A
399
76.307
54.885
−8.659
1.00
66.71
C


ATOM
2187
C
GLY
A
399
76.392
54.549
−7.181
1.00
65.56
C


ATOM
2188
O
GLY
A
399
77.351
53.912
−6.739
1.00
65.55
O


ATOM
2189
N
SER
A
400
75.398
54.976
−6.410
1.00
63.82
N


ATOM
2190
CA
SER
A
400
75.391
54.697
−4.980
1.00
61.70
C


ATOM
2191
C
SER
A
400
74.256
53.761
−4.602
1.00
59.98
C


ATOM
2192
O
SER
A
400
73.086
54.095
−4.768
1.00
60.36
O


ATOM
2193
CS
SER
A
400
75.267
55.997
−4.185
1.00
61.29
C


ATOM
2194
OG
SER
A
400
76.440
56.778
−4.317
1.00
62.16
O


ATOM
2195
N
VAL
A
401
74.606
52.583
−4.101
1.00
58.09
N


ATOM
2196
CA
VAL
A
401
73.602
51.617
−3.685
1.00
56.62
C


ATOM
2197
C
VAL
A
401
73.099
52.029
−2.303
1.00
56.96
C


ATOM
2198
O
VAL
A
401
73.886
52.176
−1.361
1.00
57.55
O


ATOM
2199
CS
VAL
A
401
74.190
50.198
−3.621
1.00
56.19
C


ATOM
2200
CG1
VAL
A
401
73.129
49.214
−3.161
1.00
54.63
C


ATOM
2201
CG2
VAL
A
401
74.729
49.805
−4.992
1.00
55.02
C


ATOM
2202
N
MET
A
402
71.789
52.226
−2.190
1.00
55.36
N


ATOM
2203
CA
MET
A
402
71.181
52.648
−0.935
1.00
53.84
C


ATOM
2204
C
MET
A
402
70.113
51.661
−0.482
1.00
52.61
C


ATOM
2205
O
MET
A
402
69.789
50.707
−1.188
1.00
51.84
O


ATOM
2206
CS
MET
A
402
70.521
54.022
−1.109
1.00
55.25
C


ATOM
2207
CG
MET
A
402
71.356
55.062
−1.837
1.00
55.38
C


ATOM
2208
SD
MET
A
402
72.760
55.653
−0.884
1.00
59.37
S


ATOM
2209
CE
MET
A
402
71.959
56.904
0.134
1.00
56.83
C


ATOM
2210
N
LYS
A
403
69.579
51.900
0.713
1.00
50.16
N


ATOM
2211
CA
LYS
A
403
68.506
51.082
1.258
1.00
48.17
C


ATOM
2212
C
LYS
A
403
67.452
52.043
1.791
1.00
47.24
C


ATOM
2213
O
LYS
A
403
67.776
53.124
2.285
1.00
46.17
O


ATOM
2214
CS
LYS
A
403
69.007
50.168
2.382
1.00
48.44
C


ATOM
2215
CG
LYS
A
403
69.976
49.093
1.921
1.00
48.79
C


ATOM
2216
CD
LYS
A
403
69.677
47.739
2.552
1.00
48.91
C


ATOM
2217
CE
LYS
A
403
68.415
47.121
1.972
1.00
48.79
C


ATOM
2218
NZ
LYS
A
403
68.133
45.771
2.538
1.00
47.65
N


ATOM
2219
N
GLU
A
404
66.189
51.660
1.674
1.00
46.83
N


ATOM
2220
CA
GLU
A
404
65.115
52.514
2.147
1.00
46.62
C


ATOM
2221
C
GLU
A
404
65.046
52.448
3.661
1.00
45.53
C


ATOM
2222
O
GLU
A
404
65.329
51.412
4.269
1.00
43.78
O


ATOM
2223
CB
GLU
A
404
63.776
52.064
1.582
1.00
49.02
C


ATOM
2224
CG
GLU
A
404
63.846
51.421
0.222
1.00
53.76
C


ATOM
2225
CD
GLU
A
404
62.473
51.056
−0.291
1.00
55.98
C


ATOM
2226
OE1
GLU
A
404
61.767
51.971
−0.772
1.00
56.94
O


ATOM
2227
OE2
GLU
A
404
62.100
49.863
−0.193
1.00
57.61
O


ATOM
2228
N
TYR
A
405
64.661
53.560
4.268
1.00
44.22
N


ATOM
2229
CA
TYR
A
405
64.543
53.615
5.708
1.00
43.49
C


ATOM
2230
C
TYR
A
405
63.488
54.634
6.071
1.00
42.96
C


ATOM
2231
O
TYR
A
405
63.612
55.811
5.744
1.00
43.26
O


ATOM
2232
CB
TYR
A
405
65.883
53.992
6.341
1.00
43.62
C


ATOM
2233
CG
TYR
A
405
65.853
54.018
7.851
1.00
43.93
C


ATOM
2234
CD1
TYR
A
405
65.416
52.913
8.579
1.00
42.98
C


ATOM
2235
CD2
TYR
A
405
66.258
55.150
8.554
1.00
44.65
C


ATOM
2236
CE1
TYR
A
405
65.380
52.938
9.972
1.00
44.02
C


ATOM
2237
CE2
TYR
A
405
66.227
55.184
9.946
1.00
44.86
C


ATOM
2238
CZ
TYR
A
405
65.786
54.077
10.646
1.00
43.66
C


ATOM
2239
OH
TYR
A
405
65.736
54.126
12.018
1.00
43.77
O


ATOM
2240
N
TRP
A
406
62.438
54.171
6.738
1.00
41.92
N


ATOM
2241
CA
TRP
A
406
61.361
55.052
7.149
1.00
40.82
C


ATOM
2242
C
TRP
A
406
60.985
54.760
8.594
1.00
40.62
C


ATOM
2243
O
TRP
A
406
61.088
53.622
9.056
1.00
40.00
O


ATOM
2244
CB
TRP
A
406
60.147
54.878
6.214
1.00
38.27
C


ATOM
2245
CG
TRP
A
406
59.520
53.510
6.228
1.00
35.96
C


ATOM
2246
CD1
TRP
A
406
58.543
53.065
7.074
1.00
35.09
C


ATOM
2247
CD2
TRP
A
406
59.845
52.405
5.373
1.00
35.52
C


ATOM
2248
NE1
TRP
A
406
58.239
51.752
6.800
1.00
36.00
N


ATOM
2249
CE2
TRP
A
406
59.024
51.320
5.762
1.00
36.30
C


ATOM
2250
CE3
TRP
A
406
60.750
52.225
4.315
1.00
36.42
C


ATOM
2251
CZ2
TRP
A
406
59.079
50.068
5.130
1.00
35.10
C


ATOM
2252
CZ3
TRP
A
406
60.806
50.979
3.683
1.00
35.93
C


ATOM
2253
CH2
TRP
A
406
59.972
49.918
4.096
1.00
35.80
C


ATOM
2254
N
GLY
A
407
60.568
55.800
9.307
1.00
41.39
N


ATOM
2255
CA
GLY
A
407
60.178
55.640
10.693
1.00
42.59
C


ATOM
2256
C
GLY
A
407
58.772
55.085
10.825
1.00
43.19
C


ATOM
2257
O
GLY
A
407
57.991
55.101
9.874
1.00
43.52
O


ATOM
2258
N
GLU
A
408
58.452
54.589
12.013
1.00
43.79
N


ATOM
2259
CA
GLU
A
408
57.138
54.029
12.287
1.00
43.77
C


ATOM
2260
C
GLU
A
408
56.100
55.139
12.370
1.00
45.22
C


ATOM
2261
O
GLU
A
408
54.899
54.891
12.292
1.00
45.34
O


ATOM
2262
CB
GLU
A
408
57.181
53.252
13.599
1.00
42.61
C


ATOM
2263
CG
GLU
A
408
58.025
51.997
13.524
1.00
41.23
C


ATOM
2264
CD
GLU
A
408
57.372
50.920
12.674
1.00
39.91
C


ATOM
2265
OE1
GLU
A
408
56.280
50.456
13.056
1.00
39.37
O


ATOM
2266
OE2
GLU
A
408
57.944
50.540
11.632
1.00
39.32
O


ATOM
2267
N
GLY
A
409
56.576
56.368
12.529
1.00
46.42
N


ATOM
2268
CA
GLY
A
409
55.676
57.500
12.619
1.00
48.58
C


ATOM
2269
C
GLY
A
409
55.339
58.095
11.265
1.00
49.72
C


ATOM
2270
O
GLY
A
409
54.491
58.977
11.174
1.00
49.49
O


ATOM
2271
N
SER
A
410
56.001
57.628
10.210
1.00
51.57
N


ATOM
2272
CA
SER
A
410
55.725
58.151
8.876
1.00
53.58
C


ATOM
2273
C
SER
A
410
54.411
57.566
8.385
1.00
55.64
C


ATOM
2274
O
SER
A
410
54.006
56.486
8.816
1.00
54.76
O


ATOM
2275
CB
SER
A
410
56.849
57.791
7.899
1.00
53.27
C


ATOM
2276
OG
SER
A
410
56.837
56.411
7.578
1.00
54.06
O


ATOM
2277
N
SER
A
411
53.740
58.285
7.490
1.00
58.45
N


ATOM
2278
CA
SER
A
411
52.472
57.816
6.951
1.00
61.28
C


ATOM
2279
C
SER
A
411
52.689
56.508
6.199
1.00
62.71
C


ATOM
2280
O
SER
A
411
51.794
55.662
6.123
1.00
62.97
O


ATOM
2281
CB
SER
A
411
51.875
58.873
6.020
1.00
62.05
C


ATOM
2282
OG
SER
A
411
52.807
59.264
5.028
1.00
63.19
O


ATOM
2283
N
ARG
A
412
53.892
56.343
5.658
1.00
64.06
N


ATOM
2284
CA
ARG
A
412
54.241
55.141
4.910
1.00
65.82
C


ATOM
2285
C
ARG
A
412
54.229
53.882
5.776
1.00
67.23
C


ATOM
2286
O
ARG
A
412
54.157
52.768
5.259
1.00
66.85
O


ATOM
2287
CB
ARG
A
412
55.626
55.306
4.273
1.00
64.77
C


ATOM
2288
CG
ARG
A
412
56.114
54.068
3.544
1.00
63.53
C


ATOM
2289
CD
ARG
A
412
57.441
54.298
2.845
1.00
62.50
C


ATOM
2290
NE
ARG
A
412
57.882
53.089
2.155
1.00
61.94
N


ATOM
2291
CZ
ARG
A
412
58.990
52.996
1.429
1.00
62.83
C


ATOM
2292
NH1
ARG
A
412
59.791
54.047
1.286
1.00
62.91
N


ATOM
2293
NH2
ARG
A
412
59.298
51.846
0.842
1.00
62.91
N


ATOM
2294
N
ALA
A
413
54.285
54.065
7.093
1.00
69.94
N


ATOM
2295
CA
ALA
A
413
54.315
52.940
8.022
1.00
72.61
C


ATOM
2296
C
ALA
A
413
52.973
52.554
8.631
1.00
74.53
C


ATOM
2297
O
ALA
A
413
52.439
51.485
8.337
1.00
74.51
O


ATOM
2298
CB
ALA
A
413
55.323
53.221
9.138
1.00
71.60
C


ATOM
2299
N
ARG
A
414
52.434
53.419
9.487
1.00
77.76
N


ATOM
2300
CA
ARG
A
414
51.167
53.137
10.155
1.00
80.61
C


ATOM
2301
C
ARG
A
414
49.963
53.024
9.213
1.00
81.50
C


ATOM
2302
O
ARG
A
414
48.815
53.073
9.661
1.00
81.79
O


ATOM
2303
CB
ARG
A
414
50.893
54.184
11.247
1.00
81.68
C


ATOM
2304
CG
ARG
A
414
50.556
55.589
10.755
1.00
83.90
C


ATOM
2305
CD
ARG
A
414
50.207
56.490
11.941
1.00
85.67
C


ATOM
2306
NE
ARG
A
414
49.470
57.693
11.558
1.00
87.41
N


ATOM
2307
CZ
ARG
A
414
48.918
58.537
12.426
1.00
88.02
C


ATOM
2308
NH1
ARG
A
414
49.021
58.312
13.731
1.00
87.96
N


ATOM
2309
NH2
ARG
A
414
48.253
59.602
11.994
1.00
88.30
N


ATOM
2310
N
ASN
A
415
50.226
52.867
7.916
1.00
82.42
N


ATOM
2311
CA
ASN
A
415
49.152
52.714
6.932
1.00
82.74
C


ATOM
2312
C
ASN
A
415
48.897
51.218
6.722
1.00
83.26
C


ATOM
2313
O
ASN
A
415
48.846
50.745
5.583
1.00
82.62
O


ATOM
2314
CB
ASN
A
415
49.535
53.345
5.581
1.00
83.10
C


ATOM
2315
CG
ASN
A
415
48.309
53.763
4.757
1.00
83.44
C


ATOM
2316
OD1
ASN
A
415
48.403
53.990
3.538
1.00
81.84
O


ATOM
2317
ND2
ASN
A
415
47.148
53.894
5.426
1.00
83.48
N


ATOM
2318
N
TRP
A
416
48.751
50.476
7.819
1.00
83.43
N


ATOM
2319
CA
TRP
A
416
48.504
49.039
7.734
1.00
83.29
C


ATOM
2320
C
TRP
A
416
47.153
48.658
8.340
1.00
83.50
C


ATOM
2321
O
TRP
A
416
46.650
49.328
9.246
1.00
83.70
O


ATOM
2322
CB
TRP
A
416
49.622
48.251
8.435
1.00
83.05
C


ATOM
2323
CG
TRP
A
416
49.577
48.306
9.936
1.00
83.22
C


ATOM
2324
CD1
TRP
A
416
50.081
49.288
10.742
1.00
83.70
C


ATOM
2325
CD2
TRP
A
416
48.957
47.350
10.807
1.00
83.09
C


ATOM
2326
NE1
TRP
A
416
49.812
49.003
12.062
1.00
83.83
N


ATOM
2327
CE2
TRP
A
416
49.122
47.820
12.130
1.00
83.53
C


ATOM
2328
CE3
TRP
A
416
48.274
46.143
10.597
1.00
82.77
C


ATOM
2329
CZ2
TRP
A
416
48.629
47.123
13.240
1.00
83.40
C


ATOM
2330
CZ3
TRP
A
416
47.784
45.452
11.699
1.00
82.88
C


ATOM
2331
CH2
TRP
A
416
47.965
45.945
13.005
1.00
83.24
C


ATOM
2332
N
GLU
A
431
55.027
62.893
11.346
1.00
77.68
N


ATOM
2333
CA
GLU
A
431
55.426
62.297
12.617
1.00
77.79
C


ATOM
2334
C
GLU
A
431
56.719
61.495
12.439
1.00
76.90
C


ATOM
2335
O
GLU
A
431
57.500
61.317
13.379
1.00
77.08
O


ATOM
2336
CE
GLU
A
431
54.302
61.396
13.140
1.00
79.27
C


ATOM
2337
CG
GLU
A
431
52.947
62.100
13.227
1.00
81.73
C


ATOM
2338
CD
GLU
A
431
51.852
61.222
13.817
1.00
83.20
C


ATOM
2339
OE1
GLU
A
431
51.961
60.841
15.004
1.00
83.92
O


ATOM
2340
OE2
GLU
A
431
50.881
60.914
13.093
1.00
83.75
O


ATOM
2341
N
GLY
A
432
56.936
61.018
11.218
1.00
75.40
N


ATOM
2342
CA
GLY
A
432
58.133
60.258
10.909
1.00
73.03
C


ATOM
2343
C
GLY
A
432
58.611
60.653
9.525
1.00
71.34
C


ATOM
2344
O
GLY
A
432
57.915
61.386
8.818
1.00
71.32
O


ATOM
2345
N
VAL
A
433
59.789
60.179
9.130
1.00
69.14
N


ATOM
2346
CA
VAL
A
433
60.319
60.512
7.813
1.00
66.51
C


ATOM
2347
C
VAL
A
433
60.700
59.280
6.994
1.00
64.72
C


ATOM
2348
O
VAL
A
433
60.990
58.216
7.543
1.00
64.04
O


ATOM
2349
CB
VAL
A
433
61.551
61.445
7.924
1.00
66.56
C


ATOM
2350
CG1
VAL
A
433
61.165
62.728
8.642
1.00
66.22
C


ATOM
2351
CG2
VAL
A
433
62.676
60.743
8.658
1.00
66.90
C


ATOM
2352
N
ASP
A
434
60.683
59.446
5.675
1.00
62.15
N


ATOM
2353
CA
ASP
A
434
61.019
58.387
4.732
1.00
59.84
C


ATOM
2354
C
ASP
A
434
62.320
58.807
4.046
1.00
58.55
C


ATOM
2355
O
ASP
A
434
62.383
59.876
3.441
1.00
58.58
O


ATOM
2356
CB
ASP
A
434
59.894
58.247
3.699
1.00
59.57
C


ATOM
2357
CG
ASP
A
434
60.072
57.047
2.795
1.00
59.49
C


ATOM
2358
OD1
ASP
A
434
59.322
56.927
1.804
1.00
59.07
O


ATOM
2359
OD2
ASP
A
434
60.959
56.217
3.079
1.00
60.22
O


ATOM
2360
N
SER
A
435
63.355
57.976
4.136
1.00
56.49
N


ATOM
2361
CA
SER
A
435
64.641
58.320
3.537
1.00
54.56
C


ATOM
2362
C
SER
A
435
65.459
57.138
3.031
1.00
52.57
C


ATOM
2363
O
SER
A
435
64.954
56.028
2.890
1.00
51.40
O


ATOM
2364
CB
SER
A
435
65.480
59.107
4.546
1.00
55.14
C


ATOM
2365
OG
SER
A
435
65.660
58.357
5.736
1.00
56.74
O


ATOM
2366
N
TYR
A
436
66.735
57.401
2.764
1.00
51.28
N


ATOM
2367
CA
TYR
A
436
67.664
56.391
2.269
1.00
50.73
C


ATOM
2368
C
TYR
A
436
68.936
56.359
3.114
1.00
50.04
C


ATOM
2369
O
TYR
A
436
69.356
57.382
3.657
1.00
50.12
O


ATOM
2370
CB
TYR
A
436
68.057
56.704
0.824
1.00
52.87
C


ATOM
2371
CG
TYR
A
436
66.940
56.591
−0.185
1.00
53.47
C


ATOM
2372
CD1
TYR
A
436
66.475
55.344
−0.603
1.00
53.78
C


ATOM
2373
CD2
TYR
A
436
66.356
57.733
−0.733
1.00
54.90
C


ATOM
2374
CE1
TYR
A
436
65.457
55.237
−1.545
1.00
54.59
C


ATOM
2375
CE2
TYR
A
436
65.333
57.637
−1.679
1.00
55.49
C


ATOM
2376
CZ
TYR
A
436
64.891
56.386
−2.077
1.00
55.11
C


ATOM
2377
OH
TYR
A
436
63.876
56.285
−2.999
1.00
56.28
O


ATOM
2378
N
VAL
A
437
69.541
55.180
3.227
1.00
47.66
N


ATOM
2379
CA
VAL
A
437
70.785
55.022
3.969
1.00
46.24
C


ATOM
2380
C
VAL
A
437
71.743
54.236
3.089
1.00
46.02
C


ATOM
2381
O
VAL
A
437
71.343
53.283
2.421
1.00
45.29
O


ATOM
2382
CB
VAL
A
437
70.592
54.260
5.314
1.00
46.00
C


ATOM
2383
CG1
VAL
A
437
69.654
55.037
6.227
1.00
45.51
C


ATOM
2384
CG2
VAL
A
437
70.071
52.853
5.058
1.00
44.32
C


ATOM
2385
N
PRO
A
438
73.026
54.628
3.073
1.00
46.55
N


ATOM
2386
CA
PRO
A
438
74.024
53.935
2.252
1.00
45.89
C


ATOM
2387
C
PRO
A
438
74.178
52.463
2.600
1.00
45.71
C


ATOM
2388
O
PRO
A
438
74.268
52.095
3.773
1.00
45.41
O


ATOM
2389
CE
PRO
A
438
75.301
54.738
2.506
1.00
46.50
C


ATOM
2390
CG
PRO
A
438
75.099
55.254
3.901
1.00
47.81
C


ATOM
2391
CD
PRO
A
438
73.652
55.688
3.881
1.00
46.25
C


ATOM
2392
N
TYR
A
439
74.191
51.629
1.564
1.00
44.94
N


ATOM
2393
CA
TYR
A
439
74.340
50.187
1.712
1.00
44.07
C


ATOM
2394
C
TYR
A
439
75.686
49.898
2.371
1.00
44.51
C


ATOM
2395
O
TYR
A
439
76.711
50.459
1.985
1.00
44.53
O


ATOM
2396
CB
TYR
A
439
74.273
49.521
0.334
1.00
42.82
C


ATOM
2397
CG
TYR
A
439
74.442
48.019
0.340
1.00
41.12
C


ATOM
2398
CD1
TYR
A
439
73.561
47.201
1.041
1.00
41.19
C


ATOM
2399
CD2
TYR
A
439
75.464
47.412
−0.388
1.00
42.23
C


ATOM
2400
CE1
TYR
A
439
73.690
45.811
1.014
1.00
41.86
C


ATOM
2401
CE2
TYR
A
439
75.603
46.025
−0.420
1.00
42.30
C


ATOM
2402
CZ
TYR
A
439
74.712
45.232
0.281
1.00
42.80
C


ATOM
2403
OH
TYR
A
439
74.834
43.861
0.242
1.00
44.53
O


ATOM
2404
N
ALA
A
440
75.684
49.014
3.361
1.00
44.65
N


ATOM
2405
CA
ALA
A
440
76.914
48.689
4.067
1.00
44.96
C


ATOM
2406
C
ALA
A
440
77.335
47.239
3.880
1.00
44.76
C


ATOM
2407
O
ALA
A
440
78.424
46.847
4.294
1.00
45.32
O


ATOM
2408
CB
ALA
A
440
76.751
49.001
5.549
1.00
44.41
C


ATOM
2409
N
GLY
A
441
76.479
46.447
3.248
1.00
44.13
N


ATOM
2410
CA
GLY
A
441
76.803
45.049
3.041
1.00
43.90
C


ATOM
2411
C
GLY
A
441
76.135
44.176
4.087
1.00
43.49
C


ATOM
2412
O
GLY
A
441
75.115
44.559
4.660
1.00
43.21
O


ATOM
2413
N
LYS
A
442
76.713
43.005
4.341
1.00
44.00
N


ATOM
2414
CA
LYS
A
442
76.171
42.064
5.318
1.00
44.24
C


ATOM
2415
C
LYS
A
442
76.360
42.533
6.757
1.00
43.92
C


ATOM
2416
O
LYS
A
442
77.363
43.171
7.091
1.00
44.02
O


ATOM
2417
CB
LYS
A
442
76.834
40.697
5.142
1.00
46.18
C


ATOM
2418
CG
LYS
A
442
76.608
40.085
3.766
1.00
50.07
C


ATOM
2419
CD
LYS
A
442
75.542
38.992
3.794
1.00
51.33
C


ATOM
2420
CE
LYS
A
442
76.086
37.716
4.431
1.00
54.42
C


ATOM
2421
NZ
LYS
A
442
75.115
36.573
4.373
1.00
55.91
N


ATOM
2422
N
LEU
A
443
75.393
42.200
7.605
1.00
42.94
N


ATOM
2423
CA
LEU
A
443
75.421
42.568
9.018
1.00
41.75
C


ATOM
2424
C
LEU
A
443
76.697
42.133
9.746
1.00
42.03
C


ATOM
2425
O
LEU
A
443
77.295
42.912
10.485
1.00
40.47
O


ATOM
2426
CB
LEU
A
443
74.201
41.968
9.726
1.00
40.09
C


ATOM
2427
CG
LEU
A
443
74.055
42.185
11.238
1.00
39.89
C


ATOM
2428
CD1
LEU
A
443
72.596
42.020
11.640
1.00
38.06
C


ATOM
2429
CD2
LEU
A
443
74.937
41.200
11.997
1.00
38.79
C


ATOM
2430
N
LYS
A
444
77.108
40.890
9.522
1.00
42.70
N


ATOM
2431
CA
LYS
A
444
78.281
40.315
10.178
1.00
44.85
C


ATOM
2432
C
LYS
A
444
79.577
41.134
10.229
1.00
45.18
C


ATOM
2433
O
LYS
A
444
80.073
41.445
11.314
1.00
44.50
O


ATOM
2434
CB
LYS
A
444
78.595
38.945
9.571
1.00
46.48
C


ATOM
2435
CG
LYS
A
444
79.616
38.150
10.374
1.00
50.45
C


ATOM
2436
CD
LYS
A
444
79.867
36.779
9.768
1.00
53.23
C


ATOM
2437
CE
LYS
A
444
80.731
35.935
10.688
1.00
54.88
C


ATOM
2438
NZ
LYS
A
444
82.030
36.605
10.975
1.00
55.49
N


ATOM
2439
N
ASP
A
445
80.134
41.466
9.068
1.00
45.06
N


ATOM
2440
CA
ASP
A
445
81.388
42.212
9.017
1.00
45.21
C


ATOM
2441
C
ASP
A
445
81.284
43.592
9.636
1.00
43.85
C


ATOM
2442
O
ASP
A
445
82.255
44.105
10.192
1.00
43.92
O


ATOM
2443
CB
ASP
A
445
81.880
42.349
7.573
1.00
48.38
C


ATOM
2444
CG
ASP
A
445
82.108
41.005
6.902
1.00
51.51
C


ATOM
2445
OD1
ASP
A
445
82.776
40.133
7.507
1.00
52.73
O


ATOM
2446
OD2
ASP
A
445
81.620
40.825
5.766
1.00
53.93
O


ATOM
2447
N
ASN
A
446
80.110
44.195
9.533
1.00
41.34
N


ATOM
2448
CA
ASN
A
446
79.900
45.522
10.086
1.00
40.70
C


ATOM
2449
C
ASN
A
446
79.815
45.501
11.605
1.00
39.56
C


ATOM
2450
O
ASN
A
446
80.439
46.318
12.273
1.00
40.02
O


ATOM
2451
CB
ASN
A
446
78.637
46.126
9.491
1.00
40.72
C


ATOM
2452
CG
ASN
A
446
78.823
46.520
8.046
1.00
41.93
C


ATOM
2453
OD1
ASN
A
446
79.347
47.601
7.748
1.00
42.76
O


ATOM
2454
ND2
ASN
A
446
78.416
45.640
7.134
1.00
39.05
N


ATOM
2455
N
VAL
A
447
79.039
44.571
12.146
1.00
38.14
N


ATOM
2456
CA
VAL
A
447
78.901
44.450
13.590
1.00
38.14
C


ATOM
2457
C
VAL
A
447
80.251
44.071
14.215
1.00
38.90
C


ATOM
2458
O
VAL
A
447
80.594
44.534
15.295
1.00
38.04
O


ATOM
2459
CB
VAL
A
447
77.837
43.386
13.952
1.00
37.40
C


ATOM
2460
CG1
VAL
A
447
77.891
43.065
15.437
1.00
37.24
C


ATOM
2461
CG2
VAL
A
447
76.454
43.899
13.579
1.00
36.23
C


ATOM
2462
N
GLU
A
448
81.018
43.235
13.524
1.00
39.10
N


ATOM
2463
CA
GLU
A
448
82.313
42.826
14.039
1.00
39.82
C


ATOM
2464
C
GLU
A
448
83.247
44.036
14.100
1.00
37.84
C


ATOM
2465
O
GLU
A
448
83.963
44.222
15.078
1.00
36.51
O


ATOM
2466
CB
GLU
A
448
82.917
41.728
13.153
1.00
42.41
C


ATOM
2467
CG
GLU
A
448
84.226
41.149
13.677
1.00
48.39
C


ATOM
2468
CD
GLU
A
448
84.802
40.073
12.760
1.00
53.42
C


ATOM
2469
OE1
GLU
A
448
85.409
40.422
11.718
1.00
53.76
O


ATOM
2470
OE2
GLU
A
448
84.634
38.871
13.078
1.00
56.37
O


ATOM
2471
N
ALA
A
449
83.235
44.854
13.053
1.00
36.52
N


ATOM
2472
CA
ALA
A
449
84.081
46.045
13.006
1.00
36.71
C


ATOM
2473
C
ALA
A
449
83.704
47.016
14.122
1.00
36.23
C


ATOM
2474
O
ALA
A
449
84.572
47.530
14.823
1.00
36.73
O


ATOM
2475
CB
ALA
A
449
83.951
46.741
11.646
1.00
34.97
C


ATOM
2476
N
SER
A
450
82.406
47.262
14.277
1.00
34.72
N


ATOM
2477
CA
SER
A
450
81.914
48.166
15.310
1.00
34.31
C


ATOM
2478
C
SER
A
450
82.313
47.717
16.714
1.00
34.50
C


ATOM
2479
O
SER
A
450
82.868
48.501
17.493
1.00
31.24
O


ATOM
2480
CB
SER
A
450
80.387
48.279
15.235
1.00
33.37
C


ATOM
2481
OG
SER
A
450
79.991
49.068
14.130
1.00
33.43
O


ATOM
2482
N
LEU
A
451
82.043
46.450
17.026
1.00
34.30
N


ATOM
2483
CA
LEU
A
451
82.348
45.923
18.346
1.00
35.10
C


ATOM
2484
C
LEU
A
451
83.838
45.784
18.631
1.00
36.71
C


ATOM
2485
O
LEU
A
451
84.245
45.789
19.791
1.00
36.58
O


ATOM
2486
CB
LEU
A
451
81.6.21
44.596
18.565
1.00
34.20
C


ATOM
2487
CG
LEU
A
451
80.095
44.766
18.562
1.00
34.08
C


ATOM
2488
CD1
LEU
A
451
79.423
43.457
18.926
1.00
32.06
C


ATOM
2489
CD2
LEU
A
451
79.693
45.861
19.543
1.00
32.22
C


ATOM
2490
N
ASN
A
452
84.655
45.665
17.588
1.00
37.71
N


ATOM
2491
CA
ASN
A
452
86.089
45.579
17.811
1.00
39.20
C


ATOM
2492
C
ASN
A
452
86.536
46.934
18.347
1.00
38.74
C


ATOM
2493
O
ASN
A
452
87.394
47.009
19.231
1.00
38.71
O


ATOM
2494
CB
ASN
A
452
86.853
45.263
16.523
1.00
40.36
C


ATOM
2495
CG
ASN
A
452
86.888
43.781
16.215
1.00
44.54
C


ATOM
2496
OD1
ASN
A
452
86.761
42.940
17.113
1.00
46.29
O


ATOM
2497
ND2
ASN
A
452
87.085
43.447
14.941
1.00
46.83
N


ATOM
2498
N
LYS
A
453
85.949
48.001
17.812
1.00
37.17
N


ATOM
2499
CA
LYS
A
453
86.292
49.347
18.256
1.00
37.39
C


ATOM
2500
C
LYS
A
453
85.809
49.571
19.685
1.00
35.35
C


ATOM
2501
O
LYS
A
453
86.501
50.197
20.481
1.00
35.05
O


ATOM
2502
CB
LYS
A
453
85.700
50.395
17.303
1.00
38.34
C


ATOM
2503
CG
LYS
A
453
86.488
50.492
15.995
1.00
42.57
C


ATOM
2504
CD
LYS
A
453
85.717
51.157
14.858
1.00
44.00
C


ATOM
2505
CE
LYS
A
453
85.478
52.635
15.094
1.00
45.69
C


ATOM
2506
NZ
LYS
A
453
84.699
53.222
13.962
1.00
46.71
N


ATOM
2507
N
VAL
A
454
84.631
49.048
20.008
1.00
32.74
N


ATOM
2508
CA
VAL
A
454
84.093
49.188
21.352
1.00
31.66
C


ATOM
2509
C
VAL
A
454
85.019
48.455
22.328
1.00
32.27
C


ATOM
2510
O
VAL
A
454
85.418
49.007
23.358
1.00
30.47
O


ATOM
2511
CB
VAL
A
454
82.663
48.597
21.455
1.00
31.71
C


ATOM
2512
CG1
VAL
A
454
82.225
48.527
22.920
1.00
30.29
C


ATOM
2513
CG2
VAL
A
454
81.680
49.459
20.651
1.00
30.64
C


ATOM
2514
N
LYS
A
455
85.365
47.216
21.989
1.00
32.48
N


ATOM
2515
CA
LYS
A
455
86.245
46.402
22.828
1.00
34.26
C


ATOM
2516
C
LYS
A
455
87.589
47.081
23.053
1.00
34.74
C


ATOM
2517
O
LYS
A
455
88.123
47.081
24.162
1.00
34.39
O


ATOM
2518
CB
LYS
A
455
86.483
45.035
22.182
1.00
34.75
C


ATOM
2519
CG
LYS
A
455
85.336
44.055
22.297
1.00
35.60
C


ATOM
2520
CD
LYS
A
455
85.607
42.860
21.395
1.00
38.09
C


ATOM
2521
CE
LYS
A
455
84.529
41.811
21.508
1.00
41.48
C


ATOM
2522
NZ
LYS
A
455
84.809
40.638
20.627
1.00
41.09
N


ATOM
2523
N
SER
A
456
88.140
47.652
21.989
1.00
35.13
N


ATOM
2524
CA
SER
A
456
89.421
48.327
22.090
1.00
36.02
C


ATOM
2525
C
SER
A
456
89.313
49.533
23.031
1.00
35.16
C


ATOM
2526
O
SER
A
456
90.171
49.744
23.890
1.00
33.17
O


ATOM
2527
CB
SER
A
456
89.888
48.764
20.702
1.00
36.46
C


ATOM
2528
OG
SER
A
456
91.172
49.341
20.779
1.00
39.49
O


ATOM
2529
N
THR
A
457
88.254
50.320
22.875
1.00
33.64
N


ATOM
2530
CA
THR
A
457
88.056
51.478
23.734
1.00
33.01
C


ATOM
2531
C
THR
A
457
87.863
51.029
25.182
1.00
32.03
C


ATOM
2532
O
THR
A
457
88.352
51.672
26.108
1.00
32.59
O


ATOM
2533
CB
THR
A
457
86.835
52.297
23.286
1.00
32.27
C


ATOM
2534
OG1
THR
A
457
87.050
52.756
21.949
1.00
34.93
O


ATOM
2535
CG2
THR
A
457
86.624
53.497
24.193
1.00
29.23
C


ATOM
2536
N
MET
A
458
87.150
49.926
25.379
1.00
31.95
N


ATOM
2537
CA
MET
A
458
86.925
49.419
26.723
1.00
30.89
C


ATOM
2538
C
MET
A
458
88.256
49.114
27.407
1.00
32.55
C


ATOM
2539
O
MET
A
458
88.426
49.391
28.598
1.00
31.39
O


ATOM
2540
CB
MET
A
458
86.031
48.179
26.683
1.00
30.61
C


ATOM
2541
CG
MET
A
458
84.548
48.518
26.564
1.00
28.50
C


ATOM
2542
SD
MET
A
458
83.488
47.100
26.262
1.00
29.80
S


ATOM
2543
CE
MET
A
458
83.570
46.223
27.839
1.00
27.13
C


ATOM
2544
N
CYS
A
459
89.211
48.568
26.660
1.00
32.81
N


ATOM
2545
CA
CYS
A
459
90.508
48.281
27.257
1.00
34.73
C


ATOM
2546
C
CYS
A
459
91.260
49.572
27.583
1.00
34.20
C


ATOM
2547
O
CYS
A
459
91.998
49.620
28.566
1.00
33.88
O


ATOM
2548
CB
CYS
A
459
91.347
47.380
26.350
1.00
36.62
C


ATOM
2549
SG
CYS
A
459
90.944
45.616
26.569
1.00
40.92
S


ATOM
2550
N
ASN
A
460
91.075
50.610
26.766
1.00
32.61
N


ATOM
2551
CA
ASN
A
460
91.721
51.892
27.034
1.00
32.54
C


ATOM
2552
C
ASN
A
460
91.176
52.381
28.368
1.00
31.81
C


ATOM
2553
O
ASN
A
460
91.853
53.091
29.098
1.00
32.53
O


ATOM
2554
CB
ASN
A
460
91.371
52.947
25.976
1.00
33.21
C


ATOM
2555
CG
ASN
A
460
92.034
52.693
24.646
1.00
35.78
C


ATOM
2556
OD1
ASN
A
460
91.356
52.543
23.633
1.00
36.50
O


ATOM
2557
ND2
ASN
A
460
93.365
52.648
24.634
1.00
34.40
N


ATOM
2558
N
CYS
A
461
89.932
52.010
28.668
1.00
31.68
N


ATOM
2559
CA
CYS
A
461
89.285
52.423
29.907
1.00
31.03
C


ATOM
2560
C
CYS
A
461
89.515
51.437
31.053
1.00
31.06
C


ATOM
2561
O
CYS
A
461
89.005
51.630
32.146
1.00
32.13
O


ATOM
2562
CB
CYS
A
461
87.777
52.617
29.675
1.00
32.30
C


ATOM
2563
SG
CYS
A
461
87.364
53.913
28.455
1.00
34.10
S


ATOM
2564
N
GLY
A
462
90.281
50.381
30.795
1.00
31.97
N


ATOM
2565
CA
GLY
A
462
90.569
49.393
31.822
1.00
31.72
C


ATOM
2566
C
GLY
A
462
89.412
48.464
32.149
1.00
32.82
C


ATOM
2567
O
GLY
A
462
89.277
47.995
33.282
1.00
32.24
O


ATOM
2568
N
ALA
A
463
88.588
48.171
31.151
1.00
31.78
N


ATOM
2569
CA
ALA
A
463
87.427
47.320
31.362
1.00
31.54
C


ATOM
2570
C
ALA
A
463
87.420
46.075
30.484
1.00
32.00
C


ATOM
2571
O
ALA
A
463
87.657
46.150
29.278
1.00
31.09
O


ATOM
2572
CB
ALA
A
463
86.160
48.132
31.126
1.00
30.25
C


ATOM
2573
N
LEU
A
464
87.152
44.928
31.102
1.00
32.25
N


ATOM
2574
CA
LEU
A
464
87.095
43.661
30.377
1.00
33.90
C


ATOM
2575
C
LEU
A
464
85.652
43.241
30.158
1.00
32.84
C


ATOM
2576
O
LEU
A
464
85.380
42.324
29.386
1.00
34.74
O


ATOM
2577
CB
LEU
A
464
87.829
42.550
31.144
1.00
34.92
C


ATOM
2578
CG
LEU
A
464
89.345
42.457
30.945
1.00
36.98
C


ATOM
2579
CD1
LEU
A
464
89.906
41.276
31.739
1.00
38.71
C


ATOM
2580
CD2
LEU
A
464
89.647
42.278
29.470
1.00
37.33
C


ATOM
2581
N
THR
A
465
84.732
43.906
30.850
1.00
31.76
N


ATOM
2582
CA
THR
A
465
83.312
43.602
30.734
1.00
30.63
C


ATOM
2583
C
THR
A
465
82.499
44.887
30.760
1.00
31.08
C


ATOM
2584
O
THR
A
465
83.005
45.953
31.122
1.00
29.95
O


ATOM
2585
CB
THR
A
465
82.835
42.718
31.891
1.00
31.43
C


ATOM
2586
OG1
THR
A
465
82.906
43.464
33.110
1.00
32.51
O


ATOM
2587
CG2
THR
A
465
83.710
41.464
32.010
1.00
30.28
C


ATOM
2588
N
ILE
A
466
81.234
44.791
30.377
1.00
29.59
N


ATOM
2589
CA
ILE
A
466
80.386
45.965
30.376
1.00
28.97
C


ATOM
2590
C
ILE
A
466
80.180
46.491
31.797
1.00
28.90
C


ATOM
2591
O
ILE
A
466
80.254
47.696
32.034
1.00
29.22
O


ATOM
2592
CB
ILE
A
466
79.035
45.662
29.695
1.00
29.12
C


ATOM
2593
CG1
ILE
A
466
79.270
45.502
28.187
1.00
27.85
C


ATOM
2594
CG2
ILE
A
466
78.028
46.770
29.985
1.00
26.21
C


ATOM
2595
CD1
ILE
A
466
78.052
45.094
27.404
1.00
27.38
C


ATOM
2596
N
PRO
A
467
79.923
45.597
32.765
1.00
28.55
N


ATOM
2597
CA
PRO
A
467
79.733
46.105
34.125
1.00
28.14
C


ATOM
2598
C
PRO
A
467
80.986
46.813
34.642
1.00
29.41
C


ATOM
2599
O
PRO
A
467
80.905
47.805
35.373
1.00
28.53
O


ATOM
2600
CB
PRO
A
467
79.405
44.842
34.919
1.00
29.15
C


ATOM
2601
CG
PRO
A
467
78.676
43.992
33.890
1.00
28.98
C


ATOM
2602
CD
PRO
A
467
79.588
44.163
32.688
1.00
27.09
C


ATOM
2603
N
GLN
A
468
82.151
46.314
34.253
1.00
30.32
N


ATOM
2604
CA
GLN
A
468
83.386
46.929
34.705
1.00
32.43
C


ATOM
2605
C
GLN
A
468
83.566
48.299
34.049
1.00
32.77
C


ATOM
2606
O
GLN
A
468
84.100
49.233
34.657
1.00
32.94
O


ATOM
2607
CB
GLN
A
468
84.561
46.006
34.390
1.00
34.93
C


ATOM
2608
CG
GLN
A
468
85.869
46.461
34.969
1.00
36.80
C


ATOM
2609
CD
GLN
A
468
86.912
45.364
34.940
1.00
37.36
C


ATOM
2610
OE1
GLN
A
468
87.016
44.611
33.971
1.00
33.81
O


ATOM
2611
NE2
GLN
A
468
87.703
45.281
36.000
1.00
38.34
N


ATOM
2612
N
LEU
A
469
83.106
48.418
32.808
1.00
31.40
N


ATOM
2613
CA
LEU
A
469
83.191
49.672
32.082
1.00
30.05
C


ATOM
2614
C
LEU
A
469
82.263
50.700
32.729
1.00
29.95
C


ATOM
2615
O
LEU
A
469
82.628
51.862
32.899
1.00
29.45
O


ATOM
2616
CB
LEU
A
469
82.780
49.471
30.620
1.00
30.63
C


ATOM
2617
CG
LEU
A
469
82.579
50.765
29.819
1.00
32.08
C


ATOM
2618
CD1
LEU
A
469
83.925
51.423
29.568
1.00
29.55
C


ATOM
2619
CD2
LEU
A
469
81.882
50.454
28.493
1.00
32.46
C


ATOM
2620
N
GLN
A
470
81.062
50.267
33.092
1.00
29.40
N


ATOM
2621
CA
GLN
A
470
80.089
51.169
33.697
1.00
31.46
C


ATOM
2622
C
GLN
A
470
80.599
51.680
35.039
1.00
33.28
C


ATOM
2623
O
GLN
A
470
80.275
52.790
35.479
1.00
32.37
O


ATOM
2624
CB
GLN
A
470
78.748
50.444
33.859
1.00
31.66
C


ATOM
2625
CG
GLN
A
470
78.209
49.929
32.515
1.00
32.34
C


ATOM
2626
CD
GLN
A
470
76.891
49.192
32.633
1.00
33.38
C


ATOM
2627
OE1
GLN
A
470
76.671
48.454
33.585
1.00
34.59
O


ATOM
2628
NE2
GLN
A
470
76.017
49.375
31.652
1.00
31.58
N


ATOM
2629
N
SER
A
471
81.435
50.870
35.668
1.00
33.02
N


ATOM
2630
CA
SER
A
471
81.997
51.222
36.955
1.00
34.85
C


ATOM
2631
C
SER
A
471
83.239
52.119
36.863
1.00
33.52
C


ATOM
2632
O
SER
A
471
83.374
53.070
37.625
1.00
34.04
O


ATOM
2633
CB
SER
A
471
82.329
49.934
37.722
1.00
34.20
C


ATOM
2634
OG
SER
A
471
82.985
50.221
38.940
1.00
40.00
O


ATOM
2635
N
LYS
A
472
84.121
51.837
35.910
1.00
33.54
N


ATOM
2636
CA
LYS
A
472
8.5.375
52.582
35.774
1.00
33.02
C


ATOM
2637
C
LYS
A
472
85.437
53.746
34.784
1.00
32.17
C


ATOM
2638
O
LYS
A
472
86.312
54.599
34.904
1.00
32.35
O


ATOM
2639
CB
LYS
A
472
86.505
51.605
35.431
1.00
33.39
C


ATOM
2640
CG
LYS
A
472
86.599
50.420
36.374
1.00
35.66
C


ATOM
2641
CD
LYS
A
472
87.597
49.369
35.885
1.00
37.76
C


ATOM
2642
CE
LYS
A
472
89.036
49.761
36.185
1.00
40.51
C


ATOM
2643
NZ
LYS
A
472
90.004
48.705
35.750
1.00
41.85
N


ATOM
2644
N
ALA
A
473
84.538
53.782
33.804
1.00
30.79
N


ATOM
2645
CA
ALA
A
473
84.563
54.849
32.806
1.00
30.86
C


ATOM
2646
C
ALA
A
473
84.644
56.263
33.382
1.00
30.77
C


ATOM
2647
O
ALA
A
473
83.971
56.599
34.358
1.00
31.90
O


ATOM
2648
CB
ALA
A
473
83.343
54.738
31.882
1.00
30.21
C


ATOM
2649
N
LYS
A
474
85.491
57.077
32.762
1.00
31.21
N


ATOM
2650
CA
LYS
A
474
85.685
58.476
33.136
1.00
31.60
C


ATOM
2651
C
LYS
A
474
85.118
59.211
31.930
1.00
32.45
C


ATOM
2652
O
LYS
A
474
85.681
59.165
30.829
1.00
30.42
O


ATOM
2653
CB
LYS
A
474
87.175
58.769
33.326
1.00
30.92
C


ATOM
2654
CG
LYS
A
474
87.773
58.010
34.520
1.00
31.60
C


ATOM
2655
CD
LYS
A
474
89.251
57.668
34.302
1.00
32.08
C


ATOM
2656
CE
LYS
A
474
90.125
58.906
34.302
1.00
32.99
C


ATOM
2657
NZ
LYS
A
474
91.550
58.543
34.039
1.00
33.32
N


ATOM
2658
N
ILE
A
475
83.990
59.875
32.146
1.00
32.69
N


ATOM
2659
CA
ILE
A
475
83.285
60.546
31.066
1.00
33.22
C


ATOM
2660
C
ILE
A
475
83.237
62.056
31.203
1.00
32.93
C


ATOM
2661
O
ILE
A
475
82.713
62.581
32.183
1.00
33.43
O


ATOM
2662
CB
ILE
A
475
81.848
59.991
30.977
1.00
33.86
C


ATOM
2663
CG1
ILE
A
475
81.907
58.456
30.907
1.00
34.55
C


ATOM
2664
CG2
ILE
A
475
81.128
60.569
29.758
1.00
34.88
C


ATOM
2665
CD1
ILE
A
475
80.562
57.756
31.036
1.00
33.21
C


ATOM
2666
N
THR
A
476
83.786
62.751
30.212
1.00
32.44
N


ATOM
2667
CA
THR
A
476
83.792
64.206
30.239
1.00
31.82
C


ATOM
2668
C
THR
A
476
82.921
64.803
29.154
1.00
31.41
C


ATOM
2669
O
THR
A
476
82.734
64.225
28.084
1.00
29.60
O


ATOM
2670
CB
THR
A
476
85.212
64.803
30.054
1.00
31.71
C


ATOM
2671
OG1
THR
A
476
85.143
66.233
30.185
1.00
32.39
O


ATOM
2672
CG2
THR
A
476
85.770
64.464
28.665
1.00
28.14
C


ATOM
2673
N
LEU
A
477
82.391
65.977
29.461
1.00
32.16
N


ATOM
2674
CA
LEU
A
477
81.569
66.737
28.542
1.00
34.25
C


ATOM
2675
C
LEU
A
477
82.595
67.593
27.787
1.00
34.56
C


ATOM
2676
O
LEU
A
477
83.646
67.907
28.345
1.00
32.54
O


ATOM
2677
CB
LEU
A
477
80.622
67.621
29.357
1.00
35.42
C


ATOM
2678
CG
LEU
A
477
79.408
68.279
28.719
1.00
37.43
C


ATOM
2679
CD1
LEU
A
477
78.496
67.223
28.120
1.00
34.96
C


ATOM
2680
CD2
LEU
A
477
78.667
69.082
29.798
1.00
39.05
C


ATOM
2681
N
VAL
A
478
82.320
67.941
26.531
1.00
35.71
N


ATOM
2682
CA
VAL
A
478
83.242
68.778
25.761
1.00
38.92
C


ATOM
2683
C
VAL
A
478
82.573
70.119
25.463
1.00
41.05
C


ATOM
2684
O
VAL
A
478
81.359
70.187
25.298
1.00
40.84
O


ATOM
2685
CB
VAL
A
478
83.659
68.111
24.428
1.00
39.90
C


ATOM
2686
CG1
VAL
A
478
84.015
66.662
24.672
1.00
40.76
C


ATOM
2687
CG2
VAL
A
478
82.551
68.237
23.400
1.00
41.86
C


ATOM
2688
N
SER
A
479
83.370
71.181
25.386
1.00
43.62
N


ATOM
2689
CA
SER
A
479
82.849
72.525
25.147
1.00
47.07
C


ATOM
2690
C
SER
A
479
82.082
72.745
23.854
1.00
50.19
C


ATOM
2691
O
SER
A
479
82.356
72.129
22.821
1.00
49.40
O


ATOM
2692
CB
SER
A
479
83.979
73.553
25.207
1.00
46.48
C


ATOM
2693
OG
SER
A
479
84.904
73.327
24.160
1.00
46.18
O


ATOM
2694
N
SER
A
480
81.124
73.662
23.933
1.00
54.55
N


ATOM
2695
CA
SER
A
480
80.297
74.036
22.799
1.00
59.07
C


ATOM
2696
C
SER
A
480
81.192
74.534
21.668
1.00
61.48
C


ATOM
2697
O
SER
A
480
81.036
74.146
20.505
1.00
61.36
O


ATOM
2698
CB
SER
A
480
79.327
75.143
23.224
1.00
59.36
C


ATOM
2699
OG
SER
A
480
78.625
75.669
22.113
1.00
62.01
O


ATOM
2700
N
VAL
A
481
82.145
75.382
22.040
1.00
64.75
N


ATOM
2701
CA
VAL
A
481
83.088
75.982
21.104
1.00
67.50
C


ATOM
2702
C
VAL
A
481
84.162
75.015
20.611
1.00
69.03
C


ATOM
2703
O
VAL
A
481
85.113
75.432
19.949
1.00
69.98
O


ATOM
2704
CB
VAL
A
481
83.804
77.179
21.753
1.00
67.66
C


ATOM
2705
CG1
VAL
A
481
84.155
78.211
20.693
1.00
68.62
C


ATOM
2706
CG2
VAL
A
481
82.935
77.775
22.841
1.00
67.94
C


ATOM
2707
N
SER
A
482
84.016
73.731
20.922
1.00
70.23
N


ATOM
2708
CA
SER
A
482
85.010
72.749
20.504
1.00
71.93
C


ATOM
2709
C
SER
A
482
84.445
71.675
19.590
1.00
73.15
C


ATOM
2710
O
SER
A
482
83.495
71.916
18.841
1.00
73.05
O


ATOM
2711
CB
SER
A
482
85.636
72.068
21.724
1.00
72.51
C


ATOM
2712
OG
SER
A
482
84.711
71.185
22.344
1.00
72.87
O


ATOM
2713
N
ILE
A
483
85.048
70.487
19.686
1.00
74.34
N


ATOM
2714
CA
ILE
A
483
84.698
69.305
18.899
1.00
75.21
C


ATOM
2715
C
ILE
A
483
85.510
69.316
17.609
1.00
75.65
C


ATOM
2716
O
ILE
A
483
85.821
68.263
17.049
1.00
75.17
O


ATOM
2717
CB
ILE
A
483
83.189
69.254
18.536
1.00
75.76
C


ATOM
2718
CG1
ILE
A
483
82.338
69.219
19.809
1.00
75.65
C


ATOM
2719
CG2
ILE
A
483
82.903
68.025
17.680
1.00
75.47
C


ATOM
2720
CD1
ILE
A
483
80.852
69.350
19.554
1.00
74.79
C


ATOM
2721
N
VAL
A
484
85.854
70.517
17.150
1.00
76.42
N


ATOM
2722
CA
VAL
A
484
86.630
70.686
15.924
1.00
77.07
C


ATOM
2723
C
VAL
A
484
88.022
70.077
16.085
1.00
77.20
C


ATOM
2724
O
VAL
A
484
88.540
69.442
15.163
1.00
77.05
O


ATOM
2725
CB
VAL
A
484
86.773
72.186
15.549
1.00
77.33
C


ATOM
2726
CG1
VAL
A
484
87.463
72.322
14.193
1.00
77.06
C


ATOM
2727
CG2
VAL
A
484
85.401
72.853
15.521
1.00
76.24
C


ATOM
2728
N
GLU
A
485
88.620
70.272
17.259
1.00
77.14
N


ATOM
2729
CA
GLU
A
485
89.948
69.733
17.545
1.00
77.36
C


ATOM
2730
C
GLU
A
485
89.935
68.210
17.439
1.00
77.78
C


ATOM
2731
O
GLU
A
485
90.907
67.599
16.991
1.00
77.16
O


ATOM
2732
CB
GLU
A
485
90.398
70.127
18.957
1.00
76.63
C


ATOM
2733
CG
GLU
A
485
91.730
69.499
19.372
1.00
76.08
C


ATOM
2734
CD
GLU
A
485
92.030
69.654
20.854
1.00
75.36
C


ATOM
2735
OE1
GLU
A
485
91.261
69.135
21.687
1.00
75.07
O


ATOM
2736
OE2
GLU
A
485
93.041
70.294
21.190
1.00
75.66
O


ATOM
2737
N
GLY
A
486
88.824
67.610
17.861
1.00
78.37
N


ATOM
2738
CA
GLY
A
486
88.682
66.165
17.831
1.00
79.06
C


ATOM
2739
C
GLY
A
486
88.873
65.533
16.466
1.00
79.40
C


ATOM
2740
O
GLY
A
486
89.530
64.499
16.348
1.00
79.68
O


ATOM
2741
N
GLY
A
487
88.295
66.145
15.435
1.00
79.72
N


ATOM
2742
CA
GLY
A
487
88.428
65.611
14.091
1.00
79.91
C


ATOM
2743
C
GLY
A
487
89.646
66.164
13.376
1.00
80.25
C


ATOM
2744
O
GLY
A
487
90.467
66.857
13.982
1.00
80.14
O


ATOM
2745
N
ALA
A
488
89.773
65.854
12.088
1.00
80.34
N


ATOM
2746
CA
ALA
A
488
90.896
66.341
11.292
1.00
80.30
C


ATOM
2747
C
ALA
A
488
90.694
67.833
11.037
1.00
80.42
C


ATOM
2748
O
ALA
A
488
89.584
68.272
10.730
1.00
79.93
O


ATOM
2749
CB
ALA
A
488
90.972
65.584
9.969
1.00
79.95
C


ATOM
2750
N
HIS
A
489
91.763
68.612
11.165
1.00
80.61
N


ATOM
2751
CA
HIS
A
489
91.661
70.052
10.957
1.00
81.04
C


ATOM
2752
C
HIS
A
489
92.937
70.687
10.424
1.00
81.07
C


ATOM
2753
O
HIS
A
489
94.046
70.253
10.742
1.00
80.28
O


ATOM
2754
CB
HIS
A
489
91.271
70.743
12.266
1.00
81.48
C


ATOM
2755
CG
HIS
A
489
92.196
70.442
13.405
1.00
81.91
C


ATOM
2756
ND1
HIS
A
489
92.241
69.210
14.020
1.00
81.93
N


ATOM
2757
CD2
HIS
A
489
93.121
71.209
14.030
1.00
81.89
C


ATOM
2758
CE1
HIS
A
489
93.153
69.231
14.976
1.00
81.92
C


ATOM
2759
NE2
HIS
A
489
93.702
70.432
15.002
1.00
81.66
N


ATOM
2760
N
ASP
A
490
92.758
71.727
9.614
1.00
81.38
N


ATOM
2761
CA
ASP
A
490
93.870
72.467
9.027
1.00
81.57
C


ATOM
2762
C
ASP
A
490
94.730
71.605
8.111
1.00
81.88
C


ATOM
2763
O
ASP
A
490
95.940
71.810
7.997
1.00
81.99
O


ATOM
2764
CB
ASP
A
490
94.721
73.079
10.141
1.00
81.37
C


ATOM
2765
CG
ASP
A
490
93.915
73.990
11.046
1.00
81.51
C


ATOM
2766
OD1
ASP
A
490
93.484
75.069
10.579
1.00
81.11
O


ATOM
2767
OD2
ASP
A
490
93.701
73.622
12.220
1.00
81.49
O


ATOM
2768
N
VAL
A
491
94.093
70.638
7.462
1.00
81.98
N


ATOM
2769
CA
VAL
A
491
94.779
69.748
6.537
1.00
82.24
C


ATOM
2770
C
VAL
A
491
93.841
69.392
5.390
1.00
82.41
C


ATOM
2771
O
VAL
A
491
92.621
69.331
5.566
1.00
81.92
O


ATOM
2772
CB
VAL
A
491
95.252
68.440
7.231
1.00
82.15.
C


ATOM
2773
CG1
VAL
A
491
96.314
68.755
8.273
1.00
82.08
C


ATOM
2774
CG2
VAL
A
491
94.069
67.727
7.873
1.00
82.18
C


ATOM
2775
N
ILE
A
492
94.419
69.169
4.215
1.00
82.73
N


ATOM
2776
CA
ILE
A
492
93.651
68.816
3.029
1.00
83.15
C


ATOM
2777
C
ILE
A
492
93.731
67.309
2.792
1.00
83.71
C


ATOM
2778
O
ILE
A
492
94.558
66.887
1.954
1.00
84.19
O


ATOM
2779
CB
ILE
A
492
94.180
69.565
1.782
1.00
83.08
C


ATOM
2780
CG1
ILE
A
492
94.136
71.075
2.032
1.00
82.87
C


ATOM
2781
CG2
ILE
A
492
93.342
69.211
0.560
1.00
82.77
C


ATOM
2782
CD1
ILE
A
492
94.640
71.911
0.874
1.00
83.43
C


TER
2783

ILE
A
492


HETATM
2784
NA
NA

901
65.965
62.918
15.945
1.00
69.25
NA


HETATM
2785
K
K
A
900
94.585
53.172
29.328
0.75
36.10
K


HETATM
2786
P
RVP
602
67.957
55.327
15.029
1.00
40.98
P


HETATM
2787
O1P
RVP
602
67.605
55.290
13.581
1.00
40.82
O


HETATM
2788
O2P
RVP
602
68.778
54.118
15.349
1.00
40.06
O


HETATM
2789
O3P
RVP
602
68.738
56.618
15.412
1.00
40.73
O


HETATM
2790
O5*
RVP
602
66.712
55.356
16.019
1.00
39.48
O


HETATM
2791
C5*
RVP
602
65.743
54.315
15.953
1.00
38.43
C


HETATM
2792
C4*
RVP
602
64.678
54.509
16.989
1.00
38.00
C


HETATM
2793
O4*
RVP
602
63.938
55.721
16.576
1.00
38.49
O


HETATM
2794
C3*
RVP
602
63.577
53.475
17.169
1.00
36.61
C


HETATM
2795
O3*
RVP
602
63.978
52.319
17.881
1.00
35.40
O


HETATM
2796
C2*
RVP
602
62.504
54.269
17.841
1.00
36.75
C


HETATM
2797
O2*
RVP
602
62.653
54.352
19.240
1.00
36.68
O


HETATM
2798
C1*
RVP
602
62.606
55.609
17.106
1.00
38.31
C


HETATM
2799
N9
RVP
602
61.637
55.746
15.950
1.00
40.51
N


HETATM
2800
C8
RVP
602
61.076
54.833
15.070
1.00
40.32
C


HETATM
2801
N7
RVP
602
60.285
55.383
14.214
1.00
40.61
N


HETATM
2802
C5
RVP
602
60.285
56.713
14.493
1.00
41.77
C


HETATM
2803
C6
RVP
602
59.586
57.820
13.858
1.00
41.63
C


HETATM
2804
O6
RVP
602
58.824
57.752
12.898
1.00
40.85
O


HETATM
2805
N1
RVP
602
59.848
59.109
14.451
1.00
42.44
N


HETATM
2806
N4
RVP
602
61.119
56.976
15.575
1.00
41.17
N


HETATM
2807
C1
MOA
600
60.515
58.824
19.697
0.50
46.30
C


HETATM
2808
C2
MOA
600
55.761
57.322
16.893
0.50
49.27
C


HETATM
2809
C3
MOA
600
54.536
56.866
16.570
0.50
50.25
C


HETATM
2810
C4
MOA
600
53.366
57.590
17.224
0.50
51.18
C


HETATM
2811
C5
MOA
600
52.702
56.677
18.266
0.50
52.05
C


HETATM
2812
C6
MOA
600
53.320
56.768
19.656
0.50
52.48
C


HETATM
2813
C7
MOA
600
59.541
53.995
20.040
0.50
45.22
C


HETATM
2814
C8
MOA
600
56.392
53.973
18.496
0.50
45.61
C


HETATM
2815
C9
MOA
600
54.279
55.668
15.641
0.50
50.49
C


HETATM
2816
C10
MOA
600
60.943
56.779
20.807
0.50
45.42
C


HETATM
2817
C11
MOA
600
59.925
56.532
19.711
0.50
45.86
C


HETATM
2818
C12
MOA
600
59.265
55.296
19.328
0.50
45.51
C


HETATM
2819
C13
MOA
600
58.321
55.359
18.230
0.50
45.35
C


HETATM
2820
C14
MOA
600
58.073
56.626
17.563
0.50
46.27
C


HETATM
2821
C15
MOA
600
58.756
57.824
17.978
0.50
45.96
C


HETATM
2822
C16
MOA
600
59.679
57.745
19.060
0.50
46.34
C


HETATM
2823
C17
MOA
600
57.082
56.722
16.411
0.50
47.60
C


HETATM
2824
O1
MOA
600
60.600
59.983
19.446
0.50
47.39
O


HETATM
2825
O2
MOA
600
61.200
58.218
20.669
0.50
46.12
O


HETATM
2826
O3
MOA
600
57.682
54.195
17.849
0.50
44.59
O


HETATM
2827
O4
MOA
600
58.494
59.017
17.318
0.50
45.53
O


HETATM
2828
O5
MOA
600
53.045
57.763
20.364
0.50
53.35
O


HETATM
2829
O6
MOA
600
54.072
55.841
20.036
0.50
50.72
O


HETATM
2830
O
HOH
1
86.937
48.115
13.619
1.00
53.10
O


HETATM
2831
O
HOH
2
66.156
60.715
24.787
1.00
30.04
O


HETATM
2832
O
HOH
3
57.859
59.028
28.431
1.00
32.40
O


HETATM
2833
O
HOH
4
71.017
54.648
22.049
1.00
29.86
O


HETATM
2834
O
HOH
5
59.607
45.471
36.968
1.00
31.13
O


HETATM
2835
O
HOH
6
66.879
48.121
38.970
1.00
31.37
O


HETATM
2836
O
HOH
7
79.892
42.101
29.537
1.00
28.27
O


HETATM
2837
O
HOH
8
75.265
45.936
32.827
1.00
34.43
O


HETATM
2838
O
HOH
9
56.912
79.011
34.524
1.00
32.22
O


NETATM
2839
O
HOH
10
71.224
53.547
14.238
1.00
33.27
O


HETATM
2840
O
HOH
11
87.551
55.794
31.268
1.00
29.17
O


HETATM
2841
O
HOH
12
78.951
48.244
37.321
1.00
38.69
O


HETATM
2842
O
HOH
13
76.535
44.032
31.071
1.00
33.29
O


HETATM
2843
O
NOH
14
77.984
54.327
34.370
1.00
35.16
O


HETATM
2844
O
HOH
15
84.500
53.321
21.118
1.00
31.74
O


HETATM
2845
O
HOH
16
74.544
60.085
37.904
1.00
44.09
O


HETATM
2846
O
HOH
17
88.665
54.024
33.427
1.00
31.82
O


HETATM
2847
O
HOH
18
64.790
41.466
7.903
1.00
37.49
O


HETATN
2848
O
HOH
19
73.871
57.655
36.239
1.00
31.87
O


HETATM
2849
O
HOH
20
58.900
51.481
22.980
1.00
34.30
O


HETATM
2850
O
HOH
21
64.317
56.651
20.399
1.00
39.92
O


HETATM
2851
O
HOH
22
65.490
36.877
34.840
1.00
40.17
O


HETATM
2852
O
HOH
23
60.085
50.861
20.174
1.00
43.72
O


HETATM
2853
O
HOH
24
76.358
52.869
36.274
1.00
39.41
O


HETATM
2854
O
HOH
25
64.918
73.696
32.920
1.00
32.12
O


HETATM
2855
O
HOH
26
56.665
77.507
37.267
1.00
37.89
O


HETATM
2856
O
HOH
27
72.867
38.426
33.907
1.00
35.88
O


HETATM
2857
O
HOH
28
72.686
61.731
21.624
1.00
43.41
O


HETATM
2858
O
HOH
29
67.317
67.438
30.698
1.00
36.92
O


HETATM
2859
O
HOH
30
49.555
44.437
21.119
1.00
42.21
O


HETATM
2860
O
HOH
31
70.551
33.609
27.633
1.00
41.14
O


HETATM
2861
O
HOH
32
76.699
41.425
32.331
1.00
34.07
O


HETATM
2862
O
HOH
33
61.925
50.659
17.855
1.00
31.53
O


HETATM
2863
O
HOH
34
62.610
38.767
34.074
1.00
31.70
O


HETATM
2864
O
HOH
35
56.933
57.813
38.879
1.00
41.65
O


HETATM
2865
O
HOH
36
66.624
37.892
16.896
1.00
37.69
O


HETATM
2866
O
HOH
37
69.286
68.051
32.916
1.00
43.83
O


HETATM
2867
O
HOH
38
53.353
51.944
38.099
1.00
36.77
O


HETATM
2868
O
HOH
39
82.373
67.465
31.922
1.00
39.48
O


HETATM
2869
O
HOH
40
62.969
61.940
37.710
1.00
45.75
O


HETATM
2870
O
HOH
41
60.077
59.723
30.997
1.00
46.18
O


HETATM
2871
O
HOH
42
51.139
46.321
36.000
1.00
41.32
O


HETATM
2872
O
HOH
43
59.604
51.735
16.489
1.00
35.27
O


HETATM
2873
O
HOH
44
61.183
37.811
37.337
1.00
47.18
O


HETATM
2874
O
HOH
45
66.082
58.886
21.454
1.00
35.99
O


HETATM
2875
O
HOH
46
66.187
63.971
21.615
1.00
43.24
O


HETATM
2876
O
HOH
47
68.276
38.487
46.493
1.00
41.00
O


HETATM
2877
O
HOH
48
73.810
65.033
30.854
1.00
44.46
O


HETATM
2878
O
HOH
49
59.036
45.342
5.912
1.00
45.26
O


HETATM
2879
O
HOH
50
58.693
35.801
27.026
1.00
42.44
O


HETATM
2880
O
HOH
51
54.551
73.802
39.044
1.00
44.81
O


HETATM
2881
O
HOH
52
59.942
51.276
9.798
1.00
38.47
O


HETATM
2882
O
HOH
53
75.437
38.984
31.295
1.00
41.54
O


HETATM
2883
O
HOH
54
56.511
41.592
37.450
1.00
50.73
O


HETATM
2884
O
HOH
55
55.967
71.689
16.393
1.00
42.82
O


HETATM
2885
O
HOH
56
79.457
38.647
17.552
1.00
40.99
O


HETATM
2886
O
HOH
57
61.441
73.979
39.270
1.00
51.02
O


HETATM
2887
O
HOH
58
74.980
37.209
10.810
1.00
44.24
O


HETATM
2888
O
HOH
59
87.106
70.131
23.910
1.00
48.62
O


HETATM
2889
O
HOH
60
78.921
72.296
28.132
1.00
44.83.
O


HETATM
2890
O
HOH
61
59.217
38.449
34.738
1.00
41.72
O


HETATM
2891
O
HOH
62
62.392
64.439
35.307
1.00
38.87
O


HETATM
2892
O
HOH
63
52.186
54.149
25.895
1.00
39.43
O


HETATM
2893
O
HOH
64
91.884
51.151
35.362
1.00
47.95
O


HETATM
2894
O
HOH
65
74.410
50.817
36.320
1.00
40.80
O


HETATM
2895
O
HOH
66
75.694
70.804
31.847
1.00
45.76
O


HETATM
2896
O
HOH
67
85.562
49.382
39.692
1.00
44.65
O


HETATM
2897
O
HOH
68
50.848
31.856
16.493
1.00
47.42
O


HETATM
2898
O
HOH
69
75.545
38.878
8.328
1.00
39.75
O


HETATM
2899
O
HOH
70
72.184
67.522
32.127
1.00
41.79
O


HETATM
2900
O
HOH
71
81.557
38.617
24.306
1.00
45.21
O


HETATM
2901
O
HOH
72
82.150
63.522
21.264
1.00
45.28
O


HETATM
2902
O
HOH
73
43.465
44.041
23.652
1.00
49.13
O


HETATM
2903
O
NOH
74
65.282
64.106
36.024
1.00
42.80
O


HETATM
2904
O
HOH
75
71.791
56.052
42.026
1.00
43.68
O


HETATM
2905
O
HOH
76
70.611
32.750
38.320
1.00
50.18
O


HETATM
2906
O
HOH
77
65.746
28.372
26.829
1.00
51.32
O


HETATM
2907
O
HOH
78
46.316
49.216
27.478
1.00
49.98
O


HETATM
2908
O
HOH
79
66.218
28.865
15.007
1.00
49.39
O


HETATM
2909
O
HOH
80
45.899
41.751
13.150
1.00
50.35
O


HETATM
2910
O
HOH
81
67.812
59.668
38.963
1.00
53.98
O


HETATM
2911
O
HOH
82
67.783
69.548
38.244
1.00
50.77
O


HETATM
2912
O
HOH
83
90.501
38.801
36.127
1.00
59.97
O


HETATM
2913
O
HOH
84
57.960
65.710
38.116
1.00
51.75
O


HETATM
2914
O
HOH
85
48.770
54.414
37.079
1.00
51.59
O


HETATM
2915
O
HOH
86
54.375
62.285
36.120
1.00
46.20
O


HETATM
2916
O
HOH
87
60.479
39.480
6.892
1.00
48.39
O


HETATM
2917
O
HOH
88
63.400
39.497
6.092
1.00
47.12
O


HETATM
2918
O
HOH
89
49.881
43.115
8.014
1.00
55.16
O


NETATM
2919
O
HOH
90
48.799
31.869
25.511
1.00
54.96
O


HETATM
2920
O
HOH
91
55.226
53.883
40.277
1.00
57.13
O


HETATM
2921
O
HOH
92
84.876
42.783
10.201
1.00
60.19
O


HETATM
2922
O
HOH
93
71.104
57.754
14.563
1.00
50.88
O


HETATM
2923
O
HOH
94
81.517
55.070
13.507
1.00
56.55
O


HETATM
2924
O
HOH
95
69.719
68.895
35.986
1.00
50.06
O


HETATM
2925
O
HOH
96
48.667
81.714
40.322
1.00
56.66
O


HETATM
2926
O
HOH
97
79.523
40.573
32.112
1.00
41.26
O


HETATM
2927
O
HOH
98
50.394
78.735
40.269
1.00
61.03
O


HETATM
2928
O
HOH
99
51.083
76.617
38.073
1.00
50.99
O


HETATM
2929
O
HOH
100
55.631
67.730
37.228
1.00
53.07
O


HETATM
2930
O
HOH
101
63.222
78.551
34.890
1.00
55.30
O


HETATM
2931
O
HOH
102
64.387
81.230
33.819
1.00
60.32
O


HETATM
2932
O
HOH
103
63.693
84.119
34.865
1.00
68.07
O


HETATM
2933
O
HOH
104
75.769
73.295
28.310
1.00
58.02
O


HETATM
2934
O
HOH
105
86.092
39.258
22.649
1.00
56.63
O


HETATM
2935
O
HOH
106
62.744
55.138
1.577
1.00
43.51
O


HETATM
2936
O
HOH
107
74.933
63.024
19.409
1.00
54.22
O


HETATM
2937
O
HOH
108
69.789
45.377
46.398
1.00
46.18
O


HETATM
2938
O
HOH
109
74.595
39.323
37.886
1.00
62.46
O


HETATM
2939
O
HOH
110
73.747
39.642
41.004
1.00
58.85
O


HETATM
2940
O
HOH
111
72.104
32.691
30.025
1.00
49.56
O


HETATM
2941
O
HOH
112
78.793
70.848
25.397
1.00
58.19
O


HETATM
2942
O
HOH
113
73.215
33.284
26.151
1.00
58.62
O


HETATM
2943
O
HOH
114
68.965
43.819
0.725
1.00
52.71
O


HETATM
2944
O
HOH
115
96.151
46.659
27.632
1.00
52.09
O


HETATM
2945
O
HOH
116
97.574
43.766
26.583
1.00
57.72
O


HETATM
2946
O
HOH
117
63.372
31.897
25.790
1.00
49.36
O


HETATM
2947
O
HOH
118
66.211
31.555
26.744
1.00
58.36
O


HETATM
2948
O
HOH
119
63.520
35.235
42.203
1.00
53.59
O


HETATM
2949
O
HOH
120
88.222
37.020
34.672
1.00
51.97
O













CONECT
202
2549






CONECT
2549
202


CONECT
2786
2787
2788
2789
2790


CONECT
2787
2786


CONECT
2788
2786


CONECT
2789
2786


CONECT
2790
2786
2791


CONECT
2791
2790
2792


CONECT
2792
2791
2793
2794


CONECT
2793
2792
2798


CONECT
2794
2792
2795
2796


CONECT
2795
2794


CONECT
2796
2794
2797
2798


CONECT
2797
2796


CONECT
2798
2793
2796
2799


CONECT
2799
2798
2800
2806


CONECT
2800
2799
2801


CONECT
2801
2800
2802


CONECT
2802
2801
2803
2806


CONECT
2803
2802
2804
2805


CONECT
2804
2803


CONECT
2805
2803


CONECT
2806
2799
2802


CONECT
2807
2822
2824
2825


CONECT
2808
2809
2823


CONECT
2809
2808
2810
2815


CONECT
2810
2809
2811


CONECT
2811
2810
2812


CONECT
2812
2811
2828
2829


CONECT
2813
2818


CONECT
2814
2826


CONECT
2815
2809


CONECT
2816
2817
2825


CONECT
2817
2816
2818
2822


CONECT
2818
2813
2817
2819


CONECT
2819
2818
2820
2826


CONECT
2820
2819
2821
2823


CONECT
2821
2820
2822
2827


CONECT
2822
2807
2817
2821


CONECT
2823
2808
2820


CONECT
2824
2807


CONECT
2825
2807
2816


CONECT
2826
2814
2819


CONECT
2827
2821


CONECT
2828
2812


CONECT
2829
2812




















MASTER

509
0
4
13
18
0
0
6
2948
1
46
39


END


FIG. 8


P-UC 5430


Page 1




















TABLE 7







HEADER

OXIDOREDUCTASE
08-AUG-02
1ME8









TITLE

INOSINE MONOPHOSPHATE DEHYDROGENASE (IMPDH) FROM


TITLE
2
TRITRICHOMONAS FOETUS WITH RVP BOUND








COMPND
MOL_ID: 1;









COMPND
2
MOLECULE: INOSINE-5′-MONOPHOSPHATE DEHYDROGENASE;


COMPND
3
CHAIN: A;


COMPND
4
SYNONYM: IMP DEHYDROGENASE, IMPDH;


COMPND
5
EC: 1.1.1.205;


COMPND
6
ENGINEERED: YES








SOURCE
MOL_ID: 1;









SOURCE
2
ORGANISM_SCIENTIFIC: TRITRICHOMONAS FOETUS;


SOURCE
3
GENE: IMPDH;


SOURCE
4
EXPRESSION_SYSTEM: ESCHERICHIA COLI;


SOURCE
5
EXPRESSION_SYSTEM_COMMON: BACTERIA;


SOURCE
6
EXPRESSION_SYSTEM_STRAIN: H712;


SOURCE
7
EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;


SOURCE
8
EXPRESSION_SYSTEM_PLASMID: PBACE








KEYWDS
ALPHA BETA BARREL


EXPDTA
X-RAY DIFFRACTION


AUTHOR
G. L. PROSISE, J. WU, H. LUECKE










JRNL
AUTH

G. L. PROSISE, J. WU, H. LUECKE


JRNL
TITL

CRYSTAL STRUCTURE OF T. FOETUS INOSINE


JRNL
TITL
2
MONOPHOSPHATE DEHYDROGENASE IN COMPLEX WITH THE


JRNL
TITL
3
INHIBITOR RIBAVIRIN REVEALS A CATALYSIS-DEPENDENT


JRNL
TITL
4
ION BINDING SITE


JRNL
REF

TO BE PUBLISHED


JRNL
REFN









REMARK
1



REMARK
2


REMARK
2
RESOLUTION. 1.90 ANGSTROMS.


REMARK
3


REMARK
3
REFINEMENT.












REMARK
3

PROGRAM
:
CNS 1.1


REMARK
3

AUTHORS
:
BRUNGER, ADAMS, CLORE, DELANO, GROS, GROSSE-


REMARK
3


:
KUNSTLEVE, JIANG, KUSZEWSKI, NILGES, PANNU,


REMARK
3


:
READ, RICE, SIMONSON, WARREN


REMARK
3











REMARK
3
REFINEMENT TARGET
:
ENGH & HUBER


REMARK
3









REMARK
3
DATA USED IN REFINEMENT.













REMARK
3

RESOLUTION RANGE HIGH
(ANGSTROMS)
:
1.90


REMARK
3

RESOLUTION RANGE LOW
(ANGSTROMS)
:
48.94


REMARK
3

DATA CUTOFF
(SIGMA(F))
:
0.000


REMARK
3

OUTLIER CUTOFF HIGH
(RMS(ABS(F)))
:
NULL


REMARK
3

COMPLETENESS
(WORKING + TEST) (%)
:
99.4


REMARK
3

NUMBER OF REFLECTIONS

:
50121


REMARK
3









REMARK
3
FIT TO DATA USED IN REFINEMENT.













REMARK
3

CROSS-VALIDATION METHOD

:
THROUGHOUT













REMARK
3

FREE R VALUE TEST SET SELECTION

:
RANDOM













REMARK
3

R VALUE
(WORKING SET)
:
0.243


REMARK
3

FREE R VALUE

:
0.258


REMARK
3

FREE R VALUE TEST SET SIZE
(%)
:
5.000













REMARK
3

FREE R VALUE TEST SET COUNT

:
2523


REMARK
3

ESTIMATED ERROR OF FREE R VALUE

:
0.005


REMARK
3









REMARK
3
FIT IN THE HIGHEST RESOLUTION BIN.













REMARK
3

TOTAL NUMBER OF BINS USED

:
6


REMARK
3

BIN RESOLUTION RANGE HIGH
(A)
:
1.90


REMARK
3

BIN RESOLUTION RANGE LOW
(A)
:
2.02













REMARK
3

BIN COMPLETENESS
(WORKING + TEST) (%)
:
99.90


REMARK
3

REFLECTIONS IN BIN
(WORKING SET)
:
7832


REMARK
3

BIN R VALUE
(WORKING SET)
:
0.2820


REMARK
3

BIN FREE R VALUE

:
0.2950













REMARK
3

BIN FREE R VALUE TEST SET SIZE
(%)
:
4.60


REMARK
3

BIN FREE R VALUE TEST SET COUNT

:
378


REMARK
3

ESTIMATED ERROR OF BIN FREE R VALUE

:
0.015


REMARK
3









REMARK
3
NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.












REMARK
3

PROTEIN ATOMS
:
2727


REMARK
3

NUCLEIC ACID ATOMS
:
0


REMARK
3

HETEROGEN ATOMS
:
23


REMARK
3

SOLVENT ATOMS
:
201


REMARK
3









REMARK
3
B VALUES.













REMARK
3

FROM WILSON PLOT
(A**2)
:
23.40


REMARK
3

MEAN B VALUE
(OVERALL, A**2)
:
36.90










REMARK
3

OVERALL ANISOTROPIC B VALUE.













REMARK
3

B11
(A**2)
:
0.00000


REMARK
3

B22
(A**2)
:
0.00000


REMARK
3

B33
(A**2)
:
0.00000


REMARK
3

B12
(A**2)
:
0.00000


REMARK
3

B13
(A**2)
:
0.00000


REMARK
3

B23
(A**2)
:
0.00000


REMARK
3









REMARK
3
ESTIMATED COORDINATE ERROR.













REMARK
3

ESD FROM LUZZATI PLOT
(A)
:
0.26


REMARK
3

ESD FROM SIGMAA
(A)
:
0.18


REMARK
3

LOW RESOLUTION CUTOFF
(A)
:
5.00


REMARK
3









REMARK
3
CROSS-VALIDATED ESTIMATED COORDINATE ERROR.













REMARK
3

ESD FROM C-V LUZZATI PLOT
(A)
:
0.28


REMARK
3

ESD FROM C-V SIGMAA
(A)
:
0.18


REMARK
3









REMARK
3
RMS DEVIATIONS FROM IDEAL VALUES.













REMARK
3

BOND LENGTHS
(A)
:
0.005


REMARK
3

BOND ANGLES
(DEGREES)
:
1.20


REMARK
3

DIHEDRAL ANGLES
(DEGREES)
:
22.70


REMARK
3

IMPROPER ANGLES
(DEGREES)
:
0.71


REMARK
3











REMARK
3
ISOTROPIC THERMAL MODEL
:
RESTRAINED


REMARK
3













REMARK
3
ISOTROPIC THERMAL FACTOR RESTRAINTS.
RMS

SIGMA

















REMARK
3

MAIN-CHAIN BOND
(A**2)
:
0.990
;
1.500



REMARK
3

MAIN-CHAIN ANGLE
(A**2)
:
1.660
;
2.000


REMARK
3

SIDE-CHAIN BOND
(A**2)
:
1.450
;
2.000


REMARK
3

SIDE-CHAIN ANGLE
(A**2)
:
2.260
;
2.500


REMARK
3









REMARK
3
BULK SOLVENT MODELING.












REMARK
3

METHOD USED
:
FLAT MODEL


REMARK
3

KSOL
:
0.36


REMARK
3

BSOL
:
44.08


REMARK
3











REMARK
3
NCS MODEL
:
NULL


REMARK
3














REMARK
3

NCS RESTRAINTS.
RMS

SIGMA/WEIGHT



















REMARK
3

GROUP
1
POSITIONAL
(A)
:
NULL
;
NULL



REMARK
3

GROUP
1
B-FACTOR
(A**2)
:
NULL
;
NULL


REMARK
3













REMARK
3

PARAMETER FILE
1
:
PROTEIN_REP.PARAM


REMARK
3

PARAMETER FILE
2
:
PARAM.GNSOL


REMARK
3

PARAMETER FILE
3
:
CIS_PEPTIDE.PARAM


REMARK
3

PARAMETER FILE
4
:
RMP_MPA.PAR


REMARK
3

PARAMETER FILE
5
:
ION.PARAM


REMARK
3

PARAMETER FILE
6
:
NULL


REMARK
3

TOPOLOGY FILE
1
:
PROTEIN.TOP


REMARK
3

TOPOLOGY FILE
2
:
RMP.TOP


REMARK
3

TOPOLOGY FILE
3
:
MPA.TOP


REMARK
3

TOPOLOGY FILE
4
:
ION.TOP


REMARK
3

TOPOLOGY FILE
5
:
TOPH.GNSOL


REMARK
3

TOPOLOGY FILE
6
:
NULL


REMARK
3










REMARK
3

OTHER REFINEMENT REMARKS: NULL


REMARK
4









REMARK
4
1ME8 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998


REMARK
100


REMARK
100
THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-AUG-2002.


REMARK
100
THE RCSB ID CODE IS RCSB016850.


REMARK
200


REMARK
200
EXPERIMENTAL DETAILS













REMARK
200

EXPERIMENT TYPE

:
X-RAY DIFFRACTION


REMARK
200

DATE OF DATA COLLECTION

:
12-JUN-2001


REMARK
200

TEMPERATURE
(KELVIN)
:
100.0


REMARK
200

PH

:
7.50


REMARK
200

NUMBER OF CRYSTALS USED

:
1


REMARK
200


REMARK
200

SYNCHROTRON
(Y/N)
:
Y


REMARK
200

RADIATION SOURCE

:
SSRL


REMARK
200

BEAMLINE

:
9-1


REMARK
200

X-RAY GENERATOR MODEL

:
NULL


REMARK
200

MONOCHROMATIC OR LAUE
(M/L)
:
M


REMARK
200

WAVELENGTH OR RANGE
(A)
:
0.07


REMARK
200

MONOCHROMATOR

:
NULL


REMARK
200

OPTICS

:
NULL


REMARK
200












REMARK
200

DETECTOR TYPE
:
IMAGE PLATE


REMARK
200

DETECTOR MANUFACTURER
:
MARRESEARCH


REMARK
200

INTENSITY-INTEGRATION SOFTWARE
:
DENZO


REMARK
200

DATA SCALING SOFTWARE
:
SCALEPACK


REMARK
200


REMARK
200

NUMBER OF UNIQUE REFLECTIONS
:
50290













REMARK
200

RESOLUTION RANGE HIGH
(A)
:
1.900


REMARK
200

RESOLUTION RANGE LOW
(A)
:
50.000


REMARK
200

REJECTION CRITERIA
(SIGMA(I))
:
0.000


REMARK
200









REMARK
200
OVERALL.













REMARK
200

COMPLETENESS FOR RANGE
(%)
:
99.9


REMARK
200

DATA REDUNDANCY

:
10.000


REMARK
200

R MERGE
(I)
:
0.08000


REMARK
200

R SYM
(I)
:
NULL












REMARK
200

<I/SIGMA(I)> FOR THE DATA SET
:
33.8000


REMARK
200









REMARK
200
IN THE HIGHEST RESOLUTION SHELL.













REMARK
200

HIGHEST RESOLUTION SHELL, RANGE HIGH
(A)
:
1.90


REMARK
200

HIGHEST RESOLUTION SHELL, RANGE LOW
(A)
:
1.93













REMARK
200

COMPLETENESS FOR SHELL
(%)
:
100.0


REMARK
200

DATA REDUNDANCY IN SHELL

:
NULL


REMARK
200

R MERGE FOR SHELL
(I)
:
0.60000


REMARK
200

R SYM FOR SHELL
(I)
:
NULL


REMARK
200

<I/SIGMA(I)> FOR SHELL

:
2.400


REMARK
200









REMARK
200
DIFFRACTION PROTOCOL: SINGLE WAVELENGTH


REMARK
200
METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS


REMARK
200
SOFTWARE USED: CNS


REMARK
200
STARTING MODEL: NULL


REMARK
200


REMARK
200
REMARK: NULL


REMARK
280


REMARK
280
CRYSTAL


REMARK
280
SOLVENT CONTENT, VS (%): NULL


REMARK
280
MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL


REMARK
280


REMARK
280
CRYSTALLIZATION CONDITIONS: SODIUM MALONATE, TRIS, 2-










REMARK
280

MERCAPTOETHANOL, EDTA, GLYCEROL









REMARK
290



REMARK
290
CRYSTALLOGRAPHIC SYMMETRY


REMARK
290
SYMMETRY OPERATORS FOR SPACE GROUP: P 4 3 2


REMARK
290











REMARK
290

SYMOP
SYMMETRY


REMARK
290

NNNMMM
OPERATOR


REMARK
290

1555
X, Y, Z


REMARK
290

2555
—X, —Y, Z


REMARK
290

3555
—X, Y, —Z


REMARK
290

4555
X, —Y, —Z


REMARK
290

5555
Z, X, Y


REMARK
290

6555
Z, —X, —Y


REMARK
290

7555
—Z, —X, Y


REMARK
290

8555
—Z, X, —Y


REMARK
290

9555
Y, Z, X


REMARK
290

10555
—Y, Z, —X


REMARK
290

11555
Y, —Z, —X


REMARK
290

12555
—Y, —Z, X


REMARK
290

13555
Y, X, —Z


REMARK
290

14555
—Y, —X, —Z


REMARK
290

15555
Y, —X, Z


REMARK
290

16555
—Y, X, Z


REMARK
290

17555
X, Z, —Y


REMARK
290

18555
—X, Z, Y


REMARK
290

19555
—X, —Z, —Y


REMARK
290

20555
X, —Z, Y


REMARK
290

21555
Z, Y, —X


REMARK
290

22555
Z, —Y, X


REMARK
290

23555
—Z, Y, X


REMARK
290

24555
—Z, —Y, —X


REMARK
290












REMARK
290

WHERE
NNN −>
OPERATOR NUMBER


REMARK
290


MMM −>
TRANSLATION VECTOR


REMARK
290









REMARK
290
CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS


REMARK
290
THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM


REMARK
290
RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY


REMARK
290
RELATED MOLECULES.
















REMARK
290

SMTRY1
1
1.000000
0.000000
0.000000
0.00000



REMARK
290

SMTRY2
1
0.000000
1.000000
0.000000
0.00000


REMARK
290

SMTRY3
1
0.000000
0.000000
1.000000
0.00000


REMARK
290

SMTRY1
2
−1.000000
0.000000
0.000000
0.00000


REMARK
290

SMTRY2
2
0.000000
−1.000000
0.000000
0.00000


REMARK
290

SMTRY3
2
0.000000
0.000000
1.000000
0.00000


REMARK
290

SMTRY1
3
−1.000000
0.000000
0.000000
0.00000


REMARK
290

SMTRY2
3
0.000000
1.000000
0.000000
0.00000


REMARK
290

SMTRY3
3
0.000000
0.000000
−1.000000
0.00000


REMARK
290

SMTRY1
4
1.000000
0.000000
0.000000
0.00000


REMARK
290

SMTRY2
4
0.000000
−1.000000
0.000000
0.00000


REMARK
290

SMTRY3
4
0.000000
0.000000
−1.000000
0.00000


REMARK
290

SMTRY1
5
0.000000
0.000000
1.000000
0.00000


REMARK
290

SMTRY2
5
1.000000
0.000000
0.000000
0.00000


REMARK
290

SMTRY3
5
0.000000
1.000000
0.000000
0.00000


REMARK
290

SMTRY1
6
0.000000
0.000000
1.000000
0.00000


REMARK
290

SMTRY2
6
−1.000000
0.000000
0.000000
0.00000


REMARK
290

SMTRY3
6
0.000000
−1.000000
0.000000
0.00000


REMARK
290

SMTRY1
7
0.000000
0.000000
−1.000000
0.00000


REMARK
290

SMTRY2
7
−1.000000
0.000000
0.000000
0.00000


REMARK
290

SMTRY3
7
0.000000
1.000000
0.000000
0.00000


REMARK
290

SMTRY1
8
0.000000
0.000000
−1.000000
0.00000


REMARK
290

SMTRY2
8
1.000000
0.000000
0.000000
0.00000


REMARK
290

SMTRY3
8
0.000000
−1.000000
0.000000
0.00000


REMARK
290

SMTRY1
9
0.000000
1.000000
0.000000
0.00000


REMARK
290

SMTRY2
9
0.000000
0.000000
1.000000
0.00000


REMARK
290

SMTRY3
9
1.000000
0.000000
0.000000
0.00000


REMARK
290

SMTRY1
10
0.000000
−1.000000
0.000000
0.00000


REMARK
290

SMTRY2
10
0.000000
0.000000
1.000000
0.00000


REMARK
290

SMTRY3
10
−1.000000
0.000000
0.000000
0.00000


REMARK
290

SMTRY1
11
0.000000
1.000000
0.000000
0.00000


REMARK
290

SMTRY2
11
0.000000
0.000000
−1.000000
0.00000


REMARK
290

SMTRY3
11
−1.000000
0.000000
0.000000
0.00000


REMARK
290

SMTRY1
12
0.000000
−1.000000
0.000000
0.00000


REMARK
290

SMTRY2
12
0.000000
0.000000
−1.000000
0.00000


REMARK
290

SMTRY3
12
1.000000
0.000000
0.000000
0.00000


REMARK
290

SMTRY1
13
0.000000
1.000000
0.000000
0.00000


REMARK
290

SMTRY2
13
1.000000
0.000000
0.000000
0.00000


REMARK
290

SMTRY3
13
0.000000
0.000000
−1.000000
0.00000


REMARK
290

SMTRY1
14
0.000000
−1.000000
0.000000
0.00000


REMARK
290

SMTRY2
14
−1.000000
0.000000
0.000000
0.00000


REMARK
290

SMTRY3
14
0.000000
0.000000
−1.000000
0.00000


REMARK
290

SMTRY1
15
0.000000
1.000000
0.000000
0.00000


REMARK
290

SMTRY2
15
−1.000000
0.000000
0.000000
0.00000


REMARK
290

SMTRY3
15
0.000000
0.000000
1.000000
0.00000


REMARK
290

SMTRY1
16
0.000000
−1.000000
0.000000
0.00000


REMARK
290

SMTRY2
16
1.000000
0.000000
0.000000
0.00000


REMARK
290

SMTRY3
16
0.000000
0.000000
1.000000
0.00000


REMARK
290

SMTRY1
17
1.000000
0.000000
0.000000
0.00000


REMARK
290

SMTRY2
17
0.000000
0.000000
1.000000
0.00000


REMARK
290

SMTRY3
17
0.000000
−1.000000
0.000000
0.00000


REMARK
290

SMTRY1
18
−1.000000
0.000000
0.000000
0.00000


REMARK
290

SMTRY2
18
0.000000
0.000000
1.000000
0.00000


REMARK
290

SMTRY3
18
0.000000
1.000000
0.000000
0.00000


REMARK
290

SMTRY1
19
−1.000000
0.000000
0.000000
0.00000


REMARK
290

SMTRY2
19
0.000000
0.000000
−1.000000
0.00000


REMARK
290

SMTRY3
19
0.000000
−1.000000
0.000000
0.00000


REMARK
290

SMTRY1
20
1.000000
0.000000
0.000000
0.00000


REMARK
290

SMTRY2
20
0.000000
0.000000
−1.000000
0.00000


REMARK
290

SMTRY3
20
0.000000
1.000000
0.000000
0.00000


REMARK
290

SMTRY1
21
0.000000
0.000000
1.000000
0.00000


REMARK
290

SMTRY2
21
0.000000
1.000000
0.000000
0.00000


REMARK
290

SMTRY3
21
−1.000000
0.000000
0.000000
0.00000


REMARK
290

SMTRY1
22
0.000000
0.000000
1.000000
0.00000


REMARK
290

SMTRY2
22
0.000000
−1.000000
0.000000
0.00000


REMARK
290

SMTRY3
22
1.000000
0.000000
0.000000
0.00000


REMARK
290

SMTRY1
23
0.000000
0.000000
−1.000000
0.00000


REMARK
290

SMTRY2
23
0.000000
1.000000
0.000000
0.00000


REMARK
290

SMTRY3
23
1.000000
0.000000
0.000000
0.00000


REMARK
290

SMTRY1
24
0.000000
0.000000
−1.000000
0.00000


REMARK
290

SMTRY2
24
0.000000
−1.000000
0.000000
0.00000


REMARK
290

SMTRY3
24
−1.000000
0.000000
0.000000
0.00000


REMARK
290









REMARK
290
REMARK: NULL


REMARK
300


REMARK
300
BIOMOLECULE: 1


REMARK
300
THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT


REMARK
300
WHICH CONSISTS OF 1 CHAIN(S). SEE REMARK 350 FOR


REMARK
300
INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).


REMARK
350


REMARK
350
GENERATING THE BIOMOLECULE


REMARK
350
COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN


REMARK
350
BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE


REMARK
350
MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS


REMARK
350
GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND


REMARK
350
CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.


REMARK
350


REMARK
350
BIOMOLECULE: 1


REMARK
350
APPLY THE FOLLOWING TO CHAINS: A
















REMARK
350

BIOMT1
1
1.000000
0.000000
0.000000
0.00000



REMARK
350

BIOMT2
1
0.000000
1.000000
0.000000
0.00000


REMARK
350

BIOMT3
1
0.000000
0.000000
1.000000
0.00000


REMARK
350

BIOMT1
2
−1.000000
0.000000
0.000000
154.74500


REMARK
350

BIOMT2
2
0.000000
−1.000000
0.000000
154.74500


REMARK
350

BIOMT3
2
0.000000
0.000000
1.000000
0.00000


REMARK
350

BIOMT1
3
0.000000
1.000000
0.000000
0.00000


REMARK
350

BIOMT2
3
−1.000000
0.000000
0.000000
154.74500


REMARK
350

BIOMT3
3
0.000000
0.000000
1.000000
0.00000


REMARK
350

BIOMT1
4
0.000000
−1.000000
0.000000
154.74500


REMARK
350

BIOMT2
4
1.000000
0.000000
0.000000
0.00000


REMARK
350

BIOMT3
4
0.000000
0.000000
1.000000
0.00000


REMARK
465









REMARK
465
MISSING RESIDUES


REMARK
465
THE FOLLOWING, RESIDUES WERE NOT LOCATED IN THE


REMARK
465
EXPERIMENT. (M = MODEL NUMBER; RES = RESIDUE NAME; C = CHAIN


REMARK
465
IDENTIFIER; SSSEQ = SEQUENCE NUMBER; I = INSERTION CODE.)


REMARK
465














REMARK
465

M
RES
C
SSSEQI



REMARK
465


MET
A
1


REMARK
465


GLY
A
102


REMARK
465


PHE
A
103


REMARK
465


VAL
A
104


REMARK
465


VAL
A
105


REMARK
465


SER
A
106


REMARK
465


ASP
A
107


REMARK
465


SER
A
108


REMARK
465


ASN
A
109


REMARK
465


VAL
A
110


REMARK
465


LYS
A
111


REMARK
465


PRO
A
112


REMARK
465


ASP
A
113


REMARK
465


GLN
A
114


REMARK
465


THR
A
115


REMARK
465


PHE
A
116


REMARK
465


ALA
A
117


REMARK
465


ASP
A
118


REMARK
465


VAL
A
119


REMARK
465


LEU
A
120


REMARK
465


ALA
A
121


REMARK
465


ILE
A
122


REMARK
465


SER
A
123


REMARK
465


GLN
A
124


REMARK
465


ARG
A
125


REMARK
465


THR
A
126


REMARK
465


THR
A
127


REMARK
465


HIS
A
128


REMARK
465


ASN
A
129


REMARK
465


THR
A
130


REMARK
465


VAL
A
131


REMARK
465


ALA
A
132


REMARK
465


VAL
A
133


REMARK
465


THR
A
134


REMARK
465


ASP
A
135


REMARK
465


ASP
A
136


REMARK
465


GLY
A
137


REMARK
465


THR
A
138


REMARK
465


PRO
A
139


REMARK
465


HIS
A
140


REMARK
465


GLY
A
141


REMARK
465


VAL
A
142


REMARK
465


LEU
A
143


REMARK
465


LEU
A
144


REMARK
465


GLY
A
145


REMARK
465


LEU
A
146


REMARK
465


VAL
A
147


REMARK
465


THR
A
148


REMARK
465


GLN
A
149


REMARK
465


ARG
A
150


REMARK
465


ASP
A
151


REMARK
465


TYR
A
152


REMARK
465


PRO
A
153


REMARK
465


ILE
A
154


REMARK
465


ASP
A
155


REMARK
465


LEU
A
156


REMARK
465


THR
A
157


REMARK
465


GLN
A
158


REMARK
465


THR
A
159


REMARK
465


GLU
A
160


REMARK
465


THR
A
161


REMARK
465


LYS
A
162


REMARK
465


VAL
A
163


REMARK
465


SER
A
164


REMARK
465


ASP
A
165


REMARK
465


MET
A
166


REMARK
465


MET
A
167


REMARK
465


THR
A
168


REMARK
465


PRO
A
169


REMARK
465


PHE
A
170


REMARK
465


SER
A
171


REMARK
465


LYS
A
172


REMARK
465


LEU
A
173


REMARK
465


VAL
A
174


REMARK
465


THR
A
175


REMARK
465


ALA
A
176


REMARK
465


HIS
A
177


REMARK
465


GLN
A
178


REMARK
465


ASP
A
179


REMARK
465


THR
A
180


REMARK
465


LYS
A
181


REMARK
465


LEU
A
182


REMARK
465


SER
A
183


REMARK
465


GLU
A
184


REMARK
465


ALA
A
185


REMARK
465


ASN
A
186


REMARK
465


LYS
A
187


REMARK
465


ILE
A
188


REMARK
465


ILE
A
189


REMARK
465


TRP
A
190


REMARK
465


GLU
A
191


REMARK
465


LYS
A
192


REMARK
465


LYS
A
193


REMARK
465


LEU
A
194


REMARK
465


ASN
A
195


REMARK
465


ALA
A
196


REMARK
465


LEU
A
197


REMARK
465


PRO
A
198


REMARK
465


ILE
A
199


REMARK
465


ILE
A
200


REMARK
465


ASP
A
201


REMARK
465


ASP
A
202


REMARK
465


ASP
A
203


REMARK
465


GLN
A
204


REMARK
465


HIS
A
205


REMARK
465


LEU
A
206


REMARK
465


ARG
A
207


REMARK
465


TYR
A
208


REMARK
465


ILE
A
209


REMARK
465


VAL
A
210


REMARK
465


PHE
A
211


REMARK
465


ARG
A
212


REMARK
465


LYS
A
213


REMARK
465


ASP
A
214


REMARK
465


TYR
A
215


REMARK
465


ASP
A
216


REMARK
465


ARG
A
217


REMARK
465


SER
A
218


REMARK
465


GLN
A
219


REMARK
465


VAL
A
220


REMARK
465


CYS
A
221


REMARK
465


GLN
A
417


REMARK
465


ARG
A
418


REMARK
465


TYR
A
419


REMARK
465


ASP
A
420


REMARK
465


LEU
A
421


REMARK
465


GLY
A
422


REMARK
465


GLY
A
423


REMARK
465


LYS
A
424


REMARK
465


GLN
A
425


REMARK
465


LYS
A
426


REMARK
465


LEU
A
427


REMARK
465


SER
A
428


REMARK
465


PHE
A
429


REMARK
465


GLU
A
430


REMARK
465


VAL
A
493


REMARK
465


LYS
A
494


REMARK
465


ASP
A
495


REMARK
465


ARG
A
496


REMARK
465


ILE
A
497


REMARK
465


ASN
A
498


REMARK
465


ASP
A
499


REMARK
465


TYR
A
500


REMARK
465


HIS
A
501


REMARK
465


PRO
A
502


REMARK
465


LYS
A
503


REMARK
500









REMARK
500
GEOMETRY AND STHREOCHEMISTRY


REMARK
500
SUBTOPIC: COVALENT BOND ANGLES


REMARK
500


REMARK
500
THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES


REMARK
500
HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE


REMARK
500
THAN 6*RMSD (M = MODEL NUMBER; RES = RESIDUE NAME; C = CHAIN


REMARK
500
IDENTIFIER; SSEQ = SEQUENCE NUMBER; I = INSERTION CODE).


REMARK
500


REMARK
500
STANDARD TABLE:


REMARK
500
FORMAT: (10X, I3, 1X, A3, 1X, A1, I4, A1, 3 (1X, A4, 2X), 12X, F5.1)


REMARK
500


REMARK
500
EXPECTED VALUES: ENGH AND HUBER, 1991


REMARK
500


















REMARK
500

M
RES
CSSEQI
ATM1

ATM2

ATM3





















REMARK
500


GLY
A
20
N
-
CA
-
C
ANGL. DEV. =
−7.5 DEGREES


REMARK
500


ILE
A
27
N
-
CA
-
C
ANGL. DEV. =
−9.2 DEGREES


REMARK
500


PRO
A
53
N
-
CA
-
C
ANGL. DEV. =
  7.4 DEGREES


REMARK
500


SER
A
63
N
-
CA
-
C
ANGL. DEV. =
  8.5 DEGREES


REMARK
500


SER
A
357
N
-
CA
-
C
ANGL. DEV. =
−7.3 DEGREES


REMARK
500


LYS
A
472
N
-
CA
-
C
ANGL. DEV. =
  8.2 DEGREES


REMARK
500


LYS
A
474
N
-
CA
-
C
ANGL. DEV. =
−8.8 DEGREES


REMARK
500


LEU
A
477
N
-
CA
-
C
ANGL. DEV. =
−8.6 DEGREES


REMARK
900









REMARK
900
RELATED ENTRIES










REMARK
900
RELATED ID: 1AK5
RELATED DB: PDB









REMARK
900
INOSINE MONOPHOSPHATE DEHYDROGENASE (IMPDH) FROM


REMARK
900
TRITRICHOMONAS FOETUS










REMARK
900
RELATED ID: 1ME7
RELATED DB: PDB









REMARK
900
1ME7 CONTAINS THE SAME PROTEIN WITH RRP AND MOA BOUND










REMARK
900
RELATED ID: 1ME9
RELATED DB: PDB









REMARK
900
1ME9 CONTAINS THE SAME PROTEIN WITH IMP BOUND










REMARK
900
RELATED ID: 1MEH
RELATED DB: PDB









REMARK
900
1MEH CONTAINS THE SAME PROTEIN WITH IMP AND MOA BOUND










REMARK
900
RELATED ID: 1MEI
RELATED DB: PDB









REMARK
900
1MEI CONTAINS THE SAME PROTEIN WITH XMP AND MYCOPHENOLIC


REMARK
900
ACID BOUND










REMARK
900
RELATED ID: 1MEW
RELATED DB: PDB









REMARK
900
1MEW CONTAINS THE SAME PROTEIN WITH XMP AND NAD BOUND
















DBREF
1ME8
A
1
503
SWS
P50097
IMDH_TRIFO
1
503
















SEQADV
1ME8
CSO
A
319
SWS
P50097
CYS
319
MODIFIED RESIDUE























SEQRES
1
A
503
MET
ALA
LYS
TYR
TYR
ASN
GLU
PRO
CYS
HIS
THR
PHE
ASN


SEQRES
2
A
503
GLU
TYR
LEU
LEU
ILE
PRO
GLY
LEU
SER
THR
VAL
ASP
CYS


SEQRES
3
A
503
ILE
PRO
SER
ASN
VAL
ASN
LEU
SER
THR
PRO
LEU
VAL
LYS


SEQRES
4
A
503
PHE
GLN
LYS
GLY
GLN
GLN
SER
GLU
ILE
ASN
LEU
LYS
ILE


SEQRES
5
A
503
PRO
LEU
VAL
SER
ALA
ILE
MET
GLN
SER
VAL
SER
GLY
GLU


SEQRES
6
A
503
LYS
MET
ALA
ILE
ALA
LEU
ALA
ARG
GLU
GLY
GLY
ILE
SER


SEQRES
7
A
503
PHE
ILE
PHE
GLY
SER
GLN
SER
ILE
GLU
SER
GLN
ALA
ALA


SEQRES
8
A
503
MET
VAL
HIS
ALA
VAL
LYS
ASN
PHE
LYS
ALA
GLY
PHE
VAL


SEQRES
9
A
503
VAL
SER
ASP
SER
ASN
VAL
LYS
PRO
ASP
GLN
THR
PHE
ALA


SEQRES
10
A
503
ASP
VAL
LEU
ALA
ILE
SER
GLN
ARG
THR
THR
HIS
ASN
THR


SEQRES
11
A
503
VAL
ALA
VAL
THR
ASP
ASP
GLY
THR
PRO
HIS
GLY
VAL
LEU


SEQRES
12
A
503
LEU
GLY
LEU
VAL
THR
GLN
ARG
ASP
TYR
PRO
ILE
ASP
LEU


SEQRES
13
A
503
THR
GLN
THR
GLU
THR
LYS
VAL
SER
ASP
MET
MET
THR
PRO


SEQRES
14
A
503
PHE
SER
LYS
LEU
VAL
THR
ALA
HIS
GLN
ASP
THR
LYS
LEU


SEQRES
15
A
503
SER
GLU
ALA
ASN
LYS
ILE
ILE
TRP
GLU
LYS
LYS
LEU
ASN


SEQRES
16
A
503
ALA
LEU
PRO
ILE
ILE
ASP
ASP
ASP
GLN
HIS
LEU
ARG
TYR


SEQRES
17
A
503
ILE
VAL
PHE
ARG
LYS
ASP
TYR
ASP
ARG
SER
GLN
VAL
CYS


SEQRES
18
A
503
HIS
ASN
GLU
LEU
VAL
ASP
SER
GLN
LYS
ARG
TYR
LEU
VAL


SEQRES
19
A
503
GLY
ALA
GLY
ILE
ASN
THR
ARG
ASP
PHE
ARG
GLU
ARG
VAL


SEQRES
20
A
503
PRO
ALA
LEU
VAL
GLU
ALA
GLY
ALA
ASP
VAL
LEU
CYS
ILE


SEQRES
21
A
503
ASP
SER
SER
ASP
GLY
PHE
SER
GLU
TRP
GLN
LYS
ILE
THR


SEQRES
22
A
503
ILE
GLY
TRP
ILE
ARG
GLU
LYS
TYR
GLY
ASP
LYS
VAL
LYS


SEQRES
23
A
503
VAL
GLY
ALA
GLY
ASN
ILE
VAL
ASP
GLY
GLU
GLY
PHE
ARG


SEQRES
24
A
503
TYR
LEU
ALA
ASP
ALA
GLY
ALA
ASP
PHE
ILE
LYS
ILE
GLY


SEQRES
25
A
503
ILE
GLY
GLY
GLY
SER
ILE
CSO
ILE
THR
ARG
GLU
GLN
LYS


SEQRES
26
A
503
GLY
ILE
GLY
ARG
GLY
GLN
ALA
THR
ALA
VAL
ILE
ASP
VAL


SEQRES
27
A
503
VAL
ALA
GLU
ARG
ASN
LYS
TYR
PHE
GLU
GLU
THR
GLY
ILE


SEQRES
28
A
503
TYR
ILE
PRO
VAL
CYS
SER
ASP
GLY
GLY
ILE
VAL
TYR
ASP


SEQRES
29
A
503
TYR
HIS
MET
THR
LEU
ALA
LEU
ALA
MET
GLY
ALA
ASP
PHE


SEQRES
30
A
503
ILE
MET
LEU
GLY
ARG
TYR
PHE
ALA
ARG
PHE
GLU
GLU
SER


SEQRES
31
A
503
PRO
THR
ARG
LYS
VAL
THR
ILE
ASN
GLY
SER
VAL
MET
LYS


SEQRES
32
A
503
GLU
TYR
TRP
GLY
GLU
GLY
SER
SER
ARG
ALA
ARG
ASN
TRP


SEQRES
33
A
503
GLN
ARG
TYR
ASP
LEU
GLY
GLY
LYS
GLN
LYS
LEU
SER
PHE


SEQRES
34
A
503
GLU
GLU
GLY
VAL
ASP
SER
TYR
VAL
PRO
TYR
ALA
GLY
LYS


SEQRES
35
A
503
LEU
LYS
ASP
ASN
VAL
GLU
ALA
SER
LEU
ASN
LYS
VAL
LYS


SEQRES
36
A
503
SER
THR
MET
CYS
ASN
CYS
GLY
ALA
LEU
THR
ILE
PRO
GLN


SEQRES
37
A
503
LEU
GLN
SER
LYS
ALA
LYS
ILE
THR
LEU
VAL
SER
SER
VAL


SEQRES
38
A
503
SER
ILE
VAL
GLU
GLY
GLY
ALA
HIS
ASP
VAL
ILE
VAL
LYS


SEQRES
39
A
503
ASP
ARG
ILE
ASN
ASP
TYR
HIS
PRO
LYS














MODRES
1ME8
CSO
A
319
CYS
5-HYDROXYCYSTEINE



HET
CSO
A
319

7


HET
K

900

1


HET
NA

901

1


HET
RVP

602

21









HETNAM
CSO
S-HYDROXYCYSTEINE


HETNAM
K
POTASSIUM ION


HETNAN
NA
SODIUM ION


HETNAM
RVP
RIBAVIRIN MONOPHOSPHATE














FORMUL
1
CSO
C3
H7
N1
O3
S1


FORMUL
2
K
K1
1+











FORMUL
3
NA
NA1
1+














FORMUL
4
RVP
C8
H13
N4
O8
P1










FORMUL
5
HOH
*201 (H2 O1)

















HELIX
1
1
THR
A
11
ASN
A
13
5



3


HELIX
2
2
ILE
A
27
VAL
A
31
5


5


HELIX
3
3
GLY
A
64
GLU
A
74
1


11


HELIX
4
4
SER
A
85
ASN
A
98
1


14


HELIX
5
5
ASP
A
242
GLY
A
254
1


13


HELIX
6
6
SER
A
267
GLY
A
282
1


16


HELIX
7
7
ASP
A
283
VAL
A
285
5


3


HELIX
8
8
ASP
A
294
GLY
A
305
1


12


HELIX
9
9
GLY
A
330
GLY
A
350
1


21


HELIX
10
10
TYR
A
363
MET
A
373
1


11


HELIX
11
11
GLY
A
381
ARG
A
386
1


6


HELIX
12
12
SER
A
410
ASN
A
415
1


6


HELIX
13
13
LYS
A
442
CYS
A
461
1


20


HELIX
14
14
THR
A
465
ALA
A
473
1


9


























SHEET
1
A
2
TYR
A
 15
LEU
A
 17
0











SHEET
2
A
2
ILE
A
475
LEU
A
477
−1 
O
THR
A
476
N
LEU
A
 16


SHEET
1
B
2
THR
A
 35
PRO
A
 36
0


SHEET
2
B
2
ASN
A
 49
LEU
A
 50
−1 
O
LEU
A
 50
N
THR
A
 35


SHEET
1
C
2
PHE
A
 40
GLN
A
 41
0


SHEET
2
C
2
ILE
A
351
TYR
A
352
−1 
O
TYR
A
352
N
PHE
A
 40


SHEET
1
D
9
LEU
A
 54
SER
A
 56
0


SHEET
2
D
9
ILE
A
 77
ILE
A
 80
1
O
ILE
A
 77
N
SER
A
 56


SHEET
3
D
9
GLY
A
235
ILE
A
238
1
O
GLY
A
237
N
ILE
A
 80


SHEET
4
D
9
VAL
A
257
ILE
A
260
1
O
CYS
A
259
N
ILE
A
238


SHEET
5
D
9
VAL
A
287
ILE
A
292
1
O
GLY
A
288
N
LEU
A
258


SHEET
6
D
9
PHE
A
308
ILE
A
311
1
O
LYS
A
310
N
ALA
A
289


SHEET
7
D
9
VAL
A
355
ASP
A
358
1
O
CYS
A
356
N
ILE
A
311


SHEET
8
D
9
PHE
A
377
LEU
A
380
1
O
MET
A
379
N
SER
A
357


SHEET
9
D
9
LEU
A
 54
SER
A
 56
1
N
VAL
A
 55
O
ILE
A
378


SHEET
1
E
3
LYS
A
394
ILE
A
397
0


SHEET
2
E
3
SER
A
400
TRP
A
406
−1 
O
MET
A
402
N
VAL
A
395


SHEET
3
E
3
ASP
A
434
PRO
A
438
−1 
O
SER
A
435
N
TYR
A
405
















SSBOND
1
CYS
A
26

CYS
A
459




















CISPEP
1
GLY
A
290

ASN
A
291

0
0.82

















CRYST1
154.745
154.745
154.745
90.00
90.00
90.00
P 4 3 2
24













ORIGX1
1.000000
0.000000
0.000000
0.00000



ORIGX2
0.000000
1.000000
0.000000
0.00000


ORIGX3
0.000000
0.000000
1.000000
0.00000


SCALE1
0.006462
0.000000
0.000000
0.00000


SCALE2
0.000000
0.006462
0.000000
0.00000


SCALE3
0.000000
0.000000
0.006462
0.00000


















ATOM
1
N
ALA
A
2
55.144
74.892
36.640
1.00
29.93



N


ATOM
2
CA
ALA
A
2
55.885
73.830
35.910
1.00
29.54


C


ATOM
3
C
ALA
A
2
57.177
73.489
36.647
1.00
30.30


C


ATOM
4
O
ALA
A
2
57.618
74.234
37.525
1.00
29.88


O


ATOM
5
CB
ALA
A
2
56.201
74.301
34.491
1.00
29.72


C


ATOM
6
N
LYS
A
3
57.771
72.357
36.289
1.00
29.86


N


ATOM
7
CA
LYS
A
3
59.015
71.919
36.904
1.00
30.69


C


ATOM
8
C
LYS
A
3
60.155
72.132
35.922
1.00
29.48


C


ATOM
9
O
LYS
A
3
60.040
71.777
34.753
1.00
28.89


O


ATOM
10
CB
LYS
A
3
58.943
70.434
37.275
1.00
33.07


C


ATOM
11
CG
LYS
A
3
60.304
69.840
37.628
1.00
37.75


C


ATOM
12
CD
LYS
A
3
60.240
68.344
37.872
1.00
41.04


C


ATOM
13
CE
LYS
A
3
61.628
67.728
37.773
1.00
42.33


C


ATOM
14
NZ
LYS
A
3
62.601
68.424
38.656
1.00
43.20


N


ATOM
15
N
TYR
A
4
61.252
72.704
36.407
1.00
28.93


N


ATOM
16
CA
TYR
A
4
62.425
72.961
35.581
1.00
28.85


C


ATOM
17
C
TYR
A
4
63.620
72.167
36.109
1.00
29.60


C


ATOM
18
O
TYR
A
4
63.545
71.551
37.172
1.00
28.77


O


ATOM
19
CB
TYR
A
4
62.732
74.463
35.571
1.00
28.38


C


ATOM
20
CG
TYR
A
4
61.634
75.274
34.917
1.00
27.99


C


ATOM
21
CD1
TYR
A
4
61.519
75.336
33.527
1.00
27.06


C


ATOM
22
CD2
TYR
A
4
60.684
75.946
35.686
1.00
28.17


C


ATOM
23
CE1
TYR
A
4
60.479
76.050
32.919
1.00
27.85


C


ATOM
24
CE2
TYR
A
4
59.643
76.662
35.087
1.00
27.52


C


ATOM
25
CZ
TYR
A
4
59.547
76.708
33.707
1.00
27.20


C


ATOM
26
OH
TYR
A
4
58.512
77.400
33.115
1.00
27.38


O


ATOM
27
N
TYR
A
5
64.714
72.173
35.359
1.00
30.38


N


ATOM
28
CA
TYR
A
5
65.909
71.436
35.756
1.00
31.23


C


ATOM
29
C
TYR
A
5
67.109
72.364
35.895
1.00
32.36


C


ATOM
30
O
TYR
A
5
67.143
73.440
35.300
1.00
31.65


O


ATOM
31
CB
TYR
A
5
66.204
70.330
34.739
1.00
31.26


C


ATOM
32
CG
TYR
A
5
65.063
69.349
34.584
1.00
31.28


C


ATOM
33
CD1
TYR
A
5
63.906
69.702
33.891
1.00
30.79


C


ATOM
34
CD2
TYR
A
5
65.116
68.085
35.179
1.00
31.65


C


ATOM
35
CE1
TYR
A
5
62.824
68.826
33.794
1.00
30.64


C


ATOM
36
CE2
TYR
A
5
64.039
67.199
35.088
1.00
30.49


C


ATOM
37
CZ
TYR
A
5
62.897
67.579
34.395
1.00
31.03


C


ATOM
38
OH
TYR
A
5
61.817
66.725
34.313
1.00
29.28


O


ATOM
39
N
ASN
A
6
68.090
71.942
36.687
1.00
33.08


N


ATOM
40
CA
ASN
A
6
69.285
72.744
36.925
1.00
34.41


C


ATOM
41
C
ASN
A
6
70.250
72.779
35.744
1.00
34.13


C


ATOM
42
O
ASN
A
6
70.971
73.758
35.556
1.00
34.71


O


ATOM
43
CB
ASN
A
6
70.009
72.226
38.171
1.00
37.70


C


ATOM
44
CG
ASN
A
6
69.207
72.440
39.444
1.00
39.54


C


ATOM
45
OD1
ASN
A
6
69.407
71.747
40.441
1.00
42.37


O


ATOM
46
ND2
ASN
A
6
68.303
73.414
39.420
1.00
42.40


N


ATOM
47
N
GLU
A
7
70.263
71.716
34.946
1.00
32.89


N


ATOM
48
CA
GLU
A
7
71.158
71.648
33.795
1.00
32.05


C


ATOM
49
C
GLU
A
7
70.419
71.313
32.505
1.00
30.13


C


ATOM
50
O
GLU
A
7
69.369
70.675
32.528
1.00
30.64


O


ATOM
51
CB
GLU
A
7
72.224
70.567
34.012
1.00
34.45


C


ATOM
52
CG
GLU
A
7
73.156
70.770
35.200
1.00
38.35


C


ATOM
53
CD
GLU
A
7
74.057
71.981
35.049
1.00
40.20


C


ATOM
54
OE1
GLU
A
7
74.484
72.278
33.912
1.00
41.55


O


ATOM
55
OE2
GLU
A
7
74.351
72.631
36.075
1.00
42.84


O


ATOM
56
N
PRO
A
8
70.962
71.745
31.359
1.00
28.48


N


ATOM
57
CA
PRO
A
8
70.318
71.446
30.079
1.00
27.48


C


ATOM
58
C
PRO
A
8
70.655
69.995
29.755
1.00
26.53


C


ATOM
59
O
PRO
A
8
71.595
69.448
30.326
1.00
24.18


O


ATOM
60
CB
PRO
A
8
70.992
72.423
29.121
1.00
27.72


C


ATOM
61
CG
PRO
A
8
72.380
72.532
29.688
1.00
28.52


C


ATOM
62
CD
PRO
A
8
72.113
72.649
31.172
1.00
28.72


C


ATOM
63
N
CYS
A
9
69.894
69.359
28.869
1.00
26.18


N


ATOM
64
CA
CYS
A
9
70.202
67.979
28.518
1.00
25.70


C


ATOM
65
C
CYS
A
9
71.285
67.935
27.435
1.00
25.71


C


ATOM
66
O
CYS
A
9
71.474
68.905
26.685
1.00
24.82


O


ATOM
67
CB
CYS
A
9
68.936
67.239
28.065
1.00
27.09


C


ATOM
68
SG
CYS
A
9
68.004
68.021
26.742
1.00
29.97


S


ATOM
69
N
HIS
A
10
72.003
66.816
27.370
1.00
24.60


N


ATOM
70
CA
HIS
A
10
73.095
66.632
26.414
1.00
24.16


C


ATOM
71
C
HIS
A
10
72.932
65.349
25.612
1.00
24.05


C


ATOM
72
O
HIS
A
10
72.269
64.415
26.058
1.00
22.94


O


ATOM
73
CB
HIS
A
10
74.433
66.580
27.160
1.00
24.38


C


ATOM
74
CG
HIS
A
10
74.693
67.779
28.015
1.00
25.68


C


ATOM
75
ND1
HIS
A
10
75.121
68.981
27.498
1.00
26.11


N


ATOM
76
CD2
HIS
A
10
74.544
67.973
29.347
1.00
26.09


C


ATOM
77
CE1
HIS
A
10
75.225
69.866
28.474
1.00
26.14


C


ATOM
78
NE2
HIS
A
10
74.879
69.278
29.606
1.00
27.18


N


ATOM
79
N
THR
A
11
73.549
65.311
24.432
1.00
25.34


N


ATOM
80
CA
THR
A
11
73.494
64.139
23.550
1.00
26.59


C


ATOM
81
C
THR
A
11
74.857
63.439
23.539
1.00
25.78


C


ATOM
82
O
THR
A
11
75.843
63.990
24.021
1.00
25.20


O


ATOM
83
CB
THR
A
11
73.175
64.536
22.095
1.00
28.50


C


ATOM
84
OG1
THR
A
11
74.190
65.429
21.620
1.00
31.80


O


ATOM
85
CG2
THR
A
11
71.824
65.223
22.000
1.00
31.57


C


ATOM
86
N
PHE
A
12
74.909
62.240
22.964
1.00
25.57


N


ATOM
87
CA
PHE
A
12
76.154
61.469
22.890
1.00
26.57


C


ATOM
88
C
PHE
A
12
77.334
62.201
22.244
1.00
26.75


C


ATOM
89
O
PHE
A
12
78.477
62.029
22.666
1.00
26.43


O


ATOM
90
CB
PHE
A
12
75.923
60.150
22.139
1.00
26.43


C


ATOM
91
CG
PHE
A
12
75.034
59.180
22.869
1.00
27.74


C


ATOM
92
CD1
PHE
A
12
75.212
58.940
24.226
1.00
28.25


C


ATOM
93
CD2
PHE
A
12
74.034
58.490
22.191
1.00
28.95


C


ATOM
94
CE1
PHE
A
12
74.405
58.024
24.905
1.00
29.61


C


ATOM
95
CE2
PHE
A
12
73.223
57.572
22.858
1.00
29.31


C


ATOM
96
CZ
PHE
A
12
73.408
57.339
24.215
1.00
29.14


C


ATOM
97
N
ASN
A
13
77.071
63.003
21.216
1.00
27.42


N


ATOM
98
CA
ASN
A
13
78.149
63.726
20.544
1.00
28.91


C


ATOM
99
C
ASN
A
13
78.892
64.718
21.437
1.00
27.96


C


ATOM
100
O
ASN
A
13
79.972
65.193
21.076
1.00
28.99


O


ATOM
101
CB
ASN
A
13
77.621
64.471
19.314
1.00
31.81


C


ATOM
102
CG
ASN
A
13
77.584
63.600
18.079
1.00
34.70


C


ATOM
103
OD1
ASN
A
13
78.485
62.787
17.852
1.00
36.51


O


ATOM
104
ND2
ASN
A
13
76.554
63.775
17.261
1.00
37.26


N


ATOM
105
N
GLU
A
14
78.323
65.027
22.596
1.00
26.74


N


ATOM
106
CA
GLU
A
14
78.948
65.975
23.517
1.00
26.62


C


ATOM
107
C
GLU
A
14
79.867
65.316
24.541
1.00
26.27


C


ATOM
108
O
GLU
A
14
80.414
65.992
25.408
1.00
25.62


O


ATOM
109
CB
GLU
A
14
77.873
66.763
24.263
1.00
26.66


C


ATOM
110
CG
GLU
A
14
76.939
67.529
23.347
1.00
28.65


C


ATOM
111
CD
GLU
A
14
75.890
68.293
24.114
1.00
29.22


C


ATOM
112
OE1
GLU
A
14
76.260
69.212
24.878
1.00
31.67


O


ATOM
113
OE2
GLU
A
14
74.696
67.973
23.957
1.00
29.46


O


ATOM
114
N
TYR
A
15
80.045
64.003
24.439
1.00
25.33


N


ATOM
115
CA
TYR
A
15
80.886
63.289
25.391
1.00
25.77


C


ATOM
116
C
TYR
A
15
82.069
62.544
24.788
1.00
25.99


C


ATOM
117
O
TYR
A
15
82.059
62.152
23.619
1.00
26.38


O


ATOM
118
CB
TYR
A
15
80.041
62.279
26.168
1.00
26.71


C


ATOM
119
CG
TYR
A
15
79.025
62.889
27.099
1.00
28.01


C


ATOM
120
CD1
TYR
A
15
79.377
63.262
28.397
1.00
28.23


C


ATOM
121
CD2
TYR
A
15
77.711
63.100
26.683
1.00
29.05


C


ATOM
122
CE1
TYR
A
15
78.442
63.828
29.260
1.00
30.46


C


ATOM
123
CE2
TYR
A
15
76.771
63.668
27.537
1.00
30.27


C


ATOM
124
CZ
TYR
A
15
77.144
64.028
28.820
1.00
30.91


C


ATOM
125
OH
TYR
A
15
76.219
64.604
29.659
1.00
34.07


O


ATOM
126
N
LEU
A
16
83.089
62.350
25.616
1.00
26.06


N


ATOM
127
CA
LEU
A
16
84.273
61.593
25.233
1.00
25.76


C


ATOM
128
C
LEU
A
16
84.672
60.785
26.457
1.00
24.62


C


ATOM
129
O
LEU
A
16
84.331
61.143
27.589
1.00
23.13


O


ATOM
130
CB
LEU
A
16
85.427
62.518
24.820
1.00
28.13


C


ATOM
131
CG
LEU
A
16
85.291
63.282
23.495
1.00
29.82


C


ATOM
132
CD1
LEU
A
16
86.523
64.136
23.285
1.00
30.80


C


ATOM
133
CD2
LEU
A
16
85.123
62.313
22.332
1.00
30.29


C


ATOM
134
N
LEU
A
17
85.374
59.683
26.230
1.00
24.43


N


ATOM
135
CA
LEU
A
17
85.841
58.835
27.321
1.00
25.14


C


ATOM
136
C
LEU
A
17
87.311
59.147
27.608
1.00
25.20


C


ATOM
137
O
LEU
A
17
88.097
59.336
26.682
1.00
25.84


O


ATOM
138
CB
LEU
A
17
85.706
57.359
26.933
1.00
25.29


C


ATOM
139
CG
LEU
A
17
84.288
56.777
26.938
1.00
25.32


C


ATOM
140
CD1
LEU
A
17
84.233
55.534
26.077
1.00
26.22


C


ATOM
141
CD2
LEU
A
17
83.876
56.466
28.366
1.00
25.45


C


ATOM
142
N
ILE
A
18
87.667
59.210
28.889
1.00
25.46


N


ATOM
143
CA
ILE
A
18
89.047
59.460
29.294
1.00
25.22


C


ATOM
144
C
ILE
A
18
89.608
58.101
29.718
1.00
25.38


C


ATOM
145
O
ILE
A
18
89.062
57.446
30.598
1.00
25.99


O


ATOM
146
CB
ILE
A
18
89.112
60.460
30.467
1.00
25.47


C


ATOM
147
CG1
ILE
A
18
88.653
61.843
29.979
1.00
25.88


C


ATOM
148
CG2
ILE
A
18
90.538
60.531
31.027
1.00
24.00


C


ATOM
149
CD1
ILE
A
18
88.620
62.909
31.057
1.00
28.70


C


ATOM
150
N
PRO
A
19
90.701
57.657
29.080
1.00
26.62


N


ATOM
151
CA
PRO
A
19
91.306
56.360
29.408
1.00
26.83


C


ATOM
152
C
PRO
A
19
91.605
56.116
30.889
1.00
26.38


C


ATOM
153
O
PRO
A
19
91.853
57.048
31.656
1.00
26.07


O


ATOM
154
CB
PRO
A
19
92.584
56.350
28.564
1.00
27.54


C


ATOM
155
CG
PRO
A
19
92.204
57.182
27.371
1.00
28.01


C


ATOM
156
CD
PRO
A
19
91.463
58.336
28.018
1.00
27.10


C


ATOM
157
N
GLY
A
20
91.566
54.845
31.271
1.00
25.38


N


ATOM
158
CA
GLY
A
20
91.877
54.453
32.632
1.00
26.31


C


ATOM
159
C
GLY
A
20
93.077
53.528
32.511
1.00
26.29


C


ATOM
160
O
GLY
A
20
93.662
53.423
31.437
1.00
23.85


O


ATOM
161
N
LEU
A
21
93.451
52.846
33.585
1.00
26.59


N


ATOM
162
CA
LEU
A
21
94.601
51.948
33.506
1.00
27.89


C


ATOM
163
C
LEU
A
21
94.291
50.701
32.690
1.00
28.10


C


ATOM
164
O
LEU
A
21
93.361
49.959
33.002
1.00
28.93


O


ATOM
165
CB
LEU
A
21
95.064
51.536
34.910
1.00
27.80


C


ATOM
166
CG
LEU
A
21
96.225
50.531
34.941
1.00
28.27


C


ATOM
167
CD1
LEU
A
21
97.431
51.084
34.182
1.00
27.34


C


ATOM
168
CD2
LEU
A
21
96.583
50.230
36.390
1.00
29.80


C


ATOM
169
N
SER
A
22
95.068
50.483
31.634
1.00
29.02


N


ATOM
170
CA
SER
A
22
94.900
49.310
30.788
1.00
31.01


C


ATOM
171
C
SER
A
22
95.917
48.270
31.238
1.00
32.77


C


ATOM
172
O
SER
A
22
97.118
48.530
31.234
1.00
31.01


O


ATOM
173
CB
SER
A
22
95.149
49.663
29.321
1.00
31.45


C


ATOM
174
OG
SER
A
22
94.206
50.608
28.855
1.00
30.59


O


ATOM
175
N
THR
A
23
95.435
47.096
31.632
1.00
34.58


N


ATOM
176
CA
THR
A
23
96.322
46.033
32.092
1.00
36.68


C


ATOM
177
C
THR
A
23
96.716
45.114
30.944
1.00
37.08


C


ATOM
178
O
THR
A
23
96.105
45.144
29.875
1.00
37.57


O


ATOM
179
CB
THR
A
23
95.658
45.207
33.202
1.00
37.62


C


ATOM
180
OG1
THR
A
23
94.335
44.851
32.797
1.00
40.83


O


ATOM
181
CG2
THR
A
23
95.581
46.011
34.492
1.00
39.51


C


ATOM
182
N
VAL
A
24
97.742
44.298
31.163
1.00
37.49


N


ATOM
183
CA
VAL
A
24
98.217
43.390
30.128
1.00
38.46


C


ATOM
184
C
VAL
A
24
97.187
42.348
29.697
1.00
39.49


C


ATOM
185
O
VAL
A
24
97.256
41.832
28.583
1.00
39.42


O


ATOM
186
CB
VAL
A
24
99.508
42.660
30.575
1.00
38.44


C


ATOM
187
CG1
VAL
A
24
100.651
43.662
30.713
1.00
37.27


C


ATOM
188
CG2
VAL
A
24
99.272
41.940
31.894
1.00
38.19


C


ATOM
189
N
ASP
A
25
96.224
42.045
30.562
1.00
41.42


N


ATOM
190
CA
ASP
A
25
95.219
41.047
30.210
1.00
44.00


C


ATOM
191
C
ASP
A
25
94.070
41.590
29.362
1.00
44.29


C


ATOM
192
O
ASP
A
25
93.220
40.826
28.908
1.00
44.12


O


ATOM
193
CB
ASP
A
25
94.653
40.380
31.473
1.00
46.46


C


ATOM
194
CG
ASP
A
25
93.826
41.329
32.327
1.00
49.04


C


ATOM
195
OD1
ASP
A
25
93.177
40.852
33.280
1.00
51.13


O


ATOM
196
OD2
ASP
A
25
93.819
42.545
32.058
1.00
51.46


O


ATOM
197
N
CYS
A
26
94.032
42.898
29.132
1.00
44.45


N


ATOM
198
CA
CYS
A
26
92.937
43.434
28.333
1.00
44.38


C


ATOM
199
C
CYS
A
26
93.245
43.623
26.866
1.00
44.52


C


ATOM
200
O
CYS
A
26
93.840
44.623
26.465
1.00
44.45


O


ATOM
201
CB
CYS
A
26
92.432
44.767
28.879
1.00
43.39


C


ATOM
202
SG
CYS
A
26
90.722
45.164
28.351
1.00
43.27


S


ATOM
203
N
ILE
A
27
92.835
42.646
26.071
1.00
44.85


N


ATOM
204
CA
ILE
A
27
92.984
42.712
24.631
1.00
45.31


C


ATOM
205
C
ILE
A
27
91.559
42.482
24.155
1.00
45.02


C


ATOM
206
O
ILE
A
27
90.791
41.782
24.815
1.00
44.66


O


ATOM
207
CB
ILE
A
27
93.924
41.612
24.084
1.00
46.44


C


ATOM
208
CG1
ILE
A
27
93.461
40.234
24.555
1.00
46.68


C


ATOM
209
CG2
ILE
A
27
95.358
41.893
24.524
1.00
46.86


C


ATOM
210
CD1
ILE
A
27
94.354
39.098
24.083
1.00
48.06


C


ATOM
211
N
PRO
A
28
91.179
43.089
23.024
1.00
45.29


N


ATOM
212
CA
PRO
A
28
89.836
42.959
22.453
1.00
44.96


C


ATOM
213
C
PRO
A
28
89.231
41.557
22.486
1.00
44.81


C


ATOM
214
O
PRO
A
28
88.051
41.393
22.800
1.00
44.44


O


ATOM
215
CB
PRO
A
28
90.027
43.474
21.031
1.00
45.44


C


ATOM
216
CG
PRO
A
28
91.024
44.565
21.223
1.00
45.66


C


ATOM
217
CD
PRO
A
28
92.031
43.934
22.166
1.00
45.97


C


ATOM
218
N
SER
A
29
90.035
40.549
22.167
1.00
44.03


N


ATOM
219
CA
SER
A
29
89.547
39.174
22.134
1.00
43.07


C


ATOM
220
C
SER
A
29
89.168
38.597
23.495
1.00
42.20


C


ATOM
221
O
SER
A
29
88.477
37.582
23.567
1.00
42.12


O


ATOM
222
CB
SER
A
29
90.576
38.261
21.455
1.00
43.90


C


ATOM
223
OG
SER
A
29
91.766
38.166
22.214
1.00
45.30


O


ATOM
224
N
ASN
A
30
89.615
39.227
24.575
1.00
40.59


N


ATOM
225
CA
ASN
A
30
89.271
38.735
25.902
1.00
39.15


C


ATOM
226
C
ASN
A
30
88.079
39.489
26.491
1.00
37.08


C


ATOM
227
O
ASN
A
30
87.606
39.159
27.577
1.00
36.93


O


ATOM
228
CB
ASN
A
30
90.463
38.844
26.858
1.00
41.71


C


ATOM
229
CG
ASN
A
30
91.564
37.851
26.538
1.00
44.46


C


ATOM
230
OD1
ASN
A
30
91.296
36.703
26.186
1.00
45.63


O


ATOM
231
ND2
ASN
A
30
92.811
38.283
26.677
1.00
46.20


N


ATOM
232
N
VAL
A
31
87.595
40.497
25.774
1.00
33.45


N


ATOM
233
CA
VAL
A
31
86.461
41.279
26.252
1.00
31.88


C


ATOM
234
C
VAL
A
31
85.150
40.513
26.093
1.00
30.75


C


ATOM
235
O
VAL
A
31
84.858
39.981
25.025
1.00
30.55


O


ATOM
236
CB
VAL
A
31
86.353
42.628
25.503
1.00
30.76


C


ATOM
237
CG1
VAL
A
31
85.074
43.355
25.914
1.00
30.99


C


ATOM
238
CG2
VAL
A
31
87.568
43.491
25.817
1.00
31.39


C


ATOM
239
N
ASN
A
32
84.372
40.463
27.168
1.00
30.39


N


ATOM
240
CA
ASN
A
32
83.085
39.771
27.175
1.00
30.35


C


ATOM
241
C
ASN
A
32
81.968
40.802
27.058
1.00
29.35


C


ATOM
242
O
ASN
A
32
81.837
41.675
27.916
1.00
29.27


O


ATOM
243
CB
ASN
A
32
82.929
38.965
28.474
1.00
32.17


C


ATOM
244
CG
ASN
A
32
81.509
38.449
28.685
1.00
34.34


C


ATOM
245
OD1
ASN
A
32
80.751
38.273
27.736
1.00
34.02


O


ATOM
246
ND2
ASN
A
32
81.153
38.193
29.941
1.00
38.74


N


ATOM
247
N
LEU
A
33
81.166
40.705
26.001
1.00
28.15


N


ATOM
248
CA
LEU
A
33
80.077
41.661
25.803
1.00
27.70


C


ATOM
249
C
LEU
A
33
78.693
41.128
26.178
1.00
27.94


C


ATOM
250
O
LEU
A
33
77.676
41.639
25.711
1.00
27.44


O


ATOM
251
CB
LEU
A
33
80.071
42.160
24.351
1.00
27.83


C


ATOM
252
CG
LEU
A
33
81.288
42.979
23.906
1.00
28.65


C


ATOM
253
CD1
LEU
A
33
81.127
43.403
22.448
1.00
27.96


C


ATOM
254
CD2
LEU
A
33
81.443
44.202
24.800
1.00
28.65


C


ATOM
255
N
SER
A
34
78.646
40.109
27.028
1.00
28.06


N


ATOM
256
CA
SER
A
34
77.361
39.559
27.457
1.00
29.26


C


ATOM
257
C
SER
A
34
76.628
40.593
28.310
1.00
28.04


C


ATOM
258
O
SER
A
34
77.255
41.406
28.987
1.00
27.93


O


ATOM
259
CB
SER
A
34
77.574
38.283
28.268
1.00
30.15


C


ATOM
260
OG
SER
A
34
78.220
37.308
27.471
1.00
35.29


O


ATOM
261
N
THR
A
35
75.301
40.565
28.283
1.00
27.47


N


ATOM
262
CA
THR
A
35
74.533
41.528
29.058
1.00
26.66


C


ATOM
263
C
THR
A
35
73.113
41.009
29.299
1.00
26.85


C


ATOM
264
O
THR
A
35
72.540
40.317
28.455
1.00
27.02


O


ATOM
265
CB
THR
A
35
74.497
42.896
28.320
1.00
27.50


C


ATOM
266
OG1
THR
A
35
74.222
43.949
29.252
1.00
27.27


O


ATOM
267
CG2
THR
A
35
73.425
42.894
27.234
1.00
26.76


C


ATOM
268
N
PRO
A
36
72.529
41.334
30.462
1.00
26.24


N


ATOM
269
CA
PRO
A
36
71.175
40.887
30.795
1.00
26.48


C


ATOM
270
C
PRO
A
36
70.082
41.574
29.979
1.00
26.94


C


ATOM
271
O
PRO
A
36
70.166
42.769
29.683
1.00
26.63


O


ATOM
272
CB
PRO
A
36
71.067
41.205
32.282
1.00
25.88


C


ATOM
273
CG
PRO
A
36
71.883
42.446
32.402
1.00
25.82


C


ATOM
274
CD
PRO
A
36
73.098
42.144
31.554
1.00
25.46


C


ATOM
275
N
LEU
A
37
69.054
40.810
29.627
1.00
26.53


N


ATOM
276
CA
LEU
A
37
67.942
41.344
28.857
1.00
26.66


C


ATOM
277
C
LEU
A
37
66.705
41.564
29.724
1.00
26.63


C


ATOM
278
O
LEU
A
37
65.960
42.526
29.516
1.00
26.36


O


ATOM
279
CB
LEU
A
37
67.588
40.396
27.706
1.00
27.85


C


ATOM
280
CG
LEU
A
37
66.499
40.910
26.759
1.00
27.81


C


ATOM
281
CD1
LEU
A
37
67.061
42.044
25.911
1.00
28.43


C


ATOM
282
CD2
LEU
A
37
66.006
39.780
25.869
1.00
28.49


C


ATOM
283
N
VAL
A
38
66.483
40.684
30.699
1.00
26.11


N


ATOM
284
CA
VAL
A
38
65.305
40.807
31.556
1.00
26.61


C


ATOM
285
C
VAL
A
38
65.651
40.829
33.040
1.00
27.13


C


ATOM
286
O
VAL
A
38
66.667
40.279
33.461
1.00
27.11


O


ATOM
287
CB
VAL
A
38
64.288
39.674
31.264
1.00
26.52


C


ATOM
288
CG1
VAL
A
38
63.862
39.748
29.803
1.00
27.45


C


ATOM
289
CG2
VAL
A
38
64.902
38.310
31.562
1.00
26.40


C


ATOM
290
N
LYS
A
39
64.790
41.468
33.825
1.00
27.15


N


ATOM
291
CA
LYS
A
39
65.011
41.625
35.256
1.00
27.73


C


ATOM
292
C
LYS
A
39
65.216
40.348
36.058
1.00
28.72


C


ATOM
293
O
LYS
A
39
64.724
39.274
35.695
1.00
28.88


O


ATOM
294
CB
LYS
A
39
63.865
42.425
35.885
1.00
28.20


C


ATOM
295
CG
LYS
A
39
62.508
41.718
35.873
1.00
28.09


C


ATOM
296
CD
LYS
A
39
61.492
42.510
36.690
1.00
29.72


C


ATOM
297
CE
LYS
A
39
60.107
41.877
36.642
1.00
30.35


C


ATOM
298
NZ
LYS
A
39
59.162
42.618
37.526
1.00
31.05


N


ATOM
299
N
PHE
A
40
65.947
40.502
37.159
1.00
28.59


N


ATOM
300
CA
PHE
A
40
66.254
39.424
38.089
1.00
29.38


C


ATOM
301
C
PHE
A
40
66.508
40.026
39.469
1.00
30.67


C


ATOM
302
O
PHE
A
40
66.605
41.250
39.611
1.00
31.06


O


ATOM
303
CB
PHE
A
40
67.485
38.633
37.627
1.00
29.02


C


ATOM
304
CG
PHE
A
40
68.706
39.481
37.379
1.00
28.39


C


ATOM
305
CD1
PHE
A
40
68.920
40.074
36.136
1.00
29.01


C


ATOM
306
CD2
PHE
A
40
69.649
39.671
38.381
1.00
28.07


C


ATOM
307
CE1
PHE
A
40
70.059
40.843
35.897
1.00
28.63


C


ATOM
308
CE2
PHE
A
40
70.790
40.435
38.157
1.00
28.51


C


ATOM
309
CZ
PHE
A
40
70.997
41.022
36.912
1.00
28.67


C


ATOM
310
N
GLN
A
41
66.609
39.168
40.482
1.00
30.52


N


ATOM
311
CA
GLN
A
41
66.843
39.608
41.857
1.00
32.51


C


ATOM
312
C
GLN
A
41
68.324
39.615
42.199
1.00
31.08


C


ATOM
313
O
GLN
A
41
69.120
38.950
41.544
1.00
32.21


O


ATOM
314
CB
GLN
A
41
66.131
38.677
42.852
1.00
34.57


C


ATOM
315
CG
GLN
A
41
64.623
38.683
42.769
1.00
40.18


C


ATOM
316
CD
GLN
A
41
64.029
40.014
43.189
1.00
42.08


C


ATOM
317
OE1
GLN
A
41
64.187
40.451
44.333
1.00
45.71


O


ATOM
318
NE2
GLN
A
41
63.345
40.667
42.263
1.00
44.39


N


ATOM
319
N
LYS
A
42
68.678
40.364
43.238
1.00
30.91


N


ATOM
320
CA
LYS
A
42
70.057
40.444
43.705
1.00
31.44


C


ATOM
321
C
LYS
A
42
70.606
39.028
43.937
1.00
31.78


C


ATOM
322
O
LYS
A
42
69.945
38.190
44.556
1.00
30.49


O


ATOM
323
CB
LYS
A
42
70.106
41.241
45.009
1.00
33.17


C


ATOM
324
CG
LYS
A
42
71.456
41.242
45.701
1.00
35.83


C


ATOM
325
CD
LYS
A
42
71.399
42.043
46.994
1.00
38.92


C


ATOM
326
CE
LYS
A
42
72.740
42.029
47.706
1.00
40.30


C


ATOM
327
NZ
LYS
A
42
72.711
42.865
48.938
1.00
43.53


N


ATOM
328
N
GLY
A
43
71.805
38.768
43.426
1.00
31.76


N


ATOM
329
CA
GLY
A
43
72.420
37.463
43.593
1.00
31.06


C


ATOM
330
C
GLY
A
43
72.125
36.484
42.473
1.00
30.81


C


ATOM
331
O
GLY
A
43
72.751
35.426
42.384
1.00
30.33


O


ATOM
332
N
GLN
A
44
71.170
36.822
41.615
1.00
30.18


N


ATOM
333
CA
GLN
A
44
70.817
35.946
40.507
1.00
30.45


C


ATOM
334
C
GLN
A
44
71.410
36.461
39.203
1.00
31.41


C


ATOM
335
O
GLN
A
44
72.075
37.494
39.172
1.00
30.58


O


ATOM
336
CB
GLN
A
44
69.295
35.870
40.345
1.00
31.54


C


ATOM
337
CG
GLN
A
44
68.521
35.673
41.637
1.00
32.79


C


ATOM
338
CD
GLN
A
44
67.016
35.631
41.407
1.00
34.29


C


ATOM
339
OE1
GLN
A
44
66.492
36.327
40.537
1.00
32.47


O


ATOM
340
NE2
GLN
A
44
66.316
34.827
42.299
1.00
32.10


N


ATOM
341
N
GLN
A
45
71.161
35.710
38.136
1.00
32.01


N


ATOM
342
CA
GLN
A
45
71.593
36.058
36.791
1.00
33.43


C


ATOM
343
C
GLN
A
45
70.299
36.153
35.992
1.00
32.33


C


ATOM
344
O
GLN
A
45
69.310
35.516
36.345
1.00
31.57


O


ATOM
345
CB
GLN
A
45
72.476
34.957
36.196
1.00
37.06


C


ATOM
346
CG
GLN
A
45
73.829
34.819
36.864
1.00
42.03


C


ATOM
347
CD
GLN
A
45
74.634
36.097
36.781
1.00
44.70


C


ATOM
348
OE1
GLN
A
45
74.911
36.596
35.689
1.00
47.34


O


ATOM
349
NE2
GLN
A
45
75.010
36.641
37.936
1.00
45.66


N


ATOM
350
N
SER
A
46
70.299
36.945
34.926
1.00
30.96


N


ATOM
351
CA
SER
A
46
69.103
37.082
34.107
1.00
30.90


C


ATOM
352
C
SER
A
46
68.791
35.762
33.407
1.00
31.56


C


ATOM
353
O
SER
A
46
69.700
35.004
33.078
1.00
30.43


O


ATOM
354
CB
SER
A
46
69.300
38.171
33.053
1.00
29.48


C


ATOM
355
OG
SER
A
46
68.130
38.324
32.276
1.00
28.63


O


ATOM
356
N
GLU
A
47
67.507
35.495
33.180
1.00
32.24


N


ATOM
357
CA
GLU
A
47
67.097
34.271
32.498
1.00
33.72


C


ATOM
358
C
GLU
A
47
67.495
34.336
31.033
1.00
32.95


C


ATOM
359
O
GLU
A
47
67.601
33.311
30.363
1.00
32.68


O


ATOM
360
CB
GLU
A
47
65.587
34.078
32.614
1.00
35.36


C


ATOM
361
CG
GLU
A
47
65.118
33.791
34.027
1.00
39.32


C


ATOM
362
CD
GLU
A
47
63.613
33.865
34.159
1.00
41.79


C


ATOM
363
OE1
GLU
A
47
62.918
33.052
33.513
1.00
44.11


O


ATOM
364
OE2
GLU
A
47
63.124
34.743
34.904
1.00
43.26


O


ATOM
365
N
ILE
A
48
67.701
35.551
30.531
1.00
31.57


N


ATOM
366
CA
ILE
A
48
68.114
35.736
29.143
1.00
30.16


C


ATOM
367
C
ILE
A
48
69.271
36.727
29.080
1.00
29.80


C


ATOM
368
O
ILE
A
48
69.148
37.869
29.521
1.00
29.23


O


ATOM
369
CB
ILE
A
48
66.962
36.280
28.258
1.00
31.15


C


ATOM
370
CG1
ILE
A
48
65.780
35.308
28.267
1.00
31.70


C


ATOM
371
CG2
ILE
A
48
67.461
36.479
26.835
1.00
30.35


C


ATOM
372
CD1
ILE
A
48
64.578
35.800
27.487
1.00
33.88


C


ATOM
373
N
ASN
A
49
70.396
36.280
28.536
1.00
28.20


N


ATOM
374
CA
ASN
A
49
71.567
37.129
28.403
1.00
28.79


C


ATOM
375
C
ASN
A
49
71.982
37.194
26.947
1.00
28.45


C


ATOM
376
O
ASN
A
49
72.204
36.160
26.309
1.00
28.24


O


ATOM
377
CB
ASN
A
49
72.728
36.579
29.238
1.00
29.15


C


ATOM
378
CG
ASN
A
49
72.459
36.656
30.726
1.00
30.85


C


ATOM
379
OD1
ASN
A
49
72.610
37.712
31.343
1.00
29.61


O


ATOM
380
ND2
ASN
A
49
72.041
35.538
31.310
1.00
30.46


N


ATOM
381
N
LEU
A
50
72.061
38.407
26.412
1.00
27.38


N


ATOM
382
CA
LEU
A
50
72.488
38.585
25.030
1.00
27.41


C


ATOM
383
C
LEU
A
50
73.990
38.324
25.035
1.00
27.31


C


ATOM
384
O
LEU
A
50
74.635
38.498
26.069
1.00
26.24


O


ATOM
385
CB
LEU
A
50
72.233
40.026
24.573
1.00
27.05


C


ATOM
386
CG
LEU
A
50
70.818
40.596
24.686
1.00
28.18


C


ATOM
387
CD1
LEU
A
50
70.838
42.092
24.356
1.00
28.26


C


ATOM
388
CD2
LEU
A
50
69.887
39.849
23.745
1.00
29.22


C


ATOM
389
N
LYS
A
51
74.542
37.898
23.901
1.00
28.23


N


ATOM
390
CA
LYS
A
51
75.978
37.666
23.804
1.00
28.76


C


ATOM
391
C
LYS
A
51
76.661
38.946
23.313
1.00
28.00


C


ATOM
392
O
LYS
A
51
77.867
39.118
23.478
1.00
27.68


O


ATOM
393
CB
LYS
A
51
76.275
36.463
22.897
1.00
31.27


C


ATOM
394
CG
LYS
A
51
75.819
35.155
23.546
1.00
32.77


C


ATOM
395
CD
LYS
A
51
76.238
33.915
22.771
1.00
35.29


C


ATOM
396
CE
LYS
A
51
75.732
32.661
23.486
1.00
36.18


C


ATOM
397
NZ
LYS
A
51
76.082
31.402
22.757
1.00
38.13


N


ATOM
398
N
ILE
A
52
75.877
39.834
22.700
1.00
26.71


N


ATOM
399
CA
ILE
A
52
76.359
41.150
22.277
1.00
26.00


C


ATOM
400
C
ILE
A
52
75.227
42.109
22.668
1.00
26.56


C


ATOM
401
O
ILE
A
52
74.049
41.764
22.566
1.00
26.00


O


ATOM
402
CB
ILE
A
52
76.689
41.247
20.756
1.00
26.91


C


ATOM
403
CG1
ILE
A
52
75.458
40.947
19.899
1.00
27.54


C


ATOM
404
CG2
ILE
A
52
77.856
40.303
20.421
1.00
27.36


C


ATOM
405
CD1
ILE
A
52
75.675
41.287
18.423
1.00
27.06


C


ATOM
406
N
PRO
A
53
75.570
43.322
23.124
1.00
25.59


N


ATOM
407
CA
PRO
A
53
74.590
44.326
23.556
1.00
26.47


C


ATOM
408
C
PRO
A
53
73.782
45.080
22.501
1.00
27.16


C


ATOM
409
O
PRO
A
53
73.395
46.228
22.730
1.00
26.78


O


ATOM
410
CB
PRO
A
53
75.439
45.269
24.400
1.00
25.56


C


ATOM
411
CG
PRO
A
53
76.720
45.315
23.605
1.00
25.49


C


ATOM
412
CD
PRO
A
53
76.945
43.853
23.222
1.00
25.76


C


ATOM
413
N
LEU
A
54
73.502
44.443
21.368
1.00
26.87


N


ATOM
414
CA
LEU
A
54
72.745
45.106
20.314
1.00
27.02


C


ATOM
415
C
LEU
A
54
71.426
44.404
19.979
1.00
26.78


C


ATOM
416
O
LEU
A
54
71.376
43.177
19.861
1.00
27.27


O


ATOM
417
CB
LEU
A
54
73.588
45.201
19.038
1.00
26.49


C


ATOM
418
CG
LEU
A
54
75.010
45.771
19.104
1.00
26.90


C


ATOM
419
CD1
LEU
A
54
75.588
45.807
17.692
1.00
28.33


C


ATOM
420
CD2
LEU
A
54
75.000
47.168
19.716
1.00
26.89


C


ATOM
421
N
VAL
A
55
70.359
45.186
19.847
1.00
26.28


N


ATOM
422
CA
VAL
A
55
69.061
44.641
19.461
1.00
26.52


C


ATOM
423
C
VAL
A
55
68.516
45.542
18.349
1.00
26.85


C


ATOM
424
O
VAL
A
55
68.753
46.751
18.353
1.00
27.05


O


ATOM
425
CB
VAL
A
55
68.066
44.574
20.655
1.00
26.19


C


ATOM
426
CG1
VAL
A
55
68.718
43.837
21.823
1.00
25.91


C


ATOM
427
CG2
VAL
A
55
67.614
45.963
21.064
1.00
26.54


C


ATOM
428
N
SER
A
56
67.812
44.958
17.381
1.00
26.45


N


ATOM
429
CA
SER
A
56
67.281
45.750
16.279
1.00
26.33


C


ATOM
430
C
SER
A
56
65.909
46.329
16.613
1.00
26.47


C


ATOM
431
O
SER
A
56
65.091
45.694
17.286
1.00
26.78


O


ATOM
432
CB
SER
A
56
67.239
44.916
14.985
1.00
27.61


C


ATOM
433
OG
SER
A
56
66.504
43.720
15.149
1.00
27.08


O


ATOM
434
N
ALA
A
57
65.687
47.556
16.152
1.00
26.29


N


ATOM
435
CA
ALA
A
57
64.462
48.307
16.400
1.00
26.64


C


ATOM
436
C
ALA
A
57
63.167
47.618
15.963
1.00
27.43


C


ATOM
437
O
ALA
A
57
63.161
46.798
15.045
1.00
27.98


O


ATOM
438
CB
ALA
A
57
64.572
49.672
15.739
1.00
25.98


C


ATOM
439
N
ILE
A
58
62.076
47.968
16.638
1.00
27.92


N


ATOM
440
CA
ILE
A
58
60.753
47.413
16.354
1.00
28.86


C


ATOM
441
C
ILE
A
58
60.196
48.224
15.191
1.00
29.07


C


ATOM
442
O
ILE
A
58
59.308
49.064
15.371
1.00
29.42


O


ATOM
443
CB
ILE
A
58
59.823
47.572
17.576
1.00
28.92


C


ATOM
444
CG1
ILE
A
58
60.574
47.170
18.852
1.00
28.75


C


ATOM
445
CG2
ILE
A
58
58.578
46.718
17.397
1.00
27.62


C


ATOM
446
CD1
ILE
A
58
59.752
47.286
20.126
1.00
29.63


C


ATOM
447
N
MET
A
59
60.731
47.969
14.003
1.00
29.21


N


ATOM
448
CA
MET
A
59
60.344
48.714
12.811
1.00
29.85


C


ATOM
449
C
MET
A
59
60.187
47.851
11.565
1.00
30.08


C


ATOM
450
O
MET
A
59
60.970
46.929
11.330
1.00
29.39


O


ATOM
451
CB
MET
A
59
61.395
49.793
12.537
1.00
29.69


C


ATOM
452
CG
MET
A
59
61.639
50.736
13.710
1.00
29.89


C


ATOM
453
SD
MET
A
59
63.017
51.863
13.414
1.00
30.04


S


ATOM
454
CE
MET
A
59
62.383
52.830
12.049
1.00
28.55


C


ATOM
455
N
GLN
A
60
59.182
48.181
10.756
1.00
30.89


N


ATOM
456
CA
GLN
A
60
58.906
47.452
9.520
1.00
31.91


C


ATOM
457
C
GLN
A
60
60.127
47.431
8.606
1.00
32.39


C


ATOM
458
O
GLN
A
60
60.374
46.447
7.916
1.00
32.51


O


ATOM
459
CB
GLN
A
60
57.759
48.110
8.741
1.00
32.69


C


ATOM
460
CG
GLN
A
60
56.508
48.441
9.532
1.00
33.24


C


ATOM
461
CD
GLN
A
60
55.445
49.085
8.656
1.00
35.53


C


ATOM
462
OE1
GLN
A
60
55.761
49.829
7.723
1.00
35.53


O


ATOM
463
NE2
GLN
A
60
54.178
48.813
8.957
1.00
35.36


N


ATOM
464
N
SER
A
61
60.879
48.528
8.590
1.00
32.34


N


ATOM
465
CA
SER
A
61
62.051
48.629
7.727
1.00
32.96


C


ATOM
466
C
SER
A
61
63.333
48.085
8.344
1.00
32.88


C


ATOM
467
O
SER
A
61
64.415
48.273
7.790
1.00
34.10


O


ATOM
468
CB
SER
A
61
62.273
50.089
7.312
1.00
33.69


C


ATOM
469
OG
SER
A
61
62.544
50.910
8.437
1.00
35.94


O


ATOM
470
N
VAL
A
62
63.218
47.394
9.472
1.00
32.07


N


ATOM
471
CA
VAL
A
62
64.404
46.867
10.130
1.00
31.11


C


ATOM
472
C
VAL
A
62
64.348
45.411
10.572
1.00
31.10


C


ATOM
473
O
VAL
A
62
65.145
44.590
10.126
1.00
31.19


O


ATOM
474
CB
VAL
A
62
64.764
47.713
11.383
1.00
31.46


C


ATOM
475
CG1
VAL
A
62
65.992
47.128
12.070
1.00
30.28


C


ATOM
476
CG2
VAL
A
62
65.018
49.160
10.988
1.00
30.77


C


ATOM
477
N
SER
A
63
63.399
45.091
11.444
1.00
31.39


N


ATOM
478
CA
SER
A
63
63.312
43.752
12.000
1.00
31.57


C


ATOM
479
C
SER
A
63
62.341
42.743
11.393
1.00
32.24


C


ATOM
480
O
SER
A
63
61.242
42.535
11.907
1.00
31.09


O


ATOM
481
CB
SER
A
63
63.064
43.863
13.508
1.00
31.83


C


ATOM
482
OG
SER
A
63
64.118
44.590
14.129
1.00
31.09


O


ATOM
483
N
GLY
A
64
62.778
42.112
10.307
1.00
32.50


N


ATOM
484
CA
GLY
A
64
61.986
41.087
9.651
1.00
34.07


C


ATOM
485
C
GLY
A
64
62.598
39.756
10.051
1.00
35.58


C


ATOM
486
O
GLY
A
64
63.493
39.729
10.903
1.00
33.57


O


ATOM
487
N
GLU
A
65
62.155
38.652
9.450
1.00
36.69


N


ATOM
488
CA
GLU
A
65
62.704
37.350
9.821
1.00
38.49


C


ATOM
489
C
GLU
A
65
64.187
37.205
9.494
1.00
38.04


C


ATOM
490
O
GLU
A
65
64.942
36.652
10.292
1.00
37.92


O


ATOM
491
CB
GLU
A
65
61.913
36.202
9.171
1.00
41.36


C


ATOM
492
CG
GLU
A
65
61.881
36.201
7.652
1.00
46.27


C


ATOM
493
CD
GLU
A
65
60.758
37.049
7.076
1.00
49.42


C


ATOM
494
OE1
GLU
A
65
60.603
37.055
5.835
1.00
51.56


O


ATOM
495
OE2
GLU
A
65
60.028
37.706
7.852
1.00
51.36


O


ATOM
496
N
LYS
A
66
64.606
37.700
8.333
1.00
37.76


N


ATOM
497
CA
LYS
A
66
66.006
37.612
7.934
1.00
38.96


C


ATOM
498
C
LYS
A
66
66.909
38.345
8.924
1.00
37.51


C


ATOM
499
O
LYS
A
66
67.975
37.848
9.290
1.00
36.95


O


ATOM
500
CB
LYS
A
66
66.208
38.193
6.531
1.00
40.79


C


ATOM
501
CG
LYS
A
66
65.594
37.358
5.415
1.00
45.49


C


ATOM
502
CD
LYS
A
66
65.912
37.944
4.042
1.00
48.08


C


ATOM
503
CE
LYS
A
66
65.320
37.094
2.925
1.00
49.82


C


ATOM
504
NZ
LYS
A
66
65.647
37.631
1.571
1.00
51.36


N


ATOM
505
N
MET
A
67
66.480
39.527
9.351
1.00
35.99


N


ATOM
506
CA
MET
A
67
67.254
40.314
10.304
1.00
34.82


C


ATOM
507
C
MET
A
67
67.378
39.563
11.624
1.00
34.24


C


ATOM
508
O
MET
A
67
68.468
39.447
12.182
1.00
33.61


O


ATOM
509
CB
MET
A
67
66.579
41.666
10.545
1.00
34.96


C


ATOM
510
CG
MET
A
67
67.298
42.561
11.546
1.00
34.38


C


ATOM
511
SD
MET
A
67
68.955
43.020
11.010
1.00
35.01


S


ATOM
512
CE
MET
A
67
68.573
44.146
9.657
1.00
33.42


C


ATOM
513
N
ALA
A
68
66.252
39.046
12.110
1.00
33.39


N


ATOM
514
CA
ALA
A
68
66.215
38.315
13.369
1.00
33.20


C


ATOM
515
C
ALA
A
68
67.165
37.123
13.387
1.00
33.51


C


ATOM
516
O
ALA
A
68
67.798
36.841
14.403
1.00
33.13


O


ATOM
517
CB
ALA
A
68
64.787
37.854
13.661
1.00
33.11


C


ATOM
518
N
ILE
A
69
67.262
36.419
12.265
1.00
33.68


N


ATOM
519
CA
ILE
A
69
68.147
35.265
12.182
1.00
33.04


C


ATOM
520
C
ILE
A
69
69.603
35.712
12.131
1.00
32.05


C


ATOM
521
O
ILE
A
69
70.452
35.174
12.841
1.00
33.24


O


ATOM
522
CB
ILE
A
69
67.827
34.409
10.933
1.00
34.02


C


ATOM
523
CG1
ILE
A
69
66.463
33.736
11.104
1.00
34.34


C


ATOM
524
CG2
ILE
A
69
68.911
33.365
10.719
1.00
33.54


C


ATOM
525
CD1
ILE
A
69
65.913
33.127
9.819
1.00
37.29


C


ATOM
526
N
ALA
A
70
69.884
36.709
11.300
1.00
31.48


N


ATOM
527
CA
ALA
A
70
71.236
37.225
11.149
1.00
30.65


C


ATOM
528
C
ALA
A
70
71.799
37.799
12.445
1.00
30.57


C


ATOM
529
O
ALA
A
70
72.969
37.593
12.763
1.00
29.93


O


ATOM
530
CB
ALA
A
70
71.264
38.284
10.063
1.00
30.23


C


ATOM
531
N
LEU
A
71
70.967
38.523
13.188
1.00
29.53


N


ATOM
532
CA
LEU
A
71
71.409
39.129
14.438
1.00
29.98


C


ATOM
533
C
LEU
A
71
71.553
38.098
15.552
1.00
30.25


C


ATOM
534
O
LEU
A
71
72.517
38.141
16.314
1.00
30.96


O


ATOM
535
CB
LEU
A
71
70.442
40.242
14.859
1.00
28.55


C


ATOM
536
CG
LEU
A
71
70.809
41.061
16.103
1.00
28.68


C


ATOM
537
CD1
LEU
A
71
72.271
41.482
16.041
1.00
27.67


C


ATOM
538
CD2
LEU
A
71
69.898
42.287
16.192
1.00
28.74


C


ATOM
539
N
ALA
A
72
70.607
37.166
15.645
1.00
31.21


N


ATOM
540
CA
ALA
A
72
70.683
36.131
16.672
1.00
31.98


C


ATOM
541
C
ALA
A
72
71.953
35.308
16.468
1.00
32.78


C


ATOM
542
O
ALA
A
72
72.569
34.847
17.434
1.00
31.74


O


ATOM
543
CB
ALA
A
72
69.452
35.222
16.608
1.00
31.69


C


ATOM
544
N
ARG
A
73
72.335
35.121
15.206
1.00
33.82


N


ATOM
545
CA
ARG
A
73
73.533
34.354
14.876
1.00
35.76


C


ATOM
546
C
ARG
A
73
74.786
35.010
15.435
1.00
35.30


C


ATOM
547
O
ARG
A
73
75.760
34.328
15.745
1.00
34.89


O


ATOM
548
CB
ARG
A
73
73.680
34.200
13.358
1.00
37.37


C


ATOM
549
CG
ARG
A
73
72.809
33.109
12.747
1.00
39.96


C


ATOM
550
CD
ARG
A
73
72.927
33.093
11.228
1.00
42.81


C


ATOM
551
NE
ARG
A
73
72.204
31.970
10.636
1.00
45.35


N


ATOM
552
CZ
ARG
A
73
71.945
31.844
9.337
1.00
47.16


C


ATOM
553
NH1
ARG
A
73
72.344
32.773
8.479
1.00
47.06


N


ATOM
554
NH2
ARG
A
73
71.289
30.778
8.894
1.00
48.38


N


ATOM
555
N
GLU
A
74
74.755
36.335
15.565
1.00
35.55


N


ATOM
556
CA
GLU
A
74
75.899
37.069
16.088
1.00
34.99


C


ATOM
557
C
GLU
A
74
75.796
37.327
17.591
1.00
33.84


C


ATOM
558
O
GLU
A
74
76.693
37.923
18.181
1.00
33.27


O


ATOM
559
CB
GLU
A
74
76.065
38.396
15.342
1.00
37.11


C


ATOM
560
CG
GLU
A
74
76.218
38.254
13.826
1.00
39.97


C


ATOM
561
CD
GLU
A
74
77.309
37.270
13.418
1.00
43.26


C


ATOM
562
OE1
GLU
A
74
78.448
37.383
13.924
1.00
44.46


O


ATOM
563
OE2
GLU
A
74
77.027
36.384
12.580
1.00
44.73


O


ATOM
564
N
GLY
A
75
74.702
36.893
18.209
1.00
32.10


N


ATOM
565
CA
GLY
A
75
74.562
37.081
19.645
1.00
31.13


C


ATOM
566
C
GLY
A
75
73.553
38.107
20.123
1.00
30.09


C


ATOM
567
O
GLY
A
75
73.352
38.256
21.330
1.00
29.67


O


ATOM
568
N
GLY
A
76
72.926
38.815
19.190
1.00
28.66


N


ATOM
569
CA
GLY
A
76
71.937
39.814
19.559
1.00
28.32


C


ATOM
570
C
GLY
A
76
70.526
39.294
19.342
1.00
28.09


C


ATOM
571
O
GLY
A
76
70.325
38.101
19.089
1.00
27.76


O


ATOM
572
N
ILE
A
77
69.541
40.181
19.436
1.00
27.98


N


ATOM
573
CA
ILE
A
77
68.157
39.774
19.239
1.00
27.37


C


ATOM
574
C
ILE
A
77
67.363
40.857
18.497
1.00
28.41


C


ATOM
575
O
ILE
A
77
67.632
42.053
18.638
1.00
26.87


O


ATOM
576
CB
ILE
A
77
67.491
39.456
20.603
1.00
27.78


C


ATOM
577
CG1
ILE
A
77
66.246
38.592
20.392
1.00
27.09


C


ATOM
578
CG2
ILE
A
77
67.128
40.757
21.337
1.00
26.59


C


ATOM
579
CD1
ILE
A
77
65.560
38.187
21.679
1.00
25.93


C


ATOM
580
N
SER
A
78
66.404
40.430
17.682
1.00
28.44


N


ATOM
581
CA
SER
A
78
65.570
41.364
16.936
1.00
28.97


C


ATOM
582
C
SER
A
78
64.167
41.354
17.512
1.00
28.83


C


ATOM
583
O
SER
A
78
63.714
40.342
18.041
1.00
28.85


O


ATOM
584
CB
SER
A
78
65.487
40.971
15.457
1.00
27.56


C


ATOM
585
OG
SER
A
78
66.716
41.168
14.790
1.00
28.48


O


ATOM
586
N
PHE
A
79
63.487
42.490
17.418
1.00
29.16


N


ATOM
587
CA
PHE
A
79
62.117
42.591
17.893
1.00
29.89


C


ATOM
588
C
PHE
A
79
61.237
42.769
16.668
1.00
30.19


C


ATOM
589
O
PHE
A
79
61.060
43.879
16.176
1.00
30.27


O


ATOM
590
CB
PHE
A
79
61.941
43.779
18.847
1.00
29.28


C


ATOM
591
CG
PHE
A
79
62.503
43.536
20.216
1.00
29.03


C


ATOM
592
CD1
PHE
A
79
63.855
43.737
20.477
1.00
30.34


C


ATOM
593
CD2
PHE
A
79
61.687
43.061
21.237
1.00
29.64


C


ATOM
594
CE1
PHE
A
79
64.387
43.467
21.741
1.00
30.52


C


ATOM
595
CE2
PHE
A
79
62.207
42.786
22.502
1.00
30.51


C


ATOM
596
CZ
PHE
A
79
63.561
42.990
22.753
1.00
29.61


C


ATOM
597
N
ILE
A
80
60.708
41.656
16.170
1.00
31.21


N


ATOM
598
CA
ILE
A
80
59.844
41.659
14.993
1.00
30.53


C


ATOM
599
C
ILE
A
80
58.766
42.728
15.137
1.00
30.49


C


ATOM
600
O
ILE
A
80
58.047
42.761
16.143
1.00
30.23


O


ATOM
601
CB
ILE
A
80
59.172
40.282
14.809
1.00
30.87


C


ATOM
602
CD1
ILE
A
80
60.240
39.187
14.721
1.00
30.68


C


ATOM
603
CG2
ILE
A
80
58.303
40.288
13.561
1.00
31.61


C


ATOM
604
CD1
ILE
A
80
61.174
39.319
13.536
1.00
30.88


C


ATOM
605
N
PHE
A
81
58.640
43.591
14.131
1.00
30.29


N


ATOM
606
CA
PHE
A
81
57.660
44.666
14.195
1.00
31.74


C


ATOM
607
C
PHE
A
81
56.216
44.205
14.385
1.00
32.15


C


ATOM
608
O
PHE
A
81
55.799
43.178
13.851
1.00
32.55


O


ATOM
609
CB
PHE
A
81
57.775
45.593
12.967
1.00
31.76


C


ATOM
610
CG
PHE
A
81
57.565
44.914
11.638
1.00
31.76


C


ATOM
611
CD1
PHE
A
81
58.575
44.152
11.055
1.00
31.23


C


ATOM
612
CD2
PHE
A
81
56.370
45.084
10.942
1.00
31.53


C


ATOM
613
CE1
PHE
A
81
58.401
43.574
9.793
1.00
31.24


C


ATOM
614
CE2
PHE
A
81
56.184
44.510
9.681
1.00
31.41


C


ATOM
615
CZ
PHE
A
81
57.202
43.755
9.106
1.00
32.04


C


ATOM
616
N
GLY
A
82
55.467
44.976
15.168
1.00
32.45


N


ATOM
617
CA
GLY
A
82
54.080
44.652
15.443
1.00
33.29


C


ATOM
618
C
GLY
A
82
53.117
45.479
14.616
1.00
34.37


C


ATOM
619
O
GLY
A
82
51.899
45.351
14.761
1.00
34.23


O


ATOM
620
N
SER
A
83
53.661
46.335
13.756
1.00
34.06


N


ATOM
621
CA
SER
A
83
52.844
47.173
12.886
1.00
34.88


C


ATOM
622
C
SER
A
83
52.470
46.370
11.645
1.00
35.53


C


ATOM
623
O
SER
A
83
52.775
46.745
10.513
1.00
34.34


O


ATOM
624
CB
SER
A
83
53.607
48.440
12.491
1.00
34.13


C


ATOM
625
OG
SER
A
83
54.875
48.115
11.961
1.00
35.16


O


ATOM
626
N
GLN
A
84
51.823
45.238
11.893
1.00
36.05


N


ATOM
627
CA
GLN
A
84
51.359
44.337
10.851
1.00
36.48


C


ATOM
628
C
GLN
A
84
50.308
43.459
11.520
1.00
36.44


C


ATOM
629
O
GLN
A
84
50.125
43.532
12.737
1.00
35.78


O


ATOM
630
CB
GLN
A
84
52.515
43.488
10.317
1.00
36.59


C


ATOM
631
CG
GLN
A
84
53.156
42.571
11.342
1.00
37.16


C


ATOM
632
CD
GLN
A
84
54.277
41.745
10.747
1.00
37.80


C


ATOM
633
OE1
GLN
A
84
54.114
41.137
9.689
1.00
38.49


O


ATOM
634
NE2
GLN
A
84
55.422
41.710
11.428
1.00
36.72


N


ATOM
635
N
SER
A
85
49.617
42.634
10.742
1.00
37.40


N


ATOM
636
CA
SER
A
85
48.582
41.775
11.307
1.00
37.95


C


ATOM
637
C
SER
A
85
49.166
40.812
12.333
1.00
38.81


C


ATOM
638
O
SER
A
85
50.351
40.479
12.283
1.00
39.00


O


ATOM
639
CB
SER
A
85
47.886
40.974
10.205
1.00
37.33


C


ATOM
640
OG
SER
A
85
48.700
39.902
9.768
1.00
38.10


O


ATOM
641
N
ILE
A
86
48.325
40.372
13.262
1.00
38.89


N


ATOM
642
CA
ILE
A
86
48.742
39.439
14.301
1.00
40.23


C


ATOM
643
C
ILE
A
86
49.236
38.140
13.665
1.00
41.35


C


ATOM
644
O
ILE
A
86
50.240
37.569
14.090
1.00
41.06


O


ATOM
645
CB
ILE
A
86
47.569
39.127
15.261
1.00
40.08


C


ATOM
646
CG1
ILE
A
86
47.192
40.391
16.041
1.00
40.14


C


ATOM
647
CG2
ILE
A
86
47.945
37.992
16.203
1.00
39.43


C


ATOM
648
CD1
ILE
A
86
46.003
40.226
16.973
1.00
39.32


C


ATOM
649
N
GLU
A
87
48.525
37.687
12.638
1.00
41.92


N


ATOM
650
CA
GLU
A
87
48.877
36.460
11.932
1.00
42.93


C


ATOM
651
C
GLU
A
87
50.228
36.595
11.230
1.00
41.66


C


ATOM
652
O
GLU
A
87
51.057
35.687
11.272
1.00
41.43


O


ATOM
653
CB
GLU
A
87
47.800
36.122
10.893
1.00
45.26


C


ATOM
654
CG
GLU
A
87
46.395
35.876
11.460
1.00
48.53


C


ATOM
655
CD
GLU
A
87
45.798
37.088
12.173
1.00
50.40


C


ATOM
656
OE1
GLU
A
87
45.867
38.211
11.625
1.00
50.61


O


ATOM
657
OE2
GLU
A
87
45.243
36.910
13.282
1.00
52.40


O


ATOM
658
N
SER
A
88
50.439
37.736
10.585
1.00
40.93


N


ATOM
659
CA
SER
A
88
51.677
37.993
9.857
1.00
41.02


C


ATOM
660
C
SER
A
88
52.898
38.079
10.777
1.00
39.71


C


ATOM
661
O
SER
A
88
53.979
37.595
10.438
1.00
39.05


O


ATOM
662
CB
SER
A
88
51.540
39.292
9.058
1.00
41.43


C


ATOM
663
OG
SER
A
88
52.675
39.507
8.242
1.00
44.62


O


ATOM
664
N
GLN
A
89
52.726
38.701
11.938
1.00
38.95


N


ATOM
665
CA
GLN
A
89
53.827
38.837
12.886
1.00
38.02


C


ATOM
666
C
GLN
A
89
54.165
37.484
13.506
1.00
38.23


C


ATOM
667
O
GLN
A
89
55.333
37.121
13.625
1.00
38.13


O


ATOM
668
CB
GLN
A
89
53.465
39.847
13.984
1.00
36.71


C


ATOM
669
CG
GLN
A
89
54.536
40.002
15.067
1.00
34.83


C


ATOM
670
CD
GLN
A
89
54.169
41.044
16.110
1.00
33.42


C


ATOM
671
OE1
GLN
A
89
52.998
41.217
16.443
1.00
32.85


O


ATOM
672
NE2
GLN
A
89
55.175
41.732
16.644
1.00
31.51


N


ATOM
673
N
ALA
A
90
53.137
36.734
13.890
1.00
38.39


N


ATOM
674
CA
ALA
A
90
53.343
35.419
14.487
1.00
38.40


C


ATOM
675
C
ALA
A
90
54.050
34.494
13.500
1.00
38.83


C


ATOM
676
O
ALA
A
90
54.847
33.639
13.894
1.00
38.82


O


ATOM
677
CB
ALA
A
90
52.006
34.822
14.908
1.00
38.88


C


ATOM
678
N
ALA
A
91
53.762
34.670
12.215
1.00
39.13


N


ATOM
679
CA
ALA
A
91
54.383
33.849
11.186
1.00
39.02


C


ATOM
680
C
ALA
A
91
55.893
34.091
11.157
1.00
39.29


C


ATOM
681
O
ALA
A
91
56.673
33.150
11.035
1.00
38.36


O


ATOM
682
CB
ALA
A
91
53.767
34.157
9.820
1.00
39.60


C


ATOM
683
N
MET
A
92
56.306
35.351
11.272
1.00
38.81


N


ATOM
684
CA
MET
A
92
57.733
35.670
11.263
1.00
38.78


C


ATOM
685
C
MET
A
92
58.426
35.071
12.480
1.00
37.97


C


ATOM
686
O
MET
A
92
59.518
34.516
12.369
1.00
38.17


O


ATOM
687
CB
MET
A
92
57.959
37.184
11.251
1.00
38.46


C


ATOM
688
CG
MET
A
92
57.461
37.876
10.009
1.00
39.51


C


ATOM
689
SD
MET
A
92
57.978
39.598
9.950
1.00
38.93


S


ATOM
690
CE
MET
A
92
57.344
40.065
8.337
1.00
39.38


C


ATOM
691
N
VAL
A
93
57.789
35.193
13.641
1.00
37.66


N


ATOM
692
CA
VAL
A
93
58.348
34.649
14.872
1.00
37.49


C


ATOM
693
C
VAL
A
93
58.501
33.136
14.725
1.00
38.78


C


ATOM
694
O
VAL
A
93
59.547
32.572
15.042
1.00
37.88


O


ATOM
695
CB
VAL
A
93
57.434
34.951
16.082
1.00
37.04


C


ATOM
696
CG1
VAL
A
93
57.888
34.152
17.294
1.00
36.02


C


ATOM
697
CG2
VAL
A
93
57.460
36.443
16.394
1.00
36.04


C


ATOM
698
N
HIS
A
94
57.451
32.486
14.231
1.00
39.37


N


ATOM
699
CA
HIS
A
94
57.474
31.039
14.040
1.00
39.99


C


ATOM
700
C
HIS
A
94
58.616
30.632
13.110
1.00
39.10


C


ATOM
701
O
HIS
A
94
59.331
29.663
13.378
1.00
39.42


O


ATOM
702
CB
HIS
A
94
56.144
30.560
13.449
1.00
41.81


C


ATOM
703
CG
HIS
A
94
56.048
29.072
13.312
1.00
43.35


C


ATOM
704
ND1
HIS
A
94
55.746
28.244
14.372
1.00
44.55


N


ATOM
705
CD2
HIS
A
94
56.249
28.261
12.247
1.00
44.14


C


ATOM
706
CE1
HIS
A
94
55.765
26.987
13.966
1.00
44.38


C


ATOM
707
NE2
HIS
A
94
56.069
26.970
12.681
1.00
44.90


N


ATOM
708
N
ALA
A
95
58.784
31.377
12.022
1.00
38.67


N


ATOM
709
CA
ALA
A
95
59.828
31.093
11.043
1.00
38.33


C


ATOM
710
C
ALA
A
95
61.224
31.175
11.648
1.00
38.74


C


ATOM
711
O
ALA
A
95
62.107
30.393
11.299
1.00
37.70


O


ATOM
712
CB
ALA
A
95
59.717
32.055
9.866
1.00
38.60


C


ATOM
713
N
VAL
A
96
61.429
32.126
12.554
1.00
38.74


N


ATOM
714
CA
VAL
A
96
62.732
32.279
13.186
1.00
38.66


C


ATOM
715
C
VAL
A
96
62.972
31.145
14.179
1.00
38.92


C


ATOM
716
O
VAL
A
96
64.054
30.558
14.212
1.00
39.96


O


ATOM
717
CB
VAL
A
96
62.843
33.640
13.920
1.00
38.15


C


ATOM
718
CG1
VAL
A
96
64.174
33.738
14.642
1.00
37.72


C


ATOM
719
CG2
VAL
A
96
62.709
34.776
12.919
1.00
38.27


C


ATOM
720
N
LYS
A
97
61.958
30.828
14.976
1.00
39.73


N


ATOM
721
CA
LYS
A
97
62.081
29.767
15.969
1.00
40.96


C


ATOM
722
C
LYS
A
97
62.273
28.383
15.351
1.00
42.44


C


ATOM
723
O
LYS
A
97
62.860
27.502
15.977
1.00
42.21


O


ATOM
724
CB
LYS
A
97
60.856
29.750
16.892
1.00
40.24


C


ATOM
725
CG
LYS
A
97
60.659
31.021
17.716
1.00
39.72


C


ATOM
726
CD
LYS
A
97
61.884
31.343
18.578
1.00
38.30


C


ATOM
727
CE
LYS
A
97
62.148
30.271
19.627
1.00
37.68


C


ATOM
728
NZ
LYS
A
97
63.372
30.567
20.429
1.00
37.01


N


ATOM
729
N
ASN
A
98
61.783
28.187
14.129
1.00
44.02


N


ATOM
730
CA
ASN
A
98
61.917
26.886
13.474
1.00
46.56


C


ATOM
731
C
ASN
A
98
62.802
26.915
12.232
1.00
47.43


C


ATOM
732
O
ASN
A
98
62.605
26.126
11.307
1.00
47.95


O


ATOM
733
CB
ASN
A
98
60.537
26.336
13.096
1.00
47.77


C


ATOM
734
CG
ASN
A
98
59.630
26.158
14.297
1.00
49.18


C


ATOM
735
OD1
ASN
A
98
59.106
27.127
14.843
1.00
50.44


O


ATOM
736
ND2
ASN
A
98
59.447
24.912
14.721
1.00
50.23


N


ATOM
737
N
PHE
A
99
63.784
27.811
12.215
1.00
48.01


N


ATOM
738
CA
PHE
A
99
64.676
27.927
11.068
1.00
48.77


C


ATOM
739
C
PHE
A
99
65.630
26.745
10.914
1.00
49.32


C


ATOM
740
O
PHE
A
99
66.000
26.386
9.798
1.00
49.30


O


ATOM
741
CB
PHE
A
99
65.496
29.214
11.161
1.00
48.62


C


ATOM
742
CG
PHE
A
99
66.281
29.521
9.916
1.00
48.84


C


ATOM
743
CD1
PHE
A
99
65.631
29.895
8.745
1.00
48.95


C


ATOM
744
CD2
PHE
A
99
67.669
29.439
9.914
1.00
49.12


C


ATOM
745
CE1
PHE
A
99
66.353
30.184
7.590
1.00
49.40


C


ATOM
746
CE2
PHE
A
99
68.399
29.726
8.765
1.00
48.92


C


ATOM
747
CZ
PHE
A
99
67.741
30.100
7.602
1.00
49.64


C


ATOM
748
N
LYS
A
100
66.032
26.147
12.031
1.00
49.95


N


ATOM
749
CA
LYS
A
100
66.957
25.017
11.992
1.00
51.02


C


ATOM
750
C
LYS
A
100
66.268
23.675
11.766
1.00
51.54


C


ATOM
751
O
LYS
A
100
66.911
22.628
11.824
1.00
51.71


O


ATOM
752
CB
LYS
A
100
67.771
24.953
13.287
1.00
51.20


C


ATOM
753
CG
LYS
A
100
68.664
26.160
13.528
1.00
51.10


C


ATOM
754
CD
LYS
A
100
69.464
25.986
14.808
1.00
51.19


C


ATOM
755
CE
LYS
A
100
70.428
27.136
15.032
1.00
50.48


C


ATOM
756
NZ
LYS
A
100
71.198
26.947
16.290
1.00
50.06


N


ATOM
757
N
ALA
A
101
64.965
23.708
11.508
1.00
52.15


N


ATOM
758
CA
ALA
A
101
64.201
22.486
11.272
1.00
52.52


C


ATOM
759
C
ALA
A
101
64.673
21.777
10.003
1.00
52.76


C


ATOM
760
O
ALA
A
101
64.913
22.413
8.975
1.00
52.56


O


ATOM
761
CB
ALA
A
101
62.717
22.811
11.168
1.00
52.86


C


ATOM
762
N
HIS
A
222
79.141
30.211
17.140
1.00
53.16


N


ATOM
763
CA
HIS
A
222
79.966
30.550
18.294
1.00
53.11


C


ATOM
764
C
HIS
A
222
79.233
31.452
19.280
1.00
51.53


C


ATOM
765
O
HIS
A
222
79.099
31.117
20.458
1.00
51.93


O


ATOM
766
CB
HIS
A
222
81.257
31.242
17.844
1.00
55.36


C


ATOM
767
CG
HIS
A
222
82.390
30.299
17.582
1.00
57.46


C


ATOM
768
ND1
HIS
A
222
82.940
29.508
18.568
1.00
58.71


N


ATOM
769
CD2
HIS
A
222
83.087
30.032
16.452
1.00
58.36


C


ATOM
770
CE1
HIS
A
222
83.928
28.794
18.056
1.00
59.17


C


ATOM
771
NE2
HIS
A
222
84.038
29.093
16.774
1.00
59.10


N


ATOM
772
N
ASN
A
223
78.766
32.597
18.799
1.00
49.32


N


ATOM
773
CA
ASN
A
223
78.056
33.540
19.653
1.00
47.79


C


ATOM
774
C
ASN
A
223
76.565
33.582
19.357
1.00
45.63


C


ATOM
775
O
ASN
A
223
75.905
34.587
19.624
1.00
44.59


O


ATOM
776
CB
ASN
A
223
78.643
34.945
19.496
1.00
49.26


C


ATOM
777
CG
ASN
A
223
80.075
35.035
19.981
1.00
50.67


C


ATOM
778
OD1
ASN
A
223
80.360
34.793
21.154
1.00
51.68


O


ATOM
779
ND2
ASN
A
223
80.986
35.387
19.079
1.00
52.28


N


ATOM
780
N
GLU
A
224
76.029
32.498
18.807
1.00
43.13


N


ATOM
781
CA
GLU
A
224
74.606
32.467
18.503
1.00
41.15


C


ATOM
782
C
GLU
A
224
73.799
32.540
19.786
1.00
38.97


C


ATOM
783
O
GLU
A
224
74.153
31.927
20.792
1.00
38.56


O


ATOM
784
CB
GLU
A
224
74.227
31.193
17.739
1.00
42.39


C


ATOM
785
CG
GLU
A
224
74.553
29.893
18.462
1.00
44.37


C


ATOM
786
CD
GLU
A
224
73.820
28.693
17.876
1.00
45.22


C


ATOM
787
OE1
GLU
A
224
73.539
28.698
16.658
1.00
45.16


O


ATOM
788
OE2
GLU
A
224
73.535
27.741
18.632
1.00
45.27


O


ATOM
789
N
LEU
A
225
72.718
33.309
19.747
1.00
37.03


N


ATOM
790
CA
LEU
A
225
71.842
33.454
20.897
1.00
36.33


C


ATOM
791
C
LEU
A
225
70.674
32.500
20.682
1.00
36.34


C


ATOM
792
O
LEU
A
225
69.849
32.710
19.792
1.00
34.87


O


ATOM
793
CB
LEU
A
225
71.333
34.891
20.999
1.00
35.11


C


ATOM
794
CG
LEU
A
225
70.432
35.181
22.200
1.00
34.22


C


ATOM
795
CD1
LEU
A
225
71.185
34.882
23.490
1.00
34.98


C


ATOM
796
CD2
LEU
A
225
69.981
36.633
22.161
1.00
33.29


C


ATOM
797
N
VAL
A
226
70.608
31.453
21.500
1.00
36.84


N


ATOM
798
CA
VAL
A
226
69.557
30.450
21.369
1.00
37.69


C


ATOM
799
C
VAL
A
226
68.924
30.035
22.693
1.00
38.39


C


ATOM
800
O
VAL
A
226
69.410
30.390
23.769
1.00
38.54


O


ATOM
801
CB
VAL
A
226
70.108
29.174
20.702
1.00
37.69


C


ATOM
802
CG1
VAL
A
226
70.616
29.486
19.306
1.00
36.12


C


ATOM
803
CG2
VAL
A
226
71.221
28.589
21.560
1.00
38.03


C


ATOM
804
N
ASP
A
227
67.832
29.280
22.600
1.00
39.17


N


ATOM
805
CA
ASP
A
227
67.143
28.782
23.780
1.00
39.84


C


ATOM
806
C
ASP
A
227
67.697
27.398
24.129
1.00
41.46


C


ATOM
807
O
ASP
A
227
68.671
26.944
23.526
1.00
41.37


O


ATOM
808
CB
ASP
A
227
65.625
28.702
23.543
1.00
39.27


C


ATOM
809
CG
ASP
A
227
65.253
27.900
22.299
1.00
38.93


C


ATOM
810
OD1
ASP
A
227
65.938
26.903
21.987
1.00
38.27


O


ATOM
811
OD2
ASP
A
227
64.253
28.259
21.639
1.00
38.73


O


ATOM
812
N
SER
A
228
67.073
26.733
25.096
1.00
42.85


N


ATOM
813
CA
SER
A
228
67.510
25.408
25.535
1.00
44.79


C


ATOM
814
C
SER
A
228
67.415
24.358
24.428
1.00
45.78


C


ATOM
815
O
SER
A
228
68.052
23.305
24.502
1.00
46.20


O


ATOM
816
CB
SER
A
228
66.680
24.961
26.740
1.00
44.77


C


ATOM
817
OG
SER
A
228
65.301
24.915
26.413
1.00
45.35


O


ATOM
818
N
GLN
A
229
66.618
24.653
23.405
1.00
46.62


N


ATOM
819
CA
GLN
A
229
66.433
23.748
22.278
1.00
47.22


C


ATOM
820
C
GLN
A
229
67.327
24.128
21.102
1.00
46.93


C


ATOM
821
O
GLN
A
229
67.181
23.595
20.000
1.00
46.64


O


ATOM
822
CB
GLN
A
229
64.967
23.756
21.841
1.00
48.67


C


ATOM
823
CG
GLN
A
229
64.029
23.082
22.828
1.00
51.08


C


ATOM
824
CD
GLN
A
229
62.568
23.334
22.512
1.00
52.25


C


ATOM
825
OE1
GLN
A
229
62.036
24.405
22.800
1.00
53.70


O


ATOM
826
NE2
GLN
A
229
61.913
22.349
21.907
1.00
53.63


N


ATOM
827
N
LYS
A
230
68.249
25.055
21.346
1.00
46.17


N


ATOM
828
CA
LYS
A
230
69.188
25.512
20.324
1.00
45.18


C


ATOM
829
C
LYS
A
230
68.553
26.317
19.195
1.00
43.43


C


ATOM
830
O
LYS
A
230
69.146
26.471
18.126
1.00
44.02


O


ATOM
831
CB
LYS
A
230
69.950
24.318
19.742
1.00
46.95


C


ATOM
832
CG
LYS
A
230
70.781
23.563
20.771
1.00
48.94


C


ATOM
833
CD
LYS
A
230
71.905
24.431
21.332
1.00
51.11


C


ATOM
834
CB
LYS
A
230
72.929
24.788
20.257
1.00
52.17


C


ATOM
835
NZ
LYS
A
230
74.049
25.620
20.790
1.00
53.38


N


ATOM
836
N
ARG
A
231
67.353
26.836
19.429
1.00
41.91


N


ATOM
837
CA
ARG
A
231
66.671
27.648
18.424
1.00
40.32


C


ATOM
838
C
ARG
A
231
66.997
29.116
18.691
1.00
38.38


C


ATOM
839
O
ARG
A
231
67.125
29.528
19.843
1.00
36.84


O


ATOM
840
CB
ARG
A
231
65.159
27.435
18.504
1.00
42.41


C


ATOM
841
CG
ARG
A
231
64.729
25.994
18.290
1.00
45.13


C


ATOM
842
CD
ARG
A
231
63.663
25.608
19.290
1.00
47.63


C


ATOM
843
NE
ARG
A
231
62.397
26.291
19.050
1.00
50.64


N


ATOM
844
CZ
ARG
A
231
61.549
26.636
20.013
1.00
51.82


C


ATOM
845
NH1
ARG
A
231
61.842
26.371
21.277
1.00
53.05


N


ATOM
846
NH2
ARG
A
231
60.401
27.230
19.712
1.00
52.91


N


ATOM
847
N
TYR
A
232
67.140
29.896
17.627
1.00
36.74


N


ATOM
848
CA
TYR
A
232
67.451
31.313
17.763
1.00
35.61


C


ATOM
849
C
TYR
A
232
66.388
32.035
18.579
1.00
34.70


C


ATOM
850
O
TYR
A
232
65.193
31.755
18.453
1.00
33.91


O


ATOM
851
CB
TYR
A
232
67.538
31.976
16.390
1.00
36.14


C


ATOM
852
CG
TYR
A
232
68.648
31.455
15.517
1.00
37.40


C


ATOM
853
CD1
TYR
A
232
69.973
31.464
15.955
1.00
37.55


C


ATOM
854
CD2
TYR
A
232
68.377
30.966
14.241
1.00
38.07


C


ATOM
855
CE1
TYR
A
232
71.003
30.996
15.136
1.00
39.02


C


ATOM
856
CE2
TYR
A
232
69.396
30.498
13.419
1.00
39.05


C


ATOM
857
CZ
TYR
A
232
70.703
30.516
13.870
1.00
39.19


C


ATOM
858
OH
TYR
A
232
71.704
30.060
13.045
1.00
40.49


O


ATOM
859
N
LEU
A
233
66.823
32.964
19.420
1.00
33.09


N


ATOM
860
CA
LEU
A
233
65.877
33.726
20.214
1.00
32.70


C


ATOM
861
C
LEU
A
233
65.359
34.854
19.338
1.00
31.76


C


ATOM
862
O
LEU
A
233
66.051
35.321
18.431
1.00
32.09


O


ATOM
863
CB
LEU
A
233
66.541
34.310
21.467
1.00
32.69


C


ATOM
864
CG
LEU
A
233
67.114
33.357
22.522
1.00
33.44


C


ATOM
865
CD1
LEU
A
233
67.532
34.178
23.738
1.00
33.23


C


ATOM
866
CD2
LEU
A
233
66.084
32.316
22.936
1.00
33.22


C


ATOM
867
N
VAL
A
234
64.132
35.281
19.598
1.00
32.10


N


ATOM
868
CA
VAL
A
234
63.539
36.365
18.839
1.00
31.38


C


ATOM
869
C
VAL
A
234
62.535
37.088
19.723
1.00
30.84


C


ATOM
870
O
VAL
A
234
61.919
36.487
20.601
1.00
30.80


O


ATOM
871
CB
VAL
A
234
62.832
35.845
17.560
1.00
31.94


C


ATOM
872
CG1
VAL
A
234
61.608
35.011
17.930
1.00
31.25


C


ATOM
873
CG2
VAL
A
234
62.448
37.013
16.672
1.00
30.99


C


ATOM
874
N
GLY
A
235
62.400
38.391
19.508
1.00
30.91


N


ATOM
875
CA
GLY
A
235
61.456
39.164
20.286
1.00
30.22


C


ATOM
876
C
GLY
A
235
60.382
39.673
19.349
1.00
29.78


C


ATOM
877
O
GLY
A
235
60.501
39.517
18.136
1.00
29.75


O


ATOM
878
N
ALA
A
236
59.336
40.276
19.904
1.00
29.91


N


ATOM
879
CA
ALA
A
236
58.255
40.811
19.093
1.00
29.86


C


ATOM
880
C
ALA
A
236
57.639
42.027
19.774
1.00
29.27


C


ATOM
881
O
ALA
A
236
57.439
42.037
20.986
1.00
29.23


O


ATOM
882
CB
ALA
A
236
57.192
39.741
18.868
1.00
30.79


C


ATOM
883
N
GLY
A
237
57.345
43.054
18.987
1.00
29.87


N


ATOM
884
CA
GLY
A
237
56.745
44.249
19.544
1.00
29.77


C


ATOM
885
C
GLY
A
237
55.242
44.109
19.649
1.00
30.45


C


ATOM
886
O
GLY
A
237
54.626
43.420
18.839
1.00
30.39


O


ATOM
887
N
ILE
A
238
54.650
44.744
20.656
1.00
29.85


N


ATOM
888
CA
ILE
A
238
53.206
44.703
20.835
1.00
30.46


C


ATOM
889
C
ILE
A
238
52.708
46.115
21.130
1.00
31.10


C


ATOM
890
O
ILE
A
238
53.493
47.003
21.470
1.00
30.41


O


ATOM
891
CB
ILE
A
238
52.788
43.767
22.001
1.00
29.94


C


ATOM
892
CG1
ILE
A
238
53.310
44.313
23.333
1.00
30.64


C


ATOM
893
CG2
ILE
A
238
53.322
42.357
21.758
1.00
29.80


C


ATOM
894
CD1
ILE
A
238
52.808
43.550
24.556
1.00
31.03


C


ATOM
895
N
ASN
A
239
51.406
46.328
20.980
1.00
31.30


N


ATOM
896
CA
ASN
A
239
50.825
47.632
21.249
1.00
30.86


C


ATOM
897
C
ASN
A
239
49.859
47.518
22.419
1.00
31.81


C


ATOM
898
O
ASN
A
239
49.535
46.416
22.862
1.00
30.42


O


ATOM
899
CB
ASN
A
239
50.108
48.171
20.006
1.00
31.76


C


ATOM
900
CG
ASN
A
239
49.028
47.231
19.495
1.00
31.45


C


ATOM
901
OD1
ASN
A
239
48.019
47.004
20.160
1.00
32.62


O


ATOM
902
ND2
ASN
A
239
49.240
46.678
18.309
1.00
32.41


N


ATOM
903
N
THR
A
240
49.406
48.660
22.921
1.00
32.10


N


ATOM
904
CA
THR
A
240
48.494
48.686
24.054
1.00
32.56


C


ATOM
905
C
THR
A
240
47.025
48.523
23.648
1.00
34.33


C


ATOM
906
O
THR
A
240
46.130
48.681
24.477
1.00
33.93


O


ATOM
907
CB
THR
A
240
48.653
50.004
24.831
1.00
32.45


C


ATOM
908
OG1
THR
A
240
48.432
51.107
23.941
1.00
31.46


O


ATOM
909
CG2
THR
A
240
50.065
50.112
25.418
1.00
31.19


C


ATOM
910
N
ARG
A
241
46.787
48.179
22.385
1.00
35.96


N


ATOM
911
CA
ARG
A
241
45.426
48.032
21.873
1.00
39.04


C


ATOM
912
C
ARG
A
241
44.919
46.596
21.719
1.00
39.35


C


ATOM
913
O
ARG
A
241
43.981
46.188
22.406
1.00
40.01


O


ATOM
914
CB
ARG
A
241
45.313
48.743
20.522
1.00
41.18


C


ATOM
915
CG
ARG
A
241
45.852
50.167
20.516
1.00
45.22


C


ATOM
916
CD
ARG
A
241
44.809
51.195
20.920
1.00
48.22


C


ATOM
917
NE
ARG
A
241
43.702
51.247
19.968
1.00
50.77


N


ATOM
918
CZ
ARG
A
241
42.962
52.329
19.735
1.00
52.50


C


ATOM
919
NH1
ARG
A
241
43.211
53.461
20.383
1.00
52.88


N


ATOM
920
NH2
ARG
A
241
41.971
52.279
18.853
1.00
52.52


N


ATOM
921
N
ASP
A
242
45.532
45.836
20.816
1.00
39.54


N


ATOM
922
CA
ASP
A
242
45.105
44.459
20.557
1.00
40.21


C


ATOM
923
C
ASP
A
242
45.938
43.371
21.230
1.00
39.85


C


ATOM
924
O
ASP
A
242
46.016
42.253
20.723
1.00
40.56


O


ATOM
925
CB
ASP
A
242
45.087
44.192
19.045
1.00
40.36


C


ATOM
926
CG
ASP
A
242
46.461
44.345
18.399
1.00
40.93


C


ATOM
927
OD1
ASP
A
242
47.480
44.013
19.045
1.00
41.17


O


ATOM
928
OD2
ASP
A
242
46.526
44.781
17.230
1.00
41.45


O


ATOM
929
N
PHE
A
243
46.537
43.681
22.373
1.00
39.48


N


ATOM
930
CA
PHE
A
243
47.381
42.712
23.066
1.00
39.13


C


ATOM
931
C
PHE
A
243
46.677
41.442
23.547
1.00
39.39


C


ATOM
932
O
PHE
A
243
47.293
40.380
23.604
1.00
38.77


O


ATOM
933
CB
PHE
A
243
48.108
43.392
24.235
1.00
37.88


C


ATOM
934
CG
PHE
A
243
47.198
43.915
25.305
1.00
37.59


C


ATOM
935
CD1
PHE
A
243
46.746
43.082
26.323
1.00
37.35


C


ATOM
936
CD2
PHE
A
243
46.797
45.248
25.301
1.00
37.10


C


ATOM
937
CE1
PHE
A
243
45.908
43.569
27.326
1.00
37.14


C


ATOM
938
CE2
PHE
A
243
45.959
45.744
26.299
1.00
37.25


C


ATOM
939
CZ
PHE
A
243
45.515
44.901
27.313
1.00
37.29


C


ATOM
940
N
ARG
A
244
45.395
41.543
23.887
1.00
40.11


N


ATOM
941
CA
ARG
A
244
44.653
40.375
24.354
1.00
40.93


C


ATOM
942
C
ARG
A
244
44.619
39.281
23.289
1.00
40.69


C


ATOM
943
O
ARG
A
244
44.502
38.099
23.609
1.00
41.20


O


ATOM
944
CB
ARG
A
244
43.229
40.773
24.760
1.00
41.45


C


ATOM
945
CG
ARG
A
244
43.188
41.719
25.952
1.00
42.10


C


ATOM
946
CD
ARG
A
244
41.766
42.050
26.382
1.00
43.32


C


ATOM
947
NE
ARG
A
244
41.749
43.039
27.456
1.00
44.43


N


ATOM
948
CZ
ARG
A
244
42.035
44.328
27.291
1.00
45.14


C


ATOM
949
NH1
ARG
A
244
42.357
44.793
26.090
1.00
44.75


N


ATOM
950
NH2
ARG
A
244
42.010
45.153
28.329
1.00
45.44


N


ATOM
951
N
GLU
A
245
44.726
39.677
22.026
1.00
40.84


N


ATOM
952
CA
GLU
A
245
44.732
38.718
20.928
1.00
40.87


C


ATOM
953
C
GLU
A
245
46.147
38.501
20.393
1.00
40.07


C


ATOM
954
O
GLU
A
245
46.537
37.374
20.083
1.00
39.45


O


ATOM
955
CB
GLU
A
245
43.838
39.197
19.781
1.00
43.54


C


ATOM
956
CG
GLU
A
245
42.334
39.160
20.061
1.00
47.70


C


ATOM
957
CD
GLU
A
245
41.900
40.111
21.164
1.00
50.68


C


ATOM
958
OE1
GLU
A
245
42.282
41.305
21.121
1.00
52.80


O


ATOM
959
OE2
GLU
A
245
41.162
39.665
22.072
1.00
52.45


O


ATOM
960
N
ARG
A
246
46.915
39.581
20.291
1.00
38.14


N


ATOM
961
CA
ARG
A
246
48.277
39.501
19.764
1.00
36.50


C


ATOM
962
C
ARG
A
246
49.259
38.743
20.660
1.00
36.05


C


ATOM
963
O
ARG
A
246
50.051
37.943
20.170
1.00
36.35


O


ATOM
964
CB
ARG
A
246
48.814
40.913
19.489
1.00
35.90


C


ATOM
965
CG
ARG
A
246
50.130
40.945
18.713
1.00
35.45


C


ATOM
966
CD
ARG
A
246
50.611
42.375
18.505
1.00
34.86


C


ATOM
967
NE
ARG
A
246
49.743
43.147
17.619
1.00
34.95


N


ATOM
968
CZ
ARG
A
246
49.766
43.077
16.291
1.00
34.35


C


ATOM
969
NH1
ARG
A
246
50.616
42.267
15.676
1.00
35.15


N


ATOM
970
NH2
ARG
A
246
48.939
43.827
15.574
1.00
35.50


N


ATOM
971
N
VAL
A
247
49.212
38.986
21.967
1.00
35.97


N


ATOM
972
CA
VAL
A
247
50.129
38.315
22.886
1.00
36.75


C


ATOM
973
C
VAL
A
247
50.020
36.788
22.837
1.00
37.56


C


ATOM
974
O
VAL
A
247
51.033
36.096
22.706
1.00
37.16


O


ATOM
975
CB
VAL
A
247
49.927
38.806
24.340
1.00
36.31


C


ATOM
976
CG1
VAL
A
247
50.775
37.987
25.296
1.00
35.75


C


ATOM
977
CG2
VAL
A
247
50.314
40.282
24.444
1.00
36.50


C


ATOM
978
N
PRO
A
248
48.794
36.241
22.946
1.00
37.33


N


ATOM
979
CA
PRO
A
248
48.638
34.783
22.901
1.00
36.95


C


ATOM
980
C
PRO
A
248
49.231
34.184
21.629
1.00
36.36


C


ATOM
981
O
PRO
A
248
49.897
33.155
21.677
1.00
37.14


O


ATOM
982
CB
PRO
A
248
47.125
34.598
22.979
1.00
37.52


C


ATOM
983
CG
PRO
A
248
46.709
35.735
23.858
1.00
37.69


C


ATOM
984
CD
PRO
A
248
47.515
36.890
23.290
1.00
36.69


C


ATOM
985
N
ALA
A
249
48.997
34.840
20.497
1.00
35.60


N


ATOM
986
CA
ALA
A
249
49.507
34.367
19.217
1.00
35.36


C


ATOM
987
C
ALA
A
249
51.034
34.354
19.183
1.00
35.63


C


ATOM
988
O
ALA
A
249
51.646
33.411
18.669
1.00
33.65


O


ATOM
989
CB
ALA
A
249
48.968
35.236
18.090
1.00
36.03


C


ATOM
990
N
LEU
A
250
51.646
35.403
19.728
1.00
35.24


N


ATOM
991
CA
LEU
A
250
53.099
35.505
19.754
1.00
35.85


C


ATOM
992
C
LEU
A
250
53.701
34.458
20.681
1.00
36.48


C


ATOM
993
O
LEU
A
250
54.758
33.899
20.395
1.00
36.97


O


ATOM
994
CB
LEU
A
250
53.520
36.915
20.189
1.00
34.62


C


ATOM
995
CG
LEU
A
250
53.067
38.010
19.215
1.00
34.74


C


ATOM
996
CD1
LEU
A
250
53.473
39.384
19.731
1.00
34.92


C


ATOM
997
CD2
LEU
A
250
53.678
37.749
17.847
1.00
34.43


C


ATOM
998
N
VAL
A
251
53.025
34.191
21.790
1.00
38.25


N


ATOM
999
CA
VAL
A
251
53.501
33.193
22.738
1.00
40.28


C


ATOM
1000
C
VAL
A
251
53.471
31.810
22.087
1.00
41.33


C


ATOM
1001
O
VAL
A
251
54.447
31.062
22.159
1.00
41.27


O


ATOM
1002
CB
VAL
A
251
52.632
33.173
24.013
1.00
40.67


C


ATOM
1003
CG1
VAL
A
251
53.018
31.986
24.895
1.00
42.14


C


ATOM
1004
CG2
VAL
A
251
52.813
34.474
24.780
1.00
40.95


C


ATOM
1005
N
GLU
A
252
52.355
31.480
21.439
1.00
41.97


N


ATOM
1006
CA
GLU
A
252
52.217
30.182
20.783
1.00
43.27


C


ATOM
1007
C
GLU
A
252
53.252
30.030
19.679
1.00
42.06


C


ATOM
1008
O
GLU
A
252
53.804
28.949
19.484
1.00
42.29


O


ATOM
1009
CB
GLU
A
252
50.822
30.019
20.172
1.00
45.54


C


ATOM
1010
CG
GLU
A
252
49.688
30.558
21.016
1.00
49.93


C


ATOM
1011
CD
GLU
A
252
49.586
29.929
22.392
1.00
52.52


C


ATOM
1012
OE1
GLU
A
252
48.789
30.449
23.201
1.00
54.25


O


ATOM
1013
OE2
GLU
A
252
50.280
28.924
22.670
1.00
55.02


O


ATOM
1014
N
ALA
A
253
53.503
31.116
18.953
1.00
40.26


N


ATOM
1015
CA
ALA
A
253
54.472
31.103
17.865
1.00
38.87


C


ATOM
1016
C
ALA
A
253
55.889
30.880
18.390
1.00
38.28


C


ATOM
1017
O
ALA
A
253
56.788
30.523
17.628
1.00
38.29


O


ATOM
1018
CB
ALA
A
253
54.398
32.406
17.082
1.00
39.08


C


ATOM
1019
N
GLY
A
254
56.088
31.103
19.686
1.00
37.14


N


ATOM
1020
CA
GLY
A
254
57.399
30.885
20.275
1.00
36.67


C


ATOM
1021
C
GLY
A
254
58.226
32.111
20.631
1.00
35.76


C


ATOM
1022
O
GLY
A
254
59.433
31.995
20.845
1.00
35.05


O


ATOM
1023
N
ALA
A
255
57.596
33.282
20.701
1.00
35.10


N


ATOM
1024
CA
ALA
A
255
58.321
34.502
21.045
1.00
34.05


C


ATOM
1025
C
ALA
A
255
59.011
34.342
22.399
1.00
33.03


C


ATOM
1026
O
ALA
A
255
58.402
33.902
23.372
1.00
32.76


O


ATOM
1027
CB
ALA
A
255
57.369
35.692
21.078
1.00
34.00


C


ATOM
1028
N
ASP
A
256
60.285
34.710
22.454
1.00
32.35


N


ATOM
1029
CA
ASP
A
256
61.061
34.601
23.682
1.00
32.05


C


ATOM
1030
C
ASP
A
256
60.886
35.807
24.597
1.00
31.18


C


ATOM
1031
O
ASP
A
256
61.004
35.699
25.817
1.00
30.47


O


ATOM
1032
CB
ASP
A
256
62.531
34.409
23.329
1.00
32.35


C


ATOM
1033
CG
ASP
A
256
62.770
33.118
22.575
1.00
34.08


C


ATOM
1034
OD1
ASP
A
256
62.639
32.044
23.199
1.00
34.90


O


ATOM
1035
OD2
ASP
A
256
63.068
33.172
21.365
1.00
33.17


O


ATOM
1036
N
VAL
A
257
60.602
36.957
24.002
1.00
30.50


N


ATOM
1037
CA
VAL
A
257
60.402
38.173
24.778
1.00
29.68


C


ATOM
1038
C
VAL
A
257
59.555
39.139
23.961
1.00
29.30


C


ATOM
1039
O
VAL
A
257
59.584
39.111
22.733
1.00
29.73


O


ATOM
1040
CB
VAL
A
257
61.756
38.844
25.125
1.00
29.48


C


ATOM
1041
CG1
VAL
A
257
62.462
39.273
23.848
1.00
29.83


C


ATOM
1042
CG2
VAL
A
257
61.531
40.040
26.044
1.00
29.61


C


ATOM
1043
N
LEU
A
258
58.800
39.982
24.654
1.00
28.19


N


ATOM
1044
CA
LEU
A
258
57.942
40.961
24.007
1.00
28.90


C


ATOM
1045
C
LEU
A
258
58.369
42.354
24.457
1.00
28.21


C


ATOM
1046
O
LEU
A
258
59.113
42.503
25.419
1.00
28.37


O


ATOM
1047
CB
LEU
A
258
56.485
40.746
24.425
1.00
27.71


C


ATOM
1048
CG
LEU
A
258
55.915
39.332
24.289
1.00
28.73


C


ATOM
1049
CD1
LEU
A
258
54.508
39.297
24.871
1.00
30.02


C


ATOM
1050
CD2
LEU
A
258
55.907
38.917
22.833
1.00
29.49


C


ATOM
1051
N
CYS
A
259
57.898
43.373
23.754
1.00
28.75


N


ATOM
1052
CA
CYS
A
259
58.206
44.743
24.142
1.00
28.59


C


ATOM
1053
C
CYS
A
259
57.122
45.669
23.617
1.00
28.15


C


ATOM
1054
O
CYS
A
259
56.827
45.670
22.423
1.00
28.23


O


ATOM
1055
CB
CYS
A
259
59.566
45.181
23.597
1.00
28.11


C


ATOM
1056
SG
CYS
A
259
60.079
46.808
24.215
1.00
29.44


S


ATOM
1057
N
ILE
A
260
56.525
46.443
24.518
1.00
28.54


N


ATOM
1058
CA
ILE
A
260
55.490
47.392
24.132
1.00
29.64


C


ATOM
1059
C
ILE
A
260
56.191
48.503
23.362
1.00
30.85


C


ATOM
1060
O
ILE
A
260
57.144
49.106
23.852
1.00
30.69


O


ATOM
1061
CB
ILE
A
260
54.786
47.985
25.361
1.00
29.60


C


ATOM
1062
CG1
ILE
A
260
54.254
46.849
26.238
1.00
29.82


C


ATOM
1063
CG2
ILE
A
260
53.638
48.901
24.916
1.00
29.89


C


ATOM
1064
CD1
ILE
A
260
53.659
47.309
27.557
1.00
30.44


C


ATOM
1065
N
ASP
A
261
55.702
48.760
22.156
1.00
31.00


N


ATOM
1066
CA
ASP
A
261
56.266
49.756
21.257
1.00
32.38


C


ATOM
1067
C
ASP
A
261
55.498
51.081
21.316
1.00
32.90


C


ATOM
1068
O
ASP
A
261
54.361
51.162
20.859
1.00
32.73


O


ATOM
1069
CB
ASP
A
261
56.252
49.151
19.846
1.00
33.58


C


ATOM
1070
CG
ASP
A
261
56.773
50.088
18.783
1.00
35.13


C


ATOM
1071
OD1
ASP
A
261
57.544
51.012
19.104
1.00
35.01


O


ATOM
1072
OD2
ASP
A
261
56.415
49.874
17.604
1.00
35.63


O


ATOM
1073
N
SER
A
262
56.121
52.112
21.888
1.00
32.69


N


ATOM
1074
CA
SER
A
262
55.483
53.427
22.013
1.00
32.90


C


ATOM
1075
C
SER
A
262
56.502
54.557
22.175
1.00
32.98


C


ATOM
1076
O
SER
A
262
57.598
54.339
22.686
1.00
32.40


O


ATOM
1077
CB
SER
A
262
54.529
53.423
23.213
1.00
33.69


C


ATOM
1078
OG
SER
A
262
54.010
54.716
23.469
1.00
35.09


O


ATOM
1079
N
SER
A
263
56.142
55.766
21.745
1.00
32.80


N


ATOM
1080
CA
SER
A
263
57.048
56.906
21.872
1.00
33.15


C


ATOM
1081
C
SER
A
263
56.985
57.508
23.276
1.00
33.32


C


ATOM
1082
O
SER
A
263
57.932
58.151
23.722
1.00
35.72


O


ATOM
1083
CB
SER
A
263
56.734
57.976
20.816
1.00
34.60


C


ATOM
1084
OG
SER
A
263
55.370
58.352
20.845
1.00
37.69


O


ATOM
1085
N
ASP
A
264
55.871
57.296
23.971
1.00
31.32


N


ATOM
1086
CA
ASP
A
264
55.711
57.795
25.337
1.00
29.82


C


ATOM
1087
C
ASP
A
264
55.158
56.664
26.203
1.00
29.45


C


ATOM
1088
O
ASP
A
264
53.942
56.475
26.304
1.00
28.91


O


ATOM
1089
CB
ASP
A
264
54.775
59.017
25.356
1.00
28.89


C


ATOM
1090
CG
ASP
A
264
54.352
59.436
26.769
1.00
29.68


C


ATOM
1091
OD1
ASP
A
264
55.007
59.067
27.768
1.00
26.79


O


ATOM
1092
OD2
ASP
A
264
53.348
60.168
26.877
1.00
29.53


O


ATOM
1093
N
GLY
A
265
56.071
55.914
26.815
1.00
27.82


N


ATOM
1094
CA
GLY
A
265
55.692
54.796
27.662
1.00
27.73


C


ATOM
1095
C
GLY
A
265
55.189
55.151
29.048
1.00
27.21


C


ATOM
1096
O
GLY
A
265
54.751
54.269
29.784
1.00
27.06


O


ATOM
1097
N
PHE
A
266
55.244
56.430
29.412
1.00
26.33


N


ATOM
1098
CA
PHE
A
266
54.779
56.870
30.726
1.00
26.29


C


ATOM
1099
C
PHE
A
266
53.265
56.989
30.574
1.00
27.35


C


ATOM
1100
O
PHE
A
266
52.707
58.086
30.516
1.00
26.16


O


ATOM
1101
CB
PHE
A
266
55.403
58.222
31.071
1.00
26.18


C


ATOM
1102
CG
PHE
A
266
55.499
58.503
32.553
1.00
27.83


C


ATOM
1103
CD1
PHE
A
266
54.770
57.754
33.481
1.00
26.01


C


ATOM
1104
CD2
PHE
A
266
56.305
59.541
33.017
1.00
26.81


C


ATOM
1105
CE1
PHE
A
266
54.846
58.040
34.843
1.00
27.31


C


ATOM
1106
CE2
PHE
A
266
56.385
59.833
34.373
1.00
27.03


C


ATOM
1107
CZ
PHE
A
266
55.654
59.081
35.291
1.00
27.65


C


ATOM
1108
N
SER
A
267
52.613
55.832
30.502
1.00
28.62


N


ATOM
1109
CA
SER
A
267
51.176
55.751
30.282
1.00
29.12


C


ATOM
1110
C
SER
A
267
50.490
54.634
31.061
1.00
29.52


C


ATOM
1111
O
SER
A
267
51.036
53.543
31.231
1.00
27.59


O


ATOM
1112
CB
SER
A
267
50.924
55.535
28.790
1.00
30.27


C


ATOM
1113
OG
SER
A
267
49.593
55.132
28.534
1.00
33.40


O


ATOM
1114
N
GLU
A
268
49.272
54.912
31.507
1.00
30.01


N


ATOM
1115
CA
GLU
A
268
48.493
53.936
32.246
1.00
31.53


C


ATOM
1116
C
GLU
A
268
48.208
52.753
31.328
1.00
31.63


C


ATOM
1117
O
GLU
A
268
48.000
51.627
31.790
1.00
31.90


O


ATOM
1118
CB
GLU
A
268
47.184
54.572
32.716
1.00
33.65


C


ATOM
1119
CG
GLU
A
268
46.385
53.720
33.684
1.00
36.92


C


ATOM
1120
CD
GLU
A
268
45.169
54.445
34.238
1.00
38.90


C


ATOM
1121
OE1
GLU
A
268
44.448
53.837
35.059
1.00
41.93


O


ATOM
1122
OE2
GLU
A
268
44.933
55.615
33.857
1.00
37.65


O


ATOM
1123
N
TRP
A
269
48.212
53.007
30.022
1.00
30.66


N


ATOM
1124
CA
TRP
A
269
47.960
51.950
29.053
1.00
32.73


C


ATOM
1125
C
TRP
A
269
49.023
50.858
29.122
1.00
31.60


C


ATOM
1126
O
TRP
A
269
48.717
49.678
28.951
1.00
32.00


O


ATOM
1127
CB
TRP
A
269
47.890
52.520
27.632
1.00
34.13


C


ATOM
1128
CG
TRP
A
269
46.705
53.411
27.401
1.00
38.84


C


ATOM
1129
CD1
TRP
A
269
46.723
54.759
27.170
1.00
39.63


C


ATOM
1130
CD2
TRP
A
269
45.325
53.021
27.383
1.00
40.48


C


ATOM
1131
NE1
TRP
A
269
45.442
55.229
27.009
1.00
40.70


N


ATOM
1132
CE2
TRP
A
269
44.565
54.185
27.134
1.00
40.74


C


ATOM
1133
CE3
TRP
A
269
44.657
51.800
27.553
1.00
41.39


C


ATOM
1134
CZ2
TRP
A
269
43.168
54.165
27.049
1.00
42.44


C


ATOM
1135
CZ3
TRP
A
269
43.266
51.780
27.469
1.00
42.63


C


ATOM
1136
CH2
TRP
A
269
42.539
52.957
27.219
1.00
42.95


C


ATOM
1137
N
GLN
A
270
50.273
51.237
29.370
1.00
30.36


N


ATOM
1138
CA
GLN
A
270
51.330
50.232
29.463
1.00
29.91


C


ATOM
1139
C
GLN
A
270
51.197
49.444
30.764
1.00
29.40


C


ATOM
1140
O
GLN
A
270
51.478
48.250
30.802
1.00
29.26


O


ATOM
1141
CB
GLN
A
270
52.717
50.883
29.369
1.00
28.96


C


ATOM
1142
CG
GLN
A
270
52.925
51.642
28.065
1.00
28.77


C


ATOM
1143
CD
GLN
A
270
54.293
51.420
27.438
1.00
28.29


C


ATOM
1144
OE1
GLN
A
270
55.185
50.820
28.041
1.00
27.12


O


ATOM
1145
NE2
GLN
A
270
54.463
51.916
26.217
1.00
26.63


N


ATOM
1146
N
LYS
A
271
50.763
50.113
31.828
1.00
30.02


N


ATOM
1147
CA
LYS
A
271
50.579
49.437
33.107
1.00
31.43


C


ATOM
1148
C
LYS
A
271
49.484
48.381
32.944
1.00
31.09


C


ATOM
1149
O
LYS
A
271
49.618
47.257
33.419
1.00
30.76


O


ATOM
1150
CB
LYS
A
271
50.181
50.433
34.202
1.00
33.38


C


ATOM
1151
CG
LYS
A
271
49.911
49.770
35.552
1.00
36.04


C


ATOM
1152
CD
LYS
A
271
49.607
50.779
36.655
1.00
37.85


C


ATOM
1153
CE
LYS
A
271
49.404
50.068
37.993
1.00
40.25


C


ATOM
1154
NZ
LYS
A
271
49.157
51.008
39.131
1.00
42.83


N


ATOM
1155
N
ILE
A
272
48.409
48.752
32.257
1.00
31.55


N


ATOM
1156
CA
ILE
A
272
47.291
47.841
32.018
1.00
31.85


C


ATOM
1157
C
ILE
A
272
47.745
46.632
31.202
1.00
31.95


C


ATOM
1158
O
ILE
A
272
47.433
45.490
31.544
1.00
31.04


O


ATOM
1159
CB
ILE
A
272
46.139
48.565
31.278
1.00
31.97


C


ATOM
1160
CG1
ILE
A
272
45.463
49.551
32.235
1.00
32.25


C


ATOM
1161
CG2
ILE
A
272
45.137
47.552
30.730
1.00
32.38


C


ATOM
1162
CD1
ILE
A
272
44.456
50.473
31.570
1.00
32.51


C


ATOM
1163
N
THR
A
273
48.492
46.890
30.133
1.00
30.63


N


ATOM
1164
CA
THR
A
273
48.995
45.833
29.267
1.00
31.00


C


ATOM
1165
C
THR
A
273
49.882
44.849
30.030
1.00
31.56


C


ATOM
1166
O
THR
A
273
49.702
43.633
29.927
1.00
31.43


O


ATOM
1167
CB
THR
A
273
49.796
46.422
28.084
1.00
30.85


C


ATOM
1168
OG1
THR
A
273
48.932
47.244
27.292
1.00
32.26


O


ATOM
1169
CG2
THR
A
273
50.366
45.311
27.208
1.00
30.97


C


ATOM
1170
N
ILE
A
274
50.843
45.370
30.789
1.00
31.51


N


ATOM
1171
CA
ILE
A
274
51.736
44.506
31.558
1.00
32.20


C


ATOM
1172
C
ILE
A
274
50.927
43.738
32.603
1.00
32.56


C


ATOM
1173
O
ILE
A
274
51.189
42.566
32.870
1.00
32.30


O


ATOM
1174
CB
ILE
A
274
52.825
45.314
32.288
1.00
31.42


C


ATOM
1175
CG1
ILE
A
274
53.653
46.114
31.278
1.00
32.15


C


ATOM
1176
CG2
ILE
A
274
53.718
44.367
33.091
1.00
31.67


C


ATOM
1177
CD1
ILE
A
274
54.655
47.065
31.920
1.00
32.30


C


ATOM
1178
N
GLY
A
275
49.941
44.410
33.189
1.00
32.77


N


ATOM
1179
CA
GLY
A
275
49.110
43.775
34.196
1.00
33.56


C


ATOM
1180
C
GLY
A
275
48.351
42.578
33.653
1.00
34.04


C


ATOM
1181
O
GLY
A
275
48.245
41.546
34.320
1.00
34.05


O


ATOM
1182
N
TRP
A
276
47.822
42.714
32.443
1.00
33.68


N


ATOM
1183
CA
TRP
A
276
47.065
41.642
31.804
1.00
34.90


C


ATOM
1184
C
TRP
A
276
47.980
40.451
31.536
1.00
35.94


C


ATOM
1185
O
TRP
A
276
47.581
39.293
31.700
1.00
34.92


O


ATOM
1186
CB
TRP
A
276
46.469
42.134
30.485
1.00
35.21


C


ATOM
1187
CG
TRP
A
276
45.582
41.138
29.813
1.00
36.07


C


ATOM
1188
CD1
TRP
A
276
44.237
40.972
30.002
1.00
36.67


C


ATOM
1189
CD2
TRP
A
276
45.978
40.153
28.853
1.00
36.84


C


ATOM
1190
NE1
TRP
A
276
43.772
39.944
29.212
1.00
36.48


N


ATOM
1191
CE2
TRP
A
276
44.820
39.424
28.498
1.00
37.06


C


ATOM
1192
CE3
TRP
A
276
47.201
39.814
28.255
1.00
36.59


C


ATOM
1193
CZ2
TRP
A
276
44.848
38.376
27.572
1.00
37.28


C


ATOM
1194
CZ3
TRP
A
276
47.230
38.772
27.336
1.00
37.26


C


ATOM
1195
CH2
TRP
A
276
46.057
38.065
27.004
1.00
37.96


C


ATOM
1196
N
ILE
A
277
49.211
40.740
31.121
1.00
35.54


N


ATOM
1197
CA
ILE
A
277
50.181
39.690
30.835
1.00
36.20


C


ATOM
1198
C
ILE
A
277
50.562
38.933
32.109
1.00
37.31


C


ATOM
1199
O
ILE
A
277
50.646
37.703
32.106
1.00
37.04


O


ATOM
1200
CB
ILE
A
277
51.456
40.279
30.178
1.00
35.46


C


ATOM
1201
CG1
ILE
A
277
51.112
40.828
28.791
1.00
35.23


C


ATOM
1202
CG2
ILE
A
277
52.541
39.210
30.080
1.00
35.59


C


ATOM
1203
CD1
ILE
A
277
52.273
41.503
28.081
1.00
35.42


C


ATOM
1204
N
ARG
A
278
50.787
39.666
33.194
1.00
38.07


N


ATOM
1205
CA
ARG
A
278
51.152
39.047
34.466
1.00
39.93


C


ATOM
1206
C
ARG
A
278
50.029
38.167
35.005
1.00
41.35


C


ATOM
1207
O
ARG
A
278
50.273
37.077
35.517
1.00
41.11


O


ATOM
1208
CB
ARG
A
278
51.489
40.120
35.502
1.00
39.44


C


ATOM
1209
CG
ARG
A
278
52.797
40.835
35.243
1.00
38.20


C


ATOM
1210
CD
ARG
A
278
53.989
39.927
35.511
1.00
38.69


C


ATOM
1211
NE
ARG
A
278
55.225
40.567
35.075
1.00
37.38


N


ATOM
1212
CZ
ARG
A
278
55.937
40.181
34.023
1.00
37.01


C


ATOM
1213
NH1
ARG
A
278
55.547
39.141
33.297
1.00
35.28


N


ATOM
1214
NH2
ARG
A
278
57.022
40.861
33.674
1.00
34.80


N


ATOM
1215
N
GLU
A
279
48.801
38.654
34.891
1.00
42.82


N


ATOM
1216
CA
GLU
A
279
47.634
37.922
35.369
1.00
45.18


C


ATOM
1217
C
GLU
A
279
47.353
36.655
34.559
1.00
45.03


C


ATOM
1218
O
GLU
A
279
46.793
35.686
35.076
1.00
45.43


O


ATOM
1219
CB
GLU
A
279
46.417
38.858
35.355
1.00
47.47


C


ATOM
1220
CG
GLU
A
279
45.058
38.180
35.269
1.00
51.44


C


ATOM
1221
CD
GLU
A
279
44.757
37.662
33.873
1.00
53.84


C


ATOM
1222
OE1
GLU
A
279
44.818
38.465
32.909
1.00
54.89


O


ATOM
1223
OE2
GLU
A
279
44.460
36.454
33.740
1.00
54.90


O


ATOM
1224
N
LYS
A
280
47.755
36.655
33.294
1.00
44.19


N


ATOM
1225
CA
LYS
A
280
47.513
35.515
32.421
1.00
43.85


C


ATOM
1226
C
LYS
A
280
48.704
34.558
32.319
1.00
43.09


C


ATOM
1227
O
LYS
A
280
48.523
33.356
32.109
1.00
42.03


O


ATOM
1228
CB
LYS
A
280
47.133
36.030
31.027
1.00
45.44


C


ATOM
1229
CG
LYS
A
280
46.346
35.059
30.153
1.00
48.33


C


ATOM
1230
CD
LYS
A
280
47.213
33.959
29.575
1.00
50.41


C


ATOM
1231
CE
LYS
A
280
46.394
33.011
28.702
1.00
51.95


C


ATOM
1232
NZ
LYS
A
280
45.734
33.714
27.563
1.00
52.39


N


ATOM
1233
N
TYR
A
281
49.915
35.082
32.494
1.00
41.24


N


ATOM
1234
CA
TYR
A
281
51.121
34.268
32.369
1.00
39.92


C


ATOM
1235
C
TYR
A
281
52.095
34.338
33.535
1.00
39.29


C


ATOM
1236
O
TYR
A
281
53.103
33.636
33.538
1.00
38.90


O


ATOM
1237
CB
TYR
A
281
51.882
34.674
31.110
1.00
40.32


C


ATOM
1238
CG
TYR
A
281
51.108
34.542
29.823
1.00
40.12


C


ATOM
1239
CD1
TYR
A
281
50.920
33.296
29.224
1.00
40.31


C


ATOM
1240
CD2
TYR
A
281
50.595
35.668
29.181
1.00
40.13


C


ATOM
1241
CE1
TYR
A
281
50.246
33.178
28.013
1.00
40.79


C


ATOM
1242
CE2
TYR
A
281
49.918
35.560
27.973
1.00
40.17


C


ATOM
1243
CZ
TYR
A
281
49.750
34.314
27.393
1.00
41.11


C


ATOM
1244
OH
TYR
A
281
49.097
34.208
26.188
1.00
41.85


O


ATOM
1245
N
GLY
A
282
51.812
35.181
34.517
1.00
38.90


N


ATOM
1246
CA
GLY
A
282
52.733
35.306
35.629
1.00
39.41


C


ATOM
1247
C
GLY
A
282
54.044
35.871
35.105
1.00
40.43


C


ATOM
1248
O
GLY
A
282
54.044
36.689
34.184
1.00
39.10


O


ATOM
1249
N
ASP
A
283
55.163
35.432
35.671
1.00
40.95


N


ATOM
1250
CA
ASP
A
283
56.466
35.918
35.236
1.00
42.89


C


ATOM
1251
C
ASP
A
283
57.110
35.037
34.163
1.00
42.30


C


ATOM
1252
O
ASP
A
283
58.304
35.149
33.903
1.00
43.50


O


ATOM
1253
CB
ASP
A
283
57.407
36.046
36.440
1.00
44.35


C


ATOM
1254
CG
ASP
A
283
56.985
37.154
37.400
1.00
47.46


C


ATOM
1255
OD1
ASP
A
283
57.019
38.341
37.000
1.00
47.96


O


ATOM
1256
OD2
ASP
A
283
56.620
36.840
38.555
1.00
48.36


O


ATOM
1257
N
LYS
A
284
56.321
34.171
33.534
1.00
42.27


N


ATOM
1258
CA
LYS
A
284
56.843
33.283
32.494
1.00
41.83


C


ATOM
1259
C
LYS
A
284
56.953
33.968
31.134
1.00
40.43


C


ATOM
1260
O
LYS
A
284
57.689
33.518
30.256
1.00
40.67


O


ATOM
1261
CB
LYS
A
284
55.970
32.029
32.360
1.00
44.31


C


ATOM
1262
CG
LYS
A
284
56.142
31.005
33.480
1.00
47.22


C


ATOM
1263
CD
LYS
A
284
55.534
31.467
34.794
1.00
49.17


C


ATOM
1264
CE
LYS
A
284
55.602
30.352
35.837
1.00
51.28


C


ATOM
1265
NZ
LYS
A
284
54.892
30.695
37.108
1.00
52.23


N


ATOM
1266
N
VAL
A
285
56.204
35.045
30.950
1.00
37.55


N


ATOM
1267
CA
VAL
A
285
56.257
35.784
29.696
1.00
34.84


C


ATOM
1268
C
VAL
A
285
56.954
37.100
30.007
1.00
32.72


C


ATOM
1269
O
VAL
A
285
56.514
37.847
30.876
1.00
32.13


O


ATOM
1270
CB
VAL
A
285
54.846
36.045
29.142
1.00
34.53


C


ATOM
1271
CG1
VAL
A
285
54.912
37.015
27.967
1.00
34.19


C


ATOM
1272
CG2
VAL
A
285
54.224
34.722
28.698
1.00
35.84


C


ATOM
1273
N
LYS
A
286
58.053
37.364
29.307
1.00
31.33


N


ATOM
1274
CA
LYS
A
286
58.836
38.575
29.529
1.00
29.68


C


ATOM
1275
C
LYS
A
286
58.365
39.710
28.629
1.00
28.86


C


ATOM
1276
O
LYS
A
286
58.122
39.509
27.442
1.00
29.10


O


ATOM
1277
CB
LYS
A
286
60.318
38.281
29.276
1.00
30.15


C


ATOM
1278
CG
LYS
A
286
60.847
37.084
30.062
1.00
29.04


C


ATOM
1279
CD
LYS
A
286
60.622
37.263
31.558
1.00
28.26


C


ATOM
1280
CE
LYS
A
286
61.158
36.077
32.355
1.00
29.94


C


ATOM
1281
NZ
LYS
A
286
60.950
36.259
33.822
1.00
28.63


N


ATOM
1282
N
VAL
A
287
58.254
40.907
29.195
1.00
28.83


N


ATOM
1283
CA
VAL
A
287
57.786
42.050
28.427
1.00
28.30


C


ATOM
1284
C
VAL
A
287
58.482
43.361
28.793
1.00
27.68


C


ATOM
1285
O
VAL
A
287
58.459
43.792
29.942
1.00
28.41


O


ATOM
1286
CB
VAL
A
287
56.242
42.211
28.584
1.00
27.98


C


ATOM
1287
CG1
VAL
A
287
55.874
42.312
30.049
1.00
29.20


C


ATOM
1288
CG2
VAL
A
287
55.754
43.436
27.827
1.00
28.74


C


ATOM
1289
N
GLY
A
288
59.121
43.974
27.803
1.00
28.04


N


ATOM
1290
CA
GLY
A
288
59.786
45.246
28.025
1.00
26.66


C


ATOM
1291
C
GLY
A
288
58.762
46.345
27.815
1.00
26.11


C


ATOM
1292
O
GLY
A
288
57.721
46.105
27.203
1.00
25.68


O


ATOM
1293
N
ALA
A
289
59.044
47.541
28.323
1.00
25.08


N


ATOM
1294
CA
ALA
A
289
58.126
48.669
28.192
1.00
24.74


C


ATOM
1295
C
ALA
A
289
58.906
49.955
27.935
1.00
25.55


C


ATOM
1296
O
ALA
A
289
60.115
50.007
28.151
1.00
26.30


O


ATOM
1297
CB
ALA
A
289
57.288
48.813
29.460
1.00
22.88


C


ATOM
1298
N
GLY
A
290
58.207
50.990
27.478
1.00
26.17


N


ATOM
1299
CA
GLY
A
290
58.857
52.259
27.196
1.00
25.73


C


ATOM
1300
C
GLY
A
290
58.137
52.974
26.069
1.00
26.32


C


ATOM
1301
O
GLY
A
290
57.099
52.500
25.616
1.00
27.48


O


ATOM
1302
N
ASN
A
291
58.677
54.095
25.592
1.00
25.49


N


ATOM
1303
CA
ASN
A
291
59.932
54.659
26.086
1.00
24.28


C


ATOM
1304
C
ASN
A
291
59.744
55.754
27.124
1.00
23.86


C


ATOM
1305
O
ASN
A
291
58.738
56.465
27.115
1.00
22.00


O


ATOM
1306
CB
ASN
A
291
60.729
55.245
24.919
1.00
24.80


C


ATOM
1307
CG
ASN
A
291
61.287
54.184
24.008
1.00
25.31


C


ATOM
1308
OD1
ASN
A
291
60.830
53.042
24.021
1.00
25.35


O


ATOM
1309
ND2
ASN
A
291
62.278
54.555
23.202
1.00
24.45


N


ATOM
1310
N
ILE
A
292
60.729
55.883
28.011
1.00
22.96


N


ATOM
1311
CA
ILE
A
292
60.724
56.925
29.030
1.00
22.95


C


ATOM
1312
C
ILE
A
292
62.077
57.636
28.986
1.00
23.91


C


ATOM
1313
O
ILE
A
292
63.017
57.157
28.342
1.00
23.07


O


ATOM
1314
CB
ILE
A
292
60.426
56.356
30.455
1.00
23.66


C


ATOM
1315
CG1
ILE
A
292
61.301
55.139
30.770
1.00
22.82


C


ATOM
1316
CG2
ILE
A
292
58.958
55.963
30.542
1.00
24.06


C


ATOM
1317
CD1
ILE
A
292
62.734
55.478
31.158
1.00
23.86


C


ATOM
1318
N
VAL
A
293
62.181
58.791
29.633
1.00
24.59


N


ATOM
1319
CA
VAL
A
293
63.440
59.524
29.605
1.00
25.09


C


ATOM
1320
C
VAL
A
293
63.902
60.057
30.944
1.00
25.38


C


ATOM
1321
O
VAL
A
293
64.874
60.812
31.000
1.00
24.51


O


ATOM
1322
CB
VAL
A
293
63.380
60.708
28.623
1.00
24.93


C


ATOM
1323
CG1
VAL
A
293
63.283
60.192
27.196
1.00
24.14


C


ATOM
1324
CG2
VAL
A
293
62.200
61.601
28.965
1.00
25.29


C


ATOM
1325
N
ASP
A
294
63.209
59.686
32.018
1.00
25.36


N


ATOM
1326
CA
ASP
A
294
63.610
60.140
33.342
1.00
25.43


C


ATOM
1327
C
ASP
A
294
63.315
59.123
34.439
1.00
25.22


C


ATOM
1328
O
ASP
A
294
62.705
58.082
34.188
1.00
24.53


O


ATOM
1329
CB
ASP
A
294
62.966
61.500
33.678
1.00
26.32


C


ATOM
1330
CG
ASP
A
294
61.456
61.424
33.890
1.00
26.90


C


ATOM
1331
OD1
ASP
A
294
60.831
60.369
33.659
1.00
27.35


O


ATOM
1332
OD2
ASP
A
294
60.884
62.456
34.291
1.00
28.46


O


ATOM
1333
N
GLY
A
295
63.762
59.435
35.649
1.00
25.01


N


ATOM
1334
CA
GLY
A
295
63.561
58.540
36.774
1.00
26.69


C


ATOM
1335
C
GLY
A
295
62.112
58.224
37.083
1.00
26.45


C


ATOM
1336
O
GLY
A
295
61.778
57.086
37.408
1.00
25.94


O


ATOM
1337
N
GLU
A
296
61.243
59.225
36.991
1.00
27.48


N


ATOM
1338
CA
GLU
A
296
59.825
59.013
37.275
1.00
27.87


C


ATOM
1339
C
GLU
A
296
59.191
58.014
36.317
1.00
27.05


C


ATOM
1340
O
GLU
A
296
58.438
57.136
36.736
1.00
26.56


O


ATOM
1341
CB
GLU
A
296
59.066
60.340
37.211
1.00
31.37


C


ATOM
1342
CG
GLU
A
296
59.445
61.302
38.318
1.00
37.66


C


ATOM
1343
CD
GLU
A
296
58.542
62.513
38.368
1.00
42.29


C


ATOM
1344
OE1
GLU
A
296
57.320
62.336
38.576
1.00
45.55


O


ATOM
1345
OE2
GLU
A
296
59.050
63.643
38.196
1.00
45.27


O


ATOM
1346
N
GLY
A
297
59.492
58.155
35.030
1.00
25.33


N


ATOM
1347
CA
GLY
A
297
58.939
57.249
34.042
1.00
25.17


C


ATOM
1348
C
GLY
A
297
59.456
55.839
34.273
1.00
25.62


C


ATOM
1349
O
GLY
A
297
58.719
54.863
34.137
1.00
24.83


O


ATOM
1350
N
PHE
A
298
60.737
55.734
34.610
1.00
24.52


N


ATOM
1351
CA
PHE
A
298
61.343
54.434
34.880
1.00
25.70


C


ATOM
1352
C
PHE
A
298
60.631
53.751
36.043
1.00
26.22


C


ATOM
1353
O
PHE
A
298
60.219
52.595
35.946
1.00
26.55


O


ATOM
1354
CB
PHE
A
298
62.821
54.589
35.253
1.00
24.99


C


ATOM
1355
CG
PHE
A
298
63.432
53.322
35.785
1.00
24.97


C


ATOM
1356
CD1
PHE
A
298
63.935
52.358
34.917
1.00
25.29


C


ATOM
1357
CD2
PHE
A
298
63.410
53.047
37.150
1.00
25.62


C


ATOM
1358
CE1
PHE
A
298
64.400
51.131
35.400
1.00
25.51


C


ATOM
1359
CE2
PHE
A
298
63.871
51.822
37.645
1.00
25.63


C


ATOM
1360
CZ
PHE
A
298
64.364
50.863
36.766
1.00
23.87


C


ATOM
1361
N
ARG
A
299
60.504
54.478
37.149
1.00
26.18


N


ATOM
1362
CA
ARG
A
299
59.875
53.947
38.354
1.00
27.35


C


ATOM
1363
C
ARG
A
299
58.440
53.489
38.104
1.00
27.07


C


ATOM
1364
O
ARG
A
299
58.011
52.454
38.622
1.00
26.36


O


ATOM
1365
CB
ARG
A
299
59.916
55.000
39.468
1.00
28.99


C


ATOM
1366
CG
ARG
A
299
59.457
54.503
40.837
1.00
32.84


C


ATOM
1367
CD
ARG
A
299
59.794
55.518
41.926
1.00
35.60


C


ATOM
1368
NE
ARG
A
299
61.220
55.543
42.252
1.00
37.71


N


ATOM
1369
CZ
ARG
A
299
61.834
54.631
43.006
1.00
38.54


C


ATOM
1370
NH1
ARG
A
299
61.150
53.616
43.519
1.00
37.82


N


ATOM
1371
NH2
ARG
A
299
63.133
54.738
43.258
1.00
38.76


N


ATOM
1372
N
TYR
A
300
57.702
54.249
37.303
1.00
25.60


N


ATOM
1373
CA
TYR
A
300
56.324
53.890
37.005
1.00
25.92


C


ATOM
1374
C
TYR
A
300
56.249
52.543
36.286
1.00
26.46


C


ATOM
1375
O
TYR
A
300
55.431
51.690
36.634
1.00
26.22


O


ATOM
1376
CB
TYR
A
300
55.664
54.958
36.136
1.00
26.45


C


ATOM
1377
CG
TYR
A
300
54.209
54.667
35.845
1.00
26.38


C


ATOM
1378
CD1
TYR
A
300
53.222
54.911
36.803
1.00
27.42


C


ATOM
1379
CD2
TYR
A
300
53.822
54.123
34.623
1.00
26.65


C


ATOM
1380
CE1
TYR
A
300
51.881
54.621
36.546
1.00
27.66


C


ATOM
1381
CE2
TYR
A
300
52.486
53.831
34.359
1.00
26.96


C


ATOM
1382
CZ
TYR
A
300
51.525
54.083
35.321
1.00
27.35


C


ATOM
1383
OH
TYR
A
300
50.207
53.804
35.045
1.00
28.84


O


ATOM
1384
N
LEU
A
301
57.100
52.352
35.283
1.00
24.93


N


ATOM
1385
CA
LEU
A
301
57.097
51.101
34.539
1.00
25.20


C


ATOM
1386
C
LEU
A
301
57.727
49.962
35.343
1.00
24.99


C


ATOM
1387
O
LEU
A
301
57.383
48.795
35.152
1.00
25.51


O


ATOM
1388
CB
LEU
A
301
57.814
51.281
33.192
1.00
24.73


C


ATOM
1389
CG
LEU
A
301
57.092
52.216
32.208
1.00
24.97


C


ATOM
1390
CD1
LEU
A
301
57.901
52.348
30.920
1.00
24.19


C


ATOM
1391
CD2
LEU
A
301
55.693
51.665
31.903
1.00
25.94


C


ATOM
1392
N
ALA
A
302
58.642
50.300
36.243
1.00
25.01


N


ATOM
1393
CA
ALA
A
302
59.284
49.289
37.077
1.00
26.34


C


ATOM
1394
C
ALA
A
302
58.224
48.715
38.022
1.00
27.09


C


ATOM
1395
O
ALA
A
302
58.068
47.495
38.140
1.00
27.29


O


ATOM
1396
CB
ALA
A
302
60.426
49.911
37.872
1.00
25.08


C


ATOM
1397
N
ASP
A
303
57.493
49.603
38.688
1.00
27.62


N


ATOM
1398
CA
ASP
A
303
56.439
49.182
39.602
1.00
29.54


C


ATOM
1399
C
ASP
A
303
55.335
48.444
38.853
1.00
29.82


C


ATOM
1400
O
ASP
A
303
54.670
47.574
39.423
1.00
29.45


O


ATOM
1401
CB
ASP
A
303
55.846
50.386
40.342
1.00
31.26


C


ATOM
1402
CG
ASP
A
303
56.796
50.967
41.374
1.00
34.06


C


ATOM
1403
OD1
ASP
A
303
57.678
50.226
41.863
1.00
35.03


O


ATOM
1404
OD2
ASP
A
303
56.652
52.160
41.713
1.00
35.59


O


ATOM
1405
N
ALA
A
304
55.145
48.786
37.579
1.00
28.20


N


ATOM
1406
CA
ALA
A
304
54.124
48.148
36.748
1.00
28.48


C


ATOM
1407
C
ALA
A
304
54.500
46.706
36.403
1.00
29.41


C


ATOM
1408
O
ALA
A
304
53.644
45.919
35.981
1.00
30.01


O


ATOM
1409
CB
ALA
A
304
53.913
48.943
35.467
1.00
29.13


C


ATOM
1410
N
GLY
A
305
55.779
46.371
36.558
1.00
27.94


N


ATOM
1411
CA
GLY
A
305
56.228
45.013
36.285
1.00
28.09


C


ATOM
1412
C
GLY
A
305
57.047
44.759
35.031
1.00
27.94


C


ATOM
1413
O
GLY
A
305
57.303
43.603
34.688
1.00
28.94


O


ATOM
1414
N
ALA
A
306
57.468
45.815
34.342
1.00
27.01


N


ATOM
1415
CA
ALA
A
306
58.259
45.655
33.118
1.00
26.21


C


ATOM
1416
C
ALA
A
306
59.530
44.833
33.371
1.00
25.71


C


ATOM
1417
O
ALA
A
306
60.172
44.983
34.409
1.00
26.47


O


ATOM
1418
CB
ALA
A
306
58.630
47.038
32.549
1.00
26.19


C


ATOM
1419
N
ASP
A
307
59.888
43.970
32.421
1.00
26.45


N


ATOM
1420
CA
ASP
A
307
61.087
43.135
32.549
1.00
26.38


C


ATOM
1421
C
ASP
A
307
62.351
43.883
32.137
1.00
26.11


C


ATOM
1422
O
ASP
A
307
63.459
43.517
32.523
1.00
26.90


O


ATOM
1423
CB
ASP
A
307
60.923
41.857
31.731
1.00
27.11


C


ATOM
1424
CG
ASP
A
307
59.967
40.887
32.387
1.00
29.35


C


ATOM
1425
OD1
ASP
A
307
60.312
40.373
33.470
1.00
29.58


O


ATOM
1426
OD2
ASP
A
307
58.873
40.656
31.837
1.00
30.28


O


ATOM
1427
N
PHE
A
308
62.174
44.916
31.324
1.00
24.79


N


ATOM
1428
CA
PHE
A
308
63.274
45.786
30.922
1.00
25.02


C


ATOM
1429
C
PHE
A
308
62.613
47.071
30.453
1.00
25.26


C


ATOM
1430
O
PHE
A
308
61.465
47.059
30.006
1.00
25.39


O


ATOM
1431
CB
PHE
A
308
64.194
45.142
29.855
1.00
24.16


C


ATOM
1432
CG
PHE
A
308
63.647
45.131
28.449
1.00
26.91


C


ATOM
1433
CD1
PHE
A
308
63.601
46.297
27.686
1.00
26.51


C


ATOM
1434
CD2
PHE
A
308
63.232
43.933
27.866
1.00
27.59


C


ATOM
1435
CE1
PHE
A
308
63.157
46.273
26.368
1.00
27.45


C


ATOM
1436
CE2
PHE
A
308
62.783
43.892
26.543
1.00
28.40


C


ATOM
1437
CZ
PHE
A
308
62.745
45.062
25.790
1.00
28.01


C


ATOM
1438
N
ILE
A
309
63.316
48.187
30.597
1.00
24.66


N


ATOM
1439
CA
ILE
A
309
62.737
49.469
30.227
1.00
24.56


C


ATOM
1440
C
ILE
A
309
63.565
50.185
29.171
1.00
24.22


C


ATOM
1441
O
ILE
A
309
64.781
50.319
29.304
1.00
23.11


O


ATOM
1442
CB
ILE
A
309
62.566
50.338
31.495
1.00
25.23


C


ATOM
1443
CG1
ILE
A
309
61.544
49.662
32.419
1.00
24.51


C


ATOM
1444
CG2
ILE
A
309
62.134
51.756
31.123
1.00
24.72


C


ATOM
1445
CD1
ILE
A
309
61.450
50.243
33.802
1.00
25.49


C


ATOM
1446
N
LYS
A
310
62.881
50.643
28.125
1.00
23.39


N


ATOM
1447
CA
LYS
A
310
63.527
51.310
27.003
1.00
24.09


C


ATOM
1448
C
LYS
A
310
63.573
52.825
27.202
1.00
24.12


C


ATOM
1449
O
LYS
A
310
62.578
53.449
27.575
1.00
22.87


O


ATOM
1450
CB
LYS
A
310
62.788
50.945
25.713
1.00
25.57


C


ATOM
1451
CG
LYS
A
310
63.633
51.022
24.457
1.00
27.69


C


ATOM
1452
CD
LYS
A
310
63.347
49.838
23.526
1.00
27.60


C


ATOM
1453
CE
LYS
A
310
61.915
49.849
23.020
1.00
27.87


C


ATOM
1454
NZ
LYS
A
310
61.614
51.110
22.280
1.00
28.37


N


ATOM
1455
N
ILE
A
311
64.741
53.398
26.925
1.00
23.23


N


ATOM
1456
CA
ILE
A
311
64.996
54.827
27.101
1.00
23.17


C


ATOM
1457
C
ILE
A
311
65.173
55.586
25.794
1.00
21.87


C


ATOM
1458
O
ILE
A
311
65.937
55.166
24.925
1.00
22.46


O


ATOM
1459
CB
ILE
A
311
66.301
55.045
27.901
1.00
21.23


C


ATOM
1460
CG1
ILE
A
311
66.238
54.291
29.236
1.00
22.02


C


ATOM
1461
CG2
ILE
A
311
66.537
56.532
28.122
1.00
21.42


C


ATOM
1462
CD1
ILE
A
311
67.601
54.143
29.891
1.00
21.94


C


ATOM
1463
N
GLY
A
312
64.484
56.712
25.662
1.00
24.32


N


ATOM
1464
CA
GLY
A
312
64.666
57.510
24.467
1.00
24.57


C


ATOM
1465
C
GLY
A
312
63.449
58.070
23.773
1.00
26.09


C


ATOM
1466
O
GLY
A
312
62.559
57.332
23.356
1.00
25.55


O


ATOM
1467
N
ILE
A
313
63.428
59.393
23.644
1.00
26.99


N


ATOM
1468
CA
ILE
A
313
62.357
60.089
22.950
1.00
28.73


C


ATOM
1469
C
ILE
A
313
62.968
61.275
22.215
1.00
30.51


C


ATOM
1470
O
ILE
A
313
63.531
62.172
22.845
1.00
30.13


O


ATOM
1471
CB
ILE
A
313
61.281
60.635
23.915
1.00
28.78


C


ATOM
1472
CG1
ILE
A
313
60.561
59.480
24.619
1.00
29.45


C


ATOM
1473
CG2
ILE
A
313
60.277
61.469
23.134
1.00
29.20


C


ATOM
1474
CD1
ILE
A
313
59.544
59.942
25.648
1.00
29.69


C


ATOM
1475
N
GLY
A
314
62.865
61.264
20.888
1.00
33.20


N


ATOM
1476
CA
GLY
A
314
63.385
62.357
20.087
1.00
36.88


C


ATOM
1477
C
GLY
A
314
64.748
62.144
19.454
1.00
39.48


C


ATOM
1478
O
GLY
A
314
65.102
62.843
18.499
1.00
40.62


O


ATOM
1479
N
GLY
A
315
65.506
61.177
19.967
1.00
40.05


N


ATOM
1480
CA
GLY
A
315
66.840
60.918
19.452
1.00
41.12


C


ATOM
1481
C
GLY
A
315
66.950
60.152
18.146
1.00
42.12


C


ATOM
1482
O
GLY
A
315
67.977
60.235
17.469
1.00
41.49


O


ATOM
1483
N
GLY
A
316
65.906
59.409
17.790
1.00
42.04


N


ATOM
1484
CA
GLY
A
316
65.924
58.640
16.555
1.00
42.81


C


ATOM
1485
C
GLY
A
316
66.345
59.447
15.338
1.00
43.59


C


ATOM
1486
O
GLY
A
316
66.029
60.633
15.227
1.00
44.04


O


ATOM
1487
N
SER
A
317
67.056
58.800
14.419
1.00
44.63


N


ATOM
1488
CA
SER
A
317
67.535
59.453
13.204
1.00
45.96


C


ATOM
1489
C
SER
A
317
66.400
59.929
12.303
1.00
47.12


C


ATOM
1490
O
SER
A
317
66.554
60.897
11.561
1.00
46.76


O


ATOM
1491
CB
SER
A
317
68.436
58.503
12.412
1.00
45.33


C


ATOM
1492
OG
SER
A
317
67.704
57.391
11.925
1.00
44.82


O


ATOM
1493
N
ILE
A
318
65.266
59.240
12.363
1.00
49.21


N


ATOM
1494
CA
ILE
A
318
64.115
59.604
11.544
1.00
51.92


C


ATOM
1495
C
ILE
A
318
62.986
60.204
12.374
1.00
53.83


C


ATOM
1496
O
ILE
A
318
61.811
60.095
12.019
1.00
54.17


O


ATOM
1497
CB
ILE
A
318
63.581
58.381
10.754
1.00
51.77


C


ATOM
1498
CG1
ILE
A
318
63.731
57.105
11.586
1.00
51.59


C


ATOM
1499
CG2
ILE
A
318
64.339
58.237
9.441
1.00
51.61


C


ATOM
1500
CD1
ILE
A
318
62.997
57.131
12.898
1.00
51.22


C


HETATM
1501
N
CSO
A
319
63.355
60.840
13.481
1.00
56.01


N


HETATM
1502
CA
CSO
A
319
62.387
61.468
14.371
1.00
58.61


C


HETATM
1503
CB
CSO
A
319
62.457
60.825
15.760
1.00
60.16


C


HETATM
1504
SG
CSO
A
319
60.983
61.106
16.793
1.00
64.08


S


HETATM
1505
C
CSO
A
319
62.708
62.957
14.481
1.00
59.03


C


HETATM
1506
O
CSO
A
319
63.754
63.331
15.008
1.00
58.88


O


HETATM
1507
OD
CSO
A
319
60.477
62.837
16.987
1.00
63.19


O


ATOM
1508
N
ILE
A
320
61.814
63.805
13.979
1.00
59.78


N


ATOM
1509
CA
ILE
A
320
62.028
65.250
14.034
1.00
60.48


C


ATOM
1510
C
ILE
A
320
61.159
65.875
15.125
1.00
60.65


C


ATOM
1511
O
ILE
A
320
60.074
66.397
14.856
1.00
60.82


O


ATOM
1512
CB
ILE
A
320
61.706
65.913
12.676
1.00
60.96


C


ATOM
1513
CG1
ILE
A
320
62.500
65.221
11.562
1.00
61.17


C


ATOM
1514
CG2
ILE
A
320
62.064
67.398
12.721
1.00
60.93


C


ATOM
1515
CD1
ILE
A
320
62.196
65.738
10.167
1.00
61.13


C


ATOM
1516
N
THR
A
321
61.656
65.817
16.357
1.00
60.47


N


ATOM
1517
CA
THR
A
321
60.961
66.343
17.530
1.00
60.58


C


ATOM
1518
C
THR
A
321
60.288
67.701
17.323
1.00
60.31


C


ATOM
1519
O
THR
A
321
59.072
67.828
17.474
1.00
59.52


O


ATOM
1520
CB
THR
A
321
61.928
66.469
18.726
1.00
60.88


C


ATOM
1521
OG1
THR
A
321
62.632
65.234
18.906
1.00
61.19


O


ATOM
1522
CG2
THR
A
321
61.157
66.797
19.995
1.00
60.45


C


ATOM
1523
N
ARG
A
322
61.086
68.709
16.986
1.00
60.45


N


ATOM
1524
CA
ARG
A
322
60.581
70.063
16.776
1.00
60.85


C


ATOM
1525
C
ARG
A
322
59.375
70.172
15.850
1.00
60.80


C


ATOM
1526
O
ARG
A
322
58.401
70.849
16.176
1.00
60.73


O


ATOM
1527
CB
ARG
A
322
61.695
70.967
16.251
1.00
61.37


C


ATOM
1528
CG
ARG
A
322
62.696
71.397
17.305
1.00
62.07


C


ATOM
1529
CD
ARG
A
322
63.711
72.351
16.706
1.00
62.95


C


ATOM
1530
NE
ARG
A
322
64.504
73.029
17.726
1.00
63.47


N


ATOM
1531
CZ
ARG
A
322
65.442
73.931
17.458
1.00
63.65


C


ATOM
1532
NH1
ARG
A
322
65.704
74.262
16.200
1.00
63.49


N


ATOM
1533
NH2
ARG
A
322
66.115
74.504
18.445
1.00
63.65


N


ATOM
1534
N
GLU
A
323
59.437
69.522
14.693
1.00
60.59


N


ATOM
1535
CA
GLU
A
323
58.328
69.579
13.747
1.00
60.45


C


ATOM
1536
C
GLU
A
323
57.157
68.717
14.208
1.00
59.48


C


ATOM
1537
O
GLU
A
323
56.231
68.454
13.439
1.00
59.76


O


ATOM
1538
CB
GLU
A
323
58.781
69.116
12.359
1.00
61.67


C


ATOM
1539
CG
GLU
A
323
59.935
69.914
11.778
1.00
63.67


C


ATOM
1540
CD
GLU
A
323
60.259
69.515
10.348
1.00
64.69


C


ATOM
1541
OE1
GLU
A
323
60.474
68.311
10.094
1.00
65.62


O


ATOM
1542
OE2
GLU
A
323
60.301
70.407
9.476
1.00
65.47


O


ATOM
1543
N
GLN
A
324
57.194
68.284
15.464
1.00
57.92


N


ATOM
1544
CA
GLN
A
324
56.131
67.446
16.001
1.00
56.25


C


ATOM
1545
C
GLN
A
324
55.529
67.984
17.300
1.00
54.10


C


ATOM
1546
O
GLN
A
324
54.872
69.026
17.300
1.00
54.39


O


ATOM
1547
CB
GLN
A
324
56.653
66.022
16.206
1.00
58.06


C


ATOM
1548
CG
GLN
A
324
57.155
65.370
14.924
1.00
60.13


C


ATOM
1549
CD
GLN
A
324
57.820
64.027
15.164
1.00
61.81


C


ATOM
1550
OE1
GLN
A
324
58.311
63.388
14.231
1.00
62.58


O


ATOM
1551
NE2
GLN
A
324
57.838
63.590
16.419
1.00
62.80


N


ATOM
1552
N
LYS
A
325
55.754
67.278
18.404
1.00
50.55


N


ATOM
1553
CA
LYS
A
325
55.200
67.685
19.693
1.00
46.97


C


ATOM
1554
C
LYS
A
325
56.157
68.456
20.589
1.00
43.59


C


ATOM
1555
O
LYS
A
325
55.731
69.086
21.558
1.00
42.57


O


ATOM
1556
CB
LYS
A
325
54.703
66.463
20.467
1.00
47.99


C


ATOM
1557
CG
LYS
A
325
53.491
65.775
19.876
1.00
50.14


C


ATOM
1558
CD
LYS
A
325
53.077
64.618
20.773
1.00
50.62


C


ATOM
1559
CE
LYS
A
325
51.895
63.874
20.208
1.00
51.86


C


ATOM
1560
NZ
LYS
A
325
51.526
62.721
21.067
1.00
52.95


N


ATOM
1561
N
GLY
A
326
57.446
68.400
20.283
1.00
39.82


N


ATOM
1562
CA
GLY
A
326
58.399
69.103
21.118
1.00
36.97


C


ATOM
1563
C
GLY
A
326
58.613
68.383
22.439
1.00
35.12


C


ATOM
1564
O
GLY
A
326
58.842
69.015
23.473
1.00
33.70


O


ATOM
1565
N
ILE
A
327
58.510
67.056
22.412
1.00
33.10


N


ATOM
1566
CA
ILE
A
327
58.732
66.255
23.609
1.00
31.94


C


ATOM
1567
C
ILE
A
327
60.039
65.500
23.399
1.00
30.96


C


ATOM
1568
O
ILE
A
327
60.360
65.095
22.283
1.00
29.97


O


ATOM
1569
CB
ILE
A
327
57.584
65.229
23.865
1.00
33.54


C


ATOM
1570
CC1
ILE
A
327
57.479
64.236
22.708
1.00
35.09


C


ATOM
1571
CG2
ILE
A
327
56.257
65.961
24.048
1.00
34.89


C


ATOM
1572
CD1
ILE
A
327
56.438
63.139
22.937
1.00
37.76


C


ATOM
1573
N
GLY
A
328
60.807
65.322
24.463
1.00
29.65


N


ATOM
1574
CA
GLY
A
328
62.058
64.606
24.312
1.00
29.68


C


ATOM
1575
C
GLY
A
328
63.106
65.030
25.316
1.00
28.25


C


ATOM
1576
O
GLY
A
328
62.838
65.825
26.220
1.00
27.09


O


ATOM
1577
N
ARG
A
329
64.309
64.494
25.147
1.00
27.34


N


ATOM
1578
CA
ARG
A
329
65.410
64.807
26.039
1.00
26.13


C


ATOM
1579
C
ARG
A
329
66.674
64.258
25.404
1.00
25.89


C


ATOM
1580
O
ARG
A
329
66.636
63.207
24.760
1.00
25.64


O


ATOM
1581
CB
ARG
A
329
65.178
64.141
27.400
1.00
26.27


C


ATOM
1582
CG
ARG
A
329
66.074
64.661
28.510
1.00
25.63


C


ATOM
1583
CD
ARG
A
329
65.816
63.929
29.809
1.00
25.44


C


ATOM
1584
NE
ARG
A
329
66.249
64.709
30.966
1.00
24.87


N


ATOM
1585
CZ
ARG
A
329
66.203
64.269
32.218
1.00
26.41


C


ATOM
1586
NH1
ARG
A
329
65.754
63.048
32.475
1.00
25.65


N


ATOM
1587
NH2
ARG
A
329
66.577
65.058
33.216
1.00
26.64


N


ATOM
1588
N
GLY
A
330
67.787
64.975
25.560
1.00
25.19


N


ATOM
1589
CA
GLY
A
330
69.040
64.497
25.002
1.00
24.58


C


ATOM
1590
C
GLY
A
330
69.218
63.063
25.469
1.00
24.73


C


ATOM
1591
O
GLY
A
330
69.010
62.770
26.645
1.00
23.16


O


ATOM
1592
N
GLN
A
331
69.617
62.174
24.566
1.00
24.37


N


ATOM
1593
CA
GLN
A
331
69.763
60.757
24.909
1.00
24.78


C


ATOM
1594
C
GLN
A
331
70.739
60.463
26.043
1.00
24.31


C


ATOM
1595
O
GLN
A
331
70.466
59.610
26.889
1.00
23.63


O


ATOM
1596
CB
GLN
A
331
70.162
59.947
23.667
1.00
25.13


C


ATOM
1597
CG
GLN
A
331
70.073
58.430
23.863
1.00
25.46


C


ATOM
1598
CD
GLN
A
331
68.633
57.917
23.958
1.00
28.00


C


ATOM
1599
OE1
GLN
A
331
68.391
56.774
24.355
1.00
29.62


O


ATOM
1600
NE2
GLN
A
331
67.679
58.756
23.586
1.00
26.29


N


ATOM
1601
N
ALA
A
332
71.878
61.155
26.064
1.00
23.62


N


ATOM
1602
CA
ALA
A
332
72.864
60.930
27.117
1.00
22.91


C


ATOM
1603
C
ALA
A
332
72.283
61.243
28.492
1.00
23.37


C


ATOM
1604
O
ALA
A
332
72.389
60.441
29.425
1.00
22.61


O


ATOM
1605
CB
ALA
A
332
74.115
61.778
26.864
1.00
23.28


C


ATOM
1606
N
THR
A
333
71.668
62.413
28.619
1.00
22.11


N


ATOM
1607
CA
THR
A
333
71.075
62.815
29.878
1.00
22.48


C


ATOM
1608
C
THR
A
333
69.974
61.840
30.296
1.00
22.58


C


ATOM
1609
O
THR
A
333
69.857
61.492
31.470
1.00
21.18


O


ATOM
1610
CB
THR
A
333
70.493
64.238
29.785
1.00
23.93


C


ATOM
1611
CG1
THR
A
333
71.547
65.160
29.457
1.00
24.95


O


ATOM
1612
CG2
THR
A
333
69.865
64.645
31.119
1.00
23.81


C


ATOM
1613
N
ALA
A
334
69.176
61.401
29.329
1.00
21.99


N


ATOM
1614
CA
ALA
A
334
68.093
60.462
29.600
1.00
22.69


C


ATOM
1615
C
ALA
A
334
68.630
59.149
30.178
1.00
22.31


C


ATOM
1616
O
ALA
A
334
68.113
58.632
31.175
1.00
22.17


O


ATOM
1617
CB
ALA
A
334
67.315
60.186
28.319
1.00
22.40


C


ATOM
1618
N
VAL
A
335
69.663
58.604
29.548
1.00
22.74


N


ATOM
1619
CA
VAL
A
335
70.248
57.349
30.019
1.00
21.65


C


ATOM
1620
C
VAL
A
335
70.836
57.522
31.417
1.00
22.93


C


ATOM
1621
O
VAL
A
335
70.561
56.739
32.327
1.00
22.43


O


ATOM
1622
CB
VAL
A
335
71.360
56.864
29.062
1.00
23.64


C


ATOM
1623
CG1
VAL
A
335
72.090
55.646
29.664
1.00
22.43


C


ATOM
1624
CG2
VAL
A
335
70.750
56.502
27.712
1.00
22.06


C


ATOM
1625
N
ILE
A
336
71.644
58.562
31.590
1.00
22.47


N


ATOM
1626
CA
ILE
A
336
72.275
58.816
32.879
1.00
22.53


C


ATOM
1627
C
ILE
A
336
71.251
58.936
34.005
1.00
23.00


C


ATOM
1628
O
ILE
A
336
71.418
58.363
35.087
1.00
21.54


O


ATOM
1629
CB
ILE
A
336
73.132
60.097
32.810
1.00
22.52


C


ATOM
1630
CG1
ILE
A
336
74.304
59.869
31.846
1.00
21.96


C


ATOM
1631
CG2
ILE
A
336
73.639
60.476
34.199
1.00
23.53


C


ATOM
1632
CD1
ILE
A
336
75.114
61.125
31.544
1.00
24.57


C


ATOM
1633
N
ASP
A
337
70.183
59.679
33.745
1.00
23.52


N


ATOM
1634
CA
ASP
A
337
69.146
59.880
34.750
1.00
23.90


C


ATOM
1635
C
ASP
A
337
68.406
58.575
35.066
1.00
23.59


C


ATOM
1636
O
ASP
A
337
68.220
58.212
36.234
1.00
22.64


O


ATOM
1637
CB
ASP
A
337
68.153
60.931
34.251
1.00
26.45


C


ATOM
1638
CG
ASP
A
337
67.150
61.326
35.301
1.00
28.83


C


ATOM
1639
OD1
ASP
A
337
65.975
61.536
34.943
1.00
30.37


O


ATOM
1640
OD2
ASP
A
337
67.539
61.437
36.483
1.00
32.41


O


ATOM
1641
N
VAL
A
338
67.982
57.870
34.024
1.00
22.38


N


ATOM
1642
CA
VAL
A
338
67.258
56.619
34.221
1.00
23.04


C


ATOM
1643
C
VAL
A
338
68.116
55.587
34.949
1.00
23.56


C


ATOM
1644
O
VAL
A
338
67.635
54.899
35.852
1.00
23.29


O


ATOM
1645
CB
VAL
A
338
66.776
56.030
32.875
1.00
22.58


C


ATOM
1646
CG1
VAL
A
338
66.198
54.625
33.089
1.00
21.84


C


ATOM
1647
CG2
VAL
A
338
65.707
56.941
32.269
1.00
21.24


C


ATOM
1648
N
VAL
A
339
69.383
55.489
34.559
1.00
23.76


N


ATOM
1649
CA
VAL
A
339
70.292
54.542
35.189
1.00
23.00


C


ATOM
1650
C
VAL
A
339
70.446
54.832
36.682
1.00
24.41


C


ATOM
1651
O
VAL
A
339
70.499
53.906
37.496
1.00
23.06


O


ATOM
1652
CB
VAL
A
339
71.677
54.563
34.497
1.00
23.80


C


ATOM
1653
CG1
VAL
A
339
72.729
53.905
35.382
1.00
22.59


C


ATOM
1654
CG2
VAL
A
339
71.588
53.822
33.164
1.00
22.47


C


ATOM
1655
N
ALA
A
340
70.512
56.110
37.045
1.00
23.21


N


ATOM
1656
CA
ALA
A
340
70.644
56.478
38.452
1.00
24.61


C


ATOM
1657
C
ALA
A
340
69.413
55.992
39.214
1.00
25.25


C


ATOM
1658
O
ALA
A
340
69.520
55.462
40.326
1.00
24.89


O


ATOM
1659
CB
ALA
A
340
70.783
57.992
38.591
1.00
25.22


C


ATOM
1660
N
GLU
A
341
68.243
56.168
38.608
1.00
24.78


N


ATOM
1661
CA
GLU
A
341
66.995
55.749
39.237
1.00
25.88


C


ATOM
1662
C
GLU
A
341
66.917
54.228
39.310
1.00
25.65


C


ATOM
1663
O
GLU
A
341
66.422
53.672
40.291
1.00
25.06


O


ATOM
1664
CB
GLU
A
341
65.799
56.283
38.449
1.00
26.19


C


ATOM
1665
CG
GLU
A
341
64.465
56.213
39.194
1.00
30.02


C


ATOM
1666
CD
GLU
A
341
64.419
57.128
40.411
1.00
33.39


C


ATOM
1667
OE1
GLU
A
341
64.983
58.241
40.350
1.00
35.47


O


ATOM
1668
OE2
GLU
A
341
63.804
56.744
41.424
1.00
35.11


O


ATOM
1669
N
ARG
A
342
67.403
53.566
38.265
1.00
25.58


N


ATOM
1670
CA
ARG
A
342
67.399
52.106
38.198
1.00
25.78


C


ATOM
1671
C
ARG
A
342
68.295
51.531
39.300
1.00
25.93


C


ATOM
1672
O
ARG
A
342
67.952
50.528
39.932
1.00
26.38


O


ATOM
1673
CB
ARG
A
342
67.878
51.651
36.803
1.00
24.64


C


ATOM
1674
CG
ARG
A
342
67.855
50.138
36.546
1.00
24.33


C


ATOM
1675
CD
ARG
A
342
69.100
49.431
37.092
1.00
23.54


C


ATOM
1676
NE
ARG
A
342
70.350
49.884
36.477
1.00
22.90


N


ATOM
1677
CZ
ARG
A
342
70.718
49.640
35.220
1.00
23.00


C


ATOM
1678
NH1
ARG
A
342
69.934
48.943
34.406
1.00
21.73


N


ATOM
1679
NH2
ARG
A
342
71.893
50.075
34.778
1.00
23.48


N


ATOM
1680
N
ASN
A
343
69.440
52.166
39.534
1.00
25.49


N


ATOM
1681
CA
ASN
A
343
70.355
51.697
40.571
1.00
27.07


C


ATOM
1682
C
ASN
A
343
69.774
51.944
41.964
1.00
27.92


C


ATOM
1683
O
ASN
A
343
69.976
51.150
42.887
1.00
27.27


O


ATOM
1684
CB
ASN
A
343
71.722
52.373
40.422
1.00
27.28


C


ATOM
1685
CG
ASN
A
343
72.457
51.921
39.171
1.00
28.20


C


ATOM
1686
OD1
ASN
A
343
72.178
50.844
38.634
1.00
27.39


O


ATOM
1687
ND2
ASN
A
343
73.412
52.728
38.712
1.00
27.58


N


ATOM
1688
N
LYS
A
344
69.042
53.044
42.108
1.00
27.67


N


ATOM
1689
CA
LYS
A
344
68.402
53.376
43.374
1.00
29.76


C


ATOM
1690
C
LYS
A
344
67.313
52.334
43.617
1.00
29.60


C


ATOM
1691
O
LYS
A
344
67.162
51.810
44.726
1.00
30.86


O


ATOM
1692
CB
LYS
A
344
67.790
54.780
43.290
1.00
31.91


C


ATOM
1693
CG
LYS
A
344
67.158
55.286
44.574
1.00
37.21


C


ATOM
1694
CD
LYS
A
344
66.732
56.745
44.414
1.00
40.26


C


ATOM
1695
CE
LYS
A
344
66.241
57.339
45.725
1.00
42.77


C


ATOM
1696
NZ
LYS
A
344
66.010
58.812
45.594
1.00
44.75


N


ATOM
1697
N
TYR
A
345
66.564
52.023
42.564
1.00
28.67


N


ATOM
1698
CA
TYR
A
345
65.491
51.034
42.640
1.00
28.68


C


ATOM
1699
C
TYR
A
345
66.042
49.669
43.064
1.00
29.72


C


ATOM
1700
O
TYR
A
345
65.456
48.977
43.902
1.00
29.46


O


ATOM
1701
CB
TYR
A
345
64.816
50.896
41.280
1.00
27.98


C


ATOM
1702
CG
TYR
A
345
63.497
50.163
41.314
1.00
28.95


C


ATOM
1703
CD1
TYR
A
345
62.325
50.822
41.684
1.00
30.04


C


ATOM
1704
CD2
TYR
A
345
63.412
48.821
40.945
1.00
29.16


C


ATOM
1705
CE1
TYR
A
345
61.099
50.165
41.677
1.00
30.92


C


ATOM
1706
CE2
TYR
A
345
62.189
48.154
40.937
1.00
30.52


C


ATOM
1707
CZ
TYR
A
345
61.039
48.837
41.300
1.00
31.09


C


ATOM
1708
OH
TYR
A
345
59.820
48.205
41.256
1.00
32.41


O


ATOM
1709
N
PHE
A
346
67.162
49.281
42.467
1.00
29.90


N


ATOM
1710
CA
PHE
A
346
67.795
48.003
42.784
1.00
31.06


C


ATOM
1711
C
PHE
A
346
68.170
47.932
44.262
1.00
32.66


C


ATOM
1712
O
PHE
A
346
67.958
46.913
44.918
1.00
32.46


O


ATOM
1713
CB
PHE
A
346
69.051
47.814
41.932
1.00
30.74


C


ATOM
1714
CG
PHE
A
346
69.844
46.589
42.287
1.00
31.11


C


ATOM
1715
CD1
PHE
A
346
69.329
45.319
42.053
1.00
29.91


C


ATOM
1716
CD2
PHE
A
346
71.107
46.708
42.861
1.00
32.41


C


ATOM
1717
CE1
PHE
A
346
70.061
44.177
42.383
1.00
30.76


C


ATOM
1718
CE2
PHE
A
346
71.850
45.572
43.197
1.00
33.67


C


ATOM
1719
CZ
PHE
A
346
71.321
44.303
42.954
1.00
32.41


C


ATOM
1720
N
GLU
A
347
68.726
49.021
44.782
1.00
33.10


N


ATOM
1721
CA
GLU
A
347
69.130
49.072
46.182
1.00
36.04


C


ATOM
1722
C
GLU
A
347
67.933
49.020
47.127
1.00
35.98


C


ATOM
1723
O
GLU
A
347
68.032
48.491
48.235
1.00
35.44


O


ATOM
1724
CB
GLU
A
347
69.947
50.340
46.448
1.00
37.89


C


ATOM
1725
CG
GLU
A
347
71.259
50.392
45.672
1.00
42.81


C


ATOM
1726
CD
GLU
A
347
72.257
49.319
46.102
1.00
46.57


C


ATOM
1727
OE1
GLU
A
347
73.243
49.099
45.363
1.00
48.05


O


ATOM
1728
OE2
GLU
A
347
72.071
48.702
47.177
1.00
48.54


O


ATOM
1729
N
GLU
A
348
66.802
49.560
46.687
1.00
35.06


N


ATOM
1730
CA
GLU
A
348
65.603
49.579
47.513
1.00
35.70


C


ATOM
1731
C
GLU
A
348
64.834
48.261
47.511
1.00
35.13


C


ATOM
1732
O
GLU
A
348
64.349
47.817
48.551
1.00
34.62


O


ATOM
1733
CB
GLU
A
348
64.633
50.671
47.043
1.00
37.06


C


ATOM
1734
CG
GLU
A
348
65.237
52.044
46.812
1.00
39.63


C


ATOM
1735
CD
GLU
A
348
64.207
53.056
46.324
1.00
40.78


C


ATOM
1736
OE1
GLU
A
348
63.274
52.662
45.592
1.00
40.73


O


ATOM
1737
OE2
GLU
A
348
64.340
54.251
46.660
1.00
43.08


O


ATOM
1738
N
THR
A
349
64.727
47.640
46.342
1.00
33.88


N


ATOM
1739
CA
THR
A
349
63.948
46.415
46.187
1.00
33.76


C


ATOM
1740
C
THR
A
349
64.713
45.121
45.922
1.00
33.08


C


ATOM
1741
O
THR
A
349
64.136
44.040
46.007
1.00
33.38


O


ATOM
1742
CB
THR
A
349
62.955
46.567
45.029
1.00
33.48


C


ATOM
1743
OG1
THR
A
349
63.686
46.612
43.794
1.00
32.62


O


ATOM
1744
CG2
THR
A
349
62.147
47.859
45.173
1.00
33.82


C


ATOM
1745
N
GLY
A
350
65.991
45.227
45.584
1.00
32.81


N


ATOM
1746
CA
GLY
A
350
66.762
44.035
45.283
1.00
31.80


C


ATOM
1747
C
GLY
A
350
66.481
43.557
43.865
1.00
31.19


C


ATOM
1748
O
GLY
A
350
66.976
42.515
43.440
1.00
31.53


O


ATOM
1749
N
ILE
A
351
65.687
44.327
43.125
1.00
30.11


N


ATOM
1750
CA
ILE
A
351
65.338
43.982
41.749
1.00
28.23


C


ATOM
1751
C
ILE
A
351
66.182
44.775
40.751
1.00
26.97


C


ATOM
1752
O
ILE
A
351
66.188
46.005
40.780
1.00
25.49


O


ATOM
1753
CB
ILE
A
351
63.859
44.308
41.442
1.00
30.29


C


ATOM
1754
CG1
ILE
A
351
62.934
43.608
42.442
1.00
31.76


C


ATOM
1755
CG2
ILE
A
351
63.533
43.901
40.008
1.00
30.03


C


ATOM
1756
CD1
ILE
A
351
61.497
44.104
42.383
1.00
33.25


C


ATOM
1757
N
TYR
A
352
66.888
44.075
39.872
1.00
25.98


N


ATOM
1758
CA
TYR
A
352
67.699
44.747
38.862
1.00
25.54


C


ATOM
1759
C
TYR
A
352
66.955
44.707
37.541
1.00
25.29


C


ATOM
1760
O
TYR
A
352
66.696
43.631
37.002
1.00
24.79


O


ATOM
1761
CB
TYR
A
352
69.055
44.064
38.674
1.00
26.27


C


ATOM
1762
CG
TYR
A
352
69.950
44.807
37.696
1.00
25.26


C


ATOM
1763
CD1
TYR
A
352
70.741
45.873
38.122
1.00
25.87


C


ATOM
1764
CD2
TYR
A
352
69.983
44.464
36.342
1.00
26.91


C


ATOM
1765
CE1
TYR
A
352
71.545
46.578
37.235
1.00
25.26


C


ATOM
1766
CE2
TYR
A
352
70.788
45.172
35.436
1.00
26.20


C


ATOM
1767
CZ
TYR
A
352
71.568
46.226
35.895
1.00
25.73


C


ATOM
1768
OH
TYR
A
352
72.394
46.918
35.030
1.00
24.57


O


ATOM
1769
N
ILE
A
353
66.623
45.884
37.016
1.00
24.76


N


ATOM
1770
CA
ILE
A
353
65.906
45.984
35.754
1.00
24.38


C


ATOM
1771
C
ILE
A
353
66.813
46.507
34.648
1.00
24.63


C


ATOM
1772
O
ILE
A
353
67.263
47.652
34.695
1.00
23.98


O


ATOM
1773
CB
ILE
A
353
64.697
46.939
35.877
1.00
25.07


C


ATOM
1774
CG1
ILE
A
353
63.745
46.435
36.974
1.00
25.69


C


ATOM
1775
CG2
ILE
A
353
63.977
47.030
34.531
1.00
24.50


C


ATOM
1776
CD1
ILE
A
353
62.534
47.308
37.205
1.00
25.89


C


ATOM
1777
N
PRO
A
354
67.111
45.667
33.642
1.00
24.90


N


ATOM
1778
CA
PRO
A
354
67.974
46.100
32.537
1.00
24.20


C


ATOM
1779
C
PRO
A
354
67.311
47.244
31.779
1.00
24.12


C


ATOM
1780
O
PRO
A
354
66.089
47.268
31.641
1.00
24.10


O


ATOM
1781
CB
PRO
A
354
68.085
44.846
31.669
1.00
24.27


C


ATOM
1782
CG
PRO
A
354
67.941
43.720
32.681
1.00
23.16


C


ATOM
1783
CD
PRO
A
354
66.802
44.229
33.536
1.00
24.40


C


ATOM
1784
N
VAL
A
355
68.109
48.191
31.295
1.00
23.66


N


ATOM
1785
CA
VAL
A
355
67.556
49.298
30.526
1.00
22.79


C


ATOM
1786
C
VAL
A
355
68.210
49.322
29.158
1.00
23.11


C


ATOM
1787
O
VAL
A
355
69.359
48.916
28.990
1.00
22.38


O


ATOM
1788
CB
VAL
A
355
67.735
50.671
31.239
1.00
22.02


C


ATOM
1789
CG1
VAL
A
355
66.979
50.665
32.555
1.00
22.53


C


ATOM
1790
CG2
VAL
A
355
69.209
50.981
31.456
1.00
20.21


C


ATOM
1791
N
CYS
A
356
67.454
49.794
28.178
1.00
23.23


N


ATOM
1792
CA
CYS
A
356
67.906
49.842
26.802
1.00
23.04


C


ATOM
1793
C
CYS
A
356
67.981
51.272
26.287
1.00
23.29


C


ATOM
1794
O
CYS
A
356
67.023
52.025
26.414
1.00
22.76


O


ATOM
1795
CB
CYS
A
356
66.924
49.035
25.940
1.00
25.03


C


ATOM
1796
SG
CYS
A
356
67.126
49.192
24.147
1.00
25.41


S


ATOM
1797
N
SER
A
357
69.126
51.647
25.727
1.00
22.98


N


ATOM
1798
CA
SER
A
357
69.268
52.975
25.148
1.00
22.85


C


ATOM
1799
C
SER
A
357
68.771
52.806
23.718
1.00
23.16


C


ATOM
1800
O
SER
A
357
69.398
52.122
22.913
1.00
22.80


O


ATOM
1801
CB
SER
A
357
70.724
53.428
25.138
1.00
21.98


C


ATOM
1802
OG
SER
A
357
70.813
54.733
24.584
1.00
23.23


O


ATOM
1803
N
ASP
A
358
67.646
53.441
23.417
1.00
22.79


N


ATOM
1804
CA
ASP
A
358
67.020
53.333
22.109
1.00
24.60


C


ATOM
1805
C
ASP
A
358
67.090
54.614
21.279
1.00
25.62


C


ATOM
1806
O
ASP
A
358
66.466
55.616
21.617
1.00
25.58


O


ATOM
1807
CB
ASP
A
358
65.560
52.900
22.314
1.00
24.15


C


ATOM
1808
CG
ASP
A
358
64.776
52.816
21.026
1.00
25.77


C


ATOM
1809
OD1
ASP
A
358
65.394
52.717
19.943
1.00
25.59


O


ATOM
1810
OD2
ASP
A
358
63.530
52.833
21.111
1.00
25.33


O


ATOM
1811
N
GLY
A
359
67.860
54.562
20.193
1.00
28.47


N


ATOM
1812
CA
GLY
A
359
67.989
55.702
19.302
1.00
30.93


C


ATOM
1813
C
GLY
A
359
69.129
56.657
19.604
1.00
33.00


C


ATOM
1814
O
GLY
A
359
69.679
56.665
20.706
1.00
33.66


O


ATOM
1815
N
GLY
A
360
69.490
57.463
18.610
1.00
34.46


N


ATOM
1816
CA
GLY
A
360
70.551
58.434
18.793
1.00
35.68


C


ATOM
1817
C
GLY
A
360
71.968
57.960
18.533
1.00
36.49


C


ATOM
1818
O
GLY
A
360
72.905
58.740
18.671
1.00
38.41


O


ATOM
1819
N
ILE
A
361
72.146
56.696
18.169
1.00
36.80


N


ATOM
1820
CA
ILE
A
361
73.486
56.186
17.895
1.00
37.13


C


ATOM
1821
C
ILE
A
361
73.885
56.609
16.483
1.00
38.00


C


ATOM
1822
O
ILE
A
361
73.275
56.173
15.506
1.00
37.36


O


ATOM
1823
CB
ILE
A
361
73.543
54.640
17.980
1.00
37.20


C


ATOM
1824
CG1
ILE
A
361
73.123
54.166
19.377
1.00
36.99


C


ATOM
1825
CG2
ILE
A
361
74.951
54.153
17.666
1.00
37.15


C


ATOM
1826
CD1
ILE
A
361
74.050
54.607
20.493
1.00
36.40


C


ATOM
1827
N
VAL
A
362
74.898
57.466
16.384
1.00
37.48


N


ATOM
1828
CA
VAL
A
362
75.373
57.940
15.088
1.00
38.82


C


ATOM
1829
C
VAL
A
362
76.707
57.292
14.735
1.00
38.61


C


ATOM
1830
O
VAL
A
362
76.916
56.862
13.599
1.00
39.64


O


ATOM
1831
CB
VAL
A
362
75.548
59.473
15.082
1.00
39.34


C


ATOM
1832
CG1
VAL
A
362
76.006
59.946
13.701
1.00
41.47


C


ATOM
1833
CG2
VAL
A
362
74.241
60.142
15.458
1.00
40.61


C


ATOM
1834
N
TYR
A
363
77.600
57.215
15.719
1.00
37.19


N


ATOM
1835
CA
TYR
A
363
78.921
56.624
15.530
1.00
36.38


C


ATOM
1836
C
TYR
A
363
79.131
55.425
16.447
1.00
34.11


C


ATOM
1837
O
TYR
A
363
78.471
55.303
17.477
1.00
32.33


O


ATOM
1838
CB
TYR
A
363
80.004
57.661
15.820
1.00
39.61


C


ATOM
1839
CG
TYR
A
363
79.918
58.894
14.957
1.00
43.43


C


ATOM
1840
CD1
TYR
A
363
79.948
58.795
13.565
1.00
45.21


C


ATOM
1841
CD2
TYR
A
363
79.824
60.162
15.527
1.00
44.88


C


ATOM
1842
CE1
TYR
A
363
79.889
59.933
12.761
1.00
47.51


C


ATOM
1843
CE2
TYR
A
363
79.766
61.308
14.731
1.00
47.32


C


ATOM
1844
CZ
TYR
A
363
79.800
61.184
13.351
1.00
47.96


C


ATOM
1845
OH
TYR
A
363
79.755
62.310
12.556
1.00
49.68


O


ATOM
1846
N
ASP
A
364
80.059
54.548
16.079
1.00
32.88


N


ATOM
1847
CA
ASP
A
364
80.341
53.375
16.899
1.00
32.27


C


ATOM
1848
C
ASP
A
364
80.649
53.733
18.352
1.00
30.99


C


ATOM
1849
O
ASP
A
364
80.189
53.050
19.266
1.00
31.26


O


ATOM
1850
CB
ASP
A
364
81.531
52.574
16.351
1.00
34.38


C


ATOM
1851
CG
ASP
A
364
81.224
51.867
15.040
1.00
36.34


C


ATOM
1852
OD1
ASP
A
364
80.081
51.396
14.850
1.00
37.26


O


ATOM
1853
OD2
ASP
A
364
82.147
51.767
14.205
1.00
37.51


O


ATOM
1854
N
TYR
A
365
81.421
54.796
18.576
1.00
29.18


N


ATOM
1855
CA
TYR
A
365
81.776
55.153
19.949
1.00
27.62


C


ATOM
1856
C
TYR
A
365
80.571
55.537
20.796
1.00
27.21


C


ATOM
1857
O
TYR
A
365
80.638
55.497
22.019
1.00
25.96


O


ATOM
1858
CB
TYR
A
365
82.846
56.257
19.982
1.00
28.21


C


ATOM
1859
CG
TYR
A
365
82.351
57.679
19.854
1.00
29.19


C


ATOM
1860
CD1
TYR
A
365
82.157
58.483
20.983
1.00
30.31


C


ATOM
1861
CD2
TYR
A
365
82.135
58.242
18.602
1.00
30.72


C


ATOM
1862
CE1
TYR
A
365
81.765
59.824
20.854
1.00
31.27


C


ATOM
1863
CE2
TYR
A
365
81.746
59.568
18.464
1.00
32.19


C


ATOM
1864
CZ
TYR
A
365
81.565
60.353
19.587
1.00
32.87


C


ATOM
1865
OH
TYR
A
365
81.178
61.664
19.418
1.00
35.54


O


ATOM
1866
N
HIS
A
366
79.465
55.896
20.149
1.00
25.79


N


ATOM
1867
CA
HIS
A
366
78.253
56.229
20.888
1.00
26.00


C


ATOM
1868
C
HIS
A
366
77.757
54.963
21.582
1.00
25.36


C


ATOM
1869
O
HIS
A
366
77.091
55.035
22.616
1.00
24.64


O


ATOM
1870
CB
HIS
A
366
77.160
56.760
19.956
1.00
26.79


C


ATOM
1871
CG
HIS
A
366
77.409
58.148
19.455
1.00
28.37


C


ATOM
1872
ND1
HIS
A
366
78.402
58.958
19.963
1.00
29.63


N


ATOM
1873
CD2
HIS
A
366
76.774
58.880
18.510
1.00
28.28


C


ATOM
1874
CE1
HIS
A
366
78.368
60.129
19.352
1.00
27.78


C


ATOM
1875
NE2
HIS
A
366
77.390
60.108
18.466
1.00
29.94


N


ATOM
1876
N
MET
A
367
78.067
53.803
21.000
1.00
24.84


N


ATOM
1877
CA
MET
A
367
77.663
52.530
21.602
1.00
25.78


C


ATOM
1878
C
MET
A
367
78.401
52.385
22.927
1.00
24.73


C


ATOM
1879
O
MET
A
367
77.816
52.063
23.950
1.00
23.39


O


ATOM
1880
CB
MET
A
367
78.035
51.343
20.704
1.00
26.59


C


ATOM
1881
CG
MET
A
367
77.291
51.272
19.369
1.00
30.31


C


ATOM
1882
SD
MET
A
367
77.849
49.839
18.398
1.00
32.89


S


ATOM
1883
CE
MET
A
367
77.037
50.144
16.824
1.00
32.21


C


ATOM
1884
N
THR
A
368
79.707
52.611
22.881
1.00
24.71


N


ATOM
1885
CA
THR
A
368
80.547
52.510
24.064
1.00
24.03


C


ATOM
1886
C
THR
A
368
80.063
53.484
25.135
1.00
23.45


C


ATOM
1887
O
THR
A
368
79.985
53.133
26.306
1.00
23.07


O


ATOM
1888
CB
THR
A
368
82.006
52.816
23.701
1.00
24.76


C


ATOM
1889
OG1
THR
A
368
82.349
52.081
22.518
1.00
24.31


O


ATOM
1890
CG2
THR
A
368
82.942
52.411
24.835
1.00
24.75


C


ATOM
1891
N
LEU
A
369
79.744
54.710
24.731
1.00
23.16


N


ATOM
1892
CA
LEU
A
369
79.249
55.722
25.666
1.00
24.00


C


ATOM
1893
C
LEU
A
369
77.939
55.308
26.335
1.00
23.72


C


ATOM
1894
O
LEU
A
369
77.797
55.411
27.551
1.00
23.10


O


ATOM
1895
CB
LEU
A
369
79.033
57.057
24.947
1.00
24.17


C


ATOM
1896
CG
LEU
A
369
80.281
57.884
24.624
1.00
26.48


C


ATOM
1897
CD1
LEU
A
369
79.897
59.087
23.772
1.00
26.96


C


ATOM
1898
CD2
LEU
A
369
80.943
58.342
25.926
1.00
26.87


C


ATOM
1899
N
ALA
A
370
76.986
54.837
25.533
1.00
22.35


N


ATOM
1900
CA
ALA
A
370
75.686
54.424
26.056
1.00
23.03


C


ATOM
1901
C
ALA
A
370
75.857
53.331
27.108
1.00
22.11


C


ATOM
1902
O
ALA
A
370
75.228
53.361
28.162
1.00
22.10


O


ATOM
1903
CB
ALA
A
370
74.803
53.917
24.917
1.00
21.13


C


ATOM
1904
N
LEU
A
371
76.707
52.361
26.805
1.00
21.79


N


ATOM
1905
CA
LEU
A
371
76.960
51.261
27.726
1.00
22.39


C


ATOM
1906
C
LEU
A
371
77.685
51.777
28.972
1.00
21.96


C


ATOM
1907
O
LEU
A
371
77.355
51.399
30.098
1.00
21.20


O


ATOM
1908
CB
LEU
A
371
77.803
50.186
27.030
1.00
21.70


C


ATOM
1909
CG
LEU
A
371
77.170
49.473
25.820
1.00
22.99


C


ATOM
1910
CD1
LEU
A
371
78.221
48.634
25.112
1.00
24.60


C


ATOM
1911
CD2
LEU
A
371
76.009
48.591
26.270
1.00
23.11


C


ATOM
1912
N
ALA
A
372
78.680
52.636
28.770
1.00
21.79


N


ATOM
1913
CA
ALA
A
372
79.437
53.182
29.894
1.00
21.89


C


ATOM
1914
C
ALA
A
372
78.534
53.993
30.812
1.00
23.49


C


ATOM
1915
O
ALA
A
372
78.720
54.004
32.032
1.00
22.41


O


ATOM
1916
CB
ALA
A
372
80.585
54.052
29.387
1.00
22.98


C


ATOM
1917
N
MET
A
373
77.550
54.675
30.231
1.00
22.86


N


ATOM
1918
CA
MET
A
373
76.632
55.471
31.039
1.00
23.45


C


ATOM
1919
C
MET
A
373
75.650
54.609
31.829
1.00
23.67


C


ATOM
1920
O
MET
A
373
74.913
55.119
32.665
1.00
24.88


O


ATOM
1921
CB
MET
A
373
75.884
56.474
30.159
1.00
23.86


C


ATOM
1922
CG
MET
A
373
76.792
57.571
29.612
1.00
25.21


C


ATOM
1923
SD
MET
A
373
75.984
58.618
28.385
1.00
26.48


S


ATOM
1924
CE
MET
A
373
77.324
59.787
28.016
1.00
26.43


C


ATOM
1925
N
GLY
A
374
75.635
53.302
31.572
1.00
23.45


N


ATOM
1926
CA
GLY
A
374
74.745
52.443
32.332
1.00
22.34


C


ATOM
1927
C
GLY
A
374
73.740
51.597
31.573
1.00
22.77


C


ATOM
1928
O
GLY
A
374
73.118
50.714
32.162
1.00
23.42


O


ATOM
1929
N
ALA
A
375
73.560
51.851
30.283
1.00
22.25


N


ATOM
1930
CA
ALA
A
375
72.614
51.051
29.509
1.00
22.62


C


ATOM
1931
C
ALA
A
375
73.143
49.625
29.389
1.00
23.21


C


ATOM
1932
O
ALA
A
375
74.329
49.416
29.134
1.00
23.32


O


ATOM
1933
CB
ALA
A
375
72.418
51.652
28.120
1.00
22.37


C


ATOM
1934
N
ASP
A
376
72.263
48.645
29.580
1.00
22.37


N


ATOM
1935
CA
ASP
A
376
72.661
47.244
29.478
1.00
23.13


C


ATOM
1936
C
ASP
A
376
72.750
46.840
28.012
1.00
23.56


C


ATOM
1937
O
ASP
A
376
73.624
46.064
27.624
1.00
23.83


O


ATOM
1938
CB
ASP
A
376
71.665
46.377
30.241
1.00
23.78


C


ATOM
1939
CG
ASP
A
376
71.596
46.756
31.706
1.00
24.06


C


ATOM
1940
OD1
ASP
A
376
72.420
46.246
32.499
1.00
25.54


O


ATOM
1941
OD2
ASP
A
376
70.734
47.586
32.062
1.00
23.75


O


ATOM
1942
N
PHE
A
377
71.841
47.355
27.193
1.00
23.34


N


ATOM
1943
CA
PHE
A
377
71.904
47.076
25.768
1.00
23.57


C


ATOM
1944
C
PHE
A
377
71.414
48.262
24.948
1.00
23.98


C


ATOM
1945
O
PHE
A
377
70.882
49.228
25.490
1.00
23.49


O


ATOM
1946
CB
PHE
A
377
71.168
45.778
25.385
1.00
23.30


C


ATOM
1947
CG
PHE
A
377
69.758
45.684
25.887
1.00
24.76


C


ATOM
1948
CD1
PHE
A
377
69.495
45.318
27.203
1.00
26.77


C


ATOM
1949
CD2
PHE
A
377
68.688
45.900
25.025
1.00
24.49


C


ATOM
1950
CE1
PHE
A
377
68.180
45.163
27.652
1.00
26.00


C


ATOM
1951
CE2
PHE
A
377
67.370
45.747
25.465
1.00
25.78


C


ATOM
1952
CZ
PHE
A
377
67.118
45.379
26.777
1.00
25.44


C


ATOM
1953
N
ILE
A
378
71.610
48.181
23.639
1.00
23.02


N


ATOM
1954
CA
ILE
A
378
71.278
49.271
22.738
1.00
23.35


C


ATOM
1955
C
ILE
A
378
70.335
48.846
21.621
1.00
23.49


C


ATOM
1956
O
ILE
A
378
70.502
47.778
21.045
1.00
24.62


O


ATOM
1957
CB
ILE
A
378
72.592
49.816
22.107
1.00
23.26


C


ATOM
1958
CG1
ILE
A
378
73.571
50.202
23.227
1.00
24.03


C


ATOM
1959
CG2
ILE
A
378
72.306
51.011
21.192
1.00
24.70


C


ATOM
1960
CD1
ILE
A
378
75.017
50.325
22.756
1.00
26.63


C


ATOM
1961
N
MET
A
379
69.335
49.675
21.331
1.00
23.56


N


ATOM
1962
CA
MET
A
379
68.418
49.374
20.238
1.00
23.95


C


ATOM
1963
C
MET
A
379
68.755
50.340
19.109
1.00
24.40


C


ATOM
1964
O
MET
A
379
68.915
51.540
19.338
1.00
23.43


O


ATOM
1965
CB
MET
A
379
66.952
49.551
20.661
1.00
24.65


C


ATOM
1966
CG
MET
A
379
65.968
49.319
19.508
1.00
24.74


C


ATOM
1967
SD
MET
A
379
64.236
49.290
19.988
1.00
26.39


S


ATOM
1968
CE
MET
A
379
64.115
47.609
20.644
1.00
27.00


C


ATOM
1969
N
LEU
A
380
68.881
49.815
17.896
1.00
24.73


N


ATOM
1970
CA
LEU
A
380
69.216
50.642
16.744
1.00
25.39


C


ATOM
1971
C
LEU
A
380
68.334
50.345
15.545
1.00
25.28


C


ATOM
1972
O
LEU
A
380
67.952
49.197
15.316
1.00
25.31


O


ATOM
1973
CB
LEU
A
380
70.673
50.421
16.329
1.00
26.35


C


ATOM
1974
CG
LEU
A
380
71.756
50.577
17.403
1.00
27.26


C


ATOM
1975
CD1
LEU
A
380
71.877
49.280
18.189
1.00
29.84


C


ATOM
1976
CD2
LEU
A
380
73.081
50.896
16.740
1.00
28.50


C


ATOM
1977
N
GLY
A
381
68.034
51.388
14.778
1.00
25.23


N


ATOM
1978
CA
GLY
A
381
67.221
51.232
13.584
1.00
27.24


C


ATOM
1979
C
GLY
A
381
68.057
51.437
12.331
1.00
27.95


C


ATOM
1980
O
GLY
A
381
68.330
50.493
11.592
1.00
28.13


O


ATOM
1981
N
ARG
A
382
68.473
52.680
12.107
1.00
29.76


N


ATOM
1982
CA
ARG
A
382
69.279
53.061
10.945
1.00
31.76


C


ATOM
1983
C
ARG
A
382
70.494
52.150
10.748
1.00
32.08


C


ATOM
1984
O
ARG
A
382
70.778
51.702
9.632
1.00
30.90


O


ATOM
1985
CB
ARG
A
382
69.744
54.510
11.109
1.00
34.27


C


ATOM
1986
CG
ARG
A
382
70.563
55.063
9.952
1.00
39.22


C


ATOM
1987
CD
ARG
A
382
71.207
56.388
10.339
1.00
42.02


C


ATOM
1988
NE
ARG
A
382
72.131
56.221
11.460
1.00
45.45


N


ATOM
1989
CZ
ARG
A
382
73.260
55.518
11.399
1.00
47.01


C


ATOM
1990
NH1
ARG
A
382
73.610
54.920
10.267
1.00
48.07


N


ATOM
1991
NH2
ARG
A
382
74.033
55.399
12.471
1.00
47.88


N


ATOM
1992
N
TYR
A
383
71.208
51.883
11.838
1.00
30.72


N


ATOM
1993
CA
TYR
A
383
72.395
51.032
11.804
1.00
30.04


C


ATOM
1994
C
TYR
A
383
72.136
49.699
11.098
1.00
29.56


C


ATOM
1995
O
TYR
A
383
72.922
49.272
10.252
1.00
30.58


O


ATOM
1996
CB
TYR
A
383
72.876
50.761
13.234
1.00
29.03


C


ATOM
1997
CG
TYR
A
383
74.100
49.878
13.329
1.00
28.59


C


ATOM
1998
CD1
TYR
A
383
75.381
50.413
13.201
1.00
29.36


C


ATOM
1999
CD2
TYR
A
383
73.975
48.505
13.538
1.00
28.86


C


ATOM
2000
CE1
TYR
A
383
76.509
49.602
13.280
1.00
29.26


C


ATOM
2001
CE2
TYR
A
383
75.097
47.683
13.617
1.00
28.40


C


ATOM
2002
CZ
TYR
A
383
76.360
48.240
13.486
1.00
28.60


C


ATOM
2003
OH
TYR
A
383
77.475
47.437
13.551
1.00
28.39


O


ATOM
2004
N
PHE
A
384
71.034
49.048
11.452
1.00
29.09


N


ATOM
2005
CA
PHE
A
384
70.679
47.757
10.872
1.00
29.81


C


ATOM
2006
C
PHE
A
384
69.991
47.843
9.510
1.00
30.44


C


ATOM
2007
O
PHE
A
384
70.102
46.922
8.701
1.00
30.80


O


ATOM
2008
CB
PHE
A
384
69.785
46.976
11.842
1.00
29.45


C


ATOM
2009
CG
PHE
A
384
70.511
46.460
13.057
1.00
28.89


C


ATOM
2010
CD1
PHE
A
384
71.469
45.455
12.936
1.00
28.54


C


ATOM
2011
CD2
PHE
A
384
70.237
46.980
14.322
1.00
28.04


C


ATOM
2012
CE1
PHE
A
384
72.146
44.973
14.054
1.00
28.18


C


ATOM
2013
CE2
PHE
A
384
70.905
46.506
15.446
1.00
27.99


C


ATOM
2014
CZ
PHE
A
384
71.864
45.500
15.313
1.00
27.33


C


ATOM
2015
N
ALA
A
385
69.286
48.940
9.258
1.00
31.37


N


ATOM
2016
CA
ALA
A
385
68.582
49.118
7.991
1.00
32.83


C


ATOM
2017
C
ALA
A
385
69.530
49.082
6.795
1.00
33.97


C


ATOM
2018
O
ALA
A
385
69.137
48.700
5.694
1.00
34.53


O


ATOM
2019
CB
ALA
A
385
67.815
50.433
8.004
1.00
31.76


C


ATOM
2020
N
ARG
A
386
70.779
49.482
7.018
1.00
35.25


N


ATOM
2021
CA
ARG
A
386
71.786
49.508
5.960
1.00
35.62


C


ATOM
2022
C
ARG
A
386
72.237
48.120
5.511
1.00
36.16


C


ATOM
2023
O
ARG
A
386
72.911
47.986
4.488
1.00
35.70


O


ATOM
2024
CB
ARG
A
386
73.027
50.272
6.428
1.00
36.74


C


ATOM
2025
CG
ARG
A
386
72.816
51.708
6.857
1.00
38.32


C


ATOM
2026
CD
ARG
A
386
74.090
52.191
7.536
1.00
40.83


C


ATOM
2027
NE
ARG
A
386
74.477
51.251
8.585
1.00
42.25


N


ATOM
2028
CZ
ARG
A
386
75.726
51.019
8.973
1.00
42.05


C


ATOM
2029
NH1
ARG
A
386
76.737
51.661
8.401
1.00
41.85


N


ATOM
2030
NH2
ARG
A
386
75.960
50.131
9.930
1.00
41.04


N


ATOM
2031
N
PHE
A
387
71.875
47.088
6.266
1.00
36.71


N


ATOM
2032
CA
PHE
A
387
72.309
45.740
5.928
1.00
37.28


C


ATOM
2033
C
PHE
A
387
71.442
44.973
4.938
1.00
38.78


C


ATOM
2034
O
PHE
A
387
70.249
45.233
4.779
1.00
38.34


O


ATOM
2035
CB
PHE
A
387
72.483
44.900
7.202
1.00
37.27


C


ATOM
2036
CG
PHE
A
387
73.397
45.524
8.222
1.00
36.45


C


ATOM
2037
CD1
PHE
A
387
74.507
46.263
7.826
1.00
36.98


C


ATOM
2038
CD2
PHE
A
387
73.152
45.364
9.584
1.00
36.75


C


ATOM
2039
CE1
PHE
A
387
75.362
46.838
8.771
1.00
36.90


C


ATOM
2040
CE2
PHE
A
387
73.998
45.931
10.536
1.00
35.15


C


ATOM
2041
CZ
PHE
A
387
75.104
46.670
10.130
1.00
36.18


C


ATOM
2042
N
GLU
A
388
72.081
44.013
4.280
1.00
39.94


N


ATOM
2043
CA
GLU
A
388
71.442
43.155
3.294
1.00
41.27


C


ATOM
2044
C
GLU
A
388
70.225
42.453
3.878
1.00
41.01


C


ATOM
2045
O
GLU
A
388
69.216
42.268
3.195
1.00
40.68


O


ATOM
2046
CB
GLU
A
388
72.453
42.111
2.809
1.00
42.64


C


ATOM
2047
CG
GLU
A
388
71.901
41.064
1.853
1.00
46.30


C


ATOM
2048
CD
GLU
A
388
71.435
41.660
0.542
1.00
47.81


C


ATOM
2049
OE1
GLU
A
388
72.184
42.474
−0.033
1.00
49.41


O


ATOM
2050
OE2
GLU
A
388
70.326
41.310
0.081
1.00
50.01


O


ATOM
2051
N
GLU
A
389
70.317
42.076
5.150
1.00
40.05


N


ATOM
2052
CA
GLU
A
389
69.230
41.365
5.807
1.00
39.60


C


ATOM
2053
C
GLU
A
389
68.002
42.182
6.200
1.00
39.15


C


ATOM
2054
O
GLU
A
389
67.006
41.605
6.628
1.00
38.91


O


ATOM
2055
CB
GLU
A
389
69.758
40.611
7.031
1.00
39.09


C


ATOM
2056
CG
GLU
A
389
70.789
39.544
6.685
1.00
38.57


C


ATOM
2057
CD
GLU
A
389
72.223
40.049
6.746
1.00
37.83


C


ATOM
2058
OE1
GLU
A
389
72.453
41.267
6.600
1.00
38.50


O


ATOM
2059
OE2
GLU
A
389
73.128
39.216
6.929
1.00
37.79


O


ATOM
2060
N
SER
A
390
68.057
43.505
6.080
1.00
39.34


N


ATOM
2061
CA
SER
A
390
66.879
44.303
6.417
1.00
41.26


C


ATOM
2062
C
SER
A
390
65.839
43.965
5.343
1.00
42.43


C


ATOM
2063
O
SER
A
390
66.193
43.713
4.192
1.00
42.09


O


ATOM
2064
CB
SER
A
390
67.194
45.799
6.408
1.00
40.53


C


ATOM
2065
OG
SER
A
390
67.514
46.256
5.111
1.00
44.02


O


ATOM
2066
N
PRO
A
391
64.547
43.961
5.707
1.00
43.44


N


ATOM
2067
CA
PRO
A
391
63.452
43.639
4.780
1.00
44.56


C


ATOM
2068
C
PRO
A
391
63.123
44.645
3.678
1.00
45.93


C


ATOM
2069
O
PRO
A
392
62.217
44.409
2.876
1.00
46.82


O


ATOM
2070
CB
PRO
A
391
62.273
43.423
5.722
1.00
44.41


C


ATOM
2071
CG
PRO
A
391
62.526
44.459
6.777
1.00
43.55


C


ATOM
2072
CD
PRO
A
391
64.018
44.320
7.036
1.00
42.66


C


ATOM
2073
N
THR
A
392
63.848
45.755
3.623
1.00
46.64


N


ATOM
2074
CA
THR
A
392
63.573
46.767
2.612
1.00
47.66


C


ATOM
2075
C
THR
A
392
64.258
46.479
1.282
1.00
49.02


C


ATOM
2076
O
THR
A
392
65.106
45.591
1.182
1.00
49.01


O


ATOM
2077
CB
THR
A
392
64.000
48.162
3.092
1.00
47.33


C


ATOM
2078
OG1
THR
A
392
65.419
48.188
3.286
1.00
47.34


O


ATOM
2079
CG2
THR
A
392
63.301
48.505
4.403
1.00
47.28


C


ATOM
2080
N
ARG
A
393
63.883
47.240
0.260
1.00
50.71


N


ATOM
2081
CA
ARG
A
393
64.456
47.061
−1.066
1.00
52.75


C


ATOM
2082
C
ARG
A
393
65.795
47.757
−1.219
1.00
53.23


C


ATOM
2083
O
ARG
A
393
65.993
48.876
−0.743
1.00
52.80


O


ATOM
2084
CB
ARG
A
393
63.513
47.595
−2.146
1.00
53.96


C


ATOM
2085
CG
ARG
A
393
62.189
46.865
−2.283
1.00
56.12


C


ATOM
2086
CD
ARG
A
393
61.493
47.344
−3.545
1.00
57.41


C


ATOM
2087
NE
ARG
A
393
61.452
48.802
−3.587
1.00
59.49


N


ATOM
2088
CZ
ARG
A
393
61.357
49.518
−4.702
1.00
60.61


C


ATOM
2089
NH1
ARG
A
393
61.291
48.913
−5.881
1.00
61.26


N


ATOM
2090
NH2
ARG
A
393
61.337
50.842
−4.636
1.00
61.38


N


ATOM
2091
N
LYS
A
394
66.713
47.077
−1.894
1.00
54.19


N


ATOM
2092
CA
LYS
A
394
68.031
47.621
−2.159
1.00
55.50


C


ATOM
2093
C
LYS
A
394
67.894
48.335
−3.497
1.00
56.45


C


ATOM
2094
O
LYS
A
394
67.683
47.692
−4.524
1.00
57.12


O


ATOM
2095
CB
LYS
A
394
69.053
46.492
−2.277
1.00
55.00


C


ATOM
2096
CG
LYS
A
394
70.490
46.968
−2.348
1.00
55.09


C


ATOM
2097
CD
LYS
A
394
71.417
45.863
−2.824
1.00
54.69


C


ATOM
2098
CE
LYS
A
394
71.338
44.636
−1.939
1.00
54.30


C


ATOM
2099
NZ
LYS
A
394
72.230
43.557
−2.442
1.00
53.86


N


ATOM
2100
N
VAL
A
395
67.993
49.659
−3.485
1.00
57.53


N


ATOM
2101
CA
VAL
A
395
67.860
50.432
−4.712
1.00
58.92


C


ATOM
2102
C
VAL
A
395
69.139
51.181
−5.061
1.00
60.04


C


ATOM
2103
O
VAL
A
395
69.813
51.718
−4.183
1.00
59.84


O


ATOM
2104
CB
VAL
A
395
66.704
51.448
−4.603
1.00
59.01


C


ATOM
2105
CG1
VAL
A
395
65.392
50.713
−4.362
1.00
58.97


C


ATOM
2106
CG2
VAL
A
395
66.977
52.433
−3.476
1.00
58.87


C


ATOM
2107
N
THR
A
396
69.467
51.213
−6.350
1.00
61.16


N


ATOM
2108
CA
THR
A
396
70.668
51.896
−6.818
1.00
62.32


C


ATOM
2109
C
THR
A
396
70.335
53.283
−7.351
1.00
63.18


C


ATOM
2110
O
THR
A
396
69.646
53.421
−8.363
1.00
63.24


O


ATOM
2111
CB
THR
A
396
71.367
51.099
−7.934
1.00
62.19


C


ATOM
2112
OG1
THR
A
396
71.668
49.780
−7.464
1.00
62.83


O


ATOM
2113
CG2
THR
A
396
72.662
51.785
−8.343
1.00
62.42


C


ATOM
2114
N
ILE
A
397
70.834
54.305
−6.665
1.00
64.15


N


ATOM
2115
CA
ILE
A
397
70.598
55.689
−7.055
1.00
65.10


C


ATOM
2116
C
ILE
A
397
71.899
56.356
−7.499
1.00
65.47


C


ATOM
2117
O
ILE
A
397
72.866
56.415
−6.741
1.00
65.96


O


ATOM
2118
CB
ILE
A
397
70.003
56.495
−5.884
1.00
65.41


C


ATOM
2119
CG1
ILE
A
397
68.709
55.833
−5.404
1.00
65.63


C


ATOM
2120
CG2
ILE
A
397
69.736
57.930
−6.320
1.00
65.84


C


ATOM
2121
CD1
ILE
A
397
68.079
56.509
−4.203
1.00
66.02


C


ATOM
2122
N
ASN
A
398
71.909
56.854
−8.732
1.00
65.71


N


ATOM
2123
CA
ASN
A
398
73.073
57.526
−9.307
1.00
65.41


C


ATOM
2124
C
ASN
A
398
74.417
56.895
−8.945
1.00
64.56


C


ATOM
2125
O
ASN
A
398
75.353
57.592
−8.551
1.00
64.63


O


ATOM
2126
CB
ASN
A
398
73.079
59.008
−8.910
1.00
66.44


C


ATOM
2127
CG
ASN
A
398
73.115
59.215
−7.405
1.00
67.59


C


ATOM
2128
OD1
ASN
A
398
74.046
58.779
−6.725
1.00
68.20


O


ATOM
2129
ND2
ASN
A
398
72.099
59.891
−6.878
1.00
67.87


N


ATOM
2130
N
GLY
A
399
74.508
55.576
−9.082
1.00
63.47


N


ATOM
2131
CA
GLY
A
399
75.751
54.886
−8.779
1.00
61.85


C


ATOM
2132
C
GLY
A
399
75.918
54.443
−7.338
1.00
60.93


C


ATOM
2133
O
GLY
A
399
76.854
53.709
−7.016
1.00
61.23


O


ATOM
2134
N
SER
A
400
75.019
54.882
−6.464
1.00
59.70


N


ATOM
2135
CA
SER
A
400
75.096
54.511
−5.056
1.00
57.96


C


ATOM
2136
C
SER
A
400
73.973
53.577
−4.634
1.00
56.49


C


ATOM
2137
O
SER
A
400
72.793
53.898
−4.774
1.00
56.56


O


ATOM
2138
CB
SER
A
400
75.079
55.761
−4.174
1.00
57.95


C


ATOM
2139
OG
SER
A
400
76.286
56.488
−4.305
1.00
58.53


O


ATOM
2140
N
VAL
A
401
74.351
52.414
−4.118
1.00
54.54


N


ATOM
2141
CA
VAL
A
401
73.383
51.431
−3.662
1.00
52.89


C


ATOM
2142
C
VAL
A
401
72.864
51.864
−2.293
1.00
52.23


C


ATOM
2143
O
VAL
A
401
73.637
52.020
−1.344
1.00
51.54


O


ATOM
2144
CB
VAL
A
401
74.027
50.038
−3.550
1.00
52.97


C


ATOM
2145
CG1
VAL
A
401
72.986
49.012
−3.153
1.00
52.38


C


ATOM
2146
CG2
VAL
A
401
74.670
49.660
−4.876
1.00
52.77


C


ATOM
2147
N
MET
A
402
71.554
52.066
−2.201
1.00
50.74


N


ATOM
2148
CA
MET
A
402
70.933
52.493
−0.954
1.00
49.56


C


ATOM
2149
C
MET
A
402
69.878
51.490
−0.509
1.00
48.15


C


ATOM
2150
O
MET
A
402
69.533
50.563
−1.243
1.00
47.53


O


ATOM
2151
CB
MET
A
402
70.255
53.855
−1.138
1.00
50.70


C


ATOM
2152
CG
MET
A
402
71.080
54.897
−1.873
1.00
51.69


C


ATOM
2153
SD
MET
A
402
72.539
55.428
−0.974
1.00
54.36


S


ATOM
2154
CE
MET
A
402
71.840
56.729
0.054
1.00
52.69


C


ATOM
2155
N
LYS
A
403
69.380
51.683
0.708
1.00
45.93


N


ATOM
2156
CA
LYS
A
403
68.325
50.843
1.258
1.00
43.52


C


ATOM
2157
C
LYS
A
403
67.270
51.792
1.806
1.00
42.26


C


ATOM
2158
O
LYS
A
403
67.598
52.853
2.336
1.00
41.26


O


ATOM
2159
CB
LYS
A
403
68.856
49.937
2.373
1.00
43.98


C


ATOM
2160
CG
LYS
A
403
69.833
48.880
1.887
1.00
43.45


C


ATOM
2161
CD
LYS
A
403
69.570
47.521
2.524
1.00
43.42


C


ATOM
2162
CE
LYS
A
403
68.229
46.950
2.087
1.00
42.68


C


ATOM
2163
NZ
LYS
A
403
68.000
45.572
2.601
1.00
40.87


N


ATOM
2164
N
GLU
A
404
66.003
51.425
1.659
1.00
41.41


N


ATOM
2165
CA
GLU
A
404
64.927
52.275
2.144
1.00
41.08


C


ATOM
2166
C
GLU
A
404
64.881
52.222
3.661
1.00
39.67


C


ATOM
2167
O
GLU
A
404
65.181
51.192
4.265
1.00
38.02


O


ATOM
2168
CB
GLU
A
404
63.578
51.809
1.606
1.00
42.91


C


ATOM
2169
CG
GLU
A
404
63.610
51.221
0.214
1.00
46.16


C


ATOM
2170
CD
GLU
A
404
62.230
50.819
−0.252
1.00
47.92


C


ATOM
2171
OE1
GLU
A
404
61.469
51.711
−0.685
1.00
48.56


O


ATOM
2172
OE2
GLU
A
404
61.901
49.615
−0.167
1.00
49.37


O


ATOM
2173
N
TYR
A
405
64.496
53.335
4.271
1.00
38.76


N


ATOM
2174
CA
TYR
A
405
64.390
53.402
5.717
1.00
38.34


C


ATOM
2175
C
TYR
A
405
63.347
54.438
6.094
1.00
37.84


C


ATOM
2176
O
TYR
A
405
63.499
55.622
5.796
1.00
38.50


O


ATOM
2177
CB
TYR
A
405
65.736
53.770
6.344
1.00
37.72


C


ATOM
2178
CG
TYR
A
405
65.698
53.826
7.855
1.00
37.96


C


ATOM
2179
CD1
TYR
A
405
65.285
52.723
8.602
1.00
36.71


C


ATOM
2180
CD2
TYR
A
405
66.072
54.982
8.539
1.00
38.07


C


ATOM
2181
CE1
TYR
A
405
65.245
52.770
9.995
1.00
37.68


C


ATOM
2182
CE2
TYR
A
405
66.036
55.038
9.931
1.00
38.31


C


ATOM
2183
CZ
TYR
A
405
65.621
53.929
10.650
1.00
37.39


C


ATOM
2184
OH
TYR
A
405
65.577
53.987
12.024
1.00
38.38


O


ATOM
2185
N
TRP
A
406
62.287
53.986
6.752
1.00
36.25


N


ATOM
2186
CA
TRP
A
406
61.221
54.885
7.160
1.00
35.74


C


ATOM
2187
C
TRP
A
406
60.829
54.630
8.608
1.00
35.35


C


ATOM
2188
O
TRP
A
406
60.906
53.499
9.092
1.00
34.84


O


ATOM
2189
CB
TRP
A
406
60.013
54.712
6.226
1.00
34.90


C


ATOM
2190
CG
TRP
A
406
59.374
53.345
6.257
1.00
33.53


C


ATOM
2191
CD1
TRP
A
406
58.389
52.920
7.100
1.00
33.84


C


ATOM
2192
CD2
TRP
A
406
59.679
52.232
5.405
1.00
34.08


C


ATOM
2193
NE1
TRP
A
406
58.059
51.615
6.826
1.00
34.02


N


ATOM
2194
CE2
TRP
A
406
58.835
51.167
5.791
1.00
33.93


C


ATOM
2195
CE3
TRP
A
406
60.584
52.031
4.351
1.00
35.20


C


ATOM
2196
CZ2
TRP
A
406
58.866
49.916
5.160
1.00
34.01


C


ATOM
2197
CZ3
TRP
A
406
60.615
50.784
3.722
1.00
35.05


C


ATOM
2198
CH2
TRP
A
406
59.758
49.744
4.132
1.00
34.39


C


ATOM
2199
N
GLY
A
407
60.421
55.691
9.295
1.00
36.13


N


ATOM
2200
CA
GLY
A
407
60.023
55.569
10.685
1.00
36.66


C


ATOM
2201
C
GLY
A
407
58.630
54.991
10.840
1.00
37.56


C


ATOM
2202
O
GLY
A
407
57.835
54.989
9.899
1.00
36.82


O


ATOM
2203
N
GLU
A
408
58.331
54.495
12.035
1.00
37.65


N


ATOM
2204
CA
GLU
A
408
57.022
53.917
12.316
1.00
38.92


C


ATOM
2205
C
GLU
A
408
55.950
54.998
12.390
1.00
40.20


C


ATOM
2206
O
GLU
A
408
54.756
54.704
12.374
1.00
40.37


O


ATOM
2207
CB
GLU
A
408
57.071
53.141
13.631
1.00
38.51


C


ATOM
2208
CG
GLU
A
408
57.848
51.845
13.535
1.00
37.66


C


ATOM
2209
CD
GLU
A
408
57.167
50.834
12.625
1.00
37.31


C


ATOM
2210
OE1
GLU
A
408
56.048
50.392
12.960
1.00
37.35


O


ATOM
2211
OE2
GLU
A
408
57.748
50.482
11.578
1.00
35.96


O


ATOM
2212
N
GLY
A
409
56.387
56.249
12.464
1.00
41.46


N


ATOM
2213
CA
GLY
A
409
55.455
57.358
12.544
1.00
43.94


C


ATOM
2214
C
GLY
A
409
55.111
57.955
11.193
1.00
45.38


C


ATOM
2215
O
GLY
A
409
54.268
58.844
11.105
1.00
45.63


O


ATOM
2216
N
SER
A
410
55.762
57.473
10.138
1.00
46.93


N


ATOM
2217
CA
SER
A
410
55.499
57.977
8.795
1.00
48.89


C


ATOM
2218
C
SER
A
410
54.184
57.394
8.293
1.00
50.59


C


ATOM
2219
O
SER
A
410
53.798
56.292
8.683
1.00
49.70


O


ATOM
2220
CB
SER
A
410
56.633
57.587
7.840
1.00
48.74


C


ATOM
2221
OG
SER
A
410
56.645
56.189
7.595
1.00
49.10


O


ATOM
2222
N
SER
A
411
53.495
58.137
7.433
1.00
52.78


N


ATOM
2223
CA
SER
A
411
52.224
57.674
6.890
1.00
55.38


C


ATOM
2224
C
SER
A
411
52.436
56.350
6.172
1.00
56.75


C


ATOM
2225
O
SER
A
411
51.559
55.487
6.154
1.00
57.17


O


ATOM
2226
CB
SER
A
411
51.656
58.710
5.917
1.00
56.02


C


ATOM
2227
OG
SER
A
411
52.569
58.984
4.868
1.00
56.98


O


ATOM
2228
N
ARG
A
412
53.621
56.195
5.591
1.00
58.21


N


ATOM
2229
CA
ARG
A
412
53.976
54.985
4.862
1.00
59.73


C


ATOM
2230
C
ARG
A
412
53.968
53.730
5.735
1.00
60.68


C


ATOM
2231
O
ARG
A
412
54.038
52.616
5.217
1.00
60.45


O


ATOM
2232
CB
ARG
A
412
55.362
55.157
4.227
1.00
59.28


C


ATOM
2233
CG
ARG
A
412
55.870
53.925
3.502
1.00
59.26


C


ATOM
2234
CD
ARG
A
412
57.209
54.168
2.824
1.00
58.44


C


ATOM
2235
NE
ARG
A
412
57.669
52.964
2.141
1.00
57.93


N


ATOM
2236
CZ
ARG
A
412
58.797
52.874
1.445
1.00
57.94


C


ATOM
2237
NH1
ARG
A
412
59.601
53.923
1.330
1.00
57.62


N


ATOM
2238
NH2
ARG
A
412
59.120
51.727
0.863
1.00
58.08


N


ATOM
2239
N
ALA
A
413
53.865
53.902
7.050
1.00
62.54


N


ATOM
2240
CA
ALA
A
413
53.886
52.756
7.958
1.00
63.99


C


ATOM
2241
C
ALA
A
413
52.735
52.638
8.956
1.00
65.55


C


ATOM
2242
O
ALA
A
413
52.051
51.614
8.999
1.00
65.26


O


ATOM
2243
CB
ALA
A
413
55.212
52.736
8.712
1.00
64.03


C


ATOM
2244
N
ARG
A
414
52.533
53.676
9.764
1.00
67.81


N


ATOM
2245
CA
ARG
A
414
51.489
53.671
10.789
1.00
69.46


C


ATOM
2246
C
ARG
A
414
50.087
53.325
10.285
1.00
70.36


C


ATOM
2247
O
ARG
A
414
49.181
53.071
11.084
1.00
70.13


O


ATOM
2248
CB
ARG
A
414
51.446
55.026
11.509
1.00
70.05


C


ATOM
2249
CG
ARG
A
414
50.960
56.194
10.659
1.00
71.62


C


ATOM
2250
CD
ARG
A
414
50.711
57.418
11.534
1.00
73.27


C


ATOM
2251
NE
ARG
A
414
50.149
58.551
10.799
1.00
74.95


N


ATOM
2252
CZ
ARG
A
414
50.825
59.302
9.933
1.00
75.82


C


ATOM
2253
NH1
ARG
A
414
52.102
59.047
9.682
1.00
76.36


N


ATOM
2254
NH2
ARG
A
414
50.225
60.317
9.323
1.00
76.47


N


ATOM
2255
N
ASN
A
415
49.911
53.313
8.967
1.00
71.18


N


ATOM
2256
CA
ASN
A
415
48.617
53.001
8.364
1.00
72.52


C


ATOM
2257
C
ASN
A
415
48.712
51.666
7.617
1.00
73.18


C


ATOM
2258
O
ASN
A
415
48.989
51.638
6.416
1.00
73.46


O


ATOM
2259
CB
ASN
A
415
48.218
54.124
7.393
1.00
73.28


C


ATOM
2260
CG
ASN
A
415
46.759
54.059
6.982
1.00
73.50


C


ATOM
2261
OD1
ASN
A
415
46.348
54.689
5.987
1.00
73.39


O


ATOM
2262
ND2
ASN
A
415
45.957
53.314
7.742
1.00
73.08


N


ATOM
2263
N
TRP
A
416
48.482
50.563
8.329
1.00
73.62


N


ATOM
2264
CA
TRP
A
416
48.564
49.238
7.716
1.00
74.23


C


ATOM
2265
C
TRP
A
416
47.212
48.527
7.660
1.00
73.85


C


ATOM
2266
O
TRP
A
416
46.416
48.598
8.598
1.00
73.60


O


ATOM
2267
CB
TRP
A
416
49.593
48.374
8.468
1.00
74.70


C


ATOM
2268
CG
TRP
A
416
49.043
47.556
9.609
1.00
76.10


C


ATOM
2269
CD1
TRP
A
416
48.308
46.405
9.516
1.00
76.57


C


ATOM
2270
CD2
TRP
A
416
49.195
47.819
11.010
1.00
76.67


C


ATOM
2271
NE1
TRP
A
416
47.996
45.936
10.770
1.00
76.56


N


ATOM
2272
CE2
TRP
A
416
48.527
46.784
11.705
1.00
76.89


C


ATOM
2273
CE3
TRP
A
416
49.830
48.828
11.747
1.00
77.37


C


ATOM
2274
CZ2
TRP
A
416
48.477
46.729
13.102
1.00
77.40


C


ATOM
2275
CZ3
TRP
A
416
49.780
48.772
13.138
1.00
77.75


C


ATOM
2276
CH2
TRP
A
416
49.107
47.728
13.799
1.00
77.84


C


ATOM
2277
N
GLU
A
431
54.545
62.823
11.142
1.00
66.75


N


ATOM
2278
CA
GLU
A
431
54.941
62.244
12.421
1.00
66.57


C


ATOM
2279
C
GLU
A
431
56.245
61.460
12.283
1.00
65.93


C


ATOM
2280
O
GLU
A
431
56.929
61.185
13.270
1.00
66.27


O


ATOM
2281
CB
GLU
A
431
53.832
61.328
12.945
1.00
67.44


C


ATOM
2282
CG
GLU
A
431
52.495
62.032
13.143
1.00
68.98


C


ATOM
2283
CD
GLU
A
431
51.422
61.112
13.693
1.00
69.90


C


ATOM
2284
OE1
GLU
A
431
51.073
60.126
13.010
1.00
70.49


O


ATOM
2285
OE2
GLU
A
431
50.927
61.373
14.811
1.00
70.56


O


ATOM
2286
N
GLY
A
432
56.582
61.106
11.047
1.00
64.87


N


ATOM
2287
CA
GLY
A
432
57.803
60.367
10.786
1.00
63.17


C


ATOM
2288
C
GLY
A
432
58.332
60.728
9.414
1.00
62.04


C


ATOM
2289
O
GLY
A
432
57.658
61.423
8.654
1.00
62.22


O


ATOM
2290
N
VAL
A
433
59.533
60.262
9.085
1.00
60.59


N


ATOM
2291
CA
VAL
A
433
60.117
60.564
7.785
1.00
58.60


C


ATOM
2292
C
VAL
A
433
60.530
59.318
7.000
1.00
57.08


C


ATOM
2293
O
VAL
A
433
60.849
58.276
7.576
1.00
56.04


O


ATOM
2294
CB
VAL
A
433
61.336
61.508
7.930
1.00
58.79


C


ATOM
2295
CG1
VAL
A
433
60.883
62.858
8.459
1.00
58.84


C


ATOM
2296
CG2
VAL
A
433
62.359
60.901
8.867
1.00
58.98


C


ATOM
2297
N
ASP
A
434
60.507
59.446
5.676
1.00
55.12


N


ATOM
2298
CA
ASP
A
434
60.867
58.367
4.761
1.00
53.00


C


ATOM
2299
C
ASP
A
434
62.215
58.734
4.144
1.00
51.90


C


ATOM
2300
O
ASP
A
434
62.401
59.866
3.696
1.00
51.71


O


ATOM
2301
CB
ASP
A
434
59.799
58.250
3.667
1.00
53.31


C


ATOM
2302
CG
ASP
A
434
59.932
56.984
2.841
1.00
53.22


C


ATOM
2303
OD1
ASP
A
434
59.210
56.862
1.830
1.00
53.79


O


ATOM
2304
OD2
ASP
A
434
60.744
56.108
3.199
1.00
53.37


O


ATOM
2305
N
SER
A
435
63.153
57.792
4.106
1.00
50.14


N


ATOM
2306
CA
SER
A
435
64.471
58.098
3.560
1.00
48.49


C


ATOM
2307
C
SER
A
435
65.267
56.912
3.026
1.00
47.19


C


ATOM
2308
O
SER
A
435
64.748
55.809
2.862
1.00
46.05


O


ATOM
2309
CB
SER
A
435
65.304
58.806
4.627
1.00
48.72


C


ATOM
2310
OG
SER
A
435
65.451
57.976
5.768
1.00
49.51


O


ATOM
2311
N
TYR
A
436
66.545
57.169
2.765
1.00
46.20


N


ATOM
2312
CA
TYR
A
436
67.470
56.163
2.259
1.00
46.22


C


ATOM
2313
C
TYR
A
436
68.735
56.149
3.114
1.00
45.31


C


ATOM
2314
O
TYR
A
436
69.125
57.175
3.673
1.00
45.33


O


ATOM
2315
CB
TYR
A
436
67.858
56.481
0.812
1.00
48.04


C


ATOM
2316
CG
TYR
A
436
66.731
56.356
−0.186
1.00
49.05


C


ATOM
2317
CD1
TYR
A
436
66.236
55.106
−0.555
1.00
49.71


C


ATOM
2318
CD2
TYR
A
436
66.160
57.488
−0.764
1.00
50.33


C


ATOM
2319
CE1
TYR
A
436
65.198
54.987
−1.476
1.00
50.76


C


ATOM
2320
CE2
TYR
A
436
65.119
57.381
−1.685
1.00
50.87


C


ATOM
2321
CZ
TYR
A
436
64.645
56.129
−2.035
1.00
50.97


C


ATOM
2322
OH
TYR
A
436
63.614
56.019
−2.940
1.00
52.36


O


ATOM
2323
N
VAL
A
437
69.361
54.980
3.217
1.00
44.07


N


ATOM
2324
CA
VAL
A
437
70.602
54.824
3.970
1.00
43.32


C


ATOM
2325
C
VAL
A
437
71.591
54.068
3.092
1.00
42.81


C


ATOM
2326
O
VAL
A
437
71.218
53.132
2.384
1.00
41.76


O


ATOM
2327
CB
VAL
A
437
70.401
54.034
5.290
1.00
42.99


C


ATOM
2328
CG1
VAL
A
437
69.463
54.793
6.213
1.00
42.96


C


ATOM
2329
CG2
VAL
A
437
69.868
52.645
4.997
1.00
42.44


C


ATOM
2330
N
PRO
A
438
72.873
54.460
3.133
1.00
43.06


N


ATOM
2331
CA
PRO
A
438
73.882
53.784
2.313
1.00
42.54


C


ATOM
2332
C
PRO
A
438
73.998
52.295
2.611
1.00
41.85


C


ATOM
2333
O
PRO
A
438
74.038
51.883
3.770
1.00
41.55


O


ATOM
2334
CB
PRO
A
438
75.162
54.554
2.641
1.00
43.10


C


ATOM
2335
CG
PRO
A
438
74.943
54.958
4.067
1.00
44.10


C


ATOM
2336
CD
PRO
A
438
73.501
55.422
4.056
1.00
42.97


C


ATOM
2337
N
TYR
A
439
74.034
51.491
1.554
1.00
41.03


N


ATOM
2338
CA
TYR
A
439
74.162
50.046
1.686
1.00
40.53


C


ATOM
2339
C
TYR
A
439
75.502
49.754
2.356
1.00
40.67


C


ATOM
2340
O
TYR
A
439
76.530
50.308
1.968
1.00
39.93


O


ATOM
2341
CB
TYR
A
439
74.108
49.393
0.303
1.00
40.18


C


ATOM
2342
CG
TYR
A
439
74.244
47.889
0.305
1.00
39.32


C


ATOM
2343
CD1
TYR
A
439
73.339
47.086
0.998
1.00
40.13


C


ATOM
2344
CD2
TYR
A
439
75.264
47.263
−0.411
1.00
39.93


C


ATOM
2345
CE1
TYR
A
439
73.445
45.697
0.975
1.00
40.31


C


ATOM
2346
CE2
TYR
A
439
75.380
45.878
−0.439
1.00
39.98


C


ATOM
2347
CZ
TYR
A
439
74.467
45.102
0.254
1.00
40.61


C


ATOM
2348
OH
TYR
A
439
74.576
43.731
0.226
1.00
41.51


O


ATOM
2349
N
ALA
A
440
75.485
48.885
3.361
1.00
40.76


N


ATOM
2350
CA
ALA
A
440
76.699
48.546
4.091
1.00
41.53


C


ATOM
2351
C
ALA
A
440
77.102
47.093
3.899
1.00
41.13


C


ATOM
2352
O
ALA
A
440
78.175
46.679
4.330
1.00
41.96


O


ATOM
2353
CB
ALA
A
440
76.507
48.842
5.580
1.00
40.70


C


ATOM
2354
N
GLY
A
441
76.239
46.320
3.251
1.00
41.41


N


ATOM
2355
CA
GLY
A
441
76.536
44.919
3.030
1.00
41.21


C


ATOM
2356
C
GLY
A
441
75.917
44.025
4.088
1.00
41.44


C


ATOM
2357
O
GLY
A
441
74.882
44.359
4.664
1.00
41.15


O


ATOM
2358
N
LYS
A
442
76.562
42.891
4.345
1.00
41.60


N


ATOM
2359
CA
LYS
A
442
76.097
41.917
5.329
1.00
41.97


C


ATOM
2360
C
LYS
A
442
76.237
42.410
6.771
1.00
40.70


C


ATOM
2361
O
LYS
A
442
77.189
43.112
7.114
1.00
41.12


O


ATOM
2362
CB
LYS
A
442
76.880
40.613
5.168
1.00
43.78


C


ATOM
2363
CG
LYS
A
442
76.859
40.049
3.756
1.00
46.44


C


ATOM
2364
CD
LYS
A
442
75.487
39.510
3.386
1.00
47.81


C


ATOM
2365
CE
LYS
A
442
75.159
38.260
4.179
1.00
48.88


C


ATOM
2366
NZ
LYS
A
442
73.844
37.682
3.783
1.00
51.00


N


ATOM
2367
N
LEU
A
443
75.285
42.020
7.611
1.00
39.20


N


ATOM
2368
CA
LEU
A
443
75.280
42.405
9.021
1.00
36.87


C


ATOM
2369
C
LEU
A
443
76.534
41.935
9.758
1.00
36.82


C


ATOM
2370
O
LEU
A
443
77.190
42.715
10.451
1.00
34.89


O


ATOM
2371
CB
LEU
A
443
74.032
41.829
9.703
1.00
35.37


C


ATOM
2372
CG
LEU
A
443
73.831
42.033
11.210
1.00
34.30


C


ATOM
2373
CD1
LEU
A
443
72.354
41.880
11.554
1.00
34.00


C


ATOM
2374
CD2
LEU
A
443
74.673
41.028
11.990
1.00
33.34


C


ATOM
2375
N
LYS
A
444
76.864
40.660
9.593
1.00
36.78


N


ATOM
2376
CA
LYS
A
444
78.016
40.052
10.256
1.00
37.95


C


ATOM
2377
C
LYS
A
444
79.303
40.880
10.292
1.00
37.79


C


ATOM
2378
O
LYS
A
444
79.801
41.211
11.371
1.00
36.54


O


ATOM
2379
CB
LYS
A
444
78.318
38.687
9.629
1.00
39.41


C


ATOM
2380
CG
LYS
A
444
79.374
37.896
10.380
1.00
43.18


C


ATOM
2381
CD
LYS
A
444
79.656
36.560
9.716
1.00
45.77


C


ATOM
2382
CE
LYS
A
444
80.661
35.762
10.527
1.00
47.73


C


ATOM
2383
NZ
LYS
A
444
81.910
36.539
10.764
1.00
49.70


N


ATOM
2384
N
ASP
A
445
79.839
41.207
9.120
1.00
37.04


N


ATOM
2385
CA
ASP
A
445
81.086
41.965
9.023
1.00
37.29


C


ATOM
2386
C
ASP
A
445
81.040
43.353
9.645
1.00
35.93


C


ATOM
2387
O
ASP
A
445
82.032
43.819
10.208
1.00
34.89


O


ATOM
2388
CB
ASP
A
445
81.512
42.095
7.558
1.00
39.90


C


ATOM
2389
CG
ASP
A
445
81.673
40.750
6.876
1.00
42.77


C


ATOM
2390
OD1
ASP
A
445
82.442
39.906
7.389
1.00
43.80


O


ATOM
2391
OD2
ASP
A
445
81.025
40.541
5.827
1.00
45.60


O


ATOM
2392
N
ASN
A
446
79.897
44.020
9.525
1.00
33.98


N


ATOM
2393
CA
ASN
A
446
79.739
45.359
10.075
1.00
33.10


C


ATOM
2394
C
ASN
A
446
79.657
45.330
11.596
1.00
31.88


C


ATOM
2395
O
ASN
A
446
80.257
46.167
12.272
1.00
30.91


O


ATOM
2396
CB
ASN
A
446
78.489
46.016
9.493
1.00
33.95


C


ATOM
2397
CG
ASN
A
446
78.683
46.454
8.051
1.00
35.61


C


ATOM
2398
OD1
ASN
A
446
79.267
47.505
7.785
1.00
37.12


O


ATOM
2399
ND2
ASN
A
446
78.207
45.641
7.116
1.00
34.41


N


ATOM
2400
N
VAL
A
447
78.911
44.371
12.131
1.00
31.04


N


ATOM
2401
CA
VAL
A
447
78.776
44.244
13.576
1.00
31.31


C


ATOM
2402
C
VAL
A
447
80.130
43.896
14.195
1.00
32.24


C


ATOM
2403
O
VAL
A
447
80.503
44.444
15.228
1.00
32.11


O


ATOM
2404
CE
VAL
A
447
77.740
43.160
13.949
1.00
30.45


C


ATOM
2405
CG1
VAL
A
447
77.813
42.858
15.443
1.00
30.61


C


ATOM
2406
CG2
VAL
A
447
76.336
43.642
13.587
1.00
30.05


C


ATOM
2407
N
GLU
A
448
80.863
42.988
13.559
1.00
32.57


N


ATOM
2408
CA
GLU
A
448
82.178
42.594
14.061
1.00
33.80


C


ATOM
2409
C
GLU
A
448
83.095
43.819
14.130
1.00
32.73


C


ATOM
2410
O
GLU
A
448
83.794
44.029
15.125
1.00
31.37


O


ATOM
2411
CB
GLU
A
448
82.798
41.529
13.148
1.00
37.00


C


ATOM
2412
CG
GLU
A
448
84.116
40.945
13.658
1.00
41.15


C


ATOM
2413
CD
GLU
A
448
84.710
39.904
12.714
1.00
44.90


C


ATOM
2414
OE1
GLU
A
448
85.161
40.280
11.610
1.00
47.11


O


ATOM
2415
OE2
GLU
A
448
84.720
38.705
13.075
1.00
47.09


O


ATOM
2416
N
ALA
A
449
83.086
44.630
13.076
1.00
31.13


N


ATOM
2417
CA
ALA
A
449
83.918
45.829
13.034
1.00
31.18


C


ATOM
2418
C
ALA
A
449
83.528
46.810
14.137
1.00
30.71


C


ATOM
2419
O
ALA
A
449
84.385
47.323
14.854
1.00
29.77


O


ATOM
2420
CB
ALA
A
449
83.802
46.506
11.674
1.00
31.83


C


ATOM
2421
N
SER
A
450
82.232
47.068
14.269
1.00
29.54


N


ATOM
2422
CA
SER
A
450
81.747
47.990
15.289
1.00
30.17


C


ATOM
2423
C
SER
A
450
82.130
47.528
16.694
1.00
30.40


C


ATOM
2424
O
SER
A
450
82.690
48.298
17.477
1.00
29.79


O


ATOM
2425
CB
SER
A
450
80.220
48.126
15.208
1.00
29.18


C


ATOM
2426
OG
SER
A
450
79.822
48.804
14.031
1.00
29.75


O


ATOM
2427
N
LEU
A
451
81.832
46.269
17.006
1.00
29.78


N


ATOM
2428
CA
LEU
A
451
82.123
45.734
18.330
1.00
30.57


C


ATOM
2429
C
LEU
A
451
83.614
45.586
18.620
1.00
31.46


C


ATOM
2430
O
LEU
A
451
84.022
45.603
19.781
1.00
30.55


O


ATOM
2431
CB
LEU
A
451
81.389
44.406
18.538
1.00
30.40


C


ATOM
2432
CG
LEU
A
451
79.858
44.540
18.505
1.00
30.16


C


ATOM
2433
CD1
LEU
A
451
79.219
43.219
18.883
1.00
30.36


C


ATOM
2434
CD2
LEU
A
451
79.409
45.640
19.466
1.00
30.38


C


ATOM
2435
N
ASN
A
452
84.430
45.440
17.580
1.00
32.01


N


ATOM
2436
CA
ASN
A
452
85.869
45.344
17.800
1.00
33.62


C


ATOM
2437
C
ASN
A
452
86.349
46.699
18.319
1.00
33.02


C


ATOM
2438
O
ASN
A
452
87.226
46.771
19.181
1.00
32.70


O


ATOM
2439
CB
ASN
A
452
86.615
44.988
16.510
1.00
35.58


C


ATOM
2440
CG
ASN
A
452
86.569
43.505
16.201
1.00
39.03


C


ATOM
2441
OD1
ASN
A
452
86.531
42.669
17.109
1.00
41.67


O


ATOM
2442
ND2
ASN
A
452
86.595
43.167
14.916
1.00
41.46


N


ATOM
2443
N
LYS
A
453
85.761
47.772
17.795
1.00
32.33


N


ATOM
2444
CA
LYS
A
453
86.125
49.115
18.225
1.00
32.17


C


ATOM
2445
C
LYS
A
453
85.642
49.343
19.655
1.00
30.92


C


ATOM
2446
O
LYS
A
453
86.344
49.949
20.459
1.00
29.86


O


ATOM
2447
CB
LYS
A
453
85.528
50.161
17.278
1.00
33.56


C


ATOM
2448
CG
LYS
A
453
86.172
50.131
15.889
1.00
37.25


C


ATOM
2449
CD
LYS
A
453
85.461
51.033
14.892
1.00
37.79


C


ATOM
2450
CE
LYS
A
453
85.502
52.490
15.316
1.00
39.41


C


ATOM
2451
NZ
LYS
A
453
84.804
53.342
14.314
1.00
40.64


N


ATOM
2452
N
VAL
A
454
84.447
48.849
19.966
1.00
29.21


N


ATOM
2453
CA
VAL
A
454
83.900
48.981
21.311
1.00
28.29


C


ATOM
2454
C
VAL
A
454
84.827
48.253
22.290
1.00
29.16


C


ATOM
2455
O
VAL
A
454
85.196
48.801
23.330
1.00
27.96


O


ATOM
2456
CB
VAL
A
454
82.478
48.368
21.408
1.00
28.44


C


ATOM
2457
CG1
VAL
A
454
82.016
48.334
22.867
1.00
26.28


C


ATOM
2458
CG2
VAL
A
454
81.499
49.188
20.571
1.00
27.61


C


ATOM
2459
N
LYS
A
455
85.209
47.024
21.945
1.00
28.54


N


ATOM
2460
CA
LYS
A
455
86.092
46.229
22.801
1.00
29.86


C


ATOM
2461
C
LYS
A
455
87.443
46.901
23.011
1.00
29.20


C


ATOM
2462
O
LYS
A
455
87.990
46.887
24.114
1.00
28.77


O


ATOM
2463
CB
LYS
A
455
86.322
44.838
22.202
1.00
30.13


C


ATOM
2464
CG
LYS
A
455
85.109
43.927
22.179
1.00
32.41


C


ATOM
2465
CD
LYS
A
455
85.465
42.639
21.447
1.00
34.53


C


ATOM
2466
CE
LYS
A
455
84.273
41.723
21.273
1.00
37.13


C


ATOM
2467
NZ
LYS
A
455
84.641
40.530
20.457
1.00
38.19


N


ATOM
2468
N
SER
A
456
87.985
47.483
21.946
1.00
29.06


N


ATOM
2469
CA
SER
A
456
89.271
48.152
22.036
1.00
30.21


C


ATOM
2470
C
SER
A
456
89.173
49.345
22.988
1.00
29.49


C


ATOM
2471
O
SER
A
456
90.051
49.565
23.823
1.00
28.06


O


ATOM
2472
CB
SER
A
456
89.722
48.617
20.650
1.00
31.84


C


ATOM
2473
OG
SER
A
456
91.050
49.100
20.703
1.00
36.19


O


ATOM
2474
N
THR
A
457
88.090
50.106
22.863
1.00
27.42


N


ATOM
2475
CA
THR
A
457
87.872
51.265
23.717
1.00
27.12


C


ATOM
2476
C
THR
A
457
87.689
50.822
25.163
1.00
26.61


C


ATOM
2477
O
THR
A
457
88.174
51.476
26.087
1.00
26.73


O


ATOM
2478
CB
THR
A
457
86.636
52.051
23.254
1.00
27.39


C


ATOM
2479
OG1
THR
A
457
86.833
52.456
21.897
1.00
29.71


O


ATOM
2480
CG2
THR
A
457
86.416
53.278
24.121
1.00
25.69


C


ATOM
2481
N
MET
A
458
86.993
49.706
25.362
1.00
25.76


N


ATOM
2482
CA
MET
A
458
86.791
49.197
26.708
1.00
25.74


C


ATOM
2483
C
MET
A
458
88.145
48.903
27.349
1.00
26.35


C


ATOM
2484
O
MET
A
458
88.373
49.229
28.518
1.00
24.96


O


ATOM
2485
CB
MET
A
458
85.900
47.954
26.670
1.00
25.80


C


ATOM
2486
CG
MET
A
458
84.427
48.318
26.457
1.00
25.05


C


ATOM
2487
SD
MET
A
458
83.363
46.907
26.197
1.00
26.75


S


ATOM
2488
CE
MET
A
458
83.422
46.109
27.816
1.00
25.98


C


ATOM
2489
N
CYS
A
459
89.061
48.320
26.582
1.00
26.54


N


ATOM
2490
CA
CYS
A
459
90.388
48.043
27.124
1.00
28.58


C


ATOM
2491
C
CYS
A
459
91.144
49.331
27.465
1.00
27.83


C


ATOM
2492
O
CYS
A
459
91.932
49.357
28.414
1.00
27.16


O


ATOM
2493
CB
CYS
A
459
91.201
47.183
26.159
1.00
31.43


C


ATOM
2494
SG
CYS
A
459
90.785
45.417
26.328
1.00
37.59


S


ATOM
2495
N
ASN
A
460
90.913
50.393
26.696
1.00
27.31


N


ATOM
2496
CA
ASN
A
460
91.554
51.678
26.978
1.00
26.88


C


ATOM
2497
C
ASN
A
460
91.053
52.139
28.347
1.00
27.10


C


ATOM
2498
O
ASN
A
460
91.792
52.748
29.122
1.00
25.93


O


ATOM
2499
CB
ASN
A
460
91.168
52.744
25.942
1.00
27.20


C


ATOM
2500
CG
ASN
A
460
91.839
52.542
24.595
1.00
30.02


C


ATOM
2501
OD1
ASN
A
460
91.164
52.420
23.572
1.00
29.71


O


ATOM
2502
ND2
ASN
A
460
93.170
52.524
24.583
1.00
29.98


N


ATOM
2503
N
CYS
A
461
89.786
51.847
28.631
1.00
26.43


N


ATOM
2504
CA
CYS
A
461
89.162
52.233
29.891
1.00
26.78


C


ATOM
2505
C
CYS
A
461
89.394
51.232
31.024
1.00
26.46


C


ATOM
2506
O
CYS
A
461
88.900
51.426
32.134
1.00
27.65


O


ATOM
2507
CB
CYS
A
461
87.654
52.436
29.682
1.00
26.90


C


ATOM
2508
SG
CYS
A
461
87.253
53.712
28.445
1.00
29.55


S


ATOM
2509
N
GLY
A
462
90.139
50.168
30.739
1.00
26.72


N


ATOM
2510
CA
GLY
A
462
90.430
49.155
31.745
1.00
28.25


C


ATOM
2511
C
GLY
A
462
89.272
48.226
32.081
1.00
28.51


C


ATOM
2512
O
GLY
A
462
89.174
47.712
33.204
1.00
28.75


O


ATOM
2513
N
ALA
A
463
88.405
47.979
31.106
1.00
26.73


N


ATOM
2514
CA
ALA
A
463
87.239
47.136
31.335
1.00
26.80


C


ATOM
2515
C
ALA
A
463
87.198
45.909
30.435
1.00
27.34


C


ATOM
2516
O
ALA
A
463
87.350
46.018
29.218
1.00
27.58


O


ATOM
2517
CB
ALA
A
463
85.967
47.963
31.140
1.00
26.04


C


ATOM
2518
N
LEU
A
464
86.983
44.746
31.045
1.00
26.85


N


ATOM
2519
CA
LEU
A
464
86.896
43.489
30.308
1.00
27.73


C


ATOM
2520
C
LEU
A
464
85.447
43.057
30.121
1.00
26.69


C


ATOM
2521
O
LEU
A
464
85.169
42.119
29.379
1.00
27.47


O


ATOM
2522
CB
LEU
A
464
87.654
42.378
31.038
1.00
28.53


C


ATOM
2523
CG
LEU
A
464
89.176
42.386
30.902
1.00
31.51


C


ATOM
2524
CD1
LEU
A
464
89.777
41.251
31.734
1.00
32.32


C


ATOM
2525
CD2
LEU
A
464
89.545
42.218
29.442
1.00
31.92


C


ATOM
2526
N
THR
A
465
84.531
43.734
30.806
1.00
25.40


N


ATOM
2527
CA
THR
A
465
83.108
43.421
30.709
1.00
24.59


C


ATOM
2528
C
THR
A
465
82.320
44.716
30.749
1.00
24.19


C


ATOM
2529
O
THR
A
465
82.855
45.766
31.102
1.00
22.83


O


ATOM
2530
CB
THR
A
465
82.617
42.552
31.884
1.00
24.77


C


ATOM
2531
OG1
THR
A
465
82.633
43.331
33.088
1.00
24.88


O


ATOM
2532
CG2
THR
A
465
83.507
41.317
32.061
1.00
24.23


C


ATOM
2533
N
ILE
A
466
81.040
44.639
30.401
1.00
23.48


N


ATOM
2534
CA
ILE
A
466
80.200
45.825
30.410
1.00
22.77


C


ATOM
2535
C
ILE
A
466
80.004
46.343
31.839
1.00
23.62


C


ATOM
2536
O
ILE
A
466
80.103
47.545
32.082
1.00
22.96


O


ATOM
2537
CB
ILE
A
466
78.849
45.538
29.699
1.00
23.94


C


ATOM
2538
CG1
ILE
A
466
79.113
45.363
28.194
1.00
22.77


C


ATOM
2539
CG2
ILE
A
466
77.856
46.679
29.935
1.00
23.50


C


ATOM
2540
CD1
ILE
A
466
77.886
44.941
27.377
1.00
24.77


C


ATOM
2541
N
PRO
A
467
79.742
45.448
32.809
1.00
23.36


N


ATOM
2542
CA
PRO
A
467
79.563
45.945
34.176
1.00
24.01


C


ATOM
2543
C
PRO
A
467
80.826
46.648
34.676
1.00
24.80


C


ATOM
2544
O
PRO
A
467
80.753
47.640
35.399
1.00
24.96


O


ATOM
2545
CB
PRO
A
467
79.253
44.676
34.965
1.00
24.77


C


ATOM
2546
CG
PRO
A
467
78.516
43.843
33.954
1.00
24.81


C


ATOM
2547
CD
PRO
A
467
79.367
44.024
32.720
1.00
23.03


C


ATOM
2548
N
GLN
A
468
81.988
46.136
34.287
1.00
25.14


N


ATOM
2549
CA
GLN
A
468
83.233
46.754
34.713
1.00
26.45


C


ATOM
2550
C
GLN
A
468
83.394
48.121
34.042
1.00
25.99


C


ATOM
2551
O
GLN
A
468
83.909
49.062
34.650
1.00
26.63


O


ATOM
2552
CB
GLN
A
468
84.412
45.829
34.398
1.00
27.40


C


ATOM
2553
CG
GLN
A
468
85.759
46.390
34.791
1.00
29.99


C


ATOM
2554
CD
GLN
A
468
86.838
45.328
34.836
1.00
28.82


C


ATOM
2555
OE1
GLN
A
468
86.952
44.501
33.934
1.00
27.62


O


ATOM
2556
NE2
GLN
A
468
87.648
45.356
35.890
1.00
30.42


N


ATOM
2557
N
LEU
A
469
82.940
48.238
32.796
1.00
24.88


N


ATOM
2558
CA
LEU
A
469
83.014
49.507
32.081
1.00
24.40


C


ATOM
2559
C
LEU
A
469
82.093
50.527
32.753
1.00
24.98


C


ATOM
2560
O
LEU
A
469
82.447
51.702
32.898
1.00
25.34


O


ATOM
2561
CB
LEU
A
469
82.596
49.332
30.611
1.00
24.62


C


ATOM
2562
CG
LEU
A
469
82.396
50.625
29.799
1.00
24.32


C


ATOM
2563
CD1
LEU
A
469
83.731
51.286
29.507
1.00
24.10


C


ATOM
2564
CD2
LEU
A
469
81.681
50.298
28.497
1.00
23.72


C


ATOM
2565
N
GLN
A
470
80.914
50.077
33.168
1.00
24.91


N


ATOM
2566
CA
GLN
A
470
79.951
50.965
33.807
1.00
26.70


C


ATOM
2567
C
GLN
A
470
80.461
51.471
35.151
1.00
27.35


C


ATOM
2568
O
GLN
A
470
80.103
52.560
35.601
1.00
28.25


O


ATOM
2569
CB
GLN
A
470
78.614
50.238
33.961
1.00
27.04


C


ATOM
2570
CG
GLN
A
470
78.071
49.794
32.600
1.00
26.67


C


ATOM
2571
CD
GLN
A
470
76.805
48.981
32.688
1.00
27.02


C


ATOM
2572
OE1
GLN
A
470
76.616
48.208
33.621
1.00
28.25


O


ATOM
2573
NE2
GLN
A
470
75.934
49.135
31.696
1.00
25.90


N


ATOM
2574
N
SER
A
471
81.316
50.680
35.778
1.00
26.97


N


ATOM
2575
CA
SER
A
471
81.883
51.049
37.063
1.00
28.68


C


ATOM
2576
C
SER
A
471
83.122
51.944
36.928
1.00
28.52


C


ATOM
2577
O
SER
A
471
83.289
52.908
37.680
1.00
29.15


O


ATOM
2578
CB
SER
A
471
82.244
49.775
37.839
1.00
29.10


C


ATOM
2579
OG
SER
A
471
82.934
50.081
39.037
1.00
35.37


O


ATOM
2580
N
LYS
A
472
83.968
51.651
35.946
1.00
27.16


N


ATOM
2581
CA
LYS
A
472
85.224
52.390
35.782
1.00
28.51


C


ATOM
2582
C
LYS
A
472
85.293
53.531
34.778
1.00
27.51


C


ATOM
2583
O
LYS
A
472
86.232
54.323
34.818
1.00
26.25


O


ATOM
2584
CB
LYS
A
472
86.341
51.404
35.451
1.00
29.64


C


ATOM
2585
CG
LYS
A
472
86.461
50.273
36.453
1.00
32.63


C


ATOM
2586
CD
LYS
A
472
87.440
49.205
35.994
1.00
33.81


C


ATOM
2587
CE
LYS
A
472
88.868
49.704
35.997
1.00
35.59


C


ATOM
2588
NZ
LYS
A
472
89.815
48.590
35.715
1.00
35.49


N


ATOM
2589
N
ALA
A
473
84.322
53.617
33.876
1.00
26.09


N


ATOM
2590
CA
ALA
A
473
84.345
54.660
32.860
1.00
26.12


C


ATOM
2591
C
ALA
A
473
84.461
56.080
33.410
1.00
25.21


C


ATOM
2592
O
ALA
A
473
83.827
56.432
34.400
1.00
25.99


O


ATOM
2593
CB
ALA
A
473
83.106
54.553
31.971
1.00
26.24


C


ATOM
2594
N
LYS
A
474
85.290
56.882
32.749
1.00
24.98


N


ATOM
2595
CA
LYS
A
474
85.505
58.284
33.098
1.00
25.10


C


ATOM
2596
C
LYS
A
474
84.943
59.013
31.884
1.00
24.93


C


ATOM
2597
O
LYS
A
474
85.475
58.904
30.779
1.00
24.89


O


ATOM
2598
CB
LYS
A
474
87.000
58.549
33.278
1.00
25.31


C


ATOM
2599
CG
LYS
A
474
87.589
57.732
34.424
1.00
25.41


C


ATOM
2600
CD
LYS
A
474
89.078
57.470
34.242
1.00
26.81


C


ATOM
2601
CE
LYS
A
474
89.902
58.722
34.425
1.00
28.30


C


ATOM
2602
NZ
LYS
A
474
91.346
58.422
34.183
1.00
27.67


N


ATOM
2603
N
ILE
A
475
83.858
59.750
32.093
1.00
24.28


N


ATOM
2604
CA
ILE
A
475
83.169
60.408
30.986
1.00
25.91


C


ATOM
2605
C
ILE
A
475
83.103
61.924
31.100
1.00
25.77


C


ATOM
2606
O
ILE
A
475
82.519
62.453
32.042
1.00
26.40


O


ATOM
2607
CB
ILE
A
475
81.726
59.855
30.883
1.00
25.54


C


ATOM
2608
CG1
ILE
A
475
81.763
58.319
30.868
1.00
26.29


C


ATOM
2609
CG2
ILE
A
475
81.043
60.392
29.630
1.00
27.31


C


ATOM
2610
CD1
ILE
A
475
80.394
57.657
30.959
1.00
25.53


C


ATOM
2611
N
THR
A
476
83.678
62.617
30.122
1.00
25.85


N


ATOM
2612
CA
THR
A
476
83.675
64.073
30.140
1.00
25.82


C


ATOM
2613
C
THR
A
476
82.795
64.688
29.067
1.00
25.93


C


ATOM
2614
O
THR
A
476
82.630
64.137
27.977
1.00
24.07


O


ATOM
2615
CB
THR
A
476
85.097
64.657
29.955
1.00
26.37


C


ATOM
2616
OG1
THR
A
476
85.052
66.082
30.123
1.00
28.03


O


ATOM
2617
CG2
THR
A
476
85.625
64.352
28.559
1.00
25.51


C


ATOM
2618
N
LEU
A
477
82.232
65.843
29.399
1.00
25.92


N


ATOM
2619
CA
LEU
A
477
81.406
66.596
28.472
1.00
27.45


C


ATOM
2620
C
LEU
A
477
82.433
67.442
27.722
1.00
27.85


C


ATOM
2621
O
LEU
A
477
83.469
67.780
28.290
1.00
27.59


O


ATOM
2622
CB
LEU
A
477
80.454
67.501
29.254
1.00
28.30


C


ATOM
2623
CG
LEU
A
477
79.298
68.176
28.523
1.00
30.46


C


ATOM
2624
CD1
LEU
A
477
78.351
67.123
27.980
1.00
29.78


C


ATOM
2625
CD2
LEU
A
477
78.561
69.099
29.497
1.00
32.80


C


ATOM
2626
N
VAL
A
478
82.167
67.771
26.462
1.00
29.07


N


ATOM
2627
CA
VAL
A
478
83.095
68.592
25.686
1.00
31.32


C


ATOM
2628
C
VAL
A
478
82.456
69.950
25.407
1.00
33.58


C


ATOM
2629
O
VAL
A
478
81.248
70.044
25.212
1.00
32.21


O


ATOM
2630
CB
VAL
A
478
83.480
67.912
24.348
1.00
32.07


C


ATOM
2631
CG1
VAL
A
478
83.857
66.462
24.604
1.00
32.68


C


ATOM
2632
CG2
VAL
A
478
82.342
68.018
23.341
1.00
34.67


C


ATOM
2633
N
SER
A
479
83.274
70.997
25.385
1.00
35.26


N


ATOM
2634
CA
SER
A
479
82.791
72.359
25.169
1.00
38.88


C


ATOM
2635
C
SER
A
479
81.991
72.592
23.899
1.00
41.66


C


ATOM
2636
O
SER
A
479
82.255
71.993
22.854
1.00
42.05


O


ATOM
2637
CB
SER
A
479
83.963
73.339
25.174
1.00
38.14


C


ATOM
2638
OG
SER
A
479
84.773
73.130
24.034
1.00
36.16


O


ATOM
2639
N
SER
A
480
81.019
73.494
24.004
1.00
45.75


N


ATOM
2640
CA
SER
A
480
80.169
73.865
22.881
1.00
50.07


C


ATOM
2641
C
SER
A
480
81.035
74.534
21.819
1.00
52.24


C


ATOM
2642
O
SER
A
480
80.834
74.346
20.617
1.00
51.90


O


ATOM
2643
CB
SER
A
480
79.085
74.842
23.351
1.00
50.84


C


ATOM
2644
OG
SER
A
480
78.323
75.323
22.258
1.00
52.94


O


ATOM
2645
N
VAL
A
481
82.015
75.301
22.288
1.00
54.50


N


ATOM
2646
CA
VAL
A
481
82.929
76.029
21.416
1.00
56.91


C


ATOM
2647
C
VAL
A
481
84.004
75.136
20.803
1.00
58.08


C


ATOM
2648
O
VAL
A
481
84.966
75.637
20.216
1.00
58.99


O


ATOM
2649
CB
VAL
A
481
83.641
77.154
22.193
1.00
57.54


C


ATOM
2650
CG1
VAL
A
481
83.948
78.316
21.264
1.00
57.89


C


ATOM
2651
CG2
VAL
A
481
82.789
77.596
23.366
1.00
58.34


C


ATOM
2652
N
SER
A
482
83.848
73.821
20.933
1.00
58.75


N


ATOM
2653
CA
SER
A
482
84.838
72.896
20.393
1.00
59.46


C


ATOM
2654
C
SER
A
482
84.252
71.737
19.593
1.00
60.06


C


ATOM
2655
O
SER
A
482
83.245
71.896
18.902
1.00
60.14


O


ATOM
2656
CB
SER
A
482
85.708
72.345
21.525
1.00
59.32


C


ATOM
2657
OG
SER
A
482
86.717
71.486
21.025
1.00
60.01


O


ATOM
2658
N
ILE
A
483
84.899
70.575
19.712
1.00
60.52


N


ATOM
2659
CA
ILE
A
483
84.535
69.343
19.009
1.00
60.59


C


ATOM
2660
C
ILE
A
483
85.319
69.317
17.701
1.00
60.24


C


ATOM
2661
O
ILE
A
483
85.585
68.254
17.137
1.00
60.22


O


ATOM
2662
CB
ILE
A
483
83.015
69.264
18.698
1.00
60.93


C


ATOM
2663
CG1
ILE
A
483
82.227
69.079
19.997
1.00
60.99


C


ATOM
2664
CG2
ILE
A
483
82.730
68.118
17.731
1.00
61.21


C


ATOM
2665
CD1
ILE
A
483
80.725
69.039
19.804
1.00
60.52


C


ATOM
2666
N
VAL
A
484
85.694
70.504
17.237
1.00
59.84


N


ATOM
2667
CA
VAL
A
484
86.451
70.653
16.001
1.00
59.29


C


ATOM
2668
C
VAL
A
484
87.845
70.049
16.151
1.00
58.69


C


ATOM
2669
O
VAL
A
484
88.354
69.409
15.228
1.00
58.32


O


ATOM
2670
CB
VAL
A
484
86.590
72.145
15.612
1.00
59.56


C


ATOM
2671
CG1
VAL
A
484
87.372
72.277
14.311
1.00
59.65


C


ATOM
2672
CG2
VAL
A
484
85.209
72.775
15.469
1.00
59.42


C


ATOM
2673
N
GLU
A
485
88.456
70.254
17.316
1.00
57.53


N


ATOM
2674
CA
GLU
A
485
89.790
69.725
17.584
1.00
56.68


C


ATOM
2675
C
GLU
A
485
89.765
68.200
17.523
1.00
57.27


C


ATOM
2676
O
GLU
A
485
90.758
67.565
17.164
1.00
56.78


O


ATOM
2677
CB
GLU
A
485
90.277
70.170
18.969
1.00
54.83


C


ATOM
2678
CG
GLU
A
485
91.732
69.794
19.274
1.00
52.09


C


ATOM
2679
CD
GLU
A
485
92.168
70.183
20.682
1.00
50.97


C


ATOM
2680
OE1
GLU
A
485
91.768
69.499
21.649
1.00
45.34


O


ATOM
2681
OE2
GLU
A
485
92.911
71.180
20.820
1.00
51.44


O


ATOM
2682
N
GLY
A
486
88.617
67.626
17.872
1.00
57.81


N


ATOM
2683
CA
GLY
A
486
88.462
66.182
17.875
1.00
58.97


C


ATOM
2684
C
GLY
A
486
88.580
65.524
16.515
1.00
59.51


C


ATOM
2685
O
GLY
A
486
89.142
64.435
16.398
1.00
59.72


O


ATOM
2686
N
GLY
A
487
88.045
66.176
15.487
1.00
60.19


N


ATOM
2687
CA
GLY
A
487
88.118
65.620
14.146
1.00
60.96


C


ATOM
2688
C
GLY
A
487
89.336
66.120
13.394
1.00
61.44


C


ATOM
2689
O
GLY
A
487
90.170
66.831
13.957
1.00
61.56


O


ATOM
2690
N
ALA
A
488
89.450
65.746
12.123
1.00
61.60


N


ATOM
2691
CA
ALA
A
488
90.576
66.180
11.302
1.00
61.84


C


ATOM
2692
C
ALA
A
488
90.446
67.683
11.068
1.00
62.10


C


ATOM
2693
O
ALA
A
488
89.365
68.171
10.739
1.00
61.91


O


ATOM
2694
CB
ALA
A
488
90.575
65.434
9.971
1.00
61.64


C


ATOM
2695
N
HIS
A
489
91.541
68.417
11.240
1.00
62.27


N


ATOM
2696
CA
HIS
A
489
91.499
69.863
11.049
1.00
62.65


C


ATOM
2697
C
HIS
A
489
92.786
70.469
10.503
1.00
62.69


C


ATOM
2698
O
HIS
A
489
93.887
70.008
10.809
1.00
62.31


O


ATOM
2699
CB
HIS
A
489
91.147
70.559
12.368
1.00
62.91


C


ATOM
2700
CG
HIS
A
489
92.100
70.258
13.484
1.00
63.07


C


ATOM
2701
ND1
HIS
A
489
92.136
69.038
14.124
1.00
63.07


N


ATOM
2702
CD2
HIS
A
489
93.060
71.016
14.066
1.00
63.14


C


ATOM
2703
CE1
HIS
A
489
93.074
69.058
15.054
1.00
63.28


C


ATOM
2704
NE2
HIS
A
489
93.650
70.246
15.039
1.00
63.10


N


ATOM
2705
N
ASP
A
490
92.626
71.513
9.695
1.00
62.96


N


ATOM
2706
CA
ASP
A
490
93.747
72.234
9.101
1.00
62.99


C


ATOM
2707
C
ASP
A
490
94.619
71.381
8.187
1.00
63.25


C


ATOM
2708
O
ASP
A
490
95.824
71.609
8.066
1.00
62.96


O


ATOM
2709
CB
ASP
A
490
94.593
72.857
10.210
1.00
63.04


C


ATOM
2710
CG
ASP
A
490
93.789
73.797
11.086
1.00
63.29


C


ATOM
2711
OD1
ASP
A
490
93.394
74.879
10.597
1.00
62.95


O


ATOM
2712
OD2
ASP
A
490
93.539
73.447
12.259
1.00
63.21


O


ATOM
2713
N
VAL
A
491
93.999
70.397
7.545
1.00
63.51


N


ATOM
2714
CA
VAL
A
491
94.696
69.516
6.618
1.00
63.93


C


ATOM
2715
C
VAL
A
491
93.743
69.145
5.489
1.00
64.46


C


ATOM
2716
O
VAL
A
491
92.536
69.009
5.704
1.00
64.24


O


ATOM
2717
CB
VAL
A
491
95.188
68.214
7.308
1.00
63.80


C


ATOM
2718
CG1
VAL
A
491
96.218
68.545
8.379
1.00
63.55


C


ATOM
2719
CG2
VAL
A
491
94.010
67.464
7.913
1.00
63.70


C


ATOM
2720
N
ILE
A
492
94.287
68.996
4.287
1.00
64.85


N


ATOM
2721
CA
ILE
A
492
93.486
68.633
3.125
1.00
65.38


C


ATOM
2722
C
ILE
A
492
93.564
67.121
2.911
1.00
65.68


C


ATOM
2723
O
ILE
A
492
94.423
66.665
2.123
1.00
66.09


O


ATOM
2724
CB
ILE
A
492
93.974
69.375
1.854
1.00
65.44


C


ATOM
2725
CG1
ILE
A
492
93.922
70.887
2.084
1.00
65.23


C


ATOM
2726
CG2
ILE
A
492
93.101
69.001
0.661
1.00
65.46


C


ATOM
2727
CD1
ILE
A
492
94.390
71.707
0.900
1.00
65.68


C


TER
2728

ILE
A
492


HETATM
2729
K
K

900
52.929
60.386
29.350
0.75
33.25


K


HETATM
2730
NA
NA

901
65.775
63.097
15.894
1.00
51.30


NA


HETATM
2731
P
RVP

602
67.806
55.192
15.010
1.00
32.06


P


HETATM
2732
O1P
RVP

602
67.447
55.106
13.566
1.00
33.43


O


HETATM
2733
O2P
RVP

602
68.618
53.993
15.386
1.00
33.48


O


HETATM
2734
O3P
RVP

602
68.589
56.489
15.335
1.00
32.27


O


HETATM
2735
O5*
RVP

602
66.564
55.260
15.998
1.00
32.66


O


HETATM
2736
C5*
RVP

602
65.601
54.207
15.962
1.00
31.36


C


HETATM
2737
C4*
RVP

602
64.521
54.418
16.985
1.00
30.66


C


HETATM
2738
O4*
RVP

602
63.766
55.605
16.540
1.00
29.94


O


HETATM
2739
C3*
RVP

602
63.437
53.370
17.179
1.00
29.26


C


HETATM
2740
O3*
RVP

602
63.863
52.229
17.914
1.00
28.74


O


HETATM
2741
C2*
RVP

602
62.343
54.162
17.832
1.00
30.26


C


HETATM
2742
O2*
RVP

602
62.482
54.278
19.236
1.00
30.38


O


HETATM
2743
C1*
RVP

602
62.434
55.486
17.067
1.00
31.26


C


HETATM
2744
N9
RVP

602
61.475
55.602
15.903
1.00
32.47


N


HETATM
2745
C8
RVP

602
60.989
54.694
14.978
1.00
33.70


C


HETATM
2746
N7
RVP

602
60.171
55.231
14.129
1.00
33.53


N


HETATM
2747
C5
RVP

602
60.084
56.544
14.468
1.00
34.69


C


HETATM
2748
C6
RVP

602
59.329
57.634
13.877
1.00
34.93


C


HETATM
2749
O6
RVP

602
58.592
57.567
12.906
1.00
35.34


O


HETATM
2750
N1
RVP

602
59.501
58.902
14.532
1.00
35.14


N


HETATM
2751
N4
RVP

602
60.883
56.810
15.574
1.00
33.87


N


HETATM
2752
O
HOH

1
75.701
41.635
35.059
1.00
43.94


O


HETATM
2753
O
HOH

2
74.079
38.696
40.465
1.00
55.18


O


HETATM
2754
O
HOH

3
65.938
60.588
24.743
1.00
24.75


O


HETATM
2755
O
HOH

4
90.376
44.734
34.332
1.00
58.18


O


HETATM
2756
O
HOH

5
57.606
58.768
28.316
1.00
26.20


O


HETATM
2757
O
HOH

6
73.742
57.520
36.339
1.00
22.08


O


HETATM
2758
O
HOH

7
59.439
45.332
37.045
1.00
28.29


O


HETATM
2759
O
HOH

8
66.630
48.045
39.016
1.00
24.24


O


HETATM
2760
O
HOH

9
87.313
55.537
31.236
1.00
26.94


O


HETATM
2761
O
HOH

10
79.723
41.990
29.591
1.00
24.41


O


HETATM
2762
O
HOH

11
70.855
54.607
21.999
1.00
25.98


O


HETATM
2763
O
HOH

12
75.110
45.838
32.838
1.00
30.43


O


HETATM
2764
O
HOH

13
71.016
53.391
14.308
1.00
28.65


O


HETATM
2765
O
HOH

14
75.872
56.829
34.478
1.00
29.47


O


HETATM
2766
O
HOH

15
84.437
53.172
21.050
1.00
27.86


O


HETATM
2767
O
HOH

16
76.208
43.857
31.117
1.00
21.58


O


HETATM
2768
O
HOH

17
88.575
53.835
33.310
1.00
28.69


O


HETATM
2769
O
HOH

18
78.805
48.189
37.292
1.00
30.37


O


HETATM
2770
O
HOH

19
81.282
64.691
32.797
1.00
26.40


O


HETATM
2771
O
HOH

20
74.258
59.955
37.886
1.00
35.26


O


HETATM
2772
O
HOH

21
72.681
38.221
33.950
1.00
27.93


O


HETATM
2773
O
HOH

22
56.779
57.580
38.836
1.00
33.24


O


HETATM
2774
O
HOH

23
69.275
68.052
32.909
1.00
34.10


O


HETATM
2775
O
HOH

24
58.760
51.196
23.042
1.00
28.36


O


HETATM
2776
O
HOH

25
79.310
40.417
32.071
1.00
30.06


O


HETATM
2777
O
HOH

26
77.754
54.034
34.410
1.00
31.27


O


HETATM
2778
O
HOH

27
64.140
56.432
20.380
1.00
35.64


O


HETATM
2779
O
HOH

28
62.442
38.699
34.139
1.00
30.68


O


HETATM
2780
O
HOH

29
65.481
36.753
34.839
1.00
29.52


O


HETATM
2781
O
HOH

30
49.387
44.266
21.091
1.00
32.82


O


HETATM
2782
O
HOH

31
74.171
50.758
36.345
1.00
35.61


O


HETATM
2783
O
HOH

32
76.573
41.279
32.222
1.00
30.60


O


HETATM
2784
O
HOH

33
87.348
67.083
31.015
1.00
29.38


O


HETATM
2785
O
HOH

34
66.425
37.664
16.827
1.00
27.26


O


HETATM
2786
O
HOH

35
59.765
51.154
9.792
1.00
31.75


O


HETATM
2787
O
HOH

36
61.770
50.532
17.896
1.00
26.41


O


HETATM
2788
O
HOH

37
65.804
58.780
21.469
1.00
36.21


O


HETATM
2789
O
HOH

38
76.213
52.726
36.406
1.00
34.08


O


HETATM
2790
O
HOH

39
59.631
51.746
16.407
1.00
31.30


O


HETATM
2791
O
HOH

40
82.391
67.258
31.863
1.00
31.37


O


HETATM
2792
O
HOH

41
70.252
33.623
27.556
1.00
35.71


O


HETATM
2793
O
HOH

42
72.039
67.304
32.099
1.00
35.67


O


HETATM
2794
O
HOH

43
53.140
51.705
38.165
1.00
31.55


O


HETATM
2795
O
HOH

44
67.908
38.414
46.440
1.00
32.54


O


HETATM
2796
O
HOH

45
58.797
45.284
6.070
1.00
39.86


O


HETATM
2797
O
HOH

46
50.916
46.272
35.836
1.00
39.05


O


HETATM
2798
O
HOH

47
48.468
54.286
36.992
1.00
37.90


O


HETATM
2799
O
HOH

48
79.368
38.350
17.558
1.00
37.55


O


HETATM
2800
O
HOH

49
65.917
31.312
26.738
1.00
40.60


O


HETATM
2801
O
HOH

50
75.195
38.963
31.142
1.00
31.97


O


HETATM
2802
O
HOH

51
51.201
58.619
25.886
1.00
40.51


O


HETATM
2803
O
HOH

52
56.361
77.266
37.184
1.00
34.64


O


HETATM
2804
O
HOH

53
75.373
38.767
8.255
1.00
34.82


O


HETATM
2805
O
HOH

54
62.203
64.463
35.439
1.00
32.93


O


HETATM
2806
O
HOH

55
67.513
69.374
38.251
1.00
43.30


O


HETATM
2807
O
HOH

56
59.023
38.343
34.814
1.00
35.89


O


HETATM
2808
O
HOH

57
61.282
73.583
39.232
1.00
39.52


O


HETATM
2809
O
HOH

58
74.916
47.914
35.808
1.00
36.57


O


HETATM
2810
O
HOH

59
62.673
61.732
37.514
1.00
33.12


O


HETATM
2811
O
HOH

60
74.787
37.123
10.828
1.00
36.31


O


HETATM
2812
O
HOH

61
87.050
70.287
23.795
1.00
40.37


O


HETATM
2813
O
HOH

62
60.963
37.766
37.311
1.00
46.47


O


HETATM
2814
O
HOH

63
74.898
62.998
19.440
1.00
40.44


O


HETATM
2815
O
HOH

64
60.204
41.357
39.977
1.00
48.22


O


HETATM
2816
O
HOH

65
83.322
55.796
16.450
1.00
32.01


O


HETATM
2817
O
HOH

66
74.375
34.757
40.315
1.00
36.09


O


HETATM
2818
O
HOH

67
71.494
55.957
41.977
1.00
32.49


O


HETATM
2819
O
HOH

68
59.957
50.992
20.176
1.00
43.21


O


HETATM
2820
O
HOH

69
66.080
28.763
15.101
1.00
39.12


O


HETATM
2821
O
HOH

70
50.588
31.847
16.621
1.00
43.31


O


HETATM
2822
O
HOH

71
69.529
68.913
36.005
1.00
40.30


O


HETATM
2823
O
HOH

72
73.768
64.532
30.646
1.00
40.71


O


HETATM
2824
O
HOH

73
92.829
49.112
23.281
1.00
44.30


O


HETATM
2825
O
HOH

74
70.278
54.233
17.770
1.00
32.36


O


HETATM
2826
O
HOH

75
52.179
53.975
25.940
1.00
38.86


O


HETATM
2827
O
HOH

76
70.150
32.823
38.265
1.00
49.16


O


HETATM
2828
O
HOH

77
69.559
45.202
46.424
1.00
37.45


O


HETATM
2829
O
HOH

78
81.658
38.524
24.274
1.00
39.74


O


HETATM
2830
O
HOH

79
85.501
49.287
39.572
1.00
41.67


O


HETATM
2831
O
HOH

80
43.313
43.736
23.528
1.00
38.76


O


HETATM
2832
O
HOH

81
45.058
35.260
19.329
1.00
48.10


O


HETATM
2833
O
HOH

82
86.888
47.694
13.726
1.00
42.11


O


HETATM
2834
O
HOH

83
59.990
59.432
31.077
1.00
43.45


O


HETATM
2835
O
HOH

84
65.702
28.237
26.872
1.00
41.07


O


HETATM
2836
O
HOH

85
56.392
41.602
37.511
1.00
42.34


O


HETATM
2837
O
HOH

86
89.958
53.438
35.939
1.00
44.28


O


HETATM
2838
O
HOH

87
53.813
58.314
38.115
1.00
43.91


O


HETATM
2839
O
HOH

88
54.846
33.441
37.762
1.00
45.87


O


HETATM
2840
O
HOH

89
68.555
74.630
33.270
1.00
45.09


O


HETATM
2841
O
HOH

90
46.075
48.997
27.411
1.00
39.29


O


HETATM
2842
O
HOH

91
58.611
35.738
27.091
1.00
37.48


O


HETATM
2843
O
HOH

92
65.536
61.610
38.426
1.00
47.43


O


HETATM
2844
O
HOH

93
63.014
78.411
34.747
1.00
48.43


O


HETATM
2845
O
HOH

94
69.402
35.849
7.804
1.00
43.16


O


HETATM
2846
O
HOH

95
51.178
50.724
21.941
1.00
39.55


O


HETATM
2847
O
HOH

96
85.871
39.272
22.557
1.00
42.34


O


HETATM
2848
O
HOH

97
55.141
46.898
17.592
1.00
50.68


O


HETATM
2849
O
HOH

98
54.804
53.900
40.431
1.00
53.97


O


HETATM
2850
O
HOH

99
81.143
54.940
13.409
1.00
49.06


O


HETATM
2851
O
HOH

100
60.601
30.026
22.828
1.00
51.45


O


HETATM
2852
O
HOH

101
91.377
38.681
33.317
1.00
51.98


O


HETATM
2853
O
HOH

102
50.491
32.970
12.092
1.00
45.61


O


HETATM
2854
O
HOH

103
65.951
63.935
21.639
1.00
45.03


O


HETATM
2855
O
HOH

104
92.613
40.981
20.428
1.00
51.23


O


HETATM
2856
O
HOH

105
66.842
34.584
37.015
1.00
49.51


O


HETATM
2857
O
HOH

106
79.154
37.014
24.773
1.00
43.76


O


HETATM
2858
O
HOH

107
72.247
31.318
24.007
1.00
40.85


O


HETATM
2859
O
HOH

108
60.754
51.022
46.130
1.00
52.32


O


HETATM
2860
O
HOH

109
45.352
44.922
33.115
1.00
39.72


O


HETATM
2861
O
HOH

110
43.049
56.846
35.553
1.00
56.39


O


HETATM
2862
O
HOH

111
93.844
47.843
37.235
1.00
47.50


O


HETATM
2863
O
HOH

112
72.886
49.728
42.684
1.00
42.85


O


HETATM
2864
O
HOH

113
44.622
43.340
15.564
1.00
48.15


O


HETATM
2865
O
HOH

114
56.638
31.718
23.687
1.00
50.30


O


HETATM
2866
O
HOH

115
75.960
53.691
−1.202
1.00
54.62


O


HETATM
2867
O
HOH

116
63.275
58.904
18.617
1.00
44.23


O


HETATM
2868
O
HOH

117
58.451
52.848
43.791
1.00
49.56


O


HETATM
2869
O
HOH

118
54.165
41.889
6.948
1.00
52.21


O


HETATM
2870
O
HOH

119
49.652
53.672
24.234
1.00
60.78


O


HETATM
2871
O
HOH

120
53.791
55.765
20.073
1.00
41.34


O


HETATM
2872
O
HOH

121
82.081
63.415
21.222
1.00
39.55


O


HETATM
2873
O
HOH

122
59.793
54.194
20.862
1.00
39.76


O


HETATM
2874
O
HOH

123
91.395
41.899
35.234
1.00
47.28


O


HETATM
2875
O
HOH

124
78.660
72.133
28.009
1.00
48.50


O


HETATM
2876
O
HOH

125
76.816
36.477
6.733
1.00
59.31


O


HETATM
2877
O
HOH

126
51.697
56.879
39.951
1.00
56.83


O


HETATM
2878
O
HOH

127
73.160
41.047
42.151
1.00
46.35


O


HETATM
2879
O
HOH

128
78.361
33.624
16.246
1.00
47.03


O


HETATM
2880
O
HOH

129
65.071
63.965
35.876
1.00
40.53


O


HETATM
2881
O
HOH

130
75.546
70.802
31.702
1.00
43.13


O


HETATM
2882
O
HOH

131
45.695
41.554
13.117
1.00
46.21


O


HETATM
2883
O
HOH

132
74.770
75.486
30.649
1.00
50.17


O


HETATM
2884
O
HOH

133
61.457
33.492
27.149
1.00
38.92


O


HETATM
2885
O
HOH

134
78.747
70.267
25.631
1.00
47.28


O


HETATM
2886
O
HOH

135
67.587
59.325
38.812
1.00
44.68


O


HETATM
2887
O
HOH

136
56.460
34.436
25.338
1.00
50.36


O


HETATM
2888
O
HOH

137
87.425
55.130
37.159
1.00
57.77


O


HETATM
2889
O
HOH

138
62.549
55.054
1.389
1.00
52.64


O


HETATM
2890
O
HOH

139
63.046
39.459
6.185
1.00
33.80


O


HETATM
2891
O
HOH

140
52.457
45.986
7.697
1.00
51.12


O


HETATM
2892
O
HOH

141
68.162
53.372
47.262
1.00
59.06


O


HETATM
2893
O
HOH

142
54.370
73.869
39.160
1.00
53.30


O


HETATM
2894
O
HOH

143
58.332
49.599
44.654
1.00
56.73


O


HETATM
2895
O
HOH

144
57.914
66.131
38.178
1.00
50.57


O


HETATM
2896
O
HOH

145
69.153
44.094
0.472
1.00
58.32


O


HETATM
2897
O
HOH

146
70.955
57.555
14.580
1.00
42.14


O


HETATM
2898
O
HOH

147
64.290
80.942
33.633
1.00
50.16


O


HETATM
2899
O
HOH

148
71.059
63.093
33.999
1.00
48.63


O


HETATM
2900
O
HOH

149
68.250
44.131
48.927
1.00
56.50


O


HETATM
2901
O
HOH

150
53.995
61.899
36.136
1.00
38.46


O


HETATM
2902
O
HOH

151
61.723
64.570
38.471
1.00
57.73


O


HETATM
2903
O
HOH

152
72.479
45.867
47.190
1.00
59.67


O


HETATM
2904
O
HOH

153
72.416
63.521
16.449
1.00
43.93


O


HETATM
2905
O
HOH

154
72.663
61.263
18.483
1.00
55.81


O


HETATM
2906
O
HOH

155
78.290
65.312
33.155
1.00
53.08


O


HETATM
2907
O
HOH

156
94.608
53.219
22.065
1.00
52.11


O


HETATM
2908
O
HOH

157
75.671
73.066
28.735
1.00
53.82


O


HETATM
2909
O
HOH

158
75.598
67.940
32.952
1.00
59.45


O


HETATM
2910
O
HOH

159
75.773
35.559
27.231
1.00
45.26


O


HETATM
2911
O
HOH

160
97.730
48.875
26.955
1.00
50.24


O


HETATM
2912
O
HOH

161
95.855
46.417
27.517
1.00
51.32


O


HETATM
2913
O
HOH

162
94.096
48.923
26.023
1.00
51.83


O


HETATM
2914
O
HOH

163
91.721
50.895
35.397
1.00
58.59


O


HETATM
2915
O
HOH

164
92.397
47.915
34.455
1.00
52.43


O


HETATM
2916
O
HOH

165
97.410
43.546
26.476
1.00
59.63


O


HETATM
2917
O
HOH

166
90.165
38.748
36.119
1.00
56.38


O


HETATM
2918
O
HOH

167
94.316
37.414
34.403
1.00
54.53


O


HETATM
2919
O
HOH

168
43.075
36.122
24.970
1.00
55.92


O


HETATM
2920
O
HOH

169
67.736
76.231
16.895
1.00
56.81


O


HETATM
2921
O
HOH

170
71.677
32.859
30.158
1.00
52.78


O


HETATM
2922
O
HOH

171
68.554
30.002
38.857
1.00
54.82


O


HETATM
2923
O
HOH

172
73.000
33.391
26.251
1.00
47.75


O


HETATM
2924
O
HOH

173
68.812
31.473
26.121
1.00
56.59


O


HETATM
2925
O
HOH

174
63.228
31.574
25.697
1.00
48.31


O


HETATM
2926
O
HOH

175
62.682
33.531
30.030
1.00
49.27


O


HETATM
2927
O
HOH

176
65.167
31.555
29.683
1.00
55.99


O


HETATM
2928
O
HOH

177
56.336
48.164
14.845
1.00
48.86


O


HETATM
2929
O
HOH

178
78.620
50.501
10.475
1.00
62.38


O


HETATM
2930
O
HOH

179
84.701
43.066
9.965
1.00
56.01


O


HETATM
2931
O
HOH

180
77.072
52.215
−3.925
1.00
52.09


O


HETATM
2932
O
HOH

181
81.505
72.460
16.927
1.00
56.81


O


HETATM
2933
O
HOH

182
56.776
62.766
36.110
1.00
35.88


O


HETATM
2934
O
HOH

183
52.708
50.106
19.084
1.00
46.95


O


HETATM
2935
O
HOH

184
58.949
41.892
6.150
1.00
50.09


O


HETATM
2936
O
HOH

185
66.279
40.996
3.132
1.00
51.65


O


HETATM
2937
O
HOH

186
72.364
36.495
6.684
1.00
54.90


O


HETATM
2938
O
HOH

187
64.663
41.304
7.894
1.00
34.55


O


HETATM
2939
O
HOH

188
49.873
42.836
7.978
1.00
55.76


O


HETATM
2940
O
HOH

189
57.589
27.901
17.205
1.00
55.94


O


HETATM
2941
O
HOH

190
54.487
27.148
17.217
1.00
56.50


O


HETATM
2942
O
HOH

191
74.055
29.387
14.028
1.00
55.18


O


HETATM
2943
O
HOH

192
73.877
34.935
8.889
1.00
54.31


O


HETATM
2944
O
HOH

193
64.874
25.940
14.827
1.00
47.78


O


HETATM
2945
O
HOH

194
40.739
38.113
26.191
1.00
56.93


O


HETATM
2946
O
HOH

195
81.037
48.857
11.250
1.00
51.13


O


HETATM
2947
O
HOH

196
43.149
34.719
28.062
1.00
59.10


O


HETATM
2948
O
HOH

197
63.348
58.590
43.529
1.00
57.64


O


HETATM
2949
O
HOH

198
48.595
31.656
25.612
1.00
58.04


O


HETATM
2950
O
HOH

199
58.778
58.864
41.117
1.00
54.64


O


HETATM
2951
O
HOH

200
52.055
49.602
40.062
1.00
50.74


O


HETATM
2952
O
HOH

201
55.370
44.532
39.918
1.00
58.59


O













CONECT
202
2494






CONECT
1501
1502


CONECT
1502
1501
1503
1505


CONECT
1503
1502
1504


CONECT
1504
1503
1507


CONECT
1505
1502
1506


CONECT
1506
1505


CONECT
1507
1504


CONECT
2494
202


CONECT
2731
2732
2733
2734
2735


CONECT
2732
2731


CONECT
2733
2731


CONECT
2734
2731


CONECT
2735
2731
2736


CONECT
2736
2735
2737


CONECT
2737
2736
2738
2739


CONECT
2738
2737
2743


CONECT
2739
2737
2740
2741


CONECT
2740
2739


CONECT
2741
2739
2742
2743


CONECT
2742
2741


CONECT
2743
2738
2741
2744


CONECT
2744
2743
2745
2751


CONECT
2745
2744
2746


CONECT
2746
2745
2747


CONECT
2747
2746
2748
2751


CONECT
2748
2747
2749
2750


CONECT
2749
2748


CONECT
2750
2748


CONECT
2751
2744
2747




















MASTER
497
0
4
14
18
0
0
6
2951
1
30
39



END
















TABLE 8







Comparison of published IMPDH structures.












Species
Resolution
R (Rfree) in %
Missing residues
Heteroatoms
PDB ID





Human
2.9 Å
24.4 (27.0)
2nd domain 130–139, 159–177,
CPR, SAD
1B30





flap 400–448, end 499–514


Hamster
2.6 Å
21.7 (28.5)
2nd domain 121–177, flap 421–
K+, XMP*,
1JR1





436
MPA


Borrelia
2.4 Å
21.5 (26.8)
2nd domain 92–129, flap 309–
SO4+
1EEP





344


S. pyogenes
1.9 Å
23.4 (25.8)
Flap 401–414, end 490–493
IMP
1ZFJ


T. foetus apo
2.3 Å
21.8 (26.5)
2nd domain 102–221, loop
SO4+
1AK5





314–327, flap 413–431


T. foetus +
2.6 Å
20.3 (26.4)
2nd domain 102–221, loop
XMP
N/A


XMP


314–324, flap 413–431, end





484–503





* denotes covalent intermediate













TABLE 9







Data collection and refinement statistics.









Structure
RMP
RMP + MPA












Wavelength (Å)
0.97
0.97


Resolution range (Å)
50–1.90
50–2.15


Resolution of outer shell (Å)
1.90–2.02
2.15–2.28


Current R (RFREE) (%)
24.3 (25.9)
23.3 (26.5)


Unique reflections
50,359
35,250


Total observations
1,289,813
620,781


I/σ1 overall/outer shell
33.77/2.39
23.59/2.05


Rsvm overall/outer shell (%)
6.2/68.9
7.2/49.1


Completeness overall/outer shell (%)
99.9/100
94.0/79.5


Degrees collected
25
20


Number of ordered water molecules
211
120


Deviation from ideal bond lengths (Å)
0.005
0.006


Bond angle RMSD (°)
1.2
1.2


Dihedral angle RMSD (°)
22.7
22.6


Improper angle RMSD (°)
0.71
0.70


Cell dimensions α = β = χ = 90°, a =
154.7
155.1


b = c (Å)


Space group
P432
P432


Mosaicity (°)
0.45
0.50

## Claims

1. The crystalline complex comprising T. foetus IMPDH in complex with ribavirin monophosphate (1-β-D-ribofuranosyl-1,2,4-triazole-3-carboxamide monophosphate), having atomic coordinates set forth in Table 7.

2. The crystalline complex comprising T. foetus IMPDH in complex with ribavirin monophosphate and mycophenolic acid, having atomic coordinates set forth in Table 6.