# Patent

## Title
Method for designing a compound based on the three dimensional structure of phosphoinositide dependent protein kinase 1 (PDK1)

## Abstract

A method for selecting a compound for modulating the activity of phosphoinositide dependent protein kinase 1 (PDKI) is provided. The method may comprise modelling a three dimensional structure of a plurality of molecules in a computer, comparing with the three dimensional structure of the compounds with that of a reference structure such as at least part of a protein kinase catalytic domain of PDK1, and selecting the compound based on a predicted interacting ability of the molecules to the protein kinase catalytic domain. Also a method for selecting a compound for modulating the activity of hydrophobic pocket containing protein kinase is provided. In this method, the reference structures may be one or more of a phosphate binding pocket of PDK1, a hydrophobic pocket of PDK1, and αC helix or region interacting therewith of PDK1.

## Background
CROSS-REFERENCE TO RELATED APPLICATION
The present application is the US national phase under 35 USC 371 of International Application No. PCT/GB03/02509, filed Jun. 9, 2003, and published in the English language as WO 03/104481.
REFERENCE TO SEQUENCE LISTING
The present application incorporates by reference the sequence listing submitted as an ASCII text filed via EFS-Web on Feb. 5, 2010. The Sequence Listing is provided as a file entitled 8506534.1.txt, created on-Feb. 5, 2010, which is 4 Kb in size.
FIELD OF THE INVENTION
The present invention relates to protein kinase catalytic domain structures and mutants and screening assays making use thereof.
BACKGROUND OF THE INVENTION
The 3-Phosphoinositide Dependent Protein Kinase-1 (PDK1) is a key protein kinase, regulating activity of a group of related protein kinases through phosphorylation. These kinases include isoforms of Protein Kinase B (also known as Akt) [Brazil and Hemmings, 2001, Scheid and Woodgett, 2001], p70 ribosomal S6 kinase (S6K) [Alessi et al., 1997, Volarevic and Thomas, 2001], p90 ribosomal S6 Kinase (RSK) [Frodin and Gammeltoft, 1999] and the serum and glucocorticoid induced-protein kinase (SGK) [Lang and Cohen, 2001]. These enzymes are stimulated by hormones and growth factors and phosphorylate regulatory proteins mediating the various physiological effects of these agonists.
PDK1 possesses an N-terminal kinase catalytic domain and a C-terminal pleckstrin homology (PH) domain [Alessi et al., 1997, Stephens et al., 1998]. PDK1 activates its substrates by phosphorylating these kinases at their activation loop (reviewed in [Alessi, 2001, Toker and Newton, 2000]). The phosphorylation of PKB by PDK1 is dependent upon prior activation of the phosphoinositide 3-kinase (PI-3-kinase) and the production of the second messenger, phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) which binds to the PH domains of PDK1 and PKB. This does not activate either PKB or PDK1 but instead recruits and co-localises these enzymes at the plasma membrane.
Unlike PKB, the other PDK1 substrates described thus far do not interact with PtdIns(3,4,5)P3 nor is the rate at which they are phosphorylated by PDK1 further enhanced by the binding of PDK1 to PtdIns(3,4,5)P3. Instead the ability of PDK1 to phosphorylate S6K, SGK and RSK is promoted by phosphorylation of these enzymes at a residue located C-terminal to the kinase catalytic domain in a region known as the hydrophobic motif [Alessi et al., 1997, Kobayashi and Cohen, 1999, Pullen et al., 1998]. The kinases that phosphorylate the hydrophobic motif of S6K and SGK are unknown but as the phosphorylation of this residue in vivo is dependent on PI-3-kinase activation, the hydrophobic motif kinases and/or the hydrophobic motif phosphatases may be regulated by PtdIns(3,4,5)P3. In the case of RSK isoforms, phosphorylation by the ERK1/ERK2 MAP kinases induce phosphorylation of the hydrophobic motif (reviewed in Frodin and Gammeltoft, 1999).
PDK1 belongs to the same subfamily of protein kinases as its substrates, termed the AGC protein kinases as they are related to the cAMP dependent protein kinase (PKA)/cGMP dependent protein kinase/Protein kinase C (PKC). PKA is the only AGC kinase whose crystal structure has been solved. Like all protein kinases, its catalytic core possesses an N-terminal lobe consisting mainly of β-sheet and a predominantly α-helical C-terminal lobe [Taylor et al., 1992, Husen and Kuriyan, 2002]. The ATP binding site is located in between the 2 lobes [Johnson et al., 2001, Knighton et al., 1991]. At the very C-terminus, PKA possesses an extended loop that terminates in the sequence FXXF (SEQ ID NO:1) which resembles the first part of the hydrophobic motif phosphorylation site of S6K and SGK (FXXFS/TY, SEQ ID NO:2) in which the Ser/Thr is the phosphorylated residue [Biondi et al., 2000]. In the structure of PKA, the FXXF motif (SEQ ID NO:1) is buried in a hydrophobic pocket in the small lobe of the PKA catalytic domain [Knighton et al., 1991] and mutation of either of the Phe residues drastically reduces PKA activity towards a peptide substrate [Etchebehere et al., 1997]. Unlike other AGC kinases, PDK1 does not possess a hydrophobic motif C-terminal to its catalytic domain. However, there is evidence that PDK1 possesses a hydrophobic pocket in the small lobe of its catalytic domain similar to that in PKA. We have biochemically demonstrated that the interaction of PDK1 with four of its substrates (S6K1, SGK1, PKζ and PKC related kinase-2 (PRK2)) is reduced or abolished by mutation of residues predicted to form part of this pocket [Balendran et al., 2000, Biondi et al., 2000]. Furthermore, mutation of a central residue in the predicted pocket, Leu 155, prevented PDK1 from phosphorylating and activating S6K1 and SGK1 without affecting its ability to phosphorylate either PKB or a short peptide substrate that encompasses the activation loop of PKB (T308tide) [Biondi et al., 2000]. The hydrophobic pocket on the kinase domain of PDK1 has been termed the “PIF-pocket” after the name of the first AGC-kinase hydrophobic motif-containing peptide (PDK1 Interacting Fragment) that was found to bind PDK1 [Balendran et al., 1999a]. It has been suggested that the PIF-pocket in PDK1 functions as a docking site, enabling PDK1 to interact with some of its physiological substrates. Furthermore, there is evidence that phosphorylation of the hydrophobic motif of S6K1, SGK and RSK2 [Balendran et al., 1999b, Biondi et al., 2001, Frodin et al., 2000] promotes the interaction of these enzymes with PDK1. These findings suggest that the PIF-pocket on PDK1 could contain a phosphate binding site promoting the binding of PDK1 to a subset of substrates (S6K, SGK and RSK) once these enzymes have been phosphorylated at their hydrophobic motif. This would result in a physiological phosphate dependent interaction. In addition there is evidence that occupancy of the PIF-pocket activates PDK1 as peptides that encompass the hydrophobic motif of PRK2 [Biondi et al., 2000] and RSK [Frodin et al., 2000] induce a 4-6-fold activation of PDK1.
Previous predicted structures PDK1 catalytic domain were obtained using homology modelling methods based upon structural information available from the catalytic domain of PKA (Biondi et al., 2000). These predictions of the PDK1 catalytic domain structure were thus biased towards the catalytic domain from which the structural information was obtained.
SUMMARY OF THE INVENTION
We have determined a crystal structure for the kinase domain of the AGC family protein kinase PDK. The structure defines the PIF-pocket and reveals an adjacent possible phosphate binding site. Furthermore, we have performed structure-based mutagenesis and biochemical analysis which support the existence of such a phosphate-binding site. This may mediate the phosphate dependent docking interaction with substrates such as (for PDK1) S6K and SGK. We have used a novel algorithm to define the conformational state of the crystallised PDK1 relative to all the reported structures of PKA, which shows that while PDK1 has all the signs of being in an active form in the crystal, its overall conformation is in-between and ‘open’ and ‘closed’ state. We have also determined crystal structures for the kinase domain of PDK1 in complex with modulators of PDK1 activity.
On the basis of this work we provide drug screening methods and mutated protein kinase molecules (which are useful in, for example, drug screening methods).
A first aspect of the invention provides a method for selecting or designing a compound for modulating the activity of phosphoinositide dependent protein kinase 1 (PDK1), the method comprising the step of using molecular modelling means to select or design a compound that is predicted to interact with the protein kinase catalytic domain of PDK1, wherein a three-dimensional structure of at least a part of the protein kinase catalytic domain of PDK1 is compared with a three-dimensional structure of a compound, and a compound that is predicted to interact with the said protein kinase catalytic domain is selected, wherein the three-dimensional structure of at least a part of the protein kinase catalytic domain of PDK1 is a three-dimensional structure (or part thereof) determined for a polypeptide consisting of residues equivalent to residues 51 to 359 of full length human PDK1, or a fragment or fusion thereof.



BRIEF DESCRIPTION OF THE DRAWINGS
FIG. 1 provides an overview of the PDK1 structure.
FIGS. 2A and 2B show the PIF-pocket.
FIG. 3 shows a structure-based sequence alignment
FIGS. 4A-C show PDK1 binding & activation studies.
FIGS. 5A and 5B show interactions of regulatory phosphates with the αC helix.
FIGS. 6A and 6B show essential dynamics.
FIG. 7 shows alignment of AGC protein kinase family members.
FIG. 8 shows staurosporine and UCN-01 electron density.
FIG. 9 shows details of the inhibitor binding sites.



DETAILED DESCRIPTION OF THE INVENTION
The term PDK1 as used herein includes a polypeptide (a PDK1 polypeptide) comprising the amino acid sequence identified as PDK1 in Alessi D. R et al (1997) Curr. Biol. 7: 261-269, Alessi D. R et al (1997) Curr. Biol. 7: 776-789, Stokoe D et al (1997) Science 277: 567-570 or Stephens L et al (1998) Science 279: 710-714, or a variant, fragment, fusion or derivative thereof, or a fusion of a said variant or fragment or derivative, for example as described in WO98/41638, incorporated herein by reference. It is preferred that the said PDK1 polypeptide is a protein kinase. It is preferred that the said PDK1 polypeptide is a protein kinase that is capable of phosphorylating a threonine residue that lies in a Thr-Phe-Cys-Gly-Thr-Xaa-Glu-Leu consensus motif (where the underlined Thr corresponds to the threonine that is phosphorylated by PDK1 and Xaa is a variable residue, SEQ ID NO:9), and preferably that is capable of phosphorylating PKB, for example PKBα, at residue Thr308. The rate at which the said PDK1 polypeptide is capable of phosphorylating a threonine residue as described above may be increased in the presence of PtdIns(3,4,5)P3 or PtdIns(3,4)P2 but it will be appreciated that this is not essential. The said polypeptide may be capable of phosphorylating the equivalent residues to Thr308 of PKBα on PKC isoforms (LeGood et al (1998) Science 281: 2042-2045; et al (1998) Curr. Biol. 8: 1069-1077; Dutil et al (1998) Curr. Biol. 8:1366-1375), p70 S6 kinase (Alessi et al (1998) Curr. Biol. 8: 69-81; Pullen et al (1998) Science 279, 707-710), SGK (sequence given in Webster et al (1993) Mol. Cell. Biol. 13, 1031-2040; equivalent residues identified in US application no 112217 filed on 14 Dec. 1998; GB 9919676.8, filed on 19 Aug. 1999, and Kobayashi & Cohen (1999)) and PKA (Cheng et al (1998) Proc. Natl. Acad. Sci. USA 95: 9849-9854). It may further be preferred that the substrate specificity and/or other characteristics of the said PDK1 polypeptide in vitro may be substantially as reported in Alessi D. R et al (1997) Curr. Biol. 7: 261-269, Alessi D. R et al (1997) Curr. Biol. 7: 776-789, Stokoe D et al (1997) Science 277: 567-570 or Stephens L et al (1998) Science 279: 710-714.
We have found that a fragment of PDK1 consisting essentially of residues equivalent to residues 51 to 359 of full length human PDK1 is particularly beneficial for determining a structure for the catalytic domain of PDK1. This fragment has, for example, protein kinase activity and surprisingly beneficial solubility and stability characteristics which make it particularly suitable for structural studies, for example formation of crystals which may be analysed by X-ray crystallography methods. Other fragments of PDK1 were surprisingly found to be unsuitable for crystallisation, as discussed in Example 5.
It is particularly preferred that the structure is one determined for the fragment consisting of residues 51 to 359 of full length human PDK1. The fragment may comprise an N-terminal or C-terminal fusion polypeptide (ie amino acid sequence not derived from PDK1), though this is preferably of less than or equal to about 10, 5, 4, 3, 2 or 1 amino acids. For example, it is particularly preferred that the structure is one determined for a polypeptide consisting residues 51 to 359 of full length human PDK1 and the amino acid sequence Gly-Pro (or less preferably other sequence forming part of a protease cleavage site) preceding the methionine corresponding to Met51 of human PDK1. A further preferred structure is one determined for the fragment consisting essentially of residues 71 to 359 of full length human PDK1 (or residues equivalent thereto), which also has protein kinase activity.
It is particularly preferred that the structure is one determinable by a method as described in Example 1, for example a structure obtainable by X-ray analysis from a crystal obtainable using a mother liquor solution comprising ammonium sulphate, preferably between 1.8 and 2.2M. It is particularly preferred that the mother liquor solution is of pH 7 to 9, preferably 7 to 8.5, most preferably pH8.5, and comprises ammonium sulphate and preferably ATP. Crystals may form in the absence of ATP but better crystals may be obtained in the presence of ATP. Preferably the crystal is obtainable using a mother liquor solution containing 0.1M Tris/HCl pH 8.5, 2.0 M ammonium sulphate, 16.6 mM ATP. Further preferred details of the crystallisation and X-ray analysis are described in Example 1, for example as partially summarised in Table 1 (shown in Example 1).
It is particularly preferred that the structure is that represented by the structure co-ordinates shown in Examples 2, 3 or 4, or a structure based or modelled on such a structure or co-ordinates. The co-ordinates shown in Example 2 are for the PDK1 fragment (SEQ ID NO:102) with all alternate side chains. The co-ordinates shown in Example 3 are for the PDK1 fragment (SEQ ID NO:102) without alternate side chains. The co-ordinates shown in Example 4 are for the dimer of the PDK1 fragment (SEQ ID NO:102), without alternate side chains; chain A is the molecule for which co-ordinates are given in Examples 2 and 3, and chain B is the symmetry-related molecule.
The structure may be one determined following crystallisation in the presence of a known or potential interactor with PDK1 or modulator of PDK1 activity (as discussed further below), for example a known or potential inhibitor of PDK1 activity. For example, the structure may be one determined following crystallisation in the presence of a known protein kinase inhibitor, for example an inhibitor that binds at the ATP binding site, for example an ATP-competitive inhibitor, for example staurosporine or a staurosporine derivative, for example UCN-01. Examples of such crystallisation techniques and analysis are given in Example 6, and examples of co-ordinates are given in Examples 7 and 8. Example 7 represents the co-ordinates of PDK1 fragment (SEQ ID NO:102) co-crystallised with Staurosporine, whereas in Example 8, the co-ordinates of PDK1 fragment (SEQ ID NO:102) co-crystallised with UCN-01.
It will be appreciated that some variation in crystallisation conditions (for example different mother liquors) may be required for co-crystallisation with different molecules. Techniques for investigating suitable crystallisation conditions in each case will be well known to those skilled in the art.
A further aspect of the invention provides a crystalline form of a polypeptide as defined in any of the preceding aspects of the invention, for example a polypeptide consisting of residues equivalent to residues 51 to 359 of full length human PDK1, or a fragment or fusion thereof; a polypeptide consisting of residues 51 to 359 of full length human PDK1 or a fusion thereof; a polypeptide consisting of residues 51 to 359 of full length human PDK1 and the amino acid sequence Gly-Pro preceding the methionine corresponding to Met51 of human PDK1; a polypeptide consisting of residues 71 to 359 of full length human PDK1 or a fusion thereof.
The crystalline form may further comprise co-crystallised molecule, for example a known or potential interactor with PDK1 or modulator of PDK1 activity, or a test compound whose properties vis a vis PDK1 may not be known. For example, the co-crystallised molecule, for example test compound, may be a molecule that is known to modulate protein kinase activity, or may already be known to modulate PDK1 protein kinase activity. For example, the co-crystallised molecule may be staurosporine, the staurosporine derivative UCN-01 (7-hydroxyl staurosporine) or other staurosporine derivative.
Such co-crystallisation and structures determined from co-crystallised molecules may be useful in molecular modelling and in determining features of the polypeptide and compound that are important for interaction. This may be useful in designing or selecting further test compounds, for example as discussed in Example 6.
In one embodiment it is preferred that the modelled molecule is predicted to bind to a region of the structure termed the “PIF binding pocket”, the “phosphate binding pocket” and/or the a C helix (residues equivalent to 123-136 of full length human PDK1), particularly the residue equivalent to Arg 131 of full length human PDK1, or interacting regions. As discussed in Example 1, the PIF binding pocket is considered to be formed by residues including Lys115, Ile118, Ile119 on the αB helix, Val124, Val127 on the αC helix and Leu 155 on 13-sheet 5. The phosphate binding pocket is considered to be formed by residues including Lys76, Arg 131, Thr 148 and Gln150. Residues of the αC helix that are considered to interact either with phosphate bound in the phosphate binding site or intermolecularly with phosphorylated Ser241 of PDK1 include Arg131 (phosphate binding site) and Arg 129 and His126 (phosphorylated Ser241). Glu 130 is involved in binding the α-phosphate of the bound ATP, and Val124 and Val127 form part of the PIF binding pocket, as discussed in Example 1.
It is preferred that the compound is for modulating the protein kinase activity of PDK1. The protein kinase activity of PDK1 that is modulated may be phosphorylation of the underlined residue in a polypeptide with the amino acid sequence Thr/Ser-Phe-Cys-Gly-Thr-Xaa-Glu-Leu (“PDK1” activity, SEQ ID NO:9). Alternatively or in addition, the modulated activity may be phosphorylation of the underlined residue in a polypeptide with the amino acid sequence Phe-Xaa-Xaa-Phe-Ser/Thr-Phe/Tyr (“PDK2” activity, SEQ ID NO:11). The substrate polypeptide may be, for example, a PKB, SGK, p70 S6 kinase, PKC or (in relation only to phosphorylation of the underlined residue in a polypeptide with the amino acid sequence Thr/Ser-Phe-Cys-Gly-Thr-Xaa-Glu-Leu (SEQ ID NO:9) PKA polypeptide. The modulated protein kinase activity may be towards PKB or other PH-domain-comprising/phosphoinositide-binding substrate of PDK1; or SGK, S6K or other substrate of PDK1 whose phosphorylation by PDK1 is promoted by phosphorylation of the substrate on the Ser/Thr of the “hydrophobic motif” FXXFS/TY (SEQ ID NO:2); or an artificial substrate such as T308tide (which comprises the sequence of PKB which is phosphorylated by PDK1) or PDKtide (which comprises the sequence of PKB which is phosphorylated by PDK1 (eg T308tide) fused to a sequence mimicking a phosphorylated hydrophobic motif ie FXXFZY (SEQ ID NO: 2), in which Z is a negatively charged (for example acidic) residue (eg PIFtide)). Such substrates for PDK1 are discussed, for example, in WO 01/44497. Other activities of PDK1 that may be modulated include interactions with other polypeptides or phosphoinositides and/or intramolecular interactions.
It is preferred that the three-dimensional structure of at least a part of the protein kinase catalytic domain of the PDK1 is a three-dimensional structure of at least a part of the PIF binding pocket, the phosphate binding pocket and/or the α C helix, or interacting regions of PDK1, and a compound that is predicted to interact with the said PIF binding pocket, the phosphate binding pocket and/or the α C helix, or interacting regions of PDK1 is selected. Alternatively, the compound may bind to a portion of said PDK1 polypeptide that is not the PIF binding pocket, the phosphate binding pocket and/or the α C helix, or interacting regions of PDK1, for example so as to interfere with the binding of the ATP or substrate polypeptide or their access to the catalytic site. In a still further example, the compound may bind to a portion of PDK1 so as to decrease said polypeptide's activity by an allosteric effect. This allosteric effect may be an allosteric effect that is involved in the natural regulation of PDK1's activity.
It is further preferred that the three-dimensional structure of at least a part of the protein kinase catalytic domain of PDK1 is a three-dimensional structure of the part of the protein kinase catalytic domain of PDK1 that is defined by residues Lys115, Ile118, Ile119 (on the αB helix), Val124, Val127 (on the αC helix) and Leu 155 (on 13-sheet 50 and/or residues Lys76, Arg 131, Thr 148 and Gln150 and/or residues Arg131, Arg 129, His126, Glu 130 of full-length human PDK1 and a compound that is predicted to interact with the said part of the protein kinase catalytic domain is selected.
For example, it is preferred if the portions of the structure of PDK1 shown in FIGS. 1 and 2 as forming the PIF binding pocket and/or phosphate binding pocket and/or αC helix interactions (for example with phosphoserine241) are compared with the structure of the candidate compound.
A further aspect of the invention provides a method for selecting or designing a compound for modulating the activity of a hydrophobic pocket (PIF binding pocket)-containing protein kinase having a hydrophobic pocket in the position equivalent to the hydrophobic pocket of human PDK1 that is defined by residues including Lys115, Ile118, Ile119, Val124, Val127 and/or Leu155 of full-length human PDK1 and further having a phosphate binding pocket in the position equivalent to the phosphate binding pocket of human PDK1 that is defined by residues including Lys76, Arg131, Thr148 and/or Gln150, the method comprising the step of using molecular modelling means to select or design a compound that is predicted to interact with the said hydrophobic pocket-containing protein kinase, wherein a three-dimensional structure of a compound is compared with a three-dimensional structure of the said phosphate binding pocket and optionally also the hydrophobic pocket and/or αC helix or region interacting therewith, and a compound that is predicted to interact with the said phosphate binding pocket and optionally also the hydrophobic pocket and/or αC helix or region interacting therewith, is selected.
The three-dimensional structure of a compound may be compared with the three-dimensional structure of the hydrophobic and/or phosphate binding pocket and/or αC helix or region interacting therewith, as appropriate. A compound that can interact with the hydrophobic pocket and/or phosphate binding pocket, in particular residues noted above as defining such regions, in a similar manner (for example similar separation and/or type of interaction ie hydrophobic or ionic, and/or similar cumulative energy of interaction) to an interacting polypeptide such as S6K-pHM may be selected. Methods of assessing the interaction are well known to those skilled in the art and are discussed further below.
The three-dimensional structures that are compared may be, as appropriate, predicted or modelled three-dimensional structures (for example on the basis of a PDK1 structure as referred to above, for example as represented by the co-ordinates given in Examples 2, 3 or 4 or 6 or 7) or may be three-dimensional structures that have been determined, for example by techniques such as X-ray crystallography, as well known to those skilled in the art. The three-dimensional structures may be displayed by a computer in a two-dimensional form, for example on a computer screen. The comparison may be performed using such two-dimensional displays.
The following relate to molecular modelling techniques: Blundell et al (1996) Structure-based drug design Nature 384, 23-26; Bohm (1996) Computational tools for structure-based ligand design Prog Biophys Mol Biol 66(3), 197-210; Cohen et al (1990) J Med Chem 33, 883-894; Navia et al (1992) Curr Opin Struct Biol 2, 202-210.
The following computer programs, for example, may be useful in carrying out the method of this aspect of the invention: GRID (Goodford (1985) J Med Chem 28, 849-857; available from Oxford University, Oxford, UK); MCSS (Miranker et al (1991) Proteins: Structure, Function and Genetics 11, 29-34; available from Molecular Simulations, Burlington, Mass.); AUTODOCK (Goodsell et al (1990) Proteins: Structure, Function and Genetics 8, 195-202; available from Scripps Research Institute, La Jolla, Calif.); DOCK (Kuntz et al (1982) J Mol Biol 161, 269-288; available from the University of California, San Francisco, Calif.); LUDI (Bohm (1992) J Comp Aid Molec Design 6, 61-78; available from Biosym Technologies, San Diego, Calif.); LEGEND (Nishibata et al (1991) Tetrahedron 47, 8985; available from Molecular Simulations, Burlington, Mass.); LeapFrog (available from Tripos Associates, St Louis, Mo.); Gaussian 92, for example revision C (M J Frisch, Gaussian, Inc., Pittsburgh, Pa. ©1992); AMBER, version 4.0 (P A Kollman, University of California at San Francisco, ©1994); QUANTA/CHARMM (Molecular Simulations, Inc., Burlington, Mass. ©1994); and Insight II/Discover (Biosym Technologies Inc., San Diego, Calif. ©1994). Programs may be run on, for example, a Silicon GraphicsTM workstation, Indigo2TM or IBM RISC/6000TM workstation model 550.
Several in silico methods could be employed, for example, via a substructure search for new ligands using programmes such as CHEM DRAW or CHEM FINDER. The basic structure of the natural ligand (for example a phosphorylated hydrophobic motif peptide such as 56K-pHM) capable of binding to PDK1 (or other protein kinase) is taken (or predicted) and various structural features of it (for example the hydrophobic and negatively charged entities) are submitted to a programme which will searches a set of chemical company catalogues for chemicals containing this substructure.
These compounds are then screened by eye for groups that could not interact with the PIF/phosphate binding pockets (or the αC residues/interacting region) because, for example, they are too large or have steric or charge hindrance, and those are discarded. The remaining chemicals are submitted to a PRODRG server and topologies/co-ordinates for these chemicals are created. These chemicals are modelled into the structure, from which chemicals that are possibly able to bind to the PIF/phosphate binding site domain/αC helix/interacting region are selected. Further details of the PRODRG programme are available in the art, for example, from Daan van Aalten Laboratory.
These compounds may then be ordered or synthesised and assessed, for one or more of ability to bind to and/or modulate PDK1 (or other protein kinase) activity. The compounds may be crystallised with the PDK1 or other protein kinase protein and the structure of any complex determined, as illustrated in Examples 6 to 8.
An alternative approach is to use PRODRG: a tool for generating GROMOS/MOL2/WHATIF topologies and hydrogen atom positions from small molecule PDB files. We take the natural ligand and computationally vary all possible groups at each site on the ligand, with a variety of new groups while the protein co-ordinates and the ligand back-bone co-ordinates remain fixed the results can then be screened for hindrance and repulsion, and the molecules are obtained either through catalogues or made.
As noted above, the selected or designed compound may be synthesised (if not already synthesised) or purified and tested for its effect on the relevant hydrophobic/phosphate pocket-containing protein kinase, for example its effect on the protein kinase activity. The compound may be tested in a screening method of the invention or other screening method. The compound may be formulated for pharmaceutical use, for example for use in in vivo trials in animals or humans, or for use in agriculture, for example as an antifungal agent.
It may be useful to analyse a protein kinase structure (for example a structure determined or predicted for a complex of the protein kinase with a binding partner) in order to determine the activation state of the structure. This may be useful in further modelling binding of the binding partner to the protein kinase in other activation states, and in predicting how the binding partner may affect the activation state of the protein kinase or compete with other potential binding partners. It may also be useful in designing and assessing derivatives of the binding partner.
Thus, a further aspect of the invention provides a method for assessing the activation state of a structure for a protein kinase, wherein the structure is analysed using principle component analysis of the structure co-ordinates. The method may further comprise the step of classifying the activation state of the structure as “open”, “closed” or “intermediate”. Details of the analysis, which involves the generation of eigenvectors and associated eigenvalues are given in Example 1. The analysis makes use of techniques described in Amadei et al (1993) Essential dynamics of proteins. Proteins 17, 412-425.
The hydrophobic/phosphate pocket-containing protein kinase may be PDK1. Alternatively, it may be an isoform of Serum and Glucocorticoid stimulated protein kinase (SGK), Protein Kinase B (PKB), p70 S6 kinase, p90 RSK, PKC isoforms (for example PKCα, PKCδ, PKCζ), PRK1, PRK2, MSK1 or MSK2. Hydrophobic/phosphate pocket-containing protein kinases and their EMBL database accession numbers are listed in Table I. Sequences considered to form the phosphate binding pocket from representative hydrophobic/phosphate pocket-containing protein kinases are shown in FIG. 5. All AGC family protein kinases other than PKA may be hydrophobic/phosphate pocket-containing protein kinases, as defined above. In addition to the protein kinases shown in FIG. 7, rhodopsin and G-protein coupled receptor protein kinases, for example, may possibly also have a hydrophobic/phosphate pocket as defined above.
The terms SGK, PKB, p70 S6 kinase, p90 RSK, PKCα, PKCδ, PKCζ or PRK2, for example, as used herein include a polypeptide (a SGK, PKB, PKA, p70S6 kinase, p90 RSK, PKCα, PKCδ, PKCζ or PRK2 polypeptide) comprising the amino acid sequence identified as a SGK, PKB, p70 S6 kinase, p90 RSK, PKCα, PKCδ, PKCζ or PRK2, respectively, in the relevant EMBL database records indicated in Table 2.










TABLE 2






Activation or
AGC Hydrophobic
Accession



T-Loop
Motif
number







consensus:
TFCGTxxYxAPD
FxxFSY




(SEQ ID NO:41)
(SEQ ID NO:42)



L E
YTF


PKBα
TFCGTPEYLAPE
FPQFSY
(Y15056)



(SEQ ID NO:45)
(SEQ ID NO:46)


PKBβ
TFCGTPEYLAPE
FPQFSY
(P31751)



(SEQ ID NO:47)
(SEQ ID NO:48)


PKBγ
TFCGTPEYLAPE
FPQFSY
(AF135794)



(SEQ ID NO:49)
(SEQ ID NO:50)


SGK1
TFCGTPEYLAPE
FLGFSY
(AAD41091)



(SEQ ID NO:51)
(SEQ ID NO:52)


SGK2
TFCGTPEYLAPE
FLGFSY
(AF169034)



(SEQ ID NO:53)
(SEQ ID NO:54)


SGK3
TFCGTPEYLAPE
FLGFSY
(AF169035)



(SEQ ID NO:55)
(SEQ ID NO:56)


PKCα
TFCGTPDYIAPE
FEGFSY
(4506067)



(SEQ ID NO:57)
(SEQ ID NO:58)


PKCβI
TFCGTPDYIAPE
FAGFSY
(4506069)



(SEQ ID NO:59)
(SEQ ID NO:60)


PKCβII
TFCGTPDYIAPE
FEGFSF
(P05127)



(SEQ ID NO:61)
(SEQ ID NO:62)


PKCγ
TFCGTPDYIAPE
FGGFTY
(P05129)



(SEQ ID NO:63)
(SEQ ID NO:64)


PKCδ
TFCGTPDYIAPE
FAGFSF
(5453970)



(SEQ ID NO:65)
(SEQ ID NO:66)


PCKζ
TFCGTPNYIAPE
FEGFEY
(4506079)



(SEQ ID NO:67)
(SEQ ID NO:68)


PKCι
TFCGTPNYIAPE
FEGFEY
(4506071)



(SEQ ID NO:69)
(SEQ ID NO:68)


PRK1
TFCGTPEFLAPE
FLDFDF
(AAC50209)



(SEQ ID NO:71)
(SEQ ID NO:72)


PRK2
TFCGTPEFLAPE
FRDFDY
(AAC50208)



(SEQ ID NO:73)
(SEQ ID NO:74)


p70-S6Kα
TFCGTIEYMAiPE
FLGFTY
(AAA36410)



(SEQ ID NO:75)
(SEQ ID NO:76)


p70-S6Kβ
TFCGTIEYMAPE
FLGFTY
(4506739)



(SEQ ID NO:77)
(SEQ ID NO:78)


p90-RSK1
SFCGTVEYMAPE
FRGFSF
(I38556)



(SEQ ID NO:79)
(SEQ ID NO:80)


p90-RSK2
SFCGTVEYMAPE
FRDFSF
(P51812)



(SEQ ID NO:81)
(SEQ ID NO:82)


p90-RSK3
SFCGTIEYMAPE
FRGFSF
(CAA59427)



(SEQ ID NO:83)
(SEQ ID NO:84)


MSK1
SFCGTIEYMAPD
FQGYSF
(AAC31171)



(SEQ ID NO:85)
(SEQ ID NO:86)


MSK2
SFCGTIEYMAPE
FQGYSF
(AAC67395)



(SEQ ID NO:87)
(SEQ ID NO:88)


PDK1
SFVGTAQYVSPE
(1)
(AF017995)



(SEQ ID NO:89)









Table 2. Alignment of the amino acid sequences surrounding the T-loop and the hydrophobic motif of AGC kinases. All the sequences and accession numbers are from human proteins. The underlined residues correspond to those that become phosphorylated. Footnotes: (1) PDK1 does not possess a hydrophobic motif.
It is preferred that the PDK1 (or, for example, SGK, PKB, PKA or p70 S6 kinase) is a polypeptide which consists of the amino acid sequence of the protein kinase PDK1 (or, for example, SGK, PKB, PKA or p70 S6 kinase as the case may be) sequence referred to above or naturally occurring allelic variants thereof. It is preferred that the naturally occurring allelic variants are mammalian, preferably human, but may alternatively be homologues from parasitic or pathogenic or potentially pathogenic organisms. Examples of such organisms and homologues, and of uses of modulators of such homologues are given in U.S. patent application No. 60/112,114, filed on 14 Dec. 1998, and applications claiming priority therefrom, or in Casamayor et al (1999) Curr Biol 9, 186-197.
The PDK1 may also be a polypeptide with the amino acid sequence of residues 51 to 359 or 404 (or 71 to 360) of full-length human PDK1; this may comprise the protein kinase domain of PDK1, as described in Example 2. The PDK1 (or SGK, PKB, PKA or p70 S6 kinase) may also be Myc epitope-tagged or His-tagged, as described in Example 1. The p70 S6 kinase, for example, may have a His tag at its N-terminus and/or may lack the carboxy terminal 104 residues (p70 S6K-T2). The PDK1 or SGK may be a Saccharomyces cerevisiae homologue, for example Pkh1 or Pkh2 (PDK1 homologues) or Ypk1 or Yrk2 (SGK homologues), as described in Casamayor et al (1999) Curr Biol 9, 186-197.
It is particularly preferred, although not essential, that the variant or fragment or derivative or fusion of the PDK1, or the fusion of the variant or fragment or derivative has at least 30% of the enzyme activity of full-length human PDK1 with respect to the phosphorylation of full-length human PKBα on residue Thr308 or SGK1 on residue Thr 256 in either the presence or absence of PtdIns(3,4,5)P3 or PtdIns(3,4)P2. It is more preferred if the variant or fragment or derivative or fusion of the said protein kinase, or the fusion of the variant or fragment or derivative has at least 50%, preferably at least 70% and more preferably at least 90% of the enzyme activity of PDK1 with respect to the phosphorylation of PKBα or SGK1. However, it will be appreciated that variants or fusions or derivatives or fragments which are devoid of enzymatic activity may nevertheless be useful, for example by interacting with another polypeptide. Thus, variants or fusions or derivatives or fragments which are devoid of enzymatic activity may be useful in a binding assay, which may be used, for example, in a method of the invention in which modulation of an interaction of a mutated PDK1 of the invention and optionally also PDK1 with a interacting polypeptide or compound, for example an interacting polypeptide comprising the amino acid sequence motif Phe/Tyr-Xaa-Xaa-Phe/Tyr (SEQ ID NO:92), for example Phe/Tyr-Xaa-Xaa-Phe/Tyr-Zaa-Phe/Tyr (SEQ ID NO:93), for example Phe/Tyr-Xaa-Xaa-Phe/Tyr-Asp/Glu-Phe/Tyr (SEQ ID NO:94) or Phe/Tyr-Xaa-Xaa-Phe/Tyr-PhosphoSer/PhosphoThr-Phe/Tyr (SEQ ID NO: 95) is measured.
It is preferred that the variant or fragment or derivative or fusion of the said hydrophobic/phosphate binding pocket-containing protein kinase, or the fusion of the variant or fragment or derivative comprises a hydrophobic pocket and a phosphate binding pocket in the position equivalent to the hydrophobic and phosphate binding pocket of human PDK1, as discussed further below.
Equivalent preferences apply to a variant or fragment or derivative or fusion of the SGK, PKB, p70 S6 kinase, p90 RSK, PKCα, PKCδ, PKCζ or PRK2 (for example), or the fusion of the variant or fragment or derivative, with the substitution in relation to SGK, PKB and p70S6 kinase of the peptide substrate Crosstide (GRPRTSSFAEG, SEQ ID NO:96), or for PKB and SGK of the peptide substrate RPRAATF; the substitution in relation to PKA of the peptide substrate Kemptide (LRRASLG, SEQ ID NO:97); the substitution in relation to PKC isoforms and PRK1/2 of histone H1; and the substitution in relation to MSK1/2 or p90-RSK1/2/3 of CREBtide (EILSRRPSYRK, SEQ ID NO:98).
By “variants” of a polypeptide we include insertions, deletions and substitutions, either conservative or non-conservative. In particular we include variants of the polypeptide where such changes do not substantially alter the activity of the said polypeptide, for example the protein kinase activity of PDK1, as described above.
By “conservative substitutions” is intended combinations such as Gly, Ala; Val, Ile, Leu; Asp, Glu; Asn, Gln; Ser, Thr; Lys, Arg; and Phe, Tyr.
The three-letter amino acid code of the IUPAC-IUB Biochemical Nomenclature Commission is used herein, with the exception of the symbol Zaa (negatively charged amino acid). In particular, Xaa represents any amino acid. It is preferred that Xaa and Zaa represent a naturally occurring amino acid. It is preferred that at least the amino acids corresponding to the consensus sequences defined above are L-amino acids.
It is particularly preferred if the PDK1 (or SGK, PKB, PKA or p70 S6 kinase or other hydrophobic/phosphate binding pocket-containing kinase as defined above) variant has an amino acid sequence which has at least 65% identity with the amino acid sequence of PDK1 referred to above (or the sequence for SGK (including SGK1, 2 and 3), PKB, PKA or p70 S6 kinase, for example, as appropriate, referred to above), more preferably at least 70%, 71%, 72%, 73% or 74%, still more preferably at least 75%, yet still more preferably at least 80%, in further preference at least 85%, in still further preference at least 90% and most preferably at least 95% or 97% identity with the amino acid sequence defined above.
It is still further preferred if the PDK1 (or SGK, PKB, PKA or p70 S6 kinase or other hydrophobic/phosphate binding pocket-containing kinase, as defined above) variant has an amino acid sequence which has at least 65% identity with the amino acid sequence of the catalytic domain, particularly the residues forming the hydrophobic pocket, of PDK1 (or, for example, SGK, PKB, PKA or p70 S6 kinase) in the appropriate sequence referred to above, more preferably at least 70%, 71%, 72%, 73% or 74%, still more preferably at least 75%, yet still more preferably at least 80%, in further preference at least 83 or 85%, in still further preference at least 90% and most preferably at least 95% or 97% identity with the amino acid sequence defined above. It will be appreciated that the catalytic domain of a protein kinase-related polypeptide may be readily identified by a person skilled in the art, for example using sequence comparisons as described below.
The percent sequence identity between two polypeptides may be determined using suitable computer programs, for example the GAP program of the University of Wisconsin Genetic Computing Group and it will be appreciated that percent identity is calculated in relation to polypeptides whose sequence has been aligned optimally.
The alignment may alternatively be carried out using the Clustal W program (Thompson et al (1994) Nucl Acid Res 22, 4673-4680). The parameters used may be as follows:
Fast pairwise alignment parameters: K-tuple(word) size; 1, window size; 5, gap penalty; 3, number of top diagonals; 5. Scoring method: x percent.
Multiple alignment parameters: gap open penalty; 10, gap extension penalty; 0.05.
Scoring matrix: BLOSUM.
It is preferred that the PDK1 (or, for example, SGK, PKB, PKA or p70 S6 kinase) is a polypeptide which consists of the amino acid sequence of the protein kinase PDK1 (or, for example, SGK, PKB, PKA or p70 S6 kinase as the case may be) sequence referred to above or naturally occurring allelic variants thereof. It is preferred that the naturally occurring allelic variants are mammalian, preferably human, but may alternatively be homologues from parasitic or pathogenic or potentially pathogenic organisms. Examples of such organisms and homologues, and of uses of modulators of such homologues are given in U.S. patent application No. 60/112,114, filed on 14 Dec. 1998, and applications claiming priority therefrom, or in Casamayor et al (1999) Curr Biol 9, 186-197.
It is preferred that the PDK1 (or, for example, SGK, PKB, PKA or p70 S6 kinase) is a polypeptide that is capable of interacting with a polypeptide comprising the amino acid sequence motif Phe/Tyr-Xaa-Xaa-Phe/Tyr (SEQ ID NO:92), preferably Phe-Xaa-Xaa-Phe/Tyr, more preferably Phe-Xaa-Xaa-Phe, still more preferably Phe/Tyr-Xaa-Xaa-Phe/Tyr-Xaa-Phe/Tyr (SEQ ID NO:93) or Phe/Tyr-Xaa-Xaa-Phe/Tyr-COOH, for example the polypeptide PIF or PIFtide, as defined below. Further preferences for the said polypeptide are as given above.
The protein kinase activity of PKB, SGK or p70 S6 kinase that is modulated may be phosphorylation of the underlined residue in a polypeptide with the amino acid sequence Arg-Xaa-Arg-Xaa-Xaa-Ser/Thr (SEQ ID NO:100). The polypeptide may be Glycogen Synthase Kinase 3 (GSK3), 40 S ribosomal subunit S6, BAD, 6-phosphofructo-2-kinase, phosphodiesterase 3b, human caspase 9, endothelial nitric oxide synthase or BRCA1.
A compound identified by a method of the invention may modulate the ability of the protein kinase to phosphorylate different substrates, for example different naturally occurring polypeptides, to different extents. The compound may inhibit the protein kinase activity in relation to one substrate but may increase the protein kinase activity in relation to a second substrate. For example, the protein kinase activity of PDK1 may be modulated to a different extent for PKB when compared with SGK, p70 S6 kinase and/or PKC.
It will be appreciated that the modulatory, for example inhibitory action of a compound found to bind (or inhibit binding of a polypeptide or compound) to the protein kinase may be confirmed by performing an assay of enzymic activity (for example PDK1 and/or PDK2 protein kinase activity) in the presence of the compound.
By “hydrophobic pocket-containing protein kinase having a hydrophobic pocket (PIF binding pocket) in the position equivalent to the hydrophobic pocket of human PDK1 that is defined by residues including Lys115, Ile118, Ile119, Val124, Val127 and/or Leu155 of full-length human PDK1 and further having a phosphate binding pocket in the position equivalent to the phosphate binding pocket of human PDK1 that is defined by residues including Lys76, Arg131, Thr148 and/or Gln150,” is meant a polypeptide having an amino acid sequence identifiable as that of a protein kinase catalytic domain, and further having a predicted or determined three-dimensional structure that includes a hydrophobic pocket corresponding to the region indicated in Example 1 as the PIF binding pocket, and a pocket corresponding to the region indicated in Example 1 as the phosphate binding pocket. The hydrophobic pocket and phosphate binding pockets in PDK1 do not overlap with the ATP or phosphorylation site binding sites on PDK1.
It is preferred that the protein kinase has identical or conserved residues that are equivalent to Lys 115, Ile118, Ile119, Val124, Val127 and/or Leu 155 of human PDK1, more preferably at least Lys115 and Leu155 of human PDK1, most preferably an identical residue equivalent to Leu155. Thus, for example, the protein kinase may have a Lys residue at the position equivalent to Lys115 of PDK1 and/or a Leu residue at the position equivalent to Leu155 of PDK1. It is preferred that the protein kinase does not have an Ala at the position equivalent to Lys115 and/or a Ser, Asp or Glu at the position equivalent to Leu155 of PDK1.
It is further preferred that the protein kinase has identical or conserved residues that are equivalent to Lys76, Arg131, Thr148 and/or Gln 150 of human PDK1, more preferably at least Lys76 and Gln150 of human PDK1, most preferably an identical residue equivalent to Gln150. FIG. 5B shows an alignment of examples of protein kinases considered to have a phosphate binding pocket at the position equivalent to the said phosphate binding pocket of PDK1. Sequence conservation/preferred residues at the positions identified are discussed further in Example 1.
An amino acid sequence may be identifiable as that of a protein kinase catalytic domain by reference to sequence identity or similarities of three dimensional structure with known protein kinase domains, as known to those skilled in the art.
Protein kinases show a conserved catalytic core, as reviewed in Johnson et al (1996) Cell, 85, 149-158 and Taylor & Radzio-Andzelm (1994) Structure 2, 345-355. This core folds into a small N-terminal lobe largely comprising anti-parallel β-sheet, and a large C-terminal lobe which is mostly α-helical.
A deep cleft at the interface between these lobes is the site of ATP binding, with the phosphate groups near the opening of the cleft.
Protein kinases also show conserved sequences within this catalytic core, and the residue equivalent to a given residue of, for example, PDK1, may be identified by alignment of the sequence of the kinase with that of known kinases in such a way as to maximise the match between the sequences. The alignment may be carried out by visual inspection and/or by the use of suitable computer programs, for example the GAP program of the University of Wisconsin Genetic Computing Group, which will also allow the percent identity of the polypeptides to be calculated. The Align program (Pearson (1994) in: Methods in Molecular Biology, Computer Analysis of Sequence Data, Part II (Griffin, A M and Griffin, H G eds) pp 365-389, Humana Press, Clifton).
The comparison of amino acid sequences or three dimension structure (for example from crystallography or computer modelling based on a known structure) may be carried out using methods well known to the skilled man, for example as described in WO 01/44497.
MAP kinase, MEK1, Cdk2 and Erk2 (for example) are not protein kinases having a hydrophobic pocket in the position equivalent to the hydrophobic (PIF binding) pocket of PDK1. MEK1, Cdk2 and ERK2 may have a larger hydrophobic pocket which interacts with an amino acid sequence motif (which may be Phe-Xaa-Phe-Pro, SEQ ID NO:101) which is not Phe-Xaa-Xaa-Phe (SEQ ID NO:99). Thus, these protein kinases do not have a hydrophobic pocket in the position equivalent to the said hydrophobic (PIF-binding) pocket of PDK1.
A further aspect of the invention provides a mutated protein kinase, wherein the protein kinase before mutation has a hydrophobic pocket in the position equivalent to the hydrophobic pocket (PIF-binding pocket) of human PDK1 that is defined by residues including Lys115, Ile118, Ile119, Val124, Val127 and/or Leu155 of full-length human PDK1 and further has a phosphate binding pocket in the position equivalent to the phosphate binding pocket of human PDK1 that is defined by residues including Lys76, Arg131, Thr148 and/or Gln150, and wherein one or more residues equivalent to Ile118, Val124, Val127, Lys76 or Thr148 forming part of the hydrophobic pocket or phosphate binding pocket of the protein kinase is mutated. It is preferred that the said protein kinase is PDK1. The said protein kinase may alternatively be, for example, SGK, PKB or p70 S6 kinase. It is particularly preferred that the residue at the position equivalent to residue Lys76 of PDK1 is mutated to an Ala. The mutated protein kinase may be useful in determining whether a polypeptide or compound interacts with the hydrophobic (PIF binding) pocket or phosphate binding pocket of the unmutated protein kinase. For example, the abilities of a compound (including polypeptide) to bind to the mutated and unmutated protein kinase, or to modulate the activity of the protein kinase towards one or more substrates of the protein kinase, may be measured and compared.
The mutated protein kinase may alternatively or in addition be mutated at a residue forming part of the “hydroxyl-pocket” discussed in Example 6, for example the residue equivalent to Thr222 and/or Gln 220 of full length human PDK1. These residues are involved in the binding of the UCN-01 7-hydroxyl group.
A further aspect of the invention provides a polynucleotide encoding a mutated protein kinase of the invention. A still further aspect of the invention provides a recombinant polynucleotide suitable for expressing a mutated protein kinase of the invention. A yet further aspect of the invention provides a host cell comprising a polynucleotide of the invention.
A further aspect of the invention provides a method of making a mutated protein kinase of the invention, the method comprising culturing a host cell of the invention which expresses said mutated protein kinase and isolating said mutated protein kinase.
A further aspect of the invention provides a mutated protein kinase obtainable by the above method.
Examples of these aspects of the invention are provided in Example 1, and may be prepared using routine methods by those skilled in the art, for example as described in WO 00/35946.
For example, the above mutated protein kinase may be made by methods well known in the art and as described below and in Example 1 or 2, for example using molecular biology methods or automated chemical peptide synthesis methods.
It will be appreciated that peptidomimetic compounds may also be useful. Thus, by “polypeptide” or “peptide” we include not only molecules in which amino acid residues are joined by peptide (—CO—NH—) linkages but also molecules in which the peptide bond is reversed. Such retro-inverso peptidomimetics may be made using methods known in the art, for example such as those described in Mézière et al (1997) J. Immunol. 159, 3230-3237, incorporated herein by reference. This approach involves making pseudopeptides containing changes involving the backbone, and not the orientation of side chains. Retro-inverse peptides, which contain NH—CO bonds instead of CO—NH peptide bonds, are much more resistant to proteolysis.
Similarly, the peptide bond may be dispensed with altogether provided that an appropriate linker moiety which retains the spacing between the Ca atoms of the amino acid residues is used; it is particularly preferred if the linker moiety has substantially the same charge distribution and substantially the same planarity as a peptide bond.
It will be appreciated that the peptide may conveniently be blocked at its N- or C-terminus so as to help reduce susceptibility to exoproteolytic digestion.
The invention further provides a method of identifying a compound that modulates the protein kinase activity of a protein kinase having a hydrophobic pocket and phosphate binding pocket in the positions equivalent to the hydrophobic (PIF binding) pocket and phosphate binding pocket of PDK1, as defined above (for example PDK1), comprising the step of determining the effect of the compound on the protein kinase activity of, or ability of the compound to bind to the said mutated protein kinase of the invention.
The method may further comprise determining the effect of the compound on the protein kinase activity of, or ability of the compound to bind to, the protein kinase (for example PDK1) which is not mutated at the said residue. When the protein kinase is PDK1, it may lack a functional PH domain (ie it may lack a PH domain capable of binding a phosphoinositide).
It will be appreciated that the protein kinase or mutated protein kinase may be a fusion protein comprising a tag, for example to aid purification, for example a GST tag, as described in Example 1.
The capability of the said PDK1 (or, for example, SGK, PKB, PKA or p70 S6 kinase) polypeptide with regard to interacting with or binding to a polypeptide or other compound may be measured by any method of detecting/measuring a protein/protein interaction or other compound/protein interaction, as discussed further below. Suitable methods include methods analagous to those described in Example 1, as well as other methods, for example yeast two-hybrid interactions, co-purification, ELISA, co-immunoprecipitation and surface plasmon resonance methods. Thus, the said PDK1 (or SGK, PKB, PKA or p70 S6 kinase) may be considered capable of binding to or interacting with a polypeptide or other compound If an interaction may be detected between the said PDK1 polypeptide and the said interacting polypeptide by ELISA, co-immunoprecipitation or surface plasmon resonance methods or by a yeast two-hybrid interaction or copurification method, for example as described in Example 1.
It is preferred that the interaction can be detected using a surface plasmon resonance method, as described in Example 1. The interacting polypeptide (for example a polypeptide comprising a phosphorylated “hydrophobic motif”, for example 56K-pHM; see example 1) may be immobilised on the test surface, for example it can be coupled through amino groups to a Sensor Chip CM5TM, according to the manufacturer's instructions, or a biotinylated polypeptide can be bound to an avidin coated Sensor Chip SA. The protein kinase (at concentrations between, for example 0 and between 10 μM and 1.0 μM, for example 2 μM) is then injected over the surface and steady state binding determined in each case. From these measurements a Kd can be determined. It is preferred that the interaction has a Kd of less than 8 μM, more preferably less than 5 μM, 2 μM, 1 μM, 500 nM, 300 nM, 200 nM or 100 nM, for example about 150 nM. Alternatively, a Kd can be determined for a polypeptide or other compound in competition with the immobilised polypeptide (or other compound). The protein kinase (for example at a concentration of 0.5 μM) is mixed with free polypeptide (for example, at concentrations between 0 and 3 μM) and the mixture injected over the immobilised polypeptides. The steady state binding is determined in each case, from which the Kd of the interaction can be determined using the Cheng-Prescott relationship. Alternatively, the interaction may be expressed in terms of an observed response or relative observed responses, measured in terms of mass of protein bound to the surface, as described in Example 2. For example, the polypeptide may be immobilised by amino coupling to a Sensor Chip CM5 and each protein kinase (for example different mutated protein kinases, as discussed below) for example at a concentration of 1.0 μM or a range of concentrations, injected over the immobilised polypeptide. Alternatively, the polypeptide may be immobilised on a SA Sensor Chip and each protein kinase, for example at a concentration of 40 nM or a range of concentrations injected over the immobilised polypeptide. The steady state response for each protein kinase is determined, for example expressed in Response Units (RU). 1000 RU corresponds to 1 ng/mm2 of protein bound to the surface. A response of less than 10 RU may indicate that no interaction has taken place. A response of at least 10 RU may indicate that the immobilised and injected molecules interact with each other.
It will be appreciated that the above methods may be used to determine whether a particular polypeptide or compound interacts with a protein kinase or mutated protein kinase.
The effect of the compound on the rate or degree of phosphorylation of a hydrophobic pocket and/or phosphate binding pocket-dependent substrate may be determined. A compound may be selected that decreases the protein kinase activity of the said protein kinase, for example PDK1, towards a hydrophobic pocket-dependent substrate or a phosphate binding pocket-dependent substrate and does not affect or increases the protein kinase activity towards a hydrophobic pocket or phosphate binding pocket-independent substrate, for example PKB when the kinase is PDK1. An activator of PDK1 may mimic insulin and may be useful in treating diabetes or obesity, and may protect cells from apoptosis.
Compounds that bind specifically to the phosphate binding site may activate PDK1 (or other AGK kinase having a phosphate binding site). Also compounds that bind to the residues forming part of the phosphate binding site might transduce the negative effect and inhibit the kinase activity. A compound interacting with the phosphate binding site of PDK1 may be an activator, but only of a subset of substrates. Some substrates of PDK1 require the interaction with the phosphate binding site, such as S6K and SGK.
To generate a specific molecule that could bind to the phosphate and/or PIF-binding pocket of PDK1 a anti-idiotype strategy using combinatorial RNA libraries could be employed. Previous studies have established that Combinatorial RNA libraries can be used to isolate specific ligands, called aptamers, for virtually any target molecule by a procedure probably best known as SELEX (Ellington, A. D., and Szostak, J. W. (1990) Nature 346, 818-822; Tuerk, C., and Gold, L. (1990) Science 249, 505-510). Using this approach RNA molecules that interact with antibodies raised against PIFtide or peptides that encompass the hydrophobic motif of AGC kinases which are phosphorylated at their hydrophobic motif would be selected (preferably antibodies that are specific for the phosphorylated form ie bind the phosphorylated form but not the non-phosphorylated form). These RNA species then may have the intrinsic conformation to interact with the phosphate binding (and possibly also the PIF-binding) pocket(s) of PDK1. Antibodies to the phosphate binding pocket may be produced. For example, animals could be immunised with wild type PDK1. Serum could then be purified with a column where the resin is coated with wild type PDK1 used for the immunisation. Specific antibodies could then be passed through columns coated with mutant PDK1 molecules differing only in that they have specific mutations in the phosphate binding pocket, such as Arg131, Lys76 or Gln150, for example mutated to Ala. Antibodies that don't bind to this mutant will either be specific antibodies that recognise the specific motifs or antibodies that are sensitive to the conformational changes associated with these mutations. The opposite development could also be performed: antibodies against a mutant PDK1 having a specific mutation(s) in the phosphate binding pocket, such as Arg131, Lys76 or Gln150, for example mutated to Ala, could be produced and the serum further purified through columns coated with wild type PDK1.
Thus, a further aspect of the invention provides an antibody reactive with the phosphate binding pocket of PDK1 or other hydrophobic pocket (PIF binding pocket)-containing protein kinase having a hydrophobic pocket in the position equivalent to the hydrophobic pocket of human PDK1 that is defined by residues including Lys115, Ile118, Ile119, Val124, Val127 and/or Leu155 of full-length human PDK1 and further having a phosphate binding pocket in the position equivalent to the phosphate binding pocket of human PDK1 that is defined by residues including Lys76, Arg131, Thr148 and/or Gln150. A further aspect of the invention provides an antibody reactive with PDK1 or other phosphate-binding pocket-containing protein kinase as defined above but not with the said protein kinase mutated at the phosphate binding site, or vice versa. A further aspect of the invention provides a method for preparing or selecting an antibody wherein the antibody is prepared or selected against a said protein kinase (for example PDK1) unmutated at the phosphate binding site and a said protein kinase mutated at the phosphate binding site.
By the term “antibody” is included synthetic antibodies and fragments and variants (for example as discussed above) of whole antibodies which retain the antigen binding site. The antibody may be a monoclonal antibody, but may also be a polyclonal antibody preparation, a part or parts thereof (for example an Fab fragment or F(ab)2) or a synthetic antibody or part thereof. Fab, Fv, ScFv and dAb antibody fragments can all be expressed in and secreted from E. coli, thus allowing the facile production of large amounts of the said fragments. By “ScFv molecules” is meant molecules wherein the VH and VL partner domains are linked via a flexible oligopeptide. IgG class antibodies are preferred.
Suitable monoclonal antibodies to selected antigens may be prepared by known techniques, for example those disclosed in “Monoclonal Antibodies: A manual of techniques”, H. Zola (CRC Press, 1988) and in “Monoclonal Hybridoma Antibodies: techniques and Applications”, JGR Hurrell (CRC Press, 1982), modified as indicated above. Bispecific antibodies may be prepared by cell fusion, by reassociation of monovalent fragments or by chemical cross-linking of whole antibodies. Methods for preparing bispecific antibodies are disclosed in Corvalen et al, (1987) Cancer Immunol. Immunother. 24, 127-132 and 133-137 and 138-143.
A general review of the techniques involved in the synthesis of antibody fragments which retain their specific binding sites is to be found in Winter & Milstein (1991) Nature 349, 293-299.
For example, an antibody that does not bind PDK1 Arg131Ala could be specifically recognising this residue in the phosphate binding site, but could also be recognising specifically the inactive conformation of PDK1, which is stabilised by Arg 131. The opposite development could also be performed: antibodies against a mutant PDK1 Arg131Ala could be produced and the serum further purified through columns coated with wild type PDK1. In this way, antibodies may be prepared that would either not be able to interact with the phosphate binding site Arg 131 but only when a small residue is in its place, or antibodies that are probes for the active conformation of PDK1. These conformational probes could be used in high throughoutput screenings, HTS, in the search of compounds that are capable of modifying the conformation of the given protein kinase. Antibodies could have been produced with previous knowledge to detect active protein kinases by immunising with active protein kinases, but in those cases, the antibodies would have recognised also the phosphorylation events that make a protein kinase be active. In the methodology here described using antibodies, the conformational probes could be easily isolated. Furthermore, antibodies obtained from an active protein kinase (with overall modifications that make it active) could be further purified through a column coated with the inactive protein kinase (keeping the non bound fraction) and then further purified on a column coated with a protein kinase consisting of an activating mutation (such as R131A in the case of PDK1), retaining the specifically bound fraction, which could be an active conformation probe. This type of approach could also allow the development of conformation specific probes by the use of activating or inhibiting mutations.
A further aspect of the invention provides a kit of parts useful in carrying out a method according to the preceding aspect of the invention, comprising (1) a mutated protein kinase of the invention and (2) the protein kinase which is not a mutated said protein kinase as defined above.
The protein structures described herein (for example with the co-ordinates shown in Examples 2, 3 or 4, or structures modelled thereon) may be useful in designing further reagents that may be useful in drug screening assays or characterisation of protein kinase activity or regulation. For example, such structures may be useful in designing mutants that may be useful in FRET-based activities, for example in which surface residues near to binding sites are mutated to cysteines to allow coupling of chromophores. For example, the cysteine residue may be fluorescently-labelled, and a change in fluorescence intensity or frequency may be detected in an assay. Any thiol-reactive fluorophore, for example BADAN (see, for example, Wadum et al Fluorescently labeled bovine acyl-CoA binding protein—an acyl-CoA sensor. Interaction with CoA and acyl-CoA esters and its use in measuring free acyl CoA esters and non-esterified fatty acids (NEFA); Hammarstrom et al (2001) Biophys J 80(6), 2867-2885; Schindel et al (2001) Eur J Biochem 268(3), 800-808), could be used to label the cysteine. An alternative suitable fluorophore is Acrylodan (Richieri et al (1992) J Biol Chem 267(33), 23495-23501).
It will be appreciated that the invention provides screening assays for drugs which may be useful in modulating, for example either enhancing or inhibiting, the protein kinase activity of a protein kinase (for example, the protein kinase activity towards a particular substrate) having a hydrophobic pocket in the position equivalent to the hydrophobic pocket of Protein Kinase A (PKA) that is defined by residues including Lys76, Leu116, Val80 and/or Lys111 of full-length mouse PKA, for example PDK1, SGK, PKB, PKA or p70 S6 kinase, for example the PDK1 or PDK2 activity (as discussed above) of PDK1. The compounds identified in the methods may themselves be useful as a drug or they may represent lead compounds for the design and synthesis of more efficacious compounds.
The compound may be a drug-like compound or lead compound for the development of a drug-like compound for each of the above methods of identifying a compound. It will be appreciated that the said methods may be useful as screening assays in the development of pharmaceutical compounds or drugs, as well known to those skilled in the art.
The term “drug-like compound” is well known to those skilled in the art, and may include the meaning of a compound that has characteristics that may make it suitable for use in medicine, for example as the active ingredient in a medicament. Thus, for example, a drug-like compound may be a molecule that may be synthesised by the techniques of organic chemistry, less preferably by techniques of molecular biology or biochemistry, and is preferably a small molecule, which may be of less than 5000 daltons. A drug-like compound may additionally exhibit features of selective interaction with a particular protein or proteins and be bioavailable and/or able to penetrate cellular membranes, but it will be appreciated that these features are not essential.
The term “lead compound” is similarly well known to those skilled in the art, and may include the meaning that the compound, whilst not itself suitable for use as a drug (for example because it is only weakly potent against its intended target, non-selective in its action, unstable, difficult to synthesise or has poor bioavailability) may provide a starting-point for the design of other compounds that may have more desirable characteristics.
It is appreciated that screening assays which are capable of high throughput operation are particularly preferred. Examples may include cell based assays and protein-protein binding assays. An SPA-based (Scintillation Proximity Assay; Amersham International) system may be used. For example, beads comprising scintillant and a substrate polypeptide or interacting polypeptide may be prepared. The beads may be mixed with a sample comprising 32P- or 33P-γ-labelled PDK1 or other protein kinase or mutated protein kinase (as defined above) and with the test compound. Conveniently this is done in a 96-well or 384-well format. The plate is then counted using a suitable scintillation counter, using known parameters for 32P or 33P SPA assays. Only 32P or 33P that is in proximity to the scintillant, i.e. only that bound to the substrate or interacting polypeptide that is bound to the beads, is detected. Variants of such an assay, for example in which the substrate or interacting polypeptide is immobilised on the scintillant beads via binding to an antibody or antibody fragment, may also be used.
It will be understood that it will be desirable to identify compounds that may modulate the activity of the protein kinase in vivo. Thus it will be understood that reagents and conditions used in the method may be chosen such that the interactions between, for example, the said protein kinase and the interacting polypeptide, are substantially the same as between the human protein kinase and a naturally occurring interacting polypeptide comprising the said amino acid sequence. It will be appreciated that the compound may bind to the protein kinase, or may bind to the interacting polypeptide.
The compounds that are tested in the screening methods of the assay or in other assays in which the ability of a compound to modulate the protein kinase activity of a protein kinase, for example a hydrophobic pocket-containing protein kinase, as defined above, may be measured, may be compounds that have been selected and/or designed (including modified) using molecular modelling techniques, for example using computer techniques.
A further aspect of the invention is a compound identified or identifiable by the above selection/design methods of the invention, for example an RNA molecule or antibody identifiable as defined above.
A still further aspect of the invention is a compound (or polypeptide or polynucleotide) of the invention or identified or identifiable by the above selection/design methods of the invention, for use in medicine. Conditions or diseases in which such compounds, polypeptides or polynucleotides may be useful are indicated below.
The compound (or polypeptide or polynucleotide) may be administered in any suitable way, usually parenterally, for example intravenously, intraperitoneally or intravesically, in standard sterile, non-pyrogenic formulations of diluents and carriers. The compound (or polypeptide or polynucleotide) may also be administered topically, which may be of particular benefit for treatment of surface wounds. The compound (or polypeptide or polynucleotide) may also be administered in a localised manner, for example by injection. The compound may be useful as an antifungal (or other parasitic, pathogenic or potentially parasitic or pathogenic organism) agent.
A further aspect of the invention is the use of a compound (or polypeptide or polynucleotide) as defined above in the manufacture of a medicament for the treatment of a patient in need of modulation of signalling by a protein kinase having a hydrophobic/phosphate binding pocket, as defined above, for example PDK1, SGK, PKB or p70 S6 kinase, for example insulin signalling pathway and/or PDK1/PDK2/SGK/PKB/p70 S6 kinase/PRK2/PKC signalling. The patient may be in need of inhibition of a said hydrophobic/phosphate binding pocket-containing kinase in an infecting organism, for example the patient may have a fungal infection for which treatment is required. The compound may inhibit the infecting organism's (for example fungal) hydrophobic/phosphate binding pocket-containing protein kinase, but may not inhibit the patient's equivalent hydrophobic/phosphate binding pocket-containing protein kinase.
A further aspect of the invention is a method of treating a patient in need of modulation of signalling by a protein kinase having a hydrophobic/phosphate binding pocket as defined above, for example PDK1, SGK, PKB or p70 S6 kinase, for example insulin signalling pathway and/or PDK1/PDK2/SGK/PKB/p70 S6 kinase/PRK2/PKC signalling, wherein the patient is administered an effective amount of a compound (or polypeptide or polynucleotide) as defined above.
A compound that is capable of reducing the activity of PKC, for example PKCβ, PRK1 or 2, PDK1 (ie the PDK1 and/or the PDK2 activity), PKB, SGK or p70 S6 kinase may be useful in treating cancer. PDK1, for example via PKB and/or SGK, may be capable of providing a survival signal that protects cells from apoptosis induced in a variety of ways (reviewed in Cross et al (1995) Nature 378, 785-789 and Alessi & Cohen (1998) Curr. Opin. Genetics. Develop. 8, 55-62). Thus, such compounds may aid apoptosis. Reduction of the activity of PDK1, PKB, SGK and/or p70 S6 kinase may promote apoptosis and may therefore be useful in treating cancer. Conditions in which aiding apoptosis may be of benefit may also include resolution of inflammation.
A compound is capable of increasing the activity of PDK1, PKB, SGK or p70 S6 kinase may be useful in treating diabetes or obesity, or may be useful in inhibiting apoptosis. Increased activity of PDK1, PKB, SGK or p70 S6 kinase may lead to increased levels of leptin, as discussed above, which may lead to weight loss; thus such compounds may lead to weight loss. For example, such compounds may suppress apoptosis, which may aid cell survival during or following cell damaging processes. It is believed that such compounds are useful in treating disease in which apoptosis is involved. Examples of such diseases include, but are not limited to, mechanical (including heat) tissue injury or ischaemic disease, for example stroke and myocardial infarction, neural injury and myocardial infarction. Thus the patient in need of modulation of the activity of PDK1, PKB, SGK or p70 S6 kinase may be a patient with cancer or with diabetes, or a patient in need of inhibition of apoptosis, for example a patient suffering from tissue injury or ischaemic injury, including stroke.
Thus, a further aspect of the invention provides a method of treating a patient with an ischaemic disease the method comprising administering to the patient an effective amount of a compound identified or identifiable by the screening methods of the invention.
A still further invention provides a use of a compound identifiable by the screening methods of the invention in the manufacture of a medicament for treating an ischaemic disease in a patient.
Thus, a further aspect of the invention provides a method of treating a patient with an ischaemic disease the method comprising administering to the patient an effective amount of a compound identifiable by the screening methods of the invention.
If the patient is a patient in need of promotion of apoptosis, for example a patient with cancer, it is preferred that the compound of the invention that is used in the preparation of the medicament is capable of reducing the activity of PDK1, PKB, SGK or p70 S6 kinase. If the patient is a patient with diabetes or a patient in need of inhibition of apoptosis, for example a patient with ischaemic disease, it is preferred that the compound of the invention that is used in the preparation of the medicament is capable of increasing the activity of PDK1, PKB, SGK or p70 S6 kinase.
All documents referred to herein are hereby incorporated by reference.
The invention is now described in more detail by reference to the following, non-limiting, Figures and Examples.
Figure Legends
1. Overview of the PDK1 Structure.
The PDK1 kinase domain backbone is shown in a ribbon representation, with the secondary structure elements for residues 74-163 in the lower half of the Figure and for residues 164-358 in the upper part of the Figure. Helix αG, encompassing residues 287-295 (which makes a crystal contact to a symmetry related PDK1 molecule, FIG. 2), is at the bottom right of the Figure. Key residues discussed in the text are shown as a sticks model. ATP is shown as a sticks model. A simulated annealing |Fo−|Fc′, φ calc map is shown in black, contoured at 3σ. The phosphoserine and the sulphate discussed in the text are also shown.
2. The PIF-Pocket
A. A surface representation of the putative PIF binding pocket is shown and compared to the pocket interacting with the C-terminal FXXF (SEQ ID NO: 1) motif in PKA. For PDK1, the αG helix of a symmetry-related molecule is shown as a ribbon, in PKA the C-terminus is also shown as a ribbon. Aromatic amino acids buried in the pocket are shown as sticks; further side chains interacting with the pocket are also shown as sticks. Helix αC is also shown as a ribbon in both PDK1 and PKA (at bottom of images). In PDK1, the ordered sulphate ion and basic residues interacting with it are also shown.
B. A stereo image of the residues lining the PIF-pocket is shown. The PDK1 backbone is shown as a grey ribbon. Side chains are shown as sticks. Hydrogen bonds to the sulphate ion are shown as black dotted lines.
3. Structure-Based Sequence Alignment
The sequences of PKA (SEQ ID NO: 103) and PDK1 (SEQ ID NO:102) are aligned according to a structural superposition performed in WHAT IF [Vriend, 1990]. Sequence numbering is according to PDK1. 13-strands (arrows) and α-helices (bars) are shown for the PDK1 structure according to a DSSP [Kabsch and Sander, 1983] secondary structure assignment, and labelled consistent with the secondary structure element names proposed for PKA [Taylor and Radzioandzelm, 1994]. Residues lining the PIF-pocket are indicated with a black dot. Residues hydrogen bonding the sulphate ion are indicated by arrows. The PDK1 residues equivalent to Ser53 and Gly186 in PKA, are labelled with an asterisk.
4. PDK1 Binding & Activation Studies
Binding and activation of wild type and mutant forms of PDK1 to a phosphopeptide derived from the hydrophobic motif of S6K1. The binding of the wild type (wt) PDK1 and indicated mutants to a phosphopeptide comprising the hydrophobic motif of S6K1 (S6K-pHM: SESANQVFLGFT*YVAPSV, where T* indicates phospho-threonine, SEQ ID NO:104) was analysed by surface plasmon resonance as described in the Materials and Methods.
A. The sensor chip SA was coated with 12RUs of the biotinylated S6K-pHM peptide and the binding was analysed following injection of 270 nM wild type PDK1, PDK1 [T148A] and PDK1 [K76A]. No detectable binding to S6K-pHM was observed using PDK1 [R131A] or PDK1 [Q150] (data not shown).
B. As in A. except that binding was analysed over a range of PDK1 concentrations (2-2150 nM). The response level at the steady state binding is plotted versus the log of the PDK1 concentration. The estimated Kd was obtained by fitting the data to a sigmoid curve using Kaleidagraph software. Kd for wild type PDK1 was 642-131 nM, PDK1 [T148A] was 64-7 nM and PDK1 [K76A] was 1744-167 nM. No detectable binding of PDK1 to the non-phosphorylated S6K-HM peptide (SESANQVFLGFTYVAPSV, SEQ ID NO:105) was detected with wild type PDK1 or any of the mutants (data not shown).
C. Activation of the indicated forms of PDK1 by 56K-pHM and S6K-HM. PDK1 activity was measured using the peptide substrate (T308tide) in the presence of the indicated concentrations of 56K-pHM (closed circles) and S6K-HM (open circles) as described in the methods. Assays were performed in triplicate and similar results obtained in 2 separate experiments. The results are the average—SD for a single experiment.
5. Interactions of Regulatory Phosphates with the αC Helix
A. The PDK1 backbone is shown as a ribbon, with helix a C in the centre of the view. Key residues are shown as sticks. The sulphate ion and the phosphate on the activation loop are also shown. A sticks model of ATP is shown. Hydrogen bonds are shown as black dotted lines.
B. Alignment of the amino acid sequence forming part of the phosphate pocket on PDK1 with the equivalent region of the indicated AGC kinases. Identical residues are denoted by white letters on a black background and similar residues by gray boxes. Arrows indicate the residues corresponding to Lys 76, Arg131, Thr148 and Gln150 of PDK1 (SEQ ID NOs:12 and 144). The aligned amino acid sequences are as follows: PKBα (SEQ ID NOs: 13 and 145), S6K1 (SEQ ID NOs: 14 and 146), SGK1 (SEQ ID NOs: 15 and 147), and Rsk1 (SEQ ID NOs: 16 and 148).
6. Essential Dynamics
A. Projection of all available PKA crystal structures (labelled dots) and the PDK1 structure (diamond) onto the first two eigenvectors (i.e. the ones with the two largest eigenvalues) calculated from the PKA structures.
B. Graphic representation of the motion along the first eigenvector, generated by projecting two structures at −4 nm (black) and +4 nm (grey).
7. Alignment of AGC Protein Kinase Family Members.
The aligned amino acid sequences and their respective corresponding sequence identifier are as follows:
P70S6Kalpha (SEQ ID NO: 17), P70S6 Kbeta (SEQ ID NO: 18), P90RSK1 (SEQ ID NO: 19), P90RSK2 (SEQ ID NO: 20), P90RSK3 (SEQ ID NO: 21), MSK1 (SEQ ID NO: 22), MSK2 (SEQ ID NO: 23), PKBalpha (SEQ ID NO: 24), PKBbeta (SEQ ID NO: 25), PKBgamma (SEQ ID NO: 26), PRK1 (SEQ ID NO: 27), PRK2 (SEQ ID NO: 28), SGK1 (SEQ ID NO: 29), SGK3 (SEQ ID NO: 30), SGK2 (SEQ ID NO: 31), PKCbeta (SEQ ID NO: 32), PKCbetaII (SEQ ID NO: 33), PKCalpha (SEQ ID NO: 34), PKCgamma (SEQ ID NO: 35), PKCzeta (SEQ ID NO: 36), PKCiota (SEQ ID NO: 37), PKCdelta (SEQ ID NO: 38), PKAgamma (SEQ ID NO: 39), and PDK1 (SEQ ID NO: 40).
8. Staurosporine and UCN-01 Electron Density.
The staurosporine and UCN-01 molecules are shown in a stick representation. Hydrogen bonding atoms (Table 4) are labelled according to [49]. The unbiased |Fo|−|Fc|, φcalc maps are contoured at 2.5σ.
9. Details of the Inhibitor Binding Sites.
The bridging water molecule is shown as a sphere. Hydrogen bonds are indicated by black dotted lines. Labelled residues hydrogen-bond the inhibitor molecules.
Example 1
High Resolution Crystal Structure of the Human PDK1 Catalytic Domain Defines the Regulatory Phosphopeptide Docking Site
The 3-Phosphoinositide Dependent Protein Kinase-1 (PDK1) plays a key role in insulin/growth factor induced signalling pathways through phosphorylation of downstream AGC-kinases such as Protein Kinase B/Akt and p70 ribosomal S6 kinase (S6K1). Here we describe the 2.0 Å crystal structure of the PDK1 kinase domain in complex with ATP. The structure defines the hydrophobic pocket termed the ‘PIF-pocket’ which plays a key role in mediating the interaction and phosphorylation of certain substrates such as S6K1. In the PDK1 structure, this pocket is occupied by an extensive crystallographic contact with another molecule of PDK1, reminiscent of the interaction of Protein Kinase A with the hydrophobic motif at its C-terminus. Previous studies have shown that phosphorylation of S6K1 at its C-terminal PIF-pocket-interacting motif, promotes the binding of S6K1 with PDK1, suggesting that there may be a phosphate docking site located nearby the PIF-pocket. Interestingly, close to the PIF-pocket on the PDK1 structure, there is an ordered sulphate ion, interacting tightly with four surrounding side chains. The roles of these residues were investigated through a combination of site directed mutagenesis and kinetic studies, the results of which suggest that this region of PDK1 does indeed represent a phosphate dependent docking site. An analogous phosphate binding regulatory motif may participate in the activation of other AGC kinases.
Results & Discussion
Overall Structure
The structure of the catalytic domain of PDK1 was solved by molecular replacement and refined to an R-factor of 0.19 (Rfree=0.22). PDK1 assumes the classic bilobal kinase fold (FIG. 1) and is similar to the only other AGC kinase structure solved, that of PKA (RMSD of 1.0 Å on C a atoms with PDB entry 1STC [Prade et al., 1997]). The form of PDK1 that was crystallized comprised residues 51 to 359. The tip of the activation loop (residues 233-236) is disordered, as observed in other kinase structures [Johnson et al., 1996]. The N-terminus (residue 51-70), which is pointing into a large void generated by the crystallographic symmetry, is also disordered. In contrast, the N-terminal extension to the kinase domain of PKA assumes an amphipathic α-helix (termed αA-helix), and packs against the kinase core [Knighton et al., 1991]. The cluster of hydrophobic residues that mediates this interaction in PKA is not present in PDK1, suggesting that the N-terminus of PDK1 could have a different function from that of PKA. Interestingly, it has recently been shown that the N-terminus of PDK1 (residues 1-50) interacts with Ral guanine nucleotide exchange factors [Tian et al., 2002]. Thus, this region may assume a unique conformation in PDK1, which is not defined by the structure described here.
PDK1 was crystallised in the presence of ATP but in the absence of any divalent cations. In the early stages of the refinement well-defined density for the entire ATP molecule could be observed. ATP adopts a different conformation to that observed in other kinase-ATP complexes (FIG. 1). Perhaps due to the absence of divalent cations, the generally observed kink between the β and γ phosphate caused by the interaction with such an ion, is not seen in the PDK1 structure.
It is known that PDK1 can phosphorylate itself on residue Ser 241 in the activation loop and that this phosphorylation is required for PDK1 activity [Alessi et al., 1997]. Indeed, we observed density for a phosphate attached to this residue (FIG. 1), and extensive interactions are observed between this phosphoserine and residues from the C-terminal lobe and αC-helix (FIG. 1). The interaction between Ser241 and the C-terminal lobe is similar to the equivalent interactions in PKA but as discussed below the binding to the αC-helix differs.
The PIF-Pocket
As outlined in the introduction, PDK1 was postulated to possess a pocket (the ‘PIF-pocket’) in the small lobe of its catalytic domain, required for the binding of PDK1 to the hydrophobic motif of its substrates [Biondi et al., 2000]. The PDK1 structure described here indeed reveals such a pocket, and shows that it lies in a location similar to the FXXF (SEQ ID NO:1)-binding pocket in PKA (FIG. 2). PDK1 residues Lys115, Ile118, Ile119 on the αB helix (FIG. 2), Val124, Val127 on the αC helix and Leu155 on β-sheet 5 form an approximately 5 Å deep pocket. Previous work has shown that mutation of Leu 155 to Glu abolishes the ability of PDK1 to interact with a peptide that encompasses the hydrophobic motif of PRK2 (PIFtide) [Biondi et al., 2000] as well as with S6K1, SGK1, PKCζ and PRK2 [Balendran et al., 2000, Biondi et al., 2000]. In addition, mutation of Lys115, Ile119, Glu150, and Leu155 to alanine, reduced the affinity of PDK1 for PIFtide approximately 10-fold, but did not affect the ability to phosphorylate and activate S6K1 and SGK1 [Biondi et al., 2001]. These results are in agreement with the crystal structure of the PIF-pocket, since Leu155 is located at the center and the other residues line the wall of the pocket (FIG. 2). Interestingly, in our structure, the PIF-pocket is occupied by helix αG of a symmetry related molecule (FIG. 2). Tyr288 and Phe291 make hydrophobic contacts in this pocket with almost all pocket-lining residues, remarkably reminiscent of the interactions of the phenylalanines in the FXXF motif in PKA and their hydrophobic docking site in the equivalent region of the kinase domain (FIG. 2). In addition, residues Glu287, Gln292, Ile295 and Lys296 on the symmetry related loop also form contacts with residues lining the PIF-pocket. In total, 2442 Å of accessible surface is buried by this contact, suggesting this is a tight interaction. However, the significance of this interaction is not clear as an oligomerisation event for PDK1 has not been demonstrated in solution previously. Indeed both the isolated catalytic domain of PDK1 that was crystallised and full length PDK1 migrate in gel filtration chromatography as apparent monomeric species (data not shown).
The Phosphate Pocket
As outlined in the introduction, substrates of PDK1, such as S6K1, interact with the PIF-pocket of PDK1 with higher affinity when they are phosphorylated at their hydrophobic motif. This suggested that a regulatory phosphate binding site may be located close to the PIF-pocket. During refinement of the PDK1 structure, it became clear that next to the PIF-pocket another small pocket was present, occupied by a tetrahedral oxy-anion (FIG. 2). As 2.0 M of sulphate was present in the crystallisation conditions, this was assigned as a sulphate ion. The ion interacts with four residues lining the pocket, namely Lys76, Arg131, Thr148 and Gln150.
Because of its close proximity to the PIF-pocket (approximately 5A) it is possible that this sulphate-occupied pocket could represent the binding site for the phosphate on the phosphopeptide. To investigate this further, we mutated Lys76, Arg131, Thr148 and Gln150 to Ala, in order to verify the contribution of each of these residues in enabling PDK1 to interact with a peptide encompassing the hydrophobic motif of S6K1, in which the residue equivalent to Thr412 was phosphorylated (termed S6K-pHM). A quantitative surface plasmon resonance based binding assay (FIG. 4A) showed that wild type PDK1 interacted with S6K-pHM, with a Kd of 0.6 μM with S6K-pHM but not detectably to the non-phosphorylated form of this peptide (S6K-HM). The PDK1[R131A] and PDK1[Q150A] mutants did not detectably interact with S6K-pHM in this assay (FIG. 4B), confirming that the interactions these residues make in the PDK1 structure are of key importance. The PDK1 [K76A] mutant interacted with 3-fold lower affinity (Kd 1.7 μM) with S6K-pHM. The PDK1[T148A] mutant however possessed about 10-fold higher (Kd 0.06 μM) affinity for S6K-pHM than wild type PDK1. Moreover, the dissociation of PDK1[T148A] from S6K-pHM is markedly slower than that of wild type PDK1 or PDK1[K76A] (FIG. 4A). These findings are unexpected as Thr148 is within hydrogen bonding distance of the sulphate (FIG. 2), but indicate that this residue may play a role in enabling the dissociation of PDK1 from S6K-pHM.
The binding of PDK1 to PIFtide stimulates up to 4-fold the rate at which PDK1 phosphorylates a small peptide that encompasses the activation loop motif of PKB (termed T308tide) [Biondi et al., 2000], indicating that occupancy of the PIF-pocket of PDK1 activates the enzyme. Similarly, the binding of a phosphopeptide corresponding to the hydrophobic motif of RSK stimulated PDK1 activity 6-fold [Frodin et al., 2000]. We have now also found that the binding of 56K-pHM to wild type PDK1 induces a maximal 5-fold activation, with a half maximal activation occurring at a concentration of approximately 50 μM S6K-pHM (FIG. 4C). We next assayed the specific activities of PDK1 [K76A], PDK1[R131A], PDK1[T148A] and PDK1[Q150A] mutants in the absence and presence of increasing concentrations of S6K-pHM (FIG. 4C). The PDK1[K76A] possessed the same specific activity towards T308tide in the absence of S6K-pHM as wild type PDK1, but an approximately 3-fold higher concentration of S6K-pHM was required to half maximally activate PDK1[K76A], consistent with the reduced affinity of this form of PDK1 for S6K-pHM (FIG. 4A,B). The PDK1[R131A] mutant possessed a 3-fold higher specific activity towards Thr308tide in the absence of S6K-pHM (FIG. 4C), as has been observed previously with certain other PIF-pocket mutants of PDK1(PDK1[K115A] and PDK1[L155E]) [Biondi et al., 2000]. However, in accordance with the inability of PDK1[R131A] to bind S6K-pHM in the Biacore assay (FIG. 4B), it was not significantly activated by concentrations of S6K-pHM below 0.1 mM and its activity was only moderately further increased by the addition of high concentrations (0.3 and 1 mM) of S6K-pHM (FIG. 4C). The activity of a mutant of PDK1 in which both Lys76 and Arg131 were changed to Ala was activated even less significantly by these high concentrations of S6K-pHM. The PDK1[T148A] and PDK1[Q150A] mutants possessed similar specific activity towards T308tide as wild type PDK1 in the absence of S6K-pHM. The PDK1[T148A] mutant was activated similarly as wild type PDK1 by S6K-pHM and consistent with the inability of PDK1[Q150A] to interact with S6K-pHM, this mutant of PDK1 was not significantly activated by concentrations of S6K-pHM below 0.1 mM but at 0.3 and 1 mM peptide a 2-3 fold activation was observed (FIG. 4).
At very high peptide concentrations (0.3-1 mM) the non-phosphorylated S6K-HM peptide induced a small (<2-fold) activation of PDK1 (FIG. 4C). Interestingly, despite the PDK1 [K76A] and PDK1[R131A] mutants being markedly less able to interact with the phosphorylated S6K-pHM peptide, than wild type PDK1, high concentrations of the S6K-HM peptide activated PDK1[K76A] and PDK1[R131A] to a similar extent as wild type PDK1, indicating that the ability of these mutants to interact weakly with the S6K-HM peptide was not affected.
We evaluated the sequence conservation in the phosphate pocket of the insulin/growth factor-activated AGC family kinases (PKBα, S6K1, SGK1 and RSK1). Sequence alignments indicate that this pocket is conserved amongst these kinases (FIG. 5A). The most conserved residue is Gln150 which is found in all of these AGC kinases and the residue equivalent to Lys76 is always a basic residue (FIG. 5A). Arg131 is conserved in S6K1, SGK1 and RSK1 but not in PKBα, or PKBβ or PKBγ, where it is an Asn or Ser. Thr148 is conserved in PKBα and SGK1 but is an Ala in S6K1 and RSK1. Interestingly, we have found the Thr 148Ala mutation in PDK1 did not disrupt the phosphate pocket (FIG. 4). As PKBα, S6K1, SGK1 and RSK1 require to be phosphorylated at their hydrophobic motif to be maximally activated, it is tempting to speculate that the C-terminal hydrophobic motifs of these enzymes, when phosphorylated, bind to their own PIF/phosphate pockets, thereby generating a network of interactions similar to that of PDK1. In support of this, PKBα, S6K1, SGK1 and RSK1 also require phosphorylation of their activation loop at the position equivalent to Ser241 for activity. Consistent with PKA not possessing a phosphate pocket, Lys76 and Gln150 are not conserved in PKA (FIG. 3), and indeed such a pocket is not observed in the PKA structure (FIG. 2).
The αC Helix
The PDK1 structure shows that, as in other protein kinases [Johnson et al., 2001, Husen and Kuriyan, 2002], the αC helix (residues 124-136) is a key signal integration motif in the kinase core. One turn of the PDK1 αC helix (residues 129-131, FIGS. 3, 5) links together the N-terminal lobe, the C-terminal lobe and the active site. Arg129 points towards the activation loop and forms two hydrogen bonds with the phosphorylated Ser241, whereas Arg131 forms two hydrogen bonds with the sulphate in the phosphate pocket (FIG. 5). Glu130 coordinates Lys111 which forms a hydrogen bond with the α-phosphate of the bound ATP. This interaction is conserved in all protein kinases and shown to be crucial for activation [Johnson et al., 2001, Husen and Kuriyan, 2002]. An additional residue, His126, forms a third hydrogen bond with the phosphorylated Ser241. Val124 and Val127 on the αC helix are involved in formation of the PIF-pocket (FIG. 5).
The αC helix provides a structural link between the putative phosphopeptide binding pocket and the phosphoserine in the activation loop. The fact that R131A has higher basal activity than wild type PDK1 may indicate that this residue plays tuning role in the PDK1 structure, not only participating in the activation of PDK1 in the presence of a phosphate ion, but also on keeping the equilibrium of the enzyme towards an inactive conformation in the absence of S6K-pHM. To our knowledge this is the first report of a kinase structure in which the αC helix is positioned by 2 regulatory phosphate binding sites on either side of the helix (FIG. 5). This provides a possible sensor-mechanism for linking the phosphorylation-state of the activation loop and the phosphopeptide binding event in the PIF-pocket to PDK1 activity.
Activation State
All structures of PKA solved to date show a phosphorylated T-loop and are therefore assumed to be in an active state. In addition to the unphosphorylated versus phosphorylated states of PKA, there appear to be two main conformational states possible for the latter [Zheng et al., 1993, Johnson et al., 2001]. In the active, closed conformation, all residues are positioned to facilitate phosphoryl transfer. In contrast, the inactive, open conformation is seen in absence of a nucleotide, and differs from the closed conformation by conformational changes of the N-terminal and C-terminal domains with respect to each other. In addition, three ‘intermediate’ structures were described from PKA, having either adenosine (PDB entry 1BKX [Narayana et al., 1997]) or the inhibitors staurosporine (PDB entry 1STC [Prade et al., 1997]) and balanol (PDB entry 1BX6 [Narayana et al., 1999]) in the ATP-binding site. Taylor and colleagues have described a method to distinguish between the active and inactive conformations, based on three distances: His87-pThr197 (αC helix positioning), Ser53-Gly186 (opening of the glycine-rich loop) and Glu170-Tyr330 (C-terminal tail distance to active site) [Johnson et al., 2001]. In PDK1, only one of these distances, the opening state of the glycine rich loop, can be measured due to sequence conservation (FIG. 3). This distance is 12.4 Å, similar to a PKA intermediate conformation (this distance in PKA is 14.2 Å for the open, 11.8 Å for intermediate and 10.0 Å for the closed conformation [Johnson et al., 2001]). To allow a more direct comparison of the PDK1 structure with the available PKA structures, we have analysed the conformational state of PDK1 in detail using a novel approach, which involves a principal component analysis (also called “essential dynamics” [Amadei et al., 1993]) of the crystallographic coordinates. In short, this involves the construction of a covariance matrix containing the correlations between atomic shifts (with respect to an average structure) in the ensemble of all available PKA crystal structures. Diagonalisation of this matrix gives eigenvector/eigenvalue sets which describe concerted shifts of atoms (eigenvectors) together with the corresponding mean square fluctuation of the structures (eigenvalues). This approach allows a condensed description of PKA conformational states using only a few degrees of freedom, as shown previously for a range of other proteins [van Aalten et al., 1997, van Aalten et al., 2000, deGroot et al., 1998]. Diagonalisation of a covariance matrix built from the backbone atoms of residues 37-196, 198-283 and 286-305 results in a set of eigenvectors that describe concerted motions of the PKA backbone. In FIG. 6A, all PKA structures are projected on a subspace spanned by the first two eigenvectors (i.e. those with the two largest eigenvalues). It appears that the PKA structures cluster in three main areas along the first eigenvector. On the left of the average structure (which by definition has a projection of 0.0 on all eigenvectors) are the structures that are known to be in the “open” conformation (FIG. 6A). Around the average structure lie the structures that have been shown to be in an “intermediate” conformation (complexes with the inhibitors staurosporine, balanol and adenosine). More to the right of the average structure are the PKA structures that are known to be in the “closed” conformation. Thus, we have captured the conformational state of PKA in a single variable, the translation along the first eigenvector. This is further clarified by investigation of the atomic shifts described by this eigenvector in Cartesian space (FIG. 6B). A hinge-bending motion is observed between the N-terminal and C-terminal lobes, opening and closing the active site. It is now possible directly to compare the PDK1 conformational state by projecting the structure (backbone atoms only) onto the PKA eigenvectors. FIG. 6A shows that the conformation of PDK1 is close to the PKA structures that are in an “intermediate” conformation, consistent with the other structural analyses described above.
Conclusions
We have reported the structure of the PDK1 catalytic domain, which, although similar to PKA, has revealed important features that increase our understanding of the mechanism by which PDK1 is regulated. The structure, together with mutational analyses, defines a phosphopeptide binding pocket, consisting of a separate hydrophobic PIF-pocket and a phosphate binding site, which mediates the interaction of PDK1 with the phosphorylated hydrophobic motif of S6K. This is consistent with the previous hypothesis that phosphorylation of S6K and SGK [Biondi et al., 2001] as well as RSK [Frodin et al., 2000] at their FXXFS/T hydrophobic motif (SEQ ID NO:2) is the trigger for their interaction and phosphorylation by PDK1. In this mechanism the PIF-pocket would physiologically only interact with the Phe residues when the Ser/Thr residue is phosphorylated. Furthermore, as the phosphate pocket is conserved in other AGC kinases, the structural features and network of interaction of the phosphate pocket with the αC-helix on PDK1, could provide insight into the mode of activation of other AGC kinases.
EXPERIMENTAL PROCEDURES
Materials
Mammalian and Insect cells culture reagents were from Life Technologies. Sensor Chips SA were from BiaCore AB. Glutathione Sepharose, as well as pre-packed HiTrap Q HP and Hiload Superdex 200 prep grade columns were from Amersham Biosciences. Dialysis cassettes were from the Slide-A-Lyzer series (Pierce). Ni-NTA Agarose was from Qiagen. Disposable ultrafiltration devices (polyethersulfone membranes) were from Vivascience. Crystallisation research tools (primary screens, additive screens and crystallisation plates) were from Hampton Research. Peptides were synthesised by Dr G. Blomberg (University of Bristol, UK).
General Methods
Molecular biology techniques were performed using standard protocols. Site directed mutagenesis was performed using a QuickChange kit (Stratagene) following instructions provided by the manufacturer. DNA constructs used for transfection were purified from bacteria using Qiagen plasmid Mega kit according to the manufacturer's protocol, and their sequence verified. Human kidney embryonic 293 cells were cultured on 10 cm diameter dishes in Dulbecco's modified Eagle's medium containing 10% foetal bovine serum.
Buffers
Low Salt Buffer: 25 mM Tris-HCl pH 7.5, 150 mM NaCl; High Salt Buffer: 25 mM Tris-HCl pH 7.5, 500 mM NaCl. Lysis Buffer: 25 mM Tris-HCl pH 7.5, 150 mM NaCl 0.07% β-mercaptoethanol, 1 mM Benzamidine, and 20 μg/ml PMSF. Buffer A: 50 mM Tris-HCl pH 7.5, 1 mM EGTA, 1 mM EDTA, 1% (by mass) Triton-X 100, 1 mM sodium orthovanadate, 50 mM sodium fluoride, 5 mM sodium pyrophosphate, 0.27 M sucrose, 1 μM microcystin-LR, 0.1% (by vol)-mercaptoethanol and “complete” proteinase inhibitor cocktail (one tablet per 50 ml, Roche). Buffer B: 50 mM Tris/HCl pH 7.5, 0.1 mM EGTA, 10 mM β-mercaptoethanol and 0.27 M sucrose.
Expression, Purification and Characterisation of the Kinase Domain of PDK1
A cDNA encoding for human PDK1 amino acid residues 51-359 with a stop codon inserted at position 360, was amplified by PCR reaction using full length human PDK1 cDNA in the pCMV5 vector [Alessi et al., 1997] as a template a 5′ primer, which incorporates a BamHI restriction site, an initiating methionine, a hexahistidine tag followed by a PreScission protease recognition sequence prior to the residue equivalent to Met51 of PDK1 (ggatcctataaatatggcacatcatcatcatcatcatctggaagttctgttccaggggcccatggacggcact gcagccgagcctcgg) (SEQ ID NO:106) and the 3′ primer applied in this reaction was: 5′-ggatcctcaggtgagcttcggaggcgtctgctggtg-3′ (SEQ ID NO: 107). The resulting PCR product was ligated into pCR 2.1 TOPO vector (Invitrogen) and then subcloned as a BamHI-BamHI fragment into pFastbac1 vector (Life Technologies) for baculovirus protein expression. The resulting construct was then used to generate recombinant baculovirus using the Bac-to-Bac system (Life Technologies) following the manufacturer's protocol. The resulting baculoviruses were used to infect Sf21 cells at 1.5×106/ml. The infected cells were harvested by centrifugation 72 hours post infection. Cell pellets corresponding to 7 l of culture were resuspended in 900 ml of Lysis Buffer and cells lysed in nitrogen cavitation chamber. Cell debris was then pelleted by centrifugation, the supernatant made 0.5 M NaCl by addition of 4M NaCl and then incubated with Ni-NTA-Agarose (10 ml resin) for one hour. The resin was then washed in 10 times with 40 ml of Lysis Buffer containing 0.5M NaCl and then placed in a disposable Econo-Pac column (BioRad), where the resin was further washed with 700 ml of high salt buffer and then with 100 ml of low salt buffer, both supplemented with 10 mM imidazole. Elution was performed with 200 mM imidazole in high salt buffer and 2 ml fractions were collected. Fractions containing protein were pooled, diluted to 200 mM NaCl with 25 mM Tris/HCl pH 7.5, and loaded onto a 5 ml Hi-trap Q sepharose column. The flow-through from this step, containing PDK1, was concentrated to 4 ml and then chromatographed on a 16/60 Superdex 200 gel filtration column using an AKTA Explorer system (Amersham Biosciences) equilibrated with high salt buffer with the addition of 1 mM DTT. PDK1 eluted in a large symmetric peak at the expected size for a monomer. The PDK1 containing peak was again pooled, concentrated and incubated with 300 μg GST-PreScission protease (expression construct kindly provided by John Heath, University of Birmingham, UK) on ice for 4 h. In order to eliminate the cleaved His-tag sequences as well as any remaining uncleaved His-PDK1 and the GST-PreScission protease, the mixture was incubated with a mixture of 200 μl glutathione-Sepharose and 200 μl Ni-NTA agarose resin for 15 minutes and the PDK1 protein that did not bind was collected. The resulting protein consists of PDK1 (51-359) preceded by a Gly-Pro at the N-terminus. The protein at this stage of the purification was apparently homogeneous as revealed by a single band after electrophoresis of 20 μg of protein on SDS-PAGE and staining with Coomasie Brilliant Blue 8250 (data not shown).
Electrospray mass spectrometry revealed a main peak mass close to the expected size of this fragment of PDK1. The specific activity of PDK1 (51-359) towards the peptide T308tide and its activation in the presence of PIFtide was identical to wild type full length PDK1 [Biondi et al., 2000], and tryptic peptide mass finger printing indicated that PDK1 was quantitatively phosphorylated at Ser241 (data not shown). In BiaCore experiments, the steady state binding of PDK1 (51-359) to the peptide PIFtide was similar to that of the His-tag PDK1 (51-556) protein characterised previously [Balendran et al., 1999a].
Crystallisation and Data Collection
The PDK1 (51-359) protein was concentrated to a final concentration of 8.5 mg/ml (as determined by a Bradford assay using bovine serum albumin as a standard). The sitting drop vapour diffusion method was used for producing crystals. Sitting drops were formed by mixing 1 μl of protein solution with 1 μl of a mother liquor solution (0.1 M Tris/HCl pH 8.5, 2.0 M ammonium sulphate, 16.6 mM ATP) with the addition of 0.2 μl EDTA (100 mM). Hexagonal crystals (Table I) of PDK1 were grown at 20° C. from a mother liquor containing 0.1M Tris/HCl pH 8.5, 2.0 M ammonium sulphate, 16.6 mM ATP). Crystals appeared after one day, growing to 0.05×0.05×0.2 mm over 20 days. Crystals were frozen in a nitrogen gas stream after being soaked in 0.075 M Tris 8.5, 1.5M ammonium sulphate, 25% (v/v) glycerol.
Expression and Purification of Wild Type and Mutant Forms of GST-PDK1.
Wild type-PDK1 [Alessi et al., 1997], PDK1[R76A], PDK1[R131A], PDK1[R76A,R131A], PDK1[T148A] and PDK1[Q150A] in the pEBG2T vector were used to express the wild type and indicated mutants of PDK1 fused through their N-terminus to glutathione S-transferase (GST). The GST fusion proteins were expressed in human embryonic kidney 293 cells. For the expression of each construct, twenty 10 cm diameter dishes of 293 cells were cultured and each dish transfected with 10 μg of the pEBG-2T construct, using a modified calcium phosphate method. 36 h post-transfection, the cells were lysed in 0.6 ml of ice-cold Buffer A, the lysates pooled, centrifuged at 4° C. for 10 min at 13000 g and the GST-fusion proteins were purified by affinity chromatography on glutathione-Sepharose and eluted in Buffer B supplemented with 20 mM glutathione as described previously [Alessi et al., 1997]. Typically between 1 and 2 mg of each GST-fusion protein was obtained and each protein was more than 75 judged by SDS polyacrylamide gel electrophoresis (data not shown).
PDK1 Catalytic Activity Measurements
The ability of wild type and mutant PDK1 to phosphorylate the synthetic peptide T308tide (KTFCGTPEYLAPEVRR ([Biondi et al., 2000]) (SEQ ID NO:108) was carried out in 30 μl assays containing 100 ng of wild type or mutant PDK1, 50 mM Tris/HCl pH 7.5, 0.1% 13-mercaptoethanol, 10 mM MgCl2, 100 μM [32γ P]ATP (200 cpm/pmol), 0.5 μM microcystin-LR, 1 mM T308tide in the presence or absence of the indicated concentrations of the 56K-pHM peptide (SESANQVFLGFT(P)YVAPSV) (SEQ ID NO:104) or 56K-HM. peptide (SESANQVFLGFTYVAPSV) (SEQ ID NO:105). After incubation for 10 min at 30° C., 25 μl of the resultant mixture was spotted into P81 phosphocellulose paper (2×2 cm) and the papers washed and analysed as described previously for assays of MAP kinase. Control assays were carried out in parallel in which either PDK1, or peptide substrate were omitted; these values were always less than 5% of the activity measured in the presence of these reagents. One Unit of PDK1 activity was defined as that amount required to catalyse the phosphorylation of 1 nmol of the T308tide in 1 min.
Biacore Analysis
Binding was analysed in a BiaCore 3000 system (BiaCore AB, Stevenage, UK). Biotinylated S6K-pHM (Biotin-C12-SESANQVFLGFT(P)YVAPSV) (SEQ ID NO:104) or the non-phosphorylated form of this peptide S6K-HM was bound to an streptavidin-coated Sensor chip (SA) (12 response units, RU). 30 μl of wild type or the indicated mutant GST-PDK1 were injected at a flow rate of 30 μl/min, in buffer HBS-P (10 mM HEPES pH 7.4, 0.15M NaCl, 0.005% (by vol) polysorbate-20) supplemented with 1 mM DTT. Specific interactions between 56K-pHM and PDK1 proteins were obtained between the concentration range of 2-2150 nM PDK1. Steady state binding was determined at each concentration. Dissociation of PDK1 from the phospho-peptide was monitored over a 1 min period. Regeneration of the sensor chip surface was performed with 1{tilde over (0)} μl injections of 0.05% SDS. As previously found for PDK1 binding to PIFtide [Biondi et al., 2000], the interaction data obtained using BiaCore did not fit to simple 1:1 interaction model. Apparent Kd values were estimated from the concentration of PDK1 which gives 50% of maximal response, which was obtained empirically using GST-PDK1[T148A] (RUmax=435). For all PDK1 construct tested, the off rates for S6Kp-HM were high in comparison to those of PIFtide binding with the time taken for 50% dissociation to occur for 56K-pHM is 30s compared to 1000s for PIFtide. This could account for the overall approximately 100-fold lower affinity of wild type PDK1 for 56K-pHM in comparison to PIFtide.
Data Collection, Structure Solution, and Refinement
Data on PDK1 crystals were collected at the European Synchrotron Radiation Facility (Grenoble, France) beamline ID14-EH1, using an ADSC Q4 CCD detector. The temperature of the crystals was maintained at 100K using a nitrogen cryostream. Data were processed using the HKL package [Otwinowski and Minor, 1997], statistics are shown in Table I.
The structure of PDK1 was solved by molecular replacement with AMoRe [Navaza, 1994] using the structure of PKA in complex with an inhibitory peptide as a search model (PDB entry 1YDB), against 8-4 Å data. A single, well separated solution was found with an R-factor of 0.479 (correlation coefficient=0.428). The structure was automatically built using warpNtrace [Perrakis et al., 1999], which found 262 of a possible 309 residues, giving an initial protein model with R=0.293 (Rfree=0.318) after simulated annealing in CNS [Brunger et al., 1998]. Iterative protein building in 0 [Jones et al., 1991] together with refinement in CNS, which included incorporation of a model for ATP, the phosphoserine in the activation loop, solvent molecules and a key sulphate molecule, resulted in a final model with R=0.195 (Rfree=0.222). No electron density was observed for residues 51-70 (the N-terminus of the construct) and 233-236 (the tip of the activation loop). All figures were made with PyMOL.







TABLE I





Details of data collection &  structure refinement for the PDK1 kinase


domain. Values between brackets are for the highest resolution shell. All


measured data were included in structure refinement.


















Wave length ( )
0.933



Space group
P3221



Unit cell ( )
a = 123.01, b = 123.01, c = 47.62



Resolution ( )
25-2.0 (2.07-1.0)



Observed reflections
77315



Unique reflections
27643



Redundancy
2.8 (2.5)



Completeness (%)
98.0 (93.5)



Rmerge
0.091 (0.454)



I/sigma I
7.3 (2.0)



Rfree reflections
579



Rcryst
0.195



Rfree
0.222







Number of groups










°°Protein residues
71-359



°°Water
200



ATP
1



SO4
5



Glycerol
8



Wilson B (2)
22.4



<B> Protein
25.6



<B> Water
35.7



<B> ATP
38.8







RMSD from ideal geometry










Bond lengths ( )
0.005



Bond angles (°)
1.34



Main chain B (2)
1.5.










REFERENCES


    Alessi, D. R. (2001). Discovery of PDK1, one of the missing links in insulin signal transduction. Biochem. Soc. Trans. 29, 1-14.
    Alessi, D. R., Deak, M., Casamayor, A., Caudwell, F. B., Morrice, N., Norman, D. G., Gaffney, P., Reese, C. B., MacDougall, C. N., Harbison, D., Ashworth, A., and Bownes, M. (1997). 3-phosphoinositide-dependent protein kinase-1 (PDK1): structural and functional homology with the drosophila DSTPK61 kinase. Curr. Biol. 7, 776-789.
    Amadei, A., Linssen, A. B. M., and Berendsen, H. J. C. (1993). Essential dynamics of proteins. Proteins 17, 412-425.
    Balendran, A., Biondi, R. M., Cheung, P. C. F., Casamayor, A., Deak, M., and Alessi, D. R. (2000). A 3-phosphoinositide-dependent protein kinase-1 (PDK1) docking site is required for the phosphorylation of protein kinase c zeta (pkc zeta) and pkc-related kinase 2 by PDK1. J. Biol. Chem. 275, 20806-20813.
    Balendran, A., Casamayor, A., Deak, M., Paterson, A., Gaffney, P., Currie, R., Downes, C. P., and Alessi, D. R. (1999a). PDK1 acquires PDK2 activity in the presence of a synthetic peptide derived from the carboxyl terminus of PRK2. Curr. Biol. 9, 393-404.
    Balendran, A., Currie, R., Armstrong, C. G., Avruch, J., and Alessi, D. R. (1999b). Evidence that 3-phosphoinositide-dependent protein kinase-1 mediatesphosphorylation of p70 56 kinase in vivo at thr-412 as well as thr-252. J. Biol. Chem. 274, 37400-37406.
    Biondi, R. M., Cheung, P. C. F., Casamayor, A., Deak, M., Currie, R. A., and Alessi, D. R. (2000). Identification of a pocket in the pdk1 kinase domain that interacts with pif and the c-terminal residues of pka. Embo J. 19, 979-988.
    Biondi, R. M., Kieloch, A., Currie, R. A., Deak, M., and Alessi, D. R. (2001). The PIF-binding pocket in PDK1 is essential for activation of S6K and SGK, but not PKB. EMBO J. 20, 4380-4390.
    Brazil, D. P. and Hemmings, B. A. (2001). Ten years of protein kinase B signalling: a hard Akt to follow. Trends Biochem. Sci. 26, 657-664.
    Brunger, A. T., Adams, P. D., Clore, G. M., Gros, P., Grosse-Kunstleve, R. W., Jiang, J.-S., Kuszewski, J., Nilges, M., Pannu, N. S., Read, R. J., Rice, L. M., Simonson, T., and Warren, G. L. (1998). Crystallography and NMR system: A new software system for macromolecular structure determination. Acta Cryst. D54, 905-921.
    De Groot, B. L., Hayward, S., van Aalten, D. M. F., Amadei, A., and Berendsen, H. J. C. (1998). Domain motions in bacteriophage t4 lysozyme: A comparison between molecular dynamics and crystallographic data. Proteins 31, 116-127.
    Etchebehere, L. C., VanBemmelen, M. X. P., Anjard, C., Traincard, F., Assemat, K., Reymond, C., and Veron, M. (1997). The catalytic subunit of dictyostelium cAMP-dependent protein kinase-role of the n-terminal domain and of the c-terminal residues in catalytic activity and stability. Eur. J. Biochem. 248, 820-826.
    Frodin, M. and Gammeltoft, S. (1999). Role and regulation of 90 kda ribosomal s6 kinase (rsk) in signal transduction. Mol. Cell. Endocrinol. 151, 65-77.
    Frodin, M., Jensen, C. J., Merienne, K., and Gammeltoft, S. (2000). A phosphoserine-regulated docking site in the protein kinase rsk2 that recruits and activates PDK1. EMBO J. 19, 2924-2934.
    Husen, M. and Kuriyan, J. (2002). The conformational plasticity of protein kinases. Cell 109 (275-282).
    Johnson, D. A., Akamine, P., Radzio-Andzelm, E., Madhusudan, and Taylor, S. S. (2001). Dynamics of camp-dependent protein kinase. Chem. Rev. 101, 2243-2270.
    Johnson, L. N., Noble, M. E. M., and Owen, D. J. (1996). Active and inactive protein kinases: Structural basis for regulation. Cell 85, 149-158.
    Jones, T. A., Zou, J. Y., Cowan, S. W., and Kjeldgaard, M. (1991). Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Cryst. A47, 110-119.
    Kabsch, W. and Sander, C. (1983). Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22, 2577-2637.
    Knighton, D. R., Zheng, J. H., Teneyck, L. F., Ashford, V. A., Xuong, N. H., Taylor, S. S., and Sowadski, J. M. (1991). Crystal-structure of the catalytic subunit of cyclic adenosinemonophosphate dependent protein-kinase. Science 253, 407-414.
    Kobayashi, T. and Cohen, P. (1999). Activation of serum- and glucocorticoid-regulated protein kinase by agonists that activate phosphatidylinositide 3-kinase is mediated by 3-phosphoinositide-dependent protein kinase-1 (pdk1) and pdk2. Biochem. J. 339, 319-328.
    Lang, F. and Cohen, P. (2001). Regulation and physiological roles of serum- and glucocorticoid-induced protein kinase isoforms. Sci. STKE RE17.
    Narayana, N., Cox, S., Xuong, N. H., TenEyck, L. F., and Taylor, S. S. (1997). A binary complex of the catalytic subunit of camp-dependent protein kinase and adenosine further defines conformational flexibility. Structure 5, 921-935.
    Narayana, N., Diller, T. C., Koide, K., Bunnage, M. E., Nicolaou, K. C., Brunton, L. L., Xuong, N. H., Ten Eyck, L. F., and Taylor, S. S. (1999). Crystal structure of the potent natural product inhibitor balanol in complex with the catalytic subunit of camp-dependent protein kinase. Biochemistry 38, 2367-2376.
    Navaza, J. (1994). AMoRe: an automated package for molecular replacement. Acta Cryst. A50, 157-163.
    Otwinowski, Z. and Minor, W. (1997). Processing of X-ray diffraction data collected in oscillation mode. Methods in Enzymology 276, 307-326.
    Perrakis, A., Morris, R., and Lamzin, V. S. (1999). Automated protein model building combined with iterative structure refinement. Nature Struct. Biol. 6, 458-463.
    Prade, L., Engh, R. A., Girod, A., Kinzel, V., Huber, R., and Bossemeyer, D. (1997). Staurosporine-induced conformational changes of camp-dependent protein kinase catalytic subunit explain inhibitory potential. Structure 5, 1627-1637.
    Pullen, N., Dennis, P. B., Andjelkovic, M., Dufner, A., Kozma, S. C., Hemmings, B. A., and Thomas, G. (1998). Phosphorylation and activation of p70(s6k) by pdk1. Science 279, 707-710.
    Scheid, M. P. and Woodgett, J. R. (2001). Pkb/akt: Functional insights from genetic models. Nat. Rev. Mol. Cell. Biol. 2, 760-768.
    Stephens, L., Anderson, K., Stokoe, D., Erdjument-Bromage, H., Painter, G. F., Holmes, A. B., Gaffney, P. R. J., Reese, C. B., McCormick, F., Tempst, P., Coadwell, J., and Hawkins, P. T. (1998). Protein kinase b kinases that mediate phosphatidylinositol 3,4,5-trisphosphate-dependent activation of protein kinase b. Science 279, 710-714.
    Taylor, S. S., Knighton, D. R., Zheng, J. H., Teneyck, L. F., and Sowadski, J. M. (1992). Structural framework for the protein-kinase family. Annu. Rev. Cell Biol. 8, 429-462.
    Taylor, S. S. and Radzioandzelm, E. (1994). 3 protein-kinase structures define a common motif. Structure 2, 345-355.
    Tian, X. J., Rusanescu, G., Hou, W. M., Schaffhausen, B., and Feig, L. A. (2002). Pdk1 mediates growth factor-induced ral-gef activation by a kinase-independent mechanism. Embo J. 21, 1327-1338.
    Toker, A. and Newton, A. C. (2000). Cellular signaling: Pivoting around pdk-1. Cell 103, 185-188.
    van Aalten, D. M. F., Chong, C. R., and Joshua-Tor, L. (2000). Crystal structure of carboxypeptidase a complexed with d-cysteine at 1.75 Å-inhibitor-induced conformational changes. Biochemistry 39, 10082-10089.
    van Aalten, D. M. F., Conn, D. A., de Groot, B. L., Berendsen, H. J. C., Findlay, J. B. C., and Amadei, A. (1997). Protein dynamics derived from clusters of crystal structures. Biophys. J. 73, 2891-2896.
    Volarevic, S, and Thomas, G. (2001). Role of s6 phosphorylation and s6 kinase in cell growth. Prog Nucl Acid Res Mol Biol 65, 101-127.
    Vriend, G. (1990). WHAT IF: a molecular modeling and drug design program. J. Mol. Graph. 8, 52-56.
    Zheng, J. H., Knighton, D. R., Xuong, N. H., Taylor, S. S., Sowadski, J. M., and Teneyck, L. F. (1993). Crystal-structures of the myristylated catalytic subunit of camp-dependent protein-kinase reveal open and closed conformations. Protein Sci. 2, 1559-1573.


Example 2
Co-Ordinates for PDK1Fragment with All Alternate Side Chains












REMARK coordinates from restrained individual B-factor refinement


REMARK refinement resolution: 25.0 - 2.0 A


REMARK starting r= 0.1972 free_r= 0.2220


REMARK final r= 0.1954 free_r= 0.2224


REMARK B rmsd for bonded mainchain atoms= 1.501 target= 1.5


REMARK B rmsd for bonded sidechain atoms= 2.235 target= 2.0


REMARK B rmsd for angle mainchain atoms= 2.347 target= 2.0


REMARK B rmsd for angle sidechain atoms= 3.302 target= 2.5


REMARK rweight= 0.0900 (with wa= 1.29263)


REMARK target= mlf steps= 30


REMARK sg= P3(2)21 a= 123.013 b= 123.013 c= 47.624 alpha= 90 beta= 90


gamma= 120


REMARK parameter file 1 : /dd1/david/projects/PDK1_new/CNS/prot.par


REMARK parameter file 2 : /dd1/david/projects/PDK1_new/CNS/atp.par


REMARK parameter file 3 : CNS_TOPPAR:water_rep.param


REMARK parameter file 4 : CNS_TOPPAR:ion.param


REMARK parameter file 5 : /dd1/david/projects/PDK1_new/CNS/glycerol.par


REMARK molecular structure file: . ./generate/alternate.mtf


REMARK input coordinates: . . /minimize/minimize.pdb


REMARK reflection file=. ./. . /1/hkl/cns.hkl


REMARK ncs= none


REMARK B-correction resolution: 6.0 - 2.0


REMARK initial B-factor correction applied to fobs :


REMARK B11= −2.766 B22= −2.766 B33= 5.532


REMARK B12= −0.375 B13= 0.000 B23= 0.000


REMARK B-factor correction applied to coordinate array B: 0.031 0.031


REMARK bulk solvent: density level= 0.378441 e/A{circumflex over ( )}3, B-factor= 52.6885 A{circumflex over ( )}2


REMARK reflections with |Fobs|/sigma_F < 0.0 rejected


REMARK reflections with |Fobs|> 10000 * rms(Fobs) rejected


REMARK theoretical total number of refl. in resol. range: 28210 ( 100.0% )


REMARK number of unobserved reflections (no entry or |F|= 0): 568 ( 2.0% )


REMARK number of reflections rejected: 0 ( 0.0% )


REMARK total number of reflections used: 27642 ( 98.0% )


REMARK number of reflections in working set: 27063 ( 95.9% )


REMARK number of reflections in test set: 579 ( 2.1% )


CRYST1 123.013 123.013 47.624 90.00 90.00 120.00 P 32 2 1


REMARK FILENAME=“bindividual.pdb”


REMARK DATE:Apr. 16, 2002 18:31:12 created by user: david


REMARK VERSTON:1.0


















ATOM
1
CB
PRO
A
71
58.912
−7.251
8.216
1.00
67.78
A


ATOM
2
CC
PRO
A
71
59.621
−6.941
9.534
1.00
69.16
A


ATOM
3
C
PRO
A
71
59.493
−6.506
5.894
1.00
67.06
A


ATOM
4
O
PRO
A
71
59.196
−5.318
5.766
1.00
66.66
A


ATOM
5
N
PRO
A
71
60.984
−6.073
7.833
1.00
67.86
A


ATOM
6
CD
PRO
A
71
60.554
−5.762
9.207
1.00
68.24
A


ATOM
7
CA
PRO
A
71
60.040
−7.03S
7.217
1.00
67.75
A


ATOM
8
N
PRO
A
72
59.356
−7.38S
4.890
1.00
66.32
A


ATOM
9
CD
PRO
A
72
59.712
−8.816
4.898
1.00
67.17
A


ATOM
10
CA
PRO
A
72
58.840
−6.986
3.S78
1.00
65.61
A


ATOM
11
CB
PRO
A
72
58.672
−8.321
2.8S8
1.00
66.47
A


ATOM
12
CG
PRO
A
72
59.796
−9.133
3.419
1.00
67.57
A


ATOM
13
C
PRO
A
72
57.527
−6.208
3.673
1.00
63.94
A


ATOM
14
O
PRO
A
72
56.710
−6.451
4.561
1.00
64.11
A


ATOM
15
N
ALA
A
73
57.341
−5.268
2.753
1.00
61.57
A


ATOM
16
CA
ALA
A
73
56.133
−4.454
2.708
1.00
58.74
A


ATOM
17
CB
ALA
A
73
56.438
−3.030
3.165
1.00
58.05
A


ATOM
18
C
ALA
A
73
55.626
−4.448
1.271
1.00
56.78
A


ATOM
19
O
ALA
A
73
56.347
−4.834
0.349
1.00
56.95
A


ATOM
20
N
PRO
A
74
54.372
−4.024
1.057
1.00
54.15
A


ATOM
21
CD
PRO
A
74
53.335
−3.610
2.018
1.00
53.31
A


ATOM
22
CA
PRO
A
74
53.856
−4.003
−0.314
1.00
52.54
A


ATOM
23
CB
PRO
A
74
52.474
−3.375
−0.148
1.00
52.86
A


ATOM
24
CG
PRO
A
74
52.067
−3.824
1.226
1.00
52.88
A


ATOM
25
C
PRO
A
74
54.772
−3.167
−1.204
1.00
50.08
A


ATOM
26
O
PRO
A
74
55.559
−2.361
−0.708
1.00
49.96
A


ATOM
27
N
ALA
A
75
54.680
−3.366
−2.514
1.00
47.58
A


ATOM
28
CA
ALA
A
75
55.503
−2.602
−3.446
1.00
44.69
A


ATOM
29
CB
ALA
A
75
55.312
−3.121
−4.870
1.00
46.14
A


ATOM
30
C
ALA
A
75
55.100
−1.134
−3.371
1.00
41.55
A


ATOM
31
O
ALA
A
75
53.947
−0.813
−3.086
1.00
41.01
A


ATOM
32
N
LYS
A
76
56.053
−0.245
−3.619
1.00
38.31
A


ATOM
33
CA
LYS
A
76
55.781
1.184
−3.588
1.00
35.72
A


ATOM
34
CB
LYS
A
76
57.053
1.957
−3.930
1.00
37.70
A


ATOM
35
CG
LYS
A
76
57.123
3.356
−3.350
1.00
40.99
A


ATOM
36
CD
LYS
A
76
57.262
3.316
−1.836
1.00
40.04
A


ATOM
37
CE
LYS
A
76
57.511
4.705
−1.277
1.00
42.08
A


ATOM
38
NZ
LYS
A
76
57.681
4.695
0.202
1.00
42.99
A


ATOM
39
C
LYS
A
76
54.708
1.467
−4.638
1.00
32.65
A


ATOM
40
O
LYS
A
76
54.814
1.005
−5.770
1.00
31.41
A


ATOM
41
N
LYS
A
77
53.668
2.207
−4.270
1.00
28.59
A


ATOM
42
CA
LYS
A
77
52.619
2.517
−5.232
1.00
25.72
A


ATOM
43
CB
LYS
A
77
51.316
2.865
−4.509
1.00
26.22
A


ATOM
44
CG
LYS
A
77
50.796
1.731
−3.631
1.00
27.15
A


ATOM
45
CD
LYS
A
77
49.487
2.089
−2.967
1.00
26.80
A


ATOM
46
CE
LYS
A
77
49.136
1.091
−1.870
1.00
27.31
A


ATOM
47
NZ
LYS
A
77
48.998
−0.296
−2.380
1.00
27.17
A


ATOM
48
C
LYS
A
77
53.053
3.668
−6.137
1.00
24.67
A


ATOM
49
O
LYS
A
77
54.010
4.377
−5.829
1.00
21.60
A


ATOM
50
N
ARG
A
78
52.351
3.838
−7.254
1.00
23.66
A


ATOM
51
CA
ARG
A
78
52.662
4.897
−8.211
1.00
26.14
A


ATOM
52
CB
ARG
A
78
53.574
4.344
−9.318
1.00
28.57
A


ATOM
53
CG
ARG
A
78
53.017
3.139
−10.050
1.00
34.78
A


ATOM
54
CD
ARG
A
78
54.092
2.465
−10.896
1.00
40.96
A


ATOM
55
NE
ARG
A
78
53.560
1.364
−11.700
1.00
48.93
A


ATOM
56
CZ
ARG
A
78
52.985
0.270
−11.203
1.00
52.58
A


ATOM
57
NH1
ARG
A
78
52.860
0.113
−9.889
1.00
54.60
A


ATOM
58
NH2
ARG
A
78
52.530
−0.672
−12.022
1.00
54.09
A


ATOM
59
C
ARG
A
78
51.382
5.488
−8.803
1.00
23.76
A


ATOM
60
O
ARG
A
78
50.311
4.888
−8.706
1.00
24.25
A


ATOM
61
N
PRO
A
79
51.475
6.676
−9.428
1.00
21.76
A


ATOM
62
CD
PRO
A
79
52.691
7.475
−9.668
1.00
20.82
A


ATOM
63
CA
PRO
A
79
50.301
7.325
−10.021
1.00
21.96
A


ATOM
64
CB
PRO
A
79
50.910
8.481
−10.816
1.00
22.27
A


ATOM
65
CG
PRO
A
79
52.124
8.831
−10.014
1.00
22.12
A


ATOM
66
C
PRO
A
79
49.446
6.413
−10.903
1.00
22.86
A


ATOM
67
O
PRO
A
79
48.213
6.461
−10.842
1.00
20.52
A


ATOM
68
N
GLU
A
80
50.103
5.586
−11.714
1.00
21.87
A


ATOM
69
CA
GLU
A
80
49.403
4.685
−12.628
1.00
22.99
A


ATOM
70
CB
GLU

80
50.393
3.994
−13.571
0.50
25.24
AC1


ATOM
71
CG
GLU

80
51.230
2.907
−12.925
0.50
28.75
AC1


ATOM
72
CD
GLU

80
52.157
2.224
−13.913
0.50
31.99
AC1


ATOM
73
OE1
GLU

80
53.072
2.897
−14.433
0.50
34.34
AC1


ATOM
74
OE2
GLU

80
51.969
1.015
−14.172
0.50
32.83
AC1


ATOM
75
C
GLU
A
80
48.556
3.631
−11.912
1.00
22.09
A


ATOM
76
O
GLU
A
80
47.692
3.013
−12.530
1.00
22.37
A


ATOM
77
N
ASP
A
81
48.804
3.413
−10.622
1.00
19.97
A


ATOM
78
CA
ASP
A
81
48.026
2.423
−9.874
1.00
19.93
A


ATOM
79
CB
ASP
A
81
48.736
2.029
−8.571
1.00
21.19
A


ATOM
80
CG
ASP
A
81
50.089
1.380
−8.807
1.00
22.46
A


ATOM
81
OD1
ASP
A
81
50.195
0.554
−9.731
1.00
24.22
A


ATOM
82
OD2
ASP
A
81
51.043
1.685
−8.058
1.00
23.33
A


ATOM
83
C
ASP
A
81
46.652
2.975
−9.518
1.00
20.85
A


ATOM
84
O
ASP
A
81
45.793
2.246
−9.015
1.00
19.96
A


ATOM
85
N
PHE
A
82
46.445
4.258
−9.804
1.00
18.91
A


ATOM
86
CA
PHE
A
82
45.200
4.934
−9.465
1.00
19.30
A


ATOM
87
CB
PHE
A
82
45.475
6.027
−8.427
1.00
18.43
A


ATOM
88
CG
PHE
A
82
46.134
5.531
−7.175
1.00
18.01
A


ATOM
89
CD1
PHE
A
82
45.371
5.136
−6.084
1.00
17.19
A


ATOM
90
CD2
PHE
A
82
47.520
5.460
−7.086
1.00
18.99
A


ATOM
91
CE1
PHE
A
82
45.977
4.676
−4.918
1.00
17.12
A


ATOM
92
CE2
PHE
A
82
48.137
5.000
−5.925
1.00
19.64
A


ATOM
93
CZ
PHE
A
82
47.361
4.607
−4.838
1.00
18.00
A


ATOM
94
C
PHE
A
82
44.476
5.596
−10.621
1.00
20.81
A


ATOM
95
O
PHE
A
82
45.066
5.933
−11.649
1.00
20.34
A


ATOM
96
N
LYS
A
83
43.182
5.792
−10.411
1.00
19.80
A


ATOM
97
CA
LYS
A
83
42.321
6.478
−11.353
1.00
21.65
A


ATOM
98
CB
LYS
A
83
41.096
5.625
−11.687
1.00
22.02
A


ATOM
99
CG
LYS
A
83
40.062
6.326
−12.550
1.00
28.93
A


ATOM
100
CD
LYS
A
83
38.974
5.355
−12.981
1.00
34.20
A


ATOM
101
CE
LYS
A
83
37.909
6.042
−13.824
1.00
38.10
A


ATOM
102
NZ
LYS
A
83
37.179
7.086
−13.043
1.00
43.33
A


ATOM
103
C
LYS
A
83
41.913
7.702
−10.541
1.00
20.74
A


ATOM
104
O
LYS
A
83
41.084
7.606
−9.635
1.00
20.98
A


ATOM
105
N
PHE
A
84
42.513
8.848
−10.835
1.00
19.99
A


ATOM
106
CA
PHE
A
84
42.188
10.049
−10.083
1.00
18.63
A


ATOM
107
CB
PHE
A
84
43.279
11.103
−10.258
1.00
18.95
A


ATOM
108
CG
PHE
A
84
44.571
10.741
−9.587
1.00
17.68
A


ATOM
109
CD1
PHE
A
84
45.498
9.926
−10.224
1.00
18.16
A


ATOM
110
CD2
PHE
A
84
44.843
11.183
−8.299
1.00
19.66
A


ATOM
111
CE1
PHE
A
84
46.676
9.556
−9.589
1.00
18.09
A


ATOM
112
CE2
PHE
A
84
46.021
10.816
−7.653
1.00
18.89
A


ATOM
113
CZ
PHE
A
84
46.936
10.002
−8.301
1.00
17.33
A


ATOM
114
C
PHE
A
84
40.834
10.617
−10.460
1.00
19.69
A


ATOM
115
O
PHE
A
84
40.391
10.489
−11.601
1.00
20.72
A


ATOM
116
N
GLY
A
85
40.178
11.233
−9.484
1.00
16.80
A


ATOM
117
CA
GLY
A
85
38.872
11.810
−9.716
1.00
17.73
A


ATOM
118
C
GLY
A
85
38.819
13.280
−9.346
1.00
18.75
A


ATOM
119
O
GLY
A
85
39.740
14.043
−9.650
1.00
18.45
A


ATOM
120
N
LYS
A
86
37.753
13.673
−8.659
1.00
16.00
A


ATOM
121
CA
LYS
A
86
37.571
15.064
−8.278
1.00
18.26
A


ATOM
122
CB
LYS
A
86
36.133
15.302
−7.812
1.00
19.00
A


ATOM
123
CG
LYS
A
86
35.793
14.660
−6.481
1.00
21.55
A


ATOM
124
CD
LYS
A
86
34.368
14.981
−6.066
1.00
26.48
A


ATOM
125
CE
LYS
A
86
33.994
14.239
−4.793
1.00
31.92
A


ATOM
126
NZ
LYS
A
86
32.568
14.457
−4.412
1.00
35.36
A


ATOM
127
C
LYS
A
86
38.523
15.571
−7.202
1.00
18.57
A


ATOM
128
O
LYS
A
86
39.045
14.807
−6.385
1.00
16.77
A


ATOM
129
N
ILE
A
87
38.737
16.881
−7.227
1.00
17.88
A


ATOM
130
CA
ILE
A
87
39.577
17.554
−6.256
1.00
18.26
A


ATOM
131
CB
ILE
A
87
39.994
18.952
−6.772
1.00
19.60
A


ATOM
132
CG2
ILE
A
87
40.593
19.786
−5.628
1.00
18.73
A


ATOM
133
CG1
ILE
A
87
40.968
18.786
−7.945
1.00
21.16
A


ATOM
134
CD1
ILE
A
87
41.412
20.087
−8.588
1.00
25.26
A


ATOM
135
C
ILE
A
87
38.731
17.709
−4.997
1.00
19.67
A


ATOM
136
O
ILE
A
87
37.628
18.249
−5.052
1.00
20.41
A


ATOM
137
N
LEU
A
88
39.240
17.229
−3.867
1.00
19.15
A


ATOM
138
CA
LEU
A
88
38.508
17.324
−2.611
1.00
20.68
A


ATOM
139
CB
LEU
A
88
38.870
16.151
−1.700
1.00
19.97
A


ATOM
140
CG
LEU
A
88
38.529
14.759
−2.237
1.00
19.24
A


ATOM
141
CD1
LEU
A
88
39.090
13.692
−1.311
1.00
21.41
A


ATOM
142
CD2
LEU
A
88
37.029
14.622
−2.359
1.00
18.84
A


ATOM
143
C
LEU
A
88
38.815
18.632
−1.901
1.00
23.11
A


ATOM
144
O
LEU
A
88
37.999
19.146
−1.139
1.00
25.10
A


ATOM
145
N
GLY
A
89
39.997
19.174
−2.149
1.00
24.09
A


ATOM
146
CA
GLY
A
89
40.367
20.418
−1.507
1.00
24.27
A


ATOM
147
C
GLY
A
89
41.658
20.954
−2.078
1.00
25.47
A


ATOM
148
O
GLY
A
89
42.445
20.202
−2.666
1.00
22.19
A


ATOM
149
N
GLU
A
90
41.870
22.254
−1.906
1.00
26.22
A


ATOM
150
CA
GLU
A
90
43.064
22.924
−2.404
1.00
29.96
A


ATOM
151
CB
GLU
A
90
42.698
23.814
−3.596
1.00
30.75
A


ATOM
152
CG
GLU
A
90
42.267
23.038
−4.831
1.00
34.32
A


ATOM
153
CD
GLU
A
90
41.711
23.930
−5.927
1.00
38.27
A


ATOM
154
OE1
GLU
A
90
40.590
24.456
−5.764
1.00
40.57
A


ATOM
155
0E2
GLU
A
90
42.398
24.110
−6.952
1.00
40.90
A


ATOM
156
C
GLU
A
90
43.711
23.768
−1.313
1.00
30.68
A


ATOM
157
O
GLU
A
90
43.049
24.574
−0.668
1.00
32.83
A


ATOM
158
N
GLY
A
91
45.006
23.566
−1.104
1.00
29.66
A


ATOM
159
CA
GLY
A
91
45.724
24.332
−0.104
1.00
29.40
A


ATOM
160
C
GLY
A
91
46.795
25.151
−0.798
1.00
29.98
A


ATOM
161
O
GLY
A
91
46.894
25.130
−2.028
1.00
28.16
A


ATOM
162
N
SER
A
92
47.605
25.870
−0.029
1.00
28.30
A


ATOM
163
CA
SER
A
92
48.653
26.681
−0.633
1.00
30.50
A


ATOM
164
CB
SER
A
92
49.165
27.717
−0.370
1.00
32.43
A


ATOM
165
OG
SER
A
92
49.520
27.099
−1.593
1.00
40.94
A


ATOM
166
C
SER
A
92
49.815
25.843
−1.164
1.00
29.77
A


ATOM
167
O
SER
A
92
50.456
26.221
−2.143
1.00
30.46
A


ATOM
168
N
PHE
A
93
50.087
24.703
−0.536
1.00
27.65
A


ATOM
169
CA
PHE
A
93
51.185
23.855
−0.995
1.00
26.34
A


ATOM
170
CB
PHE
A
93
52.281
23.785
−0.068
1.00
27.95
A


ATOM
171
CG
PHE
A
93
52.861
25.117
−0.406
1.00
31.06
A


ATOM
172
CD1
PHE
A
93
52.283
25.909
−1.392
1.00
29.96
A


ATOM
173
CD2
PHE
A
93
53.949
25.613
−0.308
1.00
31.38
A


ATOM
174
CE1
PHE
A
93
52.779
27.181
−1.665
1.00
32.69
A


ATOM
175
CE2
PHE
A
93
54.452
26.883
−0.044
1.00
32.63
A


ATOM
176
CZ
PHE
A
93
53.864
27.670
−0.945
1.00
31.81
A


ATOM
177
C
PHE
A
93
50.759
22.445
−1.365
1.00
25.39
A


ATOM
178
O
PHE
A
93
51.601
21.559
−1.522
1.00
24.59
A


ATOM
179
N
SER
A
94
49.457
22.235
−1.519
1.00
23.63
A


ATOM
180
CA
SER
A
94
48.965
20.912
−1.860
1.00
21.43
A


ATOM
181
CB
SER
A
94
49.017
20.013
−0.628
1.00
21.42
A


ATOM
182
OG
SER
A
94
48.091
20.475
−0.340
1.00
21.19
A


ATOM
183
C
SER
A
94
47.539
20.925
−2.378
1.00
19.82
A


ATOM
184
O
SER
A
94
46.795
21.882
−2.173
1.00
18.76
A


ATOM
185
N
THR
A
95
47.174
19.832
−3.038
1.00
19.38
A


ATOM
186
CA
THR
A
95
45.840
19.637
−3.580
1.00
17.98
A


ATOM
187
CB
THR
A
95
45.818
19.818
−5.110
1.00
19.25
A


ATOM
188
OG1
THR
A
95
46.196
21.162
−5.434
1.00
22.04
A


ATOM
189
CG2
THR
A
95
44.421
19.549
−5.661
1.00
17.61
A


ATOM
190
C
THR
A
95
45.455
18.201
−3.243
1.00
18.61
A


ATOM
191
O
THR
A
95
46.212
17.264
−3.524
1.00
17.10
A


ATOM
192
N
VAL
A
96
44.295
18.024
−2.623
1.00
16.53
A


ATOM
193
CA
VAL
A
96
43.845
16.685
−2.266
1.00
16.05
A


ATOM
194
CB
VAL
A
96
43.170
16.672
−0.886
1.00
16.32
A


ATOM
195
CG1
VAL
A
96
42.741
15.249
−0.532
1.00
18.02
A


ATOM
196
CG2
VAL
A
96
44.145
17.206
−0.168
1.00
16.69
A


ATOM
197
C
VAL
A
96
42.875
16.207
−3.335
1.00
16.42
A


ATOM
198
O
VAL
A
96
41.906
16.892
−3.665
1.00
16.47
A


ATOM
199
N
VAL
A
97
43.157
15.033
−3.888
1.00
16.80
A


ATOM
200
CA
VAL
A
97
42.338
14.471
−4.949
1.00
16.72
A


ATOM
201
CB
VAL
A
97
43.153
14.354
−6.255
1.00
18.43
A


ATOM
202
CG1
VAL
A
97
42.249
13.927
−7.404
1.00
19.69
A


ATOM
203
CG2
VAL
A
97
43.831
15.685
−6.569
1.00
17.84
A


ATOM
204
C
VAL
A
97
41.812
13.091
−4.583
1.00
16.77
A


ATOM
205
O
VAL
A
97
42.532
12.270
−4.014
1.00
17.13
A


ATOM
206
N
LEU
A
98
40.545
12.845
−4.895
1.00
16.62
A


ATOM
207
CA
LEU
A
98
39.947
11.548
−4.624
1.00
17.04
A


ATOM
208
CB
LEU
A
98
38.424
11.633
−4.743
1.00
16.89
A


ATOM
209
CG
LEU
A
98
37.635
10.342
−4.508
1.00
19.46
A


ATOM
210
CD1
LEU
A
98
37.990
9.762
−3.146
1.00
20.07
A


ATOM
211
CD2
LEU
A
98
36.143
10.627
−4.588
1.00
17.93
A


ATOM
212
C
LEU
A
98
40.512
10.597
−5.677
1.00
17.38
A


ATOM
213
O
LEU
A
98
40.527
10.920
−6.863
1.00
18.60
A


ATOM
214
N
ALA
A
99
40.995
9.438
−5.246
1.00
17.13
A


ATOM
215
CA
ALA
A
99
41.570
8.466
−6.168
1.00
18.42
A


ATOM
216
CB
ALA
A
99
43.090
8.524
−6.105
1.00
14.76
A


ATOM
217
C
ALA
A
99
41.102
7.055
−5.848
1.00
21.40
A


ATOM
218
O
ALA
A
99
40.941
6.691
−4.679
1.00
22.52
A


ATOM
219
N
ARG
A
100
40.878
6.261
−6.888
1.00
19.77
A


ATOM
220
CA
ARG
A
100
40.459
4.884
−6.693
1.00
20.85
A


ATOM
221
CB
ARG
A
100
39.202
4.585
−7.518
1.00
24.22
A


ATOM
222
CG
ARG
A
100
38.608
3.205
−7.256
1.00
31.78
A


ATOM
223
CD
ARG
A
100
37.326
2.979
−8.048
1.00
36.24
A


ATOM
224
NE
ARG
A
100
36.213
3.818
−7.594
1.00
41.40
A


ATOM
225
CZ
ARG
A
100
35.566
3.662
−6.439
1.00
42.05
A


ATOM
226
NH1
ARG
A
100
35.912
2.696
−5.598
1.00
40.67
A


ATOM
227
NH2
ARG
A
100
34.559
4.468
−6.128
1.00
43.65
A


ATOM
228
C
ARG
A
100
41.613
3.985
−7.129
1.00
18.63
A


ATOM
229
O
ARG
A
100
42.078
4.065
−8.271
1.00
19.49
A


ATOM
230
N
GLU
A
101
42.102
3.157
−6.212
1.00
16.43
A


ATOM
231
CA
GLU
A
101
43.196
2.246
−6.533
1.00
16.11
A


ATOM
232
CB
GLU
A
101
43.774
1.637
−5.248
1.00
16.79
A


ATOM
233
CG
GLU
A
101
44.917
0.657
−5.488
1.00
16.51
A


ATOM
234
CD
GLU
A
101
45.501
0.115
−4.200
1.00
18.20
A


ATOM
235
OE1
GLU
A
101
44.733
−0.081
−3.239
1.00
18.32
A


ATOM
236
OE2
GLU
A
101
46.725
−0.132
−4.150
1.00
17.14
A


ATOM
237
C
GLU
A
101
42.625
1.152
−7.442
1.00
17.92
A


ATOM
238
O
GLU
A
101
41.681
0.462
−7.069
1.00
18.02
A


ATOM
239
N
LEU
A
102
43.198
1.002
−8.632
1.00
19.06
A


ATOM
240
CA
LEU
A
102
42.718
0.025
−9.607
1.00
20.71
A


ATOM
241
CB
LEU
A
102
43.569
0.097
−10.878
1.00
23.42
A


ATOM
242
CG
LEU
A
102
43.531
1.426
−11.642
1.00
25.30
A


ATOM
243
CD1
LEU
A
102
44.577
1.414
−12.748
1.00
27.88
A


ATOM
244
CD2
LEU
A
102
42.140
1.647
−12.214
1.00
26.79
A


ATOM
245
C
LEU
A
102
42.671
−1.418
−9.125
1.00
21.62
A


ATOM
246
O
LEU
A
102
41.668
−2.103
−9.305
1.00
21.09
A


ATOM
247
N
ALA
A
103
43.753
−1.874
−8.507
1.00
19.38
A


ATOM
248
CA
ALA
A
103
43.836
−3.249
−8.035
1.00
20.87
A


ATOM
249
CB
ALA
A
103
45.284
−3.571
−7.671
1.00
19.23
A


ATOM
250
C
ALA
A
103
42.919
−3.629
−6.872
1.00
19.92
A


ATOM
251
O
ALA
A
103
42.703
−4.815
−6.628
1.00
20.38
A


ATOM
252
N
THR
A
104
42.361
−2.643
−6.175
1.00
18.12
A


ATOM
253
CA
THR
A
104
41.517
−2.927
−5.018
1.00
17.15
A


ATOM
254
CB
THR
A
104
42.212
−2.484
−3.717
1.00
19.54
A


ATOM
255
CC1
THR
A
104
42.456
−1.070
−3.773
1.00
19.26
A


ATOM
256
CC2
THR
A
104
43.536
−3.219
−3.529
1.00
17.02
A


ATOM
257
C
THR
A
104
40.159
−2.247
−5.026
1.00
19.44
A


ATOM
258
O
THR
A
104
39.259
−2.648
−4.285
1.00
18.70
A


ATOM
259
N
SER
A
105
40.034
−1.207
−5.847
1.00
19.65
A


ATOM
260
CA
SER
A
105
38.819
−0.400
−5.967
1.00
19.37
A


ATOM
261
CB
SER

105
37.598
−1.304
−6.173
0.50
21.81
AC1


ATOM
262
OG
SER

105
36.431
−0.539
−6.412
0.50
23.01
AC1


ATOM
263
C
SER
A
105
38.644
0.447
−4.701
1.00
18.99
A


ATOM
264
O
SER
A
105
37.602
1.070
−4.488
1.00
18.66
A


ATOM
265
N
ARC
A
106
39.674
0.468
−3.861
1.00
16.84
A


ATOM
266
CA
ARC
A
106
39.655
1.267
−2.634
1.00
16.21
A


ATOM
267
CB
ARC
A
106
40.827
0.886
−1.723
1.00
16.41
A


ATOM
268
CC
ARC
A
106
40.619
−0.367
−0.906
1.00
15.49
A


ATOM
269
CD
ARC
A
106
41.887
−0.755
−0.170
1.00
17.43
A


ATOM
270
NE
ARC
A
106
41.620
−1.792
0.824
1.00
20.47
A


ATOM
271
CZ
ARC
A
106
42.548
−2.568
1.371
1.00
20.24
A


ATOM
272
NH1
ARC
A
106
43.821
−2.433
1.017
1.00
17.80
A


ATOM
273
NH2
ARC
A
106
42.198
−3.468
2.285
1.00
20.14
A


ATOM
274
C
ARC
A
106
39.785
2.746
−2.981
1.00
17.37
A


ATOM
275
O
ARC
A
106
40.514
3.103
−3.902
1.00
17.75
A


ATOM
276
N
CLU
A
107
39.085
3.599
−2.240
1.00
16.06
A


ATOM
277
CA
CLU
A
107
39.156
5.039
−2.461
1.00
20.80
A


ATOM
278
CB
CLU
A
107
37.779
5.694
−2.337
1.00
22.93
A


ATOM
279
CC
CLU
A
107
36.711
5.171
−3.269
1.00
30.87
A


ATOM
280
CD
CLU
A
107
35.431
5.975
−3.148
1.00
32.40
A


ATOM
281
OE1
CLU
A
107
35.262
6.939
−3.923
1.00
33.74
A


ATOM
282
OE2
CLU
A
107
34.608
5.654
−2.263
1.00
36.00
A


ATOM
283
C
CLU
A
107
40.053
5.678
−1.410
1.00
18.93
A


ATOM
284
O
CLU
A
107
39.891
5.427
−0.220
1.00
19.21
A


ATOM
285
N
TYR
A
108
40.988
6.507
−1.852
1.00
16.70
A


ATOM
286
CA
TYR
A
108
41.883
7.209
−0.942
1.00
15.86
A


ATOM
287
CB
TYR
A
108
43.325
6.728
−1.104
1.00
15.30
A


ATOM
288
CC
TYR
A
108
43.593
5.328
−0.612
1.00
16.33
A


ATOM
289
CD1
TYR
A
108
43.765
5.066
0.746
1.00
16.36
A


ATOM
290
CE1
TYR
A
108
44.046
3.769
1.201
1.00
18.48
A


ATOM
291
CD2
TYR
A
108
43.701
4.268
−1.511
1.00
13.25
A


ATOM
292
CE2
TYR
A
108
43.980
2.981
−1.075
1.00
17.28
A


ATOM
293
CZ
TYR
A
108
44.152
2.736
0.276
1.00
19.17
A


ATOM
294
OH
TYR
A
108
44.440
1.461
0.688
1.00
19.38
A


ATOM
295
C
TYR
A
108
41.850
8.687
−1.292
1.00
16.80
A


ATOM
296
O
TYR
A
108
41.560
9.058
−2.431
1.00
15.22
A


ATOM
297
N
ALA
A
109
42.132
9.528
−0.306
1.00
14.61
A


ATOM
298
CA
ALA
A
109
42.207
10.957
−0.539
1.00
14.30
A


ATOM
299
CB
ALA
A
109
41.671
11.726
0.661
1.00
14.78
A


ATOM
300
C
ALA
A
109
43.713
11.136
−0.667
1.00
16.79
A


ATOM
301
O
ALA
A
109
44.450
10.983
0.317
1.00
16.52
A


ATOM
302
N
ILE
A
110
44.182
11.410
−1.881
1.00
14.80
A


ATOM
303
CA
ILE
A
110
45.609
11.574
−2.093
1.00
15.80
A


ATOM
304
CB
ILE
A
110
46.065
10.863
−3.396
1.00
16.85
A


ATOM
305
CC2
ILE
A
110
47.550
11.098
−3.632
1.00
16.80
A


ATOM
306
CC1
ILE
A
110
45.774
9.358
−3.284
1.00
17.76
A


ATOM
307
CD1
ILE
A
110
46.308
8.513
−4.437
1.00
16.07
A


ATOM
308
C
ILE
A
110
46.004
13.045
−2.129
1.00
17.78
A


ATOM
309
O
ILE
A
110
45.534
13.813
−2.976
1.00
16.24
A


ATOM
310
N
LYS
A
111
46.846
13.435
−1.177
1.00
16.15
A


ATOM
311
CA
LYS
A
111
47.326
14.808
−1.100
1.00
17.20
A


ATOM
312
CB
LYS
A
111
47.700
15.176
0.344
1.00
17.41
A


ATOM
313
CG
LYS
A
111
48.350
16.547
0.464
1.00
20.71
A


ATOM
314
CD
LYS
A
111
48.585
16.971
1.910
1.00
24.25
A


ATOM
315
CE
LYS
A
111
47.288
17.381
2.598
1.00
29.46
A


ATOM
316
NZ
LYS
A
111
47.516
17.866
4.000
1.00
30.50
A


ATOM
317
C
LYS
A
111
48.551
14.890
−1.994
1.00
16.41
A


ATOM
318
O
LYS
A
111
49.509
14.137
−1.813
1.00
18.20
A


ATOM
319
N
ILE
A
112
48.509
15.798
−2.963
1.00
15.87
A


ATOM
320
CA
ILE
A
112
49.606
15.967
−3.907
1.00
17.28
A


ATOM
321
CB
ILE
A
112
49.079
15.911
−5.358
1.00
16.43
A


ATOM
322
CG2
ILE
A
112
50.235
15.998
−6.341
1.00
15.12
A


ATOM
323
CG1
ILE
A
112
48.293
14.609
−5.565
1.00
16.82
A


ATOM
324
CD1
ILE
A
112
47.580
14.511
−6.904
1.00
18.47
A


ATOM
325
C
ILE
A
112
50.307
17.301
−3.663
1.00
19.03
A


ATOM
326
O
ILE
A
112
49.669
18.350
−3.635
1.00
19.15
A


ATOM
327
N
LEU
A
113
51.622
17.245
−3.472
1.00
20.22
A


ATOM
328
CA
LEU
A
113
52.416
18.442
−3.214
1.00
22.36
A


ATOM
329
CB
LEU
A
113
52.995
18.397
−1.794
1.00
22.13
A


ATOM
330
CG
LEU
A
113
52.042
18.063
−0.646
1.00
22.46
A


ATOM
331
CD1
LEU
A
113
51.866
16.557
−0.553
1.00
23.81
A


ATOM
332
CD2
LEU
A
113
52.603
18.595
0.660
1.00
23.68
A


ATOM
333
C
LEU
A
113
53.560
18.547
−4.215
1.00
23.37
A


ATOM
334
O
LEU
A
113
54.300
17.586
−4.424
1.00
23.11
A


ATOM
335
N
GLU
A
114
53.706
19.714
−4.834
1.00
23.88
A


ATOM
336
CA
GLU
A
114
54.771
19.920
−5.806
1.00
26.00
A


ATOM
337
CB
GLU
A
114
54.435
21.111
−6.706
1.00
27.74
A


ATOM
338
CG
GLU
A
114
55.533
21.452
−7.696
1.00
35.07
A


ATOM
339
CD
GLU
A
114
55.220
22.696
−8.497
1.00
39.24
A


ATOM
340
OE1
GLU
A
114
54.808
23.703
−7.885
1.00
41.45
A


ATOM
341
OE2
GLU
A
114
55.395
22.670
−9.736
1.00
44.05
A


ATOM
342
C
GLU
A
114
56.087
20.163
−5.067
1.00
24.37
A


ATOM
343
O
GLU
A
114
56.186
21.071
−4.238
1.00
24.43
A


ATOM
344
N
LYS
A
115
57.096
19.350
−5.360
1.00
24.10
A


ATOM
345
CA
LYS
A
115
58.376
19.493
−4.678
1.00
24.93
A


ATOM
346
CB
LYS
A
115
59.339
18.373
−5.103
1.00
23.72
A


ATOM
347
CG
LYS
A
115
59.139
17.080
−4.308
1.00
23.09
A


ATOM
348
CD
LYS
A
115
60.064
15.944
−4.743
1.00
21.92
A


ATOM
349
CE
LYS
A
115
59.691
15.400
−6.117
1.00
22.42
A


ATOM
350
NZ
LYS
A
115
60.447
14.150
−6.448
1.00
19.71
A


ATOM
351
C
LYS
A
115
59.031
20.858
−4.868
1.00
26.87
A


ATOM
352
O
LYS
A
115
59.492
21.469
−3.903
1.00
26.17
A


ATOM
353
N
ARG
A
116
59.058
21.348
−6.102
1.00
28.73
A


ATOM
354
CA
ARG
A
116
59.678
22.638
−6.380
1.00
29.66
A


ATOM
355
CB
ARG

116
59.533
22.980
−7.868
0.50
31.29
AC1


ATOM
356
CG
ARG

116
60.047
24.361
−8.267
0.50
33.19
AC1


ATOM
357
CD
ARG

116
61.368
24.710
−7.590
0.50
35.13
AC1


ATOM
358
NE
ARG

116
62.329
23.612
−7.618
0.50
36.42
AC1


ATOM
359
CZ
ARG

116
63.510
23.648
−7.009
0.50
36.18
AC1


ATOM
360
NH1
ARG

116
63.871
24.729
−6.332
0.50
36.12
AC1


ATOM
361
NH2
ARG

116
64.324
22.602
−7.067
0.50
35.77
AC1


ATOM
362
C
ARG
A
116
59.097
23.761
−5.519
1.00
29.70
A


ATOM
363
O
ARG
A
116
59.843
24.515
−4.889
1.00
29.16
A


ATOM
364
N
HIS
A
117
57.773
23.862
−5.472
1.00
27.22
A


ATOM
365
CA
HIS
A
117
57.126
24.903
−4.681
1.00
26.33
A


ATOM
366
CB
HIS
A
117
55.606
24.835
−4.848
1.00
28.41
A


ATOM
367
CG
HIS
A
117
54.881
26.00
−54.258
1.00
31.82
A


ATOM
368
CD2
HIS
A
117
55.309
27.24
−93.935
1.00
33.19
A


ATOM
369
ND1
HIS
A
117
53.536
25.97
−43.961
1.00
34.30
A


ATOM
370
CE1
HIS
A
117
53.165
27.14
−83.480
1.00
34.58
A


ATOM
371
NE2
HIS
A
117
54.222
27.94
−03.455
1.00
35.18
A


ATOM
372
C
HIS
A
117
57.477
24.78
−03.202
1.00
26.22
A


ATOM
373
O
HIS
A
117
57.737
25.77
−62.534
1.00
25.67
A


ATOM
374
N
ILE
A
118
57.469
23.554
−2.689
1.00
24.94
A


ATOM
375
CA
ILE
A
118
57.792
23.315
−1.285
1.00
23.94
A


ATOM
376
CB
ILE
A
118
57.711
21.812
−0.952
1.00
23.50
A


ATOM
377
CG2
ILE
A
118
58.374
21.533
0.389
1.00
23.76
A


ATOM
378
CG1
ILE
A
118
56.246
21.362
−0.959
1.00
24.42
A


ATOM
379
CD1
ILE
A
118
56.066
19.858
−0.834
1.00
28.06
A


ATOM
380
C
ILE
A
118
59.195
23.821
−0.958
1.00
23.78
A


ATOM
381
O
ILE
A
118
59.402
24.495
−0.048
1.00
23.49
A


ATOM
382
N
ILE
A
119
60.153
23.489
−1.815
1.00
23.46
A


ATOM
383
CA
ILE
A
119
61.534
23.913
−1.619
1.00
25.13
A


ATOM
384
CB
ILE
A
119
62.467
23.250
−2.664
1.00
24.25
A


ATOM
385
CG2
ILE
A
119
63.858
23.890
−2.617
1.00
22.47
A


ATOM
386
CG1
ILE
A
119
62.540
21.738
−2.395
1.00
25.05
A


ATOM
387
CD1
ILE
A
119
63.327
20.945
−3.439
1.00
24.62
A


ATOM
388
C
ILE
A
119
61.667
25.435
−1.705
1.00
25.96
A


ATOM
389
O
ILE
A
119
62.330
26.051
−0.872
1.00
24.78
A


ATOM
390
N
LYS
A
120
61.028
26.039
−2.704
1.00
27.67
A


ATOM
391
CA
LYS
A
120
61.100
27.489
−2.879
1.00
30.29
A


ATOM
392
CB
LYS
A
120
60.242
27.940
−4.060
1.00
32.34
A


ATOM
393
CG
LYS
A
120
60.674
27.407
−5.409
1.00
39.30
A


ATOM
394
CD
LYS
A
120
59.765
27.950
−6.512
1.00
45.19
A


ATOM
395
CE
LYS
A
120
58.294
27.636
−6.218
1.00
46.48
A


ATOM
396
NZ
LYS
A
120
57.363
28.155
−7.252
1.00
46.49
A


ATOM
397
C
LYS
A
120
60.647
28.247
−1.638
1.00
30.89
A


ATOM
398
O
LYS
A
120
61.303
29.198
−1.217
1.00
32.48
A


ATOM
399
N
GLU
A
121
59.527
27.825
−1.055
1.00
29.82
A


ATOM
400
CA
GLU
A
121
58.986
28.488
0.128
1.00
30.33
A


ATOM
401
CB
GLU
A
121
57.455
28.416
0.117
1.00
33.04
A


ATOM
402
CG
GLU
A
121
56.794
29.021
−1.120
1.00
36.45
A


ATOM
403
CD
GLU
A
121
57.221
30.456
−1.373
1.00
39.88
A


ATOM
404
OE1
GLU
A
121
57.200
31.264
−0.420
1.00
40.53
A


ATOM
405
OE2
GLU
A
121
57.573
30.778
−2.529
1.00
43.24
A


ATOM
406
C
GLU
A
121
59.511
27.930
1.451
1.00
30.37
A


ATOM
407
O
GLU
A
121
58.946
28.204
2.513
1.00
31.24
A


ATOM
408
N
ASN
A
122
60.588
27.151
1.390
1.00
29.03
A


ATOM
409
CA
ASN
A
122
61.183
26.573
2.594
1.00
28.46
A


ATOM
410
CB
ASN
A
122
61.836
27.673
3.436
1.00
31.28
A


ATOM
411
CG
ASN
A
122
62.945
28.395
2.698
1.00
34.12
A


ATOM
412
OD1
ASN
A
122
62.697
29.143
1.754
1.00
35.57
A


ATOM
413
ND2
ASN
A
122
64.181
28.169
3.127
1.00
35.73
A


ATOM
414
C
ASN
A
122
60.157
25.835
3.456
1.00
26.89
A


ATOM
415
O
ASN
A
122
60.085
26.055
4.663
1.00
27.23
A


ATOM
416
N
LYS
A
123
59.375
24.955
2.842
1.00
23.99
A


ATOM
417
CA
LYS
A
123
58.358
24.210
3.574
1.00
22.43
A


ATOM
418
CB
LYS
A
123
57.031
24.248
2.810
1.00
21.97
A


ATOM
419
CG
LYS
A
123
56.475
25.645
2.599
1.00
25.68
A


ATOM
420
CD
LYS
A
123
56.253
26.354
3.927
1.00
27.54
A


ATOM
421
CE
LYS
A
123
55.822
27.796
3.716
1.00
31.30
A


ATOM
422
NZ
LYS
A
123
55.756
28.540
5.004
1.00
33.21
A


ATOM
423
C
LYS
A
123
58.748
22.759
3.821
1.00
22.20
A


ATOM
424
O
LYS
A
123
57.924
21.960
4.264
1.00
22.50
A


ATOM
425
N
VAL
A
124
59.997
22.412
3.535
1.00
20.59
A


ATOM
426
CA
VAL
A
124
60.439
21.039
3.730
1.00
20.25
A


ATOM
427
CB
VAL
A
124
61.922
20.850
3.328
1.00
19.43
A


ATOM
428
CG1
VAL
A
124
62.346
19.407
3.573
1.00
18.69
A


ATOM
429
CG2
VAL
A
124
62.104
21.195
1.853
1.00
18.21
A


ATOM
430
C
VAL
A
124
60.236
20.561
5.163
1.00
19.53
A


ATOM
431
O
VAL
A
124
59.841
19.418
5.385
1.00
20.02
A


ATOM
432
N
PRO
A
125
60.513
21.422
6.159
1.00
20.01
A


ATOM
433
CD
PRO
A
125
61.178
22.738
6.118
1.00
18.69
A


ATOM
434
CA
PRO
A
125
60.318
20.979
7.544
1.00
19.88
A


ATOM
435
CB
PRO
A
125
60.793
22.180
8.363
1.00
19.95
A


ATOM
436
CG
PRO
A
125
61.839
22.805
7.479
1.00
18.85
A


ATOM
437
C
PRO
A
125
58.848
20.642
7.824
1.00
19.76
A


ATOM
438
O
PRO
A
125
58.544
19.700
8.550
1.00
16.99
A


ATOM
439
N
TYR
A
126
57.947
21.418
7.235
1.00
18.98
A


ATOM
440
CA
TYR
A
126
56.516
21.220
7.435
1.00
21.97
A


ATOM
441
CB
TYR
A
126
55.752
22.448
6.933
1.00
25.17
A


ATOM
442
CG
TYR
A
126
56.040
23.690
7.748
1.00
30.98
A


ATOM
443
CD1
TYR
A
126
55.438
23.886
8.991
1.00
33.95
A


ATOM
444
CE1
TYR
A
126
55.721
25.015
9.763
1.00
36.60
A


ATOM
445
CD2
TYR
A
126
56.938
24.657
7.292
1.00
35.43
A


ATOM
446
CE2
TYR
A
126
57.231
25.792
8.058
1.00
37.20
A


ATOM
447
CZ
TYR
A
126
56.618
25.962
9.291
1.00
37.40
A


ATOM
448
OH
TYR
A
126
56.903
27.073
10.052
1.00
40.85
A


ATOM
449
C
TYR
A
126
55.990
19.956
6.762
1.00
21.35
A


ATOM
450
O
TYR
A
126
55.265
19.175
7.383
1.00
20.49
A


ATOM
451
N
VAL
A
127
56.354
19.746
5.501
1.00
18.16
A


ATOM
452
CA
VAL
A
127
55.892
18.562
4.790
1.00
17.58
A


ATOM
453
CB
VAL
A
127
56.308
18.596
3.308
1.00
17.45
A


ATOM
454
CG1
VAL
A
127
55.786
17.350
2.600
1.00
17.97
A


ATOM
455
CG2
VAL
A
127
55.751
19.850
2.641
1.00
14.90
A


ATOM
456
C
VAL
A
127
56.459
17.306
5.448
1.00
18.39
A


ATOM
457
O
VAL
A
127
55.769
16.298
5.583
1.00
18.14
A


ATOM
458
N
THR
A
128
57.716
17.381
5.869
1.00
17.50
A


ATOM
459
CA
THR
A
128
58.375
16.260
6.530
1.00
18.54
A


ATOM
460
CB
THR
A
128
59.861
16.586
6.805
1.00
18.01
A


ATOM
461
OG1
THR
A
128
60.537
16.804
5.559
1.00
21.14
A


ATOM
462
CG2
THR
A
128
60.536
15.446
7.545
1.00
17.95
A


ATOM
463
C
THR
A
128
57.676
15.941
7.856
1.00
19.49
A


ATOM
464
O
THR
A
128
57.438
14.776
8.179
1.00
18.76
A


ATOM
465
N
ARG
A
129
57.345
16.981
8.619
1.00
19.60
A


ATOM
466
CA
ARG
A
129
56.673
16.804
9.904
1.00
20.12
A


ATOM
467
CB
ARG
A
129
56.534
18.144
10.621
1.00
21.33
A


ATOM
468
CG
ARG
A
129
55.948
18.029
12.023
1.00
28.02
A


ATOM
469
CD
ARG
A
129
55.721
19.404
12.597
1.00
31.25
A


ATOM
470
NE
ARG
A
129
56.940
20.205
12.560
1.00
37.78
A


ATOM
471
CZ
ARG
A
129
56.962
21.524
12.391
1.00
40.10
A


ATOM
472
NH1
ARG
A
129
55.828
22.197
12.239
1.00
40.03
A


ATOM
473
NH2
ARG
A
129
58.119
22.170
12.374
1.00
44.58
A


ATOM
474
C
ARG
A
129
55.288
16.186
9.729
1.00
20.08
A


ATOM
475
O
ARG
A
129
54.891
15.305
10.496
1.00
20.40
A


ATOM
476
N
GLU
A
130
54.553
16.654
8.724
1.00
18.79
A


ATOM
477
CA
GLU
A
130
53.222
16.125
8.454
1.00
20.10
A


ATOM
478
CB
GLU
A
130
52.638
16.749
7.183
1.00
19.92
A


ATOM
479
CG
GLU
A
130
51.350
16.087
6.708
1.00
27.85
A


ATOM
480
CD
GLU
A
130
50.581
16.933
5.707
1.00
29.72
A


ATOM
481
OE1
GLU
A
130
51.216
17.528
4.814
1.00
33.46
A


ATOM
482
OE2
GLU
A
130
49.339
16.996
5.807
1.00
30.74
A


ATOM
483
C
GLU
A
130
53.301
14.615
8.295
1.00
19.81
A


ATOM
484
O
GLU
A
130
52.553
13.875
8.935
1.00
18.37
A


ATOM
485
N
ARG
A
131
54.219
14.162
7.447
1.00
20.41
A


ATOM
486
CA
ARG
A
131
54.397
12.735
7.202
1.00
22.45
A


ATOM
487
CB
ARG
A
131
55.442
12.511
6.098
1.00
25.16
A


ATOM
488
CG
ARG
A
131
55.742
11.043
5.840
1.00
28.75
A


ATOM
489
CD
ARG
A
131
56.736
10.837
4.708
1.00
33.75
A


ATOM
490
NE
ARG
A
131
57.020
9.415
4.520
1.00
40.07
A


ATOM
491
CZ
ARG
A
131
57.756
8.915
3.532
1.00
43.07
A


ATOM
492
NH1
ARG
A
131
58.293
9.721
2.625
1.00
44.91
A


ATOM
493
NH2
ARG
A
131
57.955
7.606
3.449
1.00
44.45
A


ATOM
494
C
ARG
A
131
54.820
11.982
8.466
1.00
23.24
A


ATOM
495
O
ARG
A
131
54.241
10.948
8.804
1.00
23.86
A


ATOM
496
N
ASP
A
132
55.831
12.497
9.160
1.00
21.99
A


ATOM
497
CA
ASP
A
132
56.318
11.850
10.370
1.00
22.04
A


ATOM
498
CB
ASP
A
132
57.570
12.564
10.888
1.00
23.72
A


ATOM
499
CG
ASP
A
132
58.750
12.442
9.932
1.00
27.77
A


ATOM
500
OD1
ASP
A
132
58.681
11.620
8.989
1.00
27.34
A


ATOM
501
OD2
ASP
A
132
59.753
13.163
10.128
1.00
28.70
A


ATOM
502
C
ASP
A
132
55.258
11.772
11.474
1.00
21.69
A


ATOM
503
O
ASP
A
132
55.077
10.723
12.092
1.00
22.75
A


ATOM
504
N
VAL
A
133
54.551
12.868
11.725
1.00
19.54
A


ATOM
505
CA
VAL
A
133
53.525
12.843
12.759
1.00
18.52
A


ATOM
506
CB
VAL
A
133
52.908
14.244
12.990
1.00
19.26
A


ATOM
507
CG1
VAL
A
133
51.708
14.135
13.918
1.00
18.79
A


ATOM
508
CG2
VAL
A
133
53.953
15.180
13.604
1.00
18.80
A


ATOM
509
C
VAL
A
133
52.419
11.854
12.398
1.00
19.46
A


ATOM
510
O
VAL
A
133
52.073
10.991
13.200
1.00
19.94
A


ATOM
511
N
MET
A
134
51.878
11.957
11.187
1.00
19.15
A


ATOM
512
CA
MET
A
134
50.807
11.052
10.792
1.00
21.25
A


ATOM
513
CB
MET
A
134
50.309
11.381
9.383
1.00
17.34
A


ATOM
514
CG
MET
A
134
49.615
12.730
9.302
1.00
20.00
A


ATOM
515
SD
MET
A
134
48.643
12.952
7.798
1.00
24.21
A


ATOM
516
CE
MET
A
134
47.033
12.434
8.400
1.00
23.20
A


ATOM
517
C
MET
A
134
51.203
9.582
10.881
1.00
22.43
A


ATOM
518
O
MET
A
134
50.384
8.741
11.249
1.00
23.82
A


ATOM
519
N
SER
A
135
52.454
9.273
10.556
1.00
23.09
A


ATOM
520
CA
SER
A
135
52.939
7.895
10.615
1.00
26.13
A


ATOM
521
CB
SER
A
135
54.356
7.798
10.039
1.00
26.17
A


ATOM
522
OG
SER
A
135
54.383
8.177
8.673
1.00
31.91
A


ATOM
523
C
SER
A
135
52.957
7.358
12.045
1.00
26.58
A


ATOM
524
O
SER
A
135
52.926
6.148
12.261
1.00
26.42
A


ATOM
525
N
ARG
A
136
53.014
8.261
13.018
1.00
25.65
A


ATOM
526
CA
ARG
A
136
53.056
7.870
14.425
1.00
27.47
A


ATOM
527
CB
ARG
A
136
53.823
8.914
15.238
1.00
27.97
A


ATOM
528
CG
ARG
A
136
55.283
9.082
14.857
1.00
32.00
A


ATOM
529
CD
ARG
A
136
55.904
10.218
15.664
1.00
33.03
A


ATOM
530
NE
ARG
A
136
55.602
10.073
17.084
1.00
36.11
A


ATOM
531
CZ
ARG
A
136
55.867
10.990
18.007
1.00
39.74
A


ATOM
532
NH1
ARG
A
136
56.449
12.132
17.661
1.00
40.55
A


ATOM
533
NH2
ARG
A
136
55.540
10.769
19.276
1.00
36.72
A


ATOM
534
C
ARG
A
136
51.667
7.709
15.036
1.00
26.38
A


ATOM
535
O
ARG
A
136
51.516
7.121
16.106
1.00
27.06
A


ATOM
536
N
LEU
A
137
50.655
8.235
14.360
1.00
24.77
A


ATOM
537
CA
LEU
A
137
49.294
8.162
14.870
1.00
24.70
A


ATOM
538
CB
LEU
A
137
48.483
9.363
14.371
1.00
24.52
A


ATOM
539
CG
LEU
A
137
49.050
10.760
14.662
1.00
26.67
A


ATOM
540
CD1
LEU
A
137
48.075
11.813
14.141
1.00
27.25
A


ATOM
541
CD2
LEU
A
137
49.279
10.945
16.155
1.00
27.09
A


ATOM
542
C
LEU
A
137
48.592
6.868
14.473
1.00
25.20
A


ATOM
543
O
LEU
A
137
48.619
6.469
13.309
1.00
25.99
A


ATOM
544
N
ASP
A
138
47.971
6.218
15.451
1.00
21.89
A


ATOM
545
CA
ASP
A
138
47.239
4.977
15.219
1.00
21.35
A


ATOM
546
CB
ASP
A
138
48.124
3.761
15.523
1.00
22.14
A


ATOM
547
CC
ASP
A
138
47.432
2.448
15.201
1.00
24.90
A


ATOM
548
OD1
ASP
A
138
46.631
2.423
14.241
1.00
24.78
A


ATOM
549
OD2
ASP
A
138
47.691
1.443
15.897
1.00
25.39
A


ATOM
550
C
ASP
A
138
46.031
4.991
16.138
1.00
20.47
A


ATOM
551
O
ASP
A
138
45.967
4.248
17.118
1.00
19.06
A


ATOM
552
N
HIS
A
139
45.075
5.852
15.810
1.00
18.27
A


ATOM
553
CA
HIS
A
139
43.869
6.016
16.606
1.00
18.21
A


ATOM
554
CB
HIS
A
139
44.096
7.157
17.612
1.00
15.84
A


ATOM
555
CC
HIS
A
139
42.985
7.332
18.600
1.00
15.24
A


ATOM
556
CD2
HIS
A
139
42.884
6.964
19.900
1.00
13.97
A


ATOM
557
ND1
HIS
A
139
41.791
7.943
18.280
1.00
14.74
A


ATOM
558
CE1
HIS
A
139
41.002
7.944
19.341
1.00
14.19
A


ATOM
559
NE2
HIS
A
139
41.641
7.356
20.336
1.00
14.15
A


ATOM
560
C
HIS
A
139
42.715
6.330
15.654
1.00
18.50
A


ATOM
561
O
HIS
A
139
42.879
7.080
14.693
1.00
20.80
A


ATOM
562
N
PRO
A
140
41.527
5.767
15.913
1.00
18.32
A


ATOM
563
CD
PRO
A
140
41.143
4.984
17.100
1.00
16.71
A


ATOM
564
CA
PRO
A
140
40.367
6.001
15.048
1.00
17.43
A


ATOM
565
CB
PRO
A
140
39.273
5.157
15.704
1.00
16.64
A


ATOM
566
CC
PRO
A
140
39.643
5.204
17.152
1.00
18.43
A


ATOM
567
C
PRO
A
140
39.914
7.441
14.803
1.00
18.77
A


ATOM
568
O
PRO
A
140
39.207
7.695
13.831
1.00
19.88
A


ATOM
569
N
PHE
A
141
40.301
8.381
15.664
1.00
17.14
A


ATOM
570
CA
PHE
A
141
39.874
9.767
15.477
1.00
16.42
A


ATOM
571
CB
PHE
A
141
39.568
10.422
16.836
1.00
14.60
A


ATOM
572
CC
PHE
A
141
38.386
9.817
17.556
1.00
15.26
A


ATOM
573
CD1
PHE
A
141
37.335
9.234
16.842
1.00
14.78
A


ATOM
574
CD2
PHE
A
141
38.297
9.880
18.942
1.00
13.70
A


ATOM
575
CE1
PHE
A
141
36.215
8.727
17.502
1.00
16.94
A


ATOM
576
CE2
PHE
A
141
37.178
9.375
19.615
1.00
15.75
A


ATOM
577
CZ
PHE
A
141
36.135
8.799
18.893
1.00
16.89
A


ATOM
578
C
PHE
A
141
40.857
10.641
14.694
1.00
16.15
A


ATOM
579
O
PHE
A
141
40.799
11.871
14.761
1.00
17.35
A


ATOM
580
N
PHE
A
142
41.748
10.011
13.941
1.00
15.88
A


ATOM
581
CA
PHE
A
142
42.727
10.756
13.154
1.00
17.89
A


ATOM
582
CB
PHE
A
142
44.115
10.645
13.793
1.00
17.57
A


ATOM
583
CC
PHE
A
142
44.240
11.371
15.103
1.00
18.74
A


ATOM
584
CD1
PHE
A
142
44.559
12.726
15.135
1.00
17.77
A


ATOM
585
CD2
PHE
A
142
43.997
10.711
16.304
1.00
18.74
A


ATOM
586
CE1
PHE
A
142
44.632
13.417
16.347
1.00
15.77
A


ATOM
587
CE2
PHE
A
142
44.065
11.393
17.522
1.00
17.56
A


ATOM
588
CZ
PHE
A
142
44.383
12.747
17.542
1.00
17.14
A


ATOM
589
C
PHE
A
142
42.793
10.231
11.729
1.00
19.12
A


ATOM
590
O
PHE
A
142
42.659
9.030
11.504
1.00
20.01
A


ATOM
591
N
VAL
A
143
42.978
11.135
10.769
1.00
18.72
A


ATOM
592
CA
VAL
A
143
43.102
10.735
9.371
1.00
18.52
A


ATOM
593
CB
VAL
A
143
43.294
11.961
8.440
1.00
20.66
A


ATOM
594
Cd
VAL
A
143
43.843
11.521
7.080
1.00
21.29
A


ATOM
595
CC2
VAL
A
143
41.958
12.673
8.252
1.00
22.97
A


ATOM
596
C
VAL
A
143
44.342
9.865
9.330
1.00
18.68
A


ATOM
597
O
VAL
A
143
45.355
10.199
9.943
1.00
18.42
A


ATOM
598
N
LYS
A
144
44.259
8.745
8.623
1.00
18.30
A


ATOM
599
CA
LYS
A
144
45.384
7.824
8.535
1.00
18.78
A


ATOM
600
CB
LYS
A
144
44.889
6.373
8.608
1.00
22.27
A


ATOM
601
CC
LYS
A
144
46.017
5.340
8.557
1.00
29.72
A


ATOM
602
CD
LYS
A
144
45.491
3.912
8.674
1.00
34.16
A


ATOM
603
CE
LYS
A
144
46.631
2.896
8.577
1.00
37.67
A


ATOM
604
NZ
LYS
A
144
46.138
1.484
8.629
1.00
39.02
A


ATOM
605
C
LYS
A
144
46.192
8.002
7.261
1.00
18.53
A


ATOM
606
O
LYS
A
144
45.643
8.314
6.200
1.00
18.18
A


ATOM
607
N
LEU
A
145
47.502
7.816
7.385
1.00
16.79
A


ATOM
608
CA
LEU
A
145
48.411
7.900
6.251
1.00
17.45
A


ATOM
609
CB
LEU

145
49.686
8.653
6.641
0.50
18.82
AC1


ATOM
610
CO
LEU

145
50.734
8.902
5.549
0.50
20.23
AC1


ATOM
611
CD1
LEU

145
51.836
9.799
6.093
0.50
18.83
AC1


ATOM
612
CD2
LEU

145
51.317
7.581
5.069
0.50
19.79
AC1


ATOM
613
C
LEU
A
145
48.739
6.450
5.907
1.00
19.19
A


ATOM
614
O
LEU
A
145
49.451
5.772
6.659
1.00
17.36
A


ATOM
615
N
TYR
A
146
48.215
5.972
4.782
1.00
17.28
A


ATOM
616
CA
TYR
A
146
48.444
4.593
4.358
1.00
17.57
A


ATOM
617
CB
TYR
A
146
47.288
4.098
3.486
1.00
17.74
A


ATOM
618
CO
TYR
A
146
45.981
3.926
4.214
1.00
17.50
A


ATOM
619
CD1
TYR
A
146
45.099
4.995
4.377
1.00
16.50
A


ATOM
620
CE1
TYR
A
146
43.881
4.827
5.039
1.00
17.10
A


ATOM
621
CD2
TYR
A
146
45.620
2.686
4.735
1.00
18.28
A


ATOM
622
CE2
TYR
A
146
44.411
2.506
5.399
1.00
19.84
A


ATOM
623
CZ
TYR
A
146
43.547
3.576
5.544
1.00
17.53
A


ATOM
624
OH
TYR
A
146
42.342
3.376
6.169
1.00
20.67
A


ATOM
625
C
TYR
A
146
49.735
4.376
3.582
1.00
18.72
A


ATOM
626
O
TYR
A
146
50.382
3.338
3.715
1.00
19.51
A


ATOM
627
N
PHE
A
147
50.110
5.350
2.765
1.00
18.09
A


ATOM
628
CA
PHE
A
147
51.307
5.203
1.952
1.00
17.20
A


ATOM
629
CB
PHE
A
147
51.007
4.258
0.783
1.00
16.77
A


ATOM
630
CO
PHE
A
147
49.835
4.699
−0.070
1.00
17.75
A


ATOM
631
CD1
PHE
A
147
49.967
5.752
−0.975
1.00
16.58
A


ATOM
632
CD2
PHE
A
147
48.595
4.075
0.053
1.00
18.07
A


ATOM
633
CE1
PHE
A
147
48.886
6.178
−1.742
1.00
19.62
A


ATOM
634
CE2
PHE
A
147
47.503
4.492
−0.710
1.00
18.56
A


ATOM
635
CZ
PHE
A
147
47.647
5.546
−1.610
1.00
19.27
A


ATOM
636
C
PHE
A
147
51.768
6.533
1.395
1.00
17.13
A


ATOM
637
O
PHE
A
147
51.045
7.528
1.452
1.00
14.43
A


ATOM
638
N
THR
A
148
52.981
6.534
0.854
1.00
17.12
A


ATOM
639
CA
THR
A
148
53.541
7.718
0.232
1.00
17.96
A


ATOM
640
CB
THR
A
148
54.449
8.531
1.197
1.00
21.51
A


ATOM
641
CO1
THR
A
148
55.605
7.760
1.537
1.00
18.83
A


ATOM
642
CO2
THR
A
148
53.700
8.897
2.472
1.00
19.60
A


ATOM
643
C
THR
A
148
54.386
7.262
−0.946
1.00
20.31
A


ATOM
644
O
THR
A
148
54.860
6.124
−0.991
1.00
18.94
A


ATOM
645
N
PHE
A
149
54.543
8.149
−1.916
1.00
19.16
A


ATOM
646
CA
PHE
A
149
55.368
7.877
−3.073
1.00
18.01
A


ATOM
647
CB
PHE
A
149
54.748
6.801
−3.989
1.00
17.23
A


ATOM
648
CO
PHE
A
149
53.389
7.144
−4.544
1.00
16.88
A


ATOM
649
CD1
PHE
A
149
53.262
7.888
−5.712
1.00
18.58
A


ATOM
650
CD2
PHE
A
149
52.235
6.668
−3.927
1.00
17.31
A


ATOM
651
CE1
PHE
A
149
52.007
8.149
−6.267
1.00
19.26
A


ATOM
652
CE2
PHE
A
149
50.972
6.923
−4.470
1.00
19.17
A


ATOM
653
CZ
PHE
A
149
50.858
7.663
−5.642
1.00
19.60
A


ATOM
654
C
PHE
A
149
55.542
9.205
−3.774
1.00
20.85
A


ATOM
655
O
PHE
A
149
54.934
10.200
−3.376
1.00
19.76
A


ATOM
656
N
OLN
A
150
56.398
9.241
−4.782
1.00
19.79
A


ATOM
657
CA
OLN
A
150
56.636
10.481
−5.497
1.00
24.03
A


ATOM
658
CB
OLN
A
150
57.659
11.347
−4.739
1.00
24.45
A


ATOM
659
CO
OLN
A
150
58.986
10.645
−4.414
1.00
26.28
A


ATOM
660
CD
OLN
A
150
59.988
11.558
−3.692
1.00
29.02
A


ATOM
661
OE1
OLN
A
150
60.693
12.353
−4.321
1.00
27.05
A


ATOM
662
NE2
GIN
A
150
60.042
11.449
−2.365
1.00
26.47
A


ATOM
663
C
GIN
A
150
57.160
10.203
−6.885
1.00
23.88
A


ATOM
664
O
GIN
A
150
57.673
9.118
−7.158
1.00
24.79
A


ATOM
665
N
ASP
A
151
56.987
11.171
−7.774
1.00
25.88
A


ATOM
666
CA
ASP
A
151
57.527
11.047
−9.117
1.00
26.49
A


ATOM
667
CB
ASP
A
151
56.437
11.126
−10.199
1.00
24.54
A


ATOM
668
CC
ASP
A
151
55.544
12.336
−10.064
1.00
24.95
A


ATOM
669
OD1
ASP
A
151
56.005
13.379
−9.561
1.00
22.44
A


ATOM
670
OD2
ASP
A
151
54.369
12.242
−10.490
1.00
25.72
A


ATOM
671
C
ASP
A
151
58.515
12.203
−9.220
1.00
28.63
A


ATOM
672
O
ASP
A
151
58.890
12.780
−8.194
1.00
27.83
A


ATOM
673
N
ASP
A
152
58.934
12.560
−10.426
1.00
29.21
A


ATOM
674
CA
ASP
A
152
59.907
13.636
−10.562
1.00
31.88
A


ATOM
675
CB
ASP
A
152
60.325
13.792
−12.026
1.00
33.94
A


ATOM
676
CC
ASP
A
152
61.033
12.564
−12.557
1.00
38.88
A


ATOM
677
OD1
ASP
A
152
61.817
11.959
−11.791
1.00
39.67
A


ATOM
678
OD2
ASP
A
152
60.817
12.211
−13.738
1.00
41.57
A


ATOM
679
C
ASP
A
152
59.487
14.994
−10.013
1.00
30.90
A


ATOM
680
O
ASP
A
152
60.316
15.735
−9.482
1.00
31.69
A


ATOM
681
N
CLU
A
153
58.207
15.322
−10.107
1.00
29.44
A


ATOM
682
CA
CLU
A
153
57.767
16.632
−9.646
1.00
28.69
A


ATOM
683
CB
CLU
A
153
56.984
17.327
−10.766
1.00
32.90
A


ATOM
684
CC
CLU
A
153
57.451
16.987
−12.183
1.00
40.57
A


ATOM
685
CD
CLU
A
153
56.920
15.643
−12.675
1.00
45.78
A


ATOM
686
OE1
CLU
A
153
55.682
15.482
−12.760
1.00
48.91
A


ATOM
687
0E2
CLU
A
153
57.736
14.747
−12.979
1.00
48.95
A


ATOM
688
C
CLU
A
153
56.929
16.683
−8.372
1.00
26.43
A


ATOM
689
O
CLU
A
153
56.947
17.688
−7.660
1.00
25.08
A


ATOM
690
N
LYS
A
154
56.205
15.610
−8.069
1.00
22.39
A


ATOM
691
CA
LYS
A
154
55.318
15.631
−6.912
1.00
21.43
A


ATOM
692
CB
LYS
A
154
53.861
15.628
−7.398
1.00
20.33
A


ATOM
693
CC
LYS
A
154
53.505
16.716
−8.403
1.00
21.92
A


ATOM
694
CD
LYS
A
154
52.211
16.375
−9.146
1.00
19.70
A


ATOM
695
CE
LYS
A
154
51.775
17.503
−10.077
1.00
20.04
A


ATOM
696
NZ
LYS
A
154
50.631
17.094
−10.951
1.00
19.97
A


ATOM
697
C
LYS
A
154
55.458
14.522
−5.881
1.00
20.43
A


ATOM
698
O
LYS
A
154
55.949
13.426
−6.173
1.00
21.13
A


ATOM
699
N
LEU
A
155
54.985
14.832
−4.676
1.00
19.69
A


ATOM
700
CA
LEU
A
155
54.950
13.900
−3.553
1.00
19.10
A


ATOM
701
CB
LEU

155
55.362
14.588
−2.252
1.00
19.65
A


ATOM
702
CC
LEU
A
155
56.740
15.234
−2.129
1.00
21.20
A


ATOM
703
CD1
LEU
A
155
56.848
15.918
−0.770
1.00
23.42
A


ATOM
704
CD2
LEU
A
155
57.816
14.174
−2.277
1.00
23.08
A


ATOM
705
C
LEU
A
155
53.478
13.507
−3.427
1.00
18.87
A


ATOM
706
O
LEU
A
155
52.600
14.348
−3.620
1.00
18.61
A


ATOM
707
N
TYR
A
156
53.209
12.249
−3.091
1.00
15.02
A


ATOM
708
CA
TYR
A
156
51.834
11.783
−2.934
1.00
16.29
A


ATOM
709
CB
TYR
A
156
51.470
10.769
−4.029
1.00
14.20
A


ATOM
710
CC
TYR
A
156
51.603
11.273
−5.449
1.00
17.29
A


ATOM
711
CD1
TYR
A
156
52.857
11.429
−6.045
1.00
16.46
A


ATOM
712
CEl
TYR
A
156
52.978
11.884
−7.360
1.00
18.68
A


ATOM
713
CD2
TYR
A
156
50.474
11.588
−6.202
1.00
16.43
A


ATOM
714
CE2
TYR
A
156
50.583
12.048
−7.512
1.00
16.31
A


ATOM
715
CZ
TYR
A
156
51.835
12.192
−8.083
1.00
18.17
A


ATOM
716
OH
TYR
A
156
51.941
12.651
−9.371
1.00
17.47
A


ATOM
717
C
TYR
A
156
51.657
11.108
−1.572
1.00
16.32
A


ATOM
718
O
TYR
A
156
52.412
10.197
−1.235
1.00
16.27
A


ATOM
719
N
PHE
A
157
50.678
11.568
−0.792
1.00
15.47
A


ATOM
720
CA
PHE
A
157
50.385
10.966
0.508
1.00
16.66
A


ATOM
721
CB
PHE
A
157
50.324
12.014
1.629
1.00
16.91
A


ATOM
722
CG
PHE
A
157
51.631
12.708
1.907
1.00
18.96
A


ATOM
723
CD1
PHE
A
157
52.821
12.261
1.340
1.00
20.31
A


ATOM
724
CD2
PHE
A
157
51.664
13.829
2.732
1.00
21.12
A


ATOM
725
CE1
PHE
A
157
54.025
12.926
1.585
1.00
22.08
A


ATOM
726
CE2
PHE
A
157
52.865
14.500
2.982
1.00
22.18
A


ATOM
727
CZ
PHE
A
157
54.045
14.045
2.405
1.00
21.27
A


ATOM
728
C
PHE
A
157
49.016
10.308
0.404
1.00
16.52
A


ATOM
729
O
PHE
A
157
48.029
10.979
0.110
1.00
17.32
A


ATOM
730
N
GLY
A
158
48.953
9.002
0.644
1.00
15.97
A


ATOM
731
CA
GLY
A
158
47.684
8.299
0.572
1.00
16.13
A


ATOM
732
C
GLY
A
158
47.000
8.383
1.920
1.00
14.94
A


ATOM
733
O
GLY
A
158
47.445
7.756
2.879
1.00
16.28
A


ATOM
734
N
LEU
A
159
45.915
9.145
1.989
1.00
13.50
A


ATOM
735
CA
LEU
A
159
45.191
9.340
3.241
1.00
15.20
A


ATOM
736
CB
LEU
A
159
45.031
10.835
3.517
1.00
14.20
A


ATOM
737
CG
LEU
A
159
46.270
11.726
3.385
1.00
19.00
A


ATOM
738
CD1
LEU
A
159
45.847
13.188
3.477
1.00
17.12
A


ATOM
739
CD2
LEU
A
159
47.275
11.390
4.471
1.00
14.71
A


ATOM
740
C
LEU
A
159
43.809
8.716
3.232
1.00
15.53
A


ATOM
741
O
LEU
A
159
43.232
8.472
2.177
1.00
16.05
A


ATOM
742
N
SER
A
160
43.268
8.469
4.418
1.00
15.86
A


ATOM
743
CA
SER
A
160
41.932
7.917
4.498
1.00
19.01
A


ATOM
744
CB
SER
A
160
41.566
7.582
5.949
1.00
22.90
A


ATOM
745
OG
SER
A
160
41.901
8.629
6.833
1.00
24.18
A


ATOM
746
C
SER
A
160
40.987
8.968
3.924
1.00
20.43
A


ATOM
747
O
SER
A
160
41.213
10.173
4.062
1.00
19.96
A


ATOM
748
N
TYR
A
161
39.945
8.508
3.250
1.00
19.20
A


ATOM
749
CA
TYR
A
161
38.975
9.406
2.644
1.00
20.37
A


ATOM
750
CB
TYR
A
161
38.471
8.785
1.332
1.00
20.00
A


ATOM
751
CG
TYR
A
161
37.314
9.502
0.666
1.00
20.72
A


ATOM
752
CD1
TYR
A
161
37.222
10.895
0.682
1.00
18.22
A


ATOM
753
CE1
TYR
A
161
36.180
11.557
0.029
1.00
22.24
A


ATOM
754
CD2
TYR
A
161
36.333
8.784
−0.020
1.00
20.53
A


ATOM
755
CE2
TYR
A
161
35.287
9.436
−0.678
1.00
24.24
A


ATOM
756
CZ
TYR
A
161
35.218
10.822
−0.648
1.00
22.32
A


ATOM
757
OH
TYR
A
161
34.194
11.471
−1.298
1.00
23.03
A


ATOM
758
C
TYR
A
161
37.812
9.681
3.598
1.00
20.14
A


ATOM
759
O
TYR
A
161
36.959
8.819
3.810
1.00
19.53
A


ATOM
760
N
ALA
A
162
37.791
10.880
4.178
1.00
19.92
A


ATOM
761
CA
ALA
A
162
36.721
11.271
5.099
1.00
21.07
A


ATOM
762
CB
ALA
A
162
37.187
12.419
6.002
1.00
19.60
A


ATOM
763
C
ALA
A
162
35.542
11.712
4.238
1.00
22.07
A


ATOM
764
O
ALA
A
162
35.436
12.875
3.860
1.00
20.66
A


ATOM
765
N
LYS
A
163
34.653
10.769
3.945
1.00
23.27
A


ATOM
766
CA
LYS
A
163
33.503
11.017
3.080
1.00
27.12
A


ATOM
767
CB
LYS
A
163
32.663
9.741
2.963
1.00
29.68
A


ATOM
768
CG
LYS
A
163
33.455
8.524
2.515
1.00
37.67
A


ATOM
769
CD
LYS
A
163
32.556
7.310
2.321
1.00
42.24
A


ATOM
770
CE
LYS
A
163
33.373
6.034
2.185
1.00
44.48
A


ATOM
771
NZ
LYS
A
163
34.143
5.735
3.430
1.00
44.88
A


ATOM
772
C
LYS
A
163
32.581
12.186
3.411
1.00
25.78
A


ATOM
773
O
LYS
A
163
32.103
12.863
2.506
1.00
26.53
A


ATOM
774
N
ASN
A
164
32.327
12.441
4.689
1.00
24.57
A


ATOM
775
CA
ASN
A
164
31.420
13.522
5.033
1.00
23.77
A


ATOM
776
CB
ASN
A
164
30.610
13.129
6.265
1.00
25.02
A


ATOM
777
CG
ASN
A
164
29.537
12.101
5.932
1.00
27.54
A


ATOM
778
OD1
ASN
A
164
28.772
12.281
4.983
1.00
28.79
A


ATOM
779
ND2
ASN
A
164
29.475
11.024
6.704
1.00
27.13
A


ATOM
780
C
ASN
A
164
31.999
14.931
5.169
1.00
24.43
A


ATOM
781
O
ASN
A
164
31.306
15.856
5.589
1.00
23.98
A


ATOM
782
N
GLY
A
165
33.262
15.097
4.795
1.00
21.56
A


ATOM
783
CA
GLY
A
165
33.873
16.414
4.836
1.00
24.39
A


ATOM
784
C
GLY
A
165
34.191
17.043
6.181
1.00
23.62
A


ATOM
785
O
GLY
A
165
34.380
16.352
7.177
1.00
23.26
A


ATOM
786
N
GLU
A
166
34.234
18.373
6.186
1.00
23.22
A


ATOM
787
CA
GLU
A
166
34.563
19.176
7.362
1.00
24.54
A


ATOM
788
CB
GLU
A
166
35.055
20.558
6.913
1.00
25.04
A


ATOM
789
CG
GLU
A
166
36.419
20.569
6.229
1.00
26.48
A


ATOM
790
CD
GLU
A
166
36.699
21.889
5.517
1.00
30.02
A


ATOM
791
OE1
GLU
A
166
36.081
22.906
5.889
1.00
29.33
A


ATOM
792
0E2
GLU
A
166
37.544
21.916
4.596
1.00
30.48
A


ATOM
793
C
GLU
A
166
33.436
19.372
8.369
1.00
24.44
A


ATOM
794
O
GLU
A
166
32.279
19.541
8.001
1.00
22.76
A


ATOM
795
N
LEU
A
167
33.791
19.370
9.649
1.00
22.95
A


ATOM
796
CA
LEU
A
167
32.813
19.581
10.707
1.00
22.26
A


ATOM
797
CB
LEU
A
167
33.497
19.481
12.073
1.00
22.32
A


ATOM
798
CG
LEU
A
167
32.706
19.923
13.306
1.00
22.04
A


ATOM
799
CD1
LEU
A
167
31.454
19.074
13.463
1.00
19.66
A


ATOM
800
CD2
LEU
A
167
33.597
19.805
14.537
1.00
21.17
A


ATOM
801
C
LEU
A
167
32.193
20.971
10.529
1.00
23.49
A


ATOM
802
O
LEU
A
167
31.047
21.209
10.907
1.00
23.56
A


ATOM
803
N
LEU
A
168
32.960
21.887
9.948
1.00
24.25
A


ATOM
804
CA
LEU
A
168
32.473
23.245
9.722
1.00
26.64
A


ATOM
805
CB
LEU
A
168
33.560
24.099
9.066
1.00
25.62
A


ATOM
806
CG
LEU
A
168
33.198
25.546
8.707
1.00
27.34
A


ATOM
807
CD1
LEU
A
168
32.718
26.296
9.946
1.00
26.42
A


ATOM
808
CD2
LEU
A
168
34.418
26.238
8.119
1.00
26.74
A


ATOM
809
C
LEU
A
168
31.234
23.218
8.829
1.00
27.13
A


ATOM
810
O
LEU
A
168
30.297
23.989
9.030
1.00
26.01
A


ATOM
811
N
LYS
A
169
31.233
22.320
7.848
1.00
26.41
A


ATOM
812
CA
LYS
A
169
30.106
22.210
6.934
1.00
27.70
A


ATOM
813
CB
LYS
A
169
30.324
21.064
5.945
1.00
30.49
A


ATOM
814
CG
LYS
A
169
29.151
20.854
4.993
1.00
32.47
A


ATOM
815
CD
LYS
A
169
29.407
19.728
3.998
1.00
35.98
A


ATOM
816
CE
LYS
A
169
29.462
18.372
4.683
1.00
38.53
A


ATOM
817
NZ
LYS
A
169
29.622
17.263
3.702
1.00
41.00
A


ATOM
818
C
LYS
A
169
28.801
21.985
7.682
1.00
28.12
A


ATOM
819
O
LYS
A
169
27.785
22.608
7.371
1.00
28.08
A


ATOM
820
N
TYR
A
170
28.826
21.094
8.668
1.00
26.53
A


ATOM
821
CA
TYR
A
170
27.624
20.791
9.434
1.00
26.95
A


ATOM
822
CB
TYR
A
170
27.810
19.476
10.193
1.00
25.03
A


ATOM
823
CG
TYR
A
170
27.898
18.300
9.251
1.00
26.65
A


ATOM
824
CD1
TYR
A
170
26.745
17.661
8.790
1.00
28.27
A


ATOM
825
CE1
TYR
A
170
26.814
16.642
7.839
1.00
26.85
A


ATOM
826
CD2
TYR
A
170
29.127
17.884
8.742
1.00
27.83
A


ATOM
827
CE2
TYR
A
170
29.209
16.869
7.792
1.00
27.19
A


ATOM
828
CZ
TYR
A
170
28.049
16.254
7.343
1.00
30.02
A


ATOM
829
OH
TYR
A
170
28.130
15.268
6.382
1.00
29.23
A


ATOM
830
C
TYR
A
170
27.229
21.918
10.376
1.00
27.59
A


ATOM
831
O
TYR
A
170
26.045
22.122
10.642
1.00
29.25
A


ATOM
832
N
ILE
A
171
28.208
22.660
10.882
1.00
28.16
A


ATOM
833
CA
ILE
A
171
27.883
23.770
11.763
1.00
29.03
A


ATOM
834
CB
ILE
A
171
29.151
24.435
12.337
1.00
27.51
A


ATOM
835
CG2
ILE
A
171
28.773
25.705
13.084
1.00
27.97
A


ATOM
836
CG1
ILE
A
171
29.872
23.458
13.272
1.00
26.70
A


ATOM
837
CD1
ILE
A
171
31.163
23.996
13.856
1.00
24.07
A


ATOM
838
C
ILE
A
171
27.094
24.796
10.944
1.00
31.41
A


ATOM
839
O
ILE
A
171
26.088
25.335
11.407
1.00
31.69
A


ATOM
840
N
ARG
A
172
27.546
25.047
9.719
1.00
33.21
A


ATOM
841
CA
ARG
A
172
26.874
26.000
8.844
1.00
36.54
A


ATOM
842
CB
ARG
A
172
27.734
26.314
7.616
1.00
37.73
A


ATOM
843
CG
ARG
A
172
29.057
27.011
7.912
1.00
41.65
A


ATOM
844
CD
ARG
A
172
29.708
27.492
6.616
1.00
45.29
A


ATOM
845
NE
ARG
A
172
31.037
28.070
6.812
1.00
48.51
A


ATOM
846
CZ
ARG
A
172
31.314
29.059
7.658
1.00
51.53
A


ATOM
847
NH1
ARG
A
172
30.355
29.593
8.406
1.00
53.75
A


ATOM
848
NH2
ARG
A
172
32.553
29.526
7.748
1.00
51.21
A


ATOM
849
C
ARG
A
172
25.528
25.459
8.378
1.00
37.67
A


ATOM
850
O
ARG
A
172
24.550
26.200
8.288
1.00
39.09
A


ATOM
851
N
LYS
A
173
25.481
24.163
8.092
1.00
38.44
A


ATOM
852
CA
LYS
A
173
24.259
23.528
7.619
1.00
39.25
A


ATOM
853
CB
LYS
A
173
24.523
22.061
7.272
1.00
41.89
A


ATOM
854
CG
LYS
A
173
23.279
21.298
6.830
1.00
45.52
A


ATOM
855
CD
LYS
A
173
23.557
19.808
6.653
1.00
49.60
A


ATOM
856
CE
LYS
A
173
24.477
19.530
5.469
1.00
52.63
A


ATOM
857
NZ
LYS
A
173
23.855
19.894
4.160
1.00
54.61
A


ATOM
858
C
LYS
A
173
23.089
23.608
8.595
1.00
39.30
A


ATOM
859
O
LYS
A
173
21.981
23.960
8.201
1.00
39.62
A


ATOM
860
N
ILE
A
174
23.320
23.282
9.863
1.00
37.96
A


ATOM
861
CA
ILE
A
174
22.229
23.314
10.833
1.00
37.36
A


ATOM
862
CB
ILE
A
174
22.159
21.998
11.652
1.00
37.44
A


ATOM
863
CG2
ILE
A
174
22.058
20.802
10.709
1.00
38.37
A


ATOM
864
CG1
ILE
A
174
23.397
21.850
12.532
1.00
37.25
A


ATOM
865
CD1
ILE
A
174
23.355
20.620
13.418
1.00
36.85
A


ATOM
866
C
ILE
A
174
22.259
24.492
11.801
1.00
36.71
A


ATOM
867
O
ILE
A
174
21.448
24.556
12.724
1.00
38.05
A


ATOM
868
N
GLY
A
175
23.185
25.423
11.592
1.00
35.48
A


ATOM
869
CA
GLY
A
175
23.265
26.585
12.462
1.00
35.29
A


ATOM
870
C
GLY
A
175
24.053
26.360
13.737
1.00
35.06
A


ATOM
871
O
GLY
A
175
25.066
27.019
13.970
1.00
37.46
A


ATOM
872
N
SER
A
176
23.581
25.441
14.571
1.00
33.94
A


ATOM
873
CA
SER
A
176
24.253
25.113
15.822
1.00
32.84
A


ATOM
874
CB
SER
A
176
23.938
26.155
16.901
1.00
33.54
A


ATOM
875
OG
SER
A
176
22.599
26.056
17.347
1.00
34.86
A


ATOM
876
C
SER
A
176
23.796
23.731
16.276
1.00
32.34
A


ATOM
877
O
SER
A
176
22.726
23.263
15.884
1.00
32.82
A


ATOM
878
N
PHE
A
177
24.609
23.085
17.103
1.00
29.39
A


ATOM
879
CA
PHE
A
177
24.313
21.743
17.597
1.00
27.20
A


ATOM
880
CB
PHE
A
177
25.621
20.989
17.865
1.00
26.39
A


ATOM
881
CG
PHE
A
177
26.372
20.585
16.622
1.00
26.18
A


ATOM
882
CD1
PHE
A
177
26.210
21.277
15.426
1.00
25.30
A


ATOM
883
CD2
PHE
A
177
27.266
19.516
16.662
1.00
26.05
A


ATOM
884
CE1
PHE
A
177
26.923
20.912
14.290
1.00
26.59
A


ATOM
885
CE2
PHE
A
177
27.986
19.143
15.532
1.00
26.06
A


ATOM
886
CZ
PHE
A
177
27.815
19.841
14.343
1.00
25.42
A


ATOM
887
C
PHE
A
177
23.500
21.752
18.884
1.00
27.00
A


ATOM
888
O
PHE
A
177
23.704
22.610
19.747
1.00
26.48
A


ATOM
889
N
ASP
A
178
22.578
20.802
19.022
1.00
26.70
A


ATOM
890
CA
ASP
A
178
21.816
20.729
20.260
1.00
26.35
A


ATOM
891
CB
ASP
A
178
20.621
19.773
20.142
1.00
29.90
A


ATOM
892
CG
ASP
A
178
21.020
18.372
19.720
1.00
32.28
A


ATOM
893
OD1
ASP
A
178
22.157
17.949
20.014
1.00
35.21
A


ATOM
894
0D2
ASP
A
178
20.179
17.683
19.105
1.00
34.79
A


ATOM
895
C
ASP
A
178
22.810
20.228
21.311
1.00
25.03
A


ATOM
896
O
ASP
A
178
23.974
19.968
20.992
1.00
21.24
A


ATOM
897
N
GLU
A
179
22.361
20.083
22.552
1.00
23.60
A


ATOM
898
CA
GLU
A
179
23.247
19.644
23.619
1.00
25.18
A


ATOM
899
CB
GLU
A
179
22.542
19.770
24.971
1.00
27.60
A


ATOM
900
CC
GLU
A
179
23.324
19.176
26.130
1.00
32.58
A


ATOM
901
CD
GLU
A
179
22.997
19.845
27.449
1.00
35.82
A


ATOM
902
OE1
GLU
A
179
21.825
20.224
27.645
1.00
35.95
A


ATOM
903
OE2
GLU
A
179
23.912
19.984
28.291
1.00
38.19
A


ATOM
904
C
GLU
A
179
23.808
18.235
23.450
1.00
24.08
A


ATOM
905
O
GLU
A
179
24.977
17.989
23.756
1.00
22.79
A


ATOM
906
N
THR
A
180
22.983
17.316
22.961
1.00
23.36
A


ATOM
907
CA
THR
A
180
23.412
15.935
22.761
1.00
22.15
A


ATOM
908
CB
THR
A
180
22.224
15.054
22.320
1.00
23.77
A


ATOM
909
OG1
THR
A
180
21.222
15.075
23.341
1.00
26.37
A


ATOM
910
CC2
THR
A
180
22.670
13.616
22.088
1.00
22.66
A


ATOM
911
C
THR
A
180
24.533
15.830
21.724
1.00
22.01
A


ATOM
912
O
THR
A
180
25.533
15.141
21.944
1.00
19.87
A


ATOM
913
N
CYS
A
181
24.365
16.511
20.596
1.00
21.21
A


ATOM
914
CA
CYS
A
181
25.372
16.480
19.541
1.00
22.22
A


ATOM
915
CB
CYS
A
181
24.800
17.065
18.250
1.00
24.62
A


ATOM
916
SC
CYS
A
181
23.435
16.080
17.560
1.00
29.50
A


ATOM
917
C
CYS
A
181
26.633
17.232
19.954
1.00
23.07
A


ATOM
918
O
CYS
A
181
27.746
16.827
19.608
1.00
23.95
A


ATOM
919
N
THR
A
182
26.463
18.325
20.695
1.00
22.76
A


ATOM
920
CA
THR
A
182
27.606
19.103
21.161
1.00
21.49
A


ATOM
921
CB
THR
A
182
27.167
20.346
21.978
1.00
21.37
A


ATOM
922
OG1
THR
A
182
26.459
21.262
21.134
1.00
22.50
A


ATOM
923
CG2
THR
A
182
28.379
21.046
22.565
1.00
18.36
A


ATOM
924
C
THR
A
182
28.454
18.215
22.071
1.00
21.48
A


ATOM
925
O
THR
A
182
29.669
18.090
21.894
1.00
19.95
A


ATOM
926
N
ARC
A
183
27.798
17.602
23.050
1.00
18.97
A


ATOM
927
CA
ARC
A
183
28.468
16.723
23.996
1.00
19.39
A


ATOM
928
CB
ARC

183
27.455
16.140
24.984
0.50
19.46
AC1


ATOM
929
CC
ARC

183
28.030
15.062
25.887
0.50
18.77
AC1


ATOM
930
CD
ARC

183
27.021
14.571
26.925
0.50
21.19
AC1


ATOM
931
NE
ARC

183
26.605
15.642
27.824
0.50
19.46
AC1


ATOM
932
CZ
ARC

183
25.496
16.362
27.679
0.50
20.45
AC1


ATOM
933
NH1
ARC

183
24.672
16.123
26.666
0.50
19.81
AC1


ATOM
934
NH2
ARC

183
25.224
17.338
28.539
0.50
17.11
AC1


ATOM
935
C
ARC
A
183
29.206
15.577
23.302
1.00
20.02
A


ATOM
936
O
ARC
A
183
30.383
15.333
23.573
1.00
19.97
A


ATOM
937
N
PHE
A
184
28.520
14.871
22.409
1.00
19.24
A


ATOM
938
CA
PHE
A
184
29.144
13.746
21.722
1.00
18.04
A


ATOM
939
CB
PHE
A
184
28.158
13.078
20.764
1.00
21.05
A


ATOM
940
CC
PHE
A
184
28.719
11.857
20.098
1.00
22.67
A


ATOM
941
CD1
PHE
A
184
28.717
10.630
20.754
1.00
22.97
A


ATOM
942
CD2
PHE
A
184
29.317
11.949
18.850
1.00
19.97
A


ATOM
943
CE1
PHE
A
184
29.308
9.510
20.176
1.00
23.53
A


ATOM
944
CE2
PHE
A
184
29.915
10.833
18.263
1.00
24.11
A


ATOM
945
CZ
PHE
A
184
29.910
9.613
18.928
1.00
22.97
A


ATOM
946
C
PHE
A
184
30.403
14.127
20.941
1.00
17.99
A


ATOM
947
O
PHE
A
184
31.461
13.531
21.130
1.00
18.89
A


ATOM
948
N
TYR
A
185
30.292
15.110
20.056
1.00
15.73
A


ATOM
949
CA
TYR
A
185
31.443
15.519
19.265
1.00
15.72
A


ATOM
950
CB
TYR
A
185
30.992
16.413
18.111
1.00
17.33
A


ATOM
951
CC
TYR
A
185
30.364
15.584
17.015
1.00
19.37
A


ATOM
952
CD1
TYR
A
185
31.159
14.809
16.168
1.00
16.53
A


ATOM
953
CE1
TYR
A
185
30.590
13.952
15.232
1.00
18.12
A


ATOM
954
CD2
TYR
A
185
28.976
15.484
16.892
1.00
18.18
A


ATOM
955
CE2
TYR
A
185
28.398
14.623
15.956
1.00
18.90
A


ATOM
956
CZ
TYR
A
185
29.211
13.861
15.133
1.00
18.41
A


ATOM
957
OH
TYR
A
185
28.650
12.995
14.218
1.00
20.48
A


ATOM
958
C
TYR
A
185
32.544
16.172
20.083
1.00
15.79
A


ATOM
959
O
TYR
A
185
33.720
16.015
19.766
1.00
17.69
A


ATOM
960
N
THR
A
186
32.176
16.887
21.142
1.00
15.68
A


ATOM
961
CA
THR
A
186
33.184
17.504
21.997
1.00
16.03
A


ATOM
962
CB
THR
A
186
32.559
18.403
23.094
1.00
16.62
A


ATOM
963
OG1
THR
A
186
31.866
19.503
22.481
1.00
14.79
A


ATOM
964
CO2
THR
A
186
33.656
18.953
24.019
1.00
14.68
A


ATOM
965
C
THR
A
186
33.954
16.375
22.680
1.00
15.59
A


ATOM
966
O
THR
A
186
35.176
16.443
22.823
1.00
13.77
A


ATOM
967
N
ALA
A
187
33.234
15.333
23.097
1.00
14.06
A


ATOM
968
CA
ALA
A
187
33.869
14.196
23.757
1.00
14.74
A


ATOM
969
CB
ALA
A
187
32.810
13.195
24.224
1.00
14.32
A


ATOM
970
C
ALA
A
187
34.875
13.509
22.821
1.00
14.41
A


ATOM
971
O
ALA
A
187
35.972
13.136
23.247
1.00
15.61
A


ATOM
972
N
GLU
A
188
34.516
13.340
21.549
1.00
14.01
A


ATOM
973
CA
GLU
A
188
35.443
12.704
20.615
1.00
13.50
A


ATOM
974
CB
GLU
A
188
34.782
12.449
19.251
1.00
12.85
A


ATOM
975
CO
GLU
A
188
33.622
11.454
19.282
1.00
12.71
A


ATOM
976
CD
GLU
A
188
33.464
10.685
17.979
1.00
15.01
A


ATOM
977
OE1
GLU
A
188
33.687
11.275
16.899
1.00
13.21
A


ATOM
978
OE2
GLU
A
188
33.110
9.484
18.031
1.00
17.69
A


ATOM
979
C
GLU
A
188
36.682
13.582
20.436
1.00
13.34
A


ATOM
980
O
GLU
A
188
37.803
13.085
20.408
1.00
14.69
A


ATOM
981
N
ILE
A
189
36.486
14.893
20.326
1.00
13.52
A


ATOM
982
CA
ILE
A
189
37.627
15.787
20.159
1.00
13.35
A


ATOM
983
CB
ILE
A
189
37.169
17.247
19.939
1.00
13.95
A


ATOM
984
CO2
ILE
A
189
38.381
18.165
19.822
1.00
12.47
A


ATOM
985
CCI
ILE
A
189
36.302
17.332
18.671
1.00
13.44
A


ATOM
986
CD1
ILE
A
189
35.588
18.664
18.491
1.00
14.29
A


ATOM
987
C
ILE
A
189
38.530
15.702
21.394
1.00
14.63
A


ATOM
988
O
ILE
A
189
39.753
15.595
21.271
1.00
12.97
A


ATOM
989
N
VAL
A
190
37.927
15.751
22.582
1.00
14.35
A


ATOM
990
CA
VAL
A
190
38.684
15.655
23.832
1.00
13.22
A


ATOM
991
CB
VAL
A
190
37.743
15.690
25.061
1.00
14.28
A


ATOM
992
CCI
VAL
A
190
38.509
15.267
26.326
1.00
15.08
A


ATOM
993
C02
VAL
A
190
37.160
17.082
25.233
1.00
12.08
A


ATOM
994
C
VAL
A
190
39.468
14.338
23.859
1.00
14.61
A


ATOM
995
O
VAL
A
190
40.634
14.304
24.250
1.00
13.72
A


ATOM
996
N
SER
A
191
38.825
13.254
23.432
1.00
15.26
A


ATOM
997
CA
SER
A
191
39.478
11.943
23.421
1.00
16.81
A


ATOM
998
CB
SER

191
38.470
10.857
23.041
0.50
16.14
AC1


ATOM
999
OG
SER

191
39.018
9.569
23.238
0.50
16.94
AC1


ATOM
1000
C
SER
A
191
40.649
11.928
22.441
1.00
16.58
A


ATOM
1001
O
SER
A
191
41.697
11.335
22.713
1.00
13.96
A


ATOM
1002
N
ALA
A
192
40.468
12.586
21.300
1.00
15.26
A


ATOM
1003
CA
ALA
A
192
41.518
12.645
20.292
1.00
14.37
A


ATOM
1004
CB
ALA
A
192
40.989
13.296
19.016
1.00
14.43
A


ATOM
1005
C
ALA
A
192
42.695
13.440
20.845
1.00
16.46
A


ATOM
1006
O
ALA
A
192
43.851
13.038
20.697
1.00
17.96
A


ATOM
1007
N
LEU
A
193
42.401
14.563
21.496
1.00
15.02
A


ATOM
1008
CA
LEU
A
193
43.459
15.392
22.067
1.00
15.42
A


ATOM
1009
CB
LEU
A
193
42.884
16.712
22.600
1.00
12.88
A


ATOM
1010
CO
LEU
A
193
42.445
17.721
21.525
1.00
15.97
A


ATOM
1011
CD1
LEU
A
193
41.869
18.979
22.190
1.00
13.97
A


ATOM
1012
CD2
LEU
A
193
43.642
18.088
20.655
1.00
14.58
A


ATOM
1013
C
LEU
A
193
44.211
14.659
23.174
1.00
14.49
A


ATOM
1014
O
LEU
A
193
45.427
14.813
23.310
1.00
16.56
A


ATOM
1015
N
OLU
A
194
43.500
13.870
23.975
1.00
13.96
A


ATOM
1016
CA
GLU
A
194
44.179
13.123
25.032
1.00
14.08
A


ATOM
1017
CB
GLU
A
194
43.190
12.295
25.857
1.00
14.65
A


ATOM
1018
CC
GLU
A
194
43.882
11.301
26.789
1.00
17.09
A


ATOM
1019
CD
GLU
A
194
42.924
10.592
27.730
1.00
19.59
A


ATOM
1020
OE1
GLU
A
194
41.809
10.237
27.295
1.00
19.25
A


ATOM
1021
OE2
GLU
A
194
43.302
10.380
28.906
1.00
20.20
A


ATOM
1022
C
GLU
A
194
45.208
12.199
24.386
1.00
13.57
A


ATOM
1023
O
GLU
A
194
46.337
12.093
24.847
1.00
14.23
A


ATOM
1024
N
TYR
A
195
44.822
11.544
23.301
1.00
14.89
A


ATOM
1025
CA
TYR
A
195
45.743
10.642
22.618
1.00
16.58
A


ATOM
1026
CB
TYR
A
195
45.030
9.910
21.488
1.00
17.29
A


ATOM
1027
CC
TYR
A
195
45.956
9.058
20.649
1.00
17.92
A


ATOM
1028
CD1
TYR
A
195
46.347
7.788
21.077
1.00
17.96
A


ATOM
1029
CE1
TYR
A
195
47.203
6.996
20.304
1.00
19.77
A


ATOM
1030
CD2
TYR
A
195
46.445
9.524
19.428
1.00
16.67
A


ATOM
1031
CE2
TYR
A
195
47.299
8.744
18.650
1.00
18.51
A


ATOM
1032
CZ
TYR
A
195
47.671
7.481
19.094
1.00
20.24
A


ATOM
1033
OH
TYR
A
195
48.506
6.705
18.325
1.00
21.89
A


ATOM
1034
C
TYR
A
195
46.917
11.419
22.035
1.00
16.98
A


ATOM
1035
O
TYR
A
195
48.081
11.047
22.203
1.00
14.61
A


ATOM
1036
N
LEU
A
196
46.599
12.507
21.347
1.00
16.30
A


ATOM
1037
CA
LEU
A
196
47.619
13.328
20.720
1.00
18.15
A


ATOM
1038
CB
LEU
A
196
46.969
14.502
19.982
1.00
18.59
A


ATOM
1039
CC
LEU
A
196
47.834
15.203
18.935
1.00
22.51
A


ATOM
1040
CD1
LEU
A
196
48.222
14.206
17.841
1.00
20.94
A


ATOM
1041
CD2
LEU
A
196
47.060
16.375
18.338
1.00
22.98
A


ATOM
1042
C
LEU
A
196
48.592
13.844
21.763
1.00
17.75
A


ATOM
1043
O
LEU
A
196
49.801
13.644
21.649
1.00
18.33
A


ATOM
1044
N
HIS
A
197
48.064
14.495
22.792
1.00
17.12
A


ATOM
1045
CA
HIS
A
197
48.913
15.042
23.842
1.00
18.47
A


ATOM
1046
CB
HIS
A
197
48.069
15.866
24.817
1.00
15.90
A


ATOM
1047
CC
HIS
A
197
47.571
17.152
24.231
1.00
19.15
A


ATOM
1048
CD2
HIS
A
197
47.830
17.745
23.038
1.00
18.22
A


ATOM
1049
ND1
HIS
A
197
46.704
17.992
24.897
1.00
17.47
A


ATOM
1050
CE
HIS
A
197
46.450
19.047
24.139
1.00
19.74
A


ATOM
1051
NE2
HIS
A
197
47.119
18.921
23.007
1.00
15.69
A


ATOM
1052
C
HIS
A
197
49.696
13.958
24.572
1.00
19.40
A


ATOM
1053
O
HIS
A
197
50.823
14.192
25.021
1.00
19.42
A


ATOM
1054
N
GLY
A
198
49.106
12.770
24.679
1.00
18.59
A


ATOM
1055
CA
GLY
A
198
49.793
11.675
25.339
1.00
19.60
A


ATOM
1056
C
GLY
A
198
51.075
11.307
24.612
1.00
21.86
A


ATOM
1057
O
GLY
A
198
51.963
10.682
25.186
1.00
23.09
A


ATOM
1058
N
LYS
A
199
51.174
11.687
23.341
1.00
22.81
A


ATOM
1059
CA
LYS
A
199
52.368
11.401
22.549
1.00
24.43
A


ATOM
1060
CB
LYS
A
199
51.990
10.905
21.154
1.00
26.00
A


ATOM
1061
CC
LYS
A
199
51.378
9.520
21.133
1.00
30.98
A


ATOM
1062
CD
LYS
A
199
51.291
9.002
19.708
1.00
36.85
A


ATOM
1063
CE
LYS
A
199
50.832
7.559
19.682
1.00
40.37
A


ATOM
1064
NZ
LYS
A
199
51.646
6.691
20.581
1.00
43.48
A


ATOM
1065
C
LYS
A
199
53.253
12.631
22.414
1.00
23.88
A


ATOM
1066
O
LYS
A
199
54.144
12.669
21.568
1.00
24.97
A


ATOM
1067
N
GLY
A
200
52.997
13.638
23.243
1.00
24.00
A


ATOM
1068
CA
GLY
A
200
53.790
14.853
23.203
1.00
22.12
A


ATOM
1069
C
GLY
A
200
53.665
15.632
21.907
1.00
22.14
A


ATOM
1070
O
GLY
A
200
54.632
16.231
21.439
1.00
22.41
A


ATOM
1071
N
ILE
A
201
52.475
15.630
21.320
1.00
20.00
A


ATOM
1072
CA
ILE
A
201
52.252
16.355
20.080
1.00
18.93
A


ATOM
1073
CB
ILE
A
201
51.784
15.414
18.955
1.00
19.70
A


ATOM
1074
CC2
ILE
A
201
51.414
16.226
17.716
1.00
20.12
A


ATOM
1075
CC1
ILE
A
201
52.880
14.395
18.636
1.00
20.03
A


ATOM
1076
CD1
ILE
A
201
52.408
13.258
17.745
1.00
22.75
A


ATOM
1077
C
ILE
A
201
51.193
17.425
20.270
1.00
19.87
A


ATOM
1078
O
ILE
A
201
50.121
17.161
20.817
1.00
20.08
A


ATOM
1079
N
ILE
A
202
51.508
18.633
19.815
1.00
19.94
A


ATOM
1080
CA
ILE
A
202
50.601
19.772
19.891
1.00
20.45
A


ATOM
1081
CB
ILE
A
202
51.352
21.040
20.356
1.00
22.21
A


ATOM
1082
CC2
ILE
A
202
50.381
22.220
20.470
1.00
22.67
A


ATOM
1083
CC1
ILE
A
202
52.033
20.775
21.700
1.00
24.19
A


ATOM
1084
CD1
ILE
A
202
52.914
21.920
22.169
1.00
25.39
A


ATOM
1085
C
ILE
A
202
50.105
19.999
18.464
1.00
20.71
A


ATOM
1086
O
ILE
A
202
50.910
20.067
17.538
1.00
19.48
A


ATOM
1087
N
HIS
A
203
48.795
20.108
18.270
1.00
18.65
A


ATOM
1088
CA
HIS
A
203
48.280
20.319
16.919
1.00
18.02
A


ATOM
1089
CB
HIS
A
203
46.775
20.057
16.874
1.00
16.31
A


ATOM
1090
CC
HIS
A
203
46.199
20.136
15.495
1.00
18.36
A


ATOM
1091
CD2
HIS
A
203
46.043
21.186
14.655
1.00
16.42
A


ATOM
1092
ND1
HIS
A
203
45.759
19.026
14.806
1.00
19.50
A


ATOM
1093
CE1
HIS
A
203
45.359
19.389
13.600
1.00
17.64
A


ATOM
1094
NE2
HIS
A
203
45.522
20.694
13.483
1.00
20.87
A


ATOM
1095
C
HIS
A
203
48.589
21.738
16.405
1.00
18.92
A


ATOM
1096
O
HIS
A
203
49.073
21.906
15.282
1.00
16.21
A


ATOM
1097
N
ARC
A
204
48.301
22.744
17.232
1.00
18.60
A


ATOM
1098
CA
ARC
A
204
48.552
24.157
16.914
1.00
19.81
A


ATOM
1099
CB
ARC
A
204
49.998
24.365
16.458
1.00
21.61
A


ATOM
1100
CC
ARC
A
204
51.024
24.137
17.550
1.00
23.82
A


ATOM
1101
CD
ARC
A
204
52.323
24.870
17.252
1.00
27.62
A


ATOM
1102
NE
ARC
A
204
52.932
24.449
15.994
1.00
29.43
A


ATOM
1103
CZ
ARC
A
204
54.125
24.861
15.572
1.00
33.10
A


ATOM
1104
NH1
ARC
A
204
54.835
25.706
16.311
1.00
32.12
A


ATOM
1105
NH2
ARC
A
204
54.614
24.426
14.418
1.00
30.25
A


ATOM
1106
C
ARC
A
204
47.624
24.830
15.905
1.00
20.03
A


ATOM
1107
O
ARC
A
204
47.711
26.038
15.698
1.00
20.88
A


ATOM
1108
N
ASP
A
205
46.755
24.071
15.255
1.00
18.96
A


ATOM
1109
CA
ASP
A
205
45.828
24.692
14.325
1.00
17.90
A


ATOM
1110
CB
ASP
A
205
46.418
24.741
12.914
1.00
18.95
A


ATOM
1111
CC
ASP
A
205
45.655
25.688
12.008
1.00
20.36
A


ATOM
1112
OD1
ASP
A
205
44.939
26.560
12.545
1.00
20.35
A


ATOM
1113
OD2
ASP
A
205
45.772
25.573
10.771
1.00
22.49
A


ATOM
1114
C
ASP
A
205
44.500
23.956
14.328
1.00
19.60
A


ATOM
1115
O
ASP
A
205
43.876
23.751
13.287
1.00
21.53
A


ATOM
1116
N
LEU
A
206
44.063
23.569
15.521
1.00
18.53
A


ATOM
1117
CA
LEU
A
206
42.813
22.851
15.667
1.00
19.18
A


ATOM
1118
CB
LEU
A
206
42.693
22.295
17.087
1.00
18.94
A


ATOM
1119
CC
LEU
A
206
41.511
21.358
17.346
1.00
23.10
A


ATOM
1120
CD1
LEU
A
206
41.615
20.142
16.436
1.00
23.01
A


ATOM
1121
CD2
LEU
A
206
41.504
20.933
18.808
1.00
22.97
A


ATOM
1122
C
LEU
A
206
41.639
23.772
15.361
1.00
19.05
A


ATOM
1123
O
LEU
A
206
41.556
24.880
15.886
1.00
19.25
A


ATOM
1124
N
LYS
A
207
40.740
23.307
14.500
1.00
17.54
A


ATOM
1125
CA
LYS
A
207
39.564
24.081
14.110
1.00
18.60
A


ATOM
1126
CB
LYS
A
207
39.980
25.248
13.196
1.00
18.98
A


ATOM
1127
CC
LYS
A
207
40.786
24.817
11.982
1.00
18.20
A


ATOM
1128
CD
LYS
A
207
41.246
26.000
11.139
1.00
21.42
A


ATOM
1129
CE
LYS
A
207
42.223
25.537
10.062
1.00
23.21
A


ATOM
1130
NZ
LYS
A
207
42.561
26.604
9.084
1.00
29.61
A


ATOM
1131
C
LYS
A
207
38.566
23.181
13.388
1.00
18.18
A


ATOM
1132
O
LYS
A
207
38.921
22.100
12.915
1.00
18.11
A


ATOM
1133
N
PRO
A
208
37.298
23.614
13.293
1.00
20.26
A


ATOM
1134
CD
PRO
A
208
36.713
24.833
13.882
1.00
18.79
A


ATOM
1135
CA
PRO
A
208
36.272
22.814
12.616
1.00
19.67
A


ATOM
1136
CB
PRO
A
208
35.063
23.742
12.608
1.00
19.45
A


ATOM
1137
CG
PRO
A
208
35.231
24.509
13.891
1.00
21.81
A


ATOM
1138
C
PRO
A
208
36.674
22.372
11.209
1.00
21.04
A


ATOM
1139
O
PRO
A
208
36.264
21.307
10.751
1.00
21.19
A


ATOM
1140
N
GLU
A
209
37.474
23.188
10.528
1.00
21.69
A


ATOM
1141
CA
GLU
A
209
37.928
22.872
9.170
1.00
22.64
A


ATOM
1142
CB
GLU

209
38.644
24.084
8.558
0.50
23.65
AC1


ATOM
1143
CG
GLU

209
39.253
23.825
7.185
0.50
27.24
AC1


ATOM
1144
CD
GLU

209
40.155
24.958
6.716
0.50
29.40
AC1


ATOM
1145
OE1
GLU

209
39.660
26.094
6.553
0.50
29.68
AC1


ATOM
1146
OE2
GLU

209
41.363
24.711
6.511
0.50
30.07
AC1


ATOM
1147
C
GLU
A
209
38.879
21.668
9.159
1.00
22.28
A


ATOM
1148
O
GLU
A
209
38.955
20.933
8.170
1.00
21.36
A


ATOM
1149
N
ASN
A
210
39.600
21.490
10.263
1.00
19.90
A


ATOM
1150
CA
ASN
A
210
40.574
20.412
10.436
1.00
19.44
A


ATOM
1151
CB
ASN
A
210
41.744
20.912
11.287
1.00
20.07
A


ATOM
1152
CG
ASN
A
210
42.746
21.698
10.479
1.00
25.77
A


ATOM
1153
OD1
ASN
A
210
43.571
22.427
11.029
1.00
26.73
A


ATOM
1154
ND2
ASN
A
210
42.687
21.548
9.158
1.00
25.15
A


ATOM
1155
C
ASN
A
210
40.005
19.151
11.078
1.00
18.63
A


ATOM
1156
O
ASN
A
210
40.712
18.154
11.234
1.00
18.29
A


ATOM
1157
N
ILE
A
211
38.739
19.202
11.469
1.00
16.31
A


ATOM
1158
CA
ILE
A
211
38.090
18.058
12.085
1.00
15.49
A


ATOM
1159
CB
ILE
A
211
37.336
18.488
13.354
1.00
15.40
A


ATOM
1160
CG2
ILE
A
211
36.582
17.311
13.950
1.00
14.59
A


ATOM
1161
CG1
ILE
A
211
38.342
19.046
14.365
1.00
15.91
A


ATOM
1162
CD1
ILE
A
211
37.720
19.669
15.590
1.00
15.98
A


ATOM
1163
C
ILE
A
211
37.131
17.485
11.059
1.00
17.26
A


ATOM
1164
O
ILE
A
211
35.995
17.947
10.926
1.00
18.16
A


ATOM
1165
N
LEU

212
37.599
16.486
10.317
1.00
15.97
A


ATOM
1166
CA
LEU
A
212
36.784
15.875
9.274
1.00
17.08
A


ATOM
1167
CB
LEU
A
212
37.685
15.249
8.202
1.00
17.78
A


ATOM
1168
CG
LEU
A
212
38.785
16.157
7.640
1.00
18.92
A


ATOM
1169
CD1
LEU
A
212
39.476
15.450
6.485
1.00
22.09
A


ATOM
1170
CD2
LEU
A
212
38.188
17.482
7.166
1.00
19.91
A


ATOM
1171
C
LEU
A
212
35.843
14.825
9.837
1.00
18.35
A


ATOM
1172
O
LEU
A
212
35.957
14.433
11.002
1.00
19.39
A


ATOM
1173
N
LEU
A
213
34.915
14.368
9.000
1.00
17.84
A


ATOM
1174
CA
LEU
A
213
33.942
13.362
9.403
1.00
19.94
A


ATOM
1175
CB
LEU
A
213
32.556
14.004
9.487
1.00
20.84
A


ATOM
1176
CG
LEU
A
213
32.396
15.059
10.583
1.00
20.31
A


ATOM
1177
CD1
LEU
A
213
31.124
15.837
10.367
1.00
22.75
A


ATOM
1178
CD2
LEU
A
213
32.379
14.378
11.940
1.00
23.93
A


ATOM
1179
C
LEU
A
213
33.914
12.187
8.426
1.00
20.98
A


ATOM
1180
O
LEU
A
213
33.743
12.379
7.218
1.00
19.55
A


ATOM
1181
N
ASN
A
214
34.088
10.970
8.935
1.00
20.44
A


ATOM
1182
CA
ASN
A
214
34.055
9.814
8.049
1.00
23.77
A


ATOM
1183
CB
ASN
A
214
34.745
8.596
8.674
1.00
25.30
A


ATOM
1184
CG
ASN
A
214
34.077
8.127
9.948
1.00
32.04
A


ATOM
1185
OD1
ASN
A
214
32.908
8.422
10.206
1.00
34.43
A


ATOM
1186
ND2
ASN
A
214
34.818
7.369
10.752
1.00
33.85
A


ATOM
1187
C
ASN
A
214
32.618
9.466
7.693
1.00
24.07
A


ATOM
1188
O
ASN
A
214
31.672
10.113
8.150
1.00
19.94
A


ATOM
1189
N
GLU
A
215
32.459
8.433
6.879
1.00
25.77
A


ATOM
1190
CA
GLU
A
215
31.138
8.003
6.445
1.00
28.69
A


ATOM
1191
CB
GLU
A
215
31.275
6.796
5.513
1.00
31.98
A


ATOM
1192
CG
GLU
A
215
29.970
6.334
4.896
1.00
40.22
A


ATOM
1193
CD
GLU
A
215
30.182
5.312
3.795
1.00
44.27
A


ATOM
1194
OE1
GLU
A
215
30.817
4.268
4.065
1.00
46.46
A


ATOM
1195
OE2
GLU
A
215
29.716
5.556
2.660
1.00
46.13
A


ATOM
1196
C
GLU
A
215
30.188
7.673
7.601
1.00
28.41
A


ATOM
1197
O
GLU
A
215
28.971
7.769
7.447
1.00
28.52
A


ATOM
1198
N
ASP
A
216
30.737
7.287
8.752
1.00
26.77
A


ATOM
1199
CA
ASP
A
216
29.914
6.953
9.917
1.00
27.28
A


ATOM
1200
CB
ASP
A
216
30.538
5.795
10.696
1.00
31.27
A


ATOM
1201
CC
ASP
A
216
30.390
4.466
9.979
1.00
37.61
A


ATOM
1202
OD1
ASP
A
216
29.274
4.170
9.499
1.00
39.45
A


ATOM
1203
OD2
ASP
A
216
31.382
3.710
9.902
1.00
41.84
A


ATOM
1204
C
ASP
A
216
29.697
8.135
10.862
1.00
26.37
A


ATOM
1205
O
ASP
A
216
29.136
7.984
11.950
1.00
25.73
A


ATOM
1206
N
MET
A
217
30.156
9.306
10.441
1.00
23.02
A


ATOM
1207
CA
MET
A
217
30.015
10.527
11.218
1.00
21.83
A


ATOM
1208
CB
MET
A
217
28.537
10.789
11.517
1.00
23.24
A


ATOM
1209
CC
MET
A
217
27.742
11.186
10.274
1.00
22.98
A


ATOM
1210
SD
MET
A
217
28.464
12.616
9.430
1.00
27.57
A


ATOM
1211
CE
MET
A
217
27.679
13.974
10.332
1.00
26.68
A


ATOM
1212
C
MET
A
217
30.844
10.618
12.502
1.00
21.51
A


ATOM
1213
O
MET
A
217
30.474
11.323
13.440
1.00
18.62
A


ATOM
1214
N
HIS
A
218
31.957
9.892
12.544
1.00
20.10
A


ATOM
1215
CA
HIS
A
218
32.873
9.964
13.678
1.00
19.86
A


ATOM
1216
CB
HIS
A
218
33.482
8.594
13.977
1.00
20.21
A


ATOM
1217
CC
HIS
A
218
32.551
7.667
14.698
1.00
22.40
A


ATOM
1218
CD2
HIS
A
218
31.910
6.547
14.287
1.00
21.27
A


ATOM
1219
ND1
HIS
A
218
32.177
7.863
16.011
1.00
19.59
A


ATOM
1220
CE1
HIS
A
218
31.348
6.902
16.379
1.00
21.88
A


ATOM
1221
NE2
HIS
A
218
31.168
6.091
15.351
1.00
22.08
A


ATOM
1222
C
HIS
A
218
33.947
10.921
13.172
1.00
19.10
A


ATOM
1223
O
HIS
A
218
34.170
11.004
11.965
1.00
20.31
A


ATOM
1224
N
ILE
A
219
34.617
11.638
14.067
1.00
17.21
A


ATOM
1225
CA
ILE
A
219
35.628
12.586
13.618
1.00
15.26
A


ATOM
1226
CB
ILE
A
219
35.987
13.614
14.716
1.00
15.38
A


ATOM
1227
CC2
ILE
A
219
34.722
14.305
15.221
1.00
14.58
A


ATOM
1228
CC1
ILE
A
219
36.734
12.919
15.864
1.00
14.46
A


ATOM
1229
CD1
ILE
A
219
37.279
13.885
16.911
1.00
13.74
A


ATOM
1230
C
ILE
A
219
36.929
11.944
13.161
1.00
16.21
A


ATOM
1231
O
ILE
A
219
37.238
10.799
13.500
1.00
15.88
A


ATOM
1232
N
GIN
A
220
37.677
12.711
12.378
1.00
15.62
A


ATOM
1233
CA
GIN
A
220
38.980
12.316
11.876
1.00
17.84
A


ATOM
1234
CB
GIN
A
220
38.872
11.595
10.525
1.00
20.00
A


ATOM
1235
CC
CLN
A
220
38.463
10.129
10.659
1.00
26.97
A


ATOM
1236
CD
CLN
A
220
38.648
9.343
9.372
1.00
29.95
A


ATOM
1237
OE1
CLN
A
220
37.968
9.590
8.373
1.00
33.12
A


ATOM
1238
NE2
CLN
A
220
39.578
8.393
9.389
1.00
30.47
A


ATOM
1239
C
CLN
A
220
39.757
13.610
11.735
1.00
17.00
A


ATOM
1240
O
CLN
A
220
39.609
14.339
10.751
1.00
18.27
A


ATOM
1241
N
ILE
A
221
40.566
13.906
12.746
1.00
14.34
A


ATOM
1242
CA
ILE
A
221
41.361
15.120
12.753
1.00
14.46
A


ATOM
1243
CB
ILE
A
221
41.867
15.416
14.175
1.00
12.30
A


ATOM
1244
CC2
ILE
A
221
42.764
16.656
14.167
1.00
14.78
A


ATOM
1245
Cd
ILE
A
221
40.660
15.613
15.102
1.00
13.92
A


ATOM
1246
CD1
ILE
A
221
41.003
15.901
16.543
1.00
15.06
A


ATOM
1247
C
ILE
A
221
42.536
14.996
11.783
1.00
15.44
A


ATOM
1248
O
ILE
A
221
43.106
13.915
11.613
1.00
13.93
A


ATOM
1249
N
THR
A
222
42.877
16.101
11.127
1.00
15.36
A


ATOM
1250
CA
THR
A
222
43.980
16.098
10.174
1.00
17.52
A


ATOM
1251
CB
THR
A
222
43.470
15.836
8.750
1.00
19.92
A


ATOM
1252
OG1
THR
A
222
44.587
15.637
7.875
1.00
18.78
A


ATOM
1253
CG2
THR
A
222
42.630
17.018
8.257
1.00
18.16
A


ATOM
1254
C
THR
A
222
44.735
17.428
10.192
1.00
19.60
A


ATOM
1255
O
THR
A
222
44.509
18.257
11.084
1.00
18.59
A


ATOM
1256
N
ASP
A
223
45.630
17.610
9.216
1.00
18.69
A


ATOM
1257
CA
ASP
A
223
46.440
18.825
9.069
1.00
20.12
A


ATOM
1258
CB
ASP
A
223
45.532
20.065
9.108
1.00
23.51
A


ATOM
1259
CG
ASP
A
223
46.248
21.335
8.670
1.00
27.09
A


ATOM
1260
OD1
ASP
A
223
47.283
21.227
7.975
1.00
26.28
A


ATOM
1261
OD2
ASP
A
223
45.765
22.438
9.009
1.00
26.15
A


ATOM
1262
C
ASP
A
223
47.516
18.913
10.150
1.00
21.73
A


ATOM
1263
O
ASP
A
223
47.439
19.751
11.055
1.00
22.76
A


ATOM
1264
N
PHE
A
224
48.535
18.063
10.027
1.00
20.75
A


ATOM
1265
CA
PHE
A
224
49.611
17.988
11.009
1.00
20.11
A


ATOM
1266
CB
PHE
A
224
49.805
16.527
11.424
1.00
20.62
A


ATOM
1267
CG
PHE
A
224
48.682
15.991
12.263
1.00
21.41
A


ATOM
1268
CD1
PHE
A
224
48.598
16.312
13.614
1.00
23.05
A


ATOM
1269
CD2
PHE
A
224
47.681
15.212
11.693
1.00
22.27
A


ATOM
1270
CE1
PHE
A
224
47.528
15.868
14.389
1.00
23.30
A


ATOM
1271
CE2
PHE
A
224
46.606
14.763
12.457
1.00
21.11
A


ATOM
1272
CZ
PHE
A
224
46.530
15.093
13.807
1.00
22.02
A


ATOM
1273
C
PHE
A
224
50.957
18.583
10.619
1.00
20.45
A


ATOM
1274
O
PHE
A
224
51.905
18.547
11.407
1.00
20.73
A


ATOM
1275
N
GLY
A
225
51.049
19.125
9.412
1.00
22.02
A


ATOM
1276
CA
GLY
A
225
52.301
19.713
8.981
1.00
22.66
A


ATOM
1277
C
GLY
A
225
52.742
20.822
9.920
1.00
24.99
A


ATOM
1278
O
GLY
A
225
53.939
21.041
10.122
1.00
24.52
A


ATOM
1279
N
THR
A
226
51.779
21.524
10.508
1.00
23.50
A


ATOM
1280
CA
THR
A
226
52.106
22.613
11.416
1.00
25.16
A


ATOM
1281
CB
THR
A
226
51.199
23.829
11.160
1.00
24.76
A


ATOM
1282
OG1
THR
A
226
49.831
23.410
11.113
1.00
22.68
A


ATOM
1283
CG2
THR
A
226
51.571
24.490
9.834
1.00
25.00
A


ATOM
1284
C
THR
A
226
52.046
22.233
12.894
1.00
25.79
A


ATOM
1285
O
THR
A
226
52.019
23.100
13.768
1.00
24.54
A


ATOM
1286
N
ALA
A
227
52.037
20.935
13.173
1.00
24.97
A


ATOM
1287
CA
ALA
A
227
52.004
20.475
14.550
1.00
25.49
A


ATOM
1288
CB
ALA
A
227
51.659
18.993
14.607
1.00
22.85
A


ATOM
1289
C
ALA
A
227
53.384
20.715
15.149
1.00
27.70
A


ATOM
1290
O
ALA
A
227
54.331
21.047
14.435
1.00
26.60
A


ATOM
1291
N
LYS
A
228
53.491
20.558
16.461
1.00
28.53
A


ATOM
1292
CA
LYS
A
228
54.760
20.745
17.149
1.00
32.12
A


ATOM
1293
CB
LYS
A
228
54.699
21.974
18.054
1.00
33.81
A


ATOM
1294
CG
LYS
A
228
56.007
22.294
18.765
1.00
41.23
A


ATOM
1295
CD
LYS
A
228
57.082
22.725
17.768
1.00
47.57
A


ATOM
1296
CE
LYS
A
228
58.401
23.056
18.462
1.00
49.82
A


ATOM
1297
NZ
LYS
A
228
59.459
23.425
17.480
1.00
51.49
A


ATOM
1298
C
LYS
A
228
55.019
19.504
17.985
1.00
33.25
A


ATOM
1299
O
LYS
A
228
54.190
19.129
18.815
1.00
33.70
A


ATOM
1300
N
VAL
A
229
56.159
18.860
17.756
1.00
33.64
A


ATOM
1301
CA
VAL
A
229
56.516
17.661
18.501
1.00
34.66
A


ATOM
1302
CB
VAL
A
229
57.248
16.646
17.609
1.00
33.50
A


ATOM
1303
CG1
VAL
A
229
57.619
15.419
18.415
1.00
32.34
A


ATOM
1304
CG2
VAL
A
229
56.370
16.264
16.436
1.00
34.25
A


ATOM
1305
C
VAL
A
229
57.420
18.035
19.668
1.00
37.57
A


ATOM
1306
O
VAL
A
229
58.581
18.392
19.474
1.00
35.91
A


ATOM
1307
N
LEU
A
230
56.877
17.948
20.878
1.00
40.57
A


ATOM
1308
CA
LEU
A
230
57.615
18.289
22.088
1.00
46.10
A


ATOM
1309
CB
LEU
A
230
56.654
18.417
23.270
1.00
44.71
A


ATOM
1310
CG
LEU
A
230
55.627
19.545
23.207
1.00
44.50
A


ATOM
1311
CD1
LEU
A
230
54.673
19.430
24.383
1.00
44.39
A


ATOM
1312
CD2
LEU
A
230
56.340
20.885
23.214
1.00
44.81
A


ATOM
1313
C
LEU
A
230
58.695
17.279
22.440
1.00
50.42
A


ATOM
1314
O
LEU
A
230
58.603
16.104
22.089
1.00
51.64
A


ATOM
1315
N
SER
A
231
59.717
17.756
23.145
1.00
55.81
A


ATOM
1316
CA
SER
A
231
60.824
16.914
23.583
1.00
61.14
A


ATOM
1317
CB
SER
A
231
62.077
17.200
22.750
1.00
61.27
A


ATOM
1318
OG
SER
A
231
62.444
18.568
22.823
1.00
62.85
A


ATOM
1319
C
SER
A
231
61.124
17.126
25.071
1.00
64.65
A


ATOM
1320
O
SER
A
231
61.392
16.164
25.794
1.00
65.70
A


ATOM
1321
N
PRO
A
232
61.081
18.387
25.549
1.00
67.54
A


ATOM
1322
CD
PRO
A
232
60.854
19.651
24.823
1.00
68.60
A


ATOM
1323
CA
PRO
A
232
61.358
18.655
26.966
1.00
68.74
A


ATOM
1324
CB
PRO
A
232
61.109
20.158
27.086
1.00
68.83
A


ATOM
1325
CG
PRO
A
232
61.505
20.666
25.737
1.00
68.96
A


ATOM
1326
C
PRO
A
232
60.460
17.846
27.899
1.00
69.17
A


ATOM
1327
O
PRO
A
232
59.335
17.494
27.541
1.00
69.94
A


ATOM
1328
N
ALA
A
237
57.424
23.198
27.637
1.00
80.06
A


ATOM
1329
CA
ALA
A
237
56.783
23.047
26.335
1.00
79.29
A


ATOM
1330
CB
ALA
A
237
55.275
22.907
26.512
1.00
78.64
A


ATOM
1331
C
ALA
A
237
57.092
24.239
25.433
1.00
79.07
A


ATOM
1332
O
ALA
A
237
56.250
25.113
25.249
1.00
79.47
A


ATOM
1333
N
ALA
A
238
58.297
24.280
24.871
1.00
78.57
A


ATOM
1334
CA
ALA
A
238
58.683
25.383
23.992
1.00
78.50
A


ATOM
1335
CB
ALA
A
238
60.186
25.347
23.728
1.00
78.50
A


ATOM
1336
C
ALA
A
238
57.920
25.327
22.673
1.00
78.15
A


ATOM
1337
O
ALA
A
238
57.243
24.341
22.375
1.00
77.96
A


ATOM
1338
N
ALA
A
239
58.027
26.393
21.887
1.00
77.28
A


ATOM
1339
CA
ALA
A
239
57.338
26.452
20.603
1.00
76.27
A


ATOM
1340
CB
ALA
A
239
55.849
26.489
20.827
1.00
76.61
A


ATOM
1341
C
ALA
A
239
57.766
27.667
19.793
1.00
75.38
A


ATOM
1342
O
ALA
A
239
58.955
27.955
19.700
1.00
75.89
A


ATOM
1343
N
ASN
A
240
56.781
28.357
19.214
1.00
73.95
A


ATOM
1344
CA
ASN
A
240
56.967
29.553
18.389
1.00
71.07
A


ATOM
1345
CB
ASN
A
240
58.151
30.400
18.874
1.00
71.47
A


ATOM
1346
CG
ASN
A
240
59.459
30.055
18.174
1.00
72.06
A


ATOM
1347
OD1
ASN
A
240
59.575
30.149
16.943
1.00
72.03
A


ATOM
1348
ND2
ASN
A
240
60.470
29.665
18.964
1.00
71.91
A


ATOM
1349
C
ASN
A
240
57.188
29.178
16.928
1.00
69.41
A


ATOM
1350
O
ASN
A
240
57.480
28.024
16.624
1.00
70.09
A


ATOM
1351
N
ALA
A
241
57.055
30.165
16.038
1.00
66.62
A


ATOM
1352
CA
ALA
A
241
57.246
30.013
14.585
1.00
63.94
A


ATOM
1353
C
ALA
A
241
55.952
30.080
13.772
1.00
60.63
A


ATOM
1354
O
ALA
A
241
55.840
30.880
12.845
1.00
61.29
A


ATOM
1355
CB
ALA
A
241
57.979
28.704
14.246
1.00
65.23
A


ATOM
1356
N
PHE
A
242
54.984
29.236
14.113
1.00
56.72
A


ATOM
1357
CA
PHE
A
242
53.712
29.196
13.394
1.00
52.53
A


ATOM
1358
CB
PHE
A
242
53.419
27.767
12.923
1.00
49.14
A


ATOM
1359
CG
PHE
A
242
52.040
27.590
12.354
1.00
47.38
A


ATOM
1360
CD1
PHE
A
242
51.731
28.067
11.085
1.00
47.69
A


ATOM
1361
CD2
PHE
A
242
51.038
26.975
13.102
1.00
45.45
A


ATOM
1362
CE1
PHE
A
242
50.445
27.937
10.565
1.00
46.75
A


ATOM
1363
CE2
PHE
A
242
49.751
26.840
12.594
1.00
45.41
A


ATOM
1364
CZ
PHE
A
242
49.453
27.323
11.322
1.00
46.55
A


ATOM
1365
C
PHE
A
242
52.534
29.688
14.229
1.00
50.08
A


ATOM
1366
O
PHE
A
242
52.502
29.505
15.444
1.00
49.86
A


ATOM
1367
N
VAL
A
243
51.566
30.305
13.557
1.00
47.67
A


ATOM
1368
CA
VAL
A
243
50.355
30.809
14.200
1.00
46.21
A


ATOM
1369
CB
VAL
A
243
50.340
32.352
14.258
1.00
47.36
A


ATOM
1370
CG1
VAL
A
243
49.012
32.844
14.825
1.00
47.54
A


ATOM
1371
CG2
VAL
A
243
51.497
32.842
15.109
1.00
48.50
A


ATOM
1372
C
VAL
A
243
49.150
30.342
13.389
1.00
44.12
A


ATOM
1373
O
VAL
A
243
48.956
30.765
12.247
1.00
44.46
A


ATOM
1374
N
GLY
A
244
48.348
29.467
13.985
1.00
40.48
A


ATOM
1375
CA
GLY
A
244
47.176
28.941
13.306
1.00
37.65
A


ATOM
1376
C
GLY
A
244
46.101
29.960
12.964
1.00
35.39
A


ATOM
1377
O
GLY
A
244
46.313
31.168
13.065
1.00
35.92
A


ATOM
1378
N
THR
A
245
44.936
29.463
12.560
1.00
33.30
A


ATOM
1379
CA
THR
A
245
43.813
30.312
12.184
1.00
30.20
A


ATOM
1380
CB
THR
A
245
42.593
29.450
11.829
1.00
32.00
A


ATOM
1381
OG1
THR
A
245
42.952
28.573
10.755
1.00
32.81
A


ATOM
1382
CG2
THR
A
245
41.419
30.319
11.390
1.00
28.34
A


ATOM
1383
C
THR
A
245
43.476
31.296
13.296
1.00
27.96
A


ATOM
1384
O
THR
A
245
43.212
30.907
14.434
1.00
25.46
A


ATOM
1385
N
ALA
A
246
43.486
32.576
12.938
1.00
25.22
A


ATOM
1386
CA
ALA
A
246
43.247
33.675
13.867
1.00
23.27
A


ATOM
1387
CB
ALA
A
246
42.956
34.955
13.082
1.00
22.94
A


ATOM
1388
C
ALA
A
246
42.178
33.475
14.934
1.00
21.27
A


ATOM
1389
O
ALA
A
246
42.431
33.705
16.114
1.00
20.93
A


ATOM
1390
N
GLN
A
247
40.988
33.047
14.536
1.00
19.67
A


ATOM
1391
CA
GLN
A
247
39.911
32.886
15.504
1.00
20.17
A


ATOM
1392
CB
GLN

247
38.608
32.535
14.779
0.50
21.89
AC1


ATOM
1393
CG
GLN

247
38.522
33.076
13.355
0.50
26.18
AC1


ATOM
1394
CD
GLN

247
37.220
33.794
13.064
0.50
27.30
AC1


ATOM
1395
OE1
GLN

247
36.172
33.447
13.605
0.50
30.13
AC1


ATOM
1396
NE2
GLN

247
37.278
34.792
12.189
0.50
28.70
AC1


ATOM
1397
C
GLN
A
247
40.181
31.849
16.595
1.00
19.43
A


ATOM
1398
O
GLN
A
247
39.546
31.883
17.648
1.00
18.93
A


ATOM
1399
N
TYR
A
248
41.132
30.948
16.359
1.00
18.60
A


ATOM
1400
CA
TYR
A
248
41.441
29.896
17.329
1.00
19.20
A


ATOM
1401
CB
TYR
A
248
41.333
28.529
16.642
1.00
17.53
A


ATOM
1402
CG
TYR
A
248
40.013
28.362
15.927
1.00
19.32
A


ATOM
1403
CD1
TYR
A
248
38.859
28.010
16.625
1.00
17.69
A


ATOM
1404
CEl
TYR
A
248
37.617
27.976
15.990
1.00
18.18
A


ATOM
1405
CD2
TYR
A
248
39.897
28.664
14.569
1.00
16.87
A


ATOM
1406
CE2
TYR
A
248
38.665
28.635
13.924
1.00
19.17
A


ATOM
1407
CZ
TYR
A
248
37.527
28.295
14.643
1.00
19.46
A


ATOM
1408
OH
TYR
A
248
36.299
28.311
14.023
1.00
18.98
A


ATOM
1409
C
TYR
A
248
42.810
30.039
17.993
1.00
20.42
A


ATOM
1410
O
TYR
A
248
43.208
29.191
18.792
1.00
19.19
A


ATOM
1411
N
VAL
A
249
43.523
31.114
17.673
1.00
20.20
A


ATOM
1412
CA
VAL
A
249
44.841
31.343
18.251
1.00
20.91
A


ATOM
1413
CB
VAL
A
249
45.542
32.532
17.570
1.00
21.18
A


ATOM
1414
CG1
VAL
A
249
46.821
32.896
18.317
1.00
22.45
A


ATOM
1415
CG2
VAL
A
249
45.862
32.170
16.139
1.00
24.01
A


ATOM
1416
C
VAL
A
249
44.764
31.606
19.750
1.00
21.52
A


ATOM
1417
O
VAL
A
249
43.915
32.368
20.216
1.00
22.72
A


ATOM
1418
N
SER
A
250
45.654
30.965
20.503
1.00
20.70
A


ATOM
1419
CA
SER
A
250
45.697
31.133
21.951
1.00
21.65
A


ATOM
1420
CB
SER
A
250
46.370
29.919
22.613
1.00
22.02
A


ATOM
1421
OG
SER
A
250
47.692
29.725
22.132
1.00
22.12
A


ATOM
1422
C
SER
A
250
46.476
32.402
22.280
1.00
22.13
A


ATOM
1423
O
SER
A
250
47.332
32.828
21.511
1.00
22.77
A


ATOM
1424
N
PRO
A
251
46.180
33.029
23.425
1.00
22.23
A


ATOM
1425
CD
PRO
A
251
45.163
32.684
24.433
1.00
22.97
A


ATOM
1426
CA
PRO
A
251
46.893
34.254
23.800
1.00
22.52
A


ATOM
1427
CB
PRO
A
251
46.233
34.650
25.127
1.00
23.06
A


ATOM
1428
CG
PRO
A
251
45.726
33.329
25.676
1.00
22.55
A


ATOM
1429
C
PRO
A
251
48.414
34.115
23.907
1.00
22.15
A


ATOM
1430
O
PRO
A
251
49.143
35.047
23.563
1.00
22.62
A


ATOM
1431
N
GLU
A
252
48.901
32.966
24.367
1.00
20.69
A


ATOM
1432
CA
GLU
A
252
50.347
32.772
24.500
1.00
21.40
A


ATOM
1433
CB
GLU
A
252
50.673
31.382
25.071
1.00
20.59
A


ATOM
1434
CC
GLU
A
252
49.993
30.232
24.352
1.00
21.91
A


ATOM
1435
CD
GLU
A
252
48.691
29.822
25.014
1.00
21.51
A


ATOM
1436
OE1
GLU
A
252
47.989
30.707
25.550
1.00
21.46
A


ATOM
1437
0E2
GLU
A
252
48.367
28.613
24.993
1.00
20.23
A


ATOM
1438
C
GLU
A
252
51.071
32.970
23.167
1.00
22.99
A


ATOM
1439
O
GLU
A
252
52.191
33.480
23.136
1.00
23.17
A


ATOM
1440
N
LEU
A
253
50.441
32.576
22.064
1.00
23.00
A


ATOM
1441
CA
LEU
A
253
51.068
32.753
20.758
1.00
25.62
A


ATOM
1442
CB
LEU
A
253
50.277
32.029
19.669
1.00
26.75
A


ATOM
1443
CC
LEU
A
253
50.743
30.620
19.296
1.00
31.87
A


ATOM
1444
CD1
LEU
A
253
50.433
29.651
20.422
1.00
31.81
A


ATOM
1445
CD2
LEU
A
253
50.044
30.179
18.015
1.00
31.86
A


ATOM
1446
C
LEU
A
253
51.201
34.228
20.371
1.00
26.94
A


ATOM
1447
O
LEU
A
253
52.107
34.601
19.626
1.00
27.09
A


ATOM
1448
N
LEU
A
254
50.297
35.059
20.877
1.00
25.83
A


ATOM
1449
CA
LEU
A
254
50.297
36.485
20.564
1.00
27.26
A


ATOM
1450
CB
LEU
A
254
48.858
37.006
20.564
1.00
25.84
A


ATOM
1451
CC
LEU
A
254
47.882
36.290
19.621
1.00
24.69
A


ATOM
1452
CD1
LEU
A
254
46.459
36.724
19.932
1.00
23.64
A


ATOM
1453
CD2
LEU
A
254
48.236
36.597
18.177
1.00
24.24
A


ATOM
1454
C
LEU
A
254
51.134
37.314
21.537
1.00
30.62
A


ATOM
1455
O
LEU
A
254
51.633
38.383
21.187
1.00
32.35
A


ATOM
1456
N
THR
A
255
51.292
36.821
22.758
1.00
32.47
A


ATOM
1457
CA
THR
A
255
52.056
37.547
23.759
1.00
36.70
A


ATOM
1458
CB
THR
A
255
51.368
37.478
25.127
1.00
34.51
A


ATOM
1459
OG1
THR
A
255
51.188
36.106
25.494
1.00
35.49
A


ATOM
1460
CC2
THR
A
255
50.013
38.166
25.077
1.00
33.40
A


ATOM
1461
C
THR
A
255
53.477
37.035
23.910
1.00
40.09
A


ATOM
1462
O
THR
A
255
54.430
37.793
23.772
1.00
43.69
A


ATOM
1463
N
CLU
A
256
53.617
35.747
24.189
1.00
44.77
A


ATOM
1464
CA
CLU
A
256
54.932
35.144
24.382
1.00
49.15
A


ATOM
1465
CB
CLU
A
256
54.866
34.143
25.534
1.00
51.24
A


ATOM
1466
CC
CLU
A
256
54.514
34.786
26.862
1.00
56.03
A


ATOM
1467
CD
CLU
A
256
54.053
33.780
27.893
1.00
58.83
A


ATOM
1468
OE1
CLU
A
256
54.766
32.776
28.107
1.00
62.13
A


ATOM
1469
OE2
CLU
A
256
52.979
33.996
28.494
1.00
60.34
A


ATOM
1470
C
CLU
A
256
55.475
34.456
23.137
1.00
50.09
A


ATOM
1471
O
CLU
A
256
56.616
33.995
23.127
1.00
50.42
A


ATOM
1472
N
LYS
A
257
54.658
34.389
22.090
1.00
51.21
A


ATOM
1473
CA
LYS
A
257
55.064
33.746
20.845
1.00
51.22
A


ATOM
1474
CB
LYS
A
257
56.244
34.502
20.227
1.00
53.28
A


ATOM
1475
CC
LYS
A
257
56.558
34.125
18.790
1.00
55.19
A


ATOM
1476
CD
LYS
A
257
57.709
34.961
18.253
1.00
57.52
A


ATOM
1477
CE
LYS
A
257
57.952
34.694
16.777
1.00
58.52
A


ATOM
1478
NZ
LYS
A
257
58.290
33.268
16.515
1.00
60.88
A


ATOM
1479
C
LYS
A
257
55.467
32.302
21.138
1.00
50.74
A


ATOM
1480
O
LYS
A
257
56.432
31.790
20.577
1.00
52.26
A


ATOM
1481
N
SER
A
258
54.721
31.654
22.027
1.00
48.07
A


ATOM
1482
CA
SER
A
258
54.999
30.273
22.402
1.00
46.87
A


ATOM
1483
CB
SER
A
258
55.590
30.229
23.812
1.00
48.88
A


ATOM
1484
OG
SER
A
258
54.741
30.892
24.734
1.00
53.14
A


ATOM
1485
C
SER
A
258
53.735
29.415
22.342
1.00
44.07
A


ATOM
1486
O
SER
A
258
52.617
29.932
22.417
1.00
44.17
A


ATOM
1487
N
ALA
A
259
53.917
28.105
22.204
1.00
38.30
A


ATOM
1488
CA
ALA
A
259
52.793
27.180
22.127
1.00
34.73
A


ATOM
1489
CB
ALA
A
259
52.551
26.779
20.684
1.00
34.16
A


ATOM
1490
C
ALA
A
259
53.042
25.940
22.977
1.00
32.34
A


ATOM
1491
O
ALA
A
259
54.172
25.459
23.086
1.00
31.81
A


ATOM
1492
N
CYS
A
260
51.975
25.428
23.579
1.00
28.58
A


ATOM
1493
CA
CYS
A
260
52.056
24.244
24.425
1.00
26.27
A


ATOM
1494
CB
CYS
A
260
52.183
24.654
25.892
1.00
26.53
A


ATOM
1495
SG
CYS
A
260
50.846
25.739
26.469
1.00
32.91
A


ATOM
1496
C
CYS
A
260
50.786
23.435
24.224
1.00
22.83
A


ATOM
1497
O
CYS
A
260
49.892
23.856
23.495
1.00
22.14
A


ATOM
1498
N
LYS
A
261
50.706
22.277
24.868
1.00
20.02
A


ATOM
1499
CA
LYS
A
261
49.526
21.434
24.744
1.00
20.65
A


ATOM
1500
CB
LYS
A
261
49.619
20.243
25.696
1.00
23.28
A


ATOM
1501
CG
LYS
A
261
50.716
19.253
25.347
1.00
27.44
A


ATOM
1502
CD
LYS
A
261
50.732
18.117
26.350
1.00
29.98
A


ATOM
1503
CE
LYS
A
261
51.922
17.203
26.134
1.00
32.34
A


ATOM
1504
NZ
LYS
A
261
51.940
16.121
27.153
1.00
33.28
A


ATOM
1505
C
LYS
A
261
48.268
22.229
25.062
1.00
19.20
A


ATOM
1506
O
LYS
A
261
47.253
22.092
24.387
1.00
18.08
A


ATOM
1507
N
SER
A
262
48.358
23.068
26.089
1.00
16.92
A


ATOM
1508
CA
SER
A
262
47.235
23.883
26.534
1.00
18.13
A


ATOM
1509
CB
SER
A
262
47.644
24.698
27.770
1.00
18.27
A


ATOM
1510
CO
SER
A
262
46.517
25.258
28.421
1.00
22.53
A


ATOM
1511
C
SER
A
262
46.736
24.811
25.424
1.00
16.77
A


ATOM
1512
O
SER
A
262
45.591
25.254
25.450
1.00
15.69
A


ATOM
1513
N
SER
A
263
47.595
25.118
24.456
1.00
16.44
A


ATOM
1514
CA
SER
A
263
47.175
25.970
23.347
1.00
16.89
A


ATOM
1515
CB
SER
A
263
48.340
26.228
22.382
1.00
18.49
A


ATOM
1516
OG
SER
A
263
49.402
26.909
23.031
1.00
22.10
A


ATOM
1517
C
SER
A
263
46.040
25.257
22.612
1.00
17.79
A


ATOM
1518
O
SER
A
263
45.099
25.898
22.148
1.00
17.57
A


ATOM
1519
N
ASP
A
264
46.119
23.928
22.517
1.00
16.30
A


ATOM
1520
CA
ASP
A
264
45.069
23.166
21.836
1.00
16.72
A


ATOM
1521
CB
ASP
A
264
45.483
21.704
21.620
1.00
15.92
A


ATOM
1522
CO
ASP
A
264
46.544
21.539
20.548
1.00
17.93
A


ATOM
1523
OD1
ASP
A
264
46.642
22.412
19.661
1.00
16.78
A


ATOM
1524
OD2
ASP
A
264
47.265
20.515
20.579
1.00
16.64
A


ATOM
1525
C
ASP
A
264
43.773
23.194
22.646
1.00
17.67
A


ATOM
1526
O
ASP
A
264
42.681
23.197
22.076
1.00
18.27
A


ATOM
1527
N
LEU
A
265
43.898
23.205
23.974
1.00
15.49
A


ATOM
1528
CA
LEU
A
265
42.730
23.232
24.849
1.00
14.75
A


ATOM
1529
CB
LEU
A
265
43.147
23.038
26.313
1.00
11.38
A


ATOM
1530
CO
LEU
A
265
43.711
21.641
26.621
1.00
14.04
A


ATOM
1531
CD1
LEU
A
265
44.249
21.579
28.052
1.00
13.96
A


ATOM
1532
CD2
LEU
A
265
42.619
20.603
26.416
1.00
11.62
A


ATOM
1533
C
LEU
A
265
41.999
24.557
24.675
1.00
15.13
A


ATOM
1534
O
LEU
A
265
40.777
24.620
24.785
1.00
16.75
A


ATOM
1535
N
TRP
A
266
42.746
25.622
24.405
1.00
16.08
A


ATOM
1536
CA
TRP
A
266
42.118
26.918
24.184
1.00
16.96
A


ATOM
1537
CB
TRP
A
266
43.176
28.015
24.023
1.00
17.28
A


ATOM
1538
CO
TRP
A
266
42.618
29.326
23.521
1.00
20.54
A


ATOM
1539
CD2
TRP
A
266
42.313
30.490
24.301
1.00
20.07
A


ATOM
1540
CE2
TRP
A
266
41.782
31.459
23.417
1.00
20.46
A


ATOM
1541
CE3
TRP
A
266
42.435
30.810
25.660
1.00
20.68
A


ATOM
1542
CD1
TRP
A
266
42.270
29.631
22.231
1.00
19.53
A


ATOM
1543
NE1
TRP
A
266
41.769
30.908
22.163
1.00
19.61
A


ATOM
1544
CZ2
TRP
A
266
41.372
32.727
23.850
1.00
20.90
A


ATOM
1545
CZ3
TRP
A
266
42.026
32.073
26.091
1.00
19.45
A


ATOM
1546
CH2
TRP
A
266
41.501
33.015
25.185
1.00
20.71
A


ATOM
1547
C
TRP
A
266
41.284
26.795
22.913
1.00
17.22
A


ATOM
1548
O
TRP
A
266
40.139
27.240
22.863
1.00
18.03
A


ATOM
1549
N
ALA
A
267
41.863
26.181
21.886
1.00
17.50
A


ATOM
1550
CA
ALA
A
267
41.155
25.990
20.626
1.00
16.16
A


ATOM
1551
CB
ALA
A
267
42.050
25.290
19.621
1.00
14.28
A


ATOM
1552
C
ALA
A
267
39.901
25.159
20.891
1.00
16.28
A


ATOM
1553
O
ALA
A
267
38.835
25.436
20.346
1.00
16.46
A


ATOM
1554
N
LEU
A
268
40.031
24.144
21.739
1.00
16.57
A


ATOM
1555
CA
LEU
A
268
38.890
23.299
22.084
1.00
17.03
A


ATOM
1556
CB
LEU
A
268
39.292
22.260
23.139
1.00
15.35
A


ATOM
1557
CC
LEU
A
268
38.158
21.429
23.754
1.00
19.00
A


ATOM
1558
CD1
LEU
A
268
37.505
20.578
22.678
1.00
16.17
A


ATOM
1559
CD2
LEU
A
268
38.718
20.537
24.881
1.00
17.49
A


ATOM
1560
C
LEU
A
268
37.766
24.179
22.628
1.00
15.72
A


ATOM
1561
O
LEU
A
268
36.603
24.031
22.247
1.00
15.28
A


ATOM
1562
N
GLY
A
269
38.119
25.099
23.520
1.00
14.34
A


ATOM
1563
CA
GLY
A
269
37.124
25.989
24.092
1.00
13.39
A


ATOM
1564
C
GLY
A
269
36.406
26.808
23.031
1.00
14.94
A


ATOM
1565
O
GLY
A
269
35.193
27.014
23.114
1.00
14.76
A


ATOM
1566
N
CYS
A
270
37.146
27.279
22.030
1.00
13.86
A


ATOM
1567
CA
CYS
A
270
36.539
28.061
20.958
1.00
16.80
A


ATOM
1568
CB
CYS
A
270
37.611
28.634
20.023
1.00
15.97
A


ATOM
1569
SQ
CYS
A
270
38.751
29.810
20.780
1.00
20.48
A


ATOM
1570
C
CYS
A
270
35.598
27.175
20.140
1.00
17.50
A


ATOM
1571
O
CYS
A
270
34.516
27.604
19.741
1.00
18.38
A


ATOM
1572
N
ILE
A
271
36.022
25.939
19.887
1.00
16.99
A


ATOM
1573
CA
ILE
A
271
35.221
25.004
19.104
1.00
16.66
A


ATOM
1574
CB
ILE
A
271
36.038
23.741
18.778
1.00
16.53
A


ATOM
1575
CG2
ILE
A
271
35.155
22.694
18.102
1.00
16.34
A


ATOM
1576
Cd
ILE
A
271
37.222
24.129
17.882
1.00
15.59
A


ATOM
1577
CD1
ILE
A
271
38.239
23.018
17.690
1.00
14.88
A


ATOM
1578
C
ILE
A
271
33.920
24.626
19.809
1.00
16.74
A


ATOM
1579
O
ILE
A
271
32.865
24.576
19.179
1.00
17.12
A


ATOM
1580
N
ILE
A
272
33.990
24.357
21.111
1.00
16.13
A


ATOM
1581
CA
ILE
A
272
32.785
24.021
21.862
1.00
18.30
A


ATOM
1582
CB
ILE
A
272
33.097
23.747
23.346
1.00
17.77
A


ATOM
1583
CG2
ILE
A
272
31.796
23.666
24.152
1.00
17.96
A


ATOM
1584
Cd
ILE
A
272
33.877
22.437
23.481
1.00
19.55
A


ATOM
1585
CD1
ILE
A
272
34.446
22.217
24.886
1.00
18.64
A


ATOM
1586
C
ILE
A
272
31.824
25.207
21.776
1.00
19.51
A


ATOM
1587
O
ILE
A
272
30.624
25.037
21.554
1.00
20.44
A


ATOM
1588
N
TYR
A
273
32.362
26.409
21.947
1.00
18.52
A


ATOM
1589
CA
TYR
A
273
31.553
27.615
21.881
1.00
20.48
A


ATOM
1590
CB
TYR
A
273
32.418
28.847
22.162
1.00
18.98
A


ATOM
1591
Cd
TYR
A
273
31.663
30.161
22.125
1.00
20.26
A


ATOM
1592
CD1
TYR
A
273
31.229
30.709
20.916
1.00
20.67
A


ATOM
1593
CEl
TYR
A
273
30.536
31.917
20.880
1.00
20.98
A


ATOM
1594
CD2
TYR
A
273
31.383
30.857
23.302
1.00
19.82
A


ATOM
1595
CE2
TYR
A
273
30.691
32.062
23.280
1.00
20.62
A


ATOM
1596
CZ
TYR
A
273
30.271
32.587
22.067
1.00
21.15
A


ATOM
1597
OH
TYR
A
273
29.588
33.776
22.049
1.00
21.86
A


ATOM
1598
C
TYR
A
273
30.902
27.730
20.507
1.00
21.54
A


ATOM
1599
O
TYR
A
273
29.719
28.049
20.401
1.00
22.80
A


ATOM
1600
N
GLN
A
274
31.676
27.454
19.461
1.00
21.05
A


ATOM
1601
CA
GLN
A
274
31.176
27.538
18.095
1.00
21.48
A


ATOM
1602
CB
GLN
A
274
32.323
27.341
17.097
1.00
21.41
A


ATOM
1603
Cd
GLN
A
274
31.934
27.596
15.645
1.00
23.15
A


ATOM
1604
CD
GLN
A
274
33.131
27.588
14.706
1.00
24.80
A


ATOM
1605
OE1
GLN
A
274
34.276
27.446
15.139
1.00
22.51
A


ATOM
1606
NE2
GLN
A
274
32.870
27.750
13.413
1.00
22.96
A


ATOM
1607
C
GLN
A
274
30.076
26.517
17.828
1.00
21.51
A


ATOM
1608
O
GLN
A
274
29.123
26.806
17.108
1.00
20.50
A


ATOM
1609
N
LEU
A
275
30.207
25.324
18.403
1.00
21.44
A


ATOM
1610
CA
LEU
A
275
29.196
24.282
18.208
1.00
20.95
A


ATOM
1611
CB
LEU
A
275
29.645
22.958
18.846
1.00
19.11
A


ATOM
1612
CG
LEU
A
275
30.775
22.182
18.159
1.00
21.43
A


ATOM
1613
CD1
LEU
A
275
31.118
20.936
18.963
1.00
17.64
A


ATOM
1614
CD2
LEU
A
275
30.342
21.795
16.754
1.00
20.34
A


ATOM
1615
C
LEU
A
275
27.860
24.697
18.815
1.00
21.32
A


ATOM
1616
O
LEU
A
275
26.802
24.461
18.229
1.00
19.75
A


ATOM
1617
N
VAL
A
276
27.921
25.322
19.987
1.00
19.10
A


ATOM
1618
CA
VAL
A
276
26.724
25.750
20.702
1.00
22.47
A


ATOM
1619
CB
VAL
A
276
27.011
25.882
22.217
1.00
20.87
A


ATOM
1620
CG1
VAL
A
276
25.742
26.291
22.957
1.00
19.68
A


ATOM
1621
CG2
VAL
A
276
27.550
24.558
22.766
1.00
19.43
A


ATOM
1622
C
VAL
A
276
26.127
27.075
20.211
1.00
23.89
A


ATOM
1623
O
VAL
A
276
24.910
27.199
20.070
1.00
24.90
A


ATOM
1624
N
ALA
A
277
26.983
28.062
19.965
1.00
24.56
A


ATOM
1625
CA
ALA
A
277
26.533
29.374
19.518
1.00
24.72
A


ATOM
1626
CB
ALA
A
277
27.504
30.444
19.999
1.00
24.36
A


ATOM
1627
C
ALA
A
277
26.378
29.458
18.005
1.00
25.76
A


ATOM
1628
O
ALA
A
277
25.577
30.242
17.502
1.00
26.39
A


ATOM
1629
N
GLY
A
278
27.142
28.651
17.280
1.00
25.13
A


ATOM
1630
CA
GLY
A
278
27.062
28.673
15.834
1.00
25.58
A


ATOM
1631
C
GLY
A
278
28.163
29.524
15.231
1.00
26.50
A


ATOM
1632
O
GLY
A
278
28.374
29.510
14.015
1.00
28.17
A


ATOM
1633
N
LEU
A
279
28.866
30.262
16.086
1.00
24.44
A


ATOM
1634
CA
LEU
A
279
29.962
31.130
15.656
1.00
25.21
A


ATOM
1635
CB
LEU
A
279
29.468
32.575
15.500
1.00
25.78
A


ATOM
1636
CG
LEU
A
279
28.364
32.899
14.490
1.00
28.17
A


ATOM
1637
CD1
LEU
A
279
27.922
34.344
14.684
1.00
26.60
A


ATOM
1638
CD2
LEU
A
279
28.862
32.670
13.071
1.00
26.52
A


ATOM
1639
C
LEU
A
279
31.093
31.116
16.687
1.00
23.47
A


ATOM
1640
O
LEU
A
279
30.848
30.994
17.882
1.00
24.44
A


ATOM
1641
N
PRO
A
280
32.349
31.239
16.236
1.00
23.35
A


ATOM
1642
CD
PRO
A
280
32.831
31.404
14.855
1.00
22.26
A


ATOM
1643
CA
PRO
A
280
33.464
31.239
17.189
1.00
23.81
A


ATOM
1644
CB
PRO
A
280
34.692
31.293
16.282
1.00
23.24
A


ATOM
1645
CG
PRO
A
280
34.189
32.020
15.073
1.00
24.89
A


ATOM
1646
C
PRO
A
280
33.353
32.444
18.137
1.00
22.69
A


ATOM
1647
O
PRO
A
280
32.750
33.457
17.788
1.00
22.11
A


ATOM
1648
N
PRO
A
281
33.939
32.344
19.345
1.00
23.06
A


ATOM
1649
CD
PRO
A
281
34.810
31.223
19.734
1.00
21.37
A


ATOM
1650
CA
PRO
A
281
33.935
33.375
20.395
1.00
23.67
A


ATOM
1651
CB
PRO
A
281
34.781
32.751
21.509
1.00
24.89
A


ATOM
1652
CG
PRO
A
281
34.749
31.287
21.219
1.00
25.24
A


ATOM
1653
C
PRO
A
281
34.481
34.752
20.017
1.00
23.75
A


ATOM
1654
O
PRO
A
281
33.869
35.781
20.317
1.00
21.02
A


ATOM
1655
N
PHE
A
282
35.644
34.763
19.379
1.00
22.17
A


ATOM
1656
CA
PHE
A
282
36.293
36.007
18.998
1.00
23.16
A


ATOM
1657
CB
PHE
A
282
37.765
35.943
19.406
1.00
21.01
A


ATOM
1658
CG
PHE
A
282
37.975
35.482
20.822
1.00
22.66
A


ATOM
1659
CD1
PHE
A
282
37.806
36.361
21.888
1.00
20.06
A


ATOM
1660
CD2
PHE
A
282
38.291
34.151
21.093
1.00
20.72
A


ATOM
1661
CEl
PHE
A
282
37.947
35.921
23.206
1.00
22.66
A


ATOM
1662
CE2
PHE
A
282
38.433
33.702
22.405
1.00
20.97
A


ATOM
1663
CZ
PHE
A
282
38.261
34.590
23.466
1.00
19.58
A


ATOM
1664
C
PHE
A
282
36.169
36.263
17.503
1.00
24.39
A


ATOM
1665
O
PHE
A
282
36.802
35.585
16.694
1.00
25.80
A


ATOM
1666
N
ARC
A
283
35.355
37.248
17.142
1.00
24.99
A


ATOM
1667
CA
ARC
A
283
35.141
37.594
15.741
1.00
26.33
A


ATOM
1668
CB
ARC
A
283
33.721
37.209
15.316
1.00
28.91
A


ATOM
1669
CC
ARC
A
283
33.293
35.808
15.724
1.00
30.27
A


ATOM
1670
CD
ARC
A
283
31.904
35.493
15.188
1.00
33.36
A


ATOM
1671
NE
ARC
A
283
30.890
36.392
15.733
1.00
32.76
A


ATOM
1672
CZ
ARC
A
283
30.372
36.287
16.952
1.00
34.79
A


ATOM
1673
NH1
ARC
A
283
30.767
35.317
17.768
1.00
35.77
A


ATOM
1674
NH2
ARC
A
283
29.458
37.156
17.359
1.00
36.12
A


ATOM
1675
C
ARC
A
283
35.328
39.096
15.544
1.00
26.47
A


ATOM
1676
O
ARC
A
283
35.029
39.888
16.438
1.00
26.28
A


ATOM
1677
N
ALA
A
284
35.818
39.486
14.373
1.00
26.70
A


ATOM
1678
CA
ALA
A
284
36.033
40.899
14.079
1.00
27.84
A


ATOM
1679
CB
ALA
A
284
37.188
41.442
14.914
1.00
26.24
A


ATOM
1680
C
ALA
A
284
36.327
41.077
12.602
1.00
28.35
A


ATOM
1681
O
ALA
A
284
36.560
40.101
11.891
1.00
29.91
A


ATOM
1682
N
CLY
A
285
36.332
42.329
12.153
1.00
29.29
A


ATOM
1683
CA
CLY
A
285
36.577
42.631
10.753
1.00
29.52
A


ATOM
1684
C
CLY
A
285
37.893
42.156
10.168
1.00
30.12
A


ATOM
1685
O
CLY
A
285
37.974
41.862
8.976
1.00
30.60
A


ATOM
1686
N
ASN
A
286
38.939
42.097
10.983
1.00
28.49
A


ATOM
1687
CA
ASN
A
286
40.231
41.644
10.489
1.00
26.71
A


ATOM
1688
CB
ASN
A
286
41.050
42.825
9.945
1.00
26.11
A


ATOM
1689
CC
ASN
A
286
41.310
43.900
10.990
1.00
27.83
A


ATOM
1690
OD1
ASN
A
286
41.877
43.631
12.049
1.00
27.84
A


ATOM
1691
ND2
ASN
A
286
40.908
45.131
10.685
1.00
25.95
A


ATOM
1692
C
ASN
A
286
40.997
40.924
11.584
1.00
26.03
A


ATOM
1693
O
ASN
A
286
40.540
40.851
12.723
1.00
25.66
A


ATOM
1694
N
CLU
A
287
42.162
40.391
11.239
1.00
24.81
A


ATOM
1695
CA
CLU
A
287
42.965
39.662
12.206
1.00
27.59
A


ATOM
1696
CB
CLU
A
287
44.145
38.985
11.510
1.00
30.17
A


ATOM
1697
CC
CLU
A
287
43.776
37.632
10.931
1.00
38.21
A


ATOM
1698
CD
CLU
A
287
44.900
36.998
10.140
1.00
41.86
A


ATOM
1699
OE1
CLU
A
287
46.061
37.036
10.608
1.00
43.08
A


ATOM
1700
0E2
CLU
A
287
44.612
36.449
9.052
1.00
45.22
A


ATOM
1701
C
CLU
A
287
43.459
40.485
13.383
1.00
25.05
A


ATOM
1702
O
CLU
A
287
43.382
40.030
14.521
1.00
26.41
A


ATOM
1703
N
TYR
A
288
43.966
41.685
13.122
1.00
23.04
A


ATOM
1704
CA
TYR
A
288
44.460
42.528
14.205
1.00
22.34
A


ATOM
1705
CB
TYR
A
288
44.867
43.913
13.691
1.00
21.07
A


ATOM
1706
CC
TYR
A
288
45.275
44.858
14.805
1.00
21.07
A


ATOM
1707
CD1
TYR
A
288
46.533
44.762
15.405
1.00
21.23
A


ATOM
1708
CEl
TYR
A
288
46.891
45.588
16.475
1.00
20.43
A


ATOM
1709
CD2
TYR
A
288
44.380
45.809
15.302
1.00
22.32
A


ATOM
1710
CE2
TYR
A
288
44.725
46.637
16.373
1.00
23.28
A


ATOM
1711
CZ
TYR
A
288
45.981
46.518
16.953
1.00
22.96
A


ATOM
1712
OH
TYR
A
288
46.316
47.313
18.024
1.00
23.18
A


ATOM
1713
C
TYR
A
288
43.402
42.698
15.288
1.00
21.38
A


ATOM
1714
O
TYR
A
288
43.710
42.616
16.473
1.00
22.09
A


ATOM
1715
N
LEU
A
289
42.159
42.939
14.874
1.00
21.88
A


ATOM
1716
CA
LEU
A
289
41.055
43.130
15.811
1.00
21.98
A


ATOM
1717
CB
LEU
A
289
39.821
43.673
15.078
1.00
22.90
A


ATOM
1718
CC
LEU
A
289
39.896
45.130
14.601
1.00
26.52
A


ATOM
1719
CD1
LEU
A
289
38.706
45.436
13.696
1.00
26.55
A


ATOM
1720
CD2
LEU
A
289
39.914
46.071
15.807
1.00
23.13
A


ATOM
1721
C
LEU
A
289
40.686
41.849
16.560
1.00
21.24
A


ATOM
1722
O
LEU
A
289
40.256
41.897
17.715
1.00
20.72
A


ATOM
1723
N
ILE
A
290
40.843
40.708
15.900
1.00
19.62
A


ATOM
1724
CA
ILE
A
290
40.538
39.433
16.533
1.00
18.54
A


ATOM
1725
CB
ILE
A
290
40.560
38.281
15.509
1.00
18.52
A


ATOM
1726
C02
ILE
A
290
40.503
36.934
16.234
1.00
17.63
A


ATOM
1727
CCI
ILE
A
290
39.378
38.429
14.545
1.00
18.88
A


ATOM
1728
CD1
ILE
A
290
39.421
37.483
13.357
1.00
19.81
A


ATOM
1729
C
ILE
A
290
41.578
39.167
17.618
1.00
19.09
A


ATOM
1730
O
ILE
A
290
41.236
38.788
18.737
1.00
18.20
A


ATOM
1731
N
PHE
A
291
42.849
39.376
17.286
1.00
18.76
A


ATOM
1732
CA
PHE
A
291
43.925
39.156
18.247
1.00
20.75
A


ATOM
1733
CB
PHE
A
291
45.286
39.434
17.606
1.00
20.71
A


ATOM
1734
CC
PHE
A
291
45.644
38.480
16.503
1.00
22.92
A


ATOM
1735
CD1
PHE
A
291
45.065
37.214
16.443
1.00
22.98
A


ATOM
1736
CD2
PHE
A
291
46.588
38.830
15.543
1.00
22.91
A


ATOM
1737
CEl
PHE
A
291
45.423
36.310
15.440
1.00
24.51
A


ATOM
1738
CE2
PHE
A
291
46.954
37.931
14.535
1.00
25.54
A


ATOM
1739
CZ
PHE
A
291
46.370
36.670
14.485
1.00
23.29
A


ATOM
1740
C
PHE
A
291
43.739
40.061
19.451
1.00
21.72
A


ATOM
1741
O
PHE
A
291
43.992
39.671
20.593
1.00
22.32
A


ATOM
1742
N
GIN
A
292
43.284
41.275
19.178
1.00
23.27
A


ATOM
1743
CA
GIN
A
292
43.055
42.264
20.216
1.00
24.01
A


ATOM
1744
CB
GIN
A
292
42.574
43.559
19.562
1.00
25.77
A


ATOM
1745
CC
GIN
A
292
42.577
44.773
20.447
1.00
28.45
A


ATOM
1746
CD
GIN
A
292
42.469
46.057
19.638
1.00
29.83
A


ATOM
1747
OE1
GIN
A
292
41.520
46.244
18.872
1.00
27.16
A


ATOM
1748
NE2
GIN
A
292
43.449
46.944
19.799
1.00
27.61
A


ATOM
1749
C
GIN
A
292
42.018
41.733
21.204
1.00
22.97
A


ATOM
1750
O
GIN
A
292
42.200
41.832
22.415
1.00
21.64
A


ATOM
1751
N
LYS
A
293
40.937
41.154
20.687
1.00
21.82
A


ATOM
1752
CA
LYS
A
293
39.895
40.612
21.558
1.00
22.18
A


ATOM
1753
CB
LYS
A
293
38.664
40.223
20.740
1.00
22.69
A


ATOM
1754
CC
LYS
A
293
37.919
41.407
20.153
1.00
25.78
A


ATOM
1755
CD
LYS
A
293
36.651
40.961
19.429
1.00
27.88
A


ATOM
1756
CE
LYS
A
293
35.857
42.161
18.926
1.00
30.85
A


ATOM
1757
NZ
LYS
A
293
34.612
41.750
18.214
1.00
32.98
A


ATOM
1758
C
LYS
A
293
40.398
39.398
22.343
1.00
21.20
A


ATOM
1759
O
LYS
A
293
40.041
39.204
23.509
1.00
22.01
A


ATOM
1760
N
ILE
A
294
41.226
38.583
21.702
1.00
19.91
A


ATOM
1761
CA
ILE
A
294
41.774
37.394
22.347
1.00
20.28
A


ATOM
1762
CB
ILE
A
294
42.631
36.575
21.349
1.00
18.98
A


ATOM
1763
CC2
ILE
A
294
43.481
35.550
22.098
1.00
17.70
A


ATOM
1764
CCI
ILE
A
294
41.716
35.897
20.318
1.00
17.93
A


ATOM
1765
CD1
ILE
A
294
42.467
35.237
19.178
1.00
16.21
A


ATOM
1766
C
ILE
A
294
42.618
37.727
23.587
1.00
21.94
A


ATOM
1767
O
ILE
A
294
42.366
37.199
24.673
1.00
20.86
A


ATOM
1768
N
ILE
A
295
43.610
38.600
23.439
1.00
21.88
A


ATOM
1769
CA
ILE
A
295
44.461
38.934
24.582
1.00
24.25
A


ATOM
1770
CB
ILE
A
295
45.668
39.805
24.175
1.00
23.93
A


ATOM
1771
CC2
ILE
A
295
46.514
39.066
23.140
1.00
24.61
A


ATOM
1772
CCI
ILE
A
295
45.189
41.151
23.637
1.00
24.58
A


ATOM
1773
CD1
ILE
A
295
46.317
42.149
23.433
1.00
26.69
A


ATOM
1774
C
ILE
A
295
43.720
39.636
25.717
1.00
24.80
A


ATOM
1775
O
ILE
A
295
44.214
39.687
26.842
1.00
24.76
A


ATOM
1776
N
LYS
A
296
42.539
40.173
25.425
1.00
25.33
A


ATOM
1777
CA
LYS
A
296
41.743
40.853
26.444
1.00
26.80
A


ATOM
1778
CB
LYS
A
296
41.178
42.170
25.894
1.00
27.39
A


ATOM
1779
CC
LYS
A
296
42.240
43.141
25.413
1.00
31.79
A


ATOM
1780
CD
LYS
A
296
41.634
44.410
24.826
1.00
35.56
A


ATOM
1781
CE
LYS
A
296
41.009
45.283
25.900
1.00
39.29
A


ATOM
1782
NZ
LYS
A
296
40.564
46.603
25.357
1.00
41.72
A


ATOM
1783
C
LYS
A
296
40.593
39.958
26.893
1.00
25.50
A


ATOM
1784
O
LYS
A
296
39.770
40.361
27.713
1.00
24.02
A


ATOM
1785
N
LEU
A
297
40.550
38.742
26.349
1.00
25.67
A


ATOM
1786
CA
LEU
A
297
39.500
37.777
26.666
1.00
25.16
A


ATOM
1787
CB
LEU
A
297
39.632
37.285
28.111
1.00
24.80
A


ATOM
1788
CG
LEU
A
297
38.766
36.068
28.460
1.00
26.43
A


ATOM
1789
CD1
LEU
A
297
39.238
34.852
27.646
1.00
26.70
A


ATOM
1790
CD2
LEU
A
297
38.856
35.777
29.951
1.00
24.84
A


ATOM
1791
C
LEU
A
297
38.151
38.459
26.467
1.00
25.11
A


ATOM
1792
O
LEU
A
297
37.261
38.378
27.309
1.00
25.28
A


ATOM
1793
N
GLU
A
298
38.007
39.127
25.331
1.00
24.98
A


ATOM
1794
CA
GLU
A
298
36.786
39.847
25.023
1.00
25.31
A


ATOM
1795
CB
GLU
A
298
37.143
41.139
24.291
1.00
27.13
A


ATOM
1796
CG
GLU
A
298
35.991
42.092
24.108
1.00
31.28
A


ATOM
1797
CD
GLU
A
298
36.419
43.362
23.410
1.00
34.40
A


ATOM
1798
OE1
GLU
A
298
37.348
44.027
23.918
1.00
35.90
A


ATOM
1799
OE2
GLU
A
298
35.832
43.693
22.359
1.00
36.16
A


ATOM
1800
C
GLU
A
298
35.766
39.057
24.207
1.00
23.79
A


ATOM
1801
O
GLU
A
298
35.832
39.017
22.979
1.00
24.35
A


ATOM
1802
N
TYR
A
299
34.825
38.427
24.902
1.00
23.45
A


ATOM
1803
CA
TYR
A
299
33.760
37.663
24.265
1.00
23.98
A


ATOM
1804
CB
TYR
A
299
34.264
36.304
23.755
1.00
20.13
A


ATOM
1805
CG
TYR
A
299
34.348
35.233
24.828
1.00
21.17
A


ATOM
1806
CD1
TYR
A
299
35.336
35.279
25.810
1.00
19.32
A


ATOM
1807
CEl
TYR
A
299
35.389
34.332
26.826
1.00
19.30
A


ATOM
1808
CD2
TYR
A
299
33.410
34.201
24.888
1.00
18.96
A


ATOM
1809
CE2
TYR
A
299
33.456
33.243
25.907
1.00
19.41
A


ATOM
1810
CZ
TYR
A
299
34.449
33.321
26.870
1.00
18.79
A


ATOM
1811
OH
TYR
A
299
34.511
32.401
27.881
1.00
18.77
A


ATOM
1812
C
TYR
A
299
32.699
37.437
25.331
1.00
25.20
A


ATOM
1813
O
TYR
A
299
32.942
37.681
26.506
1.00
26.46
A


ATOM
1814
N
ASP
A
300
31.522
36.981
24.927
1.00
26.94
A


ATOM
1815
CA
ASP
A
300
30.467
36.710
25.891
1.00
30.60
A


ATOM
1816
CB
ASP
A
300
29.665
37.981
26.179
1.00
35.86
A


ATOM
1817
CG
ASP
A
300
29.228
38.687
24.923
1.00
42.04
A


ATOM
1818
ODi
ASP
A
300
28.450
38.088
24.149
1.00
45.98
A


ATOM
1819
0D2
ASP
A
300
29.666
39.840
24.707
1.00
45.69
A


ATOM
1820
C
ASP
A
300
29.564
35.608
25.363
1.00
29.26
A


ATOM
1821
O
ASP
A
300
29.590
35.299
24.172
1.00
28.64
A


ATOM
1822
N
PHE
A
301
28.778
35.011
26.253
1.00
28.96
A


ATOM
1823
CA
PHE
A
301
27.884
33.924
25.871
1.00
30.48
A


ATOM
1824
CB
PHE
A
301
27.818
32.854
26.968
1.00
29.17
A


ATOM
1825
CG
PHE
A
301
29.147
32.279
27.356
1.00
29.29
A


ATOM
1826
CD1
PHE
A
301
29.978
32.949
28.245
1.00
27.31
A


ATOM
1827
CD2
PHE
A
301
29.560
31.050
26.845
1.00
27.89
A


ATOM
1828
CEl
PHE
A
301
31.205
32.403
28.625
1.00
28.83
A


ATOM
1829
CE2
PHE
A
301
30.781
30.498
27.217
1.00
28.05
A


ATOM
1830
CZ
PHE
A
301
31.605
31.175
28.110
1.00
28.27
A


ATOM
1831
C
PHE
A
301
26.459
34.384
25.619
1.00
32.20
A


ATOM
1832
O
PHE
A
301
25.946
35.261
26.317
1.00
32.36
A


ATOM
1833
N
PRO
A
302
25.798
33.804
24.607
1.00
33.29
A


ATOM
1834
CD
PRO
A
302
26.313
32.943
23.529
1.00
34.04
A


ATOM
1835
CA
PRO
A
302
24.415
34.199
24.341
1.00
35.24
A


ATOM
1836
CB
PRO
A
302
24.144
33.608
22.959
1.00
34.01
A


ATOM
1837
CG
PRO
A
302
25.041
32.413
22.921
1.00
35.48
A


ATOM
1838
C
PRO
A
302
23.567
33.561
25.444
1.00
37.39
A


ATOM
1839
O
PRO
A
302
23.935
32.518
25.986
1.00
38.49
A


ATOM
1840
N
ALA
A
303
22.447
34.188
25.783
1.00
39.36
A


ATOM
1841
CA
ALA
A
303
21.572
33.692
26.843
1.00
40.65
A


ATOM
1842
CB
ALA
A
303
20.280
34.506
26.862
1.00
41.66
A


ATOM
1843
C
ALA
A
303
21.238
32.197
26.814
1.00
41.25
A


ATOM
1844
O
ALA
A
303
21.253
31.537
27.854
1.00
43.16
A


ATOM
1845
N
ALA
A
304
20.945
31.665
25.631
1.00
41.04
A


ATOM
1846
CA
ALA
A
304
20.569
30.258
25.480
1.00
40.66
A


ATOM
1847
CB
ALA
A
304
20.121
30.004
24.040
1.00
41.36
A


ATOM
1848
C
ALA
A
304
21.628
29.223
25.876
1.00
39.61
A


ATOM
1849
O
ALA
A
304
21.298
28.156
26.395
1.00
40.61
A


ATOM
1850
N
PHE
A
305
22.891
29.543
25.617
1.00
36.21
A


ATOM
1851
CA
PHE
A
305
24.022
28.662
25.909
1.00
32.08
A


ATOM
1852
CB
PHE
A
305
25.259
29.519
26.187
1.00
29.46
A


ATOM
1853
CG
PHE
A
305
26.536
28.917
25.690
1.00
28.15
A


ATOM
1854
CD1
PHE
A
305
27.146
27.875
26.377
1.00
26.20
A


ATOM
1855
CD2
PHE
A
305
27.127
29.386
24.521
1.00
27.05
A


ATOM
1856
CEl
PHE
A
305
28.330
27.308
25.908
1.00
26.92
A


ATOM
1857
CE2
PHE
A
305
28.312
28.826
24.042
1.00
26.62
A


ATOM
1858
CZ
PHE
A
305
28.914
27.786
24.737
1.00
26.61
A


ATOM
1859
C
PHE
A
305
23.811
27.664
27.057
1.00
30.09
A


ATOM
1860
O
PHE
A
305
23.518
28.051
28.187
1.00
31.51
A


ATOM
1861
N
PHE
A
306
23.964
26.378
26.758
1.00
27.01
A


ATOM
1862
CA
PHE
A
306
23.801
25.334
27.769
1.00
26.30
A


ATOM
1863
CB
PHE
A
306
24.157
23.970
27.170
1.00
25.03
A


ATOM
1864
CG
PHE
A
306
23.548
23.725
25.815
1.00
27.24
A


ATOM
1865
CD1
PHE
A
306
22.170
23.831
25.622
1.00
28.40
A


ATOM
1866
CD2
PHE
A
306
24.350
23.386
24.728
1.00
27.84
A


ATOM
1867
CEl
PHE
A
306
21.601
23.603
24.365
1.00
28.05
A


ATOM
1868
CE2
PHE
A
306
23.792
23.155
23.465
1.00
28.31
A


ATOM
1869
CZ
PHE
A
306
22.415
23.263
23.283
1.00
28.00
A


ATOM
1870
C
PHE
A
306
24.711
25.652
28.961
1.00
26.23
A


ATOM
1871
O
PHE
A
306
25.927
25.775
28.811
1.00
25.59
A


ATOM
1872
N
PRO
A
307
24.125
25.796
30.163
1.00
26.67
A


ATOM
1873
CD
PRO
A
307
22.685
25.625
30.430
1.00
27.95
A


ATOM
1874
CA
PRO
A
307
24.842
26.110
31.405
1.00
26.59
A


ATOM
1875
CB
PRO
A
307
23.795
25.832
32.481
1.00
26.14
A


ATOM
1876
CG
PRO
A
307
22.531
26.250
31.803
1.00
27.86
A


ATOM
1877
C
PRO
A
307
26.145
25.355
31.659
1.00
25.58
A


ATOM
1878
O
PRO
A
307
27.189
25.964
31.900
1.00
22.65
A


ATOM
1879
N
LYS
A
308
26.085
24.031
31.620
1.00
24.46
A


ATOM
1880
CA
LYS
A
308
27.274
23.232
31.867
1.00
23.91
A


ATOM
1881
CB
LYS
A
308
26.887
21.760
32.024
1.00
23.25
A


ATOM
1882
CG
LYS
A
308
26.062
21.532
33.285
1.00
28.49
A


ATOM
1883
CD
LYS
A
308
25.618
20.093
33.466
1.00
30.17
A


ATOM
1884
CE
LYS
A
308
24.760
19.973
34.722
1.00
33.12
A


ATOM
1885
NZ
LYS
A
308
24.122
18.636
34.860
1.00
34.13
A


ATOM
1886
C
LYS
A
308
28.314
23.426
30.769
1.00
22.84
A


ATOM
1887
O
LYS
A
308
29.514
23.411
31.042
1.00
22.46
A


ATOM
1888
N
ALA
A
309
27.861
23.621
29.534
1.00
21.59
A


ATOM
1889
CA
ALA
A
309
28.792
23.848
28.432
1.00
20.02
A


ATOM
1890
CB
ALA
A
309
28.056
23.856
27.106
1.00
18.80
A


ATOM
1891
C
ALA
A
309
29.481
25.191
28.662
1.00
21.41
A


ATOM
1892
O
ALA
A
309
30.680
25.335
28.427
1.00
21.39
A


ATOM
1893
N
ARG
A
310
28.717
26.179
29.121
1.00
21.39
A


ATOM
1894
CA
ARG
A
310
29.290
27.494
29.388
1.00
22.02
A


ATOM
1895
CB
ARG
A
310
28.213
28.479
29.854
1.00
22.39
A


ATOM
1896
CG
ARG
A
310
28.806
29.756
30.436
1.00
25.30
A


ATOM
1897
CD
ARG
A
310
27.780
30.852
30.664
1.00
28.33
A


ATOM
1898
NE
ARG
A
310
28.420
32.039
31.230
1.00
30.18
A


ATOM
1899
CZ
ARG
A
310
27.901
33.263
31.203
1.00
32.07
A


ATOM
1900
NH1
ARG
A
310
26.719
33.477
30.634
1.00
31.19
A


ATOM
1901
NH2
ARG
A
310
28.567
34.277
31.742
1.00
30.49
A


ATOM
1902
C
ARG
A
310
30.376
27.388
30.458
1.00
21.65
A


ATOM
1903
O
ARG
A
310
31.464
27.949
30.311
1.00
20.36
A


ATOM
1904
N
ASP
A
311
30.074
26.677
31.541
1.00
19.57
A


ATOM
1905
CA
ASP
A
311
31.043
26.512
32.615
1.00
20.18
A


ATOM
1906
CB
ASP
A
311
30.460
25.649
33.739
1.00
20.39
A


ATOM
1907
CG
ASP
A
311
31.439
25.446
34.881
1.00
23.35
A


ATOM
1908
OD1
ASP
A
311
32.158
24.428
34.885
1.00
24.91
A


ATOM
1909
OD2
ASP
A
311
31.500
26.312
35.776
1.00
26.96
A


ATOM
1910
C
ASP
A
311
32.322
25.877
32.073
1.00
19.73
A


ATOM
1911
O
ASP
A
311
33.422
26.289
32.439
1.00
19.30
A


ATOM
1912
N
LEU
A
312
32.179
24.891
31.188
1.00
16.32
A


ATOM
1913
CA
LEU
A
312
33.349
24.226
30.611
1.00
16.66
A


ATOM
1914
CB
LEU
A
312
32.927
23.035
29.744
1.00
16.12
A


ATOM
1915
CG
LEU
A
312
34.050
22.320
28.974
1.00
14.73
A


ATOM
1916
CD1
LEU
A
312
35.192
21.935
29.912
1.00
14.56
A


ATOM
1917
CD2
LEU
A
312
33.477
21.084
28.289
1.00
14.22
A


ATOM
1918
C
LEU
A
312
34.181
25.189
29.774
1.00
16.61
A


ATOM
1919
O
LEU
A
312
35.402
25.241
29.910
1.00
16.20
A


ATOM
1920
N
VAL
A
313
33.515
25.949
28.908
1.00
16.20
A


ATOM
1921
CA
VAL
A
313
34.207
26.907
28.058
1.00
15.37
A


ATOM
1922
CB
VAL
A
313
33.216
27.648
27.130
1.00
16.42
A


ATOM
1923
CG1
VAL
A
313
33.915
28.796
26.426
1.00
16.93
A


ATOM
1924
CG2
VAL
A
313
32.644
26.672
26.103
1.00
17.88
A


ATOM
1925
C
VAL
A
313
34.960
27.923
28.911
1.00
17.39
A


ATOM
1926
O
VAL
A
313
36.093
28.294
28.591
1.00
18.00
A


ATOM
1927
N
GLU
A
314
34.342
28.364
30.004
1.00
17.61
A


ATOM
1928
CA
GLU
A
314
34.986
29.331
30.885
1.00
20.43
A


ATOM
1929
CB
GLU
A
314
34.009
29.816
31.959
1.00
22.14
A


ATOM
1930
CG
GLU
A
314
32.800
30.550
31.396
1.00
26.52
A


ATOM
1931
CD
GLU
A
314
31.852
31.025
32.478
1.00
31.26
A


ATOM
1932
OE1
GLU
A
314
31.580
30.246
33.417
1.00
33.48
A


ATOM
1933
OE2
GLU
A
314
31.370
32.173
32.387
1.00
34.81
A


ATOM
1934
C
GLU
A
314
36.217
28.721
31.539
1.00
19.15
A


ATOM
1935
O
GLU
A
314
37.134
29.433
31.934
1.00
21.47
A


ATOM
1936
N
LYS
A
315
36.245
27.400
31.651
1.00
19.51
A


ATOM
1937
CA
LYS
A
315
37.394
26.749
32.258
1.00
19.17
A


ATOM
1938
CB
LYS
A
315
36.946
25.514
33.043
1.00
18.84
A


ATOM
1939
CG
LYS
A
315
36.280
25.885
34.368
1.00
19.62
A


ATOM
1940
CD
LYS
A
315
35.653
24.696
35.073
1.00
19.22
A


ATOM
1941
CE
LYS

315
35.070
25.095
36.427
0.50
21.00
AC1


ATOM
1942
NZ
LYS

315
36.119
25.552
37.381
0.50
19.53
AC1


ATOM
1943
C
LYS
A
315
38.452
26.393
31.218
1.00
18.96
A


ATOM
1944
O
LYS
A
315
39.511
25.873
31.561
1.00
19.85
A


ATOM
1945
N
LEU
A
316
38.164
26.691
29.950
1.00
17.08
A


ATOM
1946
CA
LEU
A
316
39.102
26.429
28.854
1.00
16.41
A


ATOM
1947
CB
LEU
A
316
38.414
25.636
27.738
1.00
13.81
A


ATOM
1948
CG
LEU
A
316
38.028
24.201
28.115
1.00
14.39
A


ATOM
1949
CD1
LEU
A
316
37.139
23.597
27.031
1.00
12.38
A


ATOM
1950
CD2
LEU
A
316
39.302
23.373
28.309
1.00
12.77
A


ATOM
1951
C
LEU
A
316
39.652
27.743
28.290
1.00
17.12
A


ATOM
1952
O
LEU
A
316
40.851
27.860
28.023
1.00
16.53
A


ATOM
1953
N
LEU
A
317
38.780
28.729
28.105
1.00
16.27
A


ATOM
1954
CA
LEU
A
317
39.228
30.022
27.596
1.00
17.52
A


ATOM
1955
CB
LEU
A
317
38.083
30.752
26.887
1.00
16.37
A


ATOM
1956
CG
LEU
A
317
37.448
29.973
25.727
1.00
18.81
A


ATOM
1957
CD1
LEU
A
317
36.415
30.851
25.018
1.00
16.47
A


ATOM
1958
CD2
LEU
A
317
38.528
29.526
24.741
1.00
17.87
A


ATOM
1959
C
LEU
A
317
39.745
30.841
28.774
1.00
18.27
A


ATOM
1960
O
LEU
A
317
39.078
31.753
29.273
1.00
18.58
A


ATOM
1961
N
VAL
A
318
40.937
30.475
29.229
1.00
18.02
A


ATOM
1962
CA
VAL
A
318
41.593
31.141
30.342
1.00
18.85
A


ATOM
1963
CB
VAL
A
318
41.846
30.153
31.500
1.00
19.91
A


ATOM
1964
CG1
VAL
A
318
42.590
30.848
32.634
1.00
20.01
A


ATOM
1965
CG2
VAL
A
318
40.520
29.584
31.990
1.00
19.44
A


ATOM
1966
C
VAL
A
318
42.923
31.657
29.811
1.00
19.67
A


ATOM
1967
O
VAL
A
318
43.690
30.902
29.208
1.00
18.26
A


ATOM
1968
N
LEU
A
319
43.197
32.939
30.028
1.00
20.07
A


ATOM
1969
CA
LEU
A
319
44.436
33.533
29.538
1.00
20.98
A


ATOM
1970
CB
LEU
A
319
44.521
35.002
29.968
1.00
21.64
A


ATOM
1971
CG
LEU
A
319
43.418
35.908
29.408
1.00
24.38
A


ATOM
1972
CD1
LEU
A
319
43.606
37.332
29.935
1.00
23.28
A


ATOM
1973
CD2
LEU
A
319
43.453
35.887
27.875
1.00
24.33
A


ATOM
1974
C
LEU
A
319
45.680
32.774
29.994
1.00
20.38
A


ATOM
1975
O
LEU
A
319
46.568
32.496
29.192
1.00
21.34
A


ATOM
1976
N
ASP
A
320
45.742
32.440
31.280
1.00
20.22
A


ATOM
1977
CA
ASP
A
320
46.879
31.707
31.833
1.00
20.90
A


ATOM
1978
CB
ASP
A
320
46.842
31.760
33.365
1.00
20.76
A


ATOM
1979
CG
ASP
A
320
48.049
31.102
34.004
1.00
21.51
A


ATOM
1980
OD1
ASP
A
320
48.669
30.226
33.367
1.00
23.46
A


ATOM
1981
OD2
ASP
A
320
48.371
31.450
35.159
1.00
23.89
A


ATOM
1982
C
ASP
A
320
46.814
30.247
31.367
1.00
20.06
A


ATOM
1983
O
ASP
A
320
45.988
29.476
31.840
1.00
20.54
A


ATOM
1984
N
ALA
A
321
47.700
29.876
30.451
1.00
20.68
A


ATOM
1985
CA
ALA
A
321
47.733
28.522
29.903
1.00
22.04
A


ATOM
1986
CB
ALA
A
321
48.860
28.411
28.881
1.00
20.75
A


ATOM
1987
C
ALA
A
321
47.858
27.400
30.940
1.00
21.62
A


ATOM
1988
O
ALA
A
321
47.482
26.259
30.665
1.00
21.99
A


ATOM
1989
N
THR
A
322
48.372
27.715
32.127
1.00
20.89
A


ATOM
1990
CA
THR
A
322
48.531
26.698
33.167
1.00
20.82
A


ATOM
1991
CB
THR
A
322
49.670
27.051
34.146
1.00
19.47
A


ATOM
1992
OG1
THR
A
322
49.341
28.253
34.848
1.00
20.19
A


ATOM
1993
CG2
THR
A
322
50.981
27.249
33.394
1.00
21.59
A


ATOM
1994
C
THR
A
322
47.264
26.498
33.983
1.00
19.55
A


ATOM
1995
O
THR
A
322
47.235
25.673
34.894
1.00
21.13
A


ATOM
1996
N
LYS
A
323
46.216
27.248
33.661
1.00
19.33
A


ATOM
1997
CA
LYS
A
323
44.962
27.122
34.392
1.00
21.20
A


ATOM
1998
CB
LYS
A
323
44.580
28.460
35.030
1.00
23.75
A


ATOM
1999
CG
LYS
A
323
45.562
28.933
36.084
1.00
28.45
A


ATOM
2000
CD
LYS
A
323
45.055
30.177
36.799
1.00
33.76
A


ATOM
2001
CE
LYS
A
323
46.087
30.678
37.802
1.00
36.15
A


ATOM
2002
NZ
LYS
A
323
46.532
29.569
38.693
1.00
37.34
A


ATOM
2003
C
LYS
A
323
43.806
26.614
33.539
1.00
20.68
A


ATOM
2004
O
LYS
A
323
42.649
26.757
33.915
1.00
20.42
A


ATOM
2005
N
ARG
A
324
44.114
26.019
32.392
1.00
19.97
A


ATOM
2006
CA
ARG
A
324
43.060
25.494
31.531
1.00
17.98
A


ATOM
2007
CB
ARG
A
324
43.461
25.609
30.061
1.00
15.95
A


ATOM
2008
CG
ARG
A
324
43.534
27.050
29.603
1.00
17.34
A


ATOM
2009
CD
ARG
A
324
43.996
27.194
28.172
1.00
19.80
A


ATOM
2010
NE
ARG
A
324
44.438
28.565
27.944
1.00
16.93
A


ATOM
2011
CZ
ARG
A
324
45.410
28.908
27.108
1.00
19.88
A


ATOM
2012
NH1
ARG
A
324
46.045
27.978
26.398
1.00
14.58
A


ATOM
2013
NH2
ARG
A
324
45.774
30.181
27.015
1.00
16.51
A


ATOM
2014
C
ARG
A
324
42.762
24.046
31.883
1.00
18.32
A


ATOM
2015
O
ARG
A
324
43.673
23.222
32.006
1.00
18.20
A


ATOM
2016
N
LEU
A
325
41.479
23.748
32.055
1.00
18.32
A


ATOM
2017
CA
LEU
A
325
41.050
22.403
32.395
1.00
17.79
A


ATOM
2018
CB
LEU
A
325
39.523
22.335
32.425
1.00
17.03
A


ATOM
2019
CG
LEU
A
325
38.896
21.125
33.116
1.00
15.91
A


ATOM
2020
CD1
LEU
A
325
39.392
21.048
34.557
1.00
15.93
A


ATOM
2021
CD2
LEU
A
325
37.375
21.255
33.084
1.00
16.56
A


ATOM
2022
C
LEU
A
325
41.599
21.433
31.356
1.00
18.68
A


ATOM
2023
O
LEU
A
325
41.347
21.586
30.157
1.00
18.28
A


ATOM
2024
N
GLY
A
326
42.354
20.439
31.821
1.00
18.18
A


ATOM
2025
CA
GLY
A
326
42.931
19.462
30.915
1.00
16.36
A


ATOM
2026
C
GLY
A
326
44.443
19.558
30.807
1.00
19.15
A


ATOM
2027
O
GLY
A
326
45.093
18.592
30.404
1.00
19.52
A


ATOM
2028
N
CYS
A
327
45.016
20.708
31.161
1.00
18.16
A


ATOM
2029
CA
CYS
A
327
46.463
20.867
31.075
1.00
19.30
A


ATOM
2030
CB
CYS
A
327
46.856
22.350
31.058
1.00
20.22
A


ATOM
2031
SG
CYS
A
327
46.782
23.200
32.649
1.00
21.97
A


ATOM
2032
C
CYS
A
327
47.169
20.157
32.228
1.00
20.22
A


ATOM
2033
O
CYS
A
327
46.561
19.828
33.246
1.00
17.92
A


ATOM
2034
N
GLU
A
328
48.463
19.933
32.053
1.00
20.51
A


ATOM
2035
CA
GLU
A
328
49.274
19.244
33.042
1.00
23.34
A


ATOM
2036
CB
GLU
A
328
50.710
19.139
32.507
1.00
28.68
A


ATOM
2037
CG
GLU
A
328
50.754
18.367
31.175
1.00
38.24
A


ATOM
2038
CD
GLU
A
328
52.067
18.500
30.414
1.00
43.23
A


ATOM
2039
OE1
GLU
A
328
52.535
19.643
30.218
1.00
46.22
A


ATOM
2040
0E2
GLU
A
328
52.618
17.459
29.991
1.00
44.90
A


ATOM
2041
C
GLU
A
328
49.234
19.876
34.435
1.00
22.11
A


ATOM
2042
O
GLU
A
328
49.147
19.161
35.437
1.00
20.27
A


ATOM
2043
N
GLU
A
329
49.276
21.204
34.506
1.00
18.40
A


ATOM
2044
CA
GLU
A
329
49.248
21.875
35.801
1.00
20.13
A


ATOM
2045
CB
GLU
A
329
49.587
23.363
35.657
1.00
20.36
A


ATOM
2046
CG
GLU
A
329
51.014
23.651
35.190
1.00
24.05
A


ATOM
2047
CD
GLU
A
329
51.191
23.518
33.688
1.00
25.93
A


ATOM
2048
OE1
GLU
A
329
50.213
23.154
32.995
1.00
26.61
A


ATOM
2049
0E2
GLU
A
329
52.311
23.781
33.198
1.00
27.19
A


ATOM
2050
C
GLU
A
329
47.890
21.718
36.480
1.00
19.36
A


ATOM
2051
O
GLU
A
329
47.775
21.879
37.694
1.00
18.74
A


ATOM
2052
N
MET
A
330
46.863
21.415
35.691
1.00
17.28
A


ATOM
2053
CA
MET
A
330
45.520
21.220
36.229
1.00
16.38
A


ATOM
2054
CB
MET
A
330
44.474
21.833
35.294
1.00
17.65
A


ATOM
2055
CG
MET
A
330
44.460
23.365
35.311
1.00
22.95
A


ATOM
2056
SD
MET
A
330
44.186
24.026
36.979
1.00
26.78
A


ATOM
2057
CE
MET
A
330
42.435
23.712
37.186
1.00
24.69
A


ATOM
2058
C
MET
A
330
45.257
19.730
36.422
1.00
14.30
A


ATOM
2059
O
MET
A
330
44.127
19.304
36.629
1.00
15.39
A


ATOM
2060
N
GLU
A
331
46.327
18.949
36.346
1.00
15.60
A


ATOM
2061
CA
GLU
A
331
46.289
17.501
36.531
1.00
17.08
A


ATOM
2062
CB
GLU
A
331
45.607
17.155
37.862
1.00
17.00
A


ATOM
2063
CG
GLU
A
331
46.070
18.027
39.038
1.00
17.46
A


ATOM
2064
CD
GLU
A
331
47.591
18.179
39.145
1.00
20.16
A


ATOM
2065
OE1
GLU
A
331
48.034
19.073
39.896
1.00
21.39
A


ATOM
2066
0E2
GLU
A
331
48.345
17.420
38.500
1.00
18.87
A


ATOM
2067
C
GLU
A
331
45.697
16.658
35.398
1.00
17.80
A


ATOM
2068
O
GLU
A
331
45.107
15.602
35.636
1.00
20.40
A


ATOM
2069
N
GLY
A
332
45.844
17.133
34.167
1.00
16.23
A


ATOM
2070
CA
GLY
A
332
45.420
16.353
33.015
1.00
14.10
A


ATOM
2071
C
GLY
A
332
43.982
16.154
32.596
1.00
13.54
A


ATOM
2072
O
GLY
A
332
43.063
16.864
33.017
1.00
11.96
A


ATOM
2073
N
TYR
A
333
43.804
15.141
31.750
1.00
14.37
A


ATOM
2074
CA
TYR
A
333
42.510
14.806
31.182
1.00
13.56
A


ATOM
2075
CB
TYR
A
333
42.722
13.892
29.968
1.00
15.00
A


ATOM
2076
CG
TYR
A
333
43.153
14.683
28.752
1.00
16.46
A


ATOM
2077
CD1
TYR
A
333
42.206
15.172
27.849
1.00
15.29
A


ATOM
2078
CEl
TYR
A
333
42.573
16.002
26.794
1.00
13.42
A


ATOM
2079
CD2
TYR
A
333
44.490
15.039
28.561
1.00
14.91
A


ATOM
2080
CE2
TYR
A
333
44.872
15.877
27.499
1.00
14.87
A


ATOM
2081
CZ
TYR
A
333
43.902
16.353
26.626
1.00
15.61
A


ATOM
2082
OH
TYR
A
333
44.244
17.197
25.599
1.00
17.29
A


ATOM
2083
C
TYR
A
333
41.470
14.230
32.127
1.00
15.23
A


ATOM
2084
O
TYR
A
333
40.278
14.323
31.846
1.00
16.63
A


ATOM
2085
N
GLY
A
334
41.907
13.650
33.244
1.00
15.50
A


ATOM
2086
CA
GLY
A
334
40.957
13.100
34.202
1.00
15.07
A


ATOM
2087
C
GLY
A
334
39.925
14.146
34.616
1.00
16.40
A


ATOM
2088
O
GLY
A
334
38.724
13.946
34.433
1.00
15.05
A


ATOM
2089
N
PRO
A
335
40.366
15.278
35.184
1.00
14.96
A


ATOM
2090
CD
PRO
A
335
41.727
15.531
35.689
1.00
15.88
A


ATOM
2091
CA
PRO
A
335
39.444
16.339
35.606
1.00
15.29
A


ATOM
2092
CB
PRO
A
335
40.383
17.397
36.178
1.00
13.19
A


ATOM
2093
CG
PRO
A
335
41.485
16.569
36.758
1.00
13.81
A


ATOM
2094
C
PRO
A
335
38.594
16.877
34.448
1.00
15.84
A


ATOM
2095
O
PRO
A
335
37.423
17.204
34.631
1.00
14.84
A


ATOM
2096
N
LEU
A
336
39.184
16.971
33.257
1.00
16.12
A


ATOM
2097
CA
LEU
A
336
38.450
17.465
32.094
1.00
15.52
A


ATOM
2098
CB
LEU
A
336
39.396
17.653
30.898
1.00
14.39
A


ATOM
2099
CG
LEU
A
336
38.770
17.991
29.538
1.00
15.46
A


ATOM
2100
CD1
LEU
A
336
37.836
19.182
29.662
1.00
11.25
A


ATOM
2101
CD2
LEU
A
336
39.884
18.285
28.528
1.00
14.11
A


ATOM
2102
C
LEU
A
336
37.321
16.508
31.714
1.00
16.28
A


ATOM
2103
O
LEU
A
336
36.176
16.921
31.540
1.00
15.51
A


ATOM
2104
N
LYS
A
337
37.640
15.225
31.592
1.00
17.22
A


ATOM
2105
CA
LYS
A
337
36.624
14.243
31.235
1.00
17.39
A


ATOM
2106
CB
LYS
A
337
37.293
12.900
30.921
1.00
17.68
A


ATOM
2107
CG
LYS
A
337
38.170
12.994
29.676
1.00
22.31
A


ATOM
2108
CD
LYS
A
337
39.213
11.892
29.592
1.00
24.60
A


ATOM
2109
CE
LYS
A
337
38.620
10.560
29.189
1.00
24.76
A


ATOM
2110
NZ
LYS
A
337
39.710
9.560
28.997
1.00
25.05
A


ATOM
2111
C
LYS
A
337
35.577
14.096
32.342
1.00
17.33
A


ATOM
2112
O
LYS
A
337
34.456
13.652
32.090
1.00
14.42
A


ATOM
2113
N
ALA
A
338
35.928
14.500
33.559
1.00
15.83
A


ATOM
2114
CA
ALA
A
338
34.989
14.395
34.674
1.00
17.52
A


ATOM
2115
CB
ALA
A
338
35.749
14.167
35.980
1.00
19.68
A


ATOM
2116
C
ALA
A
338
34.095
15.621
34.804
1.00
18.83
A


ATOM
2117
O
ALA
A
338
33.252
15.687
35.695
1.00
18.94
A


ATOM
2118
N
HIS
A
339
34.262
16.596
33.918
1.00
19.42
A


ATOM
2119
CA
HIS
A
339
33.438
17.796
34.004
1.00
19.28
A


ATOM
2120
CB
HIS
A
339
33.865
18.819
32.949
1.00
19.20
A


ATOM
2121
CG
HIS
A
339
33.163
20.134
33.074
1.00
20.26
A


ATOM
2122
CD2
HIS
A
339
33.549
21.299
33.649
1.00
18.95
A


ATOM
2123
ND1
HIS
A
339
31.880
20.340
32.612
1.00
19.10
A


ATOM
2124
CEl
HIS
A
339
31.506
21.576
32.896
1.00
22.19
A


ATOM
2125
NE2
HIS
A
339
32.500
22.179
33.525
1.00
21.98
A


ATOM
2126
C
HIS
A
339
31.957
17.448
33.845
1.00
19.13
A


ATOM
2127
O
HIS
A
339
31.597
16.576
33.061
1.00
19.52
A


ATOM
2128
N
PRO
A
340
31.079
18.125
34.606
1.00
19.80
A


ATOM
2129
CD
PRO
A
340
31.424
19.119
35.640
1.00
19.08
A


ATOM
2130
CA
PRO
A
340
29.630
17.900
34.569
1.00
20.52
A


ATOM
2131
CB
PRO
A
340
29.091
19.058
35.396
1.00
20.74
A


ATOM
2132
CG
PRO
A
340
30.146
19.207
36.454
1.00
19.20
A


ATOM
2133
C
PRO
A
340
29.000
17.834
33.176
1.00
21.42
A


ATOM
2134
O
PRO
A
340
28.049
17.088
32.955
1.00
22.48
A


ATOM
2135
N
PHE
A
341
29.528
18.606
32.237
1.00
21.33
A


ATOM
2136
CA
PHE
A
341
28.985
18.610
30.886
1.00
21.57
A


ATOM
2137
CB
PHE
A
341
29.739
19.624
30.017
1.00
21.64
A


ATOM
2138
CC
PHE
A
341
29.207
19.740
28.613
1.00
23.18
A


ATOM
2139
CD1
PHE
A
341
27.903
20.171
28.382
1.00
22.58
A


ATOM
2140
CD2
PHE
A
341
30.013
19.431
27.522
1.00
21.95
A


ATOM
2141
CEl
PHE
A
341
27.410
20.292
27.082
1.00
23.54
A


ATOM
2142
CE2
PHE
A
341
29.533
19.548
26.220
1.00
21.83
A


ATOM
2143
CZ
PHE
A
341
28.228
19.980
25.998
1.00
23.23
A


ATOM
2144
C
PHE
A
341
29.055
17.226
30.237
1.00
21.84
A


ATOM
2145
O
PHE
A
341
28.232
16.896
29.389
1.00
20.37
A


ATOM
2146
N
PHE
A
342
30.034
16.422
30.640
1.00
20.51
A


ATOM
2147
CA
PHE
A
342
30.221
15.085
30.077
1.00
23.01
A


ATOM
2148
CB
PHE
A
342
31.710
14.809
29.850
1.00
18.00
A


ATOM
2149
CC
PHE
A
342
32.398
15.812
28.971
1.00
17.05
A


ATOM
2150
CD1
PHE
A
342
32.010
15.987
27.652
1.00
17.78
A


ATOM
2151
CD2
PHE
A
342
33.487
16.534
29.450
1.00
15.72
A


ATOM
2152
CEl
PHE
A
342
32.702
16.867
26.811
1.00
18.08
A


ATOM
2153
CE2
PHE
A
342
34.184
17.414
28.617
1.00
17.45
A


ATOM
2154
CZ
PHE
A
342
33.790
17.578
27.298
1.00
16.56
A


ATOM
2155
C
PHE
A
342
29.679
13.972
30.976
1.00
24.95
A


ATOM
2156
O
PHE
A
342
30.002
12.798
30.777
1.00
23.95
A


ATOM
2157
N
GLU
A
343
28.861
14.333
31.958
1.00
27.35
A


ATOM
2158
CA
GLU
A
343
28.325
13.349
32.897
1.00
30.28
A


ATOM
2159
CB
GLU
A
343
27.187
13.964
33.716
1.00
32.20
A


ATOM
2160
CC
GLU
A
343
26.581
12.991
34.714
1.00
39.71
A


ATOM
2161
CD
GLU
A
343
25.628
13.661
35.688
1.00
44.72
A


ATOM
2162
OE1
GLU
A
343
24.661
14.314
35.234
1.00
47.55
A


ATOM
2163
0E2
GLU
A
343
25.847
13.526
36.911
1.00
46.89
A


ATOM
2164
C
GLU
A
343
27.852
12.017
32.305
1.00
28.98
A


ATOM
2165
O
GLU
A
343
28.225
10.952
32.800
1.00
31.73
A


ATOM
2166
N
SER
A
344
27.037
12.067
31.258
1.00
26.09
A


ATOM
2167
CA
SER
A
344
26.520
10.838
30.656
1.00
28.36
A


ATOM
2168
CB
SER
A
344
25.129
11.089
30.067
1.00
28.73
A


ATOM
2169
OG
SER
A
344
25.203
11.942
28.940
1.00
30.91
A


ATOM
2170
C
SER
A
344
27.407
10.214
29.577
1.00
27.66
A


ATOM
2171
O
SER
A
344
26.987
9.281
28.900
1.00
28.66
A


ATOM
2172
N
VAL
A
345
28.627
10.715
29.419
1.00
26.75
A


ATOM
2173
CA
VAL
A
345
29.534
10.183
28.402
1.00
23.44
A


ATOM
2174
CB
VAL
A
345
30.565
11.256
27.950
1.00
23.10
A


ATOM
2175
CCI
VAL
A
345
31.589
10.631
26.995
1.00
22.24
A


ATOM
2176
CO2
VAL
A
345
29.854
12.418
27.275
1.00
20.05
A


ATOM
2177
C
VAL
A
345
30.326
8.957
28.855
1.00
24.26
A


ATOM
2178
O
VAL
A
345
30.876
8.930
29.960
1.00
22.83
A


ATOM
2179
N
THR
A
346
30.374
7.942
27.997
1.00
21.77
A


ATOM
2180
CA
THR
A
346
31.153
6.740
28.272
1.00
23.70
A


ATOM
2181
CB
THR
A
346
30.391
5.455
27.857
1.00
26.53
A


ATOM
2182
OG1
THR
A
346
29.248
5.284
28.706
1.00
29.98
A


ATOM
2183
CO2
THR
A
346
31.289
4.231
27.990
1.00
24.28
A


ATOM
2184
C
THR
A
346
32.383
6.945
27.385
1.00
23.43
A


ATOM
2185
O
THR
A
346
32.306
6.827
26.160
1.00
24.50
A


ATOM
2186
N
TRP
A
347
33.508
7.270
28.013
1.00
22.98
A


ATOM
2187
CA
TRP
A
347
34.744
7.569
27.300
1.00
23.81
A


ATOM
2188
CB
TRP
A
347
35.683
8.352
28.219
1.00
22.54
A


ATOM
2189
CC
TRP
A
347
35.128
9.658
28.693
1.00
20.61
A


ATOM
2190
CD2
TRP
A
347
35.257
10.927
28.040
1.00
19.11
A


ATOM
2191
CE2
TRP
A
347
34.581
11.881
28.838
1.00
18.39
A


ATOM
2192
CE3
TRP
A
347
35.878
11.351
26.858
1.00
18.16
A


ATOM
2193
CD1
TRP
A
347
34.397
9.883
29.828
1.00
18.35
A


ATOM
2194
NE1
TRP
A
347
34.065
11.218
29.923
1.00
19.51
A


ATOM
2195
CZ2
TRP
A
347
34.510
13.234
28.491
1.00
16.88
A


ATOM
2196
CZ3
TRP
A
347
35.808
12.701
26.511
1.00
17.23
A


ATOM
2197
CH2
TRP
A
347
35.127
13.624
27.327
1.00
18.16
A


ATOM
2198
C
TRP
A
347
35.538
6.429
26.675
1.00
25.79
A


ATOM
2199
O
TRP
A
347
36.304
6.654
25.742
1.00
24.67
A


ATOM
2200
N
ALA
A
348
35.360
5.215
27.183
1.00
27.10
A


ATOM
2201
CA
ALA
A
348
36.116
4.063
26.697
1.00
27.46
A


ATOM
2202
CB
ALA
A
348
35.899
2.869
27.636
1.00
27.09
A


ATOM
2203
C
ALA
A
348
35.895
3.620
25.256
1.00
27.18
A


ATOM
2204
O
ALA
A
348
36.830
3.148
24.613
1.00
29.41
A


ATOM
2205
N
ASN
A
349
34.682
3.769
24.735
1.00
26.55
A


ATOM
2206
CA
ASN
A
349
34.418
3.310
23.375
1.00
27.28
A


ATOM
2207
CB
ASN
A
349
33.700
1.962
23.444
1.00
29.37
A


ATOM
2208
CG
ASN
A
349
32.299
2.088
24.013
1.00
30.92
A


ATOM
2209
ODi
ASN
A
349
32.045
2.942
24.859
1.00
30.17
A


ATOM
2210
ND2
ASN
A
349
31.386
1.237
23.553
1.00
33.52
A


ATOM
2211
C
ASN
A
349
33.599
4.265
22.509
1.00
26.47
A


ATOM
2212
O
ASN
A
349
32.669
3.843
21.819
1.00
25.87
A


ATOM
2213
N
LEU
A
350
33.947
5.543
22.518
1.00
24.45
A


ATOM
2214
CA
LEU
A
350
33.203
6.510
21.721
1.00
23.14
A


ATOM
2215
CB
LEU
A
350
33.837
7.898
21.848
1.00
23.22
A


ATOM
2216
CG
LEU
A
350
33.659
8.605
23.191
1.00
21.05
A


ATOM
2217
CD1
LEU
A
350
34.646
9.756
23.293
1.00
19.36
A


ATOM
2218
CD2
LEU
A
350
32.220
9.094
23.319
1.00
18.78
A


ATOM
2219
C
LEU
A
350
33.082
6.152
20.240
1.00
22.60
A


ATOM
2220
O
LEU
A
350
32.011
6.296
19.650
1.00
21.15
A


ATOM
2221
N
HIS
A
351
34.165
5.689
19.627
1.00
23.13
A


ATOM
2222
CA
HIS
A
351
34.089
5.387
18.204
1.00
27.83
A


ATOM
2223
CB
HIS
A
351
35.506
5.325
17.596
1.00
29.36
A


ATOM
2224
CG
HIS
A
351
36.082
3.950
17.493
1.00
32.07
A


ATOM
2225
CD2
HIS
A
351
36.611
3.128
18.431
1.00
32.39
A


ATOM
2226
ND1
HIS
A
351
36.197
3.285
16.291
1.00
33.02
A


ATOM
2227
CEl
HIS
A
351
36.775
2.113
16.493
1.00
33.58
A


ATOM
2228
NE2
HIS
A
351
37.036
1.992
17.782
1.00
31.76
A


ATOM
2229
C
HIS
A
351
33.258
4.144
17.874
1.00
28.12
A


ATOM
2230
O
HIS
A
351
33.015
3.847
16.707
1.00
29.49
A


ATOM
2231
N
GLN
A
352
32.800
3.442
18.908
1.00
29.28
A


ATOM
2232
CA
GLN
A
352
31.963
2.255
18.726
1.00
29.67
A


ATOM
2233
CB
GLN

352
32.366
1.145
19.694
0.50
30.56
AC1


ATOM
2234
CG
GLN

352
33.169
0.041
19.041
0.50
30.88
AC1


ATOM
2235
CD
GLN

352
34.493
−0.186
19.729
0.50
31.21
AC1


ATOM
2236
OE1
GLN

352
34.541
−0.450
20.928
0.50
30.76
AC1


ATOM
2237
NE2
GLN

352
35.578
−0.084
18.971
0.50
32.30
AC1


ATOM
2238
C
GLN
A
352
30.504
2.638
18.963
1.00
30.42
A


ATOM
2239
O
GLN
A
352
29.595
1.831
18.770
1.00
29.01
A


ATOM
2240
N
GLN
A
353
30.290
3.875
19.397
1.00
27.64
A


ATOM
2241
CA
GLN
A
353
28.948
4.365
19.652
1.00
27.42
A


ATOM
2242
CB
GLN
A
353
28.977
5.401
20.775
1.00
25.77
A


ATOM
2243
CG
GLN
A
353
29.408
4.837
22.115
1.00
27.34
A


ATOM
2244
CD
GLN
A
353
29.638
5.914
23.156
1.00
27.19
A


ATOM
2245
OE1
GLN
A
353
28.875
6.872
23.252
1.00
28.29
A


ATOM
2246
NE2
GLN
A
353
30.687
5.753
23.951
1.00
28.79
A


ATOM
2247
C
GLN
A
353
28.375
4.989
18.385
1.00
29.00
A


ATOM
2248
O
GLN
A
353
29.118
5.455
17.516
1.00
29.14
A


ATOM
2249
N
THR
A
354
27.053
4.984
18.276
1.00
27.31
A


ATOM
2250
CA
THR
A
354
26.390
5.568
17.119
1.00
27.85
A


ATOM
2251
CB
THR
A
354
24.991
4.941
16.904
1.00
30.69
A


ATOM
2252
OG1
THR
A
354
25.132
3.532
16.665
1.00
30.07
A


ATOM
2253
CG2
THR
A
354
24.289
5.585
15.709
1.00
29.58
A


ATOM
2254
C
THR
A
354
26.244
7.062
17.376
1.00
26.85
A


ATOM
2255
O
THR
A
354
25.592
7.475
18.329
1.00
25.77
A


ATOM
2256
N
PRO
A
355
26.867
7.898
16.533
1.00
27.22
A


ATOM
2257
CD
PRO
A
355
27.792
7.588
15.431
1.00
25.89
A


ATOM
2258
CA
PRO
A
355
26.763
9.346
16.734
1.00
27.23
A


ATOM
2259
CB
PRO
A
355
27.625
9.915
15.609
1.00
24.91
A


ATOM
2260
CC
PRO
A
355
28.643
8.838
15.385
1.00
25.54
A


ATOM
2261
C
PRO
A
355
25.322
9.837
16.641
1.00
28.07
A


ATOM
2262
O
PRO
A
355
24.548
9.364
15.810
1.00
27.24
A


ATOM
2263
N
PRO
A
356
24.941
10.792
17.500
1.00
28.28
A


ATOM
2264
CD
PRO
A
356
25.752
11.560
18.462
1.00
28.31
A


ATOM
2265
CA
PRO
A
356
23.572
11.306
17.448
1.00
28.44
A


ATOM
2266
CB
PRO
A
356
23.539
12.301
18.604
1.00
28.11
A


ATOM
2267
CC
PRO
A
356
24.946
12.832
18.612
1.00
26.86
A


ATOM
2268
C
PRO
A
356
23.363
11.978
16.097
1.00
29.25
A


ATOM
2269
O
PRO
A
356
24.304
12.537
15.529
1.00
27.27
A


ATOM
2270
N
ALA
A
357
22.143
11.910
15.575
1.00
30.45
A


ATOM
2271
CA
ALA
A
357
21.848
12.521
14.287
1.00
32.81
A


ATOM
2272
CB
ALA
A
357
20.507
12.019
13.757
1.00
31.99
A


ATOM
2273
C
ALA
A
357
21.824
14.035
14.448
1.00
35.05
A


ATOM
2274
O
ALA
A
357
21.194
14.561
15.369
1.00
35.04
A


ATOM
2275
N
LEU
A
358
22.516
14.730
13.552
1.00
37.81
A


ATOM
2276
CA
LEU
A
358
22.578
16.185
13.597
1.00
42.15
A


ATOM
2277
CB
LEU
A
358
23.679
16.681
12.658
1.00
39.54
A


ATOM
2278
CC
LEU
A
358
25.086
16.285
13.109
1.00
39.51
A


ATOM
2279
CD1
LEU
A
358
26.102
16.686
12.062
1.00
39.29
A


ATOM
2280
CD2
LEU
A
358
25.395
16.953
14.445
1.00
40.01
A


ATOM
2281
C
LEU
A
358
21.241
16.837
13.242
1.00
45.91
A


ATOM
2282
O
LEU
A
358
20.874
16.927
12.069
1.00
45.71
A


ATOM
2283
N
THR
A
359
20.530
17.290
14.275
1.00
50.06
A


ATOM
2284
CA
THR
A
359
19.223
17.939
14.140
1.00
53.73
A


ATOM
2285
CB
THR
A
359
19.353
19.428
13.726
1.00
54.04
A


ATOM
2286
001
THR
A
359
19.995
19.521
12.448
1.00
56.35
A


ATOM
2287
CC2
THR
A
359
20.158
20.204
14.763
1.00
54.32
A


ATOM
2288
C
THR
A
359
18.309
17.236
13.139
1.00
54.47
A


ATOM
2289
O
THR
A
359
18.483
16.016
12.930
1.00
55.90
A


ATOM
2290
OXT
THR
A
359
17.407
17.908
12.595
1.00
56.97
A


ATOM
2291
OH2
TIP
S
1
42.566
19.118
34.302
1.00
15.09
S


ATOM
2292
OH2
TIP
S
2
41.052
32.378
19.857
1.00
15.82
S


ATOM
2293
OH2
TIP
S
3
37.014
33.030
17.747
1.00
16.95
S


ATOM
2294
OH2
TIP
S
5
45.353
24.370
18.152
1.00
16.85
S


ATOM
2295
OH2
TIP
S
6
31.896
13.930
33.235
1.00
20.42
S


ATOM
2296
OH2
TIP
S
7
50.351
22.781
28.249
1.00
21.14
S


ATOM
2297
OH2
TIP
S
8
45.246
−0.589
−0.734
1.00
17.74
S


ATOM
2298
OH2
TIP
S
11
46.249
−0.348
−8.523
1.00
21.32
S


ATOM
2299
OH2
TIP
S
14
45.756
11.148
29.680
1.00
21.94
S


ATOM
2300
OH2
TIP
S
15
44.273
13.157
34.592
1.00
15.61
S


ATOM
2301
OH2
TIP
S
17
53.598
3.722
−1.720
1.00
21.45
S


ATOM
2302
OH2
TIP
S
18
46.049
13.087
31.565
1.00
20.35
S


ATOM
2303
OH2
TIP
S
19
53.422
22.401
−3.280
1.00
23.26
S


ATOM
2304
OH2
TIP
S
20
34.587
7.922
5.383
1.00
22.58
S


ATOM
2305
OH2
TIP
S
21
45.053
27.379
19.376
1.00
29.60
S


ATOM
2306
OH2
TIP
S
23
28.899
36.416
28.633
1.00
31.68
S


ATOM
2307
OH2
TIP
S
24
35.531
11.645
−8.219
1.00
23.45
S


ATOM
2308
OH2
TIP
S
25
47.364
28.787
19.612
1.00
23.03
S


ATOM
2309
OH2
TIP
S
27
48.859
21.588
12.634
1.00
23.76
S


ATOM
2310
OH2
TIP
S
29
48.805
8.920
23.626
1.00
22.23
S


ATOM
2311
OH2
TIP
S
31
48.619
7.247
10.112
1.00
21.32
S


ATOM
2312
OH2
TIP
S
34
44.824
28.720
15.621
1.00
25.27
S


ATOM
2313
OH2
TIP
S
35
26.030
12.634
13.407
1.00
21.61
S


ATOM
2314
OH2
TIP
S
36
50.462
19.810
40.066
1.00
25.45
S


ATOM
2315
OH2
TIP
S
37
39.631
23.510
−0.239
1.00
30.88
S


ATOM
2316
OH2
TIP
S
40
44.734
42.655
10.346
1.00
30.84
S


ATOM
2317
OH2
TIP
S
41
54.653
3.902
1.503
1.00
27.14
S


ATOM
2318
OH2
TIP
S
45
45.693
21.923
39.754
1.00
28.30
S


ATOM
2319
OH2
TIP
S
47
47.820
16.413
7.805
1.00
25.73
S


ATOM
2320
OH2
TIP
S
48
50.292
31.412
29.642
1.00
32.79
S


ATOM
2321
OH2
TIP
S
49
26.056
16.646
34.827
1.00
29.80
S


ATOM
2322
OH2
TIP
S
52
31.714
10.996
31.855
1.00
29.15
S


ATOM
2323
OH2
TIP
S
53
46.108
23.843
−4.299
1.00
24.21
S


ATOM
2324
OH2
TIP
S
54
37.645
11.206
34.448
1.00
28.56
S


ATOM
2325
OH2
TIP
S
55
26.371
28.513
12.142
1.00
32.08
S


ATOM
2326
OH2
TIP
S
58
33.564
19.700
3.483
1.00
28.28
S


ATOM
2327
OH2
TIP
S
64
48.295
−0.632
14.280
1.00
32.13
S


ATOM
2328
OH2
TIP
S
65
40.064
26.036
34.324
1.00
24.17
S


ATOM
2329
OH2
TIP
S
66
29.570
3.958
14.729
1.00
28.94
S


ATOM
2330
OH2
TIP
S
72
60.085
11.604
6.814
1.00
38.35
S


ATOM
2331
OH2
TIP
S
73
39.203
44.403
18.686
1.00
26.61
S


ATOM
2332
OH2
TIP
S
76
47.312
12.366
27.366
1.00
28.51
S


ATOM
2333
OH2
TIP
S
80
43.862
33.771
33.329
1.00
28.82
S


ATOM
2334
OH2
TIP
S
81
57.890
13.106
2.128
1.00
40.62
S


ATOM
2335
OH2
TIP
S
82
41.663
34.381
32.043
1.00
19.35
S


ATOM
2336
OH2
TIP
S
85
50.974
40.331
19.200
1.00
21.14
S


ATOM
2337
OH2
TIP
S
88
47.925
−0.832
−6.556
1.00
24.11
S


ATOM
2338
OH2
TIP
S
90
27.231
28.336
33.481
1.00
27.64
S


ATOM
2339
OH2
TIP
S
91
43.651
−7.101
−7.995
1.00
24.33
S


ATOM
2340
OH2
TIP
S
92
49.325
4.387
19.370
1.00
28.02
S


ATOM
2341
OH2
TIP
S
93
46.231
11.549
33.898
1.00
29.40
S


ATOM
2342
OH2
TIP
S
94
63.889
24.831
1.168
1.00
26.53
S


ATOM
2343
OH2
TIP
S
96
56.396
4.952
−6.749
1.00
28.00
S


ATOM
2344
OH2
TIP
S
98
35.510
27.986
11.558
1.00
29.24
S


ATOM
2345
OH2
TIP
S
100
49.942
24.366
30.265
1.00
31.61
S


ATOM
2346
OH2
TIP
S
101
56.121
7.113
−8.298
1.00
31.57
S


ATOM
2347
OH2
TIP
S
102
58.318
19.957
−8.378
1.00
26.95
S


ATOM
2348
OH2
TIP
S
103
49.647
22.446
39.624
1.00
40.57
S


ATOM
2349
OH2
TIP
S
104
45.359
7.052
13.052
1.00
26.27
S


ATOM
2350
OH2
TIP
S
105
37.150
32.340
32.346
1.00
34.45
S


ATOM
2351
OH2
TIP
S
107
43.465
40.457
8.240
1.00
40.48
S


ATOM
2352
OH2
TIP
S
119
36.644
8.257
13.418
1.00
30.70
S


ATOM
2353
OH2
TIP
S
123
41.912
−8.974
−8.264
1.00
26.08
S


ATOM
2354
OH2
TIP
S
124
62.424
15.800
−7.411
1.00
24.08
S


ATOM
2355
OH2
TIP
S
126
37.266
18.656
−9.097
1.00
28.99
S


ATOM
2356
OH2
TIP
S
127
43.129
26.845
−14.606
1.00
25.19
S


ATOM
2357
OH2
TIP
S
128
36.339
32.639
29.802
1.00
29.25
S


ATOM
2358
OH2
TIP
S
130
54.051
14.561
26.498
1.00
33.93
S


ATOM
2359
OH2
TIP
S
131
41.805
−4.242
5.492
1.00
33.72
S


ATOM
2360
OH2
TIP
S
133
38.873
25.163
36.697
1.00
30.69
S


ATOM
2361
OH2
TIP
S
134
28.777
8.553
25.307
1.00
31.43
S


ATOM
2362
OH2
TIP
S
135
53.672
10.546
−12.803
1.00
33.45
S


ATOM
2363
OH2
TIP
S
136
59.892
15.434
11.467
1.00
31.39
S


ATOM
2364
OH2
TIP
S
137
31.040
12.361
35.470
1.00
34.07
S


ATOM
2365
OH2
TIP
S
139
33.489
14.292
−0.598
1.00
40.68
S


ATOM
2366
OH2
TIP
S
140
46.918
8.748
11.662
1.00
29.23
S


ATOM
2367
OH2
TIP
S
141
46.297
−7.287
−9.196
1.00
42.20
S


ATOM
2368
OH2
TIP
S
142
58.193
6.715
−4.685
1.00
35.48
S


ATOM
2369
OH2
TIP
S
143
44.598
4.435
12.503
1.00
27.68
S


ATOM
2370
OH2
TIP
S
144
27.003
5.999
12.450
1.00
36.30
S


ATOM
2371
OH2
TIP
S
145
43.676
32.852
35.735
1.00
35.70
S


ATOM
2372
OH2
TIP
S
146
35.783
18.628
36.452
1.00
34.62
S


ATOM
2373
OH2
TIP
S
147
25.402
4.058
20.638
1.00
45.03
S


ATOM
2374
OH2
TIP
S
148
45.839
35.853
33.724
1.00
35.47
S


ATOM
2375
OH2
TIP
S
149
22.176
18.976
16.752
1.00
31.87
S


ATOM
2376
OH2
TIP
S
150
43.986
33.179
10.162
1.00
37.70
S


ATOM
2377
OH2
TIP
S
151
50.653
20.347
42.428
1.00
35.80
S


ATOM
2378
OH2
TIP
S
152
47.843
24.314
9.506
1.00
31.05
S


ATOM
2379
OH2
TIP
S
153
44.693
5.273
−14.175
1.00
29.90
S


ATOM
2380
OH2
TIP
S
155
26.560
36.851
31.684
1.00
49.29
S


ATOM
2381
OH2
TIP
S
156
46.867
8.019
−12.951
1.00
29.21
S


ATOM
2382
OH2
TIP
S
157
30.432
28.741
12.438
1.00
37.76
S


ATOM
2383
OH2
TIP
S
158
41.004
20.553
6.423
1.00
39.53
S


ATOM
2384
OH2
TIP
S
159
49.258
20.069
29.294
1.00
33.97
S


ATOM
2385
OH2
TIP
S
160
48.082
28.459
16.489
1.00
33.10
S


ATOM
2386
OH2
TIP
S
161
47.448
18.625
27.683
1.00
34.87
S


ATOM
2387
OH2
TIP
S
162
19.687
20.632
23.411
1.00
35.01
S


ATOM
2388
OH2
TIP
S
163
32.402
−1.266
22.443
1.00
37.26
S


ATOM
2389
OH2
TIP
S
164
39.475
33.468
33.237
1.00
35.34
S


ATOM
2390
OH2
TIP
S
165
44.277
18.950
5.162
1.00
45.14
S


ATOM
2391
OH2
TIP
S
166
34.797
30.523
10.736
1.00
47.55
S


ATOM
2392
OH2
TIP
S
167
46.541
3.526
−14.949
1.00
26.54
S


ATOM
2393
OH2
TIP
S
168
36.333
16.371
1.539
1.00
38.68
S


ATOM
2394
OH2
TIP
S
169
46.761
38.936
27.403
1.00
34.66
S


ATOM
2395
OH2
TIP
S
170
24.163
13.264
11.375
1.00
41.23
S


ATOM
2396
OH2
TIP
S
171
48.459
15.018
31.951
1.00
38.11
S


ATOM
2397
OH2
TIP
S
172
34.261
23.193
40.004
1.00
48.96
S


ATOM
2398
OH2
TIP
S
173
45.924
−0.026
13.224
1.00
39.55
S


ATOM
2399
OH2
TIP
S
175
41.384
37.389
32.543
1.00
40.74
S


ATOM
2400
OH2
TIP
S
177
49.394
35.312
27.150
1.00
44.33
S


ATOM
2401
OH2
TIP
S
178
29.066
29.942
34.359
1.00
41.46
S


ATOM
2402
OH2
TIP
S
180
49.354
19.467
7.273
1.00
34.56
S


ATOM
2403
OH2
TIP
S
181
25.298
17.029
31.863
1.00
47.74
S


ATOM
2404
OH2
TIP
S
182
37.071
25.027
4.669
1.00
43.87
S


ATOM
2405
OH2
TIP
S
183
22.581
7.487
18.691
1.00
41.75
S


ATOM
2406
OH2
TIP
S
184
32.269
7.011
−1.891
1.00
48.84
S


ATOM
2407
OH2
TIP
S
185
48.234
0.494
6.833
1.00
48.16
S


ATOM
2408
OH2
TIP
S
187
20.008
14.658
19.211
1.00
45.27
S


ATOM
2409
OH2
TIP
S
188
49.341
22.698
42.272
1.00
42.20
S


ATOM
2410
OH2
TIP
S
190
61.292
18.260
−8.097
1.00
45.21
S


ATOM
2411
OH2
TIP
S
191
28.152
10.606
2.819
1.00
40.38
S


ATOM
2412
OH2
TIP
S
192
25.626
12.619
23.191
1.00
34.27
S


ATOM
2413
OH2
TIP
S
193
59.876
11.603
1.216
1.00
46.54
S


ATOM
2414
OH2
TIP
S
194
57.592
21.183
−10.646
1.00
45.82
S


ATOM
2415
OH2
TIP
S
195
31.509
36.649
21.499
1.00
38.73
S


ATOM
2416
OH2
TIP
S
197
50.270
−1.543
−6.136
1.00
42.66
S


ATOM
2417
OH2
TIP
S
198
24.467
8.729
13.088
1.00
42.78
S


ATOM
2418
OH2
TIP
S
199
38.098
8.699
25.759
1.00
32.80
S


ATOM
2419
OH2
TIP
S
200
57.831
11.358
−13.255
1.00
45.31
S


ATOM
2420
OH2
TIP
S
201
23.888
22.328
30.524
1.00
37.12
S


ATOM
2421
OH2
TIP
S
202
47.691
26.068
37.666
1.00
37.92
S


ATOM
2422
OH2
TIP
S
203
38.653
7.070
29.307
1.00
50.54
S


ATOM
2423
OH2
TIP
S
206
44.424
27.583
2.092
1.00
53.50
S


ATOM
2424
OH2
TIP
S
212
22.258
2.296
17.948
1.00
47.38
S


ATOM
2425
OH2
TIP
S
214
19.843
17.943
23.303
1.00
30.36
S


ATOM
2426
OH2
TIP
S
216
27.647
11.344
24.681
1.00
31.32
S


ATOM
2427
OH2
TIP
S
217
37.953
7.817
−9.284
1.00
45.97
S


ATOM
2428
OH2
TIP
S
218
33.845
34.040
12.124
1.00
38.11
S


ATOM
2429
OH2
TIP
S
219
58.484
15.269
13.717
1.00
38.26
S


ATOM
2430
OH2
TIP
S
220
48.526
40.920
26.583
1.00
35.23
S


ATOM
2431
OH2
TIP
S
222
52.094
21.184
38.122
1.00
29.86
S


ATOM
2432
OH2
TIP
S
223
36.889
5.881
3.281
1.00
37.63
S


ATOM
2433
OH2
TIP
S
224
47.642
−1.401
−10.684
1.00
34.89
S


ATOM
2434
OH2
TIP
S
226
47.284
2.916
19.133
1.00
34.10
S


ATOM
2435
OH2
TIP
S
227
42.468
4.463
−15.039
1.00
37.98
S


ATOM
2436
OH2
TIP
S
228
19.169
22.832
21.831
1.00
41.57
S


ATOM
2437
OH2
TIP
S
231
57.592
12.689
14.880
1.00
50.22
S


ATOM
2438
OH2
TIP
S
232
27.102
9.176
5.655
1.00
40.57
S


ATOM
2439
OH2
TIP
S
233
58.618
9.072
−11.925
1.00
50.71
S


ATOM
2440
OH2
TIP
S
234
22.822
25.342
19.945
1.00
34.93
S


ATOM
2441
OH2
TIP
S
236
24.831
32.218
28.901
1.00
37.69
S


ATOM
2442
OH2
TIP
S
237
20.045
10.774
16.992
1.00
39.57
S


ATOM
2443
OH2
TIP
S
238
58.019
19.850
15.679
1.00
41.42
S


ATOM
2444
OH2
TIP
S
239
19.490
20.949
26.114
1.00
34.55
S


ATOM
2445
OH2
TIP
S
240
61.187
26.377
7.346
1.00
39.68
S


ATOM
2446
OH2
TIP
S
241
33.680
38.342
19.389
1.00
48.93
S


ATOM
2447
OH2
TIP
S
242
51.539
31.612
10.881
1.00
55.65
S


ATOM
2448
OH2
TIP
S
244
25.872
14.431
30.404
1.00
46.69
S


ATOM
2449
OH2
TIP
S
248
37.332
5.849
9.544
1.00
43.81
S


ATOM
2450
OH2
TIP
S
250
39.087
−1.293
−9.655
1.00
42.96
S


ATOM
2451
OH2
TIP
S
258
23.938
30.000
30.010
1.00
38.89
S


ATOM
2452
OH2
TIP
S
259
24.949
29.749
32.578
1.00
40.17
S


ATOM
2453
OH2
TIP
S
260
32.111
17.986
1.918
1.00
48.36
S


ATOM
2454
OH2
TIP
S
266
21.404
12.876
25.603
1.00
57.17
S


ATOM
2455
OH2
TIP
S
269
35.425
36.767
12.550
1.00
30.70
S


ATOM
2456
OH2
TIP
S
270
52.438
25.529
30.131
1.00
44.85
S


ATOM
2457
OH2
TIP
S
271
53.299
20.156
36.003
1.00
37.15
S


ATOM
2458
OH2
TIP
S
272
50.914
6.919
23.723
1.00
43.29
S


ATOM
2459
OH2
TIP
S
274
31.578
30.795
11.014
1.00
50.15
S


ATOM
2460
OH2
TIP
S
275
26.341
7.243
22.447
1.00
39.40
S


ATOM
2461
OH2
TIP
S
276
60.392
18.195
10.235
1.00
37.91
S


ATOM
2462
OH2
TIP
S
277
47.355
−9.081
−10.821
1.00
48.18
S


ATOM
2463
OH2
TIP
S
279
41.304
6.175
−16.647
1.00
38.12
S


ATOM
2464
OH2
TIP
S
282
33.299
21.620
37.881
1.00
46.29
S


ATOM
2465
OH2
TIP
S
283
56.469
26.112
−8.575
1.00
43.71
S


ATOM
2466
OH2
TIP
S
287
48.382
26.573
7.246
1.00
41.43
S


ATOM
2467
OH2
TIP
S
288
56.240
7.245
−11.331
1.00
41.79
S


ATOM
2468
OH2
TIP
S
290
49.060
14.978
28.166
1.00
37.03
S


ATOM
2469
OH2
TIP
S
291
37.095
44.270
26.442
1.00
45.08
S


ATOM
2470
OH2
TIP
S
292
47.814
−0.384
−13.299
1.00
48.60
S


ATOM
2471
OH2
TIP
S
297
58.081
2.784
−7.841
1.00
41.89
S


ATOM
2472
OH2
TIP
S
298
36.447
45.321
18.644
1.00
54.91
S


ATOM
2473
OH2
TIP
S
299
49.029
23.328
1.767
1.00
30.55
S


ATOM
2474
OH2
TIP
S
301
24.375
13.771
8.634
1.00
48.47
S


ATOM
2475
OH2
TIP
S
303
47.904
36.798
28.653
1.00
35.76
S


ATOM
2476
OH2
TIP
S
305
51.156
40.821
27.172
1.00
43.59
S


ATOM
2477
OH2
TIP
S
306
32.943
28.917
35.227
1.00
42.60
S


ATOM
2478
OH2
TIP
S
307
58.462
28.373
6.251
1.00
46.15
S


ATOM
2479
OH2
TIP
S
308
41.964
30.940
36.712
1.00
48.26
S


ATOM
2480
OH2
TIP
S
313
51.176
−1.922
−3.336
1.00
50.61
S


ATOM
2481
OH2
TIP
S
1001
21.319
36.868
23.805
1.00
36.97
S


ATOM
2482
OH2
TIP
S
1002
48.880
32.620
27.617
1.00
44.40
S


ATOM
2483
OH2
TIP
S
1003
61.880
19.473
11.767
1.00
45.49
S


ATOM
2484
OH2
TIP
S
1004
52.770
21.424
26.815
1.00
24.43
S


ATOM
2485
OH2
TIP
S
1005
35.373
29.094
36.197
1.00
35.97
S


ATOM
2486
OH2
TIP
S
1006
40.815
−6.636
4.389
1.00
43.15
S


ATOM
2487
OH2
TIP
S
1007
44.953
1.286
11.272
1.00
49.45
S


ATOM
2488
OH2
TIP
S
1010
21.004
16.168
27.009
1.00
48.51
S


ATOM
2489
OH2
TIP
S
1011
47.094
41.786
9.243
1.00
50.10
S


ATOM
2490
OH2
TIP
S
1012
32.479
2.978
14.158
1.00
49.47
S


ATOM
2491
O12
GLC
G
1
48.557
11.372
−12.279
1.00
40.72
G


ATOM
2492
C11
GLC
G
1
48.836
12.133
−11.097
1.00
38.05
G


ATOM
2493
C13
GLC
G
1
49.266
13.554
−11.476
1.00
38.09
G


ATOM
2494
O14
GLC
G
1
49.559
14.299
−10.292
1.00
33.99
G


ATOM
2495
C15
GLC
G
1
48.150
14.257
−12.257
1.00
37.32
G


ATOM
2496
O16
GLC
G
1
48.574
15.582
−12.604
1.00
36.74
G


ATOM
2497
O12
GLC
G
2
40.114
−6.634
−6.562
1.00
33.52
G


ATOM
2498
C11
GLC
G
2
38.967
−6.592
−7.404
1.00
31.05
G


ATOM
2499
C13
GLC
G
2
37.712
−6.417
−6.552
1.00
31.56
G


ATOM
2500
O14
GLC
G
2
36.554
−6.406
−7.389
1.00
30.70
G


ATOM
2501
C1S
GLC
G
2
37.792
−5.109
−5.761
1.00
30.03
G


ATOM
2502
O16
GLC
G
2
36.609
−4.961
−4.975
1.00
29.66
G


ATOM
2503
O12
GLC
G
3
44.030
8.243
−13.470
1.00
37.90
G


ATOM
2504
C11
GLC
G
3
43.950
9.648
−13.690
1.00
38.47
G


ATOM
2505
C13
GLC
G
3
42.747
9.974
−14.579
1.00
39.52
G


ATOM
2506
O14
GLC
G
3
41.551
9.526
−13.942
1.00
39.39
G


ATOM
2507
C15
GLC
G
3
42.878
9.280
−15.934
1.00
41.43
G


ATOM
2508
O16
GLC
G
3
41.736
9.613
−16.731
1.00
40.78
G


ATOM
2509
O12
GLC
G
S
40.556
1.005
2.289
1.00
45.25
G


ATOM
2510
C11
GLC
G
S
40.966
2.332
1.960
1.00
40.56
G


ATOM
2511
C13
GLC
G
S
40.187
3.327
2.814
1.00
40.36
G


ATOM
2512
O14
GLC
G
S
38.791
3.169
2.572
1.00
40.71
G


ATOM
2513
CiS
GLC
G
S
40.619
4.751
2.464
1.00
40.04
G


ATOM
2514
O16
GLC
G
S
39.885
5.681
3.256
1.00
36.89
G


ATOM
2515
O12
GLC
G
6
36.951
22.702
40.046
1.00
63.04
G


ATOM
2516
C11
GLC
G
6
37.592
21.583
39.422
1.00
62.46
G


ATOM
2517
C13
GLC
G
6
38.104
21.978
38.030
1.00
61.14
G


ATOM
2518
O14
GLC
G
6
39.034
23.054
38.168
1.00
61.72
G


ATOM
2519
C15
GLC
G
6
36.948
22.429
37.126
1.00
60.51
G


ATOM
2520
O16
GLC
G
6
35.992
21.372
36.960
1.00
58.61
G


ATOM
2521
O12
GLC
G
7
37.316
0.281
14.299
1.00
73.45
G


ATOM
2522
C11
GLC
G
7
37.655
−0.758
15.222
1.00
72.78
G


ATOM
2523
C13
GLC
G
7
36.592
−1.856
15.157
1.00
72.98
G


ATOM
2524
014
GLC
G
7
35.320
−1.299
15.498
1.00
73.88
G


ATOM
2525
C15
GLC
G
7
36.924
−2.989
16.134
1.00
73.66
G


ATOM
2526
O16
GLC
G
7
36.972
−2.493
17.478
1.00
75.38
G


ATOM
2527
O12
GLC
G
8
51.921
21.898
5.908
1.00
62.51
G


ATOM
2528
C11
GLC
G
8
52.447
20.871
5.063
1.00
63.42
G


ATOM
2529
C13
GLC
G
8
51.476
20.597
3.908
1.00
64.28
G


ATOM
2530
O14
GLC
G
8
51.297
21.794
3.150
1.00
66.28
G


ATOM
2531
C15
GLC
G
8
50.121
20.137
4.448
1.00
64.49
G


ATOM
2532
O16
GLC
G
8
49.233
19.886
3.357
1.00
64.01
G


ATOM
2533
O12
GLC
G
10
36.044
37.499
29.523
1.00
56.89
G


ATOM
2534
C11
GLC
G
10
35.164
36.645
30.259
1.00
56.97
G


ATOM
2535
C13
GLC
G
10
33.849
36.489
29.494
1.00
56.11
G


ATOM
2536
O14
GLC
G
10
33.248
37.772
29.308
1.00
56.44
G


ATOM
2537
C15
GLC
G
10
32.900
35.580
30.277
1.00
55.84
G


ATOM
2538
O16
GLC
G
10
31.674
35.442
29.557
1.00
55.39
G


ATOM
2539
O3G
ATP
N
1
46.280
25.658
5.170
1.00
51.49
N


ATOM
2540
PG
ATP
N
1
46.464
25.053
3.691
1.00
52.22
N


ATOM
2541
O1G
ATP
N
1
47.406
23.911
3.763
1.00
51.41
N


ATOM
2542
O2G
ATP
N
1
46.794
26.182
2.784
1.00
52.07
N


ATOM
2543
O3B
ATP
N
1
44.976
24.513
3.344
1.00
51.01
N


ATOM
2544
PB
ATP
N
1
44.560
22.969
3.605
1.00
50.20
N


ATOM
2545
O1B
ATP
N
1
43.083
22.898
3.669
1.00
49.41
N


ATOM
2546
O2B
ATP
N
1
45.345
22.474
4.766
1.00
50.34
N


ATOM
2547
O3A
ATP
N
1
45.070
22.231
2.255
1.00
47.77
N


ATOM
2548
PA
ATP
N
1
45.075
20.613
2.121
1.00
42.84
N


ATOM
2549
O1A
ATP
N
1
45.547
20.291
0.754
1.00
43.81
N


ATOM
2550
O2A
ATP
N
1
45.807
20.035
3.270
1.00
45.03
N


ATOM
2551
O5*
ATP
N
1
43.516
20.223
2.245
1.00
41.73
N


ATOM
2552
C5*
ATP
N
1
42.528
20.925
1.489
1.00
37.57
N


ATOM
2553
C4*
ATP
N
1
41.127
20.379
1.776
1.00
39.45
N


ATOM
2554
O4*
ATP
N
1
40.907
19.024
1.279
1.00
37.72
N


ATOM
2555
C3*
ATP
N
1
40.777
20.321
3.251
1.00
38.48
N


ATOM
2556
O3*
ATP
N
1
40.360
21.615
3.697
1.00
40.42
N


ATOM
2557
C2*
ATP
N
1
39.608
19.374
3.270
1.00
37.58
N


ATOM
2558
O2*
ATP
N
1
38.410
20.076
2.924
1.00
35.98
N


ATOM
2559
C1*
ATP
N
1
39.939
18.346
2.173
1.00
35.55
N


ATOM
2560
N9
ATP
N
1
40.628
17.1S6
2.747
1.00
31.76
N


ATOM
2561
C8
ATP
N
1
41.864
17.126
3.274
1.00
30.49
N


ATOM
2562
N7
ATP
N
1
42.143
15.877
3.667
1.00
29.7S
N


ATOM
2563
C5
ATP
N
1
41.088
15.118
3.390
1.00
27.49
N


ATOM
2564
C4
ATP
N
1
40.125
15.92S
2.810
1.00
30.02
N


ATOM
2565
N3
ATP
N
1
38.937
15.389
2.431
1.00
27.11
N


ATOM
2566
C2
ATP
N
1
38.679
14.085
2.615
1.00
25.62
N


ATOM
2567
N1
ATP
N
1
39.S97
13.283
3.175
1.00
21.76
N


ATOM
2568
C6
ATP
N
1
40.800
13.768
3.571
1.00
23.90
N


ATOM
2569
N6
ATP
N
1
41.698
12.964
4.127
1.00
21.94
N


ATOM
2570
S
SO4
I
1
58.680
8.493
−0.639
1.00
56.05
I


ATOM
2571
O1
SO4
I
1
57.956
7.875
0.483
1.00
58.83
I


ATOM
2572
O2
SO4
I
1
57.886
9.607
−1.188
1.00
57.04
I


ATOM
2573
O3
SO4
I
1
58.906
7.478
−1.683
1.00
57.47
I


ATOM
2574
O4
SO4
I
1
59.976
9.008
−0.156
1.00
57.S1
I


ATOM
2575
S
SO4
I
2
39.339
4.855
7.087
1.00
84.24
I


ATOM
2576
O1
SO4
I
2
39.390
6.175
7.711
1.00
84.02
I


ATOM
2577
O2
SO4
I
2
40.101
4.897
5.797
1.00
84.7S
I


ATOM
2578
O3
SO4
I
2
37.936
4.506
6.766
1.00
84.94
I


ATOM
2579
O4
SO4
I
2
39.931
3.842
7.9S4
1.00
84.44
I


ATOM
2580
S
SO4
I
3
38.987
−2.256
3.310
1.00
58.58
I


ATOM
2581
O1
SO4
I
3
37.734
−1.675
3.827
1.00
59.11
I


ATOM
2582
O2
SO4
I
3
39.460
−1.4S4
2.172
1.00
59.91
I


ATOM
2583
O3
SO4
I
3
38.743
−3.640
2.866
1.00
50.97
I


ATOM
2584
O4
SO4
I
3
40.014
−2.260
4.369
1.00
59.S8
I


ATOM
2585
S
SO4
I
4
34.397
5.289
30.981
1.00
64.34
I


ATOM
2586
O1
SO4
I
4
33.627
6.528
30.742
1.00
60.43
I


ATOM
2587
O2
SO4
I
4
34.337
4.427
29.782
1.00
60.11
I


ATOM
2588
O3
SO4
I
4
33.816
4.572
32.133
1.00
64.39
I


ATOM
2589
O4
SO4
I
4
35.806
S.626
31.277
1.00
63.SS
I


ATOM
2590
S
SO4
I
S
55.074
−6.984
−3.711
1.00
75.40
I


ATOM
2591
O1
SO4
I
S
54.657
−7.S18
−2.399
1.00
74.66
I


ATOM
2592
O2
SO4
I
S
54.209
−5.84S
−4.06S
1.00
74.96
I


ATOM
2593
O3
SO4
I
S
54.9S0
−8.034
−4.742
1.00
74.22
I


ATOM
2594
O4
SO4
I
S
56.477
−6.532
−3.633
1.00
7S.1S
I


ATOM
2595
O2
PO4
P
100
57.362
24.998
13.149
1.00
66.76
P


ATOM
2596
O3
PO4
P
100
59.399
26.166
13.761
1.00
66.89
P


ATOM
2597
O4
PO4
P
100
57.761
25.606
1S.462
1.00
67.43
P


ATOM
2598
O1
PO4
P
100
57.264
27.325
13.818
1.00
6S.91
P


ATOM
2599
P
PO4
P
100
57.947
26.025
14.048
1.00
66.69
P


ATOM
2600
CB
GLU

80
50.411
3.97S
−13.538
0.50
23.31
AC2


ATOM
2601
CG
GLU

80
51.306
4.896
−14.362
0.50
24.09
AC2


ATOM
2602
CD
GLU

80
52.180
5.798
−13.409
0.50
2S.31
AC2


ATOM
2603
OE1
GLU

80
52.841
5.289
−12.580
0.50
22.80
AC2


ATOM
2604
OE2
GLU

80
52.212
7.018
−13.774
0.50
28.07
AC2


ATOM
260S
CB
SER

105
37.582
−1.281
−6.192
0.502
1.16
AC2


ATOM
2606
OG
SER

105
37.127
−1.871
−4.988
0.502
0.42
AC2


ATOM
2607
CB
ARG

116
59.520
22.977
−7.867
0.503
1.00
AC2


ATOM
2608
CG
ARG

116
60.312
24.192
−8.323
0.503
2.50
AC2


ATOM
2609
CD
ARC

116
60.266
24.349
−9.838
0.503
4.11
AC2


ATOM
2610
NE
ARC

116
61.045
25.499
−10.290
0.50
36.67
AC2


ATOM
2611
CZ
ARC

116
60.729
26.766
−10.035
0.50
37.26
AC2


ATOM
2612
NH1
ARC

116
59.642
27.053
−9.331
0.50
38.99
AC2


ATOM
2613
NH2
ARC

116
61.503
27.746
−10.479
0.50
37.83
AC2


ATOM
2614
CB
LEU

145
49.693
8.642
6.631
0.50
15.29
AC2


ATOM
2615
CC
LEU

145
50.783
8.664
5.552
0.50
14.29
AC2


ATOM
2616
CD1
LEU

145
50.264
9.373
4.305
0.50
8.20
AC2


ATOM
2617
CD2
LEU

145
52.030
9.361
6.087
0.50
10.66
AC2


ATOM
2618
CB
ARC

183
27.455
16.155
24.989
0.50
19.21
AC2


ATOM
2619
CC
ARC

183
28.077
15.397
26.147
0.50
18.46
AC2


ATOM
2620
CD
ARC

183
27.002
14.945
27.127
0.50
19.72
AC2


ATOM
2621
NE
ARC

183
26.016
14.086
26.478
0.50
18.79
AC2


ATOM
2622
CZ
ARC

183
24.703
14.279
26.539
0.50
18.52
AC2


ATOM
2623
NH1
ARC

183
24.213
15.305
27.221
0.50
15.35
AC2


ATOM
2624
NH2
ARC

183
23.881
13.445
25.915
0.50
17.55
AC2


ATOM
2625
CB
SER

191
38.479
10.847
23.036
0.50
16.57
AC2


ATOM
2626
OC
SER

191
37.418
10.765
23.973
0.50
18.62
AC2


ATOM
2627
CB
CLU

209
38.645
24.079
8.551
0.50
22.02
AC2


ATOM
2628
CC
CLU

209
37.769
25.296
8.263
0.50
23.40
AC2


ATOM
2629
CD
CLU

209
37.513
26.175
9.483
0.50
24.27
AC2


ATOM
2630
OE1
CLU

209
37.076
27.328
9.288
0.50
25.25
AC2


ATOM
2631
OE2
CLU

209
37.737
25.727
10.629
0.50
20.24
AC2


ATOM
2632
CB
CLN

247
38.598
32.546
14.790
0.50
18.71
AC2


ATOM
2633
CC
CLN

247
38.077
33.665
13.900
0.50
16.95
AC2


ATOM
2634
CD
CLN

247
38.614
33.598
12.479
0.50
19.13
AC2


ATOM
2635
OE1
CLN

247
39.763
33.221
12.246
0.50
17.24
AC2


ATOM
2636
NE2
CLN

247
37.780
33.979
11.520
0.50
19.88
AC2


ATOM
2637
CE
LYS

315
34.978
25.150
36.369
0.50
20.49
AC2


ATOM
2638
NZ
LYS

315
34.183
24.074
37.023
0.50
17.05
AC2


ATOM
2639
CB
CLN

352
32.365
1.170
19.731
0.50
31.10
AC2


ATOM
2640
CC
CLN

352
33.833
0.778
19.683
0.50
32.11
AC2


ATOM
2641
CD
CLN

352
34.190
0.027
18.419
0.50
33.04
AC2


ATOM
2642
OE1
CLN

352
33.906
0.485
17.314
0.50
34.87
AC2


ATOM
2643
NE2
CLN

352
34.819
−1.133
18.575
0.50
32.08
AC2









Example 3
Co-Ordinates for the PDK1 Fragment without Alternate Side Chains













REMARK
coordinates from restrained individual B-factor refinement


REMARK
refinement resolution: 25.0-2.0 A









REMARK
starting
r = 0.1972 free_r = 0.2220


REMARK
final
r = 0.1954 free_r = 0.2224








REMARK
B rmsd for bonded mainchain atoms = 1.501 target = 1.5


REMARK
B rmsd for bonded sidechain atoms = 2.235 target = 2.0


REMARK
B rmsd for angle mainchain atoms = 2.347 target = 2.0


REMARK
B rmsd for angle sidechain atoms = 3.302 target = 2.5


REMARK
rweight = 0.0900 (with wa = 1.29263)


REMARK
target = mlf steps = 30


REMARK
sg = P3(2)21 a = 123.013 b = 123.013 c = 47.624 alpha = 90 beta = 90 gamma = 120


REMARK
parameter file 1: /dd1/david/projects/PDK1_new/CNS/prot.par


REMARK
parameter file 2: /dd1/david/projects/PDK1_new/CNS/atp.par


REMARK
parameter file 3: CNS_TOPPAR:water_rep.param


REMARK
parameter file 4: CNS_TOPPAR:ion.param


REMARK
parameter file 5: /dd1/david/projects/PDK1_new/CNS/glycerol.par


REMARK
molecular structure file: ../generate/alternate.mtf


REMARK
input coordinates: ../minimize/minimize.pdb


REMARK
reflection file = ../../1/hkl/cns.hkl


REMARK
ncs = none


REMARK
B-correction resolution: 6.0-2.0


REMARK
initial B-factor correction applied to fobs:


REMARK
B11 = −2.766 B22 = −2.766 B33 = 5.532


REMARK
B12 = −0.375 B13 =   0.000 B23 = 0.000


REMARK
B-factor correction applied to coordinate array B: 0.031


REMARK
bulk solvent: density level = 0.378441 e/A{circumflex over ( )}3, B-factor = 52.6885 A{circumflex over ( )}2


REMARK
reflections with |Fobs|/sigma_F < 0.0 rejected


REMARK
reflections with |Fobs| > 10000 * rms(Fobs) rejected










REMARK
theoretical total number of refl. in resol. range:
28210
( 100.0% )


REMARK
number of unobserved reflections (no entry or |F| = 0):
568
(  2.0% )


REMARK
number of reflections rejected:
0
(  0.0% )


REMARK
total number of reflections used:
27642
(  98.0% )


REMARK
number of reflections in working set:
27063
(  95.9% )


REMARK
number of reflections in test set:
579
(  2.1% )








CRYST1
123.013 123.013 47.624 90.00 90.00 120.00 P 32 2 1


REMARK
FILENAME = “bindividual.pdb”


REMARK
DATE: 16-Apr-2002 18:31:12   created by user: david


REMARK
VERSION: 1.0


















ATOM
1
CB
PRO
A
71
58.912
−7.251
8.216
1.00
67.78
A


ATOM
2
CG
PRO
A
71
59.621
−6.941
9.534
1.00
69.16
A


ATOM
3
C
PRO
A
71
59.493
−6.506
5.894
1.00
67.06
A


ATOM
4
O
PRO
A
71
59.196
−5.318
5.766
1.00
66.66
A


ATOM
5
N
PRO
A
71
60.984
−6.073
7.833
1.00
67.86
A


ATOM
6
CD
PRO
A
71
60.554
−5.762
9.207
1.00
68.24
A


ATOM
7
CA
PRO
A
71
60.040
−7.035
7.217
1.00
67.75
A


ATOM
8
N
PRO
A
72
59.356
−7.385
4.890
1.00
66.32
A


ATOM
9
CD
PRO
A
72
59.712
−8.816
4.898
1.00
67.17
A


ATOM
10
CA
PRO
A
72
58.840
−6.986
3.578
1.00
65.61
A


ATOM
11
CB
PRO
A
72
58.672
−8.321
2.858
1.00
66.47
A


ATOM
12
CG
PRO
A
72
59.796
−9.133
3.419
1.00
67.57
A


ATOM
13
C
PRO
A
72
57.527
−6.208
3.673
1.00
63.94
A


ATOM
14
O
PRO
A
72
56.710
−6.451
4.561
1.00
64.11
A


ATOM
15
N
ALA
A
73
57.341
−5.268
2.753
1.00
61.57
A


ATOM
16
CA
ALA
A
73
56.133
−4.454
2.708
1.00
58.74
A


ATOM
17
CB
ALA
A
73
56.438
−3.030
3.165
1.00
58.05
A


ATOM
18
C
ALA
A
73
55.626
−4.448
1.271
1.00
56.78
A


ATOM
19
O
ALA
A
73
56.347
−4.834
0.349
1.00
56.95
A


ATOM
20
N
PRO
A
74
54.372
−4.024
1.057
1.00
54.15
A


ATOM
21
CD
PRO
A
74
53.335
−3.610
2.018
1.00
53.31
A


ATOM
22
CA
PRO
A
74
53.856
−4.003
−0.314
1.00
52.54
A


ATOM
23
CB
PRO
A
74
52.474
−3.375
−0.148
1.00
52.86
A


ATOM
24
CG
PRO
A
74
52.067
−3.824
1.226
1.00
52.88
A


ATOM
25
C
PRO
A
74
54.772
−3.167
−1.204
1.00
50.08
A


ATOM
26
O
PRO
A
74
55.559
−2.361
−0.708
1.00
49.96
A


ATOM
27
N
ALA
A
75
54.680
−3.366
−2.514
1.00
47.58
A


ATOM
28
CA
ALA
A
75
55.503
−2.602
−3.446
1.00
44.69
A


ATOM
29
CB
ALA
A
75
55.312
−3.121
−4.870
1.00
46.14
A


ATOM
30
C
ALA
A
75
55.100
−1.134
−3.371
1.00
41.55
A


ATOM
31
O
ALA
A
75
53.947
−0.813
−3.086
1.00
41.01
A


ATOM
32
N
LYS
A
76
56.053
−0.245
−3.619
1.00
38.31
A


ATOM
33
CA
LYS
A
76
55.781
1.184
−3.588
1.00
35.72
A


ATOM
34
CB
LYS
A
76
57.053
1.957
−3.930
1.00
37.70
A


ATOM
35
CG
LYS
A
76
57.123
3.356
−3.350
1.00
40.99
A


ATOM
36
CD
LYS
A
76
57.262
3.316
−1.836
1.00
40.04
A


ATOM
37
CE
LYS
A
76
57.511
4.705
−1.277
1.00
42.08
A


ATOM
38
NZ
LYS
A
76
57.681
4.695
0.202
1.00
42.99
A


ATOM
39
C
LYS
A
76
54.708
1.467
−4.638
1.00
32.65
A


ATOM
40
O
LYS
A
76
54.814
1.005
−5.770
1.00
31.41
A


ATOM
41
N
LYS
A
77
53.668
2.207
−4.270
1.00
28.59
A


ATOM
42
CA
LYS
A
77
52.619
2.517
−5.232
1.00
25.72
A


ATOM
43
CB
LYS
A
77
51.316
2.865
−4.509
1.00
26.22
A


ATOM
44
CG
LYS
A
77
50.796
1.731
−3.631
1.00
27.15
A


ATOM
45
CD
LYS
A
77
49.487
2.089
−2.967
1.00
26.80
A


ATOM
46
CE
LYS
A
77
49.136
1.091
−1.870
1.00
27.31
A


ATOM
47
NZ
LYS
A
77
48.998
−0.296
−2.380
1.00
27.17
A


ATOM
48
C
LYS
A
77
53.053
3.668
−6.137
1.00
24.67
A


ATOM
49
O
LYS
A
77
54.010
4.377
−5.829
1.00
21.60
A


ATOM
50
N
ARG
A
78
52.351
3.838
−7.254
1.00
23.66
A


ATOM
51
CA
ARG
A
78
52.662
4.897
−8.211
1.00
26.14
A


ATOM
52
CB
ARG
A
78
53.574
4.344
−9.318
1.00
28.57
A


ATOM
53
CG
ARG
A
78
53.017
3.139
−10.050
1.00
34.78
A


ATOM
54
CD
ARG
A
78
54.092
2.465
−10.896
1.00
40.96
A


ATOM
55
NE
ARG
A
78
53.560
1.364
−11.700
1.00
48.93
A


ATOM
56
CZ
ARG
A
78
52.985
0.270
−11.203
1.00
52.58
A


ATOM
57
NH1
ARG
A
78
52.860
0.113
−9.889
1.00
54.60
A


ATOM
58
NH2
ARG
A
78
52.530
−0.672
−12.022
1.00
54.09
A


ATOM
59
C
ARG
A
78
51.382
5.488
−8.803
1.00
23.76
A


ATOM
60
O
ARG
A
78
50.311
4.888
−8.706
1.00
24.25
A


ATOM
61
N
PRO
A
79
51.475
6.676
−9.428
1.00
21.76
A


ATOM
62
CD
PRO
A
79
52.691
7.475
−9.668
1.00
20.82
A


ATOM
63
CA
PRO
A
79
50.301
7.325
−10.021
1.00
21.96
A


ATOM
64
CB
PRO
A
79
50.910
8.481
−10.816
1.00
22.27
A


ATOM
65
CG
PRO
A
79
52.124
8.831
−10.014
1.00
22.12
A


ATOM
66
C
PRO
A
79
49.446
6.413
−10.903
1.00
22.86
A


ATOM
67
O
PRO
A
79
48.213
6.461
−10.842
1.00
20.52
A


ATOM
68
N
GLU
A
80
50.103
5.586
−11.714
1.00
21.87
A


ATOM
69
CA
GLU
A
80
49.403
4.685
−12.628
1.00
22.99
A


ATOM
70
CB
GLU
A
80
50.393
3.994
−13.571
1.00
25.24
A


ATOM
71
CG
GLU
A
80
51.230
2.907
−12.925
1.00
28.75
A


ATOM
72
CD
GLU
A
80
52.157
2.224
−13.913
1.00
31.99
A


ATOM
73
OE1
GLU
A
80
53.072
2.897
−14.433
1.00
34.34
A


ATOM
74
OE2
GLU
A
80
51.969
1.015
−14.172
1.00
32.83
A


ATOM
75
C
GLU
A
80
48.556
3.631
−11.912
1.00
22.09
A


ATOM
76
O
GLU
A
80
47.692
3.013
−12.530
1.00
22.37
A


ATOM
77
N
ASP
A
81
48.804
3.413
−10.622
1.00
19.97
A


ATOM
78
CA
ASP
A
81
48.026
2.423
−9.874
1.00
19.93
A


ATOM
79
CB
ASP
A
81
48.736
2.029
−8.571
1.00
21.19
A


ATOM
80
CG
ASP
A
81
50.089
1.380
−8.807
1.00
22.46
A


ATOM
81
OD1
ASP
A
81
50.195
0.554
−9.731
1.00
24.22
A


ATOM
82
OD2
ASP
A
81
51.043
1.685
−8.058
1.00
23.33
A


ATOM
83
C
ASP
A
81
46.652
2.975
−9.518
1.00
20.85
A


ATOM
84
O
ASP
A
81
45.793
2.246
−9.015
1.00
19.96
A


ATOM
85
N
PHE
A
82
46.445
4.258
−9.804
1.00
18.91
A


ATOM
86
CA
PHE
A
82
45.200
4.934
−9.465
1.00
19.30
A


ATOM
87
CB
PHE
A
82
45.475
6.027
−8.427
1.00
18.43
A


ATOM
88
CG
PHE
A
82
46.134
5.531
−7.175
1.00
18.01
A


ATOM
89
CD1
PHE
A
82
45.371
5.136
−6.084
1.00
17.19
A


ATOM
90
CD2
PHE
A
82
47.520
5.460
−7.086
1.00
18.99
A


ATOM
91
CE1
PHE
A
82
45.977
4.676
−4.918
1.00
17.12
A


ATOM
92
CE2
PHE
A
82
48.137
5.000
−5.925
1.00
19.64
A


ATOM
93
CZ
PHE
A
82
47.361
4.607
−4.838
1.00
18.00
A


ATOM
94
C
PHE
A
82
44.476
5.596
−10.621
1.00
20.81
A


ATOM
95
O
PHE
A
82
45.066
5.933
−11.649
1.00
20.34
A


ATOM
96
N
LYS
A
83
43.182
5.792
−10.411
1.00
19.80
A


ATOM
97
CA
LYS
A
83
42.321
6.478
−11.353
1.00
21.65
A


ATOM
98
CB
LYS
A
83
41.096
5.625
−11.687
1.00
22.02
A


ATOM
99
CG
LYS
A
83
40.062
6.326
−12.550
1.00
28.93
A


ATOM
100
CD
LYS
A
83
38.974
5.355
−12.981
1.00
34.20
A


ATOM
101
CE
LYS
A
83
37.909
6.042
−13.824
1.00
38.10
A


ATOM
102
NZ
LYS
A
83
37.179
7.086
−13.043
1.00
43.33
A


ATOM
103
C
LYS
A
83
41.913
7.702
−10.541
1.00
20.74
A


ATOM
104
O
LYS
A
83
41.084
7.606
−9.635
1.00
20.98
A


ATOM
105
N
PHE
A
84
42.513
8.848
−10.835
1.00
19.99
A


ATOM
106
CA
PHE
A
84
42.188
10.049
−10.083
1.00
18.63
A


ATOM
107
CB
PHE
A
84
43.279
11.103
−10.258
1.00
18.95
A


ATOM
108
CG
PHE
A
84
44.571
10.741
−9.587
1.00
17.68
A


ATOM
109
CD1
PHE
A
84
45.498
9.926
−10.224
1.00
18.16
A


ATOM
110
CD2
PHE
A
84
44.843
11.183
−8.299
1.00
19.66
A


ATOM
111
CE1
PHE
A
84
46.676
9.556
−9.589
1.00
18.09
A


ATOM
112
CE2
PHE
A
84
46.021
10.816
−7.653
1.00
18.89
A


ATOM
113
CZ
PHE
A
84
46.936
10.002
−8.301
1.00
17.33
A


ATOM
114
C
PHE
A
84
40.834
10.617
−10.460
1.00
19.69
A


ATOM
115
O
PHE
A
84
40.391
10.489
−11.601
1.00
20.72
A


ATOM
116
N
GLY
A
85
40.178
11.233
−9.484
1.00
16.80
A


ATOM
117
CA
GLY
A
85
38.872
11.810
−9.716
1.00
17.73
A


ATOM
118
C
GLY
A
85
38.819
13.280
−9.346
1.00
18.75
A


ATOM
119
O
GLY
A
85
39.740
14.043
−9.650
1.00
18.45
A


ATOM
120
N
LYS
A
86
37.753
13.673
−8.659
1.00
16.00
A


ATOM
121
CA
LYS
A
86
37.571
15.064
−8.278
1.00
18.26
A


ATOM
122
CB
LYS
A
86
36.133
15.302
−7.812
1.00
19.00
A


ATOM
123
CG
LYS
A
86
35.793
14.660
−6.481
1.00
21.55
A


ATOM
124
CD
LYS
A
86
34.368
14.981
−6.066
1.00
26.48
A


ATOM
125
CE
LYS
A
86
33.994
14.239
−4.793
1.00
31.92
A


ATOM
126
NZ
LYS
A
86
32.568
14.457
−4.412
1.00
35.36
A


ATOM
127
C
LYS
A
86
38.523
15.571
−7.202
1.00
18.57
A


ATOM
128
O
LYS
A
86
39.045
14.807
−6.385
1.00
16.77
A


ATOM
129
N
ILE
A
87
38.737
16.881
−7.227
1.00
17.88
A


ATOM
130
CA
ILE
A
87
39.577
17.554
−6.256
1.00
18.26
A


ATOM
131
CB
ILE
A
87
39.994
18.952
−6.772
1.00
19.60
A


ATOM
132
CG2
ILE
A
87
40.593
19.786
−5.628
1.00
18.73
A


ATOM
133
CG1
ILE
A
87
40.968
18.786
−7.945
1.00
21.16
A


ATOM
134
CD1
ILE
A
87
41.412
20.087
−8.588
1.00
25.26
A


ATOM
135
C
ILE
A
87
38.731
17.709
−4.997
1.00
19.67
A


ATOM
136
O
ILE
A
87
37.628
18.249
−5.052
1.00
20.41
A


ATOM
137
N
LEU
A
88
39.240
17.229
−3.867
1.00
19.15
A


ATOM
138
CA
LEU
A
88
38.508
17.324
−2.611
1.00
20.68
A


ATOM
139
CB
LEU
A
88
38.870
16.151
−1.700
1.00
19.97
A


ATOM
140
CG
LEU
A
88
38.529
14.759
−2.237
1.00
19.24
A


ATOM
141
CD1
LEU
A
88
39.090
13.692
−1.311
1.00
21.41
A


ATOM
142
CD2
LEU
A
88
37.029
14.622
−2.359
1.00
18.84
A


ATOM
143
C
LEU
A
88
38.815
18.632
−1.901
1.00
23.11
A


ATOM
144
O
LEU
A
88
37.999
19.146
−1.139
1.00
25.10
A


ATOM
145
N
GLY
A
89
39.997
19.174
−2.149
1.00
24.09
A


ATOM
146
CA
GLY
A
89
40.367
20.418
−1.507
1.00
24.27
A


ATOM
147
C
GLY
A
89
41.658
20.954
−2.078
1.00
25.47
A


ATOM
148
O
GLY
A
89
42.445
20.202
−2.666
1.00
22.19
A


ATOM
149
N
GLU
A
90
41.870
22.254
−1.906
1.00
26.22
A


ATOM
150
CA
GLU
A
90
43.064
22.924
−2.404
1.00
29.96
A


ATOM
151
CB
GLU
A
90
42.698
23.814
−3.596
1.00
30.75
A


ATOM
152
CG
GLU
A
90
42.267
23.038
−4.831
1.00
34.32
A


ATOM
153
CD
GLU
A
90
41.711
23.930
−5.927
1.00
38.27
A


ATOM
154
OE1
GLU
A
90
40.590
24.456
−5.764
1.00
40.57
A


ATOM
155
OE2
GLU
A
90
42.398
24.110
−6.952
1.00
40.90
A


ATOM
156
C
GLU
A
90
43.711
23.768
−1.313
1.00
30.68
A


ATOM
157
O
GLU
A
90
43.049
24.574
−0.668
1.00
32.83
A


ATOM
158
N
GLY
A
91
45.006
23.566
−1.104
1.00
29.66
A


ATOM
159
CA
GLY
A
91
45.724
24.332
−0.104
1.00
29.40
A


ATOM
160
C
GLY
A
91
46.795
25.151
−0.798
1.00
29.98
A


ATOM
161
O
GLY
A
91
46.894
25.130
−2.028
1.00
28.16
A


ATOM
162
N
SER
A
92
47.605
25.870
−0.029
1.00
28.30
A


ATOM
163
CA
SER
A
92
48.653
26.681
−0.633
1.00
30.50
A


ATOM
164
CB
SER
A
92
49.165
27.717
0.370
1.00
32.43
A


ATOM
165
OG
SER
A
92
49.520
27.099
1.593
1.00
40.94
A


ATOM
166
C
SER
A
92
49.815
25.843
−1.164
1.00
29.77
A


ATOM
167
O
SER
A
92
50.456
26.221
−2.143
1.00
30.46
A


ATOM
168
N
PHE
A
93
50.087
24.703
−0.536
1.00
27.65
A


ATOM
169
CA
PHE
A
93
51.185
23.855
−0.995
1.00
26.34
A


ATOM
170
CB
PHE
A
93
52.281
23.785
0.068
1.00
27.95
A


ATOM
171
CG
PHE
A
93
52.861
25.117
0.406
1.00
31.06
A


ATOM
172
CD1
PHE
A
93
52.283
25.909
1.392
1.00
29.96
A


ATOM
173
CD2
PHE
A
93
53.949
25.613
−0.308
1.00
31.38
A


ATOM
174
CE1
PHE
A
93
52.779
27.181
1.665
1.00
32.69
A


ATOM
175
CE2
PHE
A
93
54.452
26.883
−0.044
1.00
32.63
A


ATOM
176
CZ
PHE
A
93
53.864
27.670
0.945
1.00
31.81
A


ATOM
177
C
PHE
A
93
50.759
22.445
−1.365
1.00
25.39
A


ATOM
178
O
PHE
A
93
51.601
21.559
−1.522
1.00
24.59
A


ATOM
179
N
SER
A
94
49.457
22.235
−1.519
1.00
23.63
A


ATOM
180
CA
SER
A
94
48.965
20.912
−1.860
1.00
21.43
A


ATOM
181
CB
SER
A
94
49.017
20.013
−0.628
1.00
21.42
A


ATOM
182
OG
SER
A
94
48.091
20.475
0.340
1.00
21.19
A


ATOM
183
C
SER
A
94
47.539
20.925
−2.378
1.00
19.82
A


ATOM
184
O
SER
A
94
46.795
21.882
−2.173
1.00
18.76
A


ATOM
185
N
THR
A
95
47.174
19.832
−3.038
1.00
19.38
A


ATOM
186
CA
THR
A
95
45.840
19.637
−3.580
1.00
17.98
A


ATOM
187
CB
THR
A
95
45.818
19.818
−5.110
1.00
19.25
A


ATOM
188
OG1
THR
A
95
46.196
21.162
−5.434
1.00
22.04
A


ATOM
189
CG2
THR
A
95
44.421
19.549
−5.661
1.00
17.61
A


ATOM
190
C
THR
A
95
45.455
18.201
−3.243
1.00
18.61
A


ATOM
191
O
THR
A
95
46.212
17.264
−3.524
1.00
17.10
A


ATOM
192
N
VAL
A
96
44.295
18.024
−2.623
1.00
16.53
A


ATOM
193
CA
VAL
A
96
43.845
16.685
−2.266
1.00
16.05
A


ATOM
194
CB
VAL
A
96
43.170
16.672
−0.886
1.00
16.32
A


ATOM
195
CG1
VAL
A
96
42.741
15.249
−0.532
1.00
18.02
A


ATOM
196
CG2
VAL
A
96
44.145
17.206
0.168
1.00
16.69
A


ATOM
197
C
VAL
A
96
42.875
16.207
−3.335
1.00
16.42
A


ATOM
198
O
VAL
A
96
41.906
16.892
−3.665
1.00
16.47
A


ATOM
199
N
VAL
A
97
43.157
15.033
−3.888
1.00
16.80
A


ATOM
200
CA
VAL
A
97
42.338
14.471
−4.949
1.00
16.72
A


ATOM
201
CB
VAL
A
97
43.153
14.354
−6.255
1.00
18.43
A


ATOM
202
CG1
VAL
A
97
42.249
13.927
−7.404
1.00
19.69
A


ATOM
203
CG2
VAL
A
97
43.831
15.685
−6.569
1.00
17.84
A


ATOM
204
C
VAL
A
97
41.812
13.091
−4.583
1.00
16.77
A


ATOM
205
O
VAL
A
97
42.532
12.270
−4.014
1.00
17.13
A


ATOM
206
N
LEU
A
98
40.545
12.845
−4.895
1.00
16.62
A


ATOM
207
CA
LEU
A
98
39.947
11.548
−4.624
1.00
17.04
A


ATOM
208
CB
LEU
A
98
38.424
11.633
−4.743
1.00
16.89
A


ATOM
209
CG
LEU
A
98
37.635
10.342
−4.508
1.00
19.46
A


ATOM
210
CD1
LEU
A
98
37.990
9.762
−3.146
1.00
20.07
A


ATOM
211
CD2
LEU
A
98
36.143
10.627
−4.588
1.00
17.93
A


ATOM
212
C
LEU
A
98
40.512
10.597
−5.677
1.00
17.38
A


ATOM
213
O
LEU
A
98
40.527
10.920
−6.863
1.00
18.60
A


ATOM
214
N
ALA
A
99
40.995
9.438
−5.246
1.00
17.13
A


ATOM
215
CA
ALA
A
99
41.570
8.466
−6.168
1.00
18.42
A


ATOM
216
CB
ALA
A
99
43.090
8.524
−6.105
1.00
14.76
A


ATOM
217
C
ALA
A
99
41.102
7.055
−5.848
1.00
21.40
A


ATOM
218
O
ALA
A
99
40.941
6.691
−4.679
1.00
22.52
A


ATOM
219
N
ARG
A
100
40.878
6.261
−6.888
1.00
19.77
A


ATOM
220
CA
ARG
A
100
40.459
4.884
−6.693
1.00
20.85
A


ATOM
221
CB
ARG
A
100
39.202
4.585
−7.518
1.00
24.22
A


ATOM
222
CG
ARG
A
100
38.608
3.205
−7.256
1.00
31.78
A


ATOM
223
CD
ARG
A
100
37.326
2.979
−8.048
1.00
36.24
A


ATOM
224
NE
ARG
A
100
36.213
3.818
−7.594
1.00
41.40
A


ATOM
225
CZ
ARG
A
100
35.566
3.662
−6.439
1.00
42.05
A


ATOM
226
NH1
ARG
A
100
35.912
2.696
−5.598
1.00
40.67
A


ATOM
227
NH2
ARG
A
100
34.559
4.468
−6.128
1.00
43.65
A


ATOM
228
C
ARG
A
100
41.613
3.985
−7.129
1.00
18.63
A


ATOM
229
O
ARG
A
100
42.078
4.065
−8.271
1.00
19.49
A


ATOM
230
N
GLU
A
101
42.102
3.157
−6.212
1.00
16.43
A


ATOM
231
CA
GLU
A
101
43.196
2.246
−6.533
1.00
16.11
A


ATOM
232
CB
GLU
A
101
43.774
1.637
−5.248
1.00
16.79
A


ATOM
233
CG
GLU
A
101
44.917
0.657
−5.488
1.00
16.51
A


ATOM
234
CD
GLU
A
101
45.501
0.115
−4.200
1.00
18.20
A


ATOM
235
OE1
GLU
A
101
44.733
−0.081
−3.239
1.00
18.32
A


ATOM
236
OE2
GLU
A
101
46.725
−0.132
−4.150
1.00
17.14
A


ATOM
237
C
GLU
A
101
42.625
1.152
−7.442
1.00
17.92
A


ATOM
238
O
GLU
A
101
41.681
0.462
−7.069
1.00
18.02
A


ATOM
239
N
LEU
A
102
43.198
1.002
−8.632
1.00
19.06
A


ATOM
240
CA
LEU
A
102
42.718
0.025
−9.607
1.00
20.71
A


ATOM
241
CB
LEU
A
102
43.569
0.097
−10.878
1.00
23.42
A


ATOM
242
CG
LEU
A
102
43.531
1.426
−11.642
1.00
25.30
A


ATOM
243
CD1
LEU
A
102
44.577
1.414
−12.748
1.00
27.88
A


ATOM
244
CD2
LEU
A
102
42.140
1.647
−12.214
1.00
26.79
A


ATOM
245
C
LEU
A
102
42.671
−1.418
−9.125
1.00
21.62
A


ATOM
246
O
LEU
A
102
41.668
−2.103
−9.305
1.00
21.09
A


ATOM
247
N
ALA
A
103
43.753
−1.874
−8.507
1.00
19.38
A


ATOM
248
CA
ALA
A
103
43.836
−3.249
−8.035
1.00
20.87
A


ATOM
249
CB
ALA
A
103
45.284
−3.571
−7.671
1.00
19.23
A


ATOM
250
C
ALA
A
103
42.919
−3.629
−6.872
1.00
19.92
A


ATOM
251
O
ALA
A
103
42.703
−4.815
−6.628
1.00
20.38
A


ATOM
252
N
THR
A
104
42.361
−2.643
−6.175
1.00
18.12
A


ATOM
253
CA
THR
A
104
41.517
−2.927
−5.018
1.00
17.15
A


ATOM
254
CB
THR
A
104
42.212
−2.484
−3.717
1.00
19.54
A


ATOM
255
OG1
THR
A
104
42.456
−1.070
−3.773
1.00
19.26
A


ATOM
256
CG2
THR
A
104
43.536
−3.219
−3.529
1.00
17.02
A


ATOM
257
C
THR
A
104
40.159
−2.247
−5.026
1.00
19.44
A


ATOM
258
O
THR
A
104
39.259
−2.648
−4.285
1.00
18.70
A


ATOM
259
N
SER
A
105
40.034
−1.207
−5.847
1.00
19.65
A


ATOM
260
CA
SER
A
105
38.819
−0.400
−5.967
1.00
19.37
A


ATOM
261
CB
SER
A
105
37.598
−1.304
−6.173
1.00
21.81
A


ATOM
262
OG
SER
A
105
36.431
−0.539
−6.412
1.00
23.01
A


ATOM
263
C
SER
A
105
38.644
0.447
−4.701
1.00
18.99
A


ATOM
264
O
SER
A
105
37.602
1.070
−4.488
1.00
18.66
A


ATOM
265
N
ARG
A
106
39.674
0.468
−3.861
1.00
16.84
A


ATOM
266
CA
ARG
A
106
39.655
1.267
−2.634
1.00
16.21
A


ATOM
267
CB
ARG
A
106
40.827
0.886
−1.723
1.00
16.41
A


ATOM
268
CG
ARG
A
106
40.619
−0.367
−0.906
1.00
15.49
A


ATOM
269
CD
ARG
A
106
41.887
−0.755
−0.170
1.00
17.43
A


ATOM
270
NE
ARG
A
106
41.620
−1.792
0.824
1.00
20.47
A


ATOM
271
CZ
ARG
A
106
42.548
−2.568
1.371
1.00
20.24
A


ATOM
272
NH1
ARG
A
106
43.821
−2.433
1.017
1.00
17.80
A


ATOM
273
NH2
ARG
A
106
42.198
−3.468
2.285
1.00
20.14
A


ATOM
274
C
ARG
A
106
39.785
2.746
−2.981
1.00
17.37
A


ATOM
275
O
ARG
A
106
40.514
3.103
−3.902
1.00
17.75
A


ATOM
276
N
GLU
A
107
39.085
3.599
−2.240
1.00
16.06
A


ATOM
277
CA
GLU
A
107
39.156
5.039
−2.461
1.00
20.80
A


ATOM
278
CB
GLU
A
107
37.779
5.694
−2.337
1.00
22.93
A


ATOM
279
CG
GLU
A
107
36.711
5.171
−3.269
1.00
30.87
A


ATOM
280
CD
GLU
A
107
35.431
5.975
−3.148
1.00
32.40
A


ATOM
281
OE1
GLU
A
107
35.262
6.939
−3.923
1.00
33.74
A


ATOM
282
OE2
GLU
A
107
34.608
5.654
−2.263
1.00
36.00
A


ATOM
283
C
GLU
A
107
40.053
5.678
−1.410
1.00
18.93
A


ATOM
284
O
GLU
A
107
39.891
5.427
−0.220
1.00
19.21
A


ATOM
285
N
TYR
A
108
40.988
6.507
−1.852
1.00
16.70
A


ATOM
286
CA
TYR
A
108
41.883
7.209
−0.942
1.00
15.86
A


ATOM
287
CB
TYR
A
108
43.325
6.728
−1.104
1.00
15.30
A


ATOM
288
CG
TYR
A
108
43.593
5.328
−0.612
1.00
16.33
A


ATOM
289
CD1
TYR
A
108
43.765
5.066
0.746
1.00
16.36
A


ATOM
290
CE1
TYR
A
108
44.046
3.769
1.201
1.00
18.48
A


ATOM
291
CD2
TYR
A
108
43.701
4.268
−1.511
1.00
13.25
A


ATOM
292
CE2
TYR
A
108
43.980
2.981
−1.075
1.00
17.28
A


ATOM
293
CZ
TYR
A
108
44.152
2.736
0.276
1.00
19.17
A


ATOM
294
OH
TYR
A
108
44.440
1.461
0.688
1.00
19.38
A


ATOM
295
C
TYR
A
108
41.850
8.687
−1.292
1.00
16.80
A


ATOM
296
O
TYR
A
108
41.560
9.058
−2.431
1.00
15.22
A


ATOM
297
N
ALA
A
109
42.132
9.528
−0.306
1.00
14.61
A


ATOM
298
CA
ALA
A
109
42.207
10.957
−0.539
1.00
14.30
A


ATOM
299
CB
ALA
A
109
41.671
11.726
0.661
1.00
14.78
A


ATOM
300
C
ALA
A
109
43.713
11.136
−0.667
1.00
16.79
A


ATOM
301
O
ALA
A
109
44.450
10.983
0.317
1.00
16.52
A


ATOM
302
N
ILE
A
110
44.182
11.410
−1.881
1.00
14.80
A


ATOM
303
CA
ILE
A
110
45.609
11.574
−2.093
1.00
15.80
A


ATOM
304
CB
ILE
A
110
46.065
10.863
−3.396
1.00
16.85
A


ATOM
305
CG2
ILE
A
110
47.550
11.098
−3.632
1.00
16.80
A


ATOM
306
CG1
ILE
A
110
45.774
9.358
−3.284
1.00
17.76
A


ATOM
307
CD1
ILE
A
110
46.308
8.513
−4.437
1.00
16.07
A


ATOM
308
C
ILE
A
110
46.004
13.045
−2.129
1.00
17.78
A


ATOM
309
O
ILE
A
110
45.534
13.813
−2.976
1.00
16.24
A


ATOM
310
N
LYS
A
111
46.846
13.435
−1.177
1.00
16.15
A


ATOM
311
CA
LYS
A
111
47.326
14.808
−1.100
1.00
17.20
A


ATOM
312
CB
LYS
A
111
47.700
15.176
0.344
1.00
17.41
A


ATOM
313
CG
LYS
A
111
48.350
16.547
0.464
1.00
20.71
A


ATOM
314
CD
LYS
A
111
48.585
16.971
1.910
1.00
24.25
A


ATOM
315
CE
LYS
A
111
47.288
17.381
2.598
1.00
29.46
A


ATOM
316
NZ
LYS
A
111
47.516
17.866
4.000
1.00
30.50
A


ATOM
317
C
LYS
A
111
48.551
14.890
−1.994
1.00
16.41
A


ATOM
318
O
LYS
A
111
49.509
14.137
−1.813
1.00
18.20
A


ATOM
319
N
ILE
A
112
48.509
15.798
−2.963
1.00
15.87
A


ATOM
320
CA
ILE
A
112
49.606
15.967
−3.907
1.00
17.28
A


ATOM
321
CB
ILE
A
112
49.079
15.911
−5.358
1.00
16.43
A


ATOM
322
CG2
ILE
A
112
50.235
15.998
−6.341
1.00
15.12
A


ATOM
323
CG1
ILE
A
112
48.293
14.609
−5.565
1.00
16.82
A


ATOM
324
CD1
ILE
A
112
47.580
14.511
−6.904
1.00
18.47
A


ATOM
325
C
ILE
A
112
50.307
17.301
−3.663
1.00
19.03
A


ATOM
326
O
ILE
A
112
49.669
18.350
−3.635
1.00
19.15
A


ATOM
327
N
LEU
A
113
51.622
17.245
−3.472
1.00
20.22
A


ATOM
328
CA
LEU
A
113
52.416
18.442
−3.214
1.00
22.36
A


ATOM
329
CB
LEU
A
113
52.995
18.397
−1.794
1.00
22.13
A


ATOM
330
CG
LEU
A
113
52.042
18.063
−0.646
1.00
22.46
A


ATOM
331
CD1
LEU
A
113
51.866
16.557
−0.553
1.00
23.81
A


ATOM
332
CD2
LEU
A
113
52.603
18.595
0.660
1.00
23.68
A


ATOM
333
C
LEU
A
113
53.560
18.547
−4.215
1.00
23.37
A


ATOM
334
O
LEU
A
113
54.300
17.586
−4.424
1.00
23.11
A


ATOM
335
N
GLU
A
114
53.706
19.714
−4.834
1.00
23.88
A


ATOM
336
CA
GLU
A
114
54.771
19.920
−5.806
1.00
26.00
A


ATOM
337
CB
GLU
A
114
54.435
21.111
−6.706
1.00
27.74
A


ATOM
338
CG
GLU
A
114
55.533
21.452
−7.696
1.00
35.07
A


ATOM
339
CD
GLU
A
114
55.220
22.696
−8.497
1.00
39.24
A


ATOM
340
OE1
GLU
A
114
54.808
23.703
−7.885
1.00
41.45
A


ATOM
341
OE2
GLU
A
114
55.395
22.670
−9.736
1.00
44.05
A


ATOM
342
C
GLU
A
114
56.087
20.163
−5.067
1.00
24.37
A


ATOM
343
O
GLU
A
114
56.186
21.071
−4.238
1.00
24.43
A


ATOM
344
N
LYS
A
115
57.096
19.350
−5.360
1.00
24.10
A


ATOM
345
CA
LYS
A
115
58.376
19.493
−4.678
1.00
24.93
A


ATOM
346
CB
LYS
A
115
59.339
18.373
−5.103
1.00
23.72
A


ATOM
347
CG
LYS
A
115
59.139
17.080
−4.308
1.00
23.09
A


ATOM
348
CD
LYS
A
115
60.064
15.944
−4.743
1.00
21.92
A


ATOM
349
CE
LYS
A
115
59.691
15.400
−6.117
1.00
22.42
A


ATOM
350
NZ
LYS
A
115
60.447
14.150
−6.448
1.00
19.71
A


ATOM
351
C
LYS
A
115
59.031
20.858
−4.868
1.00
26.87
A


ATOM
352
O
LYS
A
115
59.492
21.469
−3.903
1.00
26.17
A


ATOM
353
N
ARG
A
116
59.058
21.348
−6.102
1.00
28.73
A


ATOM
354
CA
ARG
A
116
59.678
22.638
−6.380
1.00
29.66
A


ATOM
355
CB
ARG
A
116
59.533
22.980
−7.868
1.00
31.29
A


ATOM
356
CG
ARG
A
116
60.047
24.361
−8.267
1.00
33.19
A


ATOM
357
CD
ARG
A
116
61.368
24.710
−7.590
1.00
35.13
A


ATOM
358
NE
ARG
A
116
62.329
23.612
−7.618
1.00
36.42
A


ATOM
359
CZ
ARG
A
116
63.510
23.648
−7.009
1.00
36.18
A


ATOM
360
NH1
ARG
A
116
63.871
24.729
−6.332
1.00
36.12
A


ATOM
361
NH2
ARG
A
116
64.324
22.602
−7.067
1.00
35.77
A


ATOM
362
C
ARG
A
116
59.097
23.761
−5.519
1.00
29.70
A


ATOM
363
O
ARG
A
116
59.843
24.515
−4.889
1.00
29.16
A


ATOM
364
N
HIS
A
117
57.773
23.862
−5.472
1.00
27.22
A


ATOM
365
CA
HIS
A
117
57.126
24.903
−4.681
1.00
26.33
A


ATOM
366
CB
HIS
A
117
55.606
24.835
−4.848
1.00
28.41
A


ATOM
367
CG
HIS
A
117
54.881
26.005
−4.258
1.00
31.82
A


ATOM
368
CD2
HIS
A
117
55.309
27.249
−3.935
1.00
33.19
A


ATOM
369
ND1
HIS
A
117
53.536
25.974
−3.961
1.00
34.30
A


ATOM
370
CE1
HIS
A
117
53.165
27.148
−3.480
1.00
34.58
A


ATOM
371
NE2
HIS
A
117
54.222
27.940
−3.455
1.00
35.18
A


ATOM
372
C
HIS
A
117
57.477
24.780
−3.202
1.00
26.22
A


ATOM
373
O
HIS
A
117
57.737
25.776
−2.534
1.00
25.67
A


ATOM
374
N
ILE
A
118
57.469
23.554
−2.689
1.00
24.94
A


ATOM
375
CA
ILE
A
118
57.792
23.315
−1.285
1.00
23.94
A


ATOM
376
CB
ILE
A
118
57.711
21.812
−0.952
1.00
23.50
A


ATOM
377
CG2
ILE
A
118
58.374
21.533
0.389
1.00
23.76
A


ATOM
378
CG1
ILE
A
118
56.246
21.362
−0.959
1.00
24.42
A


ATOM
379
CD1
ILE
A
118
56.066
19.858
−0.834
1.00
28.06
A


ATOM
380
C
ILE
A
118
59.195
23.821
−0.958
1.00
23.78
A


ATOM
381
O
ILE
A
118
59.402
24.495
0.048
1.00
23.49
A


ATOM
382
N
ILE
A
119
60.153
23.489
−1.815
1.00
23.46
A


ATOM
383
CA
ILE
A
119
61.534
23.913
−1.619
1.00
25.13
A


ATOM
384
CB
ILE
A
119
62.467
23.250
−2.664
1.00
24.25
A


ATOM
385
CG2
ILE
A
119
63.858
23.890
−2.617
1.00
22.47
A


ATOM
386
CG1
ILE
A
119
62.540
21.738
−2.395
1.00
25.05
A


ATOM
387
CD1
ILE
A
119
63.327
20.945
−3.439
1.00
24.62
A


ATOM
388
C
ILE
A
119
61.667
25.435
−1.705
1.00
25.96
A


ATOM
389
O
ILE
A
119
62.330
26.051
−0.872
1.00
24.78
A


ATOM
390
N
LYS
A
120
61.028
26.039
−2.704
1.00
27.67
A


ATOM
391
CA
LYS
A
120
61.100
27.489
−2.879
1.00
30.29
A


ATOM
392
CB
LYS
A
120
60.242
27.940
−4.060
1.00
32.34
A


ATOM
393
CG
LYS
A
120
60.674
27.407
−5.409
1.00
39.30
A


ATOM
394
CD
LYS
A
120
59.765
27.950
−6.512
1.00
45.19
A


ATOM
395
CE
LYS
A
120
58.294
27.636
−6.218
1.00
46.48
A


ATOM
396
NZ
LYS
A
120
57.363
28.155
−7.252
1.00
46.49
A


ATOM
397
C
LYS
A
120
60.647
28.247
−1.638
1.00
30.89
A


ATOM
398
O
LYS
A
120
61.303
29.198
−1.217
1.00
32.48
A


ATOM
399
N
GLU
A
121
59.527
27.825
−1.055
1.00
29.82
A


ATOM
400
CA
GLU
A
121
58.986
28.488
0.128
1.00
30.33
A


ATOM
401
CB
GLU
A
121
57.455
28.416
0.117
1.00
33.04
A


ATOM
402
CG
GLU
A
121
56.794
29.021
−1.120
1.00
36.45
A


ATOM
403
CD
GLU
A
121
57.221
30.456
−1.373
1.00
39.88
A


ATOM
404
OE1
GLU
A
121
57.200
31.264
−0.420
1.00
40.53
A


ATOM
405
OE2
GLU
A
121
57.573
30.778
−2.529
1.00
43.24
A


ATOM
406
C
GLU
A
121
59.511
27.930
1.451
1.00
30.37
A


ATOM
407
O
GLU
A
121
58.946
28.204
2.513
1.00
31.24
A


ATOM
408
N
ASN
A
122
60.588
27.151
1.390
1.00
29.03
A


ATOM
409
CA
ASN
A
122
61.183
26.573
2.594
1.00
28.46
A


ATOM
410
CB
ASN
A
122
61.836
27.673
3.436
1.00
31.28
A


ATOM
411
CG
ASN
A
122
62.945
28.395
2.698
1.00
34.12
A


ATOM
412
OD1
ASN
A
122
62.697
29.143
1.754
1.00
35.57
A


ATOM
413
ND2
ASN
A
122
64.181
28.169
3.127
1.00
35.73
A


ATOM
414
C
ASN
A
122
60.157
25.835
3.456
1.00
26.89
A


ATOM
415
O
ASN
A
122
60.085
26.055
4.663
1.00
27.23
A


ATOM
416
N
LYS
A
123
59.375
24.955
2.842
1.00
23.99
A


ATOM
417
CA
LYS
A
123
58.358
24.210
3.574
1.00
22.43
A


ATOM
418
CB
LYS
A
123
57.031
24.248
2.810
1.00
21.97
A


ATOM
419
CG
LYS
A
123
56.475
25.645
2.599
1.00
25.68
A


ATOM
420
CD
LYS
A
123
56.253
26.354
3.927
1.00
27.54
A


ATOM
421
CE
LYS
A
123
55.822
27.796
3.716
1.00
31.30
A


ATOM
422
NZ
LYS
A
123
55.756
28.540
5.004
1.00
33.21
A


ATOM
423
C
LYS
A
123
58.748
22.759
3.821
1.00
22.20
A


ATOM
424
O
LYS
A
123
57.924
21.960
4.264
1.00
22.50
A


ATOM
425
N
VAL
A
124
59.997
22.412
3.535
1.00
20.59
A


ATOM
426
CA
VAL
A
124
60.439
21.039
3.730
1.00
20.25
A


ATOM
427
CB
VAL
A
124
61.922
20.850
3.328
1.00
19.43
A


ATOM
428
CG1
VAL
A
124
62.346
19.407
3.573
1.00
18.69
A


ATOM
429
CG2
VAL
A
124
62.104
21.195
1.853
1.00
18.21
A


ATOM
430
C
VAL
A
124
60.236
20.561
5.163
1.00
19.53
A


ATOM
431
O
VAL
A
124
59.841
19.418
5.385
1.00
20.02
A


ATOM
432
N
PRO
A
125
60.513
21.422
6.159
1.00
20.01
A


ATOM
433
CD
PRO
A
125
61.178
22.738
6.118
1.00
18.69
A


ATOM
434
CA
PRO
A
125
60.318
20.979
7.544
1.00
19.88
A


ATOM
435
CB
PRO
A
125
60.793
22.180
8.363
1.00
19.95
A


ATOM
436
CG
PRO
A
125
61.839
22.805
7.479
1.00
18.85
A


ATOM
437
C
PRO
A
125
58.848
20.642
7.824
1.00
19.76
A


ATOM
438
O
PRO
A
125
58.544
19.700
8.550
1.00
16.99
A


ATOM
439
N
TYR
A
126
57.947
21.418
7.235
1.00
18.98
A


ATOM
440
CA
TYR
A
126
56.516
21.220
7.435
1.00
21.97
A


ATOM
441
CB
TYR
A
126
55.752
22.448
6.933
1.00
25.17
A


ATOM
442
CG
TYR
A
126
56.040
23.690
7.748
1.00
30.98
A


ATOM
443
CD1
TYR
A
126
55.438
23.886
8.991
1.00
33.95
A


ATOM
444
CE1
TYR
A
126
55.721
25.015
9.763
1.00
36.60
A


ATOM
445
CD2
TYR
A
126
56.938
24.657
7.292
1.00
35.43
A


ATOM
446
CE2
TYR
A
126
57.231
25.792
8.058
1.00
37.20
A


ATOM
447
CZ
TYR
A
126
56.618
25.962
9.291
1.00
37.40
A


ATOM
448
OH
TYR
A
126
56.903
27.073
10.052
1.00
40.85
A


ATOM
449
C
TYR
A
126
55.990
19.956
6.762
1.00
21.35
A


ATOM
450
O
TYR
A
126
55.265
19.175
7.383
1.00
20.49
A


ATOM
451
N
VAL
A
127
56.354
19.746
5.501
1.00
18.16
A


ATOM
452
CA
VAL
A
127
55.892
18.562
4.790
1.00
17.58
A


ATOM
453
CB
VAL
A
127
56.308
18.596
3.308
1.00
17.45
A


ATOM
454
CG1
VAL
A
127
55.786
17.350
2.600
1.00
17.97
A


ATOM
455
CG2
VAL
A
127
55.751
19.850
2.641
1.00
14.90
A


ATOM
456
C
VAL
A
127
56.459
17.306
5.448
1.00
18.39
A


ATOM
457
O
VAL
A
127
55.769
16.298
5.583
1.00
18.14
A


ATOM
458
N
THR
A
128
57.716
17.381
5.869
1.00
17.50
A


ATOM
459
CA
THR
A
128
58.375
16.260
6.530
1.00
18.54
A


ATOM
460
CB
THR
A
128
59.861
16.586
6.805
1.00
18.01
A


ATOM
461
OG1
THR
A
128
60.537
16.804
5.559
1.00
21.14
A


ATOM
462
CG2
THR
A
128
60.536
15.446
7.545
1.00
17.95
A


ATOM
463
C
THR
A
128
57.676
15.941
7.856
1.00
19.49
A


ATOM
464
O
THR
A
128
57.438
14.776
8.179
1.00
18.76
A


ATOM
465
N
ARG
A
129
57.345
16.981
8.619
1.00
19.60
A


ATOM
466
CA
ARG
A
129
56.673
16.804
9.904
1.00
20.12
A


ATOM
467
CB
ARG
A
129
56.534
18.144
10.621
1.00
21.33
A


ATOM
468
CG
ARG
A
129
55.948
18.029
12.023
1.00
28.02
A


ATOM
469
CD
ARG
A
129
55.721
19.404
12.597
1.00
31.25
A


ATOM
470
NE
ARG
A
129
56.940
20.205
12.560
1.00
37.78
A


ATOM
471
CZ
ARG
A
129
56.962
21.524
12.391
1.00
40.10
A


ATOM
472
NH1
ARG
A
129
55.828
22.197
12.239
1.00
40.03
A


ATOM
473
NH2
ARG
A
129
58.119
22.170
12.374
1.00
44.58
A


ATOM
474
C
ARG
A
129
55.288
16.186
9.729
1.00
20.08
A


ATOM
475
O
ARG
A
129
54.891
15.305
10.496
1.00
20.40
A


ATOM
476
N
GLU
A
130
54.553
16.654
8.724
1.00
18.79
A


ATOM
477
CA
GLU
A
130
53.222
16.125
8.454
1.00
20.10
A


ATOM
478
CB
GLU
A
130
52.638
16.749
7.183
1.00
19.92
A


ATOM
479
CG
GLU
A
130
51.350
16.087
6.708
1.00
27.85
A


ATOM
480
CD
GLU
A
130
50.581
16.933
5.707
1.00
29.72
A


ATOM
481
OE1
GLU
A
130
51.216
17.528
4.814
1.00
33.46
A


ATOM
482
OE2
GLU
A
130
49.339
16.996
5.807
1.00
30.74
A


ATOM
483
C
GLU
A
130
53.301
14.615
8.295
1.00
19.81
A


ATOM
484
O
GLU
A
130
52.553
13.875
8.935
1.00
18.37
A


ATOM
485
N
ARG
A
131
54.219
14.162
7.447
1.00
20.41
A


ATOM
486
CA
ARG
A
131
54.397
12.735
7.202
1.00
22.45
A


ATOM
487
CB
ARG
A
131
55.442
12.511
6.098
1.00
25.16
A


ATOM
488
CG
ARG
A
131
55.742
11.043
5.840
1.00
28.75
A


ATOM
489
CD
ARG
A
131
56.736
10.837
4.708
1.00
33.75
A


ATOM
490
NE
ARG
A
131
57.020
9.415
4.520
1.00
40.07
A


ATOM
491
CZ
ARG
A
131
57.756
8.915
3.532
1.00
43.07
A


ATOM
492
NH1
ARG
A
131
58.293
9.721
2.625
1.00
44.91
A


ATOM
493
NH2
ARG
A
131
57.955
7.606
3.449
1.00
44.45
A


ATOM
494
C
ARG
A
131
54.820
11.982
8.466
1.00
23.24
A


ATOM
495
O
ARG
A
131
54.241
10.948
8.804
1.00
23.86
A


ATOM
496
N
ASP
A
132
55.831
12.497
9.160
1.00
21.99
A


ATOM
497
CA
ASP
A
132
56.318
11.850
10.370
1.00
22.04
A


ATOM
498
CB
ASP
A
132
57.570
12.564
10.888
1.00
23.72
A


ATOM
499
CG
ASP
A
132
58.750
12.442
9.932
1.00
27.77
A


ATOM
500
OD1
ASP
A
132
58.681
11.620
8.989
1.00
27.34
A


ATOM
501
OD2
ASP
A
132
59.753
13.163
10.128
1.00
28.70
A


ATOM
502
C
ASP
A
132
55.258
11.772
11.474
1.00
21.69
A


ATOM
503
O
ASP
A
132
55.077
10.723
12.092
1.00
22.75
A


ATOM
504
N
VAL
A
133
54.551
12.868
11.725
1.00
19.54
A


ATOM
505
CA
VAL
A
133
53.525
12.843
12.759
1.00
18.52
A


ATOM
506
CB
VAL
A
133
52.908
14.244
12.990
1.00
19.26
A


ATOM
507
CG1
VAL
A
133
51.708
14.135
13.918
1.00
18.79
A


ATOM
508
CG2
VAL
A
133
53.953
15.180
13.604
1.00
18.80
A


ATOM
509
C
VAL
A
133
52.419
11.854
12.398
1.00
19.46
A


ATOM
510
O
VAL
A
133
52.073
10.991
13.200
1.00
19.94
A


ATOM
511
N
MET
A
134
51.878
11.957
11.187
1.00
19.15
A


ATOM
512
CA
MET
A
134
50.807
11.052
10.792
1.00
21.25
A


ATOM
513
CB
MET
A
134
50.309
11.381
9.383
1.00
17.34
A


ATOM
514
CG
MET
A
134
49.615
12.730
9.302
1.00
20.00
A


ATOM
515
SD
MET
A
134
48.643
12.952
7.798
1.00
24.21
A


ATOM
516
CE
MET
A
134
47.033
12.434
8.400
1.00
23.20
A


ATOM
517
C
MET
A
134
51.203
9.582
10.881
1.00
22.43
A


ATOM
518
O
MET
A
134
50.384
8.741
11.249
1.00
23.82
A


ATOM
519
N
SER
A
135
52.454
9.273
10.556
1.00
23.09
A


ATOM
520
CA
SER
A
135
52.939
7.895
10.615
1.00
26.13
A


ATOM
521
CB
SER
A
135
54.356
7.798
10.039
1.00
26.17
A


ATOM
522
OG
SER
A
135
54.383
8.177
8.673
1.00
31.91
A


ATOM
523
C
SER
A
135
52.957
7.358
12.045
1.00
26.58
A


ATOM
524
O
SER
A
135
52.926
6.148
12.261
1.00
26.42
A


ATOM
525
N
ARG
A
136
53.014
8.261
13.018
1.00
25.65
A


ATOM
526
CA
ARG
A
136
53.056
7.870
14.425
1.00
27.47
A


ATOM
527
CB
ARG
A
136
53.823
8.914
15.238
1.00
27.97
A


ATOM
528
CG
ARG
A
136
55.283
9.082
14.857
1.00
32.00
A


ATOM
529
CD
ARG
A
136
55.904
10.218
15.664
1.00
33.03
A


ATOM
530
NE
ARG
A
136
55.602
10.073
17.084
1.00
36.11
A


ATOM
531
CZ
ARG
A
136
55.867
10.990
18.007
1.00
39.74
A


ATOM
532
NH1
ARG
A
136
56.449
12.132
17.661
1.00
40.55
A


ATOM
533
NH2
ARG
A
136
55.540
10.769
19.276
1.00
36.72
A


ATOM
534
C
ARG
A
136
51.667
7.709
15.036
1.00
26.38
A


ATOM
535
O
ARG
A
136
51.516
7.121
16.106
1.00
27.06
A


ATOM
536
N
LEU
A
137
50.655
8.235
14.360
1.00
24.77
A


ATOM
537
CA
LEU
A
137
49.294
8.162
14.870
1.00
24.70
A


ATOM
538
CB
LEU
A
137
48.483
9.363
14.371
1.00
24.52
A


ATOM
539
CG
LEU
A
137
49.050
10.760
14.662
1.00
26.67
A


ATOM
540
CD1
LEU
A
137
48.075
11.813
14.141
1.00
27.25
A


ATOM
541
CD2
LEU
A
137
49.279
10.945
16.155
1.00
27.09
A


ATOM
542
C
LEU
A
137
48.592
6.868
14.473
1.00
25.20
A


ATOM
543
O
LEU
A
137
48.619
6.469
13.309
1.00
25.99
A


ATOM
544
N
ASP
A
138
47.971
6.218
15.451
1.00
21.89
A


ATOM
545
CA
ASP
A
138
47.239
4.977
15.219
1.00
21.35
A


ATOM
546
CB
ASP
A
138
48.124
3.761
15.523
1.00
22.14
A


ATOM
547
CG
ASP
A
138
47.432
2.448
15.201
1.00
24.90
A


ATOM
548
OD1
ASP
A
138
46.631
2.423
14.241
1.00
24.78
A


ATOM
549
OD2
ASP
A
138
47.691
1.443
15.897
1.00
25.39
A


ATOM
550
C
ASP
A
138
46.031
4.991
16.138
1.00
20.47
A


ATOM
551
O
ASP
A
138
45.967
4.248
17.118
1.00
19.06
A


ATOM
552
N
HIS
A
139
45.075
5.852
15.810
1.00
18.27
A


ATOM
553
CA
HIS
A
139
43.869
6.016
16.606
1.00
18.21
A


ATOM
554
CB
HIS
A
139
44.096
7.157
17.612
1.00
15.84
A


ATOM
555
CG
HIS
A
139
42.985
7.332
18.600
1.00
15.24
A


ATOM
556
CD2
HIS
A
139
42.884
6.964
19.900
1.00
13.97
A


ATOM
557
ND1
HIS
A
139
41.791
7.943
18.280
1.00
14.74
A


ATOM
558
CE1
HIS
A
139
41.002
7.944
19.341
1.00
14.19
A


ATOM
559
NE2
HIS
A
139
41.641
7.356
20.336
1.00
14.15
A


ATOM
560
C
HIS
A
139
42.715
6.330
15.654
1.00
18.50
A


ATOM
561
O
HIS
A
139
42.879
7.080
14.693
1.00
20.80
A


ATOM
562
N
PRO
A
140
41.527
5.767
15.913
1.00
18.32
A


ATOM
563
CD
PRO
A
140
41.143
4.984
17.100
1.00
16.71
A


ATOM
564
CA
PRO
A
140
40.367
6.001
15.048
1.00
17.43
A


ATOM
565
CB
PRO
A
140
39.273
5.157
15.704
1.00
16.64
A


ATOM
566
CG
PRO
A
140
39.643
5.204
17.152
1.00
18.43
A


ATOM
567
C
PRO
A
140
39.914
7.441
14.803
1.00
18.77
A


ATOM
568
O
PRO
A
140
39.207
7.695
13.831
1.00
19.88
A


ATOM
569
N
PHE
A
141
40.301
8.381
15.664
1.00
17.14
A


ATOM
570
CA
PHE
A
141
39.874
9.767
15.477
1.00
16.42
A


ATOM
571
CB
PHE
A
141
39.568
10.422
16.836
1.00
14.60
A


ATOM
572
CG
PHE
A
141
38.386
9.817
17.556
1.00
15.26
A


ATOM
573
CD1
PHE
A
141
37.335
9.234
16.842
1.00
14.78
A


ATOM
574
CD2
PHE
A
141
38.297
9.880
18.942
1.00
13.70
A


ATOM
575
CE1
PHE
A
141
36.215
8.727
17.502
1.00
16.94
A


ATOM
576
CE2
PHE
A
141
37.178
9.375
19.615
1.00
15.75
A


ATOM
577
CZ
PHE
A
141
36.135
8.799
18.893
1.00
16.89
A


ATOM
578
C
PHE
A
141
40.857
10.641
14.694
1.00
16.15
A


ATOM
579
O
PHE
A
141
40.799
11.871
14.761
1.00
17.35
A


ATOM
580
N
PHE
A
142
41.748
10.011
13.941
1.00
15.88
A


ATOM
581
CA
PHE
A
142
42.727
10.756
13.154
1.00
17.89
A


ATOM
582
CB
PHE
A
142
44.115
10.645
13.793
1.00
17.57
A


ATOM
583
CG
PHE
A
142
44.240
11.371
15.103
1.00
18.74
A


ATOM
584
CD1
PHE
A
142
44.559
12.726
15.135
1.00
17.77
A


ATOM
585
CD2
PHE
A
142
43.997
10.711
16.304
1.00
18.74
A


ATOM
586
CE1
PHE
A
142
44.632
13.417
16.347
1.00
15.77
A


ATOM
587
CE2
PHE
A
142
44.065
11.393
17.522
1.00
17.56
A


ATOM
588
CZ
PHE
A
142
44.383
12.747
17.542
1.00
17.14
A


ATOM
589
C
PHE
A
142
42.793
10.231
11.729
1.00
19.12
A


ATOM
590
O
PHE
A
142
42.659
9.030
11.504
1.00
20.01
A


ATOM
591
N
VAL
A
143
42.978
11.135
10.769
1.00
18.72
A


ATOM
592
CA
VAL
A
143
43.102
10.735
9.371
1.00
18.52
A


ATOM
593
CB
VAL
A
143
43.294
11.961
8.440
1.00
20.66
A


ATOM
594
CG1
VAL
A
143
43.843
11.521
7.080
1.00
21.29
A


ATOM
595
CG2
VAL
A
143
41.958
12.673
8.252
1.00
22.97
A


ATOM
596
C
VAL
A
143
44.342
9.865
9.330
1.00
18.68
A


ATOM
597
O
VAL
A
143
45.355
10.199
9.943
1.00
18.42
A


ATOM
598
N
LYS
A
144
44.259
8.745
8.623
1.00
18.30
A


ATOM
599
CA
LYS
A
144
45.384
7.824
8.535
1.00
18.78
A


ATOM
600
CB
LYS
A
144
44.889
6.373
8.608
1.00
22.27
A


ATOM
601
CG
LYS
A
144
46.017
5.340
8.557
1.00
29.72
A


ATOM
602
CD
LYS
A
144
45.491
3.912
8.674
1.00
34.16
A


ATOM
603
CE
LYS
A
144
46.631
2.896
8.577
1.00
37.67
A


ATOM
604
NZ
LYS
A
144
46.138
1.484
8.629
1.00
39.02
A


ATOM
605
C
LYS
A
144
46.192
8.002
7.261
1.00
18.53
A


ATOM
606
O
LYS
A
144
45.643
8.314
6.200
1.00
18.18
A


ATOM
607
N
LEU
A
145
47.502
7.816
7.385
1.00
16.79
A


ATOM
608
CA
LEU
A
145
48.411
7.900
6.251
1.00
17.45
A


ATOM
609
CB
LEU
A
145
49.686
8.653
6.641
1.00
18.82
A


ATOM
610
CG
LEU
A
145
50.734
8.902
5.549
1.00
20.23
A


ATOM
611
CD1
LEU
A
145
51.836
9.799
6.093
1.00
18.83
A


ATOM
612
CD2
LEU
A
145
51.317
7.581
5.069
1.00
19.79
A


ATOM
613
C
LEU
A
145
48.739
6.450
5.907
1.00
19.19
A


ATOM
614
O
LEU
A
145
49.451
5.772
6.659
1.00
17.36
A


ATOM
615
N
TYR
A
146
48.215
5.972
4.782
1.00
17.28
A


ATOM
616
CA
TYR
A
146
48.444
4.593
4.358
1.00
17.57
A


ATOM
617
CB
TYR
A
146
47.288
4.098
3.486
1.00
17.74
A


ATOM
618
CG
TYR
A
146
45.981
3.926
4.214
1.00
17.50
A


ATOM
619
CD1
TYR
A
146
45.099
4.995
4.377
1.00
16.50
A


ATOM
620
CE1
TYR
A
146
43.881
4.827
5.039
1.00
17.10
A


ATOM
621
CD2
TYR
A
146
45.620
2.686
4.735
1.00
18.28
A


ATOM
622
CE2
TYR
A
146
44.411
2.506
5.399
1.00
19.84
A


ATOM
623
CZ
TYR
A
146
43.547
3.576
5.544
1.00
17.53
A


ATOM
624
OH
TYR
A
146
42.342
3.376
6.169
1.00
20.67
A


ATOM
625
C
TYR
A
146
49.735
4.376
3.582
1.00
18.72
A


ATOM
626
O
TYR
A
146
50.382
3.338
3.715
1.00
19.51
A


ATOM
627
N
PHE
A
147
50.110
5.350
2.765
1.00
18.09
A


ATOM
628
CA
PHE
A
147
51.307
5.203
1.952
1.00
17.20
A


ATOM
629
CB
PHE
A
147
51.007
4.258
0.783
1.00
16.77
A


ATOM
630
CG
PHE
A
147
49.835
4.699
−0.070
1.00
17.75
A


ATOM
631
CD1
PHE
A
147
49.967
5.752
−0.975
1.00
16.58
A


ATOM
632
CD2
PHE
A
147
48.595
4.075
0.053
1.00
18.07
A


ATOM
633
CE1
PHE
A
147
48.886
6.178
−1.742
1.00
19.62
A


ATOM
634
CE2
PHE
A
147
47.503
4.492
−0.710
1.00
18.56
A


ATOM
635
CZ
PHE
A
147
47.647
5.546
−1.610
1.00
19.27
A


ATOM
636
C
PHE
A
147
51.768
6.533
1.395
1.00
17.13
A


ATOM
637
O
PHE
A
147
51.045
7.528
1.452
1.00
14.43
A


ATOM
638
N
THR
A
148
52.981
6.534
0.854
1.00
17.12
A


ATOM
639
CA
THR
A
148
53.541
7.718
0.232
1.00
17.96
A


ATOM
640
CB
THR
A
148
54.449
8.531
1.197
1.00
21.51
A


ATOM
641
OG1
THR
A
148
55.605
7.760
1.537
1.00
18.83
A


ATOM
642
CG2
THR
A
148
53.700
8.897
2.472
1.00
19.60
A


ATOM
643
C
THR
A
148
54.386
7.262
−0.946
1.00
20.31
A


ATOM
644
O
THR
A
148
54.860
6.124
−0.991
1.00
18.94
A


ATOM
645
N
PHE
A
149
54.543
8.149
−1.916
1.00
19.16
A


ATOM
646
CA
PHE
A
149
55.368
7.877
−3.073
1.00
18.01
A


ATOM
647
CB
PHE
A
149
54.748
6.801
−3.989
1.00
17.23
A


ATOM
648
CG
PHE
A
149
53.389
7.144
−4.544
1.00
16.88
A


ATOM
649
CD1
PHE
A
149
53.262
7.888
−5.712
1.00
18.58
A


ATOM
650
CD2
PHE
A
149
52.235
6.668
−3.927
1.00
17.31
A


ATOM
651
CE1
PHE
A
149
52.007
8.149
−6.267
1.00
19.26
A


ATOM
652
CE2
PHE
A
149
50.972
6.923
−4.470
1.00
19.17
A


ATOM
653
CZ
PHE
A
149
50.858
7.663
−5.642
1.00
19.60
A


ATOM
654
C
PHE
A
149
55.542
9.205
−3.774
1.00
20.85
A


ATOM
655
O
PHE
A
149
54.934
10.200
−3.376
1.00
19.76
A


ATOM
656
N
GLN
A
150
56.398
9.241
−4.782
1.00
19.79
A


ATOM
657
CA
GLN
A
150
56.636
10.481
−5.497
1.00
24.03
A


ATOM
658
CB
GLN
A
150
57.659
11.347
−4.739
1.00
24.45
A


ATOM
659
CG
GLN
A
150
58.986
10.645
−4.414
1.00
26.28
A


ATOM
660
CD
GLN
A
150
59.988
11.558
−3.692
1.00
29.02
A


ATOM
661
OE1
GLN
A
150
60.693
12.353
−4.321
1.00
27.05
A


ATOM
662
NE2
GLN
A
150
60.042
11.449
−2.365
1.00
26.47
A


ATOM
663
C
GLN
A
150
57.160
10.203
−6.885
1.00
23.88
A


ATOM
664
O
GLN
A
150
57.673
9.118
−7.158
1.00
24.79
A


ATOM
665
N
ASP
A
151
56.987
11.171
−7.774
1.00
25.88
A


ATOM
666
CA
ASP
A
151
57.527
11.047
−9.117
1.00
26.49
A


ATOM
667
CB
ASP
A
151
56.437
11.126
−10.199
1.00
24.54
A


ATOM
668
CG
ASP
A
151
55.544
12.336
−10.064
1.00
24.95
A


ATOM
669
OD1
ASP
A
151
56.005
13.379
−9.561
1.00
22.44
A


ATOM
670
OD2
ASP
A
151
54.369
12.242
−10.490
1.00
25.72
A


ATOM
671
C
ASP
A
151
58.515
12.203
−9.220
1.00
28.63
A


ATOM
672
O
ASP
A
151
58.890
12.780
−8.194
1.00
27.83
A


ATOM
673
N
ASP
A
152
58.934
12.560
−10.426
1.00
29.21
A


ATOM
674
CA
ASP
A
152
59.907
13.636
−10.562
1.00
31.88
A


ATOM
675
CB
ASP
A
152
60.325
13.792
−12.026
1.00
33.94
A


ATOM
676
CG
ASP
A
152
61.033
12.564
−12.557
1.00
38.88
A


ATOM
677
OD1
ASP
A
152
61.817
11.959
−11.791
1.00
39.67
A


ATOM
678
OD2
ASP
A
152
60.817
12.211
−13.738
1.00
41.57
A


ATOM
679
C
ASP
A
152
59.487
14.994
−10.013
1.00
30.90
A


ATOM
680
O
ASP
A
152
60.316
15.735
−9.482
1.00
31.69
A


ATOM
681
N
GLU
A
153
58.207
15.322
−10.107
1.00
29.44
A


ATOM
682
CA
GLU
A
153
57.767
16.632
−9.646
1.00
28.69
A


ATOM
683
CB
GLU
A
153
56.984
17.327
−10.766
1.00
32.90
A


ATOM
684
CG
GLU
A
153
57.451
16.987
−12.183
1.00
40.57
A


ATOM
685
CD
GLU
A
153
56.920
15.643
−12.675
1.00
45.78
A


ATOM
686
OE1
GLU
A
153
55.682
15.482
−12.760
1.00
48.91
A


ATOM
687
OE2
GLU
A
153
57.736
14.747
−12.979
1.00
48.95
A


ATOM
688
C
GLU
A
153
56.929
16.683
−8.372
1.00
26.43
A


ATOM
689
O
GLU
A
153
56.947
17.688
−7.660
1.00
25.08
A


ATOM
690
N
LYS
A
154
56.205
15.610
−8.069
1.00
22.39
A


ATOM
691
CA
LYS
A
154
55.318
15.631
−6.912
1.00
21.43
A


ATOM
692
CB
LYS
A
154
53.861
15.628
−7.398
1.00
20.33
A


ATOM
693
CG
LYS
A
154
53.505
16.716
−8.403
1.00
21.92
A


ATOM
694
CD
LYS
A
154
52.211
16.375
−9.146
1.00
19.70
A


ATOM
695
CE
LYS
A
154
51.775
17.503
−10.077
1.00
20.04
A


ATOM
696
NZ
LYS
A
154
50.631
17.094
−10.951
1.00
19.97
A


ATOM
697
C
LYS
A
154
55.458
14.522
−5.881
1.00
20.43
A


ATOM
698
O
LYS
A
154
55.949
13.426
−6.173
1.00
21.13
A


ATOM
699
N
LEU
A
155
54.985
14.832
−4.676
1.00
19.69
A


ATOM
700
CA
LEU
A
155
54.950
13.900
−3.553
1.00
19.10
A


ATOM
701
CB
LEU
A
155
55.362
14.588
−2.252
1.00
19.65
A


ATOM
702
CG
LEU
A
155
56.740
15.234
−2.129
1.00
21.20
A


ATOM
703
CD1
LEU
A
155
56.848
15.918
−0.770
1.00
23.42
A


ATOM
704
CD2
LEU
A
155
57.816
14.174
−2.277
1.00
23.08
A


ATOM
705
C
LEU
A
155
53.478
13.507
−3.427
1.00
18.87
A


ATOM
706
O
LEU
A
155
52.600
14.348
−3.620
1.00
18.61
A


ATOM
707
N
TYR
A
156
53.209
12.249
−3.091
1.00
15.02
A


ATOM
708
CA
TYR
A
156
51.834
11.783
−2.934
1.00
16.29
A


ATOM
709
CB
TYR
A
156
51.470
10.769
−4.029
1.00
14.20
A


ATOM
710
CG
TYR
A
156
51.603
11.273
−5.449
1.00
17.29
A


ATOM
711
CD1
TYR
A
156
52.857
11.429
−6.045
1.00
16.46
A


ATOM
712
CE1
TYR
A
156
52.978
11.884
−7.360
1.00
18.68
A


ATOM
713
CD2
TYR
A
156
50.474
11.588
−6.202
1.00
16.43
A


ATOM
714
CE2
TYR
A
156
50.583
12.048
−7.512
1.00
16.31
A


ATOM
715
CZ
TYR
A
156
51.835
12.192
−8.083
1.00
18.17
A


ATOM
716
OH
TYR
A
156
51.941
12.651
−9.371
1.00
17.47
A


ATOM
717
C
TYR
A
156
51.657
11.108
−1.572
1.00
16.32
A


ATOM
718
O
TYR
A
156
52.412
10.197
−1.235
1.00
16.27
A


ATOM
719
N
PHE
A
157
50.678
11.568
−0.792
1.00
15.47
A


ATOM
720
CA
PHE
A
157
50.385
10.966
0.508
1.00
16.66
A


ATOM
721
CB
PHE
A
157
50.324
12.014
1.629
1.00
16.91
A


ATOM
722
CG
PHE
A
157
51.631
12.708
1.907
1.00
18.96
A


ATOM
723
CD1
PHE
A
157
52.821
12.261
1.340
1.00
20.31
A


ATOM
724
CD2
PHE
A
157
51.664
13.829
2.732
1.00
21.12
A


ATOM
725
CE1
PHE
A
157
54.025
12.926
1.585
1.00
22.08
A


ATOM
726
CE2
PHE
A
157
52.865
14.500
2.982
1.00
22.18
A


ATOM
727
CZ
PHE
A
157
54.045
14.045
2.405
1.00
21.27
A


ATOM
728
C
PHE
A
157
49.016
10.308
0.404
1.00
16.52
A


ATOM
729
O
PHE
A
157
48.029
10.979
0.110
1.00
17.32
A


ATOM
730
N
GLY
A
158
48.953
9.002
0.644
1.00
15.97
A


ATOM
731
CA
GLY
A
158
47.684
8.299
0.572
1.00
16.13
A


ATOM
732
C
GLY
A
158
47.000
8.383
1.920
1.00
14.94
A


ATOM
733
O
GLY
A
158
47.445
7.756
2.879
1.00
16.28
A


ATOM
734
N
LEU
A
159
45.915
9.145
1.989
1.00
13.50
A


ATOM
735
CA
LEU
A
159
45.191
9.340
3.241
1.00
15.20
A


ATOM
736
CB
LEU
A
159
45.031
10.835
3.517
1.00
14.20
A


ATOM
737
CG
LEU
A
159
46.270
11.726
3.385
1.00
19.00
A


ATOM
738
CD1
LEU
A
159
45.847
13.188
3.477
1.00
17.12
A


ATOM
739
CD2
LEU
A
159
47.275
11.390
4.471
1.00
14.71
A


ATOM
740
C
LEU
A
159
43.809
8.716
3.232
1.00
15.53
A


ATOM
741
O
LEU
A
159
43.232
8.472
2.177
1.00
16.05
A


ATOM
742
N
SER
A
160
43.268
8.469
4.418
1.00
15.86
A


ATOM
743
CA
SER
A
160
41.932
7.917
4.498
1.00
19.01
A


ATOM
744
CB
SER
A
160
41.566
7.582
5.949
1.00
22.90
A


ATOM
745
CG
SER
A
160
41.901
8.629
6.833
1.00
24.18
A


ATOM
746
C
SER
A
160
40.987
8.968
3.924
1.00
20.43
A


ATOM
747
O
SER
A
160
41.213
10.173
4.062
1.00
19.96
A


ATOM
748
N
TYR
A
161
39.945
8.508
3.250
1.00
19.20
A


ATOM
749
CA
TYR
A
161
38.975
9.406
2.644
1.00
20.37
A


ATOM
750
CB
TYR
A
161
38.471
8.785
1.332
1.00
20.00
A


ATOM
751
CG
TYR
A
161
37.314
9.502
0.666
1.00
20.72
A


ATOM
752
CD1
TYR
A
161
37.222
10.895
0.682
1.00
18.22
A


ATOM
753
CE1
TYR
A
161
36.180
11.557
0.029
1.00
22.24
A


ATOM
754
CD2
TYR
A
161
36.333
8.784
−0.020
1.00
20.53
A


ATOM
755
CE2
TYR
A
161
35.287
9.436
−0.678
1.00
24.24
A


ATOM
756
CZ
TYR
A
161
35.218
10.822
−0.648
1.00
22.32
A


ATOM
757
OH
TYR
A
161
34.194
11.471
−1.298
1.00
23.03
A


ATOM
758
C
TYR
A
161
37.812
9.681
3.598
1.00
20.14
A


ATOM
759
O
TYR
A
161
36.959
8.819
3.810
1.00
19.53
A


ATOM
760
N
ALA
A
162
37.791
10.880
4.178
1.00
19.92
A


ATOM
761
CA
ALA
A
162
36.721
11.271
5.099
1.00
21.07
A


ATOM
762
CB
ALA
A
162
37.187
12.419
6.002
1.00
19.60
A


ATOM
763
C
ALA
A
162
35.542
11.712
4.238
1.00
22.07
A


ATOM
764
O
ALA
A
162
35.436
12.875
3.860
1.00
20.66
A


ATOM
765
N
LYS
A
163
34.653
10.769
3.945
1.00
23.27
A


ATOM
766
CA
LYS
A
163
33.503
11.017
3.080
1.00
27.12
A


ATOM
767
CB
LYS
A
163
32.663
9.741
2.963
1.00
29.68
A


ATOM
768
CG
LYS
A
163
33.455
8.524
2.515
1.00
37.67
A


ATOM
769
CD
LYS
A
163
32.556
7.310
2.321
1.00
42.24
A


ATOM
770
CE
LYS
A
163
33.373
6.034
2.185
1.00
44.48
A


ATOM
771
NZ
LYS
A
163
34.143
5.735
3.430
1.00
44.88
A


ATOM
772
C
LYS
A
163
32.581
12.186
3.411
1.00
25.78
A


ATOM
773
O
LYS
A
163
32.103
12.863
2.506
1.00
26.53
A


ATOM
774
N
ASN
A
164
32.327
12.441
4.689
1.00
24.57
A


ATOM
775
CA
ASN
A
164
31.420
13.522
5.033
1.00
23.77
A


ATOM
776
CB
ASN
A
164
30.610
13.129
6.265
1.00
25.02
A


ATOM
777
CG
ASN
A
164
29.537
12.101
5.932
1.00
27.54
A


ATOM
778
OD1
ASN
A
164
28.772
12.281
4.983
1.00
28.79
A


ATOM
779
ND2
ASN
A
164
29.475
11.024
6.704
1.00
27.13
A


ATOM
780
C
ASN
A
164
31.999
14.931
5.169
1.00
24.43
A


ATOM
781
O
ASN
A
164
31.306
15.856
5.589
1.00
23.98
A


ATOM
782
N
GLY
A
165
33.262
15.097
4.795
1.00
21.56
A


ATOM
783
CA
GLY
A
165
33.873
16.414
4.836
1.00
24.39
A


ATOM
784
C
GLY
A
165
34.191
17.043
6.181
1.00
23.62
A


ATOM
785
O
GLY
A
165
34.380
16.352
7.177
1.00
23.26
A


ATOM
786
N
GLU
A
166
34.234
18.373
6.186
1.00
23.22
A


ATOM
787
CA
GLU
A
166
34.563
19.176
7.362
1.00
24.54
A


ATOM
788
CB
GLU
A
166
35.055
20.558
6.913
1.00
25.04
A


ATOM
789
CG
GLU
A
166
36.419
20.569
6.229
1.00
26.48
A


ATOM
790
CD
GLU
A
166
36.699
21.889
5.517
1.00
30.02
A


ATOM
791
OE1
GLU
A
166
36.081
22.906
5.889
1.00
29.33
A


ATOM
792
OE2
GLU
A
166
37.544
21.916
4.596
1.00
30.48
A


ATOM
793
C
GLU
A
166
33.436
19.372
8.369
1.00
24.44
A


ATOM
794
O
GLU
A
166
32.279
19.541
8.001
1.00
22.76
A


ATOM
795
N
LEU
A
167
33.791
19.370
9.649
1.00
22.95
A


ATOM
796
CA
LEU
A
167
32.813
19.581
10.707
1.00
22.26
A


ATOM
797
CB
LEU
A
167
33.497
19.481
12.073
1.00
22.32
A


ATOM
798
CG
LEU
A
167
32.706
19.923
13.306
1.00
22.04
A


ATOM
799
CD1
LEU
A
167
31.454
19.074
13.463
1.00
19.66
A


ATOM
800
CD2
LEU
A
167
33.597
19.805
14.537
1.00
21.17
A


ATOM
801
C
LEU
A
167
32.193
20.971
10.529
1.00
23.49
A


ATOM
802
O
LEU
A
167
31.047
21.209
10.907
1.00
23.56
A


ATOM
803
N
LEU
A
168
32.960
21.887
9.948
1.00
24.25
A


ATOM
804
CA
LEU
A
168
32.473
23.245
9.722
1.00
26.64
A


ATOM
805
CB
LEU
A
168
33.560
24.099
9.066
1.00
25.62
A


ATOM
806
CG
LEU
A
168
33.198
25.546
8.707
1.00
27.34
A


ATOM
807
CD1
LEU
A
168
32.718
26.296
9.946
1.00
26.42
A


ATOM
808
CD2
LEU
A
168
34.418
26.238
8.119
1.00
26.74
A


ATOM
809
C
LEU
A
168
31.234
23.218
8.829
1.00
27.13
A


ATOM
810
O
LEU
A
168
30.297
23.989
9.030
1.00
26.01
A


ATOM
811
N
LYS
A
169
31.233
22.320
7.848
1.00
26.41
A


ATOM
812
CA
LYS
A
169
30.106
22.210
6.934
1.00
27.70
A


ATOM
813
CB
LYS
A
169
30.324
21.064
5.945
1.00
30.49
A


ATOM
814
CG
LYS
A
169
29.151
20.854
4.993
1.00
32.47
A


ATOM
815
CD
LYS
A
169
29.407
19.728
3.998
1.00
35.98
A


ATOM
816
CE
LYS
A
169
29.462
18.372
4.683
1.00
38.53
A


ATOM
817
NZ
LYS
A
169
29.622
17.263
3.702
1.00
41.00
A


ATOM
818
C
LYS
A
169
28.801
21.985
7.682
1.00
28.12
A


ATOM
819
O
LYS
A
169
27.785
22.608
7.371
1.00
28.08
A


ATOM
820
N
TYR
A
170
28.826
21.094
8.668
1.00
26.53
A


ATOM
821
CA
TYR
A
170
27.624
20.791
9.434
1.00
26.95
A


ATOM
822
CB
TYR
A
170
27.810
19.476
10.193
1.00
25.03
A


ATOM
823
CG
TYR
A
170
27.898
18.300
9.251
1.00
26.65
A


ATOM
824
CD1
TYR
A
170
26.745
17.661
8.790
1.00
28.27
A


ATOM
825
CE1
TYR
A
170
26.814
16.642
7.839
1.00
26.85
A


ATOM
826
CD2
TYR
A
170
29.127
17.884
8.742
1.00
27.83
A


ATOM
827
CE2
TYR
A
170
29.209
16.869
7.792
1.00
27.19
A


ATOM
828
CZ
TYR
A
170
28.049
16.254
7.343
1.00
30.02
A


ATOM
829
OH
TYR
A
170
28.130
15.268
6.382
1.00
29.23
A


ATOM
830
C
TYR
A
170
27.229
21.918
10.376
1.00
27.59
A


ATOM
831
O
TYR
A
170
26.045
22.122
10.642
1.00
29.25
A


ATOM
832
N
ILE
A
171
28.208
22.660
10.882
1.00
28.16
A


ATOM
833
CA
ILE
A
171
27.883
23.770
11.763
1.00
29.03
A


ATOM
834
CB
ILE
A
171
29.151
24.435
12.337
1.00
27.51
A


ATOM
835
CG2
ILE
A
171
28.773
25.705
13.084
1.00
27.97
A


ATOM
836
CG1
ILE
A
171
29.872
23.458
13.272
1.00
26.70
A


ATOM
837
CD1
ILE
A
171
31.163
23.996
13.856
1.00
24.07
A


ATOM
838
C
ILE
A
171
27.094
24.796
10.944
1.00
31.41
A


ATOM
839
O
ILE
A
171
26.088
25.335
11.407
1.00
31.69
A


ATOM
840
N
ARG
A
172
27.546
25.047
9.719
1.00
33.21
A


ATOM
841
CA
ARG
A
172
26.874
26.000
8.844
1.00
36.54
A


ATOM
842
CB
ARG
A
172
27.734
26.314
7.616
1.00
37.73
A


ATOM
843
CG
ARG
A
172
29.057
27.011
7.912
1.00
41.65
A


ATOM
844
CD
ARG
A
172
29.708
27.492
6.616
1.00
45.29
A


ATOM
845
NE
ARG
A
172
31.037
28.070
6.812
1.00
48.51
A


ATOM
846
CZ
ARG
A
172
31.314
29.059
7.658
1.00
51.53
A


ATOM
847
NH1
ARG
A
172
30.355
29.593
8.406
1.00
53.75
A


ATOM
848
NH2
ARG
A
172
32.553
29.526
7.748
1.00
51.21
A


ATOM
849
C
ARG
A
172
25.528
25.459
8.378
1.00
37.67
A


ATOM
850
O
ARG
A
172
24.550
26.200
8.288
1.00
39.09
A


ATOM
851
N
LYS
A
173
25.481
24.163
8.092
1.00
38.44
A


ATOM
852
CA
LYS
A
173
24.259
23.528
7.619
1.00
39.25
A


ATOM
853
CB
LYS
A
173
24.523
22.061
7.272
1.00
41.89
A


ATOM
854
CG
LYS
A
173
23.279
21.298
6.830
1.00
45.52
A


ATOM
855
CD
LYS
A
173
23.557
19.808
6.653
1.00
49.60
A


ATOM
856
CE
LYS
A
173
24.477
19.530
5.469
1.00
52.63
A


ATOM
857
NZ
LYS
A
173
23.855
19.894
4.160
1.00
54.61
A


ATOM
858
C
LYS
A
173
23.089
23.608
8.595
1.00
39.30
A


ATOM
859
O
LYS
A
173
21.981
23.960
8.201
1.00
39.62
A


ATOM
860
N
ILE
A
174
23.320
23.282
9.863
1.00
37.96
A


ATOM
861
CA
ILE
A
174
22.229
23.314
10.833
1.00
37.36
A


ATOM
862
CB
ILE
A
174
22.159
21.998
11.652
1.00
37.44
A


ATOM
863
CG2
ILE
A
174
22.058
20.802
10.709
1.00
38.37
A


ATOM
864
CG1
ILE
A
174
23.397
21.850
12.532
1.00
37.25
A


ATOM
865
CD1
ILE
A
174
23.355
20.620
13.418
1.00
36.85
A


ATOM
866
C
ILE
A
174
22.259
24.492
11.801
1.00
36.71
A


ATOM
867
O
ILE
A
174
21.448
24.556
12.724
1.00
38.05
A


ATOM
868
N
GLY
A
175
23.185
25.423
11.592
1.00
35.48
A


ATOM
869
CA
GLY
A
175
23.265
26.585
12.462
1.00
35.29
A


ATOM
870
C
GLY
A
175
24.053
26.360
13.737
1.00
35.06
A


ATOM
871
O
GLY
A
175
25.066
27.019
13.970
1.00
37.46
A


ATOM
872
N
SER
A
176
23.581
25.441
14.571
1.00
33.94
A


ATOM
873
CA
SER
A
176
24.253
25.113
15.822
1.00
32.84
A


ATOM
874
CB
SER
A
176
23.938
26.155
16.901
1.00
33.54
A


ATOM
875
OG
SER
A
176
22.599
26.056
17.347
1.00
34.86
A


ATOM
876
C
SER
A
176
23.796
23.731
16.276
1.00
32.34
A


ATOM
877
O
SER
A
176
22.726
23.263
15.884
1.00
32.82
A


ATOM
878
N
PHE
A
177
24.609
23.085
17.103
1.00
29.39
A


ATOM
879
CA
PHE
A
177
24.313
21.743
17.597
1.00
27.20
A


ATOM
880
CB
PHE
A
177
25.621
20.989
17.865
1.00
26.39
A


ATOM
881
CG
PHE
A
177
26.372
20.585
16.622
1.00
26.18
A


ATOM
882
CD1
PHE
A
177
26.210
21.277
15.426
1.00
25.30
A


ATOM
883
CD2
PHE
A
177
27.266
19.516
16.662
1.00
26.05
A


ATOM
884
CE1
PHE
A
177
26.923
20.912
14.290
1.00
26.59
A


ATOM
885
CE2
PHE
A
177
27.986
19.143
15.532
1.00
26.06
A


ATOM
886
CZ
PHE
A
177
27.815
19.841
14.343
1.00
25.42
A


ATOM
887
C
PHE
A
177
23.500
21.752
18.884
1.00
27.00
A


ATOM
888
O
PHE
A
177
23.704
22.610
19.747
1.00
26.48
A


ATOM
889
N
ASP
A
178
22.578
20.802
19.022
1.00
26.70
A


ATOM
890
CA
ASP
A
178
21.816
20.729
20.260
1.00
26.35
A


ATOM
891
CB
ASP
A
178
20.621
19.773
20.142
1.00
29.90
A


ATOM
892
CG
ASP
A
178
21.020
18.372
19.720
1.00
32.28
A


ATOM
893
OD1
ASP
A
178
22.157
17.949
20.014
1.00
35.21
A


ATOM
894
OD2
ASP
A
178
20.179
17.683
19.105
1.00
34.79
A


ATOM
895
C
ASP
A
178
22.810
20.228
21.311
1.00
25.03
A


ATOM
896
O
ASP
A
178
23.974
19.968
20.992
1.00
21.24
A


ATOM
897
N
GLU
A
179
22.361
20.083
22.552
1.00
23.60
A


ATOM
898
CA
GLU
A
179
23.247
19.644
23.619
1.00
25.18
A


ATOM
899
CB
GLU
A
179
22.542
19.770
24.971
1.00
27.60
A


ATOM
900
CG
GLU
A
179
23.324
19.176
26.130
1.00
32.58
A


ATOM
901
CD
GLU
A
179
22.997
19.845
27.449
1.00
35.82
A


ATOM
902
OE1
GLU
A
179
21.825
20.224
27.645
1.00
35.95
A


ATOM
903
OE2
GLU
A
179
23.912
19.984
28.291
1.00
38.19
A


ATOM
904
C
GLU
A
179
23.808
18.235
23.450
1.00
24.08
A


ATOM
905
O
GLU
A
179
24.977
17.989
23.756
1.00
22.79
A


ATOM
906
N
THR
A
180
22.983
17.316
22.961
1.00
23.36
A


ATOM
907
CA
THR
A
180
23.412
15.935
22.761
1.00
22.15
A


ATOM
908
CB
THR
A
180
22.224
15.054
22.320
1.00
23.77
A


ATOM
909
OG1
THR
A
180
21.222
15.075
23.341
1.00
26.37
A


ATOM
910
CG2
THR
A
180
22.670
13.616
22.088
1.00
22.66
A


ATOM
911
C
THR
A
180
24.533
15.830
21.724
1.00
22.01
A


ATOM
912
O
THR
A
180
25.533
15.141
21.944
1.00
19.87
A


ATOM
913
N
CYS
A
181
24.365
16.511
20.596
1.00
21.21
A


ATOM
914
CA
CYS
A
181
25.372
16.480
19.541
1.00
22.22
A


ATOM
915
CB
CYS
A
181
24.800
17.065
18.250
1.00
24.62
A


ATOM
916
SG
CYS
A
181
23.435
16.080
17.560
1.00
29.50
A


ATOM
917
C
CYS
A
181
26.633
17.232
19.954
1.00
23.07
A


ATOM
918
O
CYS
A
181
27.746
16.827
19.608
1.00
23.95
A


ATOM
919
N
THR
A
182
26.463
18.325
20.695
1.00
22.76
A


ATOM
920
CA
THR
A
182
27.606
19.103
21.161
1.00
21.49
A


ATOM
921
CB
THR
A
182
27.167
20.346
21.978
1.00
21.37
A


ATOM
922
OG1
THR
A
182
26.459
21.262
21.134
1.00
22.50
A


ATOM
923
CG2
THR
A
182
28.379
21.046
22.565
1.00
18.36
A


ATOM
924
C
THR
A
182
28.454
18.215
22.071
1.00
21.48
A


ATOM
925
O
THR
A
182
29.669
18.090
21.894
1.00
19.95
A


ATOM
926
N
ARG
A
183
27.798
17.602
23.050
1.00
18.97
A


ATOM
927
CA
ARG
A
183
28.468
16.723
23.996
1.00
19.39
A


ATOM
928
CB
ARG
A
183
27.455
16.140
24.984
1.00
19.46
A


ATOM
929
CG
ARG
A
183
28.030
15.062
25.887
1.00
18.77
A


ATOM
930
CD
ARG
A
183
27.021
14.571
26.925
1.00
21.19
A


ATOM
931
NE
ARG
A
183
26.605
15.642
27.824
1.00
19.46
A


ATOM
932
CZ
ARG
A
183
25.496
16.362
27.679
1.00
20.45
A


ATOM
933
NH1
ARG
A
183
24.672
16.123
26.666
1.00
19.81
A


ATOM
934
NH2
ARG
A
183
25.224
17.338
28.539
1.00
17.11
A


ATOM
935
C
ARG
A
183
29.206
15.577
23.302
1.00
20.02
A


ATOM
936
O
ARG
A
183
30.383
15.333
23.573
1.00
19.97
A


ATOM
937
N
PHE
A
184
28.520
14.871
22.409
1.00
19.24
A


ATOM
938
CA
PHE
A
184
29.144
13.746
21.722
1.00
18.04
A


ATOM
939
CB
PHE
A
184
28.158
13.078
20.764
1.00
21.05
A


ATOM
940
CG
PHE
A
184
28.719
11.857
20.098
1.00
22.67
A


ATOM
941
CD1
PHE
A
184
28.717
10.630
20.754
1.00
22.97
A


ATOM
942
CD2
PHE
A
184
29.317
11.949
18.850
1.00
19.97
A


ATOM
943
CE1
PHE
A
184
29.308
9.510
20.176
1.00
23.53
A


ATOM
944
CE2
PHE
A
184
29.915
10.833
18.263
1.00
24.11
A


ATOM
945
CZ
PHE
A
184
29.910
9.613
18.928
1.00
22.97
A


ATOM
946
C
PHE
A
184
30.403
14.127
20.941
1.00
17.99
A


ATOM
947
O
PHE
A
184
31.461
13.531
21.130
1.00
18.89
A


ATOM
948
N
TYR
A
185
30.292
15.110
20.056
1.00
15.73
A


ATOM
949
CA
TYR
A
185
31.443
15.519
19.265
1.00
15.72
A


ATOM
950
CB
TYR
A
185
30.992
16.413
18.111
1.00
17.33
A


ATOM
951
CG
TYR
A
185
30.364
15.584
17.015
1.00
19.37
A


ATOM
952
CD1
TYR
A
185
31.159
14.809
16.168
1.00
16.53
A


ATOM
953
CE1
TYR
A
185
30.590
13.952
15.232
1.00
18.12
A


ATOM
954
CD2
TYR
A
185
28.976
15.484
16.892
1.00
18.18
A


ATOM
955
CE2
TYR
A
185
28.398
14.623
15.956
1.00
18.90
A


ATOM
956
CZ
TYR
A
185
29.211
13.861
15.133
1.00
18.41
A


ATOM
957
OH
TYR
A
185
28.650
12.995
14.218
1.00
20.48
A


ATOM
958
C
TYR
A
185
32.544
16.172
20.083
1.00
15.79
A


ATOM
959
O
TYR
A
185
33.720
16.015
19.766
1.00
17.69
A


ATOM
960
N
THR
A
186
32.176
16.887
21.142
1.00
15.68
A


ATOM
961
CA
THR
A
186
33.184
17.504
21.997
1.00
16.03
A


ATOM
962
CB
THR
A
186
32.559
18.403
23.094
1.00
16.62
A


ATOM
963
OG1
THR
A
186
31.866
19.503
22.481
1.00
14.79
A


ATOM
964
CG2
THR
A
186
33.656
18.953
24.019
1.00
14.68
A


ATOM
965
C
THR
A
186
33.954
16.375
22.680
1.00
15.59
A


ATOM
966
O
THR
A
186
35.176
16.443
22.823
1.00
13.77
A


ATOM
967
N
ALA
A
187
33.234
15.333
23.097
1.00
14.06
A


ATOM
968
CA
ALA
A
187
33.869
14.196
23.757
1.00
14.74
A


ATOM
969
CB
ALA
A
187
32.810
13.195
24.224
1.00
14.32
A


ATOM
970
C
ALA
A
187
34.875
13.509
22.821
1.00
14.41
A


ATOM
971
O
ALA
A
187
35.972
13.136
23.247
1.00
15.61
A


ATOM
972
N
GLU
A
188
34.516
13.340
21.549
1.00
14.01
A


ATOM
973
CA
GLU
A
188
35.443
12.704
20.615
1.00
13.50
A


ATOM
974
CB
GLU
A
188
34.782
12.449
19.251
1.00
12.85
A


ATOM
975
CG
GLU
A
188
33.622
11.454
19.282
1.00
12.71
A


ATOM
976
CD
GLU
A
188
33.464
10.685
17.979
1.00
15.01
A


ATOM
977
OE1
GLU
A
188
33.687
11.275
16.899
1.00
13.21
A


ATOM
978
OE2
GLU
A
188
33.110
9.484
18.031
1.00
17.69
A


ATOM
979
C
GLU
A
188
36.682
13.582
20.436
1.00
13.34
A


ATOM
980
O
GLU
A
188
37.803
13.085
20.408
1.00
14.69
A


ATOM
981
N
ILE
A
189
36.486
14.893
20.326
1.00
13.52
A


ATOM
982
CA
ILE
A
189
37.627
15.787
20.159
1.00
13.35
A


ATOM
983
CB
ILE
A
189
37.169
17.247
19.939
1.00
13.95
A


ATOM
984
CG2
ILE
A
189
38.381
18.165
19.822
1.00
12.47
A


ATOM
985
CG1
ILE
A
189
36.302
17.332
18.671
1.00
13.44
A


ATOM
986
CD1
ILE
A
189
35.588
18.664
18.491
1.00
14.29
A


ATOM
987
C
ILE
A
189
38.530
15.702
21.394
1.00
14.63
A


ATOM
988
O
ILE
A
189
39.753
15.595
21.271
1.00
12.97
A


ATOM
989
N
VAL
A
190
37.927
15.751
22.582
1.00
14.35
A


ATOM
990
CA
VAL
A
190
38.684
15.655
23.832
1.00
13.22
A


ATOM
991
CB
VAL
A
190
37.743
15.690
25.061
1.00
14.28
A


ATOM
992
CG1
VAL
A
190
38.509
15.267
26.326
1.00
15.08
A


ATOM
993
CG2
VAL
A
190
37.160
17.082
25.233
1.00
12.08
A


ATOM
994
C
VAL
A
190
39.468
14.338
23.859
1.00
14.61
A


ATOM
995
O
VAL
A
190
40.634
14.304
24.250
1.00
13.72
A


ATOM
996
N
SER
A
191
38.825
13.254
23.432
1.00
15.26
A


ATOM
997
CA
SER
A
191
39.478
11.943
23.421
1.00
16.81
A


ATOM
998
CB
SER
A
191
38.470
10.857
23.041
1.00
16.14
A


ATOM
999
OG
SER
A
191
39.018
9.569
23.238
1.00
16.94
A


ATOM
1000
C
SER
A
191
40.649
11.928
22.441
1.00
16.58
A


ATOM
1001
O
SER
A
191
41.697
11.335
22.713
1.00
13.96
A


ATOM
1002
N
ALA
A
192
40.468
12.586
21.300
1.00
15.26
A


ATOM
1003
CA
ALA
A
192
41.518
12.645
20.292
1.00
14.37
A


ATOM
1004
CB
ALA
A
192
40.989
13.296
19.016
1.00
14.43
A


ATOM
1005
C
ALA
A
192
42.695
13.440
20.845
1.00
16.46
A


ATOM
1006
O
ALA
A
192
43.851
13.038
20.697
1.00
17.96
A


ATOM
1007
N
LEU
A
193
42.401
14.563
21.496
1.00
15.02
A


ATOM
1008
CA
LEU
A
193
43.459
15.392
22.067
1.00
15.42
A


ATOM
1009
CB
LEU
A
193
42.884
16.712
22.600
1.00
12.88
A


ATOM
1010
CG
LEU
A
193
42.445
17.721
21.525
1.00
15.97
A


ATOM
1011
CD1
LEU
A
193
41.869
18.979
22.190
1.00
13.97
A


ATOM
1012
CD2
LEU
A
193
43.642
18.088
20.655
1.00
14.58
A


ATOM
1013
C
LEU
A
193
44.211
14.659
23.174
1.00
14.49
A


ATOM
1014
O
LEU
A
193
45.427
14.813
23.310
1.00
16.56
A


ATOM
1015
N
GLU
A
194
43.500
13.870
23.975
1.00
13.96
A


ATOM
1016
CA
GLU
A
194
44.179
13.123
25.032
1.00
14.08
A


ATOM
1017
CB
GLU
A
194
43.190
12.295
25.857
1.00
14.65
A


ATOM
1018
CG
GLU
A
194
43.882
11.301
26.789
1.00
17.09
A


ATOM
1019
CD
GLU
A
194
42.924
10.592
27.730
1.00
19.59
A


ATOM
1020
OE1
GLU
A
194
41.809
10.237
27.295
1.00
19.25
A


ATOM
1021
OE2
GLU
A
194
43.302
10.380
28.906
1.00
20.20
A


ATOM
1022
C
GLU
A
194
45.208
12.199
24.386
1.00
13.57
A


ATOM
1023
O
GLU
A
194
46.337
12.093
24.847
1.00
14.23
A


ATOM
1024
N
TYR
A
195
44.822
11.544
23.301
1.00
14.89
A


ATOM
1025
CA
TYR
A
195
45.743
10.642
22.618
1.00
16.58
A


ATOM
1026
CB
TYR
A
195
45.030
9.910
21.488
1.00
17.29
A


ATOM
1027
CG
TYR
A
195
45.956
9.058
20.649
1.00
17.92
A


ATOM
1028
CD1
TYR
A
195
46.347
7.788
21.077
1.00
17.96
A


ATOM
1029
CE1
TYR
A
195
47.203
6.996
20.304
1.00
19.77
A


ATOM
1030
CD2
TYR
A
195
46.445
9.524
19.428
1.00
16.67
A


ATOM
1031
CE2
TYR
A
195
47.299
8.744
18.650
1.00
18.51
A


ATOM
1032
CZ
TYR
A
195
47.671
7.481
19.094
1.00
20.24
A


ATOM
1033
OH
TYR
A
195
48.506
6.705
18.325
1.00
21.89
A


ATOM
1034
C
TYR
A
195
46.917
11.419
22.035
1.00
16.98
A


ATOM
1035
O
TYR
A
195
48.081
11.047
22.203
1.00
14.61
A


ATOM
1036
N
LEU
A
196
46.599
12.507
21.347
1.00
16.30
A


ATOM
1037
CA
LEU
A
196
47.619
13.328
20.720
1.00
18.15
A


ATOM
1038
CB
LEU
A
196
46.969
14.502
19.982
1.00
18.59
A


ATOM
1039
CG
LEU
A
196
47.834
15.203
18.935
1.00
22.51
A


ATOM
1040
CD1
LEU
A
196
48.222
14.206
17.841
1.00
20.94
A


ATOM
1041
CD2
LEU
A
196
47.060
16.375
18.338
1.00
22.98
A


ATOM
1042
C
LEU
A
196
48.592
13.844
21.763
1.00
17.75
A


ATOM
1043
O
LEU
A
196
49.801
13.644
21.649
1.00
18.33
A


ATOM
1044
N
HIS
A
197
48.064
14.495
22.792
1.00
17.12
A


ATOM
1045
CA
HIS
A
197
48.913
15.042
23.842
1.00
18.47
A


ATOM
1046
CB
HIS
A
197
48.069
15.866
24.817
1.00
15.90
A


ATOM
1047
CG
HIS
A
197
47.571
17.152
24.231
1.00
19.15
A


ATOM
1048
CD2
HIS
A
197
47.830
17.745
23.038
1.00
18.22
A


ATOM
1049
ND1
HIS
A
197
46.704
17.992
24.897
1.00
17.47
A


ATOM
1050
CE1
HIS
A
197
46.450
19.047
24.139
1.00
19.74
A


ATOM
1051
NE2
HIS
A
197
47.119
18.921
23.007
1.00
15.69
A


ATOM
1052
C
HIS
A
197
49.696
13.958
24.572
1.00
19.40
A


ATOM
1053
O
HIS
A
197
50.823
14.192
25.021
1.00
19.42
A


ATOM
1054
N
GLY
A
198
49.106
12.770
24.679
1.00
18.59
A


ATOM
1055
CA
GLY
A
198
49.793
11.675
25.339
1.00
19.60
A


ATOM
1056
C
GLY
A
198
51.075
11.307
24.612
1.00
21.86
A


ATOM
1057
O
GLY
A
198
51.963
10.682
25.186
1.00
23.09
A


ATOM
1058
N
LYS
A
199
51.174
11.687
23.341
1.00
22.81
A


ATOM
1059
CA
LYS
A
199
52.368
11.401
22.549
1.00
24.43
A


ATOM
1060
CB
LYS
A
199
51.990
10.905
21.154
1.00
26.00
A


ATOM
1061
CG
LYS
A
199
51.378
9.520
21.133
1.00
30.98
A


ATOM
1062
CD
LYS
A
199
51.291
9.002
19.708
1.00
36.85
A


ATOM
1063
CE
LYS
A
199
50.832
7.559
19.682
1.00
40.37
A


ATOM
1064
NZ
LYS
A
199
51.646
6.691
20.581
1.00
43.48
A


ATOM
1065
C
LYS
A
199
53.253
12.631
22.414
1.00
23.88
A


ATOM
1066
O
LYS
A
199
54.144
12.669
21.568
1.00
24.97
A


ATOM
1067
N
GLY
A
200
52.997
13.638
23.243
1.00
24.00
A


ATOM
1068
CA
GLY
A
200
53.790
14.853
23.203
1.00
22.12
A


ATOM
1069
C
GLY
A
200
53.665
15.632
21.907
1.00
22.14
A


ATOM
1070
O
GLY
A
200
54.632
16.231
21.439
1.00
22.41
A


ATOM
1071
N
ILE
A
201
52.475
15.630
21.320
1.00
20.00
A


ATOM
1072
CA
ILE
A
201
52.252
16.355
20.080
1.00
18.93
A


ATOM
1073
CB
ILE
A
201
51.784
15.414
18.955
1.00
19.70
A


ATOM
1074
CG2
ILE
A
201
51.414
16.226
17.716
1.00
20.12
A


ATOM
1075
CG1
ILE
A
201
52.880
14.395
18.636
1.00
20.03
A


ATOM
1076
CD1
ILE
A
201
52.408
13.258
17.745
1.00
22.75
A


ATOM
1077
C
ILE
A
201
51.193
17.425
20.270
1.00
19.87
A


ATOM
1078
O
ILE
A
201
50.121
17.161
20.817
1.00
20.08
A


ATOM
1079
N
ILE
A
202
51.508
18.633
19.815
1.00
19.94
A


ATOM
1080
CA
ILE
A
202
50.601
19.772
19.891
1.00
20.45
A


ATOM
1081
CB
ILE
A
202
51.352
21.040
20.356
1.00
22.21
A


ATOM
1082
CG2
ILE
A
202
50.381
22.220
20.470
1.00
22.67
A


ATOM
1083
CG1
ILE
A
202
52.033
20.775
21.700
1.00
24.19
A


ATOM
1084
CD1
ILE
A
202
52.914
21.920
22.169
1.00
25.39
A


ATOM
1085
C
ILE
A
202
50.105
19.999
18.464
1.00
20.71
A


ATOM
1086
O
ILE
A
202
50.910
20.067
17.538
1.00
19.48
A


ATOM
1087
N
HIS
A
203
48.795
20.108
18.270
1.00
18.65
A


ATOM
1088
CA
HIS
A
203
48.280
20.319
16.919
1.00
18.02
A


ATOM
1089
CB
HIS
A
203
46.775
20.057
16.874
1.00
16.31
A


ATOM
1090
CG
HIS
A
203
46.199
20.136
15.495
1.00
18.36
A


ATOM
1091
CD2
HIS
A
203
46.043
21.186
14.655
1.00
16.42
A


ATOM
1092
ND1
HIS
A
203
45.759
19.026
14.806
1.00
19.50
A


ATOM
1093
CE1
HIS
A
203
45.359
19.389
13.600
1.00
17.64
A


ATOM
1094
NE2
HIS
A
203
45.522
20.694
13.483
1.00
20.87
A


ATOM
1095
C
HIS
A
203
48.589
21.738
16.405
1.00
18.92
A


ATOM
1096
O
HIS
A
203
49.073
21.906
15.282
1.00
16.21
A


ATOM
1097
N
ARG
A
204
48.301
22.744
17.232
1.00
18.60
A


ATOM
1098
CA
ARG
A
204
48.552
24.157
16.914
1.00
19.81
A


ATOM
1099
CB
ARG
A
204
49.998
24.365
16.458
1.00
21.61
A


ATOM
1100
CG
ARG
A
204
51.024
24.137
17.550
1.00
23.82
A


ATOM
1101
CD
ARG
A
204
52.323
24.870
17.252
1.00
27.62
A


ATOM
1102
NE
ARG
A
204
52.932
24.449
15.994
1.00
29.43
A


ATOM
1103
CZ
ARG
A
204
54.125
24.861
15.572
1.00
33.10
A


ATOM
1104
NH1
ARG
A
204
54.835
25.706
16.311
1.00
32.12
A


ATOM
1105
NH2
ARG
A
204
54.614
24.426
14.418
1.00
30.25
A


ATOM
1106
C
ARG
A
204
47.624
24.830
15.905
1.00
20.03
A


ATOM
1107
O
ARG
A
204
47.711
26.038
15.698
1.00
20.88
A


ATOM
1108
N
ASP
A
205
46.755
24.071
15.255
1.00
18.96
A


ATOM
1109
CA
ASP
A
205
45.828
24.692
14.325
1.00
17.90
A


ATOM
1110
CB
ASP
A
205
46.418
24.741
12.914
1.00
18.95
A


ATOM
1111
CG
ASP
A
205
45.655
25.688
12.008
1.00
20.36
A


ATOM
1112
OD1
ASP
A
205
44.939
26.560
12.545
1.00
20.35
A


ATOM
1113
OD2
ASP
A
205
45.772
25.573
10.771
1.00
22.49
A


ATOM
1114
C
ASP
A
205
44.500
23.956
14.328
1.00
19.60
A


ATOM
1115
O
ASP
A
205
43.876
23.751
13.287
1.00
21.53
A


ATOM
1116
N
LEU
A
206
44.063
23.569
15.521
1.00
18.53
A


ATOM
1117
CA
LEU
A
206
42.813
22.851
15.667
1.00
19.18
A


ATOM
1118
CB
LEU
A
206
42.693
22.295
17.087
1.00
18.94
A


ATOM
1119
CG
LEU
A
206
41.511
21.358
17.346
1.00
23.10
A


ATOM
1120
CD1
LEU
A
206
41.615
20.142
16.436
1.00
23.01
A


ATOM
1121
CD2
LEU
A
206
41.504
20.933
18.808
1.00
22.97
A


ATOM
1122
C
LEU
A
206
41.639
23.772
15.361
1.00
19.05
A


ATOM
1123
O
LEU
A
206
41.556
24.880
15.886
1.00
19.25
A


ATOM
1124
N
LYS
A
207
40.740
23.307
14.500
1.00
17.54
A


ATOM
1125
CA
LYS
A
207
39.564
24.081
14.110
1.00
18.60
A


ATOM
1126
CB
LYS
A
207
39.980
25.248
13.196
1.00
18.98
A


ATOM
1127
CG
LYS
A
207
40.786
24.817
11.982
1.00
18.20
A


ATOM
1128
CD
LYS
A
207
41.246
26.000
11.139
1.00
21.42
A


ATOM
1129
CE
LYS
A
207
42.223
25.537
10.062
1.00
23.21
A


ATOM
1130
NZ
LYS
A
207
42.561
26.604
9.084
1.00
29.61
A


ATOM
1131
C
LYS
A
207
38.566
23.181
13.388
1.00
18.18
A


ATOM
1132
O
LYS
A
207
38.921
22.100
12.915
1.00
18.11
A


ATOM
1133
N
PRO
A
208
37.298
23.614
13.293
1.00
20.26
A


ATOM
1134
CD
PRO
A
208
36.713
24.833
13.882
1.00
18.79
A


ATOM
1135
CA
PRO
A
208
36.272
22.814
12.616
1.00
19.67
A


ATOM
1136
CB
PRO
A
208
35.063
23.742
12.608
1.00
19.45
A


ATOM
1137
CG
PRO
A
208
35.231
24.509
13.891
1.00
21.81
A


ATOM
1138
C
PRO
A
208
36.674
22.372
11.209
1.00
21.04
A


ATOM
1139
O
PRO
A
208
36.264
21.307
10.751
1.00
21.19
A


ATOM
1140
N
GLU
A
209
37.474
23.188
10.528
1.00
21.69
A


ATOM
1141
CA
GLU
A
209
37.928
22.872
9.170
1.00
22.64
A


ATOM
1142
CB
GLU
A
209
38.644
24.084
8.558
1.00
23.65
A


ATOM
1143
CG
GLU
A
209
39.253
23.825
7.185
1.00
27.24
A


ATOM
1144
CD
GLU
A
209
40.155
24.958
6.716
1.00
29.40
A


ATOM
1145
OE1
GLU
A
209
39.660
26.094
6.553
1.00
29.68
A


ATOM
1146
OE2
GLU
A
209
41.363
24.711
6.511
1.00
30.07
A


ATOM
1147
C
GLU
A
209
38.879
21.668
9.159
1.00
22.28
A


ATOM
1148
O
GLU
A
209
38.955
20.933
8.170
1.00
21.36
A


ATOM
1149
N
ASN
A
210
39.600
21.490
10.263
1.00
19.90
A


ATOM
1150
CA
ASN
A
210
40.574
20.412
10.436
1.00
19.44
A


ATOM
1151
CB
ASN
A
210
41.744
20.912
11.287
1.00
20.07
A


ATOM
1152
CG
ASN
A
210
42.746
21.698
10.479
1.00
25.77
A


ATOM
1153
OD1
ASN
A
210
43.571
22.427
11.029
1.00
26.73
A


ATOM
1154
ND2
ASN
A
210
42.687
21.548
9.158
1.00
25.15
A


ATOM
1155
C
ASN
A
210
40.005
19.151
11.078
1.00
18.63
A


ATOM
1156
O
ASN
A
210
40.712
18.154
11.234
1.00
18.29
A


ATOM
1157
N
ILE
A
211
38.739
19.202
11.469
1.00
16.31
A


ATOM
1158
CA
ILE
A
211
38.090
18.058
12.085
1.00
15.49
A


ATOM
1159
CB
ILE
A
211
37.336
18.488
13.354
1.00
15.40
A


ATOM
1160
CG2
ILE
A
211
36.582
17.311
13.950
1.00
14.59
A


ATOM
1161
CG1
ILE
A
211
38.342
19.046
14.365
1.00
15.91
A


ATOM
1162
CD1
ILE
A
211
37.720
19.669
15.590
1.00
15.98
A


ATOM
1163
C
ILE
A
211
37.131
17.485
11.059
1.00
17.26
A


ATOM
1164
O
ILE
A
211
35.995
17.947
10.926
1.00
18.16
A


ATOM
1165
N
LEU
A
212
37.599
16.486
10.317
1.00
15.97
A


ATOM
1166
CA
LEU
A
212
36.784
15.875
9.274
1.00
17.08
A


ATOM
1167
CB
LEU
A
212
37.685
15.249
8.202
1.00
17.78
A


ATOM
1168
CG
LEU
A
212
38.785
16.157
7.640
1.00
18.92
A


ATOM
1169
CD1
LEU
A
212
39.476
15.450
6.485
1.00
22.09
A


ATOM
1170
CD2
LEU
A
212
38.188
17.482
7.166
1.00
19.91
A


ATOM
1171
C
LEU
A
212
35.843
14.825
9.837
1.00
18.35
A


ATOM
1172
O
LEU
A
212
35.957
14.433
11.002
1.00
19.39
A


ATOM
1173
N
LEU
A
213
34.915
14.368
9.000
1.00
17.84
A


ATOM
1174
CA
LEU
A
213
33.942
13.362
9.403
1.00
19.94
A


ATOM
1175
CB
LEU
A
213
32.556
14.004
9.487
1.00
20.84
A


ATOM
1176
CG
LEU
A
213
32.396
15.059
10.583
1.00
20.31
A


ATOM
1177
CD1
LEU
A
213
31.124
15.837
10.367
1.00
22.75
A


ATOM
1178
CD2
LEU
A
213
32.379
14.378
11.940
1.00
23.93
A


ATOM
1179
C
LEU
A
213
33.914
12.187
8.426
1.00
20.98
A


ATOM
1180
O
LEU
A
213
33.743
12.379
7.218
1.00
19.55
A


ATOM
1181
N
ASN
A
214
34.088
10.970
8.935
1.00
20.44
A


ATOM
1182
CA
ASN
A
214
34.055
9.814
8.049
1.00
23.77
A


ATOM
1183
CB
ASN
A
214
34.745
8.596
8.674
1.00
25.30
A


ATOM
1184
CG
ASN
A
214
34.077
8.127
9.948
1.00
32.04
A


ATOM
1185
OD1
ASN
A
214
32.908
8.422
10.206
1.00
34.43
A


ATOM
1186
ND2
ASN
A
214
34.818
7.369
10.752
1.00
33.85
A


ATOM
1187
C
ASN
A
214
32.618
9.466
7.693
1.00
24.07
A


ATOM
1188
O
ASN
A
214
31.672
10.113
8.150
1.00
19.94
A


ATOM
1189
N
GLU
A
215
32.459
8.433
6.879
1.00
25.77
A


ATOM
1190
CA
GLU
A
215
31.138
8.003
6.445
1.00
28.69
A


ATOM
1191
CB
GLU
A
215
31.275
6.796
5.513
1.00
31.98
A


ATOM
1192
CG
GLU
A
215
29.970
6.334
4.896
1.00
40.22
A


ATOM
1193
CD
GLU
A
215
30.182
5.312
3.795
1.00
44.27
A


ATOM
1194
OE1
GLU
A
215
30.817
4.268
4.065
1.00
46.46
A


ATOM
1195
OE2
GLU
A
215
29.716
5.556
2.660
1.00
46.13
A


ATOM
1196
C
GLU
A
215
30.188
7.673
7.601
1.00
28.41
A


ATOM
1197
O
GLU
A
215
28.971
7.769
7.447
1.00
28.52
A


ATOM
1198
N
ASP
A
216
30.737
7.287
8.752
1.00
26.77
A


ATOM
1199
CA
ASP
A
216
29.914
6.953
9.917
1.00
27.28
A


ATOM
1200
CB
ASP
A
216
30.538
5.795
10.696
1.00
31.27
A


ATOM
1201
CG
ASP
A
216
30.390
4.466
9.979
1.00
37.61
A


ATOM
1202
OD1
ASP
A
216
29.274
4.170
9.499
1.00
39.45
A


ATOM
1203
OD2
ASP
A
216
31.382
3.710
9.902
1.00
41.84
A


ATOM
1204
C
ASP
A
216
29.697
8.135
10.862
1.00
26.37
A


ATOM
1205
O
ASP
A
216
29.136
7.984
11.950
1.00
25.73
A


ATOM
1206
N
MET
A
217
30.156
9.306
10.441
1.00
23.02
A


ATOM
1207
CA
MET
A
217
30.015
10.527
11.218
1.00
21.83
A


ATOM
1208
CB
MET
A
217
28.537
10.789
11.517
1.00
23.24
A


ATOM
1209
CG
MET
A
217
27.742
11.186
10.274
1.00
22.98
A


ATOM
1210
SD
MET
A
217
28.464
12.616
9.430
1.00
27.57
A


ATOM
1211
CE
MET
A
217
27.679
13.974
10.332
1.00
26.68
A


ATOM
1212
C
MET
A
217
30.844
10.618
12.502
1.00
21.51
A


ATOM
1213
O
MET
A
217
30.474
11.323
13.440
1.00
18.62
A


ATOM
1214
N
HIS
A
218
31.957
9.892
12.544
1.00
20.10
A


ATOM
1215
CA
HIS
A
218
32.873
9.964
13.678
1.00
19.86
A


ATOM
1216
CB
HIS
A
218
33.482
8.594
13.977
1.00
20.21
A


ATOM
1217
CG
HIS
A
218
32.551
7.667
14.698
1.00
22.40
A


ATOM
1218
CD2
HIS
A
218
31.910
6.547
14.287
1.00
21.27
A


ATOM
1219
ND1
HIS
A
218
32.177
7.863
16.011
1.00
19.59
A


ATOM
1220
CE1
HIS
A
218
31.348
6.902
16.379
1.00
21.88
A


ATOM
1221
NE2
HIS
A
218
31.168
6.091
15.351
1.00
22.08
A


ATOM
1222
C
HIS
A
218
33.947
10.921
13.172
1.00
19.10
A


ATOM
1223
O
HIS
A
218
34.170
11.004
11.965
1.00
20.31
A


ATOM
1224
N
ILE
A
219
34.617
11.638
14.067
1.00
17.21
A


ATOM
1225
CA
ILE
A
219
35.628
12.586
13.618
1.00
15.26
A


ATOM
1226
CB
ILE
A
219
35.987
13.614
14.716
1.00
15.38
A


ATOM
1227
CG2
ILE
A
219
34.722
14.305
15.221
1.00
14.58
A


ATOM
1228
CG1
ILE
A
219
36.734
12.919
15.864
1.00
14.46
A


ATOM
1229
CD1
ILE
A
219
37.279
13.885
16.911
1.00
13.74
A


ATOM
1230
C
ILE
A
219
36.929
11.944
13.161
1.00
16.21
A


ATOM
1231
O
ILE
A
219
37.238
10.799
13.500
1.00
15.88
A


ATOM
1232
N
GLN
A
220
37.677
12.711
12.378
1.00
15.62
A


ATOM
1233
CA
GLN
A
220
38.980
12.316
11.876
1.00
17.84
A


ATOM
1234
CB
GLN
A
220
38.872
11.595
10.525
1.00
20.00
A


ATOM
1235
CG
GLN
A
220
38.463
10.129
10.659
1.00
26.97
A


ATOM
1236
CD
GLN
A
220
38.648
9.343
9.372
1.00
29.95
A


ATOM
1237
OE1
GLN
A
220
37.968
9.590
8.373
1.00
33.12
A


ATOM
1238
NE2
GLN
A
220
39.578
8.393
9.389
1.00
30.47
A


ATOM
1239
C
GLN
A
220
39.757
13.610
11.735
1.00
17.00
A


ATOM
1240
O
GLN
A
220
39.609
14.339
10.751
1.00
18.27
A


ATOM
1241
N
ILE
A
221
40.566
13.906
12.746
1.00
14.34
A


ATOM
1242
CA
ILE
A
221
41.361
15.120
12.753
1.00
14.46
A


ATOM
1243
CB
ILE
A
221
41.867
15.416
14.175
1.00
12.30
A


ATOM
1244
CG2
ILE
A
221
42.764
16.656
14.167
1.00
14.78
A


ATOM
1245
CG1
ILE
A
221
40.660
15.613
15.102
1.00
13.92
A


ATOM
1246
CD1
ILE
A
221
41.003
15.901
16.543
1.00
15.06
A


ATOM
1247
C
ILE
A
221
42.536
14.996
11.783
1.00
15.44
A


ATOM
1248
O
ILE
A
221
43.106
13.915
11.613
1.00
13.93
A


ATOM
1249
N
THR
A
222
42.877
16.101
11.127
1.00
15.36
A


ATOM
1250
CA
THR
A
222
43.980
16.098
10.174
1.00
17.52
A


ATOM
1251
CB
THR
A
222
43.470
15.836
8.750
1.00
19.92
A


ATOM
1252
OG1
THR
A
222
44.587
15.637
7.875
1.00
18.78
A


ATOM
1253
CG2
THR
A
222
42.630
17.018
8.257
1.00
18.16
A


ATOM
1254
C
THR
A
222
44.735
17.428
10.192
1.00
19.60
A


ATOM
1255
O
THR
A
222
44.509
18.257
11.084
1.00
18.59
A


ATOM
1256
N
ASP
A
223
45.630
17.610
9.216
1.00
18.69
A


ATOM
1257
CA
ASP
A
223
46.440
18.825
9.069
1.00
20.12
A


ATOM
1258
CB
ASP
A
223
45.532
20.065
9.108
1.00
23.51
A


ATOM
1259
CG
ASP
A
223
46.248
21.335
8.670
1.00
27.09
A


ATOM
1260
OD1
ASP
A
223
47.283
21.227
7.975
1.00
26.28
A


ATOM
1261
OD2
ASP
A
223
45.765
22.438
9.009
1.00
26.15
A


ATOM
1262
C
ASP
A
223
47.516
18.913
10.150
1.00
21.73
A


ATOM
1263
O
ASP
A
223
47.439
19.751
11.055
1.00
22.76
A


ATOM
1264
N
PHE
A
224
48.535
18.063
10.027
1.00
20.75
A


ATOM
1265
CA
PHE
A
224
49.611
17.988
11.009
1.00
20.11
A


ATOM
1266
CB
PHE
A
224
49.805
16.527
11.424
1.00
20.62
A


ATOM
1267
CG
PHE
A
224
48.682
15.991
12.263
1.00
21.41
A


ATOM
1268
CD1
PHE
A
224
48.598
16.312
13.614
1.00
23.05
A


ATOM
1269
CD2
PHE
A
224
47.681
15.212
11.693
1.00
22.27
A


ATOM
1270
CE1
PHE
A
224
47.528
15.868
14.389
1.00
23.30
A


ATOM
1271
CE2
PHE
A
224
46.606
14.763
12.457
1.00
21.11
A


ATOM
1272
CZ
PHE
A
224
46.530
15.093
13.807
1.00
22.02
A


ATOM
1273
C
PHE
A
224
50.957
18.583
10.619
1.00
20.45
A


ATOM
1274
O
PHE
A
224
51.905
18.547
11.407
1.00
20.73
A


ATOM
1275
N
GLY
A
225
51.049
19.125
9.412
1.00
22.02
A


ATOM
1276
CA
GLY
A
225
52.301
19.713
8.981
1.00
22.66
A


ATOM
1277
C
GLY
A
225
52.742
20.822
9.920
1.00
24.99
A


ATOM
1278
O
GLY
A
225
53.939
21.041
10.122
1.00
24.52
A


ATOM
1279
N
THR
A
226
51.779
21.524
10.508
1.00
23.50
A


ATOM
1280
CA
THR
A
226
52.106
22.613
11.416
1.00
25.16
A


ATOM
1281
CB
THR
A
226
51.199
23.829
11.160
1.00
24.76
A


ATOM
1282
OG1
THR
A
226
49.831
23.410
11.113
1.00
22.68
A


ATOM
1283
CG2
THR
A
226
51.571
24.490
9.834
1.00
25.00
A


ATOM
1284
C
THR
A
226
52.046
22.233
12.894
1.00
25.79
A


ATOM
1285
O
THR
A
226
52.019
23.100
13.768
1.00
24.54
A


ATOM
1286
N
ALA
A
227
52.037
20.935
13.173
1.00
24.97
A


ATOM
1287
CA
ALA
A
227
52.004
20.475
14.550
1.00
25.49
A


ATOM
1288
CB
ALA
A
227
51.659
18.993
14.607
1.00
22.85
A


ATOM
1289
C
ALA
A
227
53.384
20.715
15.149
1.00
27.70
A


ATOM
1290
O
ALA
A
227
54.331
21.047
14.435
1.00
26.60
A


ATOM
1291
N
LYS
A
228
53.491
20.558
16.461
1.00
28.53
A


ATOM
1292
CA
LYS
A
228
54.760
20.745
17.149
1.00
32.12
A


ATOM
1293
CB
LYS
A
228
54.699
21.974
18.054
1.00
33.81
A


ATOM
1294
CG
LYS
A
228
56.007
22.294
18.765
1.00
41.23
A


ATOM
1295
CD
LYS
A
228
57.082
22.725
17.768
1.00
47.57
A


ATOM
1296
CE
LYS
A
228
58.401
23.056
18.462
1.00
49.82
A


ATOM
1297
NZ
LYS
A
228
59.459
23.425
17.480
1.00
51.49
A


ATOM
1298
C
LYS
A
228
55.019
19.504
17.985
1.00
33.25
A


ATOM
1299
O
LYS
A
228
54.190
19.129
18.815
1.00
33.70
A


ATOM
1300
N
VAL
A
229
56.159
18.860
17.756
1.00
33.64
A


ATOM
1301
CA
VAL
A
229
56.516
17.661
18.501
1.00
34.66
A


ATOM
1302
CB
VAL
A
229
57.248
16.646
17.609
1.00
33.50
A


ATOM
1303
CG1
VAL
A
229
57.619
15.419
18.415
1.00
32.34
A


ATOM
1304
CG2
VAL
A
229
56.370
16.264
16.436
1.00
34.25
A


ATOM
1305
C
VAL
A
229
57.420
18.035
19.668
1.00
37.57
A


ATOM
1306
O
VAL
A
229
58.581
18.392
19.474
1.00
35.91
A


ATOM
1307
N
LEU
A
230
56.877
17.948
20.878
1.00
40.57
A


ATOM
1308
CA
LEU
A
230
57.615
18.289
22.088
1.00
46.10
A


ATOM
1309
CB
LEU
A
230
56.654
18.417
23.270
1.00
44.71
A


ATOM
1310
CG
LEU
A
230
55.627
19.545
23.207
1.00
44.50
A


ATOM
1311
CD1
LEU
A
230
54.673
19.430
24.383
1.00
44.39
A


ATOM
1312
CD2
LEU
A
230
56.340
20.885
23.214
1.00
44.81
A


ATOM
1313
C
LEU
A
230
58.695
17.279
22.440
1.00
50.42
A


ATOM
1314
O
LEU
A
230
58.603
16.104
22.089
1.00
51.64
A


ATOM
1315
N
SER
A
231
59.717
17.756
23.145
1.00
55.81
A


ATOM
1316
CA
SER
A
231
60.824
16.914
23.583
1.00
61.14
A


ATOM
1317
CB
SER
A
231
62.077
17.200
22.750
1.00
61.27
A


ATOM
1318
OG
SER
A
231
62.444
18.568
22.823
1.00
62.85
A


ATOM
1319
C
SER
A
231
61.124
17.126
25.071
1.00
64.65
A


ATOM
1320
O
SER
A
231
61.392
16.164
25.794
1.00
65.70
A


ATOM
1321
N
PRO
A
232
61.081
18.387
25.549
1.00
67.54
A


ATOM
1322
CD
PRO
A
232
60.854
19.651
24.823
1.00
68.60
A


ATOM
1323
CA
PRO
A
232
61.358
18.655
26.966
1.00
68.74
A


ATOM
1324
CB
PRO
A
232
61.109
20.158
27.086
1.00
68.83
A


ATOM
1325
CG
PRO
A
232
61.505
20.666
25.737
1.00
68.96
A


ATOM
1326
C
PRO
A
232
60.460
17.846
27.899
1.00
69.17
A


ATOM
1327
O
PRO
A
232
59.335
17.494
27.541
1.00
69.94
A


ATOM
1328
N
ALA
A
237
57.424
23.198
27.637
1.00
80.06
A


ATOM
1329
CA
ALA
A
237
56.783
23.047
26.335
1.00
79.29
A


ATOM
1330
CB
ALA
A
237
55.275
22.907
26.512
1.00
78.64
A


ATOM
1331
C
ALA
A
237
57.092
24.239
25.433
1.00
79.07
A


ATOM
1332
O
ALA
A
237
56.250
25.113
25.249
1.00
79.47
A


ATOM
1333
N
ALA
A
238
58.297
24.280
24.871
1.00
78.57
A


ATOM
1334
CA
ALA
A
238
58.683
25.383
23.992
1.00
78.50
A


ATOM
1335
CB
ALA
A
238
60.186
25.347
23.728
1.00
78.50
A


ATOM
1336
C
ALA
A
238
57.920
25.327
22.673
1.00
78.15
A


ATOM
1337
O
ALA
A
238
57.243
24.341
22.375
1.00
77.96
A


ATOM
1338
N
ALA
A
239
58.027
26.393
21.887
1.00
77.28
A


ATOM
1339
CA
ALA
A
239
57.338
26.452
20.603
1.00
76.27
A


ATOM
1340
CB
ALA
A
239
55.849
26.489
20.827
1.00
76.61
A


ATOM
1341
C
ALA
A
239
57.766
27.667
19.793
1.00
75.38
A


ATOM
1342
O
ALA
A
239
58.955
27.955
19.700
1.00
75.89
A


ATOM
1343
N
ASN
A
240
56.781
28.357
19.214
1.00
73.95
A


ATOM
1344
CA
ASN
A
240
56.967
29.553
18.389
1.00
71.07
A


ATOM
1345
CB
ASN
A
240
58.151
30.400
18.874
1.00
71.47
A


ATOM
1346
CG
ASN
A
240
59.459
30.055
18.174
1.00
72.06
A


ATOM
1347
OD1
ASN
A
240
59.575
30.149
16.943
1.00
72.03
A


ATOM
1348
ND2
ASN
A
240
60.470
29.665
18.964
1.00
71.91
A


ATOM
1349
C
ASN
A
240
57.188
29.178
16.928
1.00
69.41
A


ATOM
1350
O
ASN
A
240
57.480
28.024
16.624
1.00
70.09
A


ATOM
1351
N
ALA
A
241
57.055
30.165
16.038
1.00
66.62
A


ATOM
1352
CA
ALA
A
241
57.246
30.013
14.585
1.00
63.94
A


ATOM
1353
C
ALA
A
241
55.952
30.080
13.772
1.00
60.63
A


ATOM
1354
O
ALA
A
241
55.840
30.880
12.845
1.00
61.29
A


ATOM
1355
CB
ALA
A
241
57.979
28.704
14.246
1.00
65.23
A


ATOM
1356
N
PHE
A
242
54.984
29.236
14.113
1.00
56.72
A


ATOM
1357
CA
PHE
A
242
53.712
29.196
13.394
1.00
52.53
A


ATOM
1358
CB
PHE
A
242
53.419
27.767
12.923
1.00
49.14
A


ATOM
1359
CG
PHE
A
242
52.040
27.590
12.354
1.00
47.38
A


ATOM
1360
CD1
PHE
A
242
51.731
28.067
11.085
1.00
47.69
A


ATOM
1361
CD2
PHE
A
242
51.038
26.975
13.102
1.00
45.45
A


ATOM
1362
CE1
PHE
A
242
50.445
27.937
10.565
1.00
46.75
A


ATOM
1363
CE2
PHE
A
242
49.751
26.840
12.594
1.00
45.41
A


ATOM
1364
CZ
PHE
A
242
49.453
27.323
11.322
1.00
46.55
A


ATOM
1365
C
PHE
A
242
52.534
29.688
14.229
1.00
50.08
A


ATOM
1366
O
PHE
A
242
52.502
29.505
15.444
1.00
49.86
A


ATOM
1367
N
VAL
A
243
51.566
30.305
13.557
1.00
47.67
A


ATOM
1368
CA
VAL
A
243
50.355
30.809
14.200
1.00
46.21
A


ATOM
1369
CB
VAL
A
243
50.340
32.352
14.258
1.00
47.36
A


ATOM
1370
CG1
VAL
A
243
49.012
32.844
14.825
1.00
47.54
A


ATOM
1371
CG2
VAL
A
243
51.497
32.842
15.109
1.00
48.50
A


ATOM
1372
C
VAL
A
243
49.150
30.342
13.389
1.00
44.12
A


ATOM
1373
O
VAL
A
243
48.956
30.765
12.247
1.00
44.46
A


ATOM
1374
N
GLY
A
244
48.348
29.467
13.985
1.00
40.48
A


ATOM
1375
CA
GLY
A
244
47.176
28.941
13.306
1.00
37.65
A


ATOM
1376
C
GLY
A
244
46.101
29.960
12.964
1.00
35.39
A


ATOM
1377
O
GLY
A
244
46.313
31.168
13.065
1.00
35.92
A


ATOM
1378
N
THR
A
245
44.936
29.463
12.560
1.00
33.30
A


ATOM
1379
CA
THR
A
245
43.813
30.312
12.184
1.00
30.20
A


ATOM
1380
CB
THR
A
245
42.593
29.450
11.829
1.00
32.00
A


ATOM
1381
OG1
THR
A
245
42.952
28.573
10.755
1.00
32.81
A


ATOM
1382
CG2
THR
A
245
41.419
30.319
11.390
1.00
28.34
A


ATOM
1383
C
THR
A
245
43.476
31.296
13.296
1.00
27.96
A


ATOM
1384
O
THR
A
245
43.212
30.907
14.434
1.00
25.46
A


ATOM
1385
N
ALA
A
246
43.486
32.576
12.938
1.00
25.22
A


ATOM
1386
CA
ALA
A
246
43.247
33.675
13.867
1.00
23.27
A


ATOM
1387
CB
ALA
A
246
42.956
34.955
13.082
1.00
22.94
A


ATOM
1388
C
ALA
A
246
42.178
33.475
14.934
1.00
21.27
A


ATOM
1389
O
ALA
A
246
42.431
33.705
16.114
1.00
20.93
A


ATOM
1390
N
GLN
A
247
40.988
33.047
14.536
1.00
19.67
A


ATOM
1391
CA
GLN
A
247
39.911
32.886
15.504
1.00
20.17
A


ATOM
1392
CB
GLN
A
247
38.608
32.535
14.779
1.00
21.89
A


ATOM
1393
CG
GLN
A
247
38.522
33.076
13.355
1.00
26.18
A


ATOM
1394
CD
GLN
A
247
37.220
33.794
13.064
1.00
27.30
A


ATOM
1395
OE1
GLN
A
247
36.172
33.447
13.605
1.00
30.13
A


ATOM
1396
NE2
GLN
A
247
37.278
34.792
12.189
1.00
28.70
A


ATOM
1397
C
GLN
A
247
40.181
31.849
16.595
1.00
19.43
A


ATOM
1398
O
GLN
A
247
39.546
31.883
17.648
1.00
18.93
A


ATOM
1399
N
TYR
A
248
41.132
30.948
16.359
1.00
18.60
A


ATOM
1400
CA
TYR
A
248
41.441
29.896
17.329
1.00
19.20
A


ATOM
1401
CB
TYR
A
248
41.333
28.529
16.642
1.00
17.53
A


ATOM
1402
CG
TYR
A
248
40.013
28.362
15.927
1.00
19.32
A


ATOM
1403
CD1
TYR
A
248
38.859
28.010
16.625
1.00
17.69
A


ATOM
1404
CE1
TYR
A
248
37.617
27.976
15.990
1.00
18.18
A


ATOM
1405
CD2
TYR
A
248
39.897
28.664
14.569
1.00
16.87
A


ATOM
1406
CE2
TYR
A
248
38.665
28.635
13.924
1.00
19.17
A


ATOM
1407
CZ
TYR
A
248
37.527
28.295
14.643
1.00
19.46
A


ATOM
1408
OH
TYR
A
248
36.299
28.311
14.023
1.00
18.98
A


ATOM
1409
C
TYR
A
248
42.810
30.039
17.993
1.00
20.42
A


ATOM
1410
O
TYR
A
248
43.208
29.191
18.792
1.00
19.19
A


ATOM
1411
N
VAL
A
249
43.523
31.114
17.673
1.00
20.20
A


ATOM
1412
CA
VAL
A
249
44.841
31.343
18.251
1.00
20.91
A


ATOM
1413
CB
VAL
A
249
45.542
32.532
17.570
1.00
21.18
A


ATOM
1414
CG1
VAL
A
249
46.821
32.896
18.317
1.00
22.45
A


ATOM
1415
CG2
VAL
A
249
45.862
32.170
16.139
1.00
24.01
A


ATOM
1416
C
VAL
A
249
44.764
31.606
19.750
1.00
21.52
A


ATOM
1417
O
VAL
A
249
43.915
32.368
20.216
1.00
22.72
A


ATOM
1418
N
SER
A
250
45.654
30.965
20.503
1.00
20.70
A


ATOM
1419
CA
SER
A
250
45.697
31.133
21.951
1.00
21.65
A


ATOM
1420
CB
SER
A
250
46.370
29.919
22.613
1.00
22.02
A


ATOM
1421
OG
SER
A
250
47.692
29.725
22.132
1.00
22.12
A


ATOM
1422
C
SER
A
250
46.476
32.402
22.280
1.00
22.13
A


ATOM
1423
O
SER
A
250
47.332
32.828
21.511
1.00
22.77
A


ATOM
1424
N
PRO
A
251
46.180
33.029
23.425
1.00
22.23
A


ATOM
1425
CD
PRO
A
251
45.163
32.684
24.433
1.00
22.97
A


ATOM
1426
CA
PRO
A
251
46.893
34.254
23.800
1.00
22.52
A


ATOM
1427
CB
PRO
A
251
46.233
34.650
25.127
1.00
23.06
A


ATOM
1428
CG
PRO
A
251
45.726
33.329
25.676
1.00
22.55
A


ATOM
1429
C
PRO
A
251
48.414
34.115
23.907
1.00
22.15
A


ATOM
1430
O
PRO
A
251
49.143
35.047
23.563
1.00
22.62
A


ATOM
1431
N
GLU
A
252
48.901
32.966
24.367
1.00
20.69
A


ATOM
1432
CA
GLU
A
252
50.347
32.772
24.500
1.00
21.40
A


ATOM
1433
CB
GLU
A
252
50.673
31.382
25.071
1.00
20.59
A


ATOM
1434
CG
GLU
A
252
49.993
30.232
24.352
1.00
21.91
A


ATOM
1435
CD
GLU
A
252
48.691
29.822
25.014
1.00
21.51
A


ATOM
1436
OE1
GLU
A
252
47.989
30.707
25.550
1.00
21.46
A


ATOM
1437
OE2
GLU
A
252
48.367
28.613
24.993
1.00
20.23
A


ATOM
1438
C
GLU
A
252
51.071
32.970
23.167
1.00
22.99
A


ATOM
1439
O
GLU
A
252
52.191
33.480
23.136
1.00
23.17
A


ATOM
1440
N
LEU
A
253
50.441
32.576
22.064
1.00
23.00
A


ATOM
1441
CA
LEU
A
253
51.068
32.753
20.758
1.00
25.62
A


ATOM
1442
CB
LEU
A
253
50.277
32.029
19.669
1.00
26.75
A


ATOM
1443
CG
LEU
A
253
50.743
30.620
19.296
1.00
31.87
A


ATOM
1444
CD1
LEU
A
253
50.433
29.651
20.422
1.00
31.81
A


ATOM
1445
CD2
LEU
A
253
50.044
30.179
18.015
1.00
31.86
A


ATOM
1446
C
LEU
A
253
51.201
34.228
20.371
1.00
26.94
A


ATOM
1447
O
LEU
A
253
52.107
34.601
19.626
1.00
27.09
A


ATOM
1448
N
LEU
A
254
50.297
35.059
20.877
1.00
25.83
A


ATOM
1449
CA
LEU
A
254
50.297
36.485
20.564
1.00
27.26
A


ATOM
1450
CB
LEU
A
254
48.858
37.006
20.564
1.00
25.84
A


ATOM
1451
CG
LEU
A
254
47.882
36.290
19.621
1.00
24.69
A


ATOM
1452
CD1
LEU
A
254
46.459
36.724
19.932
1.00
23.64
A


ATOM
1453
CD2
LEU
A
254
48.236
36.597
18.177
1.00
24.24
A


ATOM
1454
C
LEU
A
254
51.134
37.314
21.537
1.00
30.62
A


ATOM
1455
O
LEU
A
254
51.633
38.383
21.187
1.00
32.35
A


ATOM
1456
N
THR
A
255
51.292
36.821
22.758
1.00
32.47
A


ATOM
1457
CA
THR
A
255
52.056
37.547
23.759
1.00
36.70
A


ATOM
1458
CB
THR
A
255
51.368
37.478
25.127
1.00
34.51
A


ATOM
1459
OG1
THR
A
255
51.188
36.106
25.494
1.00
35.49
A


ATOM
1460
CG2
THR
A
255
50.013
38.166
25.077
1.00
33.40
A


ATOM
1461
C
THR
A
255
53.477
37.035
23.910
1.00
40.09
A


ATOM
1462
O
THR
A
255
54.430
37.793
23.772
1.00
43.69
A


ATOM
1463
N
GLU
A
256
53.617
35.747
24.189
1.00
44.77
A


ATOM
1464
CA
GLU
A
256
54.932
35.144
24.382
1.00
49.15
A


ATOM
1465
CB
GLU
A
256
54.866
34.143
25.534
1.00
51.24
A


ATOM
1466
CG
GLU
A
256
54.514
34.786
26.862
1.00
56.03
A


ATOM
1467
CD
GLU
A
256
54.053
33.780
27.893
1.00
58.83
A


ATOM
1468
OE1
GLU
A
256
54.766
32.776
28.107
1.00
62.13
A


ATOM
1469
OE2
GLU
A
256
52.979
33.996
28.494
1.00
60.34
A


ATOM
1470
C
GLU
A
256
55.475
34.456
23.137
1.00
50.09
A


ATOM
1471
O
GLU
A
256
56.616
33.995
23.127
1.00
50.42
A


ATOM
1472
N
LYS
A
257
54.658
34.389
22.090
1.00
51.21
A


ATOM
1473
CA
LYS
A
257
55.064
33.746
20.845
1.00
51.22
A


ATOM
1474
CB
LYS
A
257
56.244
34.502
20.227
1.00
53.28
A


ATOM
1475
CG
LYS
A
257
56.558
34.125
18.790
1.00
55.19
A


ATOM
1476
CD
LYS
A
257
57.709
34.961
18.253
1.00
57.52
A


ATOM
1477
CE
LYS
A
257
57.952
34.694
16.777
1.00
58.52
A


ATOM
1478
NZ
LYS
A
257
58.290
33.268
16.515
1.00
60.88
A


ATOM
1479
C
LYS
A
257
55.467
32.302
21.138
1.00
50.74
A


ATOM
1480
O
LYS
A
257
56.432
31.790
20.577
1.00
52.26
A


ATOM
1481
N
SER
A
258
54.721
31.654
22.027
1.00
48.07
A


ATOM
1482
CA
SER
A
258
54.999
30.273
22.402
1.00
46.87
A


ATOM
1483
CB
SER
A
258
55.590
30.229
23.812
1.00
48.88
A


ATOM
1484
OG
SER
A
258
54.741
30.892
24.734
1.00
53.14
A


ATOM
1485
C
SER
A
258
53.735
29.415
22.342
1.00
44.07
A


ATOM
1486
O
SER
A
258
52.617
29.932
22.417
1.00
44.17
A


ATOM
1487
N
ALA
A
259
53.917
28.105
22.204
1.00
38.30
A


ATOM
1488
CA
ALA
A
259
52.793
27.180
22.127
1.00
34.73
A


ATOM
1489
CB
ALA
A
259
52.551
26.779
20.684
1.00
34.16
A


ATOM
1490
C
ALA
A
259
53.042
25.940
22.977
1.00
32.34
A


ATOM
1491
O
ALA
A
259
54.172
25.459
23.086
1.00
31.81
A


ATOM
1492
N
CYS
A
260
51.975
25.428
23.579
1.00
28.58
A


ATOM
1493
CA
CYS
A
260
52.056
24.244
24.425
1.00
26.27
A


ATOM
1494
CB
CYS
A
260
52.183
24.654
25.892
1.00
26.53
A


ATOM
1495
SG
CYS
A
260
50.846
25.739
26.469
1.00
32.91
A


ATOM
1496
C
CYS
A
260
50.786
23.435
24.224
1.00
22.83
A


ATOM
1497
O
CYS
A
260
49.892
23.856
23.495
1.00
22.14
A


ATOM
1498
N
LYS
A
261
50.706
22.277
24.868
1.00
20.02
A


ATOM
1499
CA
LYS
A
261
49.526
21.434
24.744
1.00
20.65
A


ATOM
1500
CB
LYS
A
261
49.619
20.243
25.696
1.00
23.28
A


ATOM
1501
CG
LYS
A
261
50.716
19.253
25.347
1.00
27.44
A


ATOM
1502
CD
LYS
A
261
50.732
18.117
26.350
1.00
29.98
A


ATOM
1503
CE
LYS
A
261
51.922
17.203
26.134
1.00
32.34
A


ATOM
1504
NZ
LYS
A
261
51.940
16.121
27.153
1.00
33.28
A


ATOM
1505
C
LYS
A
261
48.268
22.229
25.062
1.00
19.20
A


ATOM
1506
O
LYS
A
261
47.253
22.092
24.387
1.00
18.08
A


ATOM
1507
N
SER
A
262
48.358
23.068
26.089
1.00
16.92
A


ATOM
1508
CA
SER
A
262
47.235
23.883
26.534
1.00
18.13
A


ATOM
1509
CB
SER
A
262
47.644
24.698
27.770
1.00
18.27
A


ATOM
1510
OG
SER
A
262
46.517
25.258
28.421
1.00
22.53
A


ATOM
1511
C
SER
A
262
46.736
24.811
25.424
1.00
16.77
A


ATOM
1512
O
SER
A
262
45.591
25.254
25.450
1.00
15.69
A


ATOM
1513
N
SER
A
263
47.595
25.118
24.456
1.00
16.44
A


ATOM
1514
CA
SER
A
263
47.175
25.970
23.347
1.00
16.89
A


ATOM
1515
CB
SER
A
263
48.340
26.228
22.382
1.00
18.49
A


ATOM
1516
OG
SER
A
263
49.402
26.909
23.031
1.00
22.10
A


ATOM
1517
C
SER
A
263
46.040
25.257
22.612
1.00
17.79
A


ATOM
1518
O
SER
A
263
45.099
25.898
22.148
1.00
17.57
A


ATOM
1519
N
ASP
A
264
46.119
23.928
22.517
1.00
16.30
A


ATOM
1520
CA
ASP
A
264
45.069
23.166
21.836
1.00
16.72
A


ATOM
1521
CB
ASP
A
264
45.483
21.704
21.620
1.00
15.92
A


ATOM
1522
CG
ASP
A
264
46.544
21.539
20.548
1.00
17.93
A


ATOM
1523
OD1
ASP
A
264
46.642
22.412
19.661
1.00
16.78
A


ATOM
1524
OD2
ASP
A
264
47.265
20.515
20.579
1.00
16.64
A


ATOM
1525
C
ASP
A
264
43.773
23.194
22.646
1.00
17.67
A


ATOM
1526
O
ASP
A
264
42.681
23.197
22.076
1.00
18.27
A


ATOM
1527
N
LEU
A
265
43.898
23.205
23.974
1.00
15.49
A


ATOM
1528
CA
LEU
A
265
42.730
23.232
24.849
1.00
14.75
A


ATOM
1529
CB
LEU
A
265
43.147
23.038
26.313
1.00
11.38
A


ATOM
1530
CG
LEU
A
265
43.711
21.641
26.621
1.00
14.04
A


ATOM
1531
CD1
LEU
A
265
44.249
21.579
28.052
1.00
13.96
A


ATOM
1532
CD2
LEU
A
265
42.619
20.603
26.416
1.00
11.62
A


ATOM
1533
C
LEU
A
265
41.999
24.557
24.675
1.00
15.13
A


ATOM
1534
O
LEU
A
265
40.777
24.620
24.785
1.00
16.75
A


ATOM
1535
N
TRP
A
266
42.746
25.622
24.405
1.00
16.08
A


ATOM
1536
CA
TRP
A
266
42.118
26.918
24.184
1.00
16.96
A


ATOM
1537
CB
TRP
A
266
43.176
28.015
24.023
1.00
17.28
A


ATOM
1538
CG
TRP
A
266
42.618
29.326
23.521
1.00
20.54
A


ATOM
1539
CD2
TRP
A
266
42.313
30.490
24.301
1.00
20.07
A


ATOM
1540
CE2
TRP
A
266
41.782
31.459
23.417
1.00
20.46
A


ATOM
1541
CE3
TRP
A
266
42.435
30.810
25.660
1.00
20.68
A


ATOM
1542
CD1
TRP
A
266
42.270
29.631
22.231
1.00
19.53
A


ATOM
1543
NE1
TRP
A
266
41.769
30.908
22.163
1.00
19.61
A


ATOM
1544
CZ2
TRP
A
266
41.372
32.727
23.850
1.00
20.90
A


ATOM
1545
CZ3
TRP
A
266
42.026
32.073
26.091
1.00
19.45
A


ATOM
1546
CH2
TRP
A
266
41.501
33.015
25.185
1.00
20.71
A


ATOM
1547
C
TRP
A
266
41.284
26.795
22.913
1.00
17.22
A


ATOM
1548
O
TRP
A
266
40.139
27.240
22.863
1.00
18.03
A


ATOM
1549
N
ALA
A
267
41.863
26.181
21.886
1.00
17.50
A


ATOM
1550
CA
ALA
A
267
41.155
25.990
20.626
1.00
16.16
A


ATOM
1551
CB
ALA
A
267
42.050
25.290
19.621
1.00
14.28
A


ATOM
1552
C
ALA
A
267
39.901
25.159
20.891
1.00
16.28
A


ATOM
1553
O
ALA
A
267
38.835
25.436
20.346
1.00
16.46
A


ATOM
1554
N
LEU
A
268
40.031
24.144
21.739
1.00
16.57
A


ATOM
1555
CA
LEU
A
268
38.890
23.299
22.084
1.00
17.03
A


ATOM
1556
CB
LEU
A
268
39.292
22.260
23.139
1.00
15.35
A


ATOM
1557
CG
LEU
A
268
38.158
21.429
23.754
1.00
19.00
A


ATOM
1558
CD1
LEU
A
268
37.505
20.578
22.678
1.00
16.17
A


ATOM
1559
CD2
LEU
A
268
38.718
20.537
24.881
1.00
17.49
A


ATOM
1560
C
LEU
A
268
37.766
24.179
22.628
1.00
15.72
A


ATOM
1561
O
LEU
A
268
36.603
24.031
22.247
1.00
15.28
A


ATOM
1562
N
GLY
A
269
38.119
25.099
23.520
1.00
14.34
A


ATOM
1563
CA
GLY
A
269
37.124
25.989
24.092
1.00
13.39
A


ATOM
1564
C
GLY
A
269
36.406
26.808
23.031
1.00
14.94
A


ATOM
1565
O
GLY
A
269
35.193
27.014
23.114
1.00
14.76
A


ATOM
1566
N
CYS
A
270
37.146
27.279
22.030
1.00
13.86
A


ATOM
1567
CA
CYS
A
270
36.539
28.061
20.958
1.00
16.80
A


ATOM
1568
CB
CYS
A
270
37.611
28.634
20.023
1.00
15.97
A


ATOM
1569
SG
CYS
A
270
38.751
29.810
20.780
1.00
20.48
A


ATOM
1570
C
CYS
A
270
35.598
27.175
20.140
1.00
17.50
A


ATOM
1571
O
CYS
A
270
34.516
27.604
19.741
1.00
18.38
A


ATOM
1572
N
ILE
A
271
36.022
25.939
19.887
1.00
16.99
A


ATOM
1573
CA
ILE
A
271
35.221
25.004
19.104
1.00
16.66
A


ATOM
1574
CB
ILE
A
271
36.038
23.741
18.778
1.00
16.53
A


ATOM
1575
CG2
ILE
A
271
35.155
22.694
18.102
1.00
16.34
A


ATOM
1576
CG1
ILE
A
271
37.222
24.129
17.882
1.00
15.59
A


ATOM
1577
CD1
ILE
A
271
38.239
23.018
17.690
1.00
14.88
A


ATOM
1578
C
ILE
A
271
33.920
24.626
19.809
1.00
16.74
A


ATOM
1579
O
ILE
A
271
32.865
24.576
19.179
1.00
17.12
A


ATOM
1580
N
ILE
A
272
33.990
24.357
21.111
1.00
16.13
A


ATOM
1581
CA
ILE
A
272
32.785
24.021
21.862
1.00
18.30
A


ATOM
1582
CB
ILE
A
272
33.097
23.747
23.346
1.00
17.77
A


ATOM
1583
CG2
ILE
A
272
31.796
23.666
24.152
1.00
17.96
A


ATOM
1584
CG1
ILE
A
272
33.877
22.437
23.481
1.00
19.55
A


ATOM
1585
CD1
ILE
A
272
34.446
22.217
24.886
1.00
18.64
A


ATOM
1586
C
ILE
A
272
31.824
25.207
21.776
1.00
19.51
A


ATOM
1587
O
ILE
A
272
30.624
25.037
21.554
1.00
20.44
A


ATOM
1588
N
TYR
A
273
32.362
26.409
21.947
1.00
18.52
A


ATOM
1589
CA
TYR
A
273
31.553
27.615
21.881
1.00
20.48
A


ATOM
1590
CB
TYR
A
273
32.418
28.847
22.162
1.00
18.98
A


ATOM
1591
CG
TYR
A
273
31.663
30.161
22.125
1.00
20.26
A


ATOM
1592
CD1
TYR
A
273
31.229
30.709
20.916
1.00
20.67
A


ATOM
1593
CE1
TYR
A
273
30.536
31.917
20.880
1.00
20.98
A


ATOM
1594
CD2
TYR
A
273
31.383
30.857
23.302
1.00
19.82
A


ATOM
1595
CE2
TYR
A
273
30.691
32.062
23.280
1.00
20.62
A


ATOM
1596
CZ
TYR
A
273
30.271
32.587
22.067
1.00
21.15
A


ATOM
1597
OH
TYR
A
273
29.588
33.776
22.049
1.00
21.86
A


ATOM
1598
C
TYR
A
273
30.902
27.730
20.507
1.00
21.54
A


ATOM
1599
O
TYR
A
273
29.719
28.049
20.401
1.00
22.80
A


ATOM
1600
N
GLN
A
274
31.676
27.454
19.461
1.00
21.05
A


ATOM
1601
CA
GLN
A
274
31.176
27.538
18.095
1.00
21.48
A


ATOM
1602
CB
GLN
A
274
32.323
27.341
17.097
1.00
21.41
A


ATOM
1603
CG
GLN
A
274
31.934
27.596
15.645
1.00
23.15
A


ATOM
1604
CD
GLN
A
274
33.131
27.588
14.706
1.00
24.80
A


ATOM
1605
OE1
GLN
A
274
34.276
27.446
15.139
1.00
22.51
A


ATOM
1606
NE2
GLN
A
274
32.870
27.750
13.413
1.00
22.96
A


ATOM
1607
C
GLN
A
274
30.076
26.517
17.828
1.00
21.51
A


ATOM
1608
O
GLN
A
274
29.123
26.806
17.108
1.00
20.50
A


ATOM
1609
N
LEU
A
275
30.207
25.324
18.403
1.00
21.44
A


ATOM
1610
CA
LEU
A
275
29.196
24.282
18.208
1.00
20.95
A


ATOM
1611
CB
LEU
A
275
29.645
22.958
18.846
1.00
19.11
A


ATOM
1612
CG
LEU
A
275
30.775
22.182
18.159
1.00
21.43
A


ATOM
1613
CD1
LEU
A
275
31.118
20.936
18.963
1.00
17.64
A


ATOM
1614
CD2
LEU
A
275
30.342
21.795
16.754
1.00
20.34
A


ATOM
1615
C
LEU
A
275
27.860
24.697
18.815
1.00
21.32
A


ATOM
1616
O
LEU
A
275
26.802
24.461
18.229
1.00
19.75
A


ATOM
1617
N
VAL
A
276
27.921
25.322
19.987
1.00
19.10
A


ATOM
1618
CA
VAL
A
276
26.724
25.750
20.702
1.00
22.47
A


ATOM
1619
CB
VAL
A
276
27.011
25.882
22.217
1.00
20.87
A


ATOM
1620
CG1
VAL
A
276
25.742
26.291
22.957
1.00
19.68
A


ATOM
1621
CG2
VAL
A
276
27.550
24.558
22.766
1.00
19.43
A


ATOM
1622
C
VAL
A
276
26.127
27.075
20.211
1.00
23.89
A


ATOM
1623
O
VAL
A
276
24.910
27.199
20.070
1.00
24.90
A


ATOM
1624
N
ALA
A
277
26.983
28.062
19.965
1.00
24.56
A


ATOM
1625
CA
ALA
A
277
26.533
29.374
19.518
1.00
24.72
A


ATOM
1626
CB
ALA
A
277
27.504
30.444
19.999
1.00
24.36
A


ATOM
1627
C
ALA
A
277
26.378
29.458
18.005
1.00
25.76
A


ATOM
1628
O
ALA
A
277
25.577
30.242
17.502
1.00
26.39
A


ATOM
1629
N
GLY
A
278
27.142
28.651
17.280
1.00
25.13
A


ATOM
1630
CA
GLY
A
278
27.062
28.673
15.834
1.00
25.58
A


ATOM
1631
C
GLY
A
278
28.163
29.524
15.231
1.00
26.50
A


ATOM
1632
O
GLY
A
278
28.374
29.510
14.015
1.00
28.17
A


ATOM
1633
N
LEU
A
279
28.866
30.262
16.086
1.00
24.44
A


ATOM
1634
CA
LEU
A
279
29.962
31.130
15.656
1.00
25.21
A


ATOM
1635
CB
LEU
A
279
29.468
32.575
15.500
1.00
25.78
A


ATOM
1636
CG
LEU
A
279
28.364
32.899
14.490
1.00
28.17
A


ATOM
1637
CD1
LEU
A
279
27.922
34.344
14.684
1.00
26.60
A


ATOM
1638
CD2
LEU
A
279
28.862
32.670
13.071
1.00
26.52
A


ATOM
1639
C
LEU
A
279
31.093
31.116
16.687
1.00
23.47
A


ATOM
1640
O
LEU
A
279
30.848
30.994
17.882
1.00
24.44
A


ATOM
1641
N
PRO
A
280
32.349
31.239
16.236
1.00
23.35
A


ATOM
1642
CD
PRO
A
280
32.831
31.404
14.855
1.00
22.26
A


ATOM
1643
CA
PRO
A
280
33.464
31.239
17.189
1.00
23.81
A


ATOM
1644
CB
PRO
A
280
34.692
31.293
16.282
1.00
23.24
A


ATOM
1645
CG
PRO
A
280
34.189
32.020
15.073
1.00
24.89
A


ATOM
1646
C
PRO
A
280
33.353
32.444
18.137
1.00
22.69
A


ATOM
1647
O
PRO
A
280
32.750
33.457
17.788
1.00
22.11
A


ATOM
1648
N
PRO
A
281
33.939
32.344
19.345
1.00
23.06
A


ATOM
1649
CD
PRO
A
281
34.810
31.223
19.734
1.00
21.37
A


ATOM
1650
CA
PRO
A
281
33.935
33.375
20.395
1.00
23.67
A


ATOM
1651
CB
PRO
A
281
34.781
32.751
21.509
1.00
24.89
A


ATOM
1652
CG
PRO
A
281
34.749
31.287
21.219
1.00
25.24
A


ATOM
1653
C
PRO
A
281
34.481
34.752
20.017
1.00
23.75
A


ATOM
1654
O
PRO
A
281
33.869
35.781
20.317
1.00
21.02
A


ATOM
1655
N
PHE
A
282
35.644
34.763
19.379
1.00
22.17
A


ATOM
1656
CA
PHE
A
282
36.293
36.007
18.998
1.00
23.16
A


ATOM
1657
CB
PHE
A
282
37.765
35.943
19.406
1.00
21.01
A


ATOM
1658
CG
PHE
A
282
37.975
35.482
20.822
1.00
22.66
A


ATOM
1659
CD1
PHE
A
282
37.806
36.361
21.888
1.00
20.06
A


ATOM
1660
CD2
PHE
A
282
38.291
34.151
21.093
1.00
20.72
A


ATOM
1661
CE1
PHE
A
282
37.947
35.921
23.206
1.00
22.66
A


ATOM
1662
CE2
PHE
A
282
38.433
33.702
22.405
1.00
20.97
A


ATOM
1663
CZ
PHE
A
282
38.261
34.590
23.466
1.00
19.58
A


ATOM
1664
C
PHE
A
282
36.169
36.263
17.503
1.00
24.39
A


ATOM
1665
O
PHE
A
282
36.802
35.585
16.694
1.00
25.80
A


ATOM
1666
N
ARG
A
283
35.355
37.248
17.142
1.00
24.99
A


ATOM
1667
CA
ARG
A
283
35.141
37.594
15.741
1.00
26.33
A


ATOM
1668
CB
ARG
A
283
33.721
37.209
15.316
1.00
28.91
A


ATOM
1669
CG
ARG
A
283
33.293
35.808
15.724
1.00
30.27
A


ATOM
1670
CD
ARG
A
283
31.904
35.493
15.188
1.00
33.36
A


ATOM
1671
NE
ARG
A
283
30.890
36.392
15.733
1.00
32.76
A


ATOM
1672
CZ
ARG
A
283
30.372
36.287
16.952
1.00
34.79
A


ATOM
1673
NH1
ARG
A
283
30.767
35.317
17.768
1.00
35.77
A


ATOM
1674
NH2
ARG
A
283
29.458
37.156
17.359
1.00
36.12
A


ATOM
1675
C
ARG
A
283
35.328
39.096
15.544
1.00
26.47
A


ATOM
1676
O
ARG
A
283
35.029
39.888
16.438
1.00
26.28
A


ATOM
1677
N
ALA
A
284
35.818
39.486
14.373
1.00
26.70
A


ATOM
1678
CA
ALA
A
284
36.033
40.899
14.079
1.00
27.84
A


ATOM
1679
CB
ALA
A
284
37.188
41.442
14.914
1.00
26.24
A


ATOM
1680
C
ALA
A
284
36.327
41.077
12.602
1.00
28.35
A


ATOM
1681
O
ALA
A
284
36.560
40.101
11.891
1.00
29.91
A


ATOM
1682
N
GLY
A
285
36.332
42.329
12.153
1.00
29.29
A


ATOM
1683
CA
GLY
A
285
36.577
42.631
10.753
1.00
29.52
A


ATOM
1684
C
GLY
A
285
37.893
42.156
10.168
1.00
30.12
A


ATOM
1685
O
GLY
A
285
37.974
41.862
8.976
1.00
30.60
A


ATOM
1686
N
ASN
A
286
38.939
42.097
10.983
1.00
28.49
A


ATOM
1687
CA
ASN
A
286
40.231
41.644
10.489
1.00
26.71
A


ATOM
1688
CB
ASN
A
286
41.050
42.825
9.945
1.00
26.11
A


ATOM
1689
CG
ASN
A
286
41.310
43.900
10.990
1.00
27.83
A


ATOM
1690
OD1
ASN
A
286
41.877
43.631
12.049
1.00
27.84
A


ATOM
1691
ND2
ASN
A
286
40.908
45.131
10.685
1.00
25.95
A


ATOM
1692
C
ASN
A
286
40.997
40.924
11.584
1.00
26.03
A


ATOM
1693
O
ASN
A
286
40.540
40.851
12.723
1.00
25.66
A


ATOM
1694
N
GLU
A
287
42.162
40.391
11.239
1.00
24.81
A


ATOM
1695
CA
GLU
A
287
42.965
39.662
12.206
1.00
27.59
A


ATOM
1696
CB
GLU
A
287
44.145
38.985
11.510
1.00
30.17
A


ATOM
1697
CG
GLU
A
287
43.776
37.632
10.931
1.00
38.21
A


ATOM
1698
CD
GLU
A
287
44.900
36.998
10.140
1.00
41.86
A


ATOM
1699
OE1
GLU
A
287
46.061
37.036
10.608
1.00
43.08
A


ATOM
1700
OE2
GLU
A
287
44.612
36.449
9.052
1.00
45.22
A


ATOM
1701
C
GLU
A
287
43.459
40.485
13.383
1.00
25.05
A


ATOM
1702
O
GLU
A
287
43.382
40.030
14.521
1.00
26.41
A


ATOM
1703
N
TYR
A
288
43.966
41.685
13.122
1.00
23.04
A


ATOM
1704
CA
TYR
A
288
44.460
42.528
14.205
1.00
22.34
A


ATOM
1705
CB
TYR
A
288
44.867
43.913
13.691
1.00
21.07
A


ATOM
1706
CG
TYR
A
288
45.275
44.858
14.805
1.00
21.07
A


ATOM
1707
CD1
TYR
A
288
46.533
44.762
15.405
1.00
21.23
A


ATOM
1708
CE1
TYR
A
288
46.891
45.588
16.475
1.00
20.43
A


ATOM
1709
CD2
TYR
A
288
44.380
45.809
15.302
1.00
22.32
A


ATOM
1710
CE2
TYR
A
288
44.725
46.637
16.373
1.00
23.28
A


ATOM
1711
CZ
TYR
A
288
45.981
46.518
16.953
1.00
22.96
A


ATOM
1712
OH
TYR
A
288
46.316
47.313
18.024
1.00
23.18
A


ATOM
1713
C
TYR
A
288
43.402
42.698
15.288
1.00
21.38
A


ATOM
1714
O
TYR
A
288
43.710
42.616
16.473
1.00
22.09
A


ATOM
1715
N
LEU
A
289
42.159
42.939
14.874
1.00
21.88
A


ATOM
1716
CA
LEU
A
289
41.055
43.130
15.811
1.00
21.98
A


ATOM
1717
CB
LEU
A
289
39.821
43.673
15.078
1.00
22.90
A


ATOM
1718
CG
LEU
A
289
39.896
45.130
14.601
1.00
26.52
A


ATOM
1719
CD1
LEU
A
289
38.706
45.436
13.696
1.00
26.55
A


ATOM
1720
CD2
LEU
A
289
39.914
46.071
15.807
1.00
23.13
A


ATOM
1721
C
LEU
A
289
40.686
41.849
16.560
1.00
21.24
A


ATOM
1722
O
LEU
A
289
40.256
41.897
17.715
1.00
20.72
A


ATOM
1723
N
ILE
A
290
40.843
40.708
15.900
1.00
19.62
A


ATOM
1724
CA
ILE
A
290
40.538
39.433
16.533
1.00
18.54
A


ATOM
1725
CB
ILE
A
290
40.560
38.281
15.509
1.00
18.52
A


ATOM
1726
CG2
ILE
A
290
40.503
36.934
16.234
1.00
17.63
A


ATOM
1727
CG1
ILE
A
290
39.378
38.429
14.545
1.00
18.88
A


ATOM
1728
CD1
ILE
A
290
39.421
37.483
13.357
1.00
19.81
A


ATOM
1729
C
ILE
A
290
41.578
39.167
17.618
1.00
19.09
A


ATOM
1730
O
ILE
A
290
41.236
38.788
18.737
1.00
18.20
A


ATOM
1731
N
PHE
A
291
42.849
39.376
17.286
1.00
18.76
A


ATOM
1732
CA
PHE
A
291
43.925
39.156
18.247
1.00
20.75
A


ATOM
1733
CB
PHE
A
291
45.286
39.434
17.606
1.00
20.71
A


ATOM
1734
CG
PHE
A
291
45.644
38.480
16.503
1.00
22.92
A


ATOM
1735
CD1
PHE
A
291
45.065
37.214
16.443
1.00
22.98
A


ATOM
1736
CD2
PHE
A
291
46.588
38.830
15.543
1.00
22.91
A


ATOM
1737
CE1
PHE
A
291
45.423
36.310
15.440
1.00
24.51
A


ATOM
1738
CE2
PHE
A
291
46.954
37.931
14.535
1.00
25.54
A


ATOM
1739
CZ
PHE
A
291
46.370
36.670
14.485
1.00
23.29
A


ATOM
1740
C
PHE
A
291
43.739
40.061
19.451
1.00
21.72
A


ATOM
1741
O
PHE
A
291
43.992
39.671
20.593
1.00
22.32
A


ATOM
1742
N
GLN
A
292
43.284
41.275
19.178
1.00
23.27
A


ATOM
1743
CA
GLN
A
292
43.055
42.264
20.216
1.00
24.01
A


ATOM
1744
CB
GLN
A
292
42.574
43.559
19.562
1.00
25.77
A


ATOM
1745
CG
GLN
A
292
42.577
44.773
20.447
1.00
28.45
A


ATOM
1746
CD
GLN
A
292
42.469
46.057
19.638
1.00
29.83
A


ATOM
1747
OE1
GLN
A
292
41.520
46.244
18.872
1.00
27.16
A


ATOM
1748
NE2
GLN
A
292
43.449
46.944
19.799
1.00
27.61
A


ATOM
1749
C
GLN
A
292
42.018
41.733
21.204
1.00
22.97
A


ATOM
1750
O
GLN
A
292
42.200
41.832
22.415
1.00
21.64
A


ATOM
1751
N
LYS
A
293
40.937
41.154
20.687
1.00
21.82
A


ATOM
1752
CA
LYS
A
293
39.895
40.612
21.558
1.00
22.18
A


ATOM
1753
CB
LYS
A
293
38.664
40.223
20.740
1.00
22.69
A


ATOM
1754
CG
LYS
A
293
37.919
41.407
20.153
1.00
25.78
A


ATOM
1755
CD
LYS
A
293
36.651
40.961
19.429
1.00
27.88
A


ATOM
1756
CE
LYS
A
293
35.857
42.161
18.926
1.00
30.85
A


ATOM
1757
NZ
LYS
A
293
34.612
41.750
18.214
1.00
32.98
A


ATOM
1758
C
LYS
A
293
40.398
39.398
22.343
1.00
21.20
A


ATOM
1759
O
LYS
A
293
40.041
39.204
23.509
1.00
22.01
A


ATOM
1760
N
ILE
A
294
41.226
38.583
21.702
1.00
19.91
A


ATOM
1761
CA
ILE
A
294
41.774
37.394
22.347
1.00
20.28
A


ATOM
1762
CB
ILE
A
294
42.631
36.575
21.349
1.00
18.98
A


ATOM
1763
CG2
ILE
A
294
43.481
35.550
22.098
1.00
17.70
A


ATOM
1764
CG1
ILE
A
294
41.716
35.897
20.318
1.00
17.93
A


ATOM
1765
CD1
ILE
A
294
42.467
35.237
19.178
1.00
16.21
A


ATOM
1766
C
ILE
A
294
42.618
37.727
23.587
1.00
21.94
A


ATOM
1767
O
ILE
A
294
42.366
37.199
24.673
1.00
20.86
A


ATOM
1768
N
ILE
A
295
43.610
38.600
23.439
1.00
21.88
A


ATOM
1769
CA
ILE
A
295
44.461
38.934
24.582
1.00
24.25
A


ATOM
1770
CB
ILE
A
295
45.668
39.805
24.175
1.00
23.93
A


ATOM
1771
CG2
ILE
A
295
46.514
39.066
23.140
1.00
24.61
A


ATOM
1772
CG1
ILE
A
295
45.189
41.151
23.637
1.00
24.58
A


ATOM
1773
CD1
ILE
A
295
46.317
42.149
23.433
1.00
26.69
A


ATOM
1774
C
ILE
A
295
43.720
39.636
25.717
1.00
24.80
A


ATOM
1775
O
ILE
A
295
44.214
39.687
26.842
1.00
24.76
A


ATOM
1776
N
LYS
A
296
42.539
40.173
25.425
1.00
25.33
A


ATOM
1777
CA
LYS
A
296
41.743
40.853
26.444
1.00
26.80
A


ATOM
1778
CB
LYS
A
296
41.178
42.170
25.894
1.00
27.39
A


ATOM
1779
CG
LYS
A
296
42.240
43.141
25.413
1.00
31.79
A


ATOM
1780
CD
LYS
A
296
41.634
44.410
24.826
1.00
35.56
A


ATOM
1781
CE
LYS
A
296
41.009
45.283
25.900
1.00
39.29
A


ATOM
1782
NZ
LYS
A
296
40.564
46.603
25.357
1.00
41.72
A


ATOM
1783
C
LYS
A
296
40.593
39.958
26.893
1.00
25.50
A


ATOM
1784
O
LYS
A
296
39.770
40.361
27.713
1.00
24.02
A


ATOM
1785
N
LEU
A
297
40.550
38.742
26.349
1.00
25.67
A


ATOM
1786
CA
LEU
A
297
39.500
37.777
26.666
1.00
25.16
A


ATOM
1787
CB
LEU
A
297
39.632
37.285
28.111
1.00
24.80
A


ATOM
1788
CG
LEU
A
297
38.766
36.068
28.460
1.00
26.43
A


ATOM
1789
CD1
LEU
A
297
39.238
34.852
27.646
1.00
26.70
A


ATOM
1790
CD2
LEU
A
297
38.856
35.777
29.951
1.00
24.84
A


ATOM
1791
C
LEU
A
297
38.151
38.459
26.467
1.00
25.11
A


ATOM
1792
O
LEU
A
297
37.261
38.378
27.309
1.00
25.28
A


ATOM
1793
N
GLU
A
298
38.007
39.127
25.331
1.00
24.98
A


ATOM
1794
CA
GLU
A
298
36.786
39.847
25.023
1.00
25.31
A


ATOM
1795
CB
GLU
A
298
37.143
41.139
24.291
1.00
27.13
A


ATOM
1796
CG
GLU
A
298
35.991
42.092
24.108
1.00
31.28
A


ATOM
1797
CD
GLU
A
298
36.419
43.362
23.410
1.00
34.40
A


ATOM
1798
OE1
GLU
A
298
37.348
44.027
23.918
1.00
35.90
A


ATOM
1799
OE2
GLU
A
298
35.832
43.693
22.359
1.00
36.16
A


ATOM
1800
C
GLU
A
298
35.766
39.057
24.207
1.00
23.79
A


ATOM
1801
O
GLU
A
298
35.832
39.017
22.979
1.00
24.35
A


ATOM
1802
N
TYR
A
299
34.825
38.427
24.902
1.00
23.45
A


ATOM
1803
CA
TYR
A
299
33.760
37.663
24.265
1.00
23.98
A


ATOM
1804
CB
TYR
A
299
34.264
36.304
23.755
1.00
20.13
A


ATOM
1805
CG
TYR
A
299
34.348
35.233
24.828
1.00
21.17
A


ATOM
1806
CD1
TYR
A
299
35.336
35.279
25.810
1.00
19.32
A


ATOM
1807
CE1
TYR
A
299
35.389
34.332
26.826
1.00
19.30
A


ATOM
1808
CD2
TYR
A
299
33.410
34.201
24.888
1.00
18.96
A


ATOM
1809
CE2
TYR
A
299
33.456
33.243
25.907
1.00
19.41
A


ATOM
1810
CZ
TYR
A
299
34.449
33.321
26.870
1.00
18.79
A


ATOM
1811
OH
TYR
A
299
34.511
32.401
27.881
1.00
18.77
A


ATOM
1812
C
TYR
A
299
32.699
37.437
25.331
1.00
25.20
A


ATOM
1813
O
TYR
A
299
32.942
37.681
26.506
1.00
26.46
A


ATOM
1814
N
ASP
A
300
31.522
36.981
24.927
1.00
26.94
A


ATOM
1815
CA
ASP
A
300
30.467
36.710
25.891
1.00
30.60
A


ATOM
1816
CB
ASP
A
300
29.665
37.981
26.179
1.00
35.86
A


ATOM
1817
CG
ASP
A
300
29.228
38.687
24.923
1.00
42.04
A


ATOM
1818
OD1
ASP
A
300
28.450
38.088
24.149
1.00
45.98
A


ATOM
1819
OD2
ASP
A
300
29.666
39.840
24.707
1.00
45.69
A


ATOM
1820
C
ASP
A
300
29.564
35.608
25.363
1.00
29.26
A


ATOM
1821
O
ASP
A
300
29.590
35.299
24.172
1.00
28.64
A


ATOM
1822
N
PHE
A
301
28.778
35.011
26.253
1.00
28.96
A


ATOM
1823
CA
PHE
A
301
27.884
33.924
25.871
1.00
30.48
A


ATOM
1824
CB
PHE
A
301
27.818
32.854
26.968
1.00
29.17
A


ATOM
1825
CG
PHE
A
301
29.147
32.279
27.356
1.00
29.29
A


ATOM
1826
CD1
PHE
A
301
29.978
32.949
28.245
1.00
27.31
A


ATOM
1827
CD2
PHE
A
301
29.560
31.050
26.845
1.00
27.89
A


ATOM
1828
CE1
PHE
A
301
31.205
32.403
28.625
1.00
28.83
A


ATOM
1829
CE2
PHE
A
301
30.781
30.498
27.217
1.00
28.05
A


ATOM
1830
CZ
PHE
A
301
31.605
31.175
28.110
1.00
28.27
A


ATOM
1831
C
PHE
A
301
26.459
34.384
25.619
1.00
32.20
A


ATOM
1832
O
PHE
A
301
25.946
35.261
26.317
1.00
32.36
A


ATOM
1833
N
PRO
A
302
25.798
33.804
24.607
1.00
33.29
A


ATOM
1834
CD
PRO
A
302
26.313
32.943
23.529
1.00
34.04
A


ATOM
1835
CA
PRO
A
302
24.415
34.199
24.341
1.00
35.24
A


ATOM
1836
CB
PRO
A
302
24.144
33.608
22.959
1.00
34.01
A


ATOM
1837
CG
PRO
A
302
25.041
32.413
22.921
1.00
35.48
A


ATOM
1838
C
PRO
A
302
23.567
33.561
25.444
1.00
37.39
A


ATOM
1839
O
PRO
A
302
23.935
32.518
25.986
1.00
38.49
A


ATOM
1840
N
ALA
A
303
22.447
34.188
25.783
1.00
39.36
A


ATOM
1841
CA
ALA
A
303
21.572
33.692
26.843
1.00
40.65
A


ATOM
1842
CB
ALA
A
303
20.280
34.506
26.862
1.00
41.66
A


ATOM
1843
C
ALA
A
303
21.238
32.197
26.814
1.00
41.25
A


ATOM
1844
O
ALA
A
303
21.253
31.537
27.854
1.00
43.16
A


ATOM
1845
N
ALA
A
304
20.945
31.665
25.631
1.00
41.04
A


ATOM
1846
CA
ALA
A
304
20.569
30.258
25.480
1.00
40.66
A


ATOM
1847
CB
ALA
A
304
20.121
30.004
24.040
1.00
41.36
A


ATOM
1848
C
ALA
A
304
21.628
29.223
25.876
1.00
39.61
A


ATOM
1849
O
ALA
A
304
21.298
28.156
26.395
1.00
40.61
A


ATOM
1850
N
PHE
A
305
22.891
29.543
25.617
1.00
36.21
A


ATOM
1851
CA
PHE
A
305
24.022
28.662
25.909
1.00
32.08
A


ATOM
1852
CB
PHE
A
305
25.259
29.519
26.187
1.00
29.46
A


ATOM
1853
CG
PHE
A
305
26.536
28.917
25.690
1.00
28.15
A


ATOM
1854
CD1
PHE
A
305
27.146
27.875
26.377
1.00
26.20
A


ATOM
1855
CD2
PHE
A
305
27.127
29.386
24.521
1.00
27.05
A


ATOM
1856
CE1
PHE
A
305
28.330
27.308
25.908
1.00
26.92
A


ATOM
1857
CE2
PHE
A
305
28.312
28.826
24.042
1.00
26.62
A


ATOM
1858
CZ
PHE
A
305
28.914
27.786
24.737
1.00
26.61
A


ATOM
1859
C
PHE
A
305
23.811
27.664
27.057
1.00
30.09
A


ATOM
1860
O
PHE
A
305
23.518
28.051
28.187
1.00
31.51
A


ATOM
1861
N
PHE
A
306
23.964
26.378
26.758
1.00
27.01
A


ATOM
1862
CA
PHE
A
306
23.801
25.334
27.769
1.00
26.30
A


ATOM
1863
CB
PHE
A
306
24.157
23.970
27.170
1.00
25.03
A


ATOM
1864
CG
PHE
A
306
23.548
23.725
25.815
1.00
27.24
A


ATOM
1865
CD1
PHE
A
306
22.170
23.831
25.622
1.00
28.40
A


ATOM
1866
CD2
PHE
A
306
24.350
23.386
24.728
1.00
27.84
A


ATOM
1867
CE1
PHE
A
306
21.601
23.603
24.365
1.00
28.05
A


ATOM
1868
CE2
PHE
A
306
23.792
23.155
23.465
1.00
28.31
A


ATOM
1869
CZ
PHE
A
306
22.415
23.263
23.283
1.00
28.00
A


ATOM
1870
C
PHE
A
306
24.711
25.652
28.961
1.00
26.23
A


ATOM
1871
O
PHE
A
306
25.927
25.775
28.811
1.00
25.59
A


ATOM
1872
N
PRO
A
307
24.125
25.796
30.163
1.00
26.67
A


ATOM
1873
CD
PRO
A
307
22.685
25.625
30.430
1.00
27.95
A


ATOM
1874
CA
PRO
A
307
24.842
26.110
31.405
1.00
26.59
A


ATOM
1875
CB
PRO
A
307
23.795
25.832
32.481
1.00
26.14
A


ATOM
1876
CG
PRO
A
307
22.531
26.250
31.803
1.00
27.86
A


ATOM
1877
C
PRO
A
307
26.145
25.355
31.659
1.00
25.58
A


ATOM
1878
O
PRO
A
307
27.189
25.964
31.900
1.00
22.65
A


ATOM
1879
N
LYS
A
308
26.085
24.031
31.620
1.00
24.46
A


ATOM
1880
CA
LYS
A
308
27.274
23.232
31.867
1.00
23.91
A


ATOM
1881
CB
LYS
A
308
26.887
21.760
32.024
1.00
23.25
A


ATOM
1882
CG
LYS
A
308
26.062
21.532
33.285
1.00
28.49
A


ATOM
1883
CD
LYS
A
308
25.618
20.093
33.466
1.00
30.17
A


ATOM
1884
CE
LYS
A
308
24.760
19.973
34.722
1.00
33.12
A


ATOM
1885
NZ
LYS
A
308
24.122
18.636
34.860
1.00
34.13
A


ATOM
1886
C
LYS
A
308
28.314
23.426
30.769
1.00
22.84
A


ATOM
1887
O
LYS
A
308
29.514
23.411
31.042
1.00
22.46
A


ATOM
1888
N
ALA
A
309
27.861
23.621
29.534
1.00
21.59
A


ATOM
1889
CA
ALA
A
309
28.792
23.848
28.432
1.00
20.02
A


ATOM
1890
CB
ALA
A
309
28.056
23.856
27.106
1.00
18.80
A


ATOM
1891
C
ALA
A
309
29.481
25.191
28.662
1.00
21.41
A


ATOM
1892
O
ALA
A
309
30.680
25.335
28.427
1.00
21.39
A


ATOM
1893
N
ARG
A
310
28.717
26.179
29.121
1.00
21.39
A


ATOM
1894
CA
ARG
A
310
29.290
27.494
29.388
1.00
22.02
A


ATOM
1895
CB
ARG
A
310
28.213
28.479
29.854
1.00
22.39
A


ATOM
1896
CG
ARG
A
310
28.806
29.756
30.436
1.00
25.30
A


ATOM
1897
CD
ARG
A
310
27.780
30.852
30.664
1.00
28.33
A


ATOM
1898
NE
ARG
A
310
28.420
32.039
31.230
1.00
30.18
A


ATOM
1899
CZ
ARG
A
310
27.901
33.263
31.203
1.00
32.07
A


ATOM
1900
NH1
ARG
A
310
26.719
33.477
30.634
1.00
31.19
A


ATOM
1901
NH2
ARG
A
310
28.567
34.277
31.742
1.00
30.49
A


ATOM
1902
C
ARG
A
310
30.376
27.388
30.458
1.00
21.65
A


ATOM
1903
O
ARG
A
310
31.464
27.949
30.311
1.00
20.36
A


ATOM
1904
N
ASP
A
311
30.074
26.677
31.541
1.00
19.57
A


ATOM
1905
CA
ASP
A
311
31.043
26.512
32.615
1.00
20.18
A


ATOM
1906
CB
ASP
A
311
30.460
25.649
33.739
1.00
20.39
A


ATOM
1907
CG
ASP
A
311
31.439
25.446
34.881
1.00
23.35
A


ATOM
1908
OD1
ASP
A
311
32.158
24.428
34.885
1.00
24.91
A


ATOM
1909
OD2
ASP
A
311
31.500
26.312
35.776
1.00
26.96
A


ATOM
1910
C
ASP
A
311
32.322
25.877
32.073
1.00
19.73
A


ATOM
1911
O
ASP
A
311
33.422
26.289
32.439
1.00
19.30
A


ATOM
1912
N
LEU
A
312
32.179
24.891
31.188
1.00
16.32
A


ATOM
1913
CA
LEU
A
312
33.349
24.226
30.611
1.00
16.66
A


ATOM
1914
CB
LEU
A
312
32.927
23.035
29.744
1.00
16.12
A


ATOM
1915
CG
LEU
A
312
34.050
22.320
28.974
1.00
14.73
A


ATOM
1916
CD1
LEU
A
312
35.192
21.935
29.912
1.00
14.56
A


ATOM
1917
CD2
LEU
A
312
33.477
21.084
28.289
1.00
14.22
A


ATOM
1918
C
LEU
A
312
34.181
25.189
29.774
1.00
16.61
A


ATOM
1919
O
LEU
A
312
35.402
25.241
29.910
1.00
16.20
A


ATOM
1920
N
VAL
A
313
33.515
25.949
28.908
1.00
16.20
A


ATOM
1921
CA
VAL
A
313
34.207
26.907
28.058
1.00
15.37
A


ATOM
1922
CB
VAL
A
313
33.216
27.648
27.130
1.00
16.42
A


ATOM
1923
CG1
VAL
A
313
33.915
28.796
26.426
1.00
16.93
A


ATOM
1924
CG2
VAL
A
313
32.644
26.672
26.103
1.00
17.88
A


ATOM
1925
C
VAL
A
313
34.960
27.923
28.911
1.00
17.39
A


ATOM
1926
O
VAL
A
313
36.093
28.294
28.591
1.00
18.00
A


ATOM
1927
N
GLU
A
314
34.342
28.364
30.004
1.00
17.61
A


ATOM
1928
CA
GLU
A
314
34.986
29.331
30.885
1.00
20.43
A


ATOM
1929
CB
GLU
A
314
34.009
29.816
31.959
1.00
22.14
A


ATOM
1930
CG
GLU
A
314
32.800
30.550
31.396
1.00
26.52
A


ATOM
1931
CD
GLU
A
314
31.852
31.025
32.478
1.00
31.26
A


ATOM
1932
OE1
GLU
A
314
31.580
30.246
33.417
1.00
33.48
A


ATOM
1933
OE2
GLU
A
314
31.370
32.173
32.387
1.00
34.81
A


ATOM
1934
C
GLU
A
314
36.217
28.721
31.539
1.00
19.15
A


ATOM
1935
O
GLU
A
314
37.134
29.433
31.934
1.00
21.47
A


ATOM
1936
N
LYS
A
315
36.245
27.400
31.651
1.00
19.51
A


ATOM
1937
CA
LYS
A
315
37.394
26.749
32.258
1.00
19.17
A


ATOM
1938
CB
LYS
A
315
36.946
25.514
33.043
1.00
18.84
A


ATOM
1939
CG
LYS
A
315
36.280
25.885
34.368
1.00
19.62
A


ATOM
1940
CD
LYS
A
315
35.653
24.696
35.073
1.00
19.22
A


ATOM
1941
CE
LYS
A
315
35.070
25.095
36.427
1.00
21.00
A


ATOM
1942
NZ
LYS
A
315
36.119
25.552
37.381
1.00
19.53
A


ATOM
1943
C
LYS
A
315
38.452
26.393
31.218
1.00
18.96
A


ATOM
1944
O
LYS
A
315
39.511
25.873
31.561
1.00
19.85
A


ATOM
1945
N
LEU
A
316
38.164
26.691
29.950
1.00
17.08
A


ATOM
1946
CA
LEU
A
316
39.102
26.429
28.854
1.00
16.41
A


ATOM
1947
CB
LEU
A
316
38.414
25.636
27.738
1.00
13.81
A


ATOM
1948
CG
LEU
A
316
38.028
24.201
28.115
1.00
14.39
A


ATOM
1949
CD1
LEU
A
316
37.139
23.597
27.031
1.00
12.38
A


ATOM
1950
CD2
LEU
A
316
39.302
23.373
28.309
1.00
12.77
A


ATOM
1951
C
LEU
A
316
39.652
27.743
28.290
1.00
17.12
A


ATOM
1952
O
LEU
A
316
40.851
27.860
28.023
1.00
16.53
A


ATOM
1953
N
LEU
A
317
38.780
28.729
28.105
1.00
16.27
A


ATOM
1954
CA
LEU
A
317
39.228
30.022
27.596
1.00
17.52
A


ATOM
1955
CB
LEU
A
317
38.083
30.752
26.887
1.00
16.37
A


ATOM
1956
CG
LEU
A
317
37.448
29.973
25.727
1.00
18.81
A


ATOM
1957
CD1
LEU
A
317
36.415
30.851
25.018
1.00
16.47
A


ATOM
1958
CD2
LEU
A
317
38.528
29.526
24.741
1.00
17.87
A


ATOM
1959
C
LEU
A
317
39.745
30.841
28.774
1.00
18.27
A


ATOM
1960
O
LEU
A
317
39.078
31.753
29.273
1.00
18.58
A


ATOM
1961
N
VAL
A
318
40.937
30.475
29.229
1.00
18.02
A


ATOM
1962
CA
VAL
A
318
41.593
31.141
30.342
1.00
18.85
A


ATOM
1963
CB
VAL
A
318
41.846
30.153
31.500
1.00
19.91
A


ATOM
1964
CG1
VAL
A
318
42.590
30.848
32.634
1.00
20.01
A


ATOM
1965
CG2
VAL
A
318
40.520
29.584
31.990
1.00
19.44
A


ATOM
1966
C
VAL
A
318
42.923
31.657
29.811
1.00
19.67
A


ATOM
1967
O
VAL
A
318
43.690
30.902
29.208
1.00
18.26
A


ATOM
1968
N
LEU
A
319
43.197
32.939
30.028
1.00
20.07
A


ATOM
1969
CA
LEU
A
319
44.436
33.533
29.538
1.00
20.98
A


ATOM
1970
CB
LEU
A
319
44.521
35.002
29.968
1.00
21.64
A


ATOM
1971
CG
LEU
A
319
43.418
35.908
29.408
1.00
24.38
A


ATOM
1972
CD1
LEU
A
319
43.606
37.332
29.935
1.00
23.28
A


ATOM
1973
CD2
LEU
A
319
43.453
35.887
27.875
1.00
24.33
A


ATOM
1974
C
LEU
A
319
45.680
32.774
29.994
1.00
20.38
A


ATOM
1975
O
LEU
A
319
46.568
32.496
29.192
1.00
21.34
A


ATOM
1976
N
ASP
A
320
45.742
32.440
31.280
1.00
20.22
A


ATOM
1977
CA
ASP
A
320
46.879
31.707
31.833
1.00
20.90
A


ATOM
1978
CB
ASP
A
320
46.842
31.760
33.365
1.00
20.76
A


ATOM
1979
CG
ASP
A
320
48.049
31.102
34.004
1.00
21.51
A


ATOM
1980
OD1
ASP
A
320
48.669
30.226
33.367
1.00
23.46
A


ATOM
1981
OD2
ASP
A
320
48.371
31.450
35.159
1.00
23.89
A


ATOM
1982
C
ASP
A
320
46.814
30.247
31.367
1.00
20.06
A


ATOM
1983
O
ASP
A
320
45.988
29.476
31.840
1.00
20.54
A


ATOM
1984
N
ALA
A
321
47.700
29.876
30.451
1.00
20.68
A


ATOM
1985
CA
ALA
A
321
47.733
28.522
29.903
1.00
22.04
A


ATOM
1986
CB
ALA
A
321
48.860
28.411
28.881
1.00
20.75
A


ATOM
1987
C
ALA
A
321
47.858
27.400
30.940
1.00
21.62
A


ATOM
1988
O
ALA
A
321
47.482
26.259
30.665
1.00
21.99
A


ATOM
1989
N
THR
A
322
48.372
27.715
32.127
1.00
20.89
A


ATOM
1990
CA
THR
A
322
48.531
26.698
33.167
1.00
20.82
A


ATOM
1991
CB
THR
A
322
49.670
27.051
34.146
1.00
19.47
A


ATOM
1992
OG1
THR
A
322
49.341
28.253
34.848
1.00
20.19
A


ATOM
1993
CG2
THR
A
322
50.981
27.249
33.394
1.00
21.59
A


ATOM
1994
C
THR
A
322
47.264
26.498
33.983
1.00
19.55
A


ATOM
1995
O
THR
A
322
47.235
25.673
34.894
1.00
21.13
A


ATOM
1996
N
LYS
A
323
46.216
27.248
33.661
1.00
19.33
A


ATOM
1997
CA
LYS
A
323
44.962
27.122
34.392
1.00
21.20
A


ATOM
1998
CB
LYS
A
323
44.580
28.460
35.030
1.00
23.75
A


ATOM
1999
CG
LYS
A
323
45.562
28.933
36.084
1.00
28.45
A


ATOM
2000
CD
LYS
A
323
45.055
30.177
36.799
1.00
33.76
A


ATOM
2001
CE
LYS
A
323
46.087
30.678
37.802
1.00
36.15
A


ATOM
2002
NZ
LYS
A
323
46.532
29.569
38.693
1.00
37.34
A


ATOM
2003
C
LYS
A
323
43.806
26.614
33.539
1.00
20.68
A


ATOM
2004
O
LYS
A
323
42.649
26.757
33.915
1.00
20.42
A


ATOM
2005
N
ARG
A
324
44.114
26.019
32.392
1.00
19.97
A


ATOM
2006
CA
ARG
A
324
43.060
25.494
31.531
1.00
17.98
A


ATOM
2007
CB
ARG
A
324
43.461
25.609
30.061
1.00
15.95
A


ATOM
2008
CG
ARG
A
324
43.534
27.050
29.603
1.00
17.34
A


ATOM
2009
CD
ARG
A
324
43.996
27.194
28.172
1.00
19.80
A


ATOM
2010
NE
ARG
A
324
44.438
28.565
27.944
1.00
16.93
A


ATOM
2011
CZ
ARG
A
324
45.410
28.908
27.108
1.00
19.88
A


ATOM
2012
NH1
ARG
A
324
46.045
27.978
26.398
1.00
14.58
A


ATOM
2013
NH2
ARG
A
324
45.774
30.181
27.015
1.00
16.51
A


ATOM
2014
C
ARG
A
324
42.762
24.046
31.883
1.00
18.32
A


ATOM
2015
O
ARG
A
324
43.673
23.222
32.006
1.00
18.20
A


ATOM
2016
N
LEU
A
325
41.479
23.748
32.055
1.00
18.32
A


ATOM
2017
CA
LEU
A
325
41.050
22.403
32.395
1.00
17.79
A


ATOM
2018
CB
LEU
A
325
39.523
22.335
32.425
1.00
17.03
A


ATOM
2019
CG
LEU
A
325
38.896
21.125
33.116
1.00
15.91
A


ATOM
2020
CD1
LEU
A
325
39.392
21.048
34.557
1.00
15.93
A


ATOM
2021
CD2
LEU
A
325
37.375
21.255
33.084
1.00
16.56
A


ATOM
2022
C
LEU
A
325
41.599
21.433
31.356
1.00
18.68
A


ATOM
2023
O
LEU
A
325
41.347
21.586
30.157
1.00
18.28
A


ATOM
2024
N
GLY
A
326
42.354
20.439
31.821
1.00
18.18
A


ATOM
2025
CA
GLY
A
326
42.931
19.462
30.915
1.00
16.36
A


ATOM
2026
C
GLY
A
326
44.443
19.558
30.807
1.00
19.15
A


ATOM
2027
O
GLY
A
326
45.093
18.592
30.404
1.00
19.52
A


ATOM
2028
N
CYS
A
327
45.016
20.708
31.161
1.00
18.16
A


ATOM
2029
CA
CYS
A
327
46.463
20.867
31.075
1.00
19.30
A


ATOM
2030
CB
CYS
A
327
46.856
22.350
31.058
1.00
20.22
A


ATOM
2031
SG
CYS
A
327
46.782
23.200
32.649
1.00
21.97
A


ATOM
2032
C
CYS
A
327
47.169
20.157
32.228
1.00
20.22
A


ATOM
2033
O
CYS
A
327
46.561
19.828
33.246
1.00
17.92
A


ATOM
2034
N
GLU
A
328
48.463
19.933
32.053
1.00
20.51
A


ATOM
2035
CA
GLU
A
328
49.274
19.244
33.042
1.00
23.34
A


ATOM
2036
CB
GLU
A
328
50.710
19.139
32.507
1.00
28.68
A


ATOM
2037
CG
GLU
A
328
50.754
18.367
31.175
1.00
38.24
A


ATOM
2038
CD
GLU
A
328
52.067
18.500
30.414
1.00
43.23
A


ATOM
2039
OE1
GLU
A
328
52.535
19.643
30.218
1.00
46.22
A


ATOM
2040
OE2
GLU
A
328
52.618
17.459
29.991
1.00
44.90
A


ATOM
2041
C
GLU
A
328
49.234
19.876
34.435
1.00
22.11
A


ATOM
2042
O
GLU
A
328
49.147
19.161
35.437
1.00
20.27
A


ATOM
2043
N
GLU
A
329
49.276
21.204
34.506
1.00
18.40
A


ATOM
2044
CA
GLU
A
329
49.248
21.875
35.801
1.00
20.13
A


ATOM
2045
CB
GLU
A
329
49.587
23.363
35.657
1.00
20.36
A


ATOM
2046
CG
GLU
A
329
51.014
23.651
35.190
1.00
24.05
A


ATOM
2047
CD
GLU
A
329
51.191
23.518
33.688
1.00
25.93
A


ATOM
2048
OE1
GLU
A
329
50.213
23.154
32.995
1.00
26.61
A


ATOM
2049
OE2
GLU
A
329
52.311
23.781
33.198
1.00
27.19
A


ATOM
2050
C
GLU
A
329
47.890
21.718
36.480
1.00
19.36
A


ATOM
2051
O
GLU
A
329
47.775
21.879
37.694
1.00
18.74
A


ATOM
2052
N
MET
A
330
46.863
21.415
35.691
1.00
17.28
A


ATOM
2053
CA
MET
A
330
45.520
21.220
36.229
1.00
16.38
A


ATOM
2054
CB
MET
A
330
44.474
21.833
35.294
1.00
17.65
A


ATOM
2055
CG
MET
A
330
44.460
23.365
35.311
1.00
22.95
A


ATOM
2056
SD
MET
A
330
44.186
24.026
36.979
1.00
26.78
A


ATOM
2057
CE
MET
A
330
42.435
23.712
37.186
1.00
24.69
A


ATOM
2058
C
MET
A
330
45.257
19.730
36.422
1.00
14.30
A


ATOM
2059
O
MET
A
330
44.127
19.304
36.629
1.00
15.39
A


ATOM
2060
N
GLU
A
331
46.327
18.949
36.346
1.00
15.60
A


ATOM
2061
CA
GLU
A
331
46.289
17.501
36.531
1.00
17.08
A


ATOM
2062
CB
GLU
A
331
45.607
17.155
37.862
1.00
17.00
A


ATOM
2063
CG
GLU
A
331
46.070
18.027
39.038
1.00
17.46
A


ATOM
2064
CD
GLU
A
331
47.591
18.179
39.145
1.00
20.16
A


ATOM
2065
OE1
GLU
A
331
48.034
19.073
39.896
1.00
21.39
A


ATOM
2066
OE2
GLU
A
331
48.345
17.420
38.500
1.00
18.87
A


ATOM
2067
C
GLU
A
331
45.697
16.658
35.398
1.00
17.80
A


ATOM
2068
O
GLU
A
331
45.107
15.602
35.636
1.00
20.40
A


ATOM
2069
N
GLY
A
332
45.844
17.133
34.167
1.00
16.23
A


ATOM
2070
CA
GLY
A
332
45.420
16.353
33.015
1.00
14.10
A


ATOM
2071
C
GLY
A
332
43.982
16.154
32.596
1.00
13.54
A


ATOM
2072
O
GLY
A
332
43.063
16.864
33.017
1.00
11.96
A


ATOM
2073
N
TYR
A
333
43.804
15.141
31.750
1.00
14.37
A


ATOM
2074
CA
TYR
A
333
42.510
14.806
31.182
1.00
13.56
A


ATOM
2075
CB
TYR
A
333
42.722
13.892
29.968
1.00
15.00
A


ATOM
2076
CG
TYR
A
333
43.153
14.683
28.752
1.00
16.46
A


ATOM
2077
CD1
TYR
A
333
42.206
15.172
27.849
1.00
15.29
A


ATOM
2078
CE1
TYR
A
333
42.573
16.002
26.794
1.00
13.42
A


ATOM
2079
CD2
TYR
A
333
44.490
15.039
28.561
1.00
14.91
A


ATOM
2080
CE2
TYR
A
333
44.872
15.877
27.499
1.00
14.87
A


ATOM
2081
CZ
TYR
A
333
43.902
16.353
26.626
1.00
15.61
A


ATOM
2082
OH
TYR
A
333
44.244
17.197
25.599
1.00
17.29
A


ATOM
2083
C
TYR
A
333
41.470
14.230
32.127
1.00
15.23
A


ATOM
2084
O
TYR
A
333
40.278
14.323
31.846
1.00
16.63
A


ATOM
2085
N
GLY
A
334
41.907
13.650
33.244
1.00
15.50
A


ATOM
2086
CA
GLY
A
334
40.957
13.100
34.202
1.00
15.07
A


ATOM
2087
C
GLY
A
334
39.925
14.146
34.616
1.00
16.40
A


ATOM
2088
O
GLY
A
334
38.724
13.946
34.433
1.00
15.05
A


ATOM
2089
N
PRO
A
335
40.366
15.278
35.184
1.00
14.96
A


ATOM
2090
CD
PRO
A
335
41.727
15.531
35.689
1.00
15.88
A


ATOM
2091
CA
PRO
A
335
39.444
16.339
35.606
1.00
15.29
A


ATOM
2092
CB
PRO
A
335
40.383
17.397
36.178
1.00
13.19
A


ATOM
2093
CG
PRO
A
335
41.485
16.569
36.758
1.00
13.81
A


ATOM
2094
C
PRO
A
335
38.594
16.877
34.448
1.00
15.84
A


ATOM
2095
O
PRO
A
335
37.423
17.204
34.631
1.00
14.84
A


ATOM
2096
N
LEU
A
336
39.184
16.971
33.257
1.00
16.12
A


ATOM
2097
CA
LEU
A
336
38.450
17.465
32.094
1.00
15.52
A


ATOM
2098
CB
LEU
A
336
39.396
17.653
30.898
1.00
14.39
A


ATOM
2099
CG
LEU
A
336
38.770
17.991
29.538
1.00
15.46
A


ATOM
2100
CD1
LEU
A
336
37.836
19.182
29.662
1.00
11.25
A


ATOM
2101
CD2
LEU
A
336
39.884
18.285
28.528
1.00
14.11
A


ATOM
2102
C
LEU
A
336
37.321
16.508
31.714
1.00
16.28
A


ATOM
2103
O
LEU
A
336
36.176
16.921
31.540
1.00
15.51
A


ATOM
2104
N
LYS
A
337
37.640
15.225
31.592
1.00
17.22
A


ATOM
2105
CA
LYS
A
337
36.624
14.243
31.235
1.00
17.39
A


ATOM
2106
CB
LYS
A
337
37.293
12.900
30.921
1.00
17.68
A


ATOM
2107
CG
LYS
A
337
38.170
12.994
29.676
1.00
22.31
A


ATOM
2108
CD
LYS
A
337
39.213
11.892
29.592
1.00
24.60
A


ATOM
2109
CE
LYS
A
337
38.620
10.560
29.189
1.00
24.76
A


ATOM
2110
NZ
LYS
A
337
39.710
9.560
28.997
1.00
25.05
A


ATOM
2111
C
LYS
A
337
35.577
14.096
32.342
1.00
17.33
A


ATOM
2112
O
LYS
A
337
34.456
13.652
32.090
1.00
14.42
A


ATOM
2113
N
ALA
A
338
35.928
14.500
33.559
1.00
15.83
A


ATOM
2114
CA
ALA
A
338
34.989
14.395
34.674
1.00
17.52
A


ATOM
2115
CB
ALA
A
338
35.749
14.167
35.980
1.00
19.68
A


ATOM
2116
C
ALA
A
338
34.095
15.621
34.804
1.00
18.83
A


ATOM
2117
O
ALA
A
338
33.252
15.687
35.695
1.00
18.94
A


ATOM
2118
N
HIS
A
339
34.262
16.596
33.918
1.00
19.42
A


ATOM
2119
CA
HIS
A
339
33.438
17.796
34.004
1.00
19.28
A


ATOM
2120
CB
HIS
A
339
33.865
18.819
32.949
1.00
19.20
A


ATOM
2121
CG
HIS
A
339
33.163
20.134
33.074
1.00
20.26
A


ATOM
2122
CD2
HIS
A
339
33.549
21.299
33.649
1.00
18.95
A


ATOM
2123
ND1
HIS
A
339
31.880
20.340
32.612
1.00
19.10
A


ATOM
2124
CE1
HIS
A
339
31.506
21.576
32.896
1.00
22.19
A


ATOM
2125
NE2
HIS
A
339
32.500
22.179
33.525
1.00
21.98
A


ATOM
2126
C
HIS
A
339
31.957
17.448
33.845
1.00
19.13
A


ATOM
2127
O
HIS
A
339
31.597
16.576
33.061
1.00
19.52
A


ATOM
2128
N
PRO
A
340
31.079
18.125
34.606
1.00
19.80
A


ATOM
2129
CD
PRO
A
340
31.424
19.119
35.640
1.00
19.08
A


ATOM
2130
CA
PRO
A
340
29.630
17.900
34.569
1.00
20.52
A


ATOM
2131
CB
PRO
A
340
29.091
19.058
35.396
1.00
20.74
A


ATOM
2132
CG
PRO
A
340
30.146
19.207
36.454
1.00
19.20
A


ATOM
2133
C
PRO
A
340
29.000
17.834
33.176
1.00
21.42
A


ATOM
2134
O
PRO
A
340
28.049
17.088
32.955
1.00
22.48
A


ATOM
2135
N
PHE
A
341
29.528
18.606
32.237
1.00
21.33
A


ATOM
2136
CA
PHE
A
341
28.985
18.610
30.886
1.00
21.57
A


ATOM
2137
CB
PHE
A
341
29.739
19.624
30.017
1.00
21.64
A


ATOM
2138
CG
PHE
A
341
29.207
19.740
28.613
1.00
23.18
A


ATOM
2139
CD1
PHE
A
341
27.903
20.171
28.382
1.00
22.58
A


ATOM
2140
CD2
PHE
A
341
30.013
19.431
27.522
1.00
21.95
A


ATOM
2141
CE1
PHE
A
341
27.410
20.292
27.082
1.00
23.54
A


ATOM
2142
CE2
PHE
A
341
29.533
19.548
26.220
1.00
21.83
A


ATOM
2143
CZ
PHE
A
341
28.228
19.980
25.998
1.00
23.23
A


ATOM
2144
C
PHE
A
341
29.055
17.226
30.237
1.00
21.84
A


ATOM
2145
O
PHE
A
341
28.232
16.896
29.389
1.00
20.37
A


ATOM
2146
N
PHE
A
342
30.034
16.422
30.640
1.00
20.51
A


ATOM
2147
CA
PHE
A
342
30.221
15.085
30.077
1.00
23.01
A


ATOM
2148
CB
PHE
A
342
31.710
14.809
29.850
1.00
18.00
A


ATOM
2149
CG
PHE
A
342
32.398
15.812
28.971
1.00
17.05
A


ATOM
2150
CD1
PHE
A
342
32.010
15.987
27.652
1.00
17.78
A


ATOM
2151
CD2
PHE
A
342
33.487
16.534
29.450
1.00
15.72
A


ATOM
2152
CE1
PHE
A
342
32.702
16.867
26.811
1.00
18.08
A


ATOM
2153
CE2
PHE
A
342
34.184
17.414
28.617
1.00
17.45
A


ATOM
2154
CZ
PHE
A
342
33.790
17.578
27.298
1.00
16.56
A


ATOM
2155
C
PHE
A
342
29.679
13.972
30.976
1.00
24.95
A


ATOM
2156
O
PHE
A
342
30.002
12.798
30.777
1.00
23.95
A


ATOM
2157
N
GLU
A
343
28.861
14.333
31.958
1.00
27.35
A


ATOM
2158
CA
GLU
A
343
28.325
13.349
32.897
1.00
30.28
A


ATOM
2159
CB
GLU
A
343
27.187
13.964
33.716
1.00
32.20
A


ATOM
2160
CG
GLU
A
343
26.581
12.991
34.714
1.00
39.71
A


ATOM
2161
CD
GLU
A
343
25.628
13.661
35.688
1.00
44.72
A


ATOM
2162
OE1
GLU
A
343
24.661
14.314
35.234
1.00
47.55
A


ATOM
2163
OE2
GLU
A
343
25.847
13.526
36.911
1.00
46.89
A


ATOM
2164
C
GLU
A
343
27.852
12.017
32.305
1.00
28.98
A


ATOM
2165
O
GLU
A
343
28.225
10.952
32.800
1.00
31.73
A


ATOM
2166
N
SER
A
344
27.037
12.067
31.258
1.00
26.09
A


ATOM
2167
CA
SER
A
344
26.520
10.838
30.656
1.00
28.36
A


ATOM
2168
CB
SER
A
344
25.129
11.089
30.067
1.00
28.73
A


ATOM
2169
OG
SER
A
344
25.203
11.942
28.940
1.00
30.91
A


ATOM
2170
C
SER
A
344
27.407
10.214
29.577
1.00
27.66
A


ATOM
2171
O
SER
A
344
26.987
9.281
28.900
1.00
28.66
A


ATOM
2172
N
VAL
A
345
28.627
10.715
29.419
1.00
26.75
A


ATOM
2173
CA
VAL
A
345
29.534
10.183
28.402
1.00
23.44
A


ATOM
2174
CB
VAL
A
345
30.565
11.256
27.950
1.00
23.10
A


ATOM
2175
CG1
VAL
A
345
31.589
10.631
26.995
1.00
22.24
A


ATOM
2176
CG2
VAL
A
345
29.854
12.418
27.275
1.00
20.05
A


ATOM
2177
C
VAL
A
345
30.326
8.957
28.855
1.00
24.26
A


ATOM
2178
O
VAL
A
345
30.876
8.930
29.960
1.00
22.83
A


ATOM
2179
N
THR
A
346
30.374
7.942
27.997
1.00
21.77
A


ATOM
2180
CA
THR
A
346
31.153
6.740
28.272
1.00
23.70
A


ATOM
2181
CB
THR
A
346
30.391
5.455
27.857
1.00
26.53
A


ATOM
2182
OG1
THR
A
346
29.248
5.284
28.706
1.00
29.98
A


ATOM
2183
CG2
THR
A
346
31.289
4.231
27.990
1.00
24.28
A


ATOM
2184
C
THR
A
346
32.383
6.945
27.385
1.00
23.43
A


ATOM
2185
O
THR
A
346
32.306
6.827
26.160
1.00
24.50
A


ATOM
2186
N
TRP
A
347
33.508
7.270
28.013
1.00
22.98
A


ATOM
2187
CA
TRP
A
347
34.744
7.569
27.300
1.00
23.81
A


ATOM
2188
CB
TRP
A
347
35.683
8.352
28.219
1.00
22.54
A


ATOM
2189
CG
TRP
A
347
35.128
9.658
28.693
1.00
20.61
A


ATOM
2190
CD2
TRP
A
347
35.257
10.927
28.040
1.00
19.11
A


ATOM
2191
CE2
TRP
A
347
34.581
11.881
28.838
1.00
18.39
A


ATOM
2192
CE3
TRP
A
347
35.878
11.351
26.858
1.00
18.16
A


ATOM
2193
CD1
TRP
A
347
34.397
9.883
29.828
1.00
18.35
A


ATOM
2194
NE1
TRP
A
347
34.065
11.218
29.923
1.00
19.51
A


ATOM
2195
CZ2
TRP
A
347
34.510
13.234
28.491
1.00
16.88
A


ATOM
2196
CZ3
TRP
A
347
35.808
12.701
26.511
1.00
17.23
A


ATOM
2197
CH2
TRP
A
347
35.127
13.624
27.327
1.00
18.16
A


ATOM
2198
C
TRP
A
347
35.538
6.429
26.675
1.00
25.79
A


ATOM
2199
O
TRP
A
347
36.304
6.654
25.742
1.00
24.67
A


ATOM
2200
N
ALA
A
348
35.360
5.215
27.183
1.00
27.10
A


ATOM
2201
CA
ALA
A
348
36.116
4.063
26.697
1.00
27.46
A


ATOM
2202
CB
ALA
A
348
35.899
2.869
27.636
1.00
27.09
A


ATOM
2203
C
ALA
A
348
35.895
3.620
25.256
1.00
27.18
A


ATOM
2204
O
ALA
A
348
36.830
3.148
24.613
1.00
29.41
A


ATOM
2205
N
ASN
A
349
34.682
3.769
24.735
1.00
26.55
A


ATOM
2206
CA
ASN
A
349
34.418
3.310
23.375
1.00
27.28
A


ATOM
2207
CB
ASN
A
349
33.700
1.962
23.444
1.00
29.37
A


ATOM
2208
CG
ASN
A
349
32.299
2.088
24.013
1.00
30.92
A


ATOM
2209
OD1
ASN
A
349
32.045
2.942
24.859
1.00
30.17
A


ATOM
2210
ND2
ASN
A
349
31.386
1.237
23.553
1.00
33.52
A


ATOM
2211
C
ASN
A
349
33.599
4.265
22.509
1.00
26.47
A


ATOM
2212
O
ASN
A
349
32.669
3.843
21.819
1.00
25.87
A


ATOM
2213
N
LEU
A
350
33.947
5.543
22.518
1.00
24.45
A


ATOM
2214
CA
LEU
A
350
33.203
6.510
21.721
1.00
23.14
A


ATOM
2215
CB
LEU
A
350
33.837
7.898
21.848
1.00
23.22
A


ATOM
2216
CG
LEU
A
350
33.659
8.605
23.191
1.00
21.05
A


ATOM
2217
CD1
LEU
A
350
34.646
9.756
23.293
1.00
19.36
A


ATOM
2218
CD2
LEU
A
350
32.220
9.094
23.319
1.00
18.78
A


ATOM
2219
C
LEU
A
350
33.082
6.152
20.240
1.00
22.60
A


ATOM
2220
O
LEU
A
350
32.011
6.296
19.650
1.00
21.15
A


ATOM
2221
N
HIS
A
351
34.165
5.689
19.627
1.00
23.13
A


ATOM
2222
CA
HIS
A
351
34.089
5.387
18.204
1.00
27.83
A


ATOM
2223
CB
HIS
A
351
35.506
5.325
17.596
1.00
29.36
A


ATOM
2224
CG
HIS
A
351
36.082
3.950
17.493
1.00
32.07
A


ATOM
2225
CD2
HIS
A
351
36.611
3.128
18.431
1.00
32.39
A


ATOM
2226
ND1
HIS
A
351
36.197
3.285
16.291
1.00
33.02
A


ATOM
2227
CE1
HIS
A
351
36.775
2.113
16.493
1.00
33.58
A


ATOM
2228
NE2
HIS
A
351
37.036
1.992
17.782
1.00
31.76
A


ATOM
2229
C
HIS
A
351
33.258
4.144
17.874
1.00
28.12
A


ATOM
2230
O
HIS
A
351
33.015
3.847
16.707
1.00
29.49
A


ATOM
2231
N
GLN
A
352
32.800
3.442
18.908
1.00
29.28
A


ATOM
2232
CA
GLN
A
352
31.963
2.255
18.726
1.00
29.67
A


ATOM
2233
CB
GLN
A
352
32.366
1.145
19.694
1.00
30.56
A


ATOM
2234
CG
GLN
A
352
33.169
0.041
19.041
1.00
30.88
A


ATOM
2235
CD
GLN
A
352
34.493
−0.186
19.729
1.00
31.21
A


ATOM
2236
OE1
GLN
A
352
34.541
−0.450
20.928
1.00
30.76
A


ATOM
2237
NE2
GLN
A
352
35.578
−0.084
18.971
1.00
32.30
A


ATOM
2238
C
GLN
A
352
30.504
2.638
18.963
1.00
30.42
A


ATOM
2239
O
GLN
A
352
29.595
1.831
18.770
1.00
29.01
A


ATOM
2240
N
GLN
A
353
30.290
3.875
19.397
1.00
27.64
A


ATOM
2241
CA
GLN
A
353
28.948
4.365
19.652
1.00
27.42
A


ATOM
2242
CB
GLN
A
353
28.977
5.401
20.775
1.00
25.77
A


ATOM
2243
CG
GLN
A
353
29.408
4.837
22.115
1.00
27.34
A


ATOM
2244
CD
GLN
A
353
29.638
5.914
23.156
1.00
27.19
A


ATOM
2245
OE1
GLN
A
353
28.875
6.872
23.252
1.00
28.29
A


ATOM
2246
NE2
GLN
A
353
30.687
5.753
23.951
1.00
28.79
A


ATOM
2247
C
GLN
A
353
28.375
4.989
18.385
1.00
29.00
A


ATOM
2248
O
GLN
A
353
29.118
5.455
17.516
1.00
29.14
A


ATOM
2249
N
THR
A
354
27.053
4.984
18.276
1.00
27.31
A


ATOM
2250
CA
THR
A
354
26.390
5.568
17.119
1.00
27.85
A


ATOM
2251
CB
THR
A
354
24.991
4.941
16.904
1.00
30.69
A


ATOM
2252
OG1
THR
A
354
25.132
3.532
16.665
1.00
30.07
A


ATOM
2253
CG2
THR
A
354
24.289
5.585
15.709
1.00
29.58
A


ATOM
2254
C
THR
A
354
26.244
7.062
17.376
1.00
26.85
A


ATOM
2255
O
THR
A
354
25.592
7.475
18.329
1.00
25.77
A


ATOM
2256
N
PRO
A
355
26.867
7.898
16.533
1.00
27.22
A


ATOM
2257
CD
PRO
A
355
27.792
7.588
15.431
1.00
25.89
A


ATOM
2258
CA
PRO
A
355
26.763
9.346
16.734
1.00
27.23
A


ATOM
2259
CB
PRO
A
355
27.625
9.915
15.609
1.00
24.91
A


ATOM
2260
CG
PRO
A
355
28.643
8.838
15.385
1.00
25.54
A


ATOM
2261
C
PRO
A
355
25.322
9.837
16.641
1.00
28.07
A


ATOM
2262
O
PRO
A
355
24.548
9.364
15.810
1.00
27.24
A


ATOM
2263
N
PRO
A
356
24.941
10.792
17.500
1.00
28.28
A


ATOM
2264
CD
PRO
A
356
25.752
11.560
18.462
1.00
28.31
A


ATOM
2265
CA
PRO
A
356
23.572
11.306
17.448
1.00
28.44
A


ATOM
2266
CB
PRO
A
356
23.539
12.301
18.604
1.00
28.11
A


ATOM
2267
CG
PRO
A
356
24.946
12.832
18.612
1.00
26.86
A


ATOM
2268
C
PRO
A
356
23.363
11.978
16.097
1.00
29.25
A


ATOM
2269
O
PRO
A
356
24.304
12.537
15.529
1.00
27.27
A


ATOM
2270
N
ALA
A
357
22.143
11.910
15.575
1.00
30.45
A


ATOM
2271
CA
ALA
A
357
21.848
12.521
14.287
1.00
32.81
A


ATOM
2272
CB
ALA
A
357
20.507
12.019
13.757
1.00
31.99
A


ATOM
2273
C
ALA
A
357
21.824
14.035
14.448
1.00
35.05
A


ATOM
2274
O
ALA
A
357
21.194
14.561
15.369
1.00
35.04
A


ATOM
2275
N
LEU
A
358
22.516
14.730
13.552
1.00
37.81
A


ATOM
2276
CA
LEU
A
358
22.578
16.185
13.597
1.00
42.15
A


ATOM
2277
CB
LEU
A
358
23.679
16.681
12.658
1.00
39.54
A


ATOM
2278
CG
LEU
A
358
25.086
16.285
13.109
1.00
39.51
A


ATOM
2279
CD1
LEU
A
358
26.102
16.686
12.062
1.00
39.29
A


ATOM
2280
CD2
LEU
A
358
25.395
16.953
14.445
1.00
40.01
A


ATOM
2281
C
LEU
A
358
21.241
16.837
13.242
1.00
45.91
A


ATOM
2282
O
LEU
A
358
20.874
16.927
12.069
1.00
45.71
A


ATOM
2283
N
THR
A
359
20.530
17.290
14.275
1.00
50.06
A


ATOM
2284
CA
THR
A
359
19.223
17.939
14.140
1.00
53.73
A


ATOM
2285
CB
THR
A
359
19.353
19.428
13.726
1.00
54.04
A


ATOM
2286
OG1
THR
A
359
19.995
19.521
12.448
1.00
56.35
A


ATOM
2287
CG2
THR
A
359
20.158
20.204
14.763
1.00
54.32
A


ATOM
2288
C
THR
A
359
18.309
17.236
13.139
1.00
54.47
A


ATOM
2289
O
THR
A
359
18.483
16.016
12.930
1.00
55.90
A


ATOM
2290
OXT
THR
A
359
17.407
17.908
12.595
1.00
56.97
A


ATOM
2291
OH2
TIP
S
1
42.566
19.118
34.302
1.00
15.09
S


ATOM
2292
OH2
TIP
S
2
41.052
32.378
19.857
1.00
15.82
S


ATOM
2293
OH2
TIP
S
3
37.014
33.030
17.747
1.00
16.95
S


ATOM
2294
OH2
TIP
S
5
45.353
24.370
18.152
1.00
16.85
S


ATOM
2295
OH2
TIP
S
6
31.896
13.930
33.235
1.00
20.42
S


ATOM
2296
OH2
TIP
S
7
50.351
22.781
28.249
1.00
21.14
S


ATOM
2297
OH2
TIP
S
8
45.246
−0.589
−0.734
1.00
17.74
S


ATOM
2298
OH2
TIP
S
11
46.249
−0.348
−8.523
1.00
21.32
S


ATOM
2299
OH2
TIP
S
14
45.756
11.148
29.680
1.00
21.94
S


ATOM
2300
OH2
TIP
S
15
44.273
13.157
34.592
1.00
15.61
S


ATOM
2301
OH2
TIP
S
17
53.598
3.722
−1.720
1.00
21.45
S


ATOM
2302
OH2
TIP
S
18
46.049
13.087
31.565
1.00
20.35
S


ATOM
2303
OH2
TIP
S
19
53.422
22.401
−3.280
1.00
23.26
S


ATOM
2304
OH2
TIP
S
20
34.587
7.922
5.383
1.00
22.58
S


ATOM
2305
OH2
TIP
S
21
45.053
27.379
19.376
1.00
29.60
S


ATOM
2306
OH2
TIP
S
23
28.899
36.416
28.633
1.00
31.68
S


ATOM
2307
OH2
TIP
S
24
35.531
11.645
−8.219
1.00
23.45
S


ATOM
2308
OH2
TIP
S
25
47.364
28.787
19.612
1.00
23.03
S


ATOM
2309
OH2
TIP
S
27
48.859
21.588
12.634
1.00
23.76
S


ATOM
2310
OH2
TIP
S
29
48.805
8.920
23.626
1.00
22.23
S


ATOM
2311
OH2
TIP
S
31
48.619
7.247
10.112
1.00
21.32
S


ATOM
2312
OH2
TIP
S
34
44.824
28.720
15.621
1.00
25.27
S


ATOM
2313
OH2
TIP
S
35
26.030
12.634
13.407
1.00
21.61
S


ATOM
2314
OH2
TIP
S
36
50.462
19.810
40.066
1.00
25.45
S


ATOM
2315
OH2
TIP
S
37
39.631
23.510
−0.239
1.00
30.88
S


ATOM
2316
OH2
TIP
S
40
44.734
42.655
10.346
1.00
30.84
S


ATOM
2317
OH2
TIP
S
41
54.653
3.902
1.503
1.00
27.14
S


ATOM
2318
OH2
TIP
S
45
45.693
21.923
39.754
1.00
28.30
S


ATOM
2319
OH2
TIP
S
47
47.820
16.413
7.805
1.00
25.73
S


ATOM
2320
OH2
TIP
S
48
50.292
31.412
29.642
1.00
32.79
S


ATOM
2321
OH2
TIP
S
49
26.056
16.646
34.827
1.00
29.80
S


ATOM
2322
OH2
TIP
S
52
31.714
10.996
31.855
1.00
29.15
S


ATOM
2323
OH2
TIP
S
53
46.108
23.843
−4.299
1.00
24.21
S


ATOM
2324
OH2
TIP
S
54
37.645
11.206
34.448
1.00
28.56
S


ATOM
2325
OH2
TIP
S
55
26.371
28.513
12.142
1.00
32.08
S


ATOM
2326
OH2
TIP
S
58
33.564
19.700
3.483
1.00
28.28
S


ATOM
2327
OH2
TIP
S
64
48.295
−0.632
14.280
1.00
32.13
S


ATOM
2328
OH2
TIP
S
65
40.064
26.036
34.324
1.00
24.17
S


ATOM
2329
OH2
TIP
S
66
29.570
3.958
14.729
1.00
28.94
S


ATOM
2330
OH2
TIP
S
72
60.085
11.604
6.814
1.00
38.35
S


ATOM
2331
OH2
TIP
S
73
39.203
44.403
18.686
1.00
26.61
S


ATOM
2332
OH2
TIP
S
76
47.312
12.366
27.366
1.00
28.51
S


ATOM
2333
OH2
TIP
S
80
43.862
33.771
33.329
1.00
28.82
S


ATOM
2334
OH2
TIP
S
81
57.890
13.106
2.128
1.00
40.62
S


ATOM
2335
OH2
TIP
S
82
41.663
34.381
32.043
1.00
19.35
S


ATOM
2336
OH2
TIP
S
85
50.974
40.331
19.200
1.00
21.14
S


ATOM
2337
OH2
TIP
S
88
47.925
−0.832
−6.556
1.00
24.11
S


ATOM
2338
OH2
TIP
S
90
27.231
28.336
33.481
1.00
27.64
S


ATOM
2339
OH2
TIP
S
91
43.651
−7.101
−7.995
1.00
24.33
S


ATOM
2340
OH2
TIP
S
92
49.325
4.387
19.370
1.00
28.02
S


ATOM
2341
OH2
TIP
S
93
46.231
11.549
33.898
1.00
29.40
S


ATOM
2342
OH2
TIP
S
94
63.889
24.831
1.168
1.00
26.53
S


ATOM
2343
OH2
TIP
S
96
56.396
4.952
−6.749
1.00
28.00
S


ATOM
2344
OH2
TIP
S
98
35.510
27.986
11.558
1.00
29.24
S


ATOM
2345
OH2
TIP
S
100
49.942
24.366
30.265
1.00
31.61
S


ATOM
2346
OH2
TIP
S
101
56.121
7.113
−8.298
1.00
31.57
S


ATOM
2347
OH2
TIP
S
102
58.318
19.957
−8.378
1.00
26.95
S


ATOM
2348
OH2
TIP
S
103
49.647
22.446
39.624
1.00
40.57
S


ATOM
2349
OH2
TIP
S
104
45.359
7.052
13.052
1.00
26.27
S


ATOM
2350
OH2
TIP
S
105
37.150
32.340
32.346
1.00
34.45
S


ATOM
2351
OH2
TIP
S
107
43.465
40.457
8.240
1.00
40.48
S


ATOM
2352
OH2
TIP
S
119
36.644
8.257
13.418
1.00
30.70
S


ATOM
2353
OH2
TIP
S
123
41.912
−8.974
−8.264
1.00
26.08
S


ATOM
2354
OH2
TIP
S
124
62.424
15.800
−7.411
1.00
24.08
S


ATOM
2355
OH2
TIP
S
126
37.266
18.656
−9.097
1.00
28.99
S


ATOM
2356
OH2
TIP
S
127
43.129
26.845
14.606
1.00
25.19
S


ATOM
2357
OH2
TIP
S
128
36.339
32.639
29.802
1.00
29.25
S


ATOM
2358
OH2
TIP
S
130
54.051
14.561
26.498
1.00
33.93
S


ATOM
2359
OH2
TIP
S
131
41.805
−4.242
5.492
1.00
33.72
S


ATOM
2360
OH2
TIP
S
133
38.873
25.163
36.697
1.00
30.69
S


ATOM
2361
OH2
TIP
S
134
28.777
8.553
25.307
1.00
31.43
S


ATOM
2362
OH2
TIP
S
135
53.672
10.546
−12.803
1.00
33.45
S


ATOM
2363
OH2
TIP
S
136
59.892
15.434
11.467
1.00
31.39
S


ATOM
2364
OH2
TIP
S
137
31.040
12.361
35.470
1.00
34.07
S


ATOM
2365
OH2
TIP
S
139
33.489
14.292
−0.598
1.00
40.68
S


ATOM
2366
OH2
TIP
S
140
46.918
8.748
11.662
1.00
29.23
S


ATOM
2367
OH2
TIP
S
141
46.297
−7.287
−9.196
1.00
42.20
S


ATOM
2368
OH2
TIP
S
142
58.193
6.715
−4.685
1.00
35.48
S


ATOM
2369
OH2
TIP
S
143
44.598
4.435
12.503
1.00
27.68
S


ATOM
2370
OH2
TIP
S
144
27.003
5.999
12.450
1.00
36.30
S


ATOM
2371
OH2
TIP
S
145
43.676
32.852
35.735
1.00
35.70
S


ATOM
2372
OH2
TIP
S
146
35.783
18.628
36.452
1.00
34.62
S


ATOM
2373
OH2
TIP
S
147
25.402
4.058
20.638
1.00
45.03
S


ATOM
2374
OH2
TIP
S
148
45.839
35.853
33.724
1.00
35.47
S


ATOM
2375
OH2
TIP
S
149
22.176
18.976
16.752
1.00
31.87
S


ATOM
2376
OH2
TIP
S
150
43.986
33.179
10.162
1.00
37.70
S


ATOM
2377
OH2
TIP
S
151
50.653
20.347
42.428
1.00
35.80
S


ATOM
2378
OH2
TIP
S
152
47.843
24.314
9.506
1.00
31.05
S


ATOM
2379
OH2
TIP
S
153
44.693
5.273
−14.175
1.00
29.90
S


ATOM
2380
OH2
TIP
S
155
26.560
36.851
31.684
1.00
49.29
S


ATOM
2381
OH2
TIP
S
156
46.867
8.019
−12.951
1.00
29.21
S


ATOM
2382
OH2
TIP
S
157
30.432
28.741
12.438
1.00
37.76
S


ATOM
2383
OH2
TIP
S
158
41.004
20.553
6.423
1.00
39.53
S


ATOM
2384
OH2
TIP
S
159
49.258
20.069
29.294
1.00
33.97
S


ATOM
2385
OH2
TIP
S
160
48.082
28.459
16.489
1.00
33.10
S


ATOM
2386
OH2
TIP
S
161
47.448
18.625
27.683
1.00
34.87
S


ATOM
2387
OH2
TIP
S
162
19.687
20.632
23.411
1.00
35.01
S


ATOM
2388
OH2
TIP
S
163
32.402
−1.266
22.443
1.00
37.26
S


ATOM
2389
OH2
TIP
S
164
39.475
33.468
33.237
1.00
35.34
S


ATOM
2390
OH2
TIP
S
165
44.277
18.950
5.162
1.00
45.14
S


ATOM
2391
OH2
TIP
S
166
34.797
30.523
10.736
1.00
47.55
S


ATOM
2392
OH2
TIP
S
167
46.541
3.526
−14.949
1.00
26.54
S


ATOM
2393
OH2
TIP
S
168
36.333
16.371
1.539
1.00
38.68
S


ATOM
2394
OH2
TIP
S
169
46.761
38.936
27.403
1.00
34.66
S


ATOM
2395
OH2
TIP
S
170
24.163
13.264
11.375
1.00
41.23
S


ATOM
2396
OH2
TIP
S
171
48.459
15.018
31.951
1.00
38.11
S


ATOM
2397
OH2
TIP
S
172
34.261
23.193
40.004
1.00
48.96
S


ATOM
2398
OH2
TIP
S
173
45.924
−0.026
13.224
1.00
39.55
S


ATOM
2399
OH2
TIP
S
175
41.384
37.389
32.543
1.00
40.74
S


ATOM
2400
OH2
TIP
S
177
49.394
35.312
27.150
1.00
44.33
S


ATOM
2401
OH2
TIP
S
178
29.066
29.942
34.359
1.00
41.46
S


ATOM
2402
OH2
TIP
S
180
49.354
19.467
7.273
1.00
34.56
S


ATOM
2403
OH2
TIP
S
181
25.298
17.029
31.863
1.00
47.74
S


ATOM
2404
OH2
TIP
S
182
37.071
25.027
4.669
1.00
43.87
S


ATOM
2405
OH2
TIP
S
183
22.581
7.487
18.691
1.00
41.75
S


ATOM
2406
OH2
TIP
S
184
32.269
7.011
−1.891
1.00
48.84
S


ATOM
2407
OH2
TIP
S
185
48.234
0.494
6.833
1.00
48.16
S


ATOM
2408
OH2
TIP
S
187
20.008
14.658
19.211
1.00
45.27
S


ATOM
2409
OH2
TIP
S
188
49.341
22.698
42.272
1.00
42.20
S


ATOM
2410
OH2
TIP
S
190
61.292
18.260
−8.097
1.00
45.21
S


ATOM
2411
OH2
TIP
S
191
28.152
10.606
2.819
1.00
40.38
S


ATOM
2412
OH2
TIP
S
192
25.626
12.619
23.191
1.00
34.27
S


ATOM
2413
OH2
TIP
S
193
59.876
11.603
1.216
1.00
46.54
S


ATOM
2414
OH2
TIP
S
194
57.592
21.183
−10.646
1.00
45.82
S


ATOM
2415
OH2
TIP
S
195
31.509
36.649
21.499
1.00
38.73
S


ATOM
2416
OH2
TIP
S
197
50.270
−1.543
−6.136
1.00
42.66
S


ATOM
2417
OH2
TIP
S
198
24.467
8.729
13.088
1.00
42.78
S


ATOM
2418
OH2
TIP
S
199
38.098
8.699
25.759
1.00
32.80
S


ATOM
2419
OH2
TIP
S
200
57.831
11.358
−13.255
1.00
45.31
S


ATOM
2420
OH2
TIP
S
201
23.888
22.328
30.524
1.00
37.12
S


ATOM
2421
OH2
TIP
S
202
47.691
26.068
37.666
1.00
37.92
S


ATOM
2422
OH2
TIP
S
203
38.653
7.070
29.307
1.00
50.54
S


ATOM
2423
OH2
TIP
S
206
44.424
27.583
2.092
1.00
53.50
S


ATOM
2424
OH2
TIP
S
212
22.258
2.296
17.948
1.00
47.38
S


ATOM
2425
OH2
TIP
S
214
19.843
17.943
23.303
1.00
30.36
S


ATOM
2426
OH2
TIP
S
216
27.647
11.344
24.681
1.00
31.32
S


ATOM
2427
OH2
TIP
S
217
37.953
7.817
−9.284
1.00
45.97
S


ATOM
2428
OH2
TIP
S
218
33.845
34.040
12.124
1.00
38.11
S


ATOM
2429
OH2
TIP
S
219
58.484
15.269
13.717
1.00
38.26
S


ATOM
2430
OH2
TIP
S
220
48.526
40.920
26.583
1.00
35.23
S


ATOM
2431
OH2
TIP
S
222
52.094
21.184
38.122
1.00
29.86
S


ATOM
2432
OH2
TIP
S
223
36.889
5.881
3.281
1.00
37.63
S


ATOM
2433
OH2
TIP
S
224
47.642
−1.401
−10.684
1.00
34.89
S


ATOM
2434
OH2
TIP
S
226
47.284
2.916
19.133
1.00
34.10
S


ATOM
2435
OH2
TIP
S
227
42.468
4.463
−15.039
1.00
37.98
S


ATOM
2436
OH2
TIP
S
228
19.169
22.832
21.831
1.00
41.57
S


ATOM
2437
OH2
TIP
S
231
57.592
12.689
14.880
1.00
50.22
S


ATOM
2438
OH2
TIP
S
232
27.102
9.176
5.655
1.00
40.57
S


ATOM
2439
OH2
TIP
S
233
58.618
9.072
−11.925
1.00
50.71
S


ATOM
2440
OH2
TIP
S
234
22.822
25.342
19.945
1.00
34.93
S


ATOM
2441
OH2
TIP
S
236
24.831
32.218
28.901
1.00
37.69
S


ATOM
2442
OH2
TIP
S
237
20.045
10.774
16.992
1.00
39.57
S


ATOM
2443
OH2
TIP
S
238
58.019
19.850
15.679
1.00
41.42
S


ATOM
2444
OH2
TIP
S
239
19.490
20.949
26.114
1.00
34.55
S


ATOM
2445
OH2
TIP
S
240
61.187
26.377
7.346
1.00
39.68
S


ATOM
2446
OH2
TIP
S
241
33.680
38.342
19.389
1.00
48.93
S


ATOM
2447
OH2
TIP
S
242
51.539
31.612
10.881
1.00
55.65
S


ATOM
2448
OH2
TIP
S
244
25.872
14.431
30.404
1.00
46.69
S


ATOM
2449
OH2
TIP
S
248
37.332
5.849
9.544
1.00
43.81
S


ATOM
2450
OH2
TIP
S
250
39.087
−1.293
−9.655
1.00
42.96
S


ATOM
2451
OH2
TIP
S
258
23.938
30.000
30.010
1.00
38.89
S


ATOM
2452
OH2
TIP
S
259
24.949
29.749
32.578
1.00
40.17
S


ATOM
2453
OH2
TIP
S
260
32.111
17.986
1.918
1.00
48.36
S


ATOM
2454
OH2
TIP
S
266
21.404
12.876
25.603
1.00
57.17
S


ATOM
2455
OH2
TIP
S
269
35.425
36.767
12.550
1.00
30.70
S


ATOM
2456
OH2
TIP
S
270
52.438
25.529
30.131
1.00
44.85
S


ATOM
2457
OH2
TIP
S
271
53.299
20.156
36.003
1.00
37.15
S


ATOM
2458
OH2
TIP
S
272
50.914
6.919
23.723
1.00
43.29
S


ATOM
2459
OH2
TIP
S
274
31.578
30.795
11.014
1.00
50.15
S


ATOM
2460
OH2
TIP
S
275
26.341
7.243
22.447
1.00
39.40
S


ATOM
2461
OH2
TIP
S
276
60.392
18.195
10.235
1.00
37.91
S


ATOM
2462
OH2
TIP
S
277
47.355
−9.081
−10.821
1.00
48.18
S


ATOM
2463
OH2
TIP
S
279
41.304
6.175
−16.647
1.00
38.12
S


ATOM
2464
OH2
TIP
S
282
33.299
21.620
37.881
1.00
46.29
S


ATOM
2465
OH2
TIP
S
283
56.469
26.112
−8.575
1.00
43.71
S


ATOM
2466
OH2
TIP
S
287
48.382
26.573
7.246
1.00
41.43
S


ATOM
2467
OH2
TIP
S
288
56.240
7.245
−11.331
1.00
41.79
S


ATOM
2468
OH2
TIP
S
290
49.060
14.978
28.166
1.00
37.03
S


ATOM
2469
OH2
TIP
S
291
37.095
44.270
26.442
1.00
45.08
S


ATOM
2470
OH2
TIP
S
292
47.814
−0.384
−13.299
1.00
48.60
S


ATOM
2471
OH2
TIP
S
297
58.081
2.784
−7.841
1.00
41.89
S


ATOM
2472
OH2
TIP
S
298
36.447
45.321
18.644
1.00
54.91
S


ATOM
2473
OH2
TIP
S
299
49.029
23.328
1.767
1.00
30.55
S


ATOM
2474
OH2
TIP
S
301
24.375
13.771
8.634
1.00
48.47
S


ATOM
2475
OH2
TIP
S
303
47.904
36.798
28.653
1.00
35.76
S


ATOM
2476
OH2
TIP
S
305
51.156
40.821
27.172
1.00
43.59
S


ATOM
2477
OH2
TIP
S
306
32.943
28.917
35.227
1.00
42.60
S


ATOM
2478
OH2
TIP
S
307
58.462
28.373
6.251
1.00
46.15
S


ATOM
2479
OH2
TIP
S
308
41.964
30.940
36.712
1.00
48.26
S


ATOM
2480
OH2
TIP
S
313
51.176
−1.922
−3.336
1.00
50.61
S


ATOM
2481
OH2
TIP
S
1001
21.319
36.868
23.805
1.00
36.97
S


ATOM
2482
OH2
TIP
S
1002
48.880
32.620
27.617
1.00
44.40
S


ATOM
2483
OH2
TIP
S
1003
61.880
19.473
11.767
1.00
45.49
S


ATOM
2484
OH2
TIP
S
1004
52.770
21.424
26.815
1.00
24.43
S


ATOM
2485
OH2
TIP
S
1005
35.373
29.094
36.197
1.00
35.97
S


ATOM
2486
OH2
TIP
S
1006
40.815
−6.636
4.389
1.00
43.15
S


ATOM
2487
OH2
TIP
S
1007
44.953
1.286
11.272
1.00
49.45
S


ATOM
2488
OH2
TIP
S
1010
21.004
16.168
27.009
1.00
48.51
S


ATOM
2489
OH2
TIP
S
1011
47.094
41.786
9.243
1.00
50.10
S


ATOM
2490
OH2
TIP
S
1012
32.479
2.978
14.158
1.00
49.47
S


ATOM
2491
O12
GLC
G
1
48.557
11.372
−12.279
1.00
40.72
G


ATOM
2492
C11
GLC
G
1
48.836
12.133
−11.097
1.00
38.05
G


ATOM
2493
C13
GLC
G
1
49.266
13.554
−11.476
1.00
38.09
G


ATOM
2494
O14
GLC
G
1
49.559
14.299
−10.292
1.00
33.99
G


ATOM
2495
C15
GLC
G
1
48.150
14.257
−12.257
1.00
37.32
G


ATOM
2496
O16
GLC
G
1
48.574
15.582
−12.604
1.00
36.74
G


ATOM
2497
O12
GLC
G
2
40.114
−6.634
−6.562
1.00
33.52
G


ATOM
2498
C11
GLC
G
2
38.967
−6.592
−7.404
1.00
31.05
G


ATOM
2499
C13
GLC
G
2
37.712
−6.417
−6.552
1.00
31.56
G


ATOM
2500
O14
GLC
G
2
36.554
−6.406
−7.389
1.00
30.70
G


ATOM
2501
C15
GLC
G
2
37.792
−5.109
−5.761
1.00
30.03
G


ATOM
2502
O16
GLC
G
2
36.609
−4.961
−4.975
1.00
29.66
G


ATOM
2503
O12
GLC
G
3
44.030
8.243
−13.470
1.00
37.90
G


ATOM
2504
C11
GLC
G
3
43.950
9.648
−13.690
1.00
38.47
G


ATOM
2505
C13
GLC
G
3
42.747
9.974
−14.579
1.00
39.52
G


ATOM
2506
O14
GLC
G
3
41.551
9.526
−13.942
1.00
39.39
G


ATOM
2507
C15
GLC
G
3
42.878
9.280
−15.934
1.00
41.43
G


ATOM
2508
O16
GLC
G
3
41.736
9.613
−16.731
1.00
40.78
G


ATOM
2509
O12
GLC
G
5
40.556
1.005
2.289
1.00
45.25
G


ATOM
2510
C11
GLC
G
5
40.966
2.332
1.960
1.00
40.56
G


ATOM
2511
C13
GLC
G
5
40.187
3.327
2.814
1.00
40.36
G


ATOM
2512
O14
GLC
G
5
38.791
3.169
2.572
1.00
40.71
G


ATOM
2513
C15
GLC
G
5
40.619
4.751
2.464
1.00
40.04
G


ATOM
2514
O16
GLC
G
5
39.885
5.681
3.256
1.00
36.89
G


ATOM
2515
O12
GLC
G
6
36.951
22.702
40.046
1.00
63.04
G


ATOM
2516
C11
GLC
G
6
37.592
21.583
39.422
1.00
62.46
G


ATOM
2517
C13
GLC
G
6
38.104
21.978
38.030
1.00
61.14
G


ATOM
2518
O14
GLC
G
6
39.034
23.054
38.168
1.00
61.72
G


ATOM
2519
C15
GLC
G
6
36.948
22.429
37.126
1.00
60.51
G


ATOM
2520
O16
GLC
G
6
35.992
21.372
36.960
1.00
58.61
G


ATOM
2521
O12
GLC
G
7
37.316
0.281
14.299
1.00
73.45
G


ATOM
2522
C11
GLC
G
7
37.655
−0.758
15.222
1.00
72.78
G


ATOM
2523
C13
GLC
G
7
36.592
−1.856
15.157
1.00
72.98
G


ATOM
2524
O14
GLC
G
7
35.320
−1.299
15.498
1.00
73.88
G


ATOM
2525
C15
GLC
G
7
36.924
−2.989
16.134
1.00
73.66
G


ATOM
2526
O16
GLC
G
7
36.972
−2.493
17.478
1.00
75.38
G


ATOM
2527
O12
GLC
G
8
51.921
21.898
5.908
1.00
62.51
G


ATOM
2528
C11
GLC
G
8
52.447
20.871
5.063
1.00
63.42
G


ATOM
2529
C13
GLC
G
8
51.476
20.597
3.908
1.00
64.28
G


ATOM
2530
O14
GLC
G
8
51.297
21.794
3.150
1.00
66.28
G


ATOM
2531
C15
GLC
G
8
50.121
20.137
4.448
1.00
64.49
G


ATOM
2532
O16
GLC
G
8
49.233
19.886
3.357
1.00
64.01
G


ATOM
2533
O12
GLC
G
10
36.044
37.499
29.523
1.00
56.89
G


ATOM
2534
C11
GLC
G
10
35.164
36.645
30.259
1.00
56.97
G


ATOM
2535
C13
GLC
G
10
33.849
36.489
29.494
1.00
56.11
G


ATOM
2536
O14
GLC
G
10
33.248
37.772
29.308
1.00
56.44
G


ATOM
2537
C15
GLC
G
10
32.900
35.580
30.277
1.00
55.84
G


ATOM
2538
O16
GLC
G
10
31.674
35.442
29.557
1.00
55.39
G


ATOM
2539
O3G
ATP
N
1
46.280
25.658
5.170
1.00
51.49
N


ATOM
2540
PG
ATP
N
1
46.464
25.053
3.691
1.00
52.22
N


ATOM
2541
O1G
ATP
N
1
47.406
23.911
3.763
1.00
51.41
N


ATOM
2542
O2G
ATP
N
1
46.794
26.182
2.784
1.00
52.07
N


ATOM
2543
O3B
ATP
N
1
44.976
24.513
3.344
1.00
51.01
N


ATOM
2544
PB
ATP
N
1
44.560
22.969
3.605
1.00
50.20
N


ATOM
2545
O1B
ATP
N
1
43.083
22.898
3.669
1.00
49.41
N


ATOM
2546
O2B
ATP
N
1
45.345
22.474
4.766
1.00
50.34
N


ATOM
2547
O3A
ATP
N
1
45.070
22.231
2.255
1.00
47.77
N


ATOM
2548
PA
ATP
N
1
45.075
20.613
2.121
1.00
42.84
N


ATOM
2549
O1A
ATP
N
1
45.547
20.291
0.754
1.00
43.81
N


ATOM
2550
O2A
ATP
N
1
45.807
20.035
3.270
1.00
45.03
N


ATOM
2551
O5*
ATP
N
1
43.516
20.223
2.245
1.00
41.73
N


ATOM
2552
C5*
ATP
N
1
42.528
20.925
1.489
1.00
37.57
N


ATOM
2553
C4*
ATP
N
1
41.127
20.379
1.776
1.00
39.45
N


ATOM
2554
O4*
ATP
N
1
40.907
19.024
1.279
1.00
37.72
N


ATOM
2555
C3*
ATP
N
1
40.777
20.321
3.251
1.00
38.48
N


ATOM
2556
O3*
ATP
N
1
40.360
21.615
3.697
1.00
40.42
N


ATOM
2557
C2*
ATP
N
1
39.608
19.374
3.270
1.00
37.58
N


ATOM
2558
O2*
ATP
N
1
38.410
20.076
2.924
1.00
35.98
N


ATOM
2559
C1*
ATP
N
1
39.939
18.346
2.173
1.00
35.55
N


ATOM
2560
N9
ATP
N
1
40.628
17.156
2.747
1.00
31.76
N


ATOM
2561
C8
ATP
N
1
41.864
17.126
3.274
1.00
30.49
N


ATOM
2562
N7
ATP
N
1
42.143
15.877
3.667
1.00
29.75
N


ATOM
2563
C5
ATP
N
1
41.088
15.118
3.390
1.00
27.49
N


ATOM
2564
C4
ATP
N
1
40.125
15.925
2.810
1.00
30.02
N


ATOM
2565
N3
ATP
N
1
38.937
15.389
2.431
1.00
27.11
N


ATOM
2566
C2
ATP
N
1
38.679
14.085
2.615
1.00
25.62
N


ATOM
2567
N1
ATP
N
1
39.597
13.283
3.175
1.00
21.76
N


ATOM
2568
C6
ATP
N
1
40.800
13.768
3.571
1.00
23.90
N


ATOM
2569
N6
ATP
N
1
41.698
12.964
4.127
1.00
21.94
N


ATOM
2570
S
SO4
I
1
58.680
8.493
−0.639
1.00
56.05
I


ATOM
2571
O1
SO4
I
1
57.956
7.875
0.483
1.00
58.83
I


ATOM
2572
O2
SO4
I
1
57.886
9.607
−1.188
1.00
57.04
I


ATOM
2573
O3
SO4
I
1
58.906
7.478
−1.683
1.00
57.47
I


ATOM
2574
O4
SO4
I
1
59.976
9.008
−0.156
1.00
57.51
I


ATOM
2575
S
SO4
I
2
39.339
4.855
7.057
1.00
84.24
I


ATOM
2576
O1
SO4
I
2
39.390
6.175
7.711
1.00
85.02
I


ATOM
2577
O2
SO4
I
2
40.101
4.897
5.797
1.00
84.75
I


ATOM
2578
O3
SO4
I
2
37.936
4.506
6.766
1.00
84.94
I


ATOM
2579
O4
SO4
I
2
39.931
3.842
7.954
1.00
84.44
I


ATOM
2580
S
SO4
I
3
38.987
−2.256
3.310
1.00
58.58
I


ATOM
2581
O1
SO4
I
3
37.734
−1.675
3.827
1.00
59.11
I


ATOM
2582
O2
SO4
I
3
39.460
−1.454
2.172
1.00
59.91
I


ATOM
2583
O3
SO4
I
3
38.743
−3.640
2.866
1.00
60.97
I


ATOM
2584
O4
SO4
I
3
40.014
−2.260
4.369
1.00
59.58
I


ATOM
2585
S
SO4
I
4
34.397
5.289
30.981
1.00
64.34
I


ATOM
2586
O1
SO4
I
4
33.627
6.528
30.742
1.00
60.43
I


ATOM
2587
O2
SO4
I
4
34.337
4.427
29.782
1.00
60.11
I


ATOM
2588
O3
SO4
I
4
33.816
4.572
32.133
1.00
64.39
I


ATOM
2589
O4
SO4
I
4
35.806
5.626
31.277
1.00
63.55
I


ATOM
2590
S
SO4
I
5
55.074
−6.984
−3.711
1.00
75.40
I


ATOM
2591
O1
SO4
I
5
54.657
−7.518
−2.399
1.00
74.66
I


ATOM
2592
O2
SO4
I
5
54.209
−5.845
−4.065
1.00
74.96
I


ATOM
2593
O3
SO4
I
5
54.950
−8.034
−4.742
1.00
74.22
I


ATOM
2594
O4
SO4
I
5
56.477
−6.532
−3.633
1.00
75.15
I


ATOM
2595
O2
PO4
P
100
57.362
24.998
13.149
1.00
66.76
P


ATOM
2596
O3
PO4
P
100
59.399
26.166
13.761
1.00
66.89
P


ATOM
2597
O4
PO4
P
100
57.761
25.606
15.462
1.00
67.43
P


ATOM
2598
O1
PO4
P
100
57.264
27.325
13.818
1.00
65.91
P


ATOM
2599
P
PO4
P
100
57.947
26.025
14.048
1.00
66.69
P


END









Example 4
Co-Ordinates for the Dimer of the PDK1 Fragment, without Alternate Side Chains
Chain A is the molecule for which co-ordinates are given in Examples 2 and 3, and chain B is the symmetry-related molecule.























ATOM
1
CB
PRO
A
71
58.912
−7.251
8.216
1.00
67.78
A


ATOM
2
CG
PRO
A
71
59.621
−6.941
9.534
1.00
69.16
A


ATOM
3
C
PRO
A
71
59.493
−6.506
5.894
1.00
67.06
A


ATOM
4
O
PRO
A
71
59.196
−5.318
5.766
1.00
66.66
A


ATOM
5
N
PRO
A
71
60.984
−6.073
7.833
1.00
67.86
A


ATOM
6
CD
PRO
A
71
60.554
−5.762
9.207
1.00
68.24
A


ATOM
7
CA
PRO
A
71
60.040
−7.035
7.217
1.00
67.75
A


ATOM
8
N
PRO
A
72
59.356
−7.385
4.890
1.00
66.32
A


ATOM
9
CD
PRO
A
72
59.712
−8.816
4.898
1.00
67.17
A


ATOM
10
CA
PRO
A
72
58.840
−6.986
3.578
1.00
65.61
A


ATOM
11
CB
PRO
A
72
58.672
−8.321
2.858
1.00
66.47
A


ATOM
12
CG
PRO
A
72
59.796
−9.133
3.419
1.00
67.57
A


ATOM
13
C
PRO
A
72
57.527
−6.208
3.673
1.00
63.94
A


ATOM
14
O
PRO
A
72
56.710
−6.451
4.561
1.00
64.11
A


ATOM
15
N
ALA
A
73
57.341
−5.268
2.753
1.00
61.57
A


ATOM
16
CA
ALA
A
73
56.133
−4.454
2.708
1.00
58.74
A


ATOM
17
CB
ALA
A
73
56.438
−3.030
3.165
1.00
58.05
A


ATOM
18
C
ALA
A
73
55.626
−4.448
1.271
1.00
56.78
A


ATOM
19
O
ALA
A
73
56.347
−4.834
0.349
1.00
56.95
A


ATOM
20
N
PRO
A
74
54.372
−4.024
1.057
1.00
54.15
A


ATOM
21
CD
PRO
A
74
53.335
−3.610
2.018
1.00
53.31
A


ATOM
22
CA
PRO
A
74
53.856
−4.003
−0.314
1.00
52.54
A


ATOM
23
CB
PRO
A
74
52.474
−3.375
−0.148
1.00
52.86
A


ATOM
24
CG
PRO
A
74
52.067
−3.824
1.226
1.00
52.88
A


ATOM
25
C
PRO
A
74
54.772
−3.167
−1.204
1.00
50.08
A


ATOM
26
O
PRO
A
74
55.559
−2.361
−0.708
1.00
49.96
A


ATOM
27
N
ALA
A
75
54.680
−3.366
−2.514
1.00
47.58
A


ATOM
28
CA
ALA
A
75
55.503
−2.602
−3.446
1.00
44.69
A


ATOM
29
CB
ALA
A
75
55.312
−3.121
−4.870
1.00
46.14
A


ATOM
30
C
ALA
A
75
55.100
−1.134
−3.371
1.00
41.55
A


ATOM
31
O
ALA
A
75
53.947
−0.813
−3.086
1.00
41.01
A


ATOM
32
N
LYS
A
76
56.053
−0.245
−3.619
1.00
38.31
A


ATOM
33
CA
LYS
A
76
55.781
1.184
−3.588
1.00
35.72
A


ATOM
34
CB
LYS
A
76
57.053
1.957
−3.930
1.00
37.70
A


ATOM
35
CG
LYS
A
76
57.123
3.356
−3.350
1.00
40.99
A


ATOM
36
CD
LYS
A
76
57.262
3.316
−1.836
1.00
40.04
A


ATOM
37
CE
LYS
A
76
57.511
4.705
−1.277
1.00
42.08
A


ATOM
38
NZ
LYS
A
76
57.681
4.695
0.202
1.00
42.99
A


ATOM
39
C
LYS
A
76
54.708
1.467
−4.638
1.00
32.65
A


ATOM
40
O
LYS
A
76
54.814
1.005
−5.770
1.00
31.41
A


ATOM
41
N
LYS
A
77
53.668
2.207
−4.270
1.00
28.59
A


ATOM
42
CA
LYS
A
77
52.619
2.517
−5.232
1.00
25.72
A


ATOM
43
CB
LYS
A
77
51.316
2.865
−4.509
1.00
26.22
A


ATOM
44
CG
LYS
A
77
50.796
1.731
−3.631
1.00
27.15
A


ATOM
45
CD
LYS
A
77
49.487
2.089
−2.967
1.00
26.80
A


ATOM
46
CE
LYS
A
77
49.136
1.091
−1.870
1.00
27.31
A


ATOM
47
NZ
LYS
A
77
48.998
−0.296
−2.380
1.00
27.17
A


ATOM
48
C
LYS
A
77
53.053
3.668
−6.137
1.00
24.67
A


ATOM
49
O
LYS
A
77
54.010
4.377
−5.829
1.00
21.60
A


ATOM
50
N
ARG
A
78
52.351
3.838
−7.254
1.00
23.66
A


ATOM
51
CA
ARG
A
78
52.662
4.897
−8.211
1.00
26.14
A


ATOM
52
CB
ARG
A
78
53.574
4.344
−9.318
1.00
28.57
A


ATOM
53
CG
ARG
A
78
53.017
3.139
−10.050
1.00
34.78
A


ATOM
54
CD
ARG
A
78
54.092
2.465
−10.896
1.00
40.96
A


ATOM
55
NE
ARG
A
78
53.560
1.364
−11.700
1.00
48.93
A


ATOM
56
CZ
ARG
A
78
52.985
0.270
−11.203
1.00
52.58
A


ATOM
57
NH1
ARG
A
78
52.860
0.113
−9.889
1.00
54.60
A


ATOM
58
NH2
ARG
A
78
52.530
−0.672
−12.022
1.00
54.09
A


ATOM
59
C
ARG
A
78
51.382
5.488
−8.803
1.00
23.76
A


ATOM
60
O
ARG
A
78
50.311
4.888
−8.706
1.00
24.25
A


ATOM
61
N
PRO
A
79
51.475
6.676
−9.428
1.00
21.76
A


ATOM
62
CD
PRO
A
79
52.691
7.475
−9.668
1.00
20.82
A


ATOM
63
CA
PRO
A
79
50.301
7.325
−10.021
1.00
21.96
A


ATOM
64
CB
PRO
A
79
50.910
8.481
−10.816
1.00
22.27
A


ATOM
65
CG
PRO
A
79
52.124
8.831
−10.014
1.00
22.12
A


ATOM
66
C
PRO
A
79
49.446
6.413
−10.903
1.00
22.86
A


ATOM
67
O
PRO
A
79
48.213
6.461
−10.842
1.00
20.52
A


ATOM
68
N
GLU
A
80
50.103
5.586
−11.714
1.00
21.87
A


ATOM
69
CA
GLU
A
80
49.403
4.685
−12.628
1.00
22.99
A


ATOM
70
CB
GLU
A
80
50.393
3.994
−13.571
1.00
25.24
A


ATOM
71
CG
GLU
A
80
51.230
2.907
−12.925
1.00
28.75
A


ATOM
72
CD
GLU
A
80
52.157
2.224
−13.913
1.00
31.99
A


ATOM
73
OE1
GLU
A
80
53.072
2.897
−14.433
1.00
34.34
A


ATOM
74
OE2
GLU
A
80
51.969
1.015
−14.172
1.00
32.83
A


ATOM
75
C
GLU
A
80
48.556
3.631
−11.912
1.00
22.09
A


ATOM
76
O
GLU
A
80
47.692
3.013
−12.530
1.00
22.37
A


ATOM
77
N
ASP
A
81
48.804
3.413
−10.622
1.00
19.97
A


ATOM
78
CA
ASP
A
81
48.026
2.423
−9.874
1.00
19.93
A


ATOM
79
CB
ASP
A
81
48.736
2.029
−8.571
1.00
21.19
A


ATOM
80
CG
ASP
A
81
50.089
1.380
−8.807
1.00
22.46
A


ATOM
81
OD1
ASP
A
81
50.195
0.554
−9.731
1.00
24.22
A


ATOM
82
OD2
ASP
A
81
51.043
1.685
−8.058
1.00
23.33
A


ATOM
83
C
ASP
A
81
46.652
2.975
−9.518
1.00
20.85
A


ATOM
84
O
ASP
A
81
45.793
2.246
−9.015
1.00
19.96
A


ATOM
85
N
PHE
A
82
46.445
4.258
−9.804
1.00
18.91
A


ATOM
86
CA
PHE
A
82
45.200
4.934
−9.465
1.00
19.30
A


ATOM
87
CB
PHE
A
82
45.475
6.027
−8.427
1.00
18.43
A


ATOM
88
CG
PHE
A
82
46.134
5.531
−7.175
1.00
18.01
A


ATOM
89
CD1
PHE
A
82
45.371
5.136
−6.084
1.00
17.19
A


ATOM
90
CD2
PHE
A
82
47.520
5.460
−7.086
1.00
18.99
A


ATOM
91
CE1
PHE
A
82
45.977
4.676
−4.918
1.00
17.12
A


ATOM
92
CE2
PHE
A
82
48.137
5.000
−5.925
1.00
19.64
A


ATOM
93
CZ
PHE
A
82
47.361
4.607
−4.838
1.00
18.00
A


ATOM
94
C
PHE
A
82
44.476
5.596
−10.621
1.00
20.81
A


ATOM
95
O
PHE
A
82
45.066
5.933
−11.649
1.00
20.34
A


ATOM
96
N
LYS
A
83
43.182
5.792
−10.411
1.00
19.80
A


ATOM
97
CA
LYS
A
83
42.321
6.478
−11.353
1.00
21.65
A


ATOM
98
CB
LYS
A
83
41.096
5.625
−11.687
1.00
22.02
A


ATOM
99
CG
LYS
A
83
40.062
6.326
−12.550
1.00
28.93
A


ATOM
100
CD
LYS
A
83
38.974
5.355
−12.981
1.00
34.20
A


ATOM
101
CE
LYS
A
83
37.909
6.042
−13.824
1.00
38.10
A


ATOM
102
NZ
LYS
A
83
37.179
7.086
−13.043
1.00
43.33
A


ATOM
103
C
LYS
A
83
41.913
7.702
−10.541
1.00
20.74
A


ATOM
104
O
LYS
A
83
41.084
7.606
−9.635
1.00
20.98
A


ATOM
105
N
PHE
A
84
42.513
8.848
−10.835
1.00
19.99
A


ATOM
106
CA
PHE
A
84
42.188
10.049
−10.083
1.00
18.63
A


ATOM
107
CB
PHE
A
84
43.279
11.103
−10.258
1.00
18.95
A


ATOM
108
CG
PHE
A
84
44.571
10.741
−9.587
1.00
17.68
A


ATOM
109
CD1
PHE
A
84
45.498
9.926
−10.224
1.00
18.16
A


ATOM
110
CD2
PHE
A
84
44.843
11.183
−8.299
1.00
19.66
A


ATOM
111
CE1
PHE
A
84
46.676
9.556
−9.589
1.00
18.09
A


ATOM
112
CE2
PHE
A
84
46.021
10.816
−7.653
1.00
18.89
A


ATOM
113
CZ
PHE
A
84
46.936
10.002
−8.301
1.00
17.33
A


ATOM
114
C
PHE
A
84
40.834
10.617
−10.460
1.00
19.69
A


ATOM
115
O
PHE
A
84
40.391
10.489
−11.601
1.00
20.72
A


ATOM
116
N
GLY
A
85
40.178
11.233
−9.484
1.00
16.80
A


ATOM
117
CA
GLY
A
85
38.872
11.810
−9.716
1.00
17.73
A


ATOM
118
C
GLY
A
85
38.819
13.280
−9.346
1.00
18.75
A


ATOM
119
O
GLY
A
85
39.740
14.043
−9.650
1.00
18.45
A


ATOM
120
N
LYS
A
86
37.753
13.673
−8.659
1.00
16.00
A


ATOM
121
CA
LYS
A
86
37.571
15.064
−8.278
1.00
18.26
A


ATOM
122
CB
LYS
A
86
36.133
15.302
−7.812
1.00
19.00
A


ATOM
123
CG
LYS
A
86
35.793
14.660
−6.481
1.00
21.55
A


ATOM
124
CD
LYS
A
86
34.368
14.981
−6.066
1.00
26.48
A


ATOM
125
CE
LYS
A
86
33.994
14.239
−4.793
1.00
31.92
A


ATOM
126
NZ
LYS
A
86
32.568
14.457
−4.412
1.00
35.36
A


ATOM
127
C
LYS
A
86
38.523
15.571
−7.202
1.00
18.57
A


ATOM
128
O
LYS
A
86
39.045
14.807
−6.385
1.00
16.77
A


ATOM
129
N
ILE
A
87
38.737
16.881
−7.227
1.00
17.88
A


ATOM
130
CA
ILE
A
87
39.577
17.554
−6.256
1.00
18.26
A


ATOM
131
CB
ILE
A
87
39.994
18.952
−6.772
1.00
19.60
A


ATOM
132
CG2
ILE
A
87
40.593
19.786
−5.628
1.00
18.73
A


ATOM
133
CG1
ILE
A
87
40.968
18.786
−7.945
1.00
21.16
A


ATOM
134
CD1
ILE
A
87
41.412
20.087
−8.588
1.00
25.26
A


ATOM
135
C
ILE
A
87
38.731
17.709
−4.997
1.00
19.67
A


ATOM
136
O
ILE
A
87
37.628
18.249
−5.052
1.00
20.41
A


ATOM
137
N
LEU
A
88
39.240
17.229
−3.867
1.00
19.15
A


ATOM
138
CA
LEU
A
88
38.508
17.324
−2.611
1.00
20.68
A


ATOM
139
CB
LEU
A
88
38.870
16.151
−1.700
1.00
19.97
A


ATOM
140
CG
LEU
A
88
38.529
14.759
−2.237
1.00
19.24
A


ATOM
141
CD1
LEU
A
88
39.090
13.692
−1.311
1.00
21.41
A


ATOM
142
CD2
LEU
A
88
37.029
14.622
−2.359
1.00
18.84
A


ATOM
143
C
LEU
A
88
38.815
18.632
−1.901
1.00
23.11
A


ATOM
144
O
LEU
A
88
37.999
19.146
−1.139
1.00
25.10
A


ATOM
145
N
GLY
A
89
39.997
19.174
−2.149
1.00
24.09
A


ATOM
146
CA
GLY
A
89
40.367
20.418
−1.507
1.00
24.27
A


ATOM
147
C
GLY
A
89
41.658
20.954
−2.078
1.00
25.47
A


ATOM
148
O
GLY
A
89
42.445
20.202
−2.666
1.00
22.19
A


ATOM
149
N
GLU
A
90
41.870
22.254
−1.906
1.00
26.22
A


ATOM
150
CA
GLU
A
90
43.064
22.924
−2.404
1.00
29.96
A


ATOM
151
CB
GLU
A
90
42.698
23.814
−3.596
1.00
30.75
A


ATOM
152
CG
GLU
A
90
42.267
23.038
−4.831
1.00
34.32
A


ATOM
153
CD
GLU
A
90
41.711
23.930
−5.927
1.00
38.27
A


ATOM
154
OE1
GLU
A
90
40.590
24.456
−5.764
1.00
40.57
A


ATOM
155
OE2
GLU
A
90
42.398
24.110
−6.952
1.00
40.90
A


ATOM
156
C
GLU
A
90
43.711
23.768
−1.313
1.00
30.68
A


ATOM
157
O
GLU
A
90
43.049
24.574
−0.668
1.00
32.83
A


ATOM
158
N
GLY
A
91
45.006
23.566
−1.104
1.00
29.66
A


ATOM
159
CA
GLY
A
91
45.724
24.332
−0.104
1.00
29.40
A


ATOM
160
C
GLY
A
91
46.795
25.151
−0.798
1.00
29.98
A


ATOM
161
O
GLY
A
91
46.894
25.130
−2.028
1.00
28.16
A


ATOM
162
N
SER
A
92
47.605
25.870
−0.029
1.00
28.30
A


ATOM
163
CA
SER
A
92
48.653
26.681
−0.633
1.00
30.50
A


ATOM
164
CB
SER
A
92
49.165
27.717
0.370
1.00
32.43
A


ATOM
165
OG
SER
A
92
49.520
27.099
1.593
1.00
40.94
A


ATOM
166
C
SER
A
92
49.815
25.843
−1.164
1.00
29.77
A


ATOM
167
O
SER
A
92
50.456
26.221
−2.143
1.00
30.46
A


ATOM
168
N
PHE
A
93
50.087
24.703
−0.536
1.00
27.65
A


ATOM
169
CA
PHE
A
93
51.185
23.855
−0.995
1.00
26.34
A


ATOM
170
CB
PHE
A
93
52.281
23.785
0.068
1.00
27.95
A


ATOM
171
CG
PHE
A
93
52.861
25.117
0.406
1.00
31.06
A


ATOM
172
CD1
PHE
A
93
52.283
25.909
1.392
1.00
29.96
A


ATOM
173
CD2
PHE
A
93
53.949
25.613
−0.308
1.00
31.38
A


ATOM
174
CE1
PHE
A
93
52.779
27.181
1.665
1.00
32.69
A


ATOM
175
CE2
PHE
A
93
54.452
26.883
−0.044
1.00
32.63
A


ATOM
176
CZ
PHE
A
93
53.864
27.670
0.945
1.00
31.81
A


ATOM
177
C
PHE
A
93
50.759
22.445
−1.365
1.00
25.39
A


ATOM
178
O
PHE
A
93
51.601
21.559
−1.522
1.00
24.59
A


ATOM
179
N
SER
A
94
49.457
22.235
−1.519
1.00
23.63
A


ATOM
180
CA
SER
A
94
48.965
20.912
−1.860
1.00
21.43
A


ATOM
181
CB
SER
A
94
49.017
20.013
−0.628
1.00
21.42
A


ATOM
182
OG
SER
A
94
48.091
20.475
0.340
1.00
21.19
A


ATOM
183
C
SER
A
94
47.539
20.925
−2.378
1.00
19.82
A


ATOM
184
O
SER
A
94
46.795
21.882
−2.173
1.00
18.76
A


ATOM
185
N
THR
A
95
47.174
19.832
−3.038
1.00
19.38
A


ATOM
186
CA
THR
A
95
45.840
19.637
−3.580
1.00
17.98
A


ATOM
187
CB
THR
A
95
45.818
19.818
−5.110
1.00
19.25
A


ATOM
188
OG1
THR
A
95
46.196
21.162
−5.434
1.00
22.04
A


ATOM
189
CG2
THR
A
95
44.421
19.549
−5.661
1.00
17.61
A


ATOM
190
C
THR
A
95
45.455
18.201
−3.243
1.00
18.61
A


ATOM
191
O
THR
A
95
46.212
17.264
−3.524
1.00
17.10
A


ATOM
192
N
VAL
A
96
44.295
18.024
−2.623
1.00
16.53
A


ATOM
193
CA
VAL
A
96
43.845
16.685
−2.266
1.00
16.05
A


ATOM
194
CB
VAL
A
96
43.170
16.672
−0.886
1.00
16.32
A


ATOM
195
CG1
VAL
A
96
42.741
15.249
−0.532
1.00
18.02
A


ATOM
196
CG2
VAL
A
96
44.145
17.206
0.168
1.00
16.69
A


ATOM
197
C
VAL
A
96
42.875
16.207
−3.335
1.00
16.42
A


ATOM
198
O
VAL
A
96
41.906
16.892
−3.665
1.00
16.47
A


ATOM
199
N
VAL
A
97
43.157
15.033
−3.888
1.00
16.80
A


ATOM
200
CA
VAL
A
97
42.338
14.471
−4.949
1.00
16.72
A


ATOM
201
CB
VAL
A
97
43.153
14.354
−6.255
1.00
18.43
A


ATOM
202
CG1
VAL
A
97
42.249
13.927
−7.404
1.00
19.69
A


ATOM
203
CG2
VAL
A
97
43.831
15.685
−6.569
1.00
17.84
A


ATOM
204
C
VAL
A
97
41.812
13.091
−4.583
1.00
16.77
A


ATOM
205
O
VAL
A
97
42.532
12.270
−4.014
1.00
17.13
A


ATOM
206
N
LEU
A
98
40.545
12.845
−4.895
1.00
16.62
A


ATOM
207
CA
LEU
A
98
39.947
11.548
−4.624
1.00
17.04
A


ATOM
208
CB
LEU
A
98
38.424
11.633
−4.743
1.00
16.89
A


ATOM
209
CG
LEU
A
98
37.635
10.342
−4.508
1.00
19.46
A


ATOM
210
CD1
LEU
A
98
37.990
9.762
−3.146
1.00
20.07
A


ATOM
211
CD2
LEU
A
98
36.143
10.627
−4.588
1.00
17.93
A


ATOM
212
C
LEU
A
98
40.512
10.597
−5.677
1.00
17.38
A


ATOM
213
O
LEU
A
98
40.527
10.920
−6.863
1.00
18.60
A


ATOM
214
N
ALA
A
99
40.995
9.438
−5.246
1.00
17.13
A


ATOM
215
CA
ALA
A
99
41.570
8.466
−6.168
1.00
18.42
A


ATOM
216
CB
ALA
A
99
43.090
8.524
−6.105
1.00
14.76
A


ATOM
217
C
ALA
A
99
41.102
7.055
−5.848
1.00
21.40
A


ATOM
218
O
ALA
A
99
40.941
6.691
−4.679
1.00
22.52
A


ATOM
219
N
ARG
A
100
40.878
6.261
−6.888
1.00
19.77
A


ATOM
220
CA
ARG
A
100
40.459
4.884
−6.693
1.00
20.85
A


ATOM
221
CB
ARG
A
100
39.202
4.585
−7.518
1.00
24.22
A


ATOM
222
CG
ARG
A
100
38.608
3.205
−7.256
1.00
31.78
A


ATOM
223
CD
ARG
A
100
37.326
2.979
−8.048
1.00
36.24
A


ATOM
224
NE
ARG
A
100
36.213
3.818
−7.594
1.00
41.40
A


ATOM
225
CZ
ARG
A
100
35.566
3.662
−6.439
1.00
42.05
A


ATOM
226
NH1
ARG
A
100
35.912
2.696
−5.598
1.00
40.67
A


ATOM
227
NH2
ARG
A
100
34.559
4.468
−6.128
1.00
43.65
A


ATOM
228
C
ARG
A
100
41.613
3.985
−7.129
1.00
18.63
A


ATOM
229
O
ARG
A
100
42.078
4.065
−8.271
1.00
19.49
A


ATOM
230
N
GLU
A
101
42.102
3.157
−6.212
1.00
16.43
A


ATOM
231
CA
GLU
A
101
43.196
2.246
−6.533
1.00
16.11
A


ATOM
232
CB
GLU
A
101
43.774
1.637
−5.248
1.00
16.79
A


ATOM
233
CG
GLU
A
101
44.917
0.657
−5.488
1.00
16.51
A


ATOM
234
CD
GLU
A
101
45.501
0.115
−4.200
1.00
18.20
A


ATOM
235
OE1
GLU
A
101
44.733
−0.081
−3.239
1.00
18.32
A


ATOM
236
OE2
GLU
A
101
46.725
−0.132
−4.150
1.00
17.14
A


ATOM
237
C
GLU
A
101
42.625
1.152
−7.442
1.00
17.92
A


ATOM
238
O
GLU
A
101
41.681
0.462
−7.069
1.00
18.02
A


ATOM
239
N
LEU
A
102
43.198
1.002
−8.632
1.00
19.06
A


ATOM
240
CA
LEU
A
102
42.718
0.025
−9.607
1.00
20.71
A


ATOM
241
CB
LEU
A
102
43.569
0.097
−10.878
1.00
23.42
A


ATOM
242
CG
LEU
A
102
43.531
1.426
−11.642
1.00
25.30
A


ATOM
243
CD1
LEU
A
102
44.577
1.414
−12.748
1.00
27.88
A


ATOM
244
CD2
LEU
A
102
42.140
1.647
−12.214
1.00
26.79
A


ATOM
245
C
LEU
A
102
42.671
−1.418
−9.125
1.00
21.62
A


ATOM
246
O
LEU
A
102
41.668
−2.103
−9.305
1.00
21.09
A


ATOM
247
N
ALA
A
103
43.753
−1.874
−8.507
1.00
19.38
A


ATOM
248
CA
ALA
A
103
43.836
−3.249
−8.035
1.00
20.87
A


ATOM
249
CB
ALA
A
103
45.284
−3.571
−7.671
1.00
19.23
A


ATOM
250
C
ALA
A
103
42.919
−3.629
−6.872
1.00
19.92
A


ATOM
251
O
ALA
A
103
42.703
−4.815
−6.628
1.00
20.38
A


ATOM
252
N
THR
A
104
42.361
−2.643
−6.175
1.00
18.12
A


ATOM
253
CA
THR
A
104
41.517
−2.927
−5.018
1.00
17.15
A


ATOM
254
CB
THR
A
104
42.212
−2.484
−3.717
1.00
19.54
A


ATOM
255
OG1
THR
A
104
42.456
−1.070
−3.773
1.00
19.26
A


ATOM
256
CG2
THR
A
104
43.536
−3.219
−3.529
1.00
17.02
A


ATOM
257
C
THR
A
104
40.159
−2.247
−5.026
1.00
19.44
A


ATOM
258
O
THR
A
104
39.259
−2.648
−4.285
1.00
18.70
A


ATOM
259
N
SER
A
105
40.034
−1.207
−5.847
1.00
19.65
A


ATOM
260
CA
SER
A
105
38.819
−0.400
−5.967
1.00
19.37
A


ATOM
261
CB
SER
A
105
37.598
−1.304
−6.173
1.00
21.81
A


ATOM
262
OG
SER
A
105
36.431
−0.539
−6.412
1.00
23.01
A


ATOM
263
C
SER
A
105
38.644
0.447
−4.701
1.00
18.99
A


ATOM
264
O
SER
A
105
37.602
1.070
−4.488
1.00
18.66
A


ATOM
265
N
ARG
A
106
39.674
0.468
−3.861
1.00
16.84
A


ATOM
266
CA
ARG
A
106
39.655
1.267
−2.634
1.00
16.21
A


ATOM
267
CB
ARG
A
106
40.827
0.886
−1.723
1.00
16.41
A


ATOM
268
CG
ARG
A
106
40.619
−0.367
−0.906
1.00
15.49
A


ATOM
269
CD
ARG
A
106
41.887
−0.755
−0.170
1.00
17.43
A


ATOM
270
NE
ARG
A
106
41.620
−1.792
0.824
1.00
20.47
A


ATOM
271
CZ
ARG
A
106
42.548
−2.568
1.371
1.00
20.24
A


ATOM
272
NH1
ARG
A
106
43.821
−2.433
1.017
1.00
17.80
A


ATOM
273
NH2
ARG
A
106
42.198
−3.468
2.285
1.00
20.14
A


ATOM
274
C
ARG
A
106
39.785
2.746
−2.981
1.00
17.37
A


ATOM
275
O
ARG
A
106
40.514
3.103
−3.902
1.00
17.75
A


ATOM
276
N
GLU
A
107
39.085
3.599
−2.240
1.00
16.06
A


ATOM
277
CA
GLU
A
107
39.156
5.039
−2.461
1.00
20.80
A


ATOM
278
CB
GLU
A
107
37.779
5.694
−2.337
1.00
22.93
A


ATOM
279
CG
GLU
A
107
36.711
5.171
−3.269
1.00
30.87
A


ATOM
280
CD
GLU
A
107
35.431
5.975
−3.148
1.00
32.40
A


ATOM
281
OE1
GLU
A
107
35.262
6.939
−3.923
1.00
33.74
A


ATOM
282
OE2
GLU
A
107
34.608
5.654
−2.263
1.00
36.00
A


ATOM
283
C
GLU
A
107
40.053
5.678
−1.410
1.00
18.93
A


ATOM
284
O
GLU
A
107
39.891
5.427
−0.220
1.00
19.21
A


ATOM
285
N
TYR
A
108
40.988
6.507
−1.852
1.00
16.70
A


ATOM
286
CA
TYR
A
108
41.883
7.209
−0.942
1.00
15.86
A


ATOM
287
CB
TYR
A
108
43.325
6.728
−1.104
1.00
15.30
A


ATOM
288
CG
TYR
A
108
43.593
5.328
−0.612
1.00
16.33
A


ATOM
289
CD1
TYR
A
108
43.765
5.066
0.746
1.00
16.36
A


ATOM
290
CE1
TYR
A
108
44.046
3.769
1.201
1.00
18.48
A


ATOM
291
CD2
TYR
A
108
43.701
4.268
−1.511
1.00
13.25
A


ATOM
292
CE2
TYR
A
108
43.980
2.981
−1.075
1.00
17.28
A


ATOM
293
CZ
TYR
A
108
44.152
2.736
0.276
1.00
19.17
A


ATOM
294
OH
TYR
A
108
44.440
1.461
0.688
1.00
19.38
A


ATOM
295
C
TYR
A
108
41.850
8.687
−1.292
1.00
16.80
A


ATOM
296
O
TYR
A
108
41.560
9.058
−2.431
1.00
15.22
A


ATOM
297
N
ALA
A
109
42.132
9.528
−0.306
1.00
14.61
A


ATOM
298
CA
ALA
A
109
42.207
10.957
−0.539
1.00
14.30
A


ATOM
299
CB
ALA
A
109
41.671
11.726
0.661
1.00
14.78
A


ATOM
300
C
ALA
A
109
43.713
11.136
−0.667
1.00
16.79
A


ATOM
301
O
ALA
A
109
44.450
10.983
0.317
1.00
16.52
A


ATOM
302
N
ILE
A
110
44.182
11.410
−1.881
1.00
14.80
A


ATOM
303
CA
ILE
A
110
45.609
11.574
−2.093
1.00
15.80
A


ATOM
304
CB
ILE
A
110
46.065
10.863
−3.396
1.00
16.85
A


ATOM
305
CG2
ILE
A
110
47.550
11.098
−3.632
1.00
16.80
A


ATOM
306
CG1
ILE
A
110
45.774
9.358
−3.284
1.00
17.76
A


ATOM
307
CD1
ILE
A
110
46.308
8.513
−4.437
1.00
16.07
A


ATOM
308
C
ILE
A
110
46.004
13.045
−2.129
1.00
17.78
A


ATOM
309
O
ILE
A
110
45.534
13.813
−2.976
1.00
16.24
A


ATOM
310
N
LYS
A
111
46.846
13.435
−1.177
1.00
16.15
A


ATOM
311
CA
LYS
A
111
47.326
14.808
−1.100
1.00
17.20
A


ATOM
312
CB
LYS
A
111
47.700
15.176
0.344
1.00
17.41
A


ATOM
313
CG
LYS
A
111
48.350
16.547
0.464
1.00
20.71
A


ATOM
314
CD
LYS
A
111
48.585
16.971
1.910
1.00
24.25
A


ATOM
315
CE
LYS
A
111
47.288
17.381
2.598
1.00
29.46
A


ATOM
316
NZ
LYS
A
111
47.516
17.866
4.000
1.00
30.50
A


ATOM
317
C
LYS
A
111
48.551
14.890
−1.994
1.00
16.41
A


ATOM
318
O
LYS
A
111
49.509
14.137
−1.813
1.00
18.20
A


ATOM
319
N
ILE
A
112
48.509
15.798
−2.963
1.00
15.87
A


ATOM
320
CA
ILE
A
112
49.606
15.967
−3.907
1.00
17.28
A


ATOM
321
CB
ILE
A
112
49.079
15.911
−5.358
1.00
16.43
A


ATOM
322
CG2
ILE
A
112
50.235
15.998
−6.341
1.00
15.12
A


ATOM
323
CG1
ILE
A
112
48.293
14.609
−5.565
1.00
16.82
A


ATOM
324
CD1
ILE
A
112
47.580
14.511
−6.904
1.00
18.47
A


ATOM
325
C
ILE
A
112
50.307
17.301
−3.663
1.00
19.03
A


ATOM
326
O
ILE
A
112
49.669
18.350
−3.635
1.00
19.15
A


ATOM
327
N
LEU
A
113
51.622
17.245
−3.472
1.00
20.22
A


ATOM
328
CA
LEU
A
113
52.416
18.442
−3.214
1.00
22.36
A


ATOM
329
CB
LEU
A
113
52.995
18.397
−1.794
1.00
22.13
A


ATOM
330
CG
LEU
A
113
52.042
18.063
−0.646
1.00
22.46
A


ATOM
331
CD1
LEU
A
113
51.866
16.557
−0.553
1.00
23.81
A


ATOM
332
CD2
LEU
A
113
52.603
18.595
0.660
1.00
23.68
A


ATOM
333
C
LEU
A
113
53.560
18.547
−4.215
1.00
23.37
A


ATOM
334
O
LEU
A
113
54.300
17.586
−4.424
1.00
23.11
A


ATOM
335
N
GLU
A
114
53.706
19.714
−4.834
1.00
23.88
A


ATOM
336
CA
GLU
A
114
54.771
19.920
−5.806
1.00
26.00
A


ATOM
337
CB
GLU
A
114
54.435
21.111
−6.706
1.00
27.74
A


ATOM
338
CG
GLU
A
114
55.533
21.452
−7.696
1.00
35.07
A


ATOM
339
CD
GLU
A
114
55.220
22.696
−8.497
1.00
39.24
A


ATOM
340
OE1
GLU
A
114
54.808
23.703
−7.885
1.00
41.45
A


ATOM
341
OE2
GLU
A
114
55.395
22.670
−9.736
1.00
44.05
A


ATOM
342
C
GLU
A
114
56.087
20.163
−5.067
1.00
24.37
A


ATOM
343
O
GLU
A
114
56.186
21.071
−4.238
1.00
24.43
A


ATOM
344
N
LYS
A
115
57.096
19.350
−5.360
1.00
24.10
A


ATOM
345
CA
LYS
A
115
58.376
19.493
−4.678
1.00
24.93
A


ATOM
346
CB
LYS
A
115
59.339
18.373
−5.103
1.00
23.72
A


ATOM
347
CG
LYS
A
115
59.139
17.080
−4.308
1.00
23.09
A


ATOM
348
CD
LYS
A
115
60.064
15.944
−4.743
1.00
21.92
A


ATOM
349
CE
LYS
A
115
59.691
15.400
−6.117
1.00
22.42
A


ATOM
350
NZ
LYS
A
115
60.447
14.150
−6.448
1.00
19.71
A


ATOM
351
C
LYS
A
115
59.031
20.858
−4.868
1.00
26.87
A


ATOM
352
O
LYS
A
115
59.492
21.469
−3.903
1.00
26.17
A


ATOM
353
N
ARG
A
116
59.058
21.348
−6.102
1.00
28.73
A


ATOM
354
CA
ARG
A
116
59.678
22.638
−6.380
1.00
29.66
A


ATOM
355
CB
ARG
A
116
59.533
22.980
−7.868
1.00
31.29
A


ATOM
356
CG
ARG
A
116
60.047
24.361
−8.267
1.00
33.19
A


ATOM
357
CD
ARG
A
116
61.368
24.710
−7.590
1.00
35.13
A


ATOM
358
NE
ARG
A
116
62.329
23.612
−7.618
1.00
36.42
A


ATOM
359
CZ
ARG
A
116
63.510
23.648
−7.009
1.00
36.18
A


ATOM
360
NH1
ARG
A
116
63.871
24.729
−6.332
1.00
36.12
A


ATOM
361
NH2
ARG
A
116
64.324
22.602
−7.067
1.00
35.77
A


ATOM
362
C
ARG
A
116
59.097
23.761
−5.519
1.00
29.70
A


ATOM
363
O
ARG
A
116
59.843
24.515
−4.889
1.00
29.16
A


ATOM
364
N
HIS
A
117
57.773
23.862
−5.472
1.00
27.22
A


ATOM
365
CA
HIS
A
117
57.126
24.903
−4.681
1.00
26.33
A


ATOM
366
CB
HIS
A
117
55.606
24.835
−4.848
1.00
28.41
A


ATOM
367
CG
HIS
A
117
54.881
26.005
−4.258
1.00
31.82
A


ATOM
368
CD2
HIS
A
117
55.309
27.249
−3.935
1.00
33.19
A


ATOM
369
ND1
HIS
A
117
53.536
25.974
−3.961
1.00
34.30
A


ATOM
370
CE1
HIS
A
117
53.165
27.148
−3.480
1.00
34.58
A


ATOM
371
NE2
HIS
A
117
54.222
27.940
−3.455
1.00
35.18
A


ATOM
372
C
HIS
A
117
57.477
24.780
−3.202
1.00
26.22
A


ATOM
373
O
HIS
A
117
57.737
25.776
−2.534
1.00
25.67
A


ATOM
374
N
ILE
A
118
57.469
23.554
−2.689
1.00
24.94
A


ATOM
375
CA
ILE
A
118
57.792
23.315
−1.285
1.00
23.94
A


ATOM
376
CB
ILE
A
118
57.711
21.812
−0.952
1.00
23.50
A


ATOM
377
CG2
ILE
A
118
58.374
21.533
0.389
1.00
23.76
A


ATOM
378
CG1
ILE
A
118
56.246
21.362
−0.959
1.00
24.42
A


ATOM
379
CD1
ILE
A
118
56.066
19.858
−0.834
1.00
28.06
A


ATOM
380
C
ILE
A
118
59.195
23.821
−0.958
1.00
23.78
A


ATOM
381
O
ILE
A
118
59.402
24.495
0.048
1.00
23.49
A


ATOM
382
N
ILE
A
119
60.153
23.489
−1.815
1.00
23.46
A


ATOM
383
CA
ILE
A
119
61.534
23.913
−1.619
1.00
25.13
A


ATOM
384
CB
ILE
A
119
62.467
23.250
−2.664
1.00
24.25
A


ATOM
385
CG2
ILE
A
119
63.858
23.890
−2.617
1.00
22.47
A


ATOM
386
CG1
ILE
A
119
62.540
21.738
−2.395
1.00
25.05
A


ATOM
387
CD1
ILE
A
119
63.327
20.945
−3.439
1.00
24.62
A


ATOM
388
C
ILE
A
119
61.667
25.435
−1.705
1.00
25.96
A


ATOM
389
O
ILE
A
119
62.330
26.051
−0.872
1.00
24.78
A


ATOM
390
N
LYS
A
120
61.028
26.039
−2.704
1.00
27.67
A


ATOM
391
CA
LYS
A
120
61.100
27.489
−2.879
1.00
30.29
A


ATOM
392
CB
LYS
A
120
60.242
27.940
−4.060
1.00
32.34
A


ATOM
393
CG
LYS
A
120
60.674
27.407
−5.409
1.00
39.30
A


ATOM
394
CD
LYS
A
120
59.765
27.950
−6.512
1.00
45.19
A


ATOM
395
CE
LYS
A
120
58.294
27.636
−6.218
1.00
46.48
A


ATOM
396
NZ
LYS
A
120
57.363
28.155
−7.252
1.00
46.49
A


ATOM
397
C
LYS
A
120
60.647
28.247
−1.638
1.00
30.89
A


ATOM
398
O
LYS
A
120
61.303
29.198
−1.217
1.00
32.48
A


ATOM
399
N
GLU
A
121
59.527
27.825
−1.055
1.00
29.82
A


ATOM
400
CA
GLU
A
121
58.986
28.488
0.128
1.00
30.33
A


ATOM
401
CB
GLU
A
121
57.455
28.416
0.117
1.00
33.04
A


ATOM
402
CG
GLU
A
121
56.794
29.021
−1.120
1.00
36.45
A


ATOM
403
CD
GLU
A
121
57.221
30.456
−1.373
1.00
39.88
A


ATOM
404
OE1
GLU
A
121
57.200
31.264
−0.420
1.00
40.53
A


ATOM
405
OE2
GLU
A
121
57.573
30.778
−2.529
1.00
43.24
A


ATOM
406
C
GLU
A
121
59.511
27.930
1.451
1.00
30.37
A


ATOM
407
O
GLU
A
121
58.946
28.204
2.513
1.00
31.24
A


ATOM
408
N
ASN
A
122
60.588
27.151
1.390
1.00
29.03
A


ATOM
409
CA
ASN
A
122
61.183
26.573
2.594
1.00
28.46
A


ATOM
410
CB
ASN
A
122
61.836
27.673
3.436
1.00
31.28
A


ATOM
411
CG
ASN
A
122
62.945
28.395
2.698
1.00
34.12
A


ATOM
412
OD1
ASN
A
122
62.697
29.143
1.754
1.00
35.57
A


ATOM
413
ND2
ASN
A
122
64.181
28.169
3.127
1.00
35.73
A


ATOM
414
C
ASN
A
122
60.157
25.835
3.456
1.00
26.89
A


ATOM
415
O
ASN
A
122
60.085
26.055
4.663
1.00
27.23
A


ATOM
416
N
LYS
A
123
59.375
24.955
2.842
1.00
23.99
A


ATOM
417
CA
LYS
A
123
58.358
24.210
3.574
1.00
22.43
A


ATOM
418
CB
LYS
A
123
57.031
24.248
2.810
1.00
21.97
A


ATOM
419
CG
LYS
A
123
56.475
25.645
2.599
1.00
25.68
A


ATOM
420
CD
LYS
A
123
56.253
26.354
3.927
1.00
27.54
A


ATOM
421
CE
LYS
A
123
55.822
27.796
3.716
1.00
31.30
A


ATOM
422
NZ
LYS
A
123
55.756
28.540
5.004
1.00
33.21
A


ATOM
423
C
LYS
A
123
58.748
22.759
3.821
1.00
22.20
A


ATOM
424
O
LYS
A
123
57.924
21.960
4.264
1.00
22.50
A


ATOM
425
N
VAL
A
124
59.997
22.412
3.535
1.00
20.59
A


ATOM
426
CA
VAL
A
124
60.439
21.039
3.730
1.00
20.25
A


ATOM
427
CB
VAL
A
124
61.922
20.850
3.328
1.00
19.43
A


ATOM
428
CG1
VAL
A
124
62.346
19.407
3.573
1.00
18.69
A


ATOM
429
CG2
VAL
A
124
62.104
21.195
1.853
1.00
18.21
A


ATOM
430
C
VAL
A
124
60.236
20.561
5.163
1.00
19.53
A


ATOM
431
O
VAL
A
124
59.841
19.418
5.385
1.00
20.02
A


ATOM
432
N
PRO
A
125
60.513
21.422
6.159
1.00
20.01
A


ATOM
433
CD
PRO
A
125
61.178
22.738
6.118
1.00
18.69
A


ATOM
434
CA
PRO
A
125
60.318
20.979
7.544
1.00
19.88
A


ATOM
435
CB
PRO
A
125
60.793
22.180
8.363
1.00
19.95
A


ATOM
436
CG
PRO
A
125
61.839
22.805
7.479
1.00
18.85
A


ATOM
437
C
PRO
A
125
58.848
20.642
7.824
1.00
19.76
A


ATOM
438
O
PRO
A
125
58.544
19.700
8.550
1.00
16.99
A


ATOM
439
N
TYR
A
126
57.947
21.418
7.235
1.00
18.98
A


ATOM
440
CA
TYR
A
126
56.516
21.220
7.435
1.00
21.97
A


ATOM
441
CB
TYR
A
126
55.752
22.448
6.933
1.00
25.17
A


ATOM
442
CG
TYR
A
126
56.040
23.690
7.748
1.00
30.98
A


ATOM
443
CD1
TYR
A
126
55.438
23.886
8.991
1.00
33.95
A


ATOM
444
CE1
TYR
A
126
55.721
25.015
9.763
1.00
36.60
A


ATOM
445
CD2
TYR
A
126
56.938
24.657
7.292
1.00
35.43
A


ATOM
446
CE2
TYR
A
126
57.231
25.792
8.058
1.00
37.20
A


ATOM
447 
CZ
TYR
A
126
56.618
25.962
9.291
1.00
37.40
A


ATOM
448
OH
TYR
A
126
56.903
27.073
10.052
1.00
40.85
A


ATOM
449
C
TYR
A
126
55.990
19.956
6.762
1.00
21.35
A


ATOM
450
O
TYR
A
126
55.265
19.175
7.383
1.00
20.49
A


ATOM
451
N
VAL
A
127
56.354
19.746
5.501
1.00
18.16
A


ATOM
452
CA
VAL
A
127
55.892
18.562
4.790
1.00
17.58
A


ATOM
453
CB
VAL
A
127
56.308
18.596
3.308
1.00
17.45
A


ATOM
454
CG1
VAL
A
127
55.786
17.350
2.600
1.00
17.97
A


ATOM
455
CG2
VAL
A
127
55.751
19.850
2.641
1.00
14.90
A


ATOM
456
C
VAL
A
127
56.459
17.306
5.448
1.00
18.39
A


ATOM
457
O
VAL
A
127
55.769
16.298
5.583
1.00
18.14
A


ATOM
458
N
THR
A
128
57.716
17.381
5.869
1.00
17.50
A


ATOM
459
CA
THR
A
128
58.375
16.260
6.530
1.00
18.54
A


ATOM
460
CB
THR
A
128
59.861
16.586
6.805
1.00
18.01
A


ATOM
461
OG1
THR
A
128
60.537
16.804
5.559
1.00
21.14
A


ATOM
462
CG2
THR
A
128
60.536
15.446 
7.545
1.00
17.95
A


ATOM
463
C
THR
A
128
57.676
15.941
7.856
1.00
19.49
A


ATOM
464
O
THR
A
128
57.438
14.776
8.179
1.00
18.76
A


ATOM
465
N
ARG
A
129
57.345
16.981
8.619
1.00
19.60
A


ATOM
466
CA
ARG
A
129
56.673
16.804
9.904
1.00
20.12
A


ATOM
467
CB
ARG
A
129
56.534
18.144
10.621
1.00
21.33
A


ATOM
468
CG
ARG
A
129
55.948
18.029
12.023
1.00
28.02
A


ATOM
469
CD
ARG
A
129
55.721
19.404
12.597
1.00
31.25
A


ATOM
470
NE
ARG
A
129
56.940
20.205
12.560
1.00
37.78
A


ATOM
471
CZ
ARG
A
129
56.962
21.524
12.391
1.00
40.10
A


ATOM
472
NH1
ARG
A
129
55.828
22.197
12.239
1.00
40.03
A


ATOM
473
NH2
ARG
A
129
58.119
22.170
12.374
1.00
44.58
A


ATOM
474
C
ARG
A
129
55.288
16.186
9.729
1.00
20.08
A


ATOM
475
O
ARG
A
129
54.891
15.305
10.496
1.00
20.40
A


ATOM
476
N
GLU
A
130
54.553
16.654
8.724
1.00
18.79
A


ATOM
477
CA
GLU
A
130
53.222
16.125
8.454
1.00
20.10
A


ATOM
478
CB
GLU
A
130
52.638
16.749
7.183
1.00
19.92
A


ATOM
479
CG
GLU
A
130
51.350
16.087
6.708
1.00
27.85
A


ATOM
480
CD
GLU
A
130
50.581
16.933
5.707
1.00
29.72
A


ATOM
481
OE1
GLU
A
130
51.216
17.528
4.814
1.00
33.46
A


ATOM
482
OE2
GLU
A
130
49.339
16.996
5.807
1.00
30.74
A


ATOM
483
C
GLU
A
130
53.301
14.615
8.295
1.00
19.81
A


ATOM
484
O
GLU
A
130
52.553
13.875
8.935
1.00
18.37
A


ATOM
485
N
ARG
A
131
54.219
14.162
7.447
1.00
20.41
A


ATOM
486
CA
ARG
A
131
54.397
12.735
7.202
1.00
22.45
A


ATOM
487
CB
ARG
A
131
55.442
12.511
6.098
1.00
25.16
A


ATOM
488
CG
ARG
A
131
55.742
11.043
5.840
1.00
28.75
A


ATOM
489
CD
ARG
A
131
56.736
10.837
4.708
1.00
33.75
A


ATOM
490
NE
ARG
A
131
57.020
9.415
4.520
1.00
40.07
A


ATOM
491
CZ
ARG
A
131
57.756
8.915
3.532
1.00
43.07
A


ATOM
492
NH1
ARG
A
131
58.293
9.721
2.625
1.00
44.91
A


ATOM
493
NH2
ARG
A
131
57.955
7.606
3.449
1.00
44.45
A


ATOM
494
C
ARG
A
131
54.820
11.982
8.466
1.00
23.24
A


ATOM
495
O
ARG
A
131
54.241
10.948
8.804
1.00
23.86
A


ATOM
496
N
ASP
A
132
55.831
12.497
9.160
1.00
21.99
A


ATOM
497
CA
ASP
A
132
56.318
11.850
10.370
1.00
22.04
A


ATOM
498
CB
ASP
A
132
57.570
12.564
10.888
1.00
23.72
A


ATOM
499
CG
ASP
A
132
58.750
12.442
9.932
1.00
27.77
A


ATOM
500
OD1
ASP
A
132
58.681
11.620
8.989
1.00
27.34
A


ATOM
501
OD2
ASP
A
132
59.753
13.163
10.128
1.00
28.70
A


ATOM
502
C
ASP
A
132
55.258
11.772
11.474
1.00
21.69
A


ATOM
503
O
ASP
A
132
55.077
10.723
12.092
1.00
22.75
A


ATOM
504
N
VAL
A
133
54.551
12.868
11.725
1.00
19.54
A


ATOM
505
CA
VAL
A
133
53.525
12.843
12.759
1.00
18.52
A


ATOM
506
CB
VAL
A
133
52.908
14.244
12.990
1.00
19.26
A


ATOM
507
CG1
VAL
A
133
51.708
14.135
13.918
1.00
18.79
A


ATOM
508
CG2
VAL
A
133
53.953
15.180
13.604
1.00
18.80
A


ATOM
509
C
VAL
A
133
52.419
11.854
12.398
1.00
19.46
A


ATOM
510
O
VAL
A
133
52.073
10.991
13.200
1.00
19.94
A


ATOM
511
N
MET
A
134
51.878
11.957
11.187
1.00
19.15
A


ATOM
512
CA
MET
A
134
50.807
11.052
10.792
1.00
21.25
A


ATOM
513
CB
MET
A
134
50.309
11.381
9.383
1.00
17.34
A


ATOM
514
CG
MET
A
134
49.615
12.730
9.302
1.00
20.00
A


ATOM
515
SD
MET
A
134
48.643
12.952
7.798
1.00
24.21
A


ATOM
516
CE
MET
A
134
47.033
12.434
8.400
1.00
23.20
A


ATOM
517
C
MET
A
134
51.203
9.582
10.881
1.00
22.43
A


ATOM
518
O
MET
A
134
50.384 
8.741
11.249
1.00
23.82
A


ATOM
519
N
SER
A
135
52.454
9.273
10.556
1.00
23.09
A


ATOM
520
CA
SER
A
135
52.939
7.895
10.615
1.00
26.13
A


ATOM
521
CB
SER
A
135
54.356
7.798
10.039
1.00
26.17
A


ATOM
522
OG 
SER
A
135
54.383
8.177
8.673
1.00
31.91
A


ATOM
523
C
SER
A
135
52.957
7.358
12.045
1.00
26.58
A


ATOM
524
O
SER
A
135
52.926
6.148
12.261
1.00
26.42
A


ATOM
525
N
ARG
A
136
53.014
8.261
13.018
1.00
25.65
A


ATOM
526
CA
ARG
A
136
53.056
7.870
14.425
1.00
27.47
A


ATOM
527
CB
ARG
A
136
53.823
8.914
15.238
1.00
27.97
A


ATOM
528
CG
ARG
A
136
55.283
9.082
14.857
1.00
32.00
A


ATOM
529
CD
ARG
A
136
55.904
10.218
15.664
1.00
33.03
A


ATOM
530
NE
ARG
A
136
55.602
10.073
17.084
1.00
36.11
A


ATOM
531
CZ 
ARG
A
136
55.867
10.990
18.007
1.00
39.74
A


ATOM
532
NH1
ARG
A
136
56.449
12.132
17.661
1.00
40.55
A


ATOM
533
NH2
ARG
A
136
55.540
10.769
19.276
1.00
36.72
A


ATOM
534
C
ARG
A
136
51.667
7.709
15.036
1.00
26.38
A


ATOM
535
O
ARG
A
136
51.516
7.121
16.106
1.00
27.06
A


ATOM
536
N
LEU
A
137
50.655
8.235
14.360
1.00
24.77
A


ATOM
537
CA
LEU
A
137
49.294
8.162
14.870
1.00
24.70
A


ATOM
538
CB
LEU
A
137
48.483
9.363
14.371
1.00
24.52
A


ATOM
539
CG
LEU
A
137
49.050
10.760
14.662
1.00
26.67
A


ATOM
540
CD1
LEU
A
137
48.075
11.813
14.141
1.00
27.25
A


ATOM
541
CD2
LEU
A
137
49.279
10.945
16.155
1.00
27.09
A


ATOM
542
C
LEU
A
137
48.592
6.868
14.473
1.00
25.20
A


ATOM
543
O
LEU
A
137
48.619
6.469
13.309
1.00
25.99
A


ATOM
544
N
ASP
A
138
47.971
6.218
15.451
1.00
21.89
A


ATOM
545
CA
ASP
A
138
47.239
4.977
15.219
1.00
21.35
A


ATOM
546
CB
ASP
A
138
48.124
3.761
15.523
1.00
22.14
A


ATOM
547
CG
ASP
A
138
47.432
2.448
15.201
1.00
24.90
A


ATOM
548 
OD1
ASP
A
138
46.631
2.423
14.241
1.00
24.78
A


ATOM
549
OD2
ASP
A
138
47.691
1.443
15.897
1.00
25.39
A


ATOM
550
C
ASP
A
138
46.031
4.991
16.138
1.00
20.47
A


ATOM
551
O
ASP
A
138
45.967
4.248
17.118
1.00
19.06
A


ATOM
552
N
HIS
A
139
45.075
5.852
15.810
1.00
18.27
A


ATOM
553
CA
HIS
A
139
43.869
6.016
16.606
1.00
18.21
A


ATOM
554
CB
HIS
A
139
44.096
7.157
17.612
1.00
15.84
A


ATOM
555
CG
HIS
A
139
42.985 
7.332
18.600
1.00
15.24
A


ATOM
556
CD2
HIS
A
139
42.884
6.964
19.900
1.00
13.97
A


ATOM
557
ND1
HIS
A
139
41.791 
7.943
18.280
1.00
14.74
A


ATOM
558
CE1
HIS
A
139
41.002
7.944
19.341
1.00
14.19
A


ATOM
559
NE2
HIS
A
139
41.641
7.356
20.336
1.00
14.15
A


ATOM
560
C
HIS
A
139
42.715
6.330
15.654
1.00
18.50
A


ATOM
561
O
HIS
A
139
42.879 
7.080
14.693
1.00
20.80
A


ATOM
562
N
PRO
A
140
41.527
5.767
15.913
1.00
18.32
A


ATOM
563
CD
PRO
A
140
41.143
4.984
17.100
1.00
16.71
A


ATOM
564
CA
PRO
A
140
40.367
6.001
15.048
1.00
17.43
A


ATOM
565
CB
PRO
A
140
39.273
5.157
15.704
1.00
16.64
A


ATOM
566
CG
PRO
A
140
39.643
5.204
17.152
1.00
18.43
A


ATOM
567
C
PRO
A
140
39.914
7.441
14.803
1.00
18.77
A


ATOM
568
O 
PRO
A
140
39.207
7.695
13.831
1.00
19.88
A


ATOM
569
N
PHE
A
141
40.301
8.381
15.664
1.00
17.14
A


ATOM
570
CA
PHE
A
141
39.874
9.767
15.477
1.00
16.42
A


ATOM
571
CB
PHE
A
141
39.568
10.422
16.836
1.00
14.60
A


ATOM
572
CG
PHE
A
141
38.386
9.817
17.556
1.00
15.26
A


ATOM
573
CD1
PHE
A
141
37.335
9.234
16.842
1.00
14.78
A


ATOM
574
CD2 
PHE
A
141
38.297
9.880
18.942
1.00
13.70
A


ATOM
575
CE1 
PHE
A
141
36.215
8.727
17.502
1.00
16.94
A


ATOM
576
CE2 
PHE
A
141
37.178
9.375
19.615
1.00
15.75
A


ATOM
577
CZ
PHE
A
141
36.135
8.799
18.893
1.00
16.89
A


ATOM
578
C
PHE
A
141
40.857
10.641
14.694
1.00
16.15
A


ATOM
579
O
PHE
A
141
40.799
11.871
14.761
1.00
17.35
A


ATOM
580
N
PHE
A
142
41.748
10.011
13.941
1.00
15.88
A


ATOM
581
CA
PHE
A
142
42.727
10.756
13.154
1.00
17.89
A


ATOM
582
CB
PHE
A
142
44.115
10.645
13.793
1.00
17.57
A


ATOM
583
CG
PHE
A
142
44.240
11.371
15.103
1.00
18.74
A


ATOM
584
CD1
PHE
A
142
44.559
12.726
15.135
1.00
17.77
A


ATOM
585
CD2
PHE
A
142
43.997
10.711
16.304
1.00
18.74
A


ATOM
586
CE1
PHE
A
142
44.632
13.417
16.347
1.00
15.77
A


ATOM
587
CE2
PHE
A
142
44.065
11.393
17.522
1.00
17.56
A


ATOM
588
CZ
PHE
A
142
44.383
12.747
17.542
1.00
17.14
A


ATOM
589
C
PHE
A
142
42.793
10.231
11.729
1.00
19.12
A


ATOM
590
O
PHE
A
142
42.659
9.030
11.504
1.00
20.01
A


ATOM
591
N
VAL
A
143
42.978
11.135
10.769
1.00
18.72
A


ATOM
592
CA
VAL
A
143
43.102
10.735
9.371
1.00
18.52
A


ATOM
593
CB
VAL
A
143
43.294
11.961
8.440
1.00
20.66
A


ATOM
594
CG1
VAL
A
143
43.843
11.521
7.080
1.00
21.29
A


ATOM
595
CG2
VAL
A
143
41.958
12.673
8.252
1.00
22.97
A


ATOM
596
C
VAL
A
143
44.342
9.865
9.330
1.00
18.68
A


ATOM
597
O
VAL
A
143
45.355
10.199
9.943
1.00
18.42
A


ATOM
598
N
LYS
A
144
44.259
8.745
8.623
1.00
18.30
A


ATOM
599
CA
LYS
A
144
45.384
7.824
8.535
1.00
18.78
A


ATOM
600
CB
LYS
A
144
44.889
6.373
8.608
1.00
22.27
A


ATOM
601
CG
LYS
A
144
46.017
5.340
8.557
1.00
29.72
A


ATOM
602
CD
LYS
A
144
45.491
3.912
8.674
1.00
34.16
A


ATOM
603
CE
LYS
A
144
46.631
2.896
8.577
1.00
37.67
A


ATOM
604
NZ
LYS
A
144
46.138
1.484
8.629
1.00
39.02
A


ATOM
605
C
LYS
A
144
46.192
8.002
7.261
1.00
18.53
A


ATOM
606
O
LYS
A
144
45.643
8.314
6.200
1.00
18.18
A


ATOM
607
N
LEU
A
145
47.502
7.816
7.385
1.00
16.79
A


ATOM
608
CA
LEU
A
145
48.411
7.900
6.251
1.00
17.45
A


ATOM
609
CB
LEU
A
145
49.686
8.653
6.641
1.00
18.82
A


ATOM
610
CG
LEU
A
145
50.734
8.902
5.549
1.00
20.23
A


ATOM
611
CD1
LEU
A
145
51.836
9.799
6.093
1.00
18.83
A


ATOM
612
CD2
LEU
A
145
51.317
7.581
5.069
1.00
19.79
A


ATOM
613
C
LEU
A
145
48.739
6.450
5.907
1.00
19.19
A


ATOM
614
O
LEU
A
145
49.451
5.772
6.659
1.00
17.36
A


ATOM
615
N
TYR
A
146
48.215
5.972
4.782
1.00
17.28
A


ATOM
616
CA
TYR
A
146
48.444
4.593
4.358
1.00
17.57
A


ATOM
617
CB
TYR
A
146
47.288
4.098
3.486
1.00
17.74
A


ATOM
618
CG
TYR
A
146
45.981
3.926
4.214
1.00
17.50
A


ATOM
619
CD1
TYR
A
146
45.099
4.995
4.377
1.00
16.50
A


ATOM
620
CE1
TYR
A
146
43.881
4.827
5.039
1.00
17.10
A


ATOM
621
CD2
TYR
A
146
45.620
2.686
4.735
1.00
18.28
A


ATOM
622
CE2
TYR
A
146
44.411
2.506
5.399
1.00
19.84
A


ATOM
623
CZ
TYR
A
146
43.547
3.576
5.544
1.00
17.53
A


ATOM
624
OH
TYR
A
146
42.342
3.376
6.169
1.00
20.67
A


ATOM
625
C
TYR
A
146
49.735
4.376
3.582
1.00
18.72
A


ATOM
626
O
TYR
A
146
50.382
3.338
3.715
1.00
19.51
A


ATOM
627
N
PHE
A
147
50.110
5.350
2.765
1.00
18.09
A


ATOM
628
CA
PHE
A
147
51.307
5.203
1.952
1.00
17.20
A


ATOM
629
CB
PHE
A
147
51.007
4.258
0.783
1.00
16.77
A


ATOM
630
CG
PHE
A
147
49.835
4.699
−0.070
1.00
17.75
A


ATOM
631
CD1
PHE
A
147
49.967
5.752
−0.975
1.00
16.58
A


ATOM
632
CD2
PHE
A
147
48.595
4.075
0.053
1.00
18.07
A


ATOM
633
CE1
PHE
A
147
48.886
6.178
−1.742
1.00
19.62
A


ATOM
634
CE2
PHE
A
147
47.503
4.492
−0.710
1.00
18.56
A


ATOM
635
CZ
PHE
A
147
47.647
5.546
−1.610
1.00
19.27
A


ATOM
636
C
PHE
A
147
51.768
6.533
1.395
1.00
17.13
A


ATOM
637
O
PHE
A
147
51.045
7.528
1.452
1.00
14.43
A


ATOM
638
N
THR
A
148
52.981
6.534
0.854
1.00
17.12
A


ATOM
639
CA
THR
A
148
53.541
7.718
0.232
1.00
17.96
A


ATOM
640
CB
THR
A
148
54.449
8.531
1.197
1.00
21.51
A


ATOM
641
OG1
THR
A
148
55.605
7.760
1.537
1.00
18.83
A


ATOM
642
CG2
THR
A
148
53.700
8.897
2.472
1.00
19.60
A


ATOM
643
C
THR
A
148
54.386
7.262
−0.946
1.00
20.31
A


ATOM
644
O
THR
A
148
54.860
6.124
−0.991
1.00
18.94
A


ATOM
645
N
PHE
A
149
54.543
8.149
−1.916
1.00
19.16
A


ATOM
646
CA
PHE
A
149
55.368
7.877
−3.073
1.00
18.01
A


ATOM
647
CB
PHE
A
149
54.748
6.801
−3.989
1.00
17.23
A


ATOM
648
CG
PHE
A
149
53.389
7.144
−4.544
1.00
16.88
A


ATOM
649
CD1
PHE
A
149
53.262
7.888
−5.712
1.00
18.58
A


ATOM
650
CD2
PHE
A
149
52.235
6.668
−3.927
1.00
17.31
A


ATOM
651
CE1
PHE
A
149
52.007
8.149
−6.267
1.00
19.26
A


ATOM
652
CE2
PHE
A
149
50.972
6.923
−4.470
1.00
19.17
A


ATOM
653
CZ
PHE
A
149
50.858
7.663
−5.642
1.00
19.60
A


ATOM
654
C
PHE
A
149
55.542
9.205
−3.774
1.00
20.85
A


ATOM
655
O
PHE
A
149
54.934
10.200
−3.376
1.00
19.76
A


ATOM
656
N
GLN
A
150
56.398
9.241
−4.782
1.00
19.79
A


ATOM
657
CA
GLN
A
150
56.636
10.481
−5.497
1.00
24.03
A


ATOM
658
CB
GLN
A
150
57.659
11.347
−4.739
1.00
24.45
A


ATOM
659
CG
GLN
A
150
58.986
10.645
−4.414
1.00
26.28
A


ATOM
660
CD
GLN
A
150
59.988
11.558
−3.692
1.00
29.02
A


ATOM
661
OE1
GLN
A
150
60.693
12.353
−4.321
1.00
27.05
A


ATOM
662
NE2
GLN
A
150
60.042
11.449
−2.365
1.00
26.47
A


ATOM
663
C
GLN
A
150
57.160
10.203
−6.885
1.00
23.88
A


ATOM
664
O
GLN
A
150
57.673
9.118
−7.158
1.00
24.79
A


ATOM
665
N
ASP
A
151
56.987
11.171
−7.774
1.00
25.88
A


ATOM
666
CA
ASP
A
151
57.527
11.047
−9.117
1.00
26.49
A


ATOM
667
CB
ASP
A
151
56.437
11.126
−10.199
1.00
24.54
A


ATOM
668
CG
ASP
A
151
55.544
12.336
−10.064
1.00
24.95
A


ATOM
669
OD1
ASP
A
151
56.005
13.379
−9.561
1.00
22.44
A


ATOM
670
OD2
ASP
A
151
54.369
12.242
−10.490
1.00
25.72
A


ATOM
671
C
ASP
A
151
58.515
12.203
−9.220
1.00
28.63
A


ATOM
672
O
ASP
A
151
58.890
12.780
−8.194
1.00
27.83
A


ATOM
673
N
ASP
A
152
58.934
12.560
−10.426
1.00
29.21
A


ATOM
674
CA
ASP
A
152
59.907
13.636
−10.562
1.00
31.88
A


ATOM
675
CB
ASP
A
152
60.325
13.792
−12.026
1.00
33.94
A


ATOM
676
CG
ASP
A
152
61.033
12.564
−12.557
1.00
38.88
A


ATOM
677
OD1
ASP
A
152
61.817
11.959
−11.791
1.00
39.67
A


ATOM
678
OD2
ASP
A
152
60.817
12.211
−13.738
1.00
41.57
A


ATOM
679
C
ASP
A
152
59.487
14.994
−10.013
1.00
30.90
A


ATOM
680
O
ASP
A
152
60.316
15.735
−9.482
1.00
31.69
A


ATOM
681
N
GLU
A
153
58.207
15.322
−10.107
1.00
29.44
A


ATOM
682
CA
GLU
A
153
57.767
16.632
−9.646
1.00
28.69
A


ATOM
683
CB
GLU
A
153
56.984
17.327
−10.766
1.00
32.90
A


ATOM
684
CG
GLU
A
153
57.451
16.987
−12.183
1.00
40.57
A


ATOM
685 
CD
GLU
A
153
56.920
15.643
−12.675
1.00
45.78
A


ATOM
686
OE1
GLU
A
153
55.682
15.482
−12.760
1.00
48.91
A


ATOM
687
OE2
GLU
A
153
57.736
14.747
−12.979
1.00
48.95
A


ATOM
688
C
GLU
A
153
56.929
16.683
−8.372
1.00
26.43
A


ATOM
689
O
GLU
A
153
56.947
17.688
−7.660
1.00
25.08
A


ATOM
690
N
LYS
A
154
56.205
15.610
−8.069
1.00
22.39
A


ATOM
691
CA
LYS
A
154
55.318
15.631
−6.912
1.00
21.43
A


ATOM
692
CB
LYS
A
154
53.861
15.628
−7.398
1.00
20.33
A


ATOM
693
CG
LYS
A
154
53.505
16.716
−8.403
1.00
21.92
A


ATOM
694
CD
LYS
A
154
52.211
16.375
−9.146
1.00
19.70
A


ATOM
695
CE
LYS
A
154
51.775
17.503
−10.077
1.00
20.04
A


ATOM
696
NZ
LYS
A
154
50.631
17.094
−10.951
1.00
19.97
A


ATOM
697
C
LYS
A
154
55.458
14.522
−5.881
1.00
20.43
A


ATOM
698
O
LYS
A
154
55.949
13.426
−6.173
1.00
21.13
A


ATOM
699
N
LEU
A
155
54.985
14.832
−4.676
1.00
19.69
A


ATOM
700
CA
LEU
A
155
54.950
13.900
−3.553
1.00
19.10
A


ATOM
701
CB
LEU
A
155
55.362
14.588
−2.252
1.00
19.65
A


ATOM
702
CG
LEU
A
155
56.740
15.234
−2.129
1.00
21.20
A


ATOM
703
CD1
LEU
A
155
56.848
15.918
−0.770
1.00
23.42
A


ATOM
704
CD2
LEU
A
155
57.816
14.174
−2.277
1.00
23.08
A


ATOM
705
C
LEU
A
155
53.478
13.507
−3.427
1.00
18.87
A


ATOM
706
O
LEU
A
155
52.600
14.348
−3.620
1.00
18.61
A


ATOM
707
N
TYR
A
156
53.209
12.249
−3.091
1.00
15.02
A


ATOM
708
CA
TYR
A
156
51.834
11.783
−2.934
1.00
16.29
A


ATOM
709
CB
TYR
A
156
51.470
10.769
−4.029
1.00
14.20
A


ATOM
710
CG
TYR
A
156
51.603
11.273
−5.449
1.00
17.29
A


ATOM
711
CD1
TYR
A
156
52.857
11.429
−6.045
1.00
16.46
A


ATOM
712
CE1
TYR
A
156
52.978
11.884
−7.360
1.00
18.68
A


ATOM
713
CD2
TYR
A
156
50.474
11.588
−6.202
1.00
16.43
A


ATOM
714
CE2
TYR
A
156
50.583
12.048
−7.512
1.00
16.31
A


ATOM
715
CZ
TYR
A
156
51.835
12.192
−8.083
1.00
18.17
A


ATOM
716
OH
TYR
A
156
51.941
12.651
−9.371
1.00
17.47
A


ATOM
717
C
TYR
A
156
51.657
11.108
−1.572
1.00
16.32
A


ATOM
718
O
TYR
A
156
52.412
10.197
−1.235
1.00
16.27
A


ATOM
719
N
PHE
A
157
50.678
11.568
−0.792
1.00
15.47
A


ATOM
720
CA
PHE
A
157
50.385
10.966
0.508
1.00
16.66
A


ATOM
721
CB
PHE
A
157
50.324
12.014
1.629
1.00
16.91
A


ATOM
722
CG
PHE
A
157
51.631
12.708
1.907
1.00
18.96
A


ATOM
723
CD1
PHE
A
157
52.821
12.261
1.340
1.00
20.31
A


ATOM
724
CD2
PHE
A
157
51.664
13.829
2.732
1.00
21.12
A


ATOM
725
CE1
PHE
A
157
54.025
12.926
1.585
1.00
22.08
A


ATOM
726
CE2
PHE
A
157
52.865
14.500
2.982
1.00
22.18
A


ATOM
727
CZ
PHE
A
157
54.045
14.045
2.405
1.00
21.27
A


ATOM
728
C
PHE
A
157
49.016
10.308
0.404
1.00
16.52
A


ATOM
729
O
PHE
A
157
48.029
10.979
0.110
1.00
17.32
A


ATOM
730
N
GLY
A
158
48.953
9.002
0.644
1.00
15.97
A


ATOM
731
CA
GLY
A
158
47.684
8.299
0.572
1.00
16.13
A


ATOM
732
C
GLY
A
158
47.000
8.383
1.920
1.00
14.94
A


ATOM
733
O
GLY
A
158
47.445
7.756
2.879
1.00
16.28
A


ATOM
734
N
LEU
A
159
45.915
9.145
1.989
1.00
13.50
A


ATOM
735
CA
LEU
A
159
45.191
9.340
3.241
1.00
15.20
A


ATOM
736
CB
LEU
A
159
45.031
10.835
3.517
1.00
14.20
A


ATOM
737
CG
LEU
A
159
46.270
11.726
3.385
1.00
19.00
A


ATOM
738
CD1
LEU
A
159
45.847
13.188
3.477
1.00
17.12
A


ATOM
739
CD2
LEU
A
159
47.275
11.390
4.471
1.00
14.71
A


ATOM
740
C
LEU
A
159
43.809
8.716
3.232
1.00
15.53
A


ATOM
741
O
LEU
A
159
43.232
8.472
2.177
1.00
16.05
A


ATOM
742
N
SER
A
160
43.268
8.469
4.418
1.00
15.86
A


ATOM
743
CA
SER
A
160
41.932
7.917
4.498
1.00
19.01
A


ATOM
744
CB
SER
A
160
41.566
7.582
5.949
1.00
22.90
A


ATOM
745
OG
SER
A
160
41.901
8.629
6.833
1.00
24.18
A


ATOM
746
C
SER
A
160
40.987
8.968
3.924
1.00
20.43
A


ATOM
747
O
SER
A
160
41.213
10.173
4.062
1.00
19.96
A


ATOM
748
N
TYR
A
161
39.945
8.508
3.250
1.00
19.20
A


ATOM
749
CA
TYR
A
161
38.975
9.406
2.644
1.00
20.37
A


ATOM
750
CB
TYR
A
161
38.471
8.785
1.332
1.00
20.00
A


ATOM
751
CG
TYR
A
161
37.314
9.502
0.666
1.00
20.72
A


ATOM
752
CD1
TYR
A
161
37.222
10.895
0.682
1.00
18.22
A


ATOM
753
CE1
TYR
A
161
36.180
11.557
0.029
1.00
22.24
A


ATOM
754
CD2
TYR
A
161
36.333
8.784
−0.020
1.00
20.53
A


ATOM
755
CE2
TYR
A
161
35.287
9.436
−0.678
1.00
24.24
A


ATOM
756
CZ
TYR
A
161
35.218
10.822
−0.648
1.00
22.32
A


ATOM
757
OH
TYR
A
161
34.194
11.471
−1.298
1.00
23.03
A


ATOM
758
C
TYR
A
161
37.812
9.681
3.598
1.00
20.14
A


ATOM
759
O
TYR
A
161
36.959
8.819
3.810
1.00
19.53
A


ATOM
760
N
ALA
A
162
37.791
10.880
4.178
1.00
19.92
A


ATOM
761
CA
ALA
A
162
36.721
11.271
5.099
1.00
21.07
A


ATOM
762
CB
ALA
A
162
37.187
12.419
6.002
1.00
19.60
A


ATOM
763
C
ALA
A
162
35.542
11.712
4.238
1.00
22.07
A


ATOM
764
O
ALA
A
162
35.436 
12.875
3.860
1.00
20.66
A


ATOM
765
N
LYS
A
163
34.653
10.769
3.945
1.00
23.27
A


ATOM
766
CA
LYS
A
163
33.503
11.017
3.080
1.00
27.12
A


ATOM
767
CB
LYS
A
163
32.663
9.741
2.963
1.00
29.68
A


ATOM
768
CG
LYS
A
163
33.455
8.524
2.515
1.00
37.67
A


ATOM
769
CD
LYS
A
163
32.556 
7.310
2.321
1.00
42.24
A


ATOM
770
CE
LYS
A
163
33.373
6.034
2.185
1.00
44.48
A


ATOM
771
NZ
LYS
A
163
34.143
5.735
3.430
1.00
44.88
A


ATOM
772
C
LYS
A
163
32.581 
12.186
3.411
1.00
25.78
A


ATOM
773
O
LYS
A
163
32.103
12.863
2.506
1.00
26.53
A


ATOM
774
N
ASN
A
164
32.327
12.441
4.689
1.00
24.57
A


ATOM
775
CA
ASN
A
164
31.420
13.522
5.033
1.00
23.77
A


ATOM
776
CB
ASN
A
164
30.610
13.129
6.265
1.00
25.02
A


ATOM
777
CG
ASN
A
164
29.537
12.101
5.932
1.00
27.54
A


ATOM
778
OD1
ASN
A
164
28.772
12.281
4.983
1.00
28.79
A


ATOM
779
ND2
ASN
A
164
29.475
11.024
6.704
1.00
27.13
A


ATOM
780
C
ASN
A
164
31.999
14.931
5.169
1.00
24.43
A


ATOM
781
O
ASN
A
164
31.306
15.856
5.589
1.00
23.98
A


ATOM
782
N
GLY
A
165
33.262
15.097
4.795
1.00
21.56
A


ATOM
783
CA
GLY
A
165
33.873
16.414
4.836
1.00
24.39
A


ATOM
784
C
GLY
A
165
34.191
17.043
6.181
1.00
23.62
A


ATOM
785
O
GLY
A
165
34.380
16.352
7.177
1.00
23.26
A


ATOM
786
N
GLU
A
166
34.234
18.373
6.186
1.00
23.22
A


ATOM
787
CA
GLU
A
166
34.563
19.176
7.362
1.00
24.54
A


ATOM
788
CB
GLU
A
166
35.055
20.558
6.913
1.00
25.04
A


ATOM
789
CG
GLU
A
166
36.419
20.569
6.229
1.00
26.48
A


ATOM
790
CD
GLU
A
166
36.699
21.889
5.517
1.00
30.02
A


ATOM
791 
OE1
GLU
A
166
36.081
22.906
5.889
1.00
29.33
A


ATOM
792 
OE2
GLU
A
166
37.544
21.916
4.596
1.00
30.48
A


ATOM
793
C
GLU
A
166
33.436
19.372
8.369
1.00
24.44
A


ATOM
794
O
GLU
A
166
32.279
19.541
8.001
1.00
22.76
A


ATOM
795
N
LEU
A
167
33.791
19.370
9.649
1.00
22.95
A


ATOM
796
CA
LEU
A
167
32.813
19.581
10.707
1.00
22.26
A


ATOM
797
CB
LEU
A
167
33.497
19.481
12.073
1.00
22.32
A


ATOM
798
CG
LEU
A
167
32.706
19.923
13.306
1.00
22.04
A


ATOM
799
CD1
LEU
A
167
31.454
19.074
13.463
1.00
19.66
A


ATOM
800
CD2
LEU
A
167
33.597
19.805
14.537
1.00
21.17
A


ATOM
801
C
LEU
A
167
32.193
20.971
10.529
1.00
23.49
A


ATOM
802
O
LEU
A
167
31.047
21.209
10.907
1.00
23.56
A


ATOM
803
N
LEU
A
168
32.960
21.887
9.948
1.00
24.25
A


ATOM
804
CA
LEU
A
168
32.473
23.245
9.722
1.00
26.64
A


ATOM
805
CB
LEU
A
168
33.560
24.099
9.066
1.00
25.62
A


ATOM
806
CG
LEU
A
168
33.198
25.546
8.707
1.00
27.34
A


ATOM
807
CD1
LEU
A
168
32.718
26.296
9.946
1.00
26.42
A


ATOM
808 
CD2
LEU
A
168
34.418
26.238
8.119
1.00
26.74
A


ATOM
809
C
LEU
A
168
31.234
23.218
8.829
1.00
27.13
A


ATOM
810
O
LEU
A
168
30.297
23.989
9.030
1.00
26.01
A


ATOM
811
N
LYS
A
169
31.233
22.320
7.848
1.00
26.41
A


ATOM
812
CA
LYS
A
169
30.106
22.210
6.934
1.00
27.70
A


ATOM
813
CB
LYS
A
169
30.324
21.064
5.945
1.00
30.49
A


ATOM
814
CG
LYS
A
169
29.151
20.854
4.993
1.00
32.47
A


ATOM
815
CD
LYS
A
169
29.407
19.728
3.998
1.00
35.98
A


ATOM
816
CE
LYS
A
169
29.462
18.372
4.683
1.00
38.53
A


ATOM
817
NZ
LYS
A
169
29.622
17.263
3.702
1.00
41.00
A


ATOM
818
C
LYS
A
169
28.801
21.985
7.682
1.00
28.12
A


ATOM
819
O
LYS
A
169
27.785
22.608
7.371
1.00
28.08
A


ATOM
820
N
TYR
A
170
28.826
21.094
8.668
1.00
26.53
A


ATOM
821
CA
TYR
A
170
27.624
20.791
9.434
1.00
26.95
A


ATOM
822
CB
TYR
A
170
27.810
19.476
10.193
1.00
25.03
A


ATOM
823
CG
TYR
A
170
27.898
18.300
9.251
1.00
26.65
A


ATOM
824
CD1
TYR
A
170
26.745
17.661
8.790
1.00
28.27
A


ATOM
825
CE1
TYR
A
170
26.814
16.642
7.839
1.00
26.85
A


ATOM
826
CD2
TYR
A
170
29.127
17.884
8.742
1.00
27.83
A


ATOM
827
CE2
TYR
A
170
29.209
16.869
7.792
1.00
27.19
A


ATOM
828
CZ
TYR
A
170
28.049
16.254
7.343
1.00
30.02
A


ATOM
829
OH
TYR
A
170
28.130
15.268
6.382
1.00
29.23
A


ATOM
830
C
TYR
A
170
27.229
21.918
10.376
1.00
27.59
A


ATOM
831
O
TYR
A
170
26.045
22.122
10.642
1.00
29.25
A


ATOM
832
N
ILE
A
171
28.208
22.660
10.882
1.00
28.16
A


ATOM
833
CA
ILE
A
171
27.883
23.770
11.763
1.00
29.03
A


ATOM
834
CB
ILE
A
171
29.151
24.435
12.337
1.00
27.51
A


ATOM
835
CG2
ILE
A
171
28.773
25.705
13.084
1.00
27.97
A


ATOM
836
CG1
ILE
A
171
29.872
23.458
13.272
1.00
26.70
A


ATOM
837
CD1
ILE
A
171
31.163
23.996
13.856
1.00
24.07
A


ATOM
838
C
ILE
A
171
27.094
24.796
10.944
1.00
31.41
A


ATOM
839
O
ILE
A
171
26.088
25.335
11.407
1.00
31.69
A


ATOM
840
N
ARG
A
172
27.546
25.047
9.719
1.00
33.21
A


ATOM
841
CA
ARG
A
172
26.874
26.000
8.844
1.00
36.54
A


ATOM
842
CB
ARG
A
172
27.734
26.314
7.616
1.00
37.73
A


ATOM
843
CG
ARG
A
172
29.057
27.011
7.912
1.00
41.65
A


ATOM
844
CD
ARG
A
172
29.708
27.492
6.616
1.00
45.29
A


ATOM
845
NE
ARG
A
172
31.037
28.070
6.812
1.00
48.51
A


ATOM
846
CZ
ARG
A
172
31.314
29.059
7.658
1.00
51.53
A


ATOM
847
NH1
ARG
A
172
30.355
29.593
8.406
1.00
53.75
A


ATOM
848
NH2
ARG
A
172
32.553
29.526
7.748
1.00
51.21
A


ATOM
849
C
ARG
A
172
25.528
25.459
8.378
1.00
37.67
A


ATOM
850
O
ARG
A
172
24.550
26.200
8.288
1.00
39.09
A


ATOM
851
N
LYS
A
173
25.481
24.163
8.092
1.00
38.44
A


ATOM
852
CA
LYS
A
173
24.259
23.528
7.619
1.00
39.25
A


ATOM
853
CB
LYS
A
173
24.523
22.061
7.272
1.00
41.89
A


ATOM
854
CG
LYS
A
173
23.279
21.298
6.830
1.00
45.52
A


ATOM
855
CD
LYS
A
173
23.557
19.808
6.653
1.00
49.60
A


ATOM
856
CE
LYS
A
173
24.477
19.530
5.469
1.00
52.63
A


ATOM
857
NZ
LYS
A
173
23.855
19.894
4.160
1.00
54.61
A


ATOM
858
C
LYS
A
173
23.089
23.608
8.595
1.00
39.30
A


ATOM
859
O
LYS
A
173
21.981
23.960
8.201
1.00
39.62
A


ATOM
860
N
ILE
A
174
23.320
23.282
9.863
1.00
37.96
A


ATOM
861
CA
ILE
A
174
22.229
23.314
10.833
1.00
37.36
A


ATOM
862
CB
ILE
A
174
22.159
21.998
11.652
1.00
37.44
A


ATOM
863
CG2
ILE
A
174
22.058
20.802
10.709
1.00
38.37
A


ATOM
864
CG1
ILE
A
174
23.397
21.850
12.532
1.00
37.25
A


ATOM
865
CD1
ILE
A
174
23.355
20.620
13.418
1.00
36.85
A


ATOM
866
C
ILE
A
174
22.259
24.492
11.801
1.00
36.71
A


ATOM
867
O
ILE
A
174
21.448
24.556
12.724
1.00
38.05
A


ATOM
868
N
GLY
A
175
23.185
25.423
11.592
1.00
35.48
A


ATOM
869
CA
GLY
A
175
23.265
26.585
12.462
1.00
35.29
A


ATOM
870
C
GLY
A
175
24.053
26.360
13.737
1.00
35.06
A


ATOM
871
O
GLY
A
175
25.066
27.019
13.970
1.00
37.46
A


ATOM
872 
N
SER
A
176
23.581
25.441
14.571
1.00
33.94
A


ATOM
873
CA
SER
A
176
24.253
25.113
15.822
1.00
32.84
A


ATOM
874
CB
SER
A
176
23.938
26.155
16.901
1.00
33.54
A


ATOM
875
OG
SER
A
176
22.599
26.056
17.347
1.00
34.86
A


ATOM
876
C
SER
A
176
23.796
23.731
16.276
1.00
32.34
A


ATOM
877
O
SER
A
176
22.726
23.263
15.884
1.00
32.82
A


ATOM
878
N
PHE
A
177
24.609
23.085
17.103
1.00
29.39
A


ATOM
879
CA
PHE
A
177
24.313
21.743
17.597
1.00
27.20
A


ATOM
880
CB
PHE
A
177
25.621
20.989
17.865
1.00
26.39
A


ATOM
881
CG
PHE
A
177
26.372
20.585
16.622
1.00
26.18
A


ATOM
882
CD1
PHE
A
177
26.210
21.277
15.426
1.00
25.30
A


ATOM
883
CD2
PHE
A
177
27.266
19.516
16.662
1.00
26.05
A


ATOM
884
CE1
PHE
A
177
26.923
20.912
14.290
1.00
26.59
A


ATOM
885
CE2
PHE
A
177
27.986
19.143
15.532
1.00
26.06
A


ATOM
886 
CZ
PHE
A
177
27.815
19.841
14.343
1.00
25.42
A


ATOM
887
C
PHE
A
177
23.500
21.752
18.884
1.00
27.00
A


ATOM
888
O
PHE
A
177
23.704
22.610
19.747
1.00
26.48
A


ATOM
889
N
ASP
A
178
22.578
20.802
19.022
1.00
26.70
A


ATOM
890
CA
ASP
A
178
21.816
20.729
20.260
1.00
26.35
A


ATOM
891
CB
ASP
A
178
20.621
19.773
20.142
1.00
29.90
A


ATOM
892
CG
ASP
A
178
21.020
18.372
19.720
1.00
32.28
A


ATOM
893
OD1
ASP
A
178
22.157
17.949
20.014
1.00
35.21
A


ATOM
894
OD2
ASP
A
178
20.179
17.683
19.105
1.00
34.79
A


ATOM
895
C
ASP
A
178
22.810
20.228
21.311
1.00
25.03
A


ATOM
896
O
ASP
A
178
23.974
19.968
20.992
1.00
21.24
A


ATOM
897
N
GLU
A
179
22.361
20.083
22.552
1.00
23.60
A


ATOM
898
CA
GLU
A
179
23.247
19.644
23.619
1.00
25.18
A


ATOM
899
CB
GLU
A
179
22.542
19.770
24.971
1.00
27.60
A


ATOM
900
CG
GLU
A
179
23.324
19.176
26.130
1.00
32.58
A


ATOM
901
CD
GLU
A
179
22.997
19.845
27.449
1.00
35.82
A


ATOM
902
OE1
GLU
A
179
21.825
20.224
27.645
1.00
35.95
A


ATOM
903
OE2
GLU
A
179
23.912
19.984
28.291
1.00
38.19
A


ATOM
904
C
GLU
A
179
23.808
18.235
23.450
1.00
24.08
A


ATOM
905
O
GLU
A
179
24.977
17.989
23.756
1.00
22.79
A


ATOM
906
N
THR
A
180
22.983
17.316
22.961
1.00
23.36
A


ATOM
907
CA
THR
A
180
23.412
15.935
22.761
1.00
22.15
A


ATOM
908
CB
THR
A
180
22.224
15.054
22.320
1.00
23.77
A


ATOM
909
OG1
THR
A
180
21.222
15.075
23.341
1.00
26.37
A


ATOM
910
CG2
THR
A
180
22.670
13.616
22.088
1.00
22.66
A


ATOM
911
C
THR
A
180
24.533
15.830
21.724
1.00
22.01
A


ATOM
912
O
THR
A
180
25.533
15.141
21.944
1.00
19.87
A


ATOM
913
N
CYS 
A
181
24.365
16.511
20.596
1.00
21.21
A


ATOM
914
CA
CYS 
A
181
25.372
16.480
19.541
1.00
22.22
A


ATOM
915
CB
CYS
A
181
24.800
17.065
18.250
1.00
24.62
A


ATOM
916
SG
CYS
A
181
23.435
16.080
17.560
1.00
29.50
A


ATOM
917
C
CYS
A
181
26.633
17.232
19.954
1.00
23.07
A


ATOM
918
O
CYS
A
181
27.746
16.827
19.608
1.00
23.95
A


ATOM
919
N
THR
A
182
26.463
18.325
20.695
1.00
22.76
A


ATOM
920
CA
THR
A
182
27.606
19.103
21.161
1.00
21.49
A


ATOM
921
CB
THR
A
182
27.167
20.346
21.978
1.00
21.37
A


ATOM
922
OG1
THR
A
182
26.459
21.262
21.134
1.00
22.50
A


ATOM
923
CG2
THR
A
182
28.379
21.046
22.565
1.00
18.36
A


ATOM
924
C
THR
A
182
28.454
18.215
22.071
1.00
21.48
A


ATOM
925
O
THR
A
182
29.669
18.090
21.894
1.00
19.95
A


ATOM
926
N
ARG
A
183
27.798
17.602
23.050
1.00
18.97
A


ATOM
927
CA
ARG
A
183
28.468
16.723
23.996
1.00
19.39
A


ATOM
928
CB
ARG
A
183
27.455
16.140
24.984
1.00
19.46
A


ATOM
929 
CG
ARG
A
183
28.030
15.062
25.887
1.00
18.77
A


ATOM
930
CD
ARG
A
183
27.021
14.571
26.925
1.00
21.19
A


ATOM
931
NE
ARG
A
183
26.605
15.642
27.824
1.00
19.46
A


ATOM
932
CZ
ARG
A
183
25.496
16.362
27.679
1.00
20.45
A


ATOM
933
NH1
ARG
A
183
24.672
16.123
26.666
1.00
19.81
A


ATOM
934
NH2
ARG
A
183
25.224
17.338
28.539
1.00
17.11
A


ATOM
935
C
ARG
A
183
29.206
15.577
23.302
1.00
20.02
A


ATOM
936
O
ARG
A
183
30.383
15.333
23.573
1.00
19.97
A


ATOM
937
N
PHE
A
184
28.520
14.871
22.409
1.00
19.24
A


ATOM
938
CA
PHE
A
184
29.144
13.746
21.722
1.00
18.04
A


ATOM
939
CB
PHE
A
184
28.158
13.078
20.764
1.00
21.05
A


ATOM
940
CG
PHE
A
184
28.719
11.857
20.098
1.00
22.67
A


ATOM
941
CD1
PHE
A
184
28.717
10.630
20.754
1.00
22.97
A


ATOM
942
CD2
PHE
A
184
29.317
11.949
18.850
1.00
19.97
A


ATOM
943
CE1
PHE
A
184
29.308
9.510
20.176
1.00
23.53
A


ATOM
944
CE2
PHE
A
184
29.915
10.833
18.263
1.00
24.11
A


ATOM
945
CZ
PHE
A
184
29.910
9.613
18.928
1.00
22.97
A


ATOM
946
C
PHE
A
184
30.403
14.127
20.941
1.00
17.99
A


ATOM
947
O
PHE
A
184
31.461
13.531
21.130
1.00
18.89
A


ATOM
948
N
TYR
A
185
30.292
15.110
20.056
1.00
15.73
A


ATOM
949
CA
TYR
A
185
31.443
15.519
19.265
1.00
15.72
A


ATOM
950
CB
TYR
A
185
30.992
16.413
18.111
1.00
17.33
A


ATOM
951
CG
TYR
A
185
30.364
15.584
17.015
1.00
19.37
A


ATOM
952
CD1
TYR
A
185
31.159
14.809
16.168
1.00
16.53
A


ATOM
953
CE1
TYR
A
185
30.590
13.952
15.232
1.00
18.12
A


ATOM
954
CD2
TYR
A
185
28.976
15.484
16.892
1.00
18.18
A


ATOM
955
CE2
TYR
A
185
28.398
14.623
15.956
1.00
18.90
A


ATOM
956
CZ
TYR
A
185
29.211
13.861
15.133
1.00
18.41
A


ATOM
957
OH
TYR
A
185
28.650
12.995
14.218
1.00
20.48
A


ATOM
958
C
TYR
A
185
32.544
16.172
20.083
1.00
15.79
A


ATOM
959
O
TYR
A
185
33.720
16.015
19.766
1.00
17.69
A


ATOM
960
N
THR
A
186
32.176
16.887
21.142
1.00
15.68
A


ATOM
961
CA
THR
A
186
33.184
17.504
21.997
1.00
16.03
A


ATOM
962
CB
THR
A
186
32.559
18.403
23.094
1.00
16.62
A


ATOM
963
OG1
THR
A
186
31.866
19.503
22.481
1.00
14.79
A


ATOM
964
CG2
THR
A
186
33.656
18.953
24.019
1.00
14.68
A


ATOM
965
C
THR
A
186
33.954
16.375
22.680
1.00
15.59
A


ATOM
966
O
THR
A
186
35.176
16.443
22.823
1.00
13.77
A


ATOM
967
N
ALA
A
187
33.234
15.333
23.097
1.00
14.06
A


ATOM
968
CA
ALA
A
187
33.869
14.196
23.757
1.00
14.74
A


ATOM
969
CB
ALA
A
187
32.810
13.195
24.224
1.00
14.32
A


ATOM
970
C
ALA
A
187
34.875
13.509
22.821
1.00
14.41
A


ATOM
971
O
ALA
A
187
35.972
13.136
23.247
1.00
15.61
A


ATOM
972
N
GLU
A
188
34.516
13.340
21.549
1.00
14.01
A


ATOM
973
CA
GLU
A
188
35.443
12.704
20.615
1.00
13.50
A


ATOM
974
CB
GLU
A
188
34.782
12.449
19.251
1.00
12.85
A


ATOM
975
CG
GLU
A
188
33.622
11.454
19.282
1.00
12.71
A


ATOM
976
CD
GLU
A
188
33.464
10.685
17.979
1.00
15.01
A


ATOM
977
OE1
GLU
A
188
33.687
11.275
16.899
1.00
13.21
A


ATOM
978
OE2
GLU
A
188
33.110
9.484
18.031
1.00
17.69
A


ATOM
979
C
GLU
A
188
36.682
13.582
20.436
1.00
13.34
A


ATOM
980
O
GLU
A
188
37.803
13.085
20.408
1.00
14.69
A


ATOM
981
N
ILE
A
189
36.486
14.893
20.326
1.00
13.52
A


ATOM
982
CA
ILE
A
189
37.627
15.787
20.159
1.00
13.35
A


ATOM
983
CB
ILE
A
189
37.169
17.247
19.939
1.00
13.95
A


ATOM
984
CG2
ILE
A
189
38.381
18.165
19.822
1.00
12.47
A


ATOM
985
CG1
ILE
A
189
36.302
17.332
18.671
1.00
13.44
A


ATOM
986
CD1
ILE
A
189
35.588
18.664
18.491
1.00
14.29
A


ATOM
987
C
ILE
A
189
38.530
15.702
21.394
1.00
14.63
A


ATOM
988
O
ILE
A
189
39.753
15.595
21.271
1.00
12.97
A


ATOM
989
N
VAL
A
190
37.927
15.751
22.582
1.00
14.35
A


ATOM
990
CA
VAL
A
190
38.684
15.655
23.832
1.00
13.22
A


ATOM
991
CB
VAL
A
190
37.743
15.690
25.061
1.00
14.28
A


ATOM
992
CG1
VAL
A
190
38.509
15.267
26.326
1.00
15.08
A


ATOM
993
CG2
VAL
A
190
37.160
17.082
25.233
1.00
12.08
A


ATOM
994
C
VAL
A
190
39.468
14.338
23.859
1.00
14.61
A


ATOM
995
O
VAL
A
190
40.634
14.304
24.250
1.00
13.72
A


ATOM
996
N
SER
A
191
38.825
13.254
23.432
1.00
15.26
A


ATOM
997
CA
SER
A
191
39.478
11.943
23.421
1.00
16.81
A


ATOM
998
CB
SER
A
191
38.470
10.857
23.041
1.00
16.14
A


ATOM
999
OG
SER
A
191
39.018
9.569
23.238
1.00
16.94
A


ATOM
1000
C
SER
A
191
40.649
11.928
22.441
1.00
16.58
A


ATOM
1001
O
SER
A
191
41.697
11.335
22.713
1.00
13.96
A


ATOM
1002
N
ALA
A
192
40.468
12.586
21.300
1.00
15.26
A


ATOM
1003
CA
ALA
A
192
41.518
12.645
20.292
1.00
14.37
A


ATOM
1004
CB
ALA
A
192
40.989
13.296
19.016
1.00
14.43
A


ATOM
1005
C
ALA
A
192
42.695
13.440
20.845
1.00
16.46
A


ATOM
1006
O
ALA
A
192
43.851
13.038
20.697
1.00
17.96
A


ATOM
1007
N
LEU
A
193
42.401
14.563
21.496
1.00
15.02
A


ATOM
1008
CA
LEU
A
193
43.459
15.392
22.067
1.00
15.42
A


ATOM
1009
CB
LEU
A
193
42.884
16.712
22.600
1.00
12.88
A


ATOM
1010
CG
LEU
A
193
42.445
17.721
21.525
1.00
15.97
A


ATOM
1011
CD1
LEU
A
193
41.869
18.979
22.190
1.00
13.97
A


ATOM
1012
CD2
LEU
A
193
43.642
18.088
20.655
1.00
14.58
A


ATOM
1013
C
LEU
A
193
44.211
14.659
23.174
1.00
14.49
A


ATOM
1014
O
LEU
A
193
45.427
14.813
23.310
1.00
16.56
A


ATOM
1015
N
GLU
A
194
43.500
13.870
23.975
1.00
13.96
A


ATOM
1016
CA
GLU
A
194
44.179
13.123
25.032
1.00
14.08
A


ATOM
1017
CB
GLU
A
194
43.190
12.295
25.857
1.00
14.65
A


ATOM
1018
CG
GLU
A
194
43.882
11.301
26.789
1.00
17.09
A


ATOM
1019
CD
GLU
A
194
42.924
10.592
27.730
1.00
19.59
A


ATOM
1020
OE1
GLU
A
194
41.809
10.237
27.295
1.00
19.25
A


ATOM
1021
OE2
GLU
A
194
43.302
10.380
28.906
1.00
20.20
A


ATOM
1022
C
GLU
A
194
45.208
12.199
24.386
1.00
13.57
A


ATOM
1023
O
GLU
A
194
46.337
12.093
24.847
1.00
14.23
A


ATOM
1024
N
TYR
A
195
44.822
11.544
23.301
1.00
14.89
A


ATOM
1025
CA
TYR
A
195
45.743
10.642
22.618
1.00
16.58
A


ATOM
1026
CB
TYR
A
195
45.030
9.910
21.488
1.00
17.29
A


ATOM
1027
CG
TYR
A
195
45.956
9.058
20.649
1.00
17.92
A


ATOM
1028
CD1
TYR
A
195
46.347
7.788
21.077
1.00
17.96
A


ATOM
1029
CE1
TYR
A
195
47.203
6.996
20.304
1.00
19.77
A


ATOM
1030
CD2
TYR
A
195
46.445
9.524
19.428
1.00
16.67
A


ATOM
1031
CE2
TYR
A
195
47.299
8.744
18.650
1.00
18.51
A


ATOM
1032
CZ
TYR
A
195
47.671
7.481
19.094
1.00
20.24
A


ATOM
1033
OH
TYR
A
195
48.506
6.705
18.325
1.00
21.89
A


ATOM
1034
C
TYR
A
195
46.917
11.419
22.035
1.00
16.98
A


ATOM
1035
O
TYR
A
195
48.081
11.047
22.203
1.00
14.61
A


ATOM
1036
N
LEU
A
196
46.599
12.507
21.347
1.00
16.30
A


ATOM
1037
CA
LEU
A
196
47.619
13.328
20.720
1.00
18.15
A


ATOM
1038
CB
LEU
A
196
46.969
14.502
19.982
1.00
18.59
A


ATOM
1039
CG
LEU
A
196
47.834
15.203
18.935
1.00
22.51
A


ATOM
1040
CD1
LEU
A
196
48.222
14.206
17.841
1.00
20.94
A


ATOM
1041
CD2
LEU
A
196
47.060
16.375
18.338
1.00
22.98
A


ATOM
1042
C
LEU
A
196
48.592
13.844
21.763
1.00
17.75
A


ATOM
1043
O
LEU
A
196
49.801
13.644
21.649
1.00
18.33
A


ATOM
1044
N
HIS
A
197
48.064
14.495
22.792
1.00
17.12
A


ATOM
1045
CA
HIS
A
197
48.913
15.042
23.842
1.00
18.47
A


ATOM
1046
CB
HIS
A
197
48.069
15.866
24.817
1.00
15.90
A


ATOM
1047
CG
HIS
A
197
47.571
17.152
24.231
1.00
19.15
A


ATOM
1048
CD2
HIS
A
197
47.830
17.745
23.038
1.00
18.22
A


ATOM
1049
ND1
HIS
A
197
46.704
17.992
24.897
1.00
17.47
A


ATOM
1050
CE1
HIS
A
197
46.450
19.047
24.139
1.00
19.74
A


ATOM
1051
NE2
HIS
A
197
47.119
18.921
23.007
1.00
15.69
A


ATOM
1052
C
HIS
A
197
49.696
13.958
24.572
1.00
19.40
A


ATOM
1053
O
HIS
A
197
50.823
14.192
25.021
1.00
19.42
A


ATOM
1054
N
GLY
A
198
49.106
12.770
24.679
1.00
18.59
A


ATOM
1055
CA
GLY
A
198
49.793
11.675
25.339
1.00
19.60
A


ATOM
1056
C
GLY
A
198
51.075
11.307
24.612
1.00
21.86
A


ATOM
1057
O
GLY
A
198
51.963
10.682
25.186
1.00
23.09
A


ATOM
1058
N
LYS
A
199
51.174
11.687
23.341
1.00
22.81
A


ATOM
1059
CA
LYS
A
199
52.368
11.401
22.549
1.00
24.43
A


ATOM
1060
CB
LYS
A
199
51.990
10.905
21.154
1.00
26.00
A


ATOM
1061
CG
LYS
A
199
51.378
9.520
21.133
1.00
30.98
A


ATOM
1062
CD
LYS
A
199
51.291
9.002
19.708
1.00
36.85
A


ATOM
1063
CE
LYS
A
199
50.832
7.559
19.682
1.00
40.37
A


ATOM
1064
NZ
LYS
A
199
51.646
6.691
20.581
1.00
43.48
A


ATOM
1065
C
LYS
A
199
53.253
12.631
22.414
1.00
23.88
A


ATOM
1066
O
LYS
A
199
54.144
12.669
21.568
1.00
24.97
A


ATOM
1067
N
GLY
A
200
52.997
13.638
23.243
1.00
24.00
A


ATOM
1068
CA
GLY
A
200
53.790
14.853
23.203
1.00
22.12
A


ATOM
1069
C
GLY
A
200
53.665
15.632
21.907
1.00
22.14
A


ATOM
1070
O
GLY
A
200
54.632
16.231
21.439
1.00
22.41
A


ATOM
1071
N
ILE
A
201
52.475
15.630
21.320
1.00
20.00
A


ATOM
1072
CA
ILE
A
201
52.252
16.355
20.080
1.00
18.93
A


ATOM
1073
CB
ILE
A
201
51.784
15.414
18.955
1.00
19.70
A


ATOM
1074
CG2
ILE
A
201
51.414
16.226
17.716
1.00
20.12
A


ATOM
1075
CG1
ILE
A
201
52.880
14.395
18.636
1.00
20.03
A


ATOM
1076
CD1
ILE
A
201
52.408
13.258
17.745
1.00
22.75
A


ATOM
1077
C
ILE
A
201
51.193
17.425
20.270
1.00
19.87
A


ATOM
1078
O
ILE
A
201
50.121
17.161
20.817
1.00
20.08
A


ATOM
1079
N
ILE
A
202
51.508
18.633
19.815
1.00
19.94
A


ATOM
1080
CA
ILE
A
202
50.601
19.772
19.891
1.00
20.45
A


ATOM
1081
CB
ILE
A
202
51.352
21.040
20.356
1.00
22.21
A


ATOM
1082
CG2
ILE
A
202
50.381
22.220
20.470
1.00
22.67
A


ATOM
1083
CG1
ILE
A
202
52.033
20.775
21.700
1.00
24.19
A


ATOM
1084
CD1
ILE
A
202
52.914
21.920
22.169
1.00
25.39
A


ATOM
1085
C
ILE
A
202
50.105
19.999
18.464
1.00
20.71
A


ATOM
1086
O
ILE
A
202
50.910
20.067
17.538
1.00
19.48
A


ATOM
1087
N
HIS
A
203
48.795
20.108
18.270
1.00
18.65
A


ATOM
1088
CA
HIS
A
203
48.280
20.319
16.919
1.00
18.02
A


ATOM
1089
CB
HIS
A
203
46.775
20.057
16.874
1.00
16.31
A


ATOM
1090
CG
HIS
A
203
46.199
20.136
15.495
1.00
18.36
A


ATOM
1091
CD2
HIS
A
203
46.043
21.186
14.655
1.00
16.42
A


ATOM
1092
ND1
HIS
A
203
45.759
19.026
14.806
1.00
19.50
A


ATOM
1093
CE1
HIS
A
203
45.359
19.389
13.600
1.00
17.64
A


ATOM
1094
NE2
HIS
A
203 
45.522
20.694
13.483
1.00
20.87
A


ATOM
1095
C
HIS
A
203
48.589
21.738
16.405
1.00
18.92
A


ATOM
1096
O
HIS
A
203
49.073
21.906
15.282
1.00
16.21
A


ATOM
1097
N
ARG
A
204
48.301
22.744
17.232
1.00
18.60
A


ATOM
1098
CA
ARG
A
204
48.552
24.157
16.914
1.00
19.81
A


ATOM
1099
CB
ARG
A
204
49.998
24.365
16.458
1.00
21.61
A


ATOM
1100
CG
ARG
A
204
51.024
24.137
17.550
1.00
23.82
A


ATOM
1101
CD
ARG
A
204
52.323
24.870
17.252
1.00
27.62
A


ATOM
1102
NE
ARG
A
204
52.932
24.449
15.994
1.00
29.43
A


ATOM
1103 
CZ
ARG
A
204
54.125
24.861
15.572
1.00
33.10
A


ATOM
1104
NH1
ARG
A
204
54.835
25.706
16.311
1.00
32.12
A


ATOM
1105
NH2
ARG
A
204
54.614
24.426
14.418
1.00
30.25
A


ATOM
1106
C
ARG
A
204
47.624
24.830
15.905
1.00
20.03
A


ATOM
1107
O
ARG
A
204
47.711
26.038
15.698
1.00
20.88
A


ATOM
1108
N
ASP
A
205
46.755
24.071
15.255
1.00
18.96
A


ATOM
1109
CA
ASP
A
205
45.828
24.692
14.325
1.00
17.90
A


ATOM
1110
CB
ASP
A
205
46.418
24.741
12.914
1.00
18.95
A


ATOM
1111
CG
ASP
A
205
45.655
25.688
12.008
1.00
20.36
A


ATOM
1112
OD1
ASP
A
205
44.939
26.560
12.545
1.00
20.35
A


ATOM
1113
OD2
ASP
A
205
45.772
25.573
10.771
1.00
22.49
A


ATOM
1114
C
ASP
A
205
44.500
23.956
14.328
1.00
19.60
A


ATOM
1115
O
ASP
A
205
43.876
23.751
13.287
1.00
21.53
A


ATOM
1116
N
LEU
A
206
44.063
23.569
15.521
1.00
18.53
A


ATOM
1117
CA
LEU
A
206
42.813
22.851
15.667
1.00
19.18
A


ATOM
1118
CB
LEU
A
206
42.693
22.295
17.087
1.00
18.94
A


ATOM
1119
CG
LEU
A
206
41.511
21.358
17.346
1.00
23.10
A


ATOM
1120
CD1
LEU
A
206
41.615
20.142
16.436
1.00
23.01
A


ATOM
1121
CD2
LEU
A
206
41.504
20.933
18.808
1.00
22.97
A


ATOM
1122
C
LEU
A
206
41.639
23.772
15.361
1.00
19.05
A


ATOM
1123
O
LEU
A
206
41.556
24.880
15.886
1.00
19.25
A


ATOM
1124
N
LYS
A
207
40.740
23.307
14.500
1.00
17.54
A


ATOM
1125
CA
LYS
A
207
39.564
24.081
14.110
1.00
18.60
A


ATOM
1126
CB
LYS
A
207
39.980
25.248
13.196
1.00
18.98
A


ATOM
1127
CG
LYS
A
207
40.786
24.817
11.982
1.00
18.20
A


ATOM
1128
CD
LYS
A
207
41.246
26.000
11.139
1.00
21.42
A


ATOM
1129
CE
LYS
A
207
42.223
25.537
10.062
1.00
23.21
A


ATOM
1130
NZ
LYS
A
207
42.561
26.604
9.084
1.00
29.61
A


ATOM
1131
C
LYS
A
207
38.566
23.181
13.388
1.00
18.18
A


ATOM
1132
O
LYS
A
207
38.921
22.100
12.915
1.00
18.11
A


ATOM
1133
N
PRO
A
208
37.298
23.614
13.293
1.00
20.26
A


ATOM
1134
CD
PRO
A
208
36.713
24.833
13.882
1.00
18.79
A


ATOM
1135
CA
PRO
A
208
36.272
22.814
12.616
1.00
19.67
A


ATOM
1136
CB
PRO
A
208
35.063
23.742
12.608
1.00
19.45
A


ATOM
1137
CG
PRO
A
208
35.231
24.509
13.891
1.00
21.81
A


ATOM
1138
C
PRO
A
208
36.674
22.372
11.209
1.00
21.04
A


ATOM
1139
O
PRO
A
208
36.264
21.307
10.751
1.00
21.19
A


ATOM
1140
N
GLU
A
209
37.474
23.188
10.528
1.00
21.69
A


ATOM
1141
CA
GLU
A
209
37.928
22.872
9.170
1.00
22.64
A


ATOM
1142
CB
GLU
A
209
38.644
24.084
8.558
1.00
23.65
A


ATOM
1143
CG
GLU
A
209
39.253
23.825
7.185
1.00
27.24
A


ATOM
1144
CD
GLU
A
209
40.155
24.958
6.716
1.00
29.40
A


ATOM
1145
OE1
GLU
A
209
39.660
26.094
6.553
1.00
29.68
A


ATOM
1146
OE2
GLU
A
209
41.363
24.711
6.511
1.00
30.07
A


ATOM
1147
C
GLU
A
209
38.879
21.668
9.159
1.00
22.28
A


ATOM
1148
O
GLU
A
209
38.955
20.933
8.170
1.00
21.36
A


ATOM
1149
N
ASN
A
210
39.600
21.490
10.263
1.00
19.90
A


ATOM
1150
CA
ASN
A
210
40.574
20.412
10.436
1.00
19.44
A


ATOM
1151
CB
ASN
A
210
41.744
20.912
11.287
1.00
20.07
A


ATOM
1152
CG
ASN
A
210
42.746
21.698
10.479
1.00
25.77
A


ATOM
1153
OD1
ASN
A
210
43.571
22.427
11.029
1.00
26.73
A


ATOM
1154
ND2
ASN
A
210
42.687
21.548
9.158
1.00
25.15
A


ATOM
1155
C
ASN
A
210
40.005
19.151
11.078
1.00
18.63
A


ATOM
1156
O
ASN
A
210
40.712
18.154
11.234
1.00
18.29
A


ATOM
1157
N
ILE
A
211
38.739
19.202
11.469
1.00
16.31
A


ATOM
1158
CA
ILE
A
211
38.090
18.058
12.085
1.00
15.49
A


ATOM
1159
CB
ILE
A
211
37.336
18.488
13.354
1.00
15.40
A


ATOM
1160
CG2
ILE
A
211
36.582
17.311
13.950
1.00
14.59
A


ATOM
1161
CG1
ILE
A
211
38.342
19.046
14.365
1.00
15.91
A


ATOM
1162
CD1
ILE
A
211
37.720
19.669
15.590
1.00
15.98
A


ATOM
1163
C
ILE
A
211
37.131
17.485
11.059
1.00
17.26
A


ATOM
1164
O
ILE
A
211
35.995
17.947
10.926
1.00
18.16
A


ATOM
1165
N
LEU
A
212
37.599
16.486
10.317
1.00
15.97
A


ATOM
1166
CA
LEU
A
212
36.784
15.875
9.274
1.00
17.08
A


ATOM
1167
CB
LEU
A
212
37.685
15.249
8.202
1.00
17.78
A


ATOM
1168
CG
LEU
A
212
38.785
16.157
7.640
1.00
18.92
A


ATOM
1169
CD1
LEU
A
212
39.476
15.450
6.485
1.00
22.09
A


ATOM
1170
CD2
LEU
A
212
38.188
17.482
7.166
1.00
19.91
A


ATOM
1171
C
LEU
A
212
35.843
14.825
9.837
1.00
18.35
A


ATOM
1172
O
LEU
A
212
35.957
14.433
11.002
1.00
19.39
A


ATOM
1173
N
LEU
A
213
34.915
14.368
9.000
1.00
17.84
A


ATOM
1174
CA
LEU
A
213
33.942
13.362
9.403
1.00
19.94
A


ATOM
1175
CB
LEU
A
213
32.556
14.004
9.487
1.00
20.84
A


ATOM
1176
CG
LEU
A
213
32.396
15.059
10.583
1.00
20.31
A


ATOM
1177
CD1
LEU
A
213
31.124
15.837
10.367
1.00
22.75
A


ATOM
1178
CD2
LEU
A
213
32.379
14.378
11.940
1.00
23.93
A


ATOM
1179
C
LEU
A
213
33.914
12.187
8.426
1.00
20.98
A


ATOM
1180
O
LEU
A
213
33.743
12.379
7.218
1.00
19.55
A


ATOM
1181
N
ASN
A
214
34.088
10.970
8.935
1.00
20.44
A


ATOM
1182
CA
ASN
A
214
34.055
9.814
8.049
1.00
23.77
A


ATOM
1183
CB
ASN
A
214
34.745
8.596
8.674
1.00
25.30
A


ATOM
1184
CG
ASN
A
214
34.077
8.127
9.948
1.00
32.04
A


ATOM
1185
OD1
ASN
A
214
32.908
8.422
10.206
1.00
34.43
A


ATOM
1186
ND2
ASN
A
214
34.818
7.369
10.752
1.00
33.85
A


ATOM
1187
C
ASN
A
214
32.618
9.466
7.693
1.00
24.07
A


ATOM
1188
O
ASN
A
214
31.672
10.113
8.150
1.00
19.94
A


ATOM
1189
N
GLU
A
215
32.459
8.433
6.879
1.00
25.77
A


ATOM
1190
CA
GLU
A
215
31.138
8.003
6.445
1.00
28.69
A


ATOM
1191
CB
GLU
A
215
31.275
6.796
5.513
1.00
31.98
A


ATOM
1192
CG
GLU
A
215
29.970
6.334
4.896
1.00
40.22
A


ATOM
1193
CD
GLU
A
215
30.182
5.312
3.795
1.00
44.27
A


ATOM
1194
OE1
GLU
A
215
30.817
4.268
4.065
1.00
46.46
A


ATOM
1195
OE2
GLU
A
215
29.716
5.556
2.660
1.00
46.13
A


ATOM
1196
C
GLU
A
215
30.188
7.673
7.601
1.00
28.41
A


ATOM
1197
O
GLU
A
215
28.971
7.769
7.447
1.00
28.52
A


ATOM
1198
N
ASP
A
216
30.737
7.287
8.752
1.00
26.77
A


ATOM
1199
CA
ASP
A
216
29.914
6.953
9.917
1.00
27.28
A


ATOM
1200
CB
ASP
A
216
30.538
5.795
10.696
1.00
31.27
A


ATOM
1201
CG
ASP
A
216
30.390
4.466
9.979
1.00
37.61
A


ATOM
1202
OD1
ASP
A
216
29.274
4.170
9.499
1.00
39.45
A


ATOM
1203
OD2
ASP
A
216
31.382
3.710
9.902
1.00
41.84
A


ATOM
1204
C
ASP
A
216
29.697
8.135
10.862
1.00
26.37
A


ATOM
1205
O
ASP
A
216
29.136
7.984
11.950
1.00
25.73
A


ATOM
1206
N
MET
A
217
30.156
9.306
10.441
1.00
23.02
A


ATOM
1207
CA
MET
A
217
30.015
10.527
11.218
1.00
21.83
A


ATOM
1208
CB
MET
A
217
28.537
10.789
11.517
1.00
23.24
A


ATOM
1209
CG
MET
A
217
27.742
11.186
10.274
1.00
22.98
A


ATOM
1210
SD
MET
A
217
28.464
12.616
9.430
1.00
27.57
A


ATOM
1211
CE
MET
A
217
27.679
13.974
10.332
1.00
26.68
A


ATOM
1212
C
MET
A
217
30.844
10.618
12.502
1.00
21.51
A


ATOM
1213
O
MET
A
217
30.474
11.323
13.440
1.00
18.62
A


ATOM
1214
N
HIS
A
218
31.957
9.892
12.544
1.00
20.10
A


ATOM
1215
CA
HIS
A
218
32.873
9.964
13.678
1.00
19.86
A


ATOM
1216
CB
HIS
A
218
33.482
8.594
13.977
1.00
20.21
A


ATOM
1217
CG
HIS
A
218
32.551
7.667
14.698
1.00
22.40
A


ATOM
1218
CD2
HIS
A
218
31.910
6.547
14.287
1.00
21.27
A


ATOM
1219
ND1
HIS
A
218
32.177
7.863
16.011
1.00
19.59
A


ATOM
1220
CE1
HIS
A
218
31.348
6.902
16.379
1.00
21.88
A


ATOM
1221
NE2
HIS
A
218
31.168
6.091
15.351
1.00
22.08
A


ATOM
1222
C
HIS
A
218
33.947
10.921
13.172
1.00
19.10
A


ATOM
1223
O
HIS
A
218
34.1701
11.004
11.965
1.00
20.31
A


ATOM
1224
N
ILE
A
219
34.617
11.638
14.067
1.00
17.21
A


ATOM
1225
CA
ILE
A
219
35.628
12.586
13.618
1.00
15.26
A


ATOM
1226
CB
ILE
A
219
35.987
13.614
14.716
1.00
15.38
A


ATOM
1227
CG2
ILE
A
219
34.722
14.305
15.221
1.00
14.58
A


ATOM
1228
CG1
ILE
A
219
36.734
12.919
15.864
1.00
14.46
A


ATOM
1229
CD1
ILE
A
219
37.279
13.885
16.911
1.00
13.74
A


ATOM
1230
C
ILE
A
219
36.929
11.944
13.161
1.00
16.21
A


ATOM
1231
O
ILE
A
219
37.238
10.799
13.500
1.00
15.88
A


ATOM
1232
N
GLN
A
220
37.677
12.711
12.378
1.00
15.62
A


ATOM
1233
CA
GLN
A
220
38.980
12.316
11.876
1.00
17.84
A


ATOM
1234
CB
GLN
A
220
38.872
11.595
10.525
1.00
20.00
A


ATOM
1235
CG
GLN
A
220
38.463
10.129
10.659
1.00
26.97
A


ATOM
1236
CD
GLN
A
220
38.648
9.343
9.372
1.00
29.95
A


ATOM
1237
OE1
GLN
A
220
37.968
9.590
8.373
1.00
33.12
A


ATOM
1238
NE2
GLN
A
220
39.578
8.393
9.389
1.00
30.47
A


ATOM
1239
C
GLN
A
220
39.757
13.610
11.735
1.00
17.00
A


ATOM
1240
O
GLN
A
220
39.609
14.339
10.751
1.00
18.27
A


ATOM
1241
N
ILE
A
221
40.566
13.906
12.746
1.00
14.34
A


ATOM
1242
CA
ILE
A
221
41.361
15.120
12.753
1.00
14.46
A


ATOM
1243
CB
ILE
A
221
41.867
15.416
14.175
1.00
12.30
A


ATOM
1244
CG2
ILE
A
221
42.764
16.656
14.167
1.00
14.78
A


ATOM
1245
CG1
ILE
A
221
40.660
15.613
15.102
1.00
13.92
A


ATOM
1246
CD1
ILE
A
221
41.003
15.901
16.543
1.00
15.06
A


ATOM
1247
C
ILE
A
221
42.536
14.996
11.783
1.00
15.44
A


ATOM
1248
O
ILE
A
221
43.106
13.915
11.613
1.00
13.93
A


ATOM
1249
N
THR
A
222
42.877
16.101
11.127
1.00
15.36
A


ATOM
1250
CA
THR
A
222
43.980
16.098
10.174
1.00
17.52
A


ATOM
1251
CB
THR
A
222
43.470
15.836
8.750
1.00
19.92
A


ATOM
1252
OG1
THR
A
222
44.587
15.637
7.875
1.00
18.78
A


ATOM
1253
CG2
THR
A
222
42.630
17.018
8.257
1.00
18.16
A


ATOM
1254
C
THR
A
222
44.735
17.428
10.192
1.00
19.60
A


ATOM
1255
O
THR
A
222
44.509
18.257
11.084
1.00
18.59
A


ATOM
1256
N
ASP
A
223
45.630
17.610
9.216
1.00
18.69
A


ATOM
1257
CA
ASP
A
223
46.440
18.825
9.069
1.00
20.12
A


ATOM
1258
CB
ASP
A
223
45.532
20.065
9.108
1.00
23.51
A


ATOM
1259
CG
ASP
A
223
46.248
21.335
8.670
1.00
27.09
A


ATOM
1260
OD1
ASP
A
223
47.283
21.227
7.975
1.00
26.28
A


ATOM
1261
OD2
ASP
A
223
45.765
22.438
9.009
1.00
26.15
A


ATOM
1262
C
ASP
A
223
47.516
18.913
10.150
1.00
21.73
A


ATOM
1263
O
ASP
A
223
47.439
19.751
11.055
1.00
22.76
A


ATOM
1264
N
PHE
A
224
48.535
18.063
10.027
1.00
20.75
A


ATOM
1265
CA
PHE
A
224
49.611
17.988
11.009
1.00
20.11
A


ATOM
1266
CB
PHE
A
224
49.805
16.527
11.424
1.00
20.62
A


ATOM
1267
CG
PHE
A
224
48.682
15.991
12.263
1.00
21.41
A


ATOM
1268
CD1
PHE
A
224
48.598
16.312
13.614
1.00
23.05
A


ATOM
1269
CD2
PHE
A
224
47.681
15.212
11.693
1.00
22.27
A


ATOM
1270
CE1
PHE
A
224
47.528
15.868
14.389
1.00
23.30
A


ATOM
1271
CE2
PHE
A
224
46.606
14.763
12.457
1.00
21.11
A


ATOM
1272
CZ
PHE
A
224
46.530
15.093
13.807
1.00
22.02
A


ATOM
1273
C
PHE
A
224
50.957
18.583
10.619
1.00
20.45
A


ATOM
1274
O
PHE
A
224
51.905
18.547
11.407
1.00
20.73
A


ATOM
1275
N
GLY
A
225
51.049
19.125
9.412
1.00
22.02
A


ATOM
1276
CA
GLY
A
225
52.301
19.713
8.981
1.00
22.66
A


ATOM
1277
C
GLY
A
225
52.742
20.822
9.920
1.00
24.99
A


ATOM
1278
O
GLY
A
225
53.939
21.041
10.122
1.00
24.52
A


ATOM
1279
N
THR
A
226
51.779
21.524
10.508
1.00
23.50
A


ATOM
1280
CA
THR
A
226
52.106
22.613
11.416
1.00
25.16
A


ATOM
1281
CB
THR
A
226
51.199
23.829
11.160
1.00
24.76
A


ATOM
1282
OG1
THR
A
226
49.831
23.410
11.113
1.00
22.68
A


ATOM
1283
CG2
THR
A
226
51.571
24.490
9.834
1.00
25.00
A


ATOM
1284
C
THR
A
226
52.046
22.233
12.894
1.00
25.79
A


ATOM
1285
O
THR
A
226
52.019
23.100
13.768
1.00
24.54
A


ATOM
1286
N
ALA
A
227
52.037
20.935
13.173
1.00
24.97
A


ATOM
1287
CA
ALA
A
227
52.004
20.475
14.550
1.00
25.49
A


ATOM
1288
CB
ALA
A
227
51.659
18.993
14.607
1.00
22.85
A


ATOM
1289
C
ALA
A
227
53.384
20.715
15.149
1.00
27.70
A


ATOM
1290
O
ALA
A
227
54.331
21.047
14.435
1.00
26.60
A


ATOM
1291
N
LYS
A
228
53.491
20.558
16.461
1.00
28.53
A


ATOM
1292
CA
LYS
A
228
54.760
20.745
17.149
1.00
32.12
A


ATOM
1293
CB
LYS
A
228
54.699
21.974
18.054
1.00
33.81
A


ATOM
1294
CG
LYS
A
228
56.007
22.294
18.765
1.00
41.23
A


ATOM
1295
CD
LYS
A
228
57.082
22.725
17.768
1.00
47.57
A


ATOM
1296
CE
LYS
A
228
58.401
23.056
18.462
1.00
49.82
A


ATOM
1297
NZ
LYS
A
228
59.459
23.425
17.480
1.00
51.49
A


ATOM
1298
C
LYS
A
228
55.019
19.504
17.985
1.00
33.25
A


ATOM
1299
O
LYS
A
228
54.190
19.129
18.815
1.00
33.70
A


ATOM
1300
N
VAL
A
229
56.159
18.860
17.756
1.00
33.64
A


ATOM
1301
CA
VAL
A
229
56.516
17.661
18.501
1.00
34.66
A


ATOM
1302
CB
VAL
A
229
57.248
16.646
17.609
1.00
33.50
A


ATOM
1303
CG1
VAL
A
229
57.619
15.419
18.415
1.00
32.34
A


ATOM
1304
CG2
VAL
A
229
56.370
16.264
16.436
1.00
34.25
A


ATOM
1305
C
VAL
A
229
57.420
18.035
19.668
1.00
37.57
A


ATOM
1306
O
VAL
A
229
58.581
18.392
19.474
1.00
35.91
A


ATOM
1307
N
LEU
A
230
56.877
17.948
20.878
1.00
40.57
A


ATOM
1308
CA
LEU
A
230
57.615
18.289
22.088
1.00
46.10
A


ATOM
1309
CB
LEU
A
230
56.654
18.417
23.270
1.00
44.71
A


ATOM
1310
CG
LEU
A
230
55.627
19.545
23.207
1.00
44.50
A


ATOM
1311
CD1
LEU
A
230
54.673
19.430
24.383
1.00
44.39
A


ATOM
1312
CD2
LEU
A
230
56.340
20.885
23.214
1.00
44.81
A


ATOM
1313
C
LEU
A
230
58.695
17.279
22.440
1.00
50.42
A


ATOM
1314
O
LEU
A
230
58.603
16.104
22.089
1.00
51.64
A


ATOM
1315
N
SER
A
231
59.717
17.756
23.145
1.00
55.81
A


ATOM
1316
CA
SER
A
231
60.824
16.914
23.583
1.00
61.14
A


ATOM
1317
CB
SER
A
231
62.077
17.200
22.750
1.00
61.27
A


ATOM
1318
OG
SER
A
231
62.444
18.568
22.823
1.00
62.85
A


ATOM
1319
C
SER
A
231
61.124
17.126
25.071
1.00
64.65
A


ATOM
1320
O
SER
A
231
61.392
16.164
25.794
1.00
65.70
A


ATOM
1321
N
PRO
A
232
61.081
18.387
25.549
1.00
67.54
A


ATOM
1322
CD
PRO
A
232
60.854
19.651
24.823
1.00
68.60
A


ATOM
1323
CA
PRO
A
232
61.358
18.655
26.966
1.00
68.74
A


ATOM
1324
CB
PRO
A
232
61.109
20.158
27.086
1.00
68.83
A


ATOM
1325
CG
PRO
A
232
61.505
20.666
25.737
1.00
68.96
A


ATOM
1326
C
PRO
A
232
60.460
17.846
27.899
1.00
69.17
A


ATOM
1327
O
PRO
A
232
59.335
17.494
27.541
1.00
69.94
A


ATOM
1328
N
ALA
A
237
57.424
23.198
27.637
1.00
80.06
A


ATOM
1329
CA
ALA
A
237
56.783
23.047
26.335
1.00
79.29
A


ATOM
1330
CB
ALA
A
237
55.275
22.907
26.512
1.00
78.64
A


ATOM
1331
C
ALA
A
237
57.092
24.239
25.433
1.00
79.07
A


ATOM
1332
O
ALA
A
237
56.250
25.113
25.249
1.00
79.47
A


ATOM
1333
N
ALA
A
238
58.297
24.280
24.871
1.00
78.57
A


ATOM
1334
CA
ALA
A
238
58.683
25.383
23.992
1.00
78.50
A


ATOM
1335
CB
ALA
A
238
60.186
25.347
23.728
1.00
78.50
A


ATOM
1336
C
ALA
A
238
57.920
25.327
22.673
1.00
78.15
A


ATOM
1337
O
ALA
A
238
57.243
24.341
22.375
1.00
77.96
A


ATOM
1338
N
ALA
A
239
58.027
26.393
21.887
1.00
77.28
A


ATOM
1339
CA
ALA
A
239
57.338
26.452
20.603
1.00
76.27
A


ATOM
1340
CB
ALA
A
239
55.849
26.489
20.827
1.00
76.61
A


ATOM
1341
C
ALA
A
239
57.766
27.667
19.793
1.00
75.38
A


ATOM
1342
O
ALA
A
239
58.955
27.955
19.700
1.00
75.89
A


ATOM
1343
N
ASN
A
240
56.781
28.357
19.214
1.00
73.95
A


ATOM
1344
CA
ASN
A
240
56.967
29.553
18.389
1.00
71.07
A


ATOM
1345
CB
ASN
A
240
58.151
30.400
18.874
1.00
71.47
A


ATOM
1346
CG
ASN
A
240
59.459
30.055
18.174
1.00
72.06
A


ATOM
1347
OD1
ASN
A
240
59.575
30.149
16.943
1.00
72.03
A


ATOM
1348
ND2
ASN
A
240
60.470
29.665
18.964
1.00
71.91
A


ATOM
1349
C
ASN
A
240
57.188
29.178
16.928
1.00
69.41
A


ATOM
1350
O
ASN
A
240
57.480
28.024
16.624
1.00
70.09
A


ATOM
1351
N
ALA
A
241
57.055
30.165
16.038
1.00
66.62
A


ATOM
1352
CA
ALA
A
241
57.246
30.013
14.585
1.00
63.94
A


ATOM
1353
C
ALA
A
241
55.952
30.080
13.772
1.00
60.63
A


ATOM
1354
O
ALA
A
241
55.840
30.880
12.845
1.00
61.29
A


ATOM
1355
CB
ALA
A
241
57.979
28.704
14.246
1.00
65.23
A


ATOM
1356
N
PHE
A
242
54.984
29.236
14.113
1.00
56.72
A


ATOM
1357
CA
PHE
A
242
53.712
29.196
13.394
1.00
52.53
A


ATOM
1358
CB
PHE
A
242
53.419
27.767
12.923
1.00
49.14
A


ATOM
1359
CG
PHE
A
242
52.040
27.590
12.354
1.00
47.38
A


ATOM
1360
CD1
PHE
A
242
51.731
28.067
11.085
1.00
47.69
A


ATOM
1361
CD2
PHE
A
242
51.038
26.975
13.102
1.00
45.45
A


ATOM
1362
CE1
PHE
A
242
50.445
27.937
10.565
1.00
46.75
A


ATOM
1363
CE2
PHE
A
242
49.751
26.840
12.594
1.00
45.41
A


ATOM
1364
CZ
PHE
A
242
49.453
27.323
11.322
1.00
46.55
A


ATOM
1365
C
PHE
A
242
52.534
29.688
14.229
1.00
50.08
A


ATOM
1366
O
PHE
A
242
52.502
29.505
15.444
1.00
49.86
A


ATOM
1367
N
VAL
A
243
51.566
30.305
13.557
1.00
47.67
A


ATOM
1368
CA
VAL
A
243
50.355
30.809
14.200
1.00
46.21
A


ATOM
1369
CB
VAL
A
243
50.340
32.352
14.258
1.00
47.36
A


ATOM
1370
CG1
VAL
A
243
49.012
32.844
14.825
1.00
47.54
A


ATOM
1371
CG2
VAL
A
243
51.497
32.842
15.109
1.00
48.50
A


ATOM
1372
C
VAL
A
243
49.150
30.342
13.389
1.00
44.12
A


ATOM
1373
O
VAL
A
243
48.956
30.765
12.247
1.00
44.46
A


ATOM
1374
N
GLY
A
244
48.348
29.467
13.985
1.00
40.48
A


ATOM
1375
CA
GLY
A
244
47.176
28.941
13.306
1.00
37.65
A


ATOM
1376
C
GLY
A
244
46.101
29.960
12.964
1.00
35.39
A


ATOM
1377
O
GLY
A
244
46.313
31.168
13.065
1.00
35.92
A


ATOM
1378
N
THR
A
245
44.936
29.463
12.560
1.00
33.30
A


ATOM
1379
CA
THR
A
245
43.813
30.312
12.184
1.00
30.20
A


ATOM
1380
CB
THR
A
245
42.593
29.450
11.829
1.00
32.00
A


ATOM
1381
OG1
THR
A
245
42.952
28.573
10.755
1.00
32.81
A


ATOM
1382
CG2
THR
A
245
41.419
30.319
11.390
1.00
28.34
A


ATOM
1383
C
THR
A
245
43.476
31.296
13.296
1.00
27.96
A


ATOM
1384
O
THR
A
245
43.212
30.907
14.434
1.00
25.46
A


ATOM
1385
N
ALA
A
246
43.486
32.576
12.938
1.00
25.22
A


ATOM
1386
CA
ALA
A
246
43.247
33.675
13.867
1.00
23.27
A


ATOM
1387
CB
ALA
A
246
42.956
34.955
13.082
1.00
22.94
A


ATOM
1388
C
ALA
A
246
42.178
33.475
14.934
1.00
21.27
A


ATOM
1389
O
ALA
A
246
42.431
33.705
16.114
1.00
20.93
A


ATOM
1390
N
GLN
A
247
40.988
33.047
14.536
1.00
19.67
A


ATOM
1391
CA
GLN
A
247
39.911
32.886
15.504
1.00
20.17
A


ATOM
1392
CB
GLN
A
247
38.608
32.535
14.779
1.00
21.89
A


ATOM
1393
CG
GLN
A
247
38.522
33.076
13.355
1.00
26.18
A


ATOM
1394
CD
GLN
A
247
37.220
33.794
13.064
1.00
27.30
A


ATOM
1395
OE1
GLN
A
247
36.172
33.447
13.605
1.00
30.13
A


ATOM
1396
NE2
GLN
A
247
37.278
34.792
12.189
1.00
28.70
A


ATOM
1397
C
GLN
A
247
40.181
31.849
16.595
1.00
19.43
A


ATOM
1398
O
GLN
A
247
39.546
31.883
17.648
1.00
18.93
A


ATOM
1399
N
TYR
A
248
41.132
30.948
16.359
1.00
18.60
A


ATOM
1400
CA
TYR
A
248
41.441
29.896
17.329
1.00
19.20
A


ATOM
1401
CB
TYR
A
248
41.333
28.529
16.642
1.00
17.53
A


ATOM
1402
CG
TYR
A
248
40.013
28.362
15.927
1.00
19.32
A


ATOM
1403
CD1
TYR
A
248
38.859
28.010
16.625
1.00
17.69
A


ATOM
1404
CE1
TYR
A
248
37.617
27.976
15.990
1.00
18.18
A


ATOM
1405
CD2
TYR
A
248
39.897
28.664
14.569
1.00
16.87
A


ATOM
1406
CE2
TYR
A
248
38.665
28.635
13.924
1.00
19.17
A


ATOM
1407
CZ
TYR
A
248
37.527
28.295
14.643
1.00
19.46
A


ATOM
1408
OH
TYR
A
248
36.299
28.311
14.023
1.00
18.98
A


ATOM
1409
C
TYR
A
248
42.810
30.039
17.993
1.00
20.42
A


ATOM
1410
O
TYR
A
248
43.208
29.191
18.792
1.00
19.19
A


ATOM
1411
N
VAL
A
249
43.523
31.114
17.673
1.00
20.20
A


ATOM
1412
CA
VAL
A
249
44.841
31.343
18.251
1.00
20.91
A


ATOM
1413
CB
VAL
A
249
45.542
32.532
17.570
1.00
21.18
A


ATOM
1414
CG1
VAL
A
249
46.821
32.896
18.317
1.00
22.45
A


ATOM
1415
CG2
VAL
A
249
45.862
32.170
16.139
1.00
24.01
A


ATOM
1416
C
VAL
A
249
44.764
31.606
19.750
1.00
21.52
A


ATOM
1417
O
VAL
A
249
43.915
32.368
20.216
1.00
22.72
A


ATOM
1418
N
SER
A
250
45.654
30.965
20.503
1.00
20.70
A


ATOM
1419
CA
SER
A
250
45.697
31.133
21.951
1.00
21.65
A


ATOM
1420
CB
SER
A
250
46.370
29.919
22.613
1.00
22.02
A


ATOM
1421
OG
SER
A
250
47.692
29.725
22.132
1.00
22.12
A


ATOM
1422
C
SER
A
250
46.476
32.402
22.280
1.00
22.13
A


ATOM
1423
O
SER
A
250
47.332
32.828
21.511
1.00
22.77
A


ATOM
1424
N
PRO
A
251
46.180
33.029
23.425
1.00
22.23
A


ATOM
1425
CD
PRO
A
251
45.163
32.684
24.433
1.00
22.97
A


ATOM
1426
CA
PRO
A
251
46.893
34.254
23.800
1.00
22.52
A


ATOM
1427
CB
PRO
A
251
46.233
34.650
25.127
1.00
23.06
A


ATOM
1428
CG
PRO
A
251
45.726
33.329
25.676
1.00
22.55
A


ATOM
1429
C
PRO
A
251
48.414
34.115
23.907
1.00
22.15
A


ATOM
1430
O
PRO
A
251
49.143
35.047
23.563
1.00
22.62
A


ATOM
1431
N
GLU
A
252
48.901
32.966
24.367
1.00
20.69
A


ATOM
1432
CA
GLU
A
252
50.347
32.772
24.500
1.00
21.40
A


ATOM
1433
CB
GLU
A
252
50.673
31.382
25.071
1.00
20.59
A


ATOM
1434
CG
GLU
A
252
49.993
30.232
24.352
1.00
21.91
A


ATOM
1435
CD
GLU
A
252
48.691
29.822
25.014
1.00
21.51
A


ATOM
1436
OE1
GLU
A
252
47.989
30.707
25.550
1.00
21.46
A


ATOM
1437
OE2
GLU
A
252
48.367
28.613
24.993
1.00
20.23
A


ATOM
1438
C
GLU
A
252
51.071
32.970
23.167
1.00
22.99
A


ATOM
1439
O
GLU
A
252
52.191
33.480
23.136
1.00
23.17
A


ATOM
1440
N
LEU
A
253
50.441
32.576
22.064
1.00
23.00
A


ATOM
1441
CA
LEU
A
253
51.068
32.753
20.758
1.00
25.62
A


ATOM
1442
CB
LEU
A
253
50.277
32.029
19.669
1.00
26.75
A


ATOM
1443
CG
LEU
A
253
50.743
30.620
19.296
1.00
31.87
A


ATOM
1444
CD1
LEU
A
253
50.433
29.651
20.422
1.00
31.81
A


ATOM
1445
CD2
LEU
A
253
50.044
30.179
18.015
1.00
31.86
A


ATOM
1446
C
LEU
A
253
51.201
34.228
20.371
1.00
26.94
A


ATOM
1447
O
LEU
A
253
52.107
34.601
19.626
1.00
27.09
A


ATOM
1448
N
LEU
A
254
50.297
35.059
20.877
1.00
25.83
A


ATOM
1449
CA
LEU
A
254
50.297
36.485
20.564
1.00
27.26
A


ATOM
1450
CB
LEU
A
254
48.858
37.006
20.564
1.00
25.84
A


ATOM
1451
CG
LEU
A
254
47.882
36.290
19.621
1.00
24.69
A


ATOM
1452
CD1
LEU
A
254
46.459
36.724
19.932
1.00
23.64
A


ATOM
1453
CD2
LEU
A
254
48.236
36.597
18.177
1.00
24.24
A


ATOM
1454
C
LEU
A
254
51.134
37.314
21.537
1.00
30.62
A


ATOM
1455
O
LEU
A
254
51.633
38.383
21.187
1.00
32.35
A


ATOM
1456
N
THR
A
255
51.292
36.821
22.758
1.00
32.47
A


ATOM
1457
CA
THR
A
255
52.056
37.547
23.759
1.00
36.70
A


ATOM
1458
CB
THR
A
255
51.368
37.478
25.127
1.00
34.51
A


ATOM
1459
OG1
THR
A
255
51.188
36.106
25.494
1.00
35.49
A


ATOM
1460
CG2
THR
A
255
50.013
38.166
25.077
1.00
33.40
A


ATOM
1461
C
THR
A
255
53.477
37.035
23.910
1.00
40.09
A


ATOM
1462
O
THR
A
255
54.430
37.793
23.772
1.00
43.69
A


ATOM
1463
N
GLU
A
256
53.617
35.747
24.189
1.00
44.77
A


ATOM
1464
CA
GLU
A
256
54.932
35.144
24.382
1.00
49.15
A


ATOM
1465
CB
GLU
A
256
54.866
34.143
25.534
1.00
51.24
A


ATOM
1466
CG
GLU
A
256
54.514
34.786
26.862
1.00
56.03
A


ATOM
1467
CD
GLU
A
256
54.053
33.780
27.893
1.00
58.83
A


ATOM
1468
OE1
GLU
A
256
54.766
32.776
28.107
1.00
62.13
A


ATOM
1469
OE2
GLU
A
256
52.979
33.996
28.494
1.00
60.34
A


ATOM
1470
C
GLU
A
256
55.475
34.456
23.137
1.00
50.09
A


ATOM
1471
O
GLU
A
256
56.616
33.995
23.127
1.00
50.42
A


ATOM
1472
N
LYS
A
257
54.658
34.389
22.090
1.00
51.21
A


ATOM
1473
CA
LYS
A
257
55.064
33.746
20.845
1.00
51.22
A


ATOM
1474
CB
LYS
A
257
56.244
34.502
20.227
1.00
53.28
A


ATOM
1475
CG
LYS
A
257
56.558
34.125
18.790
1.00
55.19
A


ATOM
1476
CD
LYS
A
257
57.709
34.961
18.253
1.00
57.52
A


ATOM
1477
CE
LYS
A
257
57.952
34.694
16.777
1.00
58.52
A


ATOM
1478
NZ
LYS
A
257
58.290
33.268
16.515
1.00
60.88
A


ATOM
1479
C
LYS
A
257
55.467
32.302
21.138
1.00
50.74
A


ATOM
1480
O
LYS
A
257
56.432
31.790
20.577
1.00
52.26
A


ATOM
1481
N
SER
A
258
54.721
31.654
22.027
1.00
48.07
A


ATOM
1482
CA
SER
A
258
54.999
30.273
22.402
1.00
46.87
A


ATOM
1483
CB
SER
A
258
55.590
30.229
23.812
1.00
48.88
A


ATOM
1484
OG
SER
A
258
54.741
30.892
24.734
1.00
53.14
A


ATOM
1485
C
SER
A
258
53.735
29.415
22.342
1.00
44.07
A


ATOM
1486
O
SER
A
258
52.617
29.932
22.417
1.00
44.17
A


ATOM
1487
N
ALA
A
259
53.917
28.105
22.204
1.00
38.30
A


ATOM
1488
CA
ALA
A
259
52.793
27.180
22.127
1.00
34.73
A


ATOM
1489
CB
ALA
A
259
52.551
26.779
20.684
1.00
34.16
A


ATOM
1490
C
ALA
A
259
53.042
25.940
22.977
1.00
32.34
A


ATOM
1491
O
ALA
A
259
54.172
25.459
23.086
1.00
31.81
A


ATOM
1492
N
CYS
A
260
51.975
25.428
23.579
1.00
28.58
A


ATOM
1493
CA
CYS
A
260
52.056
24.244
24.425
1.00
26.27
A


ATOM
1494
CB
CYS
A
260
52.183
24.654
25.892
1.00
26.53
A


ATOM
1495
SG
CYS
A
260
50.846
25.739
26.469
1.00
32.91
A


ATOM
1496
C
CYS
A
260
50.786
23.435
24.224
1.00
22.83
A


ATOM
1497
O
CYS
A
260
49.892
23.856
23.495
1.00
22.14
A


ATOM
1498
N
LYS
A
261
50.706
22.277
24.868
1.00
20.02
A


ATOM
1499
CA
LYS
A
261
49.526
21.434
24.744
1.00
20.65
A


ATOM
1500
CB
LYS
A
261
49.619
20.243
25.696
1.00
23.28
A


ATOM
1501
CG
LYS
A
261
50.716
19.253
25.347
1.00
27.44
A


ATOM
1502
CD
LYS
A
261
50.732
18.117
26.350
1.00
29.98
A


ATOM
1503
CE
LYS
A
261
51.922
17.203
26.134
1.00
32.34
A


ATOM
1504
NZ
LYS
A
261
51.940
16.121
27.153
1.00
33.28
A


ATOM
1505
C
LYS
A
261
48.268
22.229
25.062
1.00
19.20
A


ATOM
1506
O
LYS
A
261
47.253
22.092
24.387
1.00
18.08
A


ATOM
1507
N
SER
A
262
48.358
23.068
26.089
1.00
16.92
A


ATOM
1508
CA
SER
A
262
47.235
23.883
26.534
1.00
18.13
A


ATOM
1509
CB
SER
A
262
47.644
24.698
27.770
1.00
18.27
A


ATOM
1510
OG
SER
A
262
46.517
25.258
28.421
1.00
22.53
A


ATOM
1511
C
SER
A
262
46.736
24.811
25.424
1.00
16.77
A


ATOM
1512
O
SER
A
262
45.591
25.254
25.450
1.00
15.69
A


ATOM
1513
N
SER
A
263
47.595
25.118
24.456
1.00
16.44
A


ATOM
1514
CA
SER
A
263
47.175
25.970
23.347
1.00
16.89
A


ATOM
1515
CB
SER
A
263
48.340
26.228
22.382
1.00
18.49
A


ATOM
1516
OG
SER
A
263
49.402
26.909
23.031
1.00
22.10
A


ATOM
1517
C
SER
A
263
46.040
25.257
22.612
1.00
17.79
A


ATOM
1518
O
SER
A
263
45.099
25.898
22.148
1.00
17.57
A


ATOM
1519
N
ASP
A
264
46.119
23.928
22.517
1.00
16.30
A


ATOM
1520
CA
ASP
A
264
45.069
23.166
21.836
1.00
16.72
A


ATOM
1521
CB
ASP
A
264
45.483
21.704
21.620
1.00
15.92
A


ATOM
1522
CG
ASP
A
264
46.544
21.539
20.548
1.00
17.93
A


ATOM
1523
OD1
ASP
A
264
46.642
22.412
19.661
1.00
16.78
A


ATOM
1524
OD2
ASP
A
264
47.265
20.515
20.579
1.00
16.64
A


ATOM
1525
C
ASP
A
264
43.773
23.194
22.646
1.00
17.67
A


ATOM
1526
O
ASP
A
264
42.681
23.197
22.076
1.00
18.27
A


ATOM
1527
N
LEU
A
265
43.898
23.205
23.974
1.00
15.49
A


ATOM
1528
CA
LEU
A
265
42.730
23.232
24.849
1.00
14.75
A


ATOM
1529
CB
LEU
A
265
43.147
23.038
26.313
1.00
11.38
A


ATOM
1530
CG
LEU
A
265
43.711
21.641
26.621
1.00
14.04
A


ATOM
1531
CD1
LEU
A
265
44.249
21.579
28.052
1.00
13.96
A


ATOM
1532
CD2
LEU
A
265
42.619
20.603
26.416
1.00
11.62
A


ATOM
1533
C
LEU
A
265
41.999
24.557
24.675
1.00
15.13
A


ATOM
1534
O
LEU
A
265
40.777
24.620
24.785
1.00
16.75
A


ATOM
1535
N
TRP
A
266
42.746
25.622
24.405
1.00
16.08
A


ATOM
1536
CA
TRP
A
266
42.118
26.918
24.184
1.00
16.96
A


ATOM
1537
CB
TRP
A
266
43.176
28.015
24.023
1.00
17.28
A


ATOM
1538
CG
TRP
A
266
42.618
29.326
23.521
1.00
20.54
A


ATOM
1539
CD2
TRP
A
266
42.313
30.490
24.301
1.00
20.07
A


ATOM
1540
CE2
TRP
A
266
41.782
31.459
23.417
1.00
20.46
A


ATOM
1541
CE3
TRP
A
266
42.435
30.810
25.660
1.00
20.68
A


ATOM
1542
CD1
TRP
A
266
42.270
29.631
22.231
1.00
19.53
A


ATOM
1543
NE1
TRP
A
266
41.769
30.908
22.163
1.00
19.61
A


ATOM
1544
CZ2
TRP
A
266
41.372
32.727
23.850
1.00
20.90
A


ATOM
1545
CZ3
TRP
A
266
42.026
32.073
26.091
1.00
19.45
A


ATOM
1546
CH2
TRP
A
266
41.501
33.015
25.185
1.00
20.71
A


ATOM
1547
C
TRP
A
266
41.284
26.795
22.913
1.00
17.22
A


ATOM
1548
O
TRP
A
266
40.139
27.240
22.863
1.00
18.03
A


ATOM
1549
N
ALA
A
267
41.863
26.181
21.886
1.00
17.50
A


ATOM
1550
CA
ALA
A
267
41.155
25.990
20.626
1.00
16.16
A


ATOM
1551
CB
ALA
A
267
42.050
25.290
19.621
1.00
14.28
A


ATOM
1552
C
ALA
A
267
39.901
25.159
20.891
1.00
16.28
A


ATOM
1553
O
ALA
A
267
38.835
25.436
20.346
1.00
16.46
A


ATOM
1554
N
LEU
A
268
40.031
24.144
21.739
1.00
16.57
A


ATOM
1555
CA
LEU
A
268
38.890
23.299
22.084
1.00
17.03
A


ATOM
1556
CB
LEU
A
268
39.292
22.260
23.139
1.00
15.35
A


ATOM
1557
CG
LEU
A
268
38.158
21.429
23.754
1.00
19.00
A


ATOM
1558
CD1
LEU
A
268
37.505
20.578
22.678
1.00
16.17
A


ATOM
1559
CD2
LEU
A
268
38.718
20.537
24.881
1.00
17.49
A


ATOM
1560
C
LEU
A
268
37.766
24.179
22.628
1.00
15.72
A


ATOM
1561
O
LEU
A
268
36.603
24.031
22.247
1.00
15.28
A


ATOM
1562
N
GLY
A
269
38.119
25.099
23.520
1.00
14.34
A


ATOM
1563
CA
GLY
A
269
37.124
25.989
24.092
1.00
13.39
A


ATOM
1564
C
GLY
A
269
36.406
26.808
23.031
1.00
14.94
A


ATOM
1565
O
GLY
A
269
35.193
27.014
23.114
1.00
14.76
A


ATOM
1566
N
CYS
A
270
37.146
27.279
22.030
1.00
13.86
A


ATOM
1567
CA
CYS
A
270
36.539
28.061
20.958
1.00
16.80
A


ATOM
1568
CB
CYS
A
270
37.611
28.634
20.023
1.00
15.97
A


ATOM
1569
SG
CYS
A
270
38.751
29.810
20.780
1.00
20.48
A


ATOM
1570
C
CYS
A
270
35.598
27.175
20.140
1.00
17.50
A


ATOM
1571
O
CYS
A
270
34.516
27.604
19.741
1.00
18.38
A


ATOM
1572
N
ILE
A
271
36.022
25.939
19.887
1.00
16.99
A


ATOM
1573
CA
ILE
A
271
35.221
25.004
19.104
1.00
16.66
A


ATOM
1574
CB
ILE
A
271
36.038
23.741
18.778
1.00
16.53
A


ATOM
1575
CG2
ILE
A
271
35.155
22.694
18.102
1.00
16.34
A


ATOM
1576
CG1
ILE
A
271
37.222
24.129
17.882
1.00
15.59
A


ATOM
1577
CD1
ILE
A
271
38.239
23.018
17.690
1.00
14.88
A


ATOM
1578
C
ILE
A
271
33.920
24.626
19.809
1.00
16.74
A


ATOM
1579
O
ILE
A
271
32.865
24.576
19.179
1.00
17.12
A


ATOM
1580
N
ILE
A
272
33.990
24.357
21.111
1.00
16.13
A


ATOM
1581
CA
ILE
A
272
32.785
24.021
21.862
1.00
18.30
A


ATOM
1582
CB
ILE
A
272
33.097
23.747
23.346
1.00
17.77
A


ATOM
1583
CG2
ILE
A
272
31.796
23.666
24.152
1.00
17.96
A


ATOM
1584
CG1
ILE
A
272
33.877
22.437
23.481
1.00
19.55
A


ATOM
1585
CD1
ILE
A
272
34.446
22.217
24.886
1.00
18.64
A


ATOM
1586
C
ILE
A
272
31.824
25.207
21.776
1.00
19.51
A


ATOM
1587
O
ILE
A
272
30.624
25.037
21.554
1.00
20.44
A


ATOM
1588
N
TYR
A
273
32.362
26.409
21.947
1.00
18.52
A


ATOM
1589
CA
TYR
A
273
31.553
27.615
21.881
1.00
20.48
A


ATOM
1590
CB
TYR
A
273
32.418
28.847
22.162
1.00
18.98
A


ATOM
1591
CG
TYR
A
273
31.663
30.161
22.125
1.00
20.26
A


ATOM
1592
CD1
TYR
A
273
31.229
30.709
20.916
1.00
20.67
A


ATOM
1593
CE1
TYR
A
273
30.536
31.917
20.880
1.00
20.98
A


ATOM
1594
CD2
TYR
A
273
31.383
30.857
23.302
1.00
19.82
A


ATOM
1595
CE2
TYR
A
273
30.691
32.062
23.280
1.00
20.62
A


ATOM
1596
CZ
TYR
A
273
30.271
32.587
22.067
1.00
21.15
A


ATOM
1597
OH
TYR
A
273
29.588
33.776
22.049
1.00
21.86
A


ATOM
1598
C
TYR
A
273
30.902
27.730
20.507
1.00
21.54
A


ATOM
1599
O
TYR
A
273
29.719
28.049
20.401
1.00
22.80
A


ATOM
1600
N
GLN
A
274
31.676
27.454
19.461
1.00
21.05
A


ATOM
1601
CA
GLN
A
274
31.176
27.538
18.095
1.00
21.48
A


ATOM
1602
CB
GLN
A
274
32.323
27.341
17.097
1.00
21.41
A


ATOM
1603
CG
GLN
A
274
31.934
27.596
15.645
1.00
23.15
A


ATOM
1604
CD
GLN
A
274
33.131
27.588
14.706
1.00
24.80
A


ATOM
1605
OE1
GLN
A
274
34.276
27.446
15.139
1.00
22.51
A


ATOM
1606
NE2
GLN
A
274
32.870
27.750
13.413
1.00
22.96
A


ATOM
1607
C
GLN
A
274
30.076
26.517
17.828
1.00
21.51
A


ATOM
1608
O
GLN
A
274
29.123
26.806
17.108
1.00
20.50
A


ATOM
1609
N
LEU
A
275
30.207
25.324
18.403
1.00
21.44
A


ATOM
1610
CA
LEU
A
275
29.196
24.282
18.208
1.00
20.95
A


ATOM
1611
CB
LEU
A
275
29.645
22.958
18.846
1.00
19.11
A


ATOM
1612
CG
LEU
A
275
30.775
22.182
18.159
1.00
21.43
A


ATOM
1613
CD1
LEU
A
275
31.118
20.936
18.963
1.00
17.64
A


ATOM
1614
CD2
LEU
A
275
30.342
21.795
16.754
1.00
20.34
A


ATOM
1615
C
LEU
A
275
27.860
24.697
18.815
1.00
21.32
A


ATOM
1616
O
LEU
A
275
26.802
24.461
18.229
1.00
19.75
A


ATOM
1617
N
VAL
A
276
27.921
25.322
19.987
1.00
19.10
A


ATOM
1618
CA
VAL
A
276
26.724
25.750
20.702
1.00
22.47
A


ATOM
1619
CB
VAL
A
276
27.011
25.882
22.217
1.00
20.87
A


ATOM
1620
CG1
VAL
A
276
25.742
26.291
22.957
1.00
19.68
A


ATOM
1621
CG2
VAL
A
276
27.550
24.558
22.766
1.00
19.43
A


ATOM
1622
C
VAL
A
276
26.127
27.075
20.211
1.00
23.89
A


ATOM
1623
O
VAL
A
276
24.910
27.199
20.070
1.00
24.90
A


ATOM
1624
N
ALA
A
277
26.983
28.062
19.965
1.00
24.56
A


ATOM
1625
CA
ALA
A
277
26.533
29.374
19.518
1.00
24.72
A


ATOM
1626
CB
ALA
A
277
27.504
30.444
19.999
1.00
24.36
A


ATOM
1627
C
ALA
A
277
26.378
29.458
18.005
1.00
25.76
A


ATOM
1628
O
ALA
A
277
25.577
30.242
17.502
1.00
26.39
A


ATOM
1629
N
GLY
A
278
27.142
28.651
17.280
1.00
25.13
A


ATOM
1630
CA
GLY
A
278
27.062
28.673
15.834
1.00
25.58
A


ATOM
1631
C
GLY
A
278
28.163
29.524
15.231
1.00
26.50
A


ATOM
1632
O
GLY
A
278
28.374
29.510
14.015
1.00
28.17
A


ATOM
1633
N
LEU
A
279
28.866
30.262
16.086
1.00
24.44
A


ATOM
1634
CA
LEU
A
279
29.962
31.130
15.656
1.00
25.21
A


ATOM
1635
CB
LEU
A
279
29.468
32.575
15.500
1.00
25.78
A


ATOM
1636
CG
LEU
A
279
28.364
32.899
14.490
1.00
28.17
A


ATOM
1637
CD1
LEU
A
279
27.922
34.344
14.684
1.00
26.60
A


ATOM
1638
CD2
LEU
A
279
28.862
32.670
13.071
1.00
26.52
A


ATOM
1639
C
LEU
A
279
31.093
31.116
16.687
1.00
23.47
A


ATOM
1640
O
LEU
A
279
30.848
30.994
17.882
1.00
24.44
A


ATOM
1641
N
PRO
A
280
32.349
31.239
16.236
1.00
23.35
A


ATOM
1642
CD
PRO
A
280
32.831
31.404
14.855
1.00
22.26
A


ATOM
1643
CA
PRO
A
280
33.464
31.239
17.189
1.00
23.81
A


ATOM
1644
CB
PRO
A
280
34.692
31.293
16.282
1.00
23.24
A


ATOM
1645
CG
PRO
A
280
34.189
32.020
15.073
1.00
24.89
A


ATOM
1646
C
PRO
A
280
33.353
32.444
18.137
1.00
22.69
A


ATOM
1647
O
PRO
A
280
32.750
33.457
17.788
1.00
22.11
A


ATOM
1648
N
PRO
A
281
33.939
32.344
19.345
1.00
23.06
A


ATOM
1649
CD
PRO
A
281
34.810
31.223
19.734
1.00
21.37
A


ATOM
1650
CA
PRO
A
281
33.935
33.375
20.395
1.00
23.67
A


ATOM
1651
CB
PRO
A
281
34.781
32.751
21.509
1.00
24.89
A


ATOM
1652
CG
PRO
A
281
34.749
31.287
21.219
1.00
25.24
A


ATOM
1653
C
PRO
A
281
34.481
34.752
20.017
1.00
23.75
A


ATOM
1654
O
PRO
A
281
33.869
35.781
20.317
1.00
21.02
A


ATOM
1655
N
PHE
A
282
35.644
34.763
19.379
1.00
22.17
A


ATOM
1656
CA
PHE
A
282
36.293
36.007
18.998
1.00
23.16
A


ATOM
1657
CB
PHE
A
282
37.765
35.943
19.406
1.00
21.01
A


ATOM
1658
CG
PHE
A
282
37.975
35.482
20.822
1.00
22.66
A


ATOM
1659
CD1
PHE
A
282
37.806
36.361
21.888
1.00
20.06
A


ATOM
1660
CD2
PHE
A
282
38.291
34.151
21.093
1.00
20.72
A


ATOM
1661
CE1
PHE
A
282
37.947
35.921
23.206
1.00
22.66
A


ATOM
1662
CE2
PHE
A
282
38.433
33.702
22.405
1.00
20.97
A


ATOM
1663
CZ
PHE
A
282
38.261
34.590
23.466
1.00
19.58
A


ATOM
1664
C
PHE
A
282
36.169
36.263
17.503
1.00
24.39
A


ATOM
1665
O
PHE
A
282
36.802
35.585
16.694
1.00
25.80
A


ATOM
1666
N
ARG
A
283
35.355
37.248
17.142
1.00
24.99
A


ATOM
1667
CA
ARG
A
283
35.141
37.594
15.741
1.00
26.33
A


ATOM
1668
CB
ARG
A
283
33.721
37.209
15.316
1.00
28.91
A


ATOM
1669
CG
ARG
A
283
33.293
35.808
15.724
1.00
30.27
A


ATOM
1670
CD
ARG
A
283
31.904
35.493
15.188
1.00
33.36
A


ATOM
1671
NE
ARG
A
283
30.890
36.392
15.733
1.00
32.76
A


ATOM
1672
CZ
ARG
A
283
30.372
36.287
16.952
1.00
34.79
A


ATOM
1673
NH1
ARG
A
283
30.767
35.317
17.768
1.00
35.77
A


ATOM
1674
NH2
ARG
A
283
29.458
37.156
17.359
1.00
36.12
A


ATOM
1675
C
ARG
A
283
35.328
39.096
15.544
1.00
26.47
A


ATOM
1676
O
ARG
A
283
35.029
39.888
16.438
1.00
26.28
A


ATOM
1677
N
ALA
A
284
35.818
39.486
14.373
1.00
26.70
A


ATOM
1678
CA
ALA
A
284
36.033
40.899
14.079
1.00
27.84
A


ATOM
1679
CB
ALA
A
284
37.188
41.442
14.914
1.00
26.24
A


ATOM
1680
C
ALA
A
284
36.327
41.077
12.602
1.00
28.35
A


ATOM
1681
O
ALA
A
284
36.560
40.101
11.891
1.00
29.91
A


ATOM
1682
N
GLY
A
285
36.332
42.329
12.153
1.00
29.29
A


ATOM
1683
CA
GLY
A
285
36.577
42.631
10.753
1.00
29.52
A


ATOM
1684
C
GLY
A
285
37.893
42.156
10.168
1.00
30.12
A


ATOM
1685
O
GLY
A
285
37.974
41.862
8.976
1.00
30.60
A


ATOM
1686
N
ASN
A
286
38.939
42.097
10.983
1.00
28.49
A


ATOM
1687
CA
ASN
A
286
40.231
41.644
10.489
1.00
26.71
A


ATOM
1688
CB
ASN
A
286
41.050
42.825
9.945
1.00
26.11
A


ATOM
1689
CG
ASN
A
286
41.310
43.900
10.990
1.00
27.83
A


ATOM
1690
OD1
ASN
A
286
41.877
43.631
12.049
1.00
27.84
A


ATOM
1691
ND2
ASN
A
286
40.908
45.131
10.685
1.00
25.95
A


ATOM
1692
C
ASN
A
286
40.997
40.924
11.584
1.00
26.03
A


ATOM
1693
O
ASN
A
286
40.540
40.851
12.723
1.00
25.66
A


ATOM
1694
N
GLU
A
287
42.162
40.391
11.239
1.00
24.81
A


ATOM
1695
CA
GLU
A
287
42.965
39.662
12.206
1.00
27.59
A


ATOM
1696
CB
GLU
A
287
44.145
38.985
11.510
1.00
30.17
A


ATOM
1697
CG
GLU
A
287
43.776
37.632
10.931
1.00
38.21
A


ATOM
1698
CD
GLU
A
287
44.900
36.998
10.140
1.00
41.86
A


ATOM
1699
OE1
GLU
A
287
46.061
37.036
10.608
1.00
43.08
A


ATOM
1700
OE2
GLU
A
287
44.612
36.449
9.052
1.00
45.22
A


ATOM
1701
C
GLU
A
287
43.459
40.485
13.383
1.00
25.05
A


ATOM
1702
O
GLU
A
287
43.382
40.030
14.521
1.00
26.41
A


ATOM
1703
N
TYR
A
288
43.966
41.685
13.122
1.00
23.04
A


ATOM
1704
CA
TYR
A
288
44.460
42.528
14.205
1.00
22.34
A


ATOM
1705
CB
TYR
A
288
44.867
43.913
13.691
1.00
21.07
A


ATOM
1706
CG
TYR
A
288
45.275
44.858
14.805
1.00
21.07
A


ATOM
1707
CD1
TYR
A
288
46.533
44.762
15.405
1.00
21.23
A


ATOM
1708
CE1
TYR
A
288
46.891
45.588
16.475
1.00
20.43
A


ATOM
1709
CD2
TYR
A
288
44.380
45.809
15.302
1.00
22.32
A


ATOM
1710
CE2
TYR
A
288
44.725
46.637
16.373
1.00
23.28
A


ATOM
1711
CZ
TYR
A
288
45.981
46.518
16.953
1.00
22.96
A


ATOM
1712
OH
TYR
A
288
46.316
47.313
18.024
1.00
23.18
A


ATOM
1713
C
TYR
A
288
43.402
42.698
15.288
1.00
21.38
A


ATOM
1714
O
TYR
A
288
43.710
42.616
16.473
1.00
22.09
A


ATOM
1715
N
LEU
A
289
42.159
42.939
14.874
1.00
21.88
A


ATOM
1716
CA
LEU
A
289
41.055
43.130
15.811
1.00
21.98
A


ATOM
1717
CB
LEU
A
289
39.821
43.673
15.078
1.00
22.90
A


ATOM
1718
CG
LEU
A
289
39.896
45.130
14.601
1.00
26.52
A


ATOM
1719
CD1
LEU
A
289
38.706
45.436
13.696
1.00
26.55
A


ATOM
1720
CD2
LEU
A
289
39.914
46.071
15.807
1.00
23.13
A


ATOM
1721
C
LEU
A
289
40.686
41.849
16.560
1.00
21.24
A


ATOM
1722
O
LEU
A
289
40.256
41.897
17.715
1.00
20.72
A


ATOM
1723
N
ILE
A
290
40.843
40.708
15.900
1.00
19.62
A


ATOM
1724
CA
ILE
A
290
40.538
39.433
16.533
1.00
18.54
A


ATOM
1725
CB
ILE
A
290
40.560
38.281
15.509
1.00
18.52
A


ATOM
1726
CG2
ILE
A
290
40.503
36.934
16.234
1.00
17.63
A


ATOM
1727
CG1
ILE
A
290
39.378
38.429
14.545
1.00
18.88
A


ATOM
1728
CD1
ILE
A
290
39.421
37.483
13.357
1.00
19.81
A


ATOM
1729
C
ILE
A
290
41.578
39.167
17.618
1.00
19.09
A


ATOM
1730
O
ILE
A
290
41.236
38.788
18.737
1.00
18.20
A


ATOM
1731
N
PHE
A
291
42.849
39.376
17.286
1.00
18.76
A


ATOM
1732
CA
PHE
A
291
43.925
39.156
18.247
1.00
20.75
A


ATOM
1733
CB
PHE
A
291
45.286
39.434
17.606
1.00
20.71
A


ATOM
1734
CG
PHE
A
291
45.644
38.480
16.503
1.00
22.92
A


ATOM
1735
CD1
PHE
A
291
45.065
37.214
16.443
1.00
22.98
A


ATOM
1736
CD2
PHE
A
291
46.588
38.830
15.543
1.00
22.91
A


ATOM
1737
CE1
PHE
A
291
45.423
36.310
15.440
1.00
24.51
A


ATOM
1738
CE2
PHE
A
291
46.954
37.931
14.535
1.00
25.54
A


ATOM
1739
CZ
PHE
A
291
46.370
36.670
14.485
1.00
23.29
A


ATOM
1740
C
PHE
A
291
43.739
40.061
19.451
1.00
21.72
A


ATOM
1741
O
PHE
A
291
43.992
39.671
20.593
1.00
22.32
A


ATOM
1742
N
GLN
A
292
43.284
41.275
19.178
1.00
23.27
A


ATOM
1743
CA
GLN
A
292
43.055
42.264
20.216
1.00
24.01
A


ATOM
1744
CB
GLN
A
292
42.574
43.559
19.562
1.00
25.77
A


ATOM
1745
CG
GLN
A
292
42.577
44.773
20.447
1.00
28.45
A


ATOM
1746
CD
GLN
A
292
42.469
46.057
19.638
1.00
29.83
A


ATOM
1747
OE1
GLN
A
292
41.520
46.244
18.872
1.00
27.16
A


ATOM
1748
NE2
GLN
A
292
43.449
46.944
19.799
1.00
27.61
A


ATOM
1749
C
GLN
A
292
42.018
41.733
21.204
1.00
22.97
A


ATOM
1750
O
GLN
A
292
42.200
41.832
22.415
1.00
21.64
A


ATOM
1751
N
LYS
A
293
40.937
41.154
20.687
1.00
21.82
A


ATOM
1752
CA
LYS
A
293
39.895
40.612
21.558
1.00
22.18
A


ATOM
1753
CB
LYS
A
293
38.664
40.223
20.740
1.00
22.69
A


ATOM
1754
CG
LYS
A
293
37.919
41.407
20.153
1.00
25.78
A


ATOM
1755
CD
LYS
A
293
36.651
40.961
19.429
1.00
27.88
A


ATOM
1756
CE
LYS
A
293
35.857
42.161
18.926
1.00
30.85
A


ATOM
1757
NZ
LYS
A
293
34.612
41.750
18.214
1.00
32.98
A


ATOM
1758
C
LYS
A
293
40.398
39.398
22.343
1.00
21.20
A


ATOM
1759
O
LYS
A
293
40.041
39.204
23.509
1.00
22.01
A


ATOM
1760
N
ILE
A
294
41.226
38.583
21.702
1.00
19.91
A


ATOM
1761
CA
ILE
A
294
41.774
37.394
22.347
1.00
20.28
A


ATOM
1762
CB
ILE
A
294
42.631
36.575
21.349
1.00
18.98
A


ATOM
1763
CG2
ILE
A
294
43.481
35.550
22.098
1.00
17.70
A


ATOM
1764
CG1
ILE
A
294
41.716
35.897
20.318
1.00
17.93
A


ATOM
1765
CD1
ILE
A
294
42.467
35.237
19.178
1.00
16.21
A


ATOM
1766
C
ILE
A
294
42.618
37.727
23.587
1.00
21.94
A


ATOM
1767
O
ILE
A
294
42.366
37.199
24.673
1.00
20.86
A


ATOM
1768
N
ILE
A
295
43.610
38.600
23.439
1.00
21.88
A


ATOM
1769
CA
ILE
A
295
44.461
38.934
24.582
1.00
24.25
A


ATOM
1770
CB
ILE
A
295
45.668
39.805
24.175
1.00
23.93
A


ATOM
1771
CG2
ILE
A
295
46.514
39.066
23.140
1.00
24.61
A


ATOM
1772
CG1
ILE
A
295
45.189
41.151
23.637
1.00
24.58
A


ATOM
1773
CD1
ILE
A
295
46.317
42.149
23.433
1.00
26.69
A


ATOM
1774
C
ILE
A
295
43.720
39.636
25.717
1.00
24.80
A


ATOM
1775
O
ILE
A
295
44.214
39.687
26.842
1.00
24.76
A


ATOM
1776
N
LYS
A
296
42.539
40.173
25.425
1.00
25.33
A


ATOM
1777
CA
LYS
A
296
41.743
40.853
26.444
1.00
26.80
A


ATOM
1778
CB
LYS
A
296
41.178
42.170
25.894
1.00
27.39
A


ATOM
1779
CG
LYS
A
296
42.240
43.141
25.413
1.00
31.79
A


ATOM
1780
CD
LYS
A
296
41.634
44.410
24.826
1.00
35.56
A


ATOM
1781
CE
LYS
A
296
41.009
45.283
25.900
1.00
39.29
A


ATOM
1782
NZ
LYS
A
296
40.564
46.603
25.357
1.00
41.72
A


ATOM
1783
C
LYS
A
296
40.593
39.958
26.893
1.00
25.50
A


ATOM
1784
O
LYS
A
296
39.770
40.361
27.713
1.00
24.02
A


ATOM
1785
N
LEU
A
297
40.550
38.742
26.349
1.00
25.67
A


ATOM
1786
CA
LEU
A
297
39.500
37.777
26.666
1.00
25.16
A


ATOM
1787
CB
LEU
A
297
39.632
37.285
28.111
1.00
24.80
A


ATOM
1788
CG
LEU
A
297
38.766
36.068
28.460
1.00
26.43
A


ATOM
1789
CD1
LEU
A
297
39.238
34.852
27.646
1.00
26.70
A


ATOM
1790
CD2
LEU
A
297
38.856
35.777
29.951
1.00
24.84
A


ATOM
1791
C
LEU
A
297
38.151
38.459
26.467
1.00
25.11
A


ATOM
1792
O
LEU
A
297
37.261
38.378
27.309
1.00
25.28
A


ATOM
1793
N
GLU
A
298
38.007
39.127
25.331
1.00
24.98
A


ATOM
1794
CA
GLU
A
298
36.786
39.847
25.023
1.00
25.31
A


ATOM
1795
CB
GLU
A
298
37.143
41.139
24.291
1.00
27.13
A


ATOM
1796
CG
GLU
A
298
35.991
42.092
24.108
1.00
31.28
A


ATOM
1797
CD
GLU
A
298
36.419
43.362
23.410
1.00
34.40
A


ATOM
1798
OE1
GLU
A
298
37.348
44.027
23.918
1.00
35.90
A


ATOM
1799
OE2
GLU
A
298
35.832
43.693
22.359
1.00
36.16
A


ATOM
1800
C
GLU
A
298
35.766
39.057
24.207
1.00
23.79
A


ATOM
1801
O
GLU
A
298
35.832
39.017
22.979
1.00
24.35
A


ATOM
1802
N
TYR
A
299
34.825
38.427
24.902
1.00
23.45
A


ATOM
1803
CA
TYR
A
299
33.760
37.663
24.265
1.00
23.98
A


ATOM
1804
CB
TYR
A
299
34.264
36.304
23.755
1.00
20.13
A


ATOM
1805
CG
TYR
A
299
34.348
35.233
24.828
1.00
21.17
A


ATOM
1806
CD1
TYR
A
299
35.336
35.279
25.810
1.00
19.32
A


ATOM
1807
CE1
TYR
A
299
35.389
34.332
26.826
1.00
19.30
A


ATOM
1808
CD2
TYR
A
299
33.410
34.201
24.888
1.00
18.96
A


ATOM
1809
CE2
TYR
A
299
33.456
33.243
25.907
1.00
19.41
A


ATOM
1810
CZ
TYR
A
299
34.449
33.321
26.870
1.00
18.79
A


ATOM
1811
OH
TYR
A
299
34.511
32.401
27.881
1.00
18.77
A


ATOM
1812
C
TYR
A
299
32.699
37.437
25.331
1.00
25.20
A


ATOM
1813
O
TYR
A
299
32.942
37.681
26.506
1.00
26.46
A


ATOM
1814
N
ASP
A
300
31.522
36.981
24.927
1.00
26.94
A


ATOM
1815
CA
ASP
A
300
30.467
36.710
25.891
1.00
30.60
A


ATOM
1816
CB
ASP
A
300
29.665
37.981
26.179
1.00
35.86
A


ATOM
1817
CG
ASP
A
300
29.228
38.687
24.923
1.00
42.04
A


ATOM
1818
OD1
ASP
A
300
28.450
38.088
24.149
1.00
45.98
A


ATOM
1819
OD2
ASP
A
300
29.666
39.840
24.707
1.00
45.69
A


ATOM
1820
C
ASP
A
300
29.564
35.608
25.363
1.00
29.26
A


ATOM
1821
O
ASP
A
300
29.590
35.299
24.172
1.00
28.64
A


ATOM
1822
N
PHE
A
301
28.778
35.011
26.253
1.00
28.96
A


ATOM
1823
CA
PHE
A
301
27.884
33.924
25.871
1.00
30.48
A


ATOM
1824
CB
PHE
A
301
27.818
32.854
26.968
1.00
29.17
A


ATOM
1825
CG
PHE
A
301
29.147
32.279
27.356
1.00
29.29
A


ATOM
1826
CD1
PHE
A
301
29.978
32.949
28.245
1.00
27.31
A


ATOM
1827
CD2
PHE
A
301
29.560
31.050
26.845
1.00
27.89
A


ATOM
1828
CE1
PHE
A
301
31.205
32.403
28.625
1.00
28.83
A


ATOM
1829
CE2
PHE
A
301
30.781
30.498
27.217
1.00
28.05
A


ATOM
1830
CZ
PHE
A
301
31.605
31.175
28.110
1.00
28.27
A


ATOM
1831
C
PHE
A
301
26.459
34.384
25.619
1.00
32.20
A


ATOM
1832
O
PHE
A
301
25.946
35.261
26.317
1.00
32.36
A


ATOM
1833
N
PRO
A
302
25.798
33.804
24.607
1.00
33.29
A


ATOM
1834
CD
PRO
A
302
26.313
32.943
23.529
1.00
34.04
A


ATOM
1835
CA
PRO
A
302
24.415
34.199
24.341
1.00
35.24
A


ATOM
1836
CB
PRO
A
302
24.144
33.608
22.959
1.00
34.01
A


ATOM
1837
CG
PRO
A
302
25.041
32.413
22.921
1.00
35.48
A


ATOM
1838
C
PRO
A
302
23.567
33.561
25.444
1.00
37.39
A


ATOM
1839
O
PRO
A
302
23.935
32.518
25.986
1.00
38.49
A


ATOM
1840
N
ALA
A
303
22.447
34.188
25.783
1.00
39.36
A


ATOM
1841
CA
ALA
A
303
21.572
33.692
26.843
1.00
40.65
A


ATOM
1842
CB
ALA
A
303
20.280
34.506
26.862
1.00
41.66
A


ATOM
1843
C
ALA
A
303
21.238
32.197
26.814
1.00
41.25
A


ATOM
1844
O
ALA
A
303
21.253
31.537
27.854
1.00
43.16
A


ATOM
1845
N
ALA
A
304
20.945
31.665
25.631
1.00
41.04
A


ATOM
1846
CA
ALA
A
304
20.569
30.258
25.480
1.00
40.66
A


ATOM
1847
CB
ALA
A
304
20.121
30.004
24.040
1.00
41.36
A


ATOM
1848
C
ALA
A
304
21.628
29.223
25.876
1.00
39.61
A


ATOM
1849
O
ALA
A
304
21.298
28.156
26.395
1.00
40.61
A


ATOM
1850
N
PHE
A
305
22.891
29.543
25.617
1.00
36.21
A


ATOM
1851
CA
PHE
A
305
24.022
28.662
25.909
1.00
32.08
A


ATOM
1852
CB
PHE
A
305
25.259
29.519
26.187
1.00
29.46
A


ATOM
1853
CG
PHE
A
305
26.536
28.917
25.690
1.00
28.15
A


ATOM
1854
CD1
PHE
A
305
27.146
27.875
26.377
1.00
26.20
A


ATOM
1855
CD2
PHE
A
305
27.127
29.386
24.521
1.00
27.05
A


ATOM
1856
CE1
PHE
A
305
28.330
27.308
25.908
1.00
26.92
A


ATOM
1857
CE2
PHE
A
305
28.312
28.826
24.042
1.00
26.62
A


ATOM
1858
CZ
PHE
A
305
28.914
27.786
24.737
1.00
26.61
A


ATOM
1859
C
PHE
A
305
23.811
27.664
27.057
1.00
30.09
A


ATOM
1860
O
PHE
A
305
23.518
28.051
28.187
1.00
31.51
A


ATOM
1861
N
PHE
A
306
23.964
26.378
26.758
1.00
27.01
A


ATOM
1862
CA
PHE
A
306
23.801
25.334
27.769
1.00
26.30
A


ATOM
1863
CB
PHE
A
306
24.157
23.970
27.170
1.00
25.03
A


ATOM
1864
CG
PHE
A
306
23.548
23.725
25.815
1.00
27.24
A


ATOM
1865
CD1
PHE
A
306
22.170
23.831
25.622
1.00
28.40
A


ATOM
1866
CD2
PHE
A
306
24.350
23.386
24.728
1.00
27.84
A


ATOM
1867
CE1
PHE
A
306
21.601
23.603
24.365
1.00
28.05
A


ATOM
1868
CE2
PHE
A
306
23.792
23.155
23.465
1.00
28.31
A


ATOM
1869
CZ
PHE
A
306
22.415
23.263
23.283
1.00
28.00
A


ATOM
1870
C
PHE
A
306
24.711
25.652
28.961
1.00
26.23
A


ATOM
1871
O
PHE
A
306
25.927
25.775
28.811
1.00
25.59
A


ATOM
1872
N
PRO
A
307
24.125
25.796
30.163
1.00
26.67
A


ATOM
1873
CD
PRO
A
307
22.685
25.625
30.430
1.00
27.95
A


ATOM
1874
CA
PRO
A
307
24.842
26.110
31.405
1.00
26.59
A


ATOM
1875
CB
PRO
A
307
23.795
25.832
32.481
1.00
26.14
A


ATOM
1876
CG
PRO
A
307
22.531
26.250
31.803
1.00
27.86
A


ATOM
1877
C
PRO
A
307
26.145
25.355
31.659
1.00
25.58
A


ATOM
1878
O
PRO
A
307
27.189
25.964
31.900
1.00
22.65
A


ATOM
1879
N
LYS
A
308
26.085
24.031
31.620
1.00
24.46
A


ATOM
1880
CA
LYS
A
308
27.274
23.232
31.867
1.00
23.91
A


ATOM
1881
CB
LYS
A
308
26.887
21.760
32.024
1.00
23.25
A


ATOM
1882
CG
LYS
A
308
26.062
21.532
33.285
1.00
28.49
A


ATOM
1883
CD
LYS
A
308
25.618
20.093
33.466
1.00
30.17
A


ATOM
1884
CE
LYS
A
308
24.760
19.973
34.722
1.00
33.12
A


ATOM
1885
NZ
LYS
A
308
24.122
18.636
34.860
1.00
34.13
A


ATOM
1886
C
LYS
A
308
28.314
23.426
30.769
1.00
22.84
A


ATOM
1887
O
LYS
A
308
29.514
23.411
31.042
1.00
22.46
A


ATOM
1888
N
ALA
A
309
27.861
23.621
29.534
1.00
21.59
A


ATOM
1889
CA
ALA
A
309
28.792
23.848
28.432
1.00
20.02
A


ATOM
1890
CB
ALA
A
309
28.056
23.856
27.106
1.00
18.80
A


ATOM
1891
C
ALA
A
309
29.481
25.191
28.662
1.00
21.41
A


ATOM
1892
O
ALA
A
309
30.680
25.335
28.427
1.00
21.39
A


ATOM
1893
N
ARG
A
310
28.717
26.179
29.121
1.00
21.39
A


ATOM
1894
CA
ARG
A
310
29.290
27.494
29.388
1.00
22.02
A


ATOM
1895
CB
ARG
A
310
28.213
28.479
29.854
1.00
22.39
A


ATOM
1896
CG
ARG
A
310
28.806
29.756
30.436
1.00
25.30
A


ATOM
1897
CD
ARG
A
310
27.780
30.852
30.664
1.00
28.33
A


ATOM
1898
NE
ARG
A
310
28.420
32.039
31.230
1.00
30.18
A


ATOM
1899
CZ
ARG
A
310
27.901
33.263
31.203
1.00
32.07
A


ATOM
1900
NH1
ARG
A
310
26.719
33.477
30.634
1.00
31.19
A


ATOM
1901
NH2
ARG
A
310
28.567
34.277
31.742
1.00
30.49
A


ATOM
1902
C
ARG
A
310
30.376
27.388
30.458
1.00
21.65
A


ATOM
1903
O
ARG
A
310
31.464
27.949
30.311
1.00
20.36
A


ATOM
1904
N
ASP
A
311
30.074
26.677
31.541
1.00
19.57
A


ATOM
1905
CA
ASP
A
311
31.043
26.512
32.615
1.00
20.18
A


ATOM
1906
CB
ASP
A
311
30.460
25.649
33.739
1.00
20.39
A


ATOM
1907
CG
ASP
A
311
31.439
25.446
34.881
1.00
23.35
A


ATOM
1908
OD1
ASP
A
311
32.158
24.428
34.885
1.00
24.91
A


ATOM
1909
OD2
ASP
A
311
31.500
26.312
35.776
1.00
26.96
A


ATOM
1910
C
ASP
A
311
32.322
25.877
32.073
1.00
19.73
A


ATOM
1911
O
ASP
A
311
33.422
26.289
32.439
1.00
19.30
A


ATOM
1912
N
LEU
A
312
32.179
24.891
31.188
1.00
16.32
A


ATOM
1913
CA
LEU
A
312
33.349
24.226
30.611
1.00
16.66
A


ATOM
1914
CB
LEU
A
312
32.927
23.035
29.744
1.00
16.12
A


ATOM
1915
CG
LEU
A
312
34.050
22.320
28.974
1.00
14.73
A


ATOM
1916
CD1
LEU
A
312
35.192
21.935
29.912
1.00
14.56
A


ATOM
1917
CD2
LEU
A
312
33.477
21.084
28.289
1.00
14.22
A


ATOM
1918
C
LEU
A
312
34.181
25.189
29.774
1.00
16.61
A


ATOM
1919
O
LEU
A
312
35.402
25.241
29.910
1.00
16.20
A


ATOM
1920
N
VAL
A
313
33.515
25.949
28.908
1.00
16.20
A


ATOM
1921
CA
VAL
A
313
34.207
26.907
28.058
1.00
15.37
A


ATOM
1922
CB
VAL
A
313
33.216
27.648
27.130
1.00
16.42
A


ATOM
1923
CG1
VAL
A
313
33.915
28.796
26.426
1.00
16.93
A


ATOM
1924
CG2
VAL
A
313
32.644
26.672
26.103
1.00
17.88
A


ATOM
1925
C
VAL
A
313
34.960
27.923
28.911
1.00
17.39
A


ATOM
1926
O
VAL
A
313
36.093
28.294
28.591
1.00
18.00
A


ATOM
1927
N
GLU
A
314
34.342
28.364
30.004
1.00
17.61
A


ATOM
1928
CA
GLU
A
314
34.986
29.331
30.885
1.00
20.43
A


ATOM
1929
CB
GLU
A
314
34.009
29.816
31.959
1.00
22.14
A


ATOM
1930
CG
GLU
A
314
32.800
30.550
31.396
1.00
26.52
A


ATOM
1931
CD
GLU
A
314
31.852
31.025
32.478
1.00
31.26
A


ATOM
1932
OE1
GLU
A
314
31.580
30.246
33.417
1.00
33.48
A


ATOM
1933
OE2
GLU
A
314
31.370
32.173
32.387
1.00
34.81
A


ATOM
1934
C
GLU
A
314
36.217
28.721
31.539
1.00
19.15
A


ATOM
1935
O
GLU
A
314
37.134
29.433
31.934
1.00
21.47
A


ATOM
1936
N
LYS
A
315
36.245
27.400
31.651
1.00
19.51
A


ATOM
1937
CA
LYS
A
315
37.394
26.749
32.258
1.00
19.17
A


ATOM
1938
CB
LYS
A
315
36.946
25.514
33.043
1.00
18.84
A


ATOM
1939
CG
LYS
A
315
36.280
25.885
34.368
1.00
19.62
A


ATOM
1940
CD
LYS
A
315
35.653
24.696
35.073
1.00
19.22
A


ATOM
1941
CE
LYS
A
315
35.070
25.095
36.427
1.00
21.00
A


ATOM
1942
NZ
LYS
A
315
36.119
25.552
37.381
1.00
19.53
A


ATOM
1943
C
LYS
A
315
38.452
26.393
31.218
1.00
18.96
A


ATOM
1944
O
LYS
A
315
39.511
25.873
31.561
1.00
19.85
A


ATOM
1945
N
LEU
A
316
38.164
26.691
29.950
1.00
17.08
A


ATOM
1946
CA
LEU
A
316
39.102
26.429
28.854
1.00
16.41
A


ATOM
1947
CB
LEU
A
316
38.414
25.636
27.738
1.00
13.81
A


ATOM
1948
CG
LEU
A
316
38.028
24.201
28.115
1.00
14.39
A


ATOM
1949
CD1
LEU
A
316
37.139
23.597
27.031
1.00
12.38
A


ATOM
1950
CD2
LEU
A
316
39.302
23.373
28.309
1.00
12.77
A


ATOM
1951
C
LEU
A
316
39.652
27.743
28.290
1.00
17.12
A


ATOM
1952
O
LEU
A
316
40.851
27.860
28.023
1.00
16.53
A


ATOM
1953
N
LEU
A
317
38.780
28.729
28.105
1.00
16.27
A


ATOM
1954
CA
LEU
A
317
39.228
30.022
27.596
1.00
17.52
A


ATOM
1955
CB
LEU
A
317
38.083
30.752
26.887
1.00
16.37
A


ATOM
1956
CG
LEU
A
317
37.448
29.973
25.727
1.00
18.81
A


ATOM
1957
CD1
LEU
A
317
36.415
30.851
25.018
1.00
16.47
A


ATOM
1958
CD2
LEU
A
317
38.528
29.526
24.741
1.00
17.87
A


ATOM
1959
C
LEU
A
317
39.745
30.841
28.774
1.00
18.27
A


ATOM
1960
O
LEU
A
317
39.078
31.753
29.273
1.00
18.58
A


ATOM
1961
N
VAL
A
318
40.937
30.475
29.229
1.00
18.02
A


ATOM
1962
CA
VAL
A
318
41.593
31.141
30.342
1.00
18.85
A


ATOM
1963
CB
VAL
A
318
41.846
30.153
31.500
1.00
19.91
A


ATOM
1964
CG1
VAL
A
318
42.590
30.848
32.634
1.00
20.01
A


ATOM
1965
CG2
VAL
A
318
40.520
29.584
31.990
1.00
19.44
A


ATOM
1966
C
VAL
A
318
42.923
31.657
29.811
1.00
19.67
A


ATOM
1967
O
VAL
A
318
43.690
30.902
29.208
1.00
18.26
A


ATOM
1968
N
LEU
A
319
43.197
32.939
30.028
1.00
20.07
A


ATOM
1969
CA
LEU
A
319
44.436
33.533
29.538
1.00
20.98
A


ATOM
1970
CB
LEU
A
319
44.521
35.002
29.968
1.00
21.64
A


ATOM
1971
CG
LEU
A
319
43.418
35.908
29.408
1.00
24.38
A


ATOM
1972
CD1
LEU
A
319
43.606
37.332
29.935
1.00
23.28
A


ATOM
1973
CD2
LEU
A
319
43.453
35.887
27.875
1.00
24.33
A


ATOM
1974
C
LEU
A
319
45.680
32.774
29.994
1.00
20.38
A


ATOM
1975
O
LEU
A
319
46.568
32.496
29.192
1.00
21.34
A


ATOM
1976
N
ASP
A
320
45.742
32.440
31.280
1.00
20.22
A


ATOM
1977
CA
ASP
A
320
46.879
31.707
31.833
1.00
20.90
A


ATOM
1978
CB
ASP
A
320
46.842
31.760
33.365
1.00
20.76
A


ATOM
1979
CG
ASP
A
320
48.049
31.102
34.004
1.00
21.51
A


ATOM
1980
OD1
ASP
A
320
48.669
30.226
33.367
1.00
23.46
A


ATOM
1981
OD2
ASP
A
320
48.371
31.450
35.159
1.00
23.89
A


ATOM
1982
C
ASP
A
320
46.814
30.247
31.367
1.00
20.06
A


ATOM
1983
O
ASP
A
320
45.988
29.476
31.840
1.00
20.54
A


ATOM
1984
N
ALA
A
321
47.700
29.876
30.451
1.00
20.68
A


ATOM
1985
CA
ALA
A
321
47.733
28.522
29.903
1.00
22.04
A


ATOM
1986
CB
ALA
A
321
48.860
28.411
28.881
1.00
20.75
A


ATOM
1987
C
ALA
A
321
47.858
27.400
30.940
1.00
21.62
A


ATOM
1988
O
ALA
A
321
47.482
26.259
30.665
1.00
21.99
A


ATOM
1989
N
THR
A
322
48.372
27.715
32.127
1.00
20.89
A


ATOM
1990
CA
THR
A
322
48.531
26.698
33.167
1.00
20.82
A


ATOM
1991
CB
THR
A
322
49.670
27.051
34.146
1.00
19.47
A


ATOM
1992
OG1
THR
A
322
49.341
28.253
34.848
1.00
20.19
A


ATOM
1993
CG2
THR
A
322
50.981
27.249
33.394
1.00
21.59
A


ATOM
1994
C
THR
A
322
47.264
26.498
33.983
1.00
19.55
A


ATOM
1995
O
THR
A
322
47.235
25.673
34.894
1.00
21.13
A


ATOM
1996
N
LYS
A
323
46.216
27.248
33.661
1.00
19.33
A


ATOM
1997
CA
LYS
A
323
44.962
27.122
34.392
1.00
21.20
A


ATOM
1998
CB
LYS
A
323
44.580
28.460
35.030
1.00
23.75
A


ATOM
1999
CG
LYS
A
323
45.562
28.933
36.084
1.00
28.45
A


ATOM
2000
CD
LYS
A
323
45.055
30.177
36.799
1.00
33.76
A


ATOM
2001
CE
LYS
A
323
46.087
30.678
37.802
1.00
36.15
A


ATOM
2002
NZ
LYS
A
323
46.532
29.569
38.693
1.00
37.34
A


ATOM
2003
C
LYS
A
323
43.806
26.614
33.539
1.00
20.68
A


ATOM
2004
O
LYS
A
323
42.649
26.757
33.915
1.00
20.42
A


ATOM
2005
N
ARG
A
324
44.114
26.019
32.392
1.00
19.97
A


ATOM
2006
CA
ARG
A
324
43.060
25.494
31.531
1.00
17.98
A


ATOM
2007
CB
ARG
A
324
43.461
25.609
30.061
1.00
15.95
A


ATOM
2008
CG
ARG
A
324
43.534
27.050
29.603
1.00
17.34
A


ATOM
2009
CD
ARG
A
324
43.996
27.194
28.172
1.00
19.80
A


ATOM
2010
NE
ARG
A
324
44.438
28.565
27.944
1.00
16.93
A


ATOM
2011
CZ
ARG
A
324
45.410
28.908
27.108
1.00
19.88
A


ATOM
2012
NH1
ARG
A
324
46.045
27.978
26.398
1.00
14.58
A


ATOM
2013
NH2
ARG
A
324
45.774
30.181
27.015
1.00
16.51
A


ATOM
2014
C
ARG
A
324
42.762
24.046
31.883
1.00
18.32
A


ATOM
2015
O
ARG
A
324
43.673
23.222
32.006
1.00
18.20
A


ATOM
2016
N
LEU
A
325
41.479
23.748
32.055
1.00
18.32
A


ATOM
2017
CA
LEU
A
325
41.050
22.403
32.395
1.00
17.79
A


ATOM
2018
CB
LEU
A
325
39.523
22.335
32.425
1.00
17.03
A


ATOM
2019
CG
LEU
A
325
38.896
21.125
33.116
1.00
15.91
A


ATOM
2020
CD1
LEU
A
325
39.392
21.048
34.557
1.00
15.93
A


ATOM
2021
CD2
LEU
A
325
37.375
21.255
33.084
1.00
16.56
A


ATOM
2022
C
LEU
A
325
41.599
21.433
31.356
1.00
18.68
A


ATOM
2023
O
LEU
A
325
41.347
21.586
30.157
1.00
18.28
A


ATOM
2024
N
GLY
A
326
42.354
20.439
31.821
1.00
18.18
A


ATOM
2025
CA
GLY
A
326
42.931
19.462
30.915
1.00
16.36
A


ATOM
2026
C
GLY
A
326
44.443
19.558
30.807
1.00
19.15
A


ATOM
2027
O
GLY
A
326
45.093
18.592
30.404
1.00
19.52
A


ATOM
2028
N
CYS
A
327
45.016
20.708
31.161
1.00
18.16
A


ATOM
2029
CA
CYS
A
327
46.463
20.867
31.075
1.00
19.30
A


ATOM
2030
CB
CYS
A
327
46.856
22.350
31.058
1.00
20.22
A


ATOM
2031
SG
CYS
A
327
46.782
23.200
32.649
1.00
21.97
A


ATOM
2032
C
CYS
A
327
47.169
20.157
32.228
1.00
20.22
A


ATOM
2033
O
CYS
A
327
46.561
19.828
33.246
1.00
17.92
A


ATOM
2034
N
GLU
A
328
48.463
19.933
32.053
1.00
20.51
A


ATOM
2035
CA
GLU
A
328
49.274
19.244
33.042
1.00
23.34
A


ATOM
2036
CB
GLU
A
328
50.710
19.139
32.507
1.00
28.68
A


ATOM
2037
CG
GLU
A
328
50.754
18.367
31.175
1.00
38.24
A


ATOM
2038
CD
GLU
A
328
52.067
18.500
30.414
1.00
43.23
A


ATOM
2039
OE1
GLU
A
328
52.535
19.643
30.218
1.00
46.22
A


ATOM
2040
OE2
GLU
A
328
52.618
17.459
29.991
1.00
44.90
A


ATOM
2041
C
GLU
A
328
49.234
19.876
34.435
1.00
22.11
A


ATOM
2042
O
GLU
A
328
49.147
19.161
35.437
1.00
20.27
A


ATOM
2043
N
GLU
A
329
49.276
21.204
34.506
1.00
18.40
A


ATOM
2044
CA
GLU
A
329
49.248
21.875
35.801
1.00
20.13
A


ATOM
2045
CB
GLU
A
329
49.587
23.363
35.657
1.00
20.36
A


ATOM
2046
CG
GLU
A
329
51.014
23.651
35.190
1.00
24.05
A


ATOM
2047
CD
GLU
A
329
51.191
23.518
33.688
1.00
25.93
A


ATOM
2048
OE1
GLU
A
329
50.213
23.154
32.995
1.00
26.61
A


ATOM
2049
OE2
GLU
A
329
52.311
23.781
33.198
1.00
27.19
A


ATOM
2050
C
GLU
A
329
47.890
21.718
36.480
1.00
19.36
A


ATOM
2051
O
GLU
A
329
47.775
21.879
37.694
1.00
18.74
A


ATOM
2052
N
MET
A
330
46.863
21.415
35.691
1.00
17.28
A


ATOM
2053
CA
MET
A
330
45.520
21.220
36.229
1.00
16.38
A


ATOM
2054
CB
MET
A
330
44.474
21.833
35.294
1.00
17.65
A


ATOM
2055
CG
MET
A
330
44.460
23.365
35.311
1.00
22.95
A


ATOM
2056
SD
MET
A
330
44.186
24.026
36.979
1.00
26.78
A


ATOM
2057
CZ
MET
A
330
42.435
23.712
37.186
1.00
24.69
A


ATOM
2058
C
MET
A
330
45.257
19.730
36.422
1.00
14.30
A


ATOM
2059
O
MET
A
330
44.127
19.304
36.629
1.00
15.39
A


ATOM
2060
N
GLU
A
331
46.327
18.949
36.346
1.00
15.60
A


ATOM
2061
CA
GLU
A
331
46.289
17.501
36.531
1.00
17.08
A


ATOM
2062
CB
GLU
A
331
45.607
17.155
37.862
1.00
17.00
A


ATOM
2063
CG
GLU
A
331
46.070
18.027
39.038
1.00
17.46
A


ATOM
2064
CD
GLU
A
331
47.591
18.179
39.145
1.00
20.16
A


ATOM
2065
OE1
GLU
A
331
48.034
19.073
39.896
1.00
21.39
A


ATOM
2066
OE2
GLU
A
331
48.345
17.420
38.500
1.00
18.87
A


ATOM
2067
C
GLU
A
331
45.697
16.658
35.398
1.00
17.80
A


ATOM
2068
O
GLU
A
331
45.107
15.602
35.636
1.00
20.40
A


ATOM
2069
N
GLY
A
332
45.844
17.133
34.167
1.00
16.23
A


ATOM
2070
CA
GLY
A
332
45.420
16.353
33.015
1.00
14.10
A


ATOM
2071
C
GLY
A
332
43.982
16.154
32.596
1.00
13.54
A


ATOM
2072
O
GLY
A
332
43.063
16.864
33.017
1.00
11.96
A


ATOM
2073
N
TYR
A
333
43.804
15.141
31.750
1.00
14.37
A


ATOM
2074
CA
TYR
A
333
42.510
14.806
31.182
1.00
13.56
A


ATOM
2075
CB
TYR
A
333
42.722
13.892
29.968
1.00
15.00
A


ATOM
2076
CG
TYR
A
333
43.153
14.683
28.752
1.00
16.46
A


ATOM
2077
CD1
TYR
A
333
42.206
15.172
27.849
1.00
15.29
A


ATOM
2078
CE1
TYR
A
333
42.573
16.002
26.794
1.00
13.42
A


ATOM
2079
CD2
TYR
A
333
44.490
15.039
28.561
1.00
14.91
A


ATOM
2080
CE2
TYR
A
333
44.872
15.877
27.499
1.00
14.87
A


ATOM
2081
CZ
TYR
A
333
43.902
16.353
26.626
1.00
15.61
A


ATOM
2082
OH
TYR
A
333
44.244
17.197
25.599
1.00
17.29
A


ATOM
2083
C
TYR
A
333
41.470
14.230
32.127
1.00
15.23
A


ATOM
2084
O
TYR
A
333
40.278
14.323
31.846
1.00
16.63
A


ATOM
2085
N
GLY
A
334
41.907
13.650
33.244
1.00
15.50
A


ATOM
2086
CA
GLY
A
334
40.957
13.100
34.202
1.00
15.07
A


ATOM
2087
C
GLY
A
334
39.925
14.146
34.616
1.00
16.40
A


ATOM
2088
O
GLY
A
334
38.724
13.946
34.433
1.00
15.05
A


ATOM
2089
N
PRO
A
335
40.366
15.278
35.184
1.00
14.96
A


ATOM
2090
CD
PRO
A
335
41.727
15.531
35.689
1.00
15.88
A


ATOM
2091
CA
PRO
A
335
39.444
16.339
35.606
1.00
15.29
A


ATOM
2092
CB
PRO
A
335
40.383
17.397
36.178
1.00
13.19
A


ATOM
2093
CG
PRO
A
335
41.485
16.569
36.758
1.00
13.81
A


ATOM
2094
C
PRO
A
335
38.594
16.877
34.448
1.00
15.84
A


ATOM
2095
O
PRO
A
335
37.423
17.204
34.631
1.00
14.84
A


ATOM
2096
N
LEU
A
336
39.184
16.971
33.257
1.00
16.12
A


ATOM
2097
CA
LEU
A
336
38.450
17.465
32.094
1.00
15.52
A


ATOM
2098
CB
LEU
A
336
39.396
17.653
30.898
1.00
14.39
A


ATOM
2099
CG
LEU
A
336
38.770
17.991
29.538
1.00
15.46
A


ATOM
2100
CD1
LEU
A
336
37.836
19.182
29.662
1.00
11.25
A


ATOM
2101
CD2
LEU
A
336
39.884
18.285
28.528
1.00
14.11
A


ATOM
2102
C
LEU
A
336
37.321
16.508
31.714
1.00
16.28
A


ATOM
2103
O
LEU
A
336
36.176
16.921
31.540
1.00
15.51
A


ATOM
2104
N
LYS
A
337
37.640
15.225
31.592
1.00
17.22
A


ATOM
2105
CA
LYS
A
337
36.624
14.243
31.235
1.00
17.39
A


ATOM
2106
CB
LYS
A
337
37.293
12.900
30.921
1.00
17.68
A


ATOM
2107
CG
LYS
A
337
38.170
12.994
29.676
1.00
22.31
A


ATOM
2108
CD
LYS
A
337
39.213
11.892
29.592
1.00
24.60
A


ATOM
2109
CE
LYS
A
337
38.620
10.560
29.189
1.00
24.76
A


ATOM
2110
NZ
LYS
A
337
39.710
9.560
28.997
1.00
25.05
A


ATOM
2111
C
LYS
A
337
35.577
14.096
32.342
1.00
17.33
A


ATOM
2112
O
LYS
A
337
34.456
13.652
32.090
1.00
14.42
A


ATOM
2113
N
ALA
A
338
35.928
14.500
33.559
1.00
15.83
A


ATOM
2114
CA
ALA
A
338
34.989
14.395
34.674
1.00
17.52
A


ATOM
2115
CB
ALA
A
338
35.749
14.167
35.980
1.00
19.68
A


ATOM
2116
C
ALA
A
338
34.095
15.621
34.804
1.00
18.83
A


ATOM
2117
O
ALA
A
338
33.252
15.687
35.695
1.00
18.94
A


ATOM
2118
N
HIS
A
339
34.262
16.596
33.918
1.00
19.42
A


ATOM
2119
CA
HIS
A
339
33.438
17.796
34.004
1.00
19.28
A


ATOM
2120
CB
HIS
A
339
33.865
18.819
32.949
1.00
19.20
A


ATOM
2121
CG
HIS
A
339
33.163
20.134
33.074
1.00
20.26
A


ATOM
2122
CD2
HIS
A
339
33.549
21.299
33.649
1.00
18.95
A


ATOM
2123
ND1
HIS
A
339
31.880
20.340
32.612
1.00
19.10
A


ATOM
2124
CE1
HIS
A
339
31.506
21.576
32.896
1.00
22.19
A


ATOM
2125
NE2
HIS
A
339
32.500
22.179
33.525
1.00
21.98
A


ATOM
2126
C
HIS
A
339
31.957
17.448
33.845
1.00
19.13
A


ATOM
2127
O
HIS
A
339
31.597
16.576
33.061
1.00
19.52
A


ATOM
2128
N
PRO
A
340
31.079
18.125
34.606
1.00
19.80
A


ATOM
2129
CD
PRO
A
340
31.424
19.119
35.640
1.00
19.08
A


ATOM
2130
CA
PRO
A
340
29.630
17.900
34.569
1.00
20.52
A


ATOM
2131
CB
PRO
A
340
29.091
19.058
35.396
1.00
20.74
A


ATOM
2132
CG
PRO
A
340
30.146
19.207
36.454
1.00
19.20
A


ATOM
2133
C
PRO
A
340
29.000
17.834
33.176
1.00
21.42
A


ATOM
2134
O
PRO
A
340
28.049
17.088
32.955
1.00
22.48
A


ATOM
2135
N
PHE
A
341
29.528
18.606
32.237
1.00
21.33
A


ATOM
2136
CA
PHE
A
341
28.985
18.610
30.886
1.00
21.57
A


ATOM
2137
CB
PHE
A
341
29.739
19.624
30.017
1.00
21.64
A


ATOM
2138
CG
PHE
A
341
29.207
19.740
28.613
1.00
23.18
A


ATOM
2139
CD1
PHE
A
341
27.903
20.171
28.382
1.00
22.58
A


ATOM
2140
CD2
PHE
A
341
30.013
19.431
27.522
1.00
21.95
A


ATOM
2141
CE1
PHE
A
341
27.410
20.292
27.082
1.00
23.54
A


ATOM
2142
CE2
PHE
A
341
29.533
19.548
26.220
1.00
21.83
A


ATOM
2143
CZ
PHE
A
341
28.228
19.980
25.998
1.00
23.23
A


ATOM
2144
C
PHE
A
341
29.055
17.226
30.237
1.00
21.84
A


ATOM
2145
O
PHE
A
341
28.232
16.896
29.389
1.00
20.37
A


ATOM
2146
N
PHE
A
342
30.034
16.422
30.640
1.00
20.51
A


ATOM
2147
CA
PHE
A
342
30.221
15.085
30.077
1.00
23.01
A


ATOM
2148
CB
PHE
A
342
31.710
14.809
29.850
1.00
18.00
A


ATOM
2149
CG
PHE
A
342
32.398
15.812
28.971
1.00
17.05
A


ATOM
2150
CD1
PHE
A
342
32.010
15.987
27.652
1.00
17.78
A


ATOM
2151
CD2
PHE
A
342
33.487
16.534
29.450
1.00
15.72
A


ATOM
2152
CE1
PHE
A
342
32.702
16.867
26.811
1.00
18.08
A


ATOM
2153
CE2
PHE
A
342
34.184
17.414
28.617
1.00
17.45
A


ATOM
2154
CZ
PHE
A
342
33.790
17.578
27.298
1.00
16.56
A


ATOM
2155
C
PHE
A
342
29.679
13.972
30.976
1.00
24.95
A


ATOM
2156
O
PHE
A
342
30.002
12.798
30.777
1.00
23.95
A


ATOM
2157
N
GLU
A
343
28.861
14.333
31.958
1.00
27.35
A


ATOM
2158
CA
GLU
A
343
28.325
13.349
32.897
1.00
30.28
A


ATOM
2159
CB
GLU
A
343
27.187
13.964
33.716
1.00
32.20
A


ATOM
2160
CG
GLU
A
343
26.581
12.991
34.714
1.00
39.71
A


ATOM
2161
CD
GLU
A
343
25.628
13.661
35.688
1.00
44.72
A


ATOM
2162
OE1
GLU
A
343
24.661
14.314
35.234
1.00
47.55
A


ATOM
2163
OE2
GLU
A
343
25.847
13.526
36.911
1.00
46.89
A


ATOM
2164
C
GLU
A
343
27.852
12.017
32.305
1.00
28.98
A


ATOM
2165
O
GLU
A
343
28.225
10.952
32.800
1.00
31.73
A


ATOM
2166
N
SER
A
344
27.037
12.067
31.258
1.00
26.09
A


ATOM
2167
CA
SER
A
344
26.520
10.838
30.656
1.00
28.36
A


ATOM
2168
CB
SER
A
344
25.129
11.089
30.067
1.00
28.73
A


ATOM
2169
OG
SER
A
344
25.203
11.942
28.940
1.00
30.91
A


ATOM
2170
C
SER
A
344
27.407
10.214
29.577
1.00
27.66
A


ATOM
2171
O
SER
A
344
26.987
9.281
28.900
1.00
28.66
A


ATOM
2172
N
VAL
A
345
28.627
10.715
29.419
1.00
26.75
A


ATOM
2173
CA
VAL
A
345
29.534
10.183
28.402
1.00
23.44
A


ATOM
2174
CB
VAL
A
345
30.565
11.256
27.950
1.00
23.10
A


ATOM
2175
CG1
VAL
A
345
31.589
10.631
26.995
1.00
22.24
A


ATOM
2176
CG2
VAL
A
345
29.854
12.418
27.275
1.00
20.05
A


ATOM
2177
C
VAL
A
345
30.326
8.957
28.855
1.00
24.26
A


ATOM
2178
O
VAL
A
345
30.876
8.930
29.960
1.00
22.83
A


ATOM
2179
N
THR
A
346
30.374
7.942
27.997
1.00
21.77
A


ATOM
2180
CA
THR
A
346
31.153
6.740
28.272
1.00
23.70
A


ATOM
2181
CB
THR
A
346
30.391
5.455
27.857
1.00
26.53
A


ATOM
2182
OG1
THR
A
346
29.248
5.284
28.706
1.00
29.98
A


ATOM
2183
CG2
THR
A
346
31.289
4.231
27.990
1.00
24.28
A


ATOM
2184
C
THR
A
346
32.383
6.945
27.385
1.00
23.43
A


ATOM
2185
O
THR
A
346
32.306
6.827
26.160
1.00
24.50
A


ATOM
2186
N
TRP
A
347
33.508
7.270
28.013
1.00
22.98
A


ATOM
2187
CA
TRP
A
347
34.744
7.569
27.300
1.00
23.81
A


ATOM
2188
CB
TRP
A
347
35.683
8.352
28.219
1.00
22.54
A


ATOM
2189
CG
TRP
A
347
35.128
9.658
28.693
1.00
20.61
A


ATOM
2190
CD2
TRP
A
347
35.257
10.927
28.040
1.00
19.11
A


ATOM
2191
CE2
TRP
A
347
34.581
11.881
28.838
1.00
18.39
A


ATOM
2192
CE3
TRP
A
347
35.878
11.351
26.858
1.00
18.16
A


ATOM
2193
CD1
TRP
A
347
34.397
9.883
29.828
1.00
18.35
A


ATOM
2194
NE1
TRP
A
347
34.065
11.218
29.923
1.00
19.51
A


ATOM
2195
CZ2
TRP
A
347
34.510
13.234
28.491
1.00
16.88
A


ATOM
2196
CZ3
TRP
A
347
35.808
12.701
26.511
1.00
17.23
A


ATOM
2197
CH2
TRP
A
347
35.127
13.624
27.327
1.00
18.16
A


ATOM
2198
C
TRP
A
347
35.538
6.429
26.675
1.00
25.79
A


ATOM
2199
O
TRP
A
347
36.304
6.654
25.742
1.00
24.67
A


ATOM
2200
N
ALA
A
348
35.360
5.215
27.183
1.00
27.10
A


ATOM
2201
CA
ALA
A
348
36.116
4.063
26.697
1.00
27.46
A


ATOM
2202
CB
ALA
A
348
35.899
2.869
27.636
1.00
27.09
A


ATOM
2203
C
ALA
A
348
35.895
3.620
25.256
1.00
27.18
A


ATOM
2204
O
ALA
A
348
36.830
3.148
24.613
1.00
29.41
A


ATOM
2205
N
ASN
A
349
34.682
3.769
24.735
1.00
26.55
A


ATOM
2206
CA
ASN
A
349
34.418
3.310
23.375
1.00
27.28
A


ATOM
2207
CB
ASN
A
349
33.700
1.962
23.444
1.00
29.37
A


ATOM
2208
CG
ASN
A
349
32.299
2.088
24.013
1.00
30.92
A


ATOM
2209
OD1
ASN
A
349
32.045
2.942
24.859
1.00
30.17
A


ATOM
2210
ND2
ASN
A
349
31.386
1.237
23.553
1.00
33.52
A


ATOM
2211
C
ASN
A
349
33.599
4.265
22.509
1.00
26.47
A


ATOM
2212
O
ASN
A
349
32.669
3.843
21.819
1.00
25.87
A


ATOM
2213
N
LEU
A
350
33.947
5.543
22.518
1.00
24.45
A


ATOM
2214
CA
LEU
A
350
33.203
6.510
21.721
1.00
23.14
A


ATOM
2215
CB
LEU
A
350
33.837
7.898
21.848
1.00
23.22
A


ATOM
2216
CG
LEU
A
350
33.659
8.605
23.191
1.00
21.05
A


ATOM
2217
CD1
LEU
A
350
34.646 
9.756
23.293
1.00
19.36
A


ATOM
2218
CD2
LEU
A
350
32.220
9.094
23.319
1.00
18.78
A


ATOM
2219
C
LEU
A
350
33.082
6.152
20.240
1.00
22.60
A


ATOM
2220
O
LEU
A
350
32.011
6.296
19.650
1.00
21.15
A


ATOM
2221
N
HIS
A
351
34.165
5.689
19.627
1.00
23.13
A


ATOM
2222
CA
HIS
A
351
34.089
5.387
18.204
1.00
27.83
A


ATOM
2223
CB
HIS
A
351
35.506
5.325
17.596
1.00
29.36
A


ATOM
2224
CG
HIS
A
351
36.082
3.950
17.493
1.00
32.07
A


ATOM
2225
CD2
HIS
A
351
36.611
3.128
18.431
1.00
32.39
A


ATOM
2226
ND1
HIS
A
351
36.197
3.285
16.291
1.00
33.02
A


ATOM
2227
CE1
HIS
A
351
36.775
2.113
16.493
1.00
33.58
A


ATOM
2228
NE2
HIS
A
351
37.036
1.992
17.782
1.00
31.76
A


ATOM
2229
C
HIS
A
351
33.258
4.144
17.874
1.00
28.12
A


ATOM
2230
O
HIS
A
351
33.015
3.847
16.707
1.00
29.49
A


ATOM
2231
N
GLN
A
352
32.800
3.442
18.908
1.00
29.28
A


ATOM
2232
CA
GLN
A
352
31.963
2.255
18.726
1.00
29.67
A


ATOM
2233
CB
GLN
A
352
32.366
1.145
19.694
1.00
30.56
A


ATOM
2234
CG
GLN
A
352
33.169
0.041
19.041
1.00
30.88
A


ATOM
2235
CD
GLN
A
352
34.493
−0.186
19.729
1.00
31.21
A


ATOM
2236
OE1
GLN
A
352
34.541
−0.450
20.928
1.00
30.76
A


ATOM
2237
NE2
GLN
A
352
35.578
−0.084
18.971
1.00
32.30
A


ATOM
2238
C
GLN
A
352
30.504
2.638
18.963
1.00
30.42
A


ATOM
2239
O
GLN
A
352
29.595
1.831
18.770
1.00
29.01
A


ATOM
2240
N
GLN
A
353
30.290
3.875
19.397
1.00
27.64
A


ATOM
2241
CA
GLN
A
353
28.948
4.365
19.652
1.00
27.42
A


ATOM
2242
CB
GLN
A
353
28.977
5.401
20.775
1.00
25.77
A


ATOM
2243
CG
GLN
A
353
29.408
4.837
22.115
1.00
27.34
A


ATOM
2244
CD
GLN
A
353
29.638
5.914
23.156
1.00
27.19
A


ATOM
2245
OE1
GLN
A
353
28.875
6.872
23.252
1.00
28.29
A


ATOM
2246
NE2
GLN
A
353
30.687
5.753
23.951
1.00
28.79
A


ATOM
2247
C
GLN
A
353
28.375
4.989
18.385
1.00
29.00
A


ATOM
2248
O
GLN
A
353
29.118
5.455
17.516
1.00
29.14
A


ATOM
2249
N
THR
A
354
27.053
4.984
18.276
1.00
27.31
A


ATOM
2250
CA
THR
A
354
26.390
5.568
17.119
1.00
27.85
A


ATOM
2251
CB
THR
A
354
24.991
4.941
16.904
1.00
30.69
A


ATOM
2252
OG1
THR
A
354
25.132
3.532
16.665
1.00
30.07
A


ATOM
2253
CG2
THR
A
354
24.289
5.585
15.709
1.00
29.58
A


ATOM
2254
C
THR
A
354
26.244
7.062
17.376
1.00
26.85
A


ATOM
2255
O
THR
A
354
25.592
7.475
18.329
1.00
25.77
A


ATOM
2256
N
PRO
A
355
26.867
7.898
16.533
1.00
27.22
A


ATOM
2257
CD
PRO
A
355
27.792
7.588
15.431
1.00
25.89
A


ATOM
2258
CA
PRO
A
355
26.763
9.346
16.734
1.00
27.23
A


ATOM
2259
CB
PRO
A
355
27.625
9.915
15.609
1.00
24.91
A


ATOM
2260
CG
PRO
A
355
28.643
8.838
15.385
1.00
25.54
A


ATOM
2261
C
PRO
A
355
25.322
9.837
16.641
1.00
28.07
A


ATOM
2262
O
PRO
A
355
24.548
9.364
15.810
1.00
27.24
A


ATOM
2263
N
PRO
A
356
24.941
10.792
17.500
1.00
28.28
A


ATOM
2264
CD
PRO
A
356
25.752
11.560
18.462
1.00
28.31
A


ATOM
2265
CA
PRO
A
356
23.572
11.306
17.448
1.00
28.44
A


ATOM
2266
CB
PRO
A
356
23.539
12.301
18.604
1.00
28.11
A


ATOM
2267
CG
PRO
A
356
24.946
12.832
18.612
1.00
26.86
A


ATOM
2268
C
PRO
A
356
23.363
11.978
16.097
1.00
29.25
A


ATOM
2269
O
PRO
A
356
24.304
12.537
15.529
1.00
27.27
A


ATOM
2270
N
ALA
A
357
22.143
11.910
15.575
1.00
30.45
A


ATOM
2271
CA
ALA
A
357
21.848
12.521
14.287
1.00
32.81
A


ATOM
2272
CB
ALA
A
357
20.507
12.019
13.757
1.00
31.99
A


ATOM
2273
C
ALA
A
357
21.824
14.035
14.448
1.00
35.05
A


ATOM
2274
O
ALA
A
357
21.194
14.561
15.369
1.00
35.04
A


ATOM
2275
N
LEU
A
358
22.516
14.730
13.552
1.00
37.81
A


ATOM
2276
CA
LEU
A
358
22.578
16.185
13.597
1.00
42.15
A


ATOM
2277
CB
LEU
A
358
23.679
16.681
12.658
1.00
39.54
A


ATOM
2278
CG
LEU
A
358
25.086
16.285
13.109
1.00
39.51
A


ATOM
2279
CD1
LEU
A
358
26.102
16.686
12.062
1.00
39.29
A


ATOM
2280
CD2
LEU
A
358
25.395
16.953
14.445
1.00
40.01
A


ATOM
2281
C
LEU
A
358
21.241
16.837
13.242
1.00
45.91
A


ATOM
2282
O
LEU
A
358
20.874
16.927
12.069
1.00
45.71
A


ATOM
2283
N
THR
A
359
20.530
17.290
14.275
1.00
50.06
A


ATOM
2284
CA
THR
A
359
19.223
17.939
14.140
1.00
53.73
A


ATOM
2285
CB
THR
A
359
19.353
19.428
13.726
1.00
54.04
A


ATOM
2286
OG1
THR
A
359
19.995
19.521
12.448
1.00
56.35
A


ATOM
2287
CG2
THR
A
359
20.158
20.204
14.763
1.00
54.32
A


ATOM
2288
C
THR
A
359
18.309
17.236
13.139
1.00
54.47
A


ATOM
2289
O
THR
A
359
18.483
16.016
12.930
1.00
55.90
A


ATOM
2290
OXT
THR
A
359
17.407
17.908
12.595
1.00
56.97
A


TER













ATOM
1
CB
PRO
B
71
99.838
54.646
−7.659
1.00
20.00
6


ATOM
2
CG
PRO
B
71
99.216
55.105
−6.341
1.00
20.00
6


ATOM
3
C
PRO
B
71
98.903
54.776
−9.981
1.00
20.00
6


ATOM
4
O
PRO
B
71
98.022
53.925
−10.109
1.00
20.00
8


ATOM
5
N
PRO
B
71
97.782
55.851
−8.042
1.00
20.00
7


ATOM
6
CD
PRO
B
71
97.728
55.323
−6.668
1.00
20.00
6


ATOM
7
CA
PRO
B
71
99.087
55.515
−8.658
1.00
20.00
6


ATOM
8
N
PRO
B
72
99.732
55.097
−10.985
1.00
20.00
7


ATOM
9
CD
PRO
B
72
100.794
56.121
−10.977
1.00
20.00
6


ATOM
10
CA
PRO
B
72
99.645
54.451
−12.297
1.00
20.00
6


ATOM
11
CB
PRO
B
72
100.885
54.973
−13.017
1.00
20.00
6


ATOM
12
CG
PRO
B
72
101.026
56.352
−12.456
1.00
20.00
6


ATOM
13
C
PRO
B
72
99.627
52.924
−12.202
1.00
20.00
6


ATOM
14
O
PRO
B
72
100.246
52.338
−11.314
1.00
20.00
8


ATOM
15
N
ALA
B
73
98.906
52.293
−13.122
1.00
20.00
7


ATOM
16
CA
ALA
B
73
98.805
50.840
−13.167
1.00
20.00
6


ATOM
17
CB
ALA
B
73
97.420
50.392
−12.710
1.00
20.00
6


ATOM
18
C
ALA
B
73
99.053
50.398
−14.604
1.00
20.00
6


ATOM
19
O
ALA
B
73
99.027
51.215
−15.526
1.00
20.00
8


ATOM
20
N
PRO
B
74
99.313
49.100
−14.818
1.00
20.00
7


ATOM
21
CD
PRO
B
74
99.473
47.995
−13.857
1.00
20.00
6


ATOM
22
CA
PRO
B
74
99.553
48.642
−16.189
1.00
20.00
6


ATOM
23
CB
PRO
B
74
99.700
47.132
−16.023
1.00
20.00
6


ATOM
24
CG
PRO
B
74
100.292
47.004
−14.649
1.00
20.00
6


ATOM
25
C
PRO
B
74
98.371
49.018
−17.079
1.00
20.00
6


ATOM
26
O
PRO
B
74
97.279
49.296
−16.583
1.00
20.00
8


ATOM
27
N
ALA
B
75
98.589
49.037
−18.389
1.00
20.00
7


ATOM
28
CA
ALA
B
75
97.516
49.368
−19.321
1.00
20.00
6


ATOM
29
CB
ALA
B
75
98.061
49.462
−20.745
1.00
20.00
6


ATOM
30
C
ALA
B
75
96.446
48.285
−19.246
1.00
20.00
6


ATOM
31
O
ALA
B
75
96.745
47.126
−18.961
1.00
20.00
8


ATOM
32
N
LYS
B
76
95.200
48.666
−19.494
1.00
20.00
7


ATOM
33
CA
LYS
B
76
94.098
47.716
−19.463
1.00
20.00
6


ATOM
34
CB
LYS
B
76
92.793
48.431
−19.805
1.00
20.00
6


ATOM
35
CG
LYS
B
76
91.546
47.792
−19.225
1.00
20.00
6


ATOM
36
CD
LYS
B
76
91.511
47.932
−17.711
1.00
20.00
6


ATOM
37
CZ
LYS
B
76
90.184
47.454
−17.152
1.00
20.00
6


ATOM
38
NZ
LYS
B
76
90.108
47.606
−15.673
1.00
20.00
7


ATOM
39
C
LYS
B
76
94.389
46.645
−20.513
1.00
20.00
6


ATOM
40
O
LYS
B
76
94.736
46.968
−21.645
1.00
20.00
8


ATOM
41
N
LYS
B
77
94.269
45.374
−20.145
1.00
20.00
7


ATOM
42
CA
LYS
B
77
94.525
44.311
−21.107
1.00
20.00
6


ATOM
43
CB
LYS
B
77
94.875
43.008
−20.384
1.00
20.00
6


ATOM
44
CG
LYS
B
77
96.117
43.125
−19.506
1.00
20.00
6


ATOM
45
CD
LYS
B
77
96.461
41.812
−18.842
1.00
20.00
6


ATOM
46
CE
LYS
B
77
97.501
42.008
−17.745
1.00
20.00
6


ATOM
47
NZ
LYS
B
77
98.771
42.582
−18.255
1.00
20.00
7


ATOM
48
C
LYS
B
77
93.311
44.111
−22.012
1.00
20.00
6


ATOM
49
O
LYS
B
77
92.218
44.585
−21.704
1.00
20.00
8


ATOM
50
N
ARG
B
78
93.514
43.418
−23.129
1.00
20.00
7


ATOM
51
CA
ARG
B
78
92.442
43.158
−24.086
1.00
20.00
6


ATOM
52
CB
ARG
B
78
92.465
44.224
−25.193
1.00
20.00
6


ATOM
53
CG
ARG
B
78
93.787
44.344
−25.925
1.00
20.00
6


ATOM
54
CD
ARG
B
78
93.833
45.612
−26.771
1.00
20.00
6


ATOM
55
NE
ARG
B
78
95.052
45.702
−27.575
1.00
20.00
7


ATOM
56
CZ
ARG
B
78
96.287
45.751
−27.078
1.00
20.00
6


ATOM
57
NH1
ARG
B
78
96.486
45.721
−25.764
1.00
20.00
7


ATOM
58
NH2
ARG
B
78
97.330
45.828
−27.897
1.00
20.00
7


ATOM
59
C
ARG
B
78
92.570
41.754
−24.678
1.00
20.00
6


ATOM
60
O
ARG
B
78
93.625
41.126
−24.581
1.00
20.00
8


ATOM
61
N
PRO
B
79
91.494
41.240
−25.303
1.00
20.00
7


ATOM
62
CD
PRO
B
79
90.195
41.894
−25.543
1.00
20.00
6


ATOM
63
CA
PRO
B
79
91.519
39.899
−25.896
1.00
20.00
6


ATOM
64
CB
PRO
B
79
90.214
39.848
−26.691
1.00
20.00
6


ATOM
65
CG
PRO
B
79
89.304
40.725
−25.889
1.00
20.00
6


ATOM
66
C
PRO
B
79
92.737
39.614
−26.778
1.00
20.00
6


ATOM
67
O
PRO
B
79
93.311
38.523
−26.717
1.00
20.00
8


ATOM
68
N
GLU
B
80
93.124
40.597
−27.589
1.00
20.00
7


ATOM
69
CA
GLU
B
80
94.254
40.441
−28.503
1.00
20.00
6


ATOM
70
CB
GLU
B
80
94.358
41.644
−29.446
1.00
20.00
6


ATOM
71
CG
GLU
B
80
94.881
42.912
−28.800
1.00
20.00
6


ATOM
72
CD
GLU
B
80
95.009
44.057
−29.788
1.00
20.00
6


ATOM
73
OE1
GLU
B
80
93.968
44.513
−30.308
1.00
20.00
8


ATOM
74
OE2
GLU
B
80
96.150
44.498
−30.047
1.00
20.00
8


ATOM
75
C
GLU
B
80
95.591
40.235
−27.787
1.00
20.00
6


ATOM
76
O
GLU
B
80
96.558
39.795
−28.405
1.00
20.00
8


ATOM
77
N
ASP
B
81
95.656
40.559
−26.497
1.00
20.00
7


ATOM
78
CA
ASP
B
81
96.902
40.380
−25.749
1.00
20.00
6


ATOM
79
CB
ASP
B
81
96.888
41.192
−24.446
1.00
20.00
6


ATOM
80
CG
ASP
B
81
96.774
42.688
−24.682
1.00
20.00
6


ATOM
81
OD1
ASP
B
81
97.436
43.193
−25.606
1.00
20.00
8


ATOM
82
OD2
ASP
B
81
96.033
43.362
−23.933
1.00
20.00
8


ATOM
83
C
ASP
B
81
97.111
38.914
−25.393
1.00
20.00
6


ATOM
84
O
ASP
B
81
98.172
38.535
−24.890
1.00
20.00
8


ATOM
85
N
PHE
B
82
96.103
38.093
−25.679
1.00
20.00
7


ATOM
86
CA
PHE
B
82
96.140
36.677
−25.340
1.00
20.00
6


ATOM
87
CB
PHE
B
82
95.056
36.369
−24.302
1.00
20.00
6


ATOM
88
CG
PHE
B
82
95.157
37.187
−23.050
1.00
20.00
6


ATOM
89
CD1
PHE
B
82
95.880
36.724
−21.959
1.00
20.00
6


ATOM
90
CD2
PHE
B
82
94.525
38.423
−22.961
1.00
20.00
6


ATOM
91
CE1
PHE
B
82
95.976
37.479
−20.793
1.00
20.00
6


ATOM
92
CE2
PHE
B
82
94.615
39.188
−21.800
1.00
20.00
6


ATOM
93
CZ
PHE
B
82
95.343
38.712
−20.713
1.00
20.00
6


ATOM
94
C
PHE
B
82
95.929
35.719
−26.496
1.00
20.00
6


ATOM
95
O
PHE
B
82
95.342
36.061
−27.524
1.00
20.00
8


ATOM
96
N
LYS
B
83
96.406
34.500
−26.286
1.00
20.00
7


ATOM
97
CA
LYS
B
83
96.242
33.411
−27.228
1.00
20.00
6


ATOM
98
CB
LYS
B
83
97.594
32.777
−27.562
1.00
20.00
6


ATOM
99
CG
LYS
B
83
97.503
31.531
−28.425
1.00
20.00
6


ATOM
100
CD
LYS
B
83
98.888
31.074
−28.856
1.00
20.00
6


ATOM
101
CE
LYS
B
83
98.826
29.808
−29.699
1.00
20.00
6


ATOM
102
NZ
LYS
B
83
98.287
28.654
−28.918
1.00
20.00
7


ATOM
103
C
LYS
B
83
95.387
32.446
−26.416
1.00
20.00
6


ATOM
104
O
LYS
B
83
95.884
31.776
−25.510
1.00
20.00
8


ATOM
105
N
PHE
B
84
94.094
32.393
−26.710
1.00
20.00
7


ATOM
106
CA
PHE
B
84
93.217
31.511
−25.958
1.00
20.00
6


ATOM
107
CB
PHE
B
84
91.758
31.928
−26.133
1.00
20.00
6


ATOM
108
CG
PHE
B
84
91.426
33.228
−25.462
1.00
20.00
6


ATOM
109
CD1
PHE
B
84
91.668
34.439
−26.099
1.00
20.00
6


ATOM
110
CD2
PHE
B
84
90.907
33.243
−24.174
1.00
20.00
6


ATOM
111
CE1
PHE
B
84
91.400
35.644
−25.464
1.00
20.00
6


ATOM
112
CE2
PHE
B
84
90.636
34.447
−23.528
1.00
20.00
6


ATOM
113
CZ
PHE
B
84
90.884
35.646
−24.176
1.00
20.00
6


ATOM
114
C
PHE
B
84
93.402
30.054
−26.335
1.00
20.00
6


ATOM
115
O
PHE
B
84
93.734
29.734
−27.476
1.00
20.00
8


ATOM
116
N
GLY
B
85
93.196
29.178
−25.359
1.00
20.00
7


ATOM
117
CA
GLY
B
85
93.349
27.758
−25.591
1.00
20.00
6


ATOM
118
C
GLY
B
85
92.103
26.977
−25.221
1.00
20.00
6


ATOM
119
O
GLY
B
85
90.982
27.393
−25.525
1.00
20.00
8


ATOM
120
N
LYS
B
86
92.296
25.858
−24.534
1.00
20.00
7


ATOM
121
CA
LYS
B
86
91.182
25.005
−24.153
1.00
20.00
6


ATOM
122
CB
LYS
B
86
91.695
23.640
−23.687
1.00
20.00
6


ATOM
123
CG
LYS
B
86
92.421
23.667
−22.356
1.00
20.00
6


ATOM
124
CD
LYS
B
86
92.855
22.272
−21.941
1.00
20.00
6


ATOM
125
CE
LYS
B
86
93.685
22.319
−20.668
1.00
20.00
6


ATOM
126
NZ
LYS
B
86
94.209
20.975
−20.287
1.00
20.00
7


ATOM
127
C
LYS
B
86
90.267
25.576
−23.077
1.00
20.00
6


ATOM
128
O
LYS
B
86
90.668
26.410
−22.260
1.00
20.00
8


ATOM
129
N
ILE
B
87
89.026
25.106
−23.102
1.00
20.00
7


ATOM
130
CA
ILE
B
87
88.023
25.497
−22.131
1.00
20.00
6


ATOM
131
CB
ILE
B
87
86.604
25.159
−22.647
1.00
20.00
6


ATOM
132
CG2
ILE
B
87
85.582
25.261
−21.503
1.00
20.00
6


ATOM
133
CG1
ILE
B
87
86.260
26.085
−23.820
1.00
20.00
6


ATOM
134
CD1
ILE
B
87
84.912
25.819
−24.463
1.00
20.00
6


ATOM
135
C
ILE
B
87
88.312
24.687
−20.872
1.00
20.00
6


ATOM
136
O
ILE
B
87
88.396
23.461
−20.927
1.00
20.00
8


ATOM
137
N
LEU
B
88
88.473
25.368
−19.742
1.00
20.00
7


ATOM
138
CA
LEU
B
88
88.757
24.686
−18.486
1.00
20.00
6


ATOM
139
CB
LEU
B
88
89.592
25.586
−17.575
1.00
20.00
6


ATOM
140
CG
LEU
B
88
90.968
25.987
−18.112
1.00
20.00
6


ATOM
141
CD1
LEU
B
88
91.611
27.006
−17.186
1.00
20.00
6


ATOM
142
CD2
LEU
B
88
91.836
24.756
−18.234
1.00
20.00
6


ATOM
143
C
LEU
B
88
87.471
24.298
−17.776
1.00
20.00
6


ATOM
144
O
LEU
B
88
87.434
23.334
−17.014
1.00
20.00
8


ATOM
145
N
GLY
B
89
86.410
25.051
−18.024
1.00
20.00
7


ATOM
146
CA
GLY
B
89
85.148
24.749
−17.382
1.00
20.00
6


ATOM
147
C
GLY
B
89
84.038
25.599
−17.953
1.00
20.00
6


ATOM
148
O
GLY
B
89
84.296
26.657
−18.541
1.00
20.00
8


ATOM
149
N
GLU
B
90
82.807
25.133
−17.781
1.00
20.00
7


ATOM
150
CA
GLU
B
90
81.629
25.832
−18.279
1.00
20.00
6


ATOM
151
CB
GLU
B
90
81.041
25.070
−19.471
1.00
20.00
6


ATOM
152
CG
GLU
B
90
81.929
25.084
−20.706
1.00
20.00
6


ATOM
153
CD
GLU
B
90
81.434
24.157
−21.802
1.00
20.00
6


ATOM
154
OE1
GLU
B
90
81.539
22.923
−21.639
1.00
20.00
8


ATOM
155
OE2
GLU
B
90
80.935
24.662
−22.827
1.00
20.00
8


ATOM
156
C
GLU
B
90
80.575
25.970
−17.188
1.00
20.00
6


ATOM
157
O
GLU
B
90
80.208
24.994
−16.543
1.00
20.00
8


ATOM
158
N
GLY
B
91
80.103
27.193
−16.979
1.00
20.00
7


ATOM
159
CA
GLY
B
91
79.080
27.431
−15.979
1.00
20.00
6


ATOM
160
C
GLY
B
91
77.835
27.949
−16.673
1.00
20.00
6


ATOM
161
O
GLY
B
91
77.804
28.046
−17.903
1.00
20.00
8


ATOM
162
N
SER
B
92
76.808
28.291
−15.904
1.00
20.00
7


ATOM
163
CA
SER
B
92
75.582
28.794
−16.508
1.00
20.00
6


ATOM
164
CB
SER
B
92
74.428
28.719
−15.505
1.00
20.00
6


ATOM
165
OG
SER
B
92
74.786
29.335
−14.282
1.00
20.00
8


ATOM
166
C
SER
B
92
75.726
30.219
−17.039
1.00
20.00
6


ATOM
167
O
SER
B
92
75.078
30.585
−18.018
1.00
20.00
8


ATOM
168
N
PHE
B
93
76.578
31.025
−16.411
1.00
20.00
7


ATOM
169
CA
PHE
B
93
76.763
32.399
−16.870
1.00
20.00
6


ATOM
170
CB
PHE
B
93
76.276
33.384
−15.807
1.00
20.00
6


ATOM
171
CG
PHE
B
93
74.832
33.220
−15.469
1.00
20.00
6


ATOM
172
CD1
PHE
B
93
74.435
32.323
−14.483
1.00
20.00
6


ATOM
173
CD2
PHE
B
93
73.859
33.914
−16.183
1.00
20.00
6


ATOM
174
CE1
PHE
B
93
73.086
32.117
−14.210
1.00
20.00
6


ATOM
175
CE2
PHE
B
93
72.507
33.715
−15.919
1.00
20.00
6


ATOM
176
CZ
PHE
B
93
72.120
32.812
−14.930
1.00
20.00
6


ATOM
177
C
PHE
B
93
78.197
32.736
−17.240
1.00
20.00
6


ATOM
178
O
PHE
B
93
78.543
33.908
−17.397
1.00
20.00
8


ATOM
179
N
SER
B
94
79.030
31.713
−17.394
1.00
20.00
7


ATOM
180
CA
SER
B
94
80.421
31.948
−17.735
1.00
20.00
6


ATOM
181
CB
SER
B
94
81.174
32.443
−16.503
1.00
20.00
6


ATOM
182
OG
SER
B
94
81.237
31.410
−15.535
1.00
20.00
8


ATOM
183
C
SER
B
94
81.123
30.707
−18.253
1.00
20.00
6


ATOM
184
O
SER
B
94
80.666
29.584
−18.048
1.00
20.00
8


ATOM
185
N
THR
B
95
82.252
30.937
−18.913
1.00
20.00
7


ATOM
186
CA
THR
B
95
83.088
29.879
−19.455
1.00
20.00
6


ATOM
187
CB
THR
B
95
82.942
29.770
−20.985
1.00
20.00
6


ATOM
188
OG1
THR
B
95
81.589
29.425
−21.309
1.00
20.00
8


ATOM
189
CG2
THR
B
95
83.873
28.694
−21.536
1.00
20.00
6


ATOM
190
C
THR
B
95
84.524
30.264
−19.118
1.00
20.00
6


ATOM
191
O
THR
B
95
84.957
31.388
−19.399
1.00
20.00
8


ATOM
192
N
VAL
B
96
85.257
29.348
−18.498
1.00
20.00
7


ATOM
193
CA
VAL
B
96
86.642
29.628
−18.141
1.00
20.00
6


ATOM
194
CB
VAL
B
96
86.991
29.050
−16.761
1.00
20.00
6


ATOM
195
CG1
VAL
B
96
88.438
29.390
−16.407
1.00
20.00
6


ATOM
196
CG2
VAL
B
96
86.041
29.627
−15.707
1.00
20.00
6


ATOM
197
C
VAL
B
96
87.541
29.027
−19.210
1.00
20.00
6


ATOM
198
O
VAL
B
96
87.432
27.845
−19.540
1.00
20.00
8


ATOM
199
N
VAL
B
97
88.416
29.858
−19.763
1.00
20.00
7


ATOM
200
CA
VAL
B
97
89.312
29.430
−20.824
1.00
20.00
6


ATOM
201
CB
VAL
B
97
89.006
30.194
−22.130
1.00
20.00
6


ATOM
202
CG1
VAL
B
97
89.828
29.624
−23.279
1.00
20.00
6


ATOM
203
CG2
VAL
B
97
87.515
30.116
−22.444
1.00
20.00
6


ATOM
204
C
VAL
B
97
90.771
29.664
−20.458
1.00
20.00
6


ATOM
205
O
VAL
B
97
91.122
30.698
−19.889
1.00
20.00
8


ATOM
206
N
LEU
B
98
91.617
28.690
−20.770
1.00
20.00
7


ATOM
207
CA
LEU
B
98
93.039
28.821
−20.499
1.00
20.00
6


ATOM
208
CB
LEU
B
98
93.727
27.459
−20.618
1.00
20.00
6


ATOM
209
CG
LEU
B
98
95.240
27.421
−20.383
1.00
20.00
6


ATOM
210
CD1
LEU
B
98
95.565
28.019
−19.021
1.00
20.00
6


ATOM
211
CD2
LEU
B
98
95.739
25.987
−20.463
1.00
20.00
6


ATOM
212
C
LEU
B
98
93.580
29.785
−21.552
1.00
20.00
6


ATOM
213
O
LEU
B
98
93.293
29.637
−22.738
1.00
20.00
8


ATOM
214
N
ALA
B
99
94.343
30.783
−21.121
1.00
20.00
7


ATOM
215
CA
ALA
B
99
94.897
31.767
−22.043
1.00
20.00
6


ATOM
216
CB
ALA
B
99
94.087
33.055
−21.980
1.00
20.00
6


ATOM
217
C
ALA
B
99
96.353
32.067
−21.723
1.00
20.00
6


ATOM
218
O
ALA
B
99
96.748
32.110
−20.554
1.00
20.00
8


ATOM
219
N
ARG
B
100
97.152
32.270
−22.763
1.00
20.00
7


ATOM
220
CA
ARG
B
100
98.554
32.596
−22.568
1.00
20.00
6


ATOM
221
CB
ARG
B
100
99.442
31.657
−23.393
1.00
20.00
6


ATOM
222
CG
ARG
B
100
100.934
31.833
−23.131
1.00
20.00
6


ATOM
223
CD
ARG
B
100
101.770
30.835
−23.923
1.00
20.00
6


ATOM
224
NE
ARG
B
100
101.600
29.452
−23.469
1.00
20.00
7


ATOM
225
CZ
ARG
B
100
102.059
28.970
−22.314
1.00
20.00
6


ATOM
226
NH1
ARG
B
100
102.722
29.752
−21.473
1.00
20.00
7


ATOM
227
NH2
ARG
B
100
101.864
27.694
−22.003
1.00
20.00
7


ATOM
228
C
ARG
B
100
98.756
34.045
−23.004
1.00
20.00
6


ATOM
229
O
ARG
B
100
98.454
34.408
−24.146
1.00
20.00
8


ATOM
230
N
GLU
B
101
99.228
34.883
−22.087
1.00
20.00
7


ATOM
231
CA
GLU
B
101
99.470
36.286
−22.408
1.00
20.00
6


ATOM
232
CB
GLU
B
101
99.709
37.091
−21.123
1.00
20.00
6


ATOM
233
CG
GLU
B
101
99.986
38.571
−21.363
1.00
20.00
6


ATOM
234
CD
GLU
B
101
100.164
39.347
−20.075
1.00
20.00
6


ATOM
235
OE1
GLU
B
101
100.717
38.780
−19.114
1.00
20.00
8


ATOM
236
OE2
GLU
B
101
99.765
40.531
−20.025
1.00
20.00
8


ATOM
237
C
GLU
B
101
100.703
36.338
−23.317
1.00
20.00
6


ATOM
238
O
GLU
B
101
101.773
35.865
−22.944
1.00
20.00
8


ATOM
239
N
LEU
B
102
100.546
36.909
−24.507
1.00
20.00
7


ATOM
240
CA
LEU
B
102
101.632
36.982
−25.482
1.00
20.00
6


ATOM
241
CB
LEU
B
102
101.145
37.683
−26.753
1.00
20.00
6


ATOM
242
CG
LEU
B
102
100.013
36.985
−27.517
1.00
20.00
6


ATOM
243
CD1
LEU
B
102
99.500
37.897
−28.623
1.00
20.00
6


ATOM
244
CD2
LEU
B
102
100.517
35.670
−28.089
1.00
20.00
6


ATOM
245
C
LEU
B
102
102.906
37.663
−25.000
1.00
20.00
6


ATOM
246
O
LEU
B
102
104.000
37.137
−25.180
1.00
20.00
8


ATOM
247
N
ALA
B
103
102.760
38.828
−24.382
1.00
20.00
7


ATOM
248
CA
ALA
B
103
103.909
39.587
−23.910
1.00
20.00
6


ATOM
249
CB
ALA
B
103
103.464
41.002
−23.546
1.00
20.00
6


ATOM
250
C
ALA
B
103
104.697
38.983
−22.747
1.00
20.00
6


ATOM
251
O
ALA
B
103
105.832
39.389
−22.503
1.00
20.00
8


ATOM
252
N
THR
B
104
104.122
38.007
−22.050
1.00
20.00
7


ATOM
253
CA
THR
B
104
104.790
37.418
−20.893
1.00
20.00
6


ATOM
254
CB
THR
B
104
104.059
37.799
−19.592
1.00
20.00
6


ATOM
255
OG1
THR
B
104
102.712
37.303
−19.648
1.00
20.00
8


ATOM
256
CG2
THR
B
104
104.033
39.313
−19.404
1.00
20.00
6


ATOM
257
C
THR
B
104
104.880
35.902
−20.901
1.00
20.00
6


ATOM
258
O
THR
B
104
105.677
35.323
−20.160
1.00
20.00
8


ATOM
259
N
SER
B
105
104.042
35.274
−21.722
1.00
20.00
7


ATOM
260
CA
SER
B
105
103.950
33.818
−21.842
1.00
20.00
6


ATOM
261
CB
SER
B
105
105.344
33.213
−22.048
1.00
20.00
6


ATOM
262
OG
SER
B
105
105.264
31.819
−22.287
1.00
20.00
8


ATOM
263
C
SER
B
105
103.304
33.243
−20.576
1.00
20.00
6


ATOM
264
O
SER
B
105
103.286
32.029
−20.363
1.00
20.00
8


ATOM
265
N
ARG
B
106
102.771
34.124
−19.736
1.00
20.00
7


ATOM
266
CA
ARG
B
106
102.089
33.709
−18.509
1.00
20.00
6


ATOM
267
CB
ARG
B
106
101.833
34.914
−17.598
1.00
20.00
6


ATOM
268
CG
ARG
B
106
103.022
35.361
−16.781
1.00
20.00
6


ATOM
269
CD
ARG
B
106
102.724
36.653
−16.045
1.00
20.00
6


ATOM
270
NE
ARG
B
106
103.756
36.940
−15.051
1.00
20.00
7


ATOM
271
CZ
ARG
B
106
103.964
38.132
−14.504
1.00
20.00
6


ATOM
272
NH1
ARG
B
106
103.210
39.167
−14.858
1.00
20.00
7


ATOM
273
NH2
ARG
B
106
104.918
38.279
−13.590
1.00
20.00
7


ATOM
274
C
ARG
B
106
100.743
33.082
−18.856
1.00
20.00
6


ATOM
275
O
ARG
B
106
100.069
33.534
−19.777
1.00
20.00
8


ATOM
276
N
GLU
B
107
100.354
32.049
−18.115
1.00
20.00
7


ATOM
277
CA
GLU
B
107
99.072
31.390
−18.336
1.00
20.00
6


ATOM
278
CB
GLU
B
107
99.193
29.870
−18.212
1.00
20.00
6


ATOM
279
CG
GLU
B
107
100.180
29.207
−19.144
1.00
20.00
6


ATOM
280
CD
GLU
B
107
100.124
27.696
−19.023
1.00
20.00
6


ATOM
281
OE1
GLU
B
107
99.373
27.068
−19.798
1.00
20.00
8


ATOM
282
OE2
GLU
B
107
100.813
27.144
−18.138
1.00
20.00
8


ATOM
283
C
GLU
B
107
98.070
31.848
−17.285
1.00
20.00
6


ATOM
284
O
GLU
B
107
98.368
31.833
−16.095
1.00
20.00
8


ATOM
285
N
TYR
B
108
96.885
32.243
−17.727
1.00
20.00
7


ATOM
286 
CA
TYR
B
108
95.829
32.667
−16.817
1.00
20.00
6


ATOM
287
CB
TYR
B
108
95.525
34.156
−16.979
1.00
20.00
6


ATOM
288
CG
TYR
B
108
96.603
35.089
−16.487
1.00
20.00
6


ATOM
289
CD1
TYR
B
108
96.744
35.369
−15.129
1.00
20.00
6


ATOM
290
CE1
TYR
B
108
97.727
36.260
−14.674
1.00
20.00
6


ATOM
291
CD2
TYR
B
108
97.467
35.712
−17.386
1.00
20.00
6


ATOM
292
CE2
TYR
B
108
98.442
36.597
−16.950
1.00
20.00
6


ATOM
293
CZ
TYR
B
108
98.569
36.869
−15.599
1.00
20.00
6


ATOM
294
OH
TYR
B
108
99.529
37.756
−15.187
1.00
20.00
8


ATOM
295
C
TYR
B
108
94.566
31.899
−17.167
1.00
20.00
6


ATOM
296
O
TYR
B
108
94.389
31.463
−18.306
1.00
20.00
8


ATOM
297
N
ALA
B
109
93.697
31.723
−16.181
1.00
20.00
7


ATOM
298
CA
ALA
B
109
92.421
31.073
−16.414
1.00
20.00
6


ATOM
299
CB
ALA
B
109
92.024
30.225
−15.214
1.00
20.00
6


ATOM
300
C
ALA
B
109
91.513
32.288
−16.542
1.00
20.00
6


ATOM
301
O
ALA
B
109
91.278
33.003
−15.558
1.00
20.00
8


ATOM
302
N
ILE
B
110
91.042
32.557
−17.756
1.00
20.00
7


ATOM
303
CA
ILE
B
110
90.186
33.711
−17.968
1.00
20.00
6


ATOM
304
CB
ILE
B
110
90.574
34.462
−19.271
1.00
20.00
6


ATOM
305
CG2
ILE
B
110
89.628
35.630
−19.507
1.00
20.00
6


ATOM
306
CG1
ILE
B
110
92.023
34.962
−19.159
1.00
20.00
6


ATOM
307
CD1
ILE
B
110
92.487
35.847
−20.312
1.00
20.00
6


ATOM
308
C
ILE
B
110
88.715
33.318
−18.004
1.00
20.00
6


ATOM
309
O
ILE
B
110
88.285
32.527
−18.851
1.00
20.00
8


ATOM
310
N
LYS
B
111
87.956
33.852
−17.052
1.00
20.00
7


ATOM
311
CA
LYS
B
111
86.527
33.581
−16.975
1.00
20.00
6


ATOM
312
CB
LYS
B
111
86.022
33.721
−15.531
1.00
20.00
6


ATOM
313
CG
LYS
B
111
84.509
33.598
−15.411
1.00
20.00
6


ATOM
314
CD
LYS
B
111
84.025
33.590
−13.965
1.00
20.00
6


ATOM
315
CE
LYS
B
111
84.318
32.262
−13.277
1.00
20.00
6


ATOM
316
NZ
LYS
B
111
83.784
32.217
−11.875
1.00
20.00
7


ATOM
317
C
LYS
B
111
85.844
34.601
−17.869
1.00
20.00
6


ATOM
318
O
LYS
B
111
86.017
35.807
−17.688
1.00
20.00
8


ATOM
319
N
ILE
B
112
85.078
34.111
−18.838
1.00
20.00
7


ATOM
320
CA
ILE
B
112
84.383
34.976
−19.782
1.00
20.00
6


ATOM
321
CB
ILE
B
112
84.695
34.548
−21.233
1.00
20.00
6


ATOM
322
CG2
ILE
B
112
84.042
35.505
−22.216
1.00
20.00
6


ATOM
323
CG1
ILE
B
112
86.216
34.518
−21.440
1.00
20.00
6


ATOM
324
CD1
ILE
B
112
86.657
33.949
−22.779
1.00
20.00
6


ATOM
325
C
ILE
B
112
82.878
34.916
−19.538
1.00
20.00
6


ATOM
326
O
ILE
B
112
82.288
33.839
−19.510
1.00
20.00
8


ATOM
327
N
LEU
B
113
82.269
36.083
−19.347
1.00
20.00
7


ATOM
328
CA
LEU
B
113
80.835
36.172
−19.089
1.00
20.00
6


ATOM
329
CB
LEU
B
113
80.585
36.696
−17.669
1.00
20.00
6


ATOM
330
CG
LEU
B
113
81.350
36.038
−16.521
1.00
20.00
6


ATOM
331
CD1
LEU
B
113
82.743
36.638
−16.428
1.00
20.00
6


ATOM
332
CD2
LEU
B
113
80.609
36.258
−15.215
1.00
20.00
6


ATOM
333
C
LEU
B
113
80.172
37.110
−20.090
1.00
20.00
6


ATOM
334
O
LEU
B
113
80.634
38.232
−20.299
1.00
20.00
8


ATOM
335
N
GLU
B
114
79.088
36.653
−20.709
1.00
20.00
7


ATOM
336
CA
GLU
B
114
78.377
37.472
−21.681
1.00
20.00
6


ATOM
337
CB
GLU
B
114
77.514
36.586
−22.581
1.00
20.00
6


ATOM
338
CG
GLU
B
114
76.670
37.366
−23.571
1.00
20.00
6


ATOM
339
CD
GLU
B
114
75.749
36.473
−24.372
1.00
20.00
6


ATOM
340
OE1
GLU
B
114
75.083
35.613
−23.760
1.00
20.00
8


ATOM
341
OE2
GLU
B
114
75.684
36.638
−25.611
1.00
20.00
8


ATOM
342
C
GLU
B
114
77.509
38.491
−20.942
1.00
20.00
6


ATOM
343
O
GLU
B
114
76.673
38.122
−20.113
1.00
20.00
8


ATOM
344
N
LYS
B
115
77.709
39.771
−21.235
1.00
20.00
7


ATOM
345
CA
LYS
B
115
76.945
40.808
−20.553
1.00
20.00
6


ATOM
346
CB
LYS
B
115
77.433
42.202
−20.978
1.00
20.00
6


ATOM
347
CG
LYS
B
115
78.653
42.675
−20.183
1.00
20.00
6


ATOM
348
CD
LYS
B
115
79.174
44.045
−20.618
1.00
20.00
6


ATOM
349
CE
LYS
B
115
79.832
43.994
−21.992
1.00
20.00
6


ATOM
350
NZ
LYS
B
115
80.536
45.273
−22.323
1.00
20.00
7


ATOM
351
C
LYS
B
115
75.435
40.693
−20.743
1.00
20.00
6


ATOM
352
O
LYS
B
115
74.676
40.787
−19.778
1.00
20.00
8


ATOM
353
N
ARG
B
116
74.997
40.471
−21.977
1.00
20.00
7


ATOM
354
CA
ARG
B
116
73.570
40.363
−22.255
1.00
20.00
6


ATOM
355
CB
ARG
B
116
73.346
40.066
−23.743
1.00
20.00
6


ATOM
356
CG
ARG
B
116
71.893
39.821
−24.142
1.00
20.00
6


ATOM
357
CD
ARG
B
116
70.931
40.791
−23.465
1.00
20.00
6


ATOM
358
NE
ARG
B
116
71.401
42.172
−23.493
1.00
20.00
7


ATOM
359
CZ
ARG
B
116
70.780
43.177
−22.884
1.00
20.00
6


ATOM
360
NH1
ARG
B
116
69.663
42.949
−22.207
1.00
20.00
7


ATOM
361
NH2
ARG
B
116
71.278
44.405
−22.942
1.00
20.00
7


ATOM
362
C
ARG
B
116
72.888
39.298
−21.394
1.00
20.00
6


ATOM
363
O
ARG
B
116
71.862
39.567
−20.764
1.00
20.00
8


ATOM
364
N
HIS
B
117
73.463
38.101
−21.347
1.00
20.00
7


ATOM
365
CA
HIS
B
117
72.885
37.020
−20.556
1.00
20.00
6


ATOM
366
CB
HIS
B
117
73.704
35.738
−20.723
1.00
20.00
6


ATOM
367
CG
HIS
B
117
73.053
34.525
−20.133
1.00
20.00
6


ATOM
368
CD2
HIS
B
117
71.762
34.274
−19.810
1.00
20.00
6


ATOM
369
ND1
HIS
B
117
73.752
33.376
−19.836
1.00
20.00
7


ATOM
370
CE1
HIS
B
117
72.921
32.467
−19.355
1.00
20.00
6


ATOM
371
NE2
HIS
B
117
71.707
32.987
−19.330
1.00
20.00
7


ATOM
372
C
HIS
B
117
72.816
37.386
−19.077
1.00
20.00
6


ATOM
373
O
HIS
B
117
71.823
37.113
−18.409
1.00
20.00
8


ATOM
374
N
ILE
B
118
73.882
37.992
−18.564
1.00
20.00
7


ATOM
375
CA
ILE
B
118
73.927
38.391
−17.160
1.00
20.00
6


ATOM
376
CB
ILE
B
118
75.269
39.073
−16.827
1.00
20.00
6


ATOM
377
CG2
ILE
B
118
75.180
39.787
−15.486
1.00
20.00
6


ATOM
378
CG1
ILE
B
118
76.392
38.029
−16.834
1.00
20.00
6


ATOM
379
CD1
ILE
B
118
77.784
38.625
−16.709
1.00
20.00
6


ATOM
380
C
ILE
B
118
72.788
39.353
−16.833
1.00
20.00
6


ATOM
381
O
ILE
B
118
72.101
39.196
−15.827
1.00
20.00
8


ATOM
382
N
ILE
B
119
72.596
40.349
−17.690
1.00
20.00
7


ATOM
383
CA
ILE
B
119
71.538
41.333
−17.494
1.00
20.00
6


ATOM
384
CB
ILE
B
119
71.646
42.473
−18.539
1.00
20.00
6


ATOM
385
CG2
ILE
B
119
70.396
43.357
−18.492
1.00
20.00
6


ATOM
386
CG1
ILE
B
119
72.919
43.292
−18.270
1.00
20.00
6


ATOM
387
CD1
ILE
B
119
73.212
44.370
−19.314
1.00
20.00
6


ATOM
388
C
ILE
B
119
70.154
40.687
−17.580
1.00
20.00
6


ATOM
389
O
ILE
B
119
69.289
40.953
−16.747
1.00
20.00
8


ATOM
390
N
LYS
B
120
69.950
39.832
−18.579
1.00
20.00
7


ATOM
391
CA
LYS
B
120
68.659
39.169
−18.754
1.00
20.00
6


ATOM
392
CB
LYS
B
120
68.697
38.200
−19.935
1.00
20.00
6


ATOM
393
CG
LYS
B
120
68.942
38.841
−21.284
1.00
20.00
6


ATOM
394
CD
LYS
B
120
68.926
37.782
−22.387
1.00
20.00
6


ATOM
395
CE
LYS
B
120
69.934
36.665
−22.093
1.00
20.00
6


ATOM
396
NZ
LYS
B
120
69.950
35.599
−23.127
1.00
20.00
7


ATOM
397
C
LYS
B
120
68.229
38.398
−17.513
1.00
20.00
6


ATOM
398
O
LYS
B
120
67.077
38.490
−17.092
1.00
20.00
8


ATOM
399
N
GLU
B
121
69.154
37.639
−16.930
1.00
20.00
7


ATOM
400
CA
GLU
B
121
68.851
36.839
−15.747
1.00
20.00
6


ATOM
401
CB
GLU
B
121
69.678
35.549
−15.758
1.00
20.00
6


ATOM
402
CG
GLU
B
121
69.485
34.674
−16.995
1.00
20.00
6


ATOM
403
CD
GLU
B
121
68.029
34.326
−17.248
1.00
20.00
6


ATOM
404
OE1
GLU
B
121
67.339
33.904
−16.295
1.00
20.00
8


ATOM
405
OE2
GLU
B
121
67.574
34.470
−18.404
1.00
20.00
8


ATOM
406
C
GLU
B
121
69.071
37.573
−14.424
1.00
20.00
6


ATOM
407
O
GLU
B
121
69.117
36.946
−13.362
1.00
20.00
8


ATOM
408
N
ASN
B
122
69.208
38.895
−14.485
1.00
20.00
7


ATOM
409
CA
ASN
B
122
69.411
39.699
−13.281
1.00
20.00
6


ATOM
410
CB
ASN
B
122
68.132
39.715
−12.439
1.00
20.00
6


ATOM
411
CG
ASN
B
122
66.952
40.314
−13.177
1.00
20.00
6


ATOM
412
OD1
ASN
B
122
66.428
39.725
−14.121
1.00
20.00
8


ATOM
413
ND2
ASN
B
122
66.530
41.498
−12.748
1.00
20.00
7


ATOM
414
C
ASN
B
122
70.563
39.180
−12.419
1.00
20.00
6


ATOM
415
O
ASN
B
122
70.408
39.007
−11.212
1.00
20.00
8


ATOM
416
N
LYS
B
123
71.716
38.942
−13.033
1.00
20.00
7


ATOM
417
CA
LYS
B
123
72.870
38.434
−12.301
1.00
20.00
6


ATOM
418
CB
LYS
B
123
73.500
37.266
−13.065
1.00
20.00
6


ATOM
419
CG
LYS
B
123
72.568
36.086
−13.276
1.00
20.00
6


ATOM
420
CD
LYS
B
123
72.065
35.539
−11.948
1.00
20.00
6


ATOM
421
CE
LYS
B
123
71.032
34.445
−12.159
1.00
20.00
6


ATOM
422
NZ
LYS
B
123
70.421
34.016
−10.871
1.00
20.00
7


ATOM
423
C
LYS
B
123
73.931
39.498
−12.054
1.00
20.00
6


ATOM
424
O
LYS
B
123
75.035
39.183
−11.611
1.00
20.00
8


ATOM
425
N
VAL
B
124
73.607
40.753
−12.340
1.00
20.00
7


ATOM
426
CA
VAL
B
124
74.575
41.822
−12.145
1.00
20.00
6


ATOM
427
CB
VAL
B
124
73.997
43.201
−12.547
1.00
20.00
6


ATOM
428
CG1
VAL
B
124
75.035
44.290
−12.302
1.00
20.00
6


ATOM
429
CG2
VAL
B
124
73.608
43.186
−14.022
1.00
20.00
6


ATOM
430
C
VAL
B
124
75.091
41.885
−10.712
1.00
20.00
6


ATOM
431
O
VAL
B
124
76.278
42.115
−10.490
1.00
20.00
8


ATOM
432
N
PRO
B
125
74.207
41.695
−9.716
1.00
20.00
7


ATOM
433
CD
PRO
B
125
72.735
41.613
−9.757
1.00
20.00
6


ATOM
434
CA
PRO
B
125
74.688
41.747
−8.331
1.00
20.00
6


ATOM
435
CB
PRO
B
125
73.411
41.558
−7.512
1.00
20.00
6


ATOM
436
CG
PRO
B
125
72.346
42.152
−8.396
1.00
20.00
6


ATOM
437
C
PRO
B
125
75.715
40.643
−8.051
1.00
20.00
6


ATOM
438
O
PRO
B
125
76.683
40.851
−7.325
1.00
20.00
8


ATOM
439
N
TYR
B
126
75.493
39.475
−8.640
1.00
20.00
7


ATOM
440
CA
TYR
B
126
76.380
38.334
−8.440
1.00
20.00
6


ATOM
441
CB
TYR
B
126
75.699
37.059
−8.942
1.00
20.00
6


ATOM
442
CG
TYR
B
126
74.479
36.687
−8.127
1.00
20.00
6


ATOM
443
CD1
TYR
B
126
74.611
36.068
−6.884
1.00
20.00
6


ATOM
444
CE1
TYR
B
126
73.491
35.748
−6.112
1.00
20.00
6


ATOM
445
CD2
TYR
B
126
73.193
36.981
−8.583
1.00
20.00
6


ATOM
446
CE2
TYR
B
126
72.063
36.667
−7.817
1.00
20.00
6


ATOM
447
CZ
TYR
B
126
72.223
36.052
−6.584
1.00
20.00
6


ATOM
448
OH
TYR
B
126
71.118
35.743
−5.823
1.00
20.00
8


ATOM
449
C
TYR
B
126
77.738
38.511
−9.113
1.00
20.00
6


ATOM
450
O
TYR
B
126
78.777
38.273
−8.492
1.00
20.00
8


ATOM
451
N
VAL
B
127
77.738
38.931
−10.374
1.00
20.00
7


ATOM
452
CA
VAL
B
127
78.994
39.123
−11.085
1.00
20.00
6


ATOM
453
CB
VAL
B
127
78.756
39.466
−12.567
1.00
20.00
6


ATOM
454
CG1
VAL
B
127
80.096
39.637
−13.275
1.00
20.00
6


ATOM
455
CG2
VAL
B
127
77.949
38.357
−13.234
1.00
20.00
6


ATOM
456
C
VAL
B
127
79.798
40.242
−10.427
1.00
20.00
6


ATOM
457
O
VAL
B
127
81.016
40.148
−10.292
1.00
20.00
8


ATOM
458
N
THR
B
128
79.105
41.293
−10.006
1.00
20.00
7


ATOM
459
CA
THR
B
128
79.746
42.424
−9.345
1.00
20.00
6


ATOM
460
CB
THR
B
128
78.721
43.548
−9.070
1.00
20.00
6


ATOM
461
OG1
THR
B
128
78.194
44.025
−10.316
1.00
20.00
8


ATOM
462
CG2
THR
B
128
79.371
44.703
−8.330
1.00
20.00
6


ATOM
463
C
THR
B
128
80.372
41.979
−8.019
1.00
20.00
6


ATOM
464
O
THR
B
128
81.500
42.355
−7.696
1.00
20.00
8


ATOM
465
N
ARG
B
129
79.637
41.172
−7.256
1.00
20.00
7


ATOM
466
CA
ARG
B
129
80.126
40.678
−5.971
1.00
20.00
6


ATOM
467
CB
ARG
B
129
79.035
39.888
−5.254
1.00
20.00
6


ATOM
468
CG
ARG
B
129
79.428
39.438
−3.852
1.00
20.00
6


ATOM
469
CD
ARG
B
129
78.351
38.554
−3.278
1.00
20.00
6


ATOM
470
NE
ARG
B
129
77.048
39.209
−3.315
1.00
20.00
7


ATOM
471
CZ
ARG
B
129
75.894
38.569
−3.484
1.00
20.00
6


ATOM
472
NH1
ARG
B
129
75.878
37.250
−3.636
1.00
20.00
7


ATOM
473
NH2
ARG
B
129
74.756
39.248
−3.501
1.00
20.00
7


ATOM
474
C
ARG
B
129
81.354
39.788
−6.146
1.00
20.00
6


ATOM
475
O
ARG
B
129
82.315
39.885
−5.379
1.00
20.00
8


ATOM
476
N
GLU
B
130
81.316
38.917
−7.151
1.00
20.00
7


ATOM
477
CA
GLU
B
130
82.439
38.029
−7.421
1.00
20.00
6


ATOM
478
CB
GLU
B
130
82.191
37.211
−8.692
1.00
20.00
6


ATOM
479
CG
GLU
B
130
83.408
36.427
−9.167
1.00
20.00
6


ATOM
480
CD
GLU
B
130
83.060
35.338
−10.168
1.00
20.00
6


ATOM
481
OE1
GLU
B
130
82.227
35.590
−11.061
1.00
20.00
8


ATOM
482
OE2
GLU
B
130
83.626
34.231
−10.068
1.00
20.00
8


ATOM
483
C
GLU
B
130
83.708
38.853
−7.580
1.00
20.00
6


ATOM
484
O
GLU
B
130
84.723
38.575
−6.940
1.00
20.00
8


ATOM
485
N
ARG
B
131
83.641
39.874
−8.428
1.00
20.00
7


ATOM
486
CA
ARG
B
131
84.788
40.742
−8.673
1.00
20.00
6


ATOM
487
CB
ARG
B
131
84.459
41.759
−9.777
1.00
20.00
6


ATOM
488
CG
ARG
B
131
85.580
42.753
−10.035
1.00
20.00
6


ATOM
489
CD
ARG
B
131
85.262
43.716
−11.167
1.00
20.00
6


ATOM
490
NE
ARG
B
131
86.351
44.673
−11.355
1.00
20.00
7


ATOM
491
CZ
ARG
B
131
86.416
45.561
−12.343
1.00
20.00
6


ATOM
492
NH1
ARG
B
131
85.450
45.623
−13.250
1.00
20.00
7


ATOM
493
NH2
ARG
B
131
87.450
46.388
−12.426
1.00
20.00
7


ATOM
494
C
ARG
B
131
85.228
41.485
−7.409
1.00
20.00
6


ATOM
495
O
ARG
B
131
86.413
41.500
−7.071
1.00
20.00
8


ATOM
496
N
ASP
B
132
84.277
42.103
−6.715
1.00
20.00
7


ATOM
497
CA
ASP
B
132
84.594
42.848
−5.505
1.00
20.00
6


ATOM
498
CB
ASP
B
132
83.350
43.575
−4.987
1.00
20.00
6


ATOM
499
CG
ASP
B
132
82.865
44.658
−5.943
1.00
20.00
6


ATOM
500
OD1
ASP
B
132
83.612
45.010
−6.886
1.00
20.00
8


ATOM
501
OD2
ASP
B
132
81.739
45.167
−5.747
1.00
20.00
8


ATOM
502
C
ASP
B
132
85.192
41.969
−4.401
1.00
20.00
6


ATOM
503
O
ASP
B
132
86.191
42.337
−3.783
1.00
20.00
8


ATOM
504
N
VAL
B
133
84.596
40.809
−4.150
1.00
20.00
7


ATOM
505
CA
VAL
B
133
85.131
39.933
−3.116
1.00
20.00
6


ATOM
506
CB
VAL
B
133
84.226
38.698
−2.885
1.00
20.00
6


ATOM
507
CG1
VAL
B
133
84.920
37.713
−1.957
1.00
20.00
6


ATOM
508
CG2
VAL
B
133
82.893
39.135
−2.271
1.00
20.00
6


ATOM
509
C
VAL
B
133
86.540
39.470
−3.477
1.00
20.00
6


ATOM
510
O
VAL
B
133
87.460
39.602
−2.675
1.00
20.00
8


ATOM
511
N
MET
B
134
86.721
38.950
−4.688
1.00
20.00
7


ATOM
512
CA
MET
B
134
88.040
38.474
−5.083
1.00
20.00
6


ATOM
513
CB
MET
B
134
88.004
37.879
−6.492
1.00
20.00
6


ATOM
514
CG
MET
B
134
87.183
36.603
−6.573
1.00
20.00
6


ATOM
515
SD
MET
B
134
87.477
35.650
−8.077
1.00
20.00
16 


ATOM
516
CE
MET
B
134
88.730
34.515
−7.475
1.00
20.00
6


ATOM
517
C
MET
B
134
89.115
39.552
−4.994
1.00
20.00
6


ATOM
518
O
MET
B
134
90.253
39.264
−4.626
1.00
20.00
8


ATOM
519
N
SER
B
135
88.758
40.790
−5.319
1.00
20.00
7


ATOM
520
CA
SER
B
135
89.708
41.899
−5.260
1.00
20.00
6


ATOM
521
CB
SER
B
135
89.084
43.175
−5.836
1.00
20.00
6


ATOM
522
OG
SER
B
135
88.742
43.009
−7.202
1.00
20.00
8


ATOM
523
C
SER
B
135
90.165
42.184
−3.830
1.00
20.00
6


ATOM
524
O
SER
B
135
91.228
42.762
−3.614
1.00
20.00
8


ATOM
525
N
ARG
B
136
89.354
41.782
−2.857
1.00
20.00
7


ATOM
526
CA
ARG
B
136
89.672
42.013
−1.450
1.00
20.00
6


ATOM
527
CB
ARG
B
136
88.384
42.156
−0.637
1.00
20.00
6


ATOM
528
CG
ARG
B
136
87.509
43.336
−1.018
1.00
20.00
6


ATOM
529
CD
ARG
B
136
86.215
43.306
−0.211
1.00
20.00
6


ATOM
530
NE
ARG
B
136
86.491
43.117
1.209
1.00
20.00
7


ATOM
531
CZ
ARG
B
136
85.565
42.888
2.132
1.00
20.00
6


ATOM
532
NH1
ARG
B
136
84.285
42.821
1.786
1.00
20.00
7


ATOM
533
NH2
ARG
B
136
85.920
42.715
3.401
1.00
20.00
7


ATOM
534
C
ARG
B
136
90.506
40.891
−0.839
1.00
20.00
6


ATOM
535
O
ARG
B
136
91.091
41.054
0.231
1.00
20.00
8


ATOM
536
N
LEU
B
137
90.556
39.752
−1.515
1.00
20.00
7


ATOM
537
CA
LEU
B
137
91.300
38.609
−1.005
1.00
20.00
6


ATOM
538
CB
LEU
B
137
90.665
37.307
−1.504
1.00
20.00
6


ATOM
539
CG
LEU
B
137
89.172
37.099
−1.213
1.00
20.00
6


ATOM
540
CD1
LEU
B
137
88.748
35.728
−1.734
1.00
20.00
6


ATOM
541
CD2
LEU
B
137
88.897
37.205
0.280
1.00
20.00
6


ATOM
542
C
LEU
B
137
92.771
38.648
−1.402
1.00
20.00
6


ATOM
543
O
LEU
B
137
93.103
38.871
−2.566
1.00
20.00
8


ATOM
544
N
ASP
B
138
93.645
38.436
−0.424
1.00
20.00
7


ATOM
545
CA
ASP
B
138
95.086
38.422
−0.656
1.00
20.00
6


ATOM
546
CB
ASP
B
138
95.696
39.797
−0.352
1.00
20.00
6


ATOM
547
CG
ASP
B
138
97.179
39.854
−0.674
1.00
20.00
6


ATOM
548
OD1
ASP
B
138
97.601
39.173
−1.634
1.00
20.00
8


ATOM
549
OD2
ASP
B
138
97.920
40.581
0.022
1.00
20.00
8


ATOM
550
C
ASP
B
138
95.678
37.369
0.263
1.00
20.00
6


ATOM
551
O
ASP
B
138
96.353
37.685
1.243
1.00
20.00
8


ATOM
552
N
HIS
B
139
95.410
36.111
−0.065
1.00
20.00
7


ATOM
553
CA
HIS
B
139
95.871
34.984
0.731
1.00
20.00
6


ATOM
554
CB
HIS
B
139
94.769
34.610
1.737
1.00
20.00
6


ATOM
555
CG
HIS
B
139
95.173
33.561
2.725
1.00
20.00
6


ATOM
556
CD2
HIS
B
139
95.543
33.657
4.025
1.00
20.00
6


ATOM
557
ND1
HIS
B
139
95.241
32.221
2.405
1.00
20.00
7


ATOM
558
CE1
HIS
B
139
95.635
31.537
3.466
1.00
20.00
6


ATOM
559
NE2
HIS
B
139
95.825
32.385
4.461
1.00
20.00
7


ATOM
560
C
HIS
B
139
96.176
33.828
−0.221
1.00
20.00
6


ATOM
561
O
HIS
B
139
95.444
33.595
−1.182
1.00
20.00
8


ATOM
562
N
PRO
B
140
97.257
33.080
0.038
1.00
20.00
7


ATOM
563
CD
PRO
B
140
98.128
33.140
1.225
1.00
20.00
6


ATOM
564
CA
PRO
B
140
97.635
31.959
−0.827
1.00
20.00
6


ATOM
565
CB
PRO
B
140
98.913
31.433
−0.171
1.00
20.00
6


ATOM
566
CG
PRO
B
140
98.687
31.730
1.277
1.00
20.00
6


ATOM
567
C
PRO
B
140
96.614
30.846
−1.072
1.00
20.00
6


ATOM
568
O
PRO
B
140
96.747
30.107
−2.044
1.00
20.00
8


ATOM
569
N
PHE
B
141
95.607
30.712
−0.211
1.00
20.00
7


ATOM
570
CA
PHE
B
141
94.620
29.649
−0.398
1.00
20.00
6


ATOM
571
CB
PHE
B
141
94.206
29.056
0.961
1.00
20.00
6


ATOM
572
CG
PHE
B
141
95.321
28.335
1.681
1.00
20.00
6


ATOM
573
CD1
PHE
B
141
96.351
27.716
0.967
1.00
20.00
6


ATOM
574
CD2
PHE
B
141
95.311
28.227
3.067
1.00
20.00
6


ATOM
575
CE1
PHE
B
141
97.350
27.000
1.627
1.00
20.00
6


ATOM
576
CE2
PHE
B
141
96.307
27.510
3.740
1.00
20.00
6


ATOM
577
CZ
PHE
B
141
97.328
26.895
3.018
1.00
20.00
6


ATOM
578
C
PHE
B
141
93.371
30.063
−1.181
1.00
20.00
6


ATOM
579
O
PHE
B
141
92.335
29.398
−1.114
1.00
20.00
8


ATOM
580
N
PHE
B
142
93.471
31.150
−1.934
1.00
20.00
7


ATOM
581
CA
PHE
B
142
92.337
31.625
−2.721
1.00
20.00
6


ATOM
582
CB
PHE
B
142
91.739
32.883
−2.082
1.00
20.00
6


ATOM
583
CG
PHE
B
142
91.048
32.628
−0.772
1.00
20.00
6


ATOM
584
CD1
PHE
B
142
89.715
32.227
−0.740
1.00
20.00
6


ATOM
585
CD2
PHE
B
142
91.741
32.747
0.429
1.00
20.00
6


ATOM
586
CE1
PHE
B
142
89.080
31.944
0.472
1.00
20.00
6


ATOM
587
CE2
PHE
B
142
91.116
32.465
1.647
1.00
20.00
6


ATOM
588
CZ
PHE
B
142
89.785
32.064
1.667
1.00
20.00
6


ATOM
589
C
PHE
B
142
92.758
31.945
−4.146
1.00
20.00
6


ATOM
590
O
PHE
B
142
93.865
32.429
−4.371
1.00
20.00
8


ATOM
591
N
VAL
B
143
91.883
31.653
−5.106
1.00
20.00
7


ATOM
592
CA
VAL
B
143
92.167
31.960
−6.504
1.00
20.00
6


ATOM
593
CB
VAL
B
143
91.009
31.513
−7.435
1.00
20.00
6


ATOM
594
CG1
VAL
B
143
91.116
32.209
−8.795
1.00
20.00
6


ATOM
595
CG2
VAL
B
143
91.061
30.000
−7.623
1.00
20.00
6


ATOM
596
C
VAL
B
143
92.301
33.469
−6.545
1.00
20.00
6


ATOM
597
O
VAL
B
143
91.505
34.179
−5.932
1.00
20.00
8


ATOM
598
N
LYS
B
144
93.312
33.957
−7.252
1.00
20.00
7


ATOM
599
CA
LYS
B
144
93.547
35.392
−7.340
1.00
20.00
6


ATOM
600
CB
LYS
B
144
95.051
35.689
−7.267
1.00
20.00
6


ATOM
601
CG
LYS
B
144
95.382
37.182
−7.318
1.00
20.00
6


ATOM
602
CD
LYS
B
144
96.881
37.441
−7.201
1.00
20.00
6


ATOM
603
CE
LYS
B
144
97.191
38.936
−7.298
1.00
20.00
6


ATOM
604
NZ
LYS
B
144
98.661
39.215
−7.246
1.00
20.00
7


ATOM
605
C
LYS
B
144
92.989
36.003
−8.614
1.00
20.00
6


ATOM
606
O
LYS
B
144
92.993
35.371
−9.675
1.00
20.00
8


ATOM
607
N
LEU
B
145
92.495
37.230
−8.490
1.00
20.00
7


ATOM
608
CA
LEU
B
145
91.968
37.975
−9.624
1.00
20.00
6


ATOM
609
CB
LEU
B
145
90.678
38.703
−9.234
1.00
20.00
6


ATOM
610
CG
LEU
B
145
89.938
39.486
−10.326
1.00
20.00
6


ATOM
611
CD1
LEU
B
145
88.611
39.992
−9.782
1.00
20.00
6


ATOM
612
CD2
LEU
B
145
90.791
40.652
−10.806
1.00
20.00
6


ATOM
613
C
LEU
B
145
93.059
38.984
−9.968
1.00
20.00
6


ATOM
614
O
LEU
B
145
93.291
39.940
−9.216
1.00
20.00
8


ATOM
615
N
TYR
B
146
93.735
38.770
−11.093
1.00
20.00
7


ATOM
616
CA
TYR
B
146
94.815
39.657
−11.517
1.00
20.00
6


ATOM
617
CB
TYR
B
146
95.821
38.904
−12.389
1.00
20.00
6


ATOM
618
CG
TYR
B
146
96.624
37.858
−11.661
1.00
20.00
6


ATOM
619
CD1
TYR
B
146
96.139
36.559
−11.498
1.00
20.00
6


ATOM
620
CE1
TYR
B
146
96.894
35.589
−10.836
1.00
20.00
6


ATOM
621
CD2
TYR
B
146
97.878
38.165
−11.140
1.00
20.00
6


ATOM
622
CE2
TYR
B
146
98.639
37.208
−10.476
1.00
20.00
6


ATOM
623
CZ
TYR
B
146
98.144
35.925
−10.331
1.00
20.00
6


ATOM
624
OH
TYR
B
146
98.920
34.981
−9.706
1.00
20.00
8


ATOM
625
C
TYR
B
146
94.357
40.884
−12.293
1.00
20.00
6


ATOM
626
O
TYR
B
146
94.933
41.963
−12.160
1.00
20.00
8


ATOM
627
N
PHE
B
147
93.326
40.722
−13.110
1.00
20.00
7


ATOM
628
CA
PHE
B
147
92.855
41.832
−13.923
1.00
20.00
6


ATOM
629
CB
PHE
B
147
93.823
42.044
−15.092
1.00
20.00
6


ATOM
630
CG
PHE
B
147
94.027
40.809
−15.945
1.00
20.00
6


ATOM
631
CD1
PHE
B
147
93.049
40.397
−16.850
1.00
20.00
6


ATOM
632
CD2
PHE
B
147
95.188
40.047
−15.822
1.00
20.00
6


ATOM
633
CE1
PHE
B
147
93.221
39.247
−17.617
1.00
20.00
6


ATOM
634
CE2
PHE
B
147
95.372
38.893
−16.585
1.00
20.00
6


ATOM
635
CZ
PHE
B
147
94.388
38.490
−17.485
1.00
20.00
6


ATOM
636
C
PHE
B
147
91.473
41.566
−14.480
1.00
20.00
6


ATOM
637
O
PHE
B
147
90.972
40.442
−14.423
1.00
20.00
8


ATOM
638
N
THR
B
148
90.865
42.616
−15.021
1.00
20.00
7


ATOM
639
CA
THR
B
148
89.560
42.509
−15.643
1.00
20.00
6


ATOM
640
CB
THR
B
148
88.402
42.889
−14.678
1.00
20.00
6


ATOM
641
OG1
THR
B
148
88.492
44.275
−14.338
1.00
20.00
8


ATOM
642
CG2
THR
B
148
88.460
42.057
−13.403
1.00
20.00
6


ATOM
643
C
THR
B
148
89.532
43.469
−16.821
1.00
20.00
6


ATOM
644
O
THR
B
148
90.281
44.448
−16.866
1.00
20.00
8


ATOM
645
N
PHE
B
149
88.685
43.161
−17.791
1.00
20.00
7


ATOM
646
CA
PHE
B
149
88.508
44.011
−18.948
1.00
20.00
6


ATOM
647
CB
PHE
B
149
89.750
44.013
−19.864
1.00
20.00
6


ATOM
648
CG
PHE
B
149
90.133
42.664
−20.419
1.00
20.00
6


ATOM
649
CD1
PHE
B
149
89.552
42.182
−21.587
1.00
20.00
6


ATOM
650
CD2
PHE
B
149
91.122
41.903
−19.802
1.00
20.00
6


ATOM
651
CE1
PHE
B
149
89.953
40.965
−22.142
1.00
20.00
6


ATOM
652
CE2
PHE
B
149
91.532
40.681
−20.345
1.00
20.00
6


ATOM
653
CZ
PHE
B
149
90.948
40.213
−21.517
1.00
20.00
6


ATOM
654
C
PHE
B
149
87.271
43.498
−19.649
1.00
20.00
6


ATOM
655
O
PHE
B
149
86.714
42.474
−19.251
1.00
20.00
8


ATOM
656
N
GLN
B
150
86.812
44.221
−20.657
1.00
20.00
7


ATOM
657
CA
GLN
B
150
85.619
43.807
−21.372
1.00
20.00
6


ATOM
658
CB
GLN
B
150
84.358
44.260
−20.614
1.00
20.00
6


ATOM
659
CG
GLN
B
150
84.302
45.761
−20.289
1.00
20.00
6


ATOM
660
CD
GLN
B
150
83.011
46.172
−19.567
1.00
20.00
6


ATOM
661
OE1
GLN
B
150
81.970
46.385
−20.196
1.00
20.00
8


ATOM
662
NE2
GLN
B
150
83.078
46.273
−18.240
1.00
20.00
7


ATOM
663
C
GLN
B
150
85.598
44.400
−22.760
1.00
20.00
6


ATOM
664
O
GLN
B
150
86.281
45.387
−23.033
1.00
20.00
8


ATOM
665
N
ASP
B
151
84.846
43.766
−23.649
1.00
20.00
7


ATOM
666
CA
ASP
B
151
84.683
44.296
−24.992
1.00
20.00
6


ATOM
667
CB
ASP
B
151
85.160
43.312
−26.074
1.00
20.00
6


ATOM
668
CG
ASP
B
151
84.558
41.934
−25.939
1.00
20.00
6


ATOM
669
OD1
ASP
B
151
83.425
41.812
−25.436
1.00
20.00
8


ATOM
670
OD2
ASP
B
151
85.227
40.963
−26.365
1.00
20.00
8


ATOM
671
C
ASP
B
151
83.188
44.573
−25.095
1.00
20.00
6


ATOM
672
O
ASP
B
151
82.501
44.610
−24.069
1.00
20.00
8


ATOM
673
N
ASP
B
152
82.669
44.758
−26.301
1.00
20.00
7


ATOM
674
CA
ASP
B
152
81.251
45.062
−26.437
1.00
20.00
6


ATOM
675
CB
ASP
B
152
80.907
45.346
−27.901
1.00
20.00
6


ATOM
676
CG
ASP
B
152
81.616
46.574
−28.432
1.00
20.00
6


ATOM
677
OD1
ASP
B
152
81.748
47.555
−27.666
1.00
20.00
8


ATOM
678
OD2
ASP
B
152
82.030
46.563
−29.613
1.00
20.00
8


ATOM
679
C
ASP
B
152
80.285
44.020
−25.888
1.00
20.00
6


ATOM
680
O
ASP
B
152
79.229
44.367
−25.357
1.00
20.00
8


ATOM
681
N
GLU
B
153
80.641
42.747
−25.982
1.00
20.00
7


ATOM
682
CA
GLU
B
153
79.727
41.711
−25.521
1.00
20.00
6


ATOM
683
CB
GLU
B
153
79.516
40.685
−26.641
1.00
20.00
6


ATOM
684
CG
GLU
B
153
79.577
41.260
−28.058
1.00
20.00
6


ATOM
685
CD
GLU
B
153
81.006
41.472
−28.550
1.00
20.00
6


ATOM
686
OE1
GLU
B
153
81.765
40.480
−28.635
1.00
20.00
8


ATOM
687
OE2
GLU
B
153
81.374
42.627
−28.854
1.00
20.00
8


ATOM
688
C
GLU
B
153
80.102
40.960
−24.247
1.00
20.00
6


ATOM
689
O
GLU
B
153
79.222
40.473
−23.535
1.00
20.00
8


ATOM
690
N
LYS
B
154
81.393
40.869
−23.944
1.00
20.00
7


ATOM
691
CA
LYS
B
154
81.818
40.091
−22.787
1.00
20.00
6


ATOM
692
CB
LYS
B
154
82.549
38.830
−23.273
1.00
20.00
6


ATOM
693
CG
LYS
B
154
81.785
37.978
−24.278
1.00
20.00
6


ATOM
694
CD
LYS
B
154
82.727
37.028
−25.021
1.00
20.00
6


ATOM
695
CE
LYS
B
154
81.968
36.086
−25.952
1.00
20.00
6


ATOM
696
NZ
LYS
B
154
82.894
35.300
−26.826
1.00
20.00
7


ATOM
697
C
LYS
B
154
82.709
40.767
−21.756
1.00
20.00
6


ATOM
698
O
LYS
B
154
83.412
41.740
−22.048
1.00
20.00
8


ATOM
699
N
LEU
B
155
82.677
40.202
−20.551
1.00
20.00
7


ATOM
700
CA
LEU
B
155
83.501
40.638
−19.428
1.00
20.00
6


ATOM
701
CB
LEU
B
155
82.700
40.651
−18.127
1.00
20.00
6


ATOM
702
CG
LEU
B
155
81.451
41.521
−18.004
1.00
20.00
6


ATOM
703
CD1
LEU
B
155
80.805
41.273
−16.645
1.00
20.00
6


ATOM
704
CD2
LEU
B
155
81.831
42.983
−18.152
1.00
20.00
6


ATOM
705
C
LEU
B
155
84.578
39.559
−19.302
1.00
20.00
6


ATOM
706
O
LEU
B
155
84.288
38.379
−19.495
1.00
20.00
8


ATOM
707
N
TYR
B
156
85.802
39.956
−18.966
1.00
20.00
7


ATOM
708
CA
TYR
B
156
86.893
38.998
−18.809
1.00
20.00
6


ATOM
709
CB
TYR
B
156
87.953
39.189
−19.904
1.00
20.00
6


ATOM
710
CG
TYR
B
156
87.450
39.053
−21.324
1.00
20.00
6


ATOM
711
CD1
TYR
B
156
86.688
40.061
−21.920
1.00
20.00
6


ATOM
712
CE1
TYR
B
156
86.233
39.938
−23.235
1.00
20.00
6


ATOM
713
CD2
TYR
B
156
87.741
37.917
−22.077
1.00
20.00
6


ATOM
714
CE2
TYR
B
156
87.288
37.782
−23.387
1.00
20.00
6


ATOM
715
CZ
TYR
B
156
86.538
38.794
−23.958
1.00
20.00
6


ATOM
716
OH
TYR
B
156
86.087
38.656
−25.246
1.00
20.00
8


ATOM
717
C
TYR
B
156
87.566
39.182
−17.447
1.00
20.00
6


ATOM
718
O
TYR
B
156
87.977
40.291
−17.110
1.00
20.00
8


ATOM
719
N
PHE
B
157
87.657
38.104
−16.667
1.00
20.00
7


ATOM
720
CA
PHE
B
157
88.325
38.152
−15.367
1.00
20.00
6


ATOM
721
CB
PHE
B
157
87.448
37.575
−14.246
1.00
20.00
6


ATOM
722
CG
PHE
B
157
86.194
38.360
−13.968
1.00
20.00
6


ATOM
723
CD1
PHE
B
157
85.986
39.614
−14.535
1.00
20.00
6


ATOM
724
CD2
PHE
B
157
85.206
37.828
−13.143
1.00
20.00
6


ATOM
725
CE1
PHE
B
157
84.808
40.324
−14.290
1.00
20.00
6


ATOM
726
CE2
PHE
B
157
84.025
38.532
−12.893
1.00
20.00
6


ATOM
727
CZ
PHE
B
157
83.829
39.782
−13.470
1.00
20.00
6


ATOM
728
C
PHE
B
157
89.579
37.295
−15.471
1.00
20.00
6


ATOM
729
O
PHE
B
157
89.492
36.105
−15.765
1.00
20.00
8


ATOM
730
N
GLY
B
158
90.742
37.893
−15.231
1.00
20.00
7


ATOM
731
CA
GLY
B
158
91.985
37.146
−15.303
1.00
20.00
6


ATOM
732
C
GLY
B
158
92.254
36.512
−13.955
1.00
20.00
6


ATOM
733
O
GLY
B
158
92.575
37.211
−12.996
1.00
20.00
8


ATOM
734
N
LEU
B
159
92.137
35.191
13.886
1.00
20.00
7


ATOM
735
CA
LEU
B
159
92.330
34.466
−12.634
1.00
20.00
6


ATOM
736
CB
LEU
B
159
91.116
33.580
−12.358
1.00
20.00
6


ATOM
737
CG
LEU
B
159
89.724
34.208
−12.490
1.00
20.00
6


ATOM
738
CD1
LEU
B
159
88.670
33.111
−12.398
1.00
20.00
6


ATOM
739
CD2
LEU
B
159
89.513
35.246
−11.404
1.00
20.00
6


ATOM
740
C
LEU
B
159
93.562
33.582
−12.643
1.00
20.00
6


ATOM
741
O
LEU
B
159
94.061
33.204
−13.698
1.00
20.00
8


ATOM
742
N
SER
B
160
94.046
33.237
−11.457
1.00
20.00
7


ATOM
743
CA
SER
B
160
95.192
32.356
−11.377
1.00
20.00
6


ATOM
744
CB
SER
B
160
95.665
32.206
−9.926
1.00
20.00
6


ATOM
745
OG
SER
B
160
94.591
31.973
'19.042
1.00
20.00
8


ATOM
746
C
SER
B
160
94.754
31.012
−11.951
1.00
20.00
6


ATOM
747
O
SER
B
160
93.598
30.605
−11.813
1.00
20.00
8


ATOM
748
N
TYR
B
161
95.674
30.339
−12.625
1.00
20.00
7


ATOM
749
CA
TYR
B
161
95.381
29.050
−13.231
1.00
20.00
6


ATOM
750
CB
TYR
B
161
96.170
28.924
−14.543
1.00
20.00
6


ATOM
751
CG
TYR
B
161
96.128
27.564
−15.209
1.00
20.00
6


ATOM
752
CD1
TYR
B
161
94.968
26.787
−15.193
1.00
20.00
6


ATOM
753
CE1
TYR
B
161
94.915
25.554
−15.846
1.00
20.00
6


ATOM
754
CD2
TYR
B
161
97.240
27.073
−15.895
1.00
20.00
6


ATOM
755
CE2
TYR
B
161
97.198
25.841
−16.553
1.00
20.00
6


ATOM
756
CZ
TYR
B
161
96.033
25.088
−16.523
1.00
20.00
6


ATOM
757
OH
TYR
B
161
95.983
23.877
−17.173
1.00
20.00
8


ATOM
758
C
TYR
B
161
95.724
27.905
−12.277
1.00
20.00
6


ATOM
759
O
TYR
B
161
96.897
27.598
−12.065
1.00
20.00
8


ATOM
760
N
ALA
B
162
94.696
27.288
−11.697
1.00
20.00
7


ATOM
761
CA
ALA
B
162
94.893
26.166
−10.776
1.00
20.00
6


ATOM
762
CB
ALA
B
162
93.666
25.995
−9.873
1.00
20.00
6


ATOM
763
C
ALA
B
162
95.100
24.924
−11.637
1.00
20.00
6


ATOM
764
O
ALA
B
162
94.146
24.251
−12.015
1.00
20.00
8


ATOM
765
N
LYS
B
163
96.361
24.626
−11.930
1.00
20.00
7


ATOM
766
CA
LYS
B
163
96.722
23.506
−12.795
1.00
20.00
6


ATOM
767
CB
LYS
B
163
98.247
23.416
−12.912
1.00
20.00
6


ATOM
768
CG
LYS
B
163
98.904
24.711
−13.360
1.00
20.00
6


ATOM
769
CD
LYS
B
163
100.405
24.539
13.554
1.00
20.00
6


ATOM
770
CE
LYS
B
163
101.102
25.885
−13.690
1.00
20.00
6


ATOM
771
NZ
LYS
B
163
100.976
26.701
−12.445
1.00
20.00
7


ATOM
772
C
LYS
B
163
96.170
22.123
12.464
1.00
20.00
6


ATOM
773
O
LYS
B
163
95.823
21.370
−13.369
1.00
20.00
8


ATOM
774
N
ASN
B
164
96.076
21.775
−11.186
1.00
20.00
7


ATOM
775
CA
ASN
B
164
95.594
20.449
−10.842
1.00
20.00
6


ATOM
776
CB
ASN
B
164
96.339
19.944
−9.610
1.00
20.00
6


ATOM
777
CG
ASN
B
164
97.766
19.529
−9.943
1.00
20.00
6


ATOM
778
OD1
ASN
B
164
97.992
18.776
−10.892
1.00
20.00
8


ATOM
779
ND2
ASN
B
164
98.730
20.014
−9.171
1.00
20.00
7


ATOM
780
C
ASN
B
164
94.084
20.246
−10.706
1.00
20.00
6


ATOM
781
O
ASN
B
164
93.630
19.183
−10.286
1.00
20.00
8


ATOM
782
N
GLY
B
165
93.309
21.257
−11.080
1.00
20.00
7


ATOM
783
CA
GLY
B
165
91.863
21.127
−11.039
1.00
20.00
6


ATOM
784
C
GLY
B
165
91.159
21.088
9.694
1.00
20.00
6


ATOM
785
O
GLY
B
165
91.663
21.598
8.698
1.00
20.00
8


ATOM
786
N
GLU
B
166
89.986
20.461
−9.689
1.00
20.00
7


ATOM
787
CA
GLU
B
166
89.126
20.344
−8.513
1.00
20.00
6


ATOM
788
CB
GLU
B
166
87.683
20.079
−8.962
1.00
20.00
6


ATOM
789
CG
GLU
B
166
86.992
21.255
−9.646
1.00
20.00
6


ATOM
790
CD
GLU
B
166
85.709
20.837
−10.358
1.00
20.00
6


ATOM
791
OE1
GLU
B
166
85.137
19.794
−9.986
1.00
20.00
8


ATOM
792
OE2
GLU
B
166
85.263
21.556
−11.279
1.00
20.00
8


ATOM
793
C
GLU
B
166
89.520
19.270
−7.506
1.00
20.00
6


ATOM
794
O
GLU
B
166
89.952
18.184
−7.874
1.00
20.00
8


ATOM
795
N
LEU
B
167
89.344
19.579
−6.226
1.00
20.00
7


ATOM
796
CA
LEU
B
167
89.651
18.626
−5.168
1.00
20.00
6


ATOM
797
CB
LEU
B
167
89.395
19.269
−3.802
1.00
20.00
6


ATOM
798
CG
LEU
B
167
89.408
18.363
−2.569
1.00
20.00
6


ATOM
799
CD1
LEU
B
167
90.769
17.703
−2.412
1.00
20.00
6


ATOM
800
CD2
LEU
B
167
89.065
19.193
−1.338
1.00
20.00
6


ATOM
801
C
LEU
B
167
88.757
17.394
−5.346
1.00
20.00
6


ATOM
802
O
LEU
B
167
89.124
16.283
−4.968
1.00
20.00
8


ATOM
803
N
LEU
B
168
87.580
17.600
−5.927
1.00
20.00
7


ATOM
804
CA
LEU
B
168
86.647
16.500
−6.153
1.00
20.00
6


ATOM
805
CB
LEU
B
168
85.364
17.014
−6.809
1.00
20.00
6


ATOM
806
CG
LEU
B
168
84.292
15.977
−7.168
1.00
20.00
6


ATOM
807
CD1
LEU
B
168
83.883
15.186
−5.929
1.00
20.00
6


ATOM
808
CD2
LEU
B
168
83.083
16.687
−7.756
1.00
20.00
6


ATOM
809
C
LEU
B
168
87.290
15.440
−7.046
1.00
20.00
6


ATOM
810
O
LEU
B
168
87.091
14.243
−6.845
1.00
20.00
8


ATOM
811
N
LYS
B
169
88.068
15.888
−8.027
1.00
20.00
7


ATOM
812
CA
LYS
B
169
88.727
14.967
−8.941
1.00
20.00
6


ATOM
813
CB
LYS
B
169
89.610
15.729
−9.930
1.00
20.00
6


ATOM
814
CG
LYS
B
169
90.379
14.818
−10.882
1.00
20.00
6


ATOM
815
CD
LYS
B
169
91.226
15.603
−11.877
1.00
20.00
6


ATOM
816
CE
LYS
B
169
92.373
16.328
−11.192
1.00
20.00
6


ATOM
817
NZ
LYS
B
169
93.253
17.021
−12.173
1.00
20.00
7


ATOM
818
C
LYS
B
169
89.574
13.949
−8.193
1.00
20.00
6


ATOM
819
O
LYS
B
169
89.543
12.758
−8.504
1.00
20.00
8


ATOM
820
N
TYR
B
170
90.334
14.417
−7.207
1.00
20.00
7


ATOM
821
CA
TYR
B
170
91.197
13.527
−6.441
1.00
20.00
6


ATOM
822
CB
TYR
B
170
92.243
14.346
−5.682
1.00
20.00
6


ATOM
823
CG
TYR
B
170
93.217
15.010
−6.624
1.00
20.00
6


ATOM
824
CD1
TYR
B
170
94.347
14.331
−7.085
1.00
20.00
6


ATOM
825
CE1
TYR
B
170
95.195
14.900
−8.036
1.00
20.00
6


ATOM
826
CD2
TYR
B
170
92.963
16.282
−7.133
1.00
20.00
6


ATOM
827
CE2
TYR
B
170
93.801
16.861
−8.083
1.00
20.00
6


ATOM
828
CZ
TYR
B
170
94.913
16.164
−8.532
1.00
20.00
6


ATOM
829
OH
TYR
B
170
95.727
16.727
−9.493
1.00
20.00
8


ATOM
830
C
TYR
B
170
90.419
12.622
−5.499
1.00
20.00
6


ATOM
831
O
TYR
B
170
90.834
11.494
−5.233
1.00
20.00
8


ATOM
832
N
ILE
B
171
89.287
13.098
−4.993
1.00
20.00
7


ATOM
833
CA
ILE
B
171
88.488
12.262
−4.112
1.00
20.00
6


ATOM
834
CB
ILE
B
171
87.278
13.028
−3.538
1.00
20.00
6


ATOM
835
CG2
ILE
B
171
86.367
12.065
−2.791
1.00
20.00
6


ATOM
836
CG1
ILE
B
171
87.764
14.141
−2.603
1.00
20.00
6


ATOM
837
CD1
ILE
B
171
86.652
14.990
−2.019
1.00
20.00
6


ATOM
838
C
ILE
B
171
87.994
11.066
−4.931
1.00
20.00
6


ATOM
839
O
ILE
B
171
88.030
9.925
−4.468
1.00
20.00
8


ATOM
840
N
ARG
B
172
87.550
11.331
−6.156
1.00
20.00
7


ATOM
841
CA
ARG
B
172
87.061
10.273
−7.031
1.00
20.00
6


ATOM
842
CB
ARG
B
172
86.359
10.861
−8.259
1.00
20.00
6


ATOM
843
CG
ARG
B
172
85.094
11.658
−7.963
1.00
20.00
6


ATOM
844
CD
ARG
B
172
84.352
11.981
−9.259
1.00
20.00
6


ATOM
845
NE
ARG
B
172
83.187
12.843
−9.063
1.00
20.00
7


ATOM
846
CZ
ARG
B
172
82.192
12.589
−8.217
1.00
20.00
6


ATOM
847
NH1
ARG
B
172
82.209
11.491
−7.469
1.00
20.00
7


ATOM
848
NH2
ARG
B
172
81.168
13.428
−8.127
1.00
20.00
7


ATOM
849
C
ARG
B
172
88.202
9.378
−7.497
1.00
20.00
6


ATOM
850
O
ARG
B
172
88.050
8.160
−7.587
1.00
20.00
8


ATOM
851
N
LYS
B
173
89.348
9.985
−7.783
1.00
20.00
7


ATOM
852
CA
LYS
B
173
90.509
9.244
−8.256
1.00
20.00
6


ATOM
853
CB
LYS
B
173
91.647
10.206
−8.603
1.00
20.00
6


ATOM
854
CG
LYS
B
173
92.930
9.511
−9.045
1.00
20.00
6


ATOM
855
CD
LYS
B
173
94.081
10.496
−9.222
1.00
20.00
6


ATOM
856
CE
LYS
B
173
93.862
11.432
−10.406
1.00
20.00
6


ATOM
857
NZ
LYS
B
173
93.858
10.711
−11.715
1.00
20.00
7


ATOM
858
C
LYS
B
173
91.025
8.191
−7.280
1.00
20.00
6


ATOM
859
O
LYS
B
173
91.274
7.055
−7.674
1.00
20.00
8


ATOM
860
N
ILE
B
174
91.192
8.554
−6.012
1.00
20.00
7


ATOM
861
CA
ILE
B
174
91.710
7.593
−5.042
1.00
20.00
6


ATOM
862
CB
ILE
B
174
92.884
8.191
−4.223
1.00
20.00
6


ATOM
863
CG2
ILE
B
174
93.970
8.701
−5.166
1.00
20.00
6


ATOM
864
CG1
ILE
B
174
92.394
9.337
−3.343
1.00
20.00
6


ATOM
865
CD1
ILE
B
174
93.480
9.916
−2.457
1.00
20.00
6


ATOM
866
C
ILE
B
174
90.674
7.030
−4.074
1.00
20.00
6


ATOM
867
O
ILE
B
174
91.025
6.296
−3.151
1.00
20.00
8


ATOM
868
N
GLY
B
175
89.405
7.367
−4.283
1.00
20.00
7


ATOM
869
CA
GLY
B
175
88.359
6.855
−3.413
1.00
20.00
6


ATOM
870
C
GLY
B
175
88.160
7.650
−2.138
1.00
20.00
6


ATOM
871
O
GLY
B
175
87.083
8.198
−1.905
1.00
20.00
8


ATOM
872
N
SER
B
176
89.192
7.701
−1.304
1.00
20.00
7


ATOM
873
CA
SER
B
176
89.140
8.447
−0.053
1.00
20.00
6


ATOM
874
CB
SER
B
176
88.395
7.653
1.026
1.00
20.00
6


ATOM
875
OG
SER
B
176
89.150
6.543
1.472
1.00
20.00
8


ATOM
876
C
SER
B
176
90.565
8.742
0.401
1.00
20.00
6


ATOM
877
O
SER
B
176
91.506
8.049
0.009
1.00
20.00
8


ATOM
878
N
PHE
B
177
90.718
9.769
1.228
1.00
20.00
7


ATOM
879
CA
PHE
B
177
92.029
10.184
1.722
1.00
20.00
6


ATOM
880
CB
PHE
B
177
92.028
11.694
1.990
1.00
20.00
6


ATOM
881
CG
PHE
B
177
92.002
12.546
0.747
1.00
20.00
6


ATOM
882
CD1
PHE
B
177
91.484
12.060
−0.449
1.00
20.00
6


ATOM
883
CD2
PHE
B
177
92.481
13.855
0.787
1.00
20.00
6


ATOM
884
CE1
PHE
B
177
91.443
12.860
−1.585
1.00
20.00
6


ATOM
885
CE2
PHE
B
177
92.444
14.665
−0.343
1.00
20.00
6


ATOM
886
CZ
PHE
B
177
91.925
14.168
−1.532
1.00
20.00
6


ATOM
887
C
PHE
B
177
92.427
9.475
3.009
1.00
20.00
6


ATOM
888
O
PHE
B
177
91.582
9.223
3.872
1.00
20.00
8


ATOM
889
N
ASP
B
178
93.711
9.152
3.147
1.00
20.00
7


ATOM
890
CA
ASP
B
178
94.155
8.529
4.385
1.00
20.00
6


ATOM
891
CB
ASP
B
178
95.581
7.972
4.267
1.00
20.00
6


ATOM
892
CG
ASP
B
178
96.594
9.018
3.845
1.00
20.00
6


ATOM
893
OD1
ASP
B
178
96.392
10.214
4.139
1.00
20.00
8


ATOM
894
OD2
ASP
B
178
97.612
8.634
3.230
1.00
20.00
8


ATOM
895
C
ASP
B
178
94.092
9.640
5.436
1.00
20.00
6


ATOM
896
O
ASP
B
178
93.736
10.778
5.117
1.00
20.00
8


ATOM
897
N
GLU
B
179
94.443
9.324
6.677
1.00
20.00
7


ATOM
898
CA
GLU
B
179
94.380
10.311
7.744
1.00
20.00
6


ATOM
899
CB
GLU
B
179
94.623
9.637
9.096
1.00
20.00
6


ATOM
900
CG
GLU
B
179
94.747
10.611
10.255
1.00
20.00
6


ATOM
901
CD
GLU
B
179
94.331
9.994
11.574
1.00
20.00
6


ATOM
902
OE1
GLU
B
179
94.589
8.789
11.770
1.00
20.00
8


ATOM
903
OE2
GLU
B
179
93.753
10.717
12.416
1.00
20.00
8


ATOM
904
C
GLU
B
179
95.320
11.501
7.575
1.00
20.00
6


ATOM
905
O
GLU
B
179
94.948
12.636
7.881
1.00
20.00
8


ATOM
906
N
THR
B
180
96.528
11.246
7.086
1.00
20.00
7


ATOM
907
CA
THR
B
180
97.509
12.308
6.886
1.00
20.00
6


ATOM
908
CB
THR
B
180
98.866
11.720
6.445
1.00
20.00
6


ATOM
909
OG1
THR
B
180
99.349
10.842
7.466
1.00
20.00
8


ATOM
910
CG2
THR
B
180
99.888
12.825
6.213
1.00
20.00
6


ATOM
911
C
THR
B
180
97.040
13.331
5.849
1.00
20.00
6


ATOM
912
O
THR
B
180
97.136
14.542
6.069
1.00
20.00
8


ATOM
913
N
CYS
B
181
96.534
12.845
4.721
1.00
20.00
7


ATOM
914
CA
CYS
B
181
96.057
13.733
3.666
1.00
20.00
6


ATOM
915
CB
CYS
B
181
95.836
12.945
2.375
1.00
20.00
6


ATOM
916
SG
CYS
B
181
97.372
12.255
1.685
1.00
20.00
16


ATOM
917
C
CYS
B
181
94.775
14.449
4.079
1.00
20.00
6


ATOM
918
O
CYS
B
181
94.570
15.615
3.733
1.00
20.00
8


ATOM
919
N
THR
B
182
93.914
13.755
4.820
1.00
20.00
7


ATOM
920
CA
THR
B
182
92.669
14.356
5.286
1.00
20.00
6


ATOM
921
CB
THR
B
182
91.812
13.354
6.103
1.00
20.00
6


ATOM
922
OG1
THR
B
182
91.372
12.283
5.259
1.00
20.00
8


ATOM
923
CG2
THR
B
182
90.600
14.054
6.690
1.00
20.00
6


ATOM
924
C
THR
B
182
93.014
15.535
6.196
1.00
20.00
6


ATOM
925
O
THR
B
182
92.515
16.649
6.019
1.00
20.00
8


ATOM
926
N
ARG
B
183
93.873
15.273
7.175
1.00
20.00
7


ATOM
927
CA
ARG
B
183
94.299
16.293
8.121
1.00
20.00
6


ATOM
928
CB
ARG
B
183
95.311
15.707
9.109
1.00
20.00
6


ATOM
929
CG
ARG
B
183
95.957
16.744
10.012
1.00
20.00
6


ATOM
930
CD
ARG
B
183
96.886
16.116
11.050
1.00
20.00
6


ATOM
931
NE
ARG
B
183
96.167
15.220
11.949
1.00
20.00
7


ATOM
932
CZ
ARG
B
183
96.098
13.900
11.804
1.00
20.00
6


ATOM
933
NH1
ARG
B
183
96.717
13.306
10.791
1.00
20.00
7


ATOM
934
NH2
ARG
B
183
95.389
13.176
12.664
1.00
20.00
7


ATOM
935
C
ARG
B
183
94.923
17.505
7.427
1.00
20.00
6


ATOM
936
O
ARG
B
183
94.545
18.646
7.698
1.00
20.00
8


ATOM
937
N
PHE
B
184
95.877
17.264
6.534
1.00
20.00
7


ATOM
938
CA
PHE
B
184
96.539
18.367
5.847
1.00
20.00
6


ATOM
939
CB
PHE
B
184
97.610
17.847
4.889
1.00
20.00
6


ATOM
940
CG
PHE
B
184
98.387
18.943
4.223
1.00
20.00
6


ATOM
941
CD1
PHE
B
184
99.451
19.555
4.879
1.00
20.00
6


ATOM
942
CD2
PHE
B
184
98.009
19.415
2.975
1.00
20.00
6


ATOM
943
CE1
PHE
B
184
100.125
20.627
4.301
1.00
20.00
6


ATOM
944
CE2
PHE
B
184
98.676
20.491
2.388
1.00
20.00
6


ATOM
945
CZ
PHE
B
184
99.735
21.097
3.053
1.00
20.00
6


ATOM
946
C
PHE
B
184
95.580
19.267
5.066
1.00
20.00
6


ATOM
947
O
PHE
B
184
95.567
20.481
5.255
1.00
20.00
8


ATOM
948
N
TYR
B
185
94.784
18.679
4.181
1.00
20.00
7


ATOM
949
CA
TYR
B
185
93.854
19.471
3.390
1.00
20.00
6


ATOM
950
CB
TYR
B
185
93.305
18.634
2.236
1.00
20.00
6


ATOM
951
CG
TYR
B
185
94.337
18.504
1.140
1.00
20.00
6


ATOM
952
CD1
TYR
B
185
94.611
19.580
0.293
1.00
20.00
6


ATOM
953
CE1
TYR
B
185
95.637
19.516
−0.643
1.00
20.00
6


ATOM
954
CD2
TYR
B
185
95.118
17.352
1.017
1.00
20.00
6


ATOM
955
CE2
TYR
B
185
96.152
17.282
0.081
1.00
20.00
6


ATOM
956
CZ
TYR
B
185
96.405
18.367
−0.742
1.00
20.00
6


ATOM
957
OH
TYR
B
185
97.436
18.314
−1.657
1.00
20.00
8


ATOM
958
C
TYR
B
185
92.738
20.098
4.208
1.00
20.00
6


ATOM
959
O
TYR
B
185
92.286
21.195
3.891
1.00
20.00
8


ATOM
960
N
THR
B
186
92.303
19.422
5.267
1.00
20.00
7


ATOM
961
CA
THR
B
186
91.265
19.987
6.122
1.00
20.00
6


ATOM
962
CB
THR
B
186
90.799
18.996
7.219
1.00
20.00
6


ATOM
96
OG1
THR
B
186
90.193
17.846
6.606
1.00
20.00
8


ATOM
964
CG2
THR
B
186
89.774
19.671
8.144
1.00
20.00
6


ATOM
965
C
THR
B
186
91.858
21.218
6.805
1.00
20.00
6


ATOM
966
O
THR
B
186
91.188
22.242
6.948
1.00
20.00
8


ATOM
967
N
ALA
B
187
93.120
21.115
7.222
1.00
20.00
7


ATOM
968
CA
ALA
B
187
93.787
22.234
7.882
1.00
20.00
6


ATOM
969
CB
ALA
B
187
95.184
21.817
8.349
1.00
20.00
6


ATOM
970
C
ALA
B
187
93.879
23.449
6.946
1.00
20.00
6


ATOM
971
O
ALA
B
187
93.654
24.585
7.372
1.00
20.00
8


ATOM
972
N
GLU
B
188
94.205
23.222
5.674
1.00
20.00
7


ATOM
973
CA
GLU
B
188
94.292
24.343
4.740
1.00
20.00
6


ATOM
974
CB
GLU
B
188
94.843
23.898
3.376
1.00
20.00
6


ATOM
975
CG
GLU
B
188
96.285
23.391
3.407
1.00
20.00
6


ATOM
976
CD
GLU
B
188
97.030
23.639
2.104
1.00
20.00
6


ATOM
977
OE1
GLU
B
188
96.407
23.537
1.024
1.00
20.00
8


ATOM
978
OE2
GLU
B
188
98.247
23.932
2.156
1.00
20.00
8


ATOM
979
C
GLU
B
188
92.912
24.977
4.561
1.00
20.00
6


ATOM
980
O
GLU
B
188
92.782
26.196
4.533
1.00
20.00
8


ATOM
981
N
ILE
B
189
91.875
24.152
4.451
1.00
20.00
7


ATOM
982
CA
ILE
B
189
90.530
24.693
4.284
1.00
20.00
6


ATOM
983
CB
ILE
B
189
89.495
23.566
4.064
1.00
20.00
6


ATOM
984
CG2
ILE
B
189
88.094
24.157
3.947
1.00
20.00
6


ATOM
985
CG1
ILE
B
189
89.855
22.773
2.796
1.00
20.00
6


ATOM
986
CD1
ILE
B
189
89.058
21.488
2.616
1.00
20.00
6


ATOM
987
C
ILE
B
189
90.152
25.517
5.519
1.00
20.00
6


ATOM
988
O
ILE
B
189
89.634
26.630
5.396
1.00
20.00
8


ATOM
989
N
VAL
B
190
90.412
24.971
6.707
1.00
20.00
7


ATOM
990
CA
VAL
B
190
90.116
25.674
7.957
1.00
20.00
6


ATOM
991
CB
VAL
B
190
90.557
24.842
9.186
1.00
20.00
6


ATOM
992
CG1
VAL
B
190
90.540
25.717
10.451
1.00
20.00
6


ATOM
993
CG2
VAL
B
190
89.643
23.641
9.358
1.00
20.00
6


ATOM
994
C
VAL
B
190
90.865
27.012
7.984
1.00
20.00
6


ATOM
995
O
VAL
B
190
90.311
28.039
8.375
1.00
20.00
8


ATOM
996
N
SER
B
191
92.125
26.997
7.557
1.00
20.00
7


ATOM
997
CA
SER
B
191
92.934
28.218
7.546
1.00
20.00
6


ATOM
998
CB
SER
B
191
94.378
27.888
7.166
1.00
20.00
6


ATOM
999
OG
SER
B
191
95.220
29.007
7.363
1.00
20.00
8


ATOM
1000
C
SER
B
191
92.361
29.240
6.566
1.00
20.00
6


ATOM
1001
O
SER
B
191
92.351
30.444
6.838
1.00
20.00
8


ATOM
1002
N
ALA
B
192
91.882
28.754
5.425
1.00
20.00
7


ATOM
1003
CA
ALA
B
192
91.306
29.634
4.417
1.00
20.00
6


ATOM
1004
CB
ALA
B
192
91.006
28.850
3.141
1.00
20.00
6


ATOM
1005
C
ALA
B
192
90.029
30.256
4.970
1.00
20.00
6


ATOM
1006
O
ALA
B
192
89.799
31.458
4.822
1.00
20.00
8


ATOM
1007
N
LEU
B
193
89.203
29.439
5.621
1.00
20.00
7


ATOM
1008
CA
LEU
B
193
87.957
29.941
6.192
1.00
20.00
6


ATOM
1009
CB
LEU
B
193
87.101
28.783
6.725
1.00
20.00
6


ATOM
1010
CG
LEU
B
193
86.447
27.898
5.650
1.00
20.00
6


ATOM
1011
CD1
LEU
B
193
85.645
26.771
6.315
1.00
20.00
6


ATOM
1012
CD2
LEU
B
193
85.530
28.752
4.780
1.00
20.00
6


ATOM
1013
C
LEU
B
193
88.215
30.959
7.299
1.00
20.00
6


ATOM
1014
O
LEU
B
193
87.474
31.935
7.435
1.00
20.00
8


ATOM
1015
N
GLU
B
194
89.254
30.738
8.100
1.00
20.00
7


ATOM
1016
CA
GLU
B
194
89.562
31.699
9.157
1.00
20.00
6


ATOM
1017
CB
GLU
B
194
90.773
31.257
9.982
1.00
20.00
6


ATOM
1018
CG
GLU
B
194
91.288
32.353
10.914
1.00
20.00
6


ATOM
1019
CD
GLU
B
194
92.381
31.878
11.855
1.00
20.00
6


ATOM
1020
OE1
GLU
B
194
93.246
31.090
11.420
1.00
20.00
8


ATOM
1021
OE2
GLU
B
194
92.376
32.312
13.031
1.00
20.00
8


ATOM
1022
C
GLU
B
194
89.847
33.053
8.511
1.00
20.00
6


ATOM
1023
O
GLU
B
194
89.375
34.083
8.972
1.00
20.00
8


ATOM
1024
N
TYR
B
195
90.608
33.046
7.426
1.00
20.00
7


ATOM
1025
CA
TYR
B
195
90.928
34.294
6.743
1.00
20.00
6


ATOM
1026
CB
TYR
B
195
91.919
34.043
5.613
1.00
20.00
6


ATOM
1027
CG
TYR
B
195
92.193
35.271
4.774
1.00
20.00
6


ATOM
1028
CD1
TYR
B
195
93.098
36.244
5.202
1.00
20.00
6


ATOM
1029
CE1
TYR
B
195
93.356
37.382
4.429
1.00
20.00
6


ATOM
1030
CD2
TYR
B
195
91.545
35.461
3.553
1.00
20.00
6


ATOM
1031
CE2
TYR
B
195
91.794
36.591
2.775
1.00
20.00
6


ATOM
1032
CZ
TYR
B
195
92.701
37.545
3.219
1.00
20.00
6


ATOM
1033
OH
TYR
B
195
92.956
38.656
2.450
1.00
20.00
8


ATOM
1034
C
TYR
B
195
89.668
34.923
6.160
1.00
20.00
6


ATOM
1035
O
TYR
B
195
89.409
36.117
6.328
1.00
20.00
8


ATOM
1036
N
LEU
B
196
88.885
34.103
5.472
1.00
20.00
7


ATOM
1037
CA
LEU
B
196
87.664
34.576
4.845
1.00
20.00
6


ATOM
1038
CB
LEU
B
196
86.972
33.426
4.107
1.00
20.00
6


ATOM
1039
CG
LEU
B
196
85.933
33.824
3.060
1.00
20.00
6


ATOM
1040
CD1
LEU
B
196
86.602
34.659
1.966
1.00
20.00
6


ATOM
1041
CD2
LEU
B
196
85.305
32.568
2.463
1.00
20.00
6


ATOM
1042
C
LEU
B
196
86.731
35.161
5.888
1.00
20.00
6


ATOM
1043
O
LEU
B
196
86.299
36.308
5.774
1.00
20.00
8


ATOM
1044
N
HIS
B
197
86.431
34.378
6.917
1.00
20.00
7


ATOM
1045
CA
HIS
B
197
85.533
34.840
7.967
1.00
20.00
6


ATOM
1046
CB
HIS
B
197
85.241
33.697
8.942
1.00
20.00
6


ATOM
1047
CG
HIS
B
197
84.377
32.622
8.356
1.00
20.00
6


ATOM
1048
CD2
HIS
B
197
83.734
32.550
7.163
1.00
20.00
6


ATOM
1049
ND1
HIS
B
197
84.083
31.452
9.022
1.00
20.00
7


ATOM
1050
CE1
HIS
B
197
83.296
30.704
8.264
1.00
20.00
6


ATOM
1051
NE2
HIS
B
197
83.071
31.346
7.132
1.00
20.00
7


ATOM
1052
C
HIS
B
197
86.080
36.060
8.697
1.00
20.00
6


ATOM
1053
O
HIS
B
197
85.314
36.919
9.146
1.00
20.00
8


ATOM
1054
N
GLY
B
198
87.404
36.143
8.804
1.00
20.00
7


ATOM
1055
CA
GLY
B
198
88.009
37.285
9.464
1.00
20.00
6


ATOM
1056
C
GLY
B
198
87.687
38.580
8.737
1.00
20.00
6


ATOM
1057
O
GLY
B
198
87.784
39.661
9.311
1.00
20.00
8


ATOM
1058
N
LYS
B
199
87.308
38.475
7.466
1.00
20.00
7


ATOM
1059
CA
LYS
B
199
86.959
39.652
6.674
1.00
20.00
6


ATOM
1060
CB
LYS
B
199
87.577
39.573
5.279
1.00
20.00
6


ATOM
1061
CG
LYS
B
199
89.082
39.736
5.258
1.00
20.00
6


ATOM
1062
CD
LYS
B
199
89.574
39.919
3.833
1.00
20.00
6


ATOM
1063
CE
LYS
B
199
91.054
40.243
3.807
1.00
20.00
6


ATOM
1064
NZ
LYS
B
199
91.398
41.382
4.706
1.00
20.00
7


ATOM
1065
C
LYS
B
199
85.451
39.804
6.539
1.00
20.00
6


ATOM
1066
O
LYS
B
199
84.972
40.556
5.693
1.00
20.00
8


ATOM
1067
N
GLY
B
200
84.707
39.079
7.368
1.00
20.00
7


ATOM
1068
CA
GLY
B
200
83.258
39.158
7.328
1.00
20.00
6


ATOM
1069
C
GLY
B
200
82.646
38.660
6.032
1.00
20.00
6


ATOM
1070
O
GLY
B
200
81.644
39.198
5.564
1.00
20.00
8


ATOM
1071
N
ILE
B
201
83.243
37.630
5.445
1.00
20.00
7


ATOM
1072
CA
ILE
B
201
82.726
37.075
4.205
1.00
20.00
6


ATOM
1073
CB
ILE
B
201
83.775
37.140
3.080
1.00
20.00
6


ATOM
1074
CG2
ILE
B
201
83.257
36.413
1.841
1.00
20.00
6


ATOM
1075
CG1
ILE
B
201
84.109
38.599
2.761
1.00
20.00
6


ATOM
1076
CD1
ILE
B
201
85.330
38.758
1.870
1.00
20.00
6


ATOM
1077
C
ILE
B
201
82.329
35.623
4.395
1.00
20.00
6


ATOM
1078
O
ILE
B
201
83.094
34.826
4.942
1.00
20.00
8


ATOM
1079
N
ILE
B
202
81.125
35.291
3.940
1.00
20.00
7


ATOM
1080
CA
ILE
B
202
80.592
33.936
4.016
1.00
20.00
6


ATOM
1081
CB
ILE
B
202
79.119
33.953
4.481
1.00
20.00
6


ATOM
1082
CG2
ILE
B
202
78.583
32.522
4.595
1.00
20.00
6


ATOM
1083
CG1
ILE
B
202
79.008
34.675
5.825
1.00
20.00
6


ATOM
1084
CD1
ILE
B
202
77.576
34.865
6.294
1.00
20.00
6


ATOM
1085
C
ILE
B
202
80.644
33.393
2.589
1.00
20.00
6


ATOM
1086
O
ILE
B
202
80.182
34.056
1.663
1.00
20.00
8


ATOM
1087
N
HIS
B
203
81.204
32.204
2.395
1.00
20.00
7


ATOM
1088
CA
HIS
B
203
81.279
31.652
1.044
1.00
20.00
6


ATOM
1089
CB
HIS
B
203
82.258
30.480
0.999
1.00
20.00
6


ATOM
1090
CG
HIS
B
203
82.478
29.942
−0.380
1.00
20.00
6


ATOM
1091
CD2
HIS
B
203
81.646
29.282
−1.220
1.00
20.00
6


ATOM
1092
ND1
HIS
B
203
83.659
30.116
−1.069
1.00
20.00
7


ATOM
1093
CE1
HIS
B
203
83.545
29.588
−2.275
1.00
20.00
6


ATOM
1094
NE2
HIS
B
203
82.333
29.076
−2.392
1.00
20.00
7


ATOM
1095
C
HIS
B
203
79.896
31.211
0.530
1.00
20.00
6


ATOM
1096
O
HIS
B
203
79.508
31.546
−0.593
1.00
20.00
8


ATOM
1097
N
ARG
B
204
79.168
30.458
1.357
1.00
20.00
7


ATOM
1098
CA
ARG
B
204
77.819
29.969
1.039
1.00
20.00
6


ATOM
1099
CB
ARG
B
204
76.916
31.117
0.583
1.00
20.00
6


ATOM
1100
CG
ARG
B
204
76.601
32.120
1.675
1.00
20.00
6


ATOM
1101
CD
ARG
B
204
75.316
32.878
1.377
1.00
20.00
6


ATOM
1102
NE
ARG
B
204
75.376
33.616
0.119
1.00
20.00
7


ATOM
1103
CZ
ARG
B
204
74.423
34.443
−0.303
1.00
20.00
6


ATOM
1104
NH1
ARG
B
204
73.336
34.636
0.436
1.00
20.00
7


ATOM
1105
NH2
ARG
B
204
74.555
35.084
−1.457
1.00
20.00
7


ATOM
1106
C
ARG
B
204
77.700
28.829
0.030
1.00
20.00
6


ATOM
1107
O
ARG
B
204
76.611
28.300
−0.177
1.00
20.00
8


ATOM
1108
N
ASP
B
205
78.792
28.456
−0.620
1.00
20.00
7


ATOM
1109
CA
ASP
B
205
78.718
27.342
−1.550
1.00
20.00
6


ATOM
1110
CB
ASP
B
205
78.380
27.829
−2.961
1.00
20.00
6


ATOM
1111
CG
ASP
B
205
77.941
26.694
−3.867
1.00
20.00
6


ATOM
1112
OD1
ASP
B
205
77.544
25.638
−3.330
1.00
20.00
8


ATOM
1113
OD2
ASP
B
205
77.982
26.853
−5.104
1.00
20.00
8


ATOM
1114
C
ASP
B
205
80.019
26.560
−1.547
1.00
20.00
6


ATOM
1115
O
ASP
B
205
80.508
26.122
−2.588
1.00
20.00
8


ATOM
1116
N
LEU
B
206
80.573
26.375
−0.354
1.00
20.00
7


ATOM
1117
CA
LEU
B
206
81.819
25.652
−0.208
1.00
20.00
6


ATOM
1118
CB
LEU
B
206
82.361
25.826
1.212
1.00
20.00
6


ATOM
1119
CG
LEU
B
206
83.764
25.271
1.471
1.00
20.00
6


ATOM
1120
CD1
LEU
B
206
84.765
25.969
0.561
1.00
20.00
6


ATOM
1121
CD2
LEU
B
206
84.135
25.477
2.933
1.00
20.00
6


ATOM
1122
C
LEU
B
206
81.609
24.174
−0.514
1.00
20.00
6


ATOM
1123
O
LEU
B
206
80.691
23.549
0.011
1.00
20.00
8


ATOM
1124
N
LYS
B
207
82.461
23.628
−1.375
1.00
20.00
7


ATOM
1125
CA
LYS
B
207
82.379
22.223
−1.765
1.00
20.00
6


ATOM
1126
CB
LYS
B
207
81.160
22.000
−2.679
1.00
20.00
6


ATOM
1127
CG
LYS
B
207
81.130
22.913
−3.893
1.00
20.00
6


ATOM
1128
CD
LYS
B
207
79.876
22.720
−4.736
1.00
20.00
6


ATOM
1129
CE
LYS
B
207
79.788
23.797
−5.813
1.00
20.00
6


ATOM
1130
NZ
LYS
B
207
78.695
23.557
−6.791
1.00
20.00
7


ATOM
1131
C
LYS
B
207
83.657
21.808
−2.487
1.00
20.00
6


ATOM
1132
O
LYS
B
207
84.416
22.656
−2.960
1.00
20.00
8


ATOM
1133
N
PRO
B
208
83.916
20.494
−2.582
1.00
20.00
7


ATOM
1134
CD
PRO
B
208
83.153
19.378
−1.993
1.00
20.00
6


ATOM
1135
CA
PRO
B
208
85.122
20.005
−3.259
1.00
20.00
6


ATOM
1136
CB
PRO
B
208
84.922
18.494
−3.267
1.00
20.00
6


ATOM
1137
CG
PRO
B
208
84.174
18.256
−1.984
1.00
20.00
6


ATOM
1138
C
PRO
B
208
85.303
20.574
−4.666
1.00
20.00
6


ATOM
1139
O
PRO
B
208
86.431
20.752
−5.124
1.00
20.00
8


ATOM
1140
N
GLU
B
209
84.197
20.859
−5.347
1.00
20.00
7


ATOM
1141
CA
GLU
B
209
84.243
21.410
−6.705
1.00
20.00
6


ATOM
1142
CB
GLU
B
209
82.836
21.424
−7.317
1.00
20.00
6


ATOM
1143
CG
GLU
B
209
82.755
22.081
−8.690
1.00
20.00
6


ATOM
1144
CD
GLU
B
209
81.323
22.296
−9.159
1.00
20.00
6


ATOM
1145
OE1
GLU
B
209
80.587
21.299
−9.322
1.00
20.00
8


ATOM
1146
OE2
GLU
B
209
80.933
23.465
−9.364
1.00
20.00
8


ATOM
1147
C
GLU
B
209
84.810
22.836
−6.716
1.00
20.00
6


ATOM
1148
O
GLU
B
209
85.409
23.269
−7.705
1.00
20.00
8


ATOM
1149
N
ASN
B
210
84.604
23.549
−5.612
1.00
20.00
7


ATOM
1150
CA
ASN
B
210
85.051
24.932
−5.439
1.00
20.00
6


ATOM
1151
CB
ASN
B
210
84.033
25.695
−4.588
1.00
20.00
6


ATOM
1152
CG
ASN
B
210
82.851
26.170
−5.396
1.00
20.00
6


ATOM
1153
OD1
ASN
B
210
81.807
26.520
−4.846
1.00
20.00
8


ATOM
1154
ND2
ASN
B
210
83.010
26.194
−6.717
1.00
20.00
7


ATOM
1155
C
ASN
B
210
86.427
25.070
−4.797
1.00
20.00
6


ATOM
1156
O
ASN
B
210
86.937
26.181
−4.641
1.00
20.00
8


ATOM
1157
N
ILE
B
211
87.016
23.948
−4.406
1.00
20.00
7


ATOM
1158
CA
ILE
B
211
88.331
23.958
−3.790
1.00
20.00
6


ATOM
1159
CB
ILE
B
211
88.336
23.090
−2.521
1.00
20.00
6


ATOM
1160
CG2
ILE
B
211
89.732
23.025
−1.925
1.00
20.00
6


ATOM
1161
CG1
ILE
B
211
87.350
23.682
−1.510
1.00
20.00
6


ATOM
1162
CD1
ILE
B
211
87.121
22.832
−0.285
1.00
20.00
6


ATOM
1163
C
ILE
B
211
89.307
23.414
−4.816
1.00
20.00
6


ATOM
1164
O
ILE
B
211
89.475
22.199
−4.949
1.00
20.00
8


ATOM
1165
N
LEU
B
212
89.938
24.319
−5.558
1.00
20.00
7


ATOM
1166
CA
LEU
B
212
90.875
23.918
−6.601
1.00
20.00
6


ATOM
1167
CB
LEU
B
212
90.966
25.012
−7.673
1.00
20.00
6


ATOM
1168
CG
LEU
B
212
89.630
25.510
−8.235
1.00
20.00
6


ATOM
1169
CD1
LEU
B
212
89.896
26.462
−9.390
1.00
20.00
6


ATOM
1170
CD2
LEU
B
212
88.781
24.331
−8.709
1.00
20.00
6


ATOM
1171
C
LEU
B
212
92.254
23.628
−6.038
1.00
20.00
6


ATOM
1172
O
LEU
B
212
92.537
23.923
−4.873
1.00
20.00
8


ATOM
1173
N
LEU
B
213
93.114
23.053
−6.875
1.00
20.00
7


ATOM
1174
CA
LEU
B
213
94.472
22.714
−6.472
1.00
20.00
6


ATOM
1175
CB
LEU
B
213
94.609
21.192
−6.388
1.00
20.00
6


ATOM
1176
CG
LEU
B
213
93.775
20.526
−5.292
1.00
20.00
6


ATOM
1177
CD1
LEU
B
213
93.737
19.035
−5.508
1.00
20.00
6


ATOM
1178
CD2
LEU
B
213
94.374
20.852
−3.935
1.00
20.00
6


ATOM
1179
C
LEU
B
213
95.503
23.277
−7.449
1.00
20.00
6


ATOM
1180
O
LEU
B
213
95.422
23.033
−8.657
1.00
20.00
8


ATOM
1181
N
ASN
B
214
96.470
24.036
−6.940
1.00
20.00
7


ATOM
1182
CA
ASN
B
214
97.488
24.585
−7.826
1.00
20.00
6


ATOM
1183
CB
ASN
B
214
98.198
25.792
−7.201
1.00
20.00
6


ATOM
1184
CG
ASN
B
214
98.938
25.448
−5.927
1.00
20.00
6


ATOM
1185
OD1
ASN
B
214
99.267
24.288
−5.669
1.00
20.00
8


ATOM
1186
ND2
ASN
B
214
99.224
26.469
−5.123
1.00
20.00
7


ATOM
1187
C
ASN
B
214
98.508
23.515
−8.182
1.00
20.00
6


ATOM
1188
O
ASN
B
214
98.420
22.372
−7.725
1.00
20.00
8


ATOM
1189
N
GLU
B
215
99.482
23.894
−8.996
1.00
20.00
7


ATOM
1190
CA
GLU
B
215
100.514
22.965
−9.430
1.00
20.00
6


ATOM
1191
CB
GLU
B
215
101.491
23.687
−10.362
1.00
20.00
6


ATOM
1192
CG
GLU
B
215
102.544
22.788
−10.979
1.00
20.00
6


ATOM
1193
CD
GLU
B
215
103.323
23.482
−12.080
1.00
20.00
6


ATOM
1194
OE1
GLU
B
215
103.909
24.554
−11.810
1.00
20.00
8


ATOM
1195
OE2
GLU
B
215
103.344
22.957
−13.215
1.00
20.00
8


ATOM
1196
C
GLU
B
215
101.275
22.307
−8.274
1.00
20.00
6


ATOM
1197
O
GLU
B
215
101.801
21.205
−8.428
1.00
20.00
8


ATOM
1198
N
ASP
B
216
101.335
22.976
−7.123
1.00
20.00
7


ATOM
1199
CA
ASP
B
216
102.036
22.430
−5.958
1.00
20.00
6


ATOM
1200
CB
ASP
B
216
102.727
23.549
−5.179
1.00
20.00
6


ATOM
1201
CG
ASP
B
216
103.952
24.086
−5.896
1.00
20.00
6


ATOM
1202
OD1
ASP
B
216
104.766
23.267
−6.376
1.00
20.00
8


ATOM
1203
OD2
ASP
B
216
104.110
25.323
−5.973
1.00
20.00
8


ATOM
1204
C
ASP
B
216
101.121
21.651
−5.013
1.00
20.00
6


ATOM
1205
O
ASP
B
216
101.532
21.241
−3.925
1.00
20.00
8


ATOM
1206
N
MET
B
217
99.877
21.463
−5.434
1.00
20.00
7


ATOM
1207
CA
MET
B
217
98.890
20.730
−4.657
1.00
20.00
6


ATOM
1208
CB
MET
B
217
99.402
19.319
−4.358
1.00
20.00
6


ATOM
1209
CG
MET
B
217
99.456
18.432
−5.601
1.00
20.00
6


ATOM
1210
SD
MET
B
217
97.857
18.342
−6.445
1.00
20.00
16


ATOM
1211
CE
MET
B
217
97.073
16.984
−5.543
1.00
20.00
6


ATOM
1212
C
MET
B
217
98.397
21.403
−3.373
1.00
20.00
6


ATOM
1213
O
MET
B
217
97.972
20.730
−2.435
1.00
20.00
8


ATOM
1214
N
HIS
B
218
98.469
22.730
−3.331
1.00
20.00
7


ATOM
1215
CA
HIS
B
218
97.949
23.487
−2.197
1.00
20.00
6


ATOM
1216
CB
HIS
B
218
98.831
24.700
−1.898
1.00
20.00
6


ATOM
1217
CG
HIS
B
218
100.100
24.357
−1.177
1.00
20.00
6


ATOM
1218
CD2
HIS
B
218
101.390
24.362
−1.588
1.00
20.00
6


ATOM
1219
ND1
HIS
B
218
100.117
23.935
0.136
1.00
20.00
7


ATOM
1220
CE1
HIS
B
218
101.364
23.698
0.504
1.00
20.00
6


ATOM
1221
NE2
HIS
B
218
102.156
23.947
−0.524
1.00
20.00
7


ATOM
1222
C
HIS
B
218
96.583
23.939
−2.703
1.00
20.00
6


ATOM
1223
O
HIS
B
218
96.400
24.090
−3.910
1.00
20.00
8


ATOM
1224
N
ILE
B
219
95.628
24.160
−1.808
1.00
20.00
7


ATOM
1225
CA
ILE
B
219
94.301
24.562
−2.257
1.00
20.00
6


ATOM
1226
CB
ILE
B
219
93.232
24.359
−1.159
1.00
20.00
6


ATOM
1227
CG2
ILE
B
219
93.266
22.918
−0.654
1.00
20.00
6


ATOM
1228
CG1
ILE
B
219
93.460
25.353
−0.011
1.00
20.00
6


ATOM
1229
CD1
ILE
B
219
92.351
25.342
1.036
1.00
20.00
6


ATOM
1230
C
ILE
B
219
94.207
26.010
−2.714
1.00
20.00
6


ATOM
1231
O
ILE
B
219
95.044
26.850
−2.375
1.00
20.00
8


ATOM
1232
N
GLN
B
220
93.168
26.274
−3.497
1.00
20.00
7


ATOM
1233
CA
GLN
B
220
92.859
27.600
−3.999
1.00
20.00
6


ATOM
1234
CB
GLN
B
220
93.537
27.867
−5.350
1.00
20.00
6


ATOM
1235
CG
GLN
B
220
95.011
28.246
−5.216
1.00
20.00
6


ATOM
1236
CD
GLN
B
220
95.599
28.799
−6.503
1.00
20.00
6


ATOM
1237
OE1
GLN
B
220
95.725
28.086
−7.502
1.00
20.00
8


ATOM
1238
NE2
GLN
B
220
95.957
30.079
−6.486
1.00
20.00
7


ATOM
1239
C
GLN
B
220
91.350
27.626
−4.140
1.00
20.00
6


ATOM
1240
O
GLN
B
220
90.792
27.133
−5.124
1.00
20.00
8


ATOM
1241
N
ILE
B
221
90.689
28.178
−3.129
1.00
20.00
7


ATOM
1242
CA
ILE
B
221
89.240
28.260
−3.122
1.00
20.00
6


ATOM
1243
CB
ILE
B
221
88.731
28.550
−1.700
1.00
20.00
6


ATOM
1244
CG2
ILE
B
221
87.209
28.707
−1.708
1.00
20.00
6


ATOM
1245
CG1
ILE
B
221
89.164
27.406
−0.773
1.00
20.00
6


ATOM
1246
CD1
ILE
B
221
88.743
27.559
0.668
1.00
20.00
6


ATOM
1247
C
ILE
B
221
88.760
29.339
−4.092
1.00
20.00
6


ATOM
1248
O
ILE
B
221
89.411
30.374
−4.262
1.00
20.00
8


ATOM
1249
N
THR
B
222
87.633
29.082
−4.748
1.00
20.00
7


ATOM
1250
CA
THR
B
222
87.084
30.039
−5.701
1.00
20.00
6


ATOM
1251
CB
THR
B
222
87.565
29.728
−7.125
1.00
20.00
6


ATOM
1252
OG1
THR
B
222
87.179
30.795
−8.000
1.00
20.00
8


ATOM
1253
CG2
THR
B
222
86.962
28.410
−7.618
1.00
20.00
6


ATOM
1254
C
THR
B
222
85.554
30.028
−5.683
1.00
20.00
6


ATOM
1255
O
THR
B
222
84.950
29.417
−4.791
1.00
20.00
8


ATOM
1256
N
ASP
B
223
84.949
30.712
−6.659
1.00
20.00
7


ATOM
1257
CA
ASP
B
223
83.492
30.806
−6.806
1.00
20.00
6


ATOM
1258
CB
ASP
B
223
82.872
29.399
−6.767
1.00
20.00
6


ATOM
1259
CG
ASP
B
223
81.414
29.384
−7.205
1.00
20.00
6


ATOM
1260
OD1
ASP
B
223
80.990
30.335
−7.900
1.00
20.00
8


ATOM
1261
OD2
ASP
B
223
80.701
28.414
−6.866
1.00
20.00
8


ATOM
1262
C
ASP
B
223
82.878
31.694
−5.725
1.00
20.00
6


ATOM
1263
O
ASP
B
223
82.191
31.208
−4.820
1.00
20.00
8


ATOM
1264
N
PHE
B
224
83.105
33.001
−5.848
1.00
20.00
7


ATOM
1265
CA
PHE
B
224
82.632
33.970
−4.866
1.00
20.00
6


ATOM
1266
CB
PHE
B
224
83.800
34.869
−4.451
1.00
20.00
6


ATOM
1267
CG
PHE
B
224
84.826
34.165
−3.612
1.00
20.00
6


ATOM
1268
CD1
PHE
B
224
84.590
33.931
−2.261
1.00
20.00
6


ATOM
1269
CD2
PHE
B
224
86.001
33.687
−4.182
1.00
20.00
6


ATOM
1270
CE1
PHE
B
224
85.509
33.227
−1.486
1.00
20.00
6


ATOM
1271
CE2
PHE
B
224
86.927
32.981
−3.418
1.00
20.00
6


ATOM
1272
CZ
PHE
B
224
86.679
32.750
−2.068
1.00
20.00
6


ATOM
1273
C
PHE
B
224
81.443
34.839
−5.256
1.00
20.00
6


ATOM
1274
O
PHE
B
224
81.001
35.678
−4.468
1.00
20.00
8


ATOM
1275
N
GLY
B
225
80.928
34.647
−6.463
1.00
20.00
7


ATOM
1276
CA
GLY
B
225
79.793
35.438
−6.894
1.00
20.00
6


ATOM
1277
C
GLY
B
225
78.612
35.265
−5.955
1.00
20.00
6


ATOM
1278
O
GLY
B
225
77.824
36.192
−5.753
1.00
20.00
8


ATOM
1279
N
THR
B
226
78.486
34.080
−5.367
1.00
20.00
7


ATOM
1280
CA
THR
B
226
77.379
33.819
−4.459
1.00
20.00
6


ATOM
1281
CB
THR
B
226
76.779
32.425
−4.715
1.00
20.00
6


ATOM
1282
OG1
THR
B
226
77.826
31.450
−4.762
1.00
20.00
8


ATOM
1283
CG2
THR
B
226
76.021
32.417
−6.041
1.00
20.00
6


ATOM
1284
C
THR
B
226
77.738
33.957
−2.981
1.00
20.00
6


ATOM
1285
O
THR
B
226
77.001
33.500
−2.107
1.00
20.00
8


ATOM
1286
N
ALA
B
227
78.867
34.598
−2.702
1.00
20.00
7


ATOM
1287
CA
ALA
B
227
79.282
34.800
−1.325
1.00
20.00
6


ATOM
1288
CB
ALA
B
227
80.738
35.242
−1.268
1.00
20.00
6


ATOM
1289
C
ALA
B
227
78.384
35.875
−0.726
1.00
20.00
6


ATOM
1290
O
ALA
B
227
77.623
36.529
−1.440
1.00
20.00
8


ATOM
1291
N
LYS
B
228
78.467
36.046
0.586
1.00
20.00
7


ATOM
1292
CA
LYS
B
228
77.670
37.051
1.274
1.00
20.00
6


ATOM
1293
CB
LYS
B
228
76.637
36.384
2.179
1.00
20.00
6


ATOM
1294
CG
LYS
B
228
75.705
37.357
2.890
1.00
20.00
6


ATOM
1295
CD
LYS
B
228
74.795
38.072
1.893
1.00
20.00
6


ATOM
1296
CE
LYS
B
228
73.849
39.049
2.587
1.00
20.00
6


ATOM
1297
NZ
LYS
B
228
73.000
39.781
1.605
1.00
20.00
7


ATOM
1298
C
LYS
B
228
78.616
37.896
2.110
1.00
20.00
6


ATOM
1299
O
LYS
B
228
79.355
37.366
2.940
1.00
20.00
8


ATOM
1300
N
VAL
B
229
78.603
39.206
1.881
1.00
20.00
7


ATOM
1301
CA
VAL
B
229
79.463
40.114
2.626
1.00
20.00
6


ATOM
1302
CB
VAL
B
229
79.976
41.256
1.734
1.00
20.00
6


ATOM
1303
CG1
VAL
B
229
80.853
42.191
2.540
1.00
20.00
6


ATOM
1304
CG2
VAL
B
229
80.746
40.686
0.561
1.00
20.00
6


ATOM
1305
C
VAL
B
229
78.687
40.710
3.793
1.00
20.00
6


ATOM
1306
O
VAL
B
229
77.798
41.537
3.599
1.00
20.00
8


ATOM
1307
N
LEU
B
230
79.034
40.284
5.003
1.00
20.00
7


ATOM
1308
CA
LEU
B
230
78.370
40.752
6.213
1.00
20.00
6


ATOM
1309
CB
LEU
B
230
78.740
39.856
7.395
1.00
20.00
6


ATOM
1310
CG
LEU
B
230
78.276
38.403
7.332
1.00
20.00
6


ATOM
1311
CD1
LEU
B
230
78.853
37.634
8.508
1.00
20.00
6


ATOM
1312
CD2
LEU
B
230
76.760
38.350
7.339
1.00
20.00
6


ATOM
1313
C
LEU
B
230
78.705
42.193
6.565
1.00
20.00
6


ATOM
1314
O
LEU
B
230
79.768
42.701
6.214
1.00
20.00
8


ATOM
1315
N
SER
B
231
77.781
42.839
7.270
1.00
20.00
7


ATOM
1316
CA
SER
B
231
77.957
44.219
7.708
1.00
20.00
6


ATOM
1317
CB
SER
B
231
77.082
45.161
6.875
1.00
20.00
6


ATOM
1318
OG
SER
B
231
75.714
44.795
6.948
1.00
20.00
8


ATOM
1319
C
SER
B
231
77.623
44.373
9.196
1.00
20.00
6


ATOM
1320
O
SER
B
231
78.322
45.086
9.919
1.00
20.00
8


ATOM
1321
N
PRO
B
232
76.553
43.705
9.674
1.00
20.00
7


ATOM
1322
CD
PRO
B
232
75.571
42.876
8.948
1.00
20.00
6


ATOM
1323
CA
PRO
B
232
76.182
43.811
11.091
1.00
20.00
6


ATOM
1324
CB
PRO
B
232
75.005
42.844
11.211
1.00
20.00
6


ATOM
1325
CG
PRO
B
232
74.367
42.933
9.862
1.00
20.00
6


ATOM
1326
C
PRO
B
232
77.332
43.438
12.024
1.00
20.00
6


ATOM
1327
O
PRO
B
232
78.199
42.640
11.666
1.00
20.00
8


ATOM
1328
N
ALA
B
237
74.215
38.132
11.762
1.00
20.00
7


ATOM
1329
CA
ALA
B
237
74.666
37.653
10.460
1.00
20.00
6


ATOM
1330
CB
ALA
B
237
75.541
36.417
10.637
1.00
20.00
6


ATOM
1331
C
ALA
B
237
73.479
37.324
9.558
1.00
20.00
6


ATOM
1332
O
ALA
B
237
73.143
36.158
9.374
1.00
20.00
8


ATOM
1333
N
ALA
B
238
72.841
38.347
8.996
1.00
20.00
7


ATOM
1334
CA
ALA
B
238
71.693
38.130
8.117
1.00
20.00
6


ATOM
1335
CB
ALA
B
238
70.973
39.450
7.853
1.00
20.00
6


ATOM
1336
C
ALA
B
238
72.123
37.497
6.798
1.00
20.00
6


ATOM
1337
O
ALA
B
238
73.315
37.404
6.500
1.00
20.00
8


ATOM
1338
N
ALA
B
239
71.146
37.057
6.012
1.00
20.00
7


ATOM
1339
CA
ALA
B
239
71.439
36.431
4.728
1.00
20.00
6


ATOM
1340
CB
ALA
B
239
72.152
35.123
4.952
1.00
20.00
6


ATOM
1341
C
ALA
B
239
70.173
36.194
3.918
1.00
20.00
6


ATOM
1342
O
ALA
B
239
69.329
37.079
3.825
1.00
20.00
8


ATOM
1343
N
ASN
B
240
70.068
34.996
3.339
1.00
20.00
7


ATOM
1344
CA
ASN
B
240
68.939
34.559
2.514
1.00
20.00
6


ATOM
1345
CB
ASN
B
240
67.614
35.160
2.999
1.00
20.00
6


ATOM
1346
CG
ASN
B
240
67.258
36.466
2.299
1.00
20.00
6


ATOM
1347
OD1
ASN
B
240
67.119
36.519
1.068
1.00
20.00
8


ATOM
1348
ND2
ASN
B
240
67.091
37.536
3.089
1.00
20.00
7


ATOM
1349
C
ASN
B
240
69.153
34.937
1.053
1.00
20.00
6


ATOM
1350
O
ASN
B
240
70.007
35.767
0.749
1.00
20.00
8


ATOM
1351
N
ALA
B
241
68.365
34.329
0.163
1.00
20.00
7


ATOM
1352
CA
ALA
B
241
68.401
34.570
−1.290
1.00
20.00
6


ATOM
1353
C
ALA
B
241
68.990
33.416
−2.103
1.00
20.00
6


ATOM
1354
O
ALA
B
241
68.353
32.919
−3.030
1.00
20.00
8


ATOM
1355
CB
ALA
B
241
69.168
35.859
−1.629
1.00
20.00
6


ATOM
1356
N
PHE
B
242
70.205
33.000
−1.762
1.00
20.00
7


ATOM
1357
CA
PHE
B
242
70.875
31.918
−2.481
1.00
20.00
6


ATOM
1358
CB
PHE
B
242
72.259
32.379
−2.952
1.00
20.00
6


ATOM
1359
CG
PHE
B
242
73.102
31.273
−3.521
1.00
20.00
6


ATOM
1360
CD1
PHE
B
242
72.843
30.767
−4.790
1.00
20.00
6


ATOM
1361
CD2
PHE
B
242
74.136
30.713
−2.773
1.00
20.00
6


ATOM
1362
CE1
PHE
B
242
73.599
29.718
−5.310
1.00
20.00
6


ATOM
1363
CE2
PHE
B
242
74.896
29.666
−3.281
1.00
20.00
6


ATOM
1364
CZ
PHE
B
242
74.627
29.166
−4.553
1.00
20.00
6


ATOM
1365
C
PHE
B
242
71.038
30.652
−1.646
1.00
20.00
6


ATOM
1366
O
PHE
B
242
71.213
30.716
−0.431
1.00
20.00
8


ATOM
1367
N
VAL
B
243
70.988
29.505
−2.318
1.00
20.00
7


ATOM
1368
CA
VAL
B
243
71.157
28.204
−1.675
1.00
20.00
6


ATOM
1369
CB
VAL
B
243
69.828
27.420
−1.617
1.00
20.00
6


ATOM
1370
CG1
VAL
B
243
70.066
26.023
−1.050
1.00
20.00
6


ATOM
1371
CG2
VAL
B
243
68.825
28.177
−0.766
1.00
20.00
6


ATOM
1372
C
VAL
B
243
72.164
27.394
−2.486
1.00
20.00
6


ATOM
1373
O
VAL
B
243
71.894
27.014
−3.628
1.00
20.00
8


ATOM
1374
N
GLY
B
244
73.323
27.137
−1.890
1.00
20.00
7


ATOM
1375
CA
GLY
B
244
74.364
26.385
−2.569
1.00
20.00
6


ATOM
1376
C
GLY
B
244
74.019
24.944
−2.911
1.00
20.00
6


ATOM
1377
O
GLY
B
244
72.867
24.524
−2.810
1.00
20.00
8


ATOM
1378
N
THR
B
245
75.032
24.184
−3.315
1.00
20.00
7


ATOM
1379
CA
THR
B
245
74.858
22.787
−3.691
1.00
20.00
6


ATOM
1380
CB
THR
B
245
76.214
22.161
−4.046
1.00
20.00
6


ATOM
1381
OG1
THR
B
245
76.794
22.911
−5.120
1.00
20.00
8


ATOM
1382
CG2
THR
B
245
76.049
20.710
−4.485
1.00
20.00
6


ATOM
1383
C
THR
B
245
74.174
22.003
−2.579
1.00
20.00
6


ATOM
1384
O
THR
B
245
74.643
21.969
−1.441
1.00
20.00
8


ATOM
1385
N
ALA
B
246
73.061
21.372
−2.937
1.00
20.00
7


ATOM
1386
CA
ALA
B
246
72.229
20.615
−2.008
1.00
20.00
6


ATOM
1387
CB
ALA
B
246
71.266
19.723
−2.793
1.00
20.00
6


ATOM
1388
C
ALA
B
246
72.936
19.789
−0.941
1.00
20.00
6


ATOM
1389
O
ALA
B
246
72.611
19.894
0.239
1.00
20.00
8


ATOM
1390
N
GLN
B
247
73.902
18.973
−1.339
1.00
20.00
7


ATOM
1391
CA
GLN
B
247
74.580
18.121
−0.371
1.00
20.00
6


ATOM
1392
CB
GLN
B
247
75.535
17.168
−1.096
1.00
20.00
6


ATOM
1393
CG
GLN
B
247
75.110
16.823
−2.520
1.00
20.00
6


ATOM
1394
CD
GLN
B
247
75.139
15.336
−2.811
1.00
20.00
6


ATOM
1395
OE1
GLN
B
247
75.963
14.602
−2.270
1.00
20.00
8


ATOM
1396
NE2
GLN
B
247
74.246
14.887
−3.686
1.00
20.00
7


ATOM
1397
C
GLN
B
247
75.343
18.873
0.720
1.00
20.00
6


ATOM
1398
O
GLN
B
247
75.631
18.306
1.773
1.00
20.00
8


ATOM
1399
N
TYR
B
248
75.648
20.147
0.484
1.00
20.00
7


ATOM
1400
CA
TYR
B
248
76.405
20.941
1.454
1.00
20.00
6


ATOM
1401
CB
TYR
B
248
77.642
21.531
0.767
1.00
20.00
6


ATOM
1402
CG
TYR
B
248
78.447
20.471
0.052
1.00
20.00
6


ATOM
1403
CD1
TYR
B
248
79.329
19.648
0.750
1.00
20.00
6


ATOM
1404
CE1
TYR
B
248
79.979
18.589
0.115
1.00
20.00
6


ATOM
1405
CD2
TYR
B
248
78.243
20.220
−1.306
1.00
20.00
6


ATOM
1406
CE2
TYR
B
248
78.884
19.167
−1.951
1.00
20.00
6


ATOM
1407
CZ
TYR
B
248
79.748
18.352
−1.232
1.00
20.00
6


ATOM
1408
OH
TYR
B
248
80.348
17.280
−1.852
1.00
20.00
8


ATOM
1409
C
TYR
B
248
75.596
22.055
2.118
1.00
20.00
6


ATOM
1410
O
TYR
B
248
76.132
22.824
2.917
1.00
20.00
8


ATOM
1411
N
VAL
B
249
74.309
22.135
1.798
1.00
20.00
7


ATOM
1412
CA
VAL
B
249
73.452
23.162
2.376
1.00
20.00
6


ATOM
1413
CB
VAL
B
249
72.071
23.174
1.695
1.00
20.00
6


ATOM
1414
CG1
VAL
B
249
71.117
24.100
2.442
1.00
20.00
6


ATOM
1415
CG2
VAL
B
249
72.225
23.632
0.264
1.00
20.00
6


ATOM
1416
C
VAL
B
249
73.262
22.964
3.875
1.00
20.00
6


ATOM
1417
O
VAL
B
249
73.027
21.847
4.341
1.00
20.00
8


ATOM
1418
N
SER
B
250
73.373
24.055
4.628
1.00
20.00
7


ATOM
1419
CA
SER
B
250
73.206
24.008
6.076
1.00
20.00
6


ATOM
1420
CB
SER
B
250
73.921
25.198
6.738
1.00
20.00
6


ATOM
1421
OG
SER
B
250
73.428
26.440
6.257
1.00
20.00
8


ATOM
1422
C
SER
B
250
71.717
24.049
6.405
1.00
20.00
6


ATOM
1423
O
SER
B
250
70.920
24.577
5.636
1.00
20.00
8


ATOM
1424
N
PRO
B
251
71.322
23.479
7.550
1.00
20.00
7


ATOM
1425
CD
PRO
B
251
72.130
22.770
8.558
1.00
20.00
6


ATOM
1426
CA
PRO
B
251
69.905
23.484
7.925
1.00
20.00
6


ATOM
1427
CB
PRO
B
251
69.892
22.714
9.252
1.00
20.00
6


ATOM
1428
CG
PRO
B
251
71.290
22.936
9.801
1.00
20.00
6


ATOM
1429
C
PRO
B
251
69.265
24.870
8.032
1.00
20.00
6


ATOM
1430
O
PRO
B
251
68.093
25.036
7.688
1.00
20.00
8


ATOM
1431
N
GLU
B
252
70.017
25.867
8.492
1.00
20.00
7


ATOM
1432
CA
GLU
B
252
69.462
27.216
8.625
1.00
20.00
6


ATOM
1433
CB
GLU
B
252
70.503
28.193
9.196
1.00
20.00
6


ATOM
1434
CG
GLU
B
252
71.838
28.180
8.477
1.00
20.00
6


ATOM
1435
CD
GLU
B
252
72.844
27.257
9.139
1.00
20.00
6


ATOM
1436
OE1
GLU
B
252
72.429
26.207
9.675
1.00
20.00
8


ATOM
1437
OE2
GLU
B
252
74.053
27.581
9.118
1.00
20.00
8


ATOM
1438
C
GLU
B
252
68.928
27.744
7.292
1.00
20.00
6


ATOM
1439
O
GLU
B
252
67.927
28.459
7.261
1.00
20.00
8


ATOM
1440
N
LEU
B
253
69.584
27.395
6.189
1.00
20.00
7


ATOM
1441
CA
LEU
B
253
69.117
27.850
4.883
1.00
20.00
6


ATOM
1442
CB
LEU
B
253
70.140
27.527
3.794
1.00
20.00
6


ATOM
1443
CG
LEU
B
253
71.127
28.635
3.421
1.00
20.00
6


ATOM
1444
CD1
LEU
B
253
72.121
28.851
4.547
1.00
20.00
6


ATOM
1445
CD2
LEU
B
253
71.858
28.250
2.140
1.00
20.00
6


ATOM
1446
C
LEU
B
253
67.774
27.227
4.496
1.00
20.00
6


ATOM
1447
O
LEU
B
253
66.997
27.826
3.751
1.00
20.00
8


ATOM
1448
N
LEU
B
254
67.506
26.029
5.002
1.00
20.00
7


ATOM
1449
CA
LEU
B
254
66.271
25.316
4.689
1.00
20.00
6


ATOM
1450
CB
LEU
B
254
66.539
23.809
4.689
1.00
20.00
6


ATOM
1451
CG
LEU
B
254
67.647
23.322
3.746
1.00
20.00
6


ATOM
1452
CD1
LEU
B
254
67.983
21.873
4.057
1.00
20.00
6


ATOM
1453
CD2
LEU
B
254
67.204
23.475
2.302
1.00
20.00
6


ATOM
1454
C
LEU
B
254
65.135
25.626
5.662
1.00
20.00
6


ATOM
1455
O
LEU
B
254
63.959
25.524
5.312
1.00
20.00
8


ATOM
1456
N
THR
B
255
65.483
26.010
6.883
1.00
20.00
7


ATOM
1457
CA
THR
B
255
64.472
26.308
7.884
1.00
20.00
6


ATOM
1458
CB
THR
B
255
64.876
25.747
9.252
1.00
20.00
6


ATOM
1459
OG1
THR
B
255
66.154
26.277
9.619
1.00
20.00
8


ATOM
1460
CG2
THR
B
255
64.958
24.230
9.202
1.00
20.00
6


ATOM
1461
C
THR
B
255
64.205
27.795
8.035
1.00
20.00
6


ATOM
1462
O
THR
B
255
63.072
28.241
7.897
1.00
20.00
8


ATOM
1463
N
GLU
B
256
65.250
28.560
8.314
1.00
20.00
7


ATOM
1464
CA
GLU
B
256
65.115
30.001
8.507
1.00
20.00
6


ATOM
1465
CB
GLU
B
256
66.015
30.444
9.659
1.00
20.00
6


ATOM
1466
CG
GLU
B
256
65.634
29.818
10.987
1.00
20.00
6


ATOM
1467
CD
GLU
B
256
66.736
29.922
12.018
1.00
20.00
6


ATOM
1468
OE1
GLU
B
256
67.249
31.041
12.232
1.00
20.00
8


ATOM
1469
OE2
GLU
B
256
67.086
28.884
12.619
1.00
20.00
8


ATOM
1470
C
GLU
B
256
65.439
30.815
7.262
1.00
20.00
6


ATOM
1471
O
GLU
B
256
65.268
32.034
7.252
1.00
20.00
8


ATOM
1472
N
LYS
B
257
65.906
30.141
6.215
1.00
20.00
7


ATOM
1473
CA
LYS
B
257
66.260
30.814
4.970
1.00
20.00
6


ATOM
1474
CB
LYS
B
257
65.015
31.458
4.352
1.00
20.00
6


ATOM
1475
CG
LYS
B
257
65.184
31.918
2.915
1.00
20.00
6


ATOM
1476
CD
LYS
B
257
63.885
32.497
2.378
1.00
20.00
6


ATOM
1477
CE
LYS
B
257
63.994
32.841
0.902
1.00
20.00
6


ATOM
1478
NZ
LYS
B
257
65.060
33.847
0.640
1.00
20.00
7


ATOM
1479
C
LYS
B
257
67.309
31.885
5.263
1.00
20.00
6


ATOM
1480
O
LYS
B
257
67.270
32.977
4.702
1.00
20.00
8


ATOM
1481
N
SER
B
258
68.243
31.563
6.152
1.00
20.00
7


ATOM
1482
CA
SER
B
258
69.300
32.494
6.527
1.00
20.00
6


ATOM
1483
CB
SER
B
258
69.043
33.028
7.937
1.00
20.00
6


ATOM
1484
OG
SER
B
258
68.893
31.962
8.859
1.00
20.00
8


ATOM
1485
C
SER
B
258
70.675
31.829
6.467
1.00
20.00
6


ATOM
1486
O
SER
B
258
70.786
30.602
6.542
1.00
20.00
8


ATOM
1487
N
ALA
B
259
71.718
32.641
6.329
1.00
20.00
7


ATOM
1488
CA
ALA
B
259
73.081
32.130
6.252
1.00
20.00
6


ATOM
1489
CB
ALA
B
259
73.549
32.121
4.809
1.00
20.00
6


ATOM
1490
C
ALA
B
259
74.031
32.966
7.102
1.00
20.00
6


ATOM
1491
O
ALA
B
259
73.882
34.185
7.211
1.00
20.00
8


ATOM
1492
N
CYS
B
260
75.008
32.298
7.704
1.00
20.00
7


ATOM
1493
CA
CYS
B
260
75.993
32.960
8.550
1.00
20.00
6


ATOM
1494
CB
CYS
B
260
75.574
32.865
10.017
1.00
20.00
6


ATOM
1495
SG
CYS
B
260
75.303
31.165
10.594
1.00
20.00
16


ATOM
1496
C
GYS
B
260
77.328
32.265
8.349
1.00
20.00
6


ATOM
1497
O
CYS
B
260
77.410
31.280
7.620
1.00
20.00
8


ATOM
1498
N
LYS
B
261
78.371
32.775
8.993
1.00
20.00
7


ATOM
1499
CA
LYS
B
261
79.691
32.174
8.869
1.00
20.00
6


ATOM
1500
CB
LYS
B
261
80.676
32.851
9.821
1.00
20.00
6


ATOM
1501
CG
LYS
B
261
80.985
34.296
9.472
1.00
20.00
6


ATOM
1502
CD
LYS
B
261
81.961
34.878
10.475
1.00
20.00
6


ATOM
1503
CE
LYS
B
261
82.157
36.365
10.259
1.00
20.00
6


ATOM
1504
NZ
LYS
B
261
83.085
36.922
11.278
1.00
20.00
7


ATOM
1505
C
LYS
B
261
79.632
30.687
9.187
1.00
20.00
6


ATOM
1506
O
LYS
B
261
80.258
29.877
8.512
1.00
20.00
8


ATOM
1507
N
SER
B
262
78.860
30.346
10.214
1.00
20.00
7


ATOM
1508
CA
SER
B
262
78.716
28.966
10.659
1.00
20.00
6


ATOM
1509
CB
SER
B
262
77.806
28.913
11.895
1.00
20.00
6


ATOM
1510
OG
SER
B
262
77.884
27.657
12.546
1.00
20.00
8


ATOM
1511
C
SER
B
262
78.161
28.070
9.549
1.00
20.00
6


ATOM
1512
O
SER
B
262
78.350
26.856
9.575
1.00
20.00
8


ATOM
1513
N
SER
B
263
77.466
28.660
8.581
1.00
20.00
7


ATOM
1514
CA
SER
B
263
76.938
27.870
7.472
1.00
20.00
6


ATOM
1515
CB
SER
B
263
76.132
28.750
6.507
1.00
20.00
6


ATOM
1516
OG
SER
B
263
75.011
29.329
7.156
1.00
20.00
8


ATOM
1517
C
SER
B
263
78.123
27.244
6.737
1.00
20.00
6


ATOM
1518
O
SER
B
263
78.038
26.108
6.273
1.00
20.00
8


ATOM
1519
N
ASP
B
264
79.234
27.977
6.642
1.00
20.00
7


ATOM
1520
CA
ASP
B
264
80.419
27.448
5.961
1.00
20.00
6


ATOM
1521
CB
ASP
B
264
81.478
28.538
5.745
1.00
20.00
6


ATOM
1522
CG
ASP
B
264
81.091
29.539
4.673
1.00
20.00
6


ATOM
1523
OD1
ASP
B
264
80.286
29.187
3.786
1.00
20.00
8


ATOM
1524
OD2
ASP
B
264
81.617
30.676
4.704
1.00
20.00
8


ATOM
1525
C
ASP
B
264
81.043
26.312
6.771
1.00
20.00
6


ATOM
1526
O
ASP
B
264
81.586
25.365
6.201
1.00
20.00
8


ATOM
1527
N
LEU
B
265
80.971
26.415
8.099
1.00
20.00
7


ATOM
1528
CA
LEU
B
265
81.532
25.390
8.974
1.00
20.00
6


ATOM
1529
CB
LEU
B
265
81.491
25.848
10.438
1.00
20.00
6


ATOM
1530
CG
LEU
B
265
82.419
27.035
10.746
1.00
20.00
6


ATOM
1531
CD1
LEU
B
265
82.204
27.532
12.177
1.00
20.00
6


ATOM
1532
CD2
LEU
B
265
83.864
26.608
10.541
1.00
20.00
6


ATOM
1533
C
LEU
B
265
80.750
24.094
8.800
1.00
20.00
6


ATOM
1534
O
LEU
B
265
81.306
23.004
8.910
1.00
20.00
8


ATOM
1535
N
TRP
B
266
79.454
24.208
8.530
1.00
20.00
7


ATOM
1536
CA
TRP
B
266
78.646
23.017
8.309
1.00
20.00
6


ATOM
1537
CB
TRP
B
266
77.167
23.384
8.148
1.00
20.00
6


ATOM
1538
CG
TRP
B
266
76.310
22.245
7.646
1.00
20.00
6


ATOM
1539
CD2
TRP
B
266
75.455
21.399
8.426
1.00
20.00
6


ATOM
1540
CE2
TRP
B
266
74.881
20.455
7.542
1.00
20.00
6


ATOM
1541
CE3
TRP
B
266
75.117
21.345
9.785
1.00
20.00
6


ATOM
1542
CD1
TRP
B
266
76.220
21.792
6.356
1.00
20.00
6


ATOM
1543
NE1
TRP
B
266
75.365
20.719
6.288
1.00
20.00
7


ATOM
1544
CZ2
TRP
B
266
73.988
19.466
7.975
1.00
20.00
6


ATOM
1545
CZ3
TRP
B
266
74.227
20.359
10.216
1.00
20.00
6


ATOM
1546
CH2
TRP
B
266
73.674
19.434
9.310
1.00
20.00
6


ATOM
1547
C
TRP
B
266
79.169
22.356
7.038
1.00
20.00
6


ATOM
1548
O
TRP
B
266
79.356
21.142
6.988
1.00
20.00
8


ATOM
1549
N
ALA
B
267
79.411
23.164
6.011
1.00
20.00
7


ATOM
1550
CA
ALA
B
267
79.930
22.646
4.751
1.00
20.00
6


ATOM
1551
CB
ALA
B
267
80.089
23.772
3.746
1.00
20.00
6


ATOM
1552
C
ALA
B
267
81.277
21.976
5.016
1.00
20.00
6


ATOM
1553
O
ALA
B
267
81.570
20.914
4.471
1.00
20.00
8


ATOM
1554
N
LEU
B
268
82.091
22.596
5.864
1.00
20.00
7


ATOM
1555
CA
LEU
B
268
83.393
22.030
6.209
1.00
20.00
6


ATOM
1556
CB
LEU
B
268
84.092
22.898
7.264
1.00
20.00
6


ATOM
1557
CG
LEU
B
268
85.379
22.332
7.879
1.00
20.00
6


ATOM
1558
CD1
LEU
B
268
86.442
22.192
6.803
1.00
20.00
6


ATOM
1559
CD2
LEU
B
268
85.872
23.263
9.006
1.00
20.00
6


ATOM
1560
C
LEU
B
268
83.193
20.617
6.753
1.00
20.00
6


ATOM
1561
O
LEU
B
268
83.903
19.684
6.372
1.00
20.00
8


ATOM
1562
N
GLY
B
269
82.220
20.463
7.645
1.00
20.00
7


ATOM
1563
CA
GLY
B
269
81.947
19.156
8.217
1.00
20.00
6


ATOM
1564
C
GLY
B
269
81.597
18.125
7.156
1.00
20.00
6


ATOM
1565
O
GLY
B
269
82.025
16.971
7.239
1.00
20.00
8


ATOM
1566
N
CYS
B
270
80.819
18.530
6.155
1.00
20.00
7


ATOM
1567
CA
CYS
B
270
80.445
17.613
5.083
1.00
20.00
6


ATOM
1568
CB
CYS
B
270
79.413
18.255
4.148
1.00
20.00
6


ATOM
1569
SG
CYS
B
270
77.824
18.654
4.905
1.00
20.00
16


ATOM
1570
C
GYS
B
270
81.682
17.241
4.265
1.00
20.00
6


ATOM
1571
O
CYS
B
270
81.852
16.090
3.866
1.00
20.00
8


ATOM
1572
N
ILE
B
271
82.541
18.226
4.012
1.00
20.00
7


ATOM
1573
CA
ILE
B
271
83.751
18.000
3.229
1.00
20.00
6


ATOM
1574
CB
ILE
B
271
84.436
19.339
2.903
1.00
20.00
6


ATOM
1575
CG2
ILE
B
271
85.784
19.098
2.227
1.00
20.00
6


ATOM
1576
CG1
ILE
B
271
83.508
20.171
2.007
1.00
20.00
6


ATOM
1577
CD1
ILE
B
271
83.962
21.607
1.815
1.00
20.00
6


ATOM
1578
C
ILE
B
271
84.729
17.063
3.934
1.00
20.00
6


ATOM
1579
O
ILE
B
271
85.300
16.174
3.304
1.00
20.00
8


ATOM
1580
N
ILE
B
272
84.927
17.258
5.236
1.00
20.00
7


ATOM
1581
CA
ILE
B
272
85.820
16.382
5.987
1.00
20.00
6


ATOM
1582
CB
ILE
B
272
85.902
16.790
7.471
1.00
20.00
6


ATOM
1583
CG2
ILE
B
272
86.623
15.703
8.277
1.00
20.00
6


ATOM
1584
CG1
ILE
B
272
86.646
18.120
7.606
1.00
20.00
6


ATOM
1585
CD1
ILE
B
272
86.553
18.723
9.011
1.00
20.00
6


ATOM
1586
C
ILE
B
272
85.274
14.957
5.901
1.00
20.00
6


ATOM
1587
O
ILE
B
272
86.021
14.003
5.679
1.00
20.00
8


ATOM
1588
N
TYR
B
273
83.964
14.822
6.072
1.00
20.00
7


ATOM
1589
CA
TYR
B
273
83.324
13.518
6.006
1.00
20.00
6


ATOM
1590
CB
TYR
B
273
81.825
13.651
6.287
1.00
20.00
6


ATOM
1591
CG
TYR
B
273
81.064
12.340
6.250
1.00
20.00
6


ATOM
1592
CD1
TYR
B
273
80.806
11.690
5.041
1.00
20.00
6


ATOM
1593
CE1
TYR
B
273
80.107
10.486
5.005
1.00
20.00
6


ATOM
1594
CD2
TYR
B
273
80.601
11.750
7.427
1.00
20.00
6


ATOM
1595
CE2
TYR
B
273
79.904
10.548
7.405
1.00
20.00
6


ATOM
1596
CZ
TYR
B
273
79.659
9.922
6.192
1.00
20.00
6


ATOM
1597
OH
TYR
B
273
78.971
8.736
6.174
1.00
20.00
8


ATOM
1598
C
TYR
B
273
83.550
12.897
4.632
1.00
20.00
6


ATOM
1599
O
TYR
B
273
83.865
11.713
4.526
1.00
20.00
8


ATOM
1600
N
GLN
B
274
83.402
13.705
3.586
1.00
20.00
7


ATOM
1601
CA
GLN
B
274
83.579
13.230
2.220
1.00
20.00
6


ATOM
1602
CB
GLN
B
274
83.176
14.322
1.222
1.00
20.00
6


ATOM
1603
CG
GLN
B
274
83.149
13.857
−0.230
1.00
20.00
6


ATOM
1604
CD
GLN
B
274
82.558
14.898
−1.169
1.00
20.00
6


ATOM
1605
OE1
GLN
B
274
82.108
15.961
−0.736
1.00
20.00
8


ATOM
1606
NE2
GLN
B
274
82.548
14.591
−2.462
1.00
20.00
7


ATOM
1607
C
GLN
B
274
85.013
12.788
1.953
1.00
20.00
6


ATOM
1608
O
GLN
B
274
85.239
11.818
1.233
1.00
20.00
8


ATOM
1609
N
LEU
B
275
85.981
13.498
2.528
1.00
20.00
7


ATOM
1610
CA
LEU
B
275
87.389
13.143
2.333
1.00
20.00
6


ATOM
1611
CB
LEU
B
275
88.311
14.194
2.971
1.00
20.00
6


ATOM
1612
CG
LEU
B
275
88.418
15.561
2.284
1.00
20.00
6


ATOM
1613
CD1
LEU
B
275
89.325
16.481
3.088
1.00
20.00
6


ATOM
1614
CD2
LEU
B
275
88.969
15.379
0.879
1.00
20.00
6


ATOM
1615
C
LEU
B
275
87.697
11.779
2.940
1.00
20.00
6


ATOM
1616
O
LEU
B
275
88.430
10.981
2.354
1.00
20.00
8


ATOM
1617
N
VAL
B
276
87.125
11.519
4.112
1.00
20.00
7


ATOM
1618
CA
VAL
B
276
87.353
10.269
4.827
1.00
20.00
6


ATOM
1619
CB
VAL
B
276
87.096
10.451
6.342
1.00
20.00
6


ATOM
1620
CG1
VAL
B
276
87.376
9.148
7.082
1.00
20.00
6


ATOM
1621
CG2
VAL
B
276
87.973
11.580
6.891
1.00
20.00
6


ATOM
1622
C
VAL
B
276
86.504
9.089
4.336
1.00
20.00
6


ATOM
1623
O
VAL
B
276
87.005
7.973
4.195
1.00
20.00
8


ATOM
1624
N
ALA
B
277
85.222
9.337
4.090
1.00
20.00
7


ATOM
1625
CA
ALA
B
277
84.310
8.291
3.643
1.00
20.00
6


ATOM
1626
CB
ALA
B
277
82.898
8.597
4.124
1.00
20.00
6


ATOM
1627
C
ALA
B
277
84.315
8.115
2.130
1.00
20.00
6


ATOM
1628
O
ALA
B
277
84.036
7.029
1.627
1.00
20.00
8


ATOM
1629
N
GLY
B
278
84.632
9.180
1.405
1.00
20.00
7


ATOM
1630
CA
GLY
B
278
84.653
9.099
−0.041
1.00
20.00
6


ATOM
1631
C
GLY
B
278
83.365
9.627
−0.644
1.00
20.00
6


ATOM
1632
O
GLY
B
278
83.272
9.817
−1.860
1.00
20.00
8


ATOM
1633
N
LEU
B
279
82.375
9.867
0.211
1.00
20.00
7


ATOM
1634
CA
LEU
B
279
81.075
10.382
−0.219
1.00
20.00
6


ATOM
1635
CB
LEU
B
279
80.070
9.232
−0.375
1.00
20.00
6


ATOM
1636
CG
LEU
B
279
80.342
8.114
−1.385
1.00
20.00
6


ATOM
1637
CD1
LEU
B
279
79.311
7.009
−1.191
1.00
20.00
6


ATOM
1638
CD2
LEU
B
279
80.291
8.660
−2.804
1.00
20.00
6


ATOM
1639
C
LEU
B
279
80.522
11.369
0.812
1.00
20.00
6


ATOM
1640
O
LEU
B
279
80.750
11.218
2.007
1.00
20.00
8


ATOM
1641
N
PRO
B
280
79.787
12.395
0.361
1.00
20.00
7


ATOM
1642
CD
PRO
B
280
79.403
12.730
−1.020
1.00
20.00
6


ATOM
1643
CA
PRO
B
280
79.230
13.361
1.314
1.00
20.00
6


ATOM
1644
CB
PRO
B
280
78.569
14.397
0.407
1.00
20.00
6


ATOM
1645
CG
PRO
B
280
78.191
13.598
−0.802
1.00
20.00
6


ATOM
1646
C
PRO
B
280
78.242
12.662
2.262
1.00
20.00
6


ATOM
1647
O
PRO
B
280
77.666
11.633
1.913
1.00
20.00
8


ATOM
1648
N
PRO
B
281
78.035
13.220
3.470
1.00
20.00
7


ATOM
1649
CD
PRO
B
281
78.571
14.535
3.859
1.00
20.00
6


ATOM
1650
CA
PRO
B
281
77.145
12.701
4.520
1.00
20.00
6


ATOM
1651
CB
PRO
B
281
77.262
13.746
5.634
1.00
20.00
6


ATOM
1652
CG
PRO
B
281
78.546
14.450
5.344
1.00
20.00
6


ATOM
1653
C
PRO
B
281
75.679
12.485
4.142
1.00
20.00
6


ATOM
1654
O
PRO
B
281
75.094
11.441
4.442
1.00
20.00
8


ATOM
1655
N
PHE
B
282
75.088
13.487
3.504
1.00
20.00
7


ATOM
1656
CA
PHE
B
282
73.686
13.427
3.123
1.00
20.00
6


ATOM
1657
CB
PHE
B
282
73.006
14.734
3.531
1.00
20.00
6


ATOM
1658
CG
PHE
B
282
73.300
15.146
4.947
1.00
20.00
6


ATOM
1659
CD1
PHE
B
282
72.624
14.560
6.013
1.00
20.00
6


ATOM
1660
CD2
PHE
B
282
74.295
16.085
5.218
1.00
20.00
6


ATOM
1661
CE1
PHE
B
282
72.934
14.902
7.331
1.00
20.00
6


ATOM
1662
CE2
PHE
B
282
74.613
16.433
6.530
1.00
20.00
6


ATOM
1663
CZ
PHE
B
282
73.930
15.840
7.591
1.00
20.00
6


ATOM
1664
C
PHE
B
282
73.527
13.191
1.628
1.00
20.00
6


ATOM
1665
O
PHE
B
282
73.797
14.079
0.819
1.00
20.00
8


ATOM
1666
N
ARG
B
283
73.080
11.994
1.267
1.00
20.00
7


ATOM
1667
CA
ARG
B
283
72.888
11.635
−0.134
1.00
20.00
6


ATOM
1668
CB
ARG
B
283
73.931
10.598
−0.559
1.00
20.00
6


ATOM
1669
CG
ARG
B
283
75.358
10.928
−0.151
1.00
20.00
6


ATOM
1670
CD
ARG
B
283
76.326
9.883
−0.687
1.00
20.00
6


ATOM
1671
NE
ARG
B
283
76.054
8.555
−0.142
1.00
20.00
7


ATOM
1672
CZ
ARG
B
283
76.404
8.159
1.077
1.00
20.00
6


ATOM
1673
NH1
ARG
B
283
77.047
8.986
1.893
1.00
20.00
7


ATOM
1674
NH2
ARG
B
283
76.108
6.933
1.484
1.00
20.00
7


ATOM
1675
C
ARG
B
283
71.493
11.046
−0.331
1.00
20.00
6


ATOM
1676
O
ARG
B
283
70.957
10.391
0.563
1.00
20.00
8


ATOM
1677
N
ALA
B
284
70.911
11.276
−1.502
1.00
20.00
7


ATOM
1678
CA
ALA
B
284
69.579
10.755
−1.796
1.00
20.00
6


ATOM
1679
CB
ALA
B
284
68.532
11.484
−0.961
1.00
20.00
6


ATOM
1680
C
ALA
B
284
69.278
10.921
−3.273
1.00
20.00
6


ATOM
1681
O
ALA
B
284
70.007
11.611
−3.984
1.00
20.00
8


ATOM
1682
N
GLY
B
285
68.191
10.299
−3.722
1.00
20.00
7


ATOM
1683
CA
GLY
B
285
67.807
10.360
−5.122
1.00
20.00
6


ATOM
1684
C
GLY
B
285
67.561
11.737
−5.707
1.00
20.00
6


ATOM
1685
O
GLY
B
285
67.775
11.955
−6.899
1.00
20.00
8


ATOM
1686
N
ASN
B
286
67.089
12.673
−4.892
1.00
20.00
7


ATOM
1687
CA
ASN
B
286
66.835
14.018
−5.386
1.00
20.00
6


ATOM
1688
CB
ASN
B
286
65.403
14.137
−5.930
1.00
20.00
6


ATOM
1689
CG
ASN
B
286
64.342
13.825
−4.885
1.00
20.00
6


ATOM
1690
OD1
ASN
B
286
64.292
14.450
−3.826
1.00
20.00
8


ATOM
1691
ND2
ASN
B
286
63.477
12.861
−5.190
1.00
20.00
7


ATOM
1692
C
ASN
B
286
67.076
15.042
−4.291
1.00
20.00
6


ATOM
1693
O
ASN
B
286
67.368
14.682
−3.152
1.00
20.00
8


ATOM
1694
N
GLU
B
287
66.955
16.317
−4.636
1.00
20.00
7


ATOM
1695
CA
GLU
B
287
67.185
17.377
−3.669
1.00
20.00
6


ATOM
1696
CB
GLU
B
287
67.181
18.738
−4.365
1.00
20.00
6


ATOM
1697
CG
GLU
B
287
68.537
19.095
−4.944
1.00
20.00
6


ATOM
1698
CD
GLU
B
287
68.524
20.385
−5.735
1.00
20.00
6


ATOM
1699
OE1
GLU
B
287
67.911
21.371
−5.267
1.00
20.00
8


ATOM
1700
OE2
GLU
B
287
69.144
20.410
−6.823
1.00
20.00
8


ATOM
1701
C
GLU
B
287
66.225
17.394
−2.492
1.00
20.00
6


ATOM
1702
O
GLU
B
287
66.658
17.554
−1.354
1.00
20.00
8


ATOM
1703
N
TYR
B
288
64.932
17.233
−2.753
1.00
20.00
7


ATOM
1704
CA
TYR
B
288
63.955
17.239
−1.670
1.00
20.00
6


ATOM
1705
CB
TYR
B
288
62.553
16.899
−2.184
1.00
20.00
6


ATOM
1706
CG
TYR
B
288
61.530
16.780
−1.070
1.00
20.00
6


ATOM
1707
CD1
TYR
B
288
60.984
17.917
−0.470
1.00
20.00
6


ATOM
1708
CE1
TYR
B
288
60.090
17.814
0.600
1.00
20.00
6


ATOM
1709
CD2
TYR
B
288
61.154
15.529
−0.573
1.00
20.00
6


ATOM
1710
CE2
TYR
B
288
60.265
15.414
0.498
1.00
20.00
6


ATOM
1711
CZ
TYR
B
288
59.740
16.561
1.078
1.00
20.00
6


ATOM
1712
OH
TYR
B
288
58.884
16.454
2.149
1.00
20.00
8


ATOM
1713
C
TYR
B
288
64.337
16.238
−0.587
1.00
20.00
6


ATOM
1714
O
TYR
B
288
64.254
16.545
0.598
1.00
20.00
8


ATOM
1715
N
LEU
B
289
64.750
15.041
−1.001
1.00
20.00
7


ATOM
1716
CA
LEU
B
289
65.137
13.989
−0.064
1.00
20.00
6


ATOM
1717
CB
LEU
B
289
65.283
12.649
−0.797
1.00
20.00
6


ATOM
1718
CG
LEU
B
289
63.984
11.985
−1.274
1.00
20.00
6


ATOM
1719
CD1
LEU
B
289
64.314
10.802
−2.179
1.00
20.00
6


ATOM
1720
CD2
LEU
B
289
63.160
11.530
−0.068
1.00
20.00
6


ATOM
1721
C
LEU
B
289
66.431
14.310
0.685
1.00
20.00
6


ATOM
1722
O
LEU
B
289
66.604
13.914
1.840
1.00
20.00
8


ATOM
1723
N
ILE
B
290
67.340
15.017
0.025
1.00
20.00
7


ATOM
1724
CA
ILE
B
290
68.597
15.390
0.658
1.00
20.00
6


ATOM
1725
CB
ILE
B
290
69.583
15.985
−0.366
1.00
20.00
6


ATOM
1726
CG2
ILE
B
290
70.778
16.609
0.359
1.00
20.00
6


ATOM
1727
CG1
ILE
B
290
70.046
14.887
−1.330
1.00
20.00
6


ATOM
1728
CD1
ILE
B
290
70.844
15.398
−2.518
1.00
20.00
6


ATOM
1729
C
ILE
B
290
68.307
16.424
1.743
1.00
20.00
6


ATOM
1730
O
ILE
B
290
68.807
16.317
2.862
1.00
20.00
8


ATOM
1731
N
PHE
B
291
67.491
17.420
1.411
1.00
20.00
7


ATOM
1732
CA
PHE
B
291
67.143
18.462
2.372
1.00
20.00
6


ATOM
1733
CB
PHE
B
291
66.222
19.502
1.731
1.00
20.00
6


ATOM
1734
CG
PHE
B
291
66.869
20.289
0.628
1.00
20.00
6


ATOM
1735
CD1
PHE
B
291
68.255
20.420
0.568
1.00
20.00
6


ATOM
1736
CD2
PHE
B
291
66.094
20.931
−0.332
1.00
20.00
6


ATOM
1737
CE1
PHE
B
291
68.859
21.182
−0.435
1.00
20.00
6


ATOM
1738
CE2
PHE
B
291
66.690
21.697
−1.340
1.00
20.00
6


ATOM
1739
CZ
PHE
B
291
68.074
21.822
−1.390
1.00
20.00
6


ATOM
1740
C
PHE
B
291
66.453
17.848
3.576
1.00
20.00
6


ATOM
1741
O
PHE
B
291
66.664
18.262
4.718
1.00
20.00
8


ATOM
1742
N
GLN
B
292
65.629
16.847
3.303
1.00
20.00
7


ATOM
1743
CA
GLN
B
292
64.887
16.154
4.341
1.00
20.00
6


ATOM
1744
CB
GLN
B
292
64.006
15.090
3.687
1.00
20.00
6


ATOM
1745
CG
GLN
B
292
62.953
14.486
4.572
1.00
20.00
6


ATOM
1746
CD
GLN
B
292
61.895
13.750
3.763
1.00
20.00
6


ATOM
1747
OE1
GLN
B
292
62.208
12.835
2.997
1.00
20.00
8


ATOM
1748
NE2
GLN
B
292
60.637
14.155
3.924
1.00
20.00
7


ATOM
1749
C
GLN
B
292
65.865
15.522
5.329
1.00
20.00
6


ATOM
1750
O
GLN
B
292
65.689
15.630
6.540
1.00
20.00
8


ATOM
1751
N
LYS
B
293
66.907
14.875
4.812
1.00
20.00
7


ATOM
1752
CA
LYS
B
293
67.898
14.244
5.683
1.00
20.00
6


ATOM
1753
CB
LYS
B
293
68.850
13.372
4.865
1.00
20.00
6


ATOM
1754
CG
LYS
B
293
68.197
12.135
4.278
1.00
20.00
6


ATOM
1755
CD
LYS
B
293
69.217
11.260
3.554
1.00
20.00
6


ATOM
1756
CE
LYS
B
293
68.575
9.972
3.051
1.00
20.00
6


ATOM
1757
NZ
LYS
B
293
69.553
9.099
2.339
1.00
20.00
7


ATOM
1758
C
LYS
B
293
68.698
15.287
6.468
1.00
20.00
6


ATOM
1759
O
LYS
B
293
69.044
15.074
7.634
1.00
20.00
8


ATOM
1760
N
ILE
B
294
68.989
16.411
5.827
1.00
20.00
7


ATOM
1761
CA
ILE
B
294
69.745
17.480
6.472
1.00
20.00
6


ATOM
1762
CB
ILE
B
294
70.026
18.632
5.474
1.00
20.00
6


ATOM
1763
CG2
ILE
B
294
70.489
19.881
6.223
1.00
20.00
6


ATOM
1764
CG1
ILE
B
294
71.070
18.178
4.443
1.00
20.00
6


ATOM
1765
CD1
ILE
B
294
71.266
19.159
3.303
1.00
20.00
6


ATOM
1766
C
ILE
B
294
69.035
18.045
7.712
1.00
20.00
6


ATOM
1767
O
ILE
B
294
69.618
18.091
8.798
1.00
20.00
8


ATOM
1768
N
ILE
B
295
67.783
18.467
7.564
1.00
20.00
7


ATOM
1769
CA
ILE
B
295
67.068
19.037
8.707
1.00
20.00
6


ATOM
1770
CB
ILE
B
295
65.710
19.647
8.300
1.00
20.00
6


ATOM
1771
CG2
ILE
B
295
65.927
20.749
7.265
1.00
20.00
6


ATOM
1772
CG1
ILE
B
295
64.784
18.559
7.762
1.00
20.00
6


ATOM
1773
CD1
ILE
B
295
63.356
19.037
7.558
1.00
20.00
6


ATOM
1774
C
ILE
B
295
66.831
18.045
9.842
1.00
20.00
6


ATOM
1775
O
ILE
B
295
66.540
18.447
10.967
1.00
20.00
8


ATOM
1776
N
LYS
B
296
66.956
16.753
9.550
1.00
20.00
7


ATOM
1777
CA
LYS
B
296
66.765
15.724
10.569
1.00
20.00
6


ATOM
1778
CB
LYS
B
296
65.907
14.576
10.019
1.00
20.00
6


ATOM
1779
CG
LYS
B
296
64.535
15.010
9.538
1.00
20.00
6


ATOM
1780
CD
LYS
B
296
63.739
13.851
8.951
1.00
20.00
6


ATOM
1781
CE
LYS
B
296
63.296
12.873
10.025
1.00
20.00
6


ATOM
1782
NZ
LYS
B
296
62.375
11.828
9.482
1.00
20.00
7


ATOM
1783
C
LYS
B
296
68.116
15.176
11.018
1.00
20.00
6


ATOM
1784
O
LYS
B
296
68.178
14.261
11.838
1.00
20.00
8


ATOM
1785
N
LEU
B
297
69.190
15.746
10.474
1.00
20.00
7


ATOM
1786
CA
LEU
B
297
70.551
15.320
10.791
1.00
20.00
6


ATOM
1787
CB
LEU
B
297
70.911
15.680
12.236
1.00
20.00
6


ATOM
1788
CG
LEU
B
297
72.398
15.538
12.585
1.00
20.00
6


ATOM
1789
CD1
LEU
B
297
73.215
16.555
11.771
1.00
20.00
6


ATOM
1790
CD2
LEU
B
297
72.605
15.762
14.076
1.00
20.00
6


ATOM
1791
C
LEU
B
297
70.635
13.810
10.592
1.00
20.00
6


ATOM
1792
O
LEU
B
297
71.150
13.080
11.434
1.00
20.00
8


ATOM
1793
N
GLU
B
298
70.128
13.351
9.456
1.00
20.00
7


ATOM
1794
CA
GLU
B
298
70.115
11.934
9.148
1.00
20.00
6


ATOM
1795
CB
GLU
B
298
68.817
11.597
8.416
1.00
20.00
6


ATOM
1796
CG
GLU
B
298
68.568
10.123
8.233
1.00
20.00
6


ATOM
1797
CD
GLU
B
298
67.254
9.858
7.535
1.00
20.00
6


ATOM
1798
OE1
GLU
B
298
66.214
10.331
8.043
1.00
20.00
8


ATOM
1799
OE2
GLU
B
298
67.261
9.185
6.484
1.00
20.00
8


ATOM
1800
C
GLU
B
298
71.309
11.446
8.332
1.00
20.00
6


ATOM
1801
O
GLU
B
298
71.310
11.523
7.104
1.00
20.00
8


ATOM
1802
N
TYR
B
299
72.325
10.946
9.027
1.00
20.00
7


ATOM
1803
CA
TYR
B
299
73.519
10.405
8.390
1.00
20.00
6


ATOM
1804
CB
TYR
B
299
74.444
11.521
7.880
1.00
20.00
6


ATOM
1805
CG
TYR
B
299
75.330
12.130
8.953
1.00
20.00
6


ATOM
1806
CD1
TYR
B
299
74.796
12.962
9.935
1.00
20.00
6


ATOM
1807
CE1
TYR
B
299
75.589
13.482
10.951
1.00
20.00
6


ATOM
1808
CD2
TYR
B
299
76.692
11.833
9.013
1.00
20.00
6


ATOM
1809
CE2
TYR
B
299
77.499
12.352
10.032
1.00
20.00
6


ATOM
1810
CZ
TYR
B
299
76.935
13.173
10.995
1.00
20.00
6


ATOM
1811
OH
TYR
B
299
77.701
13.687
12.006
1.00
20.00
8


ATOM
1812
C
TYR
B
299
74.245
9.600
9.456
1.00
20.00
6


ATOM
1813
O
TYR
B
299
73.913
9.688
10.631
1.00
20.00
8


ATOM
1814
N
ASP
B
300
75.229
8.808
9.052
1.00
20.00
7


ATOM
1815
CA
ASP
B
300
75.991
8.030
10.016
1.00
20.00
6


ATOM
1816
CB
ASP
B
300
75.291
6.700
10.304
1.00
20.00
6


ATOM
1817
CG
ASP
B
300
74.898
5.968
9.048
1.00
20.00
6


ATOM
1818
OD1
ASP
B
300
75.806
5.594
8.274
1.00
20.00
8


ATOM
1819
OD2
ASP
B
300
73.681
5.771
8.832
1.00
20.00
8


ATOM
1820
C
ASP
B
300
77.397
7.799
9.488
1.00
20.00
6


ATOM
1821
O
ASP
B
300
77.651
7.976
8.297
1.00
20.00
8


ATOM
1822
N
PHE
B
301
78.307
7.417
10.378
1.00
20.00
7


ATOM
1823
CA
PHE
B
301
79.695
7.186
9.996
1.00
20.00
6


ATOM
1824
CB
PHE
B
301
80.655
7.664
11.093
1.00
20.00
6


ATOM
1825
CG
PHE
B
301
80.488
9.103
11.481
1.00
20.00
6


ATOM
1826
CD1
PHE
B
301
79.493
9.487
12.370
1.00
20.00
6


ATOM
1827
CD2
PHE
B
301
81.346
10.075
10.970
1.00
20.00
6


ATOM
1828
CE1
PHE
B
301
79.352
10.823
12.750
1.00
20.00
6


ATOM
1829
CE2
PHE
B
301
81.214
11.408
11.342
1.00
20.00
6


ATOM
1830
CZ
PHE
B
301
80.215
11.783
12.235
1.00
20.00
6


ATOM
1831
C
PHE
B
301
80.009
5.722
9.744
1.00
20.00
6


ATOM
1832
O
PHE
B
301
79.506
4.839
10.442
1.00
20.00
8


ATOM
1833
N
PRO
B
302
80.842
5.440
8.732
1.00
20.00
7


ATOM
1834
CD
PRO
B
302
81.330
6.316
7.654
1.00
20.00
6


ATOM
1835
CA
PRO
B
302
81.191
4.044
8.466
1.00
20.00
6


ATOM
1836
CB
PRO
B
302
81.838
4.105
7.084
1.00
20.00
6


ATOM
1837
CG
PRO
B
302
82.425
5.479
7.046
1.00
20.00
6


ATOM
1838
C
PRO
B
302
82.168
3.629
9.569
1.00
20.00
6


ATOM
1839
O
PRO
B
302
82.887
4.469
10.111
1.00
20.00
8


ATOM
1840
N
ALA
B
303
82.185
2.345
9.908
1.00
20.00
7


ATOM
1841
CA
ALA
B
303
83.052
1.836
10.968
1.00
20.00
6


ATOM
1842
CB
ALA
B
303
82.993
0.310
10.987
1.00
20.00
6


ATOM
1843
C
ALA
B
303
84.513
2.294
10.939
1.00
20.00
6


ATOM
1844
O
ALA
B
303
85.078
2.637
11.979
1.00
20.00
8


ATOM
1845
N
ALA
B
304
85.121
2.306
9.756
1.00
20.00
7


ATOM
1846
CA
ALA
B
304
86.527
2.684
9.605
1.00
20.00
6


ATOM
1847
CB
ALA
B
304
86.971
2.423
8.165
1.00
20.00
6


ATOM
1848
C
ALA
B
304
86.894
4.119
10.001
1.00
20.00
6


ATOM
1849
O
ALA
B
304
87.983
4.367
10.520
1.00
20.00
8


ATOM
1850
N
PHE
B
305
85.985
5.053
9.742
1.00
20.00
7


ATOM
1851
CA
PHE
B
305
86.183
6.473
10.034
1.00
20.00
6


ATOM
1852
CB
PHE
B
305
84.822
7.115
10.312
1.00
20.00
6


ATOM
1853
CG
PHE
B
305
84.705
8.522
9.815
1.00
20.00
6


ATOM
1854
CD1
PHE
B
305
85.303
9.572
10.502
1.00
20.00
6


ATOM
1855
CD2
PHE
B
305
84.003
8.800
8.646
1.00
20.00
6


ATOM
1856
CE1
PHE
B
305
85.202
10.881
10.033
1.00
20.00
6


ATOM
1857
CE2
PHE
B
305
83.896
10.106
8.167
1.00
20.00
6


ATOM
1858
CZ
PHE
B
305
84.496
11.147
8.862
1.00
20.00
6


ATOM
1859
C
PHE
B
305
87.153
6.789
11.182
1.00
20.00
6


ATOM
1860
O
PHE
B
305
86.964
6.342
12.312
1.00
20.00
8


ATOM
1861
N
PHE
B
306
88.190
7.565
10.883
1.00
20.00
7


ATOM
1862
CA
PHE
B
306
89.176
7.945
11.894
1.00
20.00
6


ATOM
1863
CB
PHE
B
306
90.179
8.936
11.295
1.00
20.00
6


ATOM
1864
CG
PHE
B
306
90.695
8.531
9.940
1.00
20.00
6


ATOM
1865
CD1
PHE
B
306
91.292
7.284
9.747
1.00
20.00
6


ATOM
1866
CD2
PHE
B
306
90.588
9.395
8.853
1.00
20.00
6


ATOM
1867
CE1
PHE
B
306
91.774
6.906
8.490
1.00
20.00
6


ATOM
1868
CE2
PHE
B
306
91.067
9.027
7.590
1.00
20.00
6


ATOM
1869
CZ
PHE
B
306
91.662
7.780
7.408
1.00
20.00
6


ATOM
1870
C
PHE
B
306
88.445
8.575
13.086
1.00
20.00
6


ATOM
1871
O
PHE
B
306
87.731
9.566
12.936
1.00
20.00
8


ATOM
1872
N
PRO
B
307
88.614
7.995
14.288
1.00
20.00
7


ATOM
1873
CD
PRO
B
307
89.482
6.834
14.555
1.00
20.00
6


ATOM
1874
CA
PRO
B
307
87.983
8.459
15.530
1.00
20.00
6


ATOM
1875
CB
PRO
B
307
88.748
7.691
16.606
1.00
20.00
6


ATOM
1876
CG
PRO
B
307
89.018
6.388
15.928
1.00
20.00
6


ATOM
1877
C
PRO
B
307
87.986
9.965
15.784
1.00
20.00
6


ATOM
1878
O
PRO
B
307
86.936
10.565
16.025
1.00
20.00
8


ATOM
1879
N
LYS
B
308
89.162
10.575
15.745
1.00
20.00
7


ATOM
1880
CA
LYS
B
308
89.260
12.004
15.992
1.00
20.00
6


ATOM
1881
CB
LYS
B
308
90.728
12.405
16.149
1.00
20.00
6


ATOM
1882
CG
LYS
B
308
91.338
11.805
17.410
1.00
20.00
6


ATOM
1883
CD
LYS
B
308
92.806
12.140
17.591
1.00
20.00
6


ATOM
1884
CE
LYS
B
308
93.339
11.457
18.847
1.00
20.00
6


ATOM
1885
NZ
LYS
B
308
94.816
11.573
18.985
1.00
20.00
7


ATOM
1886
C
LYS
B
308
88.572
12.808
14.894
1.00
20.00
6


ATOM
1887
O
LYS
B
308
87.985
13.855
15.167
1.00
20.00
8


ATOM
1888
N
ALA
B
309
88.629
12.318
13.659
1.00
20.00
7


ATOM
1889
CA
ALA
B
309
87.967
13.011
12.557
1.00
20.00
6


ATOM
1890
CB
ALA
B
309
88.328
12.369
11.231
1.00
20.00
6


ATOM
1891
C
ALA
B
309
86.460
12.936
12.787
1.00
20.00
6


ATOM
1892
O
ALA
B
309
85.735
13.903
12.552
1.00
20.00
8


ATOM
1893
N
ARG
B
310
85.986
11.780
13.246
1.00
20.00
7


ATOM
1894
CA
ARG
B
310
84.561
11.619
13.513
1.00
20.00
6


ATOM
1895
CB
ARG
B
310
84.246
10.194
13.979
1.00
20.00
6


ATOM
1896
CG
ARG
B
310
82.844
10.069
14.561
1.00
20.00
6


ATOM
1897
CD
ARG
B
310
82.408
8.632
14.789
1.00
20.00
6


ATOM
1898
NE
ARG
B
310
81.060
8.593
15.355
1.00
20.00
7


ATOM
1899
CZ
ARG
B
310
80.259
7.532
15.328
1.00
20.00
6


ATOM
1900
NH1
ARG
B
310
80.665
6.401
14.759
1.00
20.00
7


ATOM
1901
NH2
ARG
B
310
79.048
7.601
15.867
1.00
20.00
7


ATOM
1902
C
ARG
B
310
84.110
12.613
14.583
1.00
20.00
6


ATOM
1903
O
ARG
B
310
83.080
13.274
14.436
1.00
20.00
8


ATOM
1904
N
ASP
B
311
84.876
12.707
15.666
1.00
20.00
7


ATOM
1905
CA
ASP
B
311
84.535
13.629
16.740
1.00
20.00
6


ATOM
1906
CB
ASP
B
311
85.574
13.555
17.864
1.00
20.00
6


ATOM
1907
CG
ASP
B
311
85.260
14.505
19.006
1.00
20.00
6


ATOM
1908
OD1
ASP
B
311
85.782
15.636
19.010
1.00
20.00
8


ATOM
1909
OD2
ASP
B
311
84.480
14.124
19.901
1.00
20.00
8


ATOM
1910
C
ASP
B
311
84.445
15.054
16.198
1.00
20.00
6


ATOM
1911
O
ASP
B
311
83.539
15.800
16.564
1.00
20.00
8


ATOM
1912
N
LEU
B
312
85.371
15.423
15.313
1.00
20.00
7


ATOM
1913
CA
LEU
B
312
85.362
16.769
14.736
1.00
20.00
6


ATOM
1914
CB
LEU
B
312
86.604
16.999
13.869
1.00
20.00
6


ATOM
1915
CG
LEU
B
312
86.662
18.329
13.099
1.00
20.00
6


ATOM
1916
CD1
LEU
B
312
86.424
19.510
14.037
1.00
20.00
6


ATOM
1917
CD2
LEU
B
312
88.018
18.450
12.414
1.00
20.00
6


ATOM
1918
C
LEU
B
312
84.112
17.008
13.899
1.00
20.00
6


ATOM
1919
O
LEU
B
312
83.456
18.039
14.035
1.00
20.00
8


ATOM
1920
N
VAL
B
313
83.786
16.051
13.033
1.00
20.00
7


ATOM
1921
CA
VAL
B
313
82.611
16.171
12.183
1.00
20.00
6


ATOM
1922
CB
VAL
B
313
82.464
14.942
11.255
1.00
20.00
6


ATOM
1923
CG1
VAL
B
313
81.121
14.973
10.551
1.00
20.00
6


ATOM
1924
CG2
VAL
B
313
83.595
14.935
10.228
1.00
20.00
6


ATOM
1925
C
VAL
B
313
81.354
16.315
13.036
1.00
20.00
6


ATOM
1926
O
VAL
B
313
80.467
17.111
12.716
1.00
20.00
8


ATOM
1927
N
GLU
B
314
81.282
15.559
14.129
1.00
20.00
7


ATOM
1928
CA
GLU
B
314
80.122
15.634
15.010
1.00
20.00
6


ATOM
1929
CB
GLU
B
314
80.191
14.545
16.084
1.00
20.00
6


ATOM
1930
CG
GLU
B
314
80.160
13.131
15.521
1.00
20.00
6


ATOM
1931
CD
GLU
B
314
80.222
12.073
16.603
1.00
20.00
6


ATOM
1932
OE1
GLU
B
314
81.033
12.227
17.542
1.00
20.00
8


ATOM
1933
OE2
GLU
B
314
79.469
11.081
16.512
1.00
20.00
8


ATOM
1934
C
GLU
B
314
80.035
17.005
15.664
1.00
20.00
6


ATOM
1935
O
GLU
B
314
78.960
17.443
16.059
1.00
20.00
8


ATOM
1936
N
LYS
B
315
81.165
17.690
15.776
1.00
20.00
7


ATOM
1937
CA
LYS
B
315
81.154
19.010
16.383
1.00
20.00
6


ATOM
1938
CB
LYS
B
315
82.448
19.240
17.168
1.00
20.00
6


ATOM
1939
CG
LYS
B
315
82.460
18.478
18.493
1.00
20.00
6


ATOM
1940
CD
LYS
B
315
83.803
18.529
19.198
1.00
20.00
6


ATOM
1941
CE
LYS
B
315
83.749
17.825
20.552
1.00
20.00
6


ATOM
1942
NZ
LYS
B
315
82.829
18.505
21.506
1.00
20.00
7


ATOM
1943
C
LYS
B
315
80.934
20.104
15.343
1.00
20.00
6


ATOM
1944
O
LYS
B
315
80.855
21.282
15.686
1.00
20.00
8


ATOM
1945
N
LEU
B
316
80.819
19.706
14.075
1.00
20.00
7


ATOM
1946
CA
LEU
B
316
80.577
20.649
12.979
1.00
20.00
6


ATOM
1947
CB
LEU
B
316
81.608
20.450
11.863
1.00
20.00
6


ATOM
1948
CG
LEU
B
316
83.044
20.833
12.240
1.00
20.00
6


ATOM
1949
CD1
LEU
B
316
84.011
20.365
11.156
1.00
20.00
6


ATOM
1950
CD2
LEU
B
316
83.124
22.351
12.434
1.00
20.00
6


ATOM
1951
C
LEU
B
316
79.164
20.469
12.415
1.00
20.00
6


ATOM
1952
O
LEU
B
316
78.464
21.448
12.148
1.00
20.00
8


ATOM
1953
N
LEU
B
317
78.746
19.220
12.230
1.00
20.00
7


ATOM
1954
CA
LEU
B
317
77.403
18.962
11.721
1.00
20.00
6


ATOM
1955
CB
LEU
B
317
77.343
17.605
11.012
1.00
20.00
6


ATOM
1956
CG
LEU
B
317
78.335
17.445
9.852
1.00
20.00
6


ATOM
1957
CD1
LEU
B
317
78.091
16.111
9.143
1.00
20.00
6


ATOM
1958
CD2
LEU
B
317
78.182
18.603
8.866
1.00
20.00
6


ATOM
1959
C
LEU
B
317
76.435
19.000
12.899
1.00
20.00
6


ATOM
1960
O
LEU
B
317
75.979
17.966
13.398
1.00
20.00
8


ATOM
1961
N
VAL
B
318
76.156
20.215
13.354
1.00
20.00
7


ATOM
1962
CA
VAL
B
318
75.251
20.451
14.467
1.00
20.00
6


ATOM
1963
CB
VAL
B
318
75.981
21.164
15.625
1.00
20.00
6


ATOM
1964
CG1
VAL
B
318
75.007
21.461
16.759
1.00
20.00
6


ATOM
1965
CG2
VAL
B
318
77.136
20.300
16.115
1.00
20.00
6


ATOM
1966
C
VAL
B
318
74.140
21.344
13.936
1.00
20.00
6


ATOM
1967
O
VAL
B
318
74.410
22.386
13.333
1.00
20.00
8


ATOM
1968
N
LEU
B
319
72.892
20.941
14.153
1.00
20.00
7


ATOM
1969
CA
LEU
B
319
71.758
21.717
13.663
1.00
20.00
6


ATOM
1970
CB
LEU
B
319
70.444
21.056
14.093
1.00
20.00
6


ATOM
1971
CG
LEU
B
319
70.211
19.647
13.533
1.00
20.00
6


ATOM
1972
CD1
LEU
B
319
68.883
19.098
14.060
1.00
20.00
6


ATOM
1973
CD2
LEU
B
319
70.211
19.688
12.000
1.00
20.00
6


ATOM
1974
C
LEU
B
319
71.794
23.173
14.119
1.00
20.00
6


ATOM
1975
O
LEU
B
319
71.591
24.082
13.317
1.00
20.00
8


ATOM
1976
N
ASP
B
320
72.052
23.394
15.405
1.00
20.00
7


ATOM
1977
CA
ASP
B
320
72.119
24.745
15.958
1.00
20.00
6


ATOM
1978
CB
ASP
B
320
72.091
24.687
17.490
1.00
20.00
6


ATOM
1979
CG
ASP
B
320
72.058
26.061
18.129
1.00
20.00
6


ATOM
1980
OD1
ASP
B
320
72.506
27.036
17.492
1.00
20.00
8


ATOM
1981
OD2
ASP
B
320
71.595
26.166
19.284
1.00
20.00
8


ATOM
1982
C
ASP
B
320
73.415
25.419
15.492
1.00
20.00
6


ATOM
1983
O
ASP
B
320
74.496
25.089
15.965
1.00
20.00
8


ATOM
1984
N
ALA
B
321
73.294
26.372
14.576
1.00
20.00
7


ATOM
1985
CA
ALA
B
321
74.450
27.078
14.028
1.00
20.00
6


ATOM
1986
CB
ALA
B
321
73.982
28.109
13.006
1.00
20.00
6


ATOM
1987
C
ALA
B
321
75.359
27.747
15.065
1.00
20.00
6


ATOM
1988
O
ALA
B
321
76.535
27.992
14.790
1.00
20.00
8


ATOM
1989
N
THR
B
322
74.829
28.035
16.252
1.00
20.00
7


ATOM
1990
CA
THR
B
322
75.631
28.681
17.292
1.00
20.00
6


ATOM
1991
CB
THR
B
322
74.755
29.491
18.271
1.00
20.00
6


ATOM
1992
OG1
THR
B
322
73.879
28.605
18.973
1.00
20.00
8


ATOM
1993
CG2
THR
B
322
73.928
30.527
17.519
1.00
20.00
6


ATOM
1994
C
THR
B
322
76.437
27.684
18.108
1.00
20.00
6


ATOM
1995
O
THR
B
322
77.166
28.071
19.019
1.00
20.00
8


ATOM
1996
N
LYS
B
323
76.312
26.401
17.786
1.00
20.00
7


ATOM
1997
CA
LYS
B
323
77.048
25.378
18.517
1.00
20.00
6


ATOM
1998
CB
LYS
B
323
76.080
24.378
19.155
1.00
20.00
6


ATOM
1999
CG
LYS
B
323
75.180
24.992
20.209
1.00
20.00
6


ATOM
2000
CD
LYS
B
323
74.356
23.931
20.924
1.00
20.00
6


ATOM
2001
CE
LYS
B
323
73.406
24.574
21.927
1.00
20.00
6


ATOM
2002
NZ
LYS
B
323
74.144
25.514
22.818
1.00
20.00
7


ATOM
2003
C
LYS
B
323
78.066
24.631
17.664
1.00
20.00
6


ATOM
2004
O
LYS
B
323
78.520
23.557
18.040
1.00
20.00
8


ATOM
2005
N
ARG
B
324
78.427
25.195
16.517
1.00
20.00
7


ATOM
2006
CA
ARG
B
324
79.408
24.545
15.656
1.00
20.00
6


ATOM
2007
CB
ARG
B
324
79.108
24.834
14.186
1.00
20.00
6


ATOM
2008
CG
ARG
B
324
77.824
24.177
13.728
1.00
20.00
6


ATOM
2009
CD
ARG
B
324
77.468
24.505
12.297
1.00
20.00
6


ATOM
2010
NE
ARG
B
324
76.060
24.202
12.069
1.00
20.00
7


ATOM
2011
CZ
ARG
B
324
75.277
24.873
11.233
1.00
20.00
6


ATOM
2012
NH1
ARG
B
324
75.764
25.888
10.523
1.00
20.00
7


ATOM
2013
NH2
ARG
B
324
73.992
24.551
11.140
1.00
20.00
7


ATOM
2014
C
ARG
B
324
80.811
25.011
16.008
1.00
20.00
6


ATOM
2015
O
ARG
B
324
81.070
26.212
16.131
1.00
20.00
8


ATOM
2016
N
LEU
B
325
81.711
24.049
16.180
1.00
20.00
7


ATOM
2017
CA
LEU
B
325
83.090
24.350
16.520
1.00
20.00
6


ATOM
2018
CB
LEU
B
325
83.913
23.061
16.550
1.00
20.00
6


ATOM
2019
CG
LEU
B
325
85.274
23.123
17.241
1.00
20.00
6


ATOM
2020
CD1
LEU
B
325
85.093
23.591
18.682
1.00
20.00
6


ATOM
2021
CD2
LEU
B
325
85.922
21.741
17.209
1.00
20.00
6


ATOM
2022
C
LEU
B
325
83.656
25.310
15.481
1.00
20.00
6


ATOM
2023
O
LEU
B
325
83.649
25.015
14.282
1.00
20.00
8


ATOM
2024
N
GLY
B
326
84.139
26.461
15.946
1.00
20.00
7


ATOM
2025
CA
GLY
B
326
84.697
27.449
15.040
1.00
20.00
6


ATOM
2026
C
GLY
B
326
83.857
28.711
14.932
1.00
20.00
6


ATOM
2027
O
GLY
B
326
84.369
29.757
14.529
1.00
20.00
8


ATOM
2028
N
CYS
B
327
82.575
28.632
15.286
1.00
20.00
7


ATOM
2029
CA
CYS
B
327
81.714
29.806
15.200
1.00
20.00
6


ATOM
2030
CB
CYS
B
327
80.233
29.404
15.183
1.00
20.00
6


ATOM
2031
SG
CYS
B
327
79.534
28.915
16.774
1.00
20.00
16


ATOM
2032
C
CYS
B
327
81.976
30.772
16.353
1.00
20.00
6


ATOM
2033
O
CYS
B
327
82.565
30.410
17.371
1.00
20.00
8


ATOM
2034
N
GLU
B
328
81.523
32.005
16.178
1.00
20.00
7


ATOM
2035
CA
GLU
B
328
81.714
33.052
17.167
1.00
20.00
6


ATOM
2036
CB
GLU
B
328
81.087
34.348
16.632
1.00
20.00
6


ATOM
2037
CG
GLU
B
328
81.734
34.772
15.300
1.00
20.00
6


ATOM
2038
CD
GLU
B
328
80.962
35.842
14.539
1.00
20.00
6


ATOM
2039
OE1
GLU
B
328
79.738
35.676
14.343
1.00
20.00
8


ATOM
2040
OE2
GLU
B
328
81.588
36.840
14.116
1.00
20.00
8


ATOM
2041
C
GLU
B
328
81.187
32.701
18.560
1.00
20.00
6


ATOM
2042
O
GLU
B
328
81.850
32.983
19.562
1.00
20.00
8


ATOM
2043
N
GLU
B
329
80.016
32.073
18.631
1.00
20.00
7


ATOM
2044
CA
GLU
B
329
79.449
31.714
19.926
1.00
20.00
6


ATOM
2045
CB
GLU
B
329
77.991
31.263
19.782
1.00
20.00
6


ATOM
2046
CG
GLU
B
329
77.028
32.355
19.315
1.00
20.00
6


ATOM
2047
CD
GLU
B
329
77.055
32.575
17.813
1.00
20.00
6


ATOM
2048
OE1
GLU
B
329
77.859
31.910
17.120
1.00
20.00
8


ATOM
2049
OE2
GLU
B
329
76.267
33.413
17.323
1.00
20.00
8


ATOM
2050
C
GLU
B
329
80.264
30.616
20.605
1.00
20.00
6


ATOM
2051
O
GLU
B
329
80.182
30.436
21.819
1.00
20.00
8


ATOM
2052
N
MET
B
330
81.040
29.878
19.816
1.00
20.00
7


ATOM
2053
CA
MET
B
330
81.880
28.813
20.354
1.00
20.00
6


ATOM
2054
CB
MET
B
330
81.872
27.600
19.419
1.00
20.00
6


ATOM
2055
CG
MET
B
330
80.552
26.822
19.436
1.00
20.00
6


ATOM
2056
SD
MET
B
330
80.117
26.254
21.104
1.00
20.00
16


ATOM
2057
CE
MET
B
330
81.265
24.895
21.311
1.00
20.00
6


ATOM
2058
C
MET
B
330
83.302
29.330
20.547
1.00
20.00
6


ATOM
2059
O
MET
B
330
84.236
28.564
20.754
1.00
20.00
8


ATOM
2060
N
GLU
B
331
83.443
30.647
20.471
1.00
20.00
7


ATOM
2061
CA
GLU
B
331
84.716
31.338
20.656
1.00
20.00
6


ATOM
2062
CB
GLU
B
331
85.357
30.921
21.987
1.00
20.00
6


ATOM
2063
CG
GLU
B
331
84.371
30.886
23.163
1.00
20.00
6


ATOM
2064
CD
GLU
B
331
83.478
32.127
23.270
1.00
20.00
6


ATOM
2065
OE1
GLU
B
331
82.483
32.064
24.021
1.00
20.00
8


ATOM
2066
OE2
GLU
B
331
83.759
33.159
22.625
1.00
20.00
8


ATOM
2067
C
GLU
B
331
85.742
31.247
19.523
1.00
20.00
6


ATOM
2068
O
GLU
B
331
86.952
31.264
19.761
1.00
20.00
8


ATOM
2069
N
GLY
B
332
85.257
31.137
18.292
1.00
20.00
7


ATOM
2070
CA
GLY
B
332
86.145
31.159
17.140
1.00
20.00
6


ATOM
2071
C
GLY
B
332
87.036
30.014
16.721
1.00
20.00
6


ATOM
2072
O
GLY
B
332
86.881
28.863
17.142
1.00
20.00
8


ATOM
2073
N
TYR
B
333
88.002
30.366
15.875
1.00
20.00
7


ATOM
2074
CA
TYR
B
333
88.939
29.413
15.307
1.00
20.00
6


ATOM
2075
CB
TYR
B
333
89.625
30.053
14.093
1.00
20.00
6


ATOM
2076
CG
TYR
B
333
88.724
30.031
12.877
1.00
20.00
6


ATOM
2077
CD1
TYR
B
333
88.774
28.966
11.974
1.00
20.00
6


ATOM
2078
CE1
TYR
B
333
87.872
28.869
10.919
1.00
20.00
6


ATOM
2079
CD2
TYR
B
333
87.747
31.011
12.686
1.00
20.00
6


ATOM
2080
CE2
TYR
B
333
86.831
30.923
11.624
1.00
20.00
6


ATOM
2081
CZ
TYR
B
333
86.903
29.845
10.751
1.00
20.00
6


ATOM
2082
OH
TYR
B
333
86.001
29.719
9.724
1.00
20.00
8


ATOM
2083
C
TYR
B
333
89.958
28.800
16.252
1.00
20.00
6


ATOM
2084
O
TYR
B
333
90.473
27.721
15.971
1.00
20.00
8


ATOM
2085
N
GLY
B
334
90.242
29.469
17.369
1.00
20.00
7


ATOM
2086
CA
GLY
B
334
91.193
28.921
18.327
1.00
20.00
6


ATOM
2087
C
GLY
B
334
90.803
27.504
18.741
1.00
20.00
6


ATOM
2088
O
GLY
B
334
91.577
26.564
18.558
1.00
20.00
8


ATOM
2089
N
PRO
B
335
89.603
27.320
19.309
1.00
20.00
7


ATOM
2090
CD
PRO
B
335
88.703
28.372
19.814
1.00
20.00
6


ATOM
2091
CA
PRO
B
335
89.145
25.991
19.731
1.00
20.00
6


ATOM
2092
CB
PRO
B
335
87.759
26.275
20.303
1.00
20.00
6


ATOM
2093
CG
PRO
B
335
87.925
27.644
20.883
1.00
20.00
6


ATOM
2094
C
PRO
B
335
89.104
24.986
18.573
1.00
20.00
6


ATOM
2095
O
PRO
B
335
89.406
23.808
18.756
1.00
20.00
8


ATOM
2096
N
LEU
B
336
88.727
25.450
17.382
1.00
20.00
7


ATOM
2097
CA
LEU
B
336
88.666
24.567
16.219
1.00
20.00
6


ATOM
2098
CB
LEU
B
336
88.031
25.292
15.023
1.00
20.00
6


ATOM
2099
CG
LEU
B
336
88.051
24.581
13.663
1.00
20.00
6


ATOM
2100
CD1
LEU
B
336
87.486
23.177
13.787
1.00
20.00
6


ATOM
2101
CD2
LEU
B
336
87.239
25.399
12.653
1.00
20.00
6


ATOM
2102
C
LEU
B
336
90.060
24.068
15.839
1.00
20.00
6


ATOM
2103
O
LEU
B
336
90.274
22.870
15.665
1.00
20.00
8


ATOM
2104
N
LYS
B
337
91.011
24.986
15.717
1.00
20.00
7


ATOM
2105
CA
LYS
B
337
92.370
24.597
15.360
1.00
20.00
6


ATOM
2106
CB
LYS
B
337
93.198
25.848
15.046
1.00
20.00
6


ATOM
2107
CG
LYS
B
337
92.678
26.560
13.801
1.00
20.00
6


ATOM
2108
CD
LYS
B
337
93.111
28.014
13.717
1.00
20.00
6


ATOM
2109
CE
LYS
B
337
94.561
28.167
13.314
1.00
20.00
6


ATOM
2110
NZ
LYS
B
337
94.882
29.611
13.122
1.00
20.00
7


ATOM
2111
C
LYS
B
337
93.020
23.764
16.467
1.00
20.00
6


ATOM
2112
O
LYS
B
337
93.965
23.015
16.215
1.00
20.00
8


ATOM
2113
N
ALA
B
338
92.495
23.866
17.684
1.00
20.00
7


ATOM
2114
CA
ALA
B
338
93.056
23.105
18.799
1.00
20.00
6


ATOM
2115
CB
ALA
B
338
92.873
23.877
20.105
1.00
20.00
6


ATOM
2116
C
ALA
B
338
92.441
21.718
18.929
1.00
20.00
6


ATOM
2117
O
ALA
B
338
92.805
20.955
19.820
1.00
20.00
8


ATOM
2118
N
HIS
B
339
91.513
21.375
18.043
1.00
20.00
7


ATOM
2119
CA
HIS
B
339
90.886
20.061
18.129
1.00
20.00
6


ATOM
2120
CB
HIS
B
339
89.786
19.919
17.074
1.00
20.00
6


ATOM
2121
CG
HIS
B
339
88.999
18.654
17.199
1.00
20.00
6


ATOM
2122
CD2
HIS
B
339
87.797
18.406
17.774
1.00
20.00
6


ATOM
2123
ND1
HIS
B
339
89.462
17.440
16.737
1.00
20.00
7


ATOM
2124
CE1
HIS
B
339
88.578
16.498
17.021
1.00
20.00
6


ATOM
2125
NE2
HIS
B
339
87.559
17.057
17.650
1.00
20.00
7


ATOM
2126
C
HIS
B
339
91.928
18.952
17.970
1.00
20.00
6


ATOM
2127
O
HIS
B
339
92.863
19.077
17.186
1.00
20.00
8


ATOM
2128
N
PRO
B
340
91.780
17.854
18.731
1.00
20.00
7


ATOM
2129
CD
PRO
B
340
90.747
17.655
19.765
1.00
20.00
6


ATOM
2130
CA
PRO
B
340
92.700
16.711
18.694
1.00
20.00
6


ATOM
2131
CB
PRO
B
340
91.966
15.665
19.521
1.00
20.00
6


ATOM
2132
CG
PRO
B
340
91.310
16.505
20.579
1.00
20.00
6


ATOM
2133
C
PRO
B
340
93.072
16.198
17.301
1.00
20.00
6


ATOM
2134
O
PRO
B
340
94.193
15.748
17.080
1.00
20.00
8


ATOM
2135
N
PHE
B
341
92.139
16.270
16.362
1.00
20.00
7


ATOM
2136
CA
PHE
B
341
92.407
15.797
15.011
1.00
20.00
6


ATOM
2137
CB
PHE
B
341
91.152
15.943
14.142
1.00
20.00
6


ATOM
2138
CG
PHE
B
341
91.317
15.424
12.738
1.00
20.00
6


ATOM
2139
CD1
PHE
B
341
91.596
14.080
12.507
1.00
20.00
6


ATOM
2140
CD2
PHE
B
341
91.182
16.277
11.647
1.00
20.00
6


ATOM
2141
CE1
PHE
B
341
91.738
13.592
11.207
1.00
20.00
6


ATOM
2142
CE2
PHE
B
341
91.320
15.803
10.345
1.00
20.00
6


ATOM
2143
CZ
PHE
B
341
91.599
14.457
10.123
1.00
20.00
6


ATOM
2144
C
PHE
B
341
93.571
16.550
14.362
1.00
20.00
6


ATOM
2145
O
PHE
B
341
94.268
16.002
13.514
1.00
20.00
8


ATOM
2146
N
PHE
B
342
93.777
17.800
14.765
1.00
20.00
7


ATOM
2147
CA
PHE
B
342
94.842
18.630
14.202
1.00
20.00
6


ATOM
2148
CB
PHE
B
342
94.336
20.058
13.975
1.00
20.00
6


ATOM
2149
CG
PHE
B
342
93.124
20.152
13.096
1.00
20.00
6


ATOM
2150
CD1
PHE
B
342
93.166
19.729
11.777
1.00
20.00
6


ATOM
2151
CD2
PHE
B
342
91.954
20.734
13.575
1.00
20.00
6


ATOM
2152
CE1
PHE
B
342
92.058
19.888
10.936
1.00
20.00
6


ATOM
2153
CE2
PHE
B
342
90.843
20.898
12.742
1.00
20.00
6


ATOM
2154
CZ
PHE
B
342
90.898
20.475
11.423
1.00
20.00
6


ATOM
2155
C
PHE
B
342
96.077
18.718
15.101
1.00
20.00
6


ATOM
2156
O
PHE
B
342
96.932
19.584
14.902
1.00
20.00
8


ATOM
2157
N
GLU
B
343
96.173
17.829
16.083
1.00
20.00
7


ATOM
2158
CA
GLU
B
343
97.293
17.857
17.022
1.00
20.00
6


ATOM
2159
CB
GLU
B
343
97.330
16.564
17.841
1.00
20.00
6


ATOM
2160
CG
GLU
B
343
98.475
16.525
18.839
1.00
20.00
6


ATOM
2161
CD
GLU
B
343
98.372
15.365
19.813
1.00
20.00
6


ATOM
2162
OE1
GLU
B
343
98.290
14.201
19.359
1.00
20.00
8


ATOM
2163
OE2
GLU
B
343
98.379
15.622
21.036
1.00
20.00
8


ATOM
2164
C
GLU
B
343
98.683
18.113
16.430
1.00
20.00
6


ATOM
2165
O
GLU
B
343
99.419
18.969
16.925
1.00
20.00
8


ATOM
2166
N
SER
B
344
99.047
17.382
15.383
1.00
20.00
7


ATOM
2167
CA
SER
B
344
100.370
17.549
14.781
1.00
20.00
6


ATOM
2168
CB
SER
B
344
100.848
16.219
14.192
1.00
20.00
6


ATOM
2169
OG
SER
B
344
100.072
15.856
13.065
1.00
20.00
8


ATOM
2170
C
SER
B
344
100.467
18.629
13.702
1.00
20.00
6


ATOM
2171
O
SER
B
344
101.485
18.732
13.025
1.00
20.00
8


ATOM
2172
N
VAL
B
345
99.423
19.435
13.544
1.00
20.00
7


ATOM
2173
CA
VAL
B
345
99.430
20.486
12.527
1.00
20.00
6


ATOM
2174
CB
VAL
B
345
97.985
20.843
12.075
1.00
20.00
6


ATOM
2175
CG1
VAL
B
345
98.015
22.042
11.120
1.00
20.00
6


ATOM
2176
CG2
VAL
B
345
97.335
19.646
11.400
1.00
20.00
6


ATOM
2177
C
VAL
B
345
100.096
21.785
12.980
1.00
20.00
6


ATOM
2178
O
VAL
B
345
99.844
22.275
14.085
1.00
20.00
8


ATOM
2179
N
THR
B
346
100.951
22.335
12.122
1.00
20.00
7


ATOM
2180
CA
THR
B
346
101.602
23.610
12.397
1.00
20.00
6


ATOM
2181
CB
THR
B
346
103.096
23.593
11.982
1.00
20.00
6


ATOM
2182
OG1
THR
B
346
103.816
22.688
12.831
1.00
20.00
8


ATOM
2183
CG2
THR
B
346
103.707
24.983
12.115
1.00
20.00
6


ATOM
2184
C
THR
B
346
100.810
24.573
11.510
1.00
20.00
6


ATOM
2185
O
THR
B
346
100.950
24.565
10.285
1.00
20.00
8


ATOM
2186
N
TRP
B
347
99.966
25.385
12.138
1.00
20.00
7


ATOM
2187
CA
TRP
B
347
99.089
26.306
11.425
1.00
20.00
6


ATOM
2188
CB
TRP
B
347
97.941
26.727
12.344
1.00
20.00
6


ATOM
2189
CG
TRP
B
347
97.088
25.594
12.818
1.00
20.00
6


ATOM
2190
CD2
TRP
B
347
95.924
25.071
12.165
1.00
20.00
6


ATOM
2191
CE2
TRP
B
347
95.436
24.008
12.963
1.00
20.00
6


ATOM
2192
CE3
TRP
B
347
95.247
25.397
10.983
1.00
20.00
6


ATOM
2193
CD1
TRP
B
347
97.259
24.848
13.953
1.00
20.00
6


ATOM
2194
NE1
TRP
B
347
96.269
23.893
14.048
1.00
20.00
7


ATOM
2195
CZ2
TRP
B
347
94.300
23.270
12.616
1.00
20.00
6


ATOM
2196
CZ3
TRP
B
347
94.113
24.661
10.636
1.00
20.00
6


ATOM
2197
CH2
TRP
B
347
93.654
23.610
11.452
1.00
20.00
6


ATOM
2198
C
TRP
B
347
99.679
27.563
10.800
1.00
20.00
6


ATOM
2199
O
TRP
B
347
99.101
28.114
9.867
1.00
20.00
8


ATOM
2200
N
ALA
B
348
100.820
28.016
11.308
1.00
20.00
7


ATOM
2201
CA
ALA
B
348
101.439
29.247
10.822
1.00
20.00
6


ATOM
2202
CB
ALA
B
348
102.582
29.656
11.761
1.00
20.00
6


ATOM
2203
C
ALA
B
348
101.933
29.277
9.381
1.00
20.00
6


ATOM
2204
O
ALA
B
348
101.874
30.323
8.738
1.00
20.00
8


ATOM
2205
N
ASN
B
349
102.411
28.152
8.860
1.00
20.00
7


ATOM
2206
CA
ASN
B
349
102.940
28.153
7.500
1.00
20.00
6


ATOM
2207
CB
ASN
B
349
104.466
28.205
7.569
1.00
20.00
6


ATOM
2208
CG
ASN
B
349
105.058
26.929
8.138
1.00
20.00
6


ATOM
2209
OD1
ASN
B
349
104.445
26.282
8.984
1.00
20.00
8


ATOM
2210
ND2
ASN
B
349
106.251
26.563
7.678
1.00
20.00
7


ATOM
2211
C
ASN
B
349
102.522
26.966
6.634
1.00
20.00
6


ATOM
2212
O
ASN
B
349
103.353
26.371
5.944
1.00
20.00
8


ATOM
2213
N
LEU
B
350
101.242
26.628
6.643
1.00
20.00
7


ATOM
2214
CA
LEU
B
350
100.776
25.500
5.846
1.00
20.00
6


ATOM
2215
CB
LEU
B
350
99.257
25.355
5.973
1.00
20.00
6


ATOM
2216
CG
LEU
B
350
98.734
24.848
7.316
1.00
20.00
6


ATOM
2217
CD1
LEU
B
350
97.244
25.127
7.418
1.00
20.00
6


ATOM
2218
CD2
LEU
B
350
99.030
23.357
7.444
1.00
20.00
6


ATOM
2219
C
LEU
B
350
101.147
25.574
4.365
1.00
20.00
6


ATOM
2220
O
LEU
B
350
101.557
24.575
3.775
1.00
20.00
8


ATOM
2221
N
HIS
B
351
101.006
26.744
3.752
1.00
20.00
7


ATOM
2222
CA
HIS
B
351
101.305
26.829
2.329
1.00
20.00
6


ATOM
2223
CB
HIS
B
351
100.651
28.087
1.721
1.00
20.00
6


ATOM
2224
CG
HIS
B
351
101.553
29.274
1.618
1.00
20.00
6


ATOM
2225
CD2
HIS
B
351
102.001
30.143
2.556
1.00
20.00
6


ATOM
2226
ND1
HIS
B
351
102.072
29.706
0.416
1.00
20.00
7


ATOM
2227
CE1
HIS
B
351
102.798
30.792
0.618
1.00
20.00
6


ATOM
2228
NE2
HIS
B
351
102.772
31.079
1.907
1.00
20.00
7


ATOM
2229
C
HIS
B
351
102.797
26.731
1.999
1.00
20.00
6


ATOM
2230
O
HIS
B
351
103.176
26.669
0.832
1.00
20.00
8


ATOM
2231
N
GLN
B
352
103.634
26.685
3.033
1.00
20.00
7


ATOM
2232
CA
GLN
B
352
105.081
26.554
2.851
1.00
20.00
6


ATOM
2233
CB
GLN
B
352
105.841
27.458
3.819
1.00
20.00
6


ATOM
2234
CG
GLN
B
352
106.395
28.705
3.166
1.00
20.00
6


ATOM
2235
CD
GLN
B
352
105.930
29.966
3.854
1.00
20.00
6


ATOM
2236
OE1
GLN
B
352
106.134
30.139
5.053
1.00
20.00
8


ATOM
2237
NE2
GLN
B
352
105.299
30.854
3.096
1.00
20.00
7


ATOM
2238
C
GLN
B
352
105.478
25.099
3.088
1.00
20.00
6


ATOM
2239
O
GLN
B
352
106.632
24.715
2.895
1.00
20.00
8


ATOM
2240
N
GLN
B
353
104.514
24.295
3.522
1.00
20.00
7


ATOM
2241
CA
GLN
B
353
104.761
22.888
3.777
1.00
20.00
6


ATOM
2242
CB
GLN
B
353
103.849
22.395
4.900
1.00
20.00
6


ATOM
2243
CG
GLN
B
353
104.122
23.050
6.240
1.00
20.00
6


ATOM
2244
CD
GLN
B
353
103.075
22.711
7.281
1.00
20.00
6


ATOM
2245
OE1
GLN
B
353
102.627
21.571
7.377
1.00
20.00
8


ATOM
2246
NE2
GLN
B
353
102.690
23.700
8.076
1.00
20.00
7


ATOM
2247
C
GLN
B
353
104.507
22.079
2.510
1.00
20.00
6


ATOM
2248
O
GLN
B
353
103.732
22.490
1.641
1.00
20.00
8


ATOM
2249
N
THR
B
354
105.172
20.937
2.401
1.00
20.00
7


ATOM
2250
CA
THR
B
354
104.998
20.071
1.244
1.00
20.00
6


ATOM
2251
CB
THR
B
354
106.240
19.173
1.029
1.00
20.00
6


ATOM
2252
OG1
THR
B
354
107.390
19.999
0.790
1.00
20.00
8


ATOM
2253
CG2
THR
B
354
106.033
18.243
−0.166
1.00
20.00
6


ATOM
2254
C
THR
B
354
103.777
19.197
1.501
1.00
20.00
6


ATOM
2255
O
THR
B
354
103.745
18.426
2.454
1.00
20.00
8


ATOM
2256
N
PRO
B
355
102.741
19.319
0.658
1.00
20.00
7


ATOM
2257
CD
PRO
B
355
102.547
20.275
−0.444
1.00
20.00
6


ATOM
2258
CA
PRO
B
355
101.540
18.505
0.859
1.00
20.00
6


ATOM
2259
CB
PRO
B
355
100.616
18.967
−0.266
1.00
20.00
6


ATOM
2260
CG
PRO
B
355
101.039
20.387
−0.490
1.00
20.00
6


ATOM
2261
C
PRO
B
355
101.835
17.011
0.766
1.00
20.00
6


ATOM
2262
O
PRO
B
355
102.631
16.577
−0.065
1.00
20.00
8


ATOM
2263
N
PRO
B
356
101.198
16.204
1.625
1.00
20.00
7


ATOM
2264
CD
PRO
B
356
100.128
16.522
2.587
1.00
20.00
6


ATOM
2265
CA
PRO
B
356
101.438
14.761
1.573
1.00
20.00
6


ATOM
2266
CB
PRO
B
356
100.593
14.235
2.729
1.00
20.00
6


ATOM
2267
CG
PRO
B
356
99.429
15.188
2.737
1.00
20.00
6


ATOM
2268
C
PRO
B
356
100.960
14.244
0.222
1.00
20.00
6


ATOM
2269
O
PRO
B
356
100.005
14.779
−0.346
1.00
20.00
8


ATOM
2270
N
ALA
B
357
101.629
13.221
−0.300
1.00
20.00
7


ATOM
2271
CA
ALA
B
357
101.247
12.660
−1.588
1.00
20.00
6


ATOM
2272
CB
ALA
B
357
102.352
11.750
−2.118
1.00
20.00
6


ATOM
2273
C
ALA
B
357
99.948
11.883
−1.427
1.00
20.00
6


ATOM
2274
O
ALA
B
357
99.808
11.074
−0.506
1.00
20.00
8


ATOM
2275
N
LEU
B
358
99.000
12.134
−2.323
1.00
20.00
7


ATOM
2276
CA
LEU
B
358
97.709
11.460
−2.278
1.00
20.00
6


ATOM
2277
CB
LEU
B
358
96.729
12.166
−3.217
1.00
20.00
6


ATOM
2278
CG
LEU
B
358
96.368
13.582
−2.766
1.00
20.00
6


ATOM
2279
CD1
LEU
B
358
95.513
14.262
−3.813
1.00
20.00
6


ATOM
2280
CD2
LEU
B
358
95.636
13.516
−1.430
1.00
20.00
6


ATOM
2281
C
LEU
B
358
97.813
9.976
−2.633
1.00
20.00
6


ATOM
2282
O
LEU
B
358
97.918
9.614
−3.806
1.00
20.00
8


ATOM
2283
N
THR
B
359
97.776
9.134
−1.600
1.00
20.00
7


ATOM
2284
CA
THR
B
359
97.867
7.678
−1.735
1.00
20.00
6


ATOM
2285
CB
THR
B
359
96.513
7.046
−2.149
1.00
20.00
6


ATOM
2286
OG1
THR
B
359
96.111
7.555
−3.427
1.00
20.00
8


ATOM
2287
CG2
THR
B
359
95.439
7.355
−1.112
1.00
20.00
6


ATOM
2288
C
THR
B
359
98.933
7.238
−2.736
1.00
20.00
6


ATOM
2289
O
THR
B
359
99.903
7.998
−2.945
1.00
20.00
8


ATOM
2290
OXT
THR
B
359
98.802
6.121
−3.280
1.00
20.00
8


TER













ATOM
2291
OH2
TIP
S
1
42.566
19.118
34.302
1.00
15.09
S


ATOM
2292
OH2
TIP
S
2
41.052
32.378
19.857
1.00
15.82
S


ATOM
2293
OH2
TIP
S
3
37.014
33.030
17.747
1.00
16.95
S


ATOM
2294
OH2
TIP
S
5
45.353
24.370
18.152
1.00
16.85
S


ATOM
2295
OH2
TIP
S
6
31.896
13.930
33.235
1.00
20.42
S


ATOM
2296
OH2
TIP
S
7
50.351
22.781
28.249
1.00
21.14
S


ATOM
2297
OH2
TIP
S
8
45.246
−0.589
−0.734
1.00
17.74
S


ATOM
2298
OH2
TIP
S
11
46.249
−0.348
−8.523
1.00
21.32
S


ATOM
2299
OH2
TIP
S
14
45.756
11.148
29.680
1.00
21.94
S


ATOM
2300
OH2
TIP
S
15
44.273
13.157
34.592
1.00
15.61
S


ATOM
2301
OH2
TIP
S
17
53.598
3.722
−1.720
1.00
21.45
S


ATOM
2302
OH2
TIP
S
18
46.049
13.087
31.565
1.00
20.35
S 


ATOM
2303
OH2
TIP
S
19
53.422
22.401
−3.280
1.00
23.26
S


ATOM
2304
OH2
TIP
S
20
34.587
7.922
5.383
1.00
22.58
S


ATOM
2305
OH2
TIP
S
21
45.053
27.379
19.376
1.00
29.60
S 


ATOM
2306
OH2
TIP
S
23
28.899
36.416
28.633
1.00
31.68
S


ATOM
2307
OH2
TIP
S
24
35.531
11.645
−8.219
1.00
23.45
S


ATOM
2308
OH2
TIP
S
25
47.364
28.787
19.612
1.00
23.03
S


ATOM
2309
OH2
TIP
S
27
48.859
21.588
12.634
1.00
23.76
S


ATOM
2310
OH2
TIP
S
29
48.805
8.920
23.626
1.00
22.23
S


ATOM
2311
OH2
TIP
S
31
48.619
7.247
10.112
1.00
21.32
S


ATOM
2312
OH2
TIP
S
34
44.824
28.720
15.621
1.00
25.27
S


ATOM
2313
OH2
TIP
S
35
26.030
12.634
13.407
1.00
21.61
S


ATOM
2314
OH2
TIP
S
36
50.462
19.810
40.066
1.00
25.45
S


ATOM
2315
OH2
TIP
S
37
39.631
23.510
−0.239
1.00
30.88
S


ATOM
2316
OH2
TIP
S
40
44.734
42.655
10.346
1.00
30.84
S


ATOM
2317
OH2
TIP
S
41
54.653
3.902
1.503
1.00
27.14
S


ATOM
2318
OH2
TIP
S
45
45.693
21.923
39.754
1.00
28.30
S


ATOM
2319
OH2
TIP
S
47
47.820
16.413
7.805
1.00
25.73
S


ATOM
2320
OH2
TIP
S
48
50.292
31.412
29.642
1.00
32.79
S


ATOM
2321
OH2
TIP
S
49
26.056
16.646
34.827
1.00
29.80
S


ATOM
2322
OH2
TIP
S
52
31.714
10.996
31.855
1.00
29.15
S


ATOM
2323
OH2
TIP
S
53
46.108
23.843
−4.299
1.00
24.21
S


ATOM
2324
OH2
TIP
S
54
37.645
11.206
34.448
1.00
28.56
S


ATOM
2325
OH2
TIP
S
55
26.371
28.513
12.142
1.00
32.08
S


ATOM
2326
OH2
TIP
S
58
33.564
19.700
3.483
1.00
28.28
S


ATOM
2327
OH2
TIP
S
64
48.295
−0.632
14.280
1.00
32.13
S


ATOM
2328
OH2
TIP
S
65
40.064
26.036
34.324
1.00
24.17
S


ATOM
2329
OH2
TIP
S
66
29.570
3.958
14.729
1.00
28.94
S


ATOM
2330
OH2
TIP
S
72
60.085
11.604
6.814
1.00
38.35
S


ATOM
2331
OH2
TIP
S
73
39.203
44.403
18.686
1.00
26.61
S


ATOM
2332
OH2
TIP
S
76
47.312
12.366
27.366
1.00
28.51
S


ATOM
2333
OH2
TIP
S
80
43.862
33.771
33.329
1.00
28.82
S


ATOM
2334
OH2
TIP
S
81
57.890
13.106
2.128
1.00
40.62
S


ATOM
2335
OH2
TIP
S
82
41.663
34.381
32.043
1.00
19.35
S


ATOM
2336
OH2
TIP
S
85
50.974
40.331
19.200
1.00
21.14
S


ATOM
2337
OH2
TIP
S
88
47.925
−0.832
−6.556
1.00
24.11
S


ATOM
2338
OH2
TIP
S
90
27.231
28.336
33.481
1.00
27.64
S


ATOM
2339
OH2
TIP
S
91
43.651
−7.101
−7.995
1.00
24.33
S


ATOM
2340
OH2
TIP
S
92
49.325
4.387
19.370
1.00
28.02
S


ATOM
2341
OH2
TIP
S
93
46.231
11.549
33.898
1.00
29.40
S


ATOM
2342
OH2
TIP
S
94
63.889
24.831
1.168
1.00
26.53
S


ATOM
2343
OH2
TIP
S
96
56.396
4.952
−6.749
1.00
28.00
S


ATOM
2344
OH2
TIP
S
98
35.510
27.986
11.558
1.00
29.24
S


ATOM
2345
OH2
TIP
S
100
49.942
24.366
30.265
1.00
31.61
S


ATOM
2346
OH2
TIP
S
101
56.121
7.113
−8.298
1.00
31.57
S


ATOM
2347
OH2
TIP
S
102
58.318
19.957
−8.378
1.00
26.95
S


ATOM
2348
OH2
TIP
S
103
49.647
22.446
39.624
1.00
40.57
S


ATOM
2349
OH2
TIP
S
104
45.359
7.052
13.052
1.00
26.27
S


ATOM
2350
OH2
TIP
S
105
37.150
32.340
32.346
1.00
34.45
S


ATOM
2351
OH2
TIP
S
107
43.465
40.457
8.240
1.00
40.48
S


ATOM
2352
OH2
TIP
S
119
36.644
8.257
13.418
1.00
30.70
S


ATOM
2353
OH2
TIP
S
123
41.912
−8.974
−8.264
1.00
26.08
S


ATOM
2354
OH2
TIP
S
124
62.424
15.800
−7.411
1.00
24.08
S


ATOM
2355
OH2
TIP
S
126
37.266
18.656
−9.097
1.00
28.99
S


ATOM
2356
OH2
TIP
S
127
43.129
26.845
14.606
1.00
25.19
S


ATOM
2357
OH2
TIP
S
128
36.339
32.639
29.802
1.00
29.25
S


ATOM
2358
OH2
TIP
S
130
54.051
14.561
26.498
1.00
33.93
S


ATOM
2359
OH2
TIP
S
131
41.805
−4.242
5.492
1.00
33.72
S


ATOM
2360
OH2
TIP
S
133
38.873
25.163
36.697
1.00
30.69
S


ATOM
2361
OH2
TIP
S
134
28.777
8.553
25.307
1.00
31.43
S


ATOM
2362
OH2
TIP
S
135
53.672
10.546
−12.803
1.00
33.45
S


ATOM
2363
OH2
TIP
S
136
59.892
15.434
11.467
1.00
31.39
S


ATOM
2364
OH2
TIP
S
137
31.040
12.361
35.470
1.00
34.07
S


ATOM
2365
OH2
TIP
S
139
33.489
14.292
−0.598
1.00
40.68
S


ATOM
2366
OH2
TIP
S
140
46.918
8.748
11.662
1.00
29.23
S


ATOM
2367
OH2
TIP
S
141
46.297
−7.287
−9.196
1.00
42.20
S


ATOM
2368
OH2
TIP
S
142
58.193
6.715
−4.685
1.00
35.48
S


ATOM
2369
OH2
TIP
S
143
44.598
4.435
12.503
1.00
27.68
S


ATOM
2370
OH2
TIP
S
144
27.003
5.999
12.450
1.00
36.30
S


ATOM
2371
OH2
TIP
S
145
43.676
32.852
35.735
1.00
35.70
S


ATOM
2372
OH2
TIP
S
146
35.783
18.628
36.452
1.00
34.62
S


ATOM
2373
OH2
TIP
S
147
25.402
4.058
20.638
1.00
45.03
S


ATOM
2374
OH2
TIP
S
148
45.839
35.853
33.724
1.00
35.47
S


ATOM
2375
OH2
TIP
S
149
22.176
18.976
16.752
1.00
31.87
S


ATOM
2376
OH2
TIP
S
150
43.986
33.179
10.162
1.00
37.70
S


ATOM
2377
OH2
TIP
S
151
50.653
20.347
42.428
1.00
35.80
S


ATOM
2378
OH2
TIP
S
152
47.843
24.314
9.506
1.00
31.05
S


ATOM
2379
OH2
TIP
S
153
44.693
5.273
−14.175
1.00
29.90
S


ATOM
2380
OH2
TIP
S
155
26.560
36.851
31.684
1.00
49.29
S


ATOM
2381
OH2
TIP
S
156
46.867
8.019
−12.951
1.00
29.21
S


ATOM
2382
OH2
TIP
S
157
30.432
28.741
12.438
1.00
37.76
S


ATOM
2383
OH2
TIP
S
158
41.004
20.553
6.423
1.00
39.53
S


ATOM
2384
OH2
TIP
S
159
49.258
20.069
29.294
1.00
33.97
S


ATOM
2385
OH2
TIP
S
160
48.082
28.459
16.489
1.00
33.10
S


ATOM
2386
OH2
TIP
S
161
47.448
18.625
27.683
1.00
34.87
S


ATOM
2387
OH2
TIP
S
162
19.687
20.632
23.411
1.00
35.01
S


ATOM
2388
OH2
TIP
S
163
32.402
−1.266
22.443
1.00
37.26
S


ATOM
2389
OH2
TIP
S
164
39.475
33.468
33.237
1.00
35.34
S


ATOM
2390
OH2
TIP
S
165
44.277
18.950
5.162
1.00
45.14
S


ATOM
2391
OH2
TIP
S
166
34.797
30.523
10.736
1.00
47.55
S


ATOM
2392
OH2
TIP
S
167
46.541
3.526
−14.949
1.00
26.54
S


ATOM
2393
OH2
TIP
S
168
36.333
16.371
1.539
1.00
38.68
S


ATOM
2394
OH2
TIP
S
169
46.761
38.936
27.403
1.00
34.66
S


ATOM
2395
OH2
TIP
S
170
24.163
13.264
11.375
1.00
41.23
S


ATOM
2396
OH2
TIP
S
171
48.459
15.018
31.951
1.00
38.11
S


ATOM
2397
OH2
TIP
S
172
34.261
23.193
40.004
1.00
48.96
S


ATOM
2398
OH2
TIP
S
173
45.924
−0.026
13.224
1.00
39.55
S


ATOM
2399
OH2
TIP
S
175
41.384
37.389
32.543
1.00
40.74
S


ATOM
2400
OH2
TIP
S
177
49.394
35.312
27.150
1.00
44.33
S


ATOM
2401
OH2
TIP
S
178
29.066
29.942
34.359
1.00
41.46
S


ATOM
2402
OH2
TIP
S
180
49.354
19.467
7.273
1.00
34.56
S


ATOM
2403
OH2
TIP
S
181
25.298
17.029
31.863
1.00
47.74
S


ATOM
2404
OH2
TIP
S
182
37.071
25.027
4.669
1.00
43.87
S


ATOM
2405
OH2
TIP
S
183
22.581
7.487
18.691
1.00
41.75
S


ATOM
2406
OH2
TIP
S
184
32.269
7.011
−1.891
1.00
48.84
S


ATOM
2407
OH2
TIP
S
185
48.234
0.494
6.833
1.00
48.16
S


ATOM
2408
OH2
TIP
S
187
20.008
14.658
19.211
1.00
45.27
S


ATOM
2409
OH2
TIP
S
188
49.341
22.698
42.272
1.00
42.20
S


ATOM
2410
OH2
TIP
S
190
61.292
18.260
−8.097
1.00
45.21
S


ATOM
2411
OH2
TIP
S
191
28.152
10.606
2.819
1.00
40.38
S


ATOM
2412
OH2
TIP
S
192
25.626
12.619
23.191
1.00
34.27
S


ATOM
2413
OH2
TIP
S
193
59.876
11.603
1.216
1.00
46.54
S


ATOM
2414
OH2
TIP
S
194
57.592
21.183
−10.646
1.00
45.82
S


ATOM
2415
OH2
TIP
S
195
31.509
36.649
21.499
1.00
38.73
S


ATOM
2416
OH2
TIP
S
197
50.270
−1.543
−6.136
1.00
42.66
S


ATOM
2417
OH2
TIP
S
198
24.467
8.729
13.088
1.00
42.78
S


ATOM
2418
OH2
TIP
S
199
38.098
8.699
25.759
1.00
32.80
S


ATOM
2419
OH2
TIP
S
200
57.831
11.358
−13.255
1.00
45.31
S


ATOM
2420
OH2
TIP
S
201
23.888
22.328
30.524
1.00
37.12
S


ATOM
2421
OH2
TIP
S
202
47.691
26.068
37.666
1.00
37.92
S


ATOM
2422
OH2
TIP
S
203
38.653
7.070
29.307
1.00
50.54
S


ATOM
2423
OH2
TIP
S
206
44.424
27.583
2.092
1.00
53.50
S


ATOM
2424
OH2
TIP
S
212
22.258
2.296
17.948
1.00
47.38
S


ATOM
2425
OH2
TIP
S
214
19.843
17.943
23.303
1.00
30.36
S


ATOM
2426
OH2
TIP
S
216
27.647
11.344
24.681
1.00
31.32
S


ATOM
2427
OH2
TIP
S
217
37.953
7.817
−9.284
1.00
45.97
S


ATOM
2428
OH2
TIP
S
218
33.845
34.040
12.124
1.00
38.11
S


ATOM
2429
OH2
TIP
S
219
58.484
15.269
13.717
1.00
38.26
S


ATOM
2430
OH2
TIP
S
220
48.526
40.920
26.583
1.00
35.23
S


ATOM
2431
OH2
TIP
S
222
52.094
21.184
38.122
1.00
29.86
S


ATOM
2432
OH2
TIP
S
223
36.889
5.881
3.281
1.00
37.63
S


ATOM
2433
OH2
TIP
S
224
47.642
−1.401
−10.684
1.00
34.89
S


ATOM
2434
OH2
TIP
S
226
47.284
2.916
19.133
1.00
34.10
S


ATOM
2435
OH2
TIP
S
227
42.468
4.463
−15.039
1.00
37.98
S


ATOM
2436
OH2
TIP
S
228
19.169
22.832
21.831
1.00
41.57
S


ATOM
2437
OH2
TIP
S
231
57.592
12.689
14.880
1.00
50.22
S


ATOM
2438
OH2
TIP
S
232
27.102
9.176
5.655
1.00
40.57
S


ATOM
2439
OH2
TIP
S
233
58.618
9.072
−11.925
1.00
50.71
S


ATOM
2440
OH2
TIP
S
234
22.822
25.342
19.945
1.00
34.93
S


ATOM
2441
OH2
TIP
S
236
24.831
32.218
28.901
1.00
37.69
S


ATOM
2442
OH2
TIP
S
237
20.045
10.774
16.992
1.00
39.57
S


ATOM
2443
OH2
TIP
S
238
58.019
19.850
15.679
1.00
41.42
S


ATOM
2444
OH2
TIP
S
239
19.490
20.949
26.114
1.00
34.55
S


ATOM
2445
OH2
TIP
S
240
61.187
26.377
7.346
1.00
39.68
S


ATOM
2446
OH2
TIP
S
241
33.680
38.342
19.389
1.00
48.93
S


ATOM
2447
OH2
TIP
S
242
51.539
31.612
10.881
1.00
55.65
S


ATOM
2448
OH2
TIP
S
244
25.872
14.431
30.404
1.00
46.69
S


ATOM
2449
OH2
TIP
S
248
37.332
5.849
9.544
1.00
43.81
S


ATOM
2450
OH2
TIP
S
250
39.087
−1.293
−9.655
1.00
42.96
S


ATOM
2451
OH2
TIP
S
258
23.938
30.000
30.010
1.00
38.89
S


ATOM
2452
OH2
TIP
S
259
24.949
29.749
32.578
1.00
40.17
S


ATOM
2453
OH2
TIP
S
260
32.111
17.986
1.918
1.00
48.36
S


ATOM
2454
OH2
TIP
S
266
21.404
12.876
25.603
1.00
57.17
S


ATOM
2455
OH2
TIP
S
269
35.425
36.767
12.550
1.00
30.70
S


ATOM
2456
OH2
TIP
S
270
52.438
25.529
30.131
1.00
44.85
S


ATOM
2457
OH2
TIP
S
271
53.299
20.156
36.003
1.00
37.15
S


ATOM
2458
OH2
TIP
S
272
50.914
6.919
23.723
1.00
43.29
S


ATOM
2459
OH2
TIP
S
274
31.578
30.795
11.014
1.00
50.15
S


ATOM
2460
OH2
TIP
S
275
26.341
7.243
22.447
1.00
39.40
S


ATOM
2461
OH2
TIP
S
276
60.392
18.195
10.235
1.00
37.91
S


ATOM
2462
OH2
TIP
S
277
47.355
−9.081
−10.821
1.00
48.18
S


ATOM
2463
OH2
TIP
S
279
41.304
6.175
−16.647
1.00
38.12
S


ATOM
2464
OH2
TIP
S
282
33.299
21.620
37.881
1.00
46.29
S


ATOM
2465
OH2
TIP
S
283
56.469
26.112
−8.575
1.00
43.71
S


ATOM
2466
OH2
TIP
S
287
48.382
26.573
7.246
1.00
41.43
S


ATOM
2467
OH2
TIP
S
288
56.240
7.245
−11.331
1.00
41.79
S


ATOM
2468
OH2
TIP
S
290
49.060
14.978
28.166
1.00
37.03
S


ATOM
2469
OH2
TIP
S
291
37.095
44.270
26.442
1.00
45.08
S


ATOM
2470
OH2
TIP
S
292
47.814
−0.384
−13.299
1.00
48.60
S


ATOM
2471
OH2
TIP
S
297
58.081
2.784
−7.841
1.00
41.89
S


ATOM
2472
OH2
TIP
S
298
36.447
45.321
18.644
1.00
54.91
S


ATOM
2473
OH2
TIP
S
299
49.029
23.328
1.767
1.00
30.55
S


ATOM
2474
OH2
TIP
S
301
24.375
13.771
8.634
1.00
48.47
S


ATOM
2475
OH2
TIP
S
303
47.904
36.798
28.653
1.00
35.76
S


ATOM
2476
OH2
TIP
S
305
51.156
40.821
27.172
1.00
43.59
S


ATOM
2477
OH2
TIP
S
306
32.943
28.917
35.227
1.00
42.60
S


ATOM
2478
OH2
TIP
S
307
58.462
28.373
6.251
1.00
46.15
S


ATOM
2479
OH2
TIP
S
308
41.964
30.940
36.712
1.00
48.26
S


ATOM
2480
OH2
TIP
S
313
51.176
−1.922
−3.336
1.00
50.61
S


ATOM
2481
OH2
TIP
S
1001
21.319
36.868
23.805
1.00
36.97
S


ATOM
2482
OH2
TIP
S
1002
48.880
32.620
27.617
1.00
44.40
S


ATOM
2483
OH2
TIP
S
1003
61.880
19.473
11.767
1.00
45.49
S


ATOM
2484
OH2
TIP
S
1004
52.770
21.424
26.815
1.00
24.43
S


ATOM
2485
OH2
TIP
S
1005
35.373
29.094
36.197
1.00
35.97
S


ATOM
2486
OH2
TIP
S
1006
40.815
−6.636
4.389
1.00
43.15
S


ATOM
2487
OH2
TIP
S
1007
44.953
1.286
11.272
1.00
49.45
S


ATOM
2488
OH2
TIP
S
1010
21.004
16.168
27.009
1.00
48.51
S


ATOM
2489
OH2
TIP
S
1011
47.094
41.786
9.243
1.00
50.10
S


ATOM
2490
OH2
TIP
S
1012
32.479
2.978
14.158
1.00
49.47
S


ATOM
2491
O12
GLC
G
1
48.557
11.372
−12.279
1.00
40.72
G


ATOM
2492
C11
GLC
G
1
48.836
12.133
−11.097
1.00
38.05
G


ATOM
2493
C13
GLC
G
1
49.266
13.554
−11.476
1.00
38.09
G


ATOM
2494
O14
GLC
G
1
49.559
14.299
−10.292
1.00
33.99
G


ATOM
2495
C15
GLC
G
1
48.150
14.257
−12.257
1.00
37.32
G


ATOM
2496
O16
GLC
G
1
48.574
15.582
−12.604
1.00
36.74
G


ATOM
2497
O12
GLC
G
2
40.114
−6.634
−6.562
1.00
33.52
G


ATOM
2498
C11
GLC
G
2
38.967
−6.592
−7.404
1.00
31.05
G


ATOM
2499
C13
GLC
G
2
37.712
−6.417
−6.552
1.00
31.56
G


ATOM
2500
O14
GLC
G
2
36.554
−6.406
−7.389
1.00
30.70
G


ATOM
2501
C15
GLC
G
2
37.792
−5.109
−5.761
1.00
30.03
G


ATOM
2502
O16
GLC
G
2
36.609
−4.961
−4.975
1.00
29.66
G


ATOM
2503
O12
GLC
G
3
44.030
8.243
−13.470
1.00
37.90
G


ATOM
2504
C11
GLC
G
3
43.950
9.648
−13.690
1.00
38.47
G


ATOM
2505
C13
GLC
G
3
42.747
9.974
−14.579
1.00
39.52
G


ATOM
2506
O14
GLC
G
3
41.551
9.526
−13.942
1.00
39.39
G


ATOM
2507
C15
GLC
G
3
42.878
9.280
−15.934
1.00
41.43
G


ATOM
2508
O16
GLC
G
3
41.736
9.613
−16.731
1.00
40.78
G


ATOM
2509
O12
GLC
G
5
40.556
1.005
2.289
1.00
45.25
G


ATOM
2510
C11
GLC
G
5
40.966
2.332
1.960
1.00
40.56
G


ATOM
2511
C13
GLC
G
5
40.187
3.327
2.814
1.00
40.36
G


ATOM
2512
O14
GLC
G
5
38.791
3.169
2.572
1.00
40.71
G


ATOM
2513
C15
GLC
G
5
40.619
4.751
2.464
1.00
40.04
G


ATOM
2514
O16
GLC
G
5
39.885
5.681
3.256
1.00
36.89
G


ATOM
2515
O12
GLC
G
6
36.951
22.702
40.046
1.00
63.04
G


ATOM
2516
C11
GLC
G
6
37.592
21.583
39.422
1.00
62.46
G


ATOM
2517
C13
GLC
G
6
38.104
21.978
38.030
1.00
61.14
G


ATOM
2518
O14
GLC
G
6
39.034
23.054
38.168
1.00
61.72
G


ATOM
2519
C15
GLC
G
6
36.948
22.429
37.126
1.00
60.51
G


ATOM
2520
O16
GLC
G
6
35.992
21.372
36.960
1.00
58.61
G


ATOM
2521
O12
GLC
G
7
37.316
0.281
14.299
1.00
73.45
G


ATOM
2522
C11
GLC
G
7
37.655
−0.758
15.222
1.00
72.78
G


ATOM
2523
C13
GLC
G
7
36.592
−1.856
15.157
1.00
72.98
G


ATOM
2524
O14
GLC
G
7
35.320
−1.299
15.498
1.00
73.88
G


ATOM
2525
C15
GLC
G
7
36.924
−2.989
16.134
1.00
73.66
G


ATOM
2526
O16
GLC
G
7
36.972
−2.493
17.478
1.00
75.38
G


ATOM
2527
O12
GLC
G
8
51.921
21.898
5.908
1.00
62.51
G


ATOM
2528
C11
GLC
G
8
52.447
20.871
5.063
1.00
63.42
G


ATOM
2529
C13
GLC
G
8
51.476
20.597
3.908
1.00
64.28
G


ATOM
2530
O14
GLC
G
8
51.297
21.794
3.150
1.00
66.28
G


ATOM
2531
C15
GLC
G
8
50.121
20.137
4.448
1.00
64.49
G


ATOM
2532
O16
GLC
G
8
49.233
19.886
3.357
1.00
64.01
G


ATOM
2533
O12
GLC
G
10
36.044
37.499
29.523
1.00
56.89
G


ATOM
2534
C11
GLC
G
10
35.164
36.645
30.259
1.00
56.97
G


ATOM
2535
C13
GLC
G
10
33.849
36.489
29.494
1.00
56.11
G


ATOM
2536
O14
GLC
G
10
33.248
37.772
29.308
1.00
56.44
G


ATOM
2537
C15
GLC
G
10
32.900
35.580
30.277
1.00
55.84
G


ATOM
2538
O16
GLC
G
10
31.674
35.442
29.557
1.00
55.39
G


ATOM
2539
O3G
ATP
N
1
46.280
25.658
5.170
1.00
51.49
N


ATOM
2540
PG
ATP
N
1
46.464
25.053
3.691
1.00
52.22
N


ATOM
2541
O1G
ATP
N
1
47.406
23.911
3.763
1.00
51.41
N


ATOM
2542
O2G
ATP
N
1
46.794
26.182
2.784
1.00
52.07
N


ATOM
2543
O3B
ATP
N
1
44.976
24.513
3.344
1.00
51.01
N


ATOM
2544
PB
ATP
N
1
44.560
22.969
3.605
1.00
50.20
N


ATOM
2545
O1B
ATP
N
1
43.083
22.898
3.669
1.00
49.41
N


ATOM
2546
O2B
ATP
N
1
45.345
22.474
4.766
1.00
50.34
N


ATOM
2547
O3A
ATP
N
1
45.070
22.231
2.255
1.00
47.77
N


ATOM
2548
PA
ATP
N
1
45.075
20.613
2.121
1.00
42.84
N


ATOM
2549
O1A
ATP
N
1
45.547
20.291
0.754
1.00
43.81
N


ATOM
2550
O2A
ATP
N
1
45.807
20.035
3.270
1.00
45.03
N


ATOM
2551
O5*
ATP
N
1
43.516
20.223
2.245
1.00
41.73
N


ATOM
2552
C5*
ATP
N
1
42.528
20.925
1.489
1.00
37.57
N


ATOM
2553
C4*
ATP
N
1
41.127
20.379
1.776
1.00
39.45
N


ATOM
2554
O4*
ATP
N
1
40.907
19.024
1.279
1.00
37.72
N


ATOM
2555
C3*
ATP
N
1
40.777
20.321
3.251
1.00
38.48
N


ATOM
2556
O3*
ATP
N
1
40.360
21.615
3.697
1.00
40.42
N


ATOM
2557
C2*
ATP
N
1
39.608
19.374
3.270
1.00
37.58
N


ATOM
2558
O2*
ATP
N
1
38.410
20.076
2.924
1.00
35.98
N


ATOM
2559
C1*
ATP
N
1
39.939
18.346
2.173
1.00
35.55
N


ATOM
2560
N9
ATP
N
1
40.628
17.156
2.747
1.00
31.76
N


ATOM
2561
C8
ATP
N
1
41.864
17.126
3.274
1.00
30.49
N


ATOM
2562
N7
ATP
N
1
42.143
15.877
3.667
1.00
29.75
N


ATOM
2563
C5
ATP
N
1
41.088
15.118
3.390
1.00
27.49
N


ATOM
2564
C4
ATP
N
1
40.125
15.925
2.810
1.00
30.02
N


ATOM
2565
N3
ATP
N
1
38.937
15.389
2.431
1.00
27.11
N


ATOM
2566
C2
ATP
N
1
38.679
14.085
2.615
1.00
25.62
N


ATOM
2567
N1
ATP
N
1
39.597
13.283
3.175
1.00
21.76
N


ATOM
2568
C6
ATP
N
1
40.800
13.768
3.571
1.00
23.90
N


ATOM
2569
N6
ATP
N
1
41.698
12.964
4.127
1.00
21.94
N


ATOM
2570
S
SO4
I
1
58.680
8.493
−0.639
1.00
56.05
I


ATOM
2571
O1
SO4
I
1
57.956
7.875
0.483
1.00
58.83
I


ATOM
2572
O2
SO4
I
1
57.886
9.607
−1.188
1.00
57.04
I


ATOM
2573
O3
SO4
I
1
58.906
7.478
−1.683
1.00
57.47
I


ATOM
2574
O4
SO4
I
1
59.976
9.008
−0.156
1.00
57.51
I


ATOM
2575
S
SO4
I
2
39.339
4.855
7.057
1.00
84.24
I


ATOM
2576
O1
SO4
I
2
39.390
6.175
7.711
1.00
85.02
I


ATOM
2577
O2
SO4
I
2
40.101
4.897
5.797
1.00
84.75
I


ATOM
2578
O3
SO4
I
2
37.936
4.506
6.766
1.00
84.94
I


ATOM
2579
O4
SO4
I
2
39.931
3.842
7.954
1.00
84.44
I


ATOM
2580
S
SO4
I
3
38.987
−2.256
3.310
1.00
58.58
I


ATOM
2581
O1
SO4
I
3
37.734
−1.675
3.827
1.00
59.11
I


ATOM
2582
O2
SO4
I
3
39.460
−1.454
2.172
1.00
59.91
I


ATOM
2583
O3
SO4
I
3
38.743
−3.640
2.866
1.00
60.97
I


ATOM
2584
O4
SO4
I
3
40.014
−2.260
4.369
1.00
59.58
I


ATOM
2585
S
SO4
I
4
34.397
5.289
30.981
1.00
64.34
I


ATOM
2586
O1
SO4
I
4
33.627
6.528
30.742
1.00
60.43
I


ATOM
2587
O2
SO4
I
4
34.337
4.427
29.782
1.00
60.11
I


ATOM
2588
O3
SO4
I
4
33.816
4.572
32.133
1.00
64.39
I


ATOM
2589
O4
SO4
I
4
35.806
5.626
31.277
1.00
63.55
I


ATOM
2590
S
SO4
I
5
55.074
−6.984
−3.711
1.00
75.40
I


ATOM
2591
O1
SO4
I
5
54.657
−7.518
−2.399
1.00
74.66
I


ATOM
2592
O2
SO4
I
5
54.209
−5.845
−4.065
1.00
74.96
I


ATOM
2593
O3
SO4
I
5
54.950
−8.034
−4.742
1.00
74.22
I


ATOM
2594
O4
SO4
I
5
56.477
−6.532
−3.633
1.00
75.15
I


ATOM
2595
O2
PO4
P
100
57.362
24.998
13.149
1.00
66.76
P


ATOM
2596
O3
PO4
P
100
59.399
26.166
13.761
1.00
66.89
P


ATOM
2597
O4
PO4
P
100
57.761
25.606
15.462
1.00
67.43
P


ATOM
2598
O1
PO4
P
100
57.264
27.325
13.818
1.00
65.91
P


ATOM
2599
P
PO4
P
100
57.947
26.025
14.048
1.00
66.69
P


END









Example 5
PDK1 Fragments
We produced constructs for expression of different forms of PDK1 in bacteria. The constructs were either in TRC vectors, pET-15b vector and pGEX expression vector to enable the expression of GST fused N-terminally to PDK1. PDK1 expressed from pGEX 51-556 (ie residues 51 to 556 of PDK1) was found to be highly degraded.
PDK1 protein was also expressed with N-terminal His tags from vector TRC comprising PDK1 sequences 51-556, 51-404 and 1-360, or pET15b 51-404 and tested for expression levels and activity. The expression was generally low, around 0.2 mg/L culture. The specific activity was lower than the His-tagged 51-556 protein purified from baculovirus cells. In the case of PDK1 51-404 expressed from pET-15b construct the level of expression turned out to be very variable. This was probably due to instability of the plasmid since we produced evidence that after a growth of 0.2 units of absorbance, (as measured in a spectrophotometer at 600 nm wavelength) the cells growing faster in the culture were actually not harbouring the plasmid with ampiciline resistance. The instability of the plasmid can be due to toxicity produced by basal expression of PDK1. Although production in bacteria was the theoretical best expression system to avoid heterogeneity due to the different extent of phosphorylation of the different phosphorylation sites in hPDK1, it was found that the protein was either degraded, expressed to low levels, had 5 times less specific activity, or was possibly toxic.
The His-tagged purified PDK1 51-556 protein obtained from baculovirus expression system was homogeneous as depicted by the appearance of one band after by SDS-PAGE analysis of a sample.
Nevertheless, the analysis after isoelectric focussing revealed a large smear of protein covering several units of pH. This analysis suggested that the protein was not homogeneous in terms of its isoelectric point, possibly due to the number of phosphorylation sites which were not homogeneously phosphorylated. This protein did not crystallise.
We purified to homogeneity a truncated His-Myc tagged PDK1 (51-404) which lacks the N-terminal 50 residues and the C-terminal 152 residues which include the PH domain. This protein, produced by a baculovirus expression system, had similar characteristics to the full length wild type PDK1 in terms of its activity towards the peptide substrate T308tide, its activation by the peptide PIFtide, and the binding to PIFtide (as analysed by BiaCore). The purified protein was screened for crystallisation conditions using Hampton Research kits (144 different conditions). Crystallisation conditions were screened with two concentrations of PDK1, in the presence or absence of PIFtide, Staurosporine, at 20° C. and in the presence of PIFtide at 4° C. No protein crystals were observed after 6 months, suggesting that this construct was not suitable for forming crystals although all other characteristics were similar to wild type protein.
The His-Myc PDK1 51-404 purified protein was also subjected to protease treatments in order to obtain a protease-insensitive molecule for increasing the chances of obtaining a shorter, stable variant of PDK1. Different protease treatments were tested. Treatment with Glu-C produced a polypeptide of approximately 38 KDa which was stable. This PDK1 protein was active and lacked the His-tag and part of the Myc-tag, and possibly part of the C-terminal residues. This protein was also set up for crystallography screenings. Some crystals were obtained using this preparation after 4 months, but they were not followed up.
A protein kinase corresponding to residues PDk1 51-387 was also produced, in an identical vector to that used to produce the protein PDK1 51-359. Interestingly, this protein was similar to wild type and PDK1 51-404, but had extreme problems for concentration using conventional methods. The protein could not be concentrated further than 2.5 mg/ml, and no crystals were obtained using this construct.
The PDK1 protein that finally crystallised is lacking the first 50 aminoacids and was constructed to end at position 359. This protein was stable in the absence of the PH domain and aminoacids that in hPDK1 link the catalytic domain with the PH domain. The construct PDK1 51-359 was also short enough that no other described phosphorylation sites besides activation loop phosphorylation site 241 were present.
Example 6
Structural Basis for UCN-01 Specificity and PDK1 Inhibition
The staurosporine derivative UCN-01 (7-hydroxyl staurosporine) has been reported to be a potent inhibitor for PDK1 and is currently in clinical trials for the treatment of cancer. Here we report the crystal structures of staurosporine and UCN-01 in complex with the kinase domain of PDK1. We show that although staurosporine and UCN-01 interact with the PDK1 active site in an overall similar manner, the UCN-0,7-hydroxyl group, which is not present on staurosporine, generates direct and water-mediated hydrogen bonds with active site residues. Inhibition data from UCN-01 tested against a panel of 29 different kinases show a different pattern of inhibition compared to staurosporine. We discuss how these differences in inhibition could be attributed to specific interactions with the additional 7-hydroxyl-group as well as by the size of the 7-hydroxyl-binding pocket. This information could lead to opportunities for structure-based optimisation of PDK1 inhibitors.
Insulin and growth factor signalling is mediated by the activation of a lipid kinase, phosphatidylinositol-3-kinase (PI3K), which produces the second messenger molecule phosphatidylinositol(3,4,5)trisphosphate (PtdIns(3,4,5)P) [1]. Upon generation of PtdIns(3,4,5)P, 3-Phosphoinositide Dependent protein Kinase-1 (PDK1) and protein kinase B (PKB, also known as Akt) are co-localised at the plasma membrane through interaction of their Pleckstrin Homology (PH) domains with PtdIns(3,4,5)P [2,3]. PDK1 activates PKB by phosphorylation of its T-loop (Thr308 in PKB) [4, 5]. PDK1 also activates other protein kinases related to PKB, including isoforms of p70 ribosomal S6 kinase (S6K) [6], serum and glucocorticoid responsive kinases (SGK) [7] and p90 ribosomal S6 kinase (Rsk) [8]. These kinases lack PH domains and do not bind PtdIns(3,4,5)P3, and are thought to be activated by a different mechanism, in which the substrates require a priming phosphorylation in a conserved hydrophobic motif (HM) at their C-terminus (reviewed in [9]). This phosphorylation creates a docking motif that specifically interacts with a pocket on the N-terminal lobe of the PDK1 kinase domain (termed PDK1 interacting fragment (PIF) pocket) [10,11] bringing PDK1 together with its substrate and enabling PDK1 to phosphorylate these kinases in their T-loop, thereby activating them. A significant number of human cancers possess elevated PtdIns(3,4,5)P levels due to mutations in a number of genes that regulate the production and degradation of this 3-phosphoinositide. One of the most frequently found mutations occurs in the PtdIns(3,4,5)P 3-phosphatase (PTEN) resulting in constitutive activation of PKB and S6K, which are thought to be major contributors to the proliferation and the survival of such tumour cells [12]. Thus, inhibitors of PDK1 have the potential to act as anti-cancer agents as they would be expected to suppress activation of S6K and PKB and inhibit cell growth and induce apoptosis of cancer cells that possess elevated levels of PtdIns(3,4,5)P.
PDK1 consists of an N-terminal kinase domain and a C-terminal PH-domain [13]. The structure of the PDK1 kinase domain has been solved (see the preceding Examples and [11]) and leads to a definition of the residues lining the ATP binding site and an understanding of the PDK1 activation mechanism. The PIFbinding pocket could be identified, together with a specific pocket for the phosphorylated Ser/Thr residue on the HM of substrate kinases. Staurosporine, a natural product ATP-competitive inhibitor, inhibits many kinases in the low nM range [14], and therefore displays a high cytotoxicity [15]. UCN-01 (7-hydroxyl staurosporine) is a derivative with an additional hydroxyl group on the lactam ring (FIG. 1). It was originally described as a PKC-selective inhibitor isolated from Streptomyces sp. cultures [16], although further studies showed it to be more non-specific [14, 17]. UCN-01 potently inhibits the growth and induces apoptosis of many cancer cells and these effects are thought to be unrelated to PKC inhibition [18, 19]. Due to its anti-tumour activity in vivo and in vitro, UCN-01 is currently undergoing clinical trials with positive effects being reported in the phase 1 studies (reviewed in [19]). Recent reports suggested the cell cycle checkpoint kinase Chk1 [20] and PDK1 [21] may be key targets of UCN-01 in inhibiting the growth of cancer cells, as both kinases are inhibited by UCN-01 in the low nM range.
Here we report the structures of the PDK1 kinase domain in complex with staurosporine and UCN-01, demonstrating the presence of a pocket that accommodates the 7-hydroxyl group of UCN-01. Specificity tests against a panel of 29 kinases shows that although both staurosporine and UCN-01 are relatively non-specific inhibitors, the fingerprint analysis of UCN-01 inhibition with a panel of protein kinases is significantly different from that of staurosporine. We also perform analysis of residues predicted to line the UCN-01 hydroxyl pocket on a number or protein kinases, and propose a general model that could account for the different sensitivity of protein kinases for staurosporine and UCN-01.
Methods
Expression, Purification and Crystallisation
Human PDK1 (residues 51-359) was expressed using a baculovirus mediated infection of the SF21 insect cell line and purified as described in the preceding examples and [11] with the following differences: After elution of the His-tagged protein from the Ni-NTA-agarose beads with 200 mM imidazole, the protein was dialysed against 250 mM NaCl, 25 mM Tris pH 7.5, 1 mM DTT for 3 hours at 4° C. Proteolysis with GST-tagged PreScission protease was performed overnight at 4° C.
For crystals of the PDK1-UCN-01 complex, 100 μl of PDK1 at a concentration of 6.6 mg/ml was mixed with 30 μl UCN-01 (5.3 mM in 50% ethanol) and incubated on ice for 2 hours. The protein was crystallized using sitting drop vapour diffusion. 1.25 μl of protein solution was mixed with 0.25 μl cobaltous chloride hexahydrate (0.1 M) and 1 μl mother liquor, consisting of 2.1 M ammonium sulphate, 0.1 M Tris-HCl pH 8.5. Hexagonal, rod-shaped crystals grew at 20° C. and reached a maximum size of 0.05×0.05×0.3 mm after 7 days. After soaking for 3 seconds in a cryo-protection solution (2.1 M ammonium sulphate, 0.1 M Tris-HCl pH 7.2, 25% glycerol) crystals were frozen in a stream of cold nitrogen.
PDK1 in complex with staurosporine was crystallized using the hanging drop technique. Drops consisted of 1 μl PDK1 at 7.6 mg/ml, 1 μl mother liquor (2.1 M ammonium sulphate, 0.1 M Tris-HCl pH 7.2) and 0.25 μl staurosporine (10 mM in DMSO). Hexagonal shaped crystals suitable for data collection appeared after 6 weeks at 20 C. Crystals were soaked in 1.7 M ammonium sulphate, 0.1 M Tris-HCl pH 7.2, 15% glycerol and frozen in a stream of cold nitrogen.
Data Collection, Structure Solution and Refinement
Data on the PDK1-staurosporine and PDK1-UCN-01 complexes were collected at the European Synchrotron Radiation Facility (Grenoble, France) beamline ID14-EH4. The temperature of the crystals was maintained at 100 K using a nitrogen cryostream. Data were processed using the HKL package [22] with final statistics shown in Table 3. The structures were solved by rigid body refinement with CNS [23] using the previously determined PDK1 structure (See previous Examples; PDB code 1H1W) [11] as a starting model which resulted in an initial R-factor of 0.306 (Rfree=0.284) for PDK1-staurosporine and 0.299 (Rfree=0.311) for PDK1-UCN-01. Model building with 0 [24] and iterative refinement in CNS, including solvent molecules and the T-loop phosphorylation site, resulted in final R-factors as shown in Table 3. The ATP binding site showed well-defined density in the unbiased |Fo|−Fc|, φcalc maps for all atoms of staurosporine and UCN-01, including the 7-hydroxyl group (FIG. 8). CNS topologies and coordinates for the inhibitors were generated with PRODRG [25]. No electron density could be observed for residues 51-72 (N-terminus), residues 231-239 (T-loop) and residue 359 (C-terminus) in the PDK1-UCN-01 complex. Residues 51-71 (N-terminus) and 233-238 (T-loop) were disordered in the PDK1-staurosporine complex.
Determination of Inhibition and Specificity
Protein kinase assays: PDK1 was assayed for 10 min at 30° C. in a 50 μl assay mixture in 50 mM Tris pH 7.5, 0.1 mM EGTA, 0.1% 2-mercaptoethanol, containing 100 μM PDK1tide substrate peptide (KTFCGTPEYLAPEVRREPRILSEEEQEMFRDFDYIADWC) (SEQ ID NO:112), 10 mM magnesium acetate, 100 μM [γ-32P]ATP (200 cpm/pmole) as described previously [10]. Other protein kinases employed in Table 5, were assayed as described previously [17, 26].
Results & Discussion
Structures of the Staurosporine and UCN-01 Complexes
PDK1 (residues 51-359) was co-crystallized with staurosporine and UCN-01, and synchrotron diffraction data on a thin hexagonal needle were collected to 2.3 Å and 2.5 Å resolution, respectively.
In the unbiased |Fo|−Fc|, φcalc maps well defined (>3.0σ) density could be observed in the ATP binding site of the kinase, covering all staurosporine/UCN-01 atoms including the 7-hydroxyl group (FIG. 8). After initial rounds of protein model building and inclusion of water molecules, the inhibitor molecules were built and refined with full occupancy to average B-factor of 18.5 Å2 (staurosporine) and 17.3 Å2 (UCN-01). Further refinement resulted in a final PDK1-staurosporine model with R=0.218 (Rfree=0.255) and a final PDK1-UCN-01 model with R=0.184 (Rfree=0.257), both with good stereochemistry (Table 3).
The staurosporine molecule is located in the ATP-binding site (which lies between the N-terminal and C-terminal lobes of kinases [27, 28]), at the same position described for the inhibitor in complex with the closely related (38% sequence identity) protein kinase A (PKA, [29], PDB code 1STC) (FIG. 8). Hydrophobic residues on both sides of the ATP binding cleft sandwich the heterocyclic moiety of staurosporine, namely Leu88, Val96, Ala109, Leu98 (small lobe) and Thr222, Leu212 of the larger lobe (FIG. 1).
Similar to the PKA-staurosporine complex, the lactam group mimics the interactions of the adenine base in ATP with the protein backbone, where 2 conserved hydrogen bonds are formed between the lactam-nitrogen N6 in staurosporine (nomenclature according to [30]) and the backbone-oxygen of Ser160, and the lactam-oxygen at the C5 position and the backbone-nitrogen of Ala162 (Table 4). An additional hydrogen bond is mimicked in the staurosporine sugar-moiety, where the methyl-amino group contacts oxygen O 2 of Glu166, similar to the hydrogen bond with the ribose in the PDK1-ATP complex [11], and also the backbone carbonyl of Glu209 (Table 4).
The UCN-01 molecule occupies the same position in the ATP binding site as staurosporine (maximum atomic shift=0.35 Å) (FIG. 9). The same hydrophobic interactions are made to the heterocyclic moiety in the PDK1-staurosporine complex. Hydrogen bonding interactions to the heterocycle and the sugar moiety are also conserved, with similar geometry (Table 4). However, the 7-hydroxyl group of UCN-01 forms several novel hydrogen bonds (FIG. 9, Table 4). It hydrogen bonds directly to Oγ1 of Thr222 (FIG. 9, Table 4). In addition, an ordered water molecule (B-factor=24.0 Å2) is found in a position where it contacts the 7-hydroxyl (distance=3.0 Å, Table 4) and the oxygen Oε1 of Gln220 (distance=2.5 Å) the side chain of which is shifted towards the ligand (1.5 Å for Cδ, rotation of 82° around χ1) compared to the PDK1-STO complex. However, the water molecule is buried in a predominantly hydrophobic pocket, lined by Val143, Leu212 and Cγ2 of Thr222 (FIG. 9). Val143 also changes its position compared to the PDK1-staurosporine complex (FIG. 9), moving further towards the back of the pocket (shift of 0.7° A for the Cα carbon, and a rotation of 100° around χ1) and displaces an ordered water molecule present in the PDK1-staurosporine complex (FIG. 9), and also observed in other kinase-staurosporine complexes [31, 30]. These changes result in more space to accommodate the bulky 7-hydroxyl group on UCN-01 as indicated by a 6° A3 increase in ligand volume (calculated with VOIDOO [32]).
Comparison with Chk1-UCN-01
High resolution data for the Chk1 kinase bound to staurosporine and UCN-01 is available (PDB code 1NVQ [30]). In Chk1, Ser147, the equivalent of Thr222 in PDK1, also hydrogen bonds the UCN-01 7-OH directly. In addition, a water mediated network of hydrogen bonds to UCN-01 is observed. However, in Chk1 the water molecule that hydrogen bonds UCN-01 occupies a different position (shifted 5.2 Å compared to the PDK1-UCN-01 complex). Chk1 appears to have a more extended hydrophilic cavity, as there are 2 additional buried water molecules present also in the Chk1-staurosporine complex. The corresponding residue to Gln220 in PDK1 is a Lys (Lys145) in Chk1, which does not interact with the ligand but points away from it.
UCN-01 Inhibition and Specificity
PDK1 inhibition by UCN-01 and staurosporine was measured using kinase assays with P32-labelled ATP. PDK1 is inhibited by UCN-01 with an IC50 value of 5 nM, and by staurosporine with an IC50 of 6.5 nM. As a measure for overall specificity of UCN-01 and staurosporine, the effect of these inhibitors was tested against a panel of 29 protein kinases as described previously [17, 26]. The results are shown in Table 5 as percentage of control activity. These data further confirm that UCN-01 and staurosporine are aspecific inhibitors. UCN-01 at 1 μM concentration reduces the activity of nine kinases in the panel to less than 10%, and of ten others to below 60% of control activity. Staurosporine at 1 μM will inhibit twelve kinases to less than 10% control activity, and another ten to below 60%. Interestingly, however, several of the protein kinases were differentially inhibited by staurosporine and UCN-01 (Table 5). In an attempt to understand these differences the panel of kinases was divided in four distinct classes: (a) similar inhibition, (b) stronger inhibition by staurosporine than by UCN-01, (c) stronger inhibition by UCN-01 than by staurosporine, and (d) no inhibition (Table 5). As the additional 7-hydroxyl group is the only difference in the ligand molecules (FIG. 8), and staurosporine and UCN-01 occupy the same position with similar interactions in the binding site (FIG. 9), the residues contacting the extra hydroxyl group were identified for PDK1 and extracted from a sequence alignment of all protein kinases used in the panel (Table 5). A structure-based sequence alignment of known kinase structures was obtained from [33], which was used to validate the sequence-based sequence alignment (Table 5). The nature of the side chains lining the hydroxyl-pocket could provide a partial explanation for the relative difference between UCN-01 and staurosporine inhibition. Two trends can be observed. For the kinases that are inhibited by UCN-01, there appears to be a preference for a side chain capable of hydrogen bonding the 7-hydroxyl in the hydroxyl-pocket. This is in agreement with the presence of a Thr/Ser residue that hydrogen bonds the 7-hydroxyl in the structures of PDK1 (Thr222) and Chk1 (Ser147) bound to UCN-01. Seven out of ten kinases that are hit equally by staurosporine and UCN-01 (group (a)) appear to have a potential hydrogen bonding residue (Table 5). The kinases that are more potently inhibited by UCN-01 than by staurosporine (group (c)) contain a Thr at the Thr222 equivalent position (Table 5). Five out of nine kinases that are inhibited more potently by staurosporine than by UCN-01 (group (b)) lack a potential hydrogen binding partner in the 7-hydroxyl-pocket (Table 5).
A second trend which appears to determine specificity is the size of the residues lining the hydroxyl-pocket. If the predicted total volume of the residues (calculated with the BL-set of side chain volumes [34]) at the positions indicated in Table 5 is set against the activity in the presence of UCN-01, a correlation coefficient of 0.6 is obtained. This suggests that despite inaccuracies in this approach, such as the absence of structural information on precise side chain conformation and water molecules, a weak correlation between predicted hydroxyl pocket volume and UCN-01 inhibition exists. For instance, PKA contains a possible hydrogen bonding partner for UCN-01 (Thr183), but Met134 in the centre of the hydroxyl pocket may leave no space for the extra hydroxyl group (Table 5). A similar arrangement of residues can be observed for MAPKAP-K2 (Table 5). This size dependency may also play a role for the protein kinases neither hit by staurosporine nor UCN-01. The sequence alignment shows that the Val143 and Thr222 equivalent residues are replaced by bulkier Leu or Ile residues in several of the Mitogen Activated Protein Kinase families (Table 5). To investigate the effect of these bulkier side chains on the hydroxyl pocket, we, starting from the PDK1 crystal structure, replaced residues Val143 with Ile and Thr222 with Leu in standard side chain rotamers (in O [24]), which indeed resulted in van der Waals clashes with C7 of staurosporine (shortest distances: 2.8 Å for Leu222, 3.5 Å for Ile143), and may therefore explain the lack of susceptibility towards UCN-01 in the Mitogen Activated Protein Kinase families. CDK2 is inhibited by both staurosporine and UCN-01 similarly, however this kinase lacks a hydrogen bonding partner for the 7-hydroxyl and contains a bulky Phe (Phe80) at the Leu159 equivalent position. In a superposition of CDK2-staurosporine structure [31] with PDK1-UCN-01 (RMSD=1.3 Å on Cα atoms) staurosporine is seen to be shifted by 1.2 Å out of the potential hydroxyl pocket due to presence of the bulky Phe80. Interaction of the 7-hydroxyl on UCN-01 was described to be water mediated in CDK2 due to the lack of hydrogen bonding residues [35]. This particular example highlights the limitations of the approach described above. Other examples where none of the described effects account for the observed behaviour are AMPK and MSK1. Both MSK1 and SGK1 show the same sequence in their hydroxyl-pocket with Thr406/Thr407, respectively, as potential hydrogen bonding partners, but both were placed in different groups. MSK1 activity is abolished by 1 μM staurosporine, but shows residual activity (11%) with UCN-01. SGK1 activity is at 25% of control activity with 1 μM UCN-01, but twice as high with staurosporine.
Conclusions
UCN-01 was subjected to a specificity analysis against an in-house panel of 29 protein kinases. Contrary to the suggestions of some previous reports, the data show that UCN-01 is not a specific inhibitor as it inhibited more than half of the tested kinases at significant levels. A direct comparison with staurosporine, however, showed a different pattern of inhibition, and was the subject of further analysis. We have reported the crystal structures of PDK1 in complex with the inhibitors staurosporine and UCN-01. Both inhibitors appear to bind to PDK1 in a similar fashion compared to the Chk1-UCN-01 or PKA-staurosporine [29] complex, with additional hydrogen bonding interactions at the UCN-01 7-hydroxyl group. This moiety is hydrogen bonded directly to Thr222 and indirectly via an ordered water molecule to Gln220. A different water-mediated hydrogen bonding network is also observed in other UCN-01 complexes known to date [35, 30], and might serve as a starting point for further structure-based optimisation. The residues around the 7-hydroxyl group (“hydroxyl-pocket”) were aligned with known kinase structures and kinases sequences. It is apparent that spatial effects in the identified pocket play a key role in determining UCN-01 inhibition, as does the presence of hydrogen bonding partners for the additional hydroxyl group.







TABLE 3







Details of data collection &  structure refinement. Values between


brackets are for the highest resolution shell. Crystals were cryo-


cooled to 100 K. All measured data were included in structure refinement.









Dataset
Staurosporine
UCN-01





Space group
P3221
P3221


Cell dimensions (Å)
a = 124.17
a = 123.39



b = 124.17
b = 123.39



c = 47.31
c = 47.12


Resolution range (Å)
25-2.30 (2.38-2.30)
25-2.50 (2.59-2.50)


# Observed reflections
31730 (3091)
68515 (6290)


# Unique reflections
18018 (1794)
14395 (1430)


Redundancy
1.8 (1.7)
4.8 (4.4)


I/σI
7.5 (1.8)
4.5 (2.6)


Completeness (%)
95.8 (95.8)
100.0 (99.9)


Rmerge
0.096 (0.505)
0.167 (0.688)


Rcryst, Rfree
0.218, 0.255
0.189, 0.257







RMSD from ideal geometry









Bonds (Å)
0.007
0.009


Angles (°)
1.7
1.8


B-factor RMSD (Å)
1.5
1.4


(bonded, main chain)


<B> protein (Å)
31.5
27.3


<B> inhibitor (Å)
18.5
17.4
















TABLE 4







Hydrogen bonding between inhibitors and PDK1. Hydrogen bonds


between PDK1 and UCN-01/staurosporine (STO) were calculated with


WHAT IF [36] using the HB2 algorithm [37]. This algorithm gives a 0


(no hydrogen bond) to 1 (optimal hydrogen bond) score to reflect


hydrogen bond geometry (HB2 column). Donor-acceptor distances are also


listed (D-A).















UCN-01
UCN-01





Inhibitor
Protein/H2O
D-A (Å)
HB2
STO D-A (Å)
STO HB2
Comment





O5
N-Ala162
2.8
0.76
3.0
0.81
Conserved


N6
O-Ser162
2.9
0.80
3.1
0.67
Conserved


N4′
O-Glu209
3.2
0.68
3.1
0.39
Conserved


N4′
Oε2-Glu166
2.6
0.63
2.5
0.45
Conserved


O7
Oγ1-Thr222
3.0
0.56


7-hydroxyl


O7
H2O
3.0
0.89


Water mediated to








(Oε1-Gln220)
















TABLE 5







Comparison of inhibition by UCN-01 vs. staurosporine and hydroxyl pocket-lining residues.


The indicated protein kinases were assayed at 0.1 mM ATP as described previously [17, 26], in the


absence or presence of 1 μM staurosporine (STO) or UCN-01. Results are presented as percentage of


kinase activity compared to that in control incubations. The activity results displayed in the two columns


are an average of a triplicate determination. Abbreviations not defined in main text: ROCKII, Rho-


dependent protein kinase-II; AMPK, AMP-activated protein kinase; MKK1, MAP-kinase kinase-1;


PRAK, p38-regulated/activated protein kinase; PHK, phosphorylase kinase; CK2, Casein kinase-2; CHK1,


cell cycle checkpoint kinase-1; DYRK, dual specificity tyrosine phosphorylated and regulated kinase;


CSK, C-terminal Src kinase. Residues lining the hydroxyl pocket are shown in the last five columns, as


derived from a multiple sequence alignment with T-Coffee [38].










Kinase
STO
UCN-01










Both STO and UCN-01 inhibit














PDK1
5 ± 1
0 ± 1
Met134
Val143
Leu159
Gln220
Thr222


CHK1 (1NVQ [30])
3 ± 1
1 ± 0
Ile
Val
Leu
Lys145
Ser147


PKCα
8 ± 2
1 ± 0
Leu
Thr
Met
Lys
Ala


AMPK
0 ± 0
1 ± 1
Leu
Ile
Met
Lys
Ala


PHOS.KINASE (1PHK [39])
2 ± 3
1 ± 2
Leu
Ile
Phe
Lys
Thr


Lck (1QPJ [40])
0 ± 0
3 ± 1
Met
Val
Thr
Lys
Ala


CDK2/cyclin A (1AQ1 [31])
12 ± 12
8 ± 0
Leu
Val
Phe80
Lys
Ala


PKBΔPH (1O6K [41])
8 ± 2
9 ± 1
Leu
Thr
Met
Lys
Thr


ROCK-II
9 ± 5
13 ± 2 
Met
Val
Met
Lys
Ala


S6K1
24 ± 8 
21 ± 4 
Leu
Val
Leu
Lys
Thr


GSK3β (1I09 [42])
29 ± 6 
25 ± 5 
Met
Val
Leu
Lys
Cys







STO inhibits stronger than UCN-01














MSK1
1 ± 0
11 ± 0 
Leu
Val
Leu
Val
Thr406


DYRK1α
2 ± 2
15 ± 2 
Leu
Met
Phe
Lys
Val


PKA (1STC [29])
4 ± 1
27 ± 2 
Leu
Val
Met134
Gln
Thr183


MKK1
5 ± 8
53 ± 1 
Leu
Val
Met
Lys
Cys


MAPKAP-K2
23 ± 1 
60 ± 1 
His
Val
Met
Lys
Thr


CSK (1BYG [43])
25 ± 8 
58 ± 3 
Met
Val
Thr
Lys
Ser


SAPK3/p38γ (1CM8 [44])
37 ± 0 
94 ± 8 
Leu
Ile
Met
Lys
Leu


SAPK4/p38δ
40 ± 5 
100 ± 7 
Leu
Ile
Met
Lys
Leu


PRAK
48 ± 1 
89 ± 4 
His
Val
Met
Lys
Cys







UCN-01 inhibits stronger than STO














MAPKAP-K1a
18 ± 10
1 ± 1
Leu
Val
Leu
Lys
Thr341


SGK1
51 ± 4 
22 ± 4 
Leu
Val
Leu
Val
Thr407







Neither UCN-01 nor STO inhibits














MAPK2/ERK2 (1ERK [45])
100 ± 4 
107 ± 5 
Leu
Ile
Gln
Lys
Cys


JNKSAPK1c
91 ± 3 
112 ± 6 
Met
Ile
Met
Lys
Leu


SAPK2α/p38 (1P38 [46])
76 ± 4 
107 ± 5 
Leu
Ile
Thr
Lys
Leu


SAPK2β/p38β2
84 ± 11
106 ± 4 
Leu
Ile
Thr
Arg
Leu


CK2 (1F0Q [47])
95 ± 4 
102 ± 11 
Leu
Val
Phe
Arg
Ile


CK1 (1CKI [48])
95 ± 11
96 ± 0 
Tyr
Pro
Met
Tyr
Ile


NEK6
109 ± 2 
80 ± 7 
Leu
Ile
Leu
Lys
Gly









REFERENCES


    [1] B. Vanhaesebroeck and D. R. Alessi, The PI3K-PDK1 connection: more than just a road to PKB., Biochem J, 346, 561-76 (2000).
    [2] R. A. Currie, K. S. Walker, A. Gray, M. Deak, A. Casamayor, C. P. Downes, P. Cohen, D. R. Alessi, and J. Lucocq, Role of phosphatidylinositol 3,4,5-trisphosphate in regulating the activity and localization of 3-phosphoinositide-dependent protein kinase-1, Biochem. J., 337, 575-583 (1999).
    [3] D. R. Alessi, Discovery of PDKI, one of the missing links in insulin signal transduction, Biochem. Soc. Trans., 29, 1-14 (2001).
    [4] D. P. Brazil and B. A. Hemmings, Ten years of protein kinase B signalling: a hard Akt to follow, Trends Biochem. Sci., 26, 657-664 (2001).
    [5] M. P. Scheid and J. R. Woodgett, PKB/AKT: Functional insights from genetic models, Nat. Rev. Mol. Cell. Biol., 2, 760-768 (2001).
    [6] N. Pullen, P. B. Dennis, M. Andjelkovic, A. Dufner, S. C. Kozma, B. A. Hemmings, and G. Thomas, Phosphorylation and activation of p70(s6k) by PDK1, Science, 279, 707-710 (1998).
    [7] F. Lang and P. Cohen, Regulation and physiological roles of serum- and glucocorticoid-induced protein kinase isoforms, Sci. STKE, RE17, (2001).
    [8] M. Frodin and S. Gammeltoft, Role and regulation of 90 kDa ribosomal S6 kinase (RSK) in signal transduction, Mol. Cell. Endocrinol., 151, 65-77 (1999).
    [9] R. M. Biondi and A. R. Nebreda, Signalling specificity of Ser/Thr protein kinases through docking-site-mediated interactions, Biochem. J., 372, 1-13 (2003).
    [10] R. M. Biondi, P. C. F. Cheung, A. Casamayor, M. Deak, R. A. Currie, and D. R. Alessi, Identification of a pocket in the PDK1 kinase domain that interacts with PIF and the C-terminal residues of PKA, Embo J., 19, 979-988 (2000).
    [11] R. M. Biondi, D. Komander, C. C. Thomas, J. M. LizcanoM. Deak, D. R. Alessi, and D. M. F. van Aalten, High resolution crystal structure of the human PDK1 catalytic domain defines the regulatory phosphopeptide docking site, EMBO J., 21, 4219-4228 (2002).
    [12] N. R. Leslie and C. P. Downes, PTEN: The down side of PI 3-kinase signalling, Cell. Signal., 14, 285-295 (2002).
    [13] D. R. Alessi, M. Deak, A. Casamayor, F. B. Caudwell, N. Morrice, D. G. Norman, P. Gaffney, C. B. Reese, C. N. MacDougall, D. Harbison, A. Ashworth, and M. Bownes, 3-phosphoinositide-dependent protein kinase-1 (PDK1): structural and functional homology with the Drosophila DSTPK61 kinase, Curr. Biol., 7, 776-789 (1997).
    [14] U. T. Ruegg and G. M. Burgess, Staurosporine, K-252 and UCN-01-potent but nonspecific inhibitors of protein-kinases, Trends Pharmacol. Sci., 10, 218-220 (1989).
    [15] W. T. Couldwell, D. R. Hinton, S. K. He, T. C. Chen, I. Sebat, M. H. Weiss, and R. E. Law, Protein-kinase-C inhibitors induce apoptosis in human-malignant glioma cell-lines, FEBS Lett., 345, 43-46 (1994).
    [16] I. Takahashi, Y. Saitoh, M. Yoshida, H. Sano, H. Nakano, M. Morimoto, and T. Tamaoki, Ucn-01 and ucn-02, new selective inhibitors of protein kinase-c 0.2. Purification, physicochemical properties, structural determination and biological-activities, J. Antibiot., 42, 571-576 (1989).
    [17] S. P. Davies, H. Reddy, M. Caivano, and P. Cohen, Specificity and mechanism of action of some commonly used protein kinase inhibitors, Biochem. J., 351, 95-105 (2000).
    [18] A. Gescher, Staurosporine analogues-pharmacological toys or useful antitumour agents?, Crit. Rev. Oncol. Hematol., 34, 127-133 (2000).
    [19] A. M. Senderowicz, The cell cycle as a target for cancer therapy: basic and clinical findings with the small molecule inhibitors flavopiridol and UCN-01., Oncologist, 7:3, 9-12 (2002).
    [20] P. R. Graves, L. J. Yu, J. K. Schwarz, J. Gales, E. A. Sausville, P. M. O'Connor, and H. Piwnica-Worms, The Chk1 protein kinase and the Cdc25C regulatory pathways are targets of the anticancer agent UCN-01, J. Biol. Chem., 275, 5600-5605 (2000).
    [21] S. Sato, N. Fujita, and T. Tsuruo, Interference with PDK1-Akt survival signaling pathway by UCN-01 (7-hydroxystaurosporine), Oncogene, 21, 1727-1738 (2002).
    [22] Z. Otwinowski and W. Minor, Processing of X-ray diffraction data collected in oscillation mode, Methods in Enzymology, 276, 307-326 (1997).
    [23] A. T. Brunger, P. D. Adams, G. M. Clore, P. Gros, R. W. Grosse-Kunstleve, J.-S. Jiang, J. Kuszewski, M. Nilges, N. S. Pannu, R. J. Read, L. M. Rice, T. Simonson, and G. L. Warren, Crystallography and NMR system: A new software system for macromolecular structure determination, Acta Cryst., D54, 905-921 (1998).
    [24] T. A. Jones, J. Y. Zou, S. W. Cowan, and M. Kjeldgaard, Improved methods for building protein models in electron density maps and the location of errors in these models, Acta Cryst., A47, 110-119 (1991).
    [25] D. M. F. van Aalten, R. Bywater, J. B. C. Findlay, M. Hendlich, R. W. W. Hooft, and G. Vriend, PRODRG, a program for generating molecular topologies and unique molecular descriptors from coordinates of small molecules, J. Comp. Aid. Mol. Des., 10, 255-262 (1996).
    [26] J. Bain, H. McLauchlan, M. Elliott, and P. Cohen, The specificities of protein kinase inhibitors: an update, Biochem. J., 371, 199-204 (2003).
    [27] D. R. Knighton, J. H. Zheng, L. F. Teneyck, V. A. Ashford, N. H. Xuong, S. S. Taylor, and J. M. Sowadski, Crystal-structure of the catalytic subunit of cyclic adenosinemonophosphate dependent protein-kinase, Science, 253, 407-414 (1991).
    [28] D. A. Johnson, P. Akamine, E. Radzio-Andzelm, Madhusudan, and S. S. Taylor, Dynamics of cAMP-dependent protein kinase, Chem. Rev., 101, 2243-2270 (2001).
    [29] L. Prade, R. A. Engh, A. Girod, V. Kinzel, R. Huber, and D. Bossemeyer, Staurosporine-induced conformational changes of cAMP-dependent protein kinase catalytic subunit explain inhibitory potential, Structure, 5, 1627-1637 (1997).
    [30] B. Zhao, M. J. Bower, P. J. McDevitt, H. Z. Zhao, S. T. Davis, K. O. Johanson, S. M. Green, N. O. Concha, and B. B. S. Zhou, Structural basis for Chk1 inhibition by UCN-01, J. Biol. Chem., 277, 46609-46615 (2002).
    [31] A. M. Lawrie, M. E. M. Noble, P. Tunnah, N. R. Brown, L. N. Johnson, and J. A. Endicott, Protein kinase inhibition by staurosporine revealed in details of the molecular interaction with CDK2, Nat. Struct. Biol., 4, 796-801 (1997).
    [32] G. J. Kleywegt and T. A. Jones, Detection, delineation, measurement and display of cavities in macromolecular structures, Acta Cryst., D50, 178-185 (1994).
    [33] A. Smith, Shindyalovl. N., Veretnik S., Gribskov M., Taylor S. S., TenEyckL. F., and BourneP. E., The protein kinase resource, Trends Biochem. Sci., 22, 444-446 (1997).
    [34] J. Tsai, R. Taylor, C. Chothia, and M. Gerstein, The packing density in proteins: Standard radii and volumes, J. Mol. Biol., 290, 253-266 (1999).
    [35] M. A. Johnson and B. M. Pinto, Molecular mimicry of carbohydrates by peptides, Aust. J. Chem., 55, 13-25 (2002).
    [36] G. Vriend, WHAT IF: a molecular modeling and drug design program, J. Mol. Graph., 8, 52-56 (1990).
    [37] R. W. W. Hooft, C. Sander, and G. Vriend, Positioning hydrogen atoms by optimizing hydrogen-bond networks in protein structures, Proteins, 26, 363-376 (1996).
    [38] C. Notredame, D. G. Higgins, and J. Heringa, T-Coffee: A novel method for fast and accurate multiple sequence alignment, J. Mol. Biol., 302, 205-217 (2000).
    [39] D. J. Owen, M. E. M. Noble, E. F. Garman, A. C. Papageorgiou, and L. N. Johnson, 2 structures of the catalytic domain of phosphorylase-kinase—an active protein-kinase complexed with substrate-analog and product, Structure, 3, 467-482 (1995).
    [40] X. T. Zhu, J. L. Kim, J. R. Newcomb, P. E. Rose, D. R. Stover, L. M. Toledo, H. L. Zhao, and K. A. Morgenstern, Structural analysis of the lymphocyte-specific kinase Lek in complex with non-selective and Src family selective kinase inhibitors, Struct. Fold. Des., 7, 651-661 (1999).
    [41] J. Yang, P. Cron, V. M. Good, V. Thompson, B. A. Hemmings, and D. Barford, Crystal structure of an activated Akt/protein kinase B ternary complex with GSK3-peptide and AMP-PNP, Nat. Struct. Biol., 9, 940-944 (2002).
    [42] E. ter Haar, J. T. Coll, D. A. Austen, H. M. Hsiao, L. Swenson, and J. Jain, Structure of GSK3 beta reveals a primed phosphorylation mechanism, Nat. Struct. Biol., 8, 593-596 (2001).
    [43] M. B. A. C. Lamers, A. A. Antson, R. E. Hubbard, R. K. Scott, and D. H. Williams, Structure of the protein tyrosine kinase domain of C-terminal Src kinase (CSK) in complex with staurosporine, J. Mol. Biol., 285, 713-725 (1999).
    [44] S. Bellon, M. J. Fitzgibbon, T. Fox, H. M. Hsiao, and K. P. Wilson, The structure of phosphorylated P38 gamma is monomeric and reveals a conserved activation-loop conformation, Struct. Fold. Des., 7, 1057-1065 (1999).
    [45] F. M. Zhang, A. Strand, D. Robbins, M. H. Cobb, and E. J. Goldsmith, Atomic-structure of the map kinase ERK2 at 2.3-angstrom resolution, Nature, 367, 704-711 (1994).
    [46] Z. L. Wang, P. C. Harkins, R. J. Ulevitch, J. H. Han, M. H. Cobb, and E. J. Goldsmith, The structure of mitogen-activated protein kinase p38 at 2.1 Angstrom resolution, Proc. Natl. Acad. Sci. USA, 94, 2327-2332 (1997).
    [47] R. Battistutta, S. Sarno, E. DeMoliner, E. Papinutto, G. Zanotti, and L. A. Pinna, The replacement of ATP by the competitive inhibitor emodin induces conformational modifications in the catalytic site of protein kinase CK2, J. Biol. Chem., 275, 29618-29622 (2000).
    [48] L. M. Zhai, P. R. Graves, L. C. Robinson, M. Italiano, M. R. Culbertson, J. Rowles, M. H. Cobb, A. A. Depaoliroach, and P. J. Roach, Casein kinase i-gamma subfamily-molecular-cloning, expression, and characterization of 3 mammalian isoforms and complementation of defects in the saccharomyces-cerevisiae yck genes, J. Biol. Chem., 270, 12717-12724 (1995).
    [49] I. Takahashi, E. Kobayashi, K. Asano, M. Yoshida, and H. Nakano, UCN-01, a selective inhibitor of protein-kinase-c from streptomyces, J. Antibiot., 40, 1782-1784 (1987).


Example 7
Co-Ordinates for PDK1 Fragment Co-Crystallised with Staurosporine












REMARK coordinates from restrained individual B-factor refinement


REMARK refinement resolution: 25.0 - 2.30 A


REMARK starting r= 0.2196 free— r= 0.2545


REMARK final   r= 0.2182 free_r= 0.2553


REMARK B rmsd for bonded mainchain atoms= 1.536  target= 1.5


REMARK B rmsd for bonded sidechain atoms= 2.154  target= 2.0


REMARK B rmsd for angle mainchain atoms= 2.576  target= 2.0


REMARK B rmsd for angle sidechain atoms= 3.220  target= 2.5


REMARK rweight= 0.1000 (with wa= 2.58634)


REMARK target= mlf  steps= 30


REMARK sg= P3(2)21 a= 124.172 b= 124.172 c= 47.314 alpha= 90 beta= 90


gamma= 120


REMARK parameter file 1  : /dd1/david/projects/MY_CNS/prot.par


REMARK parameter file 2  : /dd1/david/projects/MY_CNS/sto.par


REMARK parameter file 3  : CNS_TOPPAR:water_rep.param


REMARK parameter file 4  : CNS_TOPPAR:ion.param


REMARK parameter file 5  : /dd1/david/projects/MY_CNS/glycerol.par


REMARK molecular structure file: ../generate/alternate.mtf


REMARK input coordinates: ../minimize/minimize.pdb


REMARK reflection file= ../../1/hkl/cns.hkl


REMARK ncs= none


REMARK B-correction resolution: 6.0 - 2.30


REMARK initial B-factor correction applied to fobs :


REMARK B11= −4.525 B22= −4.525 B33= 9.049


REMARK B12= −1.949 B13=   0.000 B23 = 0.000


REMARK B-factor correction applied to coordinate array B:   −0.209


REMARK bulk solvent: density level=0.340909 e/A{circumflex over ( )}3, B-factor=36.8807


A{circumflex over ( )}2


REMARK reflections with  |Fobs|/sigma_F < 0.0 rejected


REMARK reflections with  |Fobs| > 1000 * rms(Fobs) rejected








REMARK theoretical total number of refl. in resol. range:
18858 (


100.0 % )


REMARK number of unobserved reflections (no entry or |F|=0):
 846 (


4.5 % )


REMARK number of reflections rejected:
  0 (


0.0 % )


REMARK total number of reflections used:
18012 (


95.5 % )


REMARK number of reflections in working set:
17259 (


91.5 % )


REMARK number of reflections in test set:
 753 (


4.0 % )







CRYST1  124.172  124.172  47.314  90.00  90.00  120.00  P  32  2  1


REMARK FILENAME=“bindindividual.pdb”








REMARK DATE:30-Jan-2003  19:44:02
created by user: david


REMARK VERSION:1.0





















ATOM
1
CB
PRO
A
72
64.267
−7.345
13.422
1.00
74.69
A


ATOM
2
CG
PRO
A
72
63.278
−8.432
13.027
1.00
74.97
A


ATOM
3
C
PRO
A
72
65.866
−6.007
12.013
1.00
73.72
A


ATOM
4
O
PRO
A
72
66.500
−6.002
10.955
1.00
73.74
A


ATOM
5
N
PRO
A
72
64.256
−7.651
11.034
1.00
74.67
A


ATOM
6
CD
PRO
A
72
63.762
−8.901
11.640
1.00
75.33
A


ATOM
7
CA
PRO
A
72
64.474
−6.639
12.090
1.00
74.30
A


ATOM
8
N
GLN
A
73
66.329
−5.474
13.141
1.00
72.17
A


ATOM
9
CA
GLN
A
73
67.635
−4.829
13.221
1.00
70.49
A


ATOM
10
CB
GLN
A
73
67.570
−3.424
12.611
1.00
69.71
A


ATOM
11
CG
GLN
A
73
66.670
−2.458
13.363
1.00
68.72
A


ATOM
12
CD
GLN
A
73
66.722
−1.054
12.795
0.00
69.01
A


ATOM
13
OE1
GLN
A
73
67.785
−0.435
12.735
0.00
68.92
A


ATOM
14
NE2
GLN
A
73
65.571
−0.541
12.376
0.00
68.92
A


ATOM
15
C
GLN
A
73
68.057
−4.728
14.683
1.00
69.53
A


ATOM
16
O
GLN
A
73
67.267
−5.015
15.585
1.00
69.69
A


ATOM
17
N
PRO
A
74
69.313
−4.321
14.940
1.00
68.34
A


ATOM
18
CD
PRO
A
74
70.411
−4.026
13.999
1.00
67.68
A


ATOM
19
CA
PRO
A
74
69.769
−4.204
16.330
1.00
67.15
A


ATOM
20
CB
PRO
A
74
71.198
−3.675
16.178
1.00
67.56
A


ATOM
21
CG
PRO
A
74
71.635
−4.254
14.855
1.00
67.46
A


ATOM
22
C
PRO
A
74
68.866
−3.240
17.105
1.00
65.27
A


ATOM
23
O
PRO
A
74
68.496
−2.186
16.584
1.00
65.27
A


ATOM
24
N
ARG
A
75
68.506
−3.598
18.337
1.00
62.56
A


ATOM
25
CA
ARG
A
75
67.642
−2.730
19.136
1.00
59.53
A


ATOM
26
CB
ARG
A
75
67.543
−3.228
20.582
1.00
62.40
A


ATOM
27
CG
ARG
A
75
66.120
−3.565
21.023
1.00
64.22
A


ATOM
28
CD
ARG
A
75
66.020
−3.746
22.537
1.00
66.65
A


ATOM
29
NE
ARG
A
75
64.741
−4.332
22.943
1.00
68.76
A


ATOM
30
CZ
ARG
A
75
64.390
−4.572
24.204
1.00
70.18
A


ATOM
31
NH1
ARG
A
75
65.218
−4.272
25.197
1.00
70.31
A


ATOM
32
NH2
ARG
A
75
63.213
−5.125
24.477
1.00
71.64
A


ATOM
33
C
ARG
A
75
68.184
−1.306
19.126
1.00
55.61
A


ATOM
34
O
ARG
A
75
69.386
−1.082
18.961
1.00
55.58
A


ATOM
35
N
LYS
A
76
67.294
−0.341
19.295
1.00
50.06
A


ATOM
36
CA
LYS
A
76
67.704
1.050
19.297
1.00
45.50
A


ATOM
37
CB
LYS
A
76
66.498
1.941
19.594
1.00
45.42
A


ATOM
38
CG
LYS
A
76
66.404
3.192
18.735
1.00
45.70
A


ATOM
39
CD
LYS
A
76
66.329
2.829
17.257
1.00
44.53
A


ATOM
40
CE
LYS
A
76
66.030
4.045
16.396
1.00
44.45
A


ATOM
41
NZ
LYS
A
76
66.091
3.733
14.939
1.00
43.30
A


ATOM
42
C
LYS
A
76
68.783
1.251
20.359
1.00
42.73
A


ATOM
43
O
LYS
A
76
68.715
0.681
21.447
1.00
42.46
A


ATOM
44
N
LYS
A
77
69.793
2.046
20.038
1.00
39.63
A


ATOM
45
CA
LYS
A
77
70.851
2.309
20.995
1.00
36.33
A


ATOM
46
CB
LYS
A
77
72.139
2.670
20.267
1.00
36.33
A


ATOM
47
CG
LYS
A
77
72.655
1.570
19.353
1.00
36.55
A


ATOM
48
CD
LYS
A
77
74.005
1.945
18.785
1.00
35.61
A


ATOM
49
CE
LYS
A
77
74.491
0.932
17.766
1.00
38.34
A


ATOM
50
NZ
LYS
A
77
74.706
−0.419
18.354
1.00
38.65
A


ATOM
51
C
LYS
A
77
70.413
3.459
21.889
1.00
35.52
A


ATOM
52
O
LYS
A
77
69.475
4.190
21.557
1.00
32.62
A


ATOM
53
N
ARG
A
78
71.097
3.608
23.020
1.00
34.95
A


ATOM
54
CA
ARG
A
78
70.801
4.654
23.991
1.00
33.79
A


ATOM
55
CB
ARG
A
78
69.917
4.094
25.114
1.00
35.78
A


ATOM
56
CG
ARG
A
78
70.211
2.652
25.483
1.00
38.18
A


ATOM
57
CD
ARG
A
78
69.036
2.040
26.239
1.00
38.81
A


ATOM
58
NE
ARG
A
78
68.995
0.578
26.160
0.00
38.43
A


ATOM
59
CZ
ARG
A
78
69.889
−0.232
26.719
0.00
38.44
A


ATOM
60
NH1
ARG
A
78
70.906
0.274
27.401
0.00
38.37
A


ATOM
61
NH2
ARG
A
78
69.760
−1.549
26.610
0.00
38.37
A


ATOM
62
C
ARG
A
78
72.099
5.230
24.544
1.00
31.96
A


ATOM
63
O
ARG
A
78
73.133
4.576
24.515
1.00
32.75
A


ATOM
64
N
PRO
A
79
72.060
6.470
25.055
1.00
30.51
A


ATOM
65
CD
PRO
A
79
70.844
7.272
25.274
1.00
27.35
A


ATOM
66
CA
PRO
A
79
73.236
7.150
25.611
1.00
29.82
A


ATOM
67
CB
PRO
A
79
72.626
8.326
26.365
1.00
28.52
A


ATOM
68
CG
PRO
A
79
71.418
8.628
25.559
1.00
29.89
A


ATOM
69
C
PRO
A
79
74.129
6.298
26.510
1.00
30.92
A


ATOM
70
O
PRO
A
79
75.356
6.357
26.412
1.00
33.32
A


ATOM
71
N
GLU
A
80
73.516
5.510
27.383
1.00
29.85
A


ATOM
72
CA
GLU
A
80
74.273
4.677
28.300
1.00
31.98
A


ATOM
73
CB
GLU
A
80
73.327
3.941
29.242
1.00
34.31
A


ATOM
74
CG
GLU
A
80
72.697
2.710
28.622
1.00
41.92
A


ATOM
75
CD
GLU
A
80
71.205
2.626
28.872
1.00
44.52
A


ATOM
76
OE1
GLU
A
80
70.461
3.466
28.317
1.00
46.38
A


ATOM
77
OE2
GLU
A
80
70.780
1.721
29.625
1.00
46.03
A


ATOM
78
C
GLU
A
80
75.157
3.663
27.578
1.00
30.62
A


ATOM
79
O
GLU
A
80
76.101
3.144
28.170
1.00
30.21
A


ATOM
80
N
ASP
A
81
74.859
3.378
26.312
1.00
28.14
A


ATOM
81
CA
ASP
A
81
75.659
2.417
25.548
1.00
27.32
A


ATOM
82
CB
ASP
A
81
74.938
1.990
24.253
1.00
27.75
A


ATOM
83
CG
ASP
A
81
73.612
1.275
24.512
1.00
30.45
A


ATOM
84
OD1
ASP
A
81
73.495
0.549
25.525
1.00
30.76
A


ATOM
85
OD2
ASP
A
81
72.686
1.424
23.686
1.00
30.74
A


ATOM
86
C
ASP
A
81
77.026
2.990
25.166
1.00
26.35
A


ATOM
87
O
ASP
A
81
77.895
2.266
24.680
1.00
25.33
A


ATOM
88
N
PHE
A
82
77.217
4.283
25.404
1.00
24.95
A


ATOM
89
CA
PHE
A
82
78.457
4.948
25.035
1.00
23.57
A


ATOM
90
CB
PHE
A
82
78.168
6.040
23.991
1.00
23.02
A


ATOM
91
CG
PHE
A
82
77.507
5.534
22.742
1.00
23.64
A


ATOM
92
CD1
PHE
A
82
78.270
5.059
21.680
1.00
23.15
A


ATOM
93
CD2
PHE
A
82
76.123
5.504
22.640
1.00
23.41
A


ATOM
94
CE1
PHE
A
82
77.670
4.559
20.540
1.00
23.43
A


ATOM
95
CE2
PHE
A
82
75.504
5.003
21.498
1.00
24.29
A


ATOM
96
CZ
PHE
A
82
76.283
4.527
20.444
1.00
25.15
A


ATOM
97
C
PHE
A
82
79.199
5.609
26.186
1.00
24.39
A


ATOM
98
O
PHE
A
82
78.647
5.847
27.259
1.00
22.78
A


ATOM
99
N
LYS
A
83
80.471
5.896
25.932
1.00
22.40
A


ATOM
100
CA
LYS
A
83
81.294
6.615
26.869
1.00
23.38
A


ATOM
101
CB
LYS
A
83
82.554
5.834
27.250
1.00
24.29
A


ATOM
102
CG
LYS
A
83
83.453
6.594
28.227
1.00
27.32
A


ATOM
103
CD
LYS
A
83
84.411
5.675
28.988
1.00
31.40
A


ATOM
104
CE
LYS
A
83
85.321
4.906
28.044
0.00
30.06
A


ATOM
105
NZ
LYS
A
83
86.145
5.819
27.207
0.00
30.54
A


ATOM
106
C
LYS
A
83
81.656
7.847
26.046
1.00
24.47
A


ATOM
107
O
LYS
A
83
82.518
7.787
25.162
1.00
26.09
A


ATOM
108
N
PHE
A
84
80.965
8.951
26.309
1.00
21.59
A


ATOM
109
CA
PHE
A
84
81.211
10.182
25.583
1.00
21.61
A


ATOM
110
CB
PHE
A
84
80.073
11.169
25.811
1.00
20.62
A


ATOM
111
CG
PHE
A
84
78.794
10.757
25.159
1.00
20.05
A


ATOM
112
CD1
PHE
A
84
77.915
9.905
25.805
1.00
18.27
A


ATOM
113
CD2
PHE
A
84
78.498
11.176
23.868
1.00
19.96
A


ATOM
114
CE1
PHE
A
84
76.764
9.473
25.183
1.00
19.47
A


ATOM
115
CE2
PHE
A
84
77.346
10.748
23.233
1.00
21.09
A


ATOM
116
CZ
PHE
A
84
76.475
9.894
23.890
1.00
20.64
A


ATOM
117
C
PHE
A
84
82.525
10.820
25.966
1.00
22.27
A


ATOM
118
O
PHE
A
84
82.900
10.822
27.129
1.00
24.09
A


ATOM
119
N
GLY
A
85
83.213
11.371
24.972
1.00
22.72
A


ATOM
120
CA
GLY
A
85
84.496
12.007
25.203
1.00
22.66
A


ATOM
121
C
GLY
A
85
84.540
13.481
24.839
1.00
22.72
A


ATOM
122
O
GLY
A
85
83.622
14.228
25.158
1.00
22.51
A


ATOM
123
N
LYS
A
86
85.608
13.894
24.162
1.00
22.49
A


ATOM
124
CA
LYS
A
86
85.794
15.291
23.784
1.00
22.53
A


ATOM
125
CB
LYS
A
86
87.238
15.530
23.333
1.00
24.44
A


ATOM
126
CG
LYS
A
86
87.617
14.804
22.051
1.00
26.94
A


ATOM
127
CD
LYS
A
86
89.033
15.120
21.594
1.00
29.52
A


ATOM
128
CE
LYS
A
86
89.166
16.571
21.154
1.00
35.93
A


ATOM
129
NZ
LYS
A
86
90.505
16.892
20.553
1.00
38.21
A


ATOM
130
C
LYS
A
86
84.857
15.798
22.699
1.00
23.09
A


ATOM
131
O
LYS
A
86
84.295
15.032
21.923
1.00
22.85
A


ATOM
132
N
ILE
A
87
84.702
17.114
22.664
1.00
22.28
A


ATOM
133
CA
ILE
A
87
83.867
17.780
21.683
1.00
21.22
A


ATOM
134
CB
ILE
A
87
83.429
19.170
22.204
1.00
22.05
A


ATOM
135
CG2
ILE
A
87
82.792
19.993
21.076
1.00
17.65
A


ATOM
136
CG1
ILE
A
87
82.493
18.998
23.406
1.00
21.65
A


ATOM
137
CD1
ILE
A
87
82.159
20.300
24.118
1.00
18.47
A


ATOM
138
C
ILE
A
87
84.707
17.963
20.418
1.00
21.83
A


ATOM
139
O
ILE
A
87
85.782
18.543
20.470
1.00
21.99
A


ATOM
140
N
LEU
A
88
84.226
17.463
19.288
1.00
22.57
A


ATOM
141
CA
LEU
A
88
84.964
17.614
18.039
1.00
22.76
A


ATOM
142
CB
LEU
A
88
84.586
16.515
17.044
1.00
20.65
A


ATOM
143
CG
LEU
A
88
84.899
15.107
17.535
1.00
20.09
A


ATOM
144
CD1
LEU
A
88
84.455
14.082
16.502
1.00
17.42
A


ATOM
145
CD2
LEU
A
88
86.392
15.004
17.813
1.00
17.76
A


ATOM
146
C
LEU
A
88
84.657
18.964
17.428
1.00
23.53
A


ATOM
147
O
LEU
A
88
85.512
19.577
16.794
1.00
24.73
A


ATOM
148
N
GLY
A
89
83.430
19.428
17.619
1.00
24.20
A


ATOM
149
CA
GLY
A
89
83.057
20.710
17.062
1.00
28.57
A


ATOM
150
C
GLY
A
89
81.649
21.131
17.431
1.00
32.57
A


ATOM
151
O
GLY
A
89
80.834
20.318
17.882
1.00
32.78
A


ATOM
152
N
GLU
A
90
81.363
22.412
17.224
1.00
35.17
A


ATOM
153
CA
GLU
A
90
80.063
22.964
17.542
1.00
39.17
A


ATOM
154
CB
GLU
A
90
80.168
23.853
18.784
1.00
41.47
A


ATOM
155
CG
GLU
A
90
80.112
23.061
20.082
1.00
47.18
A


ATOM
156
CD
GLU
A
90
80.422
23.893
21.313
1.00
50.49
A


ATOM
157
OE1
GLU
A
90
81.610
24.228
21.526
1.00
51.41
A


ATOM
158
OE2
GLU
A
90
79.476
24.210
22.067
1.00
53.44
A


ATOM
159
C
GLU
A
90
79.436
23.743
16.402
1.00
40.69
A


ATOM
160
O
GLU
A
90
80.110
24.185
15.471
1.00
40.64
A


ATOM
161
N
GLY
A
91
78.121
23.881
16.488
1.00
42.58
A


ATOM
162
CA
GLY
A
91
77.363
24.618
15.503
1.00
43.40
A


ATOM
163
C
GLY
A
91
76.303
25.335
16.306
1.00
44.83
A


ATOM
164
O
GLY
A
91
76.154
25.083
17.507
1.00
43.64
A


ATOM
165
N
SER
A
92
75.579
26.244
15.669
1.00
47.22
A


ATOM
166
CA
SER
A
92
74.522
26.969
16.366
1.00
48.94
A


ATOM
167
CB
SER
A
92
73.961
28.066
15.461
1.00
51.50
A


ATOM
168
OG
SER
A
92
73.663
27.541
14.175
1.00
54.98
A


ATOM
169
C
SER
A
92
73.454
25.928
16.625
1.00
47.87
A


ATOM
170
O
SER
A
92
72.745
25.950
17.635
1.00
47.78
A


ATOM
171
N
PHE
A
93
73.392
24.994
15.689
1.00
46.49
A


ATOM
172
CA
PHE
A
93
72.434
23.909
15.697
1.00
46.02
A


ATOM
173
CB
PHE
A
93
72.297
23.369
14.263
1.00
49.54
A


ATOM
174
CG
PHE
A
93
73.588
23.398
13.459
1.00
50.29
A


ATOM
175
CD1
PHE
A
93
74.301
22.229
13.209
1.00
52.29
A


ATOM
176
CD2
PHE
A
93
74.058
24.593
12.915
1.00
51.94
A


ATOM
177
CE1
PHE
A
93
75.459
22.245
12.424
1.00
52.28
A


ATOM
178
CE2
PHE
A
93
75.209
24.622
12.135
1.00
52.58
A


ATOM
179
CZ
PHE
A
93
75.911
23.443
11.887
1.00
53.99
A


ATOM
180
C
PHE
A
93
72.700
22.754
16.662
1.00
43.48
A


ATOM
181
O
PHE
A
93
71.772
22.245
17.292
1.00
42.15
A


ATOM
182
N
SER
A
94
73.955
22.343
16.796
1.00
39.99
A


ATOM
183
CA
SER
A
94
74.245
21.206
17.655
1.00
36.12
A


ATOM
184
CB
SER
A
94
73.839
19.937
16.921
1.00
38.79
A


ATOM
185
OG
SER
A
94
74.549
19.863
15.695
1.00
40.39
A


ATOM
186
C
SER
A
94
75.697
21.066
18.083
1.00
32.29
A


ATOM
187
O
SER
A
94
76.513
21.962
17.890
1.00
30.04
A


ATOM
188
N
THR
A
95
76.006
19.909
18.655
1.00
28.50
A


ATOM
189
CA
THR
A
95
77.350
19.614
19.116
1.00
26.86
A


ATOM
190
CB
THR
A
95
77.432
19.642
20.652
1.00
27.90
A


ATOM
191
OG1
THR
A
95
76.907
20.882
21.136
1.00
32.56
A


ATOM
192
CG2
THR
A
95
78.874
19.502
21.112
1.00
27.77
A


ATOM
193
C
THR
A
95
77.757
18.225
18.653
1.00
23.70
A


ATOM
194
O
THR
A
95
76.971
17.287
18.724
1.00
24.35
A


ATOM
195
N
VAL
A
96
78.991
18.100
18.184
1.00
22.75
A


ATOM
196
CA
VAL
A
96
79.505
16.813
17.733
1.00
20.60
A


ATOM
197
CB
VAL
A
96
80.139
16.909
16.336
1.00
17.79
A


ATOM
198
CG1
VAL
A
96
80.625
15.530
15.898
1.00
18.21
A


ATOM
199
CG2
VAL
A
96
79.131
17.447
15.344
1.00
13.79
A


ATOM
200
C
VAL
A
96
80.566
16.351
18.716
1.00
21.23
A


ATOM
201
O
VAL
A
96
81.600
17.006
18.889
1.00
22.12
A


ATOM
202
N
VAL
A
97
80.310
15.220
19.362
1.00
22.06
A


ATOM
203
CA
VAL
A
97
81.244
14.690
20.345
1.00
24.07
A


ATOM
204
CB
VAL
A
97
80.592
14.680
21.743
1.00
24.91
A


ATOM
205
CG1
VAL
A
97
79.199
14.124
21.649
1.00
28.97
A


ATOM
206
CG2
VAL
A
97
81.422
13.859
22.715
1.00
27.97
A


ATOM
207
C
VAL
A
97
81.748
13.298
20.002
1.00
23.47
A


ATOM
208
O
VAL
A
97
81.017
12.491
19.436
1.00
26.62
A


ATOM
209
N
LEU
A
98
83.007
13.024
20.329
1.00
22.92
A


ATOM
210
CA
LEU
A
98
83.586
11.713
20.063
1.00
23.27
A


ATOM
211
CB
LEU
A
98
85.117
11.777
20.110
1.00
21.94
A


ATOM
212
CG
LEU
A
98
85.932
10.495
19.854
1.00
22.83
A


ATOM
213
CD1
LEU
A
98
85.606
9.924
18.486
1.00
23.24
A


ATOM
214
CD2
LEU
A
98
87.422
10.802
19.945
1.00
21.21
A


ATOM
215
C
LEU
A
98
83.069
10.782
21.144
1.00
23.95
A


ATOM
216
O
LEU
A
98
83.143
11.099
22.322
1.00
26.02
A


ATOM
217
N
ALA
A
99
82.523
9.645
20.738
1.00
24.41
A


ATOM
218
CA
ALA
A
99
81.999
8.677
21.686
1.00
23.76
A


ATOM
219
CB
ALA
A
99
80.485
8.692
21.668
1.00
20.64
A


ATOM
220
C
ALA
A
99
82.502
7.282
21.357
1.00
26.42
A


ATOM
221
O
ALA
A
99
82.792
6.951
20.195
1.00
26.78
A


ATOM
222
N
ARG
A
100
82.602
6.462
22.394
1.00
26.77
A


ATOM
223
CA
ARG
A
100
83.055
5.094
22.238
1.00
26.80
A


ATOM
224
CB
ARG
A
100
84.362
4.897
23.001
1.00
28.29
A


ATOM
225
CG
ARG
A
100
84.967
3.522
22.853
1.00
33.87
A


ATOM
226
CD
ARG
A
100
86.281
3.447
23.617
1.00
38.01
A


ATOM
227
NE
ARG
A
100
87.337
4.240
22.983
1.00
41.22
A


ATOM
228
CZ
ARG
A
100
87.932
3.917
21.837
1.00
41.46
A


ATOM
229
NH1
ARG
A
100
87.580
2.813
21.190
1.00
41.28
A


ATOM
230
NH2
ARG
A
100
88.887
4.692
21.339
1.00
43.39
A


ATOM
231
C
ARG
A
100
81.970
4.167
22.770
1.00
24.32
A


ATOM
232
O
ARG
A
100
81.583
4.251
23.934
1.00
25.42
A


ATOM
233
N
GLU
A
101
81.456
3.308
21.900
1.00
22.41
A


ATOM
234
CA
GLU
A
101
80.417
2.367
22.281
1.00
22.87
A


ATOM
235
CB
GLU
A
101
79.787
1.775
21.025
1.00
21.96
A


ATOM
236
CG
GLU
A
101
78.819
0.652
21.292
1.00
24.68
A


ATOM
237
CD
GLU
A
101
78.203
0.137
20.018
1.00
28.27
A


ATOM
238
OE1
GLU
A
101
78.965
−0.113
19.057
1.00
28.96
A


ATOM
239
OE2
GLU
A
101
76.963
−0.022
19.971
1.00
29.77
A


ATOM
240
C
GLU
A
101
81.015
1.261
23.151
1.00
23.59
A


ATOM
241
O
GLU
A
101
81.945
0.574
22.738
1.00
24.80
A


ATOM
242
N
LEU
A
102
80.475
1.088
24.351
1.00
26.09
A


ATOM
243
CA
LEU
A
102
80.982
0.083
25.289
1.00
28.74
A


ATOM
244
CB
LEU
A
102
80.173
0.110
26.593
1.00
30.16
A


ATOM
245
CG
LEU
A
102
80.347
1.308
27.532
1.00
34.19
A


ATOM
246
CD1
LEU
A
102
81.824
1.692
27.599
1.00
33.27
A


ATOM
247
CD2
LEU
A
102
79.527
2.477
27.046
1.00
34.46
A


ATOM
248
C
LEU
A
102
81.042
−1.359
24.791
1.00
28.32
A


ATOM
249
O
LEU
A
102
82.067
−2.024
24.916
1.00
29.83
A


ATOM
250
N
ALA
A
103
79.948
−1.841
24.226
1.00
27.34
A


ATOM
251
CA
ALA
A
103
79.887
−3.218
23.763
1.00
27.81
A


ATOM
252
CB
ALA
A
103
78.466
−3.549
23.367
1.00
27.48
A


ATOM
253
C
ALA
A
103
80.828
−3.593
22.624
1.00
27.42
A


ATOM
254
O
ALA
A
103
81.172
−4.765
22.463
1.00
28.68
A


ATOM
255
N
THR
A
104
81.257
−2.612
21.842
1.00
24.97
A


ATOM
256
CA
THR
A
104
82.105
−2.907
20.695
1.00
23.79
A


ATOM
257
CB
THR
A
104
81.441
−2.472
19.393
1.00
22.01
A


ATOM
258
OG1
THR
A
104
81.355
−1.041
19.379
1.00
23.91
A


ATOM
259
CG2
THR
A
104
80.051
−3.069
19.261
1.00
17.30
A


ATOM
260
C
THR
A
104
83.444
−2.221
20.712
1.00
25.00
A


ATOM
261
O
THR
A
104
84.350
−2.616
19.972
1.00
25.02
A


ATOM
262
N
SER
A
105
83.551
−1.172
21.525
1.00
24.89
A


ATOM
263
CA
SER
A
105
84.775
−0.394
21.616
1.00
24.55
A


ATOM
264
CB
SER
A
105
85.979
−1.334
21.732
1.00
26.36
A


ATOM
265
OG
SER
A
105
87.143
−0.621
22.090
1.00
32.45
A


ATOM
266
C
SER
A
105
84.916
0.514
20.374
1.00
23.38
A


ATOM
267
O
SER
A
105
85.931
1.175
20.188
1.00
24.92
A


ATOM
268
N
ARG
A
106
83.888
0.546
19.531
1.00
20.51
A


ATOM
269
CA
ARG
A
106
83.906
1.372
18.323
1.00
19.31
A


ATOM
270
CB
ARG
A
106
82.778
0.947
17.370
1.00
19.05
A


ATOM
271
CG
ARG
A
106
83.099
−0.283
16.520
1.00
15.69
A


ATOM
272
CD
ARG
A
106
81.853
−0.804
15.832
1.00
19.45
A


ATOM
273
NE
ARG
A
106
82.144
−1.838
14.846
1.00
20.98
A


ATOM
274
CZ
ARG
A
106
81.234
−2.673
14.354
1.00
21.77
A


ATOM
275
NH1
ARG
A
106
79.974
−2.599
14.768
1.00
19.65
A


ATOM
276
NH2
ARG
A
106
81.577
−3.560
13.427
1.00
21.43
A


ATOM
277
C
ARG
A
106
83.760
2.858
18.624
1.00
17.84
A


ATOM
278
O
ARG
A
106
83.022
3.234
19.525
1.00
15.87
A


ATOM
279
N
GLU
A
107
84.463
3.691
17.863
1.00
18.23
A


ATOM
280
CA
GLU
A
107
84.395
5.144
18.039
1.00
22.75
A


ATOM
281
CB
GLU
A
107
85.773
5.800
17.929
1.00
23.58
A


ATOM
282
CG
GLU
A
107
86.828
5.254
18.859
1.00
32.15
A


ATOM
283
CD
GLU
A
107
88.066
6.131
18.878
1.00
35.04
A


ATOM
284
OE1
GLU
A
107
88.145
7.019
19.755
1.00
36.99
A


ATOM
285
OE2
GLU
A
107
88.949
5.944
18.007
1.00
37.54
A


ATOM
286
C
GLU
A
107
83.514
5.787
16.982
1.00
21.00
A


ATOM
287
O
GLU
A
107
83.709
5.577
15.787
1.00
21.37
A


ATOM
288
N
TYR
A
108
82.570
6.593
17.437
1.00
19.48
A


ATOM
289
CA
TYR
A
108
81.652
7.298
16.559
1.00
18.30
A


ATOM
290
CB
TYR
A
108
80.228
6.791
16.754
1.00
17.52
A


ATOM
291
CG
TYR
A
108
79.993
5.373
16.309
1.00
22.75
A


ATOM
292
CD1
TYR
A
108
79.727
5.075
14.972
1.00
20.94
A


ATOM
293
CE1
TYR
A
108
79.492
3.765
14.571
1.00
23.91
A


ATOM
294
CD2
TYR
A
108
80.019
4.324
17.231
1.00
19.41
A


ATOM
295
CE2
TYR
A
108
79.788
3.026
16.845
1.00
19.33
A


ATOM
296
CZ
TYR
A
108
79.527
2.744
15.521
1.00
23.13
A


ATOM
297
OH
TYR
A
108
79.333
1.438
15.143
1.00
23.65
A


ATOM
298
C
TYR
A
108
81.660
8.777
16.906
1.00
18.00
A


ATOM
299
O
TYR
A
108
81.929
9.161
18.046
1.00
18.12
A


ATOM
300
N
ALA
A
109
81.370
9.603
15.912
1.00
17.20
A


ATOM
301
CA
ALA
A
109
81.274
11.036
16.114
1.00
15.30
A


ATOM
302
CB
ALA
A
109
81.853
11.784
14.928
1.00
13.44
A


ATOM
303
C
ALA
A
109
79.759
11.205
16.178
1.00
17.20
A


ATOM
304
O
ALA
A
109
79.056
11.019
15.179
1.00
17.23
A


ATOM
305
N
ILE
A
110
79.250
11.522
17.362
1.00
17.40
A


ATOM
306
CA
ILE
A
110
77.814
11.654
17.542
1.00
17.60
A


ATOM
307
CB
ILE
A
110
77.380
10.957
18.842
1.00
16.56
A


ATOM
308
CG2
ILE
A
110
75.906
11.236
19.119
1.00
14.97
A


ATOM
309
CG1
ILE
A
110
77.672
9.453
18.728
1.00
14.02
A


ATOM
310
CD1
ILE
A
110
77.197
8.632
19.907
1.00
11.93
A


ATOM
311
C
ILE
A
110
77.306
13.089
17.548
1.00
19.83
A


ATOM
312
O
ILE
A
110
77.690
13.892
18.396
1.00
20.84
A


ATOM
313
N
LYS
A
111
76.444
13.415
16.597
1.00
18.58
A


ATOM
314
CA
LYS
A
111
75.902
14.761
16.551
1.00
20.88
A


ATOM
315
CB
LYS
A
111
75.455
15.115
15.131
1.00
21.39
A


ATOM
316
CG
LYS
A
111
75.016
16.558
14.975
1.00
24.84
A


ATOM
317
CD
LYS
A
111
75.005
16.971
13.516
1.00
27.43
A


ATOM
318
CE
LYS
A
111
74.426
18.359
13.343
1.00
28.44
A


ATOM
319
NZ
LYS
A
111
74.619
18.871
11.972
1.00
28.27
A


ATOM
320
C
LYS
A
111
74.724
14.819
17.507
1.00
20.66
A


ATOM
321
O
LYS
A
111
73.797
14.008
17.410
1.00
20.23
A


ATOM
322
N
ILE
A
112
74.772
15.765
18.441
1.00
20.09
A


ATOM
323
CA
ILE
A
112
73.704
15.914
19.426
1.00
23.02
A


ATOM
324
CB
ILE
A
112
74.261
15.882
20.863
1.00
24.20
A


ATOM
325
CG2
ILE
A
112
73.116
15.765
21.864
1.00
21.42
A


ATOM
326
CG1
ILE
A
112
75.206
14.692
21.023
1.00
24.14
A


ATOM
327
CD1
ILE
A
112
75.893
14.634
22.375
1.00
26.83
A


ATOM
328
C
ILE
A
112
72.962
17.225
19.221
1.00
22.53
A


ATOM
329
O
ILE
A
112
73.573
18.286
19.132
1.00
21.31
A


ATOM
330
N
LEU
A
113
71.641
17.138
19.150
1.00
24.04
A


ATOM
331
CA
LEU
A
113
70.800
18.313
18.940
1.00
25.81
A


ATOM
332
CB
LEU
A
113
70.135
18.264
17.555
1.00
24.66
A


ATOM
333
CG
LEU
A
113
70.988
18.095
16.295
1.00
26.73
A


ATOM
334
CD1
LEU
A
113
71.316
16.620
16.093
1.00
24.51
A


ATOM
335
CD2
LEU
A
113
70.234
18.637
15.083
1.00
26.16
A


ATOM
336
C
LEU
A
113
69.702
18.400
19.994
1.00
27.62
A


ATOM
337
O
LEU
A
113
69.053
17.398
20.314
1.00
29.70
A


ATOM
338
N
GLU
A
114
69.491
19.597
20.530
1.00
29.32
A


ATOM
339
CA
GLU
A
114
68.445
19.806
21.526
1.00
31.56
A


ATOM
340
CB
GLU
A
114
68.775
21.020
22.391
1.00
34.85
A


ATOM
341
CG
GLU
A
114
67.680
21.357
23.392
1.00
42.32
A


ATOM
342
CD
GLU
A
114
67.922
22.670
24.108
1.00
45.56
A


ATOM
343
OE1
GLU
A
114
68.086
23.700
23.417
1.00
48.01
A


ATOM
344
OE2
GLU
A
114
67.941
22.673
25.359
1.00
48.10
A


ATOM
345
C
GLU
A
114
67.107
20.036
20.816
1.00
31.02
A


ATOM
346
O
GLU
A
114
66.926
21.049
20.140
1.00
30.39
A


ATOM
347
N
LYS
A
115
66.176
19.099
20.967
1.00
30.58
A


ATOM
348
CA
LYS
A
115
64.872
19.218
20.321
1.00
31.63
A


ATOM
349
CB
LYS
A
115
63.964
18.049
20.734
1.00
28.91
A


ATOM
350
CG
LYS
A
115
64.287
16.742
20.003
1.00
28.07
A


ATOM
351
CD
LYS
A
115
63.356
15.580
20.368
1.00
23.95
A


ATOM
352
CE
LYS
A
115
63.713
14.960
21.707
1.00
23.89
A


ATOM
353
NZ
LYS
A
115
62.860
13.782
22.020
1.00
24.15
A


ATOM
354
C
LYS
A
115
64.165
20.551
20.591
1.00
33.78
A


ATOM
355
O
LYS
A
115
63.495
21.100
19.711
1.00
33.61
A


ATOM
356
N
ARG
A
116
64.325
21.076
21.801
1.00
35.55
A


ATOM
357
CA
ARG
A
116
63.682
22.332
22.176
1.00
38.66
A


ATOM
358
CB
ARG
A
116
63.932
22.627
23.663
1.00
42.20
A


ATOM
359
CG
ARG
A
116
62.949
23.603
24.302
1.00
47.35
A


ATOM
360
CD
ARG
A
116
63.670
24.685
25.109
1.00
52.44
A


ATOM
361
NE
ARG
A
116
64.526
24.141
26.166
1.00
56.30
A


ATOM
362
CZ
ARG
A
116
64.142
23.920
27.423
1.00
57.97
A


ATOM
363
NH1
ARG
A
116
62.899
24.199
27.808
1.00
58.89
A


ATOM
364
NH2
ARG
A
116
65.006
23.420
28.300
1.00
56.55
A


ATOM
365
C
ARG
A
116
64.227
23.472
21.323
1.00
37.67
A


ATOM
366
O
ARG
A
116
63.474
24.246
20.735
1.00
36.66
A


ATOM
367
N
HIS
A
117
65.550
23.555
21.259
1.00
37.78
A


ATOM
368
CA
HIS
A
117
66.236
24.590
20.501
1.00
35.88
A


ATOM
369
CB
HIS
A
117
67.744
24.417
20.676
1.00
35.60
A


ATOM
370
CG
HIS
A
117
68.560
25.532
20.101
1.00
37.06
A


ATOM
371
CD2
HIS
A
117
69.508
25.535
19.134
1.00
38.11
A


ATOM
372
ND1
HIS
A
117
68.469
26.831
20.550
1.00
37.56
A


ATOM
373
CE1
HIS
A
117
69.325
27.587
19.886
1.00
38.35
A


ATOM
374
NE2
HIS
A
117
69.969
26.825
19.021
1.00
38.67
A


ATOM
375
C
HIS
A
117
65.859
24.529
19.024
1.00
34.83
A


ATOM
376
O
HIS
A
117
65.600
25.554
18.398
1.00
35.80
A


ATOM
377
N
ILE
A
118
65.827
23.321
18.474
1.00
33.01
A


ATOM
378
CA
ILE
A
118
65.483
23.122
17.071
1.00
32.12
A


ATOM
379
CB
ILE
A
118
65.575
21.629
16.692
1.00
33.37
A


ATOM
380
CG2
ILE
A
118
64.968
21.398
15.312
1.00
33.44
A


ATOM
381
CG1
ILE
A
118
67.032
21.168
16.732
1.00
33.47
A


ATOM
382
CD1
ILE
A
118
67.195
19.685
16.479
1.00
35.01
A


ATOM
383
C
ILE
A
118
64.066
23.603
16.760
1.00
31.17
A


ATOM
384
O
ILE
A
118
63.838
24.295
15.774
1.00
29.39
A


ATOM
385
N
ILE
A
119
63.117
23.209
17.600
1.00
31.17
A


ATOM
386
CA
ILE
A
119
61.725
23.590
17.420
1.00
31.73
A


ATOM
387
CB
ILE
A
119
60.841
22.896
18.473
1.00
31.45
A


ATOM
388
CG2
ILE
A
119
59.471
23.560
18.548
1.00
26.98
A


ATOM
389
CG1
ILE
A
119
60.735
21.409
18.131
1.00
27.55
A


ATOM
390
CD1
ILE
A
119
60.092
20.574
19.205
1.00
26.52
A


ATOM
391
C
ILE
A
119
61.549
25.100
17.519
1.00
33.53
A


ATOM
392
O
ILE
A
119
60.879
25.714
16.688
1.00
32.81
A


ATOM
393
N
ALA
A
120
62.165
25.691
18.535
1.00
34.30
A


ATOM
394
CA
ALA
A
120
62.078
27.125
18.749
1.00
34.63
A


ATOM
395
CB
ALA
A
120
62.811
27.506
20.029
1.00
35.03
A


ATOM
396
C
ALA
A
120
62.657
27.889
17.574
1.00
35.68
A


ATOM
397
O
ALA
A
120
62.141
28.938
17.195
1.00
36.85
A


ATOM
398
N
GLU
A
121
63.732
27.369
16.995
1.00
35.66
A


ATOM
399
CA
GLU
A
121
64.375
28.041
15.870
1.00
36.43
A


ATOM
400
CB
GLU
A
121
65.873
27.726
15.864
1.00
40.99
A


ATOM
401
CG
GLU
A
121
66.637
28.166
17.116
1.00
45.01
A


ATOM
402
CD
GLU
A
121
66.844
29.676
17.205
1.00
48.12
A


ATOM
403
OE1
GLU
A
121
67.670
30.104
18.043
1.00
49.33
A


ATOM
404
OE2
GLU
A
121
66.188
30.433
16.451
1.00
49.20
A


ATOM
405
C
GLU
A
121
63.780
27.670
14.512
1.00
34.98
A


ATOM
406
O
GLU
A
121
64.282
28.105
13.480
1.00
34.50
A


ATOM
407
N
ASN
A
122
62.716
26.869
14.517
1.00
33.68
A


ATOM
408
CA
ASN
A
122
62.060
26.434
13.286
1.00
32.99
A


ATOM
409
CB
ASN
A
122
61.492
27.639
12.530
1.00
35.58
A


ATOM
410
CG
ASN
A
122
60.424
28.373
13.315
1.00
38.88
A


ATOM
411
OD1
ASN
A
122
60.717
29.154
14.227
1.00
38.30
A


ATOM
412
ND2
ASN
A
122
59.170
28.116
12.970
1.00
38.77
A


ATOM
413
C
ASN
A
122
63.024
25.679
12.367
1.00
31.80
A


ATOM
414
O
ASN
A
122
63.095
25.957
11.172
1.00
30.78
A


ATOM
415
N
LYS
A
123
63.754
24.716
12.919
1.00
29.93
A


ATOM
416
CA
LYS
A
123
64.717
23.966
12.120
1.00
29.87
A


ATOM
417
CB
LYS
A
123
66.100
24.016
12.775
1.00
30.75
A


ATOM
418
CG
LYS
A
123
66.669
25.406
12.895
1.00
33.94
A


ATOM
419
CD
LYS
A
123
66.810
26.049
11.527
1.00
37.59
A


ATOM
420
CE
LYS
A
123
67.354
27.466
11.646
1.00
39.07
A


ATOM
421
NZ
LYS
A
123
67.460
28.121
10.310
1.00
41.71
A


ATOM
422
C
LYS
A
123
64.337
22.514
11.880
1.00
27.38
A


ATOM
423
O
LYS
A
123
65.139
21.745
11.355
1.00
24.93
A


ATOM
424
N
VAL
A
124
63.124
22.132
12.260
1.00
24.22
A


ATOM
425
CA
VAL
A
124
62.716
20.756
12.062
1.00
22.73
A


ATOM
426
CB
VAL
A
124
61.235
20.559
12.416
1.00
22.36
A


ATOM
427
CG1
VAL
A
124
60.794
19.146
12.064
1.00
22.84
A


ATOM
428
CG2
VAL
A
124
61.031
20.802
13.905
1.00
20.63
A


ATOM
429
C
VAL
A
124
62.981
20.320
10.623
1.00
23.50
A


ATOM
430
O
VAL
A
124
63.633
19.297
10.385
1.00
21.86
A


ATOM
431
N
PRO
A
125
62.512
21.109
9.639
1.00
23.91
A


ATOM
432
CD
PRO
A
125
61.806
22.399
9.725
1.00
24.52
A


ATOM
433
CA
PRO
A
125
62.737
20.736
8.239
1.00
24.57
A


ATOM
434
CB
PRO
A
125
62.147
21.914
7.464
1.00
23.69
A


ATOM
435
CG
PRO
A
125
61.098
22.450
8.400
1.00
25.18
A


ATOM
436
C
PRO
A
125
64.217
20.520
7.923
1.00
23.84
A


ATOM
437
O
PRO
A
125
64.568
19.618
7.172
1.00
22.92
A


ATOM
438
N
TYR
A
126
65.073
21.353
8.501
1.00
24.86
A


ATOM
439
CA
TYR
A
126
66.511
21.259
8.274
1.00
28.10
A


ATOM
440
CB
TYR
A
126
67.202
22.494
8.859
1.00
32.76
A


ATOM
441
CG
TYR
A
126
66.802
23.766
8.146
1.00
39.46
A


ATOM
442
CD1
TYR
A
126
67.466
24.179
6.987
1.00
42.04
A


ATOM
443
CE1
TYR
A
126
67.063
25.322
6.292
1.00
43.67
A


ATOM
444
CD2
TYR
A
126
65.722
24.531
8.597
1.00
42.16
A


ATOM
445
CE2
TYR
A
126
65.309
25.673
7.909
1.00
43.70
A


ATOM
446
CZ
TYR
A
126
65.983
26.062
6.758
1.00
44.51
A


ATOM
447
OH
TYR
A
126
65.570
27.183
6.068
1.00
45.30
A


ATOM
448
C
TYR
A
126
67.115
19.984
8.852
1.00
26.14
A


ATOM
449
O
TYR
A
126
67.768
19.225
8.141
1.00
26.15
A


ATOM
450
N
VAL
A
127
66.891
19.756
10.141
1.00
24.35
A


ATOM
451
CA
VAL
A
127
67.396
18.568
10.819
1.00
24.93
A


ATOM
452
CB
VAL
A
127
66.956
18.568
12.296
1.00
24.24
A


ATOM
453
CG1
VAL
A
127
67.444
17.316
12.997
1.00
23.36
A


ATOM
454
CG2
VAL
A
127
67.492
19.809
12.979
1.00
21.11
A


ATOM
455
C
VAL
A
127
66.894
17.290
10.130
1.00
25.81
A


ATOM
456
O
VAL
A
127
67.655
16.351
9.903
1.00
25.79
A


ATOM
457
N
THR
A
128
65.612
17.273
9.793
1.00
25.57
A


ATOM
458
CA
THR
A
128
64.996
16.136
9.114
1.00
26.36
A


ATOM
459
CB
THR
A
128
63.486
16.384
8.908
1.00
25.21
A


ATOM
460
OG1
THR
A
128
62.827
16.390
10.181
1.00
29.29
A


ATOM
461
CG2
THR
A
128
62.883
15.317
8.043
1.00
25.73
A


ATOM
462
C
THR
A
128
65.640
15.898
7.748
1.00
26.97
A


ATOM
463
O
THR
A
128
65.929
14.760
7.366
1.00
25.68
A


ATOM
464
N
ARG
A
129
65.854
16.980
7.012
1.00
27.23
A


ATOM
465
CA
ARG
A
129
66.462
16.897
5.692
1.00
29.37
A


ATOM
466
CB
ARG
A
129
66.484
18.282
5.032
1.00
32.35
A


ATOM
467
CG
ARG
A
129
66.936
18.280
3.583
1.003
6.81
A


ATOM
468
CD
ARG
A
129
67.208
19.693
3.064
1.00
40.45
A


ATOM
469
NE
ARG
A
129
66.178
20.651
3.459
1.00
44.54
A


ATOM
470
CZ
ARG
A
129
64.874
20.474
3.268
1.00
48.21
A


ATOM
471
NH1
ARG
A
129
64.431
19.366
2.681
1.00
50.01
A


ATOM
472
NH2
ARG
A
129
64.008
21.403
3.668
1.00
47.79
A


ATOM
473
C
ARG
A
129
67.884
16.379
5.828
1.00
28.98
A


ATOM
474
O
ARG
A
129
68.316
15.532
5.054
1.00
28.26
A


ATOM
475
N
GLU
A
130
68.606
16.895
6.822
1.00
29.28
A


ATOM
476
CA
GLU
A
130
69.988
16.490
7.057
1.00
30.58
A


ATOM
477
CB
GLU
A
130
70.556
17.203
8.287
1.00
34.18
A


ATOM
478
CG
GLU
A
130
72.078
17.220
8.344
1.00
38.81
A


ATOM
479
CD
GLU
A
130
72.633
17.650
9.702
1.00
41.66
A


ATOM
480
OE1
GLU
A
130
71.946
18.408
10.427
1.00
42.36
A


ATOM
481
OE2
GLU
A
130
73.771
17.236
10.035
1.00
42.31
A


ATOM
482
C
GLU
A
130
70.063
14.984
7.273
1.00
30.12
A


ATOM
483
O
GLU
A
130
70.861
14.298
6.638
1.00
29.62
A


ATOM
484
N
ARG
A
131
69.228
14.474
8.173
1.00
29.21
A


ATOM
485
CA
ARG
A
131
69.215
13.046
8.458
1.00
30.93
A


ATOM
486
CB
ARG
A
131
68.241
12.724
9.601
1.00
32.88
A


ATOM
487
CG
ARG
A
131
68.035
11.223
9.795
1.00
36.48
A


ATOM
488
CD
ARG
A
131
67.069
10.885
10.922
1.00
41.14
A


ATOM
489
NE
ARG
A
131
66.859
9.440
11.012
1.00
45.98
A


ATOM
490
CZ
ARG
A
131
66.167
8.833
11.974
1.00
48.77
A


ATOM
491
NH1
ARG
A
131
65.605
9.546
12.946
1.00
48.39
A


ATOM
492
NH2
ARG
A
131
66.045
7.509
11.968
1.00
48.16
A


ATOM
493
C
ARG
A
131
68.836
12.226
7.224
1.00
29.97
A


ATOM
494
O
ARG
A
131
69.398
11.157
6.986
1.00
28.24
A


ATOM
495
N
ASP
A
132
67.889
12.725
6.437
1.00
28.56
A


ATOM
496
CA
ASP
A
132
67.460
11.996
5.251
1.00
29.18
A


ATOM
497
CB
ASP
A
132
66.160
12.583
4.710
1.00
31.39
A


ATOM
498
CG
ASP
A
132
65.005
12.409
5.682
1.00
38.76
A


ATOM
499
OD1
ASP
A
132
64.892
11.319
6.283
1.00
40.09
A


ATOM
500
OD2
ASP
A
132
64.206
13.355
5.846
1.00
44.19
A


ATOM
501
C
ASP
A
132
68.510
11.936
4.150
1.00
27.67
A


ATOM
502
O
ASP
A
132
68.688
10.896
3.522
1.00
27.56
A


ATOM
503
N
VAL
A
133
69.200
13.044
3.909
1.00
26.09
A


ATOM
504
CA
VAL
A
133
70.232
13.063
2.886
1.00
25.09
A


ATOM
505
CB
VAL
A
133
70.859
14.459
2.742
1.00
25.26
A


ATOM
506
CG1
VAL
A
133
72.157
14.369
1.961
1.00
24.32
A


ATOM
507
CG2
VAL
A
133
69.890
15.390
2.029
1.00
24.76
A


ATOM
508
C
VAL
A
133
71.320
12.076
3.266
1.00
25.33
A


ATOM
509
O
VAL
A
133
71.742
11.270
2.445
1.00
23.59
A


ATOM
510
N
MET
A
134
71.764
12.138
4.520
1.00
26.01
A


ATOM
511
CA
MET
A
134
72.812
11.243
4.995
1.00
27.63
A


ATOM
512
CB
MET
A
134
73.210
11.576
6.436
1.00
25.11
A


ATOM
513
CG
MET
A
134
74.056
12.834
6.539
1.00
27.52
A


ATOM
514
SD
MET
A
134
74.875
13.035
8.132
1.00
28.28
A


ATOM
515
CE
MET
A
134
73.545
13.741
9.104
1.00
28.66
A


ATOM
516
C
MET
A
134
72.431
9.779
4.901
1.00
28.59
A


ATOM
517
O
MET
A
134
73.276
8.938
4.599
1.00
31.12
A


ATOM
518
N
SER
A
135
71.168
9.467
5.165
1.00
29.14
A


ATOM
519
CA
SER
A
135
70.709
8.082
5.090
1.00
31.93
A


ATOM
520
CB
SER
A
135
69.261
7.966
5.558
1.00
32.44
A


ATOM
521
OG
SER
A
135
69.112
8.470
6.868
1.00
40.09
A


ATOM
522
C
SER
A
135
70.786
7.557
3.668
1.00
31.36
A


ATOM
523
O
SER
A
135
71.010
6.374
3.454
1.00
32.23
A


ATOM
524
N
ARG
A
136
70.597
8.448
2.701
1.00
31.66
A


ATOM
525
CA
ARG
A
136
70.602
8.075
1.293
1.00
32.53
A


ATOM
526
CB
ARG
A
136
69.798
9.095
0.491
1.00
33.51
A


ATOM
527
CG
ARG
A
136
68.361
9.274
0.962
1.00
38.41
A


ATOM
528
CD
ARG
A
136
67.676
10.352
0.137
1.00
40.27
A


ATOM
529
NE
ARG
A
136
67.850
10.090
−1.288
1.00
42.75
A


ATOM
530
CZ
ARG
A
136
67.560
10.953
−2.253
1.00
44.58
A


ATOM
531
NH1
ARG
A
136
67.071
12.151
−1.950
1.00
45.74
A


ATOM
532
NH2
ARG
A
136
67.771
10.621
−3.522
1.00
43.43
A


ATOM
533
C
ARG
A
136
71.985
7.946
0.670
1.00
32.09
A


ATOM
534
O
ARG
A
136
72.113
7.513
−0.474
1.00
32.48
A


ATOM
535
N
LEU
A
137
73.019
8.329
1.406
1.00
30.72
A


ATOM
536
CA
LEU
A
137
74.371
8.253
0.873
1.00
30.30
A


ATOM
537
CB
LEU
A
137
75.167
9.508
1.262
1.00
29.84
A


ATOM
538
CG
LEU
A
137
74.541
10.843
0.831
1.00
30.25
A


ATOM
539
CD1
LEU
A
137
75.488
11.963
1.154
1.00
29.16
A


ATOM
540
CD2
LEU
A
137
74.230
10.835
−0.656
1.00
29.68
A


ATOM
541
C
LEU
A
137
75.083
7.006
1.369
1.00
29.52
A


ATOM
542
O
LEU
A
137
75.033
6.684
2.553
1.00
31.12
A


ATOM
543
N
ASP
A
138
75.745
6.310
0.453
1.00
27.02
A


ATOM
544
CA
ASP
A
138
76.467
5.087
0.773
1.00
25.70
A


ATOM
545
CB
ASP
A
138
75.556
3.887
0.492
1.00
29.85
A


ATOM
546
CG
ASP
A
138
76.198
2.567
0.858
1.00
33.94
A


ATOM
547
OD1
ASP
A
138
76.815
2.486
1.949
1.00
34.64
A


ATOM
548
OD2
ASP
A
138
76.074
1.610
0.058
1.00
35.28
A


ATOM
549
C
ASP
A
138
77.699
5.062
−0.127
1.00
24.23
A


ATOM
550
O
ASP
A
138
77.765
4.300
−1.091
1.00
24.33
A


ATOM
551
N
HIS
A
139
78.672
5.904
0.209
1.00
20.89
A


ATOM
552
CA
HIS
A
139
79.888
6.069
−0.577
1.00
19.30
A


ATOM
553
CB
HIS
A
139
79.681
7.243
−1.553
1.00
17.75
A


ATOM
554
CG
HIS
A
139
80.774
7.410
−2.564
1.00
17.45
A


ATOM
555
CD2
HIS
A
139
80.794
7.179
−3.897
1.00
16.63
A


ATOM
556
ND1
HIS
A
139
82.034
7.862
−2.235
1.00
20.01
A


ATOM
557
CE1
HIS
A
139
82.784
7.901
−3.322
1.00
16.89
A


ATOM
558
NE2
HIS
A
139
82.054
7.491
−4.344
1.00
16.94
A


ATOM
559
C
HIS
A
139
81.066
6.347
0.352
1.00
19.25
A


ATOM
560
O
HIS
A
139
80.914
6.990
1.388
1.00
21.17
A


ATOM
561
N
PRO
A
140
82.265
5.881
−0.021
1.00
17.84
A


ATOM
562
CD
PRO
A
140
82.575
5.120
−1.243
1.00
16.07
A


ATOM
563
CA
PRO
A
140
83.467
6.079
0.789
1.00
18.04
A


ATOM
564
CB
PRO
A
140
84.518
5.240
0.055
1.00
18.70
A


ATOM
565
CG
PRO
A
140
84.061
5.315
−1.365
1.00
19.17
A


ATOM
566
C
PRO
A
140
83.919
7.523
1.014
1.00
19.75
A


ATOM
567
O
PRO
A
140
84.686
7.793
1.930
1.00
21.01
A


ATOM
568
N
PHE
A
141
83.460
8.457
0.192
1.00
20.21
A


ATOM
569
CA
PHE
A
141
83.869
9.837
0.389
1.00
20.05
A


ATOM
570
CB
PHE
A
141
84.149
10.496
−0.964
1.00
20.20
A


ATOM
571
CG
PHE
A
141
85.333
9.909
1.686
1.00
20.95
A


ATOM
572
CD1
PHE
A
141
86.362
9.297
−0.975
1.00
21.45
A


ATOM
573
CD2
PHE
A
141
85.430
9.983
−3.071
1.00
20.27
A


ATOM
574
CE1
PHE
A
141
87.476
8.765
−1.635
1.00
22.05
A


ATOM
575
CE2
PHE
A
141
86.541
9.456
−3.743
1.00
20.58
A


ATOM
576
CZ
PHE
A
141
87.562
8.848
−3.027
1.00
20.58
A


ATOM
577
C
PHE
A
141
82.881
10.679
1.210
1.00
18.71
A


ATOM
578
O
PHE
A
141
83.015
11.897
1.300
1.00
19.78
A


ATOM
579
N
PHE
A
142
81.903
10.027
1.823
1.00
18.61
A


ATOM
580
CA
PHE
A
142
80.915
10.738
2.639
1.00
19.11
A


ATOM
581
CB
PHE
A
142
79.543
10.709
1.966
1.00
17.36
A


ATOM
582
CG
PHE
A
142
79.458
11.565
0.750
1.00
19.19
A


ATOM
583
CD1
PHE
A
142
79.258
12.936
0.863
1.00
19.44
A


ATOM
584
CD2
PHE
A
142
79.649
11.016
−0.511
1.00
18.39
A


ATOM
585
CE1
PHE
A
142
79.254
13.759
−0.268
1.00
20.66
A


ATOM
586
CE2
PHE
A
142
79.648
11.824
−1.644
1.00
20.80
A


ATOM
587
CZ
PHE
A
142
79.451
13.203
−1.523
1.00
18.95
A


ATOM
588
C
PHE
A
142
80.787
10.132
4.023
1.00
18.98
A


ATOM
589
O
PHE
A
142
80.735
8.918
4.168
1.00
18.39
A


ATOM
590
N
VAL
A
143
80.736
10.983
5.041
1.00
20.79
A


ATOM
591
CA
VAL
A
143
80.578
10.499
6.401
1.00
20.94
A


ATOM
592
CB
VAL
A
143
80.456
11.670
7.404
1.00
21.95
A


ATOM
593
CG1
VAL
A
143
80.081
11.145
8.783
1.00
21.30
A


ATOM
594
CG2
VAL
A
143
81.781
12.433
7.473
1.00
19.28
A


ATOM
595
C
VAL
A
143
79.299
9.683
6.396
1.00
21.12
A


ATOM
596
O
VAL
A
143
78.280
10.124
5.895
1.00
23.63
A


ATOM
597
N
LYS
A
144
79.367
8.481
6.940
1.00
23.64
A


ATOM
598
CA
LYS
A
144
78.221
7.582
6.990
1.00
24.47
A


ATOM
599
CB
LYS
A
144
78.714
6.131
6.869
1.00
25.53
A


ATOM
600
CG
LYS
A
144
77.635
5.061
6.997
1.00
32.25
A


ATOM
601
CD
LYS
A
144
78.240
3.660
6.870
1.00
36.07
A


ATOM
602
CE
LYS
A
144
77.187
2.563
7.033
1.00
38.50
A


ATOM
603
NZ
LYS
A
144
77.791
1.186
7.051
1.00
41.46
A


ATOM
604
C
LYS
A
144
77.418
7.744
8.275
1.00
22.60
A


ATOM
605
O
LYS
A
144
77.973
8.019
9.335
1.00
23.18
A


ATOM
606
N
LEU
A
145
76.104
7.583
8.170
1.00
21.59
A


ATOM
607
CA
LEU
A
145
75.224
7.661
9.327
1.00
21.42
A


ATOM
608
CB
LEU

145
73.918
8.372
8.967
0.50
21.21
AC1


ATOM
609
CG
LEU

145
72.843
8.332
10.060
0.50
21.32
AC1


ATOM
610
CD1
LEU

145
73.356
9.036
11.309
0.50
19.59
AC1


ATOM
611
CD2
LEU

145
71.569
8.994
9.559
0.50
21.45
AC1


ATOM
612
C
LEU
A
145
74.919
6.215
9.733
1.00
21.84
A


ATOM
613
O
LEU
A
145
74.283
5.471
8.977
1.00
19.24
A


ATOM
614
N
TYR
A
146
75.363
5.816
10.921
1.00
19.77
A


ATOM
615
CA
TYR
A
146
75.143
4.444
11.368
1.00
19.92
A


ATOM
616
CB
TYR
A
146
76.326
3.944
12.188
1.00
18.05
A


ATOM
617
CG
TYR
A
146
77.601
3.803
11.415
1.00
17.64
A


ATOM
618
CD1
TYR
A
146
78.435
4.909
11.203
1.00
18.26
A


ATOM
619
CE1
TYR
A
146
79.638
4.782
10.516
1.00
17.33
A


ATOM
620
CD2
TYR
A
146
78.000
2.560
10.910
1.00
15.57
A


ATOM
621
CE2
TYR
A
146
79.208
2.419
10.215
1.00
17.53
A


ATOM
622
CZ
TYR
A
146
80.022
3.535
10.026
1.00
18.78
A


ATOM
623
OH
TYR
A
146
81.224
3.413
9.369
1.00
19.47
A


ATOM
624
C
TYR
A
146
73.884
4.194
12.170
1.00
20.60
A


ATOM
625
O
TYR
A
146
73.331
3.100
12.108
1.00
21.73
A


ATOM
626
N
PHE
A
147
73.431
5.192
12.921
1.00
20.92
A


ATOM
627
CA
PHE
A
147
72.239
5.025
13.745
1.00
22.59
A


ATOM
628
CB
PHE
A
147
72.538
4.063
14.917
1.00
22.24
A


ATOM
629
CG
PHE
A
147
73.708
4.488
15.770
1.00
21.88
A


ATOM
630
CD1
PHE
A
147
73.607
5.578
16.625
1.00
21.93
A


ATOM
631
CD2
PHE
A
147
74.936
3.843
15.657
1.00
21.57
A


ATOM
632
CE1
PHE
A
147
74.715
6.025
17.352
1.00
25.21
A


ATOM
633
CE2
PHE
A
147
76.051
4.279
16.377
1.00
21.30
A


ATOM
634
CZ
PHE
A
147
75.942
5.371
17.224
1.00
24.23
A


ATOM
635
C
PHE
A
147
71.737
6.343
14.308
1.00
23.77
A


ATOM
636
O
PHE
A
147
72.448
7.352
14.307
1.00
22.91
A


ATOM
637
N
THR
A
148
70.501
6.324
14.791
1.00
25.15
A


ATOM
638
CA
THR
A
148
69.908
7.503
15.403
1.00
25.99
A


ATOM
639
CB
THR
A
148
68.953
8.251
14.466
1.00
27.00
A


ATOM
640
OG1
THR
A
148
67.850
7.400
14.148
1.00
27.79
A


ATOM
641
CG2
THR
A
148
69.660
8.661
13.193
1.00
26.35
A


ATOM
642
C
THR
A
148
69.080
7.055
16.580
1.00
26.23
A


ATOM
643
O
THR
A
148
68.591
5.930
16.620
1.00
26.46
A


ATOM
644
N
PHE
A
149
68.942
7.943
17.550
1.00
25.72
A


ATOM
645
CA
PHE
A
149
68.133
7.662
18.706
1.00
25.10
A


ATOM
646
CB
PHE
A
149
68.789
6.593
19.602
1.00
23.02
A


ATOM
647
CG
PHE
A
149
70.088
7.011
20.231
1.00
22.26
A


ATOM
648
CD1
PHE
A
149
70.105
7.794
21.373
1.00
20.98
A


ATOM
649
CD2
PHE
A
149
71.302
6.587
19.694
1.00
21.51
A


ATOM
650
CE1
PHE
A
149
71.312
8.151
21.976
1.00
22.36
A


ATOM
651
CE2
PHE
A
149
72.511
6.939
20.288
1.00
21.06
A


ATOM
652
CZ
PHE
A
149
72.519
7.722
21.430
1.00
19.46
A


ATOM
653
C
PHE
A
149
67.931
8.974
19.427
1.00
27.05
A


ATOM
654
O
PHE
A
149
68.565
9.974
19.096
1.00
27.03
A


ATOM
655
N
GLN
A
150
67.024
8.984
20.391
1.00
29.18
A


ATOM
656
CA
GLN
A
150
66.757
10.198
21.133
1.00
31.94
A


ATOM
657
CB
GLN
A
150
65.697
11.035
20.409
1.00
32.80
A


ATOM
658
CG
GLN
A
150
64.385
10.302
20.153
1.00
34.22
A


ATOM
659
CD
GLN
A
150
63.340
11.169
19.459
1.00
36.88
A


ATOM
660
OE1
GLN
A
150
62.630
11.959
20.098
1.00
37.60
A


ATOM
661
NE2
GLN
A
150
63.248
11.033
18.141
1.00
35.03
A


ATOM
662
C
GLN
A
150
66.269
9.890
22.531
1.00
32.97
A


ATOM
663
O
GLN
A
150
65.857
8.768
22.825
1.00
33.19
A


ATOM
664
N
ASP
A
151
66.355
10.890
23.398
1.00
34.27
A


ATOM
665
CA
ASP
A
151
65.847
10.771
24.753
1.00
35.77
A


ATOM
666
CB
ASP
A
151
66.957
10.933
25.796
1.00
35.66
A


ATOM
667
CG
ASP
A
151
67.760
12.194
25.604
1.00
38.11
A


ATOM
668
OD1
ASP
A
151
67.172
13.216
25.195
1.00
39.31
A


ATOM
669
OD2
ASP
A
151
68.982
12.167
25.879
1.00
41.03
A


ATOM
670
C
ASP
A
151
64.823
11.904
24.838
1.00
36.64
A


ATOM
671
O
ASP
A
151
64.401
12.428
23.803
1.00
36.42
A


ATOM
672
N
ASP
A
152
64.427
12.301
26.041
1.00
38.18
A


ATOM
673
CA
ASP
A
152
63.427
13.357
26.171
1.00
39.81
A


ATOM
674
CB
ASP
A
152
63.022
13.534
27.637
1.00
44.46
A


ATOM
675
CG
ASP
A
152
62.291
12.324
28.186
1.00
50.02
A


ATOM
676
OD1
ASP
A
152
61.313
11.876
27.541
1.00
52.36
A


ATOM
677
OD2
ASP
A
152
62.689
11.822
29.263
1.00
52.75
A


ATOM
678
C
ASP
A
152
63.822
14.709
25.594
1.00
37.45
A


ATOM
679
O
ASP
A
152
62.988
15.408
25.026
1.00
36.81
A


ATOM
680
N
GLU
A
153
65.091
15.077
25.708
1.00
35.46
A


ATOM
681
CA
GLU
A
153
65.501
16.378
25.211
1.00
33.50
A


ATOM
682
CB
GLU
A
153
66.132
17.174
26.354
1.00
36.16
A


ATOM
683
CG
GLU
A
153
65.389
17.065
27.687
1.00
37.72
A


ATOM
684
CD
GLU
A
153
65.657
15.753
28.402
0.00
37.23
A


ATOM
685
OE1
GLU
A
153
65.063
15.530
29.479
0.00
37.39
A


ATOM
686
OE2
GLU
A
153
66.464
14.947
27.893
0.00
37.39
A


ATOM
687
C
GLU
A
153
66.432
16.425
23.995
1.00
31.79
A


ATOM
688
O
GLU
A
153
66.498
17.451
23.323
1.00
30.80
A


ATOM
689
N
LYS
A
154
67.131
15.334
23.691
1.00
30.35
A


ATOM
690
CA
LYS
A
154
68.069
15.357
22.569
1.00
28.14
A


ATOM
691
CB
LYS
A
154
69.505
15.358
23.099
1.00
27.32
A


ATOM
692
CG
LYS
A
154
69.853
16.503
24.026
1.00
29.91
A


ATOM
693
CD
LYS
A
154
71.234
16.302
24.648
1.00
30.14
A


ATOM
694
CE
LYS
A
154
71.606
17.450
25.592
1.00
32.52
A


ATOM
695
NZ
LYS
A
154
72.780
17.121
26.469
1.00
31.90
A


ATOM
696
C
LYS
A
154
67.967
14.261
21.515
1.00
26.36
A


ATOM
697
O
LYS
A
154
67.517
13.145
21.781
1.00
23.71
A


ATOM
698
N
LEU
A
155
68.413
14.610
20.311
1.00
24.76
A


ATOM
699
CA
LEU
A
155
68.462
13.691
19.178
1.00
23.29
A


ATOM
700
CB
LEU
A
155
68.012
14.382
17.891
1.00
22.72
A


ATOM
701
CG
LEU
A
155
66.588
14.916
17.739
1.00
24.25
A


ATOM
702
CD1
LEU
A
155
66.441
15.489
16.329
1.00
24.62
A


ATOM
703
CD2
LEU
A
155
65.576
13.798
17.965
1.00
23.10
A


ATOM
704
C
LEU
A
155
69.939
13.325
19.022
1.00
21.93
A


ATOM
705
O
LEU
A
155
70.812
14.167
19.233
1.00
20.17
A


ATOM
706
N
TYR
A
156
70.227
12.088
18.647
1.00
19.72
A


ATOM
707
CA
TYR
A
156
71.617
11.693
18.462
1.00
20.11
A


ATOM
708
CB
TYR
A
156
72.061
10.703
19.540
1.00
20.01
A


ATOM
709
CG
TYR
A
156
71.885
11.172
20.963
1.00
20.98
A


ATOM
710
CD1
TYR
A
156
70.619
11.313
21.520
1.00
22.18
A


ATOM
711
CE1
TYR
A
156
70.457
11.724
22.850
1.00
25.21
A


ATOM
712
CD2
TYR
A
156
72.991
11.449
21.762
1.00
21.38
A


ATOM
713
CE2
TYR
A
156
72.843
11.859
23.086
1.00
25.12
A


ATOM
714
CZ
TYR
A
156
71.576
11.995
23.622
1.00
24.83
A


ATOM
715
OH
TYR
A
156
71.431
12.410
24.923
1.00
25.97
A


ATOM
716
C
TYR
A
156
71.792
11.033
17.108
1.00
20.02
A


ATOM
717
O
TYR
A
156
70.959
10.231
16.704
1.00
22.19
A


ATOM
718
N
PHE
A
157
72.860
11.385
16.399
1.00
19.17
A


ATOM
719
CA
PHE
A
157
73.140
10.769
15.114
1.00
18.65
A


ATOM
720
CB
PHE
A
157
73.071
11.780
13.969
1.00
21.02
A


ATOM
721
CG
PHE
A
157
71.719
12.411
13.791
1.00
25.64
A


ATOM
722
CD1
PHE
A
157
70.558
11.724
14.135
1.00
27.84
A


ATOM
723
CD2
PHE
A
157
71.603
13.695
13.267
1.00
27.19
A


ATOM
724
CE1
PHE
A
157
69.301
12.310
13.964
1.00
28.87
A


ATOM
725
CE2
PHE
A
157
70.350
14.288
13.091
1.00
28.27
A


ATOM
726
CZ
PHE
A
157
69.200
13.595
13.442
1.00
26.64
A


ATOM
727
C
PHE
A
157
74.543
10.212
15.204
1.00
19.60
A


ATOM
728
O
PHE
A
157
75.489
10.952
15.467
1.00
19.26
A


ATOM
729
N
GLY
A
158
74.668
8.902
15.010
1.00
19.26
A


ATOM
730
CA
GLY
A
158
75.972
8.265
15.063
1.00
18.63
A


ATOM
731
C
GLY
A
158
76.615
8.309
13.693
1.00
16.84
A


ATOM
732
O
GLY
A
158
76.160
7.646
12.772
1.00
15.29
A


ATOM
733
N
LEU
A
159
77.677
9.096
13.567
1.00
18.10
A


ATOM
734
CA
LEU
A
159
78.386
9.263
12.302
1.00
17.32
A


ATOM
735
CB
LEU
A
159
78.502
10.753
11.984
1.00
16.80
A


ATOM
736
CG
LEU
A
159
77.161
11.485
12.068
1.00
18.21
A


ATOM
737
CD1
LEU
A
159
77.376
12.992
12.058
1.00
15.34
A


ATOM
738
CD2
LEU
A
159
76.280
11.036
10.906
1.00
14.27
A


ATOM
739
C
LEU
A
159
79.780
8.665
12.375
1.00
18.27
A


ATOM
740
O
LEU
A
159
80.338
8.518
13.465
1.00
18.92
A


ATOM
741
N
SER
A
160
80.343
8.320
11.220
1.00
16.88
A


ATOM
742
CA
SER
A
160
81.691
7.770
11.194
1.00
19.02
A


ATOM
743
CB
SER
A
160
82.086
7.362
9.771
1.00
20.02
A


ATOM
744
OG
SER
A
160
81.866
8.421
8.864
1.00
25.88
A


ATOM
745
C
SER
A
160
82.655
8.831
11.724
1.00
18.34
A


ATOM
746
O
SER
A
160
82.413
10.032
11.588
1.00
17.84
A


ATOM
747
N
TYR
A
161
83.743
8.384
12.335
1.00
17.11
A


ATOM
748
CA
TYR
A
161
84.723
9.300
12.901
1.00
19.21
A


ATOM
749
CB
TYR
A
161
85.146
8.802
14.293
1.00
19.37
A


ATOM
750
CG
TYR
A
161
86.269
9.582
14.944
1.00
22.52
A


ATOM
751
CD1
TYR
A
161
86.276
10.978
14.929
1.00
21.17
A


ATOM
752
CE1
TYR
A
161
87.283
11.703
15.559
1.00
18.10
A


ATOM
753
CD2
TYR
A
161
87.313
8.923
15.612
1.00
21.92
A


ATOM
754
CE2
TYR
A
161
88.330
9.647
16.252
1.00
20.10
A


ATOM
755
CZ
TYR
A
161
88.301
11.039
16.220
1.00
20.24
A


ATOM
756
OH
TYR
A
161
89.266
11.776
16.873
1.00
20.31
A


ATOM
757
C
TYR
A
161
85.934
9.459
11.997
1.00
20.13
A


ATOM
758
O
TYR
A
161
86.621
8.491
11.675
1.00
21.97
A


ATOM
759
N
ALA
A
162
86.182
10.686
11.571
1.00
19.13
A


ATOM
760
CA
ALA
A
162
87.320
10.969
10.717
1.00
20.60
A


ATOM
761
CB
ALA
A
162
86.907
11.919
9.592
1.00
21.18
A


ATOM
762
C
ALA
A
162
88.375
11.617
11.604
1.00
21.36
A


ATOM
763
O
ALA
A
162
88.391
12.835
11.752
1.00
20.74
A


ATOM
764
N
LYS
A
163
89.237
10.787
12.195
1.00
21.80
A


ATOM
765
CA
LYS
A
163
90.294
11.232
13.102
1.00
25.38
A


ATOM
766
CB
LYS
A
163
91.315
10.109
13.332
1.00
30.51
A


ATOM
767
CG
LYS
A
163
90.874
8.987
14.251
1.00
38.24
A


ATOM
768
CD
LYS
A
163
92.000
7.970
14.456
1.00
43.14
A


ATOM
769
CE
LYS
A
163
91.556
6.794
15.342
1.00
46.63
A


ATOM
770
NZ
LYS
A
163
91.252
7.200
16.752
1.00
47.21
A


ATOM
771
C
LYS
A
163
91.082
12.482
12.719
1.00
25.07
A


ATOM
772
O
LYS
A
163
91.276
13.373
13.541
1.00
25.50
A


ATOM
773
N
ASN
A
164
91.540
12.549
11.477
1.00
25.06
A


ATOM
774
CA
ASN
A
164
92.363
13.668
11.054
1.00
26.04
A


ATOM
775
CB
ASN
A
164
93.115
13.278
9.787
1.00
26.02
A


ATOM
776
CG
ASN
A
164
94.062
12.120
10.033
1.00
29.07
A


ATOM
777
OD1
ASN
A
164
94.854
12.155
10.969
1.00
30.18
A


ATOM
778
ND2
ASN
A
164
93.979
11.089
9.207
1.00
32.14
A


ATOM
779
C
ASN
A
164
91.725
15.040
10.915
1.00
25.35
A


ATOM
780
O
ASN
A
164
92.416
16.021
10.640
1.00
26.51
A


ATOM
781
N
GLY
A
165
90.419
15.122
11.116
1.00
23.92
A


ATOM
782
CA
GLY
A
165
89.761
16.413
11.043
1.00
24.35
A


ATOM
783
C
GLY
A
165
89.663
17.123
9.704
1.00
23.94
A


ATOM
784
O
GLY
A
165
89.632
16.501
8.643
1.00
25.49
A


ATOM
785
N
GLU
A
166
89.623
18.449
9.773
1.00
23.07
A


ATOM
786
CA
GLU
A
166
89.467
19.301
8.602
1.00
23.26
A


ATOM
787
CB
GLU
A
166
89.164
20.739
9.036
1.00
23.73
A


ATOM
788
CG
GLU
A
166
88.271
20.875
10.257
1.00
27.31
A


ATOM
789
CD
GLU
A
166
87.812
22.302
10.474
1.00
29.74
A


ATOM
790
OE1
GLU
A
166
88.586
23.221
10.130
1.00
30.87
A


ATOM
791
OE2
GLU
A
166
86.686
22.510
10.989
1.00
29.80
A


ATOM
792
C
GLU
A
166
90.612
19.354
7.602
1.00
24.47
A


ATOM
793
O
GLU
A
166
91.786
19.473
7.968
1.00
24.85
A


ATOM
794
N
LEU
A
167
90.251
19.287
6.328
1.00
23.47
A


ATOM
795
CA
LEU
A
167
91.228
19.393
5.262
1.00
24.00
A


ATOM
796
CB
LEU
A
167
90.528
19.369
3.901
1.00
22.48
A


ATOM
797
CG
LEU
A
167
91.373
19.759
2.679
1.00
23.87
A


ATOM
798
CD1
LEU
A
167
92.583
18.846
2.563
1.00
20.03
A


ATOM
799
CD2
LEU
A
167
90.516
19.680
1.418
1.00
22.08
A


ATOM
800
C
LEU
A
167
91.943
20.732
5.448
1.00
24.82
A


ATOM
801
O
LEU
A
167
93.138
20.858
5.165
1.00
24.59
A


ATOM
802
N
LEU
A
168
91.206
21.731
5.927
1.00
24.43
A


ATOM
803
CA
LEU
A
168
91.784
23.055
6.150
1.00
28.25
A


ATOM
804
CB
LEU
A
168
90.746
24.009
6.747
1.00
27.44
A


ATOM
805
CG
LEU
A
168
91.310
25.395
7.090
1.00
28.57
A


ATOM
806
CD1
LEU
A
168
91.624
26.150
5.809
1.00
28.11
A


ATOM
807
CD2
LEU
A
168
90.312
26.174
7.921
1.00
29.97
A


ATOM
808
C
LEU
A
168
92.999
23.014
7.074
1.00
28.43
A


ATOM
809
O
LEU
A
168
93.952
23.760
6.882
1.00
30.21
A


ATOM
810
N
LYS
A
169
92.958
22.152
8.081
1.00
30.23
A


ATOM
811
CA
LYS
A
169
94.072
22.050
9.008
1.00
33.52
A


ATOM
812
CB
LYS
A
169
93.821
20.955
10.046
1.00
35.45
A


ATOM
813
CG
LYS
A
169
94.972
20.784
11.033
1.00
40.43
A


ATOM
814
CD
LYS
A
169
94.808
19.562
11.943
1.00
41.43
A


ATOM
815
CE
LYS
A
169
95.047
18.261
11.186
1.00
42.67
A


ATOM
816
NZ
LYS
A
169
95.057
17.068
12.096
1.00
43.84
A


ATOM
817
C
LYS
A
169
95.329
21.718
8.228
1.00
34.58
A


ATOM
818
O
LYS
A
169
96.377
22.333
8.421
1.00
35.58
A


ATOM
819
N
TYR
A
170
95.219
20.739
7.339
1.00
34.55
A


ATOM
820
CA
TYR
A
170
96.357
20.328
6.539
1.00
35.07
A


ATOM
821
CB
TYR
A
170
96.018
19.047
5.790
1.00
35.72
A


ATOM
822
CG
TYR
A
170
96.050
17.869
6.716
1.00
37.48
A


ATOM
823
CD1
TYR
A
170
97.256
17.250
7.040
1.00
39.42
A


ATOM
824
CE1
TYR
A
170
97.313
16.230
7.987
1.00
40.93
A


ATOM
825
CD2
TYR
A
170
94.895
17.435
7.355
1.00
38.83
A


ATOM
826
CE2
TYR
A
170
94.937
16.417
8.303
1.00
41.76
A


ATOM
827
CZ
TYR
A
170
96.149
15.821
8.615
1.00
42.18
A


ATOM
828
OH
TYR
A
170
96.196
14.827
9.563
1.00
45.30
A


ATOM
829
C
TYR
A
170
96.823
21.404
5.585
1.00
35.67
A


ATOM
830
O
TYR
A
170
97.999
21.465
5.248
1.00
35.28
A


ATOM
831
N
ILE
A
171
95.904
22.260
5.154
1.00
36.78
A


ATOM
832
CA
ILE
A
171
96.272
23.333
4.252
1.00
38.95
A


ATOM
833
CB
ILE
A
171
95.032
24.048
3.682
1.00
39.15
A


ATOM
834
CG2
ILE
A
171
95.452
25.329
2.960
1.00
38.11
A


ATOM
835
CG1
ILE
A
171
94.296
23.113
2.718
1.00
37.57
A


ATOM
836
CD1
ILE
A
171
93.041
23.712
2.116
1.00
37.48
A


ATOM
837
C
ILE
A
171
97.146
24.338
4.990
1.00
41.33
A


ATOM
838
O
ILE
A
171
98.173
24.765
4.466
1.00
42.36
A


ATOM
839
N
ARG
A
172
96.748
24.713
6.203
1.00
42.79
A


ATOM
840
CA
ARG
A
172
97.541
25.662
6.981
1.00
44.62
A


ATOM
841
CB
ARG
A
172
96.809
26.103
8.253
1.00
46.82
A


ATOM
842
CG
ARG
A
172
95.492
26.828
8.033
1.00
50.73
A


ATOM
843
CD
ARG
A
172
95.124
27.643
9.271
1.00
53.80
A


ATOM
844
NE
ARG
A
172
93.747
28.136
9.247
1.00
56.88
A


ATOM
845
CZ
ARG
A
172
93.183
28.766
8.218
1.00
57.65
A


ATOM
846
NH1
ARG
A
172
93.873
28.989
7.104
1.00
57.71
A


ATOM
847
NH2
ARG
A
172
91.923
29.176
8.305
1.00
56.95
A


ATOM
848
C
ARG
A
172
98.856
25.015
7.383
1.00
44.41
A


ATOM
849
O
ARG
A
172
99.927
25.587
7.186
1.00
45.16
A


ATOM
850
N
LYS
A
173
98.759
23.817
7.949
1.00
44.01
A


ATOM
851
CA
LYS
A
173
99.923
23.069
8.398
1.00
42.99
A


ATOM
852
CB
LYS
A
173
99.538
21.616
8.667
1.00
44.20
A


ATOM
853
CG
LYS
A
173
100.721
20.689
8.908
1.00
45.81
A


ATOM
854
CD
LYS
A
173
100.272
19.238
8.987
0.00
45.28
A


ATOM
855
CE
LYS
A
173
101.457
18.296
9.120
0.00
45.43
A


ATOM
856
NZ
LYS
A
173
101.028
16.870
9.146
0.00
45.35
A


ATOM
857
C
LYS
A
173
101.081
23.108
7.412
1.00
43.20
A


ATOM
858
O
LYS
A
173
102.220
23.366
7.805
1.00
43.49
A


ATOM
859
N
ILE
A
174
100.802
22.867
6.133
1.00
41.97
A


ATOM
860
CA
ILE
A
174
101.871
22.859
5.136
1.00
40.74
A


ATOM
861
CB
ILE
A
174
101.874
21.536
4.336
1.00
40.61
A


ATOM
862
CG2
ILE
A
174
101.897
20.352
5.297
1.00
41.39
A


ATOM
863
CG1
ILE
A
174
100.638
21.448
3.442
1.00
40.75
A


ATOM
864
CD1
ILE
A
174
100.680
20.276
2.487
1.00
40.45
A


ATOM
865
C
ILE
A
174
101.882
24.024
4.149
1.00
39.97
A


ATOM
866
O
ILE
A
174
102.675
24.033
3.209
1.00
38.15
A


ATOM
867
N
GLY
A
175
101.007
25.004
4.359
1.00
40.09
A


ATOM
868
CA
GLY
A
175
100.969
26.156
3.473
1.00
39.94
A


ATOM
869
C
GLY
A
175
100.151
25.960
2.211
1.00
39.87
A


ATOM
870
O
GLY
A
175
99.152
26.646
2.005
1.00
40.53
A


ATOM
871
N
SER
A
176
100.586
25.043
1.354
1.00
39.28
A


ATOM
872
CA
SER
A
176
99.871
24.747
0.122
1.00
38.77
A


ATOM
873
CB
SER
A
176
100.169
25.804
−0.950
1.00
39.84
A


ATOM
874
OG
SER
A
176
101.537
25.823
−1.319
1.00
43.67
A


ATOM
875
C
SER
A
176
100.265
23.353
−0.358
1.00
38.39
A


ATOM
876
O
SER
A
176
101.245
22.776
0.118
1.00
39.37
A


ATOM
877
N
PHE
A
177
99.491
22.811
−1.289
1.00
35.85
A


ATOM
878
CA
PHE
A
177
99.732
21.472
−1.810
1.00
32.81
A


ATOM
879
CB
PHE
A
177
98.401
20.770
−2.095
1.00
32.30
A


ATOM
880
CG
PHE
A
177
97.645
20.344
−0.867
1.00
31.20
A


ATOM
881
CD1
PHE
A
177
97.806
21.005
0.348
1.00
29.02
A


ATOM
882
CD2
PHE
A
177
96.735
19.293
−0.939
1.00
30.11
A


ATOM
883
CE1
PHE
A
177
97.076
20.628
1.468
1.00
27.07
A


ATOM
884
CE2
PHE
A
177
95.998
18.910
0.181
1.00
29.70
A


ATOM
885
CZ
PHE
A
177
96.170
19.580
1.385
1.00
27.57
A


ATOM
886
C
PHE
A
177
100.535
21.485
−3.093
1.00
33.02
A


ATOM
887
O
PHE
A
177
100.386
22.381
−3.927
1.00
30.75
A


ATOM
888
N
ASP
A
178
101.379
20.471
−3.252
1.00
33.87
A


ATOM
889
CA
ASP
A
178
102.184
20.329
−4.454
1.00
33.45
A


ATOM
890
CB
ASP
A
178
103.269
19.275
−4.244
1.00
35.60
A


ATOM
891
CG
ASP
A
178
102.693
17.932
−3.855
1.00
40.22
A


ATOM
892
OD1
ASP
A
178
101.840
17.412
−4.612
1.00
42.64
A


ATOM
893
OD2
ASP
A
178
103.079
17.398
−2.793
1.00
43.32
A


ATOM
894
C
ASP
A
178
101.195
19.859
−5.519
1.00
32.50
A


ATOM
895
O
ASP
A
178
99.999
19.723
−5.245
1.00
30.51
A


ATOM
896
N
GLU
A
179
101.684
19.584
−6.720
1.00
31.46
A


ATOM
897
CA
GLU
A
179
100.790
19.160
−7.779
1.00
32.00
A


ATOM
898
CB
GLU
A
179
101.480
19.291
−9.138
1.00
33.70
A


ATOM
899
CG
GLU
A
179
100.666
18.711
−10.284
1.00
38.81
A


ATOM
900
CD
GLU
A
179
101.129
19.195
−11.646
1.00
42.71
A


ATOM
901
OE1
GLU
A
179
102.358
19.338
−11.844
1.00
43.96
A


ATOM
902
OE2
GLU
A
179
100.261
19.422
−12.523
1.00
44.44
A


ATOM
903
C
GLU
A
179
100.189
17.766
7.635
1.00
29.96
A


ATOM
904
O
GLU
A
179
99.023
17.564
−7.965
1.00
27.38
A


ATOM
905
N
THR
A
180
100.959
16.803
−7.141
1.00
30.09
A


ATOM
906
CA
THR
A
180
100.429
15.448
−7.007
1.00
29.75
A


ATOM
907
CB
THR
A
180
101.583
14.416
−6.738
1.00
30.62
A


ATOM
908
OG1
THR
A
180
101.050
13.206
−6.179
1.00
30.65
A


ATOM
909
CG2
THR
A
180
102.615
14.991
−5.802
1.00
32.90
A


ATOM
910
C
THR
A
180
99.331
15.372
−5.935
1.00
29.43
A


ATOM
911
O
THR
A
180
98.312
14.710
−6.130
1.00
27.52
A


ATOM
912
N
CYS
A
181
99.522
16.079
−4.823
1.00
29.55
A


ATOM
913
CA
CYS
A
181
98.535
16.091
−3.745
1.00
29.27
A


ATOM
914
CB
CYS
A
181
99.156
16.681
−2.480
1.00
31.47
A


ATOM
915
SG
CYS
A
181
100.580
15.747
−1.838
1.00
39.84
A


ATOM
916
C
CYS
A
181
97.271
16.879
−4.126
1.00
28.16
A


ATOM
917
O
CYS
A
181
96.156
16.495
−3.762
1.00
26.55
A


ATOM
918
N
THR
A
182
97.441
17.984
−4.847
1.00
25.71
A


ATOM
919
CA
THR
A
182
96.293
18.784
−5.268
1.00
24.22
A


ATOM
920
CB
THR
A
182
96.714
20.043
−6.066
1.00
24.45
A


ATOM
921
OG1
THR
A
182
97.515
20.901
−5.241
1.00
22.57
A


ATOM
922
CG2
THR
A
182
95.483
20.809
−6.537
1.00
23.42
A


ATOM
923
C
THR
A
182
95.447
17.915
−6.184
1.00
24.78
A


ATOM
924
O
THR
A
182
94.227
17.812
−6.020
1.00
23.72
A


ATOM
925
N
ARG
A
183
96.109
17.283
−7.149
1.00
23.96
A


ATOM
926
CA
ARG
A
183
95.422
16.419
−8.096
1.00
25.38
A


ATOM
927
CB
ARG
A
183
96.416
15.782
−9.073
1.00
24.74
A


ATOM
928
CG
ARG
A
183
95.740
14.821
−10.044
1.00
27.88
A


ATOM
929
CD
ARG
A
183
96.704
14.244
−11.070
1.00
30.56
A


ATOM
930
NE
ARG
A
183
97.260
15.300
−11.904
1.00
34.63
A


ATOM
931
CZ
ARG
A
183
98.502
15.756
−11.802
1.00
33.50
A


ATOM
932
NH1
ARG
A
183
99.328
15.234
−10.903
1.00
31.79
A


ATOM
933
NH2
ARG
A
183
98.901
16.754
−12.579
1.00
31.24
A


ATOM
934
C
ARG
A
183
94.648
15.318
−7.386
1.00
24.24
A


ATOM
935
O
ARG
A
183
93.466
15.099
−7.659
1.00
24.95
A


ATOM
936
N
PHE
A
184
95.319
14.628
−6.473
1.00
23.84
A


ATOM
937
CA
PHE
A
184
94.689
13.541
−5.742
1.00
23.63
A


ATOM
938
CB
PHE
A
184
95.662
12.941
−4.730
1.00
25.29
A


ATOM
939
CG
PHE
A
184
95.086
11.787
−3.961
1.00
28.53
A


ATOM
940
CD1
PHE
A
184
94.958
10.531
−4.556
1.00
30.34
A


ATOM
941
CD2
PHE
A
184
94.620
11.964
−2.663
1.00
28.04
A


ATOM
942
CE1
PHE
A
184
94.370
9.465
−3.871
1.00
29.64
A


ATOM
943
CE2
PHE
A
184
94.030
10.908
−1.969
1.00
30.28
A


ATOM
944
CZ
PHE
A
184
93.904
9.654
−2.576
1.00
29.09
A


ATOM
945
C
PHE
A
184
93.431
13.977
−5.003
1.00
23.55
A


ATOM
946
O
PHE
A
184
92.353
13.429
−5.219
1.00
24.05
A


ATOM
947
N
TYR
A
185
93.568
14.961
−4.124
1.00
22.27
A


ATOM
948
CA
TYR
A
185
92.429
15.408
−3.344
1.00
21.69
A


ATOM
949
CB
TYR
A
185
92.925
16.295
−2.200
1.00
22.66
A


ATOM
950
CG
TYR
A
185
93.539
15.447
−1.097
1.00
25.54
A


ATOM
951
CD1
TYR
A
185
92.738
14.614
−0.314
1.00
26.51
A


ATOM
952
CE1
TYR
A
185
93.290
13.738
0.620
1.00
27.53
A


ATOM
953
CD2
TYR
A
185
94.924
15.391
−0.908
1.00
28.66
A


ATOM
954
CE2
TYR
A
185
95.496
14.514
0.032
1.00
29.09
A


ATOM
955
CZ
TYR
A
185
94.667
13.688
0.790
1.00
29.75
A


ATOM
956
OH
TYR
A
185
95.204
12.806
1.702
1.00
29.03
A


ATOM
957
C
TYR
A
185
91.316
16.058
−4.167
1.00
21.02
A


ATOM
958
O
TYR
A
185
90.130
15.921
−3.851
1.00
18.76
A


ATOM
959
N
THR
A
186
91.689
16.731
−5.244
1.00
19.87
A


ATOM
960
CA
THR
A
186
90.690
17.337
−6.102
1.00
18.89
A


ATOM
961
CB
THR
A
186
91.344
18.170
−7.200
1.00
19.73
A


ATOM
962
OG1
THR
A
186
92.115
19.218
−6.603
1.00
19.38
A


ATOM
963
CG2
THR
A
186
90.282
18.765
−8.125
1.00
20.16
A


ATOM
964
C
THR
A
186
89.905
16.201
−6.753
1.00
19.05
A


ATOM
965
O
THR
A
186
88.675
16.244
−6.855
1.00
19.38
A


ATOM
966
N
ALA
A
187
90.627
15.180
−7.200
1.00
18.33
A


ATOM
967
CA
ALA
A
187
89.984
14.043
−7.841
1.00
18.09
A


ATOM
968
CB
ALA
A
187
91.024
13.035
−8.276
1.00
19.99
A


ATOM
969
C
ALA
A
187
88.986
13.402
−6.886
1.00
18.07
A


ATOM
970
O
ALA
A
187
87.873
13.055
−7.291
1.00
18.54
A


ATOM
971
N
GLU
A
188
89.366
13.253
−5.617
1.00
16.56
A


ATOM
972
CA
GLU
A
188
88.446
12.660
−4.653
1.00
16.18
A


ATOM
973
CB
GLU
A
188
89.099
12.495
−3.280
1.00
15.52
A


ATOM
974
CG
GLU
A
188
90.266
11.519
−3.259
1.00
20.99
A


ATOM
975
CD
GLU
A
188
90.297
10.636
−2.013
1.00
22.64
A


ATOM
976
OE1
GLU
A
188
90.006
11.126
−0.899
1.00
22.95
A


ATOM
977
OE2
GLU
A
188
90.629
9.439
−2.149
1.00
27.37
A


ATOM
978
C
GLU
A
188
87.189
13.508
−4.518
1.00
15.81
A


ATOM
979
O
GLU
A
188
86.080
12.978
−4.460
1.00
15.92
A


ATOM
980
N
ILE
A
189
87.364
14.825
−4.483
1.00
16.14
A


ATOM
981
CA
ILE
A
189
86.235
15.733
−4.346
1.00
16.66
A


ATOM
982
CB
ILE
A
189
86.698
17.179
−4.083
1.00
16.57
A


ATOM
983
CG2
ILE
A
189
85.485
18.098
−3.958
1.00
14.92
A


ATOM
984
CG1
ILE
A
189
87.502
17.235
−2.784
1.00
16.19
A


ATOM
985
CD1
ILE
A
189
88.202
18.559
−2.547
1.00
16.78
A


ATOM
986
C
ILE
A
189
85.349
15.712
−5.580
1.00
16.29
A


ATOM
987
O
ILE
A
189
84.123
15.667
−5.471
1.00
15.80
A


ATOM
988
N
VAL
A
190
85.962
15.743
−6.755
1.00
16.44
A


ATOM
989
CA
VAL
A
190
85.186
15.704
−7.985
1.00
15.98
A


ATOM
990
CB
VAL
A
190
86.101
15.692
−9.229
1.00
17.23
A


ATOM
991
CG1
VAL
A
190
85.280
15.380
−10.488
1.00
16.01
A


ATOM
992
CG2
VAL
A
190
86.797
17.034
−9.373
1.00
13.82
A


ATOM
993
C
VAL
A
190
84.351
14.433
−7.979
1.00
16.29
A


ATOM
994
O
VAL
A
190
83.140
14.462
−8.194
1.00
15.64
A


ATOM
995
N
SER
A
191
85.011
13.312
−7.723
1.00
18.94
A


ATOM
996
CA
SER
A
191
84.337
12.015
−7.692
1.00
18.50
A


ATOM
997
CB
SER
A
191
85.357
10.914
−7.427
1.00
19.04
A


ATOM
998
OG
SER
A
191
84.712
9.680
−7.206
1.00
23.87
A


ATOM
999
C
SER
A
191
83.233
11.961
−6.642
1.00
16.85
A


ATOM
1000
O
SER
A
191
82.227
11.281
−6.818
1.00
18.11
A


ATOM
1001
N
ALA
A
192
83.419
12.671
−5.540
1.00
17.37
A


ATOM
1002
CA
ALA
A
192
82.395
12.687
−4.501
1.00
17.10
A


ATOM
1003
CB
ALA
A
192
82.947
13.302
−3.222
1.00
17.08
A


ATOM
1004
C
ALA
A
192
81.218
13.511
−5.020
1.00
18.24
A


ATOM
1005
O
ALA
A
192
80.055
13.162
−4.798
1.00
18.91
A


ATOM
1006
N
LEU
A
193
81.524
14.597
−5.725
1.00
16.53
A


ATOM
1007
CA
LEU
A
193
80.483
15.453
−6.270
1.00
17.25
A


ATOM
1008
CB
LEU
A
193
81.091
16.750
−6.826
1.00
17.70
A


ATOM
1009
CG
LEU
A
193
81.537
17.738
−5.732
1.00
22.88
A


ATOM
1010
CD1
LEU
A
193
82.094
19.018
−6.348
1.00
22.13
A


ATOM
1011
CD2
LEU
A
193
80.345
18.057
−4.839
1.00
20.04
A


ATOM
1012
C
LEU
A
193
79.664
14.737
−7.343
1.00
17.26
A


ATOM
1013
O
LEU
A
193
78.442
14.893
−7.402
1.00
15.43
A


ATOM
1014
N
GLU
A
194
80.330
13.962
−8.195
1.00
16.22
A


ATOM
1015
CA
GLU
A
194
79.612
13.232
−9.225
1.00
19.22
A


ATOM
1016
CB
GLU
A
194
80.564
12.405
−10.086
1.00
20.77
A


ATOM
1017
CG
GLU
A
194
79.828
11.403
−10.978
1.00
26.27
A


ATOM
1018
CD
GLU
A
194
80.756
10.667
−11.934
1.00
29.43
A


ATOM
1019
OE1
GLU
A
194
81.840
10.222
−11.489
1.00
28.21
A


ATOM
1020
OE2
GLU
A
194
80.392
10.532
−13.127
1.00
31.66
A


ATOM
1021
C
GLU
A
194
78.599
12.303
−8.566
1.00
19.71
A


ATOM
1022
O
GLU
A
194
77.466
12.159
−9.027
1.00
18.40
A


ATOM
1023
N
TYR
A
195
79.012
11.672
−7.479
1.00
19.22
A


ATOM
1024
CA
TYR
A
195
78.116
10.773
−6.781
1.00
19.69
A


ATOM
1025
CB
TYR
A
195
78.867
10.041
−5.667
1.00
21.39
A


ATOM
1026
CG
TYR
A
195
77.975
9.143
−4.847
1.00
22.55
A


ATOM
1027
CD1
TYR
A
195
77.596
7.881
−5.316
1.00
23.14
A


ATOM
1028
CE1
TYR
A
195
76.743
7.065
−4.577
1.00
22.98
A


ATOM
1029
CD2
TYR
A
195
77.479
9.564
−3.618
1.00
21.58
A


ATOM
1030
CE2
TYR
A
195
76.625
8.755
−2.872
1.00
23.50
A


ATOM
1031
CZ
TYR
A
195
76.263
7.512
−3.358
1.00
23.18
A


ATOM
1032
OH
TYR
A
195
75.413
6.732
−2.632
1.00
24.19
A


ATOM
1033
C
TYR
A
195
76.939
11.546
−6.172
1.00
18.80
A


ATOM
1034
O
TYR
A
195
75.782
11.164
−6.337
1.00
19.89
A


ATOM
1035
N
LEU
A
196
77.242
12.629
−5.469
1.00
15.26
A


ATOM
1036
CA
LEU
A
196
76.210
13.430
−4.813
1.00
16.52
A


ATOM
1037
CB
LEU
A
196
76.855
14.586
−4.038
1.00
15.67
A


ATOM
1038
CG
LEU
A
196
75.923
15.401
−3.131
1.00
19.13
A


ATOM
1039
CD1
LEU
A
196
75.555
14.571
−1.903
1.00
18.42
A


ATOM
1040
CD2
LEU
A
196
76.604
16.681
−2.689
1.00
18.50
A


ATOM
1041
C
LEU
A
196
75.209
13.993
−5.814
1.00
18.12
A


ATOM
1042
O
LEU
A
196
73.990
13.892
−5.637
1.00
16.25
A


ATOM
1043
N
HIS
A
197
75.732
14.592
−6.875
1.00
17.99
A


ATOM
1044
CA
HIS
A
197
74.873
15.171
−7.878
1.00
20.69
A


ATOM
1045
CB
HIS
A
197
75.715
16.004
−8.832
1.00
19.71
A


ATOM
1046
CG
HIS
A
197
76.292
17.224
−8.190
1.00
19.55
A


ATOM
1047
CD2
HIS
A
197
76.069
17.777
−6.973
1.00
18.32
A


ATOM
1048
ND1
HIS
A
197
77.172
18.063
−8.837
1.00
20.26
A


ATOM
1049
CE1
HIS
A
197
77.463
19.084
−8.049
1.00
20.73
A


ATOM
1050
NE2
HIS
A
197
76.806
18.935
−6.913
1.00
19.92
A


ATOM
1051
C
HIS
A
197
74.091
14.093
−8.609
1.00
22.80
A


ATOM
1052
O
HIS
A
197
72.974
14.328
−9.068
1.00
21.91
A


ATOM
1053
N
GLY
A
198
74.672
12.903
−8.697
1.00
23.17
A


ATOM
1054
CA
GLY
A
198
73.990
11.815
−9.366
1.00
26.22
A


ATOM
1055
C
GLY
A
198
72.718
11.436
−8.631
1.00
27.16
A


ATOM
1056
O
GLY
A
198
71.837
10.787
−9.185
1.00
27.89
A


ATOM
1057
N
LYS
A
199
72.623
11.831
−7.369
1.00
27.84
A


ATOM
1058
CA
LYS
A
199
71.429
11.532
−6.587
1.00
28.20
A


ATOM
1059
CB
LYS
A
199
71.827
10.952
−5.227
1.00
29.35
A


ATOM
1060
CG
LYS
A
199
72.278
9.502
−5.321
1.00
32.74
A


ATOM
1061
CD
LYS
A
199
72.737
8.944
−3.990
1.00
38.22
A


ATOM
1062
CE
LYS
A
199
72.600
7.424
−3.965
1.00
41.17
A


ATOM
1063
NZ
LYS
A
199
73.173
6.779
−5.185
1.00
44.70
A


ATOM
1064
C
LYS
A
199
70.542
12.765
−6.419
1.00
26.97
A


ATOM
1065
O
LYS
A
199
69.678
12.807
−5.551
1.00
28.27
A


ATOM
1066
N
GLY
A
200
70.759
13.762
−7.269
1.00
25.62
A


ATOM
1067
CA
GLY
A
200
69.963
14.972
−7.222
1.00
24.75
A


ATOM
1068
C
GLY
A
200
70.070
15.713
−5.908
1.00
25.82
A


ATOM
1069
O
GLY
A
200
69.080
16.241
−5.401
1.00
26.10
A


ATOM
1070
N
ILE
A
201
71.275
15.759
−5.353
1.00
25.31
A


ATOM
1071
CA
ILE
A
201
71.490
16.440
−4.089
1.00
26.11
A


ATOM
1072
CB
ILE
A
201
71.886
15.438
−2.983
1.00
27.58
A


ATOM
1073
CG2
ILE
A
201
72.242
16.175
−1.704
1.00
27.99
A


ATOM
1074
CG1
ILE
A
201
70.725
14.480
−2.719
1.00
27.89
A


ATOM
1075
CD1
ILE
A
201
71.068
13.366
−1.746
1.00
30.62
A


ATOM
1076
C
ILE
A
201
72.576
17.489
−4.233
1.00
25.92
A


ATOM
1077
O
ILE
A
201
73.599
17.269
−4.887
1.00
25.94
A


ATOM
1078
N
ILE
A
202
72.337
18.640
−3.627
1.00
25.04
A


ATOM
1079
CA
ILE
A
202
73.289
19.733
−3.680
1.00
26.57
A


ATOM
1080
CB
ILE
A
202
72.640
20.990
−4.286
1.00
27.69
A


ATOM
1081
CG2
ILE
A
202
73.695
22.068
−4.516
1.00
30.47
A


ATOM
1082
CG1
ILE
A
202
71.992
20.639
−5.625
1.00
30.89
A


ATOM
1083
CD1
ILE
A
202
71.083
21.736
−6.178
1.00
31.79
A


ATOM
1084
C
ILE
A
202
73.742
20.032
−2.252
1.00
26.14
A


ATOM
1085
O
ILE
A
202
72.912
20.201
−1.351
1.00
24.75
A


ATOM
1086
N
HIS
A
203
75.054
20.075
−2.042
1.00
25.17
A


ATOM
1087
CA
HIS
A
203
75.585
20.362
−0.717
1.00
24.36
A


ATOM
1088
CB
HIS
A
203
77.095
20.131
−0.677
1.00
23.06
A


ATOM
1089
CG
HIS
A
203
77.680
20.268
0.694
1.00
24.09
A


ATOM
1090
CD2
HIS
A
203
77.956
21.366
1.434
1.00
22.36
A


ATOM
1091
ND1
HIS
A
203
77.981
19.183
1.490
1.00
23.65
A


ATOM
1092
CE1
HIS
A
203
78.418
19.607
2.661
1.00
23.87
A


ATOM
1093
NE2
HIS
A
203
78.412
20.929
2.653
1.00
25.12
A


ATOM
1094
C
HIS
A
203
75.269
21.811
−0.330
1.00
24.71
A


ATOM
1095
O
HIS
A
203
74.633
22.055
0.693
1.00
24.27
A


ATOM
1096
N
ARG
A
204
75.724
22.758
−1.154
1.00
25.89
A


ATOM
1097
CA
ARG
A
204
75.490
24.199
−0.961
1.00
25.68
A


ATOM
1098
CB
ARG
A
204
74.033
24.471
−0.596
1.00
25.57
A


ATOM
1099
CG
ARG
A
204
73.079
24.319
−1.751
1.00
29.26
A


ATOM
1100
CD
ARG
A
204
71.815
25.118
−1.509
1.00
29.86
A


ATOM
1101
NE
ARG
A
204
71.065
24.603
−0.373
1.00
33.90
A


ATOM
1102
CZ
ARG
A
204
70.021
25.219
0.170
1.00
36.01
A


ATOM
1103
NH1
ARG
A
204
69.607
26.383
−0.322
1.00
37.08
A


ATOM
1104
NH2
ARG
A
204
69.387
24.668
1.197
1.00
34.14
A


ATOM
1105
C
ARG
A
204
76.373
24.935
0.034
1.00
26.91
A


ATOM
1106
O
ARG
A
204
76.210
26.144
0.243
1.00
26.29
A


ATOM
1107
N
ASP
A
205
77.303
24.221
0.654
1.00
26.23
A


ATOM
1108
CA
ASP
A
205
78.203
24.849
1.604
1.00
24.46
A


ATOM
1109
CB
ASP
A
205
77.557
24.909
2.990
1.00
28.25
A


ATOM
1110
CG
ASP
A
205
78.203
25.954
3.890
1.00
30.95
A


ATOM
1111
OD1
ASP
A
205
78.872
26.862
3.354
1.00
35.13
A


ATOM
1112
OD2
ASP
A
205
78.034
25.880
5.127
1.00
33.48
A


ATOM
1113
C
ASP
A
205
79.483
24.039
1.631
1.00
24.22
A


ATOM
1114
O
ASP
A
205
79.998
23.676
2.685
1.00
23.62
A


ATOM
1115
N
LEU
A
206
79.995
23.755
0.442
1.00
23.31
A


ATOM
1116
CA
LEU
A
206
81.206
22.978
0.321
1.00
24.19
A


ATOM
1117
CB
LEU
A
206
81.311
22.406
−1.088
1.00
24.78
A


ATOM
1118
CG
LEU
A
206
82.353
21.309
−1.285
1.00
25.24
A


ATOM
1119
CD1
LEU
A
206
82.075
20.173
−0.317
1.00
26.72
A


ATOM
1120
CD2
LEU
A
206
82.298
20.808
−2.720
1.00
24.32
A


ATOM
1121
C
LEU
A
206
82.408
23.853
0.623
1.00
24.52
A


ATOM
1122
O
LEU
A
206
82.508
24.977
0.130
1.00
24.34
A


ATOM
1123
N
LYS
A
207
83.328
23.330
1.424
1.00
22.98
A


ATOM
1124
CA
LYS
A
207
84.517
24.083
1.796
1.00
23.05
A


ATOM
1125
CB
LYS
A
207
84.113
25.305
2.629
1.00
21.18
A


ATOM
1126
CG
LYS
A
207
83.278
24.948
3.830
1.00
19.29
A


ATOM
1127
CD
LYS
A
207
82.775
26.179
4.568
1.00
23.68
A


ATOM
1128
CE
LYS
A
207
81.913
25.781
5.767
1.00
21.99
A


ATOM
1129
NZ
LYS
A
207
81.580
26.910
6.686
1.00
25.14
A


ATOM
1130
C
LYS
A
207
85.444
23.183
2.602
1.00
23.54
A


ATOM
1131
O
LYS
A
207
85.014
22.169
3.144
1.00
26.04
A


ATOM
1132
N
PRO
A
208
86.728
23.550
2.697
1.00
23.78
A


ATOM
1133
CD
PRO
A
208
87.309
24.764
2.100
1.00
21.90
A


ATOM
1134
CA
PRO
A
208
87.754
22.801
3.429
1.00
23.64
A


ATOM
1135
CB
PRO
A
208
88.948
23.750
3.397
1.00
22.67
A


ATOM
1136
CG
PRO
A
208
88.779
24.432
2.084
1.00
23.00
A


ATOM
1137
C
PRO
A
208
87.393
22.390
4.859
1.00
24.47
A


ATOM
1138
O
PRO
A
208
87.890
21.378
5.358
1.00
24.20
A


ATOM
1139
N
GLU
A
209
86.541
23.176
5.514
1.00
25.33
A


ATOM
1140
CA
GLU
A
209
86.132
22.903
6.894
1.00
26.78
A


ATOM
1141
CB
GLU
A
209
85.641
24.190
7.570
1.00
27.82
A


ATOM
1142
CG
GLU
A
209
86.616
25.359
7.479
1.00
34.76
A


ATOM
1143
CD
GLU
A
209
86.459
26.183
6.199
1.00
39.84
A


ATOM
1144
OE1
GLU
A
209
86.575
25.628
5.079
1.00
38.56
A


ATOM
1145
OE2
GLU
A
209
86.219
27.405
6.322
1.00
44.97
A


ATOM
1146
C
GLU
A
209
85.039
21.840
6.972
1.00
26.70
A


ATOM
1147
O
GLU
A
209
84.786
21.269
8.035
1.00
29.78
A


ATOM
1148
N
ASN
A
210
84.395
21.583
5.841
1.00
24.55
A


ATOM
1149
CA
ASN
A
210
83.339
20.587
5.751
1.00
24.33
A


ATOM
1150
CB
ASN
A
210
82.195
21.105
4.866
1.00
27.29
A


ATOM
1151
CG
ASN
A
210
81.225
21.998
5.622
1.00
31.63
A


ATOM
1152
OD1
ASN
A
210
80.280
22.539
5.040
1.00
35.25
A


ATOM
1153
ND2
ASN
A
210
81.449
22.155
6.923
1.00
30.78
A


ATOM
1154
C
ASN
A
210
83.885
19.289
5.158
1.00
22.61
A


ATOM
1155
O
ASN
A
210
83.207
18.268
5.155
1.00
19.95
A


ATOM
1156
N
ILE
A
211
85.105
19.344
4.638
1.00
22.15
A


ATOM
1157
CA
ILE
A
211
85.733
18.174
4.043
1.00
21.36
A


ATOM
1158
CB
ILE
A
211
86.467
18.538
2.744
1.00
20.33
A


ATOM
1159
CG2
ILE
A
211
87.167
17.315
2.180
1.00
20.04
A


ATOM
1160
CG1
ILE
A
211
85.475
19.089
1.719
1.00
19.57
A


ATOM
1161
CD1
ILE
A
211
86.162
19.718
0.517
1.00
20.56
A


ATOM
1162
C
ILE
A
211
86.733
17.629
5.048
1.00
22.45
A


ATOM
1163
O
ILE
A
211
87.805
18.209
5.254
1.00
21.87
A


ATOM
1164
N
LEU
A
212
86.377
16.510
5.670
1.00
21.03
A


ATOM
1165
CA
LEU
A
212
87.228
15.910
6.685
1.00
20.43
A


ATOM
1166
CB
LEU
A
212
86.352
15.331
7.801
1.00
19.57
A


ATOM
1167
CG
LEU
A
212
85.270
16.281
8.347
1.00
19.01
A


ATOM
1168
CD1
LEU
A
212
84.543
15.613
9.494
1.00
16.54
A


ATOM
1169
CD2
LEU
A
212
85.903
17.592
8.817
1.00
19.58
A


ATOM
1170
C
LEU
A
212
88.148
14.833
6.139
1.00
20.95
A


ATOM
1171
O
LEU
A
212
88.034
14.420
4.983
1.00
20.16
A


ATOM
1172
N
LEU
A
213
89.069
14.379
6.978
1.00
21.07
A


ATOM
1173
CA
LEU
A
213
89.991
13.330
6.578
1.00
21.58
A


ATOM
1174
CB
LEU
A
213
91.415
13.882
6.520
1.00
21.17
A


ATOM
1175
CG
LEU
A
213
91.633
14.944
5.440
1.00
21.26
A


ATOM
1176
CD1
LEU
A
213
93.051
15.466
5.514
1.00
23.93
A


ATOM
1177
CD2
LEU
A
213
91.378
14.335
4.070
1.00
23.36
A


ATOM
1178
C
LEU
A
213
89.912
12.161
7.554
1.00
22.28
A


ATOM
1179
O
LEU
A
213
89.948
12.354
8.766
1.00
23.80
A


ATOM
1180
N
ASN
A
214
89.786
10.949
7.025
1.00
22.96
A


ATOM
1181
CA
ASN
A
214
89.718
9.766
7.872
1.00
22.83
A


ATOM
1182
CB
ASN

214
88.997
8.647
7.103
0.50
23.75
AC1


ATOM
1183
CG
ASN

214
89.144
7.286
7.756
0.50
25.62
AC1


ATOM
1184
OD1
ASN

214
90.212
6.673
7.713
0.50
25.34
AC1


ATOM
1185
ND2
ASN

214
88.066
6.803
8.363
0.50
26.41
AC1


ATOM
1186
C
ASN
A
214
91.151
9.354
8.228
1.00
23.68
A


ATOM
1187
O
ASN
A
214
92.112
9.934
7.716
1.00
20.85
A


ATOM
1188
N
GLU
A
215
91.291
8.379
9.119
1.00
25.06
A


ATOM
1189
CA
GLU
A
215
92.603
7.901
9.545
1.00
26.20
A


ATOM
1190
CB
GLU
A
215
92.453
6.669
10.435
1.00
26.19
A


ATOM
1191
CG
GLU
A
215
93.770
6.153
10.985
1.00
29.08
A


ATOM
1192
CD
GLU
A
215
93.589
4.963
11.907
0.00
28.21
A


ATOM
1193
OE1
GLU
A
215
93.064
3.927
11.449
0.00
28.42
A


ATOM
1194
OE2
GLU
A
215
93.973
5.065
13.092
0.00
28.42
A


ATOM
1195
C
GLU
A
215
93.532
7.566
8.385
1.00
26.12
A


ATOM
1196
O
GLU
A
215
94.746
7.743
8.487
1.00
29.48
A


ATOM
1197
N
ASP
A
216
92.976
7.070
7.287
1.00
25.52
A


ATOM
1198
CA
ASP
A
216
93.798
6.728
6.133
1.00
25.79
A


ATOM
1199
CB
ASP

216
93.164
5.564
5.376
0.50
27.09
AC1


ATOM
1200
CG
ASP

216
93.450
4.231
6.027
0.50
29.11
AC1


ATOM
1201
OD1
ASP

216
93.206
4.098
7.244
0.50
31.09
AC1


ATOM
1202
OD2
ASP

216
93.921
3.315
5.320
0.50
31.52
AC1


ATOM
1203
C
ASP
A
216
94.034
7.896
5.173
1.00
24.88
A


ATOM
1204
O
ASP
A
216
94.586
7.719
4.094
1.00
26.27
A


ATOM
1205
N
MET
A
217
93.615
9.087
5.578
1.00
25.04
A


ATOM
1206
CA
MET
A
217
93.789
10.301
4.792
1.00
24.86
A


ATOM
1207
CB
MET
A
217
95.270
10.503
4.454
1.00
28.81
A


ATOM
1208
CG
MET
A
217
96.139
10.834
5.676
1.00
29.66
A


ATOM
1209
SD
MET
A
217
95.577
12.323
6.551
1.00
34.79
A


ATOM
1210
CE
MET
A
217
96.130
13.598
5.411
1.00
30.61
A


ATOM
1211
C
MET
A
217
92.942
10.437
3.528
1.00
24.93
A


ATOM
1212
O
MET
A
217
93.277
11.215
2.629
1.00
23.08
A


ATOM
1213
N
HIS
A
218
91.855
9.678
3.450
1.00
21.48
A


ATOM
1214
CA
HIS
A
218
90.947
9.799
2.319
1.00
21.72
A


ATOM
1215
CB
HIS
A
218
90.325
8.444
1.963
1.00
21.43
A


ATOM
1216
CG
HIS
A
218
91.225
7.578
1.138
1.00
24.55
A


ATOM
1217
CD2
HIS
A
218
91.951
6.478
1.458
1.00
23.50
A


ATOM
1218
ND1
HIS
A
218
91.522
7.860
−0.179
1.00
23.64
A


ATOM
1219
CE1
HIS
A
218
92.392
6.975
−0.633
1.00
21.12
A


ATOM
1220
NE2
HIS
A
218
92.670
6.128
0.340
1.00
22.96
A


ATOM
1221
C
HIS
A
218
89.891
10.785
2.812
1.00
20.49
A


ATOM
1222
O
HIS
A
218
89.683
10.911
4.018
1.00
20.60
A


ATOM
1223
N
ILE
A
219
89.231
11.488
1.897
1.00
18.82
A


ATOM
1224
CA
ILE
A
219
88.244
12.473
2.306
1.00
17.27
A


ATOM
1225
CB
ILE
A
219
87.914
13.487
1.178
1.00
15.59
A


ATOM
1226
CG2
ILE
A
219
89.175
14.201
0.718
1.00
14.62
A


ATOM
1227
CG1
ILE
A
219
87.252
12.769
0.006
1.00
16.04
A


ATOM
1228
CD1
ILE
A
219
86.458
13.685
−0.888
1.00
15.29
A


ATOM
1229
C
ILE
A
219
86.934
11.885
2.772
1.00
17.64
A


ATOM
1230
O
ILE
A
219
86.564
10.774
2.402
1.00
18.93
A


ATOM
1231
N
GLN
A
220
86.240
12.658
3.597
1.00
19.19
A


ATOM
1232
CA
GLN
A
220
84.933
12.293
4.119
1.00
21.50
A


ATOM
1233
CB
GLN
A
220
85.061
11.585
5.475
1.00
23.96
A


ATOM
1234
CG
GLN
A
220
85.583
10.151
5.334
1.00
29.77
A


ATOM
1235
CD
GLN
A
220
84.945
9.182
6.319
1.00
33.77
A


ATOM
1236
OE1
GLN
A
220
85.257
9.188
7.513
1.00
37.87
A


ATOM
1237
NE2
GLN
A
220
84.040
8.347
5.821
1.00
34.29
A


ATOM
1238
C
GLN
A
220
84.158
13.599
4.240
1.00
21.53
A


ATOM
1239
O
GLN
A
220
84.367
14.393
5.166
1.00
22.54
A


ATOM
1240
N
ILE
A
221
83.284
13.833
3.270
1.00
19.63
A


ATOM
1241
CA
ILE
A
221
82.498
15.054
3.234
1.00
19.30
A


ATOM
1242
CB
ILE
A
221
82.055
15.366
1.785
1.00
20.41
A


ATOM
1243
CG2
ILE
A
221
81.237
16.639
1.738
1.00
19.39
A


ATOM
1244
CG1
ILE
A
221
83.290
15.524
0.900
1.00
19.44
A


ATOM
1245
CD1
ILE
A
221
82.977
15.802
−0.550
1.00
17.44
A


ATOM
1246
C
ILE
A
221
81.284
14.951
4.141
1.00
18.36
A


ATOM
1247
O
ILE
A
221
80.627
13.911
4.204
1.00
15.98
A


ATOM
1248
N
THR
A
222
80.995
16.024
4.864
1.00
19.59
A


ATOM
1249
CA
THR
A
222
79.844
16.008
5.753
1.00
22.76
A


ATOM
1250
CB
THR
A
222
80.218
15.420
7.126
1.00
23.86
A


ATOM
1251
OG1
THR
A
222
79.019
15.145
7.863
1.00
28.20
A


ATOM
1252
CG2
THR
A
222
81.105
16.380
7.908
1.00
23.65
A


ATOM
1253
C
THR
A
222
79.179
17.370
5.933
1.00
23.55
A


ATOM
1254
O
THR
A
222
79.505
18.334
5.229
1.00
25.65
A


ATOM
1255
N
ASP
A
223
78.248
17.427
6.881
1.00
24.38
A


ATOM
1256
CA
ASP
A
223
77.449
18.611
7.202
1.00
25.25
A


ATOM
1257
CB
ASP
A
223
78.303
19.865
7.422
1.00
26.12
A


ATOM
1258
CG
ASP
A
223
77.538
20.962
8.175
1.00
29.92
A


ATOM
1259
OD1
ASP
A
223
76.288
20.876
8.278
1.00
31.91
A


ATOM
1260
OD2
ASP
A
223
78.177
21.911
8.671
1.00
32.94
A


ATOM
1261
C
ASP
A
223
76.461
18.882
6.080
1.00
25.61
A


ATOM
1262
O
ASP
A
223
76.693
19.744
5.227
1.00
25.81
A


ATOM
1263
N
PHE
A
224
75.358
18.139
6.098
1.00
25.18
A


ATOM
1264
CA
PHE
A
224
74.310
18.266
5.096
1.00
26.75
A


ATOM
1265
CB
PHE
A
224
73.860
16.879
4.635
1.00
27.24
A


ATOM
1266
CG
PHE
A
224
74.857
16.189
3.753
1.00
28.10
A


ATOM
1267
CD1
PHE
A
224
74.889
16.450
2.388
1.00
29.12
A


ATOM
1268
CD2
PHE
A
224
75.790
15.313
4.291
1.00
28.67
A


ATOM
1269
CE1
PHE
A
224
75.841
15.847
1.567
1.00
30.28
A


ATOM
1270
CE2
PHE
A
224
76.745
14.706
3.482
1.00
31.49
A


ATOM
1271
CZ
PHE
A
224
76.770
14.973
2.117
1.00
30.54
A


ATOM
1272
C
PHE
A
224
73.124
19.038
5.632
1.00
27.73
A


ATOM
1273
O
PHE
A
224
72.005
18.895
5.140
1.00
27.84
A


ATOM
1274
N
GLY
A
225
73.378
19.862
6.643
1.00
29.36
A


ATOM
1275
CA
GLY
A
225
72.319
20.656
7.235
1.00
30.10
A


ATOM
1276
C
GLY
A
225
71.825
21.741
6.297
1.00
31.32
A


ATOM
1277
O
GLY
A
225
70.714
22.248
6.451
1.00
32.90
A


ATOM
1278
N
THR
A
226
72.640
22.091
5.311
1.00
29.95
A


ATOM
1279
CA
THR
A
226
72.261
23.132
4.365
1.00
32.06
A


ATOM
1280
CB
THR
A
226
73.381
24.167
4.226
1.00
33.35
A


ATOM
1281
OG1
THR
A
226
74.454
23.608
3.455
1.00
35.74
A


ATOM
1282
CG2
THR
A
226
73.920
24.542
5.593
1.00
34.02
A


ATOM
1283
C
THR
A
226
71.979
22.551
2.983
1.00
31.11
A


ATOM
1284
O
THR
A
226
71.801
23.288
2.012
1.00
30.89
A


ATOM
1285
N
ALA
A
227
71.938
21.230
2.899
1.00
30.02
A


ATOM
1286
CA
ALA
A
227
71.714
20.566
1.624
1.00
32.20
A


ATOM
1287
CB
ALA
A
227
71.906
19.057
1.770
1.00
29.19
A


ATOM
1288
C
ALA
A
227
70.345
20.865
1.045
1.00
32.77
A


ATOM
1289
O
ALA
A
227
69.431
21.269
1.761
1.00
34.17
A


ATOM
1290
N
ALA
A
228
70.229
20.684
−0.266
1.00
33.18
A


ATOM
1291
CA
ALA
A
228
68.980
20.902
−0.982
1.00
34.43
A


ATOM
1292
CB
ALA
A
228
69.079
22.146
−1.861
1.00
32.03
A


ATOM
1293
C
ALA
A
228
68.742
19.674
−1.846
1.00
35.25
A


ATOM
1294
O
ALA
A
228
69.612
19.284
−2.622
1.00
36.70
A


ATOM
1295
N
VAL
A
229
67.578
19.056
−1.698
1.00
36.21
A


ATOM
1296
CA
VAL
A
229
67.246
17.876
−2.488
1.00
37.95
A


ATOM
1297
CB
VAL
A
229
66.438
16.857
−1.674
1.00
37.37
A


ATOM
1298
CG1
VAL
A
229
66.192
15.609
−2.506
1.00
35.62
A


ATOM
1299
CG2
VAL
A
229
67.176
16.522
−0.394
1.00
36.39
A


ATOM
1300
C
VAL
A
229
66.393
18.341
−3.649
1.00
40.15
A


ATOM
1301
O
VAL
A
229
65.353
18.965
−3.446
1.00
39.20
A


ATOM
1302
N
LEU
A
230
66.836
18.044
−4.865
1.00
43.75
A


ATOM
1303
CA
LEU
A
230
66.105
18.455
−6.054
1.00
48.04
A


ATOM
1304
CB
LEU
A
230
67.039
18.473
−7.258
1.00
48.59
A


ATOM
1305
CG
LEU
A
230
68.123
19.552
−7.212
1.00
50.35
A


ATOM
1306
CD1
LEU
A
230
69.118
19.312
−8.326
1.00
50.62
A


ATOM
1307
CD2
LEU
A
230
67.488
20.932
−7.330
1.00
50.11
A


ATOM
1308
C
LEU
A
230
64.905
17.569
−6.346
1.00
51.38
A


ATOM
1309
O
LEU
A
230
64.929
16.364
−6.095
1.00
51.84
A


ATOM
1310
N
SER
A
231
63.854
18.190
−6.872
1.00
56.03
A


ATOM
1311
CA
SER
A
231
62.616
17.502
−7.224
1.00
60.24
A


ATOM
1312
CB
SER
A
231
61.528
17.806
−6.186
1.00
60.77
A


ATOM
1313
OG
SER
A
231
61.222
19.192
−6.150
1.00
61.08
A


ATOM
1314
C
SER
A
231
62.115
17.894
−8.622
1.00
62.65
A


ATOM
1315
O
SER
A
231
61.527
17.068
−9.326
1.00
63.42
A


ATOM
1316
N
PRO
A
232
62.334
19.161
−9.040
1.00
64.66
A


ATOM
1317
CD
PRO
A
232
62.903
20.298
−8.289
1.00
64.95
A


ATOM
1318
CA
PRO
A
232
61.882
19.604
−10.367
1.00
65.69
A


ATOM
1319
CB
PRO
A
232
62.409
21.037
−10.450
1.00
65.77
A


ATOM
1320
CG
PRO
A
232
62.341
21.493
−9.031
1.00
65.52
A


ATOM
1321
C
PRO
A
232
62.408
18.731
−11.505
1.00
66.28
A


ATOM
1322
O
PRO
A
232
62.858
19.241
−12.532
1.00
66.55
A


ATOM
1323
N
ALA
A
239
65.927
26.021
−3.995
1.00
92.57
A


ATOM
1324
CA
ALA
A
239
67.330
26.100
−3.606
1.00
92.64
A


ATOM
1325
CB
ALA
A
239
68.187
25.262
−4.558
1.00
92.15
A


ATOM
1326
C
ALA
A
239
67.769
27.558
−3.640
1.00
92.34
A


ATOM
1327
O
ALA
A
239
68.683
27.930
−4.373
1.00
92.47
A


ATOM
1328
N
ASN
A
240
67.108
28.379
−2.833
1.00
91.92
A


ATOM
1329
CA
ASN
A
240
67.396
29.809
−2.767
1.00
91.12
A


ATOM
1330
CB
ASN
A
240
66.374
30.566
−3.617
1.00
92.32
A


ATOM
1331
CG
ASN
A
240
64.947
30.084
−3.378
1.00
93.20
A


ATOM
1332
OD1
ASN
A
240
64.471
30.061
−2.244
1.00
93.46
A


ATOM
1333
ND2
ASN
A
240
64.261
29.697
−4.452
1.00
94.00
A


ATOM
1334
C
ASN
A
240
67.334
30.332
−1.335
1.00
89.78
A


ATOM
1335
O
ASN
A
240
67.766
31.453
−1.053
1.00
89.80
A


ATOM
1336
N
ALA
A
241
66.787
29.515
−0.441
1.00
88.16
A


ATOM
1337
CA
ALA
A
241
66.624
29.891
0.955
1.00
86.55
A


ATOM
1338
C
ALA
A
241
67.901
29.893
1.792
1.00
84.55
A


ATOM
1339
O
ALA
A
241
67.865
30.268
2.961
1.00
84.76
A


ATOM
1340
CB
ALA
A
241
65.583
28.978
1.623
1.00
88.01
A


ATOM
1341
N
PHE
A
242
69.028
29.494
1.216
1.00
82.28
A


ATOM
1342
CA
PHE
A
242
70.264
29.483
1.993
1.00
79.83
A


ATOM
1343
CB
PHE
A
242
70.718
28.046
2.282
1.00
79.60
A


ATOM
1344
CG
PHE
A
242
71.980
27.962
3.100
1.00
79.10
A


ATOM
1345
CD1
PHE
A
242
72.024
28.483
4.388
1.00
79.45
A


ATOM
1346
CD2
PHE
A
242
73.131
27.392
2.571
1.00
79.42
A


ATOM
1347
CE1
PHE
A
242
73.202
28.442
5.143
1.00
79.29
A


ATOM
1348
CE2
PHE
A
242
74.314
27.345
3.317
1.00
80.20
A


ATOM
1349
CZ
PHE
A
242
74.348
27.872
4.605
1.00
79.98
A


ATOM
1350
C
PHE
A
242
71.402
30.231
1.322
1.00
77.56
A


ATOM
1351
O
PHE
A
242
71.347
30.524
0.130
1.00
78.59
A


ATOM
1352
N
VAL
A
243
72.440
30.529
2.098
1.00
73.76
A


ATOM
1353
CA
VAL
A
243
73.595
31.238
1.579
1.00
70.34
A


ATOM
1354
CB
VAL
A
243
73.864
32.515
2.405
1.00
71.71
A


ATOM
1355
CG1
VAL
A
243
75.087
33.238
1.85
91.00
71.29
A


ATOM
1356
CG2
VAL
A
243
72.638
33.425
2.376
1.00
71.41
A


ATOM
1357
C
VAL
A
243
74.851
30.362
1.581
1.00
66.69
A


ATOM
1358
O
VAL
A
243
75.232
29.802
0.552
1.00
66.50
A


ATOM
1359
N
GLY
A
244
75.496
30.245
2.737
1.00
62.34
A


ATOM
1360
CA
GLY
A
244
76.708
29.444
2.829
1.00
56.48
A


ATOM
1361
C
GLY
A
244
77.889
30.327
3.168
1.00
52.17
A


ATOM
1362
O
GLY
A
244
77.769
31.547
3.136
1.00
52.14
A


ATOM
1363
N
THR
A
245
79.031
29.733
3.490
1.00
48.25
A


ATOM
1364
CA
THR
A
245
80.201
30.530
3.838
1.00
44.49
A


ATOM
1365
CB
THR
A
245
81.413
29.633
4.106
1.00
45.53
A


ATOM
1366
OG1
THR
A
245
80.994
28.514
4.899
1.00
45.14
A


ATOM
1367
CG2
THR
A
245
82.486
30.403
4.873
1.00
42.13
A


ATOM
1368
C
THR
A
245
80.523
31.537
2.734
1.00
40.69
A


ATOM
1369
O
THR
A
245
80.722
31.175
1.572
1.00
38.45
A


ATOM
1370
N
ALA
A
246
80.570
32.804
3.127
1.00
36.53
A


ATOM
1371
CA
ALA
A
246
80.816
33.915
2.219
1.00
34.68
A


ATOM
1372
CB
ALA
A
246
81.106
35.186
3.023
1.00
34.13
A


ATOM
1373
C
ALA
A
246
81.896
33.718
1.164
1.00
33.21
A


ATOM
1374
O
ALA
A
246
81.655
33.958
−0.015
1.00
33.62
A


ATOM
1375
N
GLN
A
247
83.082
33.281
1.567
1.00
31.02
A


ATOM
1376
CA
GLN
A
247
84.151
33.112
0.595
1.00
31.05
A


ATOM
1377
CB
GLN
A
247
85.476
32.814
1.310
1.00
33.25
A


ATOM
1378
CG
GLN
A
247
85.921
33.931
2.253
1.00
37.08
A


ATOM
1379
CD
GLN
A
247
87.378
33.831
2.665
1.00
40.56
A


ATOM
1380
OE1
GLN
A
247
88.272
34.328
1.972
1.00
41.24
A


ATOM
1381
NE2
GLN
A
247
87.626
33.180
3.794
1.00
41.86
A


ATOM
1382
C
GLN
A
247
83.895
32.069
−0.488
1.00
28.53
A


ATOM
1383
O
GLN
A
247
84.544
32.093
−1.527
1.00
27.93
A


ATOM
1384
N
TYR
A
248
82.934
31.177
−0.267
1.00
28.01
A


ATOM
1385
CA
TYR
A
248
82.643
30.115
−1.238
1.00
28.20
A


ATOM
1386
CB
TYR
A
248
82.725
28.757
−0.532
1.00
24.94
A


ATOM
1387
CG
TYR
A
248
84.064
28.533
0.126
1.00
23.77
A


ATOM
1388
CD1
TYR
A
248
85.153
28.073
−0.611
1.00
23.01
A


ATOM
1389
CE1
TYR
A
248
86.421
27.975
−0.039
1.00
24.66
A


ATOM
1390
CD2
TYR
A
248
84.270
28.879
1.464
1.00
24.01
A


ATOM
1391
CE2
TYR
A
248
85.535
28.785
2.050
1.00
24.49
A


ATOM
1392
CZ
TYR
A
248
86.606
28.338
1.286
1.00
26.11
A


ATOM
1393
OH
TYR
A
248
87.868
28.305
1.828
1.00
27.54
A


ATOM
1394
C
TYR
A
248
81.301
30.249
−1.961
1.00
28.78
A


ATOM
1395
O
TYR
A
248
80.939
29.405
−2.777
1.00
30.26
A


ATOM
1396
N
VAL
A
249
80.576
31.319
−1.663
1.00
28.83
A


ATOM
1397
CA
VAL
A
249
79.281
31.584
−2.275
1.00
28.70
A


ATOM
1398
CB
VAL
A
249
78.625
32.803
−1.601
1.00
29.37
A


ATOM
1399
CG1
VAL
A
249
77.333
33.163
−2.297
1.00
30.56
A


ATOM
1400
CG2
VAL
A
249
78.376
32.488
−0.127
1.00
31.25
A


ATOM
1401
C
VAL
A
249
79.404
31.837
−3.779
1.00
28.19
A


ATOM
1402
O
VAL
A
249
80.335
32.497
−4.231
1.00
27.69
A


ATOM
1403
N
SER
A
250
78.460
31.308
−4.549
1.00
28.16
A


ATOM
1404
CA
SER
A
250
78.476
31.481
−5.993
1.00
29.05
A


ATOM
1405
CB
SER
A
250
77.835
30.273
−6.691
1.00
31.08
A


ATOM
1406
OG
SER
A
250
76.497
30.058
−6.264
1.00
31.33
A


ATOM
1407
C
SER
A
250
77.737
32.752
−6.376
1.00
29.69
A


ATOM
1408
O
SER
A
250
76.820
33.191
−5.685
1.00
29.14
A


ATOM
1409
N
PRO
A
251
78.131
33.361
−7.494
1.00
29.35
A


ATOM
1410
CD
PRO
A
251
79.147
32.917
−8.463
1.00
29.28
A


ATOM
1411
CA
PRO
A
251
77.477
34.592
−7.934
1.00
30.27
A


ATOM
1412
CB
PRO
A
251
78.214
34.932
−9.235
1.00
29.87
A


ATOM
1413
CG
PRO
A
251
78.687
33.588
−9.730
1.00
30.48
A


ATOM
1414
C
PRO
A
251
75.961
34.495
−8.114
1.00
30.86
A


ATOM
1415
O
PRO
A
251
75.246
35.442
−7.801
1.00
33.28
A


ATOM
1416
N
GLU
A
252
75.459
33.367
−8.602
1.00
30.19
A


ATOM
1417
CA
GLU
A
252
74.014
33.244
−8.802
1.00
30.91
A


ATOM
1418
CB
GLU
A
252
73.649
31.903
−9.449
1.00
30.61
A


ATOM
1419
CG
GLU
A
252
74.162
30.682
−8.689
1.00
33.88
A


ATOM
1420
CD
GLU
A
252
75.493
30.171
−9.219
1.00
32.82
A


ATOM
1421
OE1
GLU
A
252
76.277
30.987
−9.747
1.00
35.25
A


ATOM
1422
OE2
GLU
A
252
75.756
28.956
−9.095
1.00
32.14
A


ATOM
1423
C
GLU
A
252
73.260
33.390
−7.494
1.00
32.09
A


ATOM
1424
O
GLU
A
252
72.157
33.928
−7.469
1.00
32.01
A


ATOM
1425
N
LEU
A
253
73.852
32.900
−6.408
1.00
33.87
A


ATOM
1426
CA
LEU
A
253
73.230
32.988
−5.096
1.00
35.16
A


ATOM
1427
CB
LEU
A
253
74.031
32.183
−4.078
1.00
37.63
A


ATOM
1428
CG
LEU
A
253
73.371
30.937
−3.479
1.00
40.98
A


ATOM
1429
CD1
LEU
A
253
74.302
30.321
−2.433
1.00
42.16
A


ATOM
1430
CD2
LEU
A
253
72.043
31.314
−2.835
1.00
40.33
A


ATOM
1431
C
LEU
A
253
73.148
34.445
−4.640
1.00
37.20
A


ATOM
1432
O
LEU
A
253
72.300
34.810
−3.820
1.00
37.33
A


ATOM
1433
N
LEU
A
254
74.036
35.276
−5.171
1.00
36.48
A


ATOM
1434
CA
LEU
A
254
74.052
36.686
−4.816
1.00
37.76
A


ATOM
1435
CB
LEU
A
254
75.481
37.235
−4.890
1.00
35.47
A


ATOM
1436
CG
LEU
A
254
76.512
36.692
−3.899
1.00
32.31
A


ATOM
1437
CD1
LEU
A
254
77.839
37.416
−4.108
1.00
32.18
A


ATOM
1438
CD2
LEU
A
254
76.019
36.891
−2.474
1.00
29.68
A


ATOM
1439
C
LEU
A
254
73.150
37.496
−5.737
1.00
39.82
A


ATOM
1440
O
LEU
A
254
72.772
38.615
−5.409
1.00
39.15
A


ATOM
1441
N
THR
A
255
72.805
36.919
−6.885
1.00
44.09
A


ATOM
1442
CA
THR
A
255
71.959
37.594
−7.865
1.00
47.95
A


ATOM
1443
CB
THR
A
255
72.591
37.544
−9.276
1.00
48.10
A


ATOM
1444
OG1
THR
A
255
73.924
38.072
−9.227
1.00
48.96
A


ATOM
1445
CG2
THR
A
255
71.768
38.376
−10.253
1.00
50.10
A


ATOM
1446
C
THR
A
255
70.538
37.032
−7.954
1.00
49.95
A


ATOM
1447
O
THR
A
255
69.631
37.537
−7.300
1.00
51.66
A


ATOM
1448
N
GLU
A
256
70.344
35.994
−8.764
1.00
52.84
A


ATOM
1449
CA
GLU
A
256
69.018
35.395
−8.939
1.00
55.77
A


ATOM
1450
CB
GLU
A
256
69.036
34.342
−10.061
1.00
55.24
A


ATOM
1451
CG
GLU
A
256
70.360
34.171
−10.790
0.00
55.40
A


ATOM
1452
CD
GLU
A
256
70.699
35.348
−11.681
0.00
55.34
A


ATOM
1453
OE1
GLU
A
256
69.831
35.760
−12.480
0.00
55.36
A


ATOM
1454
OE2
GLU
A
256
71.837
35.852
−11.593
0.00
55.36
A


ATOM
1455
C
GLU
A
256
68.451
34.743
−7.677
1.00
57.04
A


ATOM
1456
O
GLU
A
256
67.396
34.107
−7.732
1.00
56.82
A


ATOM
1457
N
LYS
A
257
69.137
34.911
−6.549
1.00
58.87
A


ATOM
1458
CA
LYS
A
257
68.711
34.308
−5.286
1.00
60.38
A


ATOM
1459
CB
LYS
A
257
67.607
35.151
−4.623
1.00
60.84
A


ATOM
1460
CG
LYS
A
257
66.327
35.322
−5.430
0.00
60.71
A


ATOM
1461
CD
LYS
A
257
65.352
36.261
−4.731
0.00
60.78
A


ATOM
1462
CE
LYS
A
257
64.943
35.734
−3.363
0.00
60.77
A


ATOM
1463
NZ
LYS
A
257
63.992
36.650
−2.674
0.00
60.78
A


ATOM
1464
C
LYS
A
257
68.227
32.878
−5.546
1.00
61.40
A


ATOM
1465
O
LYS
A
257
67.046
32.565
−5.389
1.00
61.84
A


ATOM
1466
N
SER
A
258
69.160
32.020
−5.958
1.00
61.26
A


ATOM
1467
CA
SER
A
258
68.865
30.622
−6.271
1.00
61.31
A


ATOM
1468
CB
SER
A
258
68.105
30.548
−7.605
1.00
62.95
A


ATOM
1469
OG
SER
A
258
68.707
31.374
−8.596
1.00
63.22
A


ATOM
1470
C
SER
A
258
70.149
29.771
−6.334
1.00
60.39
A


ATOM
1471
O
SER
A
258
71.257
30.312
−6.329
1.00
60.58
A


ATOM
1472
N
ALA
A
259
70.001
28.447
−6.393
1.00
57.62
A


ATOM
1473
CA
ALA
A
259
71.159
27.551
−6.441
1.00
54.75
A


ATOM
1474
CB
ALA
A
259
71.670
27.289
−5.025
1.00
54.90
A


ATOM
1475
C
ALA
A
259
70.890
26.218
−7.147
1.00
52.13
A


ATOM
1476
O
ALA
A
259
69.759
25.726
−7.175
1.00
51.63
A


ATOM
1477
N
CYS
A
260
71.945
25.641
−7.712
1.00
48.49
A


ATOM
1478
CA
CYS
A
260
71.848
24.371
−8.417
1.00
44.82
A


ATOM
1479
CB
CYS
A
260
71.499
24.596
−9.890
1.00
46.78
A


ATOM
1480
SG
CYS
A
260
72.731
25.549
−10.821
1.00
53.48
A


ATOM
1481
C
CYS
A
260
73.176
23.643
−8.310
1.00
41.48
A


ATOM
1482
O
CYS
A
260
74.085
24.090
−7.612
1.00
41.05
A


ATOM
1483
N
LYS
A
261
73.288
22.525
−9.012
1.00
37.76
A


ATOM
1484
CA
LYS
A
261
74.503
21.729
−8.980
1.00
34.90
A


ATOM
1485
CB
LYS
A
261
74.394
20.587
−9.990
1.00
35.93
A


ATOM
1486
CG
LYS
A
261
73.239
19.644
−9.691
1.00
38.46
A


ATOM
1487
CD
LYS
A
261
73.239
18.430
−10.601
1.00
39.70
A


ATOM
1488
CE
LYS
A
261
72.117
17.474
−10.229
1.00
40.95
A


ATOM
1489
NZ
LYS
A
261
72.076
16.269
−11.110
1.00
41.64
A


ATOM
1490
C
LYS
A
261
75.751
22.556
−9.247
1.00
32.19
A


ATOM
1491
O
LYS
A
261
76.780
22.366
−8.595
1.00
30.08
A


ATOM
1492
N
SER
A
262
75.651
23.480
−10.200
1.00
30.41
A


ATOM
1493
CA
SER
A
262
76.771
24.337
−10.556
1.00
27.88
A


ATOM
1494
CB
SER
A
262
76.361
25.333
−11.643
1.00
29.04
A


ATOM
1495
OG
SER
A
262
76.398
24.732
−12.921
1.00
32.20
A


ATOM
1496
C
SER
A
262
77.325
25.095
−9.360
1.00
27.01
A


ATOM
1497
O
SER
A
262
78.515
25.403
−9.320
1.00
27.37
A


ATOM
1498
N
SER
A
263
76.469
25.406
−8.392
1.00
24.83
A


ATOM
1499
CA
SER
A
263
76.924
26.115
−7.201
1.00
26.29
A


ATOM
1500
CB
SER
A
263
75.758
26.354
−6.242
1.00
26.59
A


ATOM
1501
OG
SER
A
263
74.830
27.254
−6.832
1.00
30.68
A


ATOM
1502
C
SER
A
263
78.039
25.337
−6.506
1.00
25.15
A


ATOM
503
O
SER
A
263
79.034
25.924
−6.078
1.00
25.38
A


ATOM
1504
N
ASP
A
264
77.884
24.019
−6.396
1.00
23.51
A


ATOM
1505
CA
ASP
A
264
78.930
23.215
−5.773
1.00
22.06
A


ATOM
1506
CB
ASP
A
264
78.500
21.754
−5.613
1.00
23.87
A


ATOM
1507
CG
ASP
A
264
77.378
21.577
−4.599
1.00
27.11
A


ATOM
1508
OD1
ASP
A
264
77.276
22.402
−3.662
1.00
25.60
A


ATOM
1509
OD2
ASP
A
264
76.612
20.599
4.730
1.00
26.16
A


ATOM
1510
C
ASP
A
264
80.175
23.267
−6.642
1.00
20.62
A


ATOM
1511
O
ASP
A
264
81.289
23.339
−6.129
1.00
20.01
A


ATOM
1512
N
LEU
A
265
79.985
23.246
−7.959
1.00
18.87
A


ATOM
1513
CA
LEU
A
265
81.113
23.275
−8.876
1.00
20.02
A


ATOM
1514
CB
LEU
A
265
80.634
23.131
−10.322
1.00
19.94
A


ATOM
1515
CG
LEU
A
265
80.037
21.763
−10.672
1.00
21.08
A


ATOM
1516
CD1
LEU
A
265
79.580
21.771
−12.122
1.00
22.16
A


ATOM
1517
CD2
LEU
A
265
81.077
20.659
−10.449
1.00
16.76
A


ATOM
1518
C
LEU
A
265
81.910
24.552
−8.705
1.00
20.53
A


ATOM
1519
O
LEU
A
265
83.130
24.563
−8.881
1.00
21.94
A


ATOM
1520
N
TRP
A
266
81.221
25.633
−8.361
1.00
21.74
A


ATOM
1521
CA
TRP
A
266
81.897
26.899
−8.138
1.00
20.89
A


ATOM
1522
CB
TRP
A
266
80.879
28.031
−7.960
1.00
22.97
A


ATOM
1523
CG
TRP
A
266
81.477
29.309
−7.411
1.00
24.01
A


ATOM
1524
CD2
TRP
A
266
81.814
30.487
−8.152
1.00
23.31
A


ATOM
1525
CE2
TRP
A
266
82.391
31.404
−7.243
1.00
23.27
A


ATOM
1526
CE3
TRP
A
266
81.689
30.858
−9.497
1.00
24.79
A


ATOM
1527
CD1
TRP
A
266
81.850
29.555
−6.116
1.00
24.55
A


ATOM
1528
NE1
TRP
A
266
82.401
30.811
−6.009
1.00
23.65
A


ATOM
1529
CZ2
TRP
A
266
82.839
32.663
−7.636
1.00
22.89
A


ATOM
1530
CZ3
TRP
A
266
82.139
32.116
−9.887
1.00
23.30
A


ATOM
1531
CH2
TRP
A
266
82.705
33.000
−8.959
1.00
23.32
A


ATOM
1532
C
TRP
A
266
82.739
26.735
−6.877
1.00
20.30
A


ATOM
1533
O
TRP
A
266
83.913
27.102
−6.853
1.00
20.60
A


ATOM
1534
N
ALA
A
267
82.141
26.175
−5.832
1.00
18.06
A


ATOM
1535
CA
ALA
A
267
82.868
25.966
−4.584
1.00
18.46
A


ATOM
1536
CB
ALA
A
267
81.984
25.254
−3.561
1.00
17.96
A


ATOM
1537
C
ALA
A
267
84.112
25.132
−4.877
1.00
18.05
A


ATOM
1538
O
ALA
A
267
85.173
25.340
−4.287
1.00
17.35
A


ATOM
1539
N
LEU
A
268
83.982
24.190
5.799
1.00
17.12
A


ATOM
1540
CA
LEU
A
268
85.118
23.355
−6.157
1.00
18.45
A


ATOM
1541
CB
LEU
A
268
84.703
22.326
−7.204
1.00
17.67
A


ATOM
1542
CG
LEU
A
268
85.809
21.436
−7.772
1.00
16.93
A


ATOM
1543
CD1
LEU
A
268
86.333
20.495
−6.704
1.00
17.10
A


ATOM
1544
CD2
LEU
A
268
85.258
20.651
−8.953
1.00
13.46
A


ATOM
1545
C
LEU
A
268
86.232
24.249
−6.705
1.00
19.64
A


ATOM
1546
O
LEU
A
268
87.389
24.129
−6.306
1.00
18.99
A


ATOM
1547
N
GLY
A
269
85.869
25.158
−7.606
1.00
19.16
A


ATOM
1548
CA
GLY
A
269
86.854
26.057
−8.178
1.00
18.25
A


ATOM
1549
C
GLY
A
269
87.604
26.804
−7.103
1.00
20.30
A


ATOM
1550
O
GLY
A
269
88.825
26.960
−7.178
1.00
20.24
A


ATOM
1551
N
CYS
A
270
86.874
27.266
−6.090
1.00
20.20
A


ATOM
1552
CA
CYS
A
270
87.486
27.996
−4.986
1.00
20.73
A


ATOM
1553
CB
CYS
A
270
86.418
28.523
−4.031
1.00
21.05
A


ATOM
1554
SG
CYS
A
270
85.292
29.703
−4.752
1.00
23.98
A


ATOM
1555
C
CYS
A
270
88.417
27.082
−4.206
1.00
20.77
A


ATOM
1556
O
CYS
A
270
89.550
27.449
−3.878
1.00
22.00
A


ATOM
1557
N
ILE
A
271
87.927
25.886
−3.907
1.00
19.32
A


ATOM
1558
CA
ILE
A
271
88.704
24.921
−3.147
1.00
18.46
A


ATOM
1559
CB
ILE
A
271
87.872
23.668
−2.861
1.00
15.71
A


ATOM
1560
CG2
ILE
A
271
88.722
22.607
−2.182
1.00
16.51
A


ATOM
1561
CG1
ILE
A
271
86.688
24.051
−1.974
1.00
14.97
A


ATOM
1562
CD1
ILE
A
271
85.785
22.891
−1.639
1.00
17.80
A


ATOM
1563
C
ILE
A
271
90.001
24.546
−3.856
1.00
19.30
A


ATOM
1564
O
ILE
A
271
91.062
24.532
−3.242
1.00
21.30
A


ATOM
1565
N
ILE
A
272
89.915
24.253
−5.147
1.00
20.07
A


ATOM
1566
CA
ILE
A
272
91.094
23.894
−5.906
1.00
21.50
A


ATOM
1567
CB
ILE
A
272
90.758
23.693
−7.385
1.00
22.57
A


ATOM
1568
CG2
ILE
A
272
92.041
23.498
−8.184
1.00
21.91
A


ATOM
1569
CG1
ILE
A
272
89.818
22.495
−7.542
1.00
23.57
A


ATOM
1570
CD1
ILE
A
272
89.314
22.294
−8.949
1.00
24.20
A


ATOM
1571
C
ILE
A
272
92.112
25.010
−5.794
1.00
22.90
A


ATOM
1572
O
ILE
A
272
93.287
24.783
−5.507
1.00
21.82
A


ATOM
1573
N
TYR
A
273
91.638
26.226
−6.028
1.00
24.81
A


ATOM
1574
CA
TYR
A
273
92.478
27.400
−5.969
1.00
25.15
A


ATOM
1575
CB
TYR
A
273
91.630
28.632
−6.255
1.00
26.04
A


ATOM
1576
CG
TYR
A
273
92.385
29.931
−6.173
1.00
27.80
A


ATOM
1577
CD1
TYR
A
273
92.715
30.500
−4.939
1.00
27.53
A


ATOM
1578
CE1
TYR
A
273
93.405
31.708
−4.870
1.00
27.30
A


ATOM
1579
CD2
TYR
A
273
92.765
30.602
−7.333
1.00
27.17
A


ATOM
1580
CE2
TYR
A
273
93.448
31.804
−7.277
1.00
26.68
A


ATOM
1581
CZ
TYR
A
273
93.766
32.355
−6.050
1.00
28.05
A


ATOM
1582
OH
TYR
A
273
94.433
33.562
−6.018
1.00
30.80
A


ATOM
1583
C
TYR
A
273
93.139
27.521
−4.599
1.00
26.05
A


ATOM
1584
O
TYR
A
273
94.310
27.889
−4.489
1.00
24.45
A


ATOM
1585
N
GLN
A
274
92.380
27.205
−3.556
1.00
25.95
A


ATOM
1586
CA
GLN
A
274
92.896
27.299
−2.202
1.00
25.98
A


ATOM
1587
CB
GLN
A
274
91.743
27.209
−1.199
1.00
25.56
A


ATOM
1588
CG
GLN
A
274
92.169
27.422
0.233
1.00
25.42
A


ATOM
1589
CD
GLN
A
274
90.990
27.571
1.161
1.00
28.69
A


ATOM
1590
OE1
GLN
A
274
89.838
27.506
0.732
1.00
29.84
A


ATOM
1591
NE2
GLN
A
274
91.267
27.774
2.445
1.00
29.83
A


ATOM
1592
C
GLN
A
274
93.951
26.231
−1.915
1.00
25.08
A


ATOM
1593
O
GLN
A
274
94.862
26.452
−1.120
1.00
24.38
A


ATOM
1594
N
LEU
A
275
93.838
25.081
−2.567
1.00
24.42
A


ATOM
1595
CA
LEU
A
275
94.813
24.006
−2.369
1.00
25.43
A


ATOM
1596
CB
LEU
A
275
94.335
22.713
−3.035
1.00
22.95
A


ATOM
1597
CG
LEU
A
275
93.193
21.959
−2.354
1.00
25.67
A


ATOM
1598
CD1
LEU
A
275
92.817
20.702
−3.154
1.00
22.16
A


ATOM
1599
CD2
LEU
A
275
93.633
21.580
−0.950
1.00
23.32
A


ATOM
1600
C
LEU
A
275
96.171
24.376
−2.948
1.00
25.40
A


ATOM
1601
O
LEU
A
275
97.212
24.071
−2.376
1.00
25.87
A


ATOM
1602
N
VAL
A
276
96.153
25.039
−4.094
1.00
25.78
A


ATOM
1603
CA
VAL
A
276
97.384
25.419
−4.759
1.00
26.12
A


ATOM
1604
CB
VAL
A
276
97.170
25.522
−6.280
1.00
26.14
A


ATOM
1605
CG1
VAL
A
276
98.492
25.783
−6.962
1.00
24.46
A


ATOM
1606
CG2
VAL
A
276
96.531
24.248
−6.804
1.00
22.55
A


ATOM
1607
C
VAL
A
276
97.990
26.735
−4.275
1.00
27.83
A


ATOM
1608
O
VAL
A
276
99.210
26.849
−4.164
1.00
29.55
A


ATOM
1609
N
ALA
A
277
97.148
27.723
−3.990
1.00
26.88
A


ATOM
1610
CA
ALA
A
277
97.639
29.023
−3.549
1.00
26.50
A


ATOM
1611
CB
ALA
A
277
96.765
30.126
−4.122
1.00
24.49
A


ATOM
1612
C
ALA
A
277
97.740
29.175
−2.035
1.00
26.79
A


ATOM
1613
O
ALA
A
277
98.465
30.042
−1.548
1.00
28.26
A


ATOM
1614
N
GLY
A
278
97.020
28.343
−1.290
1.00
26.17
A


ATOM
1615
CA
GLY
A
278
97.074
28.430
0.159
1.00
24.63
A


ATOM
1616
C
GLY
A
278
95.971
29.272
0.780
1.00
25.52
A


ATOM
1617
O
GLY
A
278
95.793
29.259
1.998
1.00
27.25
A


ATOM
1618
N
LEU
A
279
95.229
29.998
−0.051
1.00
24.94
A


ATOM
1619
CA
LEU
A
279
94.130
30.849
0.408
1.00
25.58
A


ATOM
1620
CB
LEU
A
279
94.603
32.302
0.522
1.00
27.65
A


ATOM
1621
CG
LEU
A
279
95.748
32.631
1.470
1.00
29.35
A


ATOM
1622
CD1
LEU
A
279
96.365
33.958
1.075
1.00
30.47
A


ATOM
1623
CD2
LEU
A
279
95.232
32.671
2.892
1.00
29.70
A


ATOM
1624
C
LEU
A
279
92.987
30.822
−0.605
1.00
25.19
A


ATOM
1625
O
LEU
A
279
93.201
30.525
−1.781
1.00
25.34
A


ATOM
1626
N
PRO
A
280
91.755
31.126
−0.165
1.00
23.60
A


ATOM
1627
CD
PRO
A
280
91.306
31.357
1.216
1.00
22.97
A


ATOM
1628
CA
PRO
A
280
90.628
31.133
−1.103
1.00
23.81
A


ATOM
1629
CB
PRO
A
280
89.417
31.338
−0.195
1.00
25.19
A


ATOM
1630
CG
PRO
A
280
89.982
32.041
1.008
1.00
25.48
A


ATOM
1631
C
PRO
A
280
90.855
32.295
−2.083
1.00
26.26
A


ATOM
1632
O
PRO
A
280
91.632
33.207
−1.792
1.00
25.42
A


ATOM
1633
N
PRO
A
281
90.178
32.284
−3.243
1.00
26.49
A


ATOM
1634
CD
PRO
A
281
89.182
31.285
−3.651
1.00
27.13
A


ATOM
1635
CA
PRO
A
281
90.307
33.316
−4.281
1.00
27.25
A


ATOM
1636
CB
PRO
A
281
89.522
32.727
−5.463
1.00
26.75
A


ATOM
1637
CG
PRO
A
281
89.354
31.291
−5.136
1.00
25.29
A


ATOM
1638
C
PRO
A
281
89.817
34.724
−3.954
1.00
27.30
A


ATOM
1639
O
PRO
A
281
90.497
35.709
−4.238
1.00
27.67
A


ATOM
1640
N
PHE
A
282
88.623
34.817
−3.388
1.00
27.79
A


ATOM
1641
CA
PHE
A
282
88.034
36.107
−3.066
1.00
28.37
A


ATOM
1642
CB
PHE
A
282
86.563
36.086
−3.467
1.00
27.77
A


ATOM
1643
CG
PHE
A
282
86.335
35.557
−4.857
1.00
29.06
A


ATOM
1644
CD1
PHE
A
282
86.454
36.392
−5.965
1.00
28.74
A


ATOM
1645
CD2
PHE
A
282
86.077
34.207
−5.063
1.00
25.80
A


ATOM
1646
CE1
PHE
A
282
86.324
35.887
−7.255
1.00
28.50
A


ATOM
1647
CE2
PHE
A
282
85.947
33.695
−6.346
1.00
26.04
A


ATOM
1648
CZ
PHE
A
282
86.071
34.535
−7.444
1.00
28.02
A


ATOM
1649
C
PHE
A
282
88.184
36.426
−1.589
1.00
29.95
A


ATOM
1650
O
PHE
A
282
87.600
35.763
−0.741
1.00
32.95
A


ATOM
1651
N
ARG
A
283
88.977
37.445
−1.285
1.00
32.36
A


ATOM
1652
CA
ARG
A
283
89.215
37.843
0.100
1.00
33.06
A


ATOM
1653
CB
ARG
A
283
90.622
37.432
0.520
1.00
33.69
A


ATOM
1654
CG
ARG
A
283
90.990
36.006
0.151
1.00
36.29
A


ATOM
1655
CD
ARG
A
283
92.341
35.635
0.727
1.00
38.81
A


ATOM
1656
NE
ARG
A
283
93.415
36.423
0.133
1.00
41.73
A


ATOM
1657
CZ
ARG
A
283
93.783
36.338
−1.142
1.00
44.14
A


ATOM
1658
NH1
ARG
A
283
93.162
35.497
−1.958
1.00
45.19
A


ATOM
1659
NH2
ARG
A
283
94.772
37.094
−1.604
1.00
44.57
A


ATOM
1660
C
ARG
A
283
89.065
39.353
0.267
1.00
32.44
A


ATOM
1661
O
ARG
A
283
89.429
40.118
−0.624
1.00
31.91
A


ATOM
1662
N
ALA
A
284
88.527
39.777
1.406
1.00
33.21
A


ATOM
1663
CA
ALA
A
284
88.348
41.199
1.682
1.00
32.82
A


ATOM
1664
CB
ALA
A
284
87.265
41.777
0.782
1.00
32.40
A


ATOM
1665
C
ALA
A
284
88.004
41.445
3.147
1.00
32.98
A


ATOM
1666
O
ALA
A
284
87.779
40.502
3.913
1.00
32.53
A


ATOM
1667
N
GLY
A
285
87.961
42.723
3.520
1.00
32.60
A


ATOM
1668
CA
GLY
A
285
87.666
43.112
4.887
1.00
30.00
A


ATOM
1669
C
GLY
A
285
86.355
42.637
5.486
1.00
29.37
A


ATOM
1670
O
GLY
A
285
86.287
42.366
6.685
1.00
29.35
A


ATOM
1671
N
ASN
A
286
85.302
42.547
4.685
1.00
28.99
A


ATOM
1672
CA
ASN
A
286
84.024
42.097
5.226
1.00
29.58
A


ATOM
1673
CB
ASN
A
286
83.238
43.281
5.801
1.00
29.54
A


ATOM
1674
CG
ASN
A
286
82.958
44.356
4.764
1.00
29.60
A


ATOM
1675
OD1
ASN
A
286
82.350
44.092
3.720
1.00
26.48
A


ATOM
1676
ND2
ASN
A
286
83.400
45.575
5.049
1.00
25.96
A


ATOM
1677
C
ASN
A
286
83.196
41.378
4.182
1.00
30.16
A


ATOM
1678
O
ASN
A
286
83.551
41.357
3.004
1.00
31.70
A


ATOM
1679
N
GLU
A
287
82.084
40.796
4.613
1.00
31.14
A


ATOM
1680
CA
GLU
A
287
81.225
40.051
3.699
1.00
32.53
A


ATOM
1681
CB
GLU
A
287
79.943
39.600
4.397
1.00
35.66
A


ATOM
1682
CG
GLU
A
287
80.168
38.813
5.666
1.00
43.05
A


ATOM
1683
CD
GLU
A
287
79.138
37.707
5.856
1.00
47.79
A


ATOM
1684
OE1
GLU
A
287
77.933
37.959
5.616
1.00
49.01
A


ATOM
1685
OE2
GLU
A
287
79.539
36.588
6.256
1.00
48.82
A


ATOM
1686
C
GLU
A
287
80.853
40.837
2.457
1.00
30.19
A


ATOM
1687
O
GLU
A
287
80.986
40.332
1.343
1.00
30.33
A


ATOM
1688
N
TYR
A
288
80.385
42.066
2.653
1.00
29.13
A


ATOM
1689
CA
TYR
A
288
79.972
42.922
1.541
1.00
27.98
A


ATOM
1690
CB
TYR
A
288
79.573
44.320
2.034
1.00
26.59
A


ATOM
1691
CG
TYR
A
288
79.080
45.217
0.917
1.00
26.43
A


ATOM
1692
CD1
TYR
A
288
77.799
45.060
0.385
1.00
28.06
A


ATOM
1693
CE1
TYR
A
288
77.350
45.854
−0.675
1.00
28.72
A


ATOM
1694
CD2
TYR
A
288
79.905
46.196
0.363
1.00
27.24
A


ATOM
1695
CE2
TYR
A
288
79.470
46.994
−0.697
1.00
28.55
A


ATOM
1696
CZ
TYR
A
288
78.192
46.814
−1.211
1.00
29.91
A


ATOM
1697
OH
TYR
A
288
77.765
47.571
−2.275
1.00
30.53
A


ATOM
1698
C
TYR
A
288
81.057
43.068
0.487
1.00
25.84
A


ATOM
1699
O
TYR
A
288
80.790
42.940
−0.701
1.00
27.88
A


ATOM
1700
N
LEU
A
289
82.279
43.344
0.919
1.00
24.24
A


ATOM
1701
CA
LEU
A
289
83.382
43.495
−0.018
1.00
26.60
A


ATOM
1702
CB
LEU
A
289
84.662
43.919
0.713
1.00
25.15
A


ATOM
1703
CG
LEU
A
289
85.005
45.411
0.817
1.00
27.82
A


ATOM
1704
CD1
LEU
A
289
83.830
46.277
0.354
1.00
27.32
A


ATOM
1705
CD2
LEU
A
289
85.404
45.727
2.251
1.00
25.62
A


ATOM
1706
C
LEU
A
289
83.622
42.184
−0.736
1.00
27.45
A


ATOM
1707
O
LEU
A
289
83.901
42.157
−1.933
1.00
30.18
A


ATOM
1708
N
ILE
A
290
83.520
41.093
0.009
1.00
28.11
A


ATOM
1709
CA
ILE
A
290
83.726
39.770
−0.551
1.00
28.84
A


ATOM
1710
CB
ILE
A
290
83.565
38.710
0.545
1.00
29.67
A


ATOM
1711
CG2
ILE
A
290
83.450
37.331
−0.071
1.00
31.47
A


ATOM
1712
CG1
ILE
A
290
84.756
38.802
1.504
1.00
29.26
A


ATOM
1713
CD1
ILE
A
290
84.604
37.995
2.779
1.00
27.48
A


ATOM
1714
C
ILE
A
290
82.727
39.530
−1.676
1.00
27.99
A


ATOM
1715
O
ILE
A
290
83.090
39.110
−2.775
1.00
26.63
A


ATOM
1716
N
PHE
A
291
81.464
39.824
−1.406
1.00
28.54
A


ATOM
1717
CA
PHE
A
291
80.432
39.638
−2.407
1.00
27.14
A


ATOM
1718
CB
PHE
A
291
79.066
39.945
−1.807
1.00
28.37
A


ATOM
1719
CG
PHE
A
291
78.674
39.024
−0.688
1.00
30.37
A


ATOM
1720
CD1
PHE
A
291
79.283
37.778
−0.543
1.00
30.07
A


ATOM
1721
CD2
PHE
A
291
77.658
39.377
0.194
1.00
29.74
A


ATOM
1722
CE1
PHE
A
291
78.885
36.897
0.463
1.00
32.11
A


ATOM
1723
CE2
PHE
A
291
77.253
38.502
1.202
1.00
32.76
A


ATOM
1724
CZ
PHE
A
291
77.867
37.259
1.336
1.00
32.01
A


ATOM
1725
C
PHE
A
291
80.690
40.525
−3.618
1.00
27.79
A


ATOM
1726
O
PHE
A
291
80.434
40.124
−4.755
1.00
26.52
A


ATOM
1727
N
GLN
A
292
81.200
41.730
−3.384
1.00
27.05
A


ATOM
1728
CA
GLN
A
292
81.478
42.613
−4.503
1.00
27.48
A


ATOM
1729
CB
GLN
A
292
82.072
43.945
−4.037
1.00
27.80
A


ATOM
1730
CG
GLN
A
292
81.041
44.984
−3.651
1.00
30.50
A


ATOM
1731
CD
GLN
A
292
81.630
46.381
−3.565
1.00
31.30
A


ATOM
1732
OE1
GLN
A
292
82.519
46.644
−2.762
1.00
33.17
A


ATOM
1733
NE2
GLN
A
292
81.133
47.284
−4.399
1.00
32.86
A


ATOM
1734
C
GLN
A
292
82.442
41.934
−5.460
1.00
26.82
A


ATOM
1735
O
GLN
A
292
82.186
41.883
−6.664
1.00
28.03
A


ATOM
1736
N
LYS
A
293
83.539
41.402
−4.924
1.00
24.08
A


ATOM
1737
CA
LYS
A
293
84.542
40.739
−5.751
1.00
24.43
A


ATOM
1738
CB
LYS
A
293
85.752
40.368
−4.901
1.00
26.19
A


ATOM
1739
CG
LYS
A
293
86.456
41.580
−4.319
1.00
28.24
A


ATOM
1740
CD
LYS
A
293
87.750
41.213
−3.608
1.00
30.60
A


ATOM
1741
CE
LYS
A
293
88.555
42.468
−3.273
1.00
32.23
A


ATOM
1742
NZ
LYS
A
293
89.849
42.170
−2.591
1.00
32.86
A


ATOM
1743
C
LYS
A
293
84.008
39.500
−6.472
1.00
25.06
A


ATOM
1744
O
LYS
A
293
84.350
39.236
−7.628
1.00
24.96
A


ATOM
1745
N
ILE
A
294
83.163
38.740
−5.793
1.00
24.33
A


ATOM
1746
CA
ILE
A
294
82.593
37.552
−6.399
1.00
24.46
A


ATOM
1747
CB
ILE
A
294
81.725
36.800
−5.385
1.00
22.52
A


ATOM
1748
CG2
ILE
A
294
80.837
35.783
−6.093
1.00
23.14
A


ATOM
1749
CG1
ILE
A
294
82.632
36.141
−4.345
1.00
21.54
A


ATOM
1750
CD1
ILE
A
294
81.892
35.535
−3.175
1.00
19.38
A


ATOM
1751
C
ILE
A
294
81.761
37.885
−7.639
1.00
27.01
A


ATOM
1752
O
ILE
A
294
81.967
37.303
−8.704
1.00
23.93
A


ATOM
1753
N
ILE
A
295
80.830
38.828
−7.513
1.00
29.79
A


ATOM
1754
CA
ILE
A
295
79.983
39.168
−8.653
1.00
32.98
A


ATOM
1755
CB
ILE
A
295
78.767
40.004
−8.228
1.00
33.96
A


ATOM
1756
CG2
ILE
A
295
77.980
39.246
−7.174
1.00
36.23
A


ATOM
1757
CG1
ILE
A
295
79.216
41.358
−7.682
1.00
35.79
A


ATOM
1758
CD1
ILE
A
295
78.062
42.266
−7.300
1.00
37.79
A


ATOM
1759
C
ILE
A
295
80.729
39.898
−9.757
1.00
33.17
A


ATOM
1760
O
ILE
A
295
80.212
40.066
−10.862
1.00
34.06
A


ATOM
1761
N
LYS
A
296
81.946
40.333
−9.462
1.00
33.65
A


ATOM
1762
CA
LYS
A
296
82.747
41.012
−10.468
1.00
34.81
A


ATOM
1763
CB
LYS
A
296
83.353
42.293
−9.895
1.00
38.05
A


ATOM
1764
CG
LYS
A
296
82.353
43.427
−9.714
1.00
40.12
A


ATOM
1765
CD
LYS
A
296
83.070
44.736
−9.401
1.00
44.01
A


ATOM
1766
CE
LYS
A
296
82.191
45.939
−9.731
1.00
46.66
A


ATOM
1767
NZ
LYS
A
296
82.972
47.209
−9.833
1.00
47.40
A


ATOM
1768
C
LYS
A
296
83.851
40.078
−10.945
1.00
34.15
A


ATOM
1769
O
LYS
A
296
84.622
40.415
−11.847
1.00
33.48
A


ATOM
1770
N
LEU
A
297
83.907
38.897
−10.333
1.00
33.82
A


ATOM
1771
CA
LEU
A
297
84.904
37.890
−10.663
1.00
32.06
A


ATOM
1772
CB
LEU
A
297
84.716
37.418
−12.110
1.00
32.43
A


ATOM
1773
CG
LEU
A
297
85.452
36.144
−12.538
1.00
33.09
A


ATOM
1774
CD1
LEU
A
297
84.959
34.966
−11.697
1.00
31.88
A


ATOM
1775
CD2
LEU
A
297
85.206
35.875
−14.025
1.00
32.51
A


ATOM
1776
C
LEU
A
297
86.275
38.515
−10.476
1.00
32.23
A


ATOM
1777
O
LEU
A
297
87.180
38.321
−11.278
1.00
32.08
A


ATOM
1778
N
GLU
A
298
86.424
39.267
−9.395
1.00
33.56
A


ATOM
1779
CA
GLU
A
298
87.682
39.936
−9.110
1.00
35.66
A


ATOM
1780
CB
GLU
A
298
87.405
41.274
−8.428
1.00
38.03
A


ATOM
1781
CG
GLU
A
298
88.641
42.125
−8.236
1.00
42.97
A


ATOM
1782
CD
GLU
A
298
88.383
43.313
−7.338
1.00
46.19
A


ATOM
1783
OE1
GLU
A
298
87.412
44.055
−7.602
1.00
48.41
A


ATOM
1784
OE2
GLU
A
298
89.153
43.504
−6.369
1.00
48.44
A


ATOM
1785
C
GLU
A
298
88.644
39.117
−8.245
1.00
34.35
A


ATOM
1786
O
GLU
A
298
88.508
39.065
−7.021
1.00
35.64
A


ATOM
1787
N
TYR
A
299
89.611
38.478
−8.894
1.00
32.46
A


ATOM
1788
CA
TYR
A
299
90.624
37.678
−8.208
1.00
30.71
A


ATOM
1789
CB
TYR
A
299
90.031
36.367
−7.672
1.00
26.01
A


ATOM
1790
CG
TYR
A
299
89.874
35.300
−8.730
1.00
26.77
A


ATOM
1791
CD1
TYR
A
299
88.871
35.390
−9.699
1.00
26.60
A


ATOM
1792
CE1
TYR
A
299
88.768
34.448
−10.724
1.00
26.10
A


ATOM
1793
CD2
TYR
A
299
90.770
34.236
−8.807
1.00
22.56
A


ATOM
1794
CE2
TYR
A
299
90.677
33.291
−9.822
1.00
24.59
A


ATOM
1795
CZ
TYR
A
299
89.674
33.400
−10.781
1.00
26.34
A


ATOM
1796
OH
TYR
A
299
89.578
32.463
−11.791
1.00
22.44
A


ATOM
1797
C
TYR
A
299
91.720
37.374
−9.229
1.00
30.95
A


ATOM
1798
O
TYR
A
299
91.528
37.575
−10.425
1.00
28.80
A


ATOM
1799
N
ASP
A
300
92.865
36.891
−8.764
1.00
33.38
A


ATOM
1800
CA
ASP
A
300
93.954
36.582
−9.680
1.00
36.47
A


ATOM
1801
CB
ASP
A
300
94.782
37.845
−9.931
1.00
42.34
A


ATOM
1802
CG
ASP
A
300
95.014
38.644
−8.666
1.00
46.20
A


ATOM
1803
OD1
ASP
A
300
95.607
38.085
−7.719
1.00
49.27
A


ATOM
1804
OD2
ASP
A
300
94.599
39.826
−8.615
1.00
49.25
A


ATOM
1805
C
ASP
A
300
94.848
35.444
−9.188
1.00
35.61
A


ATOM
1806
O
ASP
A
300
94.857
35.113
−8.002
1.00
34.48
A


ATOM
1807
N
PHE
A
301
95.602
34.854
−10.111
1.00
35.02
A


ATOM
1808
CA
PHE
A
301
96.477
33.737
−9.781
1.00
35.94
A


ATOM
1809
CB
PHE
A
301
96.501
32.700
−10.909
1.00
34.28
A


ATOM
1810
CG
PHE
A
301
95.156
32.167
−11.301
1.00
32.40
A


ATOM
1811
CD1
PHE
A
301
94.358
32.856
−12.205
1.00
30.50
A


ATOM
1812
CD2
PHE
A
301
94.708
30.947
−10.803
1.00
31.83
A


ATOM
1813
CE1
PHE
A
301
93.131
32.333
−12.617
1.00
31.48
A


ATOM
1814
CE2
PHE
A
301
93.484
30.416
−11.206
1.00
31.37
A


ATOM
1815
CZ
PHE
A
301
92.695
31.109
−12.114
1.00
31.44
A


ATOM
1816
C
PHE
A
301
97.916
34.134
−9.524
1.00
38.11
A


ATOM
1817
O
PHE
A
301
98.458
35.010
−10.196
1.00
39.06
A


ATOM
1818
N
PRO
A
302
98.559
33.498
−8.535
1.00
40.47
A


ATOM
1819
CD
PRO
A
302
98.053
32.554
−7.524
1.00
41.16
A


ATOM
1820
CA
PRO
A
302
99.955
33.843
−8.277
1.00
41.88
A


ATOM
1821
CB
PRO
A
302
100.248
33.131
−6.963
1.00
42.01
A


ATOM
1822
CG
PRO
A
302
99.328
31.947
−7.001
1.00
41.79
A


ATOM
1823
C
PRO
A
302
100.721
33.265
−9.458
1.00
44.54
A


ATOM
1824
O
PRO
A
302
100.263
32.305
−10.082
1.00
44.30
A


ATOM
1825
N
GLU
A
303
101.874
33.843
−9.770
1.00
47.35
A


ATOM
1826
CA
GLU
A
303
102.667
33.395
−10.912
1.00
50.51
A


ATOM
1827
CB
GLU
A
303
103.859
34.337
−11.105
1.00
53.23
A


ATOM
1828
CG
GLU
A
303
104.431
34.376
−12.520
1.00
56.85
A


ATOM
1829
CD
GLU
A
303
103.976
35.600
−13.314
1.00
59.62
A


ATOM
1830
OE1
GLU
A
303
104.508
35.819
−14.424
1.00
60.43
A


ATOM
1831
OE2
GLU
A
303
103.088
36.341
−12.834
1.00
60.45
A


ATOM
1832
C
GLU
A
303
103.173
31.950
−10.829
1.00
50.70
A


ATOM
1833
O
GLU
A
303
103.692
31.423
−11.815
1.00
52.21
A


ATOM
1834
N
ALA
A
304
103.018
31.309
−9.672
1.00
49.61
A


ATOM
1835
CA
ALA
A
304
103.495
29.933
−9.488
1.00
49.10
A


ATOM
1836
CB
ALA
A
304
104.077
29.779
−8.082
1.00
48.82
A


ATOM
1837
C
ALA
A
304
102.422
28.869
−9.713
1.00
47.90
A


ATOM
1838
O
ALA
A
304
102.703
27.666
−9.719
1.00
49.41
A


ATOM
1839
N
PHE
A
305
101.192
29.322
−9.899
1.00
44.69
A


ATOM
1840
CA
PHE
A
305
100.053
28.440
−10.089
1.00
40.05
A


ATOM
1841
CB
PHE
A
305
98.809
29.301
−10.299
1.00
39.69
A


ATOM
1842
CG
PHE
A
305
97.568
28.729
−9.697
1.00
37.21
A


ATOM
1843
CD1
PHE
A
305
96.824
27.775
−10.379
1.00
35.36
A


ATOM
1844
CD2
PHE
A
305
97.133
29.157
−8.445
1.00
37.52
A


ATOM
1845
CE1
PHE
A
305
95.658
27.255
−9.825
1.00
34.59
A


ATOM
1846
CE2
PHE
A
305
95.963
28.641
−7.880
1.00
37.01
A


ATOM
1847
CZ
PHE
A
305
95.226
27.688
−8.575
1.00
35.13
A


ATOM
1848
C
PHE
A
305
100.197
27.435
−11.230
1.00
37.65
A


ATOM
1849
O
PHE
A
305
100.364
27.814
−12.389
1.00
36.24
A


ATOM
1850
N
PHE
A
306
100.120
26.150
−10.892
1.00
35.64
A


ATOM
1851
CA
PHE
A
306
100.219
25.081
−11.884
1.00
32.40
A


ATOM
1852
CB
PHE
A
306
99.781
23.749
−11.268
1.00
29.92
A


ATOM
1853
CG
PHE
A
306
100.412
23.456
−9.926
1.00
28.24
A


ATOM
1854
CD1
PHE
A
306
101.796
23.457
−9.770
1.00
27.43
A


ATOM
1855
CD2
PHE
A
306
99.617
23.173
−8.816
1.00
28.59
A


ATOM
1856
CE1
PHE
A
306
102.380
23.181
−8.526
1.00
29.55
A


ATOM
1857
CE2
PHE
A
306
100.188
22.895
−7.566
1.00
29.06
A


ATOM
1858
CZ
PHE
A
306
101.575
22.901
−7.422
1.00
29.51
A


ATOM
1859
C
PHE
A
306
99.296
25.452
−13.047
1.00
32.76
A


ATOM
1860
O
PHE
A
306
98.087
25.625
−12.861
1.00
34.51
A


ATOM
1861
N
PRO
A
307
99.856
25.587
−14.262
1.00
31.43
A


ATOM
1862
CD
PRO
A
307
101.272
25.327
−14.569
1.00
30.74
A


ATOM
1863
CA
PRO
A
307
99.128
25.947
−15.485
1.00
29.54
A


ATOM
1864
CB
PRO
A
307
100.158
25.700
−16.579
1.00
29.48
A


ATOM
1865
CG
PRO
A
307
101.437
26.032
−15.895
1.00
30.81
A


ATOM
1866
C
PRO
A
307
97.826
25.193
−15.743
1.00
29.74
A


ATOM
1867
O
PRO
A
307
96.795
25.804
−16.022
1.00
31.08
A


ATOM
1868
N
LYS
A
308
97.867
23.870
−15.660
1.00
28.47
A


ATOM
1869
CA
LYS
A
308
96.672
23.086
−15.904
1.00
27.92
A


ATOM
1870
CB
LYS
A
308
97.044
21.619
−16.114
1.00
28.70
A


ATOM
1871
CG
LYS
A
308
97.696
21.405
−17.460
1.00
30.04
A


ATOM
1872
CD
LYS
A
308
98.310
20.029
−17.595
1.00
33.76
A


ATOM
1873
CE
LYS
A
308
99.106
19.926
−18.888
1.00
33.22
A


ATOM
1874
NZ
LYS
A
308
99.897
18.663
−18.948
1.00
36.67
A


ATOM
1875
C
LYS
A
308
95.632
23.247
−14.800
1.00
26.85
A


ATOM
1876
O
LYS
A
308
94.433
23.170
−15.060
1.00
25.34
A


ATOM
1877
N
ALA
A
309
96.084
23.480
−13.574
1.00
24.70
A


ATOM
1878
CA
ALA
A
309
95.145
23.685
−12.486
1.00
24.41
A


ATOM
1879
CB
ALA
A
309
95.855
23.652
−11.146
1.00
22.65
A


ATOM
1880
C
ALA
A
309
94.523
25.051
−12.712
1.00
26.56
A


ATOM
1881
O
ALA
A
309
93.327
25.238
−12.493
1.00
28.91
A


ATOM
1882
N
ARG
A
310
95.335
26.011
−13.149
1.00
26.94
A


ATOM
1883
CA
ARG
A
310
94.830
27.354
−13.402
1.00
27.56
A


ATOM
1884
CB
ARG
A
310
95.961
28.289
−13.864
1.00
28.69
A


ATOM
1885
CG
ARG
A
310
95.438
29.584
−14.480
1.00
31.42
A


ATOM
1886
CD
ARG
A
310
96.482
30.676
−14.634
1.00
33.72
A


ATOM
1887
NE
ARG
A
310
95.881
31.868
−15.233
1.00
37.73
A


ATOM
1888
CZ
ARG
A
310
96.412
33.090
−15.198
1.00
38.44
A


ATOM
1889
NH1
ARG
A
310
97.572
33.297
−14.588
1.00
37.72
A


ATOM
1890
NH2
ARG
A
310
95.775
34.108
−15.767
1.00
37.74
A


ATOM
1891
C
ARG
A
310
93.743
27.280
−14.473
1.00
26.84
A


ATOM
1892
O
ARG
A
310
92.678
27.880
−14.344
1.00
26.39
A


ATOM
1893
N
ASP
A
311
94.019
26.524
−15.527
1.00
26.91
A


ATOM
1894
CA
ASP
A
311
93.069
26.369
−16.615
1.00
28.21
A


ATOM
1895
CB
ASP
A
311
93.682
25.504
−17.713
1.00
30.32
A


ATOM
1896
CG
ASP
A
311
92.850
25.494
−18.972
1.00
35.68
A


ATOM
1897
OD1
ASP
A
311
91.894
24.691
−19.040
1.00
38.27
A


ATOM
1898
OD2
ASP
A
311
93.145
26.302
−19.888
1.00
37.07
A


ATOM
1899
C
ASP
A
311
91.769
25.748
−16.108
1.00
27.22
A


ATOM
1900
O
ASP
A
311
90.678
26.205
−16.449
1.00
29.64
A


ATOM
1901
N
LEU
A
312
91.886
24.715
−15.285
1.00
24.32
A


ATOM
1902
CA
LEU
A
312
90.708
24.062
−14.728
1.00
23.48
A


ATOM
1903
CB
LEU
A
312
91.118
22.838
−13.892
1.00
21.65
A


ATOM
1904
CG
LEU
A
312
90.067
22.228
−12.945
1.00
21.40
A


ATOM
1905
CD1
LEU
A
312
88.789
21.917
−13.694
1.00
16.90
A


ATOM
1906
CD2
LEU
A
312
90.629
20.960
−12.294
1.00
19.67
A


ATOM
1907
C
LEU
A
312
89.899
25.039
−13.871
1.00
22.73
A


ATOM
1908
O
LEU
A
312
88.684
25.141
−14.021
1.00
22.02
A


ATOM
1909
N
VAL
A
313
90.574
25.754
−12.972
1.00
22.12
A


ATOM
1910
CA
VAL
A
313
89.897
26.715
−12.108
1.00
21.16
A


ATOM
1911
CB
VAL
A
313
90.893
27.440
−11.167
1.00
23.49
A


ATOM
1912
CG1
VAL
A
313
90.221
28.679
−10.534
1.00
20.45
A


ATOM
1913
CG2
VAL
A
313
91.369
26.487
−10.080
1.00
21.63
A


ATOM
1914
C
VAL
A
313
89.161
27.771
−12.920
1.00
22.93
A


ATOM
1915
O
VAL
A
313
88.051
28.168
−12.566
1.00
21.46
A


ATOM
1916
N
GLU
A
314
89.784
28.235
−14.001
1.00
23.15
A


ATOM
1917
CA
GLU
A
314
89.156
29.252
−14.832
1.00
25.95
A


ATOM
1918
CB
GLU
A
314
90.127
29.762
−15.900
1.00
28.61
A


ATOM
1919
CG
GLU
A
314
91.319
30.523
−15.350
1.00
32.73
A


ATOM
1920
CD
GLU
A
314
92.205
31.059
−16.453
1.00
35.94
A


ATOM
1921
OE1
GLU
A
314
92.188
30.467
−17.554
1.00
40.67
A


ATOM
1922
OE2
GLU
A
314
92.923
32.059
−16.225
1.00
37.73
A


ATOM
1923
C
GLU
A
314
87.891
28.742
−15.505
1.00
24.64
A


ATOM
1924
O
GLU
A
314
87.030
29.528
−15.892
1.00
24.01
A


ATOM
1925
N
LYS
A
315
87.775
27.428
−15.654
1.00
23.67
A


ATOM
1926
CA
LYS
A
315
86.588
26.874
−16.278
1.00
23.15
A


ATOM
1927
CB
LYS
A
315
86.937
25.594
−17.042
1.00
24.76
A


ATOM
1928
CG
LYS
A
315
87.784
25.845
−18.299
1.00
22.90
A


ATOM
1929
CD
LYS
A
315
88.223
24.541
−18.929
1.00
23.63
A


ATOM
1930
CE
LYS
A
315
89.079
24.772
−20.153
1.00
23.20
A


ATOM
1931
NZ
LYS
A
315
88.332
25.582
−21.142
1.00
29.09
A


ATOM
1932
C
LYS
A
315
85.509
26.600
−15.244
1.00
23.08
A


ATOM
1933
O
LYS
A
315
84.386
26.250
−15.596
1.00
23.63
A


ATOM
1934
N
LEU
A
316
85.852
26.773
−13.969
1.00
21.74
A


ATOM
1935
CA
LEU
A
316
84.910
26.547
−12.876
1.00
21.89
A


ATOM
1936
CB
LEU
A
316
85.569
25.738
−11.760
1.00
20.54
A


ATOM
1937
CG
LEU
A
316
85.841
24.269
−12.090
1.00
20.69
A


ATOM
1938
CD1
LEU
A
316
86.600
23.611
−10.947
1.00
17.08
A


ATOM
1939
CD2
LEU
A
316
84.514
23.558
−12.336
1.00
19.15
A


ATOM
1940
C
LEU
A
316
84.404
27.860
−12.312
1.00
23.66
A


ATOM
1941
O
LEU
A
316
83.215
28.005
−12.013
1.00
25.40
A


ATOM
1942
N
LEU
A
317
85.310
28.816
−12.149
1.00
24.48
A


ATOM
1943
CA
LEU
A
317
84.933
30.121
−11.637
1.00
25.52
A


ATOM
1944
CB
LEU
A
317
86.123
30.793
−10.936
1.00
24.23
A


ATOM
1945
CG
LEU
A
317
86.656
30.035
−9.719
1.00
21.22
A


ATOM
1946
CD1
LEU
A
317
87.718
30.859
−9.015
1.00
23.73
A


ATOM
1947
CD2
LEU
A
317
85.515
29.730
−8.773
1.00
21.36
A


ATOM
1948
C
LEU
A
317
84.459
30.953
−12.815
1.00
26.00
A


ATOM
1949
O
LEU
A
317
85.148
31.856
−13.286
1.00
28.02
A


ATOM
1950
N
VAL
A
318
83.272
30.611
−13.293
1.00
27.50
A


ATOM
1951
CA
VAL
A
318
82.643
31.286
−14.421
1.00
28.43
A


ATOM
1952
CB
VAL
A
318
82.365
30.280
−15.558
1.00
28.13
A


ATOM
1953
CG1
VAL
A
318
81.624
30.953
−16.694
1.00
29.20
A


ATOM
1954
CG2
VAL
A
318
83.677
29.689
−16.045
1.00
27.12
A


ATOM
1955
C
VAL
A
318
81.331
31.842
−13.896
1.00
29.21
A


ATOM
1956
O
VAL
A
318
80.559
31.120
−13.255
1.00
30.06
A


ATOM
1957
N
LEU
A
319
81.082
33.121
−14.150
1.00
29.94
A


ATOM
1958
CA
LEU
A
319
79.858
33.758
−13.671
1.00
30.57
A


ATOM
1959
CB
LEU
A
319
79.808
35.214
−14.133
1.00
32.89
A


ATOM
1960
CG
LEU
A
319
80.908
36.115
−13.553
1.00
35.26
A


ATOM
1961
CD1
LEU
A
319
80.741
37.551
−14.059
1.00
34.63
A


ATOM
1962
CD2
LEU
A
319
80.835
36.078
−12.028
1.00
34.01
A


ATOM
1963
C
LEU
A
319
78.598
33.029
−14.117
1.00
30.01
A


ATOM
1964
O
LEU
A
319
77.704
32.768
−13.316
1.00
30.48
A


ATOM
1965
N
ASP
A
320
78.527
32.695
−15.397
1.00
30.13
A


ATOM
1966
CA
ASP
A
320
77.362
31.996
−15.919
1.00
29.97
A


ATOM
1967
CB
ASP
A
320
77.393
31.981
−17.444
1.00
32.99
A


ATOM
1968
CG
ASP
A
320
76.116
31.435
−18.040
1.00
36.86
A


ATOM
1969
OD1
ASP
A
320
75.495
30.548
−17.412
1.00
38.81
A


ATOM
1970
OD2
ASP
A
320
75.739
31.883
−19.142
1.00
38.26
A


ATOM
1971
C
ASP
A
320
77.373
30.569
−15.402
1.00
28.61
A


ATOM
1972
O
ASP
A
320
78.244
29.786
−15.758
1.00
28.87
A


ATOM
1973
N
ALA
A
321
76.398
30.233
−14.566
1.00
28.88
A


ATOM
1974
CA
ALA
A
321
76.311
28.897
−13.980
1.00
28.04
A


ATOM
1975
CB
ALA
A
321
75.156
28.842
−12.990
1.00
25.11
A


ATOM
1976
C
ALA
A
321
76.151
27.794
−15.021
1.00
27.83
A


ATOM
1977
O
ALA
A
321
76.500
26.643
−14.773
1.00
27.26
A


ATOM
1978
N
THR
A
322
75.632
28.150
−16.190
1.00
27.45
A


ATOM
1979
CA
THR
A
322
75.413
27.167
−17.243
1.00
27.18
A


ATOM
1980
CB
THR
A
322
74.294
27.615
−18.191
1.00
26.99
A


ATOM
1981
OG1
THR
A
322
74.739
28.753
−18.940
1.00
27.15
A


ATOM
1982
CG2
THR
A
322
73.045
27.997
−17.399
1.00
23.11
A


ATOM
1983
C
THR
A
322
76.654
26.909
−18.077
1.00
28.31
A


ATOM
1984
O
THR
A
322
76.605
26.133
−19.027
1.00
28.80
A


ATOM
1985
N
LYS
A
323
77.769
27.546
−17.727
1.00
28.30
A


ATOM
1986
CA
LYS
A
323
78.990
27.348
−18.491
1.00
28.51
A


ATOM
1987
CB
LYS
A
323
79.392
28.651
−19.172
1.00
30.27
A


ATOM
1988
CG
LYS
A
323
78.305
29.160
−20.095
1.00
35.72
A


ATOM
1989
CD
LYS
A
323
78.839
30.081
−21.170
1.00
37.65
A


ATOM
1990
CE
LYS
A
323
77.722
30.472
−22.131
1.00
39.59
A


ATOM
1991
NZ
LYS
A
323
77.088
29.263
−22.733
1.00
40.41
A


ATOM
1992
C
LYS
A
323
80.154
26.799
−17.683
1.00
28.68
A


ATOM
1993
O
LYS
A
323
81.298
26.847
−18.119
1.00
29.54
A


ATOM
1994
N
ARG
A
324
79.866
26.271
−16.503
1.00
27.43
A


ATOM
1995
CA
ARG
A
324
80.921
25.709
−15.684
1.00
25.01
A


ATOM
1996
CB
ARG
A
324
80.559
25.800
−14.205
1.00
22.81
A


ATOM
1997
CG
ARG
A
324
80.489
27.223
−13.715
1.00
21.68
A


ATOM
1998
CD
ARG
A
324
80.036
27.315
−12.277
1.00
20.65
A


ATOM
1999
NE
ARG
A
324
79.655
28.689
−11.971
1.00
21.18
A


ATOM
2000
CZ
ARG
A
324
78.645
29.029
−11.180
1.00
19.20
A


ATOM
2001
NH1
ARG
A
324
77.909
28.093
−10.598
1.00
19.05
A


ATOM
2002
NH2
ARG
A
324
78.349
30.307
−11.004
1.00
19.45
A


ATOM
2003
C
ARG
A
324
81.161
24.264
−16.073
1.00
24.64
A


ATOM
2004
O
ARG
A
324
80.219
23.501
−16.290
1.00
23.78
A


ATOM
2005
N
LEU
A
325
82.433
23.902
−16.177
1.00
23.92
A


ATOM
2006
CA
LEU
A
325
82.809
22.541
−16.526
1.00
25.53
A


ATOM
2007
CB
LEU
A
325
84.336
22.422
−16.558
1.00
25.18
A


ATOM
2008
CG
LEU
A
325
84.995
21.178
−17.149
1.00
25.63
A


ATOM
2009
CD1
LEU
A
325
84.541
20.949
−18.590
1.00
25.39
A


ATOM
2010
CD2
LEU
A
325
86.500
21.364
17.087
1.00
23.10
A


ATOM
2011
C
LEU
A
325
82.224
21.610
−15.466
1.00
25.01
A


ATOM
2012
O
LEU
A
325
82.449
21.809
−14.278
1.00
23.81
A


ATOM
2013
N
GLY
A
326
81.450
20.616
−15.900
1.00
26.41
A


ATOM
2014
CA
GLY
A
326
80.850
19.683
−14.964
1.00
26.13
A


ATOM
2015
C
GLY
A
326
79.338
19.771
−14.835
1.00
29.31
A


ATOM
2016
O
GLY
A
326
78.697
18.795
−14.444
1.00
31.67
A


ATOM
2017
N
CYS
A
327
78.753
20.918
−15.162
1.00
29.49
A


ATOM
2018
CA
CYS
A
327
77.308
21.073
−15.042
1.00
31.91
A


ATOM
2019
CB
CYS
A
327
76.935
22.556
−14.982
1.00
31.78
A


ATOM
2020
SG
CYS
A
327
77.084
23.397
−16.552
1.00
38.33
A


ATOM
2021
C
CYS
A
327
76.539
20.385
−16.175
1.00
32.76
A


ATOM
2022
O
CYS
A
327
77.096
20.069
−17.228
1.00
32.18
A


ATOM
2023
N
GLU
A
328
75.248
20.175
−15.952
1.00
33.60
A


ATOM
2024
CA
GLU
A
328
74.400
19.497
−16.921
1.00
36.82
A


ATOM
2025
CB
GLU
A
328
72.951
19.479
−16.408
1.00
41.60
A


ATOM
2026
CG
GLU
A
328
72.845
19.437
−14.863
1.00
48.96
A


ATOM
2027
CD
GLU
A
328
72.000
18.279
−14.321
1.00
51.75
A


ATOM
2028
OE1
GLU
A
328
72.393
17.103
−14.509
1.00
52.77
A


ATOM
2029
OE2
GLU
A
328
70.948
18.550
−13.696
1.00
52.29
A


ATOM
2030
C
GLU
A
328
74.466
20.120
−18.317
1.00
35.83
A


ATOM
2031
O
GLU
A
328
74.618
19.412
−19.318
1.00
34.85
A


ATOM
2032
N
GLU
A
329
74.370
21.443
−18.378
1.00
33.75
A


ATOM
2033
CA
GLU
A
329
74.399
22.146
−19.650
1.00
32.37
A


ATOM
2034
CB
GLU
A
329
74.153
23.640
−19.439
1.00
34.70
A


ATOM
2035
CG
GLU
A
329
72.898
23.972
−18.640
1.00
38.53
A


ATOM
2036
CD
GLU
A
329
73.017
23.589
−17.172
1.00
41.60
A


ATOM
2037
OE1
GLU
A
329
74.048
23.926
−16.548
1.00
44.03
A


ATOM
2038
OE2
GLU
A
329
72.080
22.958
−16.636
1.00
44.74
A


ATOM
2039
C
GLU
A
329
75.711
21.947
−20.399
1.00
30.96
A


ATOM
2040
O
GLU
A
329
75.757
22.114
−21.617
1.00
28.90
A


ATOM
2041
N
MET
A
330
76.773
21.605
−19.673
1.00
29.20
A


ATOM
2042
CA
MET
A
330
78.075
21.379
−20.291
1.00
27.90
A


ATOM
2043
CB
MET
A
330
79.190
22.010
−19.455
1.00
30.57
A


ATOM
2044
CG
MET
A
330
79.189
23.536
−19.446
1.00
32.33
A


ATOM
2045
SD
MET
A
330
79.488
24.269
−21.070
1.00
36.55
A


ATOM
2046
CE
MET
A
330
81.257
24.001
−21.239
1.00
35.61
A


ATOM
2047
C
MET
A
330
78.319
19.883
−20.443
1.00
27.32
A


ATOM
2048
O
MET
A
330
79.452
19.436
−20.606
1.00
25.82
A


ATOM
2049
N
GLU
A
331
77.232
19.122
−20.365
1.00
25.18
A


ATOM
2050
CA
GLU
A
331
77.246
17.677
−20.526
1.00
24.56
A


ATOM
2051
CB
GLU
A
331
77.922
17.295
−21.848
1.00
23.55
A


ATOM
2052
CG
GLU
A
331
77.395
18.099
−23.030
1.00
25.42
A


ATOM
2053
CD
GLU
A
331
75.867
18.176
−23.082
1.00
28.50
A


ATOM
2054
OE1
GLU
A
331
75.338
19.094
−23.750
1.00
31.00
A


ATOM
2055
OE2
GLU
A
331
75.190
17.323
−22.467
1.00
30.18
A


ATOM
2056
C
GLU
A
331
77.804
16.834
−19.396
1.00
24.55
A


ATOM
2057
O
GLU
A
331
78.327
15.745
−19.629
1.00
25.02
A


ATOM
2058
N
GLY
A
332
77.692
17.339
−18.172
1.00
22.83
A


ATOM
2059
CA
GLY
A
332
78.098
16.564
−17.017
1.00
20.57
A


ATOM
2060
C
GLY
A
332
79.541
16.408
−16.606
1.00
20.81
A


ATOM
2061
O
GLY
A
332
80.430
17.167
−16.999
1.00
19.36
A


ATOM
2062
N
TYR
A
333
79.753
15.374
−15.801
1.00
20.19
A


ATOM
2063
CA
TYR
A
333
81.053
15.056
−15.243
1.00
20.12
A


ATOM
2064
CB
TYR
A
333
80.860
14.127
−14.052
1.00
20.05
A


ATOM
2065
CG
TYR
A
333
80.483
14.902
−12.828
1.00
21.40
A


ATOM
2066
CD1
TYR
A
333
81.464
15.367
−11.956
1.00
22.85
A


ATOM
2067
CE1
TYR
A
333
81.141
16.181
−10.878
1.00
22.91
A


ATOM
2068
CD2
TYR
A
333
79.160
15.266
−12.590
1.00
21.24
A


ATOM
2069
CE2
TYR
A
333
78.827
16.082
−11.518
1.00
22.71
A


ATOM
2070
CZ
TYR
A
333
79.827
16.535
−10.670
1.00
21.44
A


ATOM
2071
OH
TYR
A
333
79.522
17.358
−9.621
1.00
24.72
A


ATOM
2072
C
TYR
A
333
82.076
14.484
−16.192
1.00
20.38
A


ATOM
2073
O
TYR
A
333
83.277
14.533
−15.910
1.00
18.82
A


ATOM
2074
N
GLY
A
334
81.610
13.942
−17.313
1.00
20.41
A


ATOM
2075
CA
GLY
A
334
82.534
13.378
−18.280
1.00
20.48
A


ATOM
2076
C
GLY
A
334
83.611
14.367
−18.693
1.00
20.12
A


ATOM
2077
O
GLY
A
334
84.808
14.105
−18.539
1.00
21.13
A


ATOM
2078
N
PRO
A
335
83.216
15.524
−19.230
1.00
19.75
A


ATOM
2079
CD
PRO
A
335
81.872
15.899
−19.699
1.00
19.25
A


ATOM
2080
CA
PRO
A
335
84.218
16.512
−19.644
1.00
19.66
A


ATOM
2081
CB
PRO
A
335
83.366
17.644
−20.212
1.00
17.92
A


ATOM
2082
CG
PRO
A
335
82.184
16.901
−20.784
1.00
19.24
A


ATOM
2083
C
PRO
A
335
85.115
16.967
−18.495
1.00
19.62
A


ATOM
2084
O
PRO
A
335
86.315
17.154
−18.679
1.00
21.87
A


ATOM
2085
N
LEU
A
336
84.538
17.131
−17.307
1.00
19.91
A


ATOM
2086
CA
LEU
A
336
85.312
17.576
−16.147
1.00
19.06
A


ATOM
2087
CB
LEU
A
336
84.406
17.767
−14.914
1.00
18.05
A


ATOM
2088
CG
LEU
A
336
85.073
18.119
−13.571
1.00
18.25
A


ATOM
2089
CD1
LEU
A
336
86.049
19.280
−13.746
1.00
15.57
A


ATOM
2090
CD2
LEU
A
336
84.009
18.473
−12.538
1.00
15.31
A


ATOM
2091
C
LEU
A
336
86.424
16.594
−15.832
1.00
17.85
A


ATOM
2092
O
LEU
A
336
87.582
16.986
−15.690
1.00
17.14
A


ATOM
2093
N
LYS
A
337
86.075
15.317
−15.732
1.00
17.96
A


ATOM
2094
CA
LYS
A
337
87.061
14.289
−15.438
1.00
19.15
A


ATOM
2095
CB
LYS
A
337
86.352
12.966
−15.134
1.00
21.53
A


ATOM
2096
CG
LYS
A
337
85.571
13.025
−13.821
1.00
25.58
A


ATOM
2097
CD
LYS
A
337
84.484
11.956
−13.715
1.00
26.69
A


ATOM
2098
CE
LYS
A
337
85.063
10.566
−13.571
1.00
29.78
A


ATOM
2099
NZ
LYS
A
337
83.979
9.552
−13.368
1.00
30.74
A


ATOM
2100
C
LYS
A
337
88.065
14.120
−16.576
1.00
21.13
A


ATOM
2101
O
LYS
A
337
89.170
13.631
−16.362
1.00
21.11
A


ATOM
2102
N
ALA
A
338
87.697
14.549
−17.780
1.00
21.55
A


ATOM
2103
CA
ALA
A
338
88.600
14.426
−18.922
1.00
22.23
A


ATOM
2104
CB
ALA
A
338
87.802
14.368
−20.221
1.00
21.66
A


ATOM
2105
C
ALA
A
338
89.604
15.569
−18.988
1.00
23.04
A


ATOM
2106
O
ALA
A
338
90.518
15.541
−19.800
1.00
22.63
A


ATOM
2107
N
HIS
A
339
89.447
16.570
−18.131
1.00
23.26
A


ATOM
2108
CA
HIS
A
339
90.362
17.705
−18.148
1.00
23.33
A


ATOM
2109
CB
HIS
A
339
90.017
18.680
−17.027
1.00
22.99
A


ATOM
2110
CG
HIS
A
339
90.696
20.004
−17.156
1.00
23.43
A


ATOM
2111
CD2
HIS
A
339
90.279
21.168
−17.710
1.00
24.32
A


ATOM
2112
ND1
HIS
A
339
91.993
20.219
−16.741
1.00
22.64
A


ATOM
2113
CE1
HIS
A
339
92.346
21.459
−17.036
1.00
24.03
A


ATOM
2114
NE2
HIS
A
339
91.324
22.056
−17.626
1.00
23.65
A


ATOM
2115
C
HIS
A
339
91.833
17.302
−18.046
1.00
24.36
A


ATOM
2116
O
HIS
A
339
92.186
16.376
−17.317
1.00
24.27
A


ATOM
2117
N
PRO
A
340
92.713
17.999
−18.788
1.00
25.89
A


ATOM
2118
CD
PRO
A
340
92.394
19.050
−19.777
1.00
26.27
A


ATOM
2119
CA
PRO
A
340
94.151
17.714
−18.785
1.00
26.69
A


ATOM
2120
CB
PRO
A
340
94.727
18.861
−19.613
1.00
26.46
A


ATOM
2121
CG
PRO
A
340
93.654
19.090
−20.636
1.00
25.56
A


ATOM
2122
C
PRO
A
340
94.772
17.629
−17.396
1.00
27.13
A


ATOM
2123
O
PRO
A
340
95.686
16.841
−17.167
1.00
28.89
A


ATOM
2124
N
PHE
A
341
94.281
18.438
−16.466
1.00
26.76
A


ATOM
2125
CA
PHE
A
341
94.815
18.417
−15.110
1.00
25.83
A


ATOM
2126
CB
PHE
A
341
94.100
19.451
−14.239
1.00
24.58
A


ATOM
2127
CG
PHE
A
341
94.628
19.527
−12.835
1.00
23.75
A


ATOM
2128
CD1
PHE
A
341
95.890
20.060
−12.578
1.00
24.62
A


ATOM
2129
CD2
PHE
A
341
93.867
19.066
−11.765
1.00
24.82
A


ATOM
2130
CE1
PHE
A
341
96.386
20.136
−11.273
1.00
23.48
A


ATOM
2131
CE2
PHE
A
341
94.352
19.136
−10.454
1.00
23.61
A


ATOM
2132
CZ
PHE
A
341
95.614
19.673
−10.209
1.00
23.80
A


ATOM
2133
C
PHE
A
341
94.684
17.039
−14.458
1.00
25.53
A


ATOM
2134
O
PHE
A
341
95.453
16.698
−13.572
1.00
25.60
A


ATOM
2135
N
PHE
A
342
93.718
16.248
−14.905
1.00
26.56
A


ATOM
2136
CA
PHE
A
342
93.486
14.928
−14.327
1.00
28.32
A


ATOM
2137
CB
PHE
A
342
91.992
14.724
−14.095
1.00
25.63
A


ATOM
2138
CG
PHE
A
342
91.374
15.731
−13.169
1.00
24.19
A


ATOM
2139
CD1
PHE
A
342
91.830
15.868
−11.859
1.00
24.72
A


ATOM
2140
CD2
PHE
A
342
90.285
16.492
−13.579
1.00
21.46
A


ATOM
2141
CE1
PHE
A
342
91.200
16.744
−10.969
1.00
22.95
A


ATOM
2142
CE2
PHE
A
342
89.649
17.368
−12.699
1.00
19.82
A


ATOM
2143
CZ
PHE
A
342
90.105
17.491
−11.393
1.00
20.87
A


ATOM
2144
C
PHE
A
342
94.009
13.811
−15.217
1.00
31.08
A


ATOM
2145
O
PHE
A
342
93.655
12.643
−15.047
1.00
32.72
A


ATOM
2146
N
GLU
A
343
94.863
14.183
−16.159
1.00
33.50
A


ATOM
2147
CA
GLU
A
343
95.446
13.250
−17.114
1.00
36.10
A


ATOM
2148
CB
GLU
A
343
96.738
13.853
−17.676
1.00
38.76
A


ATOM
2149
CG
GLU
A
343
96.842
13.883
−19.194
1.00
44.39
A


ATOM
2150
CD
GLU
A
343
96.911
15.307
−19.750
1.00
48.43
A


ATOM
2151
OE1
GLU
A
343
97.665
16.143
−19.190
1.00
47.87
A


ATOM
2152
OE2
GLU
A
343
96.217
15.587
−20.755
1.00
49.34
A


ATOM
2153
C
GLU
A
343
95.747
11.855
−16.552
1.00
35.54
A


ATOM
2154
O
GLU
A
343
95.210
10.847
−17.019
1.00
33.70
A


ATOM
2155
N
SER
A
344
96.604
11.810
−15.539
1.00
34.66
A


ATOM
2156
CA
SER
A
344
97.024
10.545
−14.950
1.00
33.91
A


ATOM
2157
CB
SER
A
344
98.421
10.712
−14.360
1.00
33.13
A


ATOM
2158
OG
SER
A
344
98.387
11.578
−13.242
1.00
30.32
A


ATOM
2159
C
SER
A
344
96.116
9.927
−13.886
1.00
33.50
A


ATOM
2160
O
SER
A
344
96.510
8.962
−13.234
1.00
32.98
A


ATOM
2161
N
VAL
A
345
94.908
10.448
−13.713
1.00
31.80
A


ATOM
2162
CA
VAL
A
345
94.021
9.903
−12.689
1.00
31.70
A


ATOM
2163
CB
VAL
A
345
93.039
10.981
−12.152
1.00
31.20
A


ATOM
2164
CG1
VAL
A
345
92.153
10.375
−11.079
1.00
29.96
A


ATOM
2165
CG2
VAL
A
345
93.799
12.176
−11.601
1.00
27.23
A


ATOM
2166
C
VAL
A
345
93.175
8.707
−13.133
1.00
32.88
A


ATOM
2167
O
VAL
A
345
92.597
8.712
−14.223
1.00
32.39
A


ATOM
2168
N
THR
A
346
93.109
7.688
−12.279
1.00
31.88
A


ATOM
2169
CA
THR
A
346
92.285
6.511
−12.539
1.00
32.94
A


ATOM
2170
CB
THR
A
346
93.007
5.209
−12.149
1.00
35.61
A


ATOM
2171
OG1
THR
A
346
94.137
5.012
−13.013
1.00
37.85
A


ATOM
2172
CG2
THR
A
346
92.060
4.022
−12.267
1.00
32.32
A


ATOM
2173
C
THR
A
346
91.051
6.700
−11.658
1.00
33.08
A


ATOM
2174
O
THR
A
346
91.083
6.460
−10.448
1.00
34.21
A


ATOM
2175
N
TRP
A
347
89.964
7.142
−12.274
1.00
31.78
A


ATOM
2176
CA
TRP
A
347
88.741
7.427
−11.549
1.00
31.53
A


ATOM
2177
CB
TRP
A
347
87.769
8.171
−12.463
1.00
28.28
A


ATOM
2178
CG
TRP
A
347
88.303
9.476
−12.937
1.00
23.66
A


ATOM
2179
CD2
TRP
A
347
88.263
10.722
−12.231
1.00
23.03
A


ATOM
2180
CE2
TRP
A
347
88.927
11.678
−13.031
1.00
20.77
A


ATOM
2181
CE3
TRP
A
347
87.731
11.121
−10.999
1.00
20.57
A


ATOM
2182
CD1
TRP
A
347
88.969
9.718
−14.102
1.00
21.92
A


ATOM
2183
NE1
TRP
A
347
89.348
11.041
−14.168
1.00
22.23
A


ATOM
2184
CZ2
TRP
A
347
89.074
13.008
−12.640
1.00
21.04
A


ATOM
2185
CZ3
TRP
A
347
87.876
12.444
−10.611
1.00
20.11
A


ATOM
2186
CH2
TRP
A
347
88.544
13.372
−11.430
1.00
20.44
A


ATOM
2187
C
TRP
A
347
88.014
6.267
−10.899
1.00
34.19
A


ATOM
2188
O
TRP
A
347
87.382
6.440
−9.854
1.00
34.97
A


ATOM
2189
N
GLU
A
348
88.108
5.089
−11.502
1.00
35.77
A


ATOM
2190
CA
GLU
A
348
87.405
3.913
−11.000
1.00
36.41
A


ATOM
2191
CB
GLU
A
348
87.600
2.740
−11.977
1.00
36.95
A


ATOM
2192
CG
GLU
A
348
88.990
2.626
−12.588
0.00
36.86
A


ATOM
2193
CD
GLU
A
348
89.173
3.510
−13.812
0.00
36.91
A


ATOM
2194
OE1
GLU
A
348
89.119
4.750
−13.677
0.00
36.92
A


ATOM
2195
OE2
GLU
A
348
89.370
2.960
−14.916
0.00
36.92
A


ATOM
2196
C
GLU
A
348
87.668
3.435
−9.563
1.00
36.38
A


ATOM
2197
O
GLU
A
348
86.773
2.866
−8.935
1.00
38.29
A


ATOM
2198
N
ASN
A
349
88.857
3.669
−9.019
1.00
34.41
A


ATOM
2199
CA
ASN
A
349
89.134
3.182
−7.668
1.00
33.02
A


ATOM
2200
CB
ASN
A
349
89.848
1.844
−7.765
1.00
34.07
A


ATOM
2201
CG
ASN
A
349
91.220
1.978
−8.381
1.00
35.48
A


ATOM
2202
OD1
ASN
A
349
91.409
2.742
−9.324
1.00
35.13
A


ATOM
2203
ND2
ASN
A
349
92.188
1.235
−7.852
1.00
38.04
A


ATOM
2204
C
ASN
A
349
89.970
4.116
−6.804
1.00
30.73
A


ATOM
2205
O
ASN
A
349
90.878
3.672
−6.106
1.00
30.66
A


ATOM
2206
N
LEU
A
350
89.662
5.403
−6.850
1.00
28.42
A


ATOM
2207
CA
LEU
A
350
90.390
6.397
−6.072
1.00
27.13
A


ATOM
2208
CB
LEU
A
350
89.655
7.737
−6.128
1.00
25.19
A


ATOM
2209
CG
LEU
A
350
89.803
8.543
−7.418
1.00
25.97
A


ATOM
2210
CD1
LEU
A
350
88.841
9.732
−7.428
1.00
26.30
A


ATOM
2211
CD2
LEU
A
350
91.242
9.014
−7.521
1.00
27.40
A


ATOM
2212
C
LEU
A
350
90.581
5.999
−4.614
1.00
26.30
A


ATOM
2213
O
LEU
A
350
91.645
6.201
−4.036
1.00
26.73
A


ATOM
2214
N
HIS
A
351
89.547
5.424
−4.024
1.00
27.16
A


ATOM
2215
CA
HIS
A
351
89.593
5.044
−2.622
1.00
28.60
A


ATOM
2216
CB
HIS
A
351
88.184
4.748
−2.124
1.00
29.94
A


ATOM
2217
CG
HIS
A
351
88.111
4.503
−0.653
1.00
30.99
A


ATOM
2218
CD2
HIS
A
351
88.324
5.329
0.399
1.00
31.86
A


ATOM
2219
ND1
HIS
A
351
87.790
3.275
−0.118
1.00
29.43
A


ATOM
2220
CE1
HIS
A
351
87.804
3.356
1.202
1.00
31.81
A


ATOM
2221
NE2
HIS
A
351
88.125
4.592
1.541
1.00
32.90
A


ATOM
2222
C
HIS
A
351
90.509
3.873
−2.298
1.00
28.99
A


ATOM
2223
O
HIS
A
351
90.875
3.677
−1.141
1.00
28.53
A


ATOM
2224
N
GLN
A
352
90.865
3.088
−3.307
1.00
30.57
A


ATOM
2225
CA
GLN
A
352
91.764
1.959
−3.095
1.00
33.42
A


ATOM
2226
CB
GLN
A
352
91.563
0.880
−4.162
1.00
35.01
A


ATOM
2227
CG
GLN
A
352
90.696
−0.289
−3.737
1.00
37.07
A


ATOM
2228
CD
GLN
A
352
89.275
0.123
−3.474
1.00
39.83
A


ATOM
2229
OE1
GLN
A
352
88.676
0.856
−4.267
1.00
41.90
A


ATOM
2230
NE2
GLN
A
352
88.712
−0.351
−2.365
1.00
39.86
A


ATOM
2231
C
GLN
A
352
93.197
2.457
−3.173
1.00
33.85
A


ATOM
2232
O
GLN
A
352
94.126
1.782
−2.734
1.00
35.32
A


ATOM
2233
N
GLN
A
353
93.368
3.647
−3.734
1.00
32.53
A


ATOM
2234
CA
GLN
A
353
94.693
4.216
−3.886
1.00
32.78
A


ATOM
2235
CB
GLN
A
353
94.666
5.298
−4.965
1.00
32.07
A


ATOM
2236
CG
GLN
A
353
94.373
4.739
−6.345
1.00
31.94
A


ATOM
2237
CD
GLN
A
353
94.206
5.819
−7.382
1.00
32.50
A


ATOM
2238
OE1
GLN
A
353
95.008
6.749
−7.452
1.00
35.33
A


ATOM
2239
NE2
GLN
A
353
93.167
5.701
−8.204
1.00
31.02
A


ATOM
2240
C
GLN
A
353
95.246
4.779
−2.588
1.00
33.27
A


ATOM
2241
O
GLN
A
353
94.494
5.209
−1.717
1.00
32.38
A


ATOM
2242
N
THR
A
354
96.570
4.746
−2.462
1.00
33.29
A


ATOM
2243
CA
THR
A
354
97.239
5.267
−1.280
1.00
34.35
A


ATOM
2244
CB
THR
A
354
98.615
4.601
−1.069
1.00
35.88
A


ATOM
2245
OG1
THR
A
354
98.430
3.232
−0.690
1.00
36.70
A


ATOM
2246
CG2
THR
A
354
99.403
5.325
0.027
1.00
36.08
A


ATOM
2247
C
THR
A
354
97.440
6.760
−1.478
1.00
33.06
A


ATOM
2248
O
THR
A
354
98.120
7.181
−2.403
1.00
31.33
A


ATOM
2249
N
PRO
A
355
96.844
7.581
−0.604
1.00
33.40
A


ATOM
2250
CD
PRO
A
355
96.000
7.220
0.544
1.00
31.90
A


ATOM
2251
CA
PRO
A
355
96.974
9.035
−0.710
1.00
34.90
A


ATOM
2252
CB
PRO
A
355
96.156
9.543
0.475
1.00
33.68
A


ATOM
2253
CG
PRO
A
355
95.160
8.452
0.698
1.00
33.37
A


ATOM
2254
C
PRO
A
355
98.428
9.475
−0.623
1.00
36.27
A


ATOM
2255
O
PRO
A
355
99.196
8.960
0.191
1.00
35.70
A


ATOM
2256
N
PRO
A
356
98.824
10.433
−1.464
1.00
37.66
A


ATOM
2257
CD
PRO
A
356
98.010
11.198
−2.423
1.00
38.22
A


ATOM
2258
CA
PRO
A
356
100.205
10.916
−1.441
1.00
39.93
A


ATOM
2259
CB
PRO
A
356
100.227
11.944
−2.570
1.00
38.83
A


ATOM
2260
CG
PRO
A
356
98.818
12.466
−2.580
1.00
38.26
A


ATOM
2261
C
PRO
A
356
100.532
11.534
−0.085
1.00
41.87
A


ATOM
2262
O
PRO
A
356
99.696
12.209
0.506
1.00
40.91
A


ATOM
2263
N
ALA
A
357
101.741
11.286
0.409
1.00
46.23
A


ATOM
2264
CA
ALA
A
357
102.160
11.837
1.691
1.00
51.16
A


ATOM
2265
CB
ALA
A
357
103.587
11.410
2.001
1.00
49.78
A


ATOM
2266
C
ALA
A
357
102.077
13.354
1.589
1.00
54.64
A


ATOM
2267
O
ALA
A
357
102.591
13.942
0.637
1.00
55.14
A


ATOM
2268
N
LEU
A
358
101.419
13.985
2.559
1.00
58.59
A


ATOM
2269
CA
LEU
A
358
101.276
15.437
2.552
1.00
62.92
A


ATOM
2270
CB
LEU
A
358
100.107
15.866
3.441
1.00
62.51
A


ATOM
2271
CG
LEU
A
358
98.732
15.752
2.783
1.00
63.05
A


ATOM
2272
CD1
LEU
A
358
97.657
16.251
3.737
1.00
63.34
A


ATOM
2273
CD2
LEU
A
358
98.721
16.570
1.494
1.00
62.56
A


ATOM
2274
C
LEU
A
358
102.536
16.173
2.984
1.00
65.81
A


ATOM
2275
O
LEU
A
358
102.675
16.559
4.148
1.00
66.45
A


ATOM
2276
N
THR
A
359
103.441
16.368
2.025
1.00
69.31
A


ATOM
2277
CA
THR
A
359
104.715
17.057
2.236
1.00
72.25
A


ATOM
2278
CB
THR
A
359
104.519
18.594
2.271
1.00
73.17
A


ATOM
2279
OG1
THR
A
359
103.564
18.937
3.284
1.00
75.38
A


ATOM
2280
CG2
THR
A
359
104.030
19.101
0.916
1.00
72.93
A


ATOM
2281
C
THR
A
359
105.468
16.627
3.497
1.00
73.76
A


ATOM
2282
O
THR
A
359
105.011
15.683
4.180
1.00
74.61
A


ATOM
2283
OXT
THR
A
359
106.523
17.237
3.780
1.00
75.50
A


ATOM
2284
OH2
TIP
S
1
82.965
32.402
−3.946
1.00
13.32
S


ATOM
2285
OH2
TIP
S
2
91.556
13.784
−17.557
1.00
22.11
S


ATOM
2286
OH2
TIP
S
3
87.391
33.155
−1.722
1.00
22.84
S


ATOM
2287
OH2
TIP
S
4
69.033
3.499
13.879
1.00
22.91
S


ATOM
2288
OH2
TIP
S
5
81.088
19.368
−18.406
1.00
24.13
S


ATOM
2289
OH2
TIP
S
6
75.641
16.130
8.209
1.00
26.44
S


ATOM
2290
OH2
TIP
S
7
74.760
20.961
3.347
1.00
27.74
S


ATOM
2291
OH2
TIP
S
8
75.152
6.784
5.545
1.00
22.53
S


ATOM
2292
OH2
TIP
S
9
77.282
11.807
−17.666
1.00
35.96
S


ATOM
2293
OH2
TIP
S
10
81.785
8.968
−8.072
1.00
25.44
S


ATOM
2294
OH2
TIP
S
11
78.609
24.424
−2.074
1.00
22.05
S


ATOM
2295
OH2
TIP
S
12
94.883
8.256
−9.981
1.00
37.17
S


ATOM
2296
OH2
TIP
S
13
73.164
38.970
−1.072
1.00
35.95
S


ATOM
2297
OH2
TIP
S
14
78.806
27.556
−3.116
1.00
39.27
S


ATOM
2298
OH2
TIP
S
15
89.050
8.041
10.604
1.00
23.40
S


ATOM
2299
OH2
TIP
S
16
73.265
40.376
−3.301
1.00
26.94
S


ATOM
2300
OH2
TIP
S
18
84.081
33.371
4.243
1.00
30.61
S


ATOM
2301
OH2
TIP
S
19
78.571
−0.530
16.531
1.00
26.61
S


ATOM
2302
OH2
TIP
S
21
70.088
3.703
17.559
1.00
28.94
S


ATOM
2303
OH2
TIP
S
22
79.212
13.330
−18.791
1.00
26.94
S


ATOM
2304
OH2
TIP
S
23
91.672
10.665
−16.153
1.00
30.26
S


ATOM
2305
OH2
TIP
S
25
104.173
17.689
−7.204
1.00
31.65
S


ATOM
2306
OH2
TIP
S
27
87.578
18.354
−20.604
1.00
25.98
S


ATOM
2307
OH2
TIP
S
28
82.272
34.870
−16.021
1.00
27.40
S


ATOM
2308
OH2
TIP
S
29
100.496
13.074
−9.812
1.00
37.92
S


ATOM
2309
OH2
TIP
S
30
65.147
10.515
28.440
1.00
40.03
S


ATOM
2310
OH2
TIP
S
31
90.721
38.800
−4.631
1.00
42.09
S


ATOM
2311
OH2
TIP
S
32
83.367
23.841
15.654
1.00
36.15
S


ATOM
2312
OH2
TIP
S
33
87.754
11.897
23.760
1.00
26.76
S


ATOM
2313
OH2
TIP
S
34
77.755
13.485
−15.395
1.00
31.85
S


ATOM
2314
OH2
TIP
S
35
79.767
43.115
5.371
1.00
35.26
S


ATOM
2315
OH2
TIP
S
37
80.173
32.998
6.198
1.00
40.03
S


ATOM
2316
OH2
TIP
S
40
85.958
19.110
24.502
1.00
24.42
S


ATOM
2317
OH2
TIP
S
42
77.719
−0.391
23.732
1.00
39.71
S


ATOM
2318
OH2
TIP
S
44
92.563
36.428
−5.574
1.00
35.43
S


ATOM
2319
OH2
TIP
S
45
90.942
34.092
3.570
1.00
43.64
S


ATOM
2320
OH2
TIP
S
46
74.357
32.157
−13.849
1.00
33.31
S


ATOM
2321
OH2
TIP
S
47
90.220
14.449
16.172
1.00
34.34
S


ATOM
2322
OH2
TIP
S
48
77.876
11.229
−13.863
1.00
23.53
S


ATOM
2323
OH2
TIP
S
50
76.289
12.589
−11.572
1.00
37.74
S


ATOM
2324
OH2
TIP
S
51
76.619
2.787
−2.969
1.00
35.95
S


ATOM
2325
OH2
TIP
S
52
65.118
19.629
24.370
1.00
34.85
S


ATOM
2326
OH2
TIP
S
53
99.690
31.473
−13.046
1.00
48.21
S


ATOM
2327
OH2
TIP
S
54
88.376
36.865
3.454
1.00
38.54
S


ATOM
2328
OH2
TIP
S
57
91.236
10.819
18.279
1.00
40.76
S


ATOM
2329
OH2
TIP
S
59
100.017
21.990
−14.622
1.00
41.65
S


ATOM
2330
OH2
TIP
S
63
87.188
25.521
11.438
1.00
41.53
S


ATOM
2331
OH2
TIP
S
65
90.264
19.625
12.286
1.00
24.22
S


ATOM
2332
OH2
TIP
S
66
83.805
26.254
−18.365
1.00
37.50
S


ATOM
2333
OH2
TIP
S
68
78.394
7.378
2.855
1.00
23.47
S


ATOM
2334
OH2
TIP
S
74
85.541
11.500
−18.436
1.00
37.35
S


ATOM
2335
OH2
TIP
S
76
98.981
8.707
2.808
1.00
47.34
S


ATOM
2336
OH2
TIP
S
78
87.802
19.118
22.522
1.00
39.99
S


ATOM
2337
OH2
TIP
S
80
92.438
3.105
2.517
1.00
37.27
S


ATOM
2338
OH2
TIP
S
81
75.580
−0.821
22.186
1.00
36.41
S


ATOM
2339
OH2
TIP
S
82
60.506
24.278
21.938
1.00
31.55
S


ATOM
2340
OH2
TIP
S
83
92.298
22.520
−21.183
1.00
42.32
S


ATOM
2341
OH2
TIP
S
84
74.351
4.211
−3.464
1.00
32.53
S


ATOM
2342
OH2
TIP
S
85
76.502
25.963
−21.839
1.00
41.89
S


ATOM
2343
OH2
TIP
S
86
97.965
13.142
9.216
1.00
41.76
S


ATOM
2344
OH2
TIP
S
87
78.657
4.418
3.361
1.00
35.63
S


ATOM
2345
OH2
TIP
S
88
93.633
28.572
3.429
1.00
34.30
S


ATOM
2346
OH2
TIP
S
89
104.691
20.306
−7.235
1.00
32.75
S


ATOM
2347
OH2
TIP
S
91
98.360
16.754
−15.558
1.00
37.92
S


ATOM
2348
OH2
TIP
S
92
88.175
32.723
−14.088
1.00
38.91
S


ATOM
2349
OH2
TIP
S
93
96.974
27.936
−17.613
1.00
34.47
S


ATOM
2350
OH2
TIP
S
94
85.585
22.346
15.199
1.00
41.12
S


ATOM
2351
OH2
TIP
S
100
80.948
−0.010
7.892
1.00
12.04
S


ATOM
2352
OH2
TIP
S
101
76.653
29.202
−3.527
1.00
22.10
S


ATOM
2353
OH2
TIP
S
102
74.980
8.979
−7.975
1.00
21.17
S


ATOM
2354
OH2
TIP
S
103
88.843
28.393
3.994
1.00
30.94
S


ATOM
2355
OH2
TIP
S
105
76.862
8.067
28.490
1.00
20.20
S


ATOM
2356
OH2
TIP
S
106
66.435
30.702
8.817
1.00
35.87
S


ATOM
2357
OH2
TIP
S
109
67.384
7.757
8.860
1.00
39.38
S


ATOM
2358
OH2
TIP
S
110
66.852
4.666
22.301
1.00
32.75
S


ATOM
2359
OH2
TIP
S
111
72.391
2.229
−3.501
1.00
51.07
S


ATOM
2360
OH2
TIP
S
116
80.209
7.061
−7.886
1.00
35.49
S


ATOM
2361
OH2
TIP
S
121
74.466
15.313
−12.357
1.00
45.36
S


ATOM
2362
OH2
TIP
S
122
79.225
28.627
0.179
1.00
30.68
S


ATOM
2363
OH2
TIP
S
124
59.090
22.126
22.498
1.00
35.94
S


ATOM
2364
OH2
TIP
S
126
73.715
24.448
−13.973
1.00
44.35
S


ATOM
2365
OH2
TIP
S
127
105.619
22.931
−11.256
1.00
43.80
S


ATOM
2366
OH2
TIP
S
128
86.658
32.319
−16.090
1.00
39.40
S


ATOM
2367
OH2
TIP
S
129
70.750
21.709
−10.875
1.00
45.74
S


ATOM
2368
OH2
TIP
S
136
77.820
12.663
6.090
1.00
47.18
S


ATOM
2369
OH2
TIP
S
142
90.942
35.947
−13.582
1.00
48.16
S


ATOM
2370
OH2
TIP
S
146
67.351
6.830
24.075
1.00
36.66
S


ATOM
2371
OH2
TIP
S
148
98.067
12.182
−7.216
1.00
38.66
S


ATOM
2372
OH2
TIP
S
156
75.211
13.809
−20.582
1.00
45.56
S


ATOM
2373
OH2
TIP
S
158
72.261
20.575
12.175
1.00
51.45
S


ATOM
2374
OH2
TIP
S
166
77.289
42.685
7.086
1.00
42.23
S


ATOM
2375
OH2
TIP
S
174
65.330
6.552
20.003
1.00
42.22
S


ATOM
2376
OH2
TIP
S
176
88.027
20.872
−20.665
1.00
35.09
S


ATOM
2377
OH2
TIP
S
178
99.488
29.517
−16.497
1.00
44.21
S


ATOM
2378
OH2
TIP
S
182
93.851
13.830
−20.448
1.00
50.19
S


ATOM
2379
OH2
TIP
S
192
83.811
26.388
9.460
1.00
39.52
S


ATOM
2380
OH2
TIP
S
193
91.704
42.080
2.405
1.00
40.67
S


ATOM
2381
O12
GLC
G
1
82.624
0.887
12.473
1.00
47.94
G


ATOM
2382
C11
GLC
G
1
82.240
2.160
13.000
1.00
48.49
G


ATOM
2383
C13
GLC
G
1
83.237
3.235
12.553
1.00
46.87
G


ATOM
2384
O14
GLC
G
1
84.544
2.903
13.022
1.00
46.62
G


ATOM
2385
C15
GLC
G
1
82.817
4.591
13.117
1.00
45.80
G


ATOM
2386
O16
GLC
G
1
83.746
5.589
12.703
1.00
43.50
G


ATOM
2387
O12
GLC
G
5
86.722
−2.593
0.107
1.00
39.62
G


ATOM
2388
C11
GLC
G
5
86.245
−1.364
−0.429
1.00
44.37
G


ATOM
2389
C13
GLC
G
5
86.764
−0.193
0.394
1.00
44.36
G


ATOM
2390
O14
GLC
G
5
86.355
−0.326
1.761
1.00
47.64
G


ATOM
2391
C15
GLC
G
5
86.231
1.132
−0.195
1.00
45.11
G


ATOM
2392
O16
GLC
G
5
86.666
1.310
−1.557
1.00
42.61
G


ATOM
2393
O12
GLC
G
8
87.512
4.414
−5.278
1.00
38.37
G


ATOM
2394
C11
GLC
G
8
86.362
5.220
−5.023
1.00
34.16
G


ATOM
2395
C13
GLC
G
8
85.750
5.654
−6.351
1.00
35.54
G


ATOM
2396
O14
GLC
G
8
86.717
6.392
−7.111
1.00
37.03
G


ATOM
2397
C15
GLC
G
8
84.521
6.523
−6.082
1.00
35.46
G


ATOM
2398
O16
GLC
G
8
83.948
6.931
−7.319
1.00
33.79
G


ATOM
2399
C34
STO
L
1
82.178
19.404
9.614
1.00
23.98
L


ATOM
2400
O33
STO
L
1
83.091
19.645
10.691
1.00
24.40
L


ATOM
2401
C25
STO
L
1
82.557
20.621
11.610
1.00
19.84
L


ATOM
2402
C26
STO
L
1
83.748
21.455
12.055
1.00
20.35
L


ATOM
2403
N31
STO
L
1
84.251
22.242
10.916
1.00
22.56
L


ATOM
2404
C32
STO
L
1
83.716
23.544
10.481
1.00
20.91
L


ATOM
2405
C27
STO
L
1
84.847
20.523
12.559
1.00
19.37
L


ATOM
2406
C28
STO
L
1
84.278
19.595
13.658
1.00
18.70
L


ATOM
2407
O29
STO
L
1
82.889
19.845
13.980
1.00
20.08
L


ATOM
2408
C24
STO
L
1
81.939
19.930
12.872
1.00
21.85
L


ATOM
2409
C35
STO
L
1
80.791
20.824
13.403
1.00
20.12
L


ATOM
2410
N6
STO
L
1
81.456
18.689
12.528
1.00
19.30
L


ATOM
2411
C5
STO
L
1
80.172
18.450
12.023
1.00
16.04
L


ATOM
2412
C4
STO
L
1
79.039
19.219
11.690
1.00
14.17
L


ATOM
2413
C3
STO
L
1
77.901
18.569
11.148
1.00
14.32
L


ATOM
2414
C2
STO
L
1
77.899
17.158
10.946
1.00
14.05
L


ATOM
2415
C1
STO
L
1
79.035
16.386
11.282
1.00
13.54
L


ATOM
2416
C23
STO
L
1
80.154
17.053
11.812
1.00
16.42
L


ATOM
2417
C22
STO
L
1
81.361
16.522
12.164
1.00
17.74
L


ATOM
2418
C7
STO
L
1
82.162
17.525
12.606
1.00
18.84
L


ATOM
2419
C8
STO
L
1
83.501
17.279
12.972
1.00
18.69
L


ATOM
2420
N9
STO
L
1
84.462
18.150
13.376
1.00
19.59
L


ATOM
2421
C10
STO
L
1
85.663
17.477
13.561
1.00
19.11
L


ATOM
2422
C11
STO
L
1
86.968
17.838
13.942
1.00
16.81
L


ATOM
2423
C12
STO
L
1
87.961
16.831
14.007
1.00
20.66
L


ATOM
2424
C13
STO
L
1
87.645
15.476
13.689
1.00
20.30
L


ATOM
2425
C14
STO
L
1
86.329
15.117
13.306
1.00
19.66
L


ATOM
2426
C15
STO
L
1
85.364
16.127
13.248
1.00
18.74
L


ATOM
2427
C16
STO
L
1
84.049
16.022
12.899
1.00
19.21
L


ATOM
2428
C17
STO
L
1
83.217
14.936
12.440
1.00
18.26
L


ATOM
2429
C21
STO
L
1
81.934
15.217
12.098
1.00
17.21
L


ATOM
2430
C20
STO
L
1
81.325
14.098
11.689
1.00
17.68
L


ATOM
2431
N19
STO
L
1
82.281
13.080
11.786
1.00
13.64
L


ATOM
2432
C18
STO
L
1
83.457
13.603
12.261
1.00
16.89
L


ATOM
2433
O30
STO
L
1
84.493
12.981
12.504
1.00
15.41
L


ATOM
2434
S
SO4
I
1
64.914
7.877
16.247
1.00
82.11
I


ATOM
2435
O1
SO4
I
1
63.624
8.415
15.778
1.00
82.68
I


ATOM
2436
O2
SO4
I
1
65.841
8.992
16.520
1.00
82.73
I


ATOM
2437
O3
SO4
I
1
65.479
7.010
15.198
1.00
83.33
I


ATOM
2438
O4
SO4
I
1
64.709
7.088
17.477
1.00
82.04
I


ATOM
2439
S
SO4
I
2
68.379
−7.029
19.810
1.00
112.82
I


ATOM
2440
O1
SO4
I
2
66.992
−6.526
19.786
1.00
112.60
I


ATOM
2441
O2
SO4
I
2
68.850
−7.226
18.425
1.00
112.21
I


ATOM
2442
O3
SO4
I
2
68.426
−8.312
20.538
1.00
112.24
I


ATOM
2443
O4
SO4
I
2
69.249
−6.051
20.491
1.00
112.72
I


ATOM
2444
S
SO4
I
3
84.927
−1.874
12.302
1.00
79.99
I


ATOM
2445
O1
SO4
I
3
84.408
−1.334
13.568
1.00
79.90
I


ATOM
2446
O2
SO4
I
3
84.442
−1.050
11.178
1.00
80.43
I


ATOM
2447
O3
SO4
I
3
84.453
−3.263
12.131
1.00
79.92
I


ATOM
2448
O4
SO4
I
3
86.402
−1.845
12.326
1.00
80.52
I


ATOM
2449
S
SO4
I
4
80.577
9.632
30.033
1.00
98.23
I


ATOM
2450
O1
SO4
I
4
79.725
9.060
28.972
1.00
96.88
I


ATOM
2451
O2
SO4
I
4
82.000
9.461
29.683
1.00
97.80
I


ATOM
2452
O3
SO4
I
4
80.304
8.944
31.309
1.00
98.08
I


ATOM
2453
O4
SO4
I
4
80.281
11.069
30.178
1.00
98.08
I


ATOM
2454
S
SO4
I
5
89.310
6.131
25.915
1.00
110.86
I


ATOM
2455
O1
SO4
I
5
89.025
6.456
27.331
1.00
110.48
I


ATOM
2456
O2
SO4
I
5
88.042
6.095
25.151
1.00
110.12
I


ATOM
2457
O3
SO4
I
5
89.970
4.810
25.844
1.00
110.72
I


ATOM
2458
O4
SO4
I
5
90.205
7.155
25.330
1.00
110.02
I


ATOM
2459
O2
PO4
P
100
64.527
26.252
2.299
1.00
88.98
P


ATOM
2460
O3
PO4
P
100
66.482
25.155
1.367
1.00
88.39
P


ATOM
2461
O4
PO4
P
100
66.688
26.504
3.376
1.00
87.87
P


ATOM
2462
O1
PO4
P
100
66.264
27.565
1.240
1.00
88.80
P


ATOM
2463
P
PO4
P
100
65.992
26.368
2.070
1.00
88.61
P


ATOM
2464
CB
LEU

145
73.932
8.398
8.961
0.50
21.29
AC2


ATOM
2465
CG
LEU

145
72.901
8.606
10.076
0.50
21.65
AC2


ATOM
2466
CD1
LEU

145
71.904
9.671
9.655
0.50
21.60
AC2


ATOM
2467
CD2
LEU

145
72.195
7.298
10.388
0.50
19.61
AC2


ATOM
2468
CB
ASN

214
88.968
8.625
7.173
0.50
22.34
AC2


ATOM
2469
CG
ASN

214
89.705
8.084
5.975
0.50
22.01
AC2


ATOM
2470
OD1
ASN

214
89.240
7.153
5.320
0.50
22.82
AC2


ATOM
2471
ND2
ASN

214
90.859
8.660
5.678
0.50
22.69
AC2


ATOM
2472
CB
ASP

216
93.187
5.546
5.379
0.50
25.98
AC2


ATOM
2473
CG
ASP

216
91.789
5.828
4.895
0.50
27.09
AC2


ATOM
2474
OD1
ASP

216
91.587
6.896
4.290
0.50
28.49
AC2


ATOM
2475
OD2
ASP

216
90.896
4.982
5.110
0.50
28.20
AC2


END









Example 8
Co-Ordinates for PDK1 Fragment Co-Crystallised with UCN-01












REMARK coordinates from restrained individual B-factor refinement


REMARK refinement resolution: 25.0-2.50 A


REMARK starting r= 0.1919 free_r= 0.2582


REMARK final   r= 0.1894 free_r= 0.2567


REMARK B rmsd for bonded mainchain atoms= 1.412 target=1.5


REMARK B rmsd for bonded sidechain atoms=  2.205 target=2.0


REMARK B rmsd for angle mainchain atoms= 2.401 target=2.0


REMARK B rmsd for angle sidechain atoms=  3.256 target=2.5


REMARK rweight= 0.1000 (with wa= 3.1611)


REMARK target= mlf steps= 30


REMARK sg= P3(2)21 a= 123.387 b= 123.387 c= 47.115 alpha= 90 beta= 90 gamma= 120


REMARK parameter file 1 : /ddl/david/refinement/MY_CNS/prot.par


REMARK parameter file 2 : /ddl/david/refinement/MY_CNS/ucn01.par


REMARK parameter file 3 : CNS_TOPPAR:water_rep.param


REMARK parameter file 4 : CNS_TOPPAR:ion.param


REMARK parameter file 5 :


/dd1/david/refinement/MY_CNS/glycerol.par


REMARK molecular structure file: . . /generate/generate.mtf


REMARK input coordinates: . . /minimize/minimize.pdb


REMARK reflection file= . ./. . /. ./data/cns.hkl


REMARK ncs= none


REMARK B-correction resolution: 6.0-2.50


REMARK initial B-factor correction applied to fobs:


REMARK B11= −4.722 B22= 4.722 B33= 9.444


REMARK B12= −3.572 B13= 0.000 B23= 0.000


REMARK B-factor correction applied to coordinate array B: −0.193 


REMARK bulk solvent: density level= 0.3837 e/A 3, B-factor=


40.9071 A 2


REMARK reflections with |Fobs|/sigma_F < 0.0 rejected


REMARK reflections with |Fobs| > 10000 * rms(Fobs) rejected


REMARK theoretical total number of refl. in resol. range: 14485


(100.0%)


REMARK number of unobserved reflections (no entry or |F|=0):


101 (0.7%)


REMARK number of reflections rejected: 0 (0.0%)


REMARK total number of reflections used: 14384 (99.3%)


REMARK number of reflections in working set: 13795 (95.2%)


REMARK number of reflections in test set: 589 (4.1%)


CRYST1 123.387 123.387 47.115 90.00 90.00 120.00 P 32 2 1


REMARK FILENAME=“bindindividual.pdb” 


REMARK DATE:25-Mar-2003 17:21:21 created by user: david


REMARK VERSION:1.0


















ATOM
1
CB
ALA
A
73
67.051
−3.293
12.591
1.00
59.77
A


ATOM
2
C
ALA
A
73
67.941
−4.753
14.416
1.00
61.14
A


ATOM
3
O
ALA
A
73
67.184
−5.270
15.240
1.00
61.61
A


ATOM
4
N
ALA
A
73
66.523
−5.729
12.643
1.00
58.89
A


ATOM
5
CA
ALA
A
73
67.564
−4.697
12.943
1.00
60.69
A


ATOM
6
N
PRO
A
74
69.130
−4.241
14.770
1.00
61.63
A


ATOM
7
CD
PRO
A
74
70.264
−3.830
13.918
1.00
61.72
A


ATOM
8
CA
PRO
A
74
69.514
−4.278
16.187
1.00
61.34
A


ATOM
9
CB
PRO
A
74
70.918
−3.663
16.181
1.00
61.79
A


ATOM
10
CG
PRO
A
74
71.458
−4.072
14.818
1.00
61.47
A


ATOM
11
C
PRO
A
74
68.523
−3.481
17.047
1.00
60.16
A


ATOM
12
O
PRO
A
74
67.625
−2.817
16.519
1.00
60.77
A


ATOM
13
N
ALA
A
75
68.680
−3.562
18.368
1.00
58.13
A


ATOM
14
CA
ALA
A
75
67.815
−2.828
19.292
1.00
54.74
A


ATOM
15
CB
ALA
A
75
68.048
−3.309
20.731
1.00
54.90
A


ATOM
16
C
ALA
A
75
68.175
−1.349
19.177
1.00
51.85
A


ATOM
17
O
ALA
A
75
69.313
−1.005
18.851
1.00
52.46
A


ATOM
18
N
LYS
A
76
67.215
−0.473
19.427
1.00
46.96
A


ATOM
19
CA
LYS
A
76
67.507
0.947
19.354
1.00
43.72
A


ATOM
20
CB
LYS
A
76
66.270
1.756
19.744
1.00
42.81
A


ATOM
21
CG
LYS
A
76
66.177
3.116
19.087
1.00
41.81
A


ATOM
22
CD
LYS
A
76
65.926
2.983
17.590
1.00
40.56
A


ATOM
23
CE
LYS
A
76
65.691
4.343
16.943
1.00
42.58
A


ATOM
24
NZ
LYS
A
76
65.362
4.231
15.495
1.00
42.73
A


ATOM
25
C
LYS
A
76
68.639
1.218
20.351
1.00
41.25
A


ATOM
26
O
LYS
A
76
68.599
0.741
21.488
1.00
41.68
A


ATOM
27
N
LYS
A
77
69.655
1.960
19.936
1.00
37.68
A


ATOM
28
CA
LYS
A
77
70.748
2.255
20.849
1.00
35.10
A


ATOM
29
CB
LYS
A
77
72.016
2.619
20.074
1.00
34.13
A


ATOM
30
CG
LYS
A
77
72.427
1.570
19.053
1.00
32.68
A


ATOM
31
CD
LYS
A
77
73.927
1.537
18.858
1.00
33.90
A


ATOM
32
CE
LYS
A
77
74.366
0.471
17.849
1.00
31.40
A


ATOM
33
NZ
LYS
A
77
73.796
−0.863
18.164
1.00
34.76
A


ATOM
34
C
LYS
A
77
70.313
3.408
21.743
1.00
34.79
A


ATOM
35
O
LYS
A
77
69.319
4.077
21.458
1.00
34.20
A


ATOM
36
N
ARG
A
78
71.023
3.626
22.845
1.00
34.88
A


ATOM
37
CA
ARG
A
78
70.687
4.723
23.759
1.00
34.62
A


ATOM
38
CB
ARG
A
78
69.694
4.247
24.839
1.00
38.43
A


ATOM
39
CG
ARG
A
78
70.027
2.884
25.353
1.00
42.71
A


ATOM
40
CD
ARG
A
78
69.355
2.424
26.625
1.00
48.52
A


ATOM
41
NE
ARG
A
78
70.365
1.702
27.412
1.00
56.10
A


ATOM
42
CZ
ARG
A
78
70.428
0.355
27.518
1.00
57.88
A


ATOM
43
NH1
ARG
A
78
69.519
−0.397
26.838
1.00
58.45
A


ATOM
44
NH2
ARG
A
78
71.335
−0.195
28.369
1.00
59.23
A


ATOM
45
C
ARG
A
78
71.967
5.330
24.382
1.00
32.26
A


ATOM
46
O
ARG
A
78
73.066
4.777
24.278
1.00
31.42
A


ATOM
47
N
PRO
A
79
71.844
6.509
24.997
1.00
30.46
A


ATOM
48
CD
PRO
A
79
70.616
7.284
25.232
1.00
28.96
A


ATOM
49
CA
PRO
A
79
72.997
7.172
25.609
1.00
30.38
A


ATOM
50
CB
PRO
A
79
72.350
8.303
26.405
1.00
28.86
A


ATOM
51
CG
PRO
A
79
71.169
8.642
25.568
1.00
27.83
A


ATOM
52
C
PRO
A
79
73.889
6.287
26.468
1.00
29.47
A


ATOM
53
O
PRO
A
79
75.108
6.377
26.391
1.00
29.57
A


ATOM
54
N
GLU
A
80
73.268
5.435
27.279
1.00
29.77
A


ATOM
55
CA
GLU
A
80
73.975
4.533
28.179
1.00
29.55
A


ATOM
56
CB
GLU
A
80
72.980
3.768
29.043
1.00
32.88
A


ATOM
57
CG
GLU
A
80
71.996
4.643
29.798
1.00
40.36
A


ATOM
58
CD
GLU
A
80
71.014
5.367
28.879
1.00
44.21
A


ATOM
59
OE1
GLU
A
80
70.422
4.700
28.000
1.00
46.94
A


ATOM
60
OE2
GLU
A
80
70.828
6.598
29.038
1.00
45.47
A


ATOM
61
C
GLU
A
80
74.872
3.524
27.479
1.00
28.32
A


ATOM
62
O
GLU
A
80
75.709
2.894
28.126
1.00
28.20
A


ATOM
63
N
ASP
A
81
74.698
3.342
26.168
1.00
26.28
A


ATOM
64
CA
ASP
A
81
75.528
2.384
25.441
1.00
23.59
A


ATOM
65
CB
ASP
A
81
74.834
1.888
24.184
1.00
25.08
A


ATOM
66
CG
ASP
A
81
73.510
1.225
24.477
1.00
28.14
A


ATOM
67
OD1
ASP
A
81
73.369
0.625
25.578
1.00
29.12
A


ATOM
68
OD2
ASP
A
81
72.617
1.294
23.601
1.00
28.33
A


ATOM
69
C
ASP
A
81
76.856
2.967
25.046
1.00
23.24
A


ATOM
70
O
ASP
A
81
77.716
2.257
24.519
1.00
24.29
A


ATOM
71
N
PHE
A
82
77.036
4.259
25.309
1.00
21.34
A


ATOM
72
CA
PHE
A
82
78.272
4.930
24.946
1.00
20.86
A


ATOM
73
CB
PHE
A
82
77.992
6.029
23.929
1.00
18.34
A


ATOM
74
CG
PHE
A
82
77.355
5.536
22.683
1.00
19.18
A


ATOM
75
CD1
PHE
A
82
78.138
5.099
21.610
1.00
19.28
A


ATOM
76
CD2
PHE
A
82
75.974
5.462
22.588
1.00
17.82
A


ATOM
77
CE1
PHE
A
82
77.551
4.597
20.461
1.00
17.94
A


ATOM
78
CE2
PHE
A
82
75.371
4.961
21.449
1.00
19.08
A


ATOM
79
CZ
PHE
A
82
76.164
4.525
20.376
1.00
20.45
A


ATOM
80
C
PHE
A
82
78.982
5.555
26.105
1.00
21.71
A


ATOM
81
O
PHE
A
82
78.418
5.739
27.173
1.00
24.82
A


ATOM
82
N
LYS
A
83
80.244
5.865
25.869
1.00
21.83
A


ATOM
83
CA
LYS
A
83
81.077
6.555
26.823
1.00
22.27
A


ATOM
84
CB
LYS
A
83
82.327
5.750
27.148
1.00
24.03
A


ATOM
85
CG
LYS
A
83
83.074
6.320
28.340
1.00
30.99
A


ATOM
86
CD
LYS
A
83
84.465
6.827
27.993
1.00
35.16
A


ATOM
87
CE
LYS
A
83
85.465
5.683
27.945
1.00
39.06
A


ATOM
88
NZ
LYS
A
83
85.512
4.974
29.266
1.00
41.00
A


ATOM
89
C
LYS
A
83
81.462
7.775
25.998
1.00
22.51
A


ATOM
90
O
LYS
A
83
82.324
7.677
25.120
1.00
23.24
A


ATOM
91
N
PHE
A
84
80.800
8.907
26.227
1.00
20.27
A


ATOM
92
CA
PHE
A
84
81.118
10.098
25.454
1.00
19.31
A


ATOM
93
CB
PHE
A
84
80.016
11.145
25.605
1.00
19.95
A


ATOM
94
CG
PHE
A
84
78.683
10.694
25.075
1.00
20.81
A


ATOM
95
CD1
PHE
A
84
77.855
9.879
25.835
1.00
21.62
A


ATOM
96
CD2
PHE
A
84
78.278
11.035
23.804
1.00
20.47
A


ATOM
97
CE1
PHE
A
84
76.665
9.418
25.339
1.00
19.26
A


ATOM
98
CE2
PHE
A
84
77.073
10.568
23.300
1.00
18.97
A


ATOM
99
CZ
PHE
A
84
76.276
9.764
24.068
1.00
19.78
A


ATOM
100
C
PHE
A
84
82.463
10.680
25.863
1.00
19.58
A


ATOM
101
O
PHE
A
84
82.888
10.540
26.998
1.00
20.60
A


ATOM
102
N
GLY
A
85
83.141
11.307
24.913
1.00
19.33
A


ATOM
103
CA
GLY
A
85
84.434
11.909
25.169
1.00
18.23
A


ATOM
104
C
GLY
A
85
84.480
13.368
24.743
1.00
19.96
A


ATOM
105
O
GLY
A
85
83.533
14.124
24.962
1.00
20.02
A


ATOM
106
N
LYS
A
86
85.568
13.764
24.101
1.00
20.79
A


ATOM
107
CA
LYS
A
86
85.736
15.159
23.704
1.00
22.45
A


ATOM
108
CB
LYS
A
86
87.168
15.400
23.210
1.00
22.06
A


ATOM
109
CG
LYS
A
86
87.399
15.048
21.751
1.00
23.37
A


ATOM
110
CD
LYS
A
86
88.832
14.591
21.505
1.00
26.45
A


ATOM
111
CE
LYS
A
86
89.451
15.275
20.294
1.00
30.25
A


ATOM
112
NZ
LYS
A
86
89.771
16.721
20.553
1.00
33.08
A


ATOM
113
C
LYS
A
86
84.750
15.668
22.661
1.00
21.50
A


ATOM
114
O
LYS
A
86
84.154
14.900
21.916
1.00
21.98
A


ATOM
115
N
ILE
A
87
84.582
16.985
22.647
1.00
20.15
A


ATOM
116
CA
ILE
A
87
83.712
17.661
21.705
1.00
19.38
A


ATOM
117
CB
ILE
A
87
83.270
19.037
22.272
1.00
17.37
A


ATOM
118
CG2
ILE
A
87
82.724
19.935
21.163
1.00
15.07
A


ATOM
119
CG1
ILE
A
87
82.222
18.800
23.371
1.00
18.62
A


ATOM
120
CD1
ILE
A
87
81.848
20.025
24.190
1.00
16.91
A


ATOM
121
C
ILE
A
87
84.549
17.836
20.436
1.00
19.85
A


ATOM
122
O
ILE
A
87
85.666
18.317
20.502
1.00
21.66
A


ATOM
123
N
LEU
A
88
84.030
17.406
19.293
1.00
19.65
A


ATOM
124
CA
LEU
A
88
84.771
17.539
18.047
1.00
20.20
A


ATOM
125
CB
LEU
A
88
84.423
16.405
17.078
1.00
18.76
A


ATOM
126
CG
LEU
A
88
84.807
14.981
17.493
1.00
16.99
A


ATOM
127
CD1
LEU
A
88
84.122
13.995
16.570
1.00
13.92
A


ATOM
128
CD2
LEU
A
88
86.305
14.809
17.441
1.00
11.51
A


ATOM
129
C
LEU
A
88
84.429
18.861
17.407
1.00
20.87
A


ATOM
130
O
LEU
A
88
85.233
19.443
16.709
1.00
21.48
A


ATOM
131
N
GLY
A
89
83.221
19.339
17.639
1.00
22.34
A


ATOM
132
CA
GLY
A
89
82.856
20.601
17.043
1.00
25.87
A


ATOM
133
C
GLY
A
89
81.476
21.057
17.451
1.00
29.45
A


ATOM
134
O
GLY
A
89
80.673
20.292
17.990
1.00
29.48
A


ATOM
135
N
GLU
A
90
81.196
22.321
17.188
1.00
32.71
A


ATOM
136
CA
GLU
A
90
79.904
22.864
17.530
1.00
37.61
A


ATOM
137
CB
GLU
A
90
80.047
23.798
18.738
1.00
38.05
A


ATOM
138
CG
GLU
A
90
80.123
22.998
20.037
1.00
42.04
A


ATOM
139
CD
GLU
A
90
80.463
23.813
21.270
1.00
45.47
A


ATOM
140
OE1
GLU
A
90
81.662
24.137
21.477
1.00
47.26
A


ATOM
141
OE2
GLU
A
90
79.524
24.119
22.041
1.00
47.39
A


ATOM
142
C
GLU
A
90
79.277
23.565
16.349
1.00
40.01
A


ATOM
143
O
GLU
A
90
79.972
24.148
15.518
1.00
42.05
A


ATOM
144
N
GLY
A
91
77.962
23.440
16.240
1.00
42.05
A


ATOM
145
CA
GLY
A
91
77.238
24.102
15.174
1.00
43.15
A


ATOM
146
C
GLY
A
91
76.276
25.035
15.892
1.00
45.06
A


ATOM
147
O
GLY
A
91
76.317
25.149
17.134
1.00
43.58
A


ATOM
148
N
SER
A
92
75.408
25.699
15.136
1.00
46.66
A


ATOM
149
CA
SER
A
92
74.430
26.606
15.742
1.00
48.21
A


ATOM
150
CB
SER
A
92
73.754
27.462
14.660
1.00
51.13
A


ATOM
151
CG
SER
A
92
73.601
26.741
13.439
1.00
54.79
A


ATOM
152
C
SER
A
92
73.382
25.827
16.538
1.00
47.10
A


ATOM
153
O
SER
A
92
73.055
26.190
17.678
1.00
49.44
A


ATOM
154
N
PHE
A
93
72.874
24.743
15.957
1.00
44.39
A


ATOM
155
CA
PHE
A
93
71.866
23.942
16.648
1.00
41.99
A


ATOM
156
CB
PHE
A
93
70.617
23.798
15.780
1.00
43.92
A


ATOM
157
CG
PHE
A
93
70.434
24.919
14.814
1.00
47.66
A


ATOM
158
CD1
PHE
A
93
70.689
24.729
13.455
1.00
49.35
A


ATOM
159
CD2
PHE
A
93
70.061
26.185
15.264
1.00
49.16
A


ATOM
160
CE1
PHE
A
93
70.581
25.789
12.551
1.00
51.11
A


ATOM
161
CE2
PHE
A
93
69.949
27.257
14.374
1.00
50.58
A


ATOM
162
CZ
PHE
A
93
70.209
27.062
13.014
1.00
51.37
A


ATOM
163
C
PHE
A
93
72.352
22.555
17.028
1.00
38.35
A


ATOM
164
O
PHE
A
93
71.532
21.670
17.257
1.00
38.33
A


ATOM
165
N
SER
A
94
73.665
22.351
17.106
1.00
33.28
A


ATOM
166
CA
SER
A
94
74.151
21.028
17.440
1.00
29.57
A


ATOM
167
CB
SER
A
94
73.996
20.106
16.227
1.00
30.45
A


ATOM
168
OG
SER
A
94
75.123
20.190
15.368
1.00
30.51
A


ATOM
169
C
SER
A
94
75.588
20.952
17.936
1.00
27.66
A


ATOM
170
O
SER
A
94
76.369
21.893
17.803
1.00
27.25
A


ATOM
171
N
THR
A
95
75.927
19.807
18.512
1.00
25.06
A


ATOM
172
CA
THR
A
95
77.264
19.572
19.027
1.00
23.70
A


ATOM
173
CB
THR
A
95
77.310
19.626
20.582
1.00
24.12
A


ATOM
174
OG1
THR
A
95
76.801
20.886
21.044
1.00
25.68
A


ATOM
175
CG2
THR
A
95
78.731
19.458
21.073
1.00
22.92
A


ATOM
176
C
THR
A
95
77.655
18.180
18.594
1.00
22.05
A


ATOM
177
O
THR
A
95
76.860
17.250
18.673
1.00
21.43
A


ATOM
178
N
VAL
A
96
78.883
18.029
18.129
1.00
21.52
A


ATOM
179
CA
VAL
A
96
79.348
16.723
17.702
1.00
19.53
A


ATOM
180
CB
VAL
A
96
79.980
16.818
16.316
1.00
19.24
A


ATOM
181
CG1
VAL
A
96
80.418
15.443
15.839
1.00
17.73
A


ATOM
182
CG2
VAL
A
96
78.983
17.442
15.353
1.00
18.03
A


ATOM
183
C
VAL
A
96
80.364
16.242
18.722
1.00
19.43
A


ATOM
184
O
VAL
A
96
81.372
16.910
18.959
1.00
19.84
A


ATOM
185
N
VAL
A
97
80.099
15.082
19.324
1.00
17.90
A


ATOM
186
CA
VAL
A
97
80.989
14.532
20.341
1.00
17.32
A


ATOM
187
CB
VAL
A
97
80.283
14.438
21.736
1.00
18.35
A


ATOM
188
CG1
VAL
A
97
79.581
15.750
22.066
1.00
20.10
A


ATOM
189
CG2
VAL
A
97
79.234
13.357
21.713
1.00
23.78
A


ATOM
190
C
VAL
A
97
81.471
13.144
19.949
1.00
17.15
A


ATOM
191
O
VAL
A
97
80.727
12.351
19.379
1.00
18.17
A


ATOM
192
N
LEU
A
98
82.735
12.866
20.243
1.00
17.34
A


ATOM
193
CA
LEU
A
98
83.331
11.575
19.974
1.00
17.44
A


ATOM
194
CB
LEU
A
98
84.853
11.689
19.990
1.00
17.84
A


ATOM
195
CG
LEU
A
98
85.656
10.407
19.737
1.00
18.59
A


ATOM
196
CD1
LEU
A
98
85.259
9.803
18.387
1.00
18.87
A


ATOM
197
CD2
LEU
A
98
87.151
10.738
19.772
1.00
16.62
A


ATOM
198
C
LEU
A
98
82.874
10.626
21.081
1.00
18.35
A


ATOM
199
O
LEU
A
98
82.992
10.926
22.259
1.00
18.60
A


ATOM
200
N
ALA
A
99
82.340
9.476
20.697
1.00
19.15
A


ATOM
201
CA
ALA
A
99
81.888
8.513
21.675
1.00
19.73
A


ATOM
202
CB
ALA
A
99
80.383
8.534
21.759
1.00
17.97
A


ATOM
203
C
ALA
A
99
82.360
7.117
21.317
1.00
21.86
A


ATOM
204
O
ALA
A
99
82.502
6.766
20.131
1.00
22.18
A


ATOM
205
N
ARG
A
100
82.631
6.324
22.345
1.00
21.93
A


ATOM
206
CA
ARG
A
100
83.025
4.963
22.102
1.00
23.29
A


ATOM
207
CB
ARG
A
100
84.333
4.637
22.805
1.00
25.99
A


ATOM
208
CG
ARG
A
100
84.870
3.271
22.388
1.00
31.56
A


ATOM
209
CD
ARG
A
100
86.146
2.923
23.129
1.00
35.19
A


ATOM
210
NE
ARG
A
100
87.220
3.875
22.847
1.00
37.39
A


ATOM
211
CZ
ARG
A
100
87.958
3.870
21.740
1.00
38.05
A


ATOM
212
NH1
ARG
A
100
87.742
2.953
20.797
1.00
37.25
A


ATOM
213
NH2
ARG
A
100
88.918
4.780
21.580
1.00
36.22
A


ATOM
214
C
ARG
A
100
81.904
4.060
22.603
1.00
22.07
A


ATOM
215
O
ARG
A
100
81.460
4.177
23.743
1.00
22.10
A


ATOM
216
N
GLU
A
101
81.417
3.189
21.734
1.00
21.29
A


ATOM
217
CA
GLU
A
101
80.357
2.262
22.119
1.00
22.87
A


ATOM
218
CB
GLU
A
101
79.747
1.631
20.867
1.00
23.10
A


ATOM
219
CG
GLU
A
101
78.740
0.563
21.148
1.00
22.71
A


ATOM
220
CD
GLU
A
101
78.128
0.040
19.878
1.00
23.56
A


ATOM
221
OE1
GLU
A
101
78.892
−0.198
18.922
1.00
21.84
A


ATOM
222
OE2
GLU
A
101
76.890
−0.143
19.832
1.00
26.29
A


ATOM
223
C
GLU
A
101
80.942
1.176
23.037
1.00
21.56
A


ATOM
224
O
GLU
A
101
81.884
0.485
22.666
1.00
20.69
A


ATOM
225
N
LEU
A
102
80.389
1.042
24.236
1.00
21.11
A


ATOM
226
CA
LEU
A
102
80.874
0.057
25.204
1.00
21.54
A


ATOM
227
CB
LEU
A
102
80.075
0.199
26.507
1.00
20.90
A


ATOM
228
CG
LEU
A
102
80.193
1.620
27.092
1.00
22.35
A


ATOM
229
CD1
LEU
A
102
79.177
1.798
28.207
1.00
20.18
A


ATOM
230
CD2
LEU
A
102
81.600
1.866
27.608
1.00
17.47
A


ATOM
231
C
LEU
A
102
80.896
−1.415
24.729
1.00
20.27
A


ATOM
232
O
LEU
A
102
81.922
−2.078
24.825
1.00
21.63
A


ATOM
233
N
ALA
A
103
79.792
−1.922
24.201
1.00
18.37
A


ATOM
234
CA
ALA
A
103
79.757
−3.307
23.731
1.00
20.54
A


ATOM
235
CB
ALA
A
103
78.333
−3.694
23.359
1.00
19.31
A


ATOM
236
C
ALA
A
103
80.688
−3.658
22.552
1.00
22.26
A


ATOM
237
O
ALA
A
103
81.002
−4.829
22.358
1.00
23.93
A


ATOM
238
N
THR
A
104
81.141
−2.677
21.775
1.00
20.79
A


ATOM
239
CA
THR
A
104
81.972
−2.999
20.622
1.00
21.40
A


ATOM
240
CB
THR
A
104
81.279
−2.632
19.326
1.00
20.97
A


ATOM
241
OG1
THR
A
104
81.174
−1.205
19.259
1.00
23.21
A


ATOM
242
CG2
THR
A
104
79.891
−3.266
19.245
1.00
19.82
A


ATOM
243
C
THR
A
104
83.304
−2.300
20.569
1.00
23.57
A


ATOM
244
O
THR
A
104
84.168
−2.687
19.796
1.00
23.41
A


ATOM
245
N
SER
A
105
83.454
−1.243
21.359
1.00
24.64
A


ATOM
246
CA
SER
A
105
84.687
−0.487
21.390
1.00
24.23
A


ATOM
247
CB
SER
A
105
85.855
−1.467
21.481
1.00
25.40
A


ATOM
248
OG
SER
A
105
87.074
−0.788
21.719
1.00
34.15
A


ATOM
249
C
SER
A
105
84.819
0.454
20.163
1.00
23.42
A


ATOM
250
O
SER
A
105
85.803
1.187
20.013
1.00
23.28
A


ATOM
251
N
ARG
A
106
83.821
0.448
19.295
1.00
21.19
A


ATOM
252
CA
ARG
A
106
83.850
1.323
18.115
1.00
22.25
A


ATOM
253
CB
ARG
A
106
82.754
0.922
17.118
1.00
24.82
A


ATOM
254
CG
ARG
A
106
83.027
−0.343
16.349
1.00
25.20
A


ATOM
255
CD
ARG
A
106
81.740
−0.942
15.884
1.00
25.19
A


ATOM
256
NE
ARG
A
106
81.972
−1.900
14.815
1.00
26.11
A


ATOM
257
CZ
ARG
A
106
81.042
−2.707
14.322
1.00
24.24
A


ATOM
258
NH1
ARG
A
106
79.805
−2.677
14.818
1.00
21.06
A


ATOM
259
NH2
ARG
A
106
81.351
−3.513
13.315
1.00
20.25
A


ATOM
260
C
ARG
A
106
83.655
2.806
18.433
1.00
19.79
A


ATOM
261
O
ARG
A
106
82.836
3.175
19.266
1.00
18.73
A


ATOM
262
N
GLU
A
107
84.404
3.646
17.736
1.00
19.82
A


ATOM
263
CA
GLU
A
107
84.294
5.086
17.903
1.00
21.14
A


ATOM
264
CB
GLU
A
107
85.656
5.746
17.777
1.00
21.88
A


ATOM
265
CG
GLU
A
107
86.562
5.428
18.926
1.00
26.09
A


ATOM
266
CD
GLU
A
107
87.916
6.043
18.746
1.00
30.29
A


ATOM
267
OE1
GLU
A
107
88.212
7.057
19.434
1.00
32.48
A


ATOM
268
OE2
GLU
A
107
88.678
5.512
17.901
1.00
31.98
A


ATOM
269
C
GLU
A
107
83.358
5.693
16.870
1.00
20.50
A


ATOM
270
O
GLU
A
107
83.474
5.429
15.676
1.00
20.70
A


ATOM
271
N
TYR
A
108
82.415
6.498
17.347
1.00
20.38
A


ATOM
272
CA
TYR
A
108
81.464
7.172
16.477
1.00
18.49
A


ATOM
273
CB
TYR
A
108
80.049
6.660
16.700
1.00
17.92
A


ATOM
274
CG
TYR
A
108
79.828
5.247
16.238
1.00
23.37
A


ATOM
275
CD1
TYR
A
108
79.598
4.964
14.886
1.00
22.79
A


ATOM
276
CE1
TYR
A
108
79.357
3.648
14.458
1.00
23.56
A


ATOM
277
CD2
TYR
A
108
79.820
4.180
17.154
1.00
21.34
A


ATOM
278
CE2
TYR
A
108
79.583
2.873
16.740
1.00
20.43
A


ATOM
279
CZ
TYR
A
108
79.346
2.609
15.392
1.00
23.44
A


ATOM
280
OH
TYR
A
108
79.061
1.321
14.972
1.00
24.10
A


ATOM
281
C
TYR
A
108
81.478
8.635
16.828
1.00
18.53
A


ATOM
282
O
TYR
A
108
81.778
9.011
17.971
1.00
17.37
A


ATOM
283
N
ALA
A
109
81.169
9.453
15.829
1.00
17.24
A


ATOM
284
CA
ALA
A
109
81.053
10.885
16.006
1.00
15.98
A


ATOM
285
CB
ALA
A
109
81.597
11.600
14.788
1.00
15.20
A


ATOM
286
C
ALA
A
109
79.528
11.087
16.140
1.00
15.73
A


ATOM
287
O
ALA
A
109
78.767
10.873
15.191
1.00
15.79
A


ATOM
288
N
ILE
A
110
79.070
11.474
17.320
1.00
14.95
A


ATOM
289
CA
ILE
A
110
77.636
11.636
17.511
1.00
15.99
A


ATOM
290
CB
ILE
A
110
77.188
10.940
18.815
1.00
15.51
A


ATOM
291
CG2
ILE
A
110
75.697
11.126
19.039
1.00
14.44
A


ATOM
292
CG1
ILE
A
110
77.541
9.452
18.729
1.00
16.63
A


ATOM
293
CD1
ILE
A
110
76.964
8.595
19.847
1.00
16.83
A


ATOM
294
C
ILE
A
110
77.176
13.085
17.514
1.00
16.55
A


ATOM
295
O
ILE
A
110
77.583
13.873
18.370
1.00
16.24
A


ATOM
296
N
LYS
A
111
76.343
13.430
16.538
1.00
16.03
A


ATOM
297
CA
LYS
A
111
75.804
14.777
16.430
1.00
18.21
A


ATOM
298
CB
LYS
A
111
75.341
15.065
14.997
1.00
19.36
A


ATOM
299
CG
LYS
A
111
75.035
16.548
14.768
1.00
22.68
A


ATOM
300
CD
LYS
A
111
74.461
16.844
13.396
1.00
23.67
A


ATOM
301
CE
LYS
A
111
74.876
18.222
12.930
1.00
23.18
A


ATOM
302
NZ
LYS
A
111
73.744
18.938
12.304
1.00
28.83
A


ATOM
303
C
LYS
A
111
74.608
14.866
17.383
1.00
17.40
A


ATOM
304
O
LYS
A
111
73.646
14.115
17.239
1.00
18.27
A


ATOM
305
N
ILE
A
112
74.672
15.781
18.344
1.00
15.41
A


ATOM
306
CA
ILE
A
112
73.609
15.938
19.331
1.00
16.56
A


ATOM
307
CB
ILE
A
112
74.194
15.819
20.777
1.00
17.09
A


ATOM
308
CG2
ILE
A
112
73.073
15.926
21.830
1.00
11.60
A


ATOM
309
CG1
ILE
A
112
74.957
14.480
20.885
1.00
16.81
A


ATOM
310
CD1
ILE
A
112
75.771
14.262
22.178
1.00
15.96
A


ATOM
311
C
ILE
A
112
72.876
17.261
19.158
1.00
17.98
A


ATOM
312
O
ILE
A
112
73.504
18.314
18.965
1.00
16.70
A


ATOM
313
N
LEU
A
113
71.546
17.198
19.195
1.00
19.61
A


ATOM
314
CA
LEU
A
113
70.711
18.393
19.034
1.00
21.99
A


ATOM
315
CB
LEU
A
113
70.058
18.434
17.641
1.00
22.17
A


ATOM
316
CG
LEU
A
113
70.906
18.273
16.367
1.00
22.83
A


ATOM
317
CD1
LEU
A
113
71.124
16.792
16.059
1.00
22.72
A


ATOM
318
CD2
LEU
A
113
70.191
18.912
15.206
1.00
21.97
A


ATOM
319
C
LEU
A
113
69.612
18.419
20.088
1.00
24.22
A


ATOM
320
O
LEU
A
113
69.062
17.378
20.469
1.00
24.61
A


ATOM
321
N
GLU
A
114
69.285
19.615
20.559
1.00
27.06
A


ATOM
322
CA
GLU
A
114
68.247
19.759
21.567
1.00
28.93
A


ATOM
323
CB
GLU
A
114
68.586
20.926
22.488
1.00
31.39
A


ATOM
324
CG
GLU
A
114
67.671
21.026
23.684
1.00
39.92
A


ATOM
325
CD
GLU
A
114
67.676
22.406
24.300
1.00
45.42
A


ATOM
326
OE1
GLU
A
114
67.160
23.356
23.655
1.00
46.90
A


ATOM
327
OE2
GLU
A
114
68.204
22.540
25.429
1.00
50.09
A


ATOM
328
C
GLU
A
114
66.887
19.978
20.892
1.00
29.21
A


ATOM
329
O
GLU
A
114
66.679
20.969
20.177
1.00
29.53
A


ATOM
330
N
LYS
A
115
65.962
19.051
21.116
1.00
28.74
A


ATOM
331
CA
LYS
A
115
64.642
19.152
20.507
1.00
29.44
A


ATOM
332
CB
LYS
A
115
63.744
18.002
20.987
1.00
28.12
A


ATOM
333
CG
LYS
A
115
63.827
16.758
20.103
1.00
28.47
A


ATOM
334
CD
LYS
A
115
63.026
15.571
20.639
1.00
27.07
A


ATOM
335
CE
LYS
A
115
63.738
14.854
21.779
1.00
28.88
A


ATOM
336
NZ
LYS
A
115
62.963
13.672
22.282
1.00
26.42
A


ATOM
337
C
LYS
A
115
63.947
20.502
20.724
1.00
29.72
A


ATOM
338
O
LYS
A
115
63.310
21.025
19.799
1.00
30.03
A


ATOM
339
N
ALA
A
116
64.082
21.091
21.910
1.00
28.83
A


ATOM
340
CA
ALA
A
116
63.407
22.365
22.159
1.00
29.91
A


ATOM
341
CB
ALA
A
116
63.470
22.749
23.647
1.00
28.16
A


ATOM
342
C
ALA
A
116
63.976
23.480
21.311
1.00
30.93
A


ATOM
343
O
ALA
A
116
63.231
24.217
20.667
1.00
32.28
A


ATOM
344
N
HIS
A
117
65.297
23.593
21.292
1.00
31.66
A


ATOM
345
CA
HIS
A
117
65.951
24.645
20.523
1.00
32.13
A


ATOM
346
CB
HIS
A
117
67.472
24.571
20.728
1.00
34.12
A


ATOM
347
CG
HIS
A
117
68.219
25.741
20.169
1.00
37.74
A


ATOM
348
CD2
HIS
A
117
67.794
26.959
19.761
1.00
39.67
A


ATOM
349
ND1
HIS
A
117
69.582
25.727
19.966
1.00
42.04
A


ATOM
350
CE1
HIS
A
117
69.965
26.884
19.454
1.00
41.07
A


ATOM
351
NE2
HIS
A
117
68.899
27.649
19.320
1.00
40.56
A


ATOM
352
C
HIS
A
117
65.600
24.547
19.040
1.00
31.36
A


ATOM
353
O
HIS
A
117
65.466
25.560
18.350
1.00
32.37
A


ATOM
354
N
ILE
A
118
65.430
23.330
18.544
1.00
30.26
A


ATOM
355
CA
ILE
A
118
65.102
23.158
17.132
1.00
29.28
A


ATOM
356
CB
ILE
A
118
65.266
21.696
16.712
1.00
27.64
A


ATOM
357
CG2
ILE
A
118
64.560
21.439
15.401
1.00
22.46
A


ATOM
358
CG1
ILE
A
118
66.756
21.371
16.642
1.00
27.22
A


ATOM
359
CD1
ILE
A
118
67.036
19.917
16.437
1.00
30.51
A


ATOM
360
C
ILE
A
118
63.688
23.618
16.816
1.00
30.41
A


ATOM
361
O
ILE
A
118
63.444
24.251
15.785
1.00
29.55
A


ATOM
362
N
ILE
A
119
62.756
23.291
17.705
1.00
29.59
A


ATOM
363
CA
ILE
A
119
61.376
23.682
17.497
1.00
29.18
A


ATOM
364
CB
ILE
A
119
60.447
22.979
18.506
1.00
27.15
A


ATOM
365
CG2
ILE
A
119
59.071
23.623
18.486
1.00
22.69
A


ATOM
366
CG1
ILE
A
119
60.394
21.486
18.173
1.00
23.45
A


ATOM
367
CD1
ILE
A
119
59.666
20.665
19.173
1.00
19.08
A


ATOM
368
C
ILE
A
119
61.223
25.194
17.617
1.00
30.65
A


ATOM
369
O
ILE
A
119
60.574
25.832
16.786
1.00
30.59
A


ATOM
370
N
ALA
A
120
61.837
25.768
18.642
1.00
31.95
A


ATOM
371
CA
ALA
A
120
61.752
27.205
18.848
1.00
33.69
A


ATOM
372
CB
ALA
A
120
62.473
27.608
20.150
1.00
33.17
A


ATOM
373
C
ALA
A
120
62.330
27.973
17.671
1.00
34.80
A


ATOM
374
O
ALA
A
120
61.865
29.067
17.362
1.00
37.34
A


ATOM
375
N
GLU
A
121
63.328
27.413
16.997
1.00
35.09
A


ATOM
376
CA
GLU
A
121
63.941
28.116
15.872
1.00
35.31
A


ATOM
377
CB
GLU
A
121
65.453
27.927
15.933
1.00
39.72
A


ATOM
378
CG
GLU
A
121
66.103
28.735
17.038
1.00
45.91
A


ATOM
379
CD
GLU
A
121
65.955
30.225
16.784
1.00
49.51
A


ATOM
380
OE1
GLU
A
121
66.634
30.736
15.866
1.00
52.87
A


ATOM
381
OE2
GLU
A
121
65.148
30.879
17.482
1.00
51.35
A


ATOM
382
C
GLU
A
121
63.421
27.699
14.499
1.00
34.14
A


ATOM
383
O
GLU
A
121
63.964
28.109
13.468
1.00
31.41
A


ATOM
384
N
ASN
A
122
62.363
26.891
14.497
1.00
33.86
A


ATOM
385
CA
ASN
A
122
61.771
26.367
13.266
1.00
34.00
A


ATOM
386
CB
ASN
A
122
61.112
27.473
12.464
1.00
36.75
A


ATOM
387
CG
ASN
A
122
59.962
28.081
13.193
1.00
39.62
A


ATOM
388
OD1
ASN
A
122
60.148
28.788
14.185
1.00
39.90
A


ATOM
389
ND2
ASN
A
122
58.753
27.794
12.727
1.00
41.02
A


ATOM
390
C
ASN
A
122
62.798
25.686
12.397
1.00
31.78
A


ATOM
391
O
ASN
A
122
62.958
26.035
11.230
1.00
32.05
A


ATOM
392
N
LYS
A
123
63.494
24.714
12.965
1.00
28.71
A


ATOM
393
CA
LYS
A
123
64.508
24.008
12.217
1.00
29.39
A


ATOM
394
CB
LYS
A
123
65.842
24.036
12.974
1.00
31.70
A


ATOM
395
CG
LYS
A
123
66.434
25.416
13.132
1.00
33.49
A


ATOM
396
CD
LYS
A
123
66.612
26.076
11.763
1.00
37.43
A


ATOM
397
CE
LYS
A
123
67.174
27.491
11.898
1.00
38.52
A


ATOM
398
NZ
LYS
A
123
67.337
28.176
10.582
1.00
37.85
A


ATOM
399
C
LYS
A
123
64.116
22.572
11.931
1.00
28.30
A


ATOM
400
O
LYS
A
123
64.867
21.844
11.289
1.00
29.68
A


ATOM
401
N
VAL
A
124
62.944
22.162
12.404
1.00
26.80
A


ATOM
402
CA
VAL
A
124
62.484
20.796
12.175
1.00
26.73
A


ATOM
403
CB
VAL
A
124
61.024
20.593
12.622
1.00
26.31
A


ATOM
404
CG1
VAL
A
124
60.532
19.222
12.191
1.00
25.31
A


ATOM
405
CG2
VAL
A
124
60.918
20.720
14.134
1.00
26.73
A


ATOM
406
C
VAL
A
124
62.594
20.351
10.722
1.00
27.11
A


ATOM
407
O
VAL
A
124
62.973
19.218
10.450
1.00
29.79
A


ATOM
408
N
PRO
A
125
62.270
21.228
9.763
1.00
27.28
A


ATOM
409
CD
PRO
A
125
61.610
22.544
9.818
1.00
27.49
A


ATOM
410
CA
PRO
A
125
62.386
20.758
8.378
1.00
27.41
A


ATOM
411
CB
PRO
A
125
61.775
21.904
7.563
1.00
26.08
A


ATOM
412
CG
PRO
A
125
60.821
22.546
8.524
1.00
27.54
A


ATOM
413
C
PRO
A
125
63.837
20.506
8.006
1.00
27.90
A


ATOM
414
O
PRO
A
125
64.162
19.572
7.260
1.00
26.27
A


ATOM
415
N
TYR
A
126
64.703
21.350
8.550
1.00
28.64
A


ATOM
416
CA
TYR
A
126
66.123
21.271
8.288
1.00
30.11
A


ATOM
417
CB
TYR
A
126
66.791
22.528
8.809
1.00
36.70
A


ATOM
418
CG
TYR
A
126
66.440
23.774
8.013
1.00
44.64
A


ATOM
419
CD1
TYR
A
126
66.984
23.988
6.744
1.00
47.43
A


ATOM
420
CE1
TYR
A
126
66.737
25.173
6.037
1.00
50.16
A


ATOM
421
CD2
TYR
A
126
65.620
24.774
8.557
1.00
47.03
A


ATOM
422
CE2
TYR
A
126
65.369
25.955
7.861
1.00
49.52
A


ATOM
423
CZ
TYR
A
126
65.936
26.152
6.605
1.00
50.60
A


ATOM
424
OH
TYR
A
126
65.754
27.349
5.941
1.00
52.77
A


ATOM
425
C
TYR
A
126
66.794
20.041
8.874
1.00
28.69
A


ATOM
426
O
TYR
A
126
67.613
19.407
8.208
1.00
28.32
A


ATOM
427
N
VAL
A
127
66.464
19.714
10.118
1.00
25.64
A


ATOM
428
CA
VAL
A
127
67.033
18.550
10.766
1.00
24.89
A


ATOM
429
CB
VAL
A
127
66.664
18.513
12.258
1.00
26.70
A


ATOM
430
CG1
VAL
A
127
67.158
17.206
12.881
1.00
22.51
A


ATOM
431
CG2
VAL
A
127
67.255
19.743
12.972
1.00
23.84
A


ATOM
432
C
VAL
A
127
66.521
17.276
10.097
1.00
24.81
A


ATOM
433
O
VAL
A
127
67.260
16.315
9.890
1.00
24.02
A


ATOM
434
N
THR
A
128
65.245
17.290
9.755
1.00
24.02
A


ATOM
435
CA
THR
A
128
64.608
16.164
9.088
1.00
24.59
A


ATOM
436
CB
THR
A
128
63.123
16.471
8.843
1.00
25.38
A


ATOM
437
CG1
THR
A
128
62.478
16.652
10.106
1.00
25.76
A


ATOM
438
CG2
THR
A
128
62.451
15.354
8.066
1.00
22.88
A


ATOM
439
C
THR
A
128
65.266
15.875
7.744
1.00
24.53
A


ATOM
440
O
THR
A
128
65.560
14.729
7.426
1.00
25.53
A


ATOM
441
N
ARG
A
129
65.477
16.925
6.957
1.00
24.82
A


ATOM
442
CA
ARG
A
129
66.099
16.812
5.646
1.00
25.49
A


ATOM
443
CB
ARG
A
129
66.111
18.181
4.959
1.00
26.78
A


ATOM
444
CG
ARG
A
129
66.648
18.175
3.529
1.00
32.33
A


ATOM
445
CD
ARG
A
129
66.579
19.563
2.878
1.00
36.93
A


ATOM
446
NE
ARG
A
129
65.326
20.249
3.184
1.00
42.70
A


ATOM
447
CZ
ARG
A
129
65.254
21.462
3.730
1.00
46.67
A


ATOM
448
NH1
ARG
A
129
66.366
22.128
4.018
1.00
48.50
A


ATOM
449
NH2
ARG
A
129
64.073
21.997
4.027
1.00
48.90
A


ATOM
450
C
ARG
A
129
67.532
16.296
5.801
1.00
26.46
A


ATOM
451
O
ARG
A
129
68.002
15.456
5.020
1.00
24.76
A


ATOM
452
N
GLU
A
130
68.216
16.795
6.825
1.00
25.56
A


ATOM
453
CA
GLU
A
130
69.582
16.393
7.076
1.00
28.29
A


ATOM
454
CB
GLU
A
130
70.118
17.106
8.310
1.00
27.95
A


ATOM
455
CG
GLU
A
130
71.591
16.875
8.539
1.00
29.48
A


ATOM
456
CD
GLU
A
130
72.107
17.566
9.787
1.00
32.14
A


ATOM
457
OE1
GLU
A
130
71.297
18.221
10.483
1.00
32.67
A


ATOM
458
OE2
GLU
A
130
73.325
17.450
10.069
1.00
32.21
A


ATOM
459
C
GLU
A
130
69.665
14.886
7.279
1.00
29.86
A


ATOM
460
O
GLU
A
130
70.498
14.200
6.668
1.00
29.35
A


ATOM
461
N
ARG
A
131
68.797
14.382
8.150
1.00
30.84
A


ATOM
462
CA
ARG
A
131
68.763
12.966
8.451
1.00
31.62
A


ATOM
463
CB
ARG
A
131
67.786
12.684
9.598
1.00
33.12
A


ATOM
464
CG
ARG
A
131
67.557
11.190
9.831
1.00
36.17
A


ATOM
465
CD
ARG
A
131
66.560
10.925
10.946
1.00
41.69
A


ATOM
466
NE
ARG
A
131
66.330
9.492
11.166
1.00
46.62
A


ATOM
467
CZ
ARG
A
131
65.692
8.986
12.224
1.00
48.29
A


ATOM
468
NH1
ARG
A
131
65.215
9.795
13.165
1.00
49.51
A


ATOM
469
NH2
ARG
A
131
65.544
7.671
12.352
1.00
48.76
A


ATOM
470
C
ARG
A
131
68.371
12.138
7.235
1.00
30.59
A


ATOM
471
O
ARG
A
131
68.897
11.051
7.026
1.00
29.96
A


ATOM
472
N
ASP
A
132
67.446
12.649
6.433
1.00
29.54
A


ATOM
473
CA
ASP
A
132
67.000
11.913
5.259
1.00
29.40
A


ATOM
474
CB
ASP
A
132
65.735
12.565
4.708
1.00
32.43
A


ATOM
475
CG
ASP
A
132
64.531
12.395
5.655
1.00
38.15
A


ATOM
476
OD1
ASP
A
132
64.749
12.227
6.881
1.00
40.40
A


ATOM
477
OD2
ASP
A
132
63.365
12.439
5.186
1.00
41.19
A


ATOM
478
C
ASP
A
132
68.088
11.789
4.189
1.00
27.62
A


ATOM
479
O
ASP
A
132
68.232
10.744
3.553
1.00
26.54
A


ATOM
480
N
VAL
A
133
68.862
12.850
4.011
1.00
25.14
A


ATOM
481
CA
VAL
A
133
69.939
12.857
3.044
1.00
24.12
A


ATOM
482
CB
VAL
A
133
70.451
14.272
2.833
1.00
24.07
A


ATOM
483
CG1
VAL
A
133
71.802
14.247
2.143
1.00
23.77
A


ATOM
484
CG2
VAL
A
133
69.461
15.030
2.008
1.00
24.30
A


ATOM
485
C
VAL
A
133
71.099
11.975
3.504
1.00
24.97
A


ATOM
486
O
VAL
A
133
71.672
11.221
2.712
1.00
24.95
A


ATOM
487
N
MET
A
134
71.458
12.074
4.779
1.00
23.41
A


ATOM
488
CA
MET
A
134
72.539
11.255
5.268
1.00
23.12
A


ATOM
489
CB
MET
A
134
72.932
11.653
6.683
1.00
21.12
A


ATOM
490
CG
MET
A
134
73.608
13.005
6.759
1.00
21.21
A


ATOM
491
SD
MET
A
134
74.530
13.204
8.291
1.00
20.52
A


ATOM
492
CE
MET
A
134
73.172
13.347
9.534
1.00
17.71
A


ATOM
493
C
MET
A
134
72.163
9.783
5.237
1.00
24.75
A


ATOM
494
O
MET
A
134
73.027
8.918
5.039
1.00
25.73
A


ATOM
495
N
SER
A
135
70.885
9.474
5.425
1.00
23.96
A


ATOM
496
CA
SER
A
135
70.484
8.064
5.408
1.00
24.82
A


ATOM
497
CB
SER
A
135
69.048
7.889
5.917
1.00
24.63
A


ATOM
498
OG
SER
A
135
68.139
8.496
5.015
1.00
29.80
A


ATOM
499
C
SER
A
135
70.585
7.479
4.003
1.00
22.35
A


ATOM
500
O
SER
A
135
70.534
6.274
3.829
1.00
21.60
A


ATOM
501
N
ARG
A
136
70.729
8.335
3.004
1.00
21.91
A


ATOM
502
CA
ARG
A
136
70.815
7.858
1.631
1.00
23.76
A


ATOM
503
CB
ARG
A
136
69.988
8.762
0.714
1.00
25.55
A


ATOM
504
CG
ARG
A
136
68.500
8.782
1.069
1.00
31.38
A


ATOM
505
CD
ARG
A
136
67.764
9.897
0.332
1.00
33.65
A


ATOM
506
NE
ARG
A
136
68.024
9.809
−1.099
1.00
38.77
A


ATOM
507
CZ
ARG
A
136
67.654
10.718
−1.996
1.00
41.27
A


ATOM
508
NH1
ARG
A
136
66.988
11.806
−1.604
1.00
42.53
A


ATOM
509
NH2
ARG
A
136
67.971
10.544
−3.286
1.00
39.41
A


ATOM
510
C
ARG
A
136
72.248
7.789
1.131
1.00
22.64
A


ATOM
511
O
ARG
A
136
72.520
7.268
0.052
1.00
22.43
A


ATOM
512
N
LEU
A
137
73.168
8.318
1.919
1.00
22.66
A


ATOM
513
CA
LEU
A
137
74.568
8.307
1.535
1.00
22.60
A


ATOM
514
CB
LEU
A
137
75.348
9.375
2.308
1.00
20.28
A


ATOM
515
CG
LEU
A
137
74.842
10.793
2.068
1.00
19.72
A


ATOM
516
CD1
LEU
A
137
75.695
11.816
2.840
1.00
17.83
A


ATOM
517
CD2
LEU
A
137
74.855
11.062
0.564
1.00
18.39
A


ATOM
518
C
LEU
A
137
75.195
6.950
1.775
1.00
22.60
A


ATOM
519
O
LEU
A
137
75.203
6.445
2.892
1.00
23.75
A


ATOM
520
N
ASP
A
138
75.723
6.371
0.710
1.00
22.09
A


ATOM
521
CA
ASP
A
138
76.383
5.083
0.788
1.00
22.63
A


ATOM
522
CB
ASP
A
138
75.419
3.988
0.340
1.00
25.16
A


ATOM
523
CG
ASP
A
138
75.976
2.622
0.582
1.00
26.26
A


ATOM
524
OD1
ASP
A
138
76.658
2.480
1.611
1.00
27.29
A


ATOM
525
OD2
ASP
A
138
75.740
1.708
−0.237
1.00
30.75
A


ATOM
526
C
ASP
A
138
77.617
5.112
−0.124
1.00
20.82
A


ATOM
527
O
ASP
A
138
77.656
4.445
−1.155
1.00
22.94
A


ATOM
528
N
HIS
A
139
78.612
5.902
0.250
1.00
16.77
A


ATOM
529
CA
HIS
A
139
79.813
6.050
−0.557
1.00
16.21
A


ATOM
530
CB
HIS
A
139
79.614
7.180
−1.583
1.00
15.30
A


ATOM
531
CG
HIS
A
139
80.755
7.348
−2.534
1.00
16.37
A


ATOM
532
CD2
HIS
A
139
80.853
7.087
−3.860
1.00
15.32
A


ATOM
533
ND1
HIS
A
139
81.998
7.802
−2.139
1.00
17.12
A


ATOM
534
CE1
HIS
A
139
82.811
7.810
−3.184
1.00
15.92
A


ATOM
535
NE2
HIS
A
139
82.140
7.380
−4.238
1.00
13.96
A


ATOM
536
C
HIS
A
139
80.985
6.371
0.357
1.00
16.70
A


ATOM
537
O
HIS
A
139
80.848
7.116
1.317
1.00
16.89
A


ATOM
538
N
PRO
A
140
82.164
5.823
0.056
1.00
16.94
A


ATOM
539
CD
PRO
A
140
82.508
4.991
−1.108
1.00
17.10
A


ATOM
540
CA
PRO
A
140
83.334
6.079
0.895
1.00
17.98
A


ATOM
541
CB
PRO
A
140
84.390
5.163
0.291
1.00
17.03
A


ATOM
542
CG
PRO
A
140
84.003
5.114
−1.159
1.00
18.59
A


ATOM
543
C
PRO
A
140
83.822
7.528
1.070
1.00
18.59
A


ATOM
544
O
PRO
A
140
84.528
7.817
2.021
1.00
20.11
A


ATOM
545
N
PHE
A
141
83.460
8.444
0.179
1.00
19.62
A


ATOM
546
CA
PHE
A
141
83.909
9.833
0.345
1.00
18.34
A


ATOM
547
CB
PHE
A
141
84.223
10.474
−1.010
1.00
17.53
A


ATOM
548
CG
PHE
A
141
85.440
9.880
−1.694
1.00
17.38
A


ATOM
549
CD1
PHE
A
141
86.450
9.275
−0.938
1.00
17.01
A


ATOM
550
CD2
PHE
A
141
85.579
9.926
−3.081
1.00
15.76
A


ATOM
551
CE1
PHE
A
141
87.572
8.724
−1.550
1.00
16.13
A


ATOM
552
CE2
PHE
A
141
86.707
9.375
−3.708
1.00
16.99
A


ATOM
553
CZ
PHE
A
141
87.705
8.772
−2.938
1.00
15.01
A


ATOM
554
C
PHE
A
141
82.893
10.680
1.095
1.00
18.14
A


ATOM
555
O
PHE
A
141
83.012
11.896
1.144
1.00
20.74
A


ATOM
556
N
PHE
A
142
81.901
10.037
1.697
1.00
15.85
A


ATOM
557
CA
PHE
A
142
80.887
10.761
2.444
1.00
15.95
A


ATOM
558
CB
PHE
A
142
79.558
10.757
1.690
1.00
15.20
A


ATOM
559
CG
PHE
A
142
79.507
11.721
0.542
1.00
15.62
A


ATOM
560
CD1
PHE
A
142
79.295
13.086
0.768
1.00
14.51
A


ATOM
561
CD2
PHE
A
142
79.651
11.265
−0.771
1.00
12.05
A


ATOM
562
CE1
PHE
A
142
79.222
13.991
−0.291
1.00
13.97
A


ATOM
563
CE2
PHE
A
142
79.582
12.157
−1.840
1.00
15.46
A


ATOM
564
CZ
PHE
A
142
79.365
13.536
−1.601
1.00
14.89
A


ATOM
565
C
PHE
A
142
80.654
10.167
3.824
1.00
15.60
A


ATOM
566
O
PHE
A
142
80.886
8.986
4.061
1.00
15.39
A


ATOM
567
N
VAL
A
143
80.182
11.001
4.733
1.00
15.87
A


ATOM
568
CA
VAL
A
143
79.878
10.564
6.075
1.00
15.04
A


ATOM
569
CB
VAL
A
143
79.304
11.727
6.905
1.00
15.26
A


ATOM
570
CG1
VAL
A
143
78.012
12.231
6.276
1.00
11.03
A


ATOM
571
CG2
VAL
A
143
79.100
11.296
8.350
1.00
14.40
A


ATOM
572
C
VAL
A
143
78.828
9.479
5.935
1.00
15.52
A


ATOM
573
O
VAL
A
143
78.076
9.453
4.963
1.00
15.45
A


ATOM
574
N
LYS
A
144
78.794
8.580
6.907
1.00
16.29
A


ATOM
575
CA
LYS
A
144
77.848
7.482
6.933
1.00
17.45
A


ATOM
576
CB
LYS
A
144
78.625
6.150
6.895
1.00
18.05
A


ATOM
577
CG
LYS
A
144
77.963
4.967
7.596
1.00
24.34
A


ATOM
578
CD
LYS
A
144
76.922
4.263
6.752
1.00
26.35
A


ATOM
579
CE
LYS
A
144
77.461
2.926
6.213
1.00
30.22
A


ATOM
580
NZ
LYS
A
144
77.576
1.882
7.271
1.00
28.27
A


ATOM
581
C
LYS
A
144
77.024
7.626
8.222
1.00
17.39
A


ATOM
582
O
LYS
A
144
77.565
7.913
9.284
1.00
16.92
A


ATOM
583
N
LEU
A
145
75.711
7.458
8.116
1.00
17.41
A


ATOM
584
CA
LEU
A
145
74.836
7.549
9.274
1.00
18.13
A


ATOM
585
CB
LEU
A
145
73.514
8.210
8.893
1.00
18.86
A


ATOM
586
CG
LEU
A
145
72.612
8.850
9.964
1.00
20.13
A


ATOM
587
CD1
LEU
A
145
71.157
8.607
9.582
1.00
19.48
A


ATOM
588
CD2
LEU
A
145
72.900
8.311
11.331
1.00
17.86
A


ATOM
589
C
LEU
A
145
74.559
6.113
9.689
1.00
18.85
A


ATOM
590
O
LEU
A
145
73.905
5.379
8.954
1.00
20.15
A


ATOM
591
N
TYR
A
146
75.030
5.713
10.867
1.00
18.09
A


ATOM
592
CA
TYR
A
146
74.830
4.341
11.329
1.00
15.93
A


ATOM
593
CB
TYR
A
146
76.013
3.871
12.154
1.00
14.52
A


ATOM
594
CG
TYR
A
146
77.295
3.776
11.390
1.00
13.98
A


ATOM
595
CD1
TYR
A
146
78.093
4.907
11.193
1.00
15.01
A


ATOM
596
CE1
TYR
A
146
79.329
4.815
10.548
1.00
14.94
A


ATOM
597
CD2
TYR
A
146
77.752
2.541
10.912
1.00
14.36
A


ATOM
598
CE2
TYR
A
146
78.984
2.426
10.266
1.00
15.47
A


ATOM
599
CZ
TYR
A
146
79.770
3.566
10.090
1.00
15.70
A


ATOM
600
OH
TYR
A
146
80.999
3.473
9.491
1.00
16.29
A


ATOM
601
C
TYR
A
146
73.591
4.135
12.154
1.00
16.74
A


ATOM
602
O
TYR
A
146
73.004
3.050
12.132
1.00
17.63
A


ATOM
603
N
PHE
A
147
73.198
5.158
12.901
1.00
15.90
A


ATOM
604
CA
PHE
A
147
72.012
5.041
13.745
1.00
17.10
A


ATOM
605
CB
PHE
A
147
72.265
4.057
14.932
1.00
14.80
A


ATOM
606
CG
PHE
A
147
73.509
4.366
15.747
1.00
16.36
A


ATOM
607
CD1
PHE
A
147
73.526
5.427
16.657
1.00
15.38
A


ATOM
608
CD2
PHE
A
147
74.701
3.663
15.514
1.00
16.83
A


ATOM
609
CE1
PHE
A
147
74.709
5.801
17.314
1.00
15.96
A


ATOM
610
CE2
PHE
A
147
75.907
4.024
16.163
1.00
16.65
A


ATOM
611
CZ
PHE
A
147
75.908
5.107
17.069
1.00
16.96
A


ATOM
612
C
PHE
A
147
71.550
6.378
14.286
1.00
17.73
A


ATOM
613
O
PHE
A
147
72.225
7.399
14.145
1.00
18.47
A


ATOM
614
N
THR
A
148
70.376
6.352
14.897
1.00
19.28
A


ATOM
615
CA
THR
A
148
69.801
7.529
15.532
1.00
19.50
A


ATOM
616
CB
THR
A
148
68.846
8.308
14.597
1.00
19.24
A


ATOM
617
OG1
THR
A
148
67.722
7.485
14.271
1.00
18.29
A


ATOM
618
CG2
THR
A
148
69.563
8.727
13.311
1.00
18.53
A


ATOM
619
C
THR
A
148
68.976
7.071
16.718
1.00
19.68
A


ATOM
620
O
THR
A
148
68.556
5.915
16.802
1.00
20.20
A


ATOM
621
N
PHE
A
149
68.765
7.975
17.653
1.00
20.20
A


ATOM
622
CA
PHE
A
149
67.926
7.687
18.797
1.00
20.34
A


ATOM
623
CB
PHE
A
149
68.558
6.626
19.728
1.00
19.06
A


ATOM
624
CG
PHE
A
149
69.932
6.961
20.216
1.00
18.27
A


ATOM
625
CD1
PHE
A
149
70.114
7.745
21.357
1.00
19.90
A


ATOM
626
CD2
PHE
A
149
71.049
6.467
19.559
1.00
19.21
A


ATOM
627
CE1
PHE
A
149
71.387
8.028
21.840
1.00
19.04
A


ATOM
628
CE2
PHE
A
149
72.341
6.741
20.025
1.00
19.95
A


ATOM
629
CZ
PHE
A
149
72.513
7.520
21.167
1.00
21.19
A


ATOM
630
C
PHE
A
149
67.693
9.004
19.487
1.00
20.94
A


ATOM
631
O
PHE
A
149
68.192
10.035
19.042
1.00
17.91
A


ATOM
632
N
GLN
A
150
66.888
8.988
20.539
1.00
25.44
A


ATOM
633
CA
GLN
A
150
66.609
10.212
21.279
1.00
29.09
A


ATOM
634
CB
GLN
A
150
65.518
11.039
20.571
1.00
29.07
A


ATOM
635
CG
GLN
A
150
64.194
10.322
20.309
1.00
31.07
A


ATOM
636
CD
GLN
A
150
63.150
11.227
19.609
1.00
32.52
A


ATOM
637
OE1
GLN
A
150
62.503
12.075
20.243
1.00
30.50
A


ATOM
638
NE2
GLN
A
150
63.009
11.056
18.294
1.00
29.34
A


ATOM
639
C
GLN
A
150
66.190
9.927
22.707
1.00
29.59
A


ATOM
640
O
GLN
A
150
65.738
8.832
23.018
1.00
30.34
A


ATOM
641
N
ASP
A
151
66.407
10.892
23.590
1.00
31.52
A


ATOM
642
CA
ASP
A
151
65.957
10.750
24.967
1.00
32.22
A


ATOM
643
CB
ASP
A
151
67.093
10.948
25.974
1.00
31.30
A


ATOM
644
CG
ASP
A
151
67.832
12.246
25.790
1.00
32.39
A


ATOM
645
OD1
ASP
A
151
67.241
13.217
25.263
1.00
34.30
A


ATOM
646
OD2
ASP
A
151
69.011
12.290
26.195
1.00
32.02
A


ATOM
647
C
ASP
A
151
64.914
11.858
25.063
1.00
33.56
A


ATOM
648
O
ASP
A
151
64.495
12.387
24.033
1.00
34.76
A


ATOM
649
N
ASP
A
152
64.498
12.239
26.261
1.00
35.00
A


ATOM
650
CA
ASP
A
152
63.462
13.268
26.369
1.00
36.72
A


ATOM
651
CB
ASP
A
152
63.053
13.465
27.830
1.00
38.27
A


ATOM
652
CG
ASP
A
152
62.237
12.312
28.351
1.00
42.45
A


ATOM
653
OD1
ASP
A
152
61.377
11.824
27.579
1.00
43.52
A


ATOM
654
OD2
ASP
A
152
62.444
11.900
29.519
1.00
44.28
A


ATOM
655
C
ASP
A
152
63.758
14.627
25.759
1.00
36.47
A


ATOM
656
O
ASP
A
152
62.857
15.289
25.242
1.00
36.12
A


ATOM
657
N
GLU
A
153
65.021
15.029
25.781
1.00
36.09
A


ATOM
658
CA
GLU
A
153
65.358
16.343
25.292
1.00
35.16
A


ATOM
659
CB
GLU
A
153
65.976
17.137
26.442
1.00
39.45
A


ATOM
660
CG
GLU
A
153
65.486
16.714
27.830
1.00
45.94
A


ATOM
661
CD
GLU
A
153
66.383
15.652
28.468
1.00
51.78
A


ATOM
662
OE1
GLU
A
153
67.563
15.977
28.746
1.00
54.51
A


ATOM
663
OE2
GLU
A
153
65.924
14.500
28.689
1.00
52.47
A


ATOM
664
C
GLU
A
153
66.258
16.455
24.073
1.00
32.91
A


ATOM
665
O
GLU
A
153
66.304
17.524
23.457
1.00
31.19
A


ATOM
666
N
LYS
A
154
66.959
15.376
23.710
1.00
30.19
A


ATOM
667
CA
LYS
A
154
67.898
15.431
22.582
1.00
26.56
A


ATOM
668
CB
LYS
A
154
69.323
15.414
23.121
1.00
24.92
A


ATOM
669
CG
LYS
A
154
69.630
16.551
24.041
1.00
23.66
A


ATOM
670
CD
LYS
A
154
70.944
16.355
24.750
1.00
20.95
A


ATOM
671
CE
LYS
A
154
71.274
17.583
25.576
1.00
18.98
A


ATOM
672
NZ
LYS
A
154
72.491
17.388
26.360
1.00
19.19
A


ATOM
673
C
LYS
A
154
67.806
14.374
21.487
1.00
25.00
A


ATOM
674
O
LYS
A
154
67.342
13.257
21.701
1.00
25.62
A


ATOM
675
N
LEU
A
155
68.276
14.759
20.308
1.00
23.36
A


ATOM
676
CA
LEU
A
155
68.337
13.881
19.140
1.00
22.19
A


ATOM
677
CB
LEU
A
155
67.946
14.624
17.864
1.00
21.64
A


ATOM
678
CG
LEU
A
155
66.539
15.167
17.707
1.00
22.58
A


ATOM
679
CD1
LEU
A
155
66.437
15.847
16.350
1.00
22.74
A


ATOM
680
CD2
LEU
A
155
65.533
14.034
17.815
1.00
23.23
A


ATOM
681
C
LEU
A
155
69.798
13.474
19.004
1.00
20.69
A


ATOM
682
O
LEU
A
155
70.693
14.287
19.249
1.00
21.61
A


ATOM
683
N
TYR
A
156
70.036
12.238
18.592
1.00
18.69
A


ATOM
684
CA
TYR
A
156
71.393
11.737
18.431
1.00
18.65
A


ATOM
685
CB
TYR
A
156
71.690
10.661
19.489
1.00
18.51
A


ATOM
686
CG
TYR
A
156
71.602
11.148
20.913
1.00
17.86
A


ATOM
687
CD1
TYR
A
156
70.372
11.287
21.550
1.00
18.38
A


ATOM
688
CE1
TYR
A
156
70.286
11.752
22.862
1.00
18.95
A


ATOM
689
CD2
TYR
A
156
72.755
11.488
21.621
1.00
19.32
A


ATOM
690
CE2
TYR
A
156
72.690
11.957
22.942
1.00
18.14
A


ATOM
691
CZ
TYR
A
156
71.449
12.086
23.551
1.00
18.56
A


ATOM
692
OH
TYR
A
156
71.372
12.547
24.838
1.00
18.33
A


ATOM
693
C
TYR
A
156
71.640
11.125
17.059
1.00
18.03
A


ATOM
694
O
TYR
A
156
70.903
10.250
16.646
1.00
18.18
A


ATOM
695
N
PHE
A
157
72.662
11.568
16.338
1.00
17.19
A


ATOM
696
CA
PHE
A
157
72.937
10.934
15.062
1.00
17.15
A


ATOM
697
CB
PHE
A
157
72.980
11.951
13.918
1.00
21.54
A


ATOM
698
CG
PHE
A
157
71.663
12.638
13.651
1.00
26.82
A


ATOM
699
CD1
PHE
A
157
70.471
12.165
14.221
1.00
30.87
A


ATOM
700
CD2
PHE
A
157
71.617
13.794
12.869
1.00
28.42
A


ATOM
701
CE1
PHE
A
157
69.249
12.845
14.024
1.00
30.45
A


ATOM
702
CE2
PHE
A
157
70.407
14.483
12.661
1.00
29.44
A


ATOM
703
CZ
PHE
A
157
69.224
14.008
13.243
1.00
30.41
A


ATOM
704
C
PHE
A
157
74.286
10.244
15.184
1.00
16.38
A


ATOM
705
O
PHE
A
157
75.256
10.883
15.527
1.00
17.91
A


ATOM
706
N
GLY
A
158
74.347
8.942
14.919
1.00
16.20
A


ATOM
707
CA
GLY
A
158
75.614
8.232
15.009
1.00
15.78
A


ATOM
708
C
GLY
A
158
76.322
8.285
13.671
1.00
16.51
A


ATOM
709
O
GLY
A
158
75.876
7.659
12.710
1.00
17.95
A


ATOM
710
N
LEU
A
159
77.423
9.028
13.600
1.00
14.97
A


ATOM
711
CA
LEU
A
159
78.143
9.177
12.342
1.00
15.17
A


ATOM
712
CB
LEU
A
159
78.264
10.669
12.012
1.00
13.14
A


ATOM
713
CG
LEU
A
159
76.989
11.518
12.133
1.00
12.95
A


ATOM
714
CD1
LEU
A
159
77.347
13.002
11.872
1.00
 7.84
A


ATOM
715
CD2
LEU
A
159
75.926
11.020
11.138
1.00
11.24
A


ATOM
716
C
LEU
A
159
79.535
8.540
12.300
1.00
15.49
A


ATOM
717
O
LEU
A
159
80.136
8.256
13.333
1.00
15.76
A


ATOM
718
N
SER
A
160
80.051
8.313
11.097
1.00
14.32
A


ATOM
719
CA
SER
A
160
81.389
7.759
10.984
1.00
14.68
A


ATOM
720
CB
SER
A
160
81.699
7.386
9.529
1.00
12.79
A


ATOM
721
OG
SER
A
160
81.395
8.432
8.626
1.00
16.15
A


ATOM
722
C
SER
A
160
82.365
8.823
11.509
1.00
15.82
A


ATOM
723
O
SER
A
160
82.152
10.029
11.333
1.00
17.75
A


ATOM
724
N
TYR
A
161
83.418
8.386
12.184
1.00
16.30
A


ATOM
725
CA
TYR
A
161
84.399
9.309
12.740
1.00
17.11
A


ATOM
726
CB
TYR
A
161
84.863
8.785
14.100
1.00
16.09
A


ATOM
727
CG
TYR
A
161
86.020
9.529
14.717
1.00
19.80
A


ATOM
728
CD1
TYR
A
161
86.070
10.933
14.700
1.00
18.64
A


ATOM
729
CE1
TYR
A
161
87.091
11.625
15.345
1.00
19.50
A


ATOM
730
CD2
TYR
A
161
87.032
8.837
15.394
1.00
20.09
A


ATOM
731
CE2
TYR
A
161
88.057
9.517
16.047
1.00
21.66
A


ATOM
732
CZ
TYR
A
161
88.085
10.918
16.022
1.00
23.52
A


ATOM
733
OH
TYR
A
161
89.111
11.600
16.674
1.00
22.64
A


ATOM
734
C
TYR
A
161
85.594
9.495
11.815
1.00
17.86
A


ATOM
735
O
TYR
A
161
86.269
8.527
11.459
1.00
19.30
A


ATOM
736
N
ALA
A
162
85.854
10.736
11.418
1.00
18.22
A


ATOM
737
CA
ALA
A
162
86.990
11.040
10.546
1.00
19.59
A


ATOM
738
CB
ALA
A
162
86.569
12.063
9.466
1.00
19.99
A


ATOM
739
C
ALA
A
162
88.051
11.629
11.472
1.00
19.11
A


ATOM
740
O
ALA
A
162
88.050
12.828
11.736
1.00
18.81
A


ATOM
741
N
ALA
A
163
88.952
10.775
11.956
1.00
18.78
A


ATOM
742
CA
ALA
A
163
89.994
11.165
12.918
1.00
18.84
A


ATOM
743
CB
ALA
A
163
90.867
9.924
13.279
1.00
19.04
A


ATOM
744
C
ALA
A
163
90.908
12.357
12.604
1.00
18.22
A


ATOM
745
O
ALA
A
163
91.290
13.101
13.508
1.00
16.79
A


ATOM
746
N
ASN
A
164
91.251
12.560
11.340
1.00
17.46
A


ATOM
747
CA
ASN
A
164
92.148
13.645
11.023
1.00
17.79
A


ATOM
748
CB
ASN
A
164
92.990
13.270
9.803
1.00
20.45
A


ATOM
749
CG
ASN
A
164
93.919
12.092
10.097
1.00
21.08
A


ATOM
750
OD1
ASN
A
164
94.663
12.117
11.066
1.00
21.57
A


ATOM
751
ND2
ASN
A
164
93.862
11.059
9.271
1.00
24.54
A


ATOM
752
C
ASN
A
164
91.555
15.044
10.889
1.00
18.34
A


ATOM
753
O
ASN
A
164
92.293
16.005
10.634
1.00
19.83
A


ATOM
754
N
GLY
A
165
90.247
15.176
11.083
1.00
15.01
A


ATOM
755
CA
GLY
A
165
89.644
16.490
11.022
1.00
15.54
A


ATOM
756
C
GLY
A
165
89.580
17.212
9.683
1.00
17.67
A


ATOM
757
O
GLY
A
165
89.607
16.600
8.613
1.00
19.49
A


ATOM
758
N
GLU
A
166
89.510
18.534
9.753
1.00
17.46
A


ATOM
759
CA
GLU
A
166
89.378
19.379
8.577
1.00
19.26
A


ATOM
760
CB
GLU
A
166
89.064
20.805
9.019
1.00
21.87
A


ATOM
761
CG
GLU
A
166
88.057
20.917
10.149
1.00
24.70
A


ATOM
762
CD
GLU
A
166
87.723
22.359
10.477
1.00
26.05
A


ATOM
763
OE1
GLU
A
166
88.469
23.251
10.001
1.00
25.93
A


ATOM
764
OE2
GLU
A
166
86.726
22.598
11.213
1.00
25.24
A


ATOM
765
C
GLU
A
166
90.538
19.441
7.592
1.00
20.11
A


ATOM
766
O
GLU
A
166
91.707
19.501
7.978
1.00
22.88
A


ATOM
767
N
LEU
A
167
90.195
19.443
6.312
1.00
18.72
A


ATOM
768
CA
LEU
A
167
91.173
19.565
5.242
1.00
17.38
A


ATOM
769
CB
LEU
A
167
90.463
19.516
3.888
1.00
15.71
A


ATOM
770
CG
LEU
A
167
91.238
19.817
2.601
1.00
15.42
A


ATOM
771
CD1
LEU
A
167
92.242
18.704
2.343
1.00
14.98
A


ATOM
772
CD2
LEU
A
167
90.265
19.947
1.416
1.00
12.32
A


ATOM
773
C
LEU
A
167
91.817
20.940
5.438
1.00
19.75
A


ATOM
774
O
LEU
A
167
93.030
21.103
5.266
1.00
19.61
A


ATOM
775
N
LEU
A
168
91.001
21.928
5.812
1.00
20.53
A


ATOM
776
CA
LEU
A
168
91.516
23.277
6.033
1.00
22.20
A


ATOM
777
CB
LEU
A
168
90.436
24.192
6.637
1.00
20.41
A


ATOM
778
CG
LEU
A
168
90.923
25.611
7.024
1.00
21.71
A


ATOM
779
CD1
LEU
A
168
91.275
26.413
5.768
1.00
20.09
A


ATOM
780
CD2
LEU
A
168
89.837
26.341
7.797
1.00
20.84
A


ATOM
781
C
LEU
A
168
92.731
23.245
6.968
1.00
23.07
A


ATOM
782
O
LEU
A
168
93.636
24.054
6.838
1.00
22.18
A


ATOM
783
N
LYS
A
169
92.742
22.305
7.905
1.00
24.67
A


ATOM
784
CA
LYS
A
169
93.844
22.192
8.850
1.00
28.56
A


ATOM
785
CB
LYS
A
169
93.561
21.076
9.858
1.00
31.12
A


ATOM
786
CG
LYS
A
169
94.615
20.933
10.938
1.00
35.60
A


ATOM
787
CD
LYS
A
169
94.436
19.652
11.765
1.00
39.37
A


ATOM
788
CE
LYS
A
169
94.832
18.410
10.961
1.00
42.26
A


ATOM
789
NZ
LYS
A
169
94.664
17.131
11.725
1.00
42.83
A


ATOM
790
C
LYS
A
169
95.151
21.902
8.119
1.00
29.24
A


ATOM
791
O
LYS
A
169
96.190
22.505
8.398
1.00
30.32
A


ATOM
792
N
TYR
A
170
95.101
20.970
7.179
1.00
29.12
A


ATOM
793
CA
TYR
A
170
96.290
20.619
6.423
1.00
28.18
A


ATOM
794
CB
TYR
A
170
96.037
19.344
5.637
1.00
25.30
A


ATOM
795
CG
TYR
A
170
95.926
18.182
6.569
1.00
27.01
A


ATOM
796
CD1
TYR
A
170
97.072
17.533
7.053
1.00
26.92
A


ATOM
797
CE1
TYR
A
170
96.974
16.532
8.008
1.00
25.37
A


ATOM
798
CD2
TYR
A
170
94.688
17.792
7.062
1.00
25.14
A


ATOM
799
CE2
TYR
A
170
94.580
16.807
8.009
1.00
26.49
A


ATOM
800
CZ
TYR
A
170
95.720
16.179
8.484
1.00
26.98
A


ATOM
801
OH
TYR
A
170
95.580
15.223
9.456
1.00
27.66
A


ATOM
802
C
TYR
A
170
96.690
21.742
5.507
1.00
28.69
A


ATOM
803
O
TYR
A
170
97.875
21.971
5.285
1.00
30.98
A


ATOM
804
N
ILE
A
171
95.705
22.452
4.976
1.00
28.95
A


ATOM
805
CA
ILE
A
171
96.006
23.550
4.088
1.00
29.79
A


ATOM
806
CB
ILE
A
171
94.721
24.233
3.579
1.00
29.29
A


ATOM
807
CG2
ILE
A
171
95.082
25.439
2.714
1.00
28.21
A


ATOM
808
CG1
ILE
A
171
93.906
23.227
2.747
1.00
29.66
A


ATOM
809
CD1
ILE
A
171
92.567
23.754
2.224
1.00
29.13
A


ATOM
810
C
ILE
A
171
96.897
24.536
4.833
1.00
31.13
A


ATOM
811
O
ILE
A
171
97.925
24.956
4.300
1.00
30.93
A


ATOM
812
N
ARG
A
172
96.525
24.862
6.075
1.00
32.00
A


ATOM
813
CA
ARG
A
172
97.294
25.789
6.903
1.00
32.60
A


ATOM
814
CB
ARG
A
172
96.527
26.175
8.163
1.00
32.77
A


ATOM
815
CG
ARG
A
172
95.257
26.982
7.972
1.00
38.24
A


ATOM
816
CD
ARG
A
172
94.853
27.602
9.335
1.00
43.47
A


ATOM
817
NE
ARG
A
172
93.501
28.181
9.412
1.00
46.65
A


ATOM
818
CZ
ARG
A
172
92.903
28.888
8.448
1.00
47.62
A


ATOM
819
NH1
ARG
A
172
93.517
29.115
7.287
1.00
47.16
A


ATOM
820
NH2
ARG
A
172
91.691
29.398
8.659
1.00
45.61
A


ATOM
821
C
ARG
A
172
98.646
25.219
7.338
1.00
32.95
A


ATOM
822
O
ARG
A
172
99.644
25.920
7.311
1.00
34.27
A


ATOM
823
N
ALA
A
173
98.674
23.960
7.761
1.00
32.74
A


ATOM
824
CA
ALA
A
173
99.912
23.341
8.209
1.00
32.81
A


ATOM
825
CB
ALA
A
173
99.668
21.896
8.619
1.00
32.72
A


ATOM
826
C
ALA
A
173
101.005
23.400
7.152
1.00
33.67
A


ATOM
827
O
ALA
A
173
102.125
23.817
7.438
1.00
33.78
A


ATOM
828
N
ILE
A
174
100.698
22.995
5.926
1.00
33.50
A


ATOM
829
CA
ILE
A
174
101.728
23.030
4.896
1.00
33.22
A


ATOM
830
CB
ILE
A
174
101.731
21.736
4.043
1.00
33.98
A


ATOM
831
CG2
ILE
A
174
101.725
20.502
4.950
1.00
32.94
A


ATOM
832
CG1
ILE
A
174
100.517
21.709
3.125
1.00
33.93
A


ATOM
833
CD1
ILE
A
174
100.602
20.631
2.080
1.00
36.79
A


ATOM
834
C
ILE
A
174
101.638
24.231
3.957
1.00
32.69
A


ATOM
835
O
ILE
A
174
102.326
24.269
2.938
1.00
33.88
A


ATOM
836
N
GLY
A
175
100.792
25.204
4.287
1.00
31.76
A


ATOM
837
CA
GLY
A
175
100.671
26.386
3.446
1.00
32.03
A


ATOM
838
C
GLY
A
175
99.838
26.223
2.184
1.00
32.77
A


ATOM
839
O
GLY
A
175
98.870
26.958
1.976
1.00
35.12
A


ATOM
840
N
SER
A
176
100.225
25.291
1.322
1.00
31.63
A


ATOM
841
CA
SER
A
176
99.489
25.018
0.091
1.00
31.11
A


ATOM
842
CB
SER
A
176
99.810
26.040
−0.996
1.00
31.54
A


ATOM
843
OG
SER
A
176
101.141
25.874
−1.464
1.00
33.96
A


ATOM
844
C
SER
A
176
99.946
23.640
−0.354
1.00
30.72
A


ATOM
845
O
SER
A
176
100.977
23.154
0.111
1.00
31.29
A


ATOM
846
N
PHE
A
177
99.180
23.018
−1.246
1.00
28.27
A


ATOM
847
CA
PHE
A
177
99.475
21.683
−1.738
1.00
26.97
A


ATOM
848
CB
PHE
A
177
98.169
20.948
−2.060
1.00
27.18
A


ATOM
849
CG
PHE
A
177
97.376
20.530
−0.854
1.00
27.90
A


ATOM
850
CD1
PHE
A
177
97.551
21.155
0.379
1.00
26.91
A


ATOM
851
CD2
PHE
A
177
96.432
19.503
−0.957
1.00
27.62
A


ATOM
852
CE1
PHE
A
177
96.812
20.762
1.477
1.00
26.03
A


ATOM
853
CE2
PHE
A
177
95.684
19.106
0.144
1.00
23.95
A


ATOM
854
CZ
PHE
A
177
95.873
19.730
1.357
1.00
25.81
A


ATOM
855
C
PHE
A
177
100.299
21.726
−3.008
1.00
26.99
A


ATOM
856
O
PHE
A
177
100.115
22.618
−3.832
1.00
27.45
A


ATOM
857
N
ASP
A
178
101.200
20.762
−3.179
1.00
26.09
A


ATOM
858
CA
ASP
A
178
101.967
20.704
−4.411
1.00
26.09
A


ATOM
859
CB
ASP
A
178
103.135
19.730
−4.303
1.00
27.73
A


ATOM
860
CG
ASP
A
178
102.689
18.318
−4.023
1.00
33.79
A


ATOM
861
OD1
ASP
A
178
101.601
17.919
−4.510
1.00
37.57
A


ATOM
862
OD2
ASP
A
178
103.431
17.590
−3.324
1.00
35.89
A


ATOM
863
C
ASP
A
178
100.955
20.202
−5.443
1.00
25.72
A


ATOM
864
O
ASP
A
178
99.763
20.063
−5.128
1.00
24.80
A


ATOM
865
N
GLU
A
179
101.419
19.897
−6.650
1.00
24.80
A


ATOM
866
CA
GLU
A
179
100.514
19.444
−7.697
1.00
25.67
A


ATOM
867
CB
GLU
A
179
101.187
19.554
−9.052
1.00
27.44
A


ATOM
868
CG
GLU
A
179
100.197
19.921
−10.129
1.00
31.17
A


ATOM
869
CD
GLU
A
179
100.823
19.999
−11.492
1.00
35.24
A


ATOM
870
OE1
GLU
A
179
102.016
20.372
−11.572
1.00
35.82
A


ATOM
871
OE2
GLU
A
179
100.116
19.707
−12.488
1.00
38.12
A


ATOM
872
C
GLU
A
179
99.917
18.041
−7.560
1.00
24.90
A


ATOM
873
O
GLU
A
179
98.755
17.822
−7.894
1.00
23.01
A


ATOM
874
N
THR
A
180
100.709
17.095
−7.082
1.00
24.57
A


ATOM
875
CA
THR
A
180
100.240
15.723
−6.923
1.00
25.53
A


ATOM
876
CB
THR
A
180
101.395
14.803
−6.478
1.00
24.65
A


ATOM
877
OG1
THR
A
180
102.525
15.069
−7.304
1.00
25.84
A


ATOM
878
CG2
THR
A
180
101.021
13.334
−6.624
1.00
23.39
A


ATOM
879
C
THR
A
180
99.110
15.623
−5.902
1.00
25.85
A


ATOM
880
O
THR
A
180
98.149
14.892
−6.111
1.00
25.59
A


ATOM
881
N
CYS
A
181
99.237
16.359
−4.799
1.00
25.83
A


ATOM
882
CA
CYS
A
181
98.217
16.355
−3.752
1.00
26.26
A


ATOM
883
CB
CYS
A
181
98.778
16.939
−2.451
1.00
27.81
A


ATOM
884
SG
CYS
A
181
100.202
16.031
−1.775
1.00
32.72
A


ATOM
885
C
CYS
A
181
96.963
17.127
−4.169
1.00
25.20
A


ATOM
886
O
CYS
A
181
95.853
16.696
−3.878
1.00
26.19
A


ATOM
887
N
THR
A
182
97.139
18.262
−4.841
1.00
22.74
A


ATOM
888
CA
THR
A
182
96.002
19.046
−5.305
1.00
21.82
A


ATOM
889
CB
THR
A
182
96.453
20.308
−6.103
1.00
21.81
A


ATOM
890
OG1
THR
A
182
97.258
21.161
−5.276
1.00
24.55
A


ATOM
891
CG2
THR
A
182
95.252
21.080
−6.593
1.00
18.62
A


ATOM
892
C
THR
A
182
95.197
18.141
−6.249
1.00
23.45
A


ATOM
893
O
THR
A
182
93.975
17.997
−6.116
1.00
22.94
A


ATOM
894
N
ARG
A
183
95.897
17.528
−7.202
1.00
22.71
A


ATOM
895
CA
ARG
A
183
95.260
16.648
−8.158
1.00
23.26
A


ATOM
896
CB
ARG
A
183
96.285
16.118
−9.171
1.00
22.46
A


ATOM
897
CG
ARG
A
183
95.692
15.140
−10.184
1.00
24.96
A


ATOM
898
CD
ARG
A
183
96.762
14.512
−11.078
1.00
27.09
A


ATOM
899
NE
ARG
A
183
97.372
15.577
−11.849
1.00
33.02
A


ATOM
900
CZ
ARG
A
183
98.637
15.948
−11.732
1.00
33.62
A


ATOM
901
NH1
ARG
A
183
99.440
15.312
−10.885
1.00
32.57
A


ATOM
902
NH2
ARG
A
183
99.069
17.006
−12.404
1.00
33.25
A


ATOM
903
C
ARG
A
183
94.559
15.475
−7.459
1.00
22.42
A


ATOM
904
O
ARG
A
183
93.393
15.193
−7.721
1.00
21.37
A


ATOM
905
N
PHE
A
184
95.255
14.800
−6.562
1.00
21.19
A


ATOM
906
CA
PHE
A
184
94.630
13.673
−5.888
1.00
22.20
A


ATOM
907
CB
PHE
A
184
95.615
12.964
−4.966
1.00
23.58
A


ATOM
908
CG
PHE
A
184
95.029
11.766
−4.283
1.00
25.43
A


ATOM
909
CD1
PHE
A
184
94.916
10.556
−4.954
1.00
25.01
A


ATOM
910
CD2
PHE
A
184
94.508
11.867
−2.998
1.00
24.35
A


ATOM
911
CE1
PHE
A
184
94.285
9.460
−4.356
1.00
23.50
A


ATOM
912
CE2
PHE
A
184
93.881
10.782
−2.409
1.00
24.71
A


ATOM
913
CZ
PHE
A
184
93.771
9.577
−3.094
1.00
22.95
A


ATOM
914
C
PHE
A
184
93.405
14.074
−5.072
1.00
21.96
A


ATOM
915
O
PHE
A
184
92.348
13.450
−5.170
1.00
21.31
A


ATOM
916
N
TYR
A
185
93.544
15.116
−4.267
1.00
21.18
A


ATOM
917
CA
TYR
A
185
92.433
15.543
−3.445
1.00
20.50
A


ATOM
918
CB
TYR
A
185
92.956
16.425
−2.313
1.00
21.33
A


ATOM
919
CG
TYR
A
185
93.494
15.550
−1.190
1.00
22.24
A


ATOM
920
CD1
TYR
A
185
92.641
14.670
−0.507
1.00
21.55
A


ATOM
921
CE1
TYR
A
185
93.127
13.755
0.414
1.00
20.71
A


ATOM
922
CD2
TYR
A
185
94.853
15.497
−0.904
1.00
21.37
A


ATOM
923
CE2
TYR
A
185
95.353
14.579
0.019
1.00
21.80
A


ATOM
924
CZ
TYR
A
185
94.486
13.705
0.670
1.00
21.18
A


ATOM
925
OH
TYR
A
185
94.986
12.746
1.519
1.00
19.84
A


ATOM
926
C
TYR
A
185
91.273
16.182
−4.201
1.00
19.27
A


ATOM
927
O
TYR
A
185
90.112
16.056
−3.801
1.00
17.72
A


ATOM
928
N
THR
A
186
91.576
16.834
−5.314
1.00
17.25
A


ATOM
929
CA
THR
A
186
90.527
17.433
−6.110
1.00
15.61
A


ATOM
930
CB
THR
A
186
91.097
18.366
−7.188
1.00
15.69
A


ATOM
931
OG1
THR
A
186
91.710
19.508
−6.564
1.00
16.11
A


ATOM
932
CG2
THR
A
186
89.996
18.816
−8.135
1.00
12.68
A


ATOM
933
C
THR
A
186
89.756
16.302
−6.785
1.00
15.75
A


ATOM
934
O
THR
A
186
88.523
16.350
−6.899
1.00
16.51
A


ATOM
935
N
ALA
A
187
90.478
15.277
−7.218
1.00
14.94
A


ATOM
936
CA
ALA
A
187
89.841
14.136
−7.868
1.00
16.15
A


ATOM
937
CB
ALA
A
187
90.905
13.130
−8.382
1.00
13.30
A


ATOM
938
C
ALA
A
187
88.847
13.450
−6.911
1.00
16.71
A


ATOM
939
O
ALA
A
187
87.743
13.075
−7.328
1.00
16.50
A


ATOM
940
N
GLU
A
188
89.213
13.308
−5.635
1.00
17.10
A


ATOM
941
CA
GLU
A
188
88.302
12.673
−4.679
1.00
17.85
A


ATOM
942
CB
GLU
A
188
88.953
12.514
−3.302
1.00
18.83
A


ATOM
943
CG
GLU
A
188
90.219
11.665
−3.296
1.00
19.46
A


ATOM
944
CD
GLU
A
188
90.370
10.795
−2.050
1.00
20.84
A


ATOM
945
OE1
GLU
A
188
90.131
11.276
−0.920
1.00
21.14
A


ATOM
946
OE2
GLU
A
188
90.749
9.616
−2.207
1.00
23.35
A


ATOM
947
C
GLU
A
188
87.043
13.516
−4.551
1.00
17.79
A


ATOM
948
O
GLU
A
188
85.921
13.005
−4.579
1.00
18.83
A


ATOM
949
N
ILE
A
189
87.220
14.824
−4.449
1.00
17.09
A


ATOM
950
CA
ILE
A
189
86.060
15.688
−4.312
1.00
15.61
A


ATOM
951
CB
ILE
A
189
86.495
17.141
−4.054
1.00
15.83
A


ATOM
952
CG2
ILE
A
189
85.278
18.019
−3.853
1.00
14.16
A


ATOM
953
CG1
ILE
A
189
87.380
17.199
−2.794
1.00
17.34
A


ATOM
954
CD1
ILE
A
189
87.949
18.583
−2.479
1.00
15.37
A


ATOM
955
C
ILE
A
189
85.176
15.611
−5.558
1.00
16.00
A


ATOM
956
O
ILE
A
189
83.953
15.530
−5.460
1.00
15.52
A


ATOM
957
N
VAL
A
190
85.794
15.619
−6.733
1.00
15.46
A


ATOM
958
CA
VAL
A
190
85.031
15.570
−7.964
1.00
15.38
A


ATOM
959
CB
VAL
A
190
85.975
15.641
−9.181
1.00
15.37
A


ATOM
960
CG1
VAL
A
190
85.273
15.168
−10.447
1.00
14.43
A


ATOM
961
CG2
VAL
A
190
86.454
17.056
−9.350
1.00
14.03
A


ATOM
962
C
VAL
A
190
84.228
14.279
−7.987
1.00
17.35
A


ATOM
963
O
VAL
A
190
83.016
14.281
−8.258
1.00
15.96
A


ATOM
964
N
SER
A
191
84.916
13.182
−7.683
1.00
17.90
A


ATOM
965
CA
SER
A
191
84.305
11.858
−7.660
1.00
17.77
A


ATOM
966
CB
SER
A
191
85.377
10.811
−7.344
1.00
18.25
A


ATOM
967
OG
SER
A
191
84.801
9.523
−7.243
1.00
21.13
A


ATOM
968
C
SER
A
191
83.147
11.778
−6.640
1.00
17.28
A


ATOM
969
O
SER
A
191
82.153
11.095
−6.865
1.00
15.44
A


ATOM
970
N
ALA
A
192
83.291
12.490
−5.525
1.00
17.27
A


ATOM
971
CA
ALA
A
192
82.267
12.529
−4.485
1.00
15.98
A


ATOM
972
CB
ALA
A
192
82.834
13.164
−3.191
1.00
14.89
A


ATOM
973
C
ALA
A
192
81.078
13.336
−4.988
1.00
16.44
A


ATOM
974
O
ALA
A
192
79.934
12.922
−4.816
1.00
17.59
A


ATOM
975
N
LEU
A
193
81.340
14.487
−5.609
1.00
16.63
A


ATOM
976
CA
LEU
A
193
80.253
15.303
−6.140
1.00
16.11
A


ATOM
977
CB
LEU
A
193
80.769
16.632
−6.688
1.00
16.40
A


ATOM
978
CG
LEU
A
193
81.421
17.545
−5.645
1.00
18.83
A


ATOM
979
CD1
LEU
A
193
81.779
18.885
−6.276
1.00
18.24
A


ATOM
980
CD2
LEU
A
193
80.455
17.751
−4.479
1.00
18.63
A


ATOM
981
C
LEU
A
193
79.509
14.551
−7.236
1.00
16.95
A


ATOM
982
O
LEU
A
193
78.286
14.623
−7.325
1.00
18.76
A


ATOM
983
N
GLU
A
194
80.229
13.825
−8.079
1.00
17.87
A


ATOM
984
CA
GLU
A
194
79.539
13.082
−9.124
1.00
19.66
A


ATOM
985
CB
GLU
A
194
80.525
12.295
−9.990
1.00
21.82
A


ATOM
986
CG
GLU
A
194
79.844
11.333
−10.947
1.00
21.12
A


ATOM
987
CD
GLU
A
194
80.831
10.513
−11.758
1.00
25.70
A


ATOM
988
OE1
GLU
A
194
81.900
10.122
−11.216
1.00
27.41
A


ATOM
989
OE2
GLU
A
194
80.527
10.244
−12.939
1.00
26.12
A


ATOM
990
C
GLU
A
194
78.546
12.123
−8.479
1.00
19.58
A


ATOM
991
O
GLU
A
194
77.420
11.987
−8.937
1.00
17.78
A


ATOM
992
N
TYR
A
195
78.962
11.462
−7.406
1.00
19.09
A


ATOM
993
CA
TYR
A
195
78.063
10.545
−6.736
1.00
19.86
A


ATOM
994
CB
TYR
A
195
78.807
9.740
−5.673
1.00
20.01
A


ATOM
995
CG
TYR
A
195
77.871
8.975
−4.756
1.00
20.45
A


ATOM
996
CD1
TYR
A
195
77.329
7.748
−5.142
1.00
19.40
A


ATOM
997
CE1
TYR
A
195
76.471
7.044
−4.296
1.00
18.43
A


ATOM
998
CD2
TYR
A
195
77.527
9.48
−3.500
1.00
20.11
A


ATOM
999
CE2
TYR
A
195
76.678
8.79
−2.652
1.00
19.96
A


ATOM
1000
CZ
TYR
A
195
76.154
7.567
−3.057
1.00
21.07
A


ATOM
1001
OH
TYR
A
195
75.336
6.859
−2.206
1.00
21.31
A


ATOM
1002
C
TYR
A
195
76.914
11.295
−6.060
1.00
20.00
A


ATOM
1003
O
TYR
A
195
75.775
10.823
−6.033
1.00
21.42
A


ATOM
1004
N
LEU
A
196
77.222
12.455
−5.500
1.00
17.38
A


ATOM
1005
CA
LEU
A
196
76.209
13.226
−4.795
1.00
18.74
A


ATOM
1006
CB
LEU
A
196
76.846
14.412
−4.049
1.00
17.38
A


ATOM
1007
CG
LEU
A
196
75.850
15.100
−3.110
1.00
19.04
A


ATOM
1008
CD1
LEU
A
196
75.423
14.093
−2.061
1.00
17.66
A


ATOM
1009
CD2
LEU
A
196
76.462
16.338
−2.453
1.00
19.54
A


ATOM
1010
C
LEU
A
196
75.148
13.747
−5.751
1.00
18.47
A


ATOM
1011
O
LEU
A
196
73.944
13.608
−5.523
1.00
15.05
A


ATOM
1012
N
HIS
A
197
75.622
14.361
−6.824
1.00
18.35
A


ATOM
1013
CA
HIS
A
197
74.740
14.915
−7.812
1.00
20.04
A


ATOM
1014
CB
HIS
A
197
75.562
15.809
−8.718
1.00
20.29
A


ATOM
1015
CG
HIS
A
197
76.048
17.044
−8.025
1.00
21.90
A


ATOM
1016
CD2
HIS
A
197
75.766
17.539
−6.794
1.00
19.49
A


ATOM
1017
ND1
HIS
A
197
76.892
17.956
−8.621
1.00
20.69
A


ATOM
1018
CE1
HIS
A
197
77.104
18.960
−7.789
1.00
20.86
A


ATOM
1019
NE2
HIS
A
197
76.433
18.732
−6.676
1.00
19.12
A


ATOM
1020
C
HIS
A
197
73.950
13.858
−8.587
1.00
21.27
A


ATOM
1021
O
HIS
A
197
72.865
14.133
−9.099
1.00
21.23
A


ATOM
1022
N
GLY
A
198
74.487
12.644
−8.644
1.00
21.36
A


ATOM
1023
CA
GLY
A
198
73.810
11.569
−9.339
1.00
20.60
A


ATOM
1024
C
GLY
A
198
72.528
11.203
−8.632
1.00
22.72
A


ATOM
1025
O
GLY
A
198
71.593
10.742
−9.269
1.00
22.75
A


ATOM
1026
N
LYS
A
199
72.478
11.411
−7.313
1.00
24.27
A


ATOM
1027
CA
LYS
A
199
71.280
11.105
−6.523
1.00
22.95
A


ATOM
1028
CB
LYS
A
199
71.659
10.629
−5.123
1.00
24.67
A


ATOM
1029
CG
LYS
A
199
72.570
9.429
−5.109
1.00
29.22
A


ATOM
1030
CD
LYS
A
199
72.986
9.064
−3.701
1.00
33.11
A


ATOM
1031
CE
LYS
A
199
72.531
7.660
−3.366
1.00
37.28
A


ATOM
1032
NZ
LYS
A
199
72.917
6.686
−4.455
1.00
38.82
A


ATOM
1033
C
LYS
A
199
70.432
12.354
−6.398
1.00
22.39
A


ATOM
1034
O
LYS
A
199
69.558
12.431
−5.542
1.00
22.53
A


ATOM
1035
N
GLY
A
200
70.710
13.343
−7.241
1.00
21.56
A


ATOM
1036
CA
GLY
A
200
69.953
14.580
−7.203
1.00
22.28
A


ATOM
1037
C
GLY
A
200
70.006
15.326
−5.882
1.00
23.53
A


ATOM
1038
O
GLY
A
200
69.017
15.930
−5.461
1.00
24.83
A


ATOM
1039
N
ILE
A
201
71.161
15.302
−5.225
1.00
22.74
A


ATOM
1040
CA
ILE
A
201
71.314
15.985
−3.951
1.00
22.95
A


ATOM
1041
CB
ILE
A
201
71.796
15.007
−2.842
1.00
22.51
A


ATOM
1042
CG2
ILE
A
201
71.995
15.757
−1.536
1.00
21.73
A


ATOM
1043
CG1
ILE
A
201
70.788
13.876
−2.638
1.00
22.48
A


ATOM
1044
CD1
ILE
A
201
71.274
12.791
−1.687
1.00
17.26
A


ATOM
1045
C
ILE
A
201
72.361
17.086
−4.076
1.00
24.41
A


ATOM
1046
O
ILE
A
201
73.387
16.904
−4.737
1.00
26.41
A


ATOM
1047
N
ILE
A
202
72.118
18.236
−3.470
1.00
23.00
A


ATOM
1048
CA
ILE
A
202
73.137
19.267
−3.520
1.00
24.60
A


ATOM
1049
CB
ILE
A
202
72.729
20.440
−4.420
1.00
26.37
A


ATOM
1050
CG2
ILE
A
202
72.503
19.934
−5.829
1.00
28.52
A


ATOM
1051
CG1
ILE
A
202
71.450
21.086
−3.922
1.00
29.04
A


ATOM
1052
CD1
ILE
A
202
70.958
22.165
−4.845
1.00
32.55
A


ATOM
1053
C
ILE
A
202
73.482
19.732
−2.105
1.00
24.36
A


ATOM
1054
O
ILE
A
202
72.605
19.919
−1.257
1.00
25.89
A


ATOM
1055
N
HIS
A
203
74.776
19.882
−1.856
1.00
22.94
A


ATOM
1056
CA
HIS
A
203
75.289
20.273
−0.555
1.00
22.27
A


ATOM
1057
CB
HIS
A
203
76.800
20.010
−0.526
1.00
20.00
A


ATOM
1058
CG
HIS
A
203
77.401
20.051
0.840
1.00
18.45
A


ATOM
1059
CD2
HIS
A
203
77.865
19.060
1.640
1.00
19.77
A


ATOM
1060
ND1
HIS
A
203
77.569
21.222
1.542
1.00
16.33
A


ATOM
1061
CE1
HIS
A
203
78.115
20.953
2.715
1.00
17.77
A


ATOM
1062
NE2
HIS
A
203
78.306
19.650
2.800
1.00
18.48
A


ATOM
1063
C
HIS
A
203
74.978
21.731
−0.206
1.00
23.37
A


ATOM
1064
O
HIS
A
203
74.411
22.009
0.860
1.00
22.52
A


ATOM
1065
N
ARG
A
204
75.361
22.648
−1.101
1.00
23.22
A


ATOM
1066
CA
ARG
A
204
75.126
24.087
−0.934
1.00
23.42
A


ATOM
1067
CB
ARG
A
204
73.674
24.375
−0.544
1.00
22.74
A


ATOM
1068
CG
ARG
A
204
72.663
23.966
−1.561
1.00
24.57
A


ATOM
1069
CD
ARG
A
204
71.341
24.681
−1.325
1.00
26.51
A


ATOM
1070
NE
ARG
A
204
70.699
24.299
−0.074
1.00
28.25
A


ATOM
1071
CZ
ARG
A
204
69.596
24.871
0.405
1.00
28.63
A


ATOM
1072
NH1
ARG
A
204
69.013
25.849
−0.267
1.00
28.47
A


ATOM
1073
NH2
ARG
A
204
69.086
24.472
1.563
1.00
28.55
A


ATOM
1074
C
ARG
A
204
76.017
24.819
0.061
1.00
24.12
A


ATOM
1075
O
ARG
A
204
75.805
26.001
0.308
1.00
26.26
A


ATOM
1076
N
ASP
A
205
76.990
24.135
0.654
1.00
23.05
A


ATOM
1077
CA
ASP
A
205
77.887
24.789
1.595
1.00
20.96
A


ATOM
1078
CB
ASP
A
205
77.219
24.883
2.964
1.00
22.31
A


ATOM
1079
CG
ASP
A
205
77.964
25.801
3.914
1.00
26.08
A


ATOM
1080
OD1
ASP
A
205
78.812
26.582
3.439
1.00
25.93
A


ATOM
1081
OD2
ASP
A
205
77.707
25.751
5.141
1.00
29.89
A


ATOM
1082
C
ASP
A
205
79.210
24.020
1.662
1.00
20.46
A


ATOM
1083
O
ASP
A
205
79.812
23.833
2.716
1.00
21.36
A


ATOM
1084
N
LEU
A
206
79.666
23.584
0.504
1.00
18.98
A


ATOM
1085
CA
LEU
A
206
80.893
22.827
0.407
1.00
19.83
A


ATOM
1086
CB
LEU
A
206
80.983
22.229
−0.994
1.00
21.73
A


ATOM
1087
CG
LEU
A
206
82.039
21.167
−1.298
1.00
24.76
A


ATOM
1088
CD1
LEU
A
206
81.818
19.943
−0.401
1.00
24.95
A


ATOM
1089
CD2
LEU
A
206
81.941
20.789
−2.778
1.00
23.74
A


ATOM
1090
C
LEU
A
206
82.093
23.725
0.691
1.00
20.17
A


ATOM
1091
O
LEU
A
206
82.162
24.857
0.200
1.00
20.92
A


ATOM
1092
N
LYS
A
207
83.044
23.226
1.475
1.00
19.79
A


ATOM
1093
CA
LYS
A
207
84.233
24.004
1.821
1.00
19.45
A


ATOM
1094
CB
LYS
A
207
83.825
25.209
2.667
1.00
17.84
A


ATOM
1095
CG
LYS
A
207
83.123
24.820
3.933
1.00
19.19
A


ATOM
1096
CD
LYS
A
207
82.331
25.969
4.500
1.00
20.50
A


ATOM
1097
CE
LYS
A
207
81.663
25.556
5.797
1.00
22.10
A


ATOM
1098
NZ
LYS
A
207
80.955
26.674
6.480
1.00
22.34
A


ATOM
1099
C
LYS
A
207
85.241
23.130
2.565
1.00
19.59
A


ATOM
1100
O
LYS
A
207
84.917
22.025
2.985
1.00
20.21
A


ATOM
1101
N
PRO
A
208
86.480
23.618
2.737
1.00
19.79
A


ATOM
1102
CD
PRO
A
208
87.032
24.869
2.188
1.00
18.04
A


ATOM
1103
CA
PRO
A
208
87.526
22.853
3.428
1.00
19.22
A


ATOM
1104
CB
PRO
A
208
88.756
23.763
3.297
1.00
19.27
A


ATOM
1105
CG
PRO
A
208
88.496
24.521
2.027
1.00
16.27
A


ATOM
1106
C
PRO
A
208
87.221
22.477
4.883
1.00
20.50
A


ATOM
1107
O
PRO
A
208
87.791
21.511
5.411
1.00
21.44
A


ATOM
1108
N
GLU
A
209
86.335
23.231
5.530
1.00
20.19
A


ATOM
1109
CA
GLU
A
209
85.956
22.976
6.927
1.00
21.25
A


ATOM
1110
CB
GLU
A
209
85.383
24.251
7.562
1.00
21.43
A


ATOM
1111
CG
GLU
A
209
86.330
25.446
7.535
1.00
26.33
A


ATOM
1112
CD
GLU
A
209
86.203
26.315
6.270
1.00
30.17
A


ATOM
1113
OE1
GLU
A
209
86.143
25.785
5.131
1.00
30.44
A


ATOM
1114
OE2
GLU
A
209
86.173
27.557
6.422
1.00
33.49
A


ATOM
1115
C
GLU
A
209
84.920
21.839
7.040
1.00
22.45
A


ATOM
1116
O
GLU
A
209
84.733
21.255
8.114
1.00
21.98
A


ATOM
1117
N
ASN
A
210
84.269
21.545
5.915
1.00
22.73
A


ATOM
1118
CA
ASN
A
210
83.234
20.514
5.788
1.00
23.66
A


ATOM
1119
CB
ASN
A
210
82.102
21.013
4.882
1.00
26.67
A


ATOM
1120
CG
ASN
A
210
81.104
21.881
5.613
1.00
33.39
A


ATOM
1121
OD1
ASN
A
210
80.223
22.481
4.988
1.00
36.52
A


ATOM
1122
ND2
ASN
A
210
81.221
21.950
6.946
1.00
34.23
A


ATOM
1123
C
ASN
A
210
83.775
19.239
5.162
1.00
21.41
A


ATOM
1124
O
ASN
A
210
83.067
18.244
5.081
1.00
21.16
A


ATOM
1125
N
ILE
A
211
85.006
19.293
4.674
1.00
19.42
A


ATOM
1126
CA
ILE
A
211
85.619
18.141
4.029
1.00
17.43
A


ATOM
1127
CB
ILE
A
211
86.319
18.556
2.708
1.00
14.89
A


ATOM
1128
CG2
ILE
A
211
87.046
17.349
2.096
1.00
12.68
A


ATOM
1129
CG1
ILE
A
211
85.277
19.157
1.736
1.00
13.30
A


ATOM
1130
CD1
ILE
A
211
85.855
19.805
0.435
1.00
10.47
A


ATOM
1131
C
ILE
A
211
86.620
17.578
5.024
1.00
17.83
A


ATOM
1132
O
ILE
A
211
87.685
18.151
5.241
1.00
17.76
A


ATOM
1133
N
LEU
A
212
86.265
16.457
5.639
1.00
16.05
A


ATOM
1134
CA
LEU
A
212
87.121
15.871
6.656
1.00
15.84
A


ATOM
1135
CB
LEU
A
212
86.256
15.319
7.793
1.00
14.28
A


ATOM
1136
CG
LEU
A
212
85.108
16.227
8.285
1.00
14.68
A


ATOM
1137
CD1
LEU
A
212
84.606
15.715
9.647
1.00
11.38
A


ATOM
1138
CD2
LEU
A
212
85.579
17.685
8.422
1.00
10.88
A


ATOM
1139
C
LEU
A
212
88.031
14.787
6.114
1.00
16.77
A


ATOM
1140
O
LEU
A
212
87.861
14.335
4.984
1.00
16.78
A


ATOM
1141
N
LEU
A
213
88.999
14.374
6.925
1.00
16.47
A


ATOM
1142
CA
LEU
A
213
89.924
13.332
6.516
1.00
17.64
A


ATOM
1143
CB
LEU
A
213
91.323
13.926
6.378
1.00
18.08
A


ATOM
1144
CG
LEU
A
213
91.367
14.880
5.176
1.00
17.92
A


ATOM
1145
CD1
LEU
A
213
92.076
16.134
5.529
1.00
18.78
A


ATOM
1146
CD2
LEU
A
213
92.042
14.187
4.000
1.00
17.07
A


ATOM
1147
C
LEU
A
213
89.919
12.147
7.473
1.00
18.68
A


ATOM
1148
O
LEU
A
213
90.091
12.297
8.672
1.00
18.75
A


ATOM
1149
N
ASN
A
214
89.712
10.955
6.939
1.00
21.19
A


ATOM
1150
CA
ASN
A
214
89.673
9.780
7.797
1.00
23.68
A


ATOM
1151
CB
ASN
A
214
88.864
8.657
7.122
1.00
25.68
A


ATOM
1152
CG
ASN
A
214
89.613
7.979
6.012
1.00
31.70
A


ATOM
1153
OD1
ASN
A
214
90.680
8.426
5.590
1.00
35.54
A


ATOM
1154
ND2
ASN
A
214
89.057
6.886
5.521
1.00
34.56
A


ATOM
1155
C
ASN
A
214
91.077
9.328
8.203
1.00
22.08
A


ATOM
1156
O
ASN
A
214
92.056
9.972
7.864
1.00
20.25
A


ATOM
1157
N
ALA
A
215
91.170
8.239
8.953
1.00
24.03
A


ATOM
1158
CA
ALA
A
215
92.464
7.738
9.420
1.00
24.26
A


ATOM
1159
CB
ALA
A
215
92.276
6.502
10.277
1.00
21.70
A


ATOM
1160
C
ALA
A
215
93.421
7.426
8.296
1.00
24.90
A


ATOM
1161
O
ALA
A
215
94.615
7.435
8.491
1.00
26.03
A


ATOM
1162
N
ASP
A
216
92.889
7.143
7.108
1.00
25.93
A


ATOM
1163
CA
ASP
A
216
93.726
6.826
5.963
1.00
26.29
A


ATOM
1164
CB
ASP
A
216
93.048
5.773
5.091
1.00
32.31
A


ATOM
1165
CG
ASP
A
216
92.862
4.456
5.812
1.00
38.06
A


ATOM
1166
OD1
ASP
A
216
93.780
4.043
6.559
1.00
40.03
A


ATOM
1167
OD2
ASP
A
216
91.800
3.823
5.616
1.00
42.79
A


ATOM
1168
C
ASP
A
216
94.046
8.026
5.095
1.00
23.69
A


ATOM
1169
O
ASP
A
216
94.717
7.899
4.085
1.00
24.38
A


ATOM
1170
N
MET
A
217
93.546
9.187
5.478
1.00
21.45
A


ATOM
1171
CA
MET
A
217
93.752
10.418
4.726
1.00
20.48
A


ATOM
1172
CB
MET
A
217
95.226
10.614
4.396
1.00
21.48
A


ATOM
1173
CG
MET
A
217
96.081
10.894
5.629
1.00
21.46
A


ATOM
1174
SD
MET
A
217
95.504
12.311
6.580
1.00
25.32
A


ATOM
1175
CE
MET
A
217
96.079
13.722
5.573
1.00
24.08
A


ATOM
1176
C
MET
A
217
92.900
10.556
3.458
1.00
19.63
A


ATOM
1177
O
MET
A
217
93.245
11.294
2.546
1.00
19.54
A


ATOM
1178
N
HIS
A
218
91.794
9.824
3.405
1.00
18.82
A


ATOM
1179
CA
HIS
A
218
90.843
9.945
2.311
1.00
18.81
A


ATOM
1180
CB
HIS
A
218
90.206
8.589
1.994
1.00
20.61
A


ATOM
1181
CG
HIS
A
218
91.097
7.666
1.218
1.00
22.68
A


ATOM
1182
CD2
HIS
A
218
91.840
6.605
1.614
1.00
20.37
A


ATOM
1183
ND1
HIS
A
218
91.316
7.806
−0.139
1.00
21.30
A


ATOM
1184
CE1
HIS
A
218
92.153
6.867
−0.541
1.00
20.75
A


ATOM
1185
NE2
HIS
A
218
92.485
6.128
0.501
1.00
20.31
A


ATOM
1186
C
HIS
A
218
89.774
10.925
2.863
1.00
18.97
A


ATOM
1187
O
HIS
A
218
89.534
10.965
4.083
1.00
16.48
A


ATOM
1188
N
ILE
A
219
89.166
11.721
1.978
1.00
17.41
A


ATOM
1189
CA
ILE
A
219
88.165
12.702
2.387
1.00
16.48
A


ATOM
1190
CB
ILE
A
219
87.765
13.695
1.242
1.00
13.43
A


ATOM
1191
CG2
ILE
A
219
88.984
14.404
0.698
1.00
10.66
A


ATOM
1192
CG1
ILE
A
219
86.973
12.952
0.156
1.00
11.14
A


ATOM
1193
CD1
ILE
A
219
86.505
13.807
−0.995
1.00
 4.26
A


ATOM
1194
C
ILE
A
219
86.875
12.067
2.864
1.00
17.14
A


ATOM
1195
O
ILE
A
219
86.541
10.943
2.497
1.00
18.77
A


ATOM
1196
N
GLN
A
220
86.159
12.808
3.696
1.00
17.24
A


ATOM
1197
CA
GLN
A
220
84.878
12.376
4.203
1.00
18.93
A


ATOM
1198
CB
GLN
A
220
85.002
11.756
5.604
1.00
22.02
A


ATOM
1199
CG
GLN
A
220
83.791
10.874
5.952
1.00
26.68
A


ATOM
1200
CD
GLN
A
220
83.949
10.071
7.253
1.00
31.76
A


ATOM
1201
OE1
GLN
A
220
83.437
10.471
8.331
1.00
27.57
A


ATOM
1202
NE2
GLN
A
220
84.667
8.930
7.161
1.00
29.97
A


ATOM
1203
C
GLN
A
220
84.077
13.652
4.261
1.00
17.44
A


ATOM
1204
O
GLN
A
220
84.247
14.465
5.170
1.00
17.81
A


ATOM
1205
N
ILE
A
221
83.229
13.852
3.263
1.00
15.69
A


ATOM
1206
CA
ILE
A
221
82.413
15.051
3.230
1.00
16.08
A


ATOM
1207
CB
ILE
A
221
81.939
15.359
1.802
1.00
15.82
A


ATOM
1208
CG2
ILE
A
221
80.956
16.519
1.834
1.00
13.95
A


ATOM
1209
CG1
ILE
A
221
83.163
15.627
0.899
1.00
16.66
A


ATOM
1210
CD1
ILE
A
221
82.837
16.045
−0.548
1.00
13.13
A


ATOM
1211
C
ILE
A
221
81.207
14.892
4.156
1.00
16.52
A


ATOM
1212
O
ILE
A
221
80.542
13.860
4.157
1.00
16.03
A


ATOM
1213
N
THR
A
222
80.927
15.922
4.948
1.00
17.66
A


ATOM
1214
CA
THR
A
222
79.810
15.862
5.882
1.00
17.70
A


ATOM
1215
CB
THR
A
222
80.331
15.433
7.277
1.00
18.71
A


ATOM
1216
OG1
THR
A
222
79.230
15.263
8.172
1.00
16.76
A


ATOM
1217
CG2
THR
A
222
81.319
16.470
7.825
1.00
16.79
A


ATOM
1218
C
THR
A
222
79.069
17.195
5.980
1.00
17.35
A


ATOM
1219
O
THR
A
222
79.246
18.062
5.130
1.00
16.83
A


ATOM
1220
N
ASP
A
223
78.244
17.344
7.018
1.00
18.09
A


ATOM
1221
CA
ASP
A
223
77.466
18.567
7.268
1.00
19.60
A


ATOM
1222
CB
ASP
A
223
78.403
19.778
7.311
1.00
22.73
A


ATOM
1223
CG
ASP
A
223
77.763
21.006
7.959
1.00
28.30
A


ATOM
1224
OD1
ASP
A
223
76.565
20.931
8.335
1.00
28.17
A


ATOM
1225
OD2
ASP
A
223
78.480
22.042
8.081
1.00
30.99
A


ATOM
1226
C
ASP
A
223
76.382
18.799
6.210
1.00
19.52
A


ATOM
1227
O
ASP
A
223
76.528
19.655
5.340
1.00
19.39
A


ATOM
1228
N
PHE
A
224
75.283
18.058
6.303
1.00
18.74
A


ATOM
1229
CA
PHE
A
224
74.213
18.168
5.321
1.00
18.81
A


ATOM
1230
CB
PHE
A
224
73.825
16.773
4.853
1.00
17.07
A


ATOM
1231
CG
PHE
A
224
74.857
16.150
3.971
1.00
17.01
A


ATOM
1232
CD1
PHE
A
224
74.751
16.250
2.578
1.00
16.10
A


ATOM
1233
CD2
PHE
A
224
75.982
15.543
4.521
1.00
14.00
A


ATOM
1234
CE1
PHE
A
224
75.761
15.752
1.747
1.00
15.92
A


ATOM
1235
CE2
PHE
A
224
77.001
15.042
3.699
1.00
15.63
A


ATOM
1236
CZ
PHE
A
224
76.889
15.147
2.309
1.00
15.79
A


ATOM
1237
C
PHE
A
224
72.997
18.932
5.775
1.00
19.88
A


ATOM
1238
O
PHE
A
224
71.961
18.922
5.115
1.00
19.36
A


ATOM
1239
N
GLY
A
225
73.135
19.599
6.911
1.00
21.38
A


ATOM
1240
CA
GLY
A
225
72.046
20.388
7.439
1.00
21.39
A


ATOM
1241
C
GLY
A
225
71.672
21.545
6.523
1.00
23.43
A


ATOM
1242
O
GLY
A
225
70.802
22.323
6.869
1.00
26.22
A


ATOM
1243
N
THR
A
226
72.311
21.692
5.370
1.00
22.15
A


ATOM
1244
CA
THR
A
226
71.930
22.784
4.492
1.00
23.85
A


ATOM
1245
CB
THR
A
226
72.986
23.946
4.465
1.00
24.65
A


ATOM
1246
OG1
THR
A
226
74.197
23.511
3.830
1.00
24.83
A


ATOM
1247
CG2
THR
A
226
73.285
24.420
5.866
1.00
23.67
A


ATOM
1248
C
THR
A
226
71.721
22.289
3.073
1.00
24.12
A


ATOM
1249
O
THR
A
226
71.646
23.079
2.129
1.00
22.82
A


ATOM
1250
N
ALA
A
227
71.620
20.976
2.935
1.00
23.84
A


ATOM
1251
CA
ALA
A
227
71.437
20.357
1.637
1.00
26.21
A


ATOM
1252
CB
ALA
A
227
71.774
18.889
1.734
1.00
24.04
A


ATOM
1253
C
ALA
A
227
70.026
20.535
1.064
1.00
28.20
A


ATOM
1254
O
ALA
A
227
69.069
20.767
1.801
1.00
29.29
A


ATOM
1255
N
ALA
A
228
69.912
20.449
−0.258
1.00
28.91
A


ATOM
1256
CA
ALA
A
228
68.623
20.554
−0.928
1.00
31.02
A


ATOM
1257
CB
ALA
A
228
68.577
21.795
−1.856
1.00
30.45
A


ATOM
1258
C
ALA
A
228
68.501
19.276
−1.745
1.00
32.01
A


ATOM
1259
O
ALA
A
228
69.474
18.846
−2.363
1.00
32.87
A


ATOM
1260
N
VAL
A
229
67.328
18.650
−1.732
1.00
32.95
A


ATOM
1261
CA
VAL
A
229
67.126
17.424
−2.503
1.00
34.26
A


ATOM
1262
CB
VAL
A
229
66.468
16.347
−1.657
1.00
33.02
A


ATOM
1263
CG1
VAL
A
229
66.194
15.114
−2.498
1.00
33.80
A


ATOM
1264
CG2
VAL
A
229
67.356
16.011
−0.496
1.00
31.38
A


ATOM
1265
C
VAL
A
229
66.213
17.757
−3.665
1.00
36.36
A


ATOM
1266
O
VAL
A
229
65.065
18.133
−3.455
1.00
38.02
A


ATOM
1267
N
LEU
A
230
66.715
17.628
−4.889
1.00
37.75
A


ATOM
1268
CA
LEU
A
230
65.917
17.965
−6.066
1.00
39.87
A


ATOM
1269
CB
LEU
A
230
66.741
17.775
−7.335
1.00
41.23
A


ATOM
1270
CG
LEU
A
230
68.039
18.585
−7.359
1.00
44.16
A


ATOM
1271
CD1
LEU
A
230
68.843
18.208
−8.599
1.00
43.48
A


ATOM
1272
CD2
LEU
A
230
67.724
20.087
−7.313
1.00
42.99
A


ATOM
1273
C
LEU
A
230
64.646
17.137
−6.162
1.00
40.59
A


ATOM
1274
O
LEU
A
230
64.703
15.954
−6.486
1.00
41.31
A


ATOM
1275
N
ASN
A
240
65.964
27.756
−2.248
1.00
83.97
A


ATOM
1276
CA
ASN
A
240
66.331
29.165
−2.370
1.00
84.48
A


ATOM
1277
CB
ASN
A
240
65.294
29.907
−3.225
1.00
85.56
A


ATOM
1278
CG
ASN
A
240
63.949
30.053
−2.524
1.00
86.59
A


ATOM
1279
OD1
ASN
A
240
63.850
30.682
−1.465
1.00
87.31
A


ATOM
1280
ND2
ASN
A
240
62.904
29.473
−3.115
1.00
86.14
A


ATOM
1281
C
ASN
A
240
66.433
29.828
−0.994
1.00
83.85
A


ATOM
1282
O
ASN
A
240
66.898
30.963
−0.862
1.00
84.11
A


ATOM
1283
N
ALA
A
241
65.997
29.096
0.023
1.00
83.19
A


ATOM
1284
CA
ALA
A
241
65.996
29.564
1.405
1.00
81.85
A


ATOM
1285
C
ALA
A
241
67.330
29.365
2.127
1.00
79.97
A


ATOM
1286
O
ALA
A
241
67.349
28.777
3.214
1.00
79.75
A


ATOM
1287
CB
ALA
A
241
64.894
28.825
2.183
1.00
85.17
A


ATOM
1288
N
PHE
A
242
68.433
29.850
1.551
1.00
77.03
A


ATOM
1289
CA
PHE
A
242
69.737
29.680
2.197
1.00
74.85
A


ATOM
1290
CB
PHE
A
242
69.973
28.183
2.438
1.00
73.81
A


ATOM
1291
CG
PHE
A
242
71.311
27.861
3.015
1.00
72.36
A


ATOM
1292
CD1
PHE
A
242
71.595
28.116
4.353
1.00
72.39
A


ATOM
1293
CD2
PHE
A
242
72.297
27.312
2.210
1.00
72.03
A


ATOM
1294
CE1
PHE
A
242
72.855
27.823
4.879
1.00
72.87
A


ATOM
1295
CE2
PHE
A
242
73.553
27.016
2.714
1.00
72.25
A


ATOM
1296
CZ
PHE
A
242
73.837
27.270
4.054
1.00
72.96
A


ATOM
1297
C
PHE
A
242
70.951
30.283
1.462
1.00
73.13
A


ATOM
1298
O
PHE
A
242
70.958
30.425
0.233
1.00
74.08
A


ATOM
1299
N
VAL
A
243
71.972
30.625
2.250
1.00
69.64
A


ATOM
1300
CA
VAL
A
243
73.233
31.204
1.777
1.00
65.87
A


ATOM
1301
CB
VAL
A
243
73.207
32.765
1.834
1.00
66.73
A


ATOM
1302
CG1
VAL
A
243
74.498
33.344
1.271
1.00
65.65
A


ATOM
1303
CG2
VAL
A
243
72.008
33.299
1.084
1.00
66.83
A


ATOM
1304
C
VAL
A
243
74.349
30.708
2.703
1.00
62.21
A


ATOM
1305
O
VAL
A
243
74.471
31.189
3.839
1.00
61.91
A


ATOM
1306
N
GLY
A
244
75.149
29.760
2.204
1.00
57.62
A


ATOM
1307
CA
GLY
A
244
76.247
29.177
2.967
1.00
51.60
A


ATOM
1308
C
GLY
A
244
77.341
30.132
3.387
1.00
46.47
A


ATOM
1309
O
GLY
A
244
77.063
31.261
3.757
1.00
48.62
A


ATOM
1310
N
THR
A
245
78.588
29.686
3.325
1.00
42.06
A


ATOM
1311
CA
THR
A
245
79.709
30.526
3.726
1.00
36.35
A


ATOM
1312
CB
THR
A
245
80.925
29.673
4.096
1.00
35.76
A


ATOM
1313
OG1
THR
A
245
80.539
28.740
5.105
1.00
31.66
A


ATOM
1314
CG2
THR
A
245
82.043
30.534
4.651
1.00
33.72
A


ATOM
1315
C
THR
A
245
80.064
31.524
2.637
1.00
34.43
A


ATOM
1316
O
THR
A
245
80.309
31.166
1.485
1.00
33.95
A


ATOM
1317
N
ALA
A
246
80.087
32.787
3.034
1.00
32.72
A


ATOM
1318
CA
ALA
A
246
80.338
33.900
2.142
1.00
30.18
A


ATOM
1319
CB
ALA
A
246
80.684
35.127
2.952
1.00
30.18
A


ATOM
1320
C
ALA
A
246
81.374
33.678
1.062
1.00
29.56
A


ATOM
1321
O
ALA
A
246
81.099
33.895
−0.113
1.00
30.00
A


ATOM
1322
N
GLN
A
247
82.564
33.242
1.445
1.00
28.03
A


ATOM
1323
CA
GLN
A
247
83.623
33.030
0.468
1.00
26.97
A


ATOM
1324
CB
GLN
A
247
84.929
32.706
1.182
1.00
28.32
A


ATOM
1325
CG
GLN
A
247
85.208
33.659
2.319
1.00
33.33
A


ATOM
1326
CD
GLN
A
247
86.600
33.522
2.863
1.00
36.16
A


ATOM
1327
OE1
GLN
A
247
87.556
34.107
2.335
1.00
36.68
A


ATOM
1328
NE2
GLN
A
247
86.738
32.731
3.922
1.00
39.27
A


ATOM
1329
C
GLN
A
247
83.355
31.968
−0.583
1.00
25.04
A


ATOM
1330
O
GLN
A
247
83.962
31.997
−1.653
1.00
25.92
A


ATOM
1331
N
TYR
A
248
82.443
31.045
−0.304
1.00
22.51
A


ATOM
1332
CA
TYR
A
248
82.161
29.970
−1.260
1.00
21.98
A


ATOM
1333
CB
TYR
A
248
82.273
28.613
−0.541
1.00
17.74
A


ATOM
1334
CG
TYR
A
248
83.626
28.444
0.117
1.00
14.83
A


ATOM
1335
CD1
TYR
A
248
84.736
28.063
−0.630
1.00
14.53
A


ATOM
1336
CE1
TYR
A
248
86.017
28.034
−0.067
1.00
15.65
A


ATOM
1337
CD2
TYR
A
248
83.820
28.784
1.460
1.00
13.57
A


ATOM
1338
CE2
TYR
A
248
85.086
28.757
2.039
1.00
13.28
A


ATOM
1339
CZ
TYR
A
248
86.192
28.386
1.271
1.00
16.78
A


ATOM
1340
OH
TYR
A
248
87.471
28.411
1.816
1.00
15.10
A


ATOM
1341
C
TYR
A
248
80.827
30.091
−2.005
1.00
22.23
A


ATOM
1342
O
TYR
A
248
80.523
29.268
−2.866
1.00
22.78
A


ATOM
1343
N
VAL
A
249
80.054
31.126
−1.680
1.00
21.81
A


ATOM
1344
CA
VAL
A
249
78.760
31.395
−2.308
1.00
22.22
A


ATOM
1345
CB
VAL
A
249
78.077
32.634
−1.640
1.00
22.82
A


ATOM
1346
CG1
VAL
A
249
76.904
33.139
−2.496
1.00
22.57
A


ATOM
1347
CG2
VAL
A
249
77.606
32.270
−0.243
1.00
22.62
A


ATOM
1348
C
VAL
A
249
78.878
31.666
−3.818
1.00
21.92
A


ATOM
1349
O
VAL
A
249
79.733
32.428
−4.255
1.00
20.01
A


ATOM
1350
N
SER
A
250
78.012
31.045
−4.609
1.00
22.88
A


ATOM
1351
CA
SER
A
250
78.030
31.259
−6.049
1.00
24.81
A


ATOM
1352
CB
SER
A
250
77.357
30.105
−6.792
1.00
25.82
A


ATOM
1353
OG
SER
A
250
75.999
29.984
−6.419
1.00
27.07
A


ATOM
1354
C
SER
A
250
77.288
32.546
−6.357
1.00
26.22
A


ATOM
1355
O
SER
A
250
76.438
33.004
−5.582
1.00
25.88
A


ATOM
1356
N
PRO
A
251
77.592
33.148
−7.506
1.00
26.70
A


ATOM
1357
CD
PRO
A
251
78.632
32.813
−8.495
1.00
27.24
A


ATOM
1358
CA
PRO
A
251
76.908
34.393
−7.847
1.00
27.08
A


ATOM
1359
CB
PRO
A
251
77.637
34.860
−9.113
1.00
25.51
A


ATOM
1360
CG
PRO
A
251
78.171
33.590
−9.701
1.00
27.43
A


ATOM
1361
C
PRO
A
251
75.399
34.288
−8.026
1.00
28.00
A


ATOM
1362
O
PRO
A
251
74.684
35.218
−7.678
1.00
28.30
A


ATOM
1363
N
GLU
A
252
74.908
33.166
−8.550
1.00
28.81
A


ATOM
1364
CA
GLU
A
252
73.469
33.012
−8.768
1.00
29.67
A


ATOM
1365
CB
GLU
A
252
73.151
31.684
−9.463
1.00
29.72
A


ATOM
1366
CG
GLU
A
252
73.698
30.453
−8.740
1.00
31.04
A


ATOM
1367
CD
GLU
A
252
75.106
30.075
−9.191
1.00
30.61
A


ATOM
1368
OE1
GLU
A
252
75.880
30.973
−9.597
1.00
30.55
A


ATOM
1369
OE2
GLU
A
252
75.434
28.872
−9.130
1.00
30.80
A


ATOM
1370
C
GLU
A
252
72.709
33.083
−7.462
1.00
30.83
A


ATOM
1371
O
GLU
A
252
71.563
33.530
−7.423
1.00
31.87
A


ATOM
1372
N
LEU
A
253
73.351
32.639
−6.388
1.00
32.71
A


ATOM
1373
CA
LEU
A
253
72.734
32.655
−5.073
1.00
33.94
A


ATOM
1374
CB
LEU
A
253
73.612
31.901
−4.081
1.00
37.40
A


ATOM
1375
CG
LEU
A
253
72.967
31.086
−2.950
1.00
41.64
A


ATOM
1376
CD1
LEU
A
253
72.067
31.925
−2.048
1.00
43.86
A


ATOM
1377
CD2
LEU
A
253
72.144
30.017
−3.597
1.00
45.52
A


ATOM
1378
C
LEU
A
253
72.545
34.095
−4.603
1.00
35.67
A


ATOM
1379
O
LEU
A
253
71.589
34.392
−3.897
1.00
37.48
A


ATOM
1380
N
LEU
A
254
73.451
34.989
−4.995
1.00
36.38
A


ATOM
1381
CA
LEU
A
254
73.372
36.397
−4.600
1.00
36.66
A


ATOM
1382
CB
LEU
A
254
74.764
37.032
−4.572
1.00
33.81
A


ATOM
1383
CG
LEU
A
254
75.824
36.402
−3.674
1.00
33.40
A


ATOM
1384
CD1
LEU
A
254
77.183
37.022
−3.982
1.00
30.48
A


ATOM
1385
CD2
LEU
A
254
75.440
36.574
−2.208
1.00
31.43
A


ATOM
1386
C
LEU
A
254
72.485
37.240
−5.511
1.00
38.89
A


ATOM
1387
O
LEU
A
254
72.079
38.328
−5.133
1.00
38.85
A


ATOM
1388
N
THR
A
255
72.187
36.754
−6.709
1.00
42.60
A


ATOM
1389
CA
THR
A
255
71.358
37.528
−7.624
1.00
47.21
A


ATOM
1390
CB
THR
A
255
72.102
37.847
−8.941
1.00
47.08
A


ATOM
1391
OG1
THR
A
255
72.008
36.718
−9.814
1.00
48.56
A


ATOM
1392
CG2
THR
A
255
73.581
38.157
−8.686
1.00
45.65
A


ATOM
1393
C
THR
A
255
70.044
36.848
−8.009
1.00
51.00
A


ATOM
1394
O
THR
A
255
69.348
37.323
−8.903
1.00
51.80
A


ATOM
1395
N
GLU
A
256
69.696
35.745
−7.353
1.00
55.01
A


ATOM
1396
CA
GLU
A
256
68.450
35.044
−7.683
1.00
58.97
A


ATOM
1397
CB
GLU
A
256
68.679
34.057
−8.832
1.00
59.81
A


ATOM
1398
CG
GLU
A
256
68.922
34.707
−10.181
1.00
63.59
A


ATOM
1399
CD
GLU
A
256
69.343
33.707
−11.240
1.00
65.64
A


ATOM
1400
OE1
GLU
A
256
68.727
32.617
−11.310
1.00
67.44
A


ATOM
1401
OE2
GLU
A
256
70.285
34.015
−12.007
1.00
66.61
A


ATOM
1402
C
GLU
A
256
67.859
34.279
−6.512
1.00
60.83
A


ATOM
1403
O
GLU
A
256
66.701
33.861
−6.563
1.00
61.27
A


ATOM
1404
N
ALA
A
257
68.657
34.100
−5.463
1.00
62.31
A


ATOM
1405
CA
ALA
A
257
68.234
33.348
−4.285
1.00
63.29
A


ATOM
1406
CB
ALA
A
257
66.867
33.847
−3.784
1.00
62.76
A


ATOM
1407
C
ALA
A
257
68.157
31.860
−4.651
1.00
63.64
A


ATOM
1408
O
ALA
A
257
67.790
31.028
−3.825
1.00
64.96
A


ATOM
1409
N
SER
A
258
68.523
31.532
−5.888
1.00
62.79
A


ATOM
1410
CA
SER
A
258
68.485
30.150
−6.378
1.00
62.30
A


ATOM
1411
CB
SER
A
258
68.049
30.144
−7.847
1.00
63.00
A


ATOM
1412
OG
SER
A
258
68.762
31.129
−8.582
1.00
63.40
A


ATOM
1413
C
SER
A
258
69.816
29.402
−6.237
1.00
61.09
A


ATOM
1414
O
SER
A
258
70.862
30.009
−6.009
1.00
62.12
A


ATOM
1415
N
ALA
A
259
69.774
28.083
−6.389
1.00
58.47
A


ATOM
1416
CA
ALA
A
259
70.979
27.270
−6.278
1.00
55.79
A


ATOM
1417
CB
ALA
A
259
71.403
27.164
−4.837
1.00
56.24
A


ATOM
1418
C
ALA
A
259
70.738
25.886
−6.842
1.00
53.38
A


ATOM
1419
O
ALA
A
259
69.641
25.347
−6.736
1.00
54.10
A


ATOM
1420
N
CYS
A
260
71.768
25.30
−7.433
1.00
49.75
A


ATOM
1421
CA
CYS
A
260
71.623
23.988
−8.015
1.00
45.68
A


ATOM
1422
CB
CYS
A
260
71.067
24.106
−9.438
1.00
48.50
A


ATOM
1423
SG
CYS
A
260
69.936
22.732
−9.899
1.00
57.53
A


ATOM
1424
C
CYS
A
260
72.980
23.318
−8.022
1.00
41.30
A


ATOM
1425
O
CYS
A
260
73.892
23.762
−7.335
1.00
39.24
A


ATOM
1426
N
LYS
A
261
73.118
22.258
−8.805
1.00
36.63
A


ATOM
1427
CA
LYS
A
261
74.369
21.535
−8.866
1.00
33.81
A


ATOM
1428
CB
LYS
A
261
74.261
20.416
−9.897
1.00
34.27
A


ATOM
1429
CG
LYS
A
261
73.250
19.362
−9.488
1.00
34.04
A


ATOM
1430
CD
LYS
A
261
72.995
18.353
−10.577
1.00
33.10
A


ATOM
1431
CE
LYS
A
261
71.983
17.336
−10.105
1.00
32.48
A


ATOM
1432
NZ
LYS
A
261
71.660
16.357
−11.176
1.00
33.10
A


ATOM
1433
C
LYS
A
261
75.565
22.419
−9.153
1.00
31.80
A


ATOM
1434
O
LYS
A
261
76.636
22.214
−8.589
1.00
31.89
A


ATOM
1435
N
SER
A
262
75.389
23.405
−10.025
1.00
29.92
A


ATOM
1436
CA
SER
A
262
76.477
24.314
−10.354
1.00
28.19
A


ATOM
1437
CB
SER
A
262
76.034
25.309
−11.417
1.00
29.90
A


ATOM
1438
OG
SER
A
262
76.184
24.732
−12.695
1.00
34.45
A


ATOM
1439
C
SER
A
262
77.047
25.069
−9.155
1.00
25.77
A


ATOM
1440
O
SER
A
262
78.225
25.405
−9.146
1.00
26.59
A


ATOM
1441
N
SER
A
263
76.216
25.347
−8.159
1.00
23.42
A


ATOM
1442
CA
SER
A
263
76.663
26.040
−6.953
1.00
23.04
A


ATOM
1443
CB
SER
A
263
75.502
26.209
−5.979
1.00
24.64
A


ATOM
1444
OG
SER
A
263
74.463
26.963
−6.572
1.00
31.12
A


ATOM
1445
C
SER
A
263
77.777
25.233
−6.283
1.00
21.37
A


ATOM
1446
O
SER
A
263
78.745
25.803
−5.788
1.00
20.74
A


ATOM
1447
N
ASP
A
264
77.640
23.909
−6.268
1.00
19.11
A


ATOM
1448
CA
ASP
A
264
78.674
23.06
−5.682
1.00
19.35
A


ATOM
1449
CB
ASP
A
264
78.206
21.609
−5.579
1.00
18.45
A


ATOM
1450
CG
ASP
A
264
77.164
21.406
−4.500
1.00
19.39
A


ATOM
1451
OD1
ASP
A
264
76.998
22.304
−3.649
1.00
20.34
A


ATOM
1452
OD2
ASP
A
264
76.522
20.338
−4.488
1.00
19.48
A


ATOM
1453
C
ASP
A
264
79.943
23.127
−6.542
1.00
19.34
A


ATOM
1454
O
ASP
A
264
81.052
23.147
−6.018
1.00
20.70
A


ATOM
1455
N
LEU
A
265
79.772
23.16
−7.864
1.00
17.68
A


ATOM
1456
CA
LEU
A
265
80.898
23.23
−8.774
1.00
17.42
A


ATOM
1457
CB
LEU
A
265
80.406
23.058
−10.208
1.00
19.36
A


ATOM
1458
CG
LEU
A
265
79.683
21.717
−10.453
1.00
19.53
A


ATOM
1459
CD1
LEU
A
265
79.189
21.655
−11.879
1.00
17.18
A


ATOM
1460
CD2
LEU
A
265
80.625
20.550
−10.168
1.00
14.91
A


ATOM
1461
C
LEU
A
265
81.619
24.566
−8.600
1.00
19.06
A


ATOM
1462
O
LEU
A
265
82.850
24.649
−8.697
1.00
18.60
A


ATOM
1463
N
TRP
A
266
80.853
25.621
−8.350
1.00
18.60
A


ATOM
1464
CA
TRP
A
266
81.468
26.902
−8.107
1.00
18.62
A


ATOM
1465
CB
TRP
A
266
80.405
27.976
−7.876
1.00
19.75
A


ATOM
1466
CG
TRP
A
266
80.997
29.277
−7.382
1.00
21.53
A


ATOM
1467
CD2
TRP
A
266
81.357
30.420
−8.174
1.00
22.40
A


ATOM
1468
CE2
TRP
A
266
81.917
31.375
−7.296
1.00
22.70
A


ATOM
1469
CE3
TRP
A
266
81.260
30.728
−9.541
1.00
21.62
A


ATOM
1470
CD1
TRP
A
266
81.344
29.582
−6.094
1.00
20.15
A


ATOM
1471
NE1
TRP
A
266
81.896
30.835
−6.037
1.00
20.80
A


ATOM
1472
CZ2
TRP
A
266
82.382
32.624
−7.739
1.00
22.47
A


ATOM
1473
CZ3
TRP
A
266
81.721
31.961
−9.981
1.00
22.48
A


ATOM
1474
CH2
TRP
A
266
82.276
32.898
−9.080
1.00
23.40
A


ATOM
1475
C
TRP
A
266
82.338
26.734
−6.857
1.00
18.89
A


ATOM
1476
O
TRP
A
266
83.523
27.070
−6.875
1.00
20.01
A


ATOM
1477
N
ALA
A
267
81.755
26.204
−5.780
1.00
16.09
A


ATOM
1478
CA
ALA
A
267
82.502
25.994
−4.540
1.00
15.55
A


ATOM
1479
CB
ALA
A
267
81.630
25.313
−3.499
1.00
13.20
A


ATOM
1480
C
ALA
A
267
83.738
25.145
−4.813
1.00
16.44
A


ATOM
1481
O
ALA
A
267
84.802
25.345
−4.218
1.00
17.65
A


ATOM
1482
N
LEU
A
268
83.597
24.181
−5.710
1.00
15.96
A


ATOM
1483
CA
LEU
A
268
84.732
23.336
−6.055
1.00
17.56
A


ATOM
1484
CB
LEU
A
268
84.315
22.281
−7.098
1.00
16.91
A


ATOM
1485
CG
LEU
A
268
85.477
21.535
−7.775
1.00
16.43
A


ATOM
1486
CD1
LEU
A
268
86.214
20.697
−6.766
1.00
15.17
A


ATOM
1487
CD2
LEU
A
268
84.947
20.643
−8.871
1.00
17.18
A


ATOM
1488
C
LEU
A
268
85.892
24.193
−6.599
1.00
15.96
A


ATOM
1489
O
LEU
A
268
87.032
24.040
−6.178
1.00
14.54
A


ATOM
1490
N
GLY
A
269
85.578
25.092
−7.530
1.00
17.15
A


ATOM
1491
CA
GLY
A
269
86.590
25.957
−8.116
1.00
18.32
A


ATOM
1492
C
GLY
A
269
87.339
26.722
−7.042
1.00
19.39
A


ATOM
1493
O
GLY
A
269
88.579
26.777
−7.042
1.00
19.66
A


ATOM
1494
N
CYS
A
270
86.579
27.297
−6.111
1.00
17.50
A


ATOM
1495
CA
CYS
A
270
87.154
28.043
−5.010
1.00
17.72
A


ATOM
1496
CB
CYS
A
270
86.047
28.551
−4.088
1.00
18.96
A


ATOM
1497
SG
CYS
A
270
84.981
29.801
−4.798
1.00
19.62
A


ATOM
1498
C
CYS
A
270
88.114
27.182
−4.201
1.00
18.63
A


ATOM
1499
O
CYS
A
270
89.213
27.612
−3.850
1.00
18.78
A


ATOM
1500
N
ILE
A
271
87.679
25.962
−3.900
1.00
20.05
A


ATOM
1501
CA
ILE
A
271
88.479
25.019
−3.130
1.00
20.08
A


ATOM
1502
CB
ILE
A
271
87.668
23.755
−2.812
1.00
20.09
A


ATOM
1503
CG2
ILE
A
271
88.592
22.654
−2.302
1.00
18.31
A


ATOM
1504
CG1
ILE
A
271
86.558
24.104
−1.810
1.00
18.38
A


ATOM
1505
CD1
ILE
A
271
85.396
23.125
−1.783
1.00
14.68
A


ATOM
1506
C
ILE
A
271
89.761
24.629
−3.858
1.00
20.41
A


ATOM
1507
O
ILE
A
271
90.826
24.548
−3.234
1.00
21.81
A


ATOM
1508
N
ILE
A
272
89.669
24.398
−5.166
1.00
18.41
A


ATOM
1509
CA
ILE
A
272
90.860
24.035
−5.934
1.00
19.20
A


ATOM
1510
CB
ILE
A
272
90.526
23.730
−7.412
1.00
20.04
A


ATOM
1511
CG2
ILE
A
272
91.808
23.488
−8.199
1.00
17.73
A


ATOM
1512
CG1
ILE
A
272
89.602
22.523
−7.513
1.00
19.47
A


ATOM
1513
CD1
ILE
A
272
89.001
22.386
−8.872
1.00
20.31
A


ATOM
1514
C
ILE
A
272
91.858
25.191
−5.932
1.00
19.57
A


ATOM
1515
O
ILE
A
272
93.061
24.978
−5.884
1.00
20.97
A


ATOM
1516
N
TYR
A
273
91.338
26.413
−6.028
1.00
19.42
A


ATOM
1517
CA
TYR
A
273
92.157
27.606
−6.041
1.00
18.41
A


ATOM
1518
CB
TYR
A
273
91.272
28.826
−6.294
1.00
18.70
A


ATOM
1519
CG
TYR
A
273
91.998
30.147
−6.252
1.00
19.81
A


ATOM
1520
CD1
TYR
A
273
92.357
30.729
−5.035
1.00
21.25
A


ATOM
1521
CE1
TYR
A
273
93.072
31.936
−4.990
1.00
22.12
A


ATOM
1522
CD2
TYR
A
273
92.366
30.804
−7.433
1.00
20.45
A


ATOM
1523
CE2
TYR
A
273
93.081
32.005
−7.403
1.00
20.42
A


ATOM
1524
CZ
TYR
A
273
93.432
32.563
−6.178
1.00
23.33
A


ATOM
1525
OH
TYR
A
273
94.159
33.731
−6.138
1.00
23.26
A


ATOM
1526
C
TYR
A
273
92.848
27.699
−4.687
1.00
19.40
A


ATOM
1527
O
TYR
A
273
94.051
27.945
−4.598
1.00
19.44
A


ATOM
1528
N
GLN
A
274
92.079
27.471
−3.632
1.00
19.53
A


ATOM
1529
CA
GLN
A
274
92.602
27.517
−2.278
1.00
21.26
A


ATOM
1530
CB
GLN
A
274
91.450
27.399
−1.290
1.00
22.36
A


ATOM
1531
CG
GLN
A
274
91.838
27.629
0.142
1.00
21.87
A


ATOM
1532
CD
GLN
A
274
90.643
27.531
1.054
1.00
23.64
A


ATOM
1533
OE1
GLN
A
274
89.499
27.479
0.585
1.00
22.12
A


ATOM
1534
NE2
GLN
A
274
90.890
27.517
2.369
1.00
24.45
A


ATOM
1535
C
GLN
A
274
93.656
26.435
−1.980
1.00
22.20
A


ATOM
1536
O
GLN
A
274
94.549
26.652
−1.160
1.00
22.03
A


ATOM
1537
N
LEU
A
275
93.558
25.275
−2.625
1.00
21.82
A


ATOM
1538
CA
LEU
A
275
94.550
24.223
−2.385
1.00
21.95
A


ATOM
1539
CB
LEU
A
275
94.104
22.886
−3.015
1.00
19.19
A


ATOM
1540
CG
LEU
A
275
92.934
22.153
−2.341
1.00
19.86
A


ATOM
1541
CD1
LEU
A
275
92.528
20.915
−3.134
1.00
19.79
A


ATOM
1542
CD2
LEU
A
275
93.333
21.757
−0.938
1.00
16.56
A


ATOM
1543
C
LEU
A
275
95.910
24.630
−2.962
1.00
21.62
A


ATOM
1544
O
LEU
A
275
96.950
24.414
−2.353
1.00
21.98
A


ATOM
1545
N
VAL
A
276
95.884
25.239
−4.137
1.00
20.54
A


ATOM
1546
CA
VAL
A
276
97.095
25.639
−4.828
1.00
21.48
A


ATOM
1547
CB
VAL
A
276
96.810
25.795
−6.338
1.00
21.76
A


ATOM
1548
CG1
VAL
A
276
98.035
26.269
−7.061
1.00
20.72
A


ATOM
1549
CG2
VAL
A
276
96.332
24.479
−6.908
1.00
21.98
A


ATOM
1550
C
VAL
A
276
97.696
26.946
−4.315
1.00
23.17
A


ATOM
1551
O
VAL
A
276
98.913
27.055
−4.141
1.00
24.82
A


ATOM
1552
N
ALA
A
277
96.837
27.934
−4.085
1.00
22.20
A


ATOM
1553
CA
ALA
A
277
97.271
29.230
−3.628
1.00
19.31
A


ATOM
1554
CB
ALA
A
277
96.339
30.293
−4.174
1.00
19.24
A


ATOM
1555
C
ALA
A
277
97.380
29.350
−2.113
1.00
20.10
A


ATOM
1556
O
ALA
A
277
98.096
30.222
−1.622
1.00
20.73
A


ATOM
1557
N
GLY
A
278
96.686
28.493
−1.368
1.00
19.16
A


ATOM
1558
CA
GLY
A
278
96.748
28.579
0.084
1.00
18.62
A


ATOM
1559
C
GLY
A
278
95.634
29.425
0.677
1.00
21.09
A


ATOM
1560
O
GLY
A
278
95.462
29.483
1.903
1.00
20.36
A


ATOM
1561
N
LEU
A
279
94.865
30.084
−0.190
1.00
22.58
A


ATOM
1562
CA
LEU
A
279
93.742
30.917
0.254
1.00
24.03
A


ATOM
1563
CB
LEU
A
279
94.190
32.365
0.448
1.00
23.98
A


ATOM
1564
CG
LEU
A
279
95.322
32.744
1.396
1.00
25.93
A


ATOM
1565
CD1
LEU
A
279
95.622
34.215
1.140
1.00
25.95
A


ATOM
1566
CD2
LEU
A
279
94.950
32.511
2.873
1.00
24.23
A


ATOM
1567
C
LEU
A
279
92.575
30.940
−0.735
1.00
23.96
A


ATOM
1568
O
LEU
A
279
92.759
30.776
−1.939
1.00
23.93
A


ATOM
1569
N
PRO
A
280
91.353
31.151
−0.231
1.00
24.60
A


ATOM
1570
CD
PRO
A
280
90.987
31.360
1.185
1.00
23.93
A


ATOM
1571
CA
PRO
A
280
90.177
31.208
−1.109
1.00
24.56
A


ATOM
1572
CB
PRO
A
280
89.024
31.319
−0.116
1.00
24.33
A


ATOM
1573
CG
PRO
A
280
89.656
32.027
1.076
1.00
24.23
A


ATOM
1574
C
PRO
A
280
90.324
32.453
−2.033
1.00
25.82
A


ATOM
1575
O
PRO
A
280
90.892
33.458
−1.632
1.00
27.28
A


ATOM
1576
N
PRO
A
281
89.798
32.396
−3.268
1.00
25.40
A


ATOM
1577
CD
PRO
A
281
88.807
31.385
−3.660
1.00
26.04
A


ATOM
1578
CA
PRO
A
281
89.862
33.470
−4.272
1.00
24.99
A


ATOM
1579
CB
PRO
A
281
89.150
32.871
−5.489
1.00
24.76
A


ATOM
1580
CG
PRO
A
281
88.882
31.442
−5.137
1.00
26.48
A


ATOM
1581
C
PRO
A
281
89.254
34.836
−3.921
1.00
25.24
A


ATOM
1582
O
PRO
A
281
89.803
35.886
−4.272
1.00
25.07
A


ATOM
1583
N
PHE
A
282
88.103
34.821
−3.264
1.00
24.47
A


ATOM
1584
CA
PHE
A
282
87.435
36.059
−2.918
1.00
24.29
A


ATOM
1585
CB
PHE
A
282
85.964
35.961
−3.320
1.00
23.11
A


ATOM
1586
CG
PHE
A
282
85.759
35.596
−4.774
1.00
21.99
A


ATOM
1587
CD1
PHE
A
282
85.936
36.543
−5.775
1.00
20.97
A


ATOM
1588
CD2
PHE
A
282
85.448
34.285
−5.139
1.00
21.76
A


ATOM
1589
CE1
PHE
A
282
85.812
36.194
−7.124
1.00
20.59
A


ATOM
1590
CE2
PHE
A
282
85.325
33.923
−6.469
1.00
20.98
A


ATOM
1591
CZ
PHE
A
282
85.509
34.885
−7.471
1.00
23.01
A


ATOM
1592
C
PHE
A
282
87.579
36.366
−1.435
1.00
25.85
A


ATOM
1593
O
PHE
A
282
86.963
35.707
−0.596
1.00
27.04
A


ATOM
1594
N
ARG
A
283
88.414
37.358
−1.124
1.00
27.56
A


ATOM
1595
CA
ARG
A
283
88.676
37.784
0.260
1.00
27.41
A


ATOM
1596
CB
ARG
A
283
90.116
37.451
0.648
1.00
28.05
A


ATOM
1597
CG
ARG
A
283
90.523
36.020
0.327
1.00
32.73
A


ATOM
1598
CD
ARG
A
283
91.944
35.722
0.788
1.00
36.54
A


ATOM
1599
NE
ARG
A
283
92.942
36.490
0.043
1.00
39.92
A


ATOM
1600
CZ
ARG
A
283
93.202
36.329
−1.253
1.00
42.59
A


ATOM
1601
NH1
ARG
A
283
92.544
35.421
−1.961
1.00
44.54
A


ATOM
1602
NH2
ARG
A
283
94.112
37.090
−1.853
1.00
43.94
A


ATOM
1603
C
ARG
A
283
88.445
39.291
0.394
1.00
27.01
A


ATOM
1604
O
ARG
A
283
88.682
40.047
−0.557
1.00
26.54
A


ATOM
1605
N
ALA
A
284
87.977
39.724
1.568
1.00
26.05
A


ATOM
1606
CA
ALA
A
284
87.694
41.135
1.812
1.00
23.42
A


ATOM
1607
CB
ALA
A
284
86.529
41.579
0.967
1.00
21.82
A


ATOM
1608
C
ALA
A
284
87.386
41.383
3.280
1.00
24.72
A


ATOM
1609
O
ALA
A
284
87.193
40.440
4.048
1.00
24.83
A


ATOM
1610
N
GLY
A
285
87.330
42.663
3.659
1.00
25.04
A


ATOM
1611
CA
GLY
A
285
87.055
43.039
5.035
1.00
23.67
A


ATOM
1612
C
GLY
A
285
85.761
42.542
5.652
1.00
25.13
A


ATOM
1613
O
GLY
A
285
85.718
42.302
6.855
1.00
26.60
A


ATOM
1614
N
ASN
A
286
84.700
42.399
4.862
1.00
24.84
A


ATOM
1615
CA
ASN
A
286
83.418
41.923
5.391
1.00
23.82
A


ATOM
1616
CB
ASN
A
286
82.567
43.098
5.899
1.00
23.66
A


ATOM
1617
CG
ASN
A
286
82.362
44.190
4.843
1.00
24.14
A


ATOM
1618
OD1
ASN
A
286
81.835
43.947
3.747
1.00
22.27
A


ATOM
1619
ND2
ASN
A
286
82.776
45.402
5.178
1.00
24.49
A


ATOM
1620
C
ASN
A
286
82.672
41.185
4.296
1.00
24.75
A


ATOM
1621
O
ASN
A
286
83.124
41.160
3.153
1.00
25.32
A


ATOM
1622
N
GLU
A
287
81.522
40.610
4.630
1.00
26.04
A


ATOM
1623
CA
GLU
A
287
80.746
39.865
3.641
1.00
27.47
A


ATOM
1624
CB
GLU
A
287
79.549
39.175
4.287
1.00
30.33
A


ATOM
1625
CG
GLU
A
287
79.935
38.202
5.364
1.00
36.51
A


ATOM
1626
CD
GLU
A
287
78.792
37.288
5.766
1.00
41.45
A


ATOM
1627
OE1
GLU
A
287
77.608
37.712
5.641
1.00
43.02
A


ATOM
1628
OE2
GLU
A
287
79.092
36.155
6.222
1.00
41.33
A


ATOM
1629
C
GLU
A
287
80.250
40.679
2.467
1.00
25.95
A


ATOM
1630
O
GLU
A
287
80.279
40.203
1.330
1.00
25.67
A


ATOM
1631
N
TYR
A
288
79.772
41.893
2.730
1.00
25.20
A


ATOM
1632
CA
TYR
A
288
79.276
42.731
1.644
1.00
22.91
A


ATOM
1633
CB
TYR
A
288
78.870
44.113
2.152
1.00
22.98
A


ATOM
1634
CG
TYR
A
288
78.459
45.068
1.038
1.00
23.01
A


ATOM
1635
CD1
TYR
A
288
77.166
45.031
0.478
1.00
24.16
A


ATOM
1636
CE1
TYR
A
288
76.814
45.869
−0.589
1.00
22.73
A


ATOM
1637
CD2
TYR
A
288
79.376
45.965
0.508
1.00
21.34
A


ATOM
1638
CE2
TYR
A
288
79.043
46.796
−0.551
1.00
23.71
A


ATOM
1639
CZ
TYR
A
288
77.771
46.748
−1.099
1.00
25.48
A


ATOM
1640
OH
TYR
A
288
77.490
47.571
−2.172
1.00
26.98
A


ATOM
1641
C
TYR
A
288
80.352
42.882
0.578
1.00
22.37
A


ATOM
1642
O
TYR
A
288
80.068
42.735
−0.603
1.00
22.65
A


ATOM
1643
N
LEU
A
289
81.590
43.155
0.993
1.00
22.04
A


ATOM
1644
CA
LEU
A
289
82.691
43.326
0.037
1.00
23.92
A


ATOM
1645
CB
LEU
A
289
83.927
43.907
0.748
1.00
21.71
A


ATOM
1646
CG
LEU
A
289
83.661
45.326
1.298
1.00
23.89
A


ATOM
1647
CD1
LEU
A
289
84.716
45.787
2.326
1.00
17.24
A


ATOM
1648
CD2
LEU
A
289
83.570
46.273
0.118
1.00
19.08
A


ATOM
1649
C
LEU
A
289
83.050
42.025
−0.693
1.00
24.50
A


ATOM
1650
O
LEU
A
289
83.446
42.042
−1.852
1.00
24.85
A


ATOM
1651
N
ILE
A
290
82.906
40.904
−0.002
1.00
24.71
A


ATOM
1652
CA
ILE
A
290
83.182
39.601
−0.570
1.00
25.86
A


ATOM
1653
CB
ILE
A
290
83.131
38.521
0.528
1.00
26.67
A


ATOM
1654
CG2
ILE
A
290
83.229
37.154
−0.087
1.00
27.57
A


ATOM
1655
CG1
ILE
A
290
84.282
38.736
1.511
1.00
28.90
A


ATOM
1656
CD1
ILE
A
290
84.173
37.928
2.798
1.00
28.83
A


ATOM
1657
C
ILE
A
290
82.127
39.303
−1.637
1.00
26.89
A


ATOM
1658
O
ILE
A
290
82.446
38.879
−2.757
1.00
26.18
A


ATOM
1659
N
PHE
A
291
80.864
39.531
−1.294
1.00
27.48
A


ATOM
1660
CA
PHE
A
291
79.789
39.287
−2.249
1.00
28.46
A


ATOM
1661
CB
PHE
A
291
78.434
39.587
−1.620
1.00
27.24
A


ATOM
1662
CG
PHE
A
291
78.079
38.664
−0.496
1.00
27.02
A


ATOM
1663
CD1
PHE
A
291
78.716
37.431
−0.365
1.00
26.90
A


ATOM
1664
CD2
PHE
A
291
77.074
38.996
0.399
1.00
25.83
A


ATOM
1665
CE1
PHE
A
291
78.353
36.545
0.637
1.00
27.02
A


ATOM
1666
CE2
PHE
A
291
76.700
38.109
1.412
1.00
28.02
A


ATOM
1667
CZ
PHE
A
291
77.338
36.882
1.532
1.00
26.74
A


ATOM
1668
C
PHE
A
291
79.971
40.159
−3.467
1.00
29.11
A


ATOM
1669
O
PHE
A
291
79.595
39.787
−4.584
1.00
30.18
A


ATOM
1670
N
GLN
A
292
80.559
41.324
−3.240
1.00
28.88
A


ATOM
1671
CA
GLN
A
292
80.783
42.280
−4.304
1.00
30.00
A


ATOM
1672
CB
GLN
A
292
81.215
43.604
−3.679
1.00
32.57
A


ATOM
1673
CG
GLN
A
292
81.191
44.799
−4.599
1.00
35.12
A


ATOM
1674
CD
GLN
A
292
81.208
46.113
−3.817
1.00
38.65
A


ATOM
1675
OE1
GLN
A
292
82.159
46.409
−3.078
1.00
39.67
A


ATOM
1676
NE2
GLN
A
292
80.150
46.903
−3.972
1.00
38.94
A


ATOM
1677
C
GLN
A
292
81.822
41.755
−5.296
1.00
28.96
A


ATOM
1678
O
GLN
A
292
81.633
41.844
−6.510
1.00
28.45
A


ATOM
1679
N
LYS
A
293
82.910
41.193
−4.787
1.00
26.32
A


ATOM
1680
CA
LYS
A
293
83.930
40.661
−5.669
1.00
26.90
A


ATOM
1681
CB
LYS
A
293
85.174
40.319
−4.858
1.00
28.03
A


ATOM
1682
CG
LYS
A
293
85.777
41.539
−4.177
1.00
28.52
A


ATOM
1683
CD
LYS
A
293
87.065
41.208
−3.482
1.00
29.14
A


ATOM
1684
CE
LYS
A
293
87.912
42.449
−3.269
1.00
30.09
A


ATOM
1685
NZ
LYS
A
293
89.165
42.157
−2.490
1.00
30.06
A


ATOM
1686
C
LYS
A
293
83.414
39.432
−6.434
1.00
26.13
A


ATOM
1687
O
LYS
A
293
83.721
39.231
−7.617
1.00
26.02
A


ATOM
1688
N
ILE
A
294
82.617
38.621
−5.755
1.00
24.49
A


ATOM
1689
CA
ILE
A
294
82.047
37.429
−6.362
1.00
24.40
A


ATOM
1690
CB
ILE
A
294
81.168
36.680
−5.340
1.00
23.24
A


ATOM
1691
CG2
ILE
A
294
80.154
35.763
−6.046
1.00
21.00
A


ATOM
1692
CG1
ILE
A
294
82.072
35.929
−4.365
1.00
19.23
A


ATOM
1693
CD1
ILE
A
294
81.388
35.559
−3.067
1.00
17.91
A


ATOM
1694
C
ILE
A
294
81.224
37.744
−7.608
1.00
26.38
A


ATOM
1695
O
ILE
A
294
81.428
37.139
−8.661
1.00
25.96
A


ATOM
1696
N
ILE
A
295
80.303
38.694
−7.505
1.00
28.38
A


ATOM
1697
CA
ILE
A
295
79.467
39.018
−8.659
1.00
31.11
A


ATOM
1698
CB
ILE
A
295
78.243
39.852
−8.248
1.00
31.46
A


ATOM
1699
CG2
ILE
A
295
77.548
39.181
−7.068
1.00
32.78
A


ATOM
1700
CG1
ILE
A
295
78.669
41.268
−7.871
1.00
31.79
A


ATOM
1701
CD1
ILE
A
295
77.518
42.132
−7.438
1.00
33.46
A


ATOM
1702
C
ILE
A
295
80.201
39.731
−9.798
1.00
31.35
A


ATOM
1703
O
ILE
A
295
79.709
39.784
−10.930
1.00
32.03
A


ATOM
1704
N
LYS
A
296
81.374
40.269
−9.511
1.00
30.68
A


ATOM
1705
CA
LYS
A
296
82.129
40.937
−10.552
1.00
31.64
A


ATOM
1706
CB
LYS
A
296
82.683
42.275
−10.041
1.00
32.01
A


ATOM
1707
CG
LYS
A
296
81.605
43.213
−9.520
1.00
34.12
A


ATOM
1708
CD
LYS
A
296
82.184
44.441
−8.841
1.00
37.38
A


ATOM
1709
CE
LYS
A
296
82.299
45.609
−9.803
1.00
40.30
A


ATOM
1710
NZ
LYS
A
296
82.864
46.819
−9.119
1.00
42.94
A


ATOM
1711
C
LYS
A
296
83.258
40.010
−10.966
1.00
31.87
A


ATOM
1712
O
LYS
A
296
84.135
40.398
−11.745
1.00
32.98
A


ATOM
1713
N
LEU
A
297
83.227
38.780
−10.443
1.00
30.62
A


ATOM
1714
CA
LEU
A
297
84.253
37.775
−10.735
1.00
29.78
A


ATOM
1715
CB
LEU
A
297
84.100
37.253
−12.169
1.00
29.42
A


ATOM
1716
CG
LEU
A
297
84.802
35.931
−12.527
1.00
29.13
A


ATOM
1717
CD1
LEU
A
297
84.142
34.776
−11.783
1.00
27.91
A


ATOM
1718
CD2
LEU
A
297
84.725
35.682
−14.024
1.00
26.86
A


ATOM
1719
C
LEU
A
297
85.622
38.436
−10.565
1.00
29.62
A


ATOM
1720
O
LEU
A
297
86.489
38.333
−11.419
1.00
28.99
A


ATOM
1721
N
GLU
A
298
85.807
39.091
−9.427
1.00
29.81
A


ATOM
1722
CA
GLU
A
298
87.027
39.826
−9.143
1.00
30.88
A


ATOM
1723
CB
GLU
A
298
86.622
41.166
−8.510
1.00
33.22
A


ATOM
1724
CG
GLU
A
298
87.754
42.136
−8.228
1.00
38.19
A


ATOM
1725
CD
GLU
A
298
87.317
43.274
−7.303
1.00
41.34
A


ATOM
1726
OE1
GLU
A
298
86.416
44.054
−7.684
1.00
43.93
A


ATOM
1727
OE2
GLU
A
298
87.867
43.382
−6.187
1.00
43.19
A


ATOM
1728
C
GLU
A
298
88.071
39.110
−8.269
1.00
29.28
A


ATOM
1729
O
GLU
A
298
88.066
39.230
−7.045
1.00
30.04
A


ATOM
1730
N
TYR
A
299
88.972
38.375
−8.906
1.00
26.46
A


ATOM
1731
CA
TYR
A
299
90.034
37.669
−8.194
1.00
26.46
A


ATOM
1732
CB
TYR
A
299
89.548
36.315
−7.640
1.00
24.23
A


ATOM
1733
CG
TYR
A
299
89.403
35.252
−8.709
1.00
23.32
A


ATOM
1734
CD1
TYR
A
299
88.369
35.318
−9.653
1.00
23.42
A


ATOM
1735
CE1
TYR
A
299
88.274
34.392
−10.686
1.00
23.13
A


ATOM
1736
CD2
TYR
A
299
90.337
34.227
−8.829
1.00
21.77
A


ATOM
1737
CE2
TYR
A
299
90.250
33.292
−9.864
1.00
21.81
A


ATOM
1738
CZ
TYR
A
299
89.214
33.379
−10.784
1.00
22.35
A


ATOM
1739
OH
TYR
A
299
89.089
32.444
−11.780
1.00
21.61
A


ATOM
1740
C
TYR
A
299
91.102
37.416
−9.245
1.00
28.31
A


ATOM
1741
O
TYR
A
299
90.864
37.622
−10.426
1.00
27.25
A


ATOM
1742
N
ASP
A
300
92.277
36.959
−8.844
1.00
30.57
A


ATOM
1743
CA
ASP
A
300
93.282
36.687
−9.851
1.00
33.57
A


ATOM
1744
CB
ASP
A
300
94.012
37.980
−10.193
1.00
38.77
A


ATOM
1745
CG
ASP
A
300
94.382
38.768
−8.968
1.00
43.17
A


ATOM
1746
OD1
ASP
A
300
95.245
38.283
−8.197
1.00
46.59
A


ATOM
1747
OD2
ASP
A
300
93.802
39.865
−8.773
1.00
45.78
A


ATOM
1748
C
ASP
A
300
94.232
35.607
−9.364
1.00
33.20
A


ATOM
1749
O
ASP
A
300
94.311
35.354
−8.169
1.00
33.46
A


ATOM
1750
N
PHE
A
301
94.937
34.959
−10.287
1.00
32.16
A


ATOM
1751
CA
PHE
A
301
95.853
33.892
−9.910
1.00
33.41
A


ATOM
1752
CB
PHE
A
301
95.922
32.813
−11.001
1.00
32.89
A


ATOM
1753
CG
PHE
A
301
94.590
32.240
−11.403
1.00
33.05
A


ATOM
1754
CD1
PHE
A
301
93.763
32.921
−12.297
1.00
31.61
A


ATOM
1755
CD2
PHE
A
301
94.171
31.006
−10.905
1.00
30.94
A


ATOM
1756
CE1
PHE
A
301
92.548
32.387
−12.687
1.00
31.29
A


ATOM
1757
CE2
PHE
A
301
92.961
30.466
−11.287
1.00
31.42
A


ATOM
1758
CZ
PHE
A
301
92.142
31.157
−12.184
1.00
32.69
A


ATOM
1759
C
PHE
A
301
97.287
34.359
−9.649
1.00
34.23
A


ATOM
1760
O
PHE
A
301
97.784
35.274
−10.303
1.00
33.66
A


ATOM
1761
N
PRO
A
302
97.962
33.750
−8.665
1.00
35.45
A


ATOM
1762
CD
PRO
A
302
97.426
32.932
−27.564
1.00
35.55
A


ATOM
1763
CA
PRO
A
302
99.347
34.145
−8.395
1.00
35.82
A


ATOM
1764
CB
PRO
A
302
99.612
33.571
−7.009
1.00
35.09
A


ATOM
1765
CG
PRO
A
302
98.682
32.401
−6.933
1.00
34.93
A


ATOM
1766
C
PRO
A
302
100.214
33.506
−9.485
1.00
37.48
A


ATOM
1767
O
PRO
A
302
99.830
32.504
−10.083
1.00
37.30
A


ATOM
1768
N
ALA
A
303
101.370
34.100
−9.744
1.00
39.16
A


ATOM
1769
CA
ALA
A
303
102.293
33.641
−10.775
1.00
39.50
A


ATOM
1770
CB
ALA
A
303
103.612
34.393
−10.640
1.00
39.58
A


ATOM
1771
C
ALA
A
303
102.577
32.148
−10.832
1.00
41.05
A


ATOM
1772
O
ALA
A
303
102.642
31.569
−11.920
1.00
42.39
A


ATOM
1773
N
ALA
A
304
102.758
31.526
−9.671
1.00
40.38
A


ATOM
1774
CA
ALA
A
304
103.099
30.105
−9.614
1.00
39.93
A


ATOM
1775
CB
ALA
A
304
103.627
29.772
−8.212
1.00
41.64
A


ATOM
1776
C
ALA
A
304
102.025
29.089
−10.002
1.00
38.27
A


ATOM
1777
O
ALA
A
304
102.343
27.993
−10.453
1.00
39.29
A


ATOM
1778
N
PHE
A
305
100.764
29.453
−9.813
1.00
35.83
A


ATOM
1779
CA
PHE
A
305
99.614
28.587
−10.085
1.00
33.62
A


ATOM
1780
CB
PHE
A
305
98.376
29.475
−10.278
1.00
32.70
A


ATOM
1781
CG
PHE
A
305
97.096
28.857
−9.796
1.00
31.41
A


ATOM
1782
CD1
PHE
A
305
96.422
27.915
−10.574
1.00
30.30
A


ATOM
1783
CD2
PHE
A
305
96.556
29.225
−8.562
1.00
30.99
A


ATOM
1784
CE1
PHE
A
305
95.230
27.350
−10.136
1.00
29.76
A


ATOM
1785
CE2
PHE
A
305
95.352
28.663
−8.105
1.00
30.08
A


ATOM
1786
CZ
PHE
A
305
94.689
27.725
−8.897
1.00
30.22
A


ATOM
1787
C
PHE
A
305
99.735
27.580
−11.241
1.00
32.03
A


ATOM
1788
O
PHE
A
305
99.767
27.962
−12.405
1.00
32.54
A


ATOM
1789
N
PHE
A
306
99.781
26.290
−10.914
1.00
31.58
A


ATOM
1790
CA
PHE
A
306
99.886
25.235
−11.932
1.00
30.32
A


ATOM
1791
CB
PHE
A
306
99.518
23.875
−11.338
1.00
29.86
A


ATOM
1792
CG
PHE
A
306
100.087
23.639
−9.971
1.00
30.29
A


ATOM
1793
CD1
PHE
A
306
101.447
23.783
−9.733
1.00
30.37
A


ATOM
1794
CD2
PHE
A
306
99.259
23.275
−8.919
1.00
30.23
A


ATOM
1795
CE1
PHE
A
306
101.975
23.570
−8.465
1.00
30.98
A


ATOM
1796
CE2
PHE
A
306
99.773
23.061
−7.648
1.00
30.91
A


ATOM
1797
CZ
PHE
A
306
101.136
23.210
−7.418
1.00
31.14
A


ATOM
1798
C
PHE
A
306
98.949
25.545
−13.096
1.00
29.48
A


ATOM
1799
O
PHE
A
306
97.738
25.631
−12.920
1.00
30.39
A


ATOM
1800
N
PRO
A
307
99.501
25.701
−14.309
1.00
28.76
A


ATOM
1801
CD
PRO
A
307
100.934
25.575
−14.635
1.00
27.67
A


ATOM
1802
CA
PRO
A
307
98.731
26.014
−15.520
1.00
27.24
A


ATOM
1803
CB
PRO
A
307
99.757
25.848
−16.635
1.00
25.23
A


ATOM
1804
CG
PRO
A
307
101.010
26.262
−15.978
1.00
25.61
A


ATOM
1805
C
PRO
A
307
97.457
25.221
−15.787
1.00
25.86
A


ATOM
1806
O
PRO
A
307
96.419
25.808
−16.098
1.00
24.65
A


ATOM
1807
N
LYS
A
308
97.521
23.901
−15.682
1.00
25.13
A


ATOM
1808
CA
LYS
A
308
96.330
23.109
−15.952
1.00
24.53
A


ATOM
1809
CB
LYS
A
308
96.689
21.640
−16.136
1.00
24.86
A


ATOM
1810
CG
LYS
A
308
97.361
21.413
−17.490
1.00
25.50
A


ATOM
1811
CD
LYS
A
308
97.987
20.047
−17.616
1.00
27.33
A


ATOM
1812
CE
LYS
A
308
98.678
19.886
−18.961
1.00
29.39
A


ATOM
1813
NZ
LYS
A
308
99.232
18.505
−19.146
1.00
32.38
A


ATOM
1814
C
LYS
A
308
95.282
23.293
−14.890
1.00
24.82
A


ATOM
1815
O
LYS
A
308
94.085
23.281
−15.193
1.00
24.89
A


ATOM
1816
N
ALA
A
309
95.716
23.489
−13.647
1.00
24.73
A


ATOM
1817
CA
ALA
A
309
94.758
23.716
−12.573
1.00
25.03
A


ATOM
1818
CB
ALA
A
309
95.445
23.662
−11.208
1.00
24.10
A


ATOM
1819
C
ALA
A
309
94.140
25.094
−12.816
1.00
25.34
A


ATOM
1820
O
ALA
A
309
92.934
25.273
−12.679
1.00
26.34
A


ATOM
1821
N
ARG
A
310
94.958
26.067
−13.198
1.00
26.07
A


ATOM
1822
CA
ARG
A
310
94.419
27.396
−13.453
1.00
28.32
A


ATOM
1823
CB
ARG
A
310
95.513
28.359
−13.908
1.00
29.31
A


ATOM
1824
CG
ARG
A
310
94.940
29.708
−14.288
1.00
31.58
A


ATOM
1825
CD
ARG
A
310
95.917
30.588
−15.030
1.00
31.47
A


ATOM
1826
NE
ARG
A
310
95.275
31.825
−15.473
1.00
34.52
A


ATOM
1827
CZ
ARG
A
310
95.771
33.050
−15.276
1.00
35.51
A


ATOM
1828
NH1
ARG
A
310
96.929
33.205
−14.633
1.00
33.99
A


ATOM
1829
NH2
ARG
A
310
95.106
34.124
−15.720
1.00
32.10
A


ATOM
1830
C
ARG
A
310
93.331
27.348
−14.521
1.00
29.03
A


ATOM
1831
O
ARG
A
310
92.308
28.034
−14.418
1.00
29.32
A


ATOM
1832
N
ASP
A
311
93.548
26.536
−15.551
1.00
29.06
A


ATOM
1833
CA
ASP
A
311
92.571
26.432
−16.620
1.00
29.87
A


ATOM
1834
CB
ASP
A
311
93.156
25.636
−17.776
1.00
31.71
A


ATOM
1835
CG
ASP
A
311
92.207
25.537
−18.953
1.00
34.71
A


ATOM
1836
OD1
ASP
A
311
91.288
24.690
−18.912
1.00
36.90
A


ATOM
1837
OD2
ASP
A
311
92.378
26.312
−19.918
1.00
36.33
A


ATOM
1838
C
ASP
A
311
91.264
25.800
−16.128
1.00
29.70
A


ATOM
1839
O
ASP
A
311
90.169
26.238
−16.513
1.00
29.95
A


ATOM
1840
N
LEU
A
312
91.383
24.778
−15.282
1.00
26.64
A


ATOM
1841
CA
LEU
A
312
90.215
24.112
−14.715
1.00
24.92
A


ATOM
1842
CB
LEU
A
312
90.645
22.911
−13.869
1.00
23.93
A


ATOM
1843
CG
LEU
A
312
89.504
22.112
−13.227
1.00
24.48
A


ATOM
1844
CD1
LEU
A
312
88.569
21.610
−14.296
1.00
25.07
A


ATOM
1845
CD2
LEU
A
312
90.061
20.945
−12.460
1.00
25.13
A


ATOM
1846
C
LEU
A
312
89.412
25.095
−13.841
1.00
23.85
A


ATOM
1847
O
LEU
A
312
88.182
25.136
−13.896
1.00
21.21
A


ATOM
1848
N
VAL
A
313
90.121
25.886
−13.042
1.00
23.12
A


ATOM
1849
CA
VAL
A
313
89.484
26.865
−12.171
1.00
23.55
A


ATOM
1850
CB
VAL
A
313
90.536
27.583
−11.297
1.00
22.33
A


ATOM
1851
CG1
VAL
A
313
89.898
28.752
−10.559
1.00
19.05
A


ATOM
1852
CG2
VAL
A
313
91.144
26.607
−10.305
1.00
19.89
A


ATOM
1853
C
VAL
A
313
88.701
27.915
−12.975
1.00
25.59
A


ATOM
1854
O
VAL
A
313
87.590
28.305
−12.605
1.00
26.57
A


ATOM
1855
N
GLU
A
314
89.278
28.378
−14.076
1.00
26.08
A


ATOM
1856
CA
GLU
A
314
88.598
29.370
−14.895
1.00
26.79
A


ATOM
1857
CB
GLU
A
314
89.543
29.928
−15.948
1.00
27.50
A


ATOM
1858
CG
GLU
A
314
90.739
30.639
−15.381
1.00
32.29
A


ATOM
1859
CD
GLU
A
314
91.687
31.094
−16.463
1.00
35.85
A


ATOM
1860
OE1
GLU
A
314
91.967
30.280
−17.375
1.00
38.06
A


ATOM
1861
OE2
GLU
A
314
92.157
32.257
−16.399
1.00
38.48
A


ATOM
1862
C
GLU
A
314
87.370
28.787
−15.577
1.00
26.22
A


ATOM
1863
O
GLU
A
314
86.499
29.527
−16.038
1.00
27.23
A


ATOM
1864
N
LYS
A
315
87.300
27.464
−15.662
1.00
24.74
A


ATOM
1865
CA
LYS
A
315
86.151
26.832
−16.294
1.00
23.60
A


ATOM
1866
CB
LYS
A
315
86.578
25.584
−17.073
1.00
23.69
A


ATOM
1867
CG
LYS
A
315
87.393
25.865
−18.344
1.00
22.41
A


ATOM
1868
CD
LYS
A
315
87.825
24.545
−18.968
1.00
25.68
A


ATOM
1869
CE
LYS
A
315
88.768
24.695
−20.155
1.00
24.86
A


ATOM
1870
NZ
LYS
A
315
88.082
25.219
−21.346
1.00
28.62
A


ATOM
1871
C
LYS
A
315
85.119
26.471
−15.230
1.00
23.42
A


ATOM
1872
O
LYS
A
315
84.043
25.970
−15.541
1.00
25.37
A


ATOM
1873
N
LEU
A
316
85.454
26.730
−13.970
1.00
21.88
A


ATOM
1874
CA
LEU
A
316
84.549
26.461
−12.862
1.00
20.21
A


ATOM
1875
CB
LEU
A
316
85.272
25.705
−11.767
1.00
19.57
A


ATOM
1876
CG
LEU
A
316
85.409
24.221
−12.078
1.00
21.14
A


ATOM
1877
CD1
LEU
A
316
86.272
23.552
−11.009
1.00
19.21
A


ATOM
1878
CD2
LEU
A
316
84.000
23.600
−12.166
1.00
18.59
A


ATOM
1879
C
LEU
A
316
83.996
27.758
−12.290
1.00
21.31
A


ATOM
1880
O
LEU
A
316
82.811
27.848
−11.955
1.00
18.79
A


ATOM
1881
N
LEU
A
317
84.865
28.762
−12.175
1.00
20.59
A


ATOM
1882
CA
LEU
A
317
84.446
30.038
−11.646
1.00
21.64
A


ATOM
1883
CB
LEU
A
317
85.606
30.707
−10.900
1.00
21.42
A


ATOM
1884
CG
LEU
A
317
86.130
29.892
−9.711
1.00
21.80
A


ATOM
1885
CD1
LEU
A
317
87.299
30.599
−9.047
1.00
23.09
A


ATOM
1886
CD2
LEU
A
317
85.031
29.688
−8.724
1.00
20.34
A


ATOM
1887
C
LEU
A
317
83.940
30.890
−12.810
1.00
23.34
A


ATOM
1888
O
LEU
A
317
84.568
31.859
−13.242
1.00
23.29
A


ATOM
1889
N
VAL
A
318
82.786
30.485
−13.324
1.00
24.06
A


ATOM
1890
CA
VAL
A
318
82.135
31.161
−14.436
1.00
23.46
A


ATOM
1891
CB
VAL
A
318
81.829
30.150
−15.547
1.00
24.32
A


ATOM
1892
CG1
VAL
A
318
81.061
30.828
−16.670
1.00
22.57
A


ATOM
1893
CG2
VAL
A
318
83.136
29.524
−16.049
1.00
20.68
A


ATOM
1894
C
VAL
A
318
80.838
31.765
−13.918
1.00
24.59
A


ATOM
1895
O
VAL
A
318
80.050
31.086
−13.250
1.00
24.86
A


ATOM
1896
N
LEU
A
319
80.603
33.036
−14.215
1.00
24.95
A


ATOM
1897
CA
LEU
A
319
79.383
33.688
−13.731
1.00
25.79
A


ATOM
1898
CB
LEU
A
319
79.379
35.157
−14.154
1.00
25.38
A


ATOM
1899
CG
LEU
A
319
80.466
35.963
−13.417
1.00
27.04
A


ATOM
1900
CD1
LEU
A
319
80.452
37.421
−13.869
1.00
25.54
A


ATOM
1901
CD2
LEU
A
319
80.241
35.872
−11.907
1.00
23.27
A


ATOM
1902
C
LEU
A
319
78.077
32.989
−14.141
1.00
26.05
A


ATOM
1903
O
LEU
A
319
77.171
32.819
−13.319
1.00
27.69
A


ATOM
1904
N
ASP
A
320
77.982
32.580
−15.400
1.00
25.08
A


ATOM
1905
CA
ASP
A
320
76.804
31.881
−15.892
1.00
24.00
A


ATOM
1906
CB
ASP
A
320
76.788
31.907
−17.420
1.00
24.02
A


ATOM
1907
CG
ASP
A
320
75.597
31.175
−17.996
1.00
27.27
A


ATOM
1908
OD1
ASP
A
320
75.009
30.337
−17.271
1.00
29.66
A


ATOM
1909
OD2
ASP
A
320
75.253
31.417
−19.175
1.00
30.03
A


ATOM
1910
C
ASP
A
320
76.846
30.427
−15.396
1.00
24.04
A


ATOM
1911
O
ASP
A
320
77.661
29.623
−15.846
1.00
25.11
A


ATOM
1912
N
ALA
A
321
75.940
30.094
−14.489
1.00
23.73
A


ATOM
1913
CA
ALA
A
321
75.867
28.770
−13.887
1.00
23.58
A


ATOM
1914
CB
ALA
A
321
74.710
28.720
−12.916
1.00
23.62
A


ATOM
1915
C
ALA
A
321
75.765
27.599
−14.853
1.00
24.90
A


ATOM
1916
O
ALA
A
321
76.221
26.497
−14.549
1.00
24.36
A


ATOM
1917
N
THR
A
322
75.176
27.834
−16.019
1.00
25.50
A


ATOM
1918
CA
THR
A
322
75.008
26.772
−17.011
1.00
24.60
A


ATOM
1919
CB
THR
A
322
73.816
27.064
−17.909
1.00
23.09
A


ATOM
1920
OG1
THR
A
322
74.079
28.263
−18.646
1.00
23.74
A


ATOM
1921
CG2
THR
A
322
72.568
27.260
−17.080
1.00
20.71
A


ATOM
1922
C
THR
A
322
76.238
26.596
−17.893
1.00
25.24
A


ATOM
1923
O
THR
A
322
76.221
25.807
−18.832
1.00
26.45
A


ATOM
1924
N
LYS
A
323
77.300
27.331
−17.592
1.00
25.05
A


ATOM
1925
CA
LYS
A
323
78.526
27.239
−18.366
1.00
26.46
A


ATOM
1926
CB
LYS
A
323
78.972
28.627
−18.823
1.00
28.68
A


ATOM
1927
CG
LYS
A
323
78.050
29.304
−19.814
1.00
31.27
A


ATOM
1928
CD
LYS
A
323
78.470
29.004
−21.240
1.00
34.38
A


ATOM
1929
CE
LYS
A
323
77.850
29.986
−22.243
1.00
35.12
A


ATOM
1930
NZ
LYS
A
323
76.363
29.936
−22.251
1.00
36.71
A


ATOM
1931
C
LYS
A
323
79.660
26.621
−17.556
1.00
26.39
A


ATOM
1932
O
LYS
A
323
80.795
26.615
−18.010
1.00
28.51
A


ATOM
1933
N
ARG
A
324
79.372
26.114
−16.360
1.00
24.50
A


ATOM
1934
CA
ARG
A
324
80.429
25.524
−15.543
1.00
23.37
A


ATOM
1935
CB
ARG
A
324
80.087
25.633
−14.049
1.00
23.41
A


ATOM
1936
CG
ARG
A
324
80.233
27.034
−13.520
1.00
21.60
A


ATOM
1937
CD
ARG
A
324
79.594
27.220
−12.173
1.00
21.55
A


ATOM
1938
NE
ARG
A
324
79.245
28.624
−11.986
1.00
19.69
A


ATOM
1939
CZ
ARG
A
324
78.273
29.054
−11.191
1.00
19.84
A


ATOM
1940
NH1
ARG
A
324
77.555
28.183
−10.496
1.00
16.83
A


ATOM
1941
NH2
ARG
A
324
77.990
30.358
−11.129
1.00
21.41
A


ATOM
1942
C
ARG
A
324
80.717
24.085
−15.897
1.00
22.63
A


ATOM
1943
O
ARG
A
324
79.798
23.280
−16.058
1.00
24.44
A


ATOM
1944
N
LEU
A
325
82.000
23.767
−16.023
1.00
20.68
A


ATOM
1945
CA
LEU
A
325
82.414
22.411
−16.352
1.00
20.98
A


ATOM
1946
CB
LEU
A
325
83.952
22.330
−16.386
1.00
20.82
A


ATOM
1947
CG
LEU
A
325
84.596
21.147
−17.131
1.00
23.08
A


ATOM
1948
CD1
LEU
A
325
84.149
21.194
−18.595
1.00
21.39
A


ATOM
1949
CD2
LEU
A
325
86.132
21.173
−17.038
1.00
20.00
A


ATOM
1950
C
LEU
A
325
81.840
21.454
−15.290
1.00
20.43
A


ATOM
1951
O
LEU
A
325
82.062
21.633
−14.097
1.00
18.45
A


ATOM
1952
N
GLY
A
326
81.076
20.456
−15.725
1.00
21.33
A


ATOM
1953
CA
GLY
A
326
80.501
19.513
−14.778
1.00
20.60
A


ATOM
1954
C
GLY
A
326
78.984
19.523
−14.701
1.00
22.39
A


ATOM
1955
O
GLY
A
326
78.383
18.493
−14.378
1.00
22.59
A


ATOM
1956
N
CYS
A
327
78.358
20.664
−15.009
1.00
23.36
A


ATOM
1957
CA
CYS
A
327
76.896
20.771
−14.963
1.00
25.18
A


ATOM
1958
CB
CYS
A
327
76.453
22.246
−14.889
1.00
25.79
A


ATOM
1959
SG
CYS
A
327
76.742
23.237
−16.364
1.00
31.42
A


ATOM
1960
C
CYS
A
327
76.229
20.074
−16.148
1.00
24.99
A


ATOM
1961
O
CYS
A
327
76.887
19.743
−17.129
1.00
24.31
A


ATOM
1962
N
ALA
A
328
74.923
19.847
−16.040
1.00
26.34
A


ATOM
1963
CA
ALA
A
328
74.157
19.172
−17.094
1.00
27.51
A


ATOM
1964
CB
ALA
A
328
72.703
18.949
−16.629
1.00
26.81
A


ATOM
1965
C
ALA
A
328
74.179
19.905
−18.443
1.00
28.11
A


ATOM
1966
O
ALA
A
328
74.243
19.274
−19.501
1.00
27.66
A


ATOM
1967
N
GLU
A
329
74.144
21.231
−18.418
1.00
28.05
A


ATOM
1968
CA
GLU
A
329
74.172
21.973
−19.668
1.00
29.54
A


ATOM
1969
CB
GLU
A
329
73.915
23.458
−19.428
1.00
32.18
A


ATOM
1970
CG
GLU
A
329
72.539
23.783
−18.863
1.00
37.89
A


ATOM
1971
CD
GLU
A
329
72.418
23.503
−17.374
1.00
41.37
A


ATOM
1972
OE1
GLU
A
329
73.464
23.308
−16.711
1.00
43.80
A


ATOM
1973
OE2
GLU
A
329
71.273
23.495
−16.863
1.00
43.66
A


ATOM
1974
C
GLU
A
329
75.514
21.807
−20.377
1.00
29.08
A


ATOM
1975
O
GLU
A
329
75.602
21.927
−21.605
1.00
27.73
A


ATOM
1976
N
MET
A
330
76.559
21.540
−19.598
1.00
27.54
A


ATOM
1977
CA
MET
A
330
77.894
21.359
−20.148
1.00
25.71
A


ATOM
1978
CB
MET
A
330
78.945
21.963
−19.219
1.00
27.88
A


ATOM
1979
CG
MET
A
330
78.964
23.489
−19.209
1.00
30.29
A


ATOM
1980
SD
MET
A
330
79.429
24.194
−20.819
1.00
34.04
A


ATOM
1981
CE
MET
A
330
81.187
23.670
−20.936
1.00
29.55
A


ATOM
1982
C
MET
A
330
78.156
19.884
−20.343
1.00
24.53
A


ATOM
1983
O
MET
A
330
79.290
19.473
−20.575
1.00
22.65
A


ATOM
1984
N
GLU
A
331
77.089
19.095
−20.221
1.00
22.87
A


ATOM
1985
CA
GLU
A
331
77.139
17.654
−20.415
1.00
21.38
A


ATOM
1986
CB
GLU
A
331
77.854
17.339
−21.735
1.00
22.71
A


ATOM
1987
CG
GLU
A
331
76.903
16.916
−22.837
1.00
23.01
A


ATOM
1988
CD
GLU
A
331
75.599
17.720
−22.875
1.00
24.76
A


ATOM
1989
OE1
GLU
A
331
75.570
18.830
−23.441
1.00
26.12
A


ATOM
1990
OE2
GLU
A
331
74.588
17.230
−22.337
1.00
24.22
A


ATOM
1991
C
GLU
A
331
77.671
16.765
−19.290
1.00
21.01
A


ATOM
1992
O
GLU
A
331
78.075
15.619
−19.517
1.00
19.50
A


ATOM
1993
N
GLY
A
332
77.675
17.284
−18.071
1.00
19.73
A


ATOM
1994
CA
GLY
A
332
78.056
16.445
−16.954
1.00
17.80
A


ATOM
1995
C
GLY
A
332
79.494
16.243
−16.570
1.00
17.28
A


ATOM
1996
O
GLY
A
332
80.381
17.013
−16.934
1.00
16.11
A


ATOM
1997
N
TYR
A
333
79.701
15.151
−15.842
1.00
16.52
A


ATOM
1998
CA
TYR
A
333
80.997
14.791
−15.305
1.00
16.75
A


ATOM
1999
CB
TYR
A
333
80.787
13.854
−14.115
1.00
16.95
A


ATOM
2000
CG
TYR
A
333
80.369
14.624
−12.893
1.00
18.08
A


ATOM
2001
CD1
TYR
A
333
81.332
15.207
−12.059
1.00
18.77
A


ATOM
2002
CE1
TYR
A
333
80.971
16.035
−10.982
1.00
17.69
A


ATOM
2003
CD2
TYR
A
333
79.021
14.877
−12.620
1.00
17.08
A


ATOM
2004
CE2
TYR
A
333
78.646
15.713
−11.538
1.00
19.05
A


ATOM
2005
CZ
TYR
A
333
79.640
16.287
−10.728
1.00
18.04
A


ATOM
2006
OH
TYR
A
333
79.322
17.126
−9.682
1.00
18.69
A


ATOM
2007
C
TYR
A
333
82.051
14.240
−16.238
1.00
16.78
A


ATOM
2008
O
TYR
A
333
83.248
14.393
−15.977
1.00
16.04
A


ATOM
2009
N
GLY
A
334
81.633
13.598
−17.321
1.00
16.63
A


ATOM
2010
CA
GLY
A
334
82.624
13.082
−18.244
1.00
17.02
A


ATOM
2011
C
GLY
A
334
83.576
14.194
−18.683
1.00
17.47
A


ATOM
2012
O
GLY
A
334
84.802
14.063
−18.562
1.00
17.18
A


ATOM
2013
N
PRO
A
335
83.039
15.315
−19.195
1.00
17.04
A


ATOM
2014
CD
PRO
A
335
81.650
15.611
−19.590
1.00
16.18
A


ATOM
2015
CA
PRO
A
335
83.940
16.382
−19.621
1.00
17.35
A


ATOM
2016
CB
PRO
A
335
82.991
17.441
−20.178
1.00
17.48
A


ATOM
2017
CG
PRO
A
335
81.857
16.605
−20.713
1.00
18.64
A


ATOM
2018
C
PRO
A
335
84.786
16.883
−18.480
1.00
18.48
A


ATOM
2019
O
PRO
A
335
85.963
17.131
−18.661
1.00
20.84
A


ATOM
2020
N
LEU
A
336
84.204
17.034
−17.299
1.00
19.46
A


ATOM
2021
CA
LEU
A
336
84.986
17.504
−16.153
1.00
19.38
A


ATOM
2022
CB
LEU
A
336
84.071
17.692
−14.937
1.00
18.98
A


ATOM
2023
CG
LEU
A
336
84.765
17.982
−13.604
1.00
18.01
A


ATOM
2024
CD1
LEU
A
336
85.534
19.289
−13.690
1.00
16.66
A


ATOM
2025
CD2
LEU
A
336
83.724
18.055
−12.491
1.00
18.81
A


ATOM
2026
C
LEU
A
336
86.132
16.528
−15.815
1.00
19.32
A


ATOM
2027
O
LEU
A
336
87.293
16.932
−15.683
1.00
18.65
A


ATOM
2028
N
LYS
A
337
85.808
15.244
−15.688
1.00
18.38
A


ATOM
2029
CA
LYS
A
337
86.821
14.240
−15.387
1.00
18.89
A


ATOM
2030
CB
LYS
A
337
86.147
12.900
−15.082
1.00
17.70
A


ATOM
2031
CG
LYS
A
337
85.460
12.933
−13.727
1.00
19.89
A


ATOM
2032
CD
LYS
A
337
84.450
11.817
−13.523
1.00
22.66
A


ATOM
2033
CE
LYS
A
337
85.089
10.453
−13.372
1.00
22.78
A


ATOM
2034
NZ
LYS
A
337
84.025
9.444
−13.088
1.00
25.28
A


ATOM
2035
C
LYS
A
337
87.865
14.101
−16.504
1.00
20.07
A


ATOM
2036
O
LYS
A
337
88.996
13.671
−16.254
1.00
20.47
A


ATOM
2037
N
ALA
A
338
87.491
14.486
−17.725
1.00
20.38
A


ATOM
2038
CA
ALA
A
338
88.393
14.441
−18.876
1.00
20.65
A


ATOM
2039
CB
ALA
A
338
87.580
14.382
−20.178
1.00
20.29
A


ATOM
2040
C
ALA
A
338
89.357
15.636
−18.933
1.00
22.18
A


ATOM
2041
O
ALA
A
338
90.265
15.665
−19.768
1.00
24.71
A


ATOM
2042
N
HIS
A
339
89.179
16.627
−18.063
1.00
21.90
A


ATOM
2043
CA
HIS
A
339
90.072
17.785
−18.094
1.00
22.10
A


ATOM
2044
CB
HIS
A
339
89.711
18.762
−16.989
1.00
21.35
A


ATOM
2045
CG
HIS
A
339
90.357
20.097
−17.149
1.00
20.57
A


ATOM
2046
CD2
HIS
A
339
89.891
21.251
−17.683
1.00
19.19
A


ATOM
2047
ND1
HIS
A
339
91.664
20.341
−16.783
1.00
20.52
A


ATOM
2048
CE1
HIS
A
339
91.973
21.592
−17.085
1.00
22.28
A


ATOM
2049
NE2
HIS
A
339
90.914
22.165
−17.633
1.00
21.96
A


ATOM
2050
C
HIS
A
339
91.555
17.404
−17.963
1.00
22.78
A


ATOM
2051
O
HIS
A
339
91.919
16.600
−17.118
1.00
21.05
A


ATOM
2052
N
PRO
A
340
92.425
17.994
−18.801
1.00
24.12
A


ATOM
2053
CD
PRO
A
340
92.090
18.973
−19.855
1.00
23.53
A


ATOM
2054
CA
PRO
A
340
93.872
17.724
−18.795
1.00
25.11
A


ATOM
2055
CB
PRO
A
340
94.435
18.864
−19.647
1.00
22.31
A


ATOM
2056
CG
PRO
A
340
93.379
19.015
−20.685
1.00
22.50
A


ATOM
2057
C
PRO
A
340
94.540
17.654
−17.421
1.00
25.66
A


ATOM
2058
O
PRO
A
340
95.523
16.951
−17.237
1.00
27.43
A


ATOM
2059
N
PHE
A
341
94.011
18.389
−16.459
1.00
25.05
A


ATOM
2060
CA
PHE
A
341
94.596
18.399
−15.139
1.00
24.88
A


ATOM
2061
CB
PHE
A
341
93.897
19.459
−14.276
1.00
24.71
A


ATOM
2062
CG
PHE
A
341
94.482
19.607
−12.893
1.00
24.42
A


ATOM
2063
CD1
PHE
A
341
95.822
19.947
−12.721
1.00
22.55
A


ATOM
2064
CD2
PHE
A
341
93.685
19.397
−11.758
1.00
22.61
A


ATOM
2065
CE1
PHE
A
341
96.364
20.076
−11.434
1.00
23.65
A


ATOM
2066
CE2
PHE
A
341
94.204
19.522
−10.476
1.00
22.09
A


ATOM
2067
CZ
PHE
A
341
95.547
19.863
−10.304
1.00
24.01
A


ATOM
2068
C
PHE
A
341
94.511
17.026
−14.486
1.00
25.70
A


ATOM
2069
O
PHE
A
341
95.363
16.665
−13.680
1.00
27.11
A


ATOM
2070
N
PHE
A
342
93.499
16.258
−14.865
1.00
25.51
A


ATOM
2071
CA
PHE
A
342
93.262
14.929
−14.318
1.00
25.34
A


ATOM
2072
CB
PHE
A
342
91.758
14.728
−14.120
1.00
21.93
A


ATOM
2073
CG
PHE
A
342
91.120
15.728
−13.196
1.00
20.26
A


ATOM
2074
CD1
PHE
A
342
91.556
15.862
−11.888
1.00
20.03
A


ATOM
2075
CD2
PHE
A
342
90.030
16.485
−13.613
1.00
19.36
A


ATOM
2076
CE1
PHE
A
342
90.907
16.731
−11.004
1.00
19.87
A


ATOM
2077
CE2
PHE
A
342
89.377
17.348
−12.744
1.00
18.17
A


ATOM
2078
CZ
PHE
A
342
89.818
17.470
−11.431
1.00
19.27
A


ATOM
2079
C
PHE
A
342
93.805
13.815
−15.214
1.00
27.64
A


ATOM
2080
O
PHE
A
342
93.508
12.630
−15.019
1.00
27.39
A


ATOM
2081
N
GLU
A
343
94.607
14.203
−16.194
1.00
31.32
A


ATOM
2082
CA
GLU
A
343
95.185
13.262
−17.150
1.00
34.29
A


ATOM
2083
CB
GLU
A
343
96.320
13.950
−17.889
1.00
38.36
A


ATOM
2084
CG
GLU
A
343
96.735
13.314
−19.197
1.00
45.23
A


ATOM
2085
CD
GLU
A
343
97.654
14.247
−19.976
1.00
51.01
A


ATOM
2086
OE1
GLU
A
343
98.266
13.801
−20.981
1.00
51.76
A


ATOM
2087
OE2
GLU
A
343
97.755
15.439
−19.568
1.00
52.42
A


ATOM
2088
C
GLU
A
343
95.690
11.950
−16.542
1.00
33.50
A


ATOM
2089
O
GLU
A
343
95.289
10.860
−16.970
1.00
33.57
A


ATOM
2090
N
SER
A
344
96.554
12.049
−15.537
1.00
31.58
A


ATOM
2091
CA
SER
A
344
97.117
10.857
−14.906
1.00
30.38
A


ATOM
2092
CB
SER
A
344
98.447
11.217
−14.253
1.00
29.76
A


ATOM
2093
OG
SER
A
344
98.243
11.995
−13.096
1.00
30.32
A


ATOM
2094
C
SER
A
344
96.242
10.150
−13.857
1.00
30.00
A


ATOM
2095
O
SER
A
344
96.662
9.137
−13.285
1.00
31.14
A


ATOM
2096
N
VAL
A
345
95.046
10.679
−13.606
1.00
27.28
A


ATOM
2097
CA
VAL
A
345
94.135
10.126
−12.609
1.00
25.39
A


ATOM
2098
CB
VAL
A
345
93.093
11.213
−12.159
1.00
24.17
A


ATOM
2099
CG1
VAL
A
345
91.973
10.568
−11.347
1.00
19.50
A


ATOM
2100
CG2
VAL
A
345
93.779
12.321
−11.363
1.00
17.85
A


ATOM
2101
C
VAL
A
345
93.341
8.885
−13.043
1.00
26.45
A


ATOM
2102
O
VAL
A
345
92.813
8.842
−14.154
1.00
27.42
A


ATOM
2103
N
THR
A
346
93.253
7.890
−12.157
1.00
26.62
A


ATOM
2104
CA
THR
A
346
92.451
6.680
−12.406
1.00
27.91
A


ATOM
2105
CB
THR
A
346
93.194
5.388
−11.999
1.00
29.18
A


ATOM
2106
OG1
THR
A
346
94.345
5.224
−12.830
1.00
33.51
A


ATOM
2107
CG2
THR
A
346
92.300
4.171
−12.177
1.00
28.24
A


ATOM
2108
C
THR
A
346
91.229
6.856
−11.505
1.00
27.53
A


ATOM
2109
O
THR
A
346
91.297
6.621
−10.299
1.00
29.24
A


ATOM
2110
N
TRP
A
347
90.117
7.279
−12.094
1.00
27.83
A


ATOM
2111
CA
TRP
A
347
88.898
7.561
−11.336
1.00
29.15
A


ATOM
2112
CB
TRP
A
347
87.878
8.278
−12.224
1.00
27.12
A


ATOM
2113
CG
TRP
A
347
88.353
9.574
−12.758
1.00
25.48
A


ATOM
2114
CD2
TRP
A
347
88.252
10.853
−12.118
1.00
24.27
A


ATOM
2115
CE2
TRP
A
347
88.841
11.803
−12.990
1.00
23.82
A


ATOM
2116
CE3
TRP
A
347
87.723
11.292
−10.897
1.00
22.42
A


ATOM
2117
CD1
TRP
A
347
88.984
9.788
−13.952
1.00
24.47
A


ATOM
2118
NE1
TRP
A
347
89.279
11.124
−14.099
1.00
23.92
A


ATOM
2119
CZ2
TRP
A
347
88.913
13.169
−12.678
1.00
21.68
A


ATOM
2120
CZ3
TRP
A
347
87.797
12.654
−10.586
1.00
24.15
A


ATOM
2121
CH2
TRP
A
347
88.391
13.575
−11.480
1.00
22.35
A


ATOM
2122
C
TRP
A
347
88.218
6.370
−10.700
1.00
30.64
A


ATOM
2123
O
TRP
A
347
87.617
6.476
−9.631
1.00
31.21
A


ATOM
2124
N
GLU
A
348
88.318
5.242
−11.376
1.00
32.16
A


ATOM
2125
CA
GLU
A
348
87.698
4.003
−10.952
1.00
34.98
A


ATOM
2126
CB
GLU
A
348
88.157
2.890
−11.904
1.00
37.47
A


ATOM
2127
CG
GLU
A
348
87.815
3.125
−13.419
1.00
41.39
A


ATOM
2128
CD
GLU
A
348
88.619
4.257
−14.116
1.00
41.83
A


ATOM
2129
OE1
GLU
A
348
89.828
4.408
−13.841
1.00
42.27
A


ATOM
2130
OE2
GLU
A
348
88.036
4.982
−14.959
1.00
42.41
A


ATOM
2131
C
GLU
A
348
87.843
3.547
−9.478
1.00
34.74
A


ATOM
2132
O
GLU
A
348
86.866
3.111
−8.869
1.00
35.95
A


ATOM
2133
N
ASN
A
349
89.024
3.652
−8.887
1.00
33.61
A


ATOM
2134
CA
ASN
A
349
89.189
3.179
−7.507
1.00
32.34
A


ATOM
2135
CB
ASN
A
349
89.936
1.860
−7.529
1.00
33.21
A


ATOM
2136
CG
ASN
A
349
91.345
2.016
−8.089
1.00
34.48
A


ATOM
2137
OD1
ASN
A
349
91.613
2.943
−8.858
1.00
32.91
A


ATOM
2138
ND2
ASN
A
349
92.247
1.110
−7.712
1.00
35.85
A


ATOM
2139
C
ASN
A
349
89.949
4.136
−6.594
1.00
31.22
A


ATOM
2140
O
ASN
A
349
90.826
3.714
−5.839
1.00
31.07
A


ATOM
2141
N
LEU
A
350
89.611
5.416
−6.646
1.00
28.54
A


ATOM
2142
CA
LEU
A
350
90.300
6.403
−5.837
1.00
26.75
A


ATOM
2143
CB
LEU
A
350
89.632
7.762
−6.024
1.00
25.89
A


ATOM
2144
CG
LEU
A
350
90.095
8.558
−7.239
1.00
24.21
A


ATOM
2145
CD1
LEU
A
350
89.111
9.674
−7.547
1.00
23.55
A


ATOM
2146
CD2
LEU
A
350
91.475
9.118
−6.932
1.00
23.67
A


ATOM
2147
C
LEU
A
350
90.440
6.102
−4.345
1.00
27.67
A


ATOM
2148
O
LEU
A
350
91.478
6.401
−3.753
1.00
28.06
A


ATOM
2149
N
HIS
A
351
89.424
5.509
−3.722
1.00
27.81
A


ATOM
2150
CA
HIS
A
351
89.539
5.254
−2.299
1.00
29.88
A


ATOM
2151
CB
HIS
A
351
88.144
5.197
−1.646
1.00
31.47
A


ATOM
2152
CG
HIS
A
351
87.584
3.823
−1.475
1.00
32.65
A


ATOM
2153
CD2
HIS
A
351
86.926
3.009
−2.338
1.00
34.75
A


ATOM
2154
ND1
HIS
A
351
87.629
3.150
−0.273
1.00
34.31
A


ATOM
2155
CE1
lHIS
A
351
87.022
1.981
−0.402
1.00
36.41
A


ATOM
2156
NE2
HIS
A
351
86.586
1.871
−1.644
1.00
35.36
A


ATOM
2157
C
HIS
A
351
90.396
4.030
−1.978
1.00
30.93
A


ATOM
2158
O
HIS
A
351
90.674
3.741
−0.812
1.00
31.57
A


ATOM
2159
N
GLN
A
352
90.842
3.337
−3.022
1.00
31.09
A


ATOM
2160
CA
GLN
A
352
91.709
2.177
−2.864
1.00
31.86
A


ATOM
2161
CB
GLN
A
352
91.482
1.187
−3.992
1.00
35.63
A


ATOM
2162
CG
GLN
A
352
91.038
0.141
−3.497
1.00
40.62
A


ATOM
2163
CD
GLN
A
352
89.739
0.036
−2.766
1.00
42.39
A


ATOM
2164
OE1
GLN
A
352
88.684
0.133
−3.376
1.00
44.19
A


ATOM
2165
NE2
GLN
A
352
89.802
0.112
−1.447
1.00
44.81
A


ATOM
2166
C
GLN
A
352
93.167
2.626
−2.907
1.00
31.39
A


ATOM
2167
O
GLN
A
352
94.030
2.022
−2.271
1.00
31.44
A


ATOM
2168
N
GLN
A
353
93.429
3.685
−3.672
1.00
29.13
A


ATOM
2169
CA
GLN
A
353
94.769
4.237
−3.813
1.00
27.37
A


ATOM
2170
CB
GLN
A
353
94.767
5.283
−4.932
1.00
25.81
A


ATOM
2171
CG
GLN
A
353
94.250
4.702
−6.242
1.00
26.68
A


ATOM
2172
CD
GLN
A
353
94.035
5.738
−7.330
1.00
26.81
A


ATOM
2173
OE1
GLN
A
353
94.792
6.709
−7.435
1.00
25.21
A


ATOM
2174
NE2
GLN
A
353
93.011
5.520
−8.171
1.00
24.24
A


ATOM
2175
C
GLN
A
353
95.288
4.851
−2.510
1.00
28.25
A


ATOM
2176
O
GLN
A
353
94.511
5.245
−1.633
1.00
28.38
A


ATOM
2177
N
THR
A
354
96.608
4.907
−2.375
1.00
28.16
A


ATOM
2178
CA
THR
A
354
97.220
5.489
−1.193
1.00
28.54
A


ATOM
2179
CB
THR
A
354
98.564
4.848
−0.889
1.00
29.50
A


ATOM
2180
OG1
THR
A
354
98.354
3.459
−0.624
1.00
31.62
A


ATOM
2181
CG2
THR
A
354
99.225
5.517
0.334
1.00
27.68
A


ATOM
2182
C
THR
A
354
97.438
6.955
−1.468
1.00
27.76
A


ATOM
2183
O
THR
A
354
98.062
7.307
−2.453
1.00
27.12
A


ATOM
2184
N
PRO
A
355
96.928
7.832
−0.592
1.00
28.37
A


ATOM
2185
CD
PRO
A
355
96.067
7.582
0.573
1.00
27.67
A


ATOM
2186
CA
PRO
A
355
97.092
9.266
−0.802
1.00
28.53
A


ATOM
2187
CB
PRO
A
355
96.215
9.883
0.291
1.00
28.29
A


ATOM
2188
CG
PRO
A
355
95.210
8.807
0.579
1.00
28.38
A


ATOM
2189
C
PRO
A
355
98.528
9.724
−0.695
1.00
28.85
A


ATOM
2190
O
PRO
A
355
99.290
9.232
0.139
1.00
29.42
A


ATOM
2191
N
PRO
A
356
98.916
10.676
−1.548
1.00
28.20
A


ATOM
2192
CD
PRO
A
356
98.083
11.340
−2.567
1.00
27.35
A


ATOM
2193
CA
PRO
A
356
100.276
11.213
−1.539
1.00
28.63
A


ATOM
2194
CB
PRO
A
356
100.261
12.199
−2.712
1.00
29.02
A


ATOM
2195
CG
PRO
A
356
98.815
12.633
−2.781
1.00
27.44
A


ATOM
2196
C
PRO
A
356
100.483
11.899
−0.195
1.00
29.18
A


ATOM
2197
O
PRO
A
356
99.543
12.505
0.331
1.00
28.80
A


ATOM
2198
N
ALA
A
357
101.689
11.806
0.368
1.00
29.69
A


ATOM
2199
CA
ALA
A
357
101.942
12.439
1.664
1.00
31.97
A


ATOM
2200
CB
ALA
A
357
103.273
11.964
2.253
1.00
29.11
A


ATOM
2201
C
ALA
A
357
101.928
13.964
1.528
1.00
33.61
A


ATOM
2202
O
ALA
A
357
102.371
14.507
0.520
1.00
33.81
A


ATOM
2203
N
LEU
A
358
101.390
14.645
2.540
1.00
36.37
A


ATOM
2204
CA
LEU
A
358
101.295
16.110
2.543
1.00
38.03
A


ATOM
2205
CB
LEU
A
358
99.995
16.554
3.209
1.00
36.49
A


ATOM
2206
CG
LEU
A
358
98.679
16.059
2.641
1.00
35.57
A


ATOM
2207
CD1
LEU
A
358
97.568
16.398
3.620
1.00
35.78
A


ATOM
2208
CD2
LEU
A
358
98.443
16.689
1.278
1.00
37.10
A


ATOM
2209
C
LEU
A
358
102.460
16.743
3.310
1.00
39.05
A


ATOM
2210
O
LEU
A
358
102.451
16.592
4.553
1.00
39.24
A


ATOM
2211
OXT
LEU
A
358
103.348
17.370
2.679
1.00
40.12
A


ATOM
2212
OH2
TIP
S
1
82.347
32.462
−3.850
1.00
16.08
S


ATOM
2213
OH2
TIP
S
4
80.761
19.051
−18.244
1.00
23.37
S


ATOM
2214
OH2
TIP
S
7
79.269
13.051
−18.353
1.00
22.32
S


ATOM
2215
OH2
TIP
S
8
86.710
32.919
−1.646
1.00
24.05
S


ATOM
2216
OH2
TIP
S
9
78.564
−0.823
16.465
1.00
28.00
S


ATOM
2217
OH2
TIP
S
10
75.323
16.274
8.538
1.00
18.43
S


ATOM
2218
OH2
TIP
S
12
78.540
24.328
−2.128
1.00
27.08
S


ATOM
2219
OH2
TIP
S
13
91.533
13.928
−17.231
1.00
22.56
S


ATOM
2220
OH2
TIP
S
14
77.419
−0.445
24.044
1.00
23.98
S


ATOM
2221
OH2
TIP
S
19
72.498
40.164
−3.114
1.00
21.78
S


ATOM
2222
OH2
TIP
S
20
77.303
13.198
−15.393
1.00
22.49
S


ATOM
2223
OH2
TIP
S
21
75.600
−1.063
22.040
1.00
24.29
S


ATOM
2224
OH2
TIP
S
22
90.133
19.697
12.606
1.00
16.61
S


ATOM
2225
OH2
TIP
S
24
74.810
7.002
25.700
1.00
20.66
S


ATOM
2226
OH2
TIP
S
27
74.894
8.778
−8.074
1.00
23.31
S


ATOM
2227
OH2
TIP
S
28
80.070
33.741
−17.170
1.00
27.29
S


ATOM
2228
OH2
TIP
S
31
74.744
21.007
3.348
1.00
29.98
S


ATOM
2229
OH2
TIP
S
32
97.930
12.301
2.472
1.00
16.75
S


ATOM
2230
OH2
TIP
S
35
78.412
7.338
3.002
1.00
16.51
S


ATOM
2231
OH2
TIP
S
36
80.172
27.171
1.300
1.00
34.66
S


ATOM
2232
OH2
TIP
S
41
69.773
3.412
17.444
1.00
24.08
S


ATOM
2233
OH2
TIP
S
43
88.878
7.904
10.616
1.00
20.34
S


ATOM
2234
OH2
TIP
S
44
87.375
32.487
−13.928
1.00
31.99
S


ATOM
2235
OH2
TIP
S
45
91.671
10.803
−16.123
1.00
35.59
S


ATOM
2236
OH2
TIP
S
46
87.637
11.564
23.703
1.00
22.67
S


ATOM
2237
OH2
TIP
S
48
93.353
28.739
3.547
1.00
32.79
S


ATOM
2238
OH2
TIP
S
50
82.283
34.597
−16.032
1.00
23.90
S


ATOM
2239
OH2
TIP
S
52
81.673
8.965
−8.348
1.00
27.83
S


ATOM
2240
OH2
TIP
S
55
94.012
3.488
1.399
1.00
24.78
S


ATOM
2241
OH2
TIP
S
58
85.735
11.257
−18.436
1.00
27.15
S


ATOM
2242
OH2
TIP
S
61
79.069
−4.638
12.345
1.00
21.04
S


ATOM
2243
OH2
TIP
S
64
103.981
17.563
−7.228
1.00
28.86
S


ATOM
2244
OH2
TIP
S
66
79.020
43.119
5.431
1.00
33.30
S


ATOM
2245
OH2
TIP
S
69
88.177
36.956
3.079
1.00
30.87
S


ATOM
2246
OH2
TIP
S
75
78.707
27.486
−3.439
1.00
25.25
S


ATOM
2247
OH2
TIP
S
79
80.347
33.345
6.422
1.00
38.57
S


ATOM
2248
OH2
TIP
S
84
64.594
19.493
24.406
1.00
26.01
S


ATOM
2249
OH2
TIP
S
98
70.215
21.980
19.413
1.00
24.75
S


ATOM
2250
OH2
TIP
S
116
103.456
14.637
−2.925
1.00
41.84
S


ATOM
2251
OH2
TIP
S
120
97.528
14.189
−14.706
1.00
43.27
S


ATOM
2252
OH2
TIP
S
128
103.602
10.418
−1.388
1.00
37.07
S


ATOM
2253
OH2
TIP
S
129
83.353
33.273
4.410
1.00
34.78
S


ATOM
2254
OH2
TIP
S
130
74.116
4.597
−3.022
1.00
27.69
S


ATOM
2255
OH2
TIP
S
131
73.104
−1.689
21.760
1.00
32.76
S


ATOM
2256
OH2
TIP
S
133
101.510
19.036
−1.083
1.00
28.30
S


ATOM
2257
OH2
TIP
S
134
65.138
6.209
20.472
1.00
27.43
S


ATOM
2258
OH2
TIP
S
135
94.509
36.623
−12.734
1.00
40.27
S


ATOM
2259
OH2
TIP
S
136
76.896
11.412
−17.698
1.00
37.17
S


ATOM
2260
OH2
TIP
S
137
97.379
7.497
−6.673
1.00
41.53
S


ATOM
2261
OH2
TIP
S
138
62.239
17.934
24.368
1.00
34.35
S


ATOM
2262
OH2
TIP
S
139
69.630
14.360
−10.771
1.00
38.17
S


ATOM
2263
OH2
TIP
S
140
84.554
44.493
−2.658
1.00
24.74
S


ATOM
2264
OH2
TIP
S
141
94.631
8.129
−9.752
1.00
35.45
S


ATOM
2265
OH2
TIP
S
142
78.415
1.021
3.883
1.00
28.60
S


ATOM
2266
OH2
TIP
S
143
99.830
12.987
−10.148
1.00
35.79
S


ATOM
2267
OH2
TIP
S
144
71.235
20.688
11.365
1.00
51.52
S


ATOM
2268
OH2
TIP
S
145
87.138
25.623
11.165
1.00
41.92
S


ATOM
2269
OH2
TIP
S
146
60.803
15.332
23.294
1.00
32.69
S


ATOM
2270
OH2
TIP
S
148
73.970
32.165
−13.455
1.00
33.99
S


ATOM
2271
OH2
TIP
S
149
88.146
19.004
17.326
1.00
27.60
S


ATOM
2272
OH2
TIP
S
150
90.803
9.970
18.127
1.00
35.03
S


ATOM
2273
OH2
TIP
S
153
86.261
32.393
−16.403
1.00
41.89
S


ATOM
2274
OH2
TIP
S
155
102.147
7.767
−0.215
1.00
38.83
S


ATOM
2275
OH2
TIP
S
159
95.238
0.811
−7.614
1.00
47.22
S


ATOM
2276
OH2
TIP
S
163
92.356
36.543
−5.580
1.00
40.19
S


ATOM
2277
OH2
TIP
S
172
66.640
4.633
22.314
1.00
29.95
S


ATOM
2278
OH2
TIP
S
176
99.303
9.124
3.136
1.00
37.07
S


ATOM
2279
OH2
TIP
S
184
104.566
20.517
−7.318
1.00
40.83
S


ATOM
2280
OH2
TIP
S
185
90.295
6.390
−15.433
1.00
34.81
S


ATOM
2281
OH2
TIP
S
186
82.626
12.831
8.023
1.00
23.99
S


ATOM
2282
OH2
TIP
S
187
86.159
18.737
24.618
1.00
32.12
S


ATOM
2283
OH2
TIP
S
188
79.867
7.010
−7.877
1.00
28.52
S


ATOM
2284
OH2
TIP
S
189
88.469
4.967
1.404
1.00
45.39
S


ATOM
2285
OH2
TIP
S
190
95.628
28.435
−17.705
1.00
31.73
S


ATOM
2286
OH2
TIP
S
191
76.228
7.822
28.547
1.00
36.76
S


ATOM
2287
OH2
TIP
S
192
85.930
8.936
23.323
1.00
31.58
S


ATOM
2288
OH2
TIP
S
193
73.669
24.555
−14.317
1.00
34.12
S


ATOM
2289
OH2
TIP
S
194
99.847
12.959
4.319
1.00
43.06
S


ATOM
2290
OH2
TIP
S
195
76.225
28.669
−3.386
1.00
38.83
S


ATOM
2291
OH2
TIP
S
197
76.955
24.214
20.057
1.00
35.16
S


ATOM
2292
OH2
TIP
S
198
65.723
11.313
28.926
1.00
38.40
S


ATOM
2293
OH2
TIP
S
199
88.482
28.463
4.472
1.00
29.21
S


ATOM
2294
OH2
TIP
S
200
71.017
17.440
−13.980
1.00
37.15
S


ATOM
2295
OH2
TIP
S
201
64.967
12.265
13.947
1.00
55.03
S


ATOM
2296
OH2
TIP
S
204
99.611
22.229
−14.818
1.00
46.97
S


ATOM
2297
OH2
TIP
S
205
65.422
−1.944
20.970
1.00
65.13
S


ATOM
2298
OH2
TIP
S
210
89.648
5.683
12.672
1.00
38.65
S


ATOM
2299
OH2
TIP
S
213
80.842
40.555
7.721
1.00
37.38
S


ATOM
2300
OH2
TIP
S
214
77.452
22.142
23.411
1.00
36.35
S


ATOM
2301
OH2
TIP
S
216
104.280
21.111
−10.347
1.00
35.15
S


ATOM
2302
OH2
TIP
S
225
84.900
44.787
−5.575
1.00
36.10
S


ATOM
2303
OH2
TIP
S
230
74.759
19.808
9.165
1.00
29.67
S


ATOM
2304
OH2
TIP
S
231
76.375
2.991
−2.919
1.00
33.34
S


ATOM
2305
OH2
TIP
S
232
97.252
36.990
−15.430
1.00
39.17
S


ATOM
2306
OH2
TIP
S
233
70.180
4.692
8.907
1.00
29.97
S


ATOM
2307
OH2
TIP
S
234
96.055
11.349
−8.926
1.00
29.40
S


ATOM
2308
OH2
TIP
S
235
70.916
31.535
4.186
1.00
53.99
S


ATOM
2309
OH2
TIP
S
236
83.279
23.905
15.245
1.00
40.79
S


ATOM
2310
OH2
TIP
S
237
90.441
34.500
3.752
1.00
37.91
S


ATOM
2311
OH2
TIP
S
238
74.369
15.521
−11.954
1.00
36.85
S


ATOM
2312
OH2
TIP
S
239
82.630
5.971
5.382
1.00
48.63
S


ATOM
2313
OH2
TIP
S
240
101.866
29.649
1.029
1.00
48.93
S


ATOM
2314
O12
GLC
G
2
74.980
15.310
28.834
1.00
58.25
G


ATOM
2315
C11
GLC
G
2
74.113
15.072
27.724
1.00
58.49
G


ATOM
2316
C13
GLC
G
2
74.885
14.362
26.609
1.00
58.11
G


ATOM
2317
O14
GLC
G
2
73.990
14.120
25.524
1.00
58.57
G


ATOM
2318
C15
GLC
G
2
75.438
13.023
27.096
1.00
57.55
G


ATOM
2319
O16
GLC
G
2
74.357
12.183
27.507
1.00
57.24
G


ATOM
2320
O12
GLC
G
3
68.191
4.312
13.268
1.00
63.76
G


ATOM
2321
C11
GLC
G
3
67.998
3.273
14.231
1.00
63.57
G


ATOM
2322
C13
GLC
G
3
69.274
2.429
14.330
1.00
64.06
G


ATOM
2323
O14
GLC
G
3
69.570
1.858
13.049
1.00
62.75
G


ATOM
2324
C15
GLC
G
3
69.094
1.303
15.364
1.00
63.85
G


ATOM
2325
O16
GLC
G
3
68.010
0.444
14.978
1.00
65.65
G


ATOM
2326
O12
GLC
G
4
87.921
37.473
−13.378
1.00
46.73
G


ATOM
2327
C11
GLC
G
4
88.767
36.757
−14.265
1.00
46.84
G


ATOM
2328
C13
GLC
G
4
90.050
36.439
−13.526
1.00
46.74
G


ATOM
2329
O14
GLC
G
4
90.660
37.648
−13.104
1.00
46.91
G


ATOM
2330
C15
GLC
G
4
90.999
35.678
−14.435
1.00
47.60
G


ATOM
2331
O16
GLC
G
4
92.193
35.413
−13.700
1.00
50.48
G


ATOM
2332
O12
GLC
G
6
78.608
8.519
28.683
1.00
42.02
G


ATOM
2333
C11
GLC
G
6
79.227
8.721
29.956
1.00
44.70
G


ATOM
2334
C13
GLC
G
6
80.218
9.877
29.849
1.00
45.13
G


ATOM
2335
O14
GLC
G
6
81.208
9.537
28.896
1.00
47.43
G


ATOM
2336
C15
GLC
G
6
80.904
10.129
31.180
1.00
46.92
G


ATOM
2337
O16
GLC
G
6
81.611
8.950
31.564
1.00
49.38
G


ATOM
2338
O12
GLC
G
8
83.278
5.163
12.485
1.00
46.74
G


ATOM
2339
C11
GLC
G
8
82.460
3.987
12.559
1.00
50.09
G


ATOM
2340
C13
GLC
G
8
83.236
2.894
13.286
1.00
50.09
G


ATOM
2341
O14
GLC
G
8
84.408
2.621
12.529
1.00
50.75
G


ATOM
2342
C15
GLC
G
8
82.412
1.597
13.414
1.00
52.04
G


ATOM
2343
O16
GLC
G
8
82.051
1.062
12.130
1.00
53.37
G


ATOM
2344
O12
GLC
G
10
87.146
4.682
−5.006
1.00
25.46
G


ATOM
2345
C11
GLC
G
10
85.823
5.086
−5.356
1.00
27.64
G


ATOM
2346
C13
GLC
G
10
85.782
5.498
−6.835
1.00
30.79
G


ATOM
2347
O14
GLC
G
10
86.689
6.600
−7.069
1.00
29.47
G


ATOM
2348
C15
GLC
G
10
84.354
5.916
−7.219
1.00
30.60
G


ATOM
2349
O16
GLC
G
10
83.947
7.022
−6.417
1.00
31.23
G


ATOM
2350
CBI
DRG
L
1
82.223
19.878
9.473
1.00
17.56
L


ATOM
2351
OBH
DRG
L
1
82.835
19.573
10.730
1.00
20.33
L


ATOM
2352
CBG
DRG
L
1
82.419
20.512
11.733
1.00
17.87
L


ATOM
2353
CBF
DRG
L
1
83.661
21.291
12.177
1.00
16.47
L


ATOM
2354
NBK
DRG
L
1
84.171
22.133
11.085
1.00
15.68
L


ATOM
2355
CBJ
DRG
L
1
83.683
23.479
10.751
1.00
12.47
L


ATOM
2356
CBE
DRG
L
1
84.739
20.294
12.600
1.00
16.76
L


ATOM
2357
CBA
DRG
L
1
84.178
19.405
13.715
1.00
18.27
L


ATOM
2358
OBB
DRG
L
1
82.790
19.632
14.017
1.00
18.03
L


ATOM
2359
CBC
DRG
L
1
81.853
19.747
12.937
1.00
18.62
L


ATOM
2360
CBD
DRG
L
1
80.732
20.611
13.524
1.00
14.59
L


ATOM
2361
NAW
DRG
L
1
81.398
18.547
12.551
1.00
18.60
L


ATOM
2362
CAX
DRG
L
1
80.185
18.344
12.014
1.00
15.55
L


ATOM
2363
CAY
DRG
L
1
79.107
19.141
11.643
1.00
13.82
L


ATOM
2364
CAZ
DRG
L
1
77.988
18.555
11.053
1.00
16.37
L


ATOM
2365
CAP
DRG
L
1
77.930
17.180
10.830
1.00
15.88
L


ATOM
2366
CAO
DRG
L
1
78.999
16.366
11.196
1.00
15.07
L


ATOM
2367
CAN
DRG
L
1
80.107
16.973
11.783
1.00
17.80
L


ATOM
2368
CAM
DRG
L
1
81.290
16.377
12.187
1.00
19.34
L


ATOM
2369
CAH
DRG
L
1
81.811
15.087
12.083
1.00
19.93
L


ATOM
2370
CAV
DRG
L
1
82.083
17.407
12.657
1.00
18.53
L


ATOM
2371
CAU
DRG
L
1
83.404
17.144
13.014
1.00
18.70
L


ATOM
2372
NAT
DRG
L
1
84.365
17.964
13.438
1.00
17.82
L


ATOM
2373
CAS
DRG
L
1
85.523
17.317
13.610
1.00
15.80
L


ATOM
2374
CAR
DRG
L
1
86.807
17.682
14.000
1.00
14.23
L


ATOM
2375
CAQ
DRG
L
1
87.803
16.708
14.047
1.00
13.92
L


ATOM
2376
CAI
DRG
L
1
87.526
15.384
13.714
1.00
16.21
L


ATOM
2377
CAJ
DRG
L
1
86.244
15.003
13.324
1.00
16.43
L


ATOM
2378
CAK
DRG
L
1
85.264
15.988
13.278
1.00
17.76
L


ATOM
2379
CAL
DRG
L
1
83.932
15.867
12.904
1.00
18.99
L


ATOM
2380
CAG
DRG
L
1
83.130
14.829
12.439
1.00
19.47
L


ATOM
2381
CAC
DRG
L
1
83.403
13.472
12.290
1.00
18.70
L


ATOM
2382
OAB
DRG
L
1
84.471
12.895
12.480
1.00
18.10
L


ATOM
2383
NAD
DRG
L
1
82.277
12.904
11.856
1.00
18.49
L


ATOM
2384
CAE
DRG
L
1
81.128
13.799
11.622
1.00
20.08
L


ATOM
2385
OAF
DRG
L
1
80.902
13.891
10.214
1.00
24.92
L


ATOM
2386
S
SO4
I
1
64.638
8.174
16.414
1.00
89.13
I


ATOM
2387
O1
SO4
I
1
65.311
9.465
16.666
1.00
88.78
I


ATOM
2388
O2
SO4
I
1
63.197
8.413
16.200
1.00
89.62
I


ATOM
2389
O3
SO4
I
1
64.827
7.262
17.566
1.00
88.49
I


ATOM
2390
O4
SO4
I
1
65.197
7.555
15.196
1.00
89.77
I


ATOM
2391
S
SO4
I
3
84.884
−1.751
12.531
1.00
81.17
I


ATOM
2392
O1
SO4
I
3
84.762
−0.302
12.775
1.00
81.32
I


ATOM
2393
O2
SO4
I
3
84.538
−2.490
13.758
1.00
81.49
I


ATOM
2394
O3
SO4
I
3
86.280
−2.053
12.162
1.00
81.73
I


ATOM
2395
O4
SO4
I
3
83.976
−2.163
11.440
1.00
81.19
I


ATOM
2396
S
SO4
I
5
74.420
22.898
12.677
1.00
85.50
I


ATOM
2397
O1
SO4
I
5
73.256
22.153
12.161
1.00
85.36
I


ATOM
2398
O2
SO4
I
5
75.637
22.104
12.412
1.00
84.51
I


ATOM
2399
O3
SO4
I
5
74.250
23.138
14.126
1.00
84.13
I


ATOM
2400
O4
SO4
I
5
74.527
24.202
11.997
1.00
85.44
I


ATOM
2401
S
SO4
I
6
68.798
6.993
−3.457
1.00
73.84
I


ATOM
2402
O1
SO4
I
6
68.338
7.338
−4.823
1.00
72.86
I


ATOM
2403
O2
SO4
I
6
69.298
8.206
−2.791
1.00
73.61
I


ATOM
2404
O3
SO4
I
6
69.888
6.003
−3.540
1.00
73.52
I


ATOM
2405
O4
SO4
I
6
67.690
6.426
−2.658
1.00
73.19
I


ATOM
2406
O2
PO4
P
100
66.501
25.721
2.616
1.00
85.98
P


ATOM
2407
O3
PO4
P
100
64.376
25.028
1.654
1.00
86.96
P


ATOM
2408
O4
PO4
P
100
65.755
26.653
0.496
1.00
86.51
P


ATOM
2409
O1
PO4
P
100
64.621
27.279
2.570
1.00
86.98
P


ATOM
2410
P
PO4
P
100
65.315
26.170
1.832
1.00
87.36
P


ATOM
2411
S
SO4
X
3
80.775
−0.045
7.874
0.50
22.29
X


ATOM
2412
O1
SO4
X
3
81.160
0.521
9.176
0.50
22.30
X


ATOM
2413
O2
SO4
X
3
81.320
−1.407
7.778
0.50
22.49
X


ATOM
2414
O3
SO4
X
3
81.309
0.781
6.777
0.50
23.26
X


ATOM
2415
O4
SO4
X
3
79.305
−0.088
7.772
0.50
24.36
X


















END

## Claims

1. A method for selecting a compound for modulating the activity of phosphoinositide dependent protein kinase 1 (PDK1), the method comprising:
[i] generating a three-dimensional structure of the protein kinase catalytic domain of PDK1 as defined by Example 2, 3, 7 or 8;
[ii] identifying predicted binding region(s): the PDK1 Interacting Fragment (PIF) binding pocket formed by residues including residues Lys115, Ile118, Ile119 on the αB helix, Val124, Val127 on the αC helix, and Leu 155 on β-sheet 5 of full length human PDK1 as set forth in SEQ ID NO: 3, the “phosphate binding pocket” formed by residues including residues Lys76, Arg131, Thr148 and Gln150 of full length human PDK1 as set forth in SEQ ID NO: 3, and/or the αC helix formed by residues 123-136 of full length human PDK1 as set forth in SEQ ID NO: 3 in any of the models generated in step [i];
[iii] modeling a plurality of three-dimensional structures of candidate compounds;
[iv] comparing said three-dimensional structure of the protein kinase catalytic domain of PDK1 binding regions/pockets as identified in step [ii] with the three-dimensional structure of each of said candidate compounds of step [iii]; and
[v] selecting one of the candidate compounds as a compound for modulating the activity of phosphoinositide dependent protein kinase 1 (PDK1).

2. The method of claim 1 wherein the three-dimensional structure of at least a part of the protein kinase catalytic domain of PDK1 structure is a three-dimensional structure (or part thereof) determined for a polypeptide consisting of residues 51 to 359 of full length human PDK1 as set forth in SEQ ID NO: 3.

3. The method of claim 2 wherein the three-dimensional structure (or part thereof) is determined for a polypeptide consisting of residues 51 to 359 of full length human PDK1 as set forth in SEQ ID NO: 3 and the amino acid sequence Gly-Pro preceding the methionine corresponding to Met51 of human PDK1.

4. The method of claim 1 wherein the three-dimensional structure of at least a part of the protein kinase catalytic domain of PDK1 structure is a three-dimensional structure (or part thereof) determined for a polypeptide consisting of residues 71 to 359 of full length human PDK1 as set forth in SEQ ID NO: 3 or a fusion thereof.

5. The method of claim 1 wherein the three-dimensional structure of at least a part of the protein kinase catalytic domain of PDK1 structure is obtainable by X-ray analysis of a crystal obtainable using a mother liquor solution comprising ammonium sulphate.

6. The method of claim 5 wherein the mother liquor solution is of pH 7 to 9.

7. The method of claim 6 wherein the mother liquor solution is of pH 8.5.

8. The method of claim 7 wherein the mother liquor solution comprises ATP.

9. The method of claim 1 wherein the compound is for modulating the protein kinase activity of PDK1 towards protein kinase B (PKB) or other pleckstrin homology (PH)-domain-comprising/phosphoinositide-binding substrate of PDK1.

10. The method of claim 1 wherein the compound is for modulating the protein kinase activity of PDK1 towards serum and glucocorticoid stimulated protein kinase (SGK), S6 kinase (S6K) or other substrate of PDK1 whose phosphorylation by PDK1 is promoted by phosphorylation of the substrate on the Ser/Thr of the “hydrophobic motif” FXXFS/TY as set forth in SEQ ID NO: 2.

11. The method of claim 1 further comprising the step of synthesising, purifying and/or formulating the compound.

12. The method of claim 1, wherein the method further comprises:
designing one or more of said molecules prior to modelling.

13. A method for selecting a compound for modulating the activity of PDK1 Interacting Fragment (PIF) binding pocket containing protein kinase, the method comprising:
[i] modeling a three-dimensional structure of a plurality of molecules in a computer;
[ii] generating a three-dimensional structure of the protein kinase catalytic domain of PDK1 as defined by Example 2, 3, 7 or 8;
[iii] comparing the three-dimensional structure of each of said molecules with the three-dimensional structure of said phosphate binding pocket of human PDK1 and optionally also said hydrophobic pocket of human PDK1;
[iv] identifying a molecule from the plurality of the modeled molecules which binds to said PIF binding pocket in the position equivalent to a hydrophobic pocket of human PDK1 that is defined by residues including Lys115, Ile118, Ile119, Val124, Val127 and Leu155 of full-length human PDK1 as set forth in SEQ ID NO: 3, and/or a phosphate binding pocket in the position equivalent to the phosphate binding pocket of human PDK1 that is defined by residues including Lys76, Arg131, Thr148 and Gln150 of SEQ ID NO: 3; and
[v] selecting one of the modeled molecules as said compound based on a predicted ability of the molecule to interact with said phosphate binding pocket of protein kinase or said hydrophobic pocket of protein kinase,
wherein the three-dimensional structure or a part thereof is determined for a polypeptide comprising residues 51 to 359 of full length human PDK1 as set forth in SEQ ID NO: 3.

14. The method of claim 13, wherein the method further comprises:
designing one or more of said molecules prior to modelling.