# Patent

## Title
Kinase inhibition models and their uses

## Abstract

The present invention provides a c-Met inhibition model. The invention further provides a method to derive inhibition models for other kinases. The kinase inhibition models of the present invention can be used to design or screen for inhibitors for kinases.

## Background
RELATED APPLICATIONS
This application is a Divisional of U.S. Ser. No. 12/221,440, filed Jul. 31, 2008, which claims the benefit of, and priority to, U.S. Ser. No. 60/962,881, filed Aug. 1, 2007. The contents of each of these applications is incorporated herein by reference in their entirety.


BACKGROUND OF THE INVENTION
Protein tyrosine kinases perform diverse functions ranging from stimulation of cell growth and differentiation to arrest of cell proliferation. They are either receptor tyrosine kinases (RTK) or intracellular tyrosine kinases. Inhibition of kinase activity is recognized as an effective way to control disease in humans.
The activation loop (A-loop) plays a key role in the activation of kinases. Many kinases switch on and off depending on the conformational state of the A-loop. The structural nature of these changes involves the phosphorylation of 1-3 residues in the A-loop, which, in turn, leads to the formation of salt bridges in the catalytic loop (C-loop) and the N-lobe. The N-lobe comprises residues from N1049 to M1160. Three important motifs are located in this lobe; the P-loop, the αC-helix and the Lys-Glu ionic pair. The precise alignment of which plays a critical role in the kinase catalytic activity. Other kinases do not require the phosphorylation of these A-loop residues to become active. It is thought that these kinases adopt a unique conformation and, as a result acidic residues in the A-loop, form a salt bridge with a conserved arginine residue in the C-loop. This allows access to the ATP binding pocket.
Upon tyrosine residue phosphorylation, the A-loop adopts a configuration optimized for substrate binding and catalysis. In many kinase structures resolved to date, the A-loop, in the phosphorylated form, adopts similar conformations to satisfy catalytic constraints and to provide a platform for substrate binding.
The activation loops in the unphosphorylated kinases exhibit a wide range of different conformations, which may explain their role in kinase activity regulation. In this unphosphorylated state, the A-loop can assume conformations ranging from fully open to completely closed (Huse, M. and Kuriyan, J. 2002. Cell 109:275-282). The open, autoinhibited, conformation has been observed in the crystal structures of fibroblast growth factor receptor (Mohammadi, M. et al. 1996. Cell, 86, 577-587) and c-Met (Wang, W. et al. 2006. Proc. Natl. Acad. Sci. USA 103:3563-3568). In this conformation of the fibroblast growth factor receptor, the A-loop is not suitable for substrate binding but does not obstruct the ATP binding site. In the closed, canonical, autoinhibited conformation, the activation loop folds as a pseudosubstrate, obstructing binding of both ATP and the peptide substrate.
The canonical, autoinhibited conformation has been detected in the unbound insulin receptor tyrosine kinase IRK, one of the most studied receptor tyrosine kinases (Hubbard, S. R. et al. 1994. Nature 372:746-754), c-Src kinase bound to the ATP analog AMP-PNP (Xu, W. et al. 1999. Molecular Cell 3:629-638), Hck bound to a small molecule inhibitor (Schindler, T. et al. 1999. Mol. Cell 3: 639-648), FLT3 receptor tyrosine kinase (Griffith, J. et al. 2004. Molecular Cell 13:69-178), c-Abl bound to Imatinib (Schindler, T. et al. 2000. Science 289, 1938-1942; Nagar, B. et al. 2002. Cancer Research 62:4236-4243), c-Kit tyrosine kinase receptor unbound and bound to Gleevec (Mol, C. D. et al. 2004. The Journal of Biological Chemistry 279:31655-31663), and more recently cFMS (colony stimulating factor receptor-1) bound to small molecule inhibitors (Schubert, C. et al. 2007. J. Biol. Chem. 282:4094-4101).
The majority of kinase inhibitors is believed to be interacting with the protein in a region which binds ATP. The conformation of the kinase, when bound by the inhibitors, is frequently very similar to the one in which ATP is bound, i.e., the active conformation of the kinase.
Typically, kinase inhibitors binding to the ATP pocket take advantage of limited sequence variations in the nucleotide binding site as well as conformational differences between phosphorylated and unphosphorylated forms of kinases. While phosphorylated forms may adopt similar conformations in different kinases, unphosphorylated, inactive conformations of kinases show great variability. Knowledge of these distinct kinase conformations allow rational drug design of high affinity, specific compounds.
A body of knowledge has given rise to the concept of ATP-competitive ligands and the use of X-ray crystallography to aid in their design. In such approaches it has become established that the ligand is required to at least in part to mimic the binding of ATP in the active site. The notion of these ligands competing for access to this site and on binding place the A-loop in a catalytically inactive conformation has been demonstrated by X-ray studies for the insulin-like receptor IGF1, IRK, cFMS, c-Abl, c-Kit, Flt3, MusK, etc.
More recently, a different type of kinase inhibitor has become known in the field. These new inhibitors appear to interact with an inactive form of the kinase in the ATP binding site. Stabilization of unphosphorylated inactive forms of RTKs provides a different approach to modulate signaling through kinases. It provides another mechanism to control over expression and non-ligand activation.
Controlling the position of the activation loop by use of small molecule inhibitors has been documented and shown by the use of X-ray crystallography. This technique provides a detailed structural insight into the mechanism by which the A-loop is prevented from achieving a catalytically active conformation. It is this technique which provides important and valuable information for the use of the design of more efficacious and selective kinase inhibitors.
In the case of the ATP-competitive ligand STI-571 binding to the inactive form of c-Abl, X-ray studies show that DFG is in the out conformation, and that the A-loop is held in an inactive conformation (Nagar, B. et al. 2002. Cancer Research 62:4236-4243).
Despite the identification of many agents which have been described to affect such control there remains a need for additional, novel and selective agents which offer the benefits of increased specificity and reduced side effects. Despite many reports, there remains a need to identify methods to inhibit the signaling through this important class of proteins.
The references cited herein are not admitted to be prior art to the claimed invention.
SUMMARY OF THE INVENTION
The invention provides a crystal structure including c-Met or c-Met kinase domain, and a ligand complexed thereto. In one aspect of the invention, the c-Met kinase domain comprises the amino acid sequence of cMet1 (SEQ ID NO: 1) from Table 1A or cMet2 (SEQ ID NO: 2) from Table 1B.
In certain embodiments of the invention, the ligand is a selective small molecule inhibitor of c-Met. In other embodiments of the invention, the inhibitor is (−)-trans-3-(5,6-dihydro-4H-pyrrolo[3,2,1-ij]quinolin-1-yl)-4(1H-indol-3-yl)pyrrolidine-2,5-dione, also known as “the selective c-Met inhibitor.”
The invention provides a process for constructing a c-Met inhibition model including the steps of crystallizing c-Met kinase domain bound to (−)-trans-3-(5,6-dihydro-4H-pyrrolo[3,2,1-ij]quinolin-1-yl)-4(1H-indol-3-yl)pyrrolidine-2,5-dione, resolving the x-ray crystallography of the c-Met kinase domain, applying the data generated from resolving the x-ray crystallography of the c-Met kinase domain to a computer algorithm, and generating from the computer algorithm a c-Met inhibition model suitable for screening or designing c-Met inhibitors. In one aspect of the invention, resolving the x-ray crystallography includes obtaining crystallographic coordinates for the c-Met kinase domain. The invention further provides a process for screening or designing c-Met inhibitors including using the c-Met inhibition model to screen or design c-Met inhibitors.
The invention provides a c-Met inhibition model including the crystallography coordinates of c-Met amino acids I—1084, G—1085, F—1089, V—1092, A—1108, V—1109, K—1110, L—1140, V—1155, L—1157, P—1158, Y—1159, M—1160, K—1161, H—1162, G—1163, D—1164, M—1211, A—1221, D—1222, F—1223, A—1226, and R—1227 (SEQ ID NO: 11) which are within about a root mean square deviation of not more than about 1.5 Å from the backbone atoms of the amino acids according to Table 4. In one aspect of the invention, the crystallography coordinates contain coordinates of all the amino acids of c-Met that are within about a root mean square deviation of not more than about 1.5 Å from the backbone atoms of the amino acids according to Table 1A or Table 1B.
The invention provides a method for making an inhibition model for a kinase including the steps of performing sequence alignment between the amino acid sequences of the kinase and c-Met using four motifs: P-loop, salt-bridge, DFG-motif and the A-loop; identifying non-conserved residues between c-Met and the kinase, replacing the crystallography coordinates of the non-conserved residues in the c-Met inhibition model with those of the corresponding residues from the kinase, and refining the c-Met inhibition model with replaced crystallography coordinates to generate the inhibition model for the kinase. In one aspect of the invention, the method for making an inhibition model for a kinase further contains the step of evaluating the inhibition model for the kinase. In certain embodiments of the invention, the kinase is a tyrosine kinase. Alternatively, or in addition, the tyrosine kinase is a receptor tyrosine kinase. An exemplary receptor tyrosine kinase is selected from the group consisting of EGFR, VEGFR, FGFR, PDGFR, HER2, Kit, IRK, RET, AXL, FLT-3, EphB4, c-Met homologs, and c-Met mutants. In one embodiment of the invention, the receptor tyrosine kinase is FGFR-2. In another embodiment of the invention, the tyrosine kinase is a non-receptor tyrosine kinase. An exemplary non-receptor tyrosine kinase is selected from the group consisting of c-Abl, Src, Fyn, Lyn, and Yes. In one embodiment of the invention, the non-receptor tyrosine kinase is c-Abl. In one aspect of the invention, the kinase is a serine/threonine kinase. An exemplary serine/threonine kinase is selected from the group consisting of B-Raf, PIM, PAK, MEK, MAPK, AKT, and Aurora kinase.
The invention provides a c-Abl inhibition model including the crystallography coordinates of c-Abl amino acids L—266, G—267, Y—271, V—274, A—287, V—288, K—289, V—317, 1331, T—333, E—334, F—335, M—336, T—337, Y—338, G—339, N—340, L—388, A—398, D—399, F—400, S—403, and R—404 (SEQ ID NO: 8) which are within about a root mean square deviation of not more than about 1.5 Å from the backbone atoms of the amino acids according to Table 5.
The invention also provides a method of similarity assessment including comparing the inhibition models of various kinases derived from the c-Met inhibition model. In one aspect of the invention, the models are compared applying a weighting system. In another aspect of the invention, the weighting system includes positive scores for residues critical for ligand binding, residues with side chain lining the inhibition model, and residues which are part of backbone of the inhibition model; and negative scores for additions, deletions and changes in backbone flexibility, or lack of residue alignment, and dramatic changes in size and/or polarity inside the inhibition model, lack of alignment of critical residues. In a further aspect of the invention, the positive score for residues critical for ligand binding is 2, for residues with side chain lining the inhibition model is 1, and for residues which are part of backbone of the inhibition model is 1; and the negative score for additions, deletions and changes in backbone flexibility, or lack of residue alignment is −1, and that for dramatic changes in size and/or polarity inside the inhibition model, lack of alignment of critical residues is −2. Alternatively, or in addition, conserved residue substitutions are assigned 1.
The invention provides a kinase inhibition model obtained by the method of making an inhibition model for a kinase as described above.
Finally, the invention provides a FGFR-2 inhibition model including the crystallography coordinates of FGFR-2 amino acids L—487, G—488, F—492, V—495, A—515, V—516, K—517, I—548, V—562, V—564, E—565, Y—566, A—567, S—568, K—569, G—570, N—571, L—633, A—643, D—644, F—645, A—648, and R—649 (SEQ ID NO: 10) which are within about a root mean square deviation of not more than about 1.5 Å from the backbone atoms of the amino acids according to Table 7.
Other features and advantages of the present invention are apparent from the additional descriptions provided herein including the different examples. The provided examples illustrate different components and methodology useful in practicing the present invention. The examples do not limit the claimed invention. Based on the present disclosure the skilled artisan can identify and employ other components and methodology useful for practicing the present invention.



BRIEF DESCRIPTION OF THE DRAWINGS
FIG. 1 is a schematic representation of the activation loop of unphosphorylated c-Met bound to the selective c-Met inhibitor (dark grey) superimposed with the peptide substrate (light grey) as seen in the phosphorylated insultin receptor IRK in complex with ATP and a peptide (Tyr residues are shown as sticks).
FIG. 2 is a schematic representation of the c-Met kinase domain, in which the activation loop is shown in the canonical, autoinhibitory, conformation forming a typical short anti-parallel strand.
FIG. 3 is a schematic representation of unphosphorylated c-Met bound to the selective c-Met inhibitor, in which Arg 1227 forms part of the inhibitor's binding site (dark grey).
FIG. 4 is a schematic representation of unphosphorylated c-Met bound to the selective c-Met inhibitor, in which a salt bridge, usually formed by the strictly conserved Lys (β3) and Glu (αC) residues that stabilize the phosphate group transfer, is disrupted as a result of the conformational changes of the A-loop and the helix αC.



DETAILED DESCRIPTION OF THE INVENTION
The present invention relates to methods of designing and screening for kinase inhibitors. The present invention provides a c-Met inhibition model. The present invention further provides a method to derive an inhibition model for another kinase from the c-Met inhibition model. The present invention also provides a method to compare inhibition models derived from multiple kinases in order to determine the degree of similarity between inhibition models.
The receptor tyrosine kinase (RTK) c-Met belongs to the HGF receptor family, which includes tyrosine kinases encoded by three oncogenes: MET (mesenchymal-epithelial transition factor), RON (also known as MST1R, macrophage stimulating 1 receptor (c-met-related tyrosine kinase)), and SEA (S13 erythroblastosis oncogene homolog (avian)).
These RTKs share specific structural features: a heterodimeric α-β subunits, two neighboring tyrosine residues in the kinase domain responsible for the activation upon phosphorylation and two tyrosine docking sites in the C-terminal domain tail.
The extracellular α- and transmembrane-β chains are present after receptor proteolitic cleavage and linked together by disulfide bonds. The intracellular β-subunit (residues 956-1390) can be further divided into juxtamembrane (residues 956-1093), catalytic and C-terminal domains. The C-terminal docking sites mediate high affinity interactions with multiple SH2-containing transducers of several key signaling pathways, including Ras, MAPK, PI3K, Src and Stat3 which contribute to the malignant features of Met.
Ligand binding to the extracellular domain of the RTKs leads to dimerization of monomeric receptors resulting in autophosphorylation of specific tyrosine residues in the cytoplasmic domain. RTKs are subject to several auto regulatory mechanisms to limit ligand-independent activation. One of these mechanisms is the phosphorylation of the kinase activation loop. The tyrosine doublet is present at homologous locations in the A-loop in RON and SEA.
The structure of the unphosphorylated kinase domain of c-Met bound to the selective c-Met inhibitor is an example of how a small molecule can achieve specificity by recognizing and binding the canonical, autoinhibited form of the kinase. Herein we describe a novel mechanism of inhibition of the receptor tyrosine kinase (RTK) c-Met and its use to define an inhibition model of general application in the identification of novel kinase inhibitors.
1. The Structure of the c-Met Bound to the Selective c-Met Inhibitor
(−)-trans-3-(5,6-dihydro-4H-pyrrolo[3,2,1-ij]quinolin-1-yl)-4(1H-indol-3-yl)pyrrolidine-2,5-dione is a selective c-Met inhibitor (WO 2006/086484 A1).




A 2-Å resolution X-ray crystallographic shows that this compound binds to the unphosphorylated kinase domain of c-Met. This compound is referred to herein as “the selective c-Met inhibitor.”
The selective c-Met inhibitor is a single enantiomer that binds unphosphorylated c-Met at the highly conserved nucleotide-binding pocket. Overall the c-Met structure resembles the structures resolved for other tyrosine kinases in the presence of inhibitors such as Gleevec bound to c-Abl kinase and small molecules bound to cFMS. Structures of other receptor tyrosine kinases such as insulin receptor, cKit, Flt-3 in the absence of ligands also share a similar fold. In all these structures the activation loop is in the canonical, autoinhibitory conformation, blocking the access of ATP and the peptide substrate to the active site. In this particular conformation a tyrosine residue is in a pseudosubstrate conformation, buried deeply into the protein, making hydrogen bonds with important residues in the catalytic loop.
The structure of the c-Met bound to the selective c-Met inhibitor was compared with the inactive structure of c-Met in the public domain (PDB entry 2G15). In this structure, Tyr 1234 is not available for phosphorylation. The A-loop is in a different, open conformation. It is possible that the selective c-Met inhibitor recognizes and binds this particular, autoinhibitory conformation of c-Met, as it has been suggested for Gleevec bound to c-Abl and c-Kit kinases.
1.1. P-Loop Contains a Phenylalanine or a Similar Residue Able to Form Stacking Interaction with the Ligand
Another important structural motif of a kinase is the phosphate binding loop (P-loop). This loop contains a conserved glycine residue rich sequence (GXGXΦG), where Φ is usually a tyrosine or phenylalanine. The glycine residues allow the coordination of the ATP by well defined backbone interactions. In the absence of ATP, the P-loop is very flexible allowing the binding of small molecules. Some inhibitors stabilize this loop by interacting with the conserved aromatic residue, as is the case of crystal structures of Abl, FGFR in complex with inhibitors STI-571 (PDB entry 2HYY), SU-5402 (PDB entry 1FGI), and unphosphorylated c-Met bound to the selective c-Met inhibitor.
The nucleotide binding loop, the P-loop is well ordered in the structure of c-Met bound to the selective c-Met inhibitor, where residues 11084 to G1087 form part of the β1 strand. F1089 stabilizes the downfold of the loop by van de Waals contacts with the selective c-Met inhibitor.
1.2. A Tyrosine Residue in the A-Loop is Able to Interfere with the Peptide Substrate Binding
Autophosphorylation of key tyrosine residues in the catalytic core of the RTK enhances kinase activity. In the case of c-Met, Y1235 has been described as being the site of autophosphorylation and playing this regulatory role.
In the structure of c-Met bound to the selective c-Met inhibitor, the activation loop is in the canonical, autoinhibitory conformation with a short anti-parallel strand. Two tyrosine residues Y1234 and Y1235 located in the A-loop of the kinase domain are responsible for c-Met catalytic activity and in the structure of c-Met bound to the selective c-Met inhibitor, Y1234 is exposed. However, Y1235 is sequestered into the active site occupying the site of the substrate tyrosine. Un-phosphorylated Y1235 is held by a hydrogen bond network formed by catalytic loop (C-loop) D1204 and R1208. The arginine residue engages in hydrogen bonding interactions that orient asparagine ensuring the inaccessibility of Y1235.
1.3. Phenylalanine (of the DFG Motif which Consists of Residues D1222, F1223 and G1224 in the Activation Loop) Prevents the ATP Binding
Most of our knowledge about RTK comes from structural and biochemical studies on the insulin receptor kinase IRK. Structures of IRK show that sequestration of the tyrosine residue in the active site is correlated with the movement away from the active site of a number of critical important residues. When the apo structure (DFG-out) is superposed with the phosphorylated IRK (DFG-in) in complex with ATP analog and a peptide substrate (PDB entry 1RK3) the side chain of F1151 occupies the pocket of the adenine ring and the activation loop intersects the β- and γ-phosphate groups.
The positioning of phenylalanine from the DFG motif is critical for the proper orientation of the aspartic acid (DFG) which coordinates an essential Mg2+ and the ATP. Conformational changes of the DFG-motif are often linked to the conformation of the αC-helix, the only conserved helix in the β sheet-rich N terminal domain. An absolute conserved glutamic acid residue located in αC-helix forms an ion pair with another conserved lysine residue from the β3 sheet. This ion pair coordinates the α- and β-phosphates of the ATP.
In the structure of c-Met bound to the selective c-Met inhibitor, a ‘DFG-out’ conformation is present. The aspartic acid (of the DFG) points away from where the ATP would bind and phenylalanine is situated in the approximated position of the ATP adenine moiety. Stabilization of this portion of the A-loop is provided, in part, by the tricyclic group of the selective c-Met inhibitor, which makes van der Waals interactions with the phenylalanine residue from the DFG motif. In this way, although the hydroxyl group of Y1234 is in position for phospho-transfer, the DFG-out motif occludes the ATP binding site from interfering with phopho-transfer.
1.4. The Salt Bridge Between Lysine (N-Terminus) and Glutamic Acid (αC Helix) is Disrupted
The αC helix is a key regulatory element of protein kinases. Due to its proximity to the active site and its interactions with many conserved and essential kinase elements, the orientation of this helix is critical for catalytic activity. This helix contains a conserved glutamic acid residue that forms an ion pair with a lysine residue from the N-lobe. Glutamic acid is a strictly conserved feature in the kinase family and lysine is part of the protein kinase ATP binding region signature (PROSITE rule PS00107). The lysine residue coordinates the α- and the β-phosphates of ATP and is required for kinase activity. Moreover, the αC helix often interacts with the DFG motif of the activation loop.
In the structure of c-Met bound to the selective c-Met inhibitor, the alignment of the lysine-glutamic acid ion pair is disrupted, K1110 and E1127 are 16 Å apart, accentuating the inactive nature of the c-Met kinase conformation in the presence of the selective c-Met inhibitor.
When the αC helix of the complex formed by c-Met bound to the selective c-Met inhibitor is compared to the fully activated IRK structure bound to ATP and a peptide substrate, it is clear that the αC helix is partially disrupted and shifted away from the N-lobe. This movement, which is a combination of rotation and translation, results from the insertion of the activation loop deep between the P-loop and the αC helix.
In the structure formed by the complex formed when c-Met is bound to the selective c-Met inhibitor, the β3-αC loop has several contacts with the activation loop that are not observed in apo c-Met. R1114 from the β3-αC loop makes two contacts with the activation loop: R1114 forms salt bridges with G1224 from the DFG motif and with the carbonyl oxygen of R1227. In the structure of the apo c-Met kinase domain, the β3-αC loop adopts a more open conformation because the side chain of R1114 extends in the opposite direction towards the solvent.
An additional important feature of the activation loop is the conformation of R1227. It is hypothesized that R1227 plays a critical role in the stabilization of the activation loop by hydrogen bonding to the activated tyrosine upon phosphorylation (Johnson, L. M. and Noble, M. E. M. 1996. Cell, 85: 149-158). Three structures are often used to illustrate this interaction. First, the fully activated, triple phosphorylated insulin receptor kinase when bound to ATP and a peptide (1IR3). In this instance, the equivalent residue to R1227 in c-Met, residue R1155, makes hydrogen bonds with the phosphate group of Y1163. Second, a similar role has been described for R387 in the active form of the Hck tyrosine kinase (3LCK). With respect to Hck, R387 is making a hydrogen bond with the phosphorylated Y394. Finally, residue K189 of the serine/threonine kinase PKA bound to balanol (1BX6) fulfills a similar role. Using the foregoing examples as evidence, it is assumed that a critical role for R1227 is providing stabilization to the activation loop upon phosphorylation of c-Met.
The structures provided herein are contrary to published structures. For instance, in recently published structures of c-Met bound to small molecule inhibitors, the side chain of R1227 is missing (Bellon, S. F. ET AL. 2008. J. Biol. Chem. 283: 2675-2683; Albrecht, B. K. ET AL. 2008. J. Med. Chem. 51: 2879-2882). Similarly, in the structure of human Abl bound to Gleevec, the corresponding residue R386 is also missing (Cowan-Jacob, S. W. et al. 2007. ACTA CRYSTALLOGR., SECT. D 63: 80-93).
However, in the structure of the complex of c-Met bound to the selective c-Met inhibitor provided herein, R1227 is locked away from Y1234 and Y1235 through a direct hydrogen bond with N1209 and a water-mediated hydrogen bond to R1208, presenting the hydrophobic chain to the inhibitor. This van der Waals contact with the selective c-Met inhibitor restricts the movement of R1227 and prevents phosphate stabilization upon activation. Such a conformational change of this part of the activation loop, brought about by the selective c-Met inhibitor, is similar to that described for the activation loop containing R801 and a small molecule inhibitor of the autoinhibited cFMS (Schubert, C. ET AL. 2007. J. Biol. Chem. 282:4094-4101), the R815 residue of apo c-Kit bound to Gleevec (Mol, C. D. ET AL. 2004. The Journal of Biological Chemistry 279:31655-31663), and the R834 residue of apo Flt-3 (Griffith, J. ET AL. 2004. Molecular Cell 13:69-178).
1.5. A Small Molecule is Stabilizing 1-4, Preventing ATP and Peptide Binding
In the structure of c-Met bound to the selective c-Met inhibitor, the small molecule is placed in the interdomain cleft between the N (residues 1049-1160)- and C-lobes (residues 1161-1346). The carbonyl group from the succinamide ring forms hydrogen bond with the backbone amide of M1160 and the N—H group forms hydrogen bonds with the backbone carbonyl of P1158. The indole ring is close to the ATP binding site opening while the tricyclic ring is bound deep inside the hydrophobic pocket. The tricyclic moiety of the selective c-Met inhibitor forms van der Waals interactions with phenylalanine residues F1089 from the P-loop and F1223 from the DFG motif. European Patent Application No. EP1243596A2 (the contents of which are incorporated herein in their entirety) describes a small molecule bound to the kinase domain of c-Met. The structure of c-Met bound to the selective c-Met inhibitor differs significantly. Of particular note are differences in the P-loop and the A-loops. The selective c-Met inhibitor makes a van de Waals contact with the residue F1089 at the apex of the P-loop, F1089 of cMet (described in EP1243596A2, the contents of which are incorporated by reference in their entirety) is inserted towards the αC helix. Also of note are differences between the residue F1223. This residue is in the -out conformation while in the above mentioned patent it is in the -in conformation. The selective c-Met inhibitor prevents this residue from occupying a region close to the triphosphate binding site found when ATP binds the catalytic site.
1.6. Computers, Computer Software, Computer Modeling
Computers are known in the art and may include a central processing unit (CPU), a working memory, which can be random-access memory, core memory, mass-storage memory, or combinations of all of the aforementioned.
The CPU may encode one or more programs. Computers may also include display, and input and output devices, such as one or more cathode-ray tube display terminals, keyboards, modems, input lines and output lines. Persons skilled in the computer art will understand that many variations of a computer exist in the art and all such variations are applicable to the present invention. Further, said computers may be networked to computer servers (the machine on which large calculations can be run in batch), and file servers (the main machine for all the centralized databases). Machine-readable media containing data, such as the crystal structure coordinates of the polypeptides of the invention may be inputted using various hardware, including modems, CD-ROM drives, disk drives, or keyboards
Output hardware, such as a CRT display terminal may be used for displaying a graphical representation of the HGFR polypeptide of the invention or the c-Met substrate-binding domain of these polypeptides using programs such as QUANTA. Output hardware may also include a printer, and disk drives.
The CPU coordinates the use of the various input and output devices, coordinates data accesses from storage and accesses to and from working memory, and determines the sequence of data processing steps. A number of programs may be used to process the machine-readable data of this invention. Such programs are discussed in reference to the computational methods of drug discovery as described herein.
Thus, one embodiment of the present invention includes X-ray coordinate data capable of being processed into a three dimensional graphical display of a molecule or molecular complex that comprises an c-Met-like substrate-binding pocket stored in a machine-readable storage medium. The three-dimensional structure of a molecule or molecular complex comprising an c-Met-like substrate-binding pocket may be used for a variety of purposes, including, but not limited to, drug discovery.
For example, the three-dimensional structure derived from the structure coordinate data may be computationally evaluated for its ability to associate with chemical entities. Such entities would be potential drug candidates and would be evaluated for their ability to inhibit or modulate the activity of c-Met.
As used herein, the term “three dimensional representation” refers to converting the lists of structure coordinates into structural models or graphical representation in three-dimensional space. The three dimensional structure may be displayed or used to perform computer modeling or fitting operations.
“Inhibition model”, refers to a region or regions of proteins that can associate with another chemical entity or compound. Such regions are of significant utility in fields such as drug discovery. These regions are formed by amino acid residues key for ligand binding or may be residues that are spatially related and define a three-dimensional shape of the binding pocket. The amino acid residues may be contiguous or non-contiguous in primary sequence. The region or regions may be embodied as a dataset (e.g. an array) recorded on computer readable media.
The term “motif” refers to a group of amino acid residues in proteins that defines a structural compartment or carries out a function in the protein, for example, catalysis, structural stabilization or phosphorylation. The motif may be conserved in sequence, structure and function. The motif can be contiguous in primary sequence or three-dimensional space. Examples of a motif include, but are not limited to, a binding pocket; activation loop, the glycine-rich or P-loop, and the DFG loop.
The term “homology model” refers to a set of coordinates derived from known three-dimensional structure used as a template. Generation of the homology model, termed “homology modeling”, involves sequence alignment, residue replacement, residue conformation adjustment through energy minimization
The term “part of the inhibition model” also referred as “part of a binding pocket” refers to less than all of the amino acid residues that define the binding pocket. The structure coordinates of amino acid residues that constitute part of a binding pocket may be specific for defining the chemical environment of the binding pocket, or useful in designing fragments of an inhibitor that may interact with those residues. Part of the inhibition model has at least five amino acid residues, preferably at least, ten to fourteen amino acid residues.
The term “chemical entity” refers to chemical compounds, complexes of at least two chemical compounds, and fragments of such compounds or complexes.
The “Chemical structure” term is applied to any atom or group of atoms that constitute a part of a molecule. Normally, chemical structures of a scaffold or ligand have a role in binding to a target molecule.
The term “associating with” or “binds to” or “binding affinity” refers to a condition of proximity between a chemical entity or compound, or portions thereof, and the inhibition model, or binding pocket or binding site on a protein. The association may be non-covalent, for example, wherein the juxtaposition is energetically favored by hydrogen bonding, van der Waals and/or electrostatic interactions
The term “interaction energy” refers to the energy determined for the interaction of a chemical entity and a binding pocket, domain, molecule or molecular complex or portion thereof, Interactions include but are not limited to one or more of covalent interactions, non-covalent interactions such as hydrogen bond, electrostatic, hydrophobic, aromatic, van der Waals interactions, and non-complementary electrostatic interactions such as repulsive charge-charge, dipole-dipole and charge-dipole interactions. As interaction energies are measured in negative values, the lower the value the more favorable the interaction.
For the purposes of this description and the following claims, the term “crystal structure” of a composition shall mean a computer readable medium in which is stored a representation of three dimensional positional information for atoms of the composition.
2.1 Construction of c-Met Inhibition Model
The model for the inhibition of c-Met kinase is constructed by the preparation of the 3-dimensional representation of the c-Met protein based on crystallographic structure of c-Met bound to the selective c-Met inhibitor complex.
An electronic representation of c-Met-ligand kinase domain structure was obtained from X-ray crystallographic data. Crystals of the ligand complexes of c-Met kinase can be grown by a number of techniques including batch crystallization, vapor diffusion (either by sitting drop or hanging drop) and by microdialysis. Seeding of the crystals in some instances is required to obtain X-ray quality crystals. Standard micro and/or macro seeding of crystals may therefore be used.
Once a crystal of the present invention is grown, X-ray diffraction data can be collected. X-ray diffraction data collection can be obtained using, for example, a MAR imaging plate detector. Crystals can be characterized by using X-rays produced in a conventional source (such as a sealed tube or a rotating anode) or using a synchrotron source.
Data processing and reduction can be carried out using programs such as HKL, DENZO, and SCALEPACK (Otwinowski and Minor, 1997, Meth. Enymol. 276:307-326 (1997)). In addition, X-PLOR, (Bruger, X-PLOR v.3.1 Manual, New Haven: Yale University, (1993)) or Heavy (T. Terwilliger, Los Alamos National Laboratory) may be utilized for bulk solvent correction and B-factor scaling. Electron density maps can be calculated using SHARP (La Fortelle, E. D. and Bricogne G., Meth. Enzymol. 276:472-494 (1997)) and SOLOMON. Molecular models can be built into this map using O (Jones, T. et al., ACTA Crystallogr. A47:110-119 (1991)), XTALVIEW (Scripps Research) or QUANTA96 (Accelrys, Inc. San Diego). Refinement can be done using XPLOR (Brunger, “X-PLOR:A System for X-ray Crystallography and NMR,” Yale University Press, New Haven, Conn.), using the free R-value to monitor the course of refinement. Molecular replacement involves using a known three-dimensional structure as a search model to determine the structure of an identical or closely related molecule or protein-ligand complex in a new crystal form. The measured X-ray diffraction properties of the new crystal are compared with those calculated from a search model structure to compute the position and orientation of the protein in the new crystal. Computer programs that can be used for this purpose include: X-PLOR, EPMR (Kissinger et al. Acta Cryst. D55:484-491 (1999)), ProLSQ and AMORE (J. Navaza, Acta Crystrallographics ASO, 157-163 (1994)). Once the position and orientation are known an electron density map can be calculated using the search model to provide X-ray phases. Thereafter, the electron density is inspected for structural differences and the search model is modified to conform to the new structure. Other computer programs that can be used to solve the structures of kinase crystals include X-site, QUANTA, INSIGHT, ARP/wARP, and ICM.
The amino acids of the kinase domain of c-Met1 bound to the selective c-Met inhibitor are described herein and are defined by a set of structure coordinates set forth in Table 1A. The amino acids of the kinase domain of c-Met2 bound to the selective c-Met inhibitor are described herein and are defined by a set of structure coordinates set forth in Table 1B. The terms “structure coordinates” or “atomic coordinates” refer to Cartesian coordinates derived from mathematical equations related to the patterns obtained on diffraction of a monochromatic beam of X-rays by the atoms (scattering centers) of a protein or protein-ligand complex in crystal form. The diffraction data are used to calculate an electron density map of the repeating unit of the crystal. The electron density maps are then used to establish the positions of the individual atoms of the enzyme or enzyme complex.







TABLE 1A





(SEQ ID NO: 1)
























ATOM
1
CB
LEU
A1046
−12.128
23.172
12.578
56.91
C


ATOM
2
CG
LEU
A1046
−10.61
22.897
12.417
57.12
C


ATOM
3
CD1
LEU
A1046
−10.172
21.715
13.29
57.11
C


ATOM
4
CD2
LEU
A1046
−10.196
22.666
10.944
56.48
C


ATOM
5
C
LEU
A1046
−11.878
25.227
14.012
55.44
C


ATOM
6
O
LEU
A1046
−11.778
26.019
13.032
55.74
O


ATOM
7
N
LEU
A1046
−14.148
24.094
13.796
56.63
N


ATOM
8
CA
LEU
A1046
−12.645
23.903
13.852
56.54
C


ATOM
9
N
LEU
A1047
−11.331
25.48
15.21
53.3
N


ATOM
10
CA
LEU
A1047
−10.406
26.598
15.301
50.4
C


ATOM
11
CB
LEU
A1047
−10.5
27.402
16.574
51.71
C


ATOM
12
CG
LEU
A1047
−10.362
28.806
15.979
51.83
C


ATOM
13
CD1
LEU
A1047
−11.47
28.957
14.891
53.47
C


ATOM
14
CD2
LEU
A1047
−10.363
29.918
17.042
52
C


ATOM
15
C
LEU
A1047
−8.96
26.289
14.95
48.45
C


ATOM
16
O
LEU
A1047
−8.275
25.497
15.594
48.01
O


ATOM
17
N
GLN
A1048
−8.562
26.995
13.891
44.96
N


ATOM
18
CA
GLN
A1048
−7.335
26.9
13.179
40.88
C


ATOM
19
CB
GLN
A1048
−7.455
25.718
12.207
42.63
C


ATOM
20
CG
GLN
A1048
−7.818
25.972
10.72
41.6
C


ATOM
21
CD
GLN
A1048
−6.669
25.468
9.808
44.09
C


ATOM
22
OE1
GLN
A1048
−5.912
26.261
9.217
39.73
O


ATOM
23
NE2
GLN
A1048
−6.52
24.143
9.728
46.71
N


ATOM
24
C
GLN
A1048
−7.28
28.319
12.517
38.85
C


ATOM
25
O
GLN
A1048
−6.273
28.777
11.876
36.37
O


ATOM
26
N
ALA
A1049
−8.408
29.017
12.748
35.35
N


ATOM
27
CA
ALA
A1049
−8.506
30.471
12.686
31.97
C


ATOM
28
CB
ALA
A1049
−9.981
30.902
12.748
31.67
C


ATOM
29
C
ALA
A1049
−7.691
30.943
13.89
29.81
C


ATOM
30
O
ALA
A1049
−7.868
32.004
14.431
29.2
O


ATOM
31
N
THR
A1050
−6.732
30.11
14.251
27.92
N


ATOM
32
CA
THR
A1050
−5.889
30.248
15.41
26.75
C


ATOM
33
CB
THR
A1050
−6.401
29.283
16.498
27.8
C


ATOM
34
OG1
THR
A1050
−5.967
29.726
17.75
29.58
O


ATOM
35
CG2
THR
A1050
−5.908
27.822
16.32
31.14
C


ATOM
36
C
THR
A1050
−4.448
29.924
15.044 
24.25
C


ATOM
37
O
THR
A1050
−3.59
30.157
15.797
24.4
O


ATOM
38
N
VAL
A1051
−4.212
29.439
13.836
23.39
N


ATOM
39
CA
VAL
A1051
−2.877
28.99
13.358
22.24
C


ATOM
40
CB
VAL
A1051
−2.947
27.788
12.359
20.45
C


ATOM
41
CG1
VAL
A1051
−1.579
27.485
11.875
18.55
C


ATOM
42
CG2
VAL
A1051
−3.595
26.532
13.011
19.38
C


ATOM
43
C
VAL
A1051
−2.1
30.118
12.657
22.8
C


ATOM
44
O
VAL
A1051
−2.522
30.662
11.621
22.92
O


ATOM
45
N
HIS
A1052
−0.978
30.488
13.223
22.7
N


ATOM
46
CA
HIS
A1052
−0.228
31.494
12.584
23.68
C


ATOM
47
CB
HIS
A1052
−0.265
32.834
13.364
22.38
C


ATOM
48
CG
HIS
A1052
0.836
33.742
12.975
22.43
C


ATOM
49
CD2
HIS
A1052
2.061
33.943
13.536
27.19
C


ATOM
50
ND1
HIS
A1052
0.821
34.463
11.794
19.13
N


ATOM
51
CE1
HIS
A1052
1.969
35.092
11.658
24.7
C


ATOM
52
NE2
HIS
A1052
2.74
34.811
12.711
28.02
N


ATOM
53
C
HIS
A1052
1.174
30.932
12.455
24.4
C


ATOM
54
O
HIS
A1052
1.745
30.455
13.427
24.15
O


ATOM
55
N
ILE
A1053
1.716
30.972
11.242
26.45
N


ATOM
56
CA
ILE
A1053
3.121
30.613
11.024
27.16
C


ATOM
57
CB
ILE
A1053
3.251
29.516
9.914
28.26
C


ATOM
58
CG2
ILE
A1053
4.734
29.093
9.685
26.49
C


ATOM
59
CG1
ILE
A1053
2.359
28.302
10.239
29.2
C


ATOM
60
CD1
ILE
A1053
2.763
27.523
11.503
29.05
C


ATOM
61
C
ILE
A1053
3.87
31.843
10.573
27.98
C


ATOM
62
O
ILE
A1053
3.477
32.505
9.609
28.95
O


ATOM
63
N
ASP
A1054
4.961
32.165
11.241
29.63
N


ATOM
64
CA
ASP
A1054
5.824
33.221
10.723
31.12
C


ATOM
65
CB
ASP
A1054
6.616
33.903
11.853
31.79
C


ATOM
66
CG
ASP
A1054
7.232
35.248
11.435
33.67
C


ATOM
67
OD1
ASP
A1054
7.123
35.707
10.245
31.69
O


ATOM
68
OD2
ASP
A1054
7.858
35.842
12.343
36.33
O


ATOM
69
C
ASP
A1054
6.716
32.541
9.714
31.2
C


ATOM
70
O
ASP
A1054
7.551
31.707
10.089
30.57
O


ATOM
71
N
LEU
A1055
6.476
32.851
8.443
33.07
N


ATOM
72
CA
LEU
A1055
7.198
32.223
7.316
35.79
C


ATOM
73
CB
LEU
A1055
6.468
32.463
5.965
35.66
C


ATOM
74
CG
LEU
A1055
5.094
31.724
5.872
35.17
C


ATOM
75
CD1
LEU
A1055
4.42
31.654
4.439
30.21
C


ATOM
76
CD2
LEU
A1055
5.19
30.345
6.57
30.42
C


ATOM
77
C
LEU
A1055
8.702
32.622
7.259
37.77
C


ATOM
78
O
LEU
A1055
9.593
31.826
6.823
38.16
O


ATOM
79
N
SER
A1056
8.996
33.842
7.712
38.44
N


ATOM
80
CA
SER
A1056
10.361
34.138
8.058
39.83
C


ATOM
81
CB
SER
A1056
10.53
35.611
8.209
39.82
C


ATOM
82
OG
SER
A1056
11.807
35.884
7.633
46.45
O


ATOM
83
C
SER
A1056
10.692
33.399
9.366
39.54
C


ATOM
84
O
SER
A1056
9.778
32.908
10.012
40.79
O


ATOM
85
N
ALA
A1057
11.954
33.251
9.762
38.82
N


ATOM
86
CA
ALA
A1057
12.222
32.456
10.987
38.37
C


ATOM
87
CB
ALA
A1057
11.15
32.739
12.058
38.35
C


ATOM
88
C
ALA
A1057
12.288
30.949
10.736
38.3
C


ATOM
89
O
ALA
A1057
12.676
30.15
11.618
37.56
O


ATOM
90
N
LEU
A1058
11.81
30.567
9.554
38.37
N


ATOM
91
CA
LEU
A1058
11.986
29.242
9.036
38.18
C


ATOM
92
CB
LEU
A1058
11.113
29.053
7.79
38.51
C


ATOM
93
CG
LEU
A1058
9.756
28.341
7.928
37.27
C


ATOM
94
CD1
LEU
A1058
9.136
28.263
6.541
35.77
C


ATOM
95
CD2
LEU
A1058
9.864
26.954
8.632
34.79
C


ATOM
96
C
LEU
A1058
13.445
29.182
8.652
38.37
C


ATOM
97
O
LEU
A1058
13.942
30.156
8.091
36.78
O


ATOM
98
N
ASN
A1059
14.11
28.051
8.952
39.31
N


ATOM
99
CA
ASN
A1059
15.505
27.793
8.556
40.53
C


ATOM
100
CB
ASN
A1059
15.835
26.343
8.802
41.11
C


ATOM
101
CG
ASN
A1059
17.226
25.977
8.342
45.43
C


ATOM
102
OD1
ASN
A1059
17.992
25.369
9.092
51.44
O


ATOM
103
ND2
ASN
A1059
17.569
26.327
7.112
49.14
N


ATOM
104
C
ASN
A1059
15.768
28.158
7.071
41.05
C


ATOM
105
O
ASN
A1059
15.198
27.542
6.158
40.67
O


ATOM
106
N
PRO
A1060
16.577
29.206
6.827
41.31
N


ATOM
107
CD
PRO
A1060
17.241
30.03
7.84
41.79
C


ATOM
108
CA
PRO
A1060
16.835
29.7
5.483
41.66
C


ATOM
109
CB
PRO
A1060
17.753
30.888
5.721
42.18
C


ATOM
110
CG
PRO
A1060
17.385
31.301
7.127
43.84
C


ATOM
111
C
PRO
A1060
17.483
28.659
4.578
41.37
C


ATOM
112
O
PRO
A1060
17.289
28.689
3.372
40.14
O


ATOM
113
N
GLU
A1061
18.217
27.727
5.17
41.83
N


ATOM
114
CA
GLU
A1061
18.738
26.625
4.399
42.84
C


ATOM
115
CB
GLU
A1061
19.811
25.863
5.194
44.84
C


ATOM
116
CG
GLU
A1061
21.075
25.53
4.347
48.59
C


ATOM
117
CD
GLU
A1061
21.714
26.811
3.785
53.07
C


ATOM
118
OE1
GLU
A1061
21.973
27.726
4.605
55.39
O


ATOM
119
OE2
GLU
A1061
21.919
26.916
2.539
55.02
O


ATOM
120
C
GLU
A1061
17.627
25.663
3.957
41.97
C


ATOM
121
O
GLU
A1061
17.714
25.019
2.895
42.05
O


ATOM
122
N
LEU
A1062
16.596
25.539
4.785
39.78
N


ATOM
123
CA
LEU
A1062
15.602
24.545
4.529
37.71
C


ATOM
124
CB
LEU
A1062
14.842
24.154
5.797
37.57
C


ATOM
125
CG
LEU
A1062
13.492
23.442
5.605
38.39
C


ATOM
126
CD1
LEU
A1062
13.118
22.609
6.804
41.69
C


ATOM
127
CD2
LEU
A1062
12.386
24.433
5.387
38.42
C


ATOM
128
C
LEU
A1062
14.701
25.111
3.449
36.6
C


ATOM
129
O
LEU
A1062
14.26
24.355
2.556
35.41
O


ATOM
130
N
VAL
A1063
14.492
26.43
3.493
34.92
N


ATOM
131
CA
VAL
A1063
13.566
27.111
2.567
34.29
C


ATOM
132
CB
VAL
A1063
13.244
28.526
3.087
34.3
C


ATOM
133
CG1
VAL
A1063
12.661
28.432
4.463
34.16
C


ATOM
134
CG2
VAL
A1063
14.486
29.41
3.087
33.47
C


ATOM
135
C
VAL
A1063
14.00
527.153
1.079
34.81
C


ATOM
136
O
VAL
A1063
13.196
27.221
0.151
33.36
O


ATOM
137
N
GLN
A1064
15.317
27.136
0.839
36.44
N


ATOM
138
CA
GLN
A1064
15.766
27.189
−0.531
36.8
C


ATOM
139
CB
GLN
A1064
17.107
27.891
−0.714
37.34
C


ATOM
140
CG
GLN
A1064
18.298
26.933
−0.903
42.24
C


ATOM
141
CD
GLN
A1064
18.941
26.556
0.423
48.21
C


ATOM
142
OE1
GLN
A1064
19.424
25.401
0.631
46.84
O


ATOM
143
NE2
GLN
A1064
18.93
27.533
1.361
49.57
N


ATOM
144
C
GLN
A1064
15.785
25.789
−1.019
35.4
C


ATOM
145
O
GLN
A1064
15.745
25.572
−2.223
36.53
O


ATOM
146
N
ALA
A1065
15.822
24.836
−0.102
34.9
N


ATOM
147
CA
ALA
A1065
15.734
23.427
−0.484
34.73
C


ATOM
148
CB
ALA
A1065
16.265
22.522
0.617
33.98
C


ATOM
149
C
ALA
A1065
14.294
23.02
−0.867
35.39
C


ATOM
150
O
ALA
A1065
14.084
21.938
−1.404
37.15
O


ATOM
151
N
VAL
A1066
13.299
23.857
−0.567
34.68
N


ATOM
152
CA
VAL
A1066
11.925
23.526
−0.857
33.72
C


ATOM
153
CB
VAL
A1066
11.105
23.259
0.451
33.44
C


ATOM
154
CG1
VAL
A1066
11.819
22.214
1.276
35.84
C


ATOM
155
CG2
VAL
A1066
10.853
24.515
1.308
31.99
C


ATOM
156
C
VAL
A1066
11.255
24.559
−1.73
34.18
C


ATOM
157
O
VAL
A1066
10.05
24.555
−1.852
34.26
O


ATOM
158
N
GLN
A1067
12.006
25.457
−2.355
34.69
N


ATOM
159
CA
GLN
A1067
11.311
26.561
−3.041
35.45
C


ATOM
160
CB
GLN
A1067
12.234
27.745
−3.342
35.7
C


ATOM
161
CG
GLN
A1067
13.58
27.38
−4.01
39.46
C


ATOM
162
CD
GLN
A1067
13.902
28.27
−5.218
41.67
C


ATOM
163
OE1
GLN
A1067
15.065
28.643
−5.421
40.43
O


ATOM
164
NE2
GLN
A1067
12.864
28.609
−6.03
41.3
N


ATOM
165
C
GLN
A1067
10.592
26.046
−4.298
34.39
C


ATOM
166
O
GLN
A1067
9.513
26.551
−4.704
33.28
O


ATOM
167
N
HIS
A1068
11.184
24.999
−4.874
33.52
N


ATOM
168
CA
HIS
A1068
10.604
24.326
−6.044
32.41
C


ATOM
169
CB
HIS
A1068
11.598
23.345
−6.731
31.19
C


ATOM
170
CG
HIS
A1068
11.982
22.16
−5.912
30.41
C


ATOM
171
CD2
HIS
A1068
11.716
20.828
−6.08
32.9
C


ATOM
172
ND1
HIS
A1068
12.762
22.256
−4.775
30.19
N


ATOM
173
CE1
HIS
A1068
12.951
21.041
−4.273
27.55
C


ATOM
174
NE2
HIS
A1068
12.318
20.159
−5.038
30.41
N


ATOM
175
C
HIS
A1068
9.28
23.677
−5.688
31.32
C


ATOM
176
O
HIS
A1068
8.382
23.674
−6.484
33.73
O


ATOM
177
N
VAL
A1069
9.13
23.197
−4.467
30.56
N


ATOM
178
CA
VAL
A1069
7.856
22.582
−3.983
29.15
C


ATOM
179
CB
VAL
A1069
8.163
21.81
−2.733
29.55
C


ATOM
180
CG1
VAL
A1069
7.234
20.651
−2.639
31.08
C


ATOM
181
CG2
VAL
A1069
9.625
21.383
−2.751
30.94
C


ATOM
182
C
VAL
A1069
6.711
23.542
−3.57
26.86
C


ATOM
183
O
VAL
A1069
5.518
23.206
−3.653
25.45
O


ATOM
184
N
VAL
A1070
7.105
24.72
−3.111
24.89
N


ATOM
185
CA
VAL
A1070
6.187
25.716
−2.632
25.08
C


ATOM
186
CB
VAL
A1070
6.875
26.794
−1.768
24.76
C


ATOM
187
CG1
VAL
A1070
5.823
27.937
−1.397
27.38
C


ATOM
188
CG2
VAL
A1070
7.398
26.161
−0.518
22.87
C


ATOM
189
C
VAL
A1070
5.335
26.363
−3.725
24.92
C


ATOM
190
O
VAL
A1070
5.866
26.883
−4.671
25.57
O


ATOM
191
N
ILE
A1071
4.017
26.331
−3.539
24.9
N


ATOM
192
CA
ILE
A1071
3.066
26.947
−4.426
25.41
C


ATOM
193
CB
ILE
A1071
1.841
25.984
−4.658
26.26
C


ATOM
194
CG2
ILE
A1071
0.936
26.512
−5.742
25.59
C


ATOM
195
CG1
ILE
A1071
2.322
24.56
−5.002
27.15
C


ATOM
196
CD1
ILE
A1071
1.219
23.495
−5.119
24.77
C


ATOM
197
C
ILE
A1071
2.552
28.291
−3.916
25.98
C


ATOM
198
O
ILE
A1071
2.139
28.459
−2.744
25.3
O


ATOM
199
N
GLY
A1072
2.475
29.24
−4.825
26.18
N


ATOM
200
CA
GLY
A1072
1.98
30.52
−4.46
26.79
C


ATOM
201
C
GLY
A1072
0.488
30.535
−4.409
27.83
C


ATOM
202
O
GLY
A1072
−0.147
29.872
−5.205
26.82
O


ATOM
203
N
PRO
A1073
−0.085
31.374
−3.509
29.78
N


ATOM
204
CD
PRO
A1073
0.556
32.418
−2.675
30.6
C


ATOM
205
CA
PRO
A1073
−1.515
31.335
−3.283
30.69
C


ATOM
206
CB
PRO
A1073
−1.744
32.379
−2.15
31.44
C


ATOM
207
CG
PRO
A1073
−0.627
33.301
−2.24
30.55
C


ATOM
208
C
PRO
A1073
−2.233
31.821
−4.49
31.3
C


ATOM
209
O
PRO
A1073
−3.436
31.784
−4.49
33.38
O


ATOM
210
N
SER
A1074
−1.532
32.348
−5.49
30.64
N


ATOM
211
CA
SER
A1074
−2.259
32.82
−6.665
29
C


ATOM
212
CB
SER
A1074
−1.796
34.218
−7.058
28.51
C


ATOM
213
OG
SER
A1074
−2.372
35.183
−6.185
26.91
O


ATOM
214
C
SER
A1074
−2.124
31.81
−7.79
28.72
C


ATOM
215
O
SER
A1074
−2.763
31.956
−8.833
28.82
O


ATOM
216
N
SER
A1075
−1.311
30.771
−7.522
27.32
N


ATOM
217
CA
SER
A1075
−1.055
29.665
−8.421
25.33
C


ATOM
218
CB
SER
A1075
0.381
29.215
−8.266
25.63
C


ATOM
219
OG
SER
A1075
1.239
30.134
−8.912
26.14
O


ATOM
220
C
SER
A1075
−1.978
28.476
−8.173
25.13
C


ATOM
221
O
SER
A1075
−1.868
27.453
−8.857
25.41
O


ATOM
222
N
LEU
A1076
−2.879
28.615
−7.2
23.73
N


ATOM
223
CA
LEU
A1076
−3.72
27.546
−6.762
21.91
C


ATOM
224
CB
LEU
A1076
−3.187
26.898
−5.467
20.79
C


ATOM
225
CG
LEU
A1076
−4.03
25.669
−5.036
20.11
C


ATOM
226
CD1
LEU
A1076
−3.951
24.503
−6.038
15.91
C


ATOM
227
CD2
LEU
A1076
−3.717
25.152
−3.646
19.98
C


ATOM
228
C
LEU
A1076
−5.131
28.047
−6.533
22.97
C


ATOM
229
O
LEU
A1076
−5.408
28.796
−5.548
24.03
O


ATOM
230
N
ILE
A1077
−6.029
27.628
−7.42
22.57
N


ATOM
231
CA
ILE
A1077
−7.439
27.868
−7.216
23.08
C


ATOM
232
CB
ILE
A1077
−8.261
27.904
−8.53
24.06
C


ATOM
233
CG2
ILE
A1077
−9.65
28.526
−8.221
20.11
C


ATOM
234
CG1
ILE
A1077
−7.464
28.606
−9.652
22.13
C


ATOM
235
CD1
ILE
A1077
−7.14
30.062
−9.29
25.62
C


ATOM
236
C
ILE
A1077
−8.061
26.798
−6.385
23.17
C


ATOM
237
O
ILE
A1077
−7.874
25.639
−6.679
24.09
O


ATOM
238
N
VAL
A1078
−8.804
27.195
−5.351
23.26
N


ATOM
239
CA
VAL
A1078
−9.607
26.28
−4.572
23.02
C


ATOM
240
CB
VAL
A1078
−8.916
25.876
−3.223
22.97
C


ATOM
241
CG1
VAL
A1078
−9.859
25.009
−2.365
22.11
C


ATOM
242
CG2
VAL
A1078
−7.658
25.173
−3.466
23.96
C


ATOM
243
C
VAL
A1078
−10.893
26.989
−4.227
23.24
C


ATOM
244
O
VAL
A1078
−10.877
27.922
−3.464
23.89
O


ATOM
245
N
HIS
A1079
−12.003
26.51
−4.758
24.26
N


ATOM
246
CA
HIS
A1079
−13.337
26.941
−4.381
24.97
C


ATOM
247
CB
HIS
A1079
−14.21
26.807
−5.596
24.57
C


ATOM
248
CG
HIS
A1079
−13.671
27.5
−6.804
24.97
C


ATOM
249
CD2
HIS
A1079
−13.2
27.014
−7.974
26.02
C


ATOM
250
ND1
HIS
A1079
−13.61
28.875
−6.909
24.64
N


ATOM
251
CE1
HIS
A1079
−13.12
29.202
−8.093
25.68
C


ATOM
252
NE2
HIS
A1079
−12.871
28.09
−8.763
25.4
N


ATOM
253
C
HIS
A1079
−13.875
26.039
−3.251
27.07
C


ATOM
254
O
HIS
A1079
−13.889
24.8
−3.387
26.98
O


ATOM
255
N
PHE
A1080
−14.317
26.624
−2.137
28.58
N


ATOM
256
CA
PHE
A1080
−14.61
25.778
−0.968
31.3
C


ATOM
257
CB
PHE
A1080
−14.449
26.52
0.389
33.68
C


ATOM
258
CG
PHE
A1080
−13.052
26.915
0.647
35.21
C


ATOM
259
CD1
PHE
A1080
−12.68
28.264
0.595
40.09
C


ATOM
260
CD2
PHE
A1080
−12.079
25.927
0.826
32.59
C


ATOM
261
CE1
PHE
A1080
−11.294
28.615
0.751
42.72
C


ATOM
262
CE2
PHE
A1080
−10.769
26.232
1
35.14
C


ATOM
263
CZ
PHE
A1080
−10.341
27.577
0.966
40.38
C


ATOM
264
C
PHE
A1080
−15.91
25.034
−0.977
30.93
C


ATOM
265
O
PHE
A1080
−16.144
24.233
−0.073
31.9
O


ATOM
266
N
ASN
A1081
−16.749
25.261
−1.98
29.99
N


ATOM
267
CA
ASN
A1081
−17.951
24.477
−2.052
28.6
C


ATOM
268
CB
ASN
A1081
−19.041
25.218
−2.808
29.48
C


ATOM
269
CG
ASN
A1081
−18.671
25.483
−4.236
31.25
C


ATOM
270
OD1
ASN
A1081
−17.865
26.382
−4.541
29.24
O


ATOM
271
ND2
ASN
A1081
−19.204
24.643
−5.131
31.12
N


ATOM
272
C
ASN
A1081
−17.608
23.185
−2.732
27.52
C


ATOM
273
O
ASN
A1081
−18.403
22.229
−2.665
29.53
O


ATOM
274
N
GLU
A1082
−16.414
23.124
−3.333
24.89
N


ATOM
275
CA
GLU
A1082
−16.04
22.01
−4.213
22.44
C


ATOM
276
CB
GLU
A1082
−15.32
22.481
−5.481
22.29
C


ATOM
277
CG
GLU
A1082
−16.068
23.386
−6.341
22.97
C


ATOM
278
CD
GLU
A1082
−15.26
23.767
−7.575
27.8
C


ATOM
279
OE1
GLU
A1082
−15.742
24.562
−8.432
28.49
O


ATOM
280
OE2
GLU
A1082
−14.136
23.253
−7.713
29.66
O


ATOM
281
C
GLU
A1082
−15.21
20.951
−3.497
20.44
C


ATOM
282
O
GLU
A1082
−14.018
21.015
−3.435
20.29
O


ATOM
283
N
VAL
A1083
−15.888
19.932
−3.019
19.69
N


ATOM
284
CA
VAL
A1083
−15.309
18.879
−2.201
16.58
C


ATOM
285
CB
VAL
A1083
−16.098
18.697
−0.886
15.58
C


ATOM
286
CG1
VAL
A1083
−15.45
17.604
−0.042
12.74
C


ATOM
287
CG2
VAL
A1083
−16.132
20.05
−0.121
12.18
C


ATOM
288
C
VAL
A1083
−15.236
17.566 
−2.955
16.73
C


ATOM
289
O
VAL
A1083
−16.201
17.105
−3.555
16.56
O


ATOM
290
N
ILE
A1084
−14.054
16.977
−2.913
16.19
N


ATOM
291
CA
ILE
A1084
−13.822
15.663
−3.494
15.78
C


ATOM
292
CB
ILE
A1084
−12.32
15.465
−3.831
14.2
C


ATOM
293
CG2
ILE
A1084
−12.057
14.095
−4.192
12.01
C


ATOM
294
CG1
ILE
A1084
−11.939
16.363
−5.007
14.72
C


ATOM
295
CD1
ILE
A1084
−10.462
16.58
−5.098
12.82
C


ATOM
296
C
ILE
A1084
−14.343
14.608
−2.533
15.45
C


ATOM
297
O
ILE
A1084
−15.065
13.716
−2.937
15.82
O


ATOM
298
N
GLY
A1085
−13.969
14.733
−1.273
14.58
N


ATOM
299
CA
GLY
A1085
−14.324
13.76
−0.272
15.49
C


ATOM
300
C
GLY
A1085
−14.158
14.328
1.144
16.4
C


ATOM
301
O
GLY
A1085
−13.28
15.137
1.41
14.09
O


ATOM
302
N
ARG
A1086
−15.036
13.887
2.039
18.79
N


ATOM
303
CA
ARG
A1086
−14.945
14.135
3.466
20.86
C


ATOM
304
CB
ARG
A1086
−16.251
14.676
3.989
21.21
C


ATOM
305
CG
ARG
A1086
−16.373
16.172
3.885
23.45
C


ATOM
306
CD
ARG
A1086
−17.9
16.646
3.969
26.42
C


ATOM
307
NE
ARG
A1086
−18.001
18.021
3.466
27.6
N


ATOM
308
CZ
ARG
A1086
−17.48
19.093
4.091
32.33
C


ATOM
309
NH1
ARG
A1086
−16.816
18.961
5.242
35.28
N


ATOM
310
NH2
ARG
A1086
−17.595
20.32
3.569
32.16
N


ATOM
311
C
ARG
A1086
−14.682
12.807
4.096
20.17
C


ATOM
312
O
ARG
A1086
−14.958
11.754
3.495
20.3
O


ATOM
313
N
GLY
A1087
−14.079
12.823
5.28
20.64
N


ATOM
314
CA
GLY
A1087
−13.973
11.578
6.063
20.22
C


ATOM
315
C
GLY
A1087
−13.277
11.809
7.358
19.8
C


ATOM
316
O
GLY
A1087
−13.267
12.898
7.864
20.95
O


ATOM
317
N
HIS
A1088
−12.638
10.785
7.88
19.64
N


ATOM
318
CA
HIS
A1088
−11.928
10.907
9.153
18.07
C


ATOM
319
CB
HIS
A1088
−11.39
9.532
9.544
18.11
C


ATOM
320
CG
HIS
A1088
−12.414
8.645
10.11
18.13
C


ATOM
321
CD2
HIS
A1088
−12.848
7.416
9.726
19.99
C


ATOM
322
ND1
HIS
A1088
−13.147
8.999
11.226
19.52
N


ATOM
323
CE1
HIS
A1088
−13.989
8.018
11.518
20.66
C


ATOM
324
NE2
HIS
A1088
−13.831
7.051
10.622
21.93
N


ATOM
325
C
HIS
A1088
−10.732
11.749
8.888
16.52
C


ATOM
326
O
HIS
A1088
−10.263
12.502
9.743
16.94
O


ATOM
327
N
PHE
A1089
−10.193
11.522
7.698
14.83
N


ATOM
328
CA
PHE
A1089
−9.003
12.234
7.244
13.7
C


ATOM
329
CB
PHE
A1089
−8.494
11.675
5.925
11.64
C


ATOM
330
CG
PHE
A1089
−9.525
11.593
4.91
10.95
C


ATOM
331
CD1
PHE
A1089
−9.965
12.794
4.219
13.52
C


ATOM
332
CD2
PHE
A1089
−10.09
10.376
4.612
8.32
C


ATOM
333
CE1
PHE
A1089
−10.956
12.734
3.249
10.64
C


ATOM
334
CE2
PHE
A1089
−11.079
10.261
3.648
10.05
C


ATOM
335
CZ
PHE
A1089
−11.543
11.452
2.966
15.19
C


ATOM
336
C
PHE
A1089
−9.287
13.746
7.164
12.68
C


ATOM
337
O
PHE
A1089
−8.348
14.505
7.187
11.45
O


ATOM
338
N
GLY
A1090
−10.577
14.126
7.178
11.98
N


ATOM
339
CA
GLY
A1090
−11.019
15.513
7.028
13.34
C


ATOM
340
C
GLY
A1090
−11.674
15.859
5.68
14
C


ATOM
341
O
GLY
A1090
−12.487
15.12
5.127
14.32
O


ATOM
342
N
CYS
A1091
−11.346
17.001
5.142
14.77
N


ATOM
343
CA
CYS
A1091
−12.027
17.454
3.959
14.05
C


ATOM
344
CB
CYS
A1091
−12.905
18.65
4.304
14.11
C


ATOM
345
SG
CYS
A1091
−13.959
19.211
2.883
19.49
S


ATOM
346
C
CYS
A1091
−11.019
17.769
2.824
13.5
C


ATOM
347
O
CYS
A1091
−10.098
18.585
2.975
11.93
O


ATOM
348
N
VAL
A1092
−11.215
17.09
1.711
12.32
N


ATOM
349
CA
VAL
A1092
−10.36
17.217
0.573
12.75
C


ATOM
350
CB
VAL
A1092
−9.928
15.823
0.058
12.83
C


ATOM
351
CG1
VAL
A1092
−9.089
15.986
−1.186
13.1
C


ATOM
352
CG2
VAL
A1092
−9.154
15.079
1.144
10.11
C


ATOM
353
C
VAL
A1092
−11.092
17.993
−0.543
13.41
C


ATOM
354
O
VAL
A1092
−12.196
17.644
−0.947
11.1
O


ATOM
355
N
TYR
A1093
−10.405
19.012
−1.084
14.21
N


ATOM
356
CA
TYR
A1093
−10.987
19.843
−2.087
13.01
C


ATOM
357
CB
TYR
A1093
−10.838
21.298
−1.671
15.58
C


ATOM
358
CG
TYR
A1093
−11.421
21.639
−0.338
16.74
C


ATOM
359
CD1
TYR
A1093
−10.62
21.582
0.8
20.27
C


ATOM
360
CE1
TYR
A1093
−11.131
21.931
2.072
24.42
C


ATOM
361
CD2
TYR
A1093
−12.767
22.025
−0.212
15.71
C


ATOM
362
CE2
TYR
A1093
−13.326
22.363
1.026
19.23
C


ATOM
363
CZ
TYR
A1093
−12.491
22.32
72.2
24.72
C


ATOM
364
OH
TYR
A1093
−12.946
22.676
3.505
25.2
O


ATOM
365
C
TYR
A1093
−10.429
19.689
−3.461
13.15
C


ATOM
366
O
TYR
A1093
−9.223
19.373
−3.67
10.61
O


ATOM
367
N
HIS
A1094
−11.288
20.032
−4.413
13.11
N


ATOM
368
CA
HIS
A1094
−10.809
20.226
−5.759
14.03
C


ATOM
369
CB
HIS
A1094
−11.964
20.459
−6.695
13.93
C


ATOM
370
CG
HIS
A1094
−12.696
19.219
−7.059
13.98
C


ATOM
371
CD2
HIS
A1094
−13.885
18.736
−6.647
15.38
C


ATOM
372
ND1
HIS
A1094
−12.217
18.329
−7.988
16.1
N


ATOM
373
CE1
HIS
A1094
−13.102
17.372
−8.161
19.29
C


ATOM
374
NE2
HIS
A1094
−14.106
17.58
−7.337
18.15
N


ATOM
375
C
HIS
A1094
−9.891
21.425
−5.84
14.5
C


ATOM
376
O
HIS
A1094
−10.192
22.432
−5.262
14.97
O


ATOM
377
N
GLY
A1095
−8.78
21.306
−6.553
15.67
N


ATOM
378
CA
GLY
A1095
−7.939
22.453
−6.806
17.79
C


ATOM
379
C
GLY
A1095
−7.533
22.565
−8.27
18.77
C


ATOM
380
O
GLY
A1095
−7.707
21.662
−9.049
17.49
O


ATOM
381
N
THR
A1096
−7.015
23.715
−8.636
21.94
N


ATOM
382
CA
THR
A1096
−6.45
23.941
−9.964
24.75
C


ATOM
383
CB
THR
A1096
−7.362
24.783
−10.89
24.55
C


ATOM
384
OG1
THR
A1096
−8.54
24.038
−11.201
25.91
O


ATOM
385
CG2
THR
A1096
−6.679
25.036
−12.2
24.08
C


ATOM
386
C
THR
A1096
−5.135
24.63
−9.743
26.07
C


ATOM
387
O
THR
A1096
−5.071
25.709
−9.187
26.93
O


ATOM
388
N
LEU
A1097
−4.081
23.94
−10.117
28.65
N


ATOM
389
CA
LEU
A1097
−2.772
24.458
−10.032
31.8
C


ATOM
390
CB
LEU
A1097
−1.85
23.345
−9.609
30.83
C


ATOM
391
CG
LEU
A1097
−0.375
23.607
−9.399
32.94
C


ATOM
392
CD1
LEU
A1097
−0.234
24.57
−8.252
32.31
C


ATOM
393
CD2
LEU
A1097
0.493
22.298
−9.219
30.24
C


ATOM
394
C
LEU
A1097
−2.449
25.09
−11.421
35.83
C


ATOM
395
O
LEU
A1097
−2.405
24.415
−12.477
35.53
O


ATOM
396
N
LEU
A1098
−2.31
26.421
−11.415
39.47
N


ATOM
397
CA
LEU
A1098
−1.987
27.14
−12.619
43.37
C


ATOM
398
CB
LEU
A1098
−2.541
28.54
−12.571
41.93
C


ATOM
399
CG
LEU
A1098
−3.928
28.572
−11.927
43.36
C


ATOM
400
CD1
LEU
A1098
−4.141
29.836
−11.071
41.52
C


ATOM
401
CD2
LEU
A1098
−5.056
28.35
−12.955
42.76
C


ATOM
402
C
LEU
A1098
−0.512
27.166
−12.525
47.12
C


ATOM
403
O
LEU
A1098
0.04
27.78
−11.624
48.42
O


ATOM
404
N
ASP
A1099
0.157
26.422
−13.379
51.62
N


ATOM
405
CA
ASP
A1099
1.604
26.58
−13.384
56.85
C


ATOM
406
CB
ASP
A1099
2.383
25.931
−12.186
57.68
C


ATOM
407
CG
ASP
A1099
2.043
24.437
−11.941
63.37
C


ATOM
408
OD1
ASP
A1099
0.976
23.902
−12.415
70.78
O


ATOM
409
OD2
ASP
A1099
2.863
23.795
−11.226
65.81
O


ATOM
410
C
ASP
A1099
2.297
26.411
−14.726
58.47
C


ATOM
411
O
ASP
A1099
2.446
25.303
−15.282
59.18
O


ATOM
412
N
ASN
A1100
2.591
27.597
−15.241
60.14
N


ATOM
413
CA
ASN
A1100
3.733
27.913
−16.05
61.85
C


ATOM
414
CB
ASN
A1100
5.058
27.881
−15.346
62.48
C


ATOM
415
CG
ASN
A1100
5.207
29.074
−14.421
64.67
C


ATOM
416
OD1
ASN
A1100
4.493
30.084
−14.6
66.33
O


ATOM
417
ND2
ASN
A1100
6.098
28.973
−13.414
65.49
N


ATOM
418
C
ASN
A1100
3.704
28.415
−17.45
61.64
C


ATOM
419
O
ASN
A1100
3.76
27.649
−18.43
61.43
O


ATOM
420
N
ASP
A1101
3.616
29.729
−17.532
61.13
N


ATOM
421
CA
ASP
A1101
2.785
30.288
−18.571
61.44
C


ATOM
422
CB
ASP
A1101
3.612
30.958
−19.687
62.05
C


ATOM
423
CG
ASP
A1101
2.907
32.203
−20.251
63.68
C


ATOM
424
OD1
ASP
A1101
2.526
32.22
−21.452
62.73
O


ATOM
425
OD2
ASP
A1101
2.702
33.157
−19.455
66.21
O


ATOM
426
C
ASP
A1101
1.805
29.22
−19.135
60.4
C


ATOM
427
O
ASP
A1101
2.226
28.267
−19.83
60.81
O


ATOM
428
N
GLY
A1102
0.516
29.356
−18.804
58.95
N


ATOM
429
CA
GLY
A1102
−0.534
28.677
−19.573
56.58
C


ATOM
430
C
GLY
A1102
−1.253
27.537
−18.885
54.7
C


ATOM
431
O
GLY
A1102
−2.465
27.587
−18.683
53.95
O


ATOM
432
N
LYS
A1103
−0.534
26.476
−18.542
53.24
N


ATOM
433
CA
LYS
A1103
−1.278
25.235
−18.237
51.22
C


ATOM
434
CB
LYS
A1103
−0.65
23.93
−18.814
51.58
C


ATOM
435
CG
LYS
A1103
0.762
23.585
−18.409
54.34
C


ATOM
436
CD
LYS
A1103
1.789
24.509
−19.112
57.47
C


ATOM
437
CE
LYS
A1103
2.423
25.478
−18.11
55.46
C


ATOM
438
NZ
LYS
A1103
3.733
24.994
−17.598
53.32
N


ATOM
439
C
LYS
A1103
−1.924
25.068
−16.843
48.72
C


ATOM
440
O
LYS
A1103
−1.492
25.647
−15.82
48.06
O


ATOM
441
N
LYS
A1104
−3.032
24.329
−16.899
45.99
N


ATOM
442
CA
LYS
A1104
−3.879
24.011
−15.771
43.3
C


ATOM
443
CB
LYS
A1104
−5.317
24.45
−16.004
42.65
C


ATOM
444
CG
LYS
A1104
−5.508
25.939
−15.923
41.8
C


ATOM
445
CD
LYS
A1104
−6.917
26.243
−16.354
40.69
C


ATOM
446
CE
LYS
A1104
−6.952
27.394
−17.336
40.81
C


ATOM
447
NZ
LYS
A1104
−8.305
28.012
−17.239
41.64
N


ATOM
448
C
LYS
A1104
−3.825
22.516
−15.436
41.44
C


ATOM
449
O
LYS
A1104
−3.898
21.605
−16.313
40.97
O


ATOM
450
N
ILE
A1105
−3.657
22.291
−14.142
37.97
N


ATOM
451
CA
ILE
A1105
−3.705
20.976
−13.612
34.91
C


ATOM
452
CB
ILE
A1105
−2.301
20.361
−13.454
35.61
C


ATOM
453
CG2
ILE
A1105
−1.135
21.401
−13.762
37.19
C


ATOM
454
CG1
ILE
A1105
−2.155
19.599
−12.139
36.65
C


ATOM
455
CD1
ILE
A1105
−0.883
18.749
−12.072
36.89
C


ATOM
456
C
ILE
A1105
−4.701
20.852
−12.444
31.98
C


ATOM
457
O
ILE
A1105
−4.608
21.565
−11.427
27.87
O


ATOM
458
N
HIS
A1106
−5.686
19.967
−12.693
28.84
N


ATOM
459
CA
HIS
A1106
−6.645
19.518
−11.728
26.8
C


ATOM
460
CB
HIS
A1106
−7.622
18.551
−12.383
28.08
C


ATOM
461
CG
HIS
A1106
−8.818
18.218
−11.543
30.25
C


ATOM
462
CD2
HIS
A1106
−9.146
18.556
−10.269
31.62
C


ATOM
463
ND1
HIS
A1106
−9.881
17.478
−12.03
33.44
N


ATOM
464
CE1
HIS
A1106
−10.804
17.357
−11.087
33.23
C


ATOM
465
NE2
HIS
A1106
−10.375
17.991
−10.003
35.32
N


ATOM
466
C
HIS
A1106
−5.886
18.793
−10.631
24.68
C


ATOM
467
O
HIS
A1106
−4.955
18.018
−10.904
25.45
O


ATOM
468
N
CYS
A1107
−6.243
19.048
−9.386
21.07
N


ATOM
469
CA
CYS
A1107
−5.523
18.458
−8.31
19.54
C


ATOM
470
CB
CYS
A1107
−4.265
19.297
−8
20.32
C


ATOM
471
SG
CYS
A1107
−4.67
21.059
−7.642
21.01
S


ATOM
472
C
CYS
A1107
−6.454
18.368
−7.115
18.93
C


ATOM
473
O
CYS
A1107
−7.648
18.819
−7.131
17.53
O


ATOM
474
N
ALA
A1108
−5.915
17.78
−6.063
17.24
N


ATOM
475
CA
ALA
A1108
−6.65
17.696
−4.829
15.77
C


ATOM
476
CB
ALA
A1108
−6.865
16.206
−4.395
15.49
C


ATOM
477
C
ALA
A1108
−5.856
18.437
−3.791
14.69
C


ATOM
478
O
ALA
A1108
−4.645
18.317
−3.75
14.65
O


ATOM
479
N
VAL
A1109
−6.559
19.158
−2.927
13.84
N


ATOM
480
CA
VAL
A1109
−5.932
20.008
−1.939
12.57
C


ATOM
481
CB
VAL
A1109
−6.094
21.513
−2.247
12.13
C


ATOM
482
CG1
VAL
A1109
−5.136
22.321
−1.227
11.45
C


ATOM
483
CG2
VAL
A1109
−5.762
21.768
−3.729
8.23
C


ATOM
484
C
VAL
A1109
−6.49
19.734
−0.554
12.99
C


ATOM
485
O
VAL
A1109
−7.719
19.469
−0.365
12.53
O


ATOM
486
N
LYS
A1110
−5.587
19.781
0.41
12.17
N


ATOM
487
CA
LYS
A1110
−5.977
19.552
1.81
14.24
C


ATOM
488
CB
LYS
A1110
−5.985
18.063
2.167
13.99
C


ATOM
489
CG
LYS
A1110
−6.46
17.861
3.594
21.03
C


ATOM
490
CD
LYS
A1110
−6.867
16.451
3.838
23.19
C


ATOM
491
CE
LYS
A1110
−7.619
16.316
5.141
25.85
C


ATOM
492
NZ
LYS
A1110
−7.133
17.189
6.257
25.05
N


ATOM
493
C
LYS
A1110
−5.123
20.326
2.802
13.07
C


ATOM
494
O
LYS
A1110
−3.911
20.547
2.592
11.93
O


ATOM
495
N
SER
A1111
−5.803
20.812
3.831
13.22
N


ATOM
496
CA
SER
A1111
−5.157 
21.588
4.925
13.91
C


ATOM
497
CB
SER
A1111
−6.208
22.486
5.632
13.19
C


ATOM
498
OG
SER
A1111
−5.588
23.295
6.645
16.46
O


ATOM
499
C
SER
A1111
−4.531
20.633
5.894
12.91
C


ATOM
500
O
SER
A1111
−5.173
19.691
6.345
13.35
O


ATOM
501
N
LEU
A1112
−3.251
20.769
6.16
13.27
N


ATOM
502
CA
LEU
A1112
−2.67
19.886
7.215
12.16
C


ATOM
503
CB
LEU
A1112
−1.183
19.77
6.984
12.71
C


ATOM
504
CG
LEU
A1112
−0.892
19.329
5.545
13.33
C


ATOM
505
CD1
LEU
A1112
0.556
19.371
5.272
10.72
C


ATOM
506
CD2
LEU
A1112
−1.401
17.897
5.255
16.22
C


ATOM
507
C
LEU
A1112
−2.964
20.401
8.632
12.03
C


ATOM
508
O
LEU
A1112
−2.145
21.009
9.264
11.5
O


ATOM
509
N
ASN
A1113
−4.201
20.228
9.091
13.41
N


ATOM
510
CA
ASN
A1113
−4.652
20.809
10.366
12.87
C


ATOM
511
CB
ASN
A1113
−6.092
20.435
10.644
13.74
C


ATOM
512
CG
ASN
A1113
−6.994
20.782
9.52
11.65
C


ATOM
513
OD1
ASN
A1113
−6.819
21.773
8.853
17.02
O


ATOM
514
ND2
ASN
A1113
−7.919
19.946
9.271
13.53
N


ATOM
515
C
ASN
A1113
−3.822
20.364
11.556
12.79
C


ATOM
516
O
ASN
A1113
−3.905
20.982
12.625
11.81
O


ATOM
517
N
ARG
A1114
−2.993
19.335
11.362
11.67
N


ATOM
518
CA
ARG
A1114
−2.192
18.838
12.447
11.69
C


ATOM
519
CB
ARG
A1114
−1.872
17.402
12.26
12.4
C


ATOM
520
CG
ARG
A1114
−3.031
16.474
12.672
15.55
C


ATOM
521
CD
ARG
A1114
−2.856
15.116
12.074
19.31
C


ATOM
522
NE
ARG
A1114
−1.941
14.212
12.787
25.78
N


ATOM
523
CZ
ARG
A1114
−1.491
13.059
12.246
29.79
C


ATOM
524
NH1
ARG
A1114
−1.851
12.685
10.979
24.36
N


ATOM
525
NH2
ARG
A1114
−0.693
12.264
12.964
26.37
N


ATOM
526
C
ARG
A1114
−0.933
19.587
12.57
12.08
C


ATOM
527
O
ARG
A1114
−0.203
19.386
13.495
12.99
O


ATOM
528
N
ILE
A1115
−0.645
20.425
11.59
13.44
N


ATOM
529
CA
ILE
A1115
0.508
21.284
11.629
14.59
C


ATOM
530
CB
ILE
A1115
1.202
21.342
10.297
14.68
C


ATOM
531
CG2
ILE
A1115
2.221
22.495
10.326
12.88
C


ATOM
532
CG1
ILE
A1115
1.808
19.959
9.988
12.83
C


ATOM
533
CD1
ILE
A1115
2.105
19.74
28.559
15.91
C


ATOM
534
C
ILE
A1115
0.012
22.649
12.063
16.19
C


ATOM
535
O
ILE
A1115
−0.616
23.356
11.311
15.61
O


ATOM
536
N
THR
A1116
0.255
22.94
13.329
18.45
N


ATOM
537
CA
THR
A1116
−0.373
24.035
14.047
20.84
C


ATOM
538
CB
THR
A1116
−0.99
23.595
15.441
20
C


ATOM
539
OG1
THR
A1116
0.063
23.267
16.354
22.88
O


ATOM
540
CG2
THR
A1116
−1.914
22.399
15.325
19.02
C


ATOM
541
C
THR
A1116
0.647
25.161
14.281
22.42
C


ATOM
542
O
THR
A1116
0.262
26.269
14.657
24.01
O


ATOM
543
N
ASP
A1117
1.925
24.88
414.072
24.01
N


ATOM
544
CA
ASP
A1117
2.966
25.857
14.387
27.46
C


ATOM
545
CB
ASP
A1117
3.215
25.998
15.919
28.91
C


ATOM
546
CG
ASP
A1117
4.169
24.937
16.472
33.12
C


ATOM
547
OD1
ASP
A1117
5.406
25.172
16.513
42.43
O


ATOM
548
OD2
ASP
A1117
3.693
23.861
16.88
39.9
O


ATOM
549
C
ASP
A1117
4.283
25.595
13.691
27.09
C


ATOM
550
O
ASP
A1117
4.521
24.504
13.158
27.63
O


ATOM
551
N
ILE
A1118
5.154
26.598
13.782
27.49
N


ATOM
552
CA
ILE
A1118
6.42
26.628
13.014
28.72
C


ATOM
553
CB
ILE
A1118
7.229
27.969
13.169
28.25
C


ATOM
554
CG2
ILE
A1118
7.455
28.31
14.587
28.16
C


ATOM
555
CG1
ILE
A1118
8.569
27.892
12.419
29.89
C


ATOM
556
CD1
ILE
A1118
8.654
28.76
11.192
26.9
C


ATOM
557
C
ILE
A1118
7.296
25.38
13.127
28.67
C


ATOM
558
O
ILE
A1118
7.848
24.949
12.137
29.24
O


ATOM
559
N
GLY
A1119
7.361
24.755
14.293
28.57
N


ATOM
560
CA
GLY
A1119
8.258
23.631
14.422
28.01
C


ATOM
561
C
GLY
A1119
7.757
22.432
13.65
28.19
C


ATOM
562
O
GLY
A1119
8.574
21.626
13.154
28.46
O


ATOM
563
N
GLU
A1120
6.428
22.287
13.578
26.88
N


ATOM
564
CA
GLU
A1120
5.838
21.15
12.906
26.64
C


ATOM
565
CB
GLU
A1120
4.42
20.865
13.421
27.07
C


ATOM
566
CG
GLU
A1120
4.269
20.751
14.884
27.63
C


ATOM
567
CD
GLU
A1120
2.846
21.044
15.39
28.22
C


ATOM
568
OE1
GLU
A1120
2.099
21.807
14.783
28.44
O


ATOM
569
OE2
GLU
A1120
2.46
20.487
16.42
29.07
O


ATOM
570
C
GLU
A1120
5.81
21.407
11.383
26.7
C


ATOM
571
O
GLU
A1120
5.802
20.462
10.573
25.57
O


ATOM
572
N
VAL
A1121
5.748
22.693
11.022
27.37
N


ATOM
573
CA
VAL
A1121
5.922
23.13
9.647
27.71
C


ATOM
574
CB
VAL
A1121
5.683
24.628
9.497
27.27
C


ATOM
575
CG1
VAL
A1121
6.097
25.15
8.094
23.83
C


ATOM
576
CG2
VAL
A1121
4.232
24.897
9.771
27.4
C


ATOM
577
C
VAL
A1121
7.325
22.81
9.246
28.92
C


ATOM
578
O
VAL
A1121
7.574
22.155
8.242
29.26
O


ATOM
579
N
SER
A1122
8.239
23.273
10.055
29.93
N


ATOM
580
CA
SER
A1122
9.619
23.092
9.773
32.48
C


ATOM
581
CB
SER
A1122
10.424
23.719
10.877
32.29
C


ATOM
582
OG
SER
A1122
11.749
23.285
10.758
38.18
O


ATOM
583
C
SER
A1122
9.979
21.618
9.585
32.67
C


ATOM
584
O
SER
A1122
10.711
21.274
8.654
32.69
O


ATOM
585
N
GLN
A1123
9.433
20.778
10.459
33.88
N


ATOM
586
CA
GLN
A1123
9.694
19.352
10.488
35.82
C


ATOM
587
CB
GLN
A1123
9.422
18.731
11.856
36.63
C


ATOM
588
CG
GLN
A1123
10.061
17.303
11.912
43.42
C


ATOM
589
CD
GLN
A1123
9.12
16.204
12.492
51.27
C


ATOM
590
OE1
GLN
A1123
8.588
16.34
13.639
52.06
O


ATOM
591
NE2
GLN
A1123
8.934
15.093
11.713
49.85
N


ATOM
592
C
GLN
A1123
8.86
18.583
9.502
35.76
C


ATOM
593
O
GLN
A1123
9.02
17.389
9.395
36.26
O


ATOM
594
N
PHE
A1124
7.937
19.267
8.837
35.73
N


ATOM
595
CA
PHE
A1124
7.195
18.716
7.759
35.08
C


ATOM
596
CB
PHE
A1124
5.78
19.251
7.763
34.12
C


ATOM
597
CG
PHE
A1124
5.026
18.881
6.552
33.72
C


ATOM
598
CD1
PHE
A1124
4.905
17.538
6.189
33.01
C


ATOM
599
CD2
PHE
A1124
4.467
19.855
5.735
34.39
C


ATOM
600
CE1
PHE
A1124
4.217
17.146
5.019
35.69
C


ATOM
601
CE2
PHE
A1124
3.769
19.486
4.546
37.38
C


ATOM
602
CZ
PHE
A1124
3.623
18.098
4.198
33.44
C


ATOM
603
C
PHE
A1124
7.856
19.11
6.465
36.22
C


ATOM
604
O
PHE
A1124
7.758
18.418
5.471
36.62
O


ATOM
605
N
LEU
A1125
8.515
20.253
6.458
37.74
N


ATOM
606
CA
LEU
A1125
9.041
20.818
5.213
38.87
C


ATOM
607
CB
LEU
A1125
9.55
22.25
5.41
37.31
C


ATOM
608
CG
LEU
A1125
8.45
23.306
5.26
31.73
C


ATOM
609
CD1
LEU
A1125
9.085
24.585
5.245
27.34
C


ATOM
610
CD2
LEU
A1125
7.633
23.113
4.006
29.13
C


ATOM
611
C
LEU
A1125
10.118
19.936
4.675
41.71
C


ATOM
612
O
LEU
A1125
10.5
20.024
3.508
43.58
O


ATOM
613
N
THR
A1126
10.569
19.051
5.536
44.24
N


ATOM
614
CA
THR
A1126
11.528
18.045
5.199
47.41
C


ATOM
615
CB
THR
A1126
12.226
17.613
6.523
46.64
C


ATOM
616
OG1
THR
A1126
12.818
18.766
7.167
44.19
O


ATOM
617
CG2
THR
A1126
13.246
16.566
6.262
44.87
C


ATOM
618
C
THR
A1126
10.862
16.834
4.43
49.62
C


ATOM
619
O
THR
A1126
11.561
15.942
3.935
50.03
O


ATOM
620
N
GLU
A1127
9.516
16.791
4.341
52.19
N


ATOM
621
CA
GLU
A1127
8.783
15.674
3.645
52.2
C


ATOM
622
CB
GLU
A1127
7.449
15.293
4.324
52.31
C


ATOM
623
CG
GLU
A1127
7.501
15.199
5.841
53.81
C


ATOM
624
CD
GLU
A1127
8.832
14.692
6.389
55.9
C


ATOM
625
OE1
GLU
A1127
9.174
15.026
7.545
57.21
O


ATOM
626
OE2
GLU
A1127
9.547
13.971
5.665
57.62
O


ATOM
627
C
GLU
A1127
8.545
15.969
2.176
53.81
C


ATOM
628
O
GLU
A1127
8.112
15.1
1.439
55.01
O


ATOM
629
N
GLY
A1128
8.782
17.202
1.749
54.61
N


ATOM
630
CA
GLY
A1128
9.106
17.403
0.357
55.06
C


ATOM
631
C
GLY
A1128
10.488
16.749
0.176
55.64
C


ATOM
632
O
GLY
A1128
10.614
15.726
−0.532
55.14
O


ATOM
633
N
ILE
A1129
11.511
17.316
0.845
55.99
N


ATOM
634
CA
ILE
A1129
12.95
16.959
0.641
56.67
C


ATOM
635
CB
ILE
A1129
13.908
17.69
11.668
56.95
C


ATOM
636
CG2
ILE
A1129
13.492
19.182
1.83
55.72
C


ATOM
637
CG1
ILE
A1129
14.077
16.912
3.024
56.78
C


ATOM
638
CD1
ILE
A1129
15.422
16.113
3.3
53.37
C


ATOM
639
C
ILE
A1129
13.277
15.432
0.541
57.46
C


ATOM
640
O
ILE
A1129
14.386
15.035
0.094
58.01
O


ATOM
641
N
ILE
A1130
12.309
14.597
0.965
57.33
N


ATOM
642
CA
ILE
A1130
12.338
13.139
0.758
55.98
C


ATOM
643
CB
ILE
A1130
12.578
12.337
2.059
55.97
C


ATOM
644
CG2
ILE
A1130
13.335
11.008
1.723
56.77
C


ATOM
645
CG1
ILE
A1130
13.265
13.188
3.132
55.59
C


ATOM
646
CD1
ILE
A1130
13.016
12.698
4.536
57.13
C


ATOM
647
C
ILE
A1130
11.017
12.641
0.192
54.95
C


ATOM
648
O
ILE
A1130
10.363
11.849
0.881
54.45
O


ATOM
649
N
MET
A1131
10.628
13.064
−1.032
53.3
N


ATOM
650
CA
MET
A1131
9.326
12.664
−1.518
52.51
C


ATOM
651
CB
MET
A1131
8.386
12.568
−0.315
52.76
C


ATOM
652
CG
MET
A1131
6.879
12.691
−0.612
55.76
C


ATOM
653
SD
MET
A1131
5.963
12.687
0.939
55.65
S


ATOM
654
CE
MET
A1131
6.21
10.987
1.559
53.64
C


ATOM
655
C
MET
A1131
8.643
13.474
−2.611
51.28
C


ATOM
656
O
MET
A1131
8.018
12.882
−3.51
51.1
O


ATOM
657
N
LYS
A1132
8.644
14.809
−2.476
49.59
N


ATOM
658
CA
LYS
A1132
8.324
15.729
−3.595
47.3
C


ATOM
659
CB
LYS
A1132
8.789
17.164
−3.285
48.03
C


ATOM
660
CG
LYS
A1132
10.293
17.164
−2.812
50.92
C


ATOM
661
CD
LYS
A1132
11.15
18.336
−3.247
55.23
C


ATOM
662
CE
LYS
A1132
12.093
18.78
−2.115
59.29
C


ATOM
663
NZ
LYS
A1132
11.331
19.555
−1.032
62.84
N


ATOM
664
C
LYS
A1132
9.143
15.254
−4.799
44.44
C


ATOM
665
O
LYS
A1132
8.7
15.357
−5.954
44.56
O


ATOM
666
N
ASP
A1133
10.318
14.71
−4.467
40.34
N


ATOM
667
CA
ASP
A1133
11.375
14.342
−5.376
36.85
C


ATOM
668
CB
ASP
A1133
12.709
14.419
−4.644
38.1
C


ATOM
669
CG
ASP
A1133
13.169
15.86
−4.393
39.25
C


ATOM
670
OD1
ASP
A1133
12.747
16.789
−5.118
41.64
O


ATOM
671
OD2
ASP
A1133
13.953
16.054
−3.429
43.78
O


ATOM
672
C
ASP
A1133
11.207
12.94
−5.944
34.05
C


ATOM
673
O
ASP
A1133
11.739
12.66
−7.041
34.56
O


ATOM
674
N
PHE
A1134
10.49
12.067
−5.218
28.41
N


ATOM
675
CA
PHE
A1134
10.146
10.735
−5.744
24.7
C


ATOM
676
CB
PHE
A1134
9.28
9.939
−4.749
23.35
C


ATOM
677
CG
PHE
A1134
10.06
9.444
−3.583
22.72
C


ATOM
678
CD1
PHE
A1134
9.434
8.928
−2.485
22.8
C


ATOM
679
CD2
PHE
A1134
11.454
9.545
−3.574
22.21
C


ATOM
680
CE1
PHE
A1134
10.225
8.477
−1.407
26.8
C


ATOM
681
CE2
PHE
A1134
12.231
9.132
−2.522
23.45
C


ATOM
682
CZ
PHE
A1134
11.652
8.565
−1.446
22.5
C


ATOM
683
C
PHE
A1134
9.473
10.818
−7.109
22.06
C


ATOM
684
O
PHE
A1134
8.578
11.597
−7.275
21.7
O


ATOM
685
N
SER
A1135
9.928
10.048
−8.079
19.56
N


ATOM
686
CA
SER
A1135
9.24
10.001
−9.339
18.42
C


ATOM
687
CB
SER
A1135
10.033
10.836
−10.349
19.51
C


ATOM
688
OG
SER
A1135
9.252
11.189
−11.487
19.35
O


ATOM
689
C
SER
A1135
9.127
8.538
−9.816
17.14
C


ATOM
690
O
SER
A1135
10.052
7.971
−10.389
16.98
O


ATOM
691
N
HIS
A1136
8.002
7.906
−9.564
15.18
N


ATOM
692
CA
HIS
A1136
7.775
6.589
−10.15
12.41
C


ATOM
693
CB
HIS
A1136
8.12
5.487
−9.143
11.98
C


ATOM
694
CG
HIS
A1136
8.054
4.111
−9.726
12.38
C


ATOM
695
CD2
HIS
A1136
9.014
3.342
−10.296
12.91
C


ATOM
696
ND1
HIS
A1136
6.887
3.402
−9.823
10.71
N


ATOM
697
CE1
HIS
A1136
7.124
2.27
−10.449
14.23
C


ATOM
698
NE2
HIS
A1136
8.415
2.198
−10.725
8.48
N


ATOM
699
C
HIS
A1136
6.306
6.582
−10.556
11.29
C


ATOM
700
O
HIS
A1136
5.478
7.238
−9.9
10.24
O


ATOM
701
N
PRO
A1137
5.981
5.977
−11.708
10.16
N


ATOM
702
CD
PRO
A1137
6.95
5.593
−12.754
10.83
C


ATOM
703
CA
PRO
A1137
4.582
5.808
−12.11
9.53
C


ATOM
704
CB
PRO
A1137
4.65
5.004
−13.437
10.43
C


ATOM
705
CG
PRO
A1137
6.114
4.696
−13.672
11.57
C


ATOM
706
C
PRO
A1137
3.648
5.099
−11.124
9.5
C


ATOM
707
O
PRO
A1137
2.46
5.254
−11.205
11.49
O


ATOM
708
N
ASN
A1138
4.153
4.305
−10.205
9.85
N


ATOM
709
CA
ASN
A1138
3.317
3.68
−9.221
9.77
C


ATOM
710
CB
ASN
A1138
3.543
2.164
−9.193
9.54
C


ATOM
711
CG
ASN
A1138
3.25
1.539
−10.487
9.02
C


ATOM
712
OD1
ASN
A1138
4.175
0.982
−11.148
10.24
O


ATOM
713
ND2
ASN
A1138
1.987
1.653
−10.932
9.34
N


ATOM
714
C
ASN
A1138
3.502
4.246
−7.809
10.27
C


ATOM
715
O
ASN
A1138
3.104
3.638
−6.837
9.17
O


ATOM
716
N
VAL
A1139
4.045
5.448
−7.727
11.2
N


ATOM
717
CA
VAL
A1139
4.147
6.196
−6.473
11.12
C


ATOM
718
CB
VAL
A1139
5.614
6.467
−6.114
10.21
C


ATOM
719
CG1
VAL
A1139
5.682
7.242
−4.755
9.07
C


ATOM
720
CG2
VAL
A1139
6.356
5.132
−6.068
5.79
C


ATOM
721
C
VAL
A1139
3.411
7.492
−6.689
11.77
C


ATOM
722
O
VAL
A1139
3.647
8.158
−7.713
10.94
O


ATOM
723
N
LEU
A1140
2.522
7.823
−5.745
13.02
N


ATOM
724
CA
LEU
A1140
1.71
9.03
−5.83
15.05
C


ATOM
725
CB
LEU
A1140
0.503
8.927
−4.925
15.32
C


ATOM
726
CG
LEU
A1140
−0.733
9.865
−4.978
14.43
C


ATOM
727
CD1
LEU
A1140
−0.669
10.86
−3.921
17.59
C


ATOM
728
CD2
LEU
A1140
−0.925
10.507
−6.316
12.71
C


ATOM
729
C
LEU
A1140
2.641
10.14
−5.355
17.56
C


ATOM
730
O
LEU
A1140
3.161
10.068
−4.248
18.36
O


ATOM
731
N
SER
A1141
2.944
11.121
−6.193
18.73
N


ATOM
732
CA
SER
A1141
3.834
12.13
−5.697
21.1
C


ATOM
733
CB
SER
A1141
5.055
12.328 
−6.649
24.1
C


ATOM
734
OG
SER
A1141
6.3
11.941
−6.014
26.54
O


ATOM
735
C
SER
A1141
3.144
13.464
−5.374
20.71
C


ATOM
736
O
SER
A1141
2.13
13.815
−5.93
19.98
O


ATOM
737
N
LEU
A1142
3.752
14.182
−4.45
20.91
N


ATOM
738
CA
LEU
A1142
3.323
15.505
−4.03
22.16
C


ATOM
739
CB
LEU
A1142
4.34
15.894
−2.937
23.71
C


ATOM
740
CG
LEU
A1142
4.041
16.699
−1.689
23.78
C


ATOM
741
CD1
LEU
A1142
3.912
18.061
−2.193
27.43
C


ATOM
742
CD2
LEU
A1142
2.719
16.18
−1.182
26.21
C


ATOM
743
C
LEU
A1142
3.373
16.496
−5.235
21.52
C


ATOM
744
O
LEU
A1142
4.395
16.47
−5.96
19.46
O


ATOM
745
N
LEU
A1143
2.31
17.314
−5.498
19.99
N


ATOM
746
CA
LEU
A1143
2.485
18.436
−6.495
19.13
C


ATOM
747
CB
LEU
A1143
1.204
18.79
−7.251
18.43
C


ATOM
748
CG
LEU
A1143
0.689
17.786
−8.297
18.69
C


ATOM
749
CD1
LEU
A1143
−0.597
18.167
−8.903
12.55
C


ATOM
750
CD2
LEU
A1143
1.731
17.452
−9.369
14.52
C


ATOM
751
C
LEU
A1143
3.082
19.719
−5.899
18.63
C


ATOM
752
O
LEU
A1143
3.836
20.444
−6.547
17.14
O


ATOM
753
N
GLY
A1144
2.692
20.033
−4.675
18.45
N


ATOM
754
CA
GLY
A1144
3.367
21.071
−3.916
18.59
C


ATOM
755
C
GLY
A1144
2.707
21.3
−2.586
19.82
C


ATOM
756
O
GLY
A1144
1.828
20.563
−2.135
19.78
O


ATOM
757
N
ILE
A1145
3.144
22.371
−1.964
22.33
N


ATOM
758
CA
ILE
A1145
2.663
22.855
−0.703
22.29
C


ATOM
759
CB
ILE
A1145
3.805
22.853
0.339
23.4
C


ATOM
760
CG2
ILE
A1145
3.223
22.796
1.739
22.81
C


ATOM
761
CG1
ILE
A1145
4.753
21.695
0.117
23.81
C


ATOM
762
CD1
ILE
A1145
4.176
20.356
0.659
27.04
C


ATOM
763
C
ILE
A1145
2.325
24.302
−0.914
22.87
C


ATOM
764
O
ILE
A1145
3.085
24.998
−1.56
22.95
O


ATOM
765
N
CYS
A1146
1.213
24.758
−0.345
24.26
N


ATOM
766
CA
CYS
A1146
1.049
26.164
−0.048
27.33
C


ATOM
767
CB
CYS
A1146
−0.335
26.706
−0.453
27.93
C


ATOM
768
SG
CYS
A1146
−0.799
25.936
−2.042
40.01
S


ATOM
769
C
CYS
A1146
1.314
26.435
1.413
26.36
C


ATOM
770
O
CYS
A1146
0.576
26.01
72.263
26.54
O


ATOM
771
N
LEU
A1147
2.381
27.169
1.681
26.97
N


ATOM
772
CA
LEU
A1147
2.702
27.677
3.028
26.84
C


ATOM
773
CB
LEU
A1147
4.215
27.96
3.13
25.24
C


ATOM
774
CG
LEU
A1147
5.124
26.744
3.04
23.65
C


ATOM
775
CD1
LEU
A1147
6.564
27.203
3.331
22.66
C


ATOM
776
CD2
LEU
A1147
4.686
25.628
4.009
22.26
C


ATOM
777
C
LEU
A1147
1.92
28.956
3.281
27.19
C


ATOM
778
O
LEU
A1147
2.092
29.949
2.592
27.3
O


ATOM
779
N
ARG
A1148
1.034
28.926
4.254
29.23
N


ATOM
780
CA
ARG
A1148
0.26
30.107
4.572
30.63
C


ATOM
781
CB
ARG
A1148
−1.216
29.77
4.627
29.46
C


ATOM
782
CG
ARG
A1148
−1.673
29.076
3.423
29.26
C


ATOM
783
CD
ARG
A1148
−3.153
29.009
3.391
24.3
C


ATOM
784
NE
ARG
A1148
−3.536
28.04
4.382
23.08
N


ATOM
785
CZ
ARG
A1148
−4.774
27.756
4.699
22.68
C


ATOM
786
NH1
ARG
A1148
−5.728
28.404
4.05
25.32
N


ATOM
787
NH2
ARG
A1148
−5.034
26.805
5.596
19.48
N


ATOM
788
C
ARG
A1148
0.772
30.687
5.885
32.3
C


ATOM
789
O
ARG
A1148
1.33
29.934
6.749
32.98
O


ATOM
790
N
SER
A1149
0.656
32.013
6.005
33.88
N


ATOM
791
CA
SER
A1149
0.938
32.721
7.301
35.81
C


ATOM
792
CB
SER
A1149
1.614
34.074
7.063
36.19
C


ATOM
793
OG
SER
A1149
3.02
34.017
7.166
40.64
O


ATOM
794
C
SER
A1149
−0.398
33.008
7.919
35.4
C


ATOM
795
O
SER
A1149
−0.839
34.149
7.871
38.1
O


ATOM
796
N
GLU
A1150
−1.06
31.972
8.401
33.94
N


ATOM
797
CA
GLU
A1150
−2.447
31.964
8.87
33.33
C


ATOM
798
CB
GLU
A1150
−3.232
33.244
8.587
33.3
C


ATOM
799
CG
GLU
A1150
−2.992
34.371
9.613
35.05
C


ATOM
800
CD
GLU
A1150
−3.965
35.531
9.472
36.72
C


ATOM
801
OE1
GLU
A1150
−3.696
36.603
10.093
41.98
O


ATOM
802
OE2
GLU
A1150
−5.026
35.391
8.789
41.29
O


ATOM
803
C
GLU
A1150
−3.119
30.737
8.235
30.98
C


ATOM
804
O
GLU
A1150
−3.349
30.674
7.024
29.7
O


ATOM
805
N
GLY
A1151
−3.385
29.744
9.066
28.12
N


ATOM
806
CA
GLY
A1151
−3.827
28.45
8.559
24.41
C


ATOM
807
C
GLY
A1151
−2.653
27.52
8.348
21.21
C


ATOM
808
O
GLY
A1151
−1.513
27.918
8.1
20.6
O


ATOM
809
N
SER
A1152
−2.965
26.243
8.455
19.89
N


ATOM
810
CA
SER
A1152
−2.038
25.175
8.252
16.36
C


ATOM
811
CB
SER
A1152
−2.709
23.894
8.687
16.61
C


ATOM
812
OG
SER
A1152
−2.738
23.798
10.107
17.18
O


ATOM
813
C
SER
A1152
−1.604
25.15
6.792
15.1
C


ATOM
814
O
SER
A1152
−2.313
25.628
5.915
16.63
O


ATOM
815
N
PRO
A1153
−0.426
24.621
6.515
13.76
N


ATOM
816
CD
PRO
A1153
0.58
24.139
7.483
13.56
C


ATOM
817
CA
PRO
A1153
−0.015
24.444
5.132
13.75
C


ATOM
818
CB
PRO
A1153
1.3
23.722
5.273
13.97
C


ATOM
819
CG
PRO
A1153
1.807
24.225
6.721
13.45
C


ATOM
820
C
PRO
A1153
−0.982
23.58
4.363
14.15
C


ATOM
821
O
PRO
A1153
−1.705
22.739
4.935
15.18
O


ATOM
822
N
LEU
A1154
−1.04
23.84
3.079
14.16
N


ATOM
823
CA
LEU
A1154
−1.901
23.118
2.192
15.42
C


ATOM
824
CB
LEU
A1154
−2.525
24.029
1.175
14.91
C


ATOM
825
CG
LEU
A1154
−3.898
24.572
1.467
19.4
C


ATOM
826
CD1
LEU
A1154
−4.454
24.434
2.886
17.68
C


ATOM
827
CD2
LEU
A1154
−3.97
25.964
0.981
16.05
C


ATOM
828
C
LEU
A1154
−0.996
22.156
1.485
14.7
C


ATOM
829
O
LEU
A1154
0.175
22.461
1.248
15.04
O


ATOM
830
N
VAL
A1155
−1.527
20.973
1.215
13.24
N


ATOM
831
CA
VAL
A1155
−0.806
20.022
0.444
12.27
C


ATOM
832
CB
VAL
A1155
−0.535
18.73
1.26
12.93
C


ATOM
833
CG1
VAL
A1155
−1.88
17.94
1.51
11.63
C


ATOM
834
CG2
VAL
A1155
0.462
17.886
0.543
13.81
C


ATOM
835
C
VAL
A1155
−1.622
19.8
−0.827
10.87
C


ATOM
836
O
VAL
A1155
−2.762
19.527
−0.794
12.07
O


ATOM
837
N
VAL
A1156
−0.977
19.902
−1.962
12.01
N


ATOM
838
CA
VAL
A1156
−1.583
19.681
−3.277
11.31
C


ATOM
839
CB
VAL
A1156
−1.229
20.937
−4.185
10.29
C


ATOM
840
CG1
VAL
A1156
−1.952
20.883
−5.456
11.18
C


ATOM
841
CG2
VAL
A1156
−1.469
22.212
−3.418
6.3
C


ATOM
842
C
VAL
A1156
−1.103
18.318
−3.926
11.26
C


ATOM
843
O
VAL
A1156
0.103
18.047
−4.127
11.04
O


ATOM
844
N
LEU
A1157
−2.064
17.505
−4.295
11.75
N


ATOM
845
CA
LEU
A1157
−1.796
16.193
−4.836
13.19
C


ATOM
846
CB
LEU
A1157
−2.393
15.103
−3.892
14.39
C


ATOM
847
CG
LEU
A1157
−1.414
14.668
−2.797
14.11
C


ATOM
848
CD1
LEU
A1157
−1.38
15.742
−1.819
18.43
C


ATOM
849
CD2
LEU
A1157
−1.93
13.478
−2.133
20.54
C


ATOM
850
C
LEU
A1157
−2.435
16.028
−6.195
14
C


ATOM
851
O
LEU
A1157
−3.476
16.716
−6.456
14.03
O


ATOM
852
N
PRO
A1158
−1.868
15.084
−7.043
13.2
N


ATOM
853
CD
PRO
A1158
−0.643
14.268
−6.906
11.65
C


ATOM
854
CA
PRO
A1158
−2.582
14.75
−8.303
13.36
C


ATOM
855
CB
PRO
A1158
−1.725
13.611
−8.951
11.42
C


ATOM
856
CG
PRO
A1158
−0.418
13.751
−8.253
10.64
C


ATOM
857
C
PRO
A1158
−4.015
14.35
−8.05
12.86
C


ATOM
858
O
PRO
A1158
−4.261
13.651
−7.092
14.24
O


ATOM
859
N
TYR
A1159
−4.932
14.859
−8.858
13.23
N


ATOM
860
CA
TYR
A1159
−6.252
14.393
−8.865
13.78
C


ATOM
861
CB
TYR
A1159
−7.058
15.142
−9.93
15.01
C


ATOM
862
CG
TYR
A1159
−8.481
14.649
−9.961
12.86
C


ATOM
863
CD1
TYR
A1159
−9.297
14.773
−8.806
12.4
C


ATOM
864
CE1
TYR
A1159
−10.556
14.308
−8.758
11.04
C


ATOM
865
CD2
TYR
A1159
−8.985
13.989
−11.08
13.73
C


ATOM
866
CE2
TYR
A1159
−10.307
13.454
−11.037
13.1
C


ATOM
867
CZ
TYR
A1159
−11.07
13.657
−9.875
13.4
C


ATOM
868
OH
TYR
A1159
−12.355
13.191
−9.804
16.89
O


ATOM
869
C
TYR
A1159
−6.2
12.948
−9.211
15.49
C


ATOM
870
O
TYR
A1159
−5.444
12.519
−10.099
16.43
O


ATOM
871
N
MET
A1160
−6.991
12.165
−8.506
16.74
N


ATOM
872
CA
MET
A1160
−6.931
10.714
−8.614
16.11
C


ATOM
873
CB
MET
A1160
−6.311
10.119
−7.325
17.37
C


ATOM
874
CG
MET
A1160
−5.161
9.13
−7.551
19.28
C


ATOM
875
SD
MET
A1160
−3.813
9.522
−8.699
23.59
S


ATOM
876
CE
MET
A1160
−3.543
7.869
−9.241
22.32
C


ATOM
877
C
MET
A1160
−8.355
10.257
−8.795
16.51
C


ATOM
878
O
MET
A1160
−9.082
9.992
−7.822
14.78
O


ATOM
879
N
LYS
A1161
−8.752
10.184
−10.066
16.45
N


ATOM
880
CA
LYS
A1161
−10.146
9.947
−10.418
17.31
C


ATOM
881
CB
LYS
A1161
−10.245
9.711
−11.902
17.73
C


ATOM
882
CG
LYS
A1161
−11.664
9.683
−12.341
20.77
C


ATOM
883
CD
LYS
A1161
−11.705
9.365
−13.814
24.83
C


ATOM
884
CE
LYS
A1161
−13.144
9.363
−14.295
25.08
C


ATOM
885
NZ
LYS
A1161
−13.025
9.002
−15.7
26.92
N


ATOM
886
C
LYS
A1161
−10.867
8.77
−9.707
16.89
C


ATOM
887
O
LYS
A1161
−12.07
8.888
−9.275
17.09
O


ATOM
888
N
HIS
A1162
−10.193
7.624
−9.613
15.69
N


ATOM
889
CA
HIS
A1162
−10.88
6.482
−8.989
15.59
C


ATOM
890
CB
HIS
A1162
−10.72
5.207
−9.789
14.21
C


ATOM
891
CG
HIS
A1162
−11.262
5.341
−11.169
13.81
C


ATOM
892
CD2
HIS
A1162
−10.65
5.378
−12.376
15.14
C


ATOM
893
ND1
HIS
A1162
−12.602
5.556
−11.41
14.06
N


ATOM
894
CE1
HIS
A1162
−12.797
5.689
−12.713
16.19
C


ATOM
895
NE2
HIS
A1162
−11.631
5.557
−13.328
16.34
N


ATOM
896
C
HIS
A1162
−10.631
6.293
−7.505
15.76
C


ATOM
897
O
HIS
A1162
−11.07
5.273
−6.918
17.54
O


ATOM
898
N
GLY
A1163
−9.981
7.281
−6.891
14.54
N


ATOM
899
CA
GLY
A1163
−9.797
7.311
−5.446
13.69
C


ATOM
900
C
GLY
A1163
−8.933
6.175
−4.992
13.15
C


ATOM
901
O
GLY
A1163
−8.07
5.685
−5.752
12.3
O


ATOM
902
N
ASP
A1164
−9.204
5.721
−3.784
13.21
N


ATOM
903
CA
ASP
A1164
−8.424
4.633
−3.228
15.24
C


ATOM
904
CB
ASP
A1164
−8.358
4.621
−1.67
15.61
C


ATOM
905
CG
ASP
A1164
−9.602
3.98
−0.995
20.21
C


ATOM
906
OD1
ASP
A1164 
−10.69
4.556
−0.969 
25.32
O


ATOM
907
OD2
ASP
A1164
−9.498
2.888
−0.421
27.01
O


ATOM
908
C
ASP
A1164
−8.831
3.266
−3.739
15.25
C


ATOM
909
O
ASP
A1164
−9.991
2.932
−3.954
14.63
O


ATOM
910
N
LEU
A1165
−7.802
2.456
−3.823
16.8
N


ATOM
911
CA
LEU
A1165
−7.867
1.131
−4.346
18.15
C


ATOM
912
CB
LEU
A1165
−6.471
0.555
−4.155
18.15
C


ATOM
913
CG
LEU
A1165
−6.254
−0.82
−4.745
18.98
C


ATOM
914
CD1
LEU
A1165
−6.799
−0.956
−6.187
19.58
C


ATOM
915
CD2
LEU
A1165
−4.782
−0.942
−4.773
23.5
C


ATOM
916
C
LEU
A1165
−8.88
0.262
−3.617
18.36
C


ATOM
917
O
LEU
A1165
−9.566
−0.575
−4.2
17.43
O


ATOM
918
O
GLN
A1166
−11.809
−1.243
−1.678
23.09
O


ATOM
919
N
GLN
A1166
−8.781
0.307
−2.284
20



ATOM
920
CA
GLN
A1166
−9.693
−0.321
−1.354
20



ATOM
921
C
GLN
A1166
−11.177
−0.243
−1.617
20



ATOM
922
CB
GLN
A1166
−9.303
−0.104
0.131
20



ATOM
923
CG
GLN
A1166
−9.599
−1.201
1.163
20



ATOM
924
CD
GLN
A1166
−11.008
−1.183
1.711
20



ATOM
925
OE1
GLN
A1166
−11.667
−0.191
1.668
20



ATOM
926
NE2
GLN
A1166
−11.455
−2.294
2.208
20



ATOM
927
N
ASN
A1167
−11.721
0.971
−1.76
22.82
N


ATOM
928
CA
ASN
A1167
−13.142
1.243
−2.091
22.98
C


ATOM
929
CB
ASN
A1167
−13.482
2.739
−1.849
23.61
C


ATOM
930
CG
ASN
A1167
−13.721
3.05
−0.404
24.86
C


ATOM
931
OD1
ASN
A1167
−14.747
2.681
0.17
29.97
O


ATOM
932
ND2
ASN
A1167
−12.777
3.729
0.201
24.59
N


ATOM
933
C
ASN
A1167
−13.365
0.97
−3.554
22.09
C


ATOM
934
O
ASN
A1167
−14.472
0.568
−3.972
22.42
O


ATOM
935
N
PHE
A1168
−12.336
1.214
−4.352
20.93
N


ATOM
936
CA
PHE
A1168
−12.444
0.801
−5.741
21.8
C


ATOM
937
CB
PHE
A1168
−11.238
1.267
−6.545
22.22
C


ATOM
938
CG
PHE
A1168
−11.36
1.012
−7.966
23.93
C


ATOM
939
CD1
PHE
A1168
−12.022
1.922
−8.777
28.08
C


ATOM
940
CD2
PHE
A1168
−10.854
−0.18
−8.513
28.78
C


ATOM
941
CE1
PHE
A1168
−12.208
1.659
−10.153
31.38
C


ATOM
942
CE2
PHE
A1168
−11.014
−0.482
−9.875
30.49
C


ATOM
943
CZ
PHE
A1168
−11.688
0.438
−10.709
29.96
C


ATOM
944
C
PHE
A1168
−12.742
−0.711
−5.906
20.84
C


ATOM
945
O
PHE
A1168
−13.71
−1.104
−6.509
21.8
O


ATOM
946
N
ILE
A1169
−11.932
−1.557
−5.318
21.69
N


ATOM
947
CA
ILE
A1169
−12.101
−3.02
−5.434
21.21
C


ATOM
948
CB
ILE
A1169
−10.79
−3.818
−4.97
20.88
C


ATOM
949
CG2
ILE
A1169
−9.584
−3.379
−5.84
16.89
C


ATOM
950
CG1
ILE
A1169
−10.53
−3.655
−3.444
20.13
C


ATOM
951
CD1
ILE
A1169
−9.219
−4.284
−2.912
17.66
C


ATOM
952
C
ILE
A1169
−13.327
−3.475
−4.699
22.65
C


ATOM
953
O
ILE
A1169
−13.956
−4.433
−5.044
24.92
O


ATOM
954
N
ARG
A1170
−13.696
−2.769
−3.675
24.78
N


ATOM
955
CA
ARG
A1170
−14.841
−3.173
−2.895
27.45
C


ATOM
956
CB
ARG
A1170
−14.573
−2.797
−1.471
26.7
C


ATOM
957
CG
ARG
A1170
−15.698
−2.707
−0.613
29.73
C


ATOM
958
CD
ARG
A1170
−15.338
−1.544
0.225
36.17
C


ATOM
959
NE
ARG
A1170
−15.115
−1.902
1.627
43.74
N


ATOM
960
CZ
ARG
A1170
−14.896
−0.989
2.59
45.61
C


ATOM
961
NH1
ARG
A1170
−14.837
0.324
2.25
37.76
N


ATOM
962
NH2
ARG
A1170
−14.718
−1.399
3.877
43.16
N


ATOM
963
C
ARG
A1170
−16.198
−2.692
−3.43
29.47
C


ATOM
964
O
ARG
A1170
−17.234
−3.059
−2.907
31.36
O


ATOM
965
N
ASN
A1171
−16.217
−1.936
−4.522
32.08
N


ATOM
966
CA
ASN
A1171
−17.475
−1.556
−5.177
33.39
C


ATOM
967
CB
ASN
A1171
−17.367
−0.142
−5.702
34.28
C


ATOM
968
CG
ASN
A1171
−18.728
0.484
−5.977
34.85
C


ATOM
969
OD1
ASN
A1171
−18.83
1.706
−6.129
32.84
O


ATOM
970
ND2
ASN
A1171
−19.779
−0.34
−6.017
34.99
N


ATOM
971
C
ASN
A1171
−17.889
−2.476
−6.327
33.85
C


ATOM
972
O
ASN
A1171
−17.171
−2.562
−7.326
32.39
O


ATOM
973
N
GLU
A1172
−19.046
−3.143
−6.172
35.59
N


ATOM
974
CA
GLU
A1172
−19.548
−4.089
−7.207
37.83
C


ATOM
975
CB
GLU
A1172
−20.558
−5.143
−6.681
38.24
C


ATOM
976
CG
GLU
A1172
−20.166
−5.831
−5.304
42.55
C


ATOM
977
CD
GLU
A1172
−18.806
−6.659
−5.293
48.09
C


ATOM
978
OE1
GLU
A1172
−18.827
−7.858
−5.695
49.77
O


ATOM
979
OE2
GLU
A1172
−17.727
−6.153
−4.82
48.47
O


ATOM
980
C
GLU
A1172
−20.001
−3.393
−8.499
37.62
C


ATOM
981
O
GLU
A1172
−20.113
−4.038
−9.537
38.48
O


ATOM
982
N
THR
A1173
−20.151
−2.072
−8.448
37.81
N


ATOM
983
CA
THR
A1173
−20.229
−1.225
−9.646
38.22
C


ATOM
984
CB
THR
A1173
−20.255
0.238
−9.247
38.54
C


ATOM
985
OG1
THR
A1173
−21.41
0.471
−8.421
42.46
O


ATOM
986
CG2
THR
A1173
−20.294
1.169
−10.489
39.4
C


ATOM
987
C
THR
A1173
−19.051
−1.353
−10.595
37.94
C


ATOM
988
O
THR
A1173
−19.151
−0.997
−11.783
39.05
O


ATOM
989
N
HIS
A1174
−17.913
−1.768
−10.058
36.95
N


ATOM
990
CA
HIS
A1174
−16.674
−1.912
−10.826
36.02
C


ATOM
991
CB
HIS
A1174
−15.462
−1.363
−10.036
37.52
C


ATOM
992
CG
HIS
A1174
−15.661
−0.004
−9.393
41.68
C


ATOM
993
CD2
HIS
A1174
−14.856
1.087
−9.375
42.46
C


ATOM
994
ND1
HIS
A1174
−16.769
0.337
−8.635
47.13
N


ATOM
995
CE1
HIS
A1174
−16.646
1.581
−8.205
44.27
C


ATOM
996
NE2
HIS
A1174
−15.493
2.056
−8.641
44.18
N


ATOM
997
C
HIS
A1174
−16.519
−3.437
−11
33.97
C


ATOM
998
O
HIS
A1174
−17.201
−4.25
−10.316
33.49
O


ATOM
999
N
ASN
A1175
−15.63
−3.856
−11.89
31.33
N


ATOM
1000
CA
ASN
A1175
−15.406
−5.303
−12.013
28.29
C


ATOM
1001
CB
ASN
A1175
−16.401
−5.944
−13.003
26.81
C


ATOM
1002
CG
ASN
A1175
−16.56
−7.457
−12.797
27.33
C


ATOM
1003
OD1
ASN
A1175
−16.965
−7.914
−11.714
25.48
O


ATOM
1004
ND2
ASN
A1175
−16.234
−8.25
−13.846
23.69
N


ATOM
1005
C
ASN
A1175
−13.967
−5.677
−12.35
26.55
C


ATOM
1006
O
ASN
A1175
−13.708
−6.266
−13.408
26.61
O


ATOM
1007
N
PRO
A1176
−13.036
−5.42
−11.418
25.23
N


ATOM
1008
CD
PRO
A1176
−13.117
−4.731
−10.105
24.47
C


ATOM
1009
CA
PRO
A1176
−11.683
−5.913
−11.71
24.16
C


ATOM
1010
CB
PRO
A1176
−10.826
−5.27
−10.581
24.13
C


ATOM
1011
CG
PRO
A1176
−11.784
−5.014
−9.455
23.25
C


ATOM
1012
C
PRO
A1176
−11.63
−7.463
−11.712
22.75
C


ATOM
1013
O
PRO
A1176
−12.121
−8.118
−10.79
23.37
O


ATOM
1014
N
THR
A1177
−11.114
−8.04
−12.784
21.08
N


ATOM
1015
CA
THR
A1177
−10.898
−9.469
−12.874
18.85
C


ATOM
1016
CB
THR
A1177
−10.494
−9.914
−14.3
18.88
C


ATOM
1017
OG1
THR
A1177
−9.242
−9.28
−14.634
19.84
O


ATOM
1018
CG2
THR
A1177
−11.598
−9.527
−15.347
18.87
C


ATOM
1019
C
THR
A1177
−9.757
−9.846
−11.899
17.26
C


ATOM
1020
O
THR
A1177
−9.065
−9.003
−11.348
15.8
O


ATOM
1021
N
VAL
A1178
−9.607
−11.133
−11.684
15.8
N


ATOM
1022
CA
VAL
A1178
−8.509
−11.651
−10.904
16.14
C


ATOM
1023
CB
VAL
A1178
−8.5
−13.223
−10.915
15.53
C


ATOM
1024
CG1
VAL
A1178
−7.309
−13.705
−10.261
15.69
C


ATOM
1025
CG2
VAL
A1178
−9.747
−13.793
−10.221
15.73
C


ATOM
1026
C
VAL
A1178
−7.219
−11.17
−11.532
14.86
C


ATOM
1027
O
VAL
A1178
−6.359
−10.704
−10.845
15.18
O


ATOM
1028
N
LYS
A1179
−7.085
−11.347
−12.847
15.44
N


ATOM
1029
CA
LYS
A1179
−5.966
−10.765
−13.584
16.04
C


ATOM
1030
CB
LYS
A1179
−6.177
−10.988
−15.109
16.98
C


ATOM
1031
CG
LYS
A1179
−5.079
−10.35
−16.015
18.66
C


ATOM
1032
CD
LYS
A1179
−4.147
−11.355
−16.683
18.04
C


ATOM
1033
CE
LYS
A1179
−3.388
−10.723
−17.929
20.93
C


ATOM
1034
NZ
LYS
A1179
−2.56
−11.797
−18.707
22.94
N


ATOM
1035
C
LYS
A1179
−5.727
−9.246
−13.248
14.25
C


ATOM
1036
O
LYS
A1179
−4.607
−8.793
−13.141
11.31
O


ATOM
1037
N
ASP
A1180
−6.812
−8.495
−13.133
14.79
N


ATOM
1038
CA
ASP
A1180
−6.788
−7.03
−12.867
15.14
C


ATOM
1039
CB
ASP
A1180
−8.224
−6.451
−13.001
15.66
C


ATOM
1040
CG
ASP
A1180
−8.624
−6.138
−14.446
21.29
C


ATOM
1041
OD1
ASP
A1180
−9.866
−5.915
−14.763
24.01
O


ATOM
1042
OD2
ASP
A1180
−7.679
−6.095
−15.281
27.62
O


ATOM
1043
C
ASP
A1180
−6.25
−6.82
−11.46
13.2
C


ATOM
1044
O
ASP
A1180
−5.379
−5.979
−11.212
13.36
O


ATOM
1045
N
LEU
A1181
−6.756
−7.615
−10.527
11.47
N


ATOM
1046
CA
LEU
A1181
−6.303
−7.517
−9.13
9.77
C


ATOM
1047
CB
LEU
A1181
−7.187
−8.413
−8.305
9.68
C


ATOM
1048
CG
LEU
A1181
−8.476
−7.975
−7.638
7.92
C


ATOM
1049
CD1
LEU
A1181
−8.865
−6.576
−7.944
8.74
C


ATOM
1050
CD2
LEU
A1181
−9.58
−9
−7.905
3.42
C


ATOM
1051
C
LEU
A1181
−4.848
−7.876
−8.912
8.81
C


ATOM
1052
O
LEU
A1181
−4.104
−7.223
−8.163
8.69
O


ATOM
1053
N
ILE
A1182
−4.408
−8.927
−9.57
8.8
N


ATOM
1054
CA
ILE
A1182
−2.986
−9.267
−9.562
8.84
C


ATOM
1055
CB
ILE
A1182
−2.76
−10.613
−10.313
10.68
C


ATOM
1056
CG2
ILE
A1182
−1.247
−11.036
−10.247
7.66
C


ATOM
1057
CG1
ILE
A1182
−3.664
−11.715
−9.681
10.62
C


ATOM
1058
CD1
ILE
A1182
−3.664
−13.062
−10.422
12.08
C


ATOM
1059
C
ILE
A1182
−2.176
−8.16
−10.181
8.2
C


ATOM
1060
O
ILE
A1182
−1.12
−7.817
−9.686
8.72
O


ATOM
1061
N
GLY
A1183
−2.646
−7.59
−11.278
7.96
N


ATOM
1062
CA
GLY
A1183
−2.02
−6.43
−11.836
8.15
C


ATOM
1063
C
GLY
A1183
−1.877
−5.284
−10.854
9.46
C


ATOM
1064
O
GLY
A1183
−0.836
−4.71
−10.786
9.11
O


ATOM
1065
N
PHE
A1184
−2.966
−4.912
−10.133
11.34
N


ATOM
1066
CA
PHE
A1184
−2.919
−3.923
−9.065
10.26
C


ATOM
1067
CB
PHE
A1184
−4.239
−3.763
−8.316
9.89
C


ATOM
1068
CG
PHE
A1184
−5.4
−3.275
−9.179
11.92
C


ATOM
1069
CD1
PHE
A1184
−5.194
−2.497
−10.285
14.53
C


ATOM
1070
CD2
PHE
A1184
−6.724
−3.591
−8.847
14.63
C


ATOM
1071
CE1
PHE
A1184
−6.273
−2.09
−11.091
15.48
C


ATOM
1072
CE2
PHE
A1184
−7.779
−3.188
−9.636
14.52
C


ATOM
1073
CZ
PHE
A1184
−7.539
−2.445
−10.775
12.06
C


ATOM
1074
C
PHE
A1184
−1.799
−4.254
−8.124
10.46
C


ATOM
1075
O
PHE
A1184
−0.991
−3.356
−7.809
10.91
O


ATOM
1076
N
GLY
A1185
−1.732
−5.534
−7.687
10.44
N


ATOM
1077
CA
GLY
A1185
−0.685
−6.022
−6.776
7.06
C


ATOM
1078
C
GLY
A1185
0.675
−5.808
−7.442
7.98
C


ATOM
1079
O
GLY
A1185
1.649
−5.263
−6.834
8.85
O


ATOM
1080
N
LEU
A1186
0.788
−6.237
−8.698
7.09
N


ATOM
1081
CA
LEU
A1186
2.034
−5.966
−9.473
6.15
C


ATOM
1082
CB
LEU
A1186
1.97
−6.564
−10.864
3.48
C


ATOM
1083
CG
LEU
A1186
3.21
−6.47
−11.81
7.84
C


ATOM
1084
CD1
LEU
A1186
4.5
−6.921 
−11.173
10.47
C


ATOM
1085
CD2
LEU
A1186
2.965
−7.238
−13.117
5.94
C


ATOM
1086
C
LEU
A1186
2.456
−4.469
−9.46
6.45
C


ATOM
1087
O
LEU
A1186
3.646
−4.159
−9.149
8.35
O


ATOM
1088
N
GLN
A1187
1.518
−3.556
−9.706
4.69
N


ATOM
1089
CA
GLN
A1187
1.827
−2.119
−9.774
7.07
C


ATOM
1090
CB
GLN
A1187
0.559
−1.336
−10.225
7.15
C


ATOM
1091
CG
GLN
A1187
0.145
−1.578
−11.706
9.39
C


ATOM
1092
CD
GLN
A1187
−1.053
−0.767
−12.136
9.26
C


ATOM
1093
OE1
GLN
A1187
−1.039
0.462
−12.092
11.28
O


ATOM
1094
NE2
GLN
A1187
−2.08
−1.441
−12.595
10.28
N


ATOM
1095
C
GLN
A1187
2.328
−1.586
−8.435
7.09
C


ATOM
1096
O
GLN
A1187
3.262
−0.835
−8.35
8.11
O


ATOM
1097
N
VAL
A1188
1.657
−1.962
−7.355
8.62
N


ATOM
1098
CA
VAL
A1188
2.069
−1.609
−6.017
7.25
C


ATOM
1099
CB
VAL
A1188
1.029
−2.178
−4.976
7.78
C


ATOM
1100
CG1
VAL
A1188
1.56
−1.976
−3.526
6.03
C


ATOM
1101
CG2
VAL
A1188
−0.316
−1.492
−5.103
6.83
C


ATOM
1102
C
VAL
A1188
3.452
−2.217
−5.683
7.86
C


ATOM
1103
O
VAL
A1188
4.251
−1.56
−5.06
9.73
O


ATOM
1104
N
ALA
A1189
3.692
−3.491
−5.993
6.51
N


ATOM
1105
CA
ALA
A1189
5.007
−4.053
−5.813
6.67
C


ATOM
1106
CB
ALA
A1189
5.075
−5.504
−6.374
5.44
C


ATOM
1107
C
ALA
A1189
6.071
−3.189
−6.516
7.79
C


ATOM
1108
O
ALA
A1189
7.194
−3.024
−5.945
7.89
O


ATOM
1109
N
LYS
A1190
5.787
−2.67
−7.758
6.25
N


ATOM
1110
CA
LYS
A1190
6.796
−1.834
−8.454
4.83
C


ATOM
1111
CB
LYS
A1190
6.361
−1.573
−9.894
5.09
C


ATOM
1112
CG
LYS
A1190
6.426
−2.867
−10.641
6.53
C


ATOM
1113
CD
LYS
A1190
5.901
−2.797
−12.039
11.48
C


ATOM
1114
CE
LYS
A1190
6.178
−4.122
−12.805
10.35
C


ATOM
1115
NZ
LYS
A1190
5.376
−4.012
−14.119
5.13
N


ATOM
1116
C
LYS
A1190
7.025
−0.52
−7.774
5.07
C


ATOM
1117
O
LYS
A1190
8.171
−0.069
−7.643
6.03
O


ATOM
1118
N
GLY
A1191
5.919
0.157
−7.41
5.61
N


ATOM
1119
CA
GLY
A1191
5.97
1.325
−6.513
5.95
C


ATOM
1120
C
GLY
A1191
6.781
1.045
−5.299
6.41
C


ATOM
1121
O
GLY
A1191
7.707
1.773
−4.994
7.75
O


ATOM
1122
N
MET
A1192
6.487
−0.048
−4.587
7.71
N


ATOM
1123
CA
MET
A1192
7.236
−0.323
−3.339
8.41
C


ATOM
1124
CB
MET
A1192
6.577
−1.482
−2.653
10.35
C


ATOM
1125
CG
MET
A1192
5.282
−1.115
−1.963
9.89
C


ATOM
1126
SD
MET
A1192
5.581
0.263
−0.802
14.47
S


ATOM
1127
CE
MET
A1192
6.863
−0.345
0.254
11.37
C


ATOM
1128
C
MET
A1192
8.718
−0.659
−3.568
9.94
C


ATOM
1129
O
MET
A1192
9.61
−0.216
−2.828
9.3
O


ATOM
1130
N
LYS
A1193
9.004
−1.42
−4.634
9.24
N


ATOM
1131
CA
LYS
A1193
10.367
−1.654
−5.007
8.67
C


ATOM
1132
CB
LYS
A1193
10.443
−2.536
−6.202
8.81
C


ATOM
1133
CG
LYS
A1193
11.81
−3.023
−6.484
10.02
C


ATOM
1134
CD
LYS
A1193
11.979
−3.575
−7.901
8.96
C


ATOM
1135
CE
LYS
A1193
13.498
−3.572
−8.277
9.49
C


ATOM
1136
NZ
LYS
A1193
13.743
−4.27
−9.513
15.27
N


ATOM
1137
C
LYS
A1193
11.12
−0.367
−5.26
9.78
C


ATOM
1138
O
LYS
A1193
12.272
−0.228
−4.873
9.11
O


ATOM
1139
N
TYR
A1194
10.451
0.594
−5.896
10.85
N


ATOM
1140
CA
TYR
A1194
11.023
1.904
−6.061
10.32
C


ATOM
1141
CB
TYR
A1194
10.051
2.76
−6.851
11.52
C


ATOM
1142
CG
TYR
A1194
10.526
4.172
−6.973
11.52
C


ATOM
1143
CD1
TYR
A1194
11.52
4.483
−7.857
9.72
C


ATOM
1144
CE1
TYR
A1194
11.998
5.785
−7.936
16.28
C


ATOM
1145
CD2
TYR
A1194
9.963
5.196
−6.179
12.54
C


ATOM
1146
CE2
TYR
A1194
10.407
6.485
−6.224
14.38
C


ATOM
1147
CZ
TYR
A1194
11.42
6.793
−7.129
18.51
C


ATOM
1148
OH
TYR
A1194
11.878
8.103
−7.25
19.47
O


ATOM
1149
C
TYR
A1194
11.39
2.561
−4.701
10.21
C


ATOM
1150
O
TYR
A1194
12.564
2.975
−4.43
9.3
O


ATOM
1151
N
LEU
A1195
10.378
2.622
−3.829
10.8
N


ATOM
1152
CA
LEU
A1195
10.464
3.313
−2.54
10.49
C


ATOM
1153
CB
LEU
A1195
9.125
3.189
−1.851
11.47
C


ATOM
1154
CG
LEU
A1195
8.115
4.35
−1.972
9.95
C


ATOM
1155
CD1
LEU
A1195
7.944
4.563
−3.323
16.01
C


ATOM
1156
CD2
LEU
A1195
6.792
3.895
−1.414
10.13
C


ATOM
1157
C
LEU
A1195
11.53
2.694
−1.692
10.23
C


ATOM
1158
O
LEU
A1195
12.311
3.368
−1.107
11.31
O


ATOM
1159
N
ALA
A1196
11.587
1.377
−1.681
11.66
N


ATOM
1160
CA
ALA
A1196
12.606
0.636
−0.935
12.04
C


ATOM
1161
CB
ALA
A1196
12.259
−0.832
−0.918
14.25
C


ATOM
1162
C
ALA
A1196
14.031
0.83
−1.442
11.92
C


ATOM
1163
O
ALA
A1196
14.956
0.679
−0.685
10.62
O


ATOM
1164
N
SER
A1197
14.196
1.198
−2.704
12.53
N


ATOM
1165
CA
SER
A1197
15.516
1.523
−3.258
14.34
C


ATOM
1166
CB
SER
A1197
15.512
1.502
−4.809
12.95
C


ATOM
1167
OG
SER
A1197
14.768
2.609
−5.335
18.14
O


ATOM
1168
C
SER
A1197
15.982
2.872
−2.776
15.31
C


ATOM
1169
O
SER
A1197
17.15
13.148
−2.812
15.58
O


ATOM
1170
N
LYS
A1198
15.038
3.733
−2.368
17.2
N


ATOM
1171
CA
LYS
A1198
15.335
5.058
−1.872
17.87
C


ATOM
1172
CB
LYS
A1198
14.182
5.996
−2.238
18.38
C


ATOM
1173
CG
LYS
A1198
13.869
6.115
−3.698
20.26
C


ATOM
1174
CD
LYS
A1198
15.011
6.846
−4.464
25.11
C


ATOM
1175
CE
LYS
A1198
14.913
6.593
−6.028
30.26
C


ATOM
1176
NZ
LYS
A1198
16.214
6.552
−6.827
23.87
N


ATOM
1177
C
LYS
A1198
15.376
4.861
−0.383
19
C


ATOM
1178
O
LYS
A1198
15.387
5.808
0.383
20.3
O


ATOM
1179
N
LYS
A1199
15.344
3.605
0.022
18.71
N


ATOM
1180
CA
LYS
A1199
15.19
3.22
1.411
20.01
C


ATOM
1181
CB
LYS
A1199
16.523
3.188
2.164
20.74
C


ATOM
1182
CG
LYS
A1199
17.471
4.222
1.788
21.64
C


ATOM
1183
CD
LYS
A1199
18.294
3.84
0.543
31.5
C


ATOM
1184
CE
LYS
A1199
19.039
2.467
0.574
29.62
C


ATOM
1185
NZ
LYS
A1199
18.412
1.599
1.567
28.43
N


ATOM
1186
C
LYS
A1199
14.135
4.038
2.147
19.36
C


ATOM
1187
O
LYS
A1199
14.377
4.557
3.212
19.28
O


ATOM
1188
N
PHE
A1200
12.961
4.151
1.547
18.79
N


ATOM
1189
CA
PHE
A1200
11.834
4.788
2.197
17.86
C


ATOM
1190
CB
PHE
A1200
11.029
5.568
1.14
17.17
C


ATOM
1191
CG
PHE
A1200
9.743
6.111
1.664
18.38
C


ATOM
1192
CD1
PHE
A1200
8.571
5.39
1.535
12.53
C


ATOM
1193
CD2
PHE
A1200
9.718
7.361
2.338
17
C


ATOM
1194
CE1
PHE
A1200
7.385
5.872
2.071
15.8
C


ATOM
1195
CE2
PHE
A1200
8.535
7.851
2.811
14.97
C


ATOM
1196
CZ
PHE
A1200
7.349
7.091
2.689
13.81
C


ATOM
1197
C
PHE
A1200
11.01
3.658
2.786
16.62
C


ATOM
1198
O
PHE
A1200
10.479
2.841
2.025
16.28
O


ATOM
1199
N
VAL
A1201
10.893
3.612
4.107
16.06
N


ATOM
1200
CA
VAL
A1201
9.965
2.684
4.803
14.92
C


ATOM
1201
CB
VAL
A1201
10.506
2.167
6.16
14.85
C


ATOM
1202
CG1
VAL
A1201
9.448
1.315
6.839
14.19
C


ATOM
1203
CG2
VAL
A1201
11.84 
1.313
5.982
12.79
C


ATOM
1204
C
VAL
A1201
8.575
3.318
4.939
15.98
C


ATOM
1205
O
VAL
A1201
8.428
4.412
5.475
18.87
O


ATOM
1206
N
HIS
A1202
7.552
2.661
4.405
15.17
N


ATOM
1207
CA
HIS
A1202
6.283
3.264
4.251
14.89
C


ATOM
1208
CB
HIS
A1202
5.491
2.509
3.135
15.35
C


ATOM
1209
CG
HIS
A1202
4.164
3.144
2.826
17.55
C


ATOM
1210
CD2
HIS
A1202
3.75
3.885
1.765
20.15
C


ATOM
1211
ND1
HIS
A1202
3.118
3.161
3.736
15.04
N


ATOM
1212
CE1
HIS
A1202
2.11
3.845
3.218
17.84
C


ATOM
1213
NE2
HIS
A1202
2.462
4.291
2.023
17.78
N


ATOM
1214
C
HIS
A1202
5.505
3.343
5.591
14.91
C


ATOM
1215
O
HIS
A1202
4.95
4.386
5.964
12.58
O


ATOM
1216
N
ARG
A1203
5.426
2.179
6.266
16.87
N


ATOM
1217
CA
ARG
A1203
4.83
1.98
7.621
17.09
C


ATOM
1218
CB
ARG
A1203
5.296
3.035
8.654
16.92
C


ATOM
1219
CG
ARG
A1203
6.843
3.146
8.598
25.55
C


ATOM
1220
CD
ARG
A1203
7.385
3.934
9.684
35.04
C


ATOM
1221
NE
ARG
A1203
6.647
5.198
9.715
46.62
N


ATOM
1222
CZ
ARG
A1203
7.231
6.397
9.8
50.6
C


ATOM
1223
NH1
ARG
A1203
6.485
7.493
9.835
51.11
N


ATOM
1224
NH2
ARG
A1203
8.569
6.492
9.91
52.32
N


ATOM
1225
C
ARG
A1203
3.316
1.808
7.598
15.31
C


ATOM
1226
O
ARG
A1203
2.804
1.194
8.459
16.7
O


ATOM
1227
N
ASP
A1204
2.634
2.256
6.567
14.71
N


ATOM
1228
CA
ASP
A1204
1.216
2.108
6.521
13.7
C


ATOM
1229
CB
ASP
A1204
0.457
3.387
6.964
12.97
C


ATOM
1230
CG
ASP
A1204
−1.043
3.076
7.256
14.25
C


ATOM
1231
OD1
ASP
A1204
−1.836
4.044
7.394
15.49
O


ATOM
1232
OD2
ASP
A1204
−1.44
1.858
7.263
9.66
O


ATOM
1233
C
ASP
A1204
0.774
1.643
5.141
12.88
C


ATOM
1234
O
ASP
A1204
−0.186
2.174
4.56
14.12
O


ATOM
1235
N
LEU
A1205
1.478
0.646
4.609
11.34
N


ATOM
1236
CA
LEU
A1205
1.112
0.108
3.321
8.79
C


ATOM
1237
CB
LEU
A1205
2.258
−0.744
2.749
8.43
C


ATOM
1238
CG
LEU
A1205
1.935
−1.463
1.458
10.04
C


ATOM
1239
CD1
LEU
A1205
1.684
−0.398
0.27
13.53
C


ATOM
1240
CD2
LEU
A1205
3.076
−2.419
1.125
13.6
C


ATOM
1241
C
LEU
A1205
−0.146
−0.673
3.471
7.99
C


ATOM
1242
O
LEU
A1205
−0.17
−1.624
4.263
8.8
O


ATOM
1243
N
ALA
A1206
−1.204
−0.28
2.738
7.11
N


ATOM
1244
CA
ALA
A1206
−2.522
−0.922
2.824
5.5
C


ATOM
1245
CB
ALA
A1206
−3.232
−0.459
4.063
4.27
C


ATOM
1246
C
ALA
A1206
−3.265
−0.446
1.584
6.81
C


ATOM
1247
O
ALA
A1206
−2.838
0.581
1.02
8.33
O


ATOM
1248
N
ALA
A1207
−4.313
−1.167
1.132
5.92
N


ATOM
1249
CA
ALA
A1207
−5.061
−0.819
−0.065
6.86
C


ATOM
1250
CB
ALA
A1207
−6.198
−1.931
−0.465
6.56
C


ATOM
1251
C
ALA
A1207
−5.664
0.575
−0.007
6.43
C


ATOM
1252
O
ALA
A1207
−5.717
1.282
−0.997
7.31
O


ATOM
1253
N
ARG
A1208
−6.118
0.96
1.163
8.2
N


ATOM
1254
CA
ARG
A1208
−6.685
2.317
1.469
7.4
C


ATOM
1255
CB
ARG
A1208
−7.153
2.406
2.935
5.83
C


ATOM
1256
CG
ARG
A1208
−6.069
2.35
3.935
6.41
C


ATOM
1257
CD
ARG
A1208
−6.516
2.624
5.392
7.75
C


ATOM
1258
NE
ARG
A1208
−5.463
2.178
6.312
9.76
N


ATOM
1259
CZ
ARG
A1208
−5.268
0.92
6.703
10.11
C


ATOM
1260
NH1
ARG
A1208
−6.079
−0.022
6.275
11.92
N


ATOM
1261
NH2
ARG
A1208
−4.249
0.595
7.505
10.73
N


ATOM
1262
C
ARG
A1208
−5.723
3.419
1.17
8.21
C


ATOM
1263
O
ARG
A1208
−6.139
4.544
0.915
9.68
O


ATOM
1264
N
ASN
A1209
−4.444
3.09
1.145
8.68
N


ATOM
1265
CA
ASN
A1209
−3.399
4.061
0.811
11.82
C


ATOM
1266
CB
ASN
A1209
−2.244
4.061
1.85
11.24
C


ATOM
1267
CG
ASN
A1209
−2.656
4.697
3.119
14.87
C


ATOM
1268
OD1
ASN
A1209
−3.234
5.806
3.092
17.92
O


ATOM
1269
ND2
ASN
A1209
−2.404
4.018
4.255
12.83
N


ATOM
1270
C
ASN
A1209
−2.83
3.996
−0.638
11.91
C


ATOM
1271
O
ASN
A1209
−1.844
4.607
−0.923
11.85
O


ATOM
1272
N
CYS
A1210
−3.491
3.295
−1.537
12.5
N


ATOM
1273
CA
CYS
A1210
−3.014
3.254
−2.893
12.98
C


ATOM
1274
CB
CYS
A1210
−2.797
1.789
−3.34
14.54
C


ATOM
1275
SG
CYS
A1210
−1.63
0.848
−2.296
12.02
S


ATOM
1276
C
CYS
A1210
−4.108
3.876
−3.657
13.31
C


ATOM
1277
O
CYS
A1210
−5.28
3.55
−3.418
13.93
O


ATOM
1278
N
MET
A1211
−3.749
4.745
−4.594
13.69
N


ATOM
1279
CA
MET
A1211
−4.737
5.583
−5.243
14.05
C


ATOM
1280
CB
MET
A1211
−4.318
7.044
−5.221
13.18
C


ATOM
1281
CG
MET
A1211
−4.372
7.766
−3.853
14.65
C


ATOM
1282
SD
MET
A1211
−6.007
7.72
−3.108
19.96
S


ATOM
1283
CE
MET
A1211
−5.754
6.684
−1.674
18.93
C


ATOM
1284
C
MET
A1211
−4.793
5.093
−6.651
15.42
C


ATOM
1285
O
MET
A1211
−3.861
4.454
−7.062
17.43
O


ATOM
1286
N
LEU
A1212
−5.844
5.432
−7.405
15.97
N


ATOM
1287
CA
LEU
A1212
−6.055
4.901
−8.741
16.16
C


ATOM
1288
CB
LEU
A1212
−7.151
3.801
−8.617
16.56
C


ATOM
1289
CG
LEU
A1212
−7.139
2.614
−9.573
17.65
C


ATOM
1290
CD1
LEU
A1212
−5.859
1.949
−9.639
23.51
C


ATOM
1291
CD2
LEU
A1212
−8.148
1.645
−9.272
19.13
C


ATOM
1292
C
LEU
A1212
−6.465
6.014
−9.699
16.21
C


ATOM
1293
O
LEU
A1212
−7.471
6.687
−9.487
14.42
O


ATOM
1294
N
ASP
A1213
−5.64
6.267
−10.72
17.29
N


ATOM
1295
CA
ASP
A1213
−5.966
7.277
−11.686
17.98
C


ATOM
1296
CB
ASP
A1213
−4.714
7.942
−12.234
17.61
C


ATOM
1297
CG
ASP
A1213
−4.057
7.162
−13.362
21.66
C


ATOM
1298
OD1
ASP
A1213
−4.672
6.193
−13.876
24.08
O


ATOM
1299
OD2
ASP
A1213
−2.912
7.535
−13.769
20.5
O


ATOM
1300
C
ASP
A1213
−6.965
6.79
−12.774
20.22
C


ATOM
1301
O
ASP
A1213
−7.448
5.629
−12.725
19.55
O


ATOM
1302
N
GLU
A1214
−7.314
7.705
−13.703
21.62
N


ATOM
1303
CA
GLU
A1214
−8.236
7.449
−14.83
23.37
C


ATOM
1304
CB
GLU
A1214
−8.604
8.755
−15.616
23.66
C


ATOM
1305
CG
GLU
A1214
−7.572
9.41
−16.542
26.65
C


ATOM
1306
CD
GLU
A1214
−6.209
9.664
−15.865
35.32
C


ATOM
1307
OE1
GLU
A1214
−5.163
9.62
−16.55
34.94
O


ATOM
1308
OE2
GLU
A1214
−6.161
9.901
−14.619
42.76
O


ATOM
1309
C
GLU
A1214
−7.781
6.309
−15.745
23.4
C


ATOM
1310
O
GLU
A1214
−8.61
5.643
−16.379
24.55
O


ATOM
1311
N
LYS
A1215
−6.481
6.04
−15.762
22.3
N


ATOM
1312
CA
LYS
A1215
−6.01
4.85
−16.476
22.72
C


ATOM
1313
CB
LYS
A1215
−4.601
5.007
−17.096
23.86
C


ATOM
1314
CG
LYS
A1215
−4.485
6.167
−18.063
27.17
C


ATOM
1315
CD
LYS
A1215
−5.679
6.128
−19.019
38.23
C


ATOM
1316
CE
LYS
A1215
−5.745
7.422
−19.897
43.79
C


ATOM
1317
NZ
LYS
A1215
−7.201
7.763
−20.262
43.62
N


ATOM
1318
C
LYS
A1215
−5.995
3.604
−15.657
20.86
C


ATOM
1319
O
LYS
A1215
−5.58
2.607
−16.183
20.64
O


ATOM
1320
N
PHE
A1216
−6.37
3.659
−14.377
18.46
N


ATOM
1321
CA
PHE
A1216
−6.214
2.522
−13.522
17.8
C


ATOM
1322
CB
PHE
A1216
−6.913
1.295
−14.107
17.25
C


ATOM
1323
CG
PHE
A1216
−8.348
1.556
−14.511
20.05
C


ATOM
1324
CD1
PHE
A1216
−8.761
1.389
−15.824
22.43
C


ATOM
1325
CD2
PHE
A1216
−9.284
2.024
−13.58
22.9
C


ATOM
1326
CE1
PHE
A1216
−10.076
1.681
−16.183
24.6
C


ATOM
1327
CE2
PHE
A1216
−10.624
2.314
−13.951
23.53 
C


ATOM
1328
CZ
PHE
A1216
−11.008
2.147
−15.237
22.85
C


ATOM
1329
C
PHE
A1216
−4.741
2.253
−13.216
17.5
C


ATOM
1330
O
PHE
A1216
−4.304
1.15
−13.082
18.14
O


ATOM
1331
N
THR
A1217
−3.957
3.298
−13.18
17.79
N


ATOM
1332
CA
THR
A1217
−2.607
3.219
−12.693
17.79
C


ATOM
1333
CB
THR
A1217
−1.804
4.287
−13.327
18.38
C


ATOM
1334
OG1
THR
A1217
−1.948
4.137
−14.748
21.49
O


ATOM
1335
CG2
THR
A1217
−0.354
4.224
−12.873
13.71
C


ATOM
1336
C
THR
A1217
−2.699
3.462
−11.183
17.99
C


ATOM
1337
O
THR
A1217
−3.245
4.477
−10.67
16.42
O


ATOM
1338
N
VAL
A1218
−2.215
2.44
−10.491
18.2
N


ATOM
1339
CA
VAL
A1218
−2.219
2.359
−9.016
15.99
C


ATOM
1340
CB
VAL
A1218
−2.161
0.864
−8.566
15.74
C


ATOM
1341
CG1
VAL
A1218
−2.229
0.783
−7.046
16.54
C


ATOM
1342
CG2
VAL
A1218
−3.25
0.032
−9.306
10.74
C


ATOM
1343
C
VAL
A1218
−0.991
3.132
−8.554
14.73
C


ATOM
1344
O
VAL
A1218
0.099
2.884
−9.049
13.83
O


ATOM
1345
N
LYS
A1219
−1.17
4.075
−7.639
14.58
N


ATOM
1346
CA
LYS
A1219
−0.015
4.811
−7.058
13.67
C


ATOM
1347
CB
LYS
A1219
−0.099
6.274
−7.451
15.2
C


ATOM
1348
CG
LYS
A1219
−0.59
6.535
−8.83
12.87
C


ATOM
1349
CD
LYS
A1219
0.553
7.063
−9.626
17.61
C


ATOM
1350
CE
LYS
A1219
0.129
8.243
−10.531
17.38
C


ATOM
1351
NZ
LYS
A1219
0.955
8.178
−11.791
20.39
N


ATOM
1352
C
LYS
A1219
0.04
4.726
−5.535
12.93
C


ATOM
1353
O
LYS
A1219
−0.889
5.08
−4.853
12.69
O


ATOM
1354
N
VAL
A1220
1.133
4.22
−5.006
13.18
N


ATOM
1355
CA
VAL
A1220
1.295
4.11
−3.584
14.16
C


ATOM
1356
CB
VAL
A1220
2.612
3.296
−3.195
15.1
C


ATOM
1357
CG1
VAL
A1220
2.647
2.973
−1.626
10.24
C


ATOM
1358
CG2
VAL
A1220
2.803
2.046
−4.12
13.42
C


ATOM
1359
C
VAL
A1220
1.368
5.516
−2.973
13.35
C


ATOM
1360
O
VAL
A1220
2.135
6.359
−3.443
12.9
O


ATOM
1361
N
ALA
A1221
0.59
5.731
−1.934
13.13
N


ATOM
1362
CA
ALA
A1221
0.477
7.015
−1.251
15.47
C


ATOM
1363
CB
ALA
A1221
−0.897
7.657
−1.458
14.33
C


ATOM
1364
C
ALA
A1221
0.767
6.868
0.204
17.59
C


ATOM
1365
O
ALA
A1221
0.471
5.839
0.824
17.38
O


ATOM
1366
N
ASP
A1222
1.379
7.919
0.731
22.48
N


ATOM
1367
CA
ASP
A1222
1.684
8.106
2.149
25.6
C


ATOM
1368
CB
ASP
A1222
3.192
8.125
2.428
27.07
C


ATOM
1369
CG
ASP
A1222
3.493
8.453
3.94
32.14
C


ATOM
1370
OD1
ASP
A1222
2.699
7.951
4.822
33.77
O


ATOM
1371
OD2
ASP
A1222
4.486
9.212
4.217
33.87
O


ATOM
1372
C
ASP
A1222
1.168
9.469
2.525
26.89
C


ATOM
1373
O
ASP
A1222
1.8
10.507
2.234
27.25
O


ATOM
1374
N
PHE
A1223
0.002
9.486
3.138
28.9
N


ATOM
1375
CA
PHE
A1223
−0.585
10.751
3.509
29.85
C


ATOM
1376
CB
PHE
A1223
−2.098
10.611
3.545
29.09
C


ATOM
1377
CG
PHE
A1223
−2.653
10.334
2.195
27.66
C


ATOM
1378
CD1
PHE
A1223
−2.643
11.317
1.22
26.86
C


ATOM
1379
CD2
PHE
A1223
−3.137
9.056
1.86
30.65
C


ATOM
1380
CE1
PHE
A1223
−3.089
11.039
−0.071
24.73
C


ATOM
1381
CE2
PHE
A1223
−3.645
8.786 
0.589
25.98
C


ATOM
1382
CZ
PHE
A1223
−3.582
9.774
−0.378
26.39
C


ATOM
1383
C
PHE
A1223
0.116
11.46
4.721
31.22
C


ATOM
1384
O
PHE
A1223
0.264
12.703
4.723
29.93
O


ATOM
1385
N
GLY
A1224
0.646
10.652
5.659
32.26
N


ATOM
1386
CA
GLY
A1224
1.429
11.172
6.793
32.77
C


ATOM
1387
C
GLY
A1224
1.115
12.632
7.186
32.9
C


ATOM
1388
O
GLY
A1224
1.627
13.595
6.547
34.83
O


ATOM
1389
N
LEU
A1225
0.298
12.814
8.224
30.34
N


ATOM
1390
CA
LEU
A1225
−0.024
14.15
8.732
28.57
C


ATOM
1391
CB
LEU
A1225
1.211
15.102
8.77
29.79
C


ATOM
1392
CG
LEU
A1225
1.929
15.448
10.104
30.95
C


ATOM
1393
CD1
LEU
A1225
3.437
15.355
10.005
34.31
C


ATOM
1394
CD2
LEU
A1225
1.597
16.811
10.571
30.73
C


ATOM
1395
C
LEU
A1225
−1.205
14.74
7.982
25.9
C


ATOM
1396
O
LEU
A1225
−1.955
15.535
8.544
24.79
O


ATOM
1397
N
ALA
A1226
−1.367
14.336
6.721
24.64
N


ATOM
1398
CA
ALA
A1226
−2.529
14.746
5.877
23.24
C


ATOM
1399
CB
ALA
A1226
−2.28
14.5
4.418
22.44
C


ATOM
1400
C
ALA
A1226
−3.874
14.179
6.293
22.93
C


ATOM
1401
O
ALA
A1226
−4.884
14.705
5.881
25.88
O


ATOM
1402
N
ARG
A1227
−3.899
13.13
7.111
21.9
N


ATOM
1403
CA
ARG
A1227
−5.103
12.644
7.801
20.66
C


ATOM
1404
CB
ARG
A1227
−5.072
11.105
8.016
20.71
C


ATOM
1405
CG
ARG
A1227
−4.785
10.27
16.78
21.21
C


ATOM
1406
CD
ARG
A1227
−4.87
8.73
7.056
25.36
C


ATOM
1407
NE
ARG
A1227
−4.892
7.917
5.827
26.96
N


ATOM
1408
CZ
ARG
A1227
−5.974
7.695
5.082
27.88
C


ATOM
1409
NH1
ARG
A1227
−7.16
8.212
5.416
26.34
N


ATOM
1410
NH2
ARG
A1227
−5.871
6.976
3.966
28.15
N


ATOM
1411
C
ARG
A1227
−5.291
13.342
9.152
18.83
C


ATOM
1412
O
ARG
A1227
−4.498
13.203
10.087
17.34
O


ATOM
1413
N
ASP
A1228
−6.334
14.138
9.243
18.68
N


ATOM
1414
CA
ASP
A1228
−6.686
14.721
10.519
18.91
C


ATOM
1415
CB
ASP
A1228
−7.921
15.575
10.374
17.57
C


ATOM
1416
CG
ASP
A1228
−7.668
16.824
9.579
19.31
C


ATOM
1417
OD1
ASP
A1228
−6.496 
17.218
9.34
19.72
O


ATOM
1418
OD2
ASP
A1228
−8.671
17.429
9.178
20.69
O


ATOM
1419
C
ASP
A1228
−6.912
13.643
11.584
19.75
C


ATOM
1420
O
ASP
A1228
−6.289
13.678
12.62
19.14
O


ATOM
1421
N
MET
A1229
−7.813
12.698
11.298
21.88
N


ATOM
1422
CA
MET
A1229
−8.063
11.56
12.135
25.64
C


ATOM
1423
CB
MET
A1229
−9.439
11.661
12.693
24.99
C


ATOM
1424
CG
MET
A1229
−9.704
12.994
13.452
30.42
C


ATOM
1425
SD
MET
A1229
−11.278
12.878
14.395
36.16
S


ATOM
1426
CE
MET
A1229
−12.571
12.228
13.252
35.24
C


ATOM
1427
C
MET
A1229
−7.998
10.279
11.382
24.56
C


ATOM
1428
O
MET
A1229
−8.016
10.252
10.174
24.7
O


ATOM
1429
N
TYR
A1230
−7.966
9.201
12.145
26.77
N


ATOM
1430
CA
TYR
A1230
−7.921
7.806
11.669
26.42
C


ATOM
1431
CB
TYR
A1230
−6.702
7.141
12.275
27.51
C


ATOM
1432
CG
TYR
A1230
−5.446
7.784
11.808
28.23
C


ATOM
1433
CD1
TYR
A1230
−5.082
9.065
12.25
29.43
C


ATOM
1434
CE1
TYR
A1230
−3.974
9.693
11.788
28.12
C


ATOM
1435
CD2
TYR
A1230
−4.679
7.176
10.867
28.14
C


ATOM
1436
CE2
TYR
A1230
−3.527
7.772
10.422
32.14
C


ATOM
1437
CZ
TYR
A1230
−3.187
9.036
10.871
30.68
C


ATOM
1438
OH
TYR
A1230
−2.021
9.609
10.379
32.92
O


ATOM
1439
C
TYR
A1230
−9.133
7.062
12.158
27.27
C


ATOM
1440
O
TYR
A1230
−9.575
7.242
13.318
28.05
O


ATOM
1441
N
ASP
A1231
−9.672
6.224
11.281
27.51
N


ATOM
1442
CA
ASP
A1231
−10.722
5.291
11.618
27.33
C


ATOM
1443
CB
ASP
A1231
−11.113
4.53
10.355
28.35
C


ATOM
1444
CG
ASP
A1231
−12.533
3.939
10.428
30.8
C


ATOM
1445
OD1
ASP
A1231
−12.904
3.368
11.506
27.15
O


ATOM
1446
OD2
ASP
A1231
−13.254
4.051
9.374
32.11
O


ATOM
1447
C
ASP
A1231
−10.189
4.316
12.672
26.73
C


ATOM
1448
O
ASP
A1231
−9.124
3.73
12.492
26.31
O


ATOM
1449
N
LYS
A1232
−10.921
4.162
13.772
26.23
N


ATOM
1450
CA
LYS
A1232
−10.512
3.29
14.858
26.77
C


ATOM
1451
CB
LYS
A1232
−11.386
3.552
16.076
27.66
C


ATOM
1452
CG
LYS
A1232
−12.866
3.335
15.895
29.64
C


ATOM
1453
CD
LYS
A1232
−13.584
3.778
17.234
33.88
C


ATOM
1454
CE
LYS
A1232
−15.158
3.919
17.075
37.98
C


ATOM
1455
NZ
LYS
A1232
−15.727
5.229
17.684
37.47
N


ATOM
1456
C
LYS
A1232
−10.572
1.803
14.483
26.25
C


ATOM
1457
O
LYS
A1232
−10.143
0.931
15.234
25.01
O


ATOM
1458
N
GLU
A1233
−11.11
1.547
13.299
25.77
N


ATOM
1459
CA
GLU
A1233
−11.279
0.232
12.787
25.68
C


ATOM
1460
CB
GLU
A1233
−12.34
0.277
11.688
26.68
C


ATOM
1461
CG
GLU
A1233
−13.789
−0.168
12.099
33.83
C


ATOM
1462
CD
GLU
A1233
−14.499
0.709
13.208
42.96
C


ATOM
1463
OE1
GLU
A1233
−14.86
0.117
14.302
42.59
O


ATOM
1464
OE2
GLU
A1233
−14.717
1.954
12.977
42.71
O


ATOM
1465
C
GLU
A1233
−9.963
−0.242
12.227
24.54
C


ATOM
1466
O
GLU
A1233
−9.769
−1.414
12.19
24.6
O


ATOM
1467
N
TYR
A1234
−9.048
0.655
11.801
23.56
N


ATOM
1468
CA
TYR
A1234
−7.777
0.205
11.19
22.08
C


ATOM
1469
CB
TYR
A1234
−7.554
0.688
9.75
24.83
C


ATOM
1470
CG
TYR
A1234
−8.779
0.596
8.908
27.05
C


ATOM
1471
CD1
TYR
A1234
−9.405
1.764
8.447
32.67
C


ATOM
1472
CE1
TYR
A1234
−10.59
1.71
7.702
34.74
C


ATOM
1473
CD2
TYR
A1234
−9.363
−0.637
8.628
28.02
C


ATOM
1474
CE2
TYR
A1234
−10.562
−0.729
7.895
30.43
C


ATOM
1475
CZ
TYR
A1234
−11.173
0.445
7.448
33.92
C


ATOM
1476
OH
TYR
A1234
−12.348
0.376
6.709
35.91
O


ATOM
1477
C
TYR
A1234
−6.604
0.532
12.054
19.79
C


ATOM
1478
O
TYR
A1234
−5.57
−0.125
11.991
19.58
O


ATOM
1479
N
TYR
A1235
−6.787
1.532
12.906
17.81
N


ATOM
1480
CA
TYR
A1235
−5.682
1.997
13.724
14.18
C


ATOM
1481
CB
TYR
A1235
−5.331
3.388
13.366
13.99
C


ATOM
1482
CG
TYR
A1235
−5.008
3.583
11.916
12.91
C


ATOM
1483
CD1
TYR
A1235
−3.681
3.405
11.449
8.54
C


ATOM
1484
CE1
TYR
A1235
−3.357
3.532
10.153
6.16
C


ATOM
1485
CD2
TYR
A1235
−6.053
3.895
10.984
12.53
C


ATOM
1486
CE2
TYR
A1235
−5.743
4.111
9.651
14.2
C


ATOM
1487
CZ
TYR
A1235
−4.38
3.917
9.229
14.55
C


ATOM
1488
OH
TYR
A1235
−4.077
4.129
7.868
15.24
O


ATOM
1489
C
TYR
A1235
−5.972
1.952
15.171
13.04
C


ATOM
1490
O
TYR
A1235
−7.039
2.27
15.597
12.41
O


ATOM
1491
N
SER
A1236
−4.999
1.454
15.887
12.87
N


ATOM
1492
CA
SER
A1236
−4.921
1.538
17.288
13.9
C


ATOM
1493
CB
SER
A1236
−4.209
0.295
17.817
13.75
C


ATOM
1494
OG
SER
A1236
−5.074
−0.828
17.649
14.05
O


ATOM
1495
C
SER
A1236
−4.083
2.768
17.579
15.02
C


ATOM
1496
O
SER
A1236
−3.273
3.238
16.72
13.02
O


ATOM
1497
N
VAL
A1237
−4.271
3.257
18.8
15.2
N


ATOM
1498
CA
VAL
A1237
−3.669
4.477
19.233
15.62
C


ATOM
1499
CB
VAL
A1237
−4.713
5.574
19.68
16.92
C


ATOM
1500
CG1
VAL
A1237
−3.991
6.947
19.977
14.81
C


ATOM
1501
CG2
VAL
A1237
−5.918
5.75
18.643
14.15
C


ATOM
1502
C
VAL
A1237
−2.757
4.186
20.391
17.2
C


ATOM
1503
O
VAL
A1237
−3.164
3.555
21.401
17.99
O


ATOM
1504
N
HIS
A1238
−1.532
4.675
20.285
16.58
N


ATOM
1505
CA
HIS
A1238
−0.63
4.538
21.372
16.6
C


ATOM
1506
CB
HIS
A1238
0.79
4.641
20.897
14.86
C


ATOM
1507
CG
HIS
A1238
1.781
4.197
21.91
18.5
C


ATOM
1508
CD2
HIS
A1238
2.607
3.122
21.943
22.35
C


ATOM
1509
ND1
HIS
A1238
2.023
4.899
23.075
21.05
N


ATOM
1510
CE1
HIS
A1238
2.961
4.28
23.78
23.43
C


ATOM
1511
NE2
HIS
A1238
3.336
3.197
23.116
23.63
N


ATOM
1512
C
HIS
A1238
−0.941
5.544
22.475
17.59
C


ATOM
1513
O
HIS
A1238
−0.965
6.753
22.219
16.29
O


ATOM
1514
N
ASN
A1239
−1.161
5.013
23.705
19.38
N


ATOM
1515
CA
ASN
A1239
−1.566
5.784
24.887
20.91
C


ATOM
1516
CB
ASN
A1239
−1.67
4.904
26.147
19.93
C


ATOM
1517
CG
ASN
A1239
−2.929
4.038
26.166
18.41
C


ATOM
1518
OD1
ASN
A1239
−2.947
2.919
26.751
13.41
O


ATOM
1519
ND2
ASN
A1239
−3.987
4.536
25.513
13.83
N


ATOM
1520
C
ASN
A1239
−0.63
6.964
25.164
23.6
C


ATOM
1521
O
ASN
A1239
−1.11
8.123
25.292
24.04
O


ATOM
1522
N
LYS
A1240
0.679
6.679
25.225
25.19
N


ATOM
1523
CA
LYS
A1240
1.674
7.662
25.602
27.16
C


ATOM
1524
CB
LYS
A1240
2.949
6.948
25.947
27.24
C


ATOM
1525
CG
LYS
A1240
2.753
5.852
27.025
31.39
C


ATOM
1526
CD
LYS
A1240
2.092
6.44
28.311
33.31
C


ATOM
1527
CE
LYS
A1240
1.02
5.512
28.908
35.74
C


ATOM
1528
NZ
LYS
A1240
0.389
6.132
30.138
33.11
N


ATOM
1529
C
LYS
A1240
1.924
8.663
24.477
29.32
C


ATOM
1530
O
LYS
A1240
1.67
9.871
24.627
30.53
O


ATOM
1531
N
THR
A1241
2.43
8.188
23.337
29.79
N


ATOM
1532
CA
THR
A1241
2.509
9.073
22.222
29.89
C


ATOM
1533
CB
THR
A1241
3.467
8.616
21.201
30.25
C


ATOM
1534
OG1
THR
A1241
3.185
9.403
20.037
33.35
O


ATOM
1535
CG2
THR
A1241
3.344
7.112
20.901
28.34
C


ATOM
1536
C
THR
A1241
1.096
9.212
21.643
30.22
C


ATOM
1537
O
THR
A1241
0.134
9.339
22.39
32.12
O


ATOM
1538
N
GLY
A1242
0.921
9.192
20.345
27.97
N


ATOM
1539
CA
GLY
A1242
−0.442
9.02
19.841
25.59
C


ATOM
1540
C
GLY
A1242
−0.261
8.357
18.492
23.61
C


ATOM
1541
O
GLY
A1242
−1.07
8.496
17.614
23.73
O


ATOM
1542
N
ALA
A1243
0.859
7.673
18.364
22.33
N


ATOM
1543
CA
ALA
A1243
1.246
6.956
17.18
21.48
C


ATOM
1544
CB
ALA
A1243
2.497
6.121
17.461
19.16
C


ATOM
1545
C
ALA
A1243
0.044
6.081
16.798
20.06
C


ATOM
1546
O
ALA
A1243
−0.532
5.452
17.648
18.79
O


ATOM
1547
N
LYS
A1244
−0.377
6.218
15.54
19.98
N


ATOM
1548
CA
LYS
A1244
−1.313
5.355
14.829
20.6
C


ATOM
1549
CB
LYS
A1244
−1.695
5.942
13.468
21.8
C


ATOM
1550
CG
LYS
A1244
−2.614
7.095
13.55
724.9
C


ATOM
1551
CD
LYS
A1244
−2.3
7.965
14.744
29.39
C


ATOM
1552
CE
LYS
A1244
−3.596
8.051
15.56
37.57
C


ATOM
1553
NZ
LYS
A1244
−4.284
6.676
15.714
36.7
N


ATOM
1554
C
LYS
A1244
−0.646
4.085
14.508
19.2
C


ATOM
1555
O
LYS
A1244
0.49
4.124
14.123
19.11
O


ATOM
1556
N
LEU
A1245
−1.368
2.966
14.627
18.63
N


ATOM
1557
CA
LEU
A1245
−0.791
1.644
14.347
17.18
C


ATOM
1558
CB
LEU
A1245
−0.369
0.954
15.664
16.59
C


ATOM
1559
CG
LEU
A1245
0.56
1.802
16.567
19.65
C


ATOM
1560
CD1
LEU
A1245
0.157
1.66
18.01
17.13
C


ATOM
1561
CD2
LEU
A1245
2.037
1.413
16.357
21.7
C


ATOM
1562
C
LEU
A1245
−1.757
0.774
13.587
14.78
C


ATOM
1563
O
LEU
A1245
−2.652
0.238
14.189
15
O


ATOM
1564
N
PRO
A1246
−1.545
0.587
12.279
13.51
N


ATOM
1565
CD
PRO
A1246
−0.403
1.159
11.572
14.89
C


ATOM
1566
CA
PRO
A1246
−2.353
−0.239
11.366
13.3
C


ATOM
1567
CB
PRO
A1246
−1.767
0.072
9.956
12.09
C


ATOM
1568
CG
PRO
A1246
−0.694
0.867
10.104
11.81
C


ATOM
1569
C
PRO
A1246
−2.172
−1.735
11.687
13.12
C


ATOM
1570
O
PRO
A1246
−1.721
−2.584
10.83
12.05
O


ATOM
1571
N
VAL
A1247
−2.472
−2.017
12.935
11.59
N


ATOM
1572
CA
VAL
A1247
−2.334
−3.363
13.565
12.32
C


ATOM
1573
CB
VAL
A1247
−3.255
−3.391
14.805
10.84
C


ATOM
1574
CG1
VAL
A1247
−3.524
−4.818
15.249
15.86
C


ATOM
1575
CG2
VAL
A1247
−2.617
−2.612
15.917
6.8
C


ATOM
1576
C
VAL
A1247
−2.446
−4.663
12.667
11.2
C


ATOM
1577
O
VAL
A1247
−1.546
−5.488
12.665
11.23
O


ATOM
1578
N
LYS
A1248
−3.525
−4.804
11.918
10.8
N


ATOM
1579
CA
LYS
A1248
−3.743
−5.957
11.027
12.03
C


ATOM
1580
CB
LYS
A1248
−5.177
−5.964
10.572
13.05
C


ATOM
1581
CG
LYS
A1248
−6.152
−5.331
11.58
19.76
C


ATOM
1582
CD
LYS
A1248
−7.062
−6.387
12.249
23.58
C


ATOM
1583
CE
LYS
A1248
−8.534
−5.932
12.134
30.55
C


ATOM
1584
NZ
LYS
A1248
−9.463
−6.69
13.084
34.02
N


ATOM
1585
C
LYS
A1248
−2.883
−6.023
9.745
10.65
C


ATOM
1586
O
LYS
A1248
−2.959
−6.994
8.999
9.86
O


ATOM
1587
N
TRP
A1249
−2.086
−4.981
9.491
10.31
N


ATOM
1588
CA
TRP
A1249
−1.18
−4.913
8.351
8.47
C


ATOM
1589
CB
TRP
A1249
−1.359
−3.605
7.607
8.12
C


ATOM
1590
CG
TRP
A1249
−2.504
−3.633
6.747
7.42
C


ATOM
1591
CD2
TRP
A1249
−3.871
−3.47
7.156
5.46
C


ATOM
1592
CE2
TRP
A1249
−4.665
−3.607
5.983
5.77
C


ATOM
1593
CE3
TRP
A1249
−4.494
−3.162
8.381
6
C


ATOM
1594
CD1
TRP
A1249
−2.526
−3.943
5.372
4.82
C


ATOM
1595
NE1
TRP
A1249
−3.811
−3.91
4.929
5.43
N


ATOM
1596
CZ2
TRP
A1249
−6.098
−3.459
6.001
6.63
C


ATOM
1597
CZ3
TRP
A1249
−5.928
−2.947
8.392
4.82
C


ATOM
1598
CH2
TRP
A1249
−6.698
−3.109
7.2
7.88
C


ATOM
1599
C
TRP
A1249
0.225
−5.008
8.863
8.81
C


ATOM
1600
O
TRP
A1249
1.186
−5.191
8.069
8.2
O


ATOM
1601
N
MET
A1250
0.346
−4.956
10.201
9.07
N


ATOM
1602
CA
MET
A1250
1.668
−4.953
10.821
10.3
C


ATOM
1603
CB
MET
A1250
1.62
−4.238
12.155
8.96
C


ATOM
1604
CG
MET
A1250
1.667
−2.721
12.005
10.76
C


ATOM
1605
SD
MET
A1250
1.131
−1.902
13.583
11.56
S


ATOM
1606
CE
MET
A1250
2.534
−2.069
14.536
12.6
C


ATOM
1607
C
MET
A1250
2.295
−6.361
10.962
12.06
C


ATOM
1608
O
MET
A1250
1.611
−7.327
11.333
11.13
O


ATOM
1609
N
ALA
A1251
3.614
−6.434
10.703
13.83
N


ATOM
1610
CA
ALA
A1251
4.46
−7.603
11.026
14.52
C


ATOM
1611
CB
ALA
A1251
5.94
−7.409
10.539
11.9
C


ATOM
1612
C
ALA
A1251
4.402
−7.944
12.522
16.24
C


ATOM
1613
O
ALA
A1251
4.346
−7.052
13.376
16.66
O


ATOM
1614
N
LEU
A1252
4.438
−9.232
12.86
18.73
N


ATOM
1615
CA
LEU
A1252
4.276
−9.537
14.27
21.52
C


ATOM
1616
CB
LEU
A1252
3.851
−10.996
14.594
21.72
C


ATOM
1617
CG
LEU
A1252
4.851
−12.116
14.433
23.21
C


ATOM
1618
CD1
LEU
A1252
5.321
−12.497
15.742
28.6
C


ATOM
1619
CD2
LEU
A1252
4.261
−13.324
13.792
24.47
C


ATOM
1620
C
LEU
A1252
5.478
−9.077
15.042
21.57
C


ATOM
1621
O
LEU
A1252
5.406
−8.936
16.224
23.8
O


ATOM
1622
N
GLU
A1253
6.569
−8.764
14.386
22.36
N


ATOM
1623
CA
GLU
A1253
7.621
−8.143
15.118
23.04
C


ATOM
1624
CB
GLU
A1253
9.001
−8.442
14.545
22.64
C


ATOM
1625
CG
GLU
A1253
9.349
−7.787
13.254
25.77
C


ATOM
1626
CD
GLU
A1253
8.924
−8.608
12.003
31.65
C


ATOM
1627
OE1
GLU
A1253
8.158
−9.631
12.111
30.46
O


ATOM
1628
OE2
GLU
A1253
9.38
−8.206
10.895
34.18
O


ATOM
1629
C
GLU
A1253
7.37
−6.682
15.304
24.06
C


ATOM
1630
O
GLU
A1253
7.937
−6.101
16.209
25.96
O


ATOM
1631
N
SER
A1254
6.544
−6.048
14.464
25.72
N


ATOM
1632
CA
SER
A1254
6.234
−4.615
14.679
26.4
C


ATOM
1633
CB
SER
A1254
5.766
−3.88
13.427
25.25
C


ATOM
1634
OG
SER
A1254
6.77
−3.938
12.44
25.06
O


ATOM
1635
C
SER
A1254
5.177
−4.542
15.769
27.38
C


ATOM
1636
O
SER
A1254
5.149
−3.604
16.568
26.76
O


ATOM
1637
N
LEU
A1255
4.311
−5.555
15.81
28.96
N


ATOM
1638
CA
LEU
A1255
3.313
−5.671
16.904
30.09
C


ATOM
1639
CB
LEU
A1255
2.445
−6.892
16.682
28.19
C


ATOM
1640
CG
LEU
A1255
1.457
−6.67
15.571
25.9
C


ATOM
1641
CD1
LEU
A1255
0.648
−7.916
15.545
21.2
C


ATOM
1642
CD2
LEU
A1255
0.623
−5.462
15.862
22.34
C


ATOM
1643
C
LEU
A1255
4.029
−5.854
18.256
31.71
C


ATOM
1644
O
LEU
A1255
3.438
−5.765
19.341
32.56
O


ATOM
1645
N
GLN
A1256
5.315
−6.125
18.161
32.58
N


ATOM
1646
CA
GLN
A1256
6.02
−6.599
19.279
34.23
C


ATOM
1647
CB
GLN
A1256
6.598
−7.935
18.872
34.77
C


ATOM
1648
CG
GLN
A1256
6.603
−9.017
19.89
37.62
C


ATOM
1649
CD
GLN
A1256
6.165
−10.365
19.269
41.02
C


ATOM
1650
OE1
GLN
A1256
4.976
−10.64
19.236
42.75
O


ATOM
1651
NE2
GLN
A1256
7.116
−11.184
18.775
39.8
N


ATOM
1652
C
GLN
A1256
7.164
−5.65
19.573
33.79
C


ATOM
1653
O
GLN
A1256
8.044
−5.999
20.347
35.8
O


ATOM
1654
N
THR
A1257
7.218
−4.49
18.945
32.41
N


ATOM
1655
CA
THR
A1257
8.397
−3.635
19.143
31.17
C


ATOM
1656
CB
THR
A1257
9.718
−4.095
18.392
31.52
C


ATOM
1657
OG1
THR
A1257
9.638
−3.809
16.969
30.13
O


ATOM
1658
CG2
THR
A1257
10.112
−5.605
18.665
30.26
C


ATOM
1659
C
THR
A1257
8.147
−2.263
18.645
30.43
C


ATOM
1660
O
THR
A1257
8.877
−1.356
19.008
30.95
O


ATOM
1661
N
GLN
A1258
7.193
−2.138
17.734
29.57
N


ATOM
1662
CA
GLN
A1258
6.735
−0.853
17.219
30.28
C


ATOM
1663
CB
GLN
A1258
6.459
0.13
18.384
31.08
C


ATOM
1664
CG
GLN
A1258
5.144
0.893
18.275
33.11
C


ATOM
1665
CD
GLN
A1258
5.061
2.095
19.274
33.27
C


ATOM
1666
OE1
GLN
A1258
5.397
1.939
20.463
39.41
O


ATOM
1667
NE2
GLN
A1258
4.584
3.27
18.798
29.74
N


ATOM
1668
C
GLN
A1258
7.729
−0.263
16.224
28.93
C


ATOM
1669
O
GLN
A1258
7.637
0.916
15.872
29.28
O


ATOM
1670
N
LYS
A1259
8.64
−1.096
15.742
28.14
N


ATOM
1671
CA
LYS
A1259
9.582
−0.677
14.701
28.14
C


ATOM
1672
CB
LYS
A1259
11.05
−0.984
15.129
30.57
C


ATOM
1673
CG
LYS
A1259
11.648
0.003
16.193
31.76
C


ATOM
1674
CD
LYS
A1259
12.782
−0.73
16.978
32.91
C


ATOM
1675
CE
LYS
A1259
13.536
0.295
17.915
37.06
C


ATOM
1676
NZ
LYS
A1259
14.494
−0.291
18.924
32.88
N


ATOM
1677
C
LYS
A1259
9.293
−1.259
13.316
24.48
C


ATOM
1678
O
LYS
A1259
8.873
−2.411
13.2
21.83
O


ATOM
1679
N
PHE
A1260
9.596
−0.455
12.288
21.57
N


ATOM
1680
CA
PHE
A1260
9.234
−0.778
10.91
19.9
C


ATOM
1681
CB
PHE
A1260
8.242
0.249
10.37
18.27
C


ATOM
1682
CG
PHE
A1260
7
0.392
11.208
16.53
C


ATOM
1683
CD1
PHE
A1260
6.991
1.259
12.353
17.28
C


ATOM
1684
CD2
PHE
A1260
5.851
−0.336
10.909
14.62
C


ATOM
1685
CE1
PHE
A1260
5.874
1.39
13.158
14.55
C


ATOM
1686
CE2
PHE
A1260
4.706
−0.221
11.702
16.06
C


ATOM
1687
CZ
PHE
A1260
4.698
0.646
12.807
18.96
C


ATOM
1688
C
PHE
A1260
10.446
−0.912
9.984
20.79
C


ATOM
1689
O
PHE
A1260
11.497
−0.282
10.19
22.74
O


ATOM
1690
N
THR
A1261
10.319
−1.739
8.958
19.25
N


ATOM
1691
CA
THR
A1261
11.369
−1.894
7.99
17.76
C


ATOM
1692
CB
THR
A1261
12.358
−3.043
8.369
18.7
C


ATOM
1693
OG1
THR
A1261
11.668
−4.302
8.396
18.46
O


ATOM
1694
CG2
THR
A1261
13
−2.793
9.746
19.38
C


ATOM
1695
C
THR
A1261
10.726
−2.181
6.637
16.24
C


ATOM
1696
O
THR
A1261
9.519
−2.344
6.549
15.68
O


ATOM
1697
N
THR
A1262
11.542
−2.225
5.581
13.6
N


ATOM
1698
CA
THR
A1262
11.063
−2.608
4.321
12.49
C


ATOM
1699
CB
THR
A1262
12.175
−2.541
3.221
14.06
C


ATOM
1700
OG1
THR
A1262
12.656
−1.212
3.086
11.22
O


ATOM
1701
CG2
THR
A1262
11.636
−2.914
1.843
14.36
C


ATOM
1702
C
THR
A1262
10.525
−3.996
4.475
11.49
C


ATOM
1703
O
THR
A1262
9.629
−4.349
3.817
11.81
O


ATOM
1704
N
LYS
A1263
11.132
−4.822
5.318
12.87
N


ATOM
1705
CA
LYS
A1263
10.597
−6.177
5.595
12.76
C


ATOM
1706
CB
LYS
A1263
11.604
−6.976
6.408
13.32
C


ATOM
1707
CG
LYS
A1263
12.832
−7.445
5.589
14.58
C


ATOM
1708
CD
LYS
A1263
12.449
−8.002
4.24
10.3
C


ATOM
1709
CE
LYS
A1263
13.641
−8.874
3.828
14.06
C


ATOM
1710
NZ
LYS
A1263
13.635
−9.233
2.408
10.78
N


ATOM
1711
C
LYS
A1263
9.235
−6.256
6.256
10.99
C


ATOM
1712
O
LYS
A1263
8.509
−7.228
6.056
10.11
O


ATOM
1713
N
SER
A1264
8.925
−5.263
7.076
10.36
N


ATOM
1714
CA
SER
A1264
7.575
−5.162
7.644
11.41
C


ATOM
1715
CB
SER
A1264
7.54
−4.346
8.93
11.47
C


ATOM
1716
OG
SER
A1264
7.752
−2.984
8.714
14.16
O


ATOM
1717
C
SER
A1264
6.633
−4.601
6.598
11.2
C


ATOM
1718
O
SER
A1264
5.43
−4.992
6.553
11.68
O


ATOM
1719
N
ASP
A1265
7.204
−3.819
5.679
9.67
N


ATOM
1720
CA
ASP
A1265
6.45
−3.364
4.538
11.37
C


ATOM
1721
CB
ASP
A1265
7.171
−2.28
3.753
10.45
C


ATOM
1722
CG
ASP
A1265
6.956
−0.879
4.332
14.18
C


ATOM
1723
OD1
ASP
A1265
7.593
0.032
3.753
14.77
O


ATOM
1724
OD2
ASP
A1265
6.163
−0.667
5.331
16.48
O


ATOM
1725
C
ASP
A1265
6.041
−4.533
3.618
11.53
C


ATOM
1726
O
ASP
A1265
4.944
−4.545
3.046
14.2
O


ATOM
1727
N
VAL
A1266
6.856
−5.549
3.576
10.63
N


ATOM
1728
CA
VAL
A1266
6.602
−6.704
2.752
11.03
C


ATOM
1729
CB
VAL
A1266
7.949
−7.558
2.57
10.66
C


ATOM
1730
CG1
VAL
A1266
7.661
−9.023
2.243
8.73
C


ATOM
1731
CG2
VAL
A1266
8.825
−6.919
1.505
8.25
C


ATOM
1732
C
VAL
A1266
5.475
−7.515
3.393
10.47
C


ATOM
1733
O
VAL
A1266
4.63
−8.017
2.669
12.51
O


ATOM
1734
N
TRP
A1267
5.455
−7.602
4.728
9.37
N


ATOM
1735
CA
TRP
A1267
4.375
−8.239
5.466
8.82
C


ATOM
1736
CB
TRP
A1267
4.633
−8.156
7
8.16
C


ATOM
1737
CG
TRP
A1267
3.559
−8.824
7.849
10.92
C


ATOM
1738
CD2
TRP
A1267
3.665
−10.046
8.612
9.89
C


ATOM
1739
CE2
TRP
A1267
2.394
−10.3
9.176
9.5
C


ATOM
1740
CE3
TRP
A1267
4.712
−10.904
8.911
8.75
C


ATOM
1741
CD1
TRP
A1267
2.232
−8.433
7.972
10.68
C


ATOM
1742
NE1
TRP
A1267
1.552
−9.29
8.779
6.35
N


ATOM
1743
CZ2
TRP
A1267
2.156
−11.378
10.068
8.31
C


ATOM
1744
CZ3
TRP
A1267
4.465
−11.994
9.747
10.23
C


ATOM
1745
CH2
TRP
A1267
3.187
−12.215
10.325
8.98
C


ATOM
1746
C
TRP
A1267
3.041
−7.557
5.104
8.67
C


ATOM
1747
O
TRP
A1267
2.055
−8.236
4.836
9.65
O


ATOM
1748
N
SER
A1268
3
−6.206
5.109
9.54
N


ATOM
1749
CA
SER
A1268
1.746
−5.456
4.795
7.78
C


ATOM
1750
CB
SER
A1268
1.913
−3.967
5.045
7.03
C


ATOM
1751
OG
SER
A1268
2.513
−3.772
6.256
8.59
O


ATOM
1752
C
SER
A1268
1.365 
−5.634
3.342
7.8
C


ATOM
1753
O
SER
A1268
0.17
−5.677
3.001
7.51
O


ATOM
1754
N
PHE
A1269
2.387
−5.73
2.479
8.59
N


ATOM
1755
CA
PHE
A1269
2.169
−5.956
1.088
9.1
C


ATOM
1756
CB
PHE
A1269
3.473
−5.888
0.338
8.27
C


ATOM
1757
CG
PHE
A1269
3.314
−6.245
−1.096
8.45
C


ATOM
1758
CD1
PHE
A1269
2.619
−5.363
−1.972
9.17
C


ATOM
1759
CD2
PHE
A1269
3.719
−7.495
−1.559
8.51
C


ATOM
1760
CE1
PHE
A1269
2.369
−5.68
−3.271
7.04
C


ATOM
1761
CE2
PHE
A1269
3.495
−7.836
−2.88
8.56
C


ATOM
1762
CZ
PHE
A1269
2.784
−6.942
−3.728
9.89
C


ATOM
1763
C
PHE
A1269
1.442
−7.323
0.919
10.64
C


ATOM
1764
O
PHE
A1269
0.49
−7.477
0.111
11.13
O


ATOM
1765
N
GLY
A1270
1.857
−8.317
1.702
11.64
N


ATOM
1766
CA
GLY
A1270
1.14
−9.587
1.648
11.42
C


ATOM
1767
C
GLY
A1270
−0.332
−9.417
2.029
10.97
C


ATOM
1768
O
GLY
A1270
−1.199
−10.04
1.413
11.25
O


ATOM
1769
N
VAL
A1271
−0.613
−8.596
3.059
9.54
N


ATOM
1770
CA
VAL
A1271
−2.01
−8.356
3.569
8.57
C


ATOM
1771
CB
VAL
A1271
−2.033
−7.621
4.946
8.56
C


ATOM
1772
CG1
VAL
A1271
−3.47
−7.359
5.392
7
C


ATOM
1773
CG2
VAL
A1271
−1.271
−8.389
6.08
3.23
C


ATOM
1774
C
VAL
A1271
−2.833
−7.584
2.516
9.92
C


ATOM
1775
O
VAL
A1271
−4.001
−7.95
2.211
10.22
O


ATOM
1776
N
LEU
A1272
−2.175
−6.593
1.899
10.19
N


ATOM
1777
CA
LEU
A1272
−2.68
−5.873
0.716
11.37
C


ATOM
1778
CB
LEU
A1272
−1.764
−4.681
0.411
11.24
C


ATOM
1779
CG
LEU
A1272
−1.525
−3.908
−0.905
14.03
C


ATOM
1780
CD1
LEU
A1272
−2.293
−4.472
−2.089
13.62
C


ATOM
1781
CD2
LEU
A1272
−1.645
−2.378
−0.821
13.61
C


ATOM
1782
C
LEU
A1272
−3.038
−6.764
−0.501
11.35
C


ATOM
1783
O
LEU
A1272
−4.086
−6.613
−1.146
11.16
O


ATOM
1784
N
LEU
A1273
−2.208
−7.748
−0.75
10.97
N


ATOM
1785
CA
LEU
A1273
−2.507
−8.766
−1.748
10.03
C


ATOM
1786
CB
LEU
A1273
−1.341
−9.755
−1.831
9.71
C


ATOM
1787
CG
LEU
A1273
−0.17
−9.307
−2.652
12.95
C


ATOM
1788
CD1
LEU
A1273
0.852
−10.401
−2.848
13.19
C


ATOM
1789
CD2
LEU
A1273
−0.706
−8.847
−3.99
16.74
C


ATOM
1790
C
LEU
A1273
−3.716
−9.555
−1.395
8.67
C


ATOM
1791
O
LEU
A1273
−4.436
−9.945
−2.273
7.96
O


ATOM
1792
N
TRP
A1274
−3.86
−9.879
−0.092
9.8
N


ATOM
1793
CA
TRP
A1274
−5.031
−10.602
0.426
8.39
C


ATOM
1794
CB
TRP
A1274
−4.81
−11.063
1.856
7.65
C


ATOM
1795
CG
TRP
A1274
−5.841
−11.888
2.417
3.72
C


ATOM
1796
CD2
TRP
A1274
−7.005
−11.445
3.132
4.89
C


ATOM
1797
CE2
TRP
A1274
−7.731
−12.617
3.507
2
C


ATOM
1798
CE3
TRP
A1274
−7.48
−10.181
3.54
4.57
C


ATOM
1799
CD1
TRP
A1274
−5.909
−13.249
2.383
4.08
C


ATOM
1800
NE1
TRP
A1274
−7.037
−13.694
3.025
2.01
N


ATOM
1801
CZ2
TRP
A1274
−8.903
−12.574
4.242
2.67
C


ATOM
1802
CZ3
TRP
A1274
−8.727
−10.127
4.267
8.33
C


ATOM
1803
CH2
TRP
A1274
−9.417
−11.329
4.607
3.57
C


ATOM
1804
C
TRP
A1274
−6.228
−9.715
0.277
9.2
C


ATOM
1805
O
TRP
A1274
−7.31
−10.183
−0.178
10.85
O


ATOM
1806
N
GLU
A1275
−6.053
−8.426
0.596
9.74
N


ATOM
1807
CA
GLU
A1275
−7.159
−7.458
0.406
10.36
C


ATOM
1808
CB
GLU
A1275
−6.761
−6.009
0.771
9.95
C


ATOM
1809
CG
GLU
A1275
−6.544
−5.683
2.246
11
C


ATOM
1810
CD
GLU
A1275
−6.205
−4.183
2.392
12.14
C


ATOM
1811
OE1
GLU
A1275
−5.043
−3.754
2.104
12.7
O


ATOM
1812
OE2
GLU
A1275
−7.131
−3.392
2.7
11.37
O


ATOM
1813
C
GLU
A1275
−7.61
−7.445
−1.028
10.04
C


ATOM
1814
O
GLU
A1275
−8.794
−7.315
−1.306
10.34
O


ATOM
1815
N
LEU
A1276
−6.641
−7.421
−1.934
11.02
N


ATOM
1816
CA
LEU
A1276
−6.883
−7.423
−3.355
11.94
C


ATOM
1817
CB
LEU
A1276
−5.549
−7.374
−4.068
11.7
C


ATOM
1818
CG
LEU
A1276
−5.098
−6.161
−4.878
13.84
C


ATOM
1819
CD1
LEU
A1276
−5.77
−4.882
−4.59
15.07
C


ATOM
1820
CD2
LEU
A1276
−3.588
−6.017
−4.794
14.8
C


ATOM
1821
C
LEU
A1276
−7.649
−8.691
−3.79
12.76
C


ATOM
1822
O
LEU
A1276
−8.688
−8.584
−4.439
14.11
O


ATOM
1823
N
MET
A1277
−7.181
−9.872
−3.387
12.53
N


ATOM
1824
CA
MET
A1277
−7.783
−11.114
−3.844
13.7
C


ATOM
1825
CB
MET
A1277
−6.838
−12.32
−3.715
11.99
C


ATOM
1826
CG
MET
A1277
−5.573
−12.151
−4.52
16.79
C


ATOM
1827
SD
MET
A1277
−5.667
−11.426
−6.22
25.77
S


ATOM
1828
CE
MET
A1277
−6.432
−12.816
−7.071
17.04
C


ATOM
1829
C
MET
A1277
−9.1
−11.424
−3.185
14.22
C


ATOM
1830
O
MET
A1277
−9.877
−12.227
−3.727
15.37
O


ATOM
1831
N
THR
A1278
−9.345
−10.845
−2.007
14.32
N


ATOM
1832
CA
THR
A1278
−10.683
−10.929
−1.389
12.59
C


ATOM
1833
CB
THR
A1278
−10.597
−10.94
0.12
13.16
C


ATOM
1834
OG1
THR
A1278
−10.167
−9.64
0.627
9.42
O


ATOM
1835
CG2
THR
A1278
−9.611
−12.04
0.543
8.23
C


ATOM
1836
C
THR
A1278
−11.582
−9.779
−1.809
13.58
C


ATOM
1837
O
THR
A1278
−12.71
−9.661
−1.286
14.22
O


ATOM
1838
N
ARG
A1279
−11.094
−8.931
−2.726
12.97
N


ATOM
1839
CA
ARG
A1279
−11.853
−7.804
−3.23
15.57
C


ATOM
1840
CB
ARG
A1279
−13.12
−8.298
−3.949
14.48
C


ATOM
1841
CG
ARG
A1279
−13.201
−7.815
−5.354
20.35
C


ATOM
1842
CD
ARG
A1279
−14.28
−8.526
−6.25
20.34
C


ATOM
1843
NE
ARG
A1279
−13.757
−9.783
−6.773
27.23
N


ATOM
1844
CZ
ARG
A1279
−13.268
−10.03
−8.019
29.48
C


ATOM
1845
NH1
ARG
A1279
−13.237
−9.082
−8.967
19.95
N


ATOM
1846
NH2
ARG
A1279
−12.773
−11.281
−8.296
29.36
N


ATOM
1847
C
ARG
A1279
−12.252
−6.851
−2.08
15.31
C


ATOM
1848
O
ARG
A1279
−13.412
−6.454
−1.997
16.43
O


ATOM
1849
N
GLY
A1280
−11.316
−6.472
−1.202
14.52
N


ATOM
1850
CA
GLY
A1280
−11.607
−5.431
−0.235
14.65
C


ATOM
1851
C
GLY
A1280
−12.149
−5.991
1.088
15.17
C


ATOM
1852
O
GLY
A1280
−12.617
−5.233
1.934
13.6
O


ATOM
1853
N
ALA
A1281
−12.066
−7.311
1.31
14.02
N


ATOM
1854
CA
ALA
A1281
−12.479
−7.784
2.644
14.68
C


ATOM
1855
CB
ALA
A1281
−12.698
−9.349
2.709
13.99
C


ATOM
1856
C
ALA
A1281
−11.512
−7.29
3.732
14.17
C


ATOM
1857
O
ALA
A1281
−10.291
−7.095
3.428
13.46
O


ATOM
1858
N
PRO
A1282
−12.025
−7.152
4.989
13.83
N


ATOM
1859
CD
PRO
A1282
−13.426
−7.463
5.268
15.14
C


ATOM
1860
CA
PRO
A1282
−11.327
−6.761
6.233
15.61
C


ATOM
1861
CB
PRO
A1282
−12.477
−6.518
7.241
16.49
C


ATOM
1862
CG
PRO
A1282
−13.805
−6.384
6.27
16.92
C


ATOM
1863
C
PRO
A1282
−10.542
−7.972
6.721
16.94
C


ATOM
1864
O
PRO
A1282
−11.135
−9.035
6.958
17.36
O


ATOM
1865
N
PRO
A1283
−9.212
−7.829
6.868
17.68
N


ATOM
1866
CD
PRO
A1283
−8.431
−6.615
6.538
17.72
C


ATOM
1867
CA
PRO
A1283
−8.407
−8.909
7.458
17.23
C


ATOM
1868
CB
PRO
A1283
−6.978
−8.369
7.397
17.46
C


ATOM
1869
CG
PRO
A1283
−7.01
−6.992
6.83
17.37
C


ATOM
1870
C
PRO
A1283
−8.809
−9.139 
8.924
17.48
C


ATOM
1871
O
PRO
A1283
−9.079
−8.155
9.671
17.71
O


ATOM
1872
N
TYR
A1284
−8.86
−10.402
9.336
16.72
N


ATOM
1873
CA
TYR
A1284
−9.106
−10.759
10.742
17.3
C


ATOM
1874
CB
TYR
A1284
−7.938
−10.382
11.624
16.01
C


ATOM
1875
CG
TYR
A1284
−6.551
−10.698
11.111
17.42
C


ATOM
1876
CD1
TYR
A1284
−5.946
−11.957
11.312
15.84
C


ATOM
1877
CE1
TYR
A1284
−4.631
−12.201
10.876
14.8
C


ATOM
1878
CD2
TYR
A1284
−5.809
−9.724
10.468
16.16
C


ATOM
1879
CE2
TYR
A1284
−4.539
−9.98
10.008
16.45
C


ATOM
1880
CZ
TYR
A1284
−3.932
−11.185
10.22
16.76
C


ATOM
1881
OH
TYR
A1284
−2.656
−11.326
9.687
16.71
O


ATOM
1882
C
TYR
A1284
−10.342
−10.136
11.365
18.43
C


ATOM
1883
O
TYR
A1284
−10.225
−9.475
12.388
18.85
O


ATOM
1884
N
PRO
A1285
−11.519
−10.319
10.758
20.37
N


ATOM
1885
CD
PRO
A1285
−11.84
−11.196
9.635
20.13
C


ATOM
1886
CA
PRO
A1285
−12.689
−9.555
11.184
23.29
C


ATOM
1887
CB
PRO
A1285
−13.739
−9.907
10.135
22.39
C


ATOM
1888
CG
PRO
A1285
−13.326
−11.24
9.66
21.13
C


ATOM
1889
C
PRO
A1285
−13.166
−9.872
12.61
26.8
C


ATOM
1890
O
PRO
A1285
−13.433
−8.936
13.408
25.99
O


ATOM
1891
N
ASP
A1286
−13.265
−11.154
12.972
30.65
N


ATOM
1892
CA
ASP
A1286
−13.848
−11.408
14.323
35.35
C


ATOM
1893
CB
ASP
A1286
−14.553
−12.807
14.453
37.22
C


ATOM
1894
CG
ASP
A1286
−15.524
−13.112
13.255
43.19
C


ATOM
1895
OD1
ASP
A1286
−14.994
−13.477
12.169
46.45
O


ATOM
1896
OD2
ASP
A1286
−16.782
−12.965
13.391
46.26
O


ATOM
1897
C
ASP
A1286
−12.895
−11.155
15.535
35.1
C


ATOM
1898
O
ASP
A1286
−13.065
−11.858
16.549
36.23
O


ATOM
1899
N
VAL
A1287
−11.959
−10.172
15.481
32.52
N


ATOM
1900
CA
VAL
A1287
−10.802
−10.275
16.39
29.97
C


ATOM
1901
CB
VAL
A1287
−9.744
−11.371
15.935
29.53
C


ATOM
1902
CG1
VAL
A1287
−9.59
−11.36
14.514
30.14
C


ATOM
1903
CG2
VAL
A1287
−8.408
−11.176
16.544
30.07
C


ATOM
1904
C
VAL
A1287
−10.145
−9.032
16.83
28.88
C


ATOM
1905
O
VAL
A1287
−9.891
−8.145
16.02
29.31
O


ATOM
1906
N
ASN
A1288
−9.858
−8.968
18.137
26.64
N


ATOM
1907
CA
ASN
A1288
−9.176
−7.828
18.689
24.13
C


ATOM
1908
CB
ASN
A1288
−9.554
−7.638
20.164
25
C


ATOM
1909
CG
ASN
A1288
−9.045
−8.774
21.085
25.21
C


ATOM
1910
OD1
ASN
A1288
−7.878
−9.281
20.965
21.19
O


ATOM
1911
ND2
ASN
A1288
−9.928
−9.165
22.048
22.42
N


ATOM
1912
C
ASN
A1288
−7.678
−7.882
18.51
23.31
C


ATOM
1913
O
ASN
A1288
−7.145
−8.852
18.011
22.44
O


ATOM
1914
N
THR
A1289
−7.008
−6.829
18.966
23.16
N


ATOM
1915
CA
THR
A1289
−5.58
−6.648
18.82
22.72
C


ATOM
1916
CB
THR
A1289
−5.102
−5.234
19.26
23.85
C


ATOM
1917
OG1
THR
A1289
−5.823
−4.741
20.416
26.46
O


ATOM
1918
CG2
THR
A1289
−5.304
−4.207
18.143
25.64
C


ATOM
1919
C
THR
A1289
−4.739
−7.686
19.517
22.02
C


ATOM
1920
O
THR
A1289
−3.619
−8.007
19.065
23
O


ATOM
1921
N
PHE
A1290
−5.251
−8.222
20.614
20.54
N


ATOM
1922
CA
PHE
A1290
−4.486
−9.215
21.359
19.45
C


ATOM
1923
CB
PHE
A1290
−4.935
−9.309
22.861
19.8
C


ATOM
1924
CG
PHE
A1290
−4.062
−10.269
23.708
18.62
C


ATOM
1925
CD1
PHE
A1290
−2.808
−9.855
24.201
16.3
C


ATOM
1926
CD2
PHE
A1290
−4.466
−11.598
23.931
20.15
C


ATOM
1927
CE1
PHE
A1290
−1.999
−10.702
24.984
19.55
C


ATOM
1928
CE2
PHE
A1290
−3.661
−12.486
24.692
18.86
C


ATOM
1929
CZ
PHE
A1290
−2.404
−12.053
25.206
20.06
C


ATOM
1930
C
PHE
A1290
−4.587
−10.609
20.684
18.03
C


ATOM
1931
O
PHE
A1290
−3.605
−11.325
20.562
16.43
O


ATOM
1932
N
ASP
A1291
−5.793
−10.996
20.303
17.58
N


ATOM
1933
CA
ASP
A1291
−5.964
−12.302
19.726
19.32
C


ATOM
1934
CB
ASP
A1291
−7.414
−12.688
19.644
18.53
C


ATOM
1935
CG
ASP
A1291
−8.056
−12.83
20.984
21.78
C


ATOM
1936
OD1
ASP
A1291
−7.39
−13.29
21.98
19.49
O


ATOM
1937
OD2
ASP
A1291
−9.277
−12.483
21.039
24.79
O


ATOM
1938
C
ASP
A1291
−5.301
−12.414
18.338
20.96
C


ATOM
1939
O
ASP
A1291
−4.776
−13.486
17.993
21.73
O


ATOM
1940
N
ILE
A1292
−5.313
−11.32
17.569
20.88
N


ATOM
1941
CA
ILE
A1292
−4.576
−11.26
16.303
21.43
C


ATOM
1942
CB
ILE
A1292
−4.718
−9.857
15.559
20.9
C


ATOM
1943
CG2
ILE
A1292
−3.601
−9.658
14.6
22.73
C


ATOM
1944
CG1
ILE
A1292
−5.981
−9.858
14.679
22.1
C


ATOM
1945
CD1
ILE
A1292
−6.854
−8.575
14.742
27.9
C


ATOM
1946
C
ILE
A1292
−3.153
−11.697
16.529
20.67
C


ATOM
1947
O
ILE
A1292
−2.569
−12.403
15.728
21.89
O


ATOM
1948
N
THR
A1293
−2.591
−11.277
17.633
20.67
N


ATOM
1949
CA
THR
A1293
−1.187
−11.53
17.92
21.87
C


ATOM
1950
CB
THR
A1293
−0.769
−10.598
19.089
22.47
C


ATOM
1951
OG1
THR
A1293
−0.81
−9.23
18.606
25.62
O


ATOM
1952
CG2
THR
A1293
0.571
−10.944
19.614
20.56
C


ATOM
1953
C
THR
A1293
−0.949
−13.006
18.292
22.24
C


ATOM
1954
O
THR
A1293
0.01
−13.642
17.844
22.94
O


ATOM
1955
N
VAL
A1294
−1.844
−13.548
19.105
22.43
N


ATOM
1956
CA
VAL
A1294
−1.887
−14.965
19.401
22.79
C


ATOM
1957
CB
VAL
A1294
−3.039
−15.316
20.484
24.33
C


ATOM
1958
CG1
VAL
A1294
−2.905
−16.703
20.93
21.06
C


ATOM
1959
CG2
VAL
A1294
−3.012
−14.34
21.698
22.9
C


ATOM
1960
C
VAL
A1294
−2.137
−15.775
18.156
22.04
C


ATOM
1961
O
VAL
A1294
−1.472
−16.737
17.979
23.52
O


ATOM
1962
N
TYR
A1295
−3.127
−15.42
17.336
21.11
N


ATOM
1963
CA
TYR
A1295
−3.378
−16.062
16.036
21.27
C


ATOM
1964
CB
TYR
A1295
−4.387
−15.233
15.215
21.55
C


ATOM
1965
CG
TYR
A1295
−4.827
−15.809
13.847
22.76
C


ATOM
1966
CD1
TYR
A1295
−5.852
−16.772
13.788
24.13
C


ATOM
1967
CE1
TYR
A1295
−6.251
−17.347
12.586
22.48
C


ATOM
1968
CD2
TYR
A1295
−4.24
−15.406
12.639
18.86
C


ATOM
1969
CE2
TYR
A1295
−4.647
−15.975
11.44
19.4
C


ATOM
1970
CZ
TYR
A1295
−5.662
−16.957
11.412
22
C


ATOM
1971
OH
TYR
A1295
−6.157
−17.572
10.245
15.34
O


ATOM
1972
C
TYR
A1295
−2.05
−16.149
15.285
21.71
C


ATOM
1973
O
TYR
A1295
−1.72
−17.214
14.76
23.7
O


ATOM
1974
N
LEU
A1296
−1.278
−15.061
15.253
20.06
N


ATOM
1975
CA
LEU
A1296
−0.1
−15.031
14.463
19.72
C


ATOM
1976
CB
LEU
A1296
0.315
−13.583
14.173
18.7
C


ATOM
1977
CG
LEU
A1296
−0.563
−12.717
13.227
17.29
C


ATOM
1978
CD1
LEU
A1296
−0.108
−11.231
13.155
14.74
C


ATOM
1979
CD2
LEU
A1296
−0.67
−13.32
11.866
13.27
C


ATOM
1980
C
LEU
A1296
1.069
−15.809
15.034
21.48
C


ATOM
1981
O
LEU
A1296
1.891
−16.348
14.288
20.81
O


ATOM
1982
N
LEU
A1297
1.202
−15.8
16.367
23.54
N


ATOM
1983
CA
LEU
A1297
2.303
−16.527
17.031
23.91
C


ATOM
1984
CB
LEU
A1297
2.543
−16.042
18.472
23.89
C


ATOM
1985
CG
LEU
A1297
3.38
−14.752
18.474
27.22
C


ATOM
1986
CD1
LEU
A1297
3.407
−13.97
19.768
28.81
C


ATOM
1987
CD2
LEU
A1297
4.763
−15.022
18.017
31.47
C


ATOM
1988
C
LEU
A1297
2.053
−18.024
17.018
24.35
C


ATOM
1989
O
LEU
A1297
2.956
−18.785
17.371
26.26
O


ATOM
1990
N
GLN
A1298
0.865
−18.444
16.598
23.07
N


ATOM
1991
CA
GLN
A1298
0.509
−19.839
16.478
23.56
C


ATOM
1992
CB
GLN
A1298
−0.975 
−20.019
16.765
23.4
C


ATOM
1993
CG
GLN
A1298
−1.185
−20.016
18.319
29.5
C


ATOM
1994
CD
GLN
A1298
−2.609
−20.215
18.746
33.61
C


ATOM
1995
OE1
GLN
A1298
−3.551 
−19.932
17.988
33.3
O


ATOM
1996
NE2
GLN
A1298
−2.79
−20.662
20.004
36.42
N


ATOM
1997
C
GLN
A1298
0.813
−20.336
15.092
23.28
C


ATOM
1998
O
GLN
A1298
0.486
−21.504
14.767
23.77
O


ATOM
1999
N
GLY
A1299
1.427
−19.453
14.293
21.11
N


ATOM
2000
CA
GLY
A1299
1.761
−19.705
12.913
19.57
C


ATOM
2001
C
GLY
A1299
0.552
−19.613
11.985
19.57
C


ATOM
2002
O
GLY
A1299
0.69
−19.848
10.779
19.65
O


ATOM
2003
N
ARG
A1300
−0.642
−19.294
12.519
17.34
N


ATOM
2004
CA
ARG
A1300
−1.791
−19.147
11.663
15.11
C


ATOM
2005
CB
ARG
A1300
−3.068
−19.072
12.496
15.35
C


ATOM
2006
CG
ARG
A1300
−3.227
−20.162
13.511
17.32
C


ATOM
2007
CD
ARG
A1300
−4.385
−19.878
14.443
19
C


ATOM
2008
NE
ARG
A1300
−5.495
−20.632
13.951
26.17
N


ATOM
2009
CZ
ARG
A1300
−5.943
−21.75
14.51
26.18
C


ATOM
2010
NH1
ARG
A1300
−5.407
−22.226
15.639
26.4
N


ATOM
2011
NH2
ARG
A1300
−6.947
−22.383
13.935
28.78
N


ATOM
2012
C
ARG
A1300
−1.625
−17.896
10.789
13.95
C


ATOM
2013
O
ARG
A1300
−0.906
−16.952
11.167
11.48
O


ATOM
2014
N
ARG
A1301
−2.292
−17.914
9.62
12.59
N


ATOM
2015
CA
ARG
A1301
−2.296
−16.803
8.679
10.68
C


ATOM
2016
CB
ARG
A1301
−1.227
−17.008
7.66
9.76
C


ATOM
2017
CG
ARG
A1301
0.201
−17.075
8.265
9.66
C


ATOM
2018
CD
ARG
A1301
0.732
−15.697
8.706
10.28
C


ATOM
2019
NE
ARG
A1301
2.117
−15.7
9.169
7.99
N


ATOM
2020
CZ
ARG
A1301
2.433
−16.002
10.423
11.74
C


ATOM
2021
NH1
ARG
A1301
1.466
−16.398
11.307
6.97
N


ATOM
2022
NH2
ARG
A1301
3.713
−15.986
10.777
11.06
N


ATOM
2023
C
ARG
A1301
−3.668
−16.6
8.022 
11.29
C


ATOM
2024
O
ARG
A1301
−4.596
−17.417
8.188
10.02
O


ATOM
2025
N
LEU
A1302
−3.83
−15.488
7.303
11.13
N


ATOM
2026
CA
LEU
A1302
−5.106
−15.197
6.609
10.8
C


ATOM
2027
CB
LEU
A1302
−5.014
−13.85
5.963
9.1
C


ATOM
2028
CG
LEU
A1302
−4.833
−12.681
6.864
6.48
C


ATOM
2029
CD1
LEU
A1302
−4.307
−11.511
6.008
9.35
C


ATOM
2030
CD2
LEU
A1302
−6.153
−12.358
7.484
4.82
C


ATOM
2031
C
LEU
A1302
−5.312
−16.286
5.57
12.1
C


ATOM
2032
O
LEU
A1302
−4.346
−16.769
5.013
13.45
O


ATOM
2033
N
LEU
A1303
−6.537
−16.737
5.331
14.81
N


ATOM
2034
CA
LEU
A1303
−6.711
−18
4.542
15.67
C


ATOM
2035
CB
LEU
A1303
−8.023
−18.684
4.826
14.95
C


ATOM
2036
CG
LEU
A1303
−8.178
−19.581
6.054
18.31
C


ATOM
2037
CD1
LEU
A1303
−6.996
−19.498
6.984
20.03
C


ATOM
2038
CD2
LEU
A1303
−9.492
−19.163
6.791
15.76
C


ATOM
2039
C
LEU
A1303
−6.66
−17.616
3.1
16.46
C


ATOM
2040
O
LEU
A1303
−6.816
−16.433
2.806
17.16
O


ATOM
2041
N
GLN
A1304
−6.44
−18.594
2.224
16.59
N


ATOM
2042
CA
GLN
A1304
−6.3
−18.347
0.838
16.9
C


ATOM
2043
CB
GLN
A1304
−5.86
−19.567
0.157
15.65
C


ATOM
2044
CG
GLN
A1304
−5.653
−19.308
−1.266
15.99
C


ATOM
2045
CD
GLN
A1304
−5.059
−20.498
−2.033
18.57
C


ATOM
2046
OE1
GLN
A1304
−4.449
−21.434
−1.479
14.91
O


ATOM
2047
NE2
GLN
A1304
−5.186
−20.415
−3.343
19.66
N


ATOM
2048
C
GLN
A1304
−7.665
−17.96
0.305
20.07
C


ATOM
2049
O
GLN
A1304
−8.661
−18.688
0.48
21.65
O


ATOM
2050
N
PRO
A1305
−7.758
−16.779
−0.303
20.86
N


ATOM
2051
CD
PRO
A1305
−6.779
−15.677
−0.48
21.62
C


ATOM
2052
CA
PRO
A1305
−9.075
−16.464
−0.792
21.48
C


ATOM
2053
CB
PRO
A1305
−8.959
−14.995
−1.167
20.75
C


ATOM
2054
CG
PRO
A1305
−7.643
−14.505
−0.558
21.05
C


ATOM
2055
C
PRO
A1305
−9.462
−17.375
−1.955
23.17
C


ATOM
2056
O
PRO
A1305
−8.602
−18.053
−2.505
22.48
O


ATOM
2057
N
GLU
A1306
−10.761
−17.436
−2.283
26
N


ATOM
2058
CA
GLU
A1306
−11.26
−18.192
−3.458
28.18
C


ATOM
2059
CB
GLU
A1306
−12.763
−18.089
−3.506
29.06
C


ATOM
2060
CG
GLU
A1306
−13.503
−19.357
−3.241
32.62
C


ATOM
2061
CD
GLU
A1306
−15.012
−19.072
−3.204
38.95
C


ATOM
2062
OE1
GLU
A1306
−15.586
−18.781
−4.279
38.36
O


ATOM
2063
OE2
GLU
A1306
−15.613
−19.109
−2.096
42.58
O


ATOM
2064
C
GLU
A1306
−10.727
−17.481
−4.699
29.17
C


ATOM
2065
O
GLU
A1306
−10.623
−16.223
−4.716
28.95
O


ATOM
2066
N
TYR
A1307
−10.373
−18.239
−5.733
29.22
N


ATOM
2067
CA
TYR
A1307
−9.876
−17.566
−6.982
29.91
C


ATOM
2068
CB
TYR
A1307
−10.817
−16.438
−7.467
31.22
C


ATOM
2069
CG
TYR
A1307
−12.238
−16.847
−7.415
34.72
C


ATOM
2070
CD1
TYR
A1307
−12.651
−17.996
−8.093
37.5
C


ATOM
2071
CE1
TYR
A1307
−13.982
−18.423
−8.057
37.34
C


ATOM
2072
CD2
TYR
A1307
−13.183
−16.105
−6.674
37.26
C


ATOM
2073
CE2
TYR
A1307
−14.515
−16.517
−6.635
38.36
C


ATOM
2074
CZ
TYR
A1307
−14.896
−17.692
−7.347
37.41
C


ATOM
2075
OH
TYR
A1307
−16.196
−18.158
−7.348
37.73
O


ATOM
2076
C
TYR
A1307
−8.469
−16.946
−6.918
27.27
C


ATOM
2077
O
TYR
A1307
−8.005
−16.415
−7.922
28.16
O


ATOM
2078
N
CYS
A1308
−7.836
−16.986
−5.76
24.33
N


ATOM
2079
CA
CYS
A1308
−6.448
−16.581
−5.609
22.31
C


ATOM
2080
CB
CYS
A1308
−6.179
−16.264
−4.155
21.21
C


ATOM
2081
SG
CYS
A1308
−4.524
−15.866
−3.835
21.98
S


ATOM
2082
C
CYS
A1308
−5.63
−17.792
−5.972
21.69
C


ATOM
2083
O
CYS
A1308
−5.657
−18.776
−5.197
21.71
O


ATOM
2084
N
PRO
A1309
−4.895
−17.737
−7.136
20.38
N


ATOM
2085
CD
PRO
A1309
−4.914
−16.66
−8.151
20.39
C


ATOM
2086
CA
PRO
A1309
−3.952
−18.758
−7.524
18.95
C


ATOM
2087
CB
PRO
A1309
−3.177
−18.102
−8.703
18.71
C


ATOM
2088
CG
PRO
A1309
−3.54
−16.76
−8.732
21.17
C


ATOM
2089
C
PRO
A1309
−2.999
−19.167
−6.393
17.95
C


ATOM
2090
O
PRO
A1309
−2.449
−18.309
−5.682
16.25
O


ATOM
2091
N
ASP
A1310
−2.831
−20.485
−6.258
17.69
N


ATOM
2092
CA
ASP
A1310
−1.936
−21.129
−5.289
18.08
C


ATOM
2093
CB
ASP
A1310
−1.805
−22.64
−5.628
17.94
C


ATOM
2094
CG
ASP
A1310
−3.062
−23.451
−5.251
26.79
C


ATOM
2095
OD1
ASP
A1310
−4.071
−22.782
−4.899
31.89
O


ATOM
2096
OD2
ASP
A1310
−3.076
−24.745
−5.262
29.15
O


ATOM
2097
C
ASP
A1310
−0.53
−20.464
−5.191
17.75
C


ATOM
2098
O
ASP
A1310
−0.043
−20.203
−4.067
18.85
O


ATOM
2099
N
PRO
A1311
0.177
−20.268
−6.356
17.25
N


ATOM
2100
CD
PRO
A1311
−0.102
−20.803
−7.725
16.88
C


ATOM
2101
CA
PRO
A1311
1.465
−19.559
−6.343
15.19
C


ATOM
2102
CB
PRO
A1311
1.82
−19.434
−7.84
13.7
C


ATOM
2103
CG
PRO
A1311
1.293
−20.726
−8.404
14.93
C


ATOM
2104
C
PRO
A1311
1.351
−18.218
−5.741
15.13
C


ATOM
2105
O
PRO
A1311
2.274
−17.853
−5.016
15.93
O


ATOM
2106
N
LEU
A1312
0.248
−17.498
−5.99
13.68
N


ATOM
2107
CA
LEU
A1312
0.124
−16.184
−5.399
14.9
C


ATOM
2108
CB
LEU
A1312
−1.102
−15.427
−5.875
15.12
C


ATOM
2109
CG
LEU
A1312
−1.007
−13.901
−6.065
16.16
C


ATOM
2110
CD1
LEU
A1312
−2.415
−13.27
−6.038
17.09
C


ATOM
2111
CD2
LEU
A1312
−0.203
−13.323
−5.007
22.34
C


ATOM
2112
C
LEU
A1312
0.05
−16.301
−3.88
15.48
C


ATOM
2113
O
LEU
A1312
0.695
−15.523
−3.154
14.57
O


ATOM
2114
N
TYR
A1313
−0.724
−17.288
−3.406
15.42
N


ATOM
2115
CA
TYR
A1313
−0.859
−17.479
−1.998
15.15
C


ATOM
2116
CB
TYR
A1313
−1.893
−18.528
−1.643
15.52
C


ATOM
2117
CG
TYR
A1313
−2.23
−18.548
−0.145
16.45
C


ATOM
2118
CD1
TYR
A1313
−2.56
−17.358
0.54
15.64
C


ATOM
2119
CE1
TYR
A1313
−2.936
−17.372
1.926
16.19
C


ATOM
2120
CD2
TYR
A1313
−2.212
−19.754
0.591
15.35
C


ATOM
2121
CE2
TYR
A1313
−2.591
−19.791
1.956
15.48
C


ATOM
2122
CZ
TYR
A1313
−2.936
−18.585
2.613
17.43
C


ATOM
2123
OH
TYR
A1313
−3.289
−18.608
3.927
14.53
O


ATOM
2124
C
TYR
A1313
0.474
−17.838
−1.447
15.35
C


ATOM
2125
O
TYR
A1313
0.814
−17.353
−0.375
14.4
O


ATOM
2126
N
GLU
A1314
1.256
−18.633
−2.188
15.71
N


ATOM
2127
CA
GLU
A1314
2.582
−18.991
−1.697
18.23
C


ATOM
2128
CB
GLU
A1314
3.388
−19.844
−2.715
18.61
C


ATOM
2129
CG
GLU
A1314
2.698
−21.155
−3.256
25.52
C


ATOM
2130
CD
GLU
A1314
3.287
−21.719
−4.675
29.14
C


ATOM
2131
OE1
GLU
A1314
4.453
−21.269
−5.127
32.9
O


ATOM
2132
OE2
GLU
A1314
2.545
−22.601
−5.337
34.86
O


ATOM
2133
C
GLU
A1314
3.328
−17.677
−1.454
15.23
C


ATOM
2134
O
GLU
A1314
4.172
−17.576
−0.566
14.59
O


ATOM
2135
N
VAL
A1315
3.088
−16.69
−2.301
13.92
N


ATOM
2136
CA
VAL
A1315
3.813
−15.431
−2.161
13.5
C


ATOM
2137
CB
VAL
A1315
3.785
−14.546
−3.475
14.69
C


ATOM
2138
CG1
VAL
A1315
4.069
−13.078
−3.177
14.19
C


ATOM
2139
CG2
VAL
A1315
4.77
−15.107
−4.591
12.06
C


ATOM
2140
C
VAL
A1315
3.327
−14.682
−0.917
12.08
C


ATOM
2141
O
VAL
A1315
4.137
−14.155
−0.228
10.73
O


ATOM
2142
N
MET
A1316
2.033
−14.671
−0.63
11.53
N


ATOM
2143
CA
MET
A1316
1.517
−13.987
0.538
13.7
C


ATOM
2144
CB
MET
A1316
−0.01
−13.976
0.634
12.56
C


ATOM
2145
CG
MET
A1316
−0.722
−13.524
−0.618
15.54
C


ATOM
2146
SD
MET
A1316
−2.547
−13.416
−0.347
20.85
S


ATOM
2147
CE
MET
A1316
−3.235
−14.193
−1.73
19.52
C


ATOM
2148
C
MET
A1316
2.079
−14.643
1.748
13.01
C


ATOM
2149
O
MET
A1316
2.561
−13.971
2.65
15.31
O


ATOM
2150
N
LEU
A1317
2.056
−15.963
1.801
12.31
N


ATOM
2151
CA
LEU
A1317
2.673
−16.625
2.935
11.49
C


ATOM
2152
CB
LEU
A1317
2.497
−18.127
2.873
9.86
C


ATOM
2153
CG
LEU
A1317
1.111
−18.695
2.882
7.48
C


ATOM
2154
CD1
LEU
A1317
1.176
−20.143
2.433
7.53
C


ATOM
2155
CD2
LEU
A1317
0.443
−18.515
4.217
3.61
C


ATOM
2156
C
LEU
A1317
4.115
−16.342
3.052
11.01
C


ATOM
2157
O
LEU
A1317
4.637
−16.294
4.137
14.42
O


ATOM
2158
N
LYS
A1318
4.837
−16.313
1.961
12.75
N


ATOM
2159
CA
LYS
A1318
6.254
−15.938
2.056
15.07
C


ATOM
2160
CB
LYS
A1318
6.876
−15.918
0.675
15.17
C


ATOM
2161
CG
LYS
A1318
7.096
−17.29
0.083
24.05
C


ATOM
2162
CD
LYS
A1318
8.157
−18.097
0.911
34.28
C


ATOM
2163
CE
LYS
A1318
9.463
−17.244
1.089
35.3
C


ATOM
2164
NZ
LYS
A1318
10.632
−18.122
0.888
37.08
N


ATOM
2165
C
LYS
A1318
6.414
−14.497
2.746
14.84
C


ATOM
2166
O
LYS
A1318
7.365
−14.269
3.513
15.47
O


ATOM
2167
N
CYS
A1319
5.472
−13.595
2.467
12.45
N


ATOM
2168
CA
CYS
A1319
5.395
−12.258
3.016
13.65
C


ATOM
2169
CB
CYS
A1319
4.184
−11.562
2.396
13.17
C


ATOM
2170
SG
CYS
A1319
4.626
−11.089
0.668
17.23
S


ATOM
2171
C
CYS
A1319
5.242
−12.206
4.498
11.7
C


ATOM
2172
O
CYS
A1319
5.657
−11.255
5.129
11.48
O


ATOM
2173
N
TRP
A1320
4.674
−13.272
5.038
11.74
N


ATOM
2174
CA
TRP
A1320
4.364
−13.378
6.418
11.21
C


ATOM
2175
CB
TRP
A1320
2.956
−13.816
6.577
10.12
C


ATOM
2176
CG
TRP
A1320
1.981
−12.93
5.933
8.99
C


ATOM
2177
CD2
TRP
A1320
0.794
−13.355
5.289
8.09
C


ATOM
2178
CE2
TRP
A1320
0.173
−12.196
4.77
6.13
C


ATOM
2179
CE3
TRP
A1320
0.152
−14.624
5.15
10.88
C


ATOM
2180
CD1
TRP
A1320
2.052
−11.549
5.778
7.31
C


ATOM
2181
NE1
TRP
A1320
0.971
−11.113
5.077
5.04
N


ATOM
2182
CZ2
TRP
A1320
−1.05
−12.246
4.139
5.59
C


ATOM
2183
CZ3
TRP
A1320
−1.066
−14.693
4.483
7.31
C


ATOM
2184
CH2
TRP
A1320
−1.641
−13.517
3.956
8.66
C


ATOM
2185
C
TRP
A1320
5.244
−14.353
7.147
13.67
C


ATOM
2186
O
TRP
A1320
4.827
−14.909
8.143
14.64
O


ATOM
2187
N
HIS
A1321
6.471
−14.547
6.666
15.52
N


ATOM
2188
CA
HIS
A1321
7.441
−15.283
7.387
15.52
C


ATOM
2189
CB
HIS
A1321
8.71
−15.494
6.566
15.45
C


ATOM
2190
CG
HIS
A1321
9.52
−16.676
7.019
19.13
C


ATOM
2191
CD2
HIS
A1321
9.627
−17.924
6.509
18.26
C


ATOM
2192
ND1
HIS
A1321
10.327
−16.649
8.147
17.94
N


ATOM
2193
CE1
HIS
A1321
10.873
−17.836
8.318
19.05
C


ATOM
2194
NE2
HIS
A1321
10.487
−18.617
7.323
21
N


ATOM
2195
C
HIS
A1321
7.723
−14.594
8.724
16.55
C


ATOM
2196
O
HIS
A1321
7.91
−13.367
8.798
14.69
O


ATOM
2197
N
PRO
A1322
7.719
−15.401
9.805
18.27
N


ATOM
2198
CD
PRO
A1322
7.45
−16.846
9.725
17.64
C


ATOM
2199
CA
PRO
A1322
8.004
−14.959
11.159
20.5
C


ATOM
2200
CB
PRO
A1322
8.069
−16.273
11.949
20.57
C


ATOM
2201
CG
PRO
A1322
7.257
−17.255
11.109
20.2
C


ATOM
2202
C
PRO
A1322
9.373
−14.272
11.183
22.28
C


ATOM
2203
O
PRO
A1322
9.553
−13.274
11.887
24.17
O


ATOM
2204
N
LYS
A1323
10.32
−14.818
10.441
23.53
N


ATOM
2205
CA
LYS
A1323
11.644
−14.265
10.317
26.14
C


ATOM
2206
CB
LYS
A1323
12.676
−15.384
10.057
26.85
C


ATOM
2207
CG
LYS
A1323
13.098
−16.183
11.289
32.8
C


ATOM
2208
CD
LYS
A1323
14.653
−16.203
11.372
40.5
C


ATOM
2209
CE
LYS
A1323
15.207
−14.739
11.543
40.83
C


ATOM
2210
NZ
LYS
A1323
16.672
−14.663
11.818
38.1
N


ATOM
2211
C
LYS
A1323
11.736
−13.231
9.224
26.02
C


ATOM
2212
O
LYS
A1323
11.931
−13.568
8.042
27.17
O


ATOM
2213
N
ALA
A1324
11.669
−11.973
9.63
27.03
N


ATOM
2214
CA
ALA
A1324
11.753
−10.83
8.711
27.52
C


ATOM
2215
CB
ALA
A1324
12.013
−9.546
9.448
27.19
C


ATOM
2216
C
ALA
A1324
12.743
−10.992
7.585
28.21
C


ATOM
2217
O
ALA
A1324
12.55
−10.353
6.541
29.23
O


ATOM
2218
N
GLU
A1325
13.758
−11.855
7.76
28.16
N


ATOM
2219
CA
GLU
A1325
14.848
−11.996
6.775
28.45
C


ATOM
2220
CB
GLU
A1325
16.188
−12.172
7.469
30.57
C


ATOM
2221
CG
GLU
A1325
16.132
−13.059
8.745
36.13
C


ATOM
2222
CD
GLU
A1325
17.211
−14.16
8.711
44.36
C


ATOM
2223
OE1
GLU
A1325
16.858
−15.364
8.463
44.39
O


ATOM
2224
OE2
GLU
A1325
18.411
−13.803
8.91
45.7
O


ATOM
2225
C
GLU
A1325
14.615
−13.104
5.73
26.67
C


ATOM
2226
O
GLU
A1325
15.22
−13.121
4.643
24.01
O


ATOM
2227
N
MET
A1326
13.683
−13.99
6.047
25.01
N


ATOM
2228
CA
MET
A1326
13.262
−14.975
5.077
24.44
C


ATOM
2229
CB
MET
A1326
12.799
−16.21
5.822
25.54
C


ATOM
2230
CG
MET
A1326
13.81
−16.689
6.838
30.66
C


ATOM
2231
SD
MET
A1326
15.391
−17.066
6.07
39.12
S


ATOM
2232
CE
MET
A1326
15.057
−18.795
5.656
38.1
C


ATOM
2233
C
MET
A1326
12.146
−14.455
4.17
22.62
C


ATOM
2234
O
MET
A1326
11.629
−15.161
3.301
22.3
O


ATOM
2235
N
ARG
A1327
11.718
−13.218
4.398
20.92
N


ATOM
2236
CA
ARG
A1327
10.72
−12.616
3.544
17.8
C


ATOM
2237
CB
ARG
A1327
10.117
−11.425
4.234
16.42
C


ATOM
2238
CG
ARG
A1327
9.313
−11.875
5.335
17.54
C


ATOM
2239
CD
ARG
A1327
8.503
−10.757
5.939
16.7
C


ATOM
2240
NE
ARG
A1327
8.293
−11.1
7.326
18.93
N


ATOM
2241
CZ
ARG
A1327
8.294
−10.232
8.337
12.34
C


ATOM
2242
NH1
ARG
A1327
8.497
−8.965
8.137
8.64
N


ATOM
2243
NH2
ARG
A1327
8.151
−10.678
9.537
12.79
N


ATOM
2244
C
ARG
A1327
11.36
−12.196
2.213
15.89
C


ATOM
2245
O
ARG
A1327
12.484
−11.73
2.175
14.94
O


ATOM
2246
N
PRO
A1328
10.609
−12.309
1.126
14.58
N


ATOM
2247
CD
PRO
A1328
9.266
−12.869
1.009
12.52
C


ATOM
2248
CA
PRO
A1328
11.167
−11.836
−0.146
13.78
C


ATOM
2249
CB
PRO
A1328
10.127
−12.248
−1.161
12.76
C


ATOM
2250
CG
PRO
A1328
8.86
−12.432
−0.349
15.33
C


ATOM
2251
C
PRO
A1328
11.328
−10.322
−0.181
14.39
C


ATOM
2252
O
PRO
A1328
10.566
−9.595
0.486
14.86
O


ATOM
2253
N
SER
A1329
12.302
−9.858
−0.972
14.35
N


ATOM
2254
CA
SER
A1329
12.494
−8.429
−1.282
14.19
C


ATOM
2255
CB
SER
A1329
13.904
−8.201
−1.891
13.44
C


ATOM
2256
OG
SER
A1329
13.89
−8.853
−3.18
15.17
O


ATOM
2257
C
SER
A1329
11.481
−8.011
−2.31
11.85
C


ATOM
2258
O
SER
A1329
11
−8.862
−3.097
14.08
O


ATOM
2259
N
PHE
A1330
11.222
−6.713
−2.389
10.58
N


ATOM
2260
CA
PHE
A1330
10.322
−6.24
−3.391
12.2
C


ATOM
2261
CB
PHE
A1330
9.996
−4.758
−3.212
11.92
C


ATOM
2262
CG
PHE
A1330
9.043
−4.493
−2.073
10.86
C


ATOM
2263
CD1
PHE
A1330
7.729
−4.902
−2.161
6
C


ATOM
2264
CD2
PHE
A1330
9.494
−3.884
−0.896
6.99
C


ATOM
2265
CE1
PHE
A1330
6.91
−4.709
−1.126
6.91
C


ATOM
2266
CE2
PHE
A1330
8.643
−3.633
0.136
9.1
C


ATOM
2267
CZ
PHE
A1330
7.349
−4.088
0.049
8.01
C


ATOM
2268
C
PHE
A1330
10.798
−6.542
−4.805
13.02
C


ATOM
2269
O
PHE
A1330
10
−6.6
−5.692
14.88
O


ATOM
2270
N
SER
A1331
12.086
−6.71
−5.022
14.67
N


ATOM
2271
CA
SER
A1331
12.609
−7.117
−6.325
16.24
C


ATOM
2272
CB
SER
A1331
14.109
−7.298
−6.207
17.17
C


ATOM
2273
OG
SER
A1331
14.734
−6.176
−6.688
18.61
O


ATOM
2274
C
SER
A1331
12.083
−8.473
−6.71
17.27
C


ATOM
2275
O
SER
A1331
11.591
−8.652
−7.857
18.02
O


ATOM
2276
N
GLU
A1332
12.201
−9.432
−5.777
17.22
N


ATOM
2277
CA
GLU
A1332
11.72
−10.756
−6.074
18.79
C


ATOM
2278
CB
GLU
A1332
12.302
−11.826
−5.205
19.77
C


ATOM
2279
CG
GLU
A1332
11.983
−13.29
−5.763
28.13
C


ATOM
2280
CD
GLU
A1332
12.543
−13.635
−7.25
32
C


ATOM
2281
OE1
GLU
A1332
12.099
−14.666
−7.872
28.88
O


ATOM
2282
OE2
GLU
A1332
13.401
−12.879
−7.778
32.58
O


ATOM
2283
C
GLU
A1332
10.214
−10.791
−6.033
18.26
C


ATOM
2284
O
GLU
A1332
9.584
−11.529
−6.828
18.92
O


ATOM
2285
N
LEU
A1333
9.602
−9.984
−5.174
16.87
N


ATOM
2286
CA
LEU
A1333
8.122
−9.956
−5.252
16.38
C


ATOM
2287
CB
LEU
A1333
7.522
−9.018
−4.227
16.3
C


ATOM
2288
CG
LEU
A1333
6.986
−9.505
−2.882
16.8
C


ATOM
2289
CD1
LEU
A1333
6.727
−11.004
−2.852
14.42 C



ATOM
2290
CD2
LEU
A1333
7.787
−9.07
−1.725
11.65
C


ATOM
2291
C
LEU
A1333
7.685
−9.55
−6.66
16
C


ATOM
2292
O
LEU
A1333
6.84
−10.217
−7.241
14.65
O


ATOM
2293
N
VAL
A1334
8.31
−8.508
−7.243
15.24
N


ATOM
2294
CA
VAL
A1334
7.993
−8.138
−8.648
14.36
C


ATOM
2295
CB
VAL
A1334
8.677
−6.82
−9.026
14.96
C


ATOM
2296
CG1
VAL
A1334
8.585
−6.5
−10.556
10.22
C


ATOM
2297
CG2
VAL
A1334
8.057
−5.675
−8.214
14.56
C


ATOM
2298
C
VAL
A1334
8.255
−9.218
−9.724
13.55
C


ATOM
2299
O
VAL
A1334
7.422
−9.446
−10.626
12.74
O


ATOM
2300
N
SER
A1335
9.399
−9.865
−9.634
13.77
N


ATOM
2301
CA
SER
A1335
9.72
−10.93
−10.566
14.73
C


ATOM
2302
CB
SER
A1335
11.063
−11.566
−10.217
14.19
C


ATOM
2303
OG
SER
A1335
12.091
−10.61
−10.426
16.15
O


ATOM
2304
C
SER
A1335
8.633
−11.994
−10.579
15.13
C


ATOM
2305
O
SER
A1335
8.096
−12.389
−11.628
14.15
O


ATOM
2306
N
ARG
A1336
8.282
−12.397
−9.376
15.11
N


ATOM
2307
CA
ARG
A1336
7.33
−13.462
−9.19
16.04
C


ATOM
2308
CB
ARG
A1336
7.326
−13.919
−7.745
15
C


ATOM
2309
CG
ARG
A1336
8.714
−14.435
−7.37
18.51
C


ATOM
2310
CD
ARG
A1336
8.656
−14.946
−5.887
31.61
C


ATOM
2311
NE
ARG
A1336
8.945
−16.391
−5.826
37.59
N


ATOM
2312
CZ
ARG
A1336
8.352
−17.326
−5.074
35.7
C


ATOM
2313
NH1
ARG
A1336
7.332
−17.055
−4.267
33.74
N


ATOM
2314
NH2
ARG
A1336
8.82
−18.576
−5.162
35.74
N


ATOM
2315
C
ARG
A1336
5.961
−13.09
−9.649
14.98
C


ATOM
2316
O
ARG
A1336
5.399
−13.775
−10.522
16.44
O


ATOM
2317
N
ILE
A1337
5.422
−12.005
−9.104
14.66
N


ATOM
2318
CA
ILE
A1337
4.113
−11.611
−9.481
16.19
C


ATOM
2319
CB
ILE
A1337
3.342
−10.739
−8.46
16.11
C


ATOM
2320
CG2
ILE
A1337
4.17
−9.721
−7.791
20.81
C


ATOM
2321
CG1
ILE
A1337
2.252
−9.97
−9.195
20.46
C


ATOM
2322
CD1
ILE
A1337
1.345
−9.167
−8.18
23.81
C


ATOM
2323
C
ILE
A1337
4.012
−11.191
−10.902
12.25
C


ATOM
2324
O
ILE
A1337
3.022
−11.435
−11.54
14.02
O


ATOM
2325
N
SER
A1338
5.028
−10.58
−11.446
11.38
N


ATOM
2326
CA
SER
A1338
5.013
−10.42
−12.924
10.49
C


ATOM
2327
CB
SER
A1338
6.354
−9.854
−13.388
10.85
C


ATOM
2328
OG
SER
A1338
6.152
−9.131
−14.566
10.54
O


ATOM
2329
C
SER
A1338
4.757
−11.755
−13.658
10
C


ATOM
2330
O
SER
A1338
4.007
−11.788
−14.66
110.17
O


ATOM
2331
N
ALA
A1339
5.416
−12.836
−13.207
8.72
N


ATOM
2332
CA
ALA
A1339
5.326
−14.152
−13.868
7.99
C


ATOM
2333
CB
ALA
A1339
6.29
−15.077
−13.294
5.14
C


ATOM
2334
C
ALA
A1339
3.925
−14.703
−13.758
9.66
C


ATOM
2335
O
ALA
A1339
3.353
−15.213
−14.736
9.27
O


ATOM
2336
N
ILE
A1340
3.359
−14.594
−12.542
11.06
N


ATOM
2337
CA
ILE
A1340
1.997
−14.976
−12.258
10.27
C


ATOM
2338
CB
ILE
A1340
1.733
−14.767
−10.76
10.82
C


ATOM
2339
CG2
ILE
A1340
0.282
−14.868
−10.418
8.31
C


ATOM
2340
CG1
ILE
A1340
2.558
−15.733
−9.91
10.31
C


ATOM
2341
CD1
ILE
A1340
2.557
−15.363
−8.468
8.49
C


ATOM
2342
C
ILE
A1340
1.016
−14.125
−13.086
11.55
C


ATOM
2343
O
ILE
A1340
0.04
−14.636
−13.667
12.6
O


ATOM
2344
N
PHE
A1341
1.239
−12.82
−13.094
11.83 
N


ATOM
2345
CA
PHE
A1341
0.472
−11.93
−13.942
12.83
C


ATOM
2346
CB
PHE
A1341
0.933
−10.462
−13.794
11.93
C


ATOM
2347
CG
PHE
A1341
0.097
−9.488
−14.628
10.99
C


ATOM
2348
CD1
PHE
A1341
−1.227
−9.222
−14.264
7.52
C


ATOM
2349
CD2
PHE
A1341
0.627
−8.868
−15.775
8.04
C


ATOM
2350
CE1
PHE
A1341
−2.058
−8.307
−15.048
11.01
C


ATOM
2351
CE2
PHE
A1341
−0.177
−7.999
−16.562
11.88
C


ATOM
2352
CZ
PHE
A1341
−1.556
−7.711
−16.174
9.93
C


ATOM
2353
C
PHE
A1341
0.463
−12.325
−15.397
12.79
C


ATOM
2354
O
PHE
A1341
−0.587
−12.401
−15.997
14.47
O


ATOM
2355
N
SER
A1342
1.638
−12.488
−15.974
15.32
N


ATOM
2356
CA
SER
A1342
1.824
−12.793
−17.415
17.78
C


ATOM
2357
CB
SER
A1342
3.315
−12.827
−17.797
16.79
C


ATOM
2358
OG
SER
A1342
3.831
−11.526
−17.777
21.88
O


ATOM
2359
C
SER
A1342
1.264
−14.123
−17.826
18.08
C


ATOM
2360
O
SER
A1342
0.703
−14.274
−18.9
17.24
O


ATOM
2361
N
THR
A1343
1.455
−15.104
−16.971
19.94
N


ATOM
2362
CA
THR
A1343
1.061
−16.422
−17.358
22.37
C


ATOM
2363
CB
THR
A1343
2.005
−17.478
−16.806
21.44
C


ATOM
2364
OG1
THR
A1343
2.055
−17.379
−15.369
21.47
O


ATOM
2365
CG2
THR
A1343
3.42
−17.315
−17.408
20.58
C


ATOM
2366
C
THR
A1343
−0.371
−16.659
−16.921
25.51
C


ATOM
2367
O
THR
A1343
−0.857
−17.769
−17.004
26.88
O


ATOM
2368
N
PHE
A1344
−1.054
−15.641
−16.409
28.5
N


ATOM
2369
CA
PHE
A1344
−2.33
−15.953
−15.798
30.95
C


ATOM
2370
CB
PHE
A1344
−2.881
−14.847
−14.904
30.06
C


ATOM
2371
CG
PHE
A1344
−4.151
−15.235
−14.222
27
C


ATOM
2372
CD1
PHE
A1344
−4.119
−16.097
−13.114
24.24
C


ATOM
2373
CD2
PHE
A1344
−5.368
−14.795
−14.711
23.57
C


ATOM
2374
CE1
PHE
A1344
−5.268
−16.519
−12.49
25.54
C


ATOM
2375
CE2
PHE
A1344
−6.539
−15.163
−14.084
27.12
C


ATOM
2376
CZ
PHE
A1344
−6.52
−16.033
−12.955
27.52
C


ATOM
2377
C
PHE
A1344
−3.35
−16.303
−16.855
33.54
C


ATOM
2378
O
PHE
A1344
−3.642
−15.49 
−17.717
34.12
O


ATOM
2379
N
ILE
A1345
−3.911
−17.508
−16.715
37.1
N


ATOM
2380
CA
ILE
A1345
−4.975
−18.047
−17.583
40.92
C


ATOM
2381
CB
ILE
A1345
−6.372
−17.424
−17.281
40.56
C


ATOM
2382
CG2
ILE
A1345
−7.344
−17.479
−18.492
43.36
C


ATOM
2383
CG1
ILE
A1345
−6.946
−18.152
−16.051
43.45
C


ATOM
2384
CD1
ILE
A1345
−6.095
−19.438
−15.574
42.93
C


ATOM
2385
C
ILE
A1345
−4.582
−18.074
−19.053
42.84
C


ATOM
2386
O
ILE
A1345
−4.93
−17.184
−19.846
43.44
O


ATOM
2387
N
GLY
A1346
−3.853
−19.135
−19.387
44.61
N


ATOM
2388
CA
GLY
A1346
−3.191
−19.289
−20.675
47.27
C


ATOM
2389
C
GLY
A1346
−1.718
−19.513
−20.354
49.35
C


ATOM
2390
O
GLY
A1346
−0.836
−18.874
−20.993
50.37
O


ATOM
2391
OXT
GLY
A1346
−1.376
−20.327
−19.436
49.81
O


ATOM
2392
CB
LEU
B1046
−19.47
−2.928
−35.925
40.32
C


ATOM
2393
CG
LEU
B1046
−19.758
−3.718
−34.616
42.01
C


ATOM
2394
CD1
LEU
B1046
−20.832
−2.953
−33.779
43.06
C


ATOM
2395
CD2
LEU
B1046
−20.105
−5.302
−34.77
43.57
C


ATOM
2396
C
LEU
B1046
−21.81
−3.071
−37.017
38.8
C


ATOM
2397
O
LEU
B1046
−22.337
−1.936
−36.888
38.58
O


ATOM
2398
N
LEU
B1046
−19.683
−2.665
−38.453
39.51
N


ATOM
2399
CA
LEU
B1046
−20.269
−3.271
−37.199
39.72
C


ATOM
2400
N
LEU
B1047
−22.5
−4.219
−37.024
36.75
N


ATOM
2401
CA
LEU
B1047
−23.938
−4.27
−37.208
35
C


ATOM
2402
CB
LEU
B1047
−24.394
−5.715
−37.47
35.39
C


ATOM
2403
CG
LEU
B1047
−23.713
−6.205
−38.741
35.87
C


ATOM
2404
CD1
LEU
B1047
−23.788
−7.735
−38.824
37.42
C


ATOM
2405
CD2
LEU
B1047
−24.313
−5.475
−39.975
37.06
C


ATOM
2406
C
LEU
B1047
−24.768
−3.645
−36.094
34.09
C


ATOM
2407
O
LEU
B1047
−25.941
−3.357
−36.318
34.1
O


ATOM
2408
N
GLN
B1048
−24.173
−3.443
−34.92
32.01
N


ATOM
2409
CA
GLN
B1048
−24.918
−2.908
−33.804
31.29
C


ATOM
2410
CB
GLN
B1048
−24.251
−3.227
−32.485
32.27
C


ATOM
2411
CG
GLN
B1048
−25.255
−3.176
−31.342
33.61
C


ATOM
2412
CD
GLN
B1048
−26.259
−4.273
−31.386
32.27
C


ATOM
2413
OE1
GLN
B1048
−27.227
−4.221
−30.635
33.78
O


ATOM
2414
NE2
GLN
B1048
−26.062
−5.279
−32.267
31.81
N


ATOM
2415
C
GLN
B1048
−25.025
−1.417
−33.875
29.15
C


ATOM
2416
O
GLN
B1048
−25.992
−0.848
−33.361
27.54
O


ATOM
2417
N
ASN
B1049
−24.017
−0.83
−34.532
26.05
N


ATOM
2418
CA
ASN
B1049
−23.931
0.576
−34.716
23.59
C


ATOM
2419
CB
ASN
B1049
−22.482
1.001
−34.97
24.38
C


ATOM
2420
CG
ASN
B1049
−21.622
0.973
−33.648
24.85
C


ATOM
2421
OD1
ASN
B1049
−22.107
1.324
−32.587
26.09
O


ATOM
2422
ND2
ASN
B1049
−20.402
0.522
−33.731
21.98
N


ATOM
2423
C
ASN
B1049
−24.868
1.003
−35.796
22.45
C


ATOM
2424
O
ASN
B1049
−24.841
2.144
−36.211
23.31
O


ATOM
2425
N
THR
B1050
−25.734
0.094
−36.206
20.21
N


ATOM
2426
CA
THR
B1050
−26.721
0.383
−37.195
20.27
C


ATOM
2427
CB
THR
B1050
−26.531
−0.463
−38.515
21.41
C


ATOM
2428
OG1
THR
B1050
−26.525
−1.886
−38.239
19.46
O


ATOM
2429
CG2
THR
B1050
−25.199
−0.064
−39.193
19.7
C


ATOM
2430
C
THR
B1050
−28.101
0.169
−36.592
20.15
C


ATOM
2431
O
THR
B1050
−29.095
0.325
−37.282
21.67
O


ATOM
2432
N
VAL
B1051
−28.179
−0.187
−35.313
18.2
N


ATOM
2433
CA
VAL
B1051
−29.469
−0.378
−34.68
16.02
C


ATOM
2434
CB
VAL
B1051
−29.476
−1.635
−33.802
15.07
C


ATOM
2435
CG1
VAL
B1051
−30.907
−1.929
−33.219
13
C


ATOM
2436
CG2
VAL
B1051
−28.978
−2.812
−34.622
14.4
C


ATOM
2437
C
VAL
B1051
−29.942
0.86
−33.933
15.78
C


ATOM
2438
O
VAL
B1051
−29.384
1.279
−32.964
16.31
O


ATOM
2439
N
HIS
B1052
−31.027
1.411
−34.394
16.59
N


ATOM
2440
CA
HIS
B1052
−31.618
2.529
−33.778
18.42
C


ATOM
2441
CB
HIS
B1052
−31.387
3.822
−34.557
18.24
C


ATOM
2442
CG
HIS
B1052
−32.216
4.963
−34.042
19.56
C


ATOM
2443
CD2
HIS
B1052
−33.382
5.5
−34.497
21.3
C


ATOM
2444
ND1
HIS
B1052
−31.871
5.688
−32.909
18.28
N


ATOM
2445
CE1
HIS
B1052
−32.789
6.613
−32.687
21.03
C


ATOM
2446
NE2
HIS
B1052
−33.717
6.522
−33.639
22.99
N


ATOM
2447
C
HIS
B1052
−33.121
2.309
−33.659
19.7
C


ATOM
2448
O
HIS
B1052
−33.795
2.169
−34.623
17.97
O


ATOM
2449
N
ILE
B1053
−33.613
2.326
−32.421
22.55
N


ATOM
2450
CA
ILE
B1053
−35.034
2.208
−32.114
23.12
C


ATOM
2451
CB
ILE
B1053
−35.285
0.984
−31.134
23.12
C


ATOM
2452
CG2
ILE
B1053
−36.733
0.925
−30.644
24.87
C


ATOM
2453
CG1
ILE
B1053
−35.093
−0.36
−31.88
25.79
C


ATOM
2454
CD1
ILE
B1053
−33.685
−0.82
−31.89
125.97
C


ATOM
2455
C
ILE
B1053
−35.501
3.595
−31.605
22.88
C


ATOM
2456
O
ILE
B1053
−34.884
4.229
−30.723
21.71
O


ATOM
2457
N
ASP
B1054
−36.547
4.089
−32.257
23.62
N


ATOM
2458
CA
ASP
B1054
−37.259
5.279
−31.796
22.76
C


ATOM
2459
CB
ASP
B1054
−37.853
6.041
−32.94
21.73
C


ATOM
2460
CG
ASP
B1054
−38.49
7.376
−32.487
25.42
C


ATOM
2461
OD1
ASP
B1054
−38.42
7.74
−31.259
22.46
O


ATOM
2462
OD2
ASP
B1054
−39.062
8.047
−33.389
24.97
O


ATOM
2463
C
ASP
B1054
−38.321
4.895
−30.767
22.65
C


ATOM
2464
O
ASP
B1054
−39.403
4.347
−31.071
21.94
O


ATOM
2465
N
LEU
B1055
−37.966
5.172
−29.529
22.61
N


ATOM
2466
CA
LEU
B1055
−38.7
4.625
−28.442
22.29
C


ATOM
2467
CB
LEU
B1055
−37.762
4.498
−27.224
22.09
C


ATOM
2468
CG
LEU
B1055
−36.525
3.601
−27.266
18
C


ATOM
2469
CD1
LEU
B1055
−35.705
4.088
−26.122
12.81
C


ATOM
2470
CD2
LEU
B1055
−36.869
2.13
−27.07
13.43
C


ATOM
2471
C
LEU
B1055
−39.982
5.424
−28.134
22.75
C


ATOM
2472
O
LEU
B1055
−40.843
4.978
−27.358
23.67
O


ATOM
2473
N
SER
B1056
−40.102
6.61
−28.713
22.3
N


ATOM
2474
CA
SER
B1056
−41.315
7.386
−28.546
22.63
C


ATOM
2475
CB
SER
B1056
−41.038
8.903
−28.703
22.8
C


ATOM
2476
OG
SER
B1056
−41.157
9.337
−30.088
27.69
O


ATOM
2477
C
SER
B1056
−42.349
6.877
−29.561
21.86
C


ATOM
2478
O
SER
B1056
−43.533
7.151
−29.427
21.84
O


ATOM
2479
N
ALA
B1057
−41.879
6.157
−30.584
20.99
N


ATOM
2480
CA
ALA
B1057
−42.734
5.647
−31.616
20.22
C


ATOM
2481
CB
ALA
B1057
−41.99
5.632
−32.978
18.95
C


ATOM
2482
C
ALA
B1057
−43.307
4.264
−31.229
21.18
C


ATOM
2483
O
ALA
B1057
−44.219
3.778
−31.926
20.6
O


ATOM
2484
N
ILE
B1058
−42.83
3.636
−30.124
21.64
N


ATOM
2485
CA
ILE
B1058
−43.436
2.342
−29.748
24.04
C


ATOM
2486
CB
ILE
B1058
−42.458
1.292
−28.981
25.07
C


ATOM
2487
CG2
ILE
B1058
−42.049
0.035
−29.832
24.86
C


ATOM
2488
CG1
ILE
B1058
−41.062
1.827
−28.705
27.45
C


ATOM
2489
CD1
ILE
B1058
−40.264
0.856
−27.838
24.61
C


ATOM
2490
C
ILE
B1058
−44.831
2.573
−29.065
24.88
C


ATOM
2491
O
ILE
B1058
−45.074
3.592
−28.422
23.85
O


ATOM
2492
N
ASP
B1059
−45.751
1.635
−29.243
25.65
N


ATOM
2493
CA
ASP
B1059
−47.12
1.761
−28.726
27.02
C


ATOM
2494
CB
ASP
B1059
−47.874
0.466
−29.066
27.56
C


ATOM
2495
CG
ASP
B1059
−49.325
0.485
−28.635
30.75
C


ATOM
2496
OD1
ASP
B1059
−49.705
1.293
−27.785
40.3
O


ATOM
2497
OD2
ASP
B1059
−50.123
−0.314
−29.14
31.86
O


ATOM
2498
C
ASP
B1059
−47.181
2.078
−27.208
26.95
C


ATOM
2499
O
ASP
B1059
−46.646
1.356
−26.4
26.36
O


ATOM
2500
N
PRO
B1060
−47.829
3.179
−26.83
27.49
N


ATOM
2501
CD
PRO
B1060
−48.573
4.133
−27.673
27.27
C


ATOM
2502
CA
PRO
B1060
−47.769
3.579
−25.41
28.26
C


ATOM
2503
CB
PRO
B1060
−48.521
4.909
−25.366
27.9
C


ATOM
2504
CG
PRO
B1060
−48.629
5.373
−26.822
28.06
C


ATOM
2505
C
PRO
B1060
−48.32
2.587
−24.385
29.45
C


ATOM
2506
O
PRO
B1060
−47.748
2.415
−23.307
30.22
O


ATOM
2507
N
GLU
B1061
−49.408
1.942
−24.706
30.74
N


ATOM
2508
CA
GLU
B1061
−49.959
0.958
−23.839
33.13
C


ATOM
2509
CB
GLU
B1061
−51.478
0.826
−24.17
34.78
C


ATOM
2510
CG
GLU
B1061
−51.864
−0.178
−25.282
40.8
C


ATOM
2511
CD
GLU
B1061
−52.775
0.432
−26.428
49.08
C


ATOM
2512
OE1
GLU
B1061
−52.827
1.704
−26.613
48.2
O


ATOM
2513
OE2
GLU
B1061
−53.38
−0.394
−27.2
48.8
O


ATOM
2514
C
GLU
B1061
−49.165
−0.372
−23.908
33.24
C


ATOM
2515
O
GLU
B1061
−49.181
−1.18
−22.979
34.27
O


ATOM
2516
N
LEU
B1062
−48.453
−0.62
−25.007
32.69
N


ATOM
2517
CA
LEU
B1062
−47.536
−1.766
−25.044
30.44
C


ATOM
2518
CB
LEU
B1062
−47.052
−2.023
−26.48
29.15
C


ATOM
2519
CG
LEU
B1062
−45.923
−2.999
−26.687
27.13
C


ATOM
2520
CD1
LEU
B1062
−46.297
−4.408
−26.216
31.15
C


ATOM
2521
CD2
LEU
B1062
−45.616
−3.05
−28.073
27.14
C


ATOM
2522
C
LEU
B1062
−46.37
−1.497
−24.1
30
C


ATOM
2523
O
LEU
B1062
−45.786
−2.41
−23.486
30.93
O


ATOM
2524
N
VAL
B1063
−46.038
−0.227
−23.992
29.06
N


ATOM
2525
CA
VAL
B1063
−44.925
0.206
−23.206
29
C


ATOM
2526
CB
VAL
B1063
−44.365
1.581
−23.717
29.34
C


ATOM
2527
CG1
VAL
B1063
−43.55
12.311
−22.617
29.44
C


ATOM
2528
CG2
VAL
B1063
−43.511
1.386
−24.988
28.58
C


ATOM
2529
C
VAL
B1063
−45.321
0.238
−21.745
29.41
C


ATOM
2530
O
VAL
B1063
−44.469
0.028
−20.86
30.22
O


ATOM
2531
N
GLN
B1064
−46.6
0.454
−21.467
29.08
N


ATOM
2532
CA
GLN
B1064
−47.005
0.512
−20.079
30.44
C


ATOM
2533
CB
GLN
B1064
−48.222
1.421
−19.809
30.98
C


ATOM
2534
CG
GLN
B1064
−49.62
0.775
−19.89
33.87
C


ATOM
2535
CD
GLN
B1064
−50.76
11.864
−19.961
35.5
C


ATOM
2536
OE1
GLN
B1064
−50.849
2.665
−20.92
36.93
O


ATOM
2537
NE2
GLN
B1064
−51.619
1.884
−18.929
38.37
N


ATOM
2538
C
GLN
B1064
−47.189
−0.853
−19.531
28.49
C


ATOM
2539
O
GLN
B1064
−46.973
−1.035
−18.366
29.12
O


ATOM
2540
N
ALA
B1065
−47.533
−1.823
−20.37
27.57
N


ATOM
2541
CA
ALA
B1065
−47.577
−3.233
−19.945
26.74
C


ATOM
2542
CB
ALA
B1065
−48.221
−4.172
−21.041
25.84
C


ATOM
2543
C
ALA
B1065
−46.183
−3.745
−19.532
25.79
C


ATOM
2544
O
ALA
B1065
−46.007
−4.275
−18.419
27.1
O


ATOM
2545
N
VAL
B1066
−45.179
−3.577
−20.408
24.07
N


ATOM
2546
CA
VAL
B1066
−43.793
−3.985
−20.03
720.35
C


ATOM
2547
CB
VAL
B1066
−42.881
−4.179
−21.255
19.59
C


ATOM
2548
CG1
VAL
B1066
−43.498
−5.217
−22.2
21.58
C


ATOM
2549
CG2
VAL
B1066
−42.557
−2.906
−21.898
16.39
C


ATOM
2550
C
VAL
B1066
−43.041
−3.122
−19.037
18.35
C


ATOM
2551
O
VAL
B1066
−42.011
−3.581
−18.522
15.66
O


ATOM
2552
N
GLN
B1067
−43.518
−1.892
−18.781
17.6
N


ATOM
2553
CA
GLN
B1067
−42.692
−0.943
−18.001
18.58
C


ATOM
2554
CB
GLN
B1067
−43.438
0.308
−17.614
19.35
C


ATOM
2555
CG
GLN
B1067
−42.496
1.426
−17.248
21.19
C


ATOM
2556
CD
GLN
B1067
−42.009
2.22
−18.529
28.66
C


ATOM
2557
OE1
GLN
B1067
−42.801
2.91
−19.19
34.61
O


ATOM
2558
NE2
GLN
B1067
−40.715
2.116
−18.857
29.45
N


ATOM
2559
C
GLN
B1067
−42.037
−1.527
−16.752
18.71
C


ATOM
2560
O
GLN
B1067
−40.856
−1.297
−16.503
18.11
O


ATOM
2561
N
HIS
B1068
−42.803
−2.315
−15.979
18.98
N


ATOM
2562
CA
HIS
B1068
−42.268
−2.956
−14.767
17.95
C


ATOM
2563
CB
HIS
B1068
−43.383
−3.675
−13.987
17.82
C


ATOM
2564
CG
HIS
B1068
−43.839
−4.954
−14.606
17.17
C


ATOM
2565
CD2
HIS
B1068
−43.713
−6.237
−14.176
14.13
C


ATOM
2566
ND1
HIS
B1068
−44.53
−5.009
−15.811
17.44
N


ATOM
2567
CE1
HIS
B1068
−44.793
−6.274
−16.089
13.01
C


ATOM
2568
NE2
HIS
B1068
−44.304
−7.033
−15.11
18.61
N


ATOM
2569
C
HIS
B1068
−41.102
−3.933
−15.002
18.08
C


ATOM
2570
O
HIS
B1068
−40.532
−4.395
−14.033
18.66
O


ATOM
2571
N
VAL
B1069
−40.726
−4.255
−16.243
16.48
N


ATOM
2572
CA
VAL
B1069
−39.549
−5.075
−16.433
16.15
C


ATOM
2573
CB
VAL
B1069
−39.863
−6.453
−17.109
16.83
C


ATOM
2574
CG1
VAL
B1069
−41.014
−7.1
−16.412
19.33
C


ATOM
2575
CG2
VAL
B1069
−40.229
−6.338
−18.559
14.34
C


ATOM
2576
C
VAL
B1069
−38.471
−4.345
−17.176
17.86
C


ATOM
2577
O
VAL
B1069
−37.419
−4.952
−17.516
16.09
O


ATOM
2578
N
VAL
B1070
−38.712
−3.044
−17.429
18.48
N


ATOM
2579
CA
VAL
B1070
−37.723
−2.234
−18.045
20.54
C


ATOM
2580
CB
VAL
B1070
−38.351
−1.049
−18.735
20.78
C


ATOM
2581
CG1
VAL
B1070
−37.268
0.109
−19.063
18.98
C


ATOM
2582
CG2
VAL
B1070
−39.005
−1.533
−19.984
18.5
C


ATOM
2583
C
VAL
B1070
−36.728
−1.82
−16.945
24.51
C


ATOM
2584
O
VAL
B1070
−37.163
−1.379
−15.872
24.82
O


ATOM
2585
N
ILE
B1071
−35.412
−1.965
−17.193
26.55
N


ATOM
2586
CA
ILE
B1071
−34.446
−1.77
−16.119
30.01
C


ATOM
2587
CB
ILE
B1071
−33.245
−2.653
−16.216
30.69
C


ATOM
2588
CG2
ILE
B1071
−32.383
−2.125
−17.338
33.43
C


ATOM
2589
CG1
ILE
B1071
−32.445
−2.495
−14.932
33.59
C


ATOM
2590
CD1
ILE
B1071
−31.103
−3.292
−14.886
40.65
C


ATOM
2591
C
ILE
B1071
−33.891
−0.359
−15.933
30.56
C


ATOM
2592
O
ILE
B1071
−33.696
0.101
−14.76
134.27
O


ATOM
2593
N
GLY
B1072
−33.597
0.356
−17.004
29.37
N


ATOM
2594
CA
GLY
B1072
−33.137
1.712
−16.772
26.85
C


ATOM
2595
C
GLY
B1072
−31.662
1.57
−16.679
26.99
C


ATOM
2596
O
GLY
B1072
−31.176
0.816
−15.851
25.3
O


ATOM
2597
N
PRO
B1073
−30.927
2.277
−17.567
27.71
N


ATOM
2598
CD
PRO
B1073
−31.427
3.359
−18.434
27.61
C


ATOM
2599
CA
PRO
B1073
−29.496
2.058
−17.766
27.02
C


ATOM
2600
CB
PRO
B1073
−29.153
3.005
−18.892
27.25
C


ATOM
2601
CG
PRO
B1073
−30.131
4.068
−18.823
28.49
C


ATOM
2602
C
PRO
B1073
−28.623
2.277
−16.545
27.4
C


ATOM
2603
O
PRO
B1073
−27.721
1.477
−16.282
29
O


ATOM
2604
N
SER
B1074
−28.896
3.3
−15.759
26.53 
N


ATOM
2605
CA
SER
B1074
−28.106
3.497
−14.564
25.63
C


ATOM
2606
CB
SER
B1074
−28.601
4.769
−13.836
27.59
C


ATOM
2607
OG
SER
B1074
−29.856
4.546
−13.133
31.65
O


ATOM
2608
C
SER
B1074
−28.251
2.296
−13.622
23.1
C


ATOM
2609
O
SER
B1074
−27.384
2.065
−12.768
23.98
O


ATOM
2610
N
SER
B1075
−29.357
1.574
−13.71
18.79
N


ATOM
2611
CA
SER
B1075
−29.571
0.456
−12.794
18.39
C


ATOM
2612
CB
SER
B1075
−31.059
0.086
−12.656
17.77
C


ATOM
2613
OG
SER
B1075
−31.839
1.212
−12.351
19.47
O


ATOM
2614
C
SER
B1075
−28.779
−0.81
−13.213
17.24
C


ATOM
2615
O
SER
B1075
−28.733
−1.788
−12.462
16.14
O


ATOM
2616
N
LEU
B1076
−28.205
−0.789
−14.42
16.22
N


ATOM
2617
CA
LEU
B1076
−27.525
−1.956
−14.919
17.04
C


ATOM
2618
CB
LEU
B1076
−28.278
−2.618
−16.083
15.02
C


ATOM
2619
CG
LEU
B1076
−27.488
−3.894
−16.519
13.13
C


ATOM
2620
CD1
LEU
B1076
−27.606
−5.133
−15.543
7.07
C


ATOM
2621
CD2
LEU
B1076
−27.827
−4.35
−17.936
8.37
C


ATOM
2622
C
LEU
B1076
−26.094
−1.653
−15.374
18
C


ATOM
2623
O
LEU
B1076
−25.845
−0.71
−16.155
18.86
O


ATOM
2624
N
ILE
B1077
−25.169
−2.464
−14.871
18.31
N


ATOM
2625
CA
ILE
B1077
−23.807
−2.441
−15.319
18.16
C


ATOM
2626
CB
ILE
B1077
−22.839
−2.115
−14.189
19.53
C


ATOM
2627
CG2
ILE
B1077
−22.56
−3.33
−13.34
22.33
C


ATOM
2628
CG1
ILE
B1077
−21.569
−1.492
−14.799
21.29
C


ATOM
2629
CD1
ILE
B1077
−21.712
0.173
−14.883
24.57
C


ATOM
2630
C
ILE
B1077
−23.434
−3.727
−16.041
16.53
C


ATOM
2631
O
ILE
B1077
−23.573
−4.818
−15.513
15.15
O


ATOM
2632
N
VAL
B1078
−23.04
−3.586
−17.297
15.26
N


ATOM
2633
CA
VAL
B1078
−22.6
−4.742
−18.049
15.42
C


ATOM
2634
CB
VAL
B1078
−23.043
−4.673
−19.544
16.36
C


ATOM
2635
CG1
VAL
B1078
−22.471
−5.905
−20.285
14.87
C


ATOM
2636
CG2
VAL
B1078
−24.636
−4.51
−19.726
11.11
C


ATOM
2637
C
VAL
B1078
−21.104
−4.807
−17.967
15.76
C


ATOM
2638
O
VAL
B1078
−20.415
−3.899
−18.399
16.11
O


ATOM
2639
N
HIS
B1079
−20.585
−5.882
−17.405
17.22
N


ATOM
2640
CA
HIS
B1079
−19.151
−6.04
−17.273
17.57
C


ATOM
2641
CB
HIS
B1079
−18.811
−6.974
−16.077
16.84
C


ATOM
2642
CG
HIS
B1079
−19.364
−6.485
−14.776
17.03
C


ATOM
2643
CD2
HIS
B1079
−20.056
−7.12
−13.793
21.02
C


ATOM
2644
ND1
HIS
B1079
−19.275
−5.165
−14.389
16.77
N


ATOM
2645
CE1
HIS
B1079
−19.92
−5
−13.24
19.8
C


ATOM
2646
NE2
HIS
B1079
−20.386
−6.173
−12.847
20.06
N


ATOM
2647
C
HIS
B1079
−18.635
−6.581
−18.64
18.29
C


ATOM
2648
O
HIS
B1079
−18.643
−7.789
−18.891
19.18
O


ATOM
2649
N
PHE
B1080
−18.201
−5.68
−19.514
18.22
N


ATOM
2650
CA
PHE
B1080
−17.706
−6.073
−20.82
19.57
C


ATOM
2651
CB
PHE
B1080
−17.608
−4.889
−21.759
19.74
C


ATOM
2652
CG
PHE
B1080
−18.942
−4.432
−22.233
19.46
C


ATOM
2653
CD1
PHE
B1080
−19.751
−5.295
−22.93
23.85
C


ATOM
2654
CD2
PHE
B1080
−19.403
−3.179
−21.925
22.05
C


ATOM
2655
CE1
PHE
B1080
−21.015
−4.902
−23.356
26.81
C


ATOM
2656
CE2
PHE
B1080
−20.663
−2.732
−22.313
21.69
C


ATOM
2657
CZ
PHE
B1080
−21.491
−3.592
−23.037
25.84
C


ATOM
2658
C
PHE
B1080
−16.419
−6.756
−20.781
20.12
C


ATOM
2659
O
PHE
B1080
−15.98
−7.259
−21.786
21.86
O


ATOM
2660
N
ASN
B1081
−15.811
−6.815
−19.61
20.99
N


ATOM
2661
CA
ASN
B1081
−14.49
−7.401
−19.465
21.84
C


ATOM
2662
CB
ASN
B1081
−13.673
−6.529
−18.514
21.63
C


ATOM
2663
CG
ASN
B1081
−14.274
−6.49
−17.069
20.2
C


ATOM
2664
OD1
ASN
B1081
−15.501
−6.616
−16.867
16.99
O


ATOM
2665
ND2
ASN
B1081
−13.405
−6.322
−16.085
15.89
N


ATOM
2666
C
ASN
B1081
−14.606
−8.795
−18.867
23.39
C


ATOM
2667
O
ASN
B1081
−13.604
−9.426
−18.54
24.79
O


ATOM
2668
N
GLU
B1082
−15.829
−9.267
−18.702
24.64
N


ATOM
2669
CA
GLU
B1082
−16.084
−10.518
−18.036
26.06
C


ATOM
2670
CB
GLU
B1082
−16.522
−10.215
−16.577
29.29
C


ATOM
2671
CG
GLU
B1082
−16.231
−11.268
−15.473
34.27
C


ATOM
2672
CD
GLU
B1082
−14.907
−11.959
−15.704
44.49
C


ATOM
2673
OE1
GLU
B1082
−14.676
−13.031
−15.057
45.75
O


ATOM
2674
OE2
GLU
B1082
−14.119
−11.43
−16.551
46.68
O


ATOM
2675
C
GLU
B1082
−17.217
−11.233
−18.766
24.39
C


ATOM
2676
O
GLU
B1082
−18.366
−11.067
−18.417
23.91
O


ATOM
2677
N
VAL
B1083
−16.87
−12.048
−19.745
22.94
N


ATOM
2678
CA
VAL
B1083
−17.822
−12.922
−20.483
21.14
C


ATOM
2679
CB
VAL
B1083
−17.234
−13.339
−21.91
20.22
C


ATOM
2680
CG1
VAL
B1083
−18.168
−14.113
−22.678
20.65
C


ATOM
2681
CG2
VAL
B1083
−16.972
−12.155
−22.701
20.7
C


ATOM
2682
C
VAL
B1083
−18.119
−14.182
−19.678
19.57
C


ATOM
2683
O
VAL
B1083
−17.216
−14.89
−19.278
20.67
O


ATOM
2684
N
ILE
B1084
−19.388
−14.495
−19.475
18.67
N


ATOM
2685
CA
ILE
B1084
−19.753
−15.742
−18.846
16.22
C


ATOM
2686
CB
ILE
B1084
−21.28
−15.711
−18.512
17.63
C


ATOM
2687
CG2
ILE
B1084
−21.768
−17.038
−17.916
17.14
C


ATOM
2688
CG1
ILE
B1084
−21.664
−14.544
−17.596
17.65
C


ATOM
2689
CD1
ILE
B1084
−23.067
−14.626
−17.029
11.56
C


ATOM
2690
C
ILE
B1084
−19.458
−16.902
−19.867
16.46
C


ATOM
2691
O
ILE
B1084
−18.887
−17.914
−19.53
15.12
O


ATOM
2692
N
GLY
B1085
−19.893
−16.739
−21.118
16.34
N


ATOM
2693
CA
GLY
B1085
−19.514
−17.614
−22.216
16.79
C


ATOM
2694
C
GLY
B1085
−19.858
−17.033
−23.558
18.48
C


ATOM
2695
O
GLY
B1085
−20.736
−16.182
−23.688
17.84
O


ATOM
2696
N
ARG
B1086
−19.122
−17.454
−24.572
21.62
N


ATOM
2697
CA
ARG
B1086
−19.513
−17.188
−25.976
24.64
C


ATOM
2698
CB
ARG
B1086
−18.458
−16.397
−26.721
24.78
C


ATOM
2699
CG
ARG
B1086
−17.073
−16.877
−26.491
31.15
C


ATOM
2700
CD
ARG
B1086
−16.223
−15.631
−26.219
35.05
C


ATOM
2701
NE
ARG
B1086
−16.505
−14.628
−27.228
34.79
N


ATOM
2702
CZ
ARG
B1086
−16.196
−13.337
−27.146
39.83
C


ATOM
2703
NH1
ARG
B1086
−15.603
−12.816
−26.057
37.31
N


ATOM
2704
NH2
ARG
B1086
−16.52
−12.555
−28.176
42.02
N


ATOM
2705
C
ARG
B1086
−19.868
−18.464
−26.719
24.15
C


ATOM
2706
O
ARG
B1086
−19.849
−19.536
−26.129
25.44
O


ATOM
2707
N
GLY
B1087
−20.246
−18.354
−27.988
24.14
N


ATOM
2708
CA
GLY
B1087
−20.613
−19.541
−28.764
22.48
C


ATOM
2709
C
GLY
B1087
−21.557
−19.128
−29.866
22.96
C


ATOM
2710
O
GLY
B1087
−21.668
−17.947
−30.179
22.52
O


ATOM
2711
N
HIS
B1088
−22.276
−20.087
−30.435
22.87
N


ATOM
2712
CA
HIS
B1088
−23.123
−19.797
−31.547
23.11
C


ATOM
2713
CB
HIS
B1088
−23.739
−21.099
−32.06
23.86
C


ATOM
2714
CG
HIS
B1088
−22.764
−22.012
−32.747
29.02
C


ATOM
2715
CD2
HIS
B1088
−21.826
−21.771
−33.703
33.46
C


ATOM
2716
ND1
HIS
B1088
−22.688
−23.375
−32.471
31.16
N


ATOM
2717
CE1
HIS
B1088
−21.741
−23.927
−33.216
31.77
C


ATOM
2718
NE2
HIS
B1088
−21.198
−22.979
−33.969
35.52
N


ATOM
2719
C
HIS
B1088
−24.199
−18.805
−31.131
22.73
C


ATOM
2720
O
HIS
B1088
−24.67
−18.004
−31.946
23.01
O


ATOM
2721
N
PHE
B1089
−24.611 
−18.88
−29.856
21.15 
N


ATOM
2722
CA
PHE
B1089
−25.64
−17.965
−29.292
19.41
C


ATOM
2723
CB
PHE
B1089
−26.116
−18.361
−27.851
17.09
C


ATOM
2724
CG
PHE
B1089
−24.998
−18.644
−26.906
15.09
C


ATOM
2725
CD1
PHE
B1089
−24.57
−19.945
−26.708
10.23
C


ATOM
2726
CD2
PHE
B1089
−24.337
−17.606
−26.235
15.28
C


ATOM
2727
CE1
PHE
B1089
−23.533
−20.227
−25.91
12.01
C


ATOM
2728
CE2
PHE
B1089
−23.256
−17.882
−25.376
11.78
C


ATOM
2729
CZ
PHE
B1089
−22.833
−19.17
−25.219
12.66
C


ATOM
2730
C
PHE
B1089
−25.193
−16.546
−29.29
18.49
C


ATOM
2731
O
PHE
B1089
−26.008
−15.624
−29.268
19.76
O


ATOM
2732
N
GLY
B1090
−23.888
−16.375
−29.266
18.92
N


ATOM
2733
CA
GLY
B1090
−23.269
−15.059
−29.181
18.6
C


ATOM
2734
C
GLY
B1090
−22.421
−14.958
−27.952
19.37
C


ATOM
2735
O
GLY
B1090
−21.628
−15.857
−27.601
19.8
O


ATOM
2736
N
CYS
B1091
−22.632
−13.863
−27.246
20.89
N


ATOM
2737
CA
CYS
B1091
−21.784
−13.532
−26.131
18.73
C


ATOM
2738
CB
CYS
B1091
−20.765
−12.491
−26.582
17.69
C


ATOM
2739
SG
CYS
B1091
−19.599
−12.191
−25.292
25.76
S


ATOM
2740
C
CYS
B1091
−22.658
−13.055
−24.95
16.84
C


ATOM
2741
O
CYS
B1091
−23.368
−12.093
−25.073
16.87
O


ATOM
2742
N
VAL
B1092
−22.606
−13.784
−23.821
15.9
N


ATOM
2743
CA
VAL
B1092
−23.285
−13.453
−22.564
13.08
C


ATOM
2744
CB
VAL
B1092
−23.925
−14.71
−22.003
13.11
C


ATOM
2745
CG1
VAL
B1092
−24.666
−14.416
−20.667
11.81
C


ATOM
2746
CG2
VAL
B1092
−24.849
−15.318
−23.044
9.74
C


ATOM
2747
C
VAL
B1092
−22.28
−12.846
−21.558
13.31
C


ATOM
2748
O
VAL
B1092
−21.195
−13.45
−21.285
12.97
O


ATOM
2749
N
TYR
B1093
−22.614
−11.675
−21.01
12.17
N


ATOM
2750
CA
TYR
B1093
−21.69
−11.008
−20.081
12.63
C


ATOM
2751
CB
TYR
B1093
−21.487
−9.535
−20.455
15.65
C


ATOM
2752
CG
TYR
B1093
−20.841
−9.296
−21.779
19.09
C


ATOM
2753
CD1
TYR
B1093
−21.625
−9.162
−22.952
23.98
C


ATOM
2754
CE1
TYR
B1093
−21.015
−8.929
−24.224
24.21
C


ATOM
2755
CD2
TYR
B1093
−19.438
−9.231
−21.89
23.44
C


ATOM
2756
CE2
TYR
B1093
−18.811
−9.033
−23.136
22.72
C


ATOM
2757
CZ
TYR
B1093
−19.613
−8.866
−24.294
24.32
C


ATOM
2758
OH
TYR
B1093
−19.014
−8.678
−25.537
26.39
O


ATOM
2759
C
TYR
B1093
−22.208
−11.057
−18.669
11.68
C


ATOM
2760
O
TYR
B1093
−23.387
−11.169
−18.415
10.89
O


ATOM
2761
N
HIS
B1094
−21.299
−10.925
−17.749
12.3
N


ATOM
2762
CA
HIS
B1094
−21.586
−10.755
−16.356
13.94
C


ATOM
2763
CB
HIS
B1094
−20.262
−10.865
−15.54
14.31
C


ATOM
2764
CG
HIS
B1094
−19.78
−12.281
−15.292
17.39
C


ATOM
2765
CD2
HIS
B1094
−18.702
−12.953
−15.769
16.61
C


ATOM
2766
ND1
HIS
B1094
−20.423
−13.158
−14.434
19.34
N


ATOM
2767
CE1
HIS
B1094
−19.751
−14.297
−14.387
17.95
C


ATOM
2768
NE2
HIS
B1094
−18.701
−14.196
−15.185
16.9
N


ATOM
2769
C
HIS
B1094
−22.193
−9.334
−16.234
14.54
C


ATOM
2770
O
HIS
B1094
−21.766
−8.464
−16.954
14.33
O


ATOM
2771
N
GLY
B1095
−23.174
−9.125
−15.343
15.33
N


ATOM
2772
CA
GLY
B1095
−23.679
−7.799
−15.024
17.33
C


ATOM
2773
C
GLY
B1095
−24.024
−7.644
−13.537
19.43
C


ATOM
2774
O
GLY
B1095
−24.178
−8.645
−12.821
20.21
O


ATOM
2775
N
THR
B1096
−24.127
−6.395
−13.075
19.44
N


ATOM
2776
CA
THR
B1096
−24.62
−6.053
−11.77
20.54
C


ATOM
2777
CB
THR
B1096
−23.533
−5.296
−10.884
22.73
C


ATOM
2778
OG1
THR
B1096
−22.325
−6.063
−10.81
24.87
O


ATOM
2779
CG2
THR
B1096
−23.999
−4.975
−9.458
21.73
C


ATOM
2780
C
THR
B1096
−25.899
−5.216
−11.944
20.08
C


ATOM
2781
O
THR
B1096
−25.953
−4.19
−12.614
18.92
O


ATOM
2782
N
LEU
B1097
−26.939
−5.68
−11.29
20.8
N


ATOM
2783
CA
LEU
B1097
−28.208
−5.019
−11.339
21.12
C


ATOM
2784
CB
LEU
B1097
−29.271
−6.052
−11.687
20.87
C


ATOM
2785
CG
LEU
B1097
−30.728
−5.667
−11.808
20.41
C


ATOM
2786
CD1
LEU
B1097
−30.878
−4.58
−12.837
16.06
C


ATOM
2787
CD2
LEU
B1097
−31.543
−6.919
−12.214
21.59
C


ATOM
2788
C
LEU
B1097
−28.466
−4.378
−9.989
21.74
C


ATOM
2789
O
LEU
B1097
−28.114
−4.932
−8.956
21.45
O


ATOM
2790
N
LEU
B1098
−29.026
−3.183
−10.009
22.86
N


ATOM
2791
CA
LEU
B1098
−29.656
−2.633
−8.818
25.58
C


ATOM
2792
CB
LEU
B1098
−29.714
−1.129
−8.928
27.1
C


ATOM
2793
CG
LEU
B1098
−28.506
−0.437
−8.287
32.12
C


ATOM
2794
CD1
LEU
B1098
−28.999
0.999
−7.909
35.01
C


ATOM
2795
CD2
LEU
B1098
−27.972
−1.212
−7.019
32.02
C


ATOM
2796
C
LEU
B1098
−31.076
−3.162
−8.549
26.01
C


ATOM
2797
O
LEU
B1098
−32.028
−2.912
−9.356
25.42
O


ATOM
2798
N
ASP
B1099
−31.232
−3.895
−7.445
25.81
N


ATOM
2799
CA
ASP
B1099
−32.545
−4.391
−7.105
27.24
C


ATOM
2800
CB
ASP
B1099
−32.484
−5.6
−6.116
28.47
C


ATOM
2801
CG
ASP
B1099
−32.237
−5.18
−4.638
30.23
C


ATOM
2802
OD1
ASP
B1099
−32.055
−6.081
−3.819
34.88
O


ATOM
2803
OD2
ASP
B1099
−32.207
−3.984
−4.275
32.44
O


ATOM
2804
C
ASP
B1099
−33.44
−3.248
−6.602
27.3
C


ATOM
2805
O
ASP
B1099
−32.963
−2.101
−6.454
25.57
O


ATOM
2806
N
ASN
B1100
−34.724
−3.579
−6.33
28.29
N


ATOM
2807
CA
ASN
B1100
−35.721
−2.609
−5.847
28.31
C


ATOM
2808
CB
ASN
B1100
−37.072
−3.219
−5.631
26.71
C


ATOM
2809
CG
ASN
B1100
−38.145
−2.143
−5.454
26.73
C


ATOM
2810
OD1
ASN
B1100
−38.8
−2.068
−4.398
20.33
O


ATOM
2811
ND2
ASN
B1100
−38.335
−1.282
−6.52
26.17
N


ATOM
2812
C
ASN
B1100
−35.348
−1.864
−4.576
29.84
C


ATOM
2813
O
ASN
B1100
−35.804
−0.737
−4.363
29.24
O


ATOM
2814
N
ASP
B1101
−34.554
−2.538
−3.74
31.72
N


ATOM
2815
CA
ASP
B1101
−33.82
−1.927
−2.64
34.59
C


ATOM
2816
CB
ASP
B1101
−33.808
−2.889
−1.481
33.48
C


ATOM
2817
CG
ASP
B1101
−35.207
−2.991
−0.827
39.38
C


ATOM
2818
OD1
ASP
B1101
−35.775
−1.921
−0.349
45.14
O


ATOM
2819
OD2
ASP
B1101
−35.761
−4.108
−0.813
36.72
O


ATOM
2820
C
ASP
B1101
−32.413
−1.465
−3.077
36.69
C


ATOM
2821
O
ASP
B1101
−32.127
−1.237
−4.265
36.88
O


ATOM
2822
N
GLY
B1102
−31.498
−1.305
−2.143
39.09
N


ATOM
2823
CA
GLY
B1102
−30.124
−0.924
−2.613
40.88
C


ATOM
2824
C
GLY
B1102
−29.297
−2.014
−3.32
39.37
C


ATOM
2825
O
GLY
B1102
−28.518
−1.73
−4.196
39.26
O


ATOM
2826
N
LYS
B1103
−29.521
−3.246
−2.908
38.65
N


ATOM
2827
CA
LYS
B1103
−28.754
−4.403
−3.272
38.51
C


ATOM
2828
CB
LYS
B1103
−29.56
−5.646
−2.852
39.63
C


ATOM
2829
CG
LYS
B1103
−28.778
−6.767
−2.134
44.66
C


ATOM
2830
CD
LYS
B1103
−29.167
−6.92
−0.629
52.43
C


ATOM
2831
CE
LYS
B1103
−30.716
−6.764
−0.3
54.14
C


ATOM
2832
NZ
LYS
B1103
−31.134
−5.32
0.054
55.6
N


ATOM
2833
C
LYS
B1103
−28.243
−4.509
−4.736
36.26
C


ATOM
2834
O
LYS
B1103
−28.98
−4.338
−5.686
35.57
O


ATOM
2835
N
LYS
B1104
−26.964
−4.828
−4.861
34.09
N


ATOM
2836
CA
LYS
B1104
−26.323
−5.12
−6.123
34.17
C


ATOM
2837
CB
LYS
B1104
−24.868
−4.601
−6.109
34.35
C


ATOM
2838
CG
LYS
B1104
−24.593
−3.486
−5.057
36.56
C


ATOM
2839
CD
LYS
B1104
−23.171
−2.909
−5.185
38.62
C


ATOM
2840
CE
LYS
B1104
−23.128
−1.452
−5.724
43.22
C


ATOM
2841
NZ
LYS
B1104
−23.341
−1.512
−7.206
46.31
N


ATOM
2842
C
LYS
B1104
−26.402
−6.652
−6.38
31.81
C


ATOM
2843
O
LYS
B1104
−25.87
−7.441
−5.616
31.44
O


ATOM
2844
N
ILE
B1105
−27.149
−7.033
−7.414
29.56
N


ATOM
2845
CA
ILE
B1105
−27.428
−8.426
−7.813
27.18
C


ATOM
2846
CB
ILE
B1105
−28.907
−8.58
−8.179
27.2
C


ATOM
2847
CG2
ILE
B1105
−29.283
−9.993
−8.613
26.76
C


ATOM
2848
CG1
ILE
B1105
−29.777
−8.168
−6.994
29.84
C


ATOM
2849
CD1
ILE
B1105
−29.216
−8.504
−5.573
31.01
C


ATOM
2850
C
ILE
B1105
−26.605
−8.859
−9.06
26.17
C


ATOM
2851
O
ILE
B1105
−26.553
−8.178
−10.122
24.06
O


ATOM
2852
N
HIS
B1106
−26.01
−10.031
−8.905
24.12
N


ATOM
2853
CA
HIS
B1106
−25.326
−10.679
−9.971
23.11
C


ATOM
2854
CB
HIS
B1106
−24.395
−11.738
−9.411
22.82
C


ATOM
2855
CG
HIS
B1106
−23.467
−12.292
−10.441
26.43
C


ATOM
2856
CD2
HIS
B1106
−23.107
−11.797
−11.66
26.36
C


ATOM
2857
ND1
HIS
B1106
−22.832
−13.509
−10.306
25.2
N


ATOM
2858
CE1
HIS
B1106
−22.083
−13.705
−11.374
29.25 
C


ATOM
2859
NE2
HIS
B1106
−22.239
−12.687
−12.212
25.17
N


ATOM
2860
C
HIS
B1106
−26.274
−11.204
−11.077
21.62
C


ATOM
2861
O
HIS
B1106
−27.227
−11.865
−10.811
22.59
O


ATOM
2862
N
CYS
B1107
−26.007
−10.883
−12.33
19.48
N


ATOM
2863
CA
CYS
B1107
−26.835
−11.388
−13.385
17.55
C


ATOM
2864
CB
CYS
B1107
−27.965
−10.384
−13.666
18.07
C


ATOM
2865
SG
CYS
B1107
−27.227
−8.718
−14.16
18.42
S


ATOM
2866
C
CYS
B1107
−26
−11.588
−14.661
16.17
C


ATOM
2867
O
CYS
B1107
−24.815
−11.264
−14.744
15.08
O


ATOM
2868
N
ALA
B1108
−26.695
−12.123
−15.666
15.55
N


ATOM
2869
CA
ALA
B1108
−26.16
−12.448
−16.975
11.19
C


ATOM
2870
CB
ALA
B1108
−26.452
−13.869
−17.222
10.83
C


ATOM
2871
C
ALA
B1108
−26.894
−11.561
−17.972
9.92
C


ATOM
2872
O
ALA
B1108
−28.124
−11.399
−17.883
6.01
O


ATOM
2873
N
VAL
B1109
−26.136
−10.926
−18.872
8.97
N


ATOM
2874
CA
VAL
B1109
−26.774
−10.01
−19.843
9.33
C


ATOM
2875
CB
VAL
B1109
−26.807
−8.391
−19.481
9.45
C


ATOM
2876
CG1
VAL
B1109
−26.032
−8.005
−18.3
8.25
C


ATOM
2877
CG2
VAL
B1109
−26.452
−7.547
−20.668
8.77
C


ATOM
2878
C
VAL
B1109
−26.389
−10.338
−21.304
9.24
C


ATOM
2879
0
VAL
B1109
−25.3
−10.815
−21.579
7.3
O


ATOM
2880
N
LYS
B1110
−27.33
−10.08
−22.194
9.22
N


ATOM
2881
CA
LYS
B1110
−27.189
−10.462
−23.567
11.63
C


ATOM
2882
CB
LYS
B1110
−27.786
−11.887
−23.756
12.52
C


ATOM
2883
CG
LYS
B1110
−27.781
−12.443
−25.149
13.32
C


ATOM
2884
CD
LYS
B1110
−26.441
−13.135
−25.377
11.87
C


ATOM
2885
CE
LYS
B1110
−26.107
−13.203
−26.846
21
C


ATOM
2886
NZ
LYS
B1110
−27.201
−13.071
−27.897
14.68
N


ATOM
2887
C
LYS
B1110
−27.941
−9.431
−24.432
11.11
C


ATOM
2888
O
LYS
B1110
−29.071
−9.075
−24.095
8.61
O


ATOM
2889
N
SER
B1111
−27.245
−8.907
−25.467
11.93
N


ATOM
2890
CA
SER
B1111
−27.887
−8.092
−26.53
13.48
C


ATOM
2891
CB
SER
B1111
−26.851
−7.147
−27.199
14.94
C


ATOM
2892
OG
SER
B1111
−27.026
−7.007
−28.604
13.55
O


ATOM
2893
C
SER
B1111
−28.647
−8.977
−27.532
13.17
C


ATOM
2894
O
SER
B1111
−28.147
−10.014
−27.985
11.98
O


ATOM
2895
N
LEU
B1112
−29.896 
−8.608
−27.816
14.3
N


ATOM
2896
CA
LEU
B1112
−30.675
−9.407
−28.783
14.87
C


ATOM
2897
CB
LEU
B1112
−32.192
−9.38
−28.546
15.11
C


ATOM
2898
CG
LEU
B1112
−32.469
−9.532
−27.068
12.54
C


ATOM
2899
CD1
LEU
B1112
−33.858
−9.321
−26.935
11.61
C


ATOM
2900
CD2
LEU
B1112
−32.111
−10.95
−26.66
12.26
C


ATOM
2901
C
LEU
B1112
−30.323
−8.969
−30.187
14.57
C


ATOM
2902
O
LEU
B1112
−31.054
−8.269
−30.824
13.73
O


ATOM
2903
N
ASN
B1113
−29.169
−9.435
−30.641
15.7
N


ATOM
2904
CA
ASN
B1113
−28.644
−9.036
−31.913
17.23
C


ATOM
2905
CB
ASN
B1113
−27.293
−9.678
−32.137
16.16
C


ATOM
2906
CG
ASN
B1113
−26.265
−9.178
−31.126
15.4
C


ATOM
2907
OD1
ASN
B1113
−26.097
−7.984
−30.918
15.23
O


ATOM
2908
ND2
ASN
B1113
−25.602
−10.073
−30.507
16.3
N


ATOM
2909
C
ASN
B1113
−29.569
−9.245
−33.104
18.32
C


ATOM
2910
O
ASN
B1113
−29.219
−8.847
−34.181
21.69
O


ATOM
2911
N
ARG
B1114
−30.765
−9.776
−32.907
16.84
N


ATOM
2912
CA
ARG
B1114
−31.561
−10.105
−34.016
16.33
C


ATOM
2913
CB
ARG
B1114
−32.027
−11.553
−33.914
17.05
C


ATOM
2914
CG
ARG
B1114
−30.88
−12.544
−34.163
19.42
C


ATOM
2915
CD
ARG
B1114
−31.261
−13.954
−33.837
22.69
C


ATOM
2916
NE
ARG
B1114
−32.327
−14.399
−34.716
29.67
N


ATOM
2917
CZ
ARG
B1114
−33.248
−15.305
−34.36
37.44
C


ATOM
2918
NH1
ARG
B1114
−33.236
−15.907
−33.125
34.6
N


ATOM
2919
NH2
ARG
B1114
−34.174
−15.635
−35.285
34.77
N


ATOM
2920
C
ARG
B1114
−32.719
−9.186
−34.121
16.57
C


ATOM
2921
O
ARG
B1114
−33.455
−9.265
−35.114
15.8
O


ATOM
2922
N
ILE
B1115
−32.923
−8.377
−33.064
16.18
N


ATOM
2923
CA
ILE
B1115
−33.885
−7.318
−33.061
15.66
C


ATOM
2924
CB
ILE
B1115
−34.432
−6.958
−31.659
16.8
C


ATOM
2925
CG2
ILE
B1115
−35.521
−5.899
−31.741
14.64
C


ATOM
2926
CG1
ILE
B1115
−34.762
−8.167
−30.74
19.85
C


ATOM
2927
CD1
ILE
B1115
−35.743
−9.11
−31.195
21.64
C


ATOM
2928
C
ILE
B1115
−33.133
−6.119
−33.611
15.81
C


ATOM
2929
O
ILE
B1115
−32.31
−5.46
−32.89
15.75
O


ATOM
2930
N
THR
B1116
−33.362
−5.856
−34.901
15.82
N


ATOM
2931
CA
THR
B1116
−32.576
−4.842
−35.64
16.62
C


ATOM
2932
CB
THR
B1116
−32.017
−5.435
−36.928
15.6
C


ATOM
2933
OG1
THR
B1116
−33.084
−5.709
−37.85
15.48
O


ATOM
2934
CG2
THR
B1116
−31.311
−6.728
−36.622
14.81
C


ATOM
2935
C
THR
B1116
−33.361
−3.528
−35.902
18
C


ATOM
2936
O
THR
B1116
−32.808
−2.563
−36.384
19.97
O


ATOM
2937
N
ASP
B1117
−34.652
−3.498
−35.583
18.89
N


ATOM
2938
CA
ASP
B1117
−35.485
−2.31
−35.723
18.62
C


ATOM
2939
CB
ASP
B1117
−35.95
−2.156
−37.175
20.27
C


ATOM
2940
CG
ASP
B1117
−36.778
−3.349
−37.646
23.06
C


ATOM
2941
OD1
ASP
B1117
−37.751
−3.729
−36.981
29.38
O


ATOM
2942
OD2
ASP
B1117
−36.46
−3.945
−38.686
32.03
O


ATOM
2943
C
ASP
B1117
−36.701
−2.351
−34.8
17.98
C


ATOM
2944
O
ASP
B1117
−36.942
−3.363
−34.138
18.33
O


ATOM
2945
N
ILE
B1118
−37.435
−1.232
−34.758
17.89
N


ATOM
2946
CA
ILE
B1118
−38.546
−1.012
−33.845
18.34
C


ATOM
2947
CB
ILE
B1118
−39.083
0.396
−33.961
19.06
C


ATOM
2948
CG2
ILE
B1118
−39.857
0.592
−35.276
18.01
C


ATOM
2949
CG1
ILE
B1118
−39.932
0.715
−32.733
20.21
C


ATOM
2950
CD1
ILE
B1118
−40.595
2.106
−32.764
20.59
C


ATOM
2951
C
ILE
B1118
−39.722
−1.987
−34.056
18.2
C


ATOM
2952
O
ILE
B1118
−40.434
−2.352
−33.116
16.36
O


ATOM
2953
N
GLY
B1119
−39.912
−2.41
−35.296
18.21
N


ATOM
2954
CA
GLY
B1119
−40.961
−3.359
−35.567
19.58
C


ATOM
2955
C
GLY
B1119
−40.705
−4.683
−34.836
20.43
C


ATOM
2956
O
GLY
B1119
−41.653
−5.29
−34.339
19.99
O


ATOM
2957
N
GLU
B1120
−39.423
−5.094
−34.794
19.5
N


ATOM
2958
CA
GLU
B1120
−38.965
−6.307
−34.155
20.69
C


ATOM
2959
CB
GLU
B1120
−37.588
−6.722
−34.711
20.04
C


ATOM
2960
CG
GLU
B1120
−37.682
−6.969
−36.176
23
C


ATOM
2961
CD
GLU
B1120
−36.343
−7.215
−36.859
26.75 
C


ATOM
2962
OE1
GLU
B1120
−35.262
−6.975
−36.243
25.12
O


ATOM
2963
OE2
GLU
B1120
−36.4
−7.619
−38.049
28.35
O


ATOM
2964
C
GLU
B1120
−38.938
−6.188
−32.6
20.23
C


ATOM
2965
O
GLU
B1120
−39.085
−7.197
−31.923
18.33
O


ATOM
2966
N
VAL
B1121
−38.754
−4.954
−32.08
20.43
N


ATOM
2967
CA
VAL
B1121
−38.787
−4.699
−30.651
20.56
C


ATOM
2968
CB
VAL
B1121
−38.324
−3.278
−30.303
20.8
C


ATOM
2969
CG1
VAL
B1121
−38.445
−3.064
−28.833
20.21
C


ATOM
2970
CG2
VAL
B1121
−36.884
−3.082
−30.672
19.6
C


ATOM
2971
C
VAL
B1121
−40.217
−4.911
−30.185
21.33
C


ATOM
2972
O
VAL
B1121
−40.487
−5.678
−29.252
23.1
O


ATOM
2973
N
SER
B1122
−41.141
−4.252
−30.869
21.22
N


ATOM
2974
CA
SER
B1122
−42.512
−4.24
−30.503
20.16
C


ATOM
2975
CB
SER
B1122
−43.213
−3.315
−31.468
20.41
C


ATOM
2976
OG
SER
B1122
−44.646
−3.36
−31.284
27.62
O


ATOM
2977
C
SER
B1122
−43.054
−5.679
−30.533
20.02
C


ATOM
2978
O
SER
B1122
−43.856
−6.091
−29.659
16.24
O


ATOM
2979
N
GLN
B1123
−42.557
−6.467
−31.517
20.28
N


ATOM
2980
CA
GLN
B1123
−42.983
−7.86
−31.617
20.71
C


ATOM
2981
CB
GLN
B1123
−42.579
−8.467
−32.959
21.57
C


ATOM
2982
CG
GLN
B1123
−42.542
−9.975
−32.88
26.83
C


ATOM
2983
CD
GLN
B1123
−42.828
−10.698
−34.188
34.81
C


ATOM
2984
OE1
GLN
B1123
−41.885
−11.107
−34.907
30.93
O


ATOM
2985
NE2
GLN
B1123
−44.141
−10.923
−34.478
34.08
N


ATOM
2986
C
GLN
B1123
−42.472
−8.71
−30.43
19.33
C


ATOM
2987
O
GLN
B1123
−43.164
−9.598
−29.906
18.63
O


ATOM
2988
N
PHE
B1124
−41.245
−8.416
−30.046
18.92
N


ATOM
2989
CA
PHE
B1124
−40.593
−8.976
−28.889
19.21
C


ATOM
2990
CB
PHE
B1124
−39.17
−8.464
−28.855
19.71 
C


ATOM
2991
CG
PHE
B1124
−38.487
−8.783
−27.6
20.88
C


ATOM
2992
CD1
PHE
B1124
−38.26
−10.104
−27.248
23.63
C


ATOM
2993
CD2
PHE
B1124
−38.134
−7.77
−26.724
20.85
C


ATOM
2994
CE1
PHE
B1124
−37.659
−10.407
−26.031
24.95
C


ATOM
2995
CE2
PHE
B1124
−37.538
−8.052
−25.524
20.74
C


ATOM
2996
CZ
PHE
B1124
−37.297
−9.35
−25.178
23.67
C


ATOM
2997
C
PHE
B1124
−41.296
−8.611
−27.564
18.85
C


ATOM
2998
O
PHE
B1124
−41.446
−9.435
−26.68
18.31
O


ATOM
2999
N
LEU
B1125
−41.75
−7.369
−27.439
18.95
N


ATOM
3000
CA
LEU
B1125
−42.379
−6.957
−26.208
19.31
C


ATOM
3001
CB
LEU
B1125
−42.611
−5.444
−26.14
18.61
C


ATOM
3002
CG
LEU
B1125
−41.395
−4.544
−26.055
17.81
C


ATOM
3003
CD1
LEU
B1125
−41.888
−3.154
−25.953
13.16
C


ATOM
3004
CD2
LEU
B1125
−40.476
−4.981
−24.911
14.76
C


ATOM
3005
C
LEU
B1125
−43.664
−7.693
−26.029
20.43
C


ATOM
3006
O
LEU
B1125
−43.999
−8.102
−24.885
19.8
O


ATOM
3007
N
THR
B1126
−44.346
−7.892
−27.165
21.81
N


ATOM
3008
CA
THR
B1126
−45.593
−8.636
−27.203
24.27
C


ATOM
3009
CB
THR
B1126
−46.294
−8.457
−28.491
25.04
C


ATOM
3010
OG1
THR
B1126
−46.77
−7.12
−28.565
27.43
O


ATOM
3011
CG2
THR
B1126
−47.491
−9.396
−28.593
27.15
C


ATOM
3012
C
THR
B1126
−45.397
−10.114
−26.995
25.94
C


ATOM
3013
O
THR
B1126
−45.977
−10.651
−26.074
25.49
O


ATOM
3014
N
GLU
B1127
−44.56
−10.747
−27.849
28.18
N


ATOM
3015
CA
GLU
B1127
−44.342
−12.216
−27.902
29.09
C


ATOM
3016
CB
GLU
B1127
−43.6
−12.615
−29.212
29.43
C


ATOM
3017
CG
GLU
B1127
−44.366
−12.433
−30.585
34.63
C


ATOM
3018
CD
GLU
B1127
−43.93
−13.447
−31.739
36.34
C


ATOM
3019
OE1
GLU
B1127
−42.932
−14.233
−31.583
42.77
O


ATOM
3020
OE2
GLU
B1127
−44.616
−13.46
−32.813
43.01
O


ATOM
3021
C
GLU
B1127
−43.509
−12.73
−26.759
27.06
C


ATOM
3022
O
GLU
B1127
−43.782
−13.746
−26.167
28.65
O


ATOM
3023
N
GLY
B1128
−42.419
−12.061
−26.507
25.65
N


ATOM
3024
CA
GLY
B1128
−41.409
−12.606
−25.676
23.56
C


ATOM
3025
C
GLY
B1128
−41.495
−12.108
−24.259
22.44
C


ATOM
3026
O
GLY
B1128
−40.861
−12.688
−23.385
23.01
O


ATOM
3027
N
ILE
B1129
−42.313
−11.087
−23.994
21.65
N


ATOM
3028
CA
ILE
B1129
−42.452
−10.613
−22.605
20.71
C


ATOM
3029
CB
ILE
B1129
−41.976
−9.163
−22.398
20.57
C


ATOM
3030
CG2
ILE
B1129
−42.295
−8.632
−20.984
16.98
C


ATOM
3031
CG1
ILE
B1129
−40.527
−8.996
−22.884
22.44
C


ATOM
3032
CD1
ILE
B1129
−39.511
−8.768
−21.844
27.47
C


ATOM
3033
C
ILE
B1129
−43.868
−10.773
−22.116
21.37
C


ATOM
3034
O
ILE
B1129
−44.074
−11.484
−21.141
22.91
O


ATOM
3035
N
ILE
B1130
−44.83
−10.116
−22.768
21.42
N


ATOM
3036
CA
ILE
B1130
−46.225
−10.12
−22.373
21.54
C


ATOM
3037
CB
ILE
B1130
−46.963
−8.979
−23.165
23.73
C


ATOM
3038
CG2
ILE
B1130
−48.557
−9.195
−23.349
23.9
C


ATOM
3039
CG1
ILE
B1130
−46.652
−7.612
−22.528
22.28
C


ATOM
3040
CD1
ILE
B1130
−46.984
−6.542
−23.431
29.63
C


ATOM
3041
C
ILE
B1130
−46.9
−11.48 
−22.593
21.67
C


ATOM
3042
O
ILE
B1130
−47.808
−11.858
−21.875
20.59
O


ATOM
3043
N
MET
B1131
−46.453
−12.211
−23.587
21.62
N


ATOM
3044
CA
MET
B1131
−47.003
−13.489
−23.86
25.06
C


ATOM
3045
CB
MET
B1131
−46.974
−13.796
−25.365
25.52
C


ATOM
3046
CG
MET
B1131
−48.265
−13.463
−26.138
28.21
C


ATOM
3047
SD
MET
B1131
−47.881
−13.85
−27.932
37.9
S


ATOM
3048
CE
MET
B1131
−48.83
−12.507
−28.735
33.81
C


ATOM
3049
C
MET
B1131
−46.236
−14.575
−23.133
23.04
C


ATOM
3050
O
MET
B1131
−46.56
−15.74
−23.305
22.39
O


ATOM
3051
N
LYS
B1132
−45.22 
−14.212
−22.347
22.43
N


ATOM
3052
CA
LYS
B1132
−44.486 
−15.183
−21.513
21.49
C


ATOM
3053
CB
LYS
B1132
−43.145 
−15.617
−22.13
21.65
C


ATOM
3054
CG
LYS
B1132
−43.284
−16.095
−23.534 
24.27
C


ATOM
3055
CD
LYS
B1132
−41.954 
−16.295
−24.221
26.68
C


ATOM
3056
CE
LYS
B1132
−42.215 
−17.072
−25.529
31.37
C


ATOM
3057
NZ
LYS
B1132
−40.981 
−17.343
−26.409
30.29
N


ATOM
3058
C
LYS
B1132
−44.264 
−14.664
−20.109
19.94
C


ATOM
3059
O
LYS
B1132
−43.142
−14.619 
−19.637
18.91
O


ATOM
3060
N
ASP
B1133
−45.356 
−14.262
−19.461
19.36
N


ATOM
3061
CA
ASP
B1133
−45.318 
−13.836
−18.068
18.25
C


ATOM
3062
CB
ASP
B1133
−46.394 
−12.803
−17.826
19.04
C


ATOM
3063
CG
ASP
B1133
−46.025
−11.787 
−16.716
25.02
C


ATOM
3064
OD1
ASP
B1133
−46.678 
−10.734
−16.677
32.68
O


ATOM
3065
OD2
ASP
B1133
−45.12 
−11.971
−15.874
27.29
O


ATOM
3066
C
ASP
B1133
−45.459
−15.042
−17.07 1 
6.25
C


ATOM
3067
O
ASP
B1133
−46.575
−15.418
−16.702
15.72 
O


ATOM
3068
N
PHE
B1134
−44.334
−15.661
−16.703
13.2
N


ATOM
3069
CA
PHE
B1134
−44.371 
−16.847
−15.908
13.49
C


ATOM
3070
CB
PHE
B1134
−43.749 
−18.062
−16.681
13.84
C


ATOM
3071
CG
PHE
B1134
−44.392 
−18.326
−17.977
12.66
C


ATOM
3072
CD1
PHE
B1134
−43.665
−18.247
−19.149
8.62
C


ATOM
3073
CD2
PHE
B1134
−45.74 
−18.598
−18.038
13.15
C


ATOM
3074
CE1
PHE
B1134
−44.24 
−18.472
−20.34
49.63
C


ATOM
3075
CE2
PHE
B1134
−46.381 
−18.775
−19.284
11.64
C


ATOM
3076
CZ
PHE
B1134
−45.626
−18.693
−20.441
12.7
C


ATOM
3077
C
PHE
B1134
−43.658
−16.664 
−14.532
12.63
C


ATOM
3078
O
PHE
B1134
−42.758
−15.847
−14.405
12.68 
O


ATOM
3079
N
SER
B1135
−44.032 
−17.467
−13.554
11.18
N


ATOM
3080
CA
SER
B1135
−43.437 
−17.455
−12.292
12.48
C


ATOM
3081
CB
SER
B1135
−44.072 
−16.389
−11.376
13.66
C


ATOM
3082
OG
SER
B1135
−43.358
−16.274 
−10.114
19.22
O


ATOM
3083
C
SER
B1135
−43.606
−18.843
−11.714 
11.96
C


ATOM
3084
O
SER
B1135
−44.722
−19.284
−11.4
10.34 
O


ATOM
3085
N
HIS
B1136
−42.453
−19.496
−11.574
10.83 
N


ATOM
3086
CA
HIS
B1136
−42.306
−20.857
−11.158
9.03
C


ATOM
3087
CB
HIS
B1136
−42.855
−21.851
−12.194
7.78
C


ATOM
3088
CG
HIS
B1136
−42.977
−23.233
−11.645
7.34
C


ATOM
3089
CD2
HIS
B1136
−44.027
−23.881
−11.077
7.24
C


ATOM
3090
ND1
HIS
B1136
−41.892
−24.076
−11.5
8.84
N


ATOM
3091
CE1
HIS
B1136
−42.293 
−25.22
−10.952
7.21
C


ATOM
3092
NE2
HIS
B1136
−43.589
−25.13 
−10.706
4.2
N


ATOM
3093
C
HIS
B1136
−40.833
−21.147
−10.873
9.44
C


ATOM
3094
O
HIS
B1136
−39.956
−20.823
−11.676
8.14
O


ATOM
3095
N
PRO
B1137
−40.546
−21.776
−9.716 
9.87
N


ATOM
3096
CD
PRO
B1137
−41.499
−22.126 
−8.63
10.69
C


ATOM
3097
CA
PRO
B1137
−39.187 
−22.146
−9.357
10.54 
C


ATOM
3098
CB
PRO
B1137
−39.406
−23.019
−8.096 
11.7
C


ATOM
3099
CG
PRO
B1137
−40.94 
−23.414 
−8.112
11.22 
C


ATOM
3100
C
PRO
B1137
−38.38 
−22.924 
−10.41
10.67
C


ATOM
3101
O
PRO
B1137
−37.14
−22.846
−10.452
11.71 
O


ATOM
3102
N
ASN
B1138
−39.037 
−23.703
−11.254
10.13
N


ATOM
3103
CA
ASN
B1138
−38.29 
−24.439
−12.246
9.9
C


ATOM
3104
CB
ASN
B1138
−38.763
−25.865
−12.216
9.42
C


ATOM
3105
CG
ASN
B1138
−38.553
−26.473
−10.929
8.48
C


ATOM
3106
OD1
ASN
B1138
−39.522
−26.863 
−10.251
15.21
O


ATOM
3107
ND2
ASN
B1138
−37.308
−26.552
−10.52 
8.93
N


ATOM
3108
C
ASN
B1138
−38.452 
−23.889
−13.678
10.14
C


ATOM
3109
O
ASN
B1138
−38.23 
−24.616
−14.66
48.96
O


ATOM
3110
N
VAL
B1139
−38.924
−22.657
−13.75
49.25
N


ATOM
3111
CA
VAL
B1139
−39.065
−21.923
−15.004
10.14 
C


ATOM
3112
CB
VAL
B1139
−40.54
−21.427
−15.265
8.36
C


ATOM
3113
CG1
VAL
B1139
−40.555 
−20.35
−16.371
8.76
C


ATOM
3114
CG2
VAL
B1139
−41.434
−22.588
−15.597
5.54
C


ATOM
3115
C
VAL
B1139
−38.13 
−20.705 
−14.944
10.69
C


ATOM
3116
O
VAL
B1139
−38.19 
−19.885
−14.027
10.15 
O


ATOM
3117
N
LEU
B1140
−37.28 
−20.593
−15.945
12.82
N


ATOM
3118
CA
LEU
B1140
−36.349 
−19.437
−16.033
13.46
C


ATOM
3119
CB
LEU
B1140
−35.175 
−19.772
−16.941
12.15
C


ATOM
3120
CG
LEU
B1140
−34.135
−18.663
−17.089
15.4
C


ATOM
3121
CD1
LEU
B1140
−33.713
−18.075
−15.707
18.65 
C


ATOM
3122
CD2
LEU
B1140
−32.907 
−19.173
−17.841
12.12
C


ATOM
3123
C
LEU
B1140
−37.037
−18.175
−16.586
13.98 
C


ATOM
3124
O
LEU
B1140
−37.475
−18.138
−17.745
13.7
O


ATOM
3125
N
SER
B1141
−37.085 
−17.129
−15.779
14.05
N


ATOM
3126
CA
SER
B1141
−37.655
−15.877
−16.224
14.32 
C


ATOM
3127
CB
SER
B1141
−38.768
−15.484
−15.25 
13.42
C


ATOM
3128
OG
SER
B1141
−39.906 
−16.321
−15.411
13.02
O


ATOM
3129
C
SER
B1141
−36.596 
−14.766
−16.233
15.85
C


ATOM
3130
O
SER
B1141
−35.669
−14.739
−15.377
15.5
O


ATOM
3131
N
LEU
B1142
−36.725 
−13.818
−17.152
16.95
N


ATOM
3132
CA
LEU
B1142
−35.742 
−12.734
−17.138
18.29
C


ATOM
3133
CB
LEU
B1142
−35.65 
−12.031
−18.472
20.03
C


ATOM
3134
CG
LEU
B1142
−36.683 
−11.192
−19.185
24.65
C


ATOM
3135
CD1
LEU
B1142
−36.465
−11.506
−20.665 
29.86
C


ATOM
3136
CD2
LEU
B1142
−38.054 
−11.563
−18.827
32.52
C


ATOM
3137
C
LEU
B1142
−35.978 
−11.764
−15.999
17.94
C


ATOM
3138
O
LEU
B1142
−37.135 
−11.543
−15.618
17.46
O


ATOM
3139
N
LEU
B1143
−34.899
−11.216
−15.437 
16.77
N


ATOM
3140
CA
LEU
B1143
−35.012 
−10.281
−14.378
16.17
C


ATOM
3141
CB
LEU
B1143
−33.665 
−9.964 
−13.809
16.58
C


ATOM
3142
CG
LEU
B1143
−32.949 
−11.007
−12.956
20.56
C


ATOM
3143
CD1
LEU
B1143
−31.483 
−10.458
−12.607
16.47
C


ATOM
3144
CD2
LEU
B1143
−33.812
−11.432 
−11.674
18.65
C


ATOM
3145
C
LEU
B1143
−35.629 
−9.006
−14.915
17.22
C


ATOM
3146
O
LEU
B1143
−36.534
−8.435 
−14.265
18.1
O


ATOM
3147
N
GLY
B1144
−35.191
−8.583 
−16.1
15.71
N


ATOM
3148
CA
GLY
B1144
−35.812 
−7.492
−16.747
17.55
C


ATOM
3149
C
GLY
B1144
−35.253
−7.37
−18.15
20.81 
C


ATOM
3150
O
GLY
B1144
−34.589
−8.28
−18.639
19.87 
O


ATOM
3151
N
ILE
B1145
−35.47 
−6.183
−18.749
23.32
N


ATOM
3152
CA
ILE
B1145
−35.234
−5.948
−20.142
25.4
C


ATOM
3153
CB
ILE
B1145
−36.486
−6.088
−21.066
25.54
C


ATOM
3154
CG2
ILE
B1145
−37.502
−4.876
−21.036
24.37
C


ATOM
3155
CG1
ILE
B1145
−36.033
−6.509
−22.437
26.57
C


ATOM
3156
CD1
ILE
B1145
−35.844
−5.401
−23.399
27.64
C


ATOM
3157
C
ILE
B1145
−34.341
−4.823
−20.522
26.94
C


ATOM
3158
O
ILE
B1145
−33.335
−5.104
−21.145
31.01
O


ATOM
3159
N
CYS
B1146
−34.585
−3.572
−20.255
26.18
N


ATOM
3160
CA
CYS
B1146
−33.589
−2.676
−20.911
27.81
C


ATOM
3161
CB
CYS
B1146
−32.206
−3.307
−20.8
28.25
C


ATOM
3162
SG
CYS
B1146
−30.968
−2.29
−20.084
39.86
S


ATOM
3163
C
CYS
B1146
−33.773
−2.264
−22.392
25.44
C


ATOM
3164
O
CYS
B1146
−33.198
−2.858
−23.32 
23.13
O


ATOM
3165
N
LEU
B1147
−34.518
−1.171
−22.583
25.47
N


ATOM
3166
CA
LEU
B1147
−34.844
−0.701
−23.923
24.48
C


ATOM
3167
CB
LEU
B1147
−36.316
−0.258
−23.981
25.28
C


ATOM
3168
CG
LEU
B1147
−37.558
−1.097
−24.228
25.29
C


ATOM
3169
CD1
LEU
B1147
−37.319
−2.1
−25.298
27.97
C


ATOM
3170
CD2
LEU
B1147
−37.919
−1.835
−23.005
29.1
C


ATOM
3171
C
LEU
B1147
−33.936
0.474
−24.325
24.42
C


ATOM
3172
O
LEU
B1147
−34.008
1.556
−23.735
23.15
O


ATOM
3173
N
ARG
B1148
−33.121
0.273
−25.353
23.32
N


ATOM
3174
CA
ARG
B1148
−32.146
1.268
−25.796
21.75
C


ATOM
3175
CB
ARG
B1148
−30.787
0.593
−25.999
20.87
C


ATOM
3176
CG
ARG
B1148
−30.383
−0.248
−24.849
19.8
C


ATOM
3177
CD
ARG
B1148
−28.89 
−0.531
−24.978
18.29
C


ATOM
3178
NE
ARG
B1148
−28.626
−1.545
−25.976
13.37
N


ATOM
3179
CZ
ARG
B1148
−27.407
−1.955
−26.323
16.93
C


ATOM
3180
NH1
ARG
B1148
−26.329
−1.435
−25.77
16.14
N


ATOM
3181
NH2
ARG
B1148
−27.271
−2.924
−27.214
14.69
N


ATOM
3182
C
ARG
B1148
−32.559
1.823
−27.148
21.36
C


ATOM
3183
O
ARG
B1148
−33.208
1.153
−27.92 
20.58
O


ATOM
3184
N
SER
B1149
−32.145
3.03
−27.46 
20.94
N


ATOM
3185
CA
SER
B1149
−32.415
3.529
−28.803
23.03
C


ATOM
3186
CB
SER
B1149
−32.81 
5
−28.785
23.52
C


ATOM
3187
OG
SER
B1149
−32.164
5.688
−27.735
27.64
O


ATOM
3188
C
SER
B1149
−31.197
3.354
−29.678
22.72
C


ATOM
3189
O
SER
B1149
−31.312
3.299
−30.88 
24.19
O


ATOM
3190
N
GLU
B1150
−30.026
3.218
−29.085
22.05
N


ATOM
3191
CA
GLU
B1150
−28.968
2.623
−29.868
22.66
C


ATOM
3192
CB
GLU
B1150
−27.718
3.501
−29.894
23.8
C


ATOM
3193
CG
GLU
B1150
−28.005
4.95
−30.295
30
C


ATOM
3194
CD
GLU
B1150
−26.698
5.665
−30.456
40.1
C


ATOM
3195
OE1
GLU
B1150
−25.743
5.351
−29.649
44.42
O


ATOM
3196
OE2
GLU
B1150
−26.6
6.507
−31.39 
41.6
O


ATOM
3197
C
GLU
B1150
−28.647
1.196
−29.458
20.41
C


ATOM
3198
O
GLU
B1150
−28.415
0.889
−28.303
18.54
O


ATOM
3199
N
GLY
B1151
−28.638
0.337
−30.449
18.5
N


ATOM
3200
CA
GLY
B1151
−28.221
−1.006
−30.23
17.16
C


ATOM
3201
C
GLY
B1151
−29.443
−1.827 
−29.963
16.88
C


ATOM
3202
O
GLY
B1151
−30.511 
−1.283
−29.731 
17.89
O


ATOM
3203
N
SER
B1152
−29.291 
−3.138
−30.001 
16.38
N


ATOM
3204
CA
SER
B1152
−30.385
−4.035 
−29.793
15.73
C


ATOM
3205
CB
SER
B1152
−29.973 
−5.418
−30.296 
16.22
C


ATOM
3206
OG
SER
B1152
−29.949 
−5.455
−31.709
17.36
O


ATOM
3207
C
SER
B1152
−30.776
−4.049 
−28.296
15.34 
C


ATOM
3208
O
SER
B1152
−29.979
−3.74
−27.395
14.35 
O


ATOM
3209
N
PRO
B1153
−32.021 
−4.399
−28.026
15.04
N


ATOM
3210
CD
PRO
B1153
−33.116 
−4.774
−28.945
13.23
C


ATOM
3211
CA
PRO
B1153
−32.397 
−4.431
−26.604
15.68
C


ATOM
3212
CB
PRO
B1153
−33.902 
−4.764
−26.616
14.25
C


ATOM
3213
CG
PRO
B1153
−34.335
−4.63
−28.038 
14.42
C


ATOM
3214
C
PRO
B1153
−31.597 
−5.479 
−25.808
16.25
C


ATOM
3215
O
PRO
B1153
−31.076 
−6.412
−26.374
18.1
O


ATOM
3216
N
LEU
B1154
−31.453 
−5.274
−24.505
16.93 
N


ATOM
3217
CA
LEU
B1154
−30.681 
−6.147
−23.64
15.03
C


ATOM
3218
CB
LEU
B1154
−29.958
−5.32
−22.638
15.08 
C


ATOM
3219
CG
LEU
B1154
−28.563 
−4.899
−23.086
18.21 
C


ATOM
3220
CD1
LEU
B1154
−28.269
−5.2
−24.556
12.75
C


ATOM
3221
CD2
LEU
B1154
−28.33 
−3.462
−22.734
14.99
C


ATOM
3222
C
LEU
B1154
−31.623 
−7.012
−22.876 
14.73
C


ATOM
3223
O
LEU
B1154
−32.705 
−6.607
−22.574
13.4
O


ATOM
3224
N
VAL
B1155
−31.199 
−8.227
−22.585
13.87
N


ATOM
3225
CA
VAL
B1155
−32.019 
−9.147
−21.863
13.52 
C


ATOM
3226
CB
VAL
B1155
−32.349 
−10.322
−22.832
14.55
C


ATOM
3227
CG1
VAL
B1155
−31.496 
−11.534
−22.58
14.03
C


ATOM
3228
CG2
VAL
B1155
−33.823
−10.609 
−22.785
18.15
C


ATOM
3229
C
VAL
B1155
−31.204 
−9.502
−20.622
11.35
C


ATOM
3230
O
VAL
B1155
−30.018 
−9.713
−20.715
11.04
O


ATOM
3231
N
VAL
B1156
−31.81 
−9.371
−19.455
11.53
N


ATOM
3232
CA
VAL
B1156
−31.118 
−9.533
−18.172 
11.14
C


ATOM
3233
CB
VAL
B1156
−31.192 
−8.245
−17.256
12.17
C


ATOM
3234
CG1
VAL
B1156
−30.313 
−8.371
−15.994
10.66
C


ATOM
3235
CG2
VAL
B1156
−30.748 
−6.969
−18.047
10.76
C


ATOM
3236
C
VAL
B1156
−31.722 
−10.771
−17.483
12.56
C


ATOM
3237
O
VAL
B1156
−32.97 
−10.885
−17.293
12.88
O


ATOM
3238
N
LEU
B1157
−30.847 
−11.733
−17.187
11.87
N


ATOM
3239
CA
LEU
B1157
−31.252
−12.933
−16.52 
10.49 
C


ATOM
3240
CB
LEU
B1157
−31.067 
−14.103
−17.467
11.83
C


ATOM
3241
CG
LEU
B1157
−32.163
−14.083
−18.539
10.1
C


ATOM
3242
CD1
LEU
B1157
−31.622
−13.381 
−19.796
10.35
C


ATOM
3243
CD2
LEU
B1157
−32.674
−15.419
−18.81
8.6
C


ATOM
3244
C
LEU
B1157
−30.496 
−13.192
−15.263
10.83
C


ATOM
3245
O
LEU
B1157
−29.321 
−12.728
−15.103
11.75
O


ATOM
3246
N
PRO
B1158
−31.122 
−13.969
−14.366
10.41
N


ATOM
3247
CD
PRO
B1158
−32.504
−14.489
−14.459
9.43
C


ATOM
3248
CA
PRO
B1158
−30.416
−14.389
−13.147
9.97
C


ATOM
3249
CB
PRO
B1158
−31.426
−15.321
−12.386
8.9
C


ATOM
3250
CG
PRO
B1158
−32.711 
−15.132
−13.099
11.26
C


ATOM
3251
C
PRO
B1158
−29.15
−15.139
−13.487
10.1
C


ATOM
3252
O
PRO
B1158
−29.076
−15.847
−14.493
9.14
O


ATOM
3253
N
TYR
B1159
−28.138
−14.912
−12.675
11.58
N


ATOM
3254
CA
TYR
B1159
−26.951
−15.703
−12.742
13.59
C


ATOM
3255
CB
TYR
B1159
−25.849
−15.174
−11.787
13.68
C


ATOM
3256
CG
TYR
B1159
−24.551
−15.855
−12.053
11.81
C


ATOM
3257
CD1
TYR
B1159
−24.019
−15.89
−13.372
10.98
C


ATOM
3258
CE1
TYR
B1159
−22.863
−16.554
−13.655
13.01
C


ATOM
3259
CD2
TYR
B1159
−23.877
−16.487
−11.057
9.14
C


ATOM
3260
CE2
TYR
B1159
−22.661
−17.182
−11.319
13.66
C


ATOM
3261
CZ
TYR
B1159
−22.136
−17.193
−12.616
14.72
C


ATOM
3262
OH
TYR
B1159
−20.946
−17.909
−12.902
14.73
O


ATOM
3263
C
TYR
B1159
−27.242
−17.175
−12.476
15.39
C


ATOM
3264
O
TYR
B1159
−27.802
−17.531
−11.415
15.7
O


ATOM
3265
N
MET
B1160
−26.915
−18.017
−13.469
16.37
N


ATOM
3266
CA
MET
B1160
−27.146
−19.454
−13.38
17.49
C


ATOM
3267
CB
MET
B1160
−27.924
−20.031
−14.581
16.46
C


ATOM
3268
CG
MET
B1160
−29.345
−19.722
−14.506
18.94
C


ATOM
3269
SD
MET
B1160
−30.35
−20.465
−13.143
24.07
S


ATOM
3270
CE
MET
B1160
−30.719
−19.019
−12.29
18.12
C


ATOM
3271
C
MET
B1160
−25.792
−20.045
−13.308
17.29
C


ATOM
3272
O
MET
B1160
−25.206
−20.378
−14.31
18
O


ATOM
3273
N
LYS
B1161
−25.318
−20.191
−12.09
18.45
N


ATOM
3274
CA
LYS
B1161
−23.951
−20.603
−11.824
18.74
C


ATOM
3275
CB
LYS
B1161
−23.776
−20.791
−10.319
19.72
C


ATOM
3276
CG
LYS
B1161
−22.35
−21.047
−9.981
23.56
C


ATOM
3277
CD
LYS
B1161
−22.224
−21.793
−8.725
29.41
C


ATOM
3278
CE
LYS
B1161
−20.946
−22.585
−8.754
30.13
C


ATOM
3279
NZ
LYS
B1161
−20.265
−22.285
−7.519
27.21
N


ATOM
3280
C
LYS
B1161
−23.5
−21.856
−12.55
18.52
C


ATOM
3281
O
LYS
B1161
−22.321
−21.926
−12.981
18.11
O


ATOM
3282
N
HIS
B1162
−24.405
−22.857
−12.644
17.41
N


ATOM
3283
CA
HIS
B1162
−24.078
−24.115
−13.34
16.48
C


ATOM
3284
CB
HIS
B1162
−24.523
−25.36
−12.589
16.27
C


ATOM
3285
CG
HIS
B1162
−23.83
−25.477
−11.266
16.91
C


ATOM
3286
CD2
HIS
B1162
−24.284
−25.341
−10.003
16.13
C


ATOM
3287
ND1
HIS
B1162
−22.46
−25.683
−11.166
17.49
N


ATOM
3288
CE1
HIS
B1162
−22.101
−25.672
−9.901
14.86
C


ATOM
3289
NE2
HIS
B1162
−23.179
−25.435
−9.173
20.15
N


ATOM
3290
C
HIS
B1162
−24.306
−24.198
−14.829
15.43
C


ATOM
3291
O
HIS
B1162
−23.91
−25.177
−15.453
16.77
O


ATOM
3292
N
GLY
B1163
−24.847
−23.142
−15.4
14.23
N


ATOM
3293
CA
GLY
B1163
−25.038
−23.084
−16.822
14.76
C


ATOM
3294
C
GLY
B1163
−26.047
−24.096
−17.255
15.34
C


ATOM
3295
O
GLY
B1163
−26.976
−24.428
−16.501
16.36
O


ATOM
3296
N
ASP
B1164
−25.917
−24.588
−18.48
16.34
N


ATOM
3297
CA
ASP
B1164
−26.945
−25.538
−18.957
18.41
C


ATOM
3298
CB
ASP
B1164
−27.121
−25.598
−20.496
18.9
C


ATOM
3299
CG
ASP
B1164
−25.891
−26.048
−21.199
21.41
C


ATOM
3300
OD1
ASP
B1164
−24.914
−25.301
−21.18
28.55
O


ATOM
3301
OD2
ASP
B1164
−25.853
−27.138
−21.785
29.67
O


ATOM
3302
C
ASP
B1164
−26.682
−26.928
−18.37
17.3
C


ATOM
3303
O
ASP
B1164
−25.566
−27.291
−18.054
16
O


ATOM
3304
N
LEU
B1165
−27.774
−27.648
−18.211
17.7
N


ATOM
3305
CA
LEU
B1165
−27.81
−28.965
−17.592
18.17
C


ATOM
3306
CB
LEU
B1165
−29.266
−29.359
−17.491
17.68
C


ATOM
3307
CG
LEU
B1165
−29.707
−30.465
−16.606
19.62
C


ATOM
3308
CD1
LEU
B1165
−29.32
−30.147
−15.204
16.24
C


ATOM
3309
CD2
LEU
B1165
−31.247
−30.479
−16.754
18.87
C


ATOM
3310
C
LEU
B1165
−27.036
−29.93
−18.463
18.24
C


ATOM
3311
O
LEU
B1165
−26.37
−30.857
−17.984
19.49
O


CATOM
3312
O
GLN
B1166
−24.217
−31.36
−20.284
19.01
O


ATOM
3313
N
GLN
B1166
−27.018
−29.582
−19.74
20



ATOM
3314
CA
GLN
B1166
−26.241
−30.315
−20.685
20



ATOM
3315
C
GLN
B1166
−24.776
−30.339
−20.427
20



ATOM
3316
CB
GLN
B1166
−26.63
−30.114
−22.143
20



ATOM
3317
CG
GLN
B1166
−26.508
−31.277
−22.946
20



ATOM
3318
CD
GLN
B1166
−25.18
−31.389
−23.537
20



ATOM
3319
OE1
GLN
B1166
−24.559
−30.388
−23.785
20



ATOM
3320
NE2
GLN
B1166
−24.739
−32.604
−23.846
20



ATOM
3321
N
ASN
B1167
−24.187
−29.18
−20.32
17.24
N


ATOM
3322
CA
ASN
B1167
−22.791
−29.026
−20.108
16.95
C


ATOM
3323
CB
ASN
B1167
−22.376
−27.567
−20.263
20.74
C


ATOM
3324
CG
ASN
B1167
−22.142
−27.188
−21.735
27.08
C


ATOM
3325
OD1
ASN
B1167
−22.25
−26.022
−22.133
31.53
O


ATOM
3326
ND2
ASN
B1167
−21.845
−28.203
−22.554
33.46
N


ATOM
3327
C
ASN
B1167
−22.438
−29.459
−18.73
15.8
C


ATOM
3328
O
ASN
B1167
−21.324
−29.908
−18.491
15.55
O


ATOM
3329
N
PHE
B1168
−23.407
−29.357
−17.815
13.95
N


ATOM
3330
CA
PHE
B1168
−23.214
−29.806
−16.451
10.88
C


ATOM
3331
CB
PHE
B1168
−24.361
−29.366
−15.595
11.09
C


ATOM
3332
CG
PHE
B1168
−24.158
−29.635
−14.117
11.13
C


ATOM
3333
CD1
PHE
B1168
−23.363
−28.811
−13.353
10.57
C


ATOM
3334
CD2
PHE
B1168
−24.695
−30.78
−13.517
12.93
C


ATOM
3335
CE1
PHE
B1168
−23.163
−29.081
−11.984
10.74
C


ATOM
3336
CE2
PHE
B1168
−24.481
−31.042
−12.106
11.1
C


ATOM
3337
CZ
PHE
B1168
−23.755
−30.167
−11.369
8.04
C


ATOM
3338
C
PHE
B1168
−22.949
−31.297
−16.311
10.98
C


ATOM
3339
O
PHE
B1168
−21.953
−31.673
−15.737
11.29
O


ATOM
3340
N
ILE
B1169
−23.815
−32.144
−16.851
11.3
N


ATOM
3341
CA
ILE
B1169
−23.729
−33.567
−16.649
12.11
C


ATOM
3342
CB
ILE
B1169
−25.098
−34.24
−16.912
12.31
C


ATOM
3343
CG2
ILE
B1169
−26.225
−33.639
−16.073
10.67
C


ATOM
3344
CG1
ILE
B1169
−25.46
−34.188
−18.407
13.38
C


ATOM
3345
CD1
ILE
B1169
−26.855
−34.265
−18.702
10.53
C


ATOM
3346
C
ILE
B1169
−22.594
−34.162
−17.527
15.08
C


ATOM
3347
O
ILE
B1169
−22.133
−35.264
−17.321
15.78
O


ATOM
3348
N
ARG
B1170
−22.087
−33.403
−18.478
18.02
N


ATOM
3349
CA
ARG
B1170
−20.955
−33.871
−19.3
20.11
C


ATOM
3350
CB
ARG
B1170
−20.93
−33.178
−20.633
20.14
C


ATOM
3351
CG
ARG
B1170
−21.93
−33.631
−21.507
25.59
C


ATOM
3352
CD
ARG
B1170
−21.717
−32.821
−22.713
37.19
C


ATOM
3353
NE
ARG
B1170
−20.989
−33.521
−23.777
45.62
N


ATOM
3354
CZ
ARG
B1170
−20.98
−34.84 
−23.999
48.56
C


ATOM
3355
NH1
ARG
B1170
−21.656
−35.705
−23.257
49.01
N


ATOM
3356
NH2
ARG
B1170
−20.276
−35.287
−25.009
53.39
N


ATOM
3357
C
ARG
B1170
−19.646
−33.526
−18.713
19.84
C


ATOM
3358
O
ARG
B1170
−18.677
−34.145
−19.024
20.06
O


ATOM
3359
N
ASN
B1171
−19.618
−32.485
−17.907
21.49
N


ATOM
3360
CA
ASN
B1171
−18.43
−32.106
−17.182
22.67
C


ATOM
3361
CB
ASN
B1171
−18.795
−30.932
−16.286
23.22
C


ATOM
3362
CG
ASN
B1171
−17.572
−30.201
−15.733
23.88
C


ATOM
3363
OD1
ASN
B1171
−16.55
−30.813
−15.4
20.38
O


ATOM
3364
ND2
ASN
B1171
−17.694
−28.874
−15.624
20.34
N


ATOM
3365
C
ASN
B1171
−17.885
−33.289
−16.354
24.16
C


ATOM
3366
O
ASN
B1171
−18.536
−33.819
−15.452
22.97
O


ATOM
3367
N
GLU
B1172
−16.678
−33.712
−16.71
26.75
N


ATOM
3368
CA
GLU
B1172
−16.009
−34.843
−16.074
28.61
C


ATOM
3369
CB
GLU
B1172
−14.887
−35.381
−16.95
29.06
C


ATOM
3370
CG
GLU
B1172
−15.267
−35.539
−18.398
35.59
C


ATOM
3371
CD
GLU
B1172
−14.865
−34.295
−19.239
43.46
C


ATOM
3372
OE1
GLU
B1172
−15.514
−33.222
−19.077
43.38
O


ATOM
3373
OE2
GLU
B1172
−13.887
−34.403
−20.063
47.72
O


ATOM
3374
C
GLU
B1172
−15.483
−34.444
−14.708
27.92
C


ATOM
3375
O
GLU
B1172
−15.003
−35.266
−13.956
29.83
O


ATOM
3376
N
THR
B1173
−15.636
−33.183
−14.372
27.32
N


ATOM
3377
CA
THR
B1173
−15.43
−32.68
−13.012
26.3
C


ATOM
3378
CB
THR
B1173
−15.075
−31.202
−13.127
26.43
C


ATOM
3379
OG1
THR
B1173
−13.63
−31.125
−13.229
30.48
O


ATOM
3380
CG2
THR
B1173
−15.66
−30.328
−12.025
23.88
C


ATOM
3381
C
THR
B1173
−16.558
−32.937
−11.996
24.95
C


ATOM
3382
O
THR
B1173
−16.435
−32.607
−10.82
24.21
O


ATOM
3383
N
HIS
B1174
−17.62
−33.571
−12.472
24.38
N


ATOM
3384
CA
HIS
B1174
−18.893
−33.624
−11.786
25.17
C


ATOM
3385
CB
HIS
B1174
−20.018
−32.862
−12.503
25.48
C


ATOM
3386
CG
HIS
B1174
−19.887
−31.375
−12.444
29.5
C


ATOM
3387
CD2
HIS
B1174
−19.494
−30.546
−11.44
31.51
C


ATOM
3388
ND1
HIS
B1174
−20.152
−30.563
−13.535
33.78
N


ATOM
3389
CE1
HIS
B1174
−19.929
−29.297
−13.204
33.6
C


ATOM
3390
NE2
HIS
B1174
−19.518
−29.261
−11.942
33.57
N


ATOM
3391
C
HIS
B1174
−19.237
−35.06
−11.806
24.6
C


ATOM
3392
O
HIS
B1174
−19.048
−35.739
−12.822
25
O


ATOM
3393
N
ASN
B1175
−19.709
−35.531
−10.662
23.47
N


ATOM
3394
CA
ASN
B1175
−20.013
−36.93
−10.504
22.28
C


ATOM
3395
CB
ASN
B1175
−18.961
−37.601
−9.664
20.86
C


ATOM
3396
CG
ASN
B1175
−17.621
−37.656
−10.387
19.89
C


ATOM
3397
OD1
ASN
B1175
−17.519
−38.384
−11.343
22.05
O


ATOM
3398
ND2
ASN
B1175
−16.619
−36.852
−9.971
16.3
N


ATOM
3399
C
ASN
B1175
−21.423
−37.021
−9.946
23.32
C


ATOM
3400
O
ASN
B1175
−21.635
−37.437
−8.785
24.86
O


ATOM
3401
N
PRO
B1176
−22.414
−36.616
−10.773
22.41
N


ATOM
3402
CD
PRO
B1176
−22.338
−36.215
−12.177
22.32
C


ATOM
3403
CA
PRO
B1176
−23.771
−36.663
−10.305
23.02
C


ATOM
3404
CB
PRO
B1176
−24.534
−35.94
−11.415
22.38
C


ATOM
3405
CG
PRO
B1176
−23.765
−36.251
−12.623
22.63
C


ATOM
3406
C
PRO
B1176
−24.193
−38.161
−10.156
23.36
C


ATOM
3407
O
PRO
B1176
−23.874
−38.971
−11.045
23.72
O


ATOM
3408
N
THR
B1177
−24.891
−38.522
−9.066
22.41
N


ATOM
3409
CA
THR
B1177
−25.329 
−39.894
−8.913
22.82
C


ATOM
3410
CB
THR
B1177
−25.906
−40.189
−7.496
23.27
C


ATOM
3411
OG1
THR
B1177
−26.923
−39.244
−7.205
25.75
O


ATOM
3412
CG2
THR
B1177
−24.846
−40.122
−6.402
24.8
C


ATOM
3413
C
THR
B1177
−26.445
−40.103
−9.907
21.38
C


ATOM
3414
O
THR
B1177
−27.015
−39.122
−10.377
22.43
O


ATOM
3415
N
VAL
B1178
−26.814
−41.362
−10.162
20.22
N


ATOM
3416
CA
VAL
B1178
−28.127
−41.672
−10.826
18.98
C


ATOM
3417
CB
VAL
B1178
−28.384
−43.198
−10.992
18.34
C


ATOM
3418
CG1
VAL
B1178
−29.81
−43.489
−11.15
15.54
C


ATOM
3419
CG2
VAL
B1178
−27.665
−43.704
−12.223
21.1
C


ATOM
3420
C
VAL
B1178
−29.339
−40.965
−10.181
17.51
C


ATOM
3421
O
VAL
B1178
−30.123
−40.409
−10.878
18.57
O


ATOM
3422
N
LYS
B1179
−29.475
−40.98
−8.856
17.04
N


ATOM
3423
CA
LYS
B1179
−30.533
−40.228
−8.217
16.95
C


ATOM
3424
CB
LYS
B1179
−30.434
−40.373
−6.733
17.15
C


ATOM
3425
CG
LYS
B1179
−31.75
−40.037
−6.122
20.25
C


ATOM
3426
CD
LYS
B1179
−31.633
−39.315
−4.835
21.96
C


ATOM
3427
CE
LYS
B1179
−32.453
−40.04
−3.77
20.85
C


ATOM
3428
NZ
LYS
B1179
−33.846
−39.761
−3.562
19.21
N


ATOM
3429
C
LYS
B1179
−30.573
−38.71
−8.511
16.1
C


ATOM
3430
O
LYS
B1179
−31.638
−38.131
−8.72
14.21
O


ATOM
3431
N
ASP
B1180
−29.418
−38.055
−8.42
16.12
N


ATOM
3432
CA
ASP
B1180
−29.33
−36.644
−8.707
16.31
C


ATOM
3433
CB
ASP
B1180
−27.843
−36.248
−8.692
19.77
C


ATOM
3434
CG
ASP
B1180
−27.216
−36.236
−7.291
22.65
C


ATOM
3435
OD1
ASP
B1180
−25.969
−36.124
−7.281
24.69
O


ATOM
3436
OD2
ASP
B1180
−27.935
−36.383
−6.262
27.87
O


ATOM
3437
C
ASP
B1180
−29.828
−36.325
−10.131
14.91
C


ATOM
3438
O
ASP
B1180
−30.496
−35.363
−10.344
13.63
O


ATOM
3439
N
LEU
B1181
−29.413
−37.128
−11.104
13.93
N


ATOM
3440
CA
LEU
B1181
−29.865
−36.965
−12.49
13.81
C


ATOM
3441
CB
LEU
B1181
−29.123
−37.972
−13.366
13.28
C


ATOM
3442
CG
LEU
B1181
−27.901
−37.653
−14.197
9.73
C


ATOM
3443
CD1
LEU
B1181
−27.341
−36.303
−14.092
9.56
C


ATOM
3444
CD2
LEU
B1181
−26.891
−38.75
−13.897
10.5
C


ATOM
3445
C
LEU
B1181
−31.377
−37.123
−12.681
13.36
C


ATOM
3446
O
LEU
B1181
−32.047
−36.419
−13.479
14.36
O


ATOM
3447
N
ILE
B1182
−31.922
−38.037
−11.915
13.26
N


ATOM
3448
CA
ILE
B1182
−33.364
−38.243
−11.922
14.38
C


ATOM
3449
CB
ILE
B1182
−33.811
−39.543
−11.232
14.16
C


ATOM
3450
CG2
ILE
B1182
−35.3
−39.644
−11.367
14.28
C


ATOM
3451
CG1
ILE
B1182
−33.124
−40.796
−11.852
16.35
C


ATOM
3452
CD1
ILE
B1182
−33.51
−42.162
−11.15
13.84
C


ATOM
3453
C
ILE
B1182
−34.013
−37.034
−11.248
12.99
C


ATOM
3454
O
ILE
B1182
−35.112
−36.592
−11.651
13.57
O


ATOM
3455
N
GLY
B1183
−33.296
−36.464
−10.297
11.14
N


ATOM
3456
CA
GLY
B1183
−33.788
−35.294
−9.552
11.95
C


ATOM
3457
C
GLY
B1183
−33.881
−34.082
−10.45
11.52
C


ATOM
3458
O
GLY
B1183
−34.842
−33.342
−10.372
12.52
O


ATOM
3459
N
PHE
B1184
−32.878
−33.895
−11.321
11.73
N


ATOM
3460
CA
PHE
B1184
−32.913
−32.822
−12.365
11.3
C


ATOM
3461
CB
PHE
B1184
−31.571
−32.746
−13.138
10.96
C


ATOM
3462
CG
PHE
B1184
−30.39
−32.459
−12.273
11.49
C


ATOM
3463
CD1
PHE
B1184
−30.525
−31.643
−11.109
13.87
C


ATOM
3464
CD2
PHE
B1184
−29.157
−32.957
−12.595
11.09
C


ATOM
3465
CE1
PHE
B1184
−29.436
−31.36
−10.293
9.36
C


ATOM
3466
CE2
PHE
B1184
−28.055
−32.649
−11.827
13.76
C


ATOM
3467
CZ
PHE
B1184
−28.201
−31.849
−10.646
13.97
C


ATOM
3468
C
PHE
B1184
−34.078
−33.017
−13.34
10.31
C


ATOM
3469
O
PHE
B1184
−34.762
−32.09
−13.67
9.73
O


ATOM
3470
N
GLY
B1185
−34.284
−34.259
−13.786
11.17
N


ATOM
3471
CA
GLY
B1185
−35.405
−34.585
−14.702
10.09
C


ATOM
3472
C
GLY
B1185
−36.727
−34.315
−14.063
9.24
C


ATOM
3473
O
GLY
B1185
−37.591
−33.763
−14.709
10.87
O


ATOM
3474
N
LEU
B1186
−36.874
−34.646
−12.779
8.52
N


ATOM
3475
CA
LEU
B1186
−38.075
−34.268
−11.99
7.28
C


ATOM
3476
CB
LEU
B1186
−38.072
−34.915
−10.56
6.85
C


ATOM
3477
CG
LEU
B1186
−39.207
−34.583
−9.582
5.42
C


ATOM
3478
CD1
LEU
B1186
−40.59
−34.846
−10.16
2
C


ATOM
3479
CD2
LEU
B1186
−38.918
−35.353
−8.286
3.95
C


ATOM
3480
C
LEU
B1186
−38.308
−32.767
−11.899
8.57
C


ATOM
3481
O
LEU
B1186
−39.442
−32.313
−12.096
12.45
O


ATOM
3482
N
GLN
B1187
−37.292
−31.971
−11.621
8.71
N


ATOM
3483
CA
GLN
B1187
−37.472
−30.518
−11.66
10.1
C


ATOM
3484
CB
GLN
B1187
−36.18
−29.843
−11.25
11.08
C


ATOM
3485
CG
GLN
B1187
−35.743
−30.165
−9.871
11.17
C


ATOM
3486
CD
GLN
B1187
−34.601
−29.239
−9.455
13.84
C


ATOM
3487
OE1
GLN
B1187
−34.721
−28.008
−9.538
14.08
O


ATOM
3488
NE2
GLN
B1187
−33.476
−29.829
−9.045
15.84
N


ATOM
3489
C
GLN
B1187
−37.887
−29.991
−13.027
9.54
C


ATOM
3490
O
GLN
B1187
−38.666
−29.035
−13.151
11.12
O


ATOM
3491
N
VAL
B1188
−37.347
−30.555
−14.079
7.7
N


ATOM
3492
CA
VAL
B1188
−37.784
−30.081
−15.428
7.36
C


ATOM
3493
CB
VAL
B1188
−36.91
−30.734
−16.527
6.86
C


ATOM
3494
CG1
VAL
B1188
−37.338
−30.385
−17.939
3.33
C


ATOM
3495
CG2
VAL
B1188
−35.458
−30.404
−16.278
2
C


ATOM
3496
C
VAL
B1188
−39.245
−30.414
−15.687
8.4
C


ATOM
3497
O
VAL
B1188
−39.952
−29.679
−16.346
9.43
O


ATOM
3498
N
ALA
B1189
−39.704
−31.547
−15.173
9.65
N


ATOM
3499
CA
ALA
B1189
−41.041
−31.997
−15.446
9.84
C


ATOM
3500
CB
ALA
B1189
−41.181
−33.479
−15.04
9.75
C


ATOM
3501
C
ALA
B1189
−41.986
−31.113
−14.676
10.41
C


ATOM
3502
O
ALA
B1189
−43.117
−30.837
−15.14
11.55
O


ATOM
3503
N
LYS
B1190
−41.51
−30.588
−13.543
10.99
N


ATOM
3504
CA
LYS
B1190
−42.341
−29.679
−12.721
12.28
C


ATOM
3505
CB
LYS
B1190
−41.775
−29.502
−11.359
12.77
C


ATOM
3506
CG
LYS
B1190
−41.7
−30.717
−10.574
12.61
C


ATOM
3507
CD
LYS
B1190
−41.08
−30.362
−9.251
15.08
C


ATOM
3508
CE
LYS
B1190
−41.464
−31.401
−8.288
19.04
C


ATOM
3509
NZ
LYS
B1190
−40.942
−30.924
−6.946
25.19
N


ATOM
3510
C
LYS
B1190
−42.506
−28.293
−13.3
11.94
C


ATOM
3511
O
LYS
B1190
−43.611
−27.659
−13.176
14.36
O


ATOM
3512
N
GLY
B1191
−41.439 
−27.806
−13.918 
10.85
N


ATOM
3513
CA
GLY
B1191
−41.463
−26.55
−14.72
8.71
C


ATOM
3514
C
GLY
B1191
−42.34
−26.777
−15.935
8
C


ATOM
3515
O
GLY
B1191
−43.19
−25.951
−16.236
8.54
O


ATOM
3516
N
MET
B1192
−42.205
−27.936
−16.602
7.97
N


ATOM
3517
CA
MET
B1192
−42.971
−28.222
−17.854
8.25
C


ATOM
3518
CB
MET
B1192
−42.501
−29.543
−18.507
8.8
C


ATOM
3519
CG
MET
B1192
−41.361
−29.451
−19.436
11.12
C


ATOM
3520
SD
MET
B1192
−41.314
−27.838
−20.283
18
S


ATOM
3521
CE
MET
B1192
−42.181
−27.995
−21.823
11.46
C


ATOM
3522
C
MET
B1192
−44.437
−28.371
−17.563
7.29
C


ATOM
3523
O
MET
B1192
−45.335
−27.941
−18.337 
7.17
O


ATOM
3524
N
LYS
B1193
−44.691
−29.027
−16.451
7.48
N


ATOM
3525
CA
LYS
B1193
−46.097
−29.193
−15.988
9.21
C


ATOM
3526
CB
LYS
B1193
−46.127
−30.004
−14.713
7.62
C


ATOM
3527
CG
LYS
B1193
−47.429
−30.099
−14.098
7.45
C


ATOM
3528
CD
LYS
B1193
−47.198
−30.498
−12.681
10.42
C


ATOM
3529
CE
LYS
B1193
−48.442
−30.778
−12.021
14.83
C


ATOM
3530
NZ
LYS
B1193
−48.088
−30.966
−10.58
22.35
N


ATOM
3531
C
LYS
B1193
−46.75
−27.808
−15.773
8.79
C


ATOM
3532
O
LYS
B1193
−47.911
−27.589
−16.18
9.23
O


ATOM
3533
N
TYR
B1194
−45.974
−26.879
−15.186
9.48
N


ATOM
3534
CA
TYR
B1194
−46.435
−25.503
−15.04
10.02
C


ATOM
3535
CB
TYR
B1194
−45.485
−24.704
−14.143
10.13
C


ATOM
3536
CG
TYR
B1194
−45.798
−23.213
−14.084
9.08
C


ATOM
3537
CD1
TYR
B1194
−46.675
−22.706
−13.116
7.43
C


ATOM
3538
CE1
TYR
B1194
−46.958
−21.357
−13.076
9.59
C


ATOM
3539
CD2
TYR
B1194
−45.186
−22.323
−14.971
5.88
C


ATOM
3540
CE2
TYR
B1194
−45.424
−20.998
−14.942
7.13
C


ATOM
3541
CZ
TYR
B1194
−46.329
−20.48
−14.019
12.26
C


ATOM
3542
OH
TYR
B1194
−46.625
−19.107
−14.038
11.64
O


ATOM
3543
C
TYR
B1194
−46.645
−24.811
−16.41
10.44
C


ATOM
3544
O
TYR
B1194
−47.777
−24.356
−16.745
11.5
O


ATOM
3545
N
LEU
B1195
−45.606
−24.771
−17.235
9.91
N


ATOM
3546
CA
LEU
B1195
−45.724
−24.136
−18.545
10.18
C


ATOM
3547
CB
LEU
B1195
−44.469
−24.386
−19.357
11.31
C


ATOM
3548
CG
LEU
B1195
−43.235
−23.478
−19.274
8.14
C


ATOM
3549
CD1
LEU
B1195
−43.559
−22.302
−18.412
11.05
C


ATOM
3550
CD2
LEU
B1195
−42.091
−24.231
−18.759
11.77
C


ATOM
3551
C
LEU
B1195
−46.878
−24.77
−19.256
12.15
C


ATOM
3552
O
LEU
B1195
−47.733
−24.094
−19.829
12.53
O


ATOM
3553
N
ALA
B1196
−46.971 
−26.096
−19.173
12.77
N


ATOM
3554
CA
ALA
B1196
−48.058
−26.765
−19.89
13.11
C


ATOM
3555
CB
ALA
B1196
−47.874
−28.244
−19.778
14.13
C


ATOM
3556
C
ALA
B1196
−49.452
−26.395
−19.441
13.63
C


ATOM
3557
O
ALA
B1196
−50.383
−26.608
−20.204
15.78
O


ATOM
3558
N
SER
B1197
−49.639
−25.911
−18.196
14.48
N


ATOM
3559
CA
SER
B1197
−50.99
−25.572
−17.664
12.95
C


ATOM
3560
CB
SER
B1197
−51.017
−25.758
−16.192
12.98
C


ATOM
3561
OG
SER
B1197
−50.055
−24.902
−15.565
17.5
O


ATOM
3562
C
SER
B1197
−51.308
−24.121
−18.035
12.58
C


ATOM
3563
O
SER
B1197
−52.442
−23.652
−17.985
12.68
O


ATOM
3564
N
LYS
B1198
−50.286
−23.398
−18.441
13.13
N


ATOM
3565
CA
LYS
B1198
−50.489
−22.056
−18.999
13.05
C


ATOM
3566
CB
LYS
B1198
−49.29
−21.187
−18.707
12.52
C


ATOM
3567
CG
LYS
B1198
−48.959
−21.126
−17.249
12.04
C


ATOM
3568
CD
LYS
B1198
−50.273 
−20.967
−16.457
13.08
C


ATOM
3569
CE
LYS
B1198
−49.936
−21.012
−14.985
17.36
C


ATOM
3570
NZ
LYS
B1198
−51.129
−20.589
−14.245
21.98
N


ATOM
3571
C
LYS
B1198
−50.649
−22.161
−20.484
13.41
C


ATOM
3572
O
LYS
B1198
−50.651
−21.132
−21.155
13.33
O


ATOM
3573
N
LYS
B1199
−50.755
−23.418
−20.98
13.76
N


ATOM
3574
CA
LYS
B1199
−50.809
−23.725
−22.414
14.88
C


ATOM
3575
CB
LYS
B1199
−52.085
−23.141
−23.005
14.84
C


ATOM
3576
CG
LYS
B1199
−53.317
−23.86
−22.454
21.78
C


ATOM
3577
CD
LYS
B1199
−54.523
−22.873
−22.192
33.81
C


ATOM
3578
CE
LYS
B1199
−55.034
−22.06
−23.489
35.48
C


ATOM
3579
NZ
LYS
B1199
−55.173
−22.933
−24.757
39.92
N


ATOM
3580
C
LYS
B1199
−49.553
−23.275
−23.214
14.93
C


ATOM
3581
O
LYS
B1199
−49.62
−22.835
−24.357
14.95
O


ATOM
3582
N
PHE
B1200
−48.393
−23.358
−22.585
14.67
N


ATOM
3583
CA
PHE
B1200
−47.225
−22.929
−23.253
14.24
C


ATOM
3584
CB
PHE
B1200
−46.337
−22.153
−22.308
12.15
C


ATOM
3585
CG
PHE
B1200
−45.039
−21.734
−22.94
11.68
C


ATOM
3586
CD1
PHE
B1200
−43.852
−22.502
−22.753
12.56
C


ATOM
3587
CD2
PHE
B1200
−44.986
−20.629
−23.723
7.4
C


ATOM
3588
CE1
PHE
B1200
−42.662
−22.101
−23.342
11.48 
C


ATOM
3589
CE2
PHE
B1200
−43.803
−20.209
−24.297
10.2
C


ATOM
3590
CZ
PHE
B1200
−42.657
−20.938
−24.138
10.48
C


ATOM
3591
C
PHE
B1200
−46.522
−24.127
−23.913
14.52 
C


ATOM
3592
O
PHE
B1200
−46.239
−25.117
−23.274
14.04
O


ATOM
3593
N
VAL
B1201
−46.278
−24.026
−25.212
15.61
N


ATOM
3594
CA
VAL
B1201
−45.552
−25.077
−25.937
16.14
C


ATOM
3595
CB
VAL
B1201
−46.223
−25.368
−27.276
16.14
C


ATOM
3596
CG1
VAL
B1201
−45.37
−26.28
−28.169
14.77 C



ATOM
3597
CG2
VAL
B1201
−47.68
−25.93
−27.046
16.33
C


ATOM
3598
C
VAL
B1201
−44.093
−24.6
−26.108
16.79
C


ATOM
3599
O
VAL
B1201
−43.794
−23.635
−26.791
17.87
O


ATOM
3600
N
HIS
B1202
−43.185
−25.274
−25.451
15.99
N


ATOM
3601
CA
HIS
B1202
−41.85
−24.848
−25.49
17.06
C


ATOM
3602
CB
HIS
B1202
−41.108
−25.639
−24.44
16.49
C


ATOM
3603
CG
HIS
B1202
−39.733
−25.142
−24.188
15.87
C


ATOM
3604
CD2
HIS
B1202
−39.216
−24.479
−23.131
13.61
C


ATOM
3605
ND1
HIS
B1202
−38.697
−25.338
−25.084
16.33
N


ATOM
3606
CE1
HIS
B1202
−37.596
−24.822
−24.575
15.98
C


ATOM
3607
NE2
HIS
B1202
−37.887
−24.287
−23.392
16.78
N


ATOM
3608
C
HIS
B1202
−41.223
−25.044
−26.903
18.23
C


ATOM
3609
O
HIS
B1202
−40.688
−24.086
−27.441
18.63
O


ATOM
3610
N
ARG
B1203
−41.276
−26.276
−27.479
19.01
N


ATOM
3611
CA
ARG
B1203
−40.731
−26.604
−28.854
18.59
C


ATOM
3612
CB
ARG
B1203
−41.156
−25.584
−29.948
17.85
C


ATOM
3613
CG
ARG
B1203
−42.573
−25.201
−29.778
22.3
C


ATOM
3614
CD
ARG
B1203
−42.853
−23.874
−30.255
27.82
C


ATOM
3615
NE
ARG
B1203
−42.669
−23.825
−31.688
36.07
N


ATOM
3616
CZ
ARG
B1203
−43.656
−23.621
−32.572
35.92
C


ATOM
3617
NH1
ARG
B1203
−44.903
−23.457
−32.111
34.73
N


ATOM
3618
NH2
ARG
B1203
−43.375
−23.574
−33.901
31.08
N


ATOM
3619
C
ARG
B1203
−39.217
−26.786
−28.933
17.32
C


ATOM
3620
O
ARG
B1203
−38.669
−26.981
−30.009
16.84
O


ATOM
3621
N
ASP
B1204
−38.537
−26.693
−27.819
16.22
N


ATOM
3622
CA
ASP
B1204
−37.087
−26.9
−27.88
15.93
C


ATOM
3623
CB
ASP
B1204
−36.399
−25.605
−28.307
14.57
C


ATOM
3624
CG
ASP
B1204
−34.994
−25.832
−28.815
19.07
C


ATOM
3625
OD1
ASP
B1204
−34.264
−24.803
−28.903
18.92
O


ATOM
3626
OD2
ASP
B1204
−34.581
−27.029
−29.074
21.21
O


ATOM
3627
C
ASP
B1204
−36.575
−27.412
−26.517
14.81
C


ATOM
3628
O
ASP
B1204
−35.502
−27.041
−26.05
15.16
O


ATOM
3629
N
LEU
B1205
−37.383
−28.239
−25.875
13.6
N


ATOM
3630
CA
LEU
B1205
−37.041
−28.817
−24.611
13.38
C


ATOM
3631
CB
LEU
B1205
−38.261
−29.547
−24.046
11.84
C


ATOM
3632
CG
LEU
B1205
−38.072
−30.052
−22.634
10.06
C


ATOM
3633
CD1
LEU
B1205
−37.692
−28.865
−21.634
7.06
C


ATOM
3634
CD2
LEU
B1205
−39.28
−30.784
−22.242
7.43
C


ATOM
3635
C
LEU
B1205
−35.89
−29.815
−24.833
14.11
C


ATOM
3636
O
LEU
B1205
−36.033
−30.718
−25.665
15.58
O


ATOM
3637
N
ALA
B1206
−34.783
−29.619
−24.1
11.95
N


ATOM
3638
CA
ALA
B1206
−33.535
−30.33
−24.23
10.68
C


ATOM
3639
CB
ALA
B1206
−32.831
−30.034
−25.596
12.55
C


ATOM
3640
C
ALA
B1206
−32.67
−29.834
−23.122
8.83
C


ATOM
3641
O
ALA
B1206
−32.888
−28.723
−22.579
8.67
O


ATOM
3642
N
ALA
B1207
−31.68
−30.636
−22.748
7.74
N


ATOM
3643
CA
ALA
B1207
−30.893
−30.32
−21.534
6.84
C


ATOM
3644
CB
ALA
B1207
−29.986
−31.448
−21.186
7.04
C


ATOM
3645
C
ALA
B1207
−30.145
−29.037
−21.756
6.97
C


ATOM
3646
O
ALA
B1207
−29.853
−28.316
−20.814
7.07
O


ATOM
3647
N
ARG
B1208
−29.857
−28.723
−23.021
8.48
N


ATOM
3648
CA
ARG
B1208
−29.105
−27.484
−23.376
10.48
C


ATOM
3649
CB
ARG
B1208
−28.612
−27.459
−24.831
10.31
C


ATOM
3650
CG
ARG
B1208
−29.687
−27.862
−25.863
11.12
C


ATOM
3651
CD
ARG
B1208
−29.252
−27.63
−27.365
8.82
C


ATOM
3652
NE
ARG
B1208
−30.465
−27.73
−28.2
13.09
N


ATOM
3653
CZ
ARG
B1208
−31.072
−28.876
−28.53
11.69
C


ATOM
3654
NH1
ARG
B1208
−30.58
−30.006
−28.144
16.97
N


ATOM
3655
NH2
ARG
B1208
−32.179
−28.902
−29.258
16.72
N


ATOM
3656
C
ARG
B1208
−29.912
−26.26
−23.043
11.65
C


ATOM
3657
O
ARG
B1208
−29.374
−25.15
−22.889
12.53
O


ATOM
3658
N
ASN
B1209
−31.213
−26.477
−22.842
13.13
N


ATOM
3659
CA
ASN
B1209
−32.14
−25.374
−22.622
12.9
C


ATOM
3660
CB
ASN
B1209
−33.281
−25.547
−23.589
12.61
C


ATOM
3661
CG
ASN
B1209
−32.907
−25.053
−24.946
14.64
C


ATOM
3662
OD1
ASN
B1209
−32.141
−24.081
−25.051
14.89
O


ATOM
3663
ND2
ASN
B1209
−33.363
−25.722
−25.976
14.02
N


ATOM
3664
C
ASN
B1209
−32.641
−25.213
−21.198
13.91
C


ATOM
3665
O
ASN
B1209
−33.525
−24.39
−20.955
16.03
O


ATOM
3666
N
CYS
B1210
−32.125
−26.041
−20.284
13.09
N


ATOM
3667
CA
CYS
B1210
−32.375
−25.967
−18.881
11.8
C


ATOM
3668
CB
CYS
B1210
−32.63
−27.335
−18.338
12.69
C


ATOM
3669
SG
CYS
B1210
−34.022
−28.189
−19.054
17.53
S


ATOM
3670
C
CYS
B1210
−31.137
−25.492
−18.22
11.23
C


ATOM
3671
O
CYS
B1210
−30.016
−26.019
−18.489
11.67
O


ATOM
3672
N
MET
B1211
−31.34
−24.527
−17.333
10.14
N


ATOM
3673
CA
MET
B1211
−30.242
−23.886
−16.565
10.47
C


ATOM
3674
CB
MET
B1211
−30.323
−22.352
−16.588
9.5
C


ATOM
3675
CG
MET
B1211
−30.138
−21.749
−18.03
11.4
C


ATOM
3676
SD
MET
B1211
−28.622 
−22.258
−18.911
15.66
S


ATOM
3677
CE
MET
B1211
−29.284
−22.438
−20.557
15.6
C


ATOM
3678
C
MET
B1211
−30.211
−24.387
−15.127
11.73
C


ATOM
3679
O
MET
B1211
−31.275
−24.724
−14.552
12.17
O


ATOM
3680
N
LEU
B1212
−29
−24.496
−14.577
12.21
N


ATOM
3681
CA
LEU
B1212
−28.819
−24.898
−13.23
13.72
C


ATOM
3682
CB
LEU
B1212
−27.911
−26.104
−13.209
15.2
C


ATOM
3683
CG
LEU
B1212
−28.199
−27.458
−12.58
14.9
C


ATOM
3684
CD1
LEU
B1212
−26.877
−27.911
−12.068
19.56
C


ATOM
3685
CD2
LEU
B1212
−29.154
−27.446
−11.458
18.72
C


ATOM
3686
C
LEU
B1212
−28.209
−23.774
−12.394
15.72
C


ATOM
3687
O
LEU
B1212
−27.178
−23.229
−12.73
14.42
O


ATOM
3688
N
ASP
B1213
−28.835
−23.439
−11.272
17.77
N


ATOM
3689
CA
ASP
B1213
−28.276
−22.395
−10.489
19.65
C


ATOM
3690
CB
ASP
B1213
−29.353
−21.455
−9.98
21.08
C


ATOM
3691
CG
ASP
B1213
−30.28
−22.092
−8.886
26.99
C


ATOM
3692
OD1
ASP
B1213
−29.903
−23.095
−8.188
30.93
O


ATOM
3693
OD2
ASP
B1213
−31.406
−21.543
−8.717
30.83
O


ATOM
3694
C
ASP
B1213
−27.46
−22.962
−9.377
20.76
C


ATOM
3695
O
ASP
B1213
−27.306
−24.167
−9.271
20.15
O


ATOM
3696
N
GLU
B1214
−26.976
−22.073
−8.511
23.75
N


ATOM
3697
CA
GLU
B1214
−25.965
−22.404
−7.491
25.83
C


ATOM
3698
CB
GLU
B1214
−25.358
−21.152
−6.856
25.58
C


ATOM
3699
CG
GLU
B1214
−25.832
−20.942
−5.458
33.06
C


ATOM
3700
CD
GLU
B1214
−26.949
−19.858
−5.364
42.46
C


ATOM
3701
OE1
GLU
B1214
−27.904
−19.886
−6.208
40.39
O


ATOM
3702
OE2
GLU
B1214
−26.834
−18.969
−4.437
46.68
O


ATOM
3703
C
GLU
B1214
−26.478
−23.378
−6.427
25.29
C


ATOM
3704
O
GLU
B1214
−25.668
−24.107
−5.833
26.69
O


ATOM
3705
N
LYS
B1215
−27.791
−23.455
−6.219
24.02
N


ATOM
3706
CA
LYS
B1215
−28.295
−24.503
−5.337
23.76
C


ATOM
3707
CB
LYS
B1215
−29.237
−23.983
−4.278
24.17
C


ATOM
3708
CG
LYS
B1215
−30.271
−23.059
−4.778
28.88
C


ATOM
3709
CD
LYS
B1215
−29.893
−21.669
−4.214
37.25
C


ATOM
3710
CE
LYS
B1215
−29.192
−21.827
−2.79
40.05
C


ATOM
3711
NZ
LYS
B1215
−30.165
−22.103
−1.649
40.23
N


ATOM
3712
C
LYS
B1215
−28.935
−25.684
−6.053
22.81
C


ATOM
3713
O
LYS
B1215
−29.587
−26.555
−5.397
21.67
O


ATOM
3714
N
PHE
B1216
−28.742
−25.725
−7.378
19.98
N


ATOM
3715
CA
PHE
B1216
−29.093
−26.908
−8.121
19.25
C


ATOM
3716
CB
PHE
B1216
−28.596
−28.213
−7.422
18.9
C


ATOM
3717
CG
PHE
B1216
−27.111
−28.264
−7.317
17.96
C


ATOM
3718
CD1
PHE
B1216
−26.472
−27.984
−6.089
22.08
C


ATOM
3719
CD2
PHE
B1216
−26.341
−28.452
−8.451
15.15
C


ATOM
3720
CE1
PHE
B1216
−25.082
−27.968
−5.993
22.25
C


ATOM
3721
CE2
PHE
B1216
−24.969
−28.436
−8.389
16.63
C


ATOM
3722
CZ
PHE
B1216
−24.317
−28.182
−7.178
20.9
C


ATOM
3723
C
PHE
B1216
−30.579
−26.93
−8.405
18.18
C


ATOM
3724
O
PHE
B1216
−31.197
−28.017
−8.558
17.35
O


ATOM
3725
N
THR
B1217
−31.133 
−25.72
−8.503
16.24
N


ATOM
3726
CA
THR
B1217
−32.471
−25.614
−9.048
15.6
C


ATOM
3727
CB
THR
B1217
−33.189
−24.352
−8.566
15.47
C


ATOM
3728
OG1
THR
B1217
−33.024
−24.2
−7.158
18.4
O


ATOM
3729
CG2
THR
B1217
−34.651
−24.371
−8.888
13.83
C


ATOM
3730
C
THR
B1217
−32.262
−25.557
−10.554
14.84
C


ATOM
3731
O
THR
B1217
−31.423
−24.774
−11.038
14.57
O


ATOM
3732
N
VAL
B1218
−33.01
−26.395
−11.268
14.15
N


ATOM
3733
CA
VAL
B1218
−33.018
−26.406
−12.706
12.77
C


ATOM
3734
CB
VAL
B1218
−33.159
−27.874
−13.298
13.49
C


ATOM
3735
CG1
VAL
B1218
−33.104
−27.847
−14.83
9.57
C


ATOM
3736
CG2
VAL
B1218
−32.179
−28.925
−12.674
7.77
C


ATOM
3737
C
VAL
B1218
−34.221
−25.557
−13.152
13.52
C


ATOM
3738
O
VAL
B1218
−35.325
−25.715
−12.656
13.44
O


ATOM
3739
N
LYS
B1219
−34.008
−24.668
−14.112
13.6
N


ATOM
3740
CA
LYS
B1219
−35.076
−23.906
−14.656
13.99
C


ATOM
3741
CB
LYS
B1219
−34.912
−22.43
−14.337
13.77
C


ATOM
3742
CG
LYS
B1219
−34.736
−22.145
−12.842
15.83
C


ATOM
3743
CD
LYS
B1219
−34.667
−20.645
−12.534
17.05
C


ATOM
3744
CE
LYS
B1219
−34.331
−20.44
−11.093
19.12
C


ATOM
3745
NZ
LYS
B1219
−35.386
−20.985
−10.223
12.71
N


ATOM
3746
C
LYS
B1219
−35.093
−24.089
−16.135
13.43
C


ATOM
3747
O
LYS
B1219
−34.081
−23.949
−16.788
14.83
O


ATOM
3748
N
VAL
B1220
−36.266
−24.392
−16.652
13.41
N


ATOM
3749
CA
VAL
B1220
−36.505
−24.466
−18.075
14.22
C


ATOM
3750
CB
VAL
B1220
−37.875
−25.175
−18.41
13.64
C


ATOM
3751
CG1
VAL
B1220
−38.048
−25.272
−19.877
8.54
C


ATOM
3752
CG2
VAL
B1220
−37.865
−26.569
−17.79
14.53
C


ATOM
3753
C
VAL
B1220
−36.449
−23.09
−18.686
14.19
C


ATOM
3754
O
VAL
B1220
−37.167
−22.162
−18.266
14.96
O


ATOM
3755
N
ALA
B1221
−35.561
−22.963
−19.636
13.87
N


ATOM
3756
CA
ALA
B1221
−35.328
−21.717
−20.301
15.19
C


ATOM
3757
CB
ALA
B1221
−33.785
−21.418
−20.29
15.26
C


ATOM
3758
C
ALA
B1221
−35.897
−21.712
−21.722
16.2
C


ATOM
3759
O
ALA
B1221
−35.991
−22.79
−22.392
17.52
O


ATOM
3760
O
ASP
B1222
−36.185
−18.2
−23.979
22.75
O


ATOM
3761
N
ASP
B1222
−36.322
−20.808
−22.202
20



ATOM
3762
CA
ASP
B1222
−36.839
−20.404
−23.504
20



ATOM
3763
C
ASP
B1222
−35.94
−19.354
−24.15
20



ATOM
3764
CB
ASP
B1222
−38.265
−19.865
−23.371
20



ATOM
3765
CG
ASP
B1222
−38.851
−19.436
−24.701
20



ATOM
3766
OD1
ASP
B1222
−38.859
−20.258
−25.641
20



ATOM
3767
OD2
ASP
B1222
−39.327
−18.297
−24.9
20



ATOM
3768
N
PHE
B1223
−34.78
−19.366
−24.725
23.53
N


ATOM
3769
CA
PHE
B1223
−33.976
−18.324
−25.306
24.64
C


ATOM
3770
CB
PHE
B1223
−32.475
−18.638
−25.161
24.08
C


ATOM
3771
CG
PHE
B1223
−31.998
−18.609
−23.729
21.07
C


ATOM
3772
CD1
PHE
B1223
−31.895
−17.386
−23.043
18.95
C


ATOM
3773
CD2
PHE
B1223
−31.693
−19.817
−23.064
21.87
C


ATOM
3774
CE1
PHE
B1223
−31.484
−17.347
−21.715
19.02
C


ATOM
3775
CE2
PHE
B1223
−31.278
−19.813
−21.75
22.36
C


ATOM
3776
CZ
PHE
B1223
−31.168
−18.553
−21.058
20.58
C


ATOM
3777
C
PHE
B1223
−34.433
−18.023
−26.752
25.93
C


ATOM
3778
O
PHE
B1223
−35.098
−17.003
−26.979
28.12
O


ATOM
3779
N
GLY
B1224
−34.139
−18.899
−27.696
26.17
N


ATOM
3780
CA
GLY
B1224
−34.669
−18.762
−29.081
26.43
C


ATOM
3781
C
GLY
B1224
−34.263
−17.432
−29.737
25.34
C


ATOM
3782
O
GLY
B1224
−33.489
−17.382
−30.665
26.25
O


ATOM
3783
N
LEU
B1225
−34.786
−16.339
−29.259
24.71
N


ATOM
3784
CA
LEU
B1225
−34.479
−15.087
−29.874
24.72
C


ATOM
3785
CB
LEU
B1225
−35.596
−14.08
−29.58
26.46
C


ATOM
3786
CG
LEU
B1225
−35.598
−12.769
−30.422
27.12
C


ATOM
3787
CD1
LEU
B1225
−35.356
−12.934
−31.951
23.65
C


ATOM
3788
CD2
LEU
B1225
−36.986
−12.146
−30.112
29.78
C


ATOM
3789
C
LEU
B1225
−33.148
−14.542
−29.381
22.87
C


ATOM
3790
O
LEU
B1225
−32.485
−13.767
−30.09
22.83
O


ATOM
3791
N
ALA
B1226
−32.77 
−14.953
−28.178
20.34
N


ATOM
3792
CA
ALA
B1226
−31.498
−14.569
−27.602
19.02
C


ATOM
3793
CB
ALA
B1226
−31.531
−14.727
−26.109
17.46
C


ATOM
3794
C
ALA
B1226
−30.378
−15.378
−28.218
19.07
C


ATOM
3795
O
ALA
B1226
−29.225
−15.02
−28.061
20.39
O


ATOM
3796
N
ARG
B1227
−30.703
−16.45
−28.964
18.81
N


ATOM
3797
CA
ARG
B1227
−29.694
−17.22
−29.655
18.06
C


ATOM
3798
CB
ARG
B1227
−30.088
−18.681
−29.784
18.31
C


ATOM
3799
CG
ARG
B1227
−29.835
−19.543
−28.561
17.06
C


ATOM
3800
CD
ARG
B1227
−30.517
−20.942
−28.639
18.88
C


ATOM
3801
NE
ARG
B1227
−30.674
−21.617
−27.318
20.95
N


ATOM
3802
CZ
ARG
B1227
−29.662
−22.079
−26.576
19.76
C


ATOM
3803
NH1
ARG
B1227
−28.432
−21.986
−27.052
18.11
N


ATOM
3804
NH2
ARG
B1227
−29.864
−22.635
−25.366
17.86
N


ATOM
3805
C
ARG
B1227
−29.386
−16.612
−31.009
18.92
C


ATOM
3806
O
ARG
B1227
−30.151
−16.787
−31.98
20.81
O


ATOM
3807
N
ASP
B1228
−28.265
−15.897
−31.089
18.42
N


ATOM
3808
CA
ASP
B1228
−27.778
−15.365
−32.373
19.28
C


ATOM
3809
CB
ASP
B1228
−26.42
−14.667
−32.241
19.39
C


ATOM
3810
CG
ASP
B1228
−26.49
−13.339
−31.488
19.96
C


ATOM
3811
OD1
ASP
B1228
−27.59
−12.824
−31.102
21.82
O


ATOM
3812
OD2
ASP
B1228
−25.385
−12.84
−31.234
19.46
O


ATOM
3813
C
ASP
B1228
−27.707
−16.324
−33.54
19.83
C


ATOM
3814
O
ASP
B1228
−28.274
−16.027
−34.579
19.82
O


ATOM
3815
N
MET
B1229
−26.956
−17.419
−33.38
22.04
N


ATOM
3816
CA
MET
B1229
−27.017
−18.611
−34.222
24.36
C


ATOM
3817
CB
MET
B1229
−25.71
−18.746
−34.988
23.85
C


ATOM
3818
CG
MET
B1229
−25.502
−17.629
−35.865
25.1
C


ATOM
3819
SD
MET
B1229
−23.917
−17.588
−36.672
29.2
S


ATOM
3820
CE
MET
B1229
−22.717
−18.577
−35.636
32.72
C


ATOM
3821
C
MET
B1229
−27.217
−19.932
−33.479
25.51
C


ATOM
3822
O
MET
B1229
−27.127
−19.978
−32.257
24
O


ATOM
3823
N
TYR
B1230
−27.46 
−21.001
−34.261
29.08
N


ATOM
3824
CA
TYR
B1230
−27.471
−22.413
−33.826
34.08
C


ATOM
3825
CB
TYR
B1230
−28.893
−22.891
−33.966
34.58
C


ATOM
3826
CG
TYR
B1230
−29.933
−21.946
−33.4
35.75
C


ATOM
3827
CD1
TYR
B1230
−30.167
−20.688
−33.993
40.7
C


ATOM
3828
CE1
TYR
B1230
−31.112
−19.783
−33.488
37.49
C


ATOM
3829
CD2
TYR
B1230
−30.716
−22.305
−32.318
35.53
C


ATOM
3830
CE2
TYR
B1230
−31.691
−21.421
−31.826
36.77
C


ATOM
3831
CZ
TYR
B1230
−31.857
−20.169
−32.419
37.26
C


ATOM
3832
OH
TYR
B1230
−32.784
−19.289
−31.938
39.37
O


ATOM
3833
C
TYR
B1230
−26.584
−23.265
−34.755
35.95
C


ATOM
3834
O
TYR
B1230
−26.276
−22.825
−35.864
36.53
O


ATOM
3835
N
ASP
B1231
−26.162
−24.491
−34.382
39.69
N


ATOM
3836
CA
ASP
B1231
−25.538
−25.425
−35.463
41.03
C


ATOM
3837
CB
ASP
B1231
−23.995
−25.454
−35.35
42.61
C


ATOM
3838
CG
ASP
B1231
−23.553
−26.179
−34.024
46.08
C


ATOM
3839
OD1
ASP
B1231
−22.866
−27.237
−34.085
44.26
O


ATOM
3840
OD2
ASP
B1231
−23.991
−25.72
−32.92
48.62
O


ATOM
3841
C
ASP
B1231
−25.93
−26.803
−35.112
40.95
C


ATOM
3842
O
ASP
B1231
−26.455
−26.898
−34.011
41.5
O


ATOM
3843
N
LYS
B1232
−25.638
−27.845
−35.959
41.51
N


ATOM
3844
CA
LYS
B1232
−25.472
−29.295
−35.504
40.13
C


ATOM
3845
CB
LYS
B1232
−24.085
−29.456
−34.835
41.34
C


ATOM
3846
CG
LYS
B1232
−23.694
−30.825
−34.164
42.89
C


ATOM
3847
CD
LYS
B1232
−23.774
−30.788
−32.596
50.15
C


ATOM
3848
CE
LYS
B1232
−22.592
−30.036
−31.827
55.04
C


ATOM
3849
NZ
LYS
B1232
−21.62
−30.864
−30.923
57.08
N


ATOM
3850
C
LYS
B1232
−26.567
−29.995
−34.603
39.71
C


ATOM
3851
O
LYS
B1232
−26.902
−31.182
−34.778
41.39
O


ATOM
3852
N
GLU
B1233
−27.076
−29.309
−33.594
36.6
N


ATOM
3853
CA
GLU
B1233
−28.291
−29.742
−32.95
34.58
C


ATOM
3854
CB
GLU
B1233
−28.459
−29.068
−31.552
33.63
C


ATOM
3855
CG
GLU
B1233
−27.201
−28.787
−30.789
34.52
C


ATOM
3856
CD
GLU
B1233
−26.607
−30.075
−30.268
39.4
C


ATOM
3857
OE1
GLU
B1233
−27.175
−31.113
−30.673
34.26
O


ATOM
3858
OE2
GLU
B1233
−25.58
−30.058
−29.494
41.29
O


ATOM
3859
C
GLU
B1233
−29.512
−29.434
−33.859
32.39
C


ATOM
3860
O
GLU
B1233
−30.54
−30.097
−33.805
31.63
O


ATOM
3861
N
TYR
B1234
−29.388
−28.4
−34.664
31.28
N


ATOM
3862
CA
TYR
B1234
−30.539
−27.798
−35.324
30.52
C


ATOM
3863
CB
TYR
B1234
−30.68
−26.355
−34.903
28.19
C


ATOM
3864
CG
TYR
B1234
−31.041
−26.123
−33.508
25.71
C


ATOM
3865
CD1
TYR
B1234
−30.067
−26.048
−32.545
23.54
C


ATOM
3866
CE1
TYR
B1234
−30.372
−25.814
−31.211
26.06
C


ATOM
3867
CD2
TYR
B1234
−32.361
−25.907
−33.142
25.16
C


ATOM
3868
CE2
TYR
B1234
−32.692
−25.663
−31.797
27.03
C


ATOM
3869
CZ
TYR
B1234
−31.676
−25.639
−30.829
27.04
C


ATOM
3870
OH
TYR
B1234
−31.945
−25.398
−29.498
27
O


ATOM
3871
C
TYR
B1234
−30.413
−27.788
−36.846
32.17
C


ATOM
3872
O
TYR
B1234
−29.369
−27.478
−37.391
31.62
O


ATOM
3873
N
TYR
B1235
−31.509
−28.08
−37.519
33.9
N


ATOM
3874
CA
TYR
B1235
−31.561
−28.031
−38.973
35.7
C


ATOM
3875
CB
TYR
B1235
−32.229
−29.329
−39.529
38.55
C


ATOM
3876
CG
TYR
B1235
−31.255
−30.498
−39.286
44.18
C


ATOM
3877
CD1
TYR
B1235
−30.527
−31.097
−40.361
48.85
C


ATOM
3878
CE1
TYR
B1235
−29.571
−32.17
−40.097
50.41
C


ATOM
3879
CD2
TYR
B1235
−30.956
−30.943
−37.925
48.72
C


ATOM
3880
CE2
TYR
B1235
−30.005
−31.974
−37.619
48.36
C


ATOM
3881
CZ
TYR
B1235
−29.309
−32.604
−38.71
51.73
C


ATOM
3882
OH
TYR
B1235
−28.405
−33.67
−38.431
50.9
O


ATOM
3883
C
TYR
B1235
−32.282
−26.749
−39.291
33.92
C


ATOM
3884
O
TYR
B1235
−33.203
−26.393
−38.584
33.68
O


ATOM
3885
N
SER
B1236
−31.824
−26.034
−40.318
32.72
N


ATOM
3886
CA
SER
B1236
−32.467
−24.785
−40.759
31.62
C


ATOM
3887
CB
SER
B1236
−31.375
−23.692
−40.958
31.66
C


ATOM
3888
OG
SER
B1236
−31.925
−22.409
−41.29
26.78
O


ATOM
3889
C
SER
B1236
−33.328
−25.04
−42.009
30.87
C


ATOM
3890
O
SER
B1236
−32.823
−25.681
−42.919
31.06
O


ATOM
3891
N
VAL
B1237
−34.614
−24.638
−42.001
30.38
N


ATOM
3892
CA
VAL
B1237
−35.513
−24.609
−43.174
31.34
C


ATOM
3893
CB
VAL
B1237
−37.02
−24.115
−42.819
31.82
C


ATOM
3894
CG1
VAL
B1237
−38.189
−24.363
−43.965
29.46
C


ATOM
3895
CG2
VAL
B1237
−37.456
−24.647
−41.483
34.13
C


ATOM
3896
C
VAL
B1237
−34.947
−23.539
−44.081
32.51
C


ATOM
3897
O
VAL
B1237
−34.477
−22.53
−43.634
32.91
O


ATOM
3898
N
HIS
B1238
−35.049
−23.735
−45.373
34.9
N


ATOM
3899
CA
HIS
B1238
−34.462
−22.809
−46.339
37.53
C


ATOM
3900
CB
HIS
B1238
−34.445
−23.514
−47.653
36.06
C


ATOM
3901
CG
HIS
B1238
−33.489
−24.626
−47.685
32.65
C


ATOM
3902
CD2
HIS
B1238
−33.56
−25.853
−48.262
30.91
C


ATOM
3903
ND1
HIS
B1238
−32.268
−24.532
−47.074
28.37
N


ATOM
3904
CE1
HIS
B1238
−31.615
−25.658
−47.287
35.6
C


ATOM
3905
NE2
HIS
B1238
−32.378
−26.476
−48.01
31.54
N


ATOM
3906
C
HIS
B1238
−35.279
−21.54
−46.54
39.46
C


ATOM
3907
O
HIS
B1238
−34.9
−20.463
−46.144
41.81
O


ATOM
3908
N
ASN
B1239
−36.386 
−21.705
−47.232
41.97
N


ATOM
3909
CA
ASN
B1239
−37.457
−20.761
−47.205
44.12
C


ATOM
3910
CB
ASN
B1239
−38.723
−21.531
−47.615
45.61
C


ATOM
3911
CG
ASN
B1239
−38.849
−21.718
−49.11
49.07
C


ATOM
3912
OD1
ASN
B1239
−39.966
−22.047
−49.593
51.28
O


ATOM
3913
ND2
ASN
B1239
−37.72
−21.548
−49.871
49.39
N


ATOM
3914
C
ASN
B1239
−37.732
−20.193
−45.825
44.34
C


ATOM
3915
O
ASN
B1239
−37.272
−19.103
−45.482
42.93
O


ATOM
3916
N
LYS
B1240
−38.44
−21.031
−45.039
46.24
N


ATOM
3917
CA
LYS
B1240
−39.575
−20.652
−44.125
46.09
C


ATOM
3918
CB
LYS
B1240
−40.686
−21.755
−44.078
47.2
C


ATOM
3919
CG
LYS
B1240
−41.403
−22.078
−42.682
48.07
C


ATOM
3920
CD
LYS
B1240
−42.986
−22.34
−42.824
48.07
C


ATOM
3921
CE
LYS
B1240
−43.353
−23.625
−43.614
47.33
C


ATOM
3922
NZ
LYS
B1240
−43.305
−24.855
−42.778
46.55
N


ATOM
3923
C
LYS
B1240
−39.042
−20.3
−42.796
44.7
C


ATOM
3924
O
LYS
B1240
−38.808
−21.142
−41.918
45.03
O


ATOM
3925
N
THR
B1241
−38.923
−19
−42.672
43.95
N


ATOM
3926
CA
THR
B1241
−37.75
−18.379
−42.113
43.68
C


ATOM
3927
CB
THR
B1241
−37.912
−17.912
−40.593
44.97
C


ATOM
3928
OG1
THR
B1241
−36.612
−17.659
−40.012
48.88
O


ATOM
3929
CG2
THR
B1241
−38.808
−18.875
−39.642
45.32
C


ATOM
3930
C
THR
B1241
−36.598
−19.286
−42.401
41.6
C


ATOM
3931
O
THR
B1241
−36.446
−19.833
−43.473
42.93
O


ATOM
3932
N
GLY
B1242
−35.739
−19.421
−41.448
39.81
N


ATOM
3933
CA
GLY
B1242
−34.996
−20.61
−41.362
36.11
C


ATOM
3934
C
GLY
B1242
−35.436
−20.956
−39.967
33.19
C


ATOM
3935
O
GLY
B1242
−34.711
−20.656
−39.027
32.74
O


ATOM
3936
N
ALA
B1243
−36.661
−21.472
−39.836
29.81
N


ATOM
3937
CA
ALA
B1243
−37.037
−22.105
−38.585
27.88
C


ATOM
3938
CB
ALA
B1243
−38.491
−22.775
−38.648
27.63
C


ATOM
3939
C
ALA
B1243
−35.917
−23.137
−38.209
25.69
C


ATOM
3940
O
ALA
B1243
−35.434
−23.861
−39.04
23.82
O


ATOM
3941
N
LYS
B1244
−35.471
−23.1
−36.955
24.7
N


ATOM
3942
CA
LYS
B1244
−34.543
−24.063
−36.429
23.56
C


ATOM
3943
CB
LYS
B1244
−33.705
−23.448
−35.326
23.12
C


ATOM
3944
CG
LYS
B1244
−33.115
−22.087
−35.698
25.56
C


ATOM
3945
CD
LYS
B1244
−31.993
−22.206
−36.679
26.2
C


ATOM
3946
CE
LYS
B1244
−31.934
−20.959
−37.564
28.44
C


ATOM
3947
NZ
LYS
B1244
−32.549
−19.815
−36.856
27.98
N


ATOM
3948
C
LYS
B1244
−35.381
−25.227
−35.908 
22.49
C


ATOM
3949
O
LYS
B1244
−36.427
−25.057
−35.33
22.76
O


ATOM
3950
N
LEU
B1245
−34.897
−26.421
−36.1442
1.42
N


ATOM
3951
CA
LEU
B1245
−35.613
−27.618
−35.829
19.61
C


ATOM
3952
CB
LEU
B1245
−36.23
−28.184
−37.127
21.08
C


ATOM
3953
CG
LEU
B1245
−37.226
−27.274
−37.878
23.54
C


ATOM
3954
CD1
LEU
B1245
−36.77
−26.914
−39.317
23.91
C


ATOM
3955
CD2
LEU
B1245
−38.488
−28.039
−37.994
30.03
C


ATOM
3956
C
LEU
B1245
−34.584
−28.554
−35.206
17.53
C


ATOM
3957
O
LEU
B1245
−33.66
−29.055
−35.916
14.78
O


ATOM
3958
N
PRO
B1246
−34.692
−28.735
−33.861
16.71
N


ATOM
3959
CD
PRO
B1246
−35.669
−28.048
−32.962
16.55
C


ATOM
3960
CA
PRO
B1246
−33.865
−29.676
−33.104
15.54
C


ATOM
3961
CB
PRO
B1246
−34.257
−29.351
−31.666
16.13
C


ATOM
3962
CG
PRO
B1246
−35.652
−28.846
−31.726
12.22
C


ATOM
3963
C
PRO
B1246
−34.36
−31.108
−33.453
15.49
C


ATOM
3964
O
PRO
B1246
−34.977
−31.795
−32.611
16.52
O


ATOM
3965
N
VAL
B1247
−34.123
−31.535
−34.689
13.12
N


ATOM
3966
CA
VAL
B1247
−34.584
−32.798
−35.143
13.03
C


ATOM
3967
CB
VAL
B1247
−34.022
−33.173
−36.545
13.66
C


ATOM
3968
CG1
VAL
B1247
−33.97
−32.026
−37.403
16.62
C


ATOM
3969
CG2
VAL
B1247
−32.671
−33.871
−36.495
16.62
C


ATOM
3970
C
VAL
B1247
−34.507
−33.995
−34.183
11.34
C


ATOM
3971
O
VAL
B1247
−35.466
−34.721
−34.083
11.5
O


ATOM
3972
N
LYS
B1248
−33.381
−34.195
−33.51
11.79
N


ATOM
3973
CA
LYS
B1248
−33.165
−35.38
−32.689
12.47
C


ATOM
3974
CB
LYS
B1248
−31.702
−35.589
−32.463
12.8
C


ATOM
3975
CG
LYS
B1248
−30.995
−36.234
−33.691
15.64
C


ATOM
3976
CD
LYS
B1248
−29.37
−36.242
−33.586
18.07
C


ATOM
3977
CE
LYS
B1248
−28.673
−36.979
−34.801
15.79
C


ATOM
3978
NZ
LYS
B1248
−29.745
−37.139
−35.892
23.64
N


ATOM
3979
C
LYS
B1248
−33.908
−35.348
−31.382
10.54
C


ATOM
3980
O
LYS
B1248
−33.981
−36.36
−30.728
10.31
O


ATOM
3981
N
TRP
B1249
−34.525
−34.213
−31.034
9.66
N


ATOM
3982
CA
TRP
B1249
−35.405
−34.107
−29.845
8.39
C


ATOM
3983
CB
TRP
B1249
−35.086
−32.836
−29.014
7.29
C


ATOM
3984
CG
TRP
B1249
−33.914
−33.017
−28.158
5.7
C


ATOM
3985
CD2
TRP
B1249
−32.548
−33.029
−28.582
4.8
C


ATOM
3986
CE2
TRP
B1249
−31.755
−33.293
−27.442
3.54
C


ATOM
3987
CE3
TRP
B1249
−31.909
−32.804
−29.806
9.04
C


ATOM
3988
CD1
TRP
B1249
−33.896
−33.289
−26.791
4.28
C


ATOM
3989
NE1
TRP
B1249
−32.607
−33.458
−26.374
2.45
N


ATOM
3990
CZ2
TRP
B1249
−30.337
−33.352
−27.5
2
C


ATOM
3991
CZ3
TRP
B1249
−30.474
−32.872
−29.844
8.31
C


ATOM
3992
CH2
TRP
B1249
−29.74
−33.16
−28.702
4.96
C


ATOM
3993
C
TRP
B1249
−36.828
−33.99
−30.325
9.48
C


ATOM
3994
O
TRP
B1249
−37.726
−33.99
−29.522
11.52
O


ATOM
3995
N
MET
B1250
−37.053
−33.901
−31.63
10.09
N


ATOM
3996
CA
MET
B1250
−38.384
−33.689
−32.159
11.64
C


ATOM
3997
CB
MET
B1250
−38.295
−33.04
−33.507
11.33
C


ATOM
3998
CG
MET
B1250
−38.313
−31.485
−33.482
12.69
C


ATOM
3999
SD
MET
B1250
−37.811
−30.796
−35.124
16.39
S


ATOM
4000
CE
MET
B1250
−39.348 
−30.884
−36.046
17.08
C


ATOM
4001
C
MET
B1250
−39.178
−34.974
−32.272
13.02
C


ATOM
4002
O
MET
B1250
−38.606
−36.105
−32.53
12.68
O


ATOM
4003
N
ALA
B1251
−40.501
−34.838
−32.06
12.87
N


ATOM
4004
CA
ALA
B1251
−41.405
−35.982
−32.177
13.1
C


ATOM
4005
CB
ALA
B1251
−42.699
−35.724
−31.481
12.42
C


ATOM
4006
C
ALA
B1251
−41.62
−36.363
−33.651
15.54
C


ATOM
4007
O
ALA
B1251
−41.512
−35.498
−34.572
14.8
O


ATOM
4008
N
LEU
B1252
−41.903
−37.662
−33.866
17.95
N


ATOM
4009
CA
LEU
B1252
−42.248
−38.215
−35.18
19.26
C


ATOM
4010
CB
LEU
B1252
−42.867
−39.609
−35.016
20.92
C


ATOM
4011
CG
LEU
B1252
−43.079
−40.544
−36.227
21.26
C


ATOM
4012
CD1
LEU
B1252
−41.988
−40.407
−37.34
19.45
C


ATOM
4013
CD2
LEU
B1252
−43.292
−42.011
−35.699
19.03
C


ATOM
4014
C
LEU
B1252
−43.215
−37.333
−35.962
19.23
C


ATOM
4015
O
LEU
B1252
−42.91
−36.899
−37.062
19.86
O


ATOM
4016
N
GLU
B1253
−44.374
−37.05
−35.405
18.89
N


ATOM
4017
CA
GLU
B1253
−45.26
−36.124
−36.066
20.29
C


ATOM
4018
CB
GLU
B1253
−46.574
−36.042
−35.299
19.85
C


ATOM
4019
CG
GLU
B1253
−46.507
−35.19
−33.996
22.81
C


ATOM
4020
CD
GLU
B1253
−46.092
−35.973
−32.754
24.46
C


ATOM
4021
OE1
GLU
B1253
−45.675
−37.15
−32.878
27.79
O


ATOM
4022
OE2
GLU
B1253
−46.214
−35.408
−31.643
26.76
O


ATOM
4023
C
GLU
B1253
−44.664
−34.692
−36.414
21.64
C


ATOM
4024
O
GLU
B1253
−44.968
−34.162
−37.492
22.96
O


ATOM
4025
N
SER
B1254
−43.818
−34.079
−35.567
21.49
N


ATOM
4026
CA
SER
B1254
−43.302
−32.735
−35.855
21.38
C


ATOM
4027
CB
SER
B1254
−42.609
−32.116
−34.647
21.56
C


ATOM
4028
OG
SER
B1254
−43.485
−32.087
−33.503
25.03
O


ATOM
4029
C
SER
B1254
−42.313
−32.823
−36.976
21.95
C


ATOM
4030
O
SER
B1254
−42.22
−31.926
−37.784
22.06
O


ATOM
4031
N
LEU
B1255
−41.534
−33.896
−37.031
22.64
N


ATOM
4032
CA
LEU
B1255
−40.623
−34.095
−38.146
22.06
C


ATOM
4033
CB
LEU
B1255
−39.865
−35.409
−37.985
20.16
C


ATOM
4034
CG
LEU
B1255
−38.889
−35.49
−36.825
17.35
C


ATOM
4035
CD1
LEU
B1255
−38.374
−36.987
−36.629
13.13
C


ATOM
4036
CD2
LEU
B1255
−37.76
−34.489
−37.004
14.62
C


ATOM
4037
C
LEU
B1255
−41.387
−34.15
−39.467
23.82
C


ATOM
4038
O
LEU
B1255
−40.89
−33.691
−40.511
25.05
O


ATOM
4039
N
GLN
B1256
−42.575
−34.753
−39.424
24.85
N


ATOM
4040
CA
GLN
B1256
−43.34
−35.01
−40.605
26.22
C


ATOM
4041
CB
GLN
B1256
−44.294
−36.186
−40.422
25.39
C


ATOM
4042
CG
GLN
B1256
−43.687
−37.577
−40.193
26.12
C


ATOM
4043
CD
GLN
B1256
−44.774
−38.604
−39.754
27.1
C


ATOM
4044
OE1
GLN
B1256
−45.184
−39.42
−40.533
29.2
O


ATOM
4045
NE2
GLN
B1256
−45.273
−38.501
−38.525
26.57
N


ATOM
4046
C
GLN
B1256
−44.166
−33.781
−40.914
27.29
C


ATOM
4047
O
GLN
B1256
−44.508
−33.567
−42.066
29.76
O


ATOM
4048
N
THR
B1257
−44.5
−32.968
−39.926
27.03
N


ATOM
4049
CA
THR
B1257
−45.449
−31.874
−40.149
26.26
C


ATOM
4050
CB
THR
B1257
−46.737
−32.13
−39.348
27.06
C


ATOM
4051
OG1
THR
B1257
−46.459
−32.004
−37.938
24.23
O


ATOM
4052
CG2
THR
B1257
−47.303
−33.527
−39.645
25.82
C


ATOM
4053
C
THR
B1257
−44.927
−30.485
−39.743
26.76
C


ATOM
4054
O
THR
B1257
−45.495
−29.455
−40.084
26.46
O


ATOM
4055
N
GLN
B1258
−43.854
−30.465
−38.979
27.16
N


ATOM
4056
CA
GLN
B1258
−43.232
−29.234
−38.532
28.56
C


ATOM
4057
CB
GLN
B1258
−42.773
−28.422
−39.75
28.63
C


ATOM
4058
CG
GLN
B1258
−41.445
−27.703
−39.541
32.3
C


ATOM
4059
CD
GLN
B1258
−41.202
−26.525
−40.556
33.04
C


ATOM
4060
OE1
GLN
B1258
−40.718
−25.425
−40.163
35.92
O


ATOM
4061
NE2
GLN
B1258
−41.511
−26.766
−41.852
31.94
N


ATOM
4062
C
GLN
B1258
−44.152
−28.424
−37.578
27.21
C


ATOM
4063
O
GLN
B1258
−43.982
−27.187
−37.391
27.96
O


ATOM
4064
N
LYS
B1259
−45.122
−29.117
−36.987
25.61
N


ATOM
4065
CA
LYS
B1259
−45.992
−28.515
−35.993
24.97
C


ATOM
4066
CB
LYS
B1259
−47.448
−28.482
−36.486
26.14
C


ATOM
4067
CG
LYS
B1259
−47.723
−27.151
−37.225
32.4
C


ATOM
4068
CD
LYS
B1259
−48.102
−27.291
−38.71
40.86
C


ATOM
4069
CE
LYS
B1259
−49.665
−27.375
−38.896
50.91
C


ATOM
4070
NZ
LYS
B1259
−50.394
−28.321
−37.902
53.68
N


ATOM
4071
C
LYS
B1259
−45.826
−29.129
−34.59
22.27
C


ATOM
4072
O
LYS
B1259
−45.634
−30.333
−34.484
21.35
O


ATOM
4073
N
PHE
B1260
−45.856
−28.275
−33.542
19.76
N


ATOM
4074
CA
PHE
B1260
−45.587
−28.652
−32.148
17.39
C


ATOM
4075
CB
PHE
B1260
−44.45
−27.875
−31.589
14.45
C


ATOM
4076
CG
PHE
B1260
−43.248
−27.866
−32.479
16.95
C


ATOM
4077
CD1
PHE
B1260
−43.232
−27.143
−33.676
12.95
C


ATOM
4078
CD2
PHE
B1260
−42.1
−28.615
−32.149
18.21
C


ATOM
4079
CE1
PHE
B1260
−42.09
−27.176
−34.51
14.99
C


ATOM
4080
CE2
PHE
B1260
−40.962
−28.61
−33.022
15.9
C


ATOM
4081
CZ
PHE
B1260
−40.981
−27.874
−34.185
11.08
C


ATOM
4082
C
PHE
B1260
−46.778
−28.545
−31.202
18.09
C


ATOM
4083
O
PHE
B1260
−47.724
−27.776
−31.422
18.72
O


ATOM
4084
N
THR
B1261
−46.726
−29.367
−30.148
17.79
N


ATOM
4085
CA
THR
B1261
−47.745
−29.416
−29.111
17.31
C


ATOM
4086
CB
THR
B1261
−48.793
−30.515
−29.388
16.69
C


ATOM
4087
OG1
THR
B1261
−48.125
−31.755
−29.671
17.09
O


ATOM
4088
CG2
THR
B1261
−49.667
−30.138
−30.574
17.08
C


ATOM
4089
C
THR
B1261
−47.083
−29.751
−27.801
16.71
C


ATOM
4090
O
THR
B1261
−45.87
−30.073
−27.768
16.18
O


ATOM
4091
N
THR
B1262
−47.886
−29.729
−26.728
15.26
N


ATOM
4092
CA
THR
B1262
−47.439
−30.274
−25.427
14.24
C


ATOM
4093
CB
THR
B1262
−48.509
−29.994
−24.355
12.83
C


ATOM
4094
OG1
THR
B1262
−48.54
−28.588
−24.19
14.64
O


ATOM
4095
CG2
THR
B1262
−48.162
−30.554
−23.009
12.65
C


ATOM
4096
C
THR
B1262
−47.08
−31.73
−25.49
13.76
C


ATOM
4097
O
THR
B1262
−46.206
−32.128
−24.782
16.54
O


ATOM
4098
N
LYS
B1263
−47.735
−32.535
−26.329
14.41
N


ATOM
4099
CA
LYS
B1263
−47.326
−33.942
−26.538
14.1
C


ATOM
4100
CB
LYS
B1263
−48.35
−34.761
−27.329
13.72
C


ATOM
4101
CG
LYS
B1263
−49.67 
−34.811
−26.68
13.94
C


ATOM
4102
CD
LYS
B1263
−49.545
−35.067
−25.196
14.53
C


ATOM
4103
CE
LYS
B1263
−50.85 
−35.583
−24.602
13.05
C


ATOM
4104
NZ
LYS
B1263
−50.49 
−36.259
−23.363
17.05
N


ATOM
4105
C
LYS
B1263
−45.98 
−34.027
−27.257
14.57
C


ATOM
4106
O
LYS
B1263
−45.2
−34.932
−26.975
15.41
O


ATOM
4107
N
SER
B1264
−45.698
−33.099
−28.16 
11.65
N


ATOM
4108
CA
SER
B1264
−44.441
−33.146
−28.787
13.31
C


ATOM
4109
CB
SER
B1264
−44.492
−32.375
−30.104
12.51
C


ATOM
4110
OG
SER
B1264
−44.451
−31.004
−29.879
16.54
O


ATOM
4111
C
SER
B1264
−43.313
−32.699
−27.811
13
C


ATOM
4112
O
SER
B1264
−42.197
−33.169
−27.925
14.49
O


ATOM
4113
N
ASP
B1265
−43.639
−31.859
−26.829
13.66
N


ATOM
4114
CA
ASP
B1265
−42.758
−31.435
−25.724
13.49
C


ATOM
4115
CB
ASP
B1265
−43.434
−30.31
−24.857
14.45
C


ATOM
4116
CG
ASP
B1265
−43.277
−28.836
−25.42
15.31
C


ATOM
4117
OD1
ASP
B1265
−42.551
−28.551
−26.437
11.54
O


ATOM
4118
OD2
ASP
B1265
−43.948
−27.93
−24.789
14.05
O


ATOM
4119
C
ASP
B1265
−42.544
−32.683
−24.821
13.36
C


ATOM
4120
O
ASP
B1265
−41.438
−32.905
−24.309
12.68
O


ATOM
4121
N
VAL
B1266
−43.595
−33.467
−24.587
10.21
N


ATOM
4122
CA
VAL
B1266
−43.391
−34.728
−23.865
10.13
C


ATOM
4123
CB
VAL
B1266
−44.755
−35.518
−23.608
10.77
C


ATOM
4124
CG1
VAL
B1266
−44.502
−36.889
−23.116
5.97
C


ATOM
4125
CG2
VAL
B1266
−45.649
−34.727
−22.654
7.57
C


ATOM
4126
C
VAL
B1266
−42.382
−35.637
−24.548
8.48
C


ATOM
4127
O
VAL
B1266
−41.442
−36.08
−23.913
9.29
O


ATOM
4128
N
TRP
B1267
−42.506
−35.856
−25.849
8.05
N


ATOM
4129
CA
TRP
B1267
−41.517
−36.661
−26.578
8.38
C


ATOM
4130
CB
TRP
B1267
−41.77
−36.609
−28.027
9.04
C


ATOM
4131
CG
TRP
B1267
−40.748
−37.362
−28.859
13.03
C


ATOM
4132
CD2
TRP
B1267
−41.036
−38.518
−29.698
11.67
C


ATOM
4133
CE2
TRP
B1267
−39.819
−38.935
−30.278
9.47
C


ATOM
4134
CE3
TRP
B1267
−42.215
−39.227
−29.994
10.04
C


ATOM
4135
CD1
TRP
B1267
−39.388
−37.129
−28.961
8.94
C


ATOM
4136
NE1
TRP
B1267
−38.826
−38.097
−29.82
12.78
N


ATOM
4137
CZ2
TRP
B1267
−39.755
−40.002
−31.17
9.52
C


ATOM
4138
CZ3
TRP
B1267
−42.168
−40.258
−30.893
10.1
C


ATOM
4139
CH2
TRP
B1267
−40.934
−40.653
−31.466
11.36
C


ATOM
4140
C
TRP
B1267
−40.119
−36.117
−26.29
9.58
C


ATOM
4141
O
TRP
B1267
−39.173
−36.924
−25.943
11.1
O


ATOM
4142
N
SER
B1268
−39.984
−34.779
−26.408
7.45
N


ATOM
4143
CA
SER
B1268
−38.736
−34.075
−26.174
5.51
C


ATOM
4144
CB
SER
B1268
−38.926
−32.562
−26.31
7.41
C


ATOM
4145
OG
SER
B1268
−38.927
−32.233
−27.655
11.13
O


ATOM
4146
C
SER
B1268
−38.241
−34.274
−24.815
4.11
C


ATOM
4147
O
SER
B1268
−37.066
−34.539
−24.634
4.39
O


ATOM
4148
N
PHE
B1269
−39.125
−34.142
−23.834
3.73
N


ATOM
4149
CA
PHE
B1269
−38.794
−34.445
−22.45
4.56
C


ATOM
4150
CB
PHE
B1269
−40.038
−34.29
−21.58
5.96
C


ATOM
4151
CG
PHE
B1269
−39.81
−34.636
−20.125
6.7
C


ATOM
4152
CD1
PHE
B1269
−39.078
−33.763
−19.287
9.71
C


ATOM
4153
CD2
PHE
B1269
−40.265
−35.832
−19.623
4.42
C


ATOM
4154
CE1
PHE
B1269
−38.847
−34.07
−17.953
8.28
C


ATOM
4155
CE2
PHE
B1269
−40.061
−36.155
−18.32
8.23
C


ATOM
4156
CZ
PHE
B1269
−39.355
−35.241
−17.468
12.92
C


ATOM
4157
C
PHE
B1269
−38.181
−35.834
−22.267
5.12
C


ATOM
4158
O
PHE
B1269
−37.199
−36.012
−21.516
6.6
O


ATOM
4159
N
GLY
B1270
−38.728
−36.828
−22.949
4.58
N


ATOM
4160
CA
GLY
B1270
−38.154
−38.129
−22.823
5.87
C


ATOM
4161
C
GLY
B1270
−36.772
−38.256
−23.358
7.68
C


ATOM
4162
O
GLY
B1270
−35.909
−38.968
−22.753
8.82
O


ATOM
4163
N
VAL
B1271
−36.514
−37.556
−24.478
8.32
N


ATOM
4164
CA
VAL
B1271
−35.076
−37.437
−25.021
8.41
C


ATOM
4165
CB
VAL
B1271
−35.045
−36.627
−26.371
7.21
C


ATOM
4166
CG1
VAL
B1271
−33.805
−36.88
−27.078
8.43
C


ATOM
4167
CG2
VAL
B1271
−36.143
−37.058
−27.294
5.25
C


ATOM
4168
C
VAL
B1271
−34.114
−36.804
−24.012
8.67
C


ATOM
4169
O
VAL
B1271
−32.971
−37.231
−23.82
9.62
O


ATOM
4170
N
LEU
B1272
−34.621
−35.749
−23.379
10.91
N


ATOM
4171
CA
LEU
B1272
−33.95
−35.009
−22.261
11.66
C


ATOM
4172
CB
LEU
B1272
−34.818
−33.81
−21.792
11.01
C


ATOM
4173
CG
LEU
B1272
−34.161
−32.875
−20.766
13.19
C


ATOM
4174
CD1
LEU
B1272
−34.927
−31.529
−20.726
7.24
C


ATOM
4175
CD2
LEU
B1272
−34.025
−33.436
−19.332
10.52
C


ATOM
4176
C
LEU
B1272
−33.668
−35.96
−21.094
10.21
C


ATOM
4177
O
LEU
B1272
−32.556
−35.972
−20.597
10.12
O


ATOM
4178
N
LEU
B1273
−34.65
−36.774
−20.685
9.18
N


ATOM
4179
CA
LEU
B1273
−34.331
−37.803
−19.659
11.07
C


ATOM
4180
CB
LEU
B1273
−35.542
−38.655
−19.303
10.87
C


ATOM
4181
CG
LEU
B1273
−36.725
−37.912
−18.694
16.19
C


ATOM
4182
CD1
LEU
B1273
−37.954
−38.84
−18.631
16.15
C


ATOM
4183
CD2
LEU
B1273
−36.396
−37.352
−17.34 
14.22
C


ATOM
4184
C
LEU
B1273
−33.183
−38.741
−20.07
69.8
C


ATOM
4185
O
LEU
B1273
−32.389
−39.109
−19.277
9.52
O


ATOM
4186
N
TRP
B1274
−33.15
−39.094
−21.358
11.24
N


ATOM
4187
CA
TRP
B1274
−32.163
−39.995
−21.948
10.94
C


ATOM
4188
CB
TRP
B1274
−32.565
−40.397
−23.414
9.58
C


ATOM
4189
CG
TRP
B1274
−31.633
−41.432
−24.04
10.2
C


ATOM
4190
CD2
TRP
B1274
−30.43
−41.158
−24.748
8.46
C


ATOM
4191
CE2
TRP
B1274
−29.842
−42.409
−25.082
9.48
C


ATOM
4192
CE3
TRP
B1274
−29.77
−39.972
−25.119
8.54
C


ATOM
4193
CD1
TRP
B1274
−31.735
−42.841
−23.974
11.41
C


ATOM
4194
NE1
TRP
B1274
−30.673
−43.405
−24.622
9.81
N


ATOM
4195
CZ2
TRP
B1274
−28.617
−42.499
−25.784
6.65
C


ATOM
4196
CZ3
TRP
B1274
−28.6
−40.065
−25.824
9.41
C


ATOM
4197
CH2
TRP
B1274
−28.024
−41.323
−26.151
8.82
C


ATOM
4198
C
TRP
B1274
−30.795
−39.344
−21.861
10.81
C


ATOM
4199
O
TRP
B1274
−29.829
−39.961
−21.379
11.74
O


ATOM
4200
N
GLU
B1275
−30.715
−38.082
−22.242
10.72
N


ATOM
4201
CA
GLU
B1275
−29.426
−37.332
−22.148
10.68
C


ATOM
4202
CB
GLU
B1275
−29.639
−35.857
−22.527
10.88
C


ATOM
4203
CG
GLU
B1275
−30.153
−35.543
−23.903
11.46
C


ATOM
4204
CD
GLU
B1275
−30.4
−34.021
−24.049
14.34
C


ATOM
4205
OE1
GLU
B1275
−31.524
−33.501
−23.805
15.39
O


ATOM
4206
OE2
GLU
B1275
−29.401
−33.309
−24.396
22.77
O


ATOM
4207
C
GLU
B1275
−28.909
−37.315
−20.749
10.34
C


ATOM
4208
O
GLU
B1275
−27.707
−37.337
−20.528
10.71
O


ATOM
4209
N
LEU
B1276
−29.809
−37.115
−19.785
11.05
N


ATOM
4210
CA
LEU
B1276
−29.43
−37.1
−18.346
10.79
C


ATOM
4211
CB
LEU
B1276
−30.632
−36.812
−17.47
12.25
C


ATOM
4212
CG
LEU
B1276
−31.013
−35.427
−16.907
13.19
C


ATOM
4213
CD1
LEU
B1276
−30.601
−34.396
−17.903
20.48
C


ATOM
4214
CD2
LEU
B1276
−32.537
−35.354
−16.588
10.2
C


ATOM
4215
C
LEU
B1276
−28.834
−38.412
−17.94
10.65
C


ATOM
4216
O
LEU
B1276
−27.765
−38.417
−17.393
11.03
O


ATOM
4217
N
MET
B1277
−29.498
−39.527
−18.296
10.47
N


ATOM
4218
CA
MET
B1277
−29.091
−40.868
−17.899
10.55
C


ATOM
4219
CB
MET
B1277
−30.237
−41.888
−18.047
10.09
C


ATOM
4220
CG
MET
B1277
−31.411
−41.644
−17.096
14.97
C


ATOM
4221
SD
MET
B1277
−30.866
−41.259
−15.312
20.21
S


ATOM
4222
CE
MET
B1277
−31.078
−42.892
−14.719
17.84
C


ATOM
4223
C
MET
B1277
−27.823
−41.309
−18.596
10.99
C


ATOM
4224
O
MET
B1277
−27.194
−42.218
−18.136
12.08
O


ATOM
4225
N
THR
B1278
−27.456
−40.657
−19.701
12.51
N


ATOM
4226
CA
THR
B1278
−26.236
−40.961
−20.482
11.87
C


ATOM
4227
CB
THR
B1278
−26.515
−41.002
−21.99
12.63
C


ATOM
4228
OG1
THR
B1278
−27.031
−39.745
−22.452
8.58
O


ATOM
4229
CG2
THR
B1278
−27.547
−42.16
−22.375
10.3
C


ATOM
4230
C
THR
B1278
−25.239
−39.865
−20.205
13.76
C


ATOM
4231
O
THR
B1278
−24.179
−39.799
−20.812
14.83
O


ATOM
4232
N
ARG
B1279
−25.582
−39.023
−19.222
14.86
N


ATOM
4233
CA
ARG
B1279
−24.78
−37.831
−18.858
15.36
C


ATOM
4234
CB
ARG
B1279
−23.525
−38.248
−18.1
15.01
C


ATOM
4235
CG
ARG
B1279
−23.844
−38.717
−16.667
15.98
C


ATOM
4236
CD
ARG
B1279
−22.587
−38.783
−15.851
19.69
C


ATOM
4237
NE
ARG
B1279
−21.75
−37.562
−15.876
19.77
N


ATOM
4238
CZ
ARG
B1279
−20.576
−37.432
−15.229
19.3
C


ATOM
4239
NH1
ARG
B1279
−20.15
−38.439
−14.507
19.24
N


ATOM
4240
NH2
ARG
B1279
−19.831
−36.31
−15.296
18.68
N


ATOM
4241
C
ARG
B1279
−24.4
−37.045
−20.084
14.5
C


ATOM
4242
O
ARG
B1279
−23.215
−36.816
−20.333
13.92
O


ATOM
4243
N
GLY
B1280
−25.398
−36.714
−20.886
14.34
N


ATOM
4244
CA
GLY
B1280
−25.185
−35.899
−22.099
16.19
C


ATOM
4245
C
GLY
B1280
−24.691
−36.567
−23.394
17.54
C


ATOM
4246
O
GLY
B1280
−24.179
−35.859
−24.239
18.98
O


ATOM
4247
N
ALA
B1281
−24.788
−37.899
−23.583
17.6
N


ATOM
4248
CA
ALA
B1281
−24.37
−38.477
−24.854
17.07
C


ATOM
4249
CB
ALA
B1281
−24.456
−39.91
−24.849
17.2
C


ATOM
4250
C
ALA
B1281
−25.354
−37.928
−25.858
18.67
C


ATOM
4251
O
ALA
B1281
−26.479
−37.691
−25.487
18.23
O


ATOM
4252
N
PRO
B1282
−24.918
−37.652
−27.114
18.85
N


ATOM
4253
CD
PRO
B1282
−23.561
−37.714
−27.7
19.07
C


ATOM
4254
CA
PRO
B1282
−25.936
−37.183
−28.063
19.03
C


ATOM
4255
CB
PRO
B1282
−25.114
−36.547
−29.185
19.41
C


ATOM
4256
CG
PRO
B1282
−23.823
−37.421
−29.231
20.06
C


ATOM
4257
C
PRO
B1282
−26.794
−38.329
−28.631
18.75
C


ATOM
4258
O
PRO
B1282
−26.266
−39.369
−28.982
18.98
O


ATOM
4259
N
PRO
B1283
−28.118
−38.108
−28.775
19.17
N


ATOM
4260
CD
PRO
B1283
−28.853
−36.859
−28.437
18.86
C


ATOM
4261
CA
PRO
B1283
−29.024
−39.124
−29.297
19.02
C


ATOM
4262
CB
PRO
B1283
−30.43
−38.501
−29.009
18.56
C


ATOM
4263
CG
PRO
B1283
−30.258
−37.142
−28.879
17.23
C


ATOM
4264
C
PRO
B1283
−28.841
−39.395
−30.798
19.32
C


ATOM
4265
O
PRO
B1283
−28.662
−38.429
−31.591
21.46
O


ATOM
4266
N
TYR
B1284
−28.971
−40.664
−31.192
19.19
N


ATOM
4267
CA
TYR
B1284
−28.753
−41.129
−32.591
18.43
C


ATOM
4268
CB
TYR
B1284
−29.945
−40.797
−33.455
18.2
C


ATOM
4269
CG
TYR
B1284
−31.282
−40.712
−32.714
17.9
C


ATOM
4270
CD1
TYR
B1284
−32.126
−41.84
−32.634
12.98
C


ATOM
4271
CE1
TYR
B1284
−33.257
−41.797
−31.972
14.34
C


ATOM
4272
CD2
TYR
B1284
−31.705
−39.506
−32.127
14.75
C


ATOM
4273
CE2
TYR
B1284
−32.907
−39.437
−31.442
13.46
C


ATOM
4274
CZ
TYR
B1284
−33.697
−40.579
−31.388
16.98
C


ATOM
4275
OH
TYR
B1284
−34.93
−40.54
−30.755
16.26
O


ATOM
4276
C
TYR
B1284
−27.438
−40.55
−33.221
19.56
C


ATOM
4277
O
TYR
B1284
−27.451
−39.885
−34.266
17.04
O


ATOM
4278
N
PRO
B1285
−26.3
−40.75
−32.519
20.97
N


ATOM
4279
CD
PRO
B1285
−26.047
−41.534
−31.294
19.88
C


ATOM
4280
CA
PRO
B1285
−25.1
−40.093
−32.988
22.62
C


ATOM
4281
CB
PRO
B1285
−24.025
−40.589
−32
20.54
C


ATOM
4282
CG
PRO
B1285
−24.632
−41.818
−31.389
22.01
C


ATOM
4283
C
PRO
B1285
−24.786
−40.524
−34.415
24.49
C


ATOM
4284
O
PRO
B1285
−24.241
−39.737
−35.18
25.5
O


ATOM
4285
N
ASP
B1286
−25.164
−41.749
−34.766
27.37
N


ATOM
4286
CA
ASP
B1286
−24.704
−42.331
−36.018
31.08
C


ATOM
4287
CB
ASP
B1286
−24.187
−43.772
−35.778
32.37
C


ATOM
4288
CG
ASP
B1286
−22.72
−43.794
−35.198
37.41
C


ATOM
4289
OD1
ASP
B1286
−22.403
−44.628
−34.255
38.84
O


ATOM
4290
OD2
ASP
B1286
−21.907
−42.938
−35.687
38.04
O


ATOM
4291
C
ASP
B1286
−25.71
−42.214
−37.204
31.19
C


ATOM
4292
O
ASP
B1286
−25.473
−42.825
−38.251
31.88
O


ATOM
4293
N
VAL
B1287
−26.783
−41.421
−37.002
29.92
N


ATOM
4294
CA
VAL
B1287
−27.83
−41.055
−37.968
28.47
C


ATOM
4295
CB
VAL
B1287
−29.195
−41.458
−37.484
28.62
C


ATOM
4296
CG1
VAL
B1287
−29.805
−42.395
−38.473
30.75
C


ATOM
4297
CG2
VAL
B1287
−29.117
−42.081
−36.084
30.13
C


ATOM
4298
C
VAL
B1287
−28.018
−39.58
−38.409
27.43
C


ATOM
4299
O
VAL
B1287
−27.907
−38.621
−37.615
24.94
O


ATOM
4300
N
ASN
B1288
−28.357
−39.439
−39.7
25.37
N


ATOM
4301
CA
ASN
B1288
−28.695
−38.162
−40.252
23.52
C


ATOM
4302
CB
ASN
B1288
−28.217
−38.016
−41.715
24.34
C


ATOM
4303
CG
ASN
B1288
−29.032
−38.899
−42.718
22.8
C


ATOM
4304
OD1
ASN
B1288
−30.22
−39.086
−42.568
23.33
O


ATOM
4305
ND2
ASN
B1288
−28.376
−39.421
−43.706
18.01
N


ATOM
4306
C
ASN
B1288
−30.196
−38.069
−40.154
22.61
C


ATOM
4307
O
ASN
B1288
−30.911
−39.051
−39.908
21.14
O


ATOM
4308
N
THR
B1289
−30.686
−36.882
−40.389
21.92
N


ATOM
4309
CA
THR
B1289
−32.097
−36.631
−40.185
22.85
C


ATOM
4310
CB
THR
B1289
−32.339
−35.133
−40.101
22.97
C


ATOM
4311
OG1
THR
B1289
−32.875
−34.697
−41.323
27.53
O


ATOM
4312
CG2
THR
B1289
−31.049
−34.441
−39.957
21.76
C


ATOM
4313
C
THR
B1289
−33.046
−37.19
−41.219
22.8
C


ATOM
4314
O
THR
B1289
−34.233
−37.072
−41.045
23.92
O


ATOM
4315
N
PHE
B1290
−32.555
−37.753
−42.324
22.88
N


ATOM
4316
CA
PHE
B1290
−33.446
−38.501
−43.188
22.14
C


ATOM
4317
CB
PHE
B1290
−32.842
−38.696
−44.574
21.33
C


ATOM
4318
CG
PHE
B1290
−33.712
−39.497
−45.465
19.38
C


ATOM
4319
CD1
PHE
B1290
−34.76
−38.915
−46.123
17.77
C


ATOM
4320
CD2
PHE
B1290
−33.516
−40.86
−45.595
22.41
C


ATOM
4321
CE1
PHE
B1290
−35.614
−39.679
−46.916
20.2
C


ATOM
4322
CE2
PHE
B1290
−34.389
−41.647
−46.369
22.41
C


ATOM
4323
CZ
PHE
B1290
−35.419
−41.053
−47.042
20.49
C


ATOM
4324
C
PHE
B1290
−33.762
−39.853
−42.511
22.8
C


ATOM
4325
O
PHE
B1290
−34.938
−40.28
−42.341
23.53
O


ATOM
4326
N
ASP
B1291
−32.691
−40.489
−42.084
23.39
N


ATOM
4327
CA
ASP
B1291
−32.716
−41.81
−41.531
25.68
C


ATOM
4328
CB
ASP
B1291
−31.286
−42.354
−41.462
26.6
C


ATOM
4329
CG
ASP
B1291
−30.783
−42.791
−42.821
31.08
C


ATOM
4330
OD1
ASP
B1291
−30.091
−41.973
−43.493
39.79
O


ATOM
4331
OD2
ASP
B1291
−31.118
−43.917
−43.254
34.14
O


ATOM
4332
C
ASP
B1291
−33.404
−41.887
−40.173
25.96
C


ATOM
4333
O
ASP
B1291
−34.082
−42.896
−39.876
27.77
O


ATOM
4334
N
ILE
B1292
−33.219
−40.865
−39.354
24.64
N


ATOM
4335
CA
ILE
B1292
−33.978
−40.718
−38.086
24.06
C


ATOM
4336
CB
ILE
B1292
−33.717
−39.333
−37.395
23.91
C


ATOM
4337
CG2
ILE
B1292
−34.52
−38.228
−38.039
22.83
C


ATOM
4338
CG1
ILE
B1292
−34.137
−39.381
−35.934
25.2
C


ATOM
4339
CD1
ILE
B1292
−33.285
−40.209
−35.142
29.16
C


ATOM
4340
C
ILE
B1292
−35.493
−40.957
−38.258
22.98
C


ATOM
4341
O
ILE
B1292
−36.167
−41.598
−37.392
22.39
O


ATOM
4342
N
THR
B1293
−36.038
−40.498
−39.379
20.83
N


ATOM
4343
CA
THR
B1293
−37.497
−40.546
−39.512
19.69
C


ATOM
4344
CB
THR
B1293
−37.956
−39.539
−40.585
19.99
C


ATOM
4345
OG1
THR
B1293
−37.454
−38.237
−40.201
19.82
O


ATOM
4346
CG2
THR
B1293
−39.542
−39.516
−40.79
18.66
C


ATOM
4347
C
THR
B1293
−37.916
−41.972
−39.768
18.48
C


ATOM
4348
O
THR
B1293
−38.92
−42.457
−39.319
18.06
O


ATOM
4349
N
VAL
B1294
−37.033
−42.675
−40.427
19.37
N


ATOM
4350
CA
VAL
B1294
−37.265
−44.057
−40.852
18.14
C


ATOM
4351
CB
VAL
B1294
−36.276
−44.44
−41.987
16.93
C


ATOM
4352
CG1
VAL
B1294
−36.204
−45.932
−42.144
16.99
C


ATOM
4353
CG2
VAL
B1294
−36.642
−43.726
−43.24
16.98
C


ATOM
4354
C
VAL
B1294
−37.007
−44.934
−39.68
18.45
C


ATOM
4355
O
VAL
B1294
−37.697
−45.952
−39.506
20.56
O


ATOM
4356
N
TYR
B1295
−35.997
−44.564
−38.899
16.67
N


ATOM
4357
CA
TYR
B1295
−35.638
−45.276
−37.722
16.51
C


ATOM
4358
CB
TYR
B1295
−34.492
−44.495
−37.098
18.46
C


ATOM
4359
CG
TYR
B1295
−33.946
−45.014
−35.785
22.08
C


ATOM
4360
CD1
TYR
B1295
−32.897
−45.936
−35.786
18.65
C


ATOM
4361
CE1
TYR
B1295
−32.39
−46.441
−34.598
21.13
C


ATOM
4362
CD2
TYR
B1295
−34.508
−44.595
−34.522
20.64
C


ATOM
4363
CE2
TYR
B1295
−33.997
−45.107
−33.318
22.26
C


ATOM
4364
CZ
TYR
B1295
−32.924
−46.021
−33.376
22.13
C


ATOM
4365
OH
TYR
B1295
−32.382
−46.571
−32.246
22.52
O


ATOM
4366
C
TYR
B1295
−36.854
−45.256
−36.846
16
C


ATOM
4367
O
TYR
B1295
−37.362
−46.275
−36.484
16.15
O


ATOM
4368
N
LEU
B1296
−37.335
−44.069
−36.518
17.4
N


ATOM
4369
CA
LEU
B1296
−38.569
−43.871
−35.695
18.14
C


ATOM
4370
CB
LEU
B1296
−38.857
−42.369
−35.415
16.41
C


ATOM
4371
CG
LEU
B1296
−37.827
−41.579
−34.591
17.12
C


ATOM
4372
CD1
LEU
B1296
−38.248
−40.118
−34.316
17.69
C


ATOM
4373
CD2
LEU
B1296
−37.568
−42.248
−33.297
19.55
C


ATOM
4374
C
LEU
B1296
−39.796
−44.499
−36.276
19.05
C


ATOM
4375
O
LEU
B1296
−40.678
−45.011
−35.565
19.99
O


ATOM
4376
N
LEU
B1297
−39.903
−44.392
−37.584
21.12
N


ATOM
4377
CA
LEU
B1297
−41.05
−44.95
−38.301
21.99
C


ATOM
4378
CB
LEU
B1297
−41.041
−44.458
−39.76
22.16
C


ATOM
4379
CG
LEU
B1297
−42.349
−43.788
−40.253
24.1
C


ATOM
4380
CD1
LEU
B1297
−42.933
−42.852
−39.23
27.09
C


ATOM
4381
CD2
LEU
B1297
−42.214
−43.055
−41.568
22.63
C


ATOM
4382
C
LEU
B1297
−40.944
−46.474
−38.189
22.27
C


ATOM
4383
O
LEU
B1297
−41.937
−47.138
−38.123
23.87
O


ATOM
4384
N
GLN
B1298
−39.745
−47.049
−38.124
22.59
N


ATOM
4385
CA
GLN
B1298
−39.64
−48.519
−37.939
22.65
C


ATOM
4386
CB
GLN
B1298
−38.239
−49.031
−38.273
22.35
C


ATOM
4387
CG
GLN
B1298
−37.925
−48.986
−39.772
22.45
C


ATOM
4388
CD
GLN
B1298
−36.406
−48.945
−40.084
25.99
C


ATOM
4389
OE1
GLN
B1298
−35.576
−48.486
−39.278
28.63
O


ATOM
4390
NE2
GLN
B1298
−36.052
−49.376
−41.283
28.14
N


ATOM
4391
C
GLN
B1298
−40.01
−48.972
−36.511
21.75
C


ATOM
4392
O
GLN
B1298
−39.95
−50.191
−36.19
21.69
O


ATOM
4393
N
GLY
B1299
−40.401
−48.004
−35.663
19.9
N


ATOM
4394
CA
GLY
B1299
−40.685
−48.284
−34.269
16.6
C


ATOM
4395
C
GLY
B1299
−39.444
−48.332
−33.427
15.5
C


ATOM
4396
O
GLY
B1299
−39.528
−48.659
−32.23
18.01
O


ATOM
4397
N
ARG
B1300
−38.279
−48.013
−33.986
13.06
N


ATOM
4398
CA
ARG
B1300
−37.018
−48.036
−33.185
11.49
C


ATOM
4399
CB
ARG
B1300
−35.761
−48.001
−34.1
10.35
C


ATOM
4400
CG
ARG
B1300
−35.596
−49.253
−34.88
18.8
C


ATOM
4401
CD
ARG
B1300
−34.804
−49.057
−36.208
11.14
C


ATOM
4402
NE
ARG
B1300
−35.001
−50.267
−37.006
14.02
N


ATOM
4403
CZ
ARG
B1300
−34.449
−51.482
−36.788
14.19
C


ATOM
4404
NH1
ARG
B1300
−33.565
−51.753
−35.769
12.76
N


ATOM
4405
NH2
ARG
B1300
−34.807
−52.443
−37.609
7.95
N


ATOM
4406
C
ARG
B1300
−36.982
−46.825
−32.278
12.12
C


ATOM
4407
O
ARG
B1300
−37.476
−45.745
−32.664
11.41
O


ATOM
4408
N
ARG
B1301
−36.379
−47.001
−31.085
12.18
N


ATOM
4409
CA
ARG
B1301
−36.242
−45.941
−30.083
10.47
C


ATOM
4410
CB
ARG
B1301
−37.226
−46.167
−28.949
10.51
C


ATOM
4411
CG
ARG
B1301
−38.659
−45.805
−29.248
10.7
C


ATOM
4412
CD
ARG
B1301
−38.823
−44.561
−30.173
12.65
C


ATOM
4413
NE
ARG
B1301
−40.219
−44.305
−30.478
10.61
N


ATOM
4414
CZ
ARG
B1301
−40.823
−44.551
−31.628
13.77
C


ATOM
4415
NH1
ARG
B1301
−40.167
−45.018
−32.687
9.33
N


ATOM
4416
NH2
ARG
B1301
−42.121
−44.303
−31.709
16.57
N


ATOM
4417
C
ARG
B1301
−34.833
−45.866
−29.54
10.44
C


ATOM
4418
O
ARG
B1301
−33.998
−46.702
−29.83
9.22
O


ATOM
4419
N
LEU
B1302
−34.55
−44.825
−28.783
9.97
N


ATOM
4420
CA
LEU
B1302
−33.246
−44.705
−28.137
9.91
C


ATOM
4421
CB
LEU
B1302
−33.199
−43.365
−27.393
8.2
C


ATOM
4422
CG
LEU
B1302
−33.005
−42.134
−28.25
7.77
C


ATOM
4423
CD1
LEU
B1302
−33.264
−40.843
−27.548
2
C


ATOM
4424
CD2
LEU
B1302
−31.622
−42.163
−28.913
7.03
C


ATOM
4425
C
LEU
B1302
−33.065
−45.833
−27.143
9.92
C


ATOM
4426
O
LEU
B1302
−33.97
−46.117
−26.398
11.67
O


ATOM
4427
N
LEU
B1303
−31.895
−46.44
−27.111
11.44
N


ATOM
4428
CA
LEU
B1303
−31.592
−47.581
−26.212
14.3
C


ATOM
4429
CB
LEU
B1303
−30.298
−48.268
−26.624
12.85
C


ATOM
4430
CG
LEU
B1303
−30.486
−49.01
−27.953
17.01
C


ATOM
4431
CD1
LEU
B1303
−29.325
−49.927
−28.102
18.45
C


ATOM
4432
CD2
LEU
B1303
−31.815
−49.797
−28.015
16.49
C


ATOM
4433
C
LEU
B1303
−31.546
−47.25
−24.715
14.72
C


ATOM
4434
O
LEU
B1303
−31.279
−46.11
−24.356
14.39
O


ATOM
4435
N
GLN
B1304
−31.854
−48.245
−23.865
15.16
N


ATOM
4436
CA
GLN
B1304
−31.831
−47.99
−22.453
15.6
C


ATOM
4437
CB
GLN
B1304
−32.393
−49.143
−21.651
14.32
C


ATOM
4438
CG
GLN
B1304
−32.316
−48.821
−20.17
16.69
C


ATOM
4439
CD
GLN
B1304
−33.193
−49.657
−19.327
17.17
C


ATOM
4440
OE1
GLN
B1304
−33.604
−49.242
−18.239
20.26
O


ATOM
4441
NE2
GLN
B1304
−33.452
−50.876
−19.778
19.03
N


ATOM
4442
C
GLN
B1304
−30.407
−47.632
−22.036
16.11
C


ATOM
4443
O
GLN
B1304
−29.497
−48.327
−22.357
18.26
O


ATOM
4444
N
PRO
B1305
−30.193
−46.471
−21.426
16.5
N


ATOM
4445
CD
PRO
B1305
−31.101
−45.362
−21.151
15.37
C


ATOM
4446
CA
PRO
B1305
−28.853
−46.198
−20.991
17.68
C


ATOM
4447
CB
PRO
B1305
−28.946
−44.768
−20.507
17.49
C


ATOM
4448
CG
PRO
B1305
−30.161
−44.252
−21.136
17.86
C


ATOM
4449
C
PRO
B1305
−28.443
−47.116
−19.839
20
C


ATOM
4450
O
PRO
B1305
−29.298
−47.56
−19.067
19.29
O


ATOM
4451
N
GLU
B1306
−27.158
−47.439
−19.757
22.81
N


ATOM
4452
CA
GLU
B1306
−26.626
−48.241
−18.644
26.21
C


ATOM
4453
CB
GLU
B1306
−25.118
−48.456
−18.828
25.64
C


ATOM
4454
CG
GLU
B1306
−24.533
−49.314
−17.738
27.34
C


ATOM
4455
CD
GLU
B1306
−23.03
−49.575
−17.862
30.37
C


ATOM
4456
OE1
GLU
B1306
−22.589
−50.618
−17.295
36.66
O


ATOM
4457
OE2
GLU
B1306
−22.289
−48.75
−18.461
32.22
O


ATOM
4458
C
GLU
B1306
−26.871
−47.488
−17.331
27.16
C


ATOM
4459
O
GLU
B1306
−26.692
−46.268
−17.269
29.39
O


ATOM
4460
N
TYR
B1307
−27.253
−48.177
−16.268
27.98
N


ATOM
4461
CA
TYR
B1307
−27.544
−47.459
−14.999
28.39
C


ATOM
4462
CB
TYR
B1307
−26.449
−46.465
−14.617
30.07
C


ATOM
4463
CG
TYR
B1307
−25.01
−46.917
−14.645
32.11
C


ATOM
4464
CD1
TYR
B1307
−24.052
−46.15
−15.339
33.72
C


ATOM
4465
CE1
TYR
B1307
−22.695
−46.523
−15.342
33.05
C


ATOM
4466
CD2
TYR
B1307
−24.578
−48.076
−13.95
33.11
C


ATOM
4467
CE2
TYR
B1307
−23.218
−48.466
−13.973
34.52
C


ATOM
4468
CZ
TYR
B1307
−22.305
−47.662
−14.672
33.21
C


ATOM
4469
OH
TYR
B1307
−20.998
−47.985
−14.726
35.57
O


ATOM
4470
C
TYR
B1307
−28.861
−46.67
−14.974
27.38
C


ATOM
4471
O
TYR
B1307
−29.237
−46.121
−13.927
27.77
O


ATOM
4472
N
CYS
B1308
−29.532
−46.556
−16.106
25.63
N


ATOM
4473
CA
CYS
B1308
−30.936
−46.164
−16.106
24.55
C


ATOM
4474
CB
CYS
B1308
−31.397
−45.777
−17.483
22.73
C


ATOM
4475
SG
CYS
B1308
−33.095
−45.158
−17.55
23.51
S


ATOM
4476
C
CYS
B1308
−31.832
−47.271
−15.538
24.84
C


ATOM
4477
O
CYS
B1308
−31.897
−48.393
−16.081
23.68
O


ATOM
4478
N
PRO
B1309
−32.6
−46.935
−14.466
25.41
N


ATOM
4479
CD
PRO
B1309
−32.656
−45.647
−13.763
24.46
C


ATOM
4480
CA
PRO
B1309
−33.584
−47.895
−13.88
24.77
C


ATOM
4481
CB
PRO
B1309
−34.204
−47.104
−12.715
23.63
C


ATOM
4482
CG
PRO
B1309
−33.172
−46.086
−12.433
25.74
C


ATOM
4483
C
PRO
B1309
−34.642
−48.229
−14.909
24.26
C


ATOM
4484
O
PRO
B1309
−34.95
−47.377
−15.795
23.66
O


ATOM
4485
N
ASP
B1310
−35.19
−49.439
−14.799
24.29
N


ATOM
4486
CA
ASP
B1310
−36.185
−49.915
−15.796
24.2
C


ATOM
4487
CB
ASP
B1310
−36.631
−51.401
−15.563
26.57
C


ATOM
4488
CG
ASP
B1310
−35.495
−52.422
−15.751
29.97
C


ATOM
4489
OD1
ASP
B1310
−34.485
−52.019
−16.361
36.47
O


ATOM
4490
OD2
ASP
B1310
−35.597
−53.597
−15.263
30.68
O


ATOM
4491
C
ASP
B1310
−37.418
−49.003
−15.83
21.98
C


ATOM
4492
O
ASP
B1310
−37.941
−48.708
−16.926
21.91
O


ATOM
4493
N
PRO
B1311
−37.923
−48.602
−14.646
19.96
N


ATOM
4494
CD
PRO
B1311
−37.599
−49.016
−13.268
20.32
C


ATOM
4495
CA
PRO
B1311
−39.113
−47.777
−14.668
19.05
C


ATOM
4496
CB
PRO
B1311
−39.524
−47.708
−13.183
18.27
C


ATOM
4497
CG
PRO
B1311
−38.379
−48.115
−12.44
18.5
C


ATOM
4498
C
PRO
B1311
−38.918
−46.399
−15.249
17.86
C


ATOM
4499
O
PRO
B1311
−39.899
−45.735
−15.688
17.53
O


ATOM
4500
N
LEU
B1312
−37.67
−45.965
−15.271
16.14
N


ATOM
4501
CA
LEU
B1312
−37.465
−44.677
−15.858
16.38
C


ATOM
4502
CB
LEU
B1312
−36.183
−43.984
−15.37
16.29
C


ATOM
4503
CG
LEU
B1312
−36.067
−42.524
−15.792
16.08
C


ATOM
4504
CD1
LEU
B1312
−37.295
−41.659
−15.348
11.99
C


ATOM
4505
CD2
LEU
B1312
−34.769
−41.986
−15.207
17.66
C


ATOM
4506
C
LEU
B1312
−37.488
−44.812
−17.338
16.51
C


ATOM
4507
O
LEU
B1312
−38.021
−43.942
−17.987
18.01
O


ATOM
4508
N
TYR
B1313
−36.933
−45.913
−17.868
17.37
N


ATOM
4509
CA
TYR
B1313
−36.921
−46.179
−19.269
16.68
C


ATOM
4510
CB
TYR
B1313
−36.045
−47.372
−19.607
18.13
C


ATOM
4511
CG
TYR
B1313
−35.809
−47.569
−21.126
19.09
C


ATOM
4512
CD1
TYR
B1313
−35.4
−46.494
−21.925
17.61
C


ATOM
4513
CE1
TYR
B1313
−35.201
−46.641
−23.29
14.2
C


ATOM
4514
CD2
TYR
B1313
−36.056
−48.82
−21.769
17.57
C


ATOM
4515
CE2
TYR
B1313
−35.828
−48.972
−23.114
13.44
C


ATOM
4516
CZ
TYR
B1313
−35.396
−47.877
−23.866
15.63
C


ATOM
4517
OH
TYR
B1313
−35.189
−47.951
−25.217
17.24
O


ATOM
4518
C
TYR
B1313
−38.286
−46.441
−19.728
17.75
C


ATOM
4519
O
TYR
B1313
−38.61
−46.123
−20.875
18.79
O


ATOM
4520
N
GLU
B1314
−39.111
−47.023
−18.873
18.63
N


ATOM
4521
CA
GLU
B1314
−40.523
−47.214
−19.258
21.23
C


ATOM
4522
CB
GLU
B1314
−41.366
−48.074
−18.279
22.12
C


ATOM
4523
CG
GLU
B1314
−42.245
−49.17
−19.065
33.76
C


ATOM
4524
CD
GLU
B1314
−43.49
−48.606
−19.922
44.3
C


ATOM
4525
OE1
GLU
B1314
−43.455
−48.565
−21.212
43.29
O


ATOM
4526
OE2
GLU
B1314
−44.521
−48.207
−19.278
47.53
O


ATOM
4527
C
GLU
B1314
−41.229
−45.89 
−19.486
19.2
C


ATOM
4528
O
GLU
B1314
−42.049
−45.786
−20.418
18.94
O


ATOM
4529
N
VAL
B1315
−40.898
−44.905
−18.64
16.5
N


ATOM
4530
CA
VAL
B1315
−41.316
−43.504
−18.813
15.13
C


ATOM
4531
CB
VAL
B1315
−40.713
−42.501
−17.729
15.61
C


ATOM
4532
CG1
VAL
B1315
−41.278
−41.055
−17.932
14.24
C


ATOM
4533
CG2
VAL
B1315
−40.98
−43.034
−16.234
13.55
C


ATOM
4534
C
VAL
B1315
−40.922
−43.015
−20.153
14.83
C


ATOM
4535
O
VAL
B1315
−41.775
−42.65
−20.949
15.7
O


ATOM
4536
N
MET
B1316
−39.633
−43.05
−20.434
15.52
N


ATOM
4537
CA
MET
B1316
−39.114
−42.518
−21.691
17.71
C


ATOM
4538
CB
MET
B1316
−37.623
−42.804
−21.81
18.78
C


ATOM
4539
CG
MET
B1316
−36.714
−42.253
−20.696
17.64
C


ATOM
4540
SD
MET
B1316
−35.014
−42.678
−21.236
22.89
S


ATOM
4541
CE
MET
B1316
−34.237
−43.094
−19.653
17.64
C


ATOM
4542
C
MET
B1316
−39.821
−43.142
−22.882
16.73
C


ATOM
4543
O
MET
B1316
−40.287
−42.435
−23.76
17.39
O


ATOM
4544
N
LEU
B1317
−39.934
−44.469
−22.886
16.32
N


ATOM
4545
CA
LEU
B1317
−40.676
−45.179
−23.93
15.32
C


ATOM
4546
CB
LEU
B1317
−40.662
−46.667
−23.706
15.3
C


ATOM
4547
CG
LEU
B1317
−39.334
−47.379
−23.955
14.27
C


ATOM
4548
CD1
LEU
B1317
−39.561
−48.82
−23.47
8.02
C


ATOM
4549
CD2
LEU
B1317
−38.892
−47.248
−25.466
9.83
C


ATOM
4550
C
LEU
B1317
−42.099
−44.727
−24.053
14.63
C


ATOM
4551
O
LEU
B1317
−42.565
−44.533
−25.151
15.33
O


ATOM
4552
N
LYS
B1318
−42.787
−44.512
−22.949
14.75
N


ATOM
4553
CA
LYS
B1318
−44.142
−43.957
−23.059
16.87
C


ATOM
4554
CB
LYS
B1318
−44.887
−43.938
−21.685
18.94
C


ATOM
4555
CG
LYS
B1318
−45.16
−45.282
−21.027
19.41
C


ATOM
4556
CD
LYS
B1318
−46.49
−45.359
−20.291
25.33
C


ATOM
4557
CE
LYS
B1318
−46.597
−46.665
−19.415
28.28
C


ATOM
4558
NZ
LYS
B1318
−45.911
−46.56
−18.01
30.63
N


ATOM
4559
C
LYS
B1318
−44.077
−42.499
−23.668
16.78
C


ATOM
4560
O
LYS
B1318
−45.021
−42.028
−24.327
18.11
O


ATOM
4561
N
CYS
B1319
−42.999
−41.776
−23.414
14.19
N


ATOM
4562
CA
CYS
B1319
−42.924
−40.434
−23.935
14.09
C


ATOM
4563
CB
CYS
B1319
−41.718
−39.695
−23.331
14.7
C


ATOM
4564
SG
CYS
B1319
−41.84
−39.372
−21.566
11.89
S


ATOM
4565
C
CYS
B1319
−42.792
−40.447
−25.456
13.72
C


ATOM
4566
O
CYS
B1319
−43.091
−39.457
−26.064
13.34
O


ATOM
4567
N
TRP
B1320
−42.324
−41.566
−26.028
13.62
N


ATOM
4568
CA
TRP
B1320
−41.978
−41.687
−27.437
14.07
C


ATOM
4569
CB
TRP
B1320
−40.553
−42.252
−27.636
11.41
C


ATOM
4570
CG
TRP
B1320
−39.484
−41.481
−26.985
11.53
C


ATOM
4571
CD2
TRP
B1320
−38.262
−42.01
−26.378
15.7
C


ATOM
4572
CE2
TRP
B1320
−37.53
−40.897
−25.884
13.52
C


ATOM
4573
CE3
TRP
B1320
−37.735
−43.317
−26.194
8.48
C


ATOM
4574
CD1
TRP
B1320
−39.384
−40.132
−26.883
10.51
C


ATOM
4575
NE1
TRP
B1320
−38.257
−39.769
−26.169
9.79
N


ATOM
4576
CZ2
TRP
B1320
−36.315
−41.053
−25.226
11.01
C


ATOM
4577
CZ3
TRP
B1320
−36.609
−43.469
−25.541
8.17
C


ATOM
4578
CH2
TRP
B1320
−35.888
−42.337
−25.043
12.57
C


ATOM
4579
C
TRP
B1320
−42.987
−42.565
−28.133
15.9
C


ATOM
4580
O
TRP
B1320
−42.714
−43.143
−29.198
16.2
O


ATOM
4581
N
HIS
B1321
−44.173
−42.685
−27.532
17.08
N


ATOM
4582
CA
HIS
B1321
−45.261
−43.363
−28.185
15.92
C


ATOM
4583
CB
HIS
B1321
−46.5
−43.344
−27.347
14.2
C


ATOM
4584
CG
HIS
B1321
−47.434
−44.45
−27.703
19.14
C


ATOM
4585
CD2
HIS
B1321
−47.608
−45.684
−27.166
22.36
C


ATOM
4586
ND1
HIS
B1321
−48.269
−44.394
−28.79
26.22
N


ATOM
4587
CE1
HIS
B1321
−48.952
−45.526
−28.89
24.74
C


ATOM
4588
NE2
HIS
B1321
−48.567
−46.322
−27.911
23.76
N


ATOM
4589
C
HIS
B1321
−45.551
−42.714
−29.528
16.58
C


ATOM
4590
O
HIS
B1321
−45.591
−41.478
−29.617
18.29
O


ATOM
4591
N
PRO
B1322
−45.786
−43.53
−30.577
16.64
N


ATOM
4592
CD
PRO
B1322
−45.701
−45.007
−30.548
16.05
C


ATOM
4593
CA
PRO
B1322
−46.182
−43.061
−31.892
16.76
C


ATOM
4594
CB
PRO
B1322
−46.609
−44.369
−32.58
17.01
C


ATOM
4595
CG
PRO
B1322
−45.74
−45.372
−31.976
14.36
C


ATOM
4596
C
PRO
B1322
−47.376
−42.105
−31.842
17.71
C


ATOM
4597
O
PRO
B1322
−47.397
−41.119
−32.583
16.57
O


ATOM
4598
N
LYS
B1323
−48.366
−42.426
−30.988
18.6
N


ATOM
4599
CA
LYS
B1323
−49.609
−41.605
−30.857
20.46
C


ATOM
4600
CB
LYS
B1323
−50.852
−42.449
−30.599
20.9
C


ATOM
4601
CG
LYS
B1323
−50.822
−43.817
−31.131
26.18
C


ATOM
4602
CD
LYS
B1323
−51.711
−43.993
−32.377
33.01
C


ATOM
4603
CE
LYS
B1323
−52.13
−45.519
−32.59
36.06
C


ATOM
4604
NZ
LYS
B1323
−52.282
−45.886
−34.085
37.09
N


ATOM
4605
C
LYS
B1323
−49.494
−40.621
−29.71
19
C


ATOM
4606
O
LYS
B1323
−49.409
−41.013
−28.554
17.22
O


ATOM
4607
N
ALA
B1324
−49.491
−39.356
−30.06
19.16
N


ATOM
4608
CA
ALA
B1324
−49.339
−38.265
−29.085
20.18
C


ATOM
4609
CB
ALA
B1324
−49.562
−36.911
−29.773
19.6
C


ATOM
4610
C
ALA
B1324
−50.25
−38.408
−27.868
20.98
C


ATOM
4611
O
ALA
B1324
−49.836
−38.189
−26.728
21.38
O


ATOM
4612
N
GLU
B1325
−51.495
−38.801
−28.113
22.65
N


ATOM
4613
CA
GLU
B1325
−52.46
−38.931
−27.031
24.7
C


ATOM
4614
CB
GLU
B1325
−53.939
−38.946
−27.489
25.28
C


ATOM
4615
CG
GLU
B1325
−54.193
−38.902
−28.924
30.62
C


ATOM
4616
CD
GLU
B1325
−53.75
−40.2
−29.585
36.79
C


ATOM
4617
OE1
GLU
B1325
−53.291
−40.133
−30.771
36.59
O


ATOM
4618
OE2
GLU
B1325
−53.846
−41.257
−28.888
38.64
O


ATOM
4619
C
GLU
B1325
−52.186
−40.048
−26.063
23.25
C


ATOM
4620
O
GLU
B1325
−52.792
−40.066
−24.997
24.62
O


ATOM
4621
N
MET
B1326
−51.276
−40.945
−26.409
22.92
N


ATOM
4622
CA
MET
B1326
−50.868
−42.053
−25.54
23.34
C


ATOM
4623
CB
MET
B1326
−50.321
−43.185
−26.382
24.62
C


ATOM
4624
CG
MET
B1326
−51.294
−43.556
−27.446
32.3
C


ATOM
4625
SD
MET
B1326
−52.808
−44.354
−26.742
38.17
S


ATOM
4626
CE
MET
B1326
−52.914
−45.848
−27.84
34.43
C


ATOM
4627
C
MET
B1326
−49.748
−41.628
−24.606
21.64
C


ATOM
4628
O
MET
B1326
−49.332
−42.397
−23.7342
2.41
O


ATOM
4629
N
ARG
B1327
−49.245
−40.425
−24.821
18.28
N


ATOM
4630
CA
ARG
B1327
−48.081
−39.982
−24.146
16.16
C


ATOM
4631
CB
ARG
B1327
−47.379
−38.925
−24.998
14.09
C


ATOM
4632
CG
ARG
B1327
−46.835
−39.546
−26.213
13.42
C


ATOM
4633
CD
ARG
B1327
−45.957
−38.589
−26.997
13.18
C


ATOM
4634
NE
ARG
B1327
−45.905
−39.079
−28.352
11.83
N


ATOM
4635
CZ
ARG
B1327
−45.771
−38.322
−29.438
13.53
C


ATOM
4636
NH1
ARG
B1327
−45.625
−37.033
−29.301
13.63
N


ATOM
4637
NH2
ARG
B1327
−45.765
−38.877
−30.668
12.12
N


ATOM
4638
C
ARG
B1327
−48.55
−39.447
−22.818
15.22
C


ATOM
4639
O
ARG
B1327
−49.596
−38.751
−22.766
15.83
O


ATOM
4640
N
PRO
B1328
−47.788
−39.734
−21.739
14.57
N


ATOM
4641
CD
PRO
B1328
−46.543
−40.522
−21.631
15.56
C


ATOM
4642
CA
PRO
B1328
−48.155
−39.17
−20.447
14.81
C


ATOM
4643
CB
PRO
B1328
−47.009
−39.646
−19.526
14.49
C


ATOM
4644
CG
PRO
B1328
−45.89
−39.938
−20.437
14.09
C


ATOM
4645
C
PRO
B1328
−48.168
−37.63
−20.504
14.44
C


ATOM
4646
O
PRO
B1328
−47.362
−37.037
−21.186
14.21
O


ATOM
4647
N
SER
B1329
−49.061
−37.013
−19.76
15.23
N


ATOM
4648
CA
SER
B1329
−49.065
−35.577
−19.489
15.32
C


ATOM
4649
CB
SER
B1329
−50.377
−35.136
−18.769
16.24
C


ATOM
4650
OG
SER
B1329
−50.475
−35.595
−17.432
17.82
O


ATOM
4651
C
SER
B1329
−47.953
−35.272
−18.598
14.45
C


ATOM
4652
O
SER
B1329
−47.386
−36.189
−17.96
15.18
O


ATOM
4653
N
PHE
B1330
−47.618
−33.985
−18.5
15.11
N


ATOM
4654
CA
PHE
B1330
−46.528
−33.582
−17.536
13.94
C


ATOM
4655
CB
PHE
B1330
−46.061
−32.16
−17.801
12.57
C


ATOM
4656
CG
PHE
B1330
−45.132
−32.059
−18.97
67.65
C


ATOM
4657
CD1
PHE
B1330
−43.828
−32.576
−18.88
25.76
C


ATOM
4658
CD2
PHE
B1330
−45.551
−31.446
−20.148
3.23
C


ATOM
4659
CE1
PHE
B1330
−42.976
−32.543
−19.978
9.3
C


ATOM
4660
CE2
PHE
B1330
−44.681
−31.378
−21.294
5.74
C


ATOM
4661
CZ
PHE
B1330
−43.408
−31.926
−21.219
6.8
C


ATOM
4662
C
PHE
B1330
−46.793
−33.884
−16.06
14.54
C


ATOM
4663
O
PHE
B1330
−45.891
−34.202
−15.333
14.93
O


ATOM
4664
N
SER
B1331
−48.054
−33.866
−15.675
16.48
N


ATOM
4665
CA
SER
B1331
−48.5
−34.249
−14.339
18.67
C


ATOM
4666
CB
SER
B1331
−50.03
−34.095
−14.237
19.21
C


ATOM
4667
OG
SER
B1331
−50.368
−32.723
−14.292
22.71
O


ATOM
4668
C
SER
B1331
−48.175
−35.696
−14.026
19.57
C


ATOM
4669
O
SER
B1331
−47.687
−35.99
−12.934
20.05
O


ATOM
4670
N
GLU
B1332
−48.47
−36.604
−14.96
19.67
N


ATOM
4671
CA
GLU
B1332
−48.151
−38.023
−14.72
20.35
C


ATOM
4672
CB
GLU
B1332
−48.712
−38.922
−15.844
21.1
C


ATOM
4673
CG
GLU
B1332
−49.989
−38.333
−16.37
25.88
C


ATOM
4674
CD
GLU
B1332
−50.609
−39.105
−17.505
32.07
C


ATOM
4675
OE1
GLU
B1332
−50.996
−40.266
−17.25
37.09
O


ATOM
4676
OE2
GLU
B1332
−50.743
−38.557
−18.626
29.37
O


ATOM
4677
C
GLU
B1332
−46.666
−38.179
−14.629
17.39
C


ATOM
4678
O
GLU
B1332
−46.157
−38.872
−13.803
18.56
O


ATOM
4679
N
LEU
B1333
−45.962
−37.512
−15.49
17.55
N


ATOM
4680
CA
LEU
B1333
−44.492
−37.546
−15.487
17
C


ATOM
4681
CB
LEU
B1333
−43.952
−36.584
−16.542
16.13
C


ATOM
4682
CG
LEU
B1333
−43.485
−37.135
−17.893
16.66
C


ATOM
4683
CD1
LEU
B1333
−43.469
−38.652
−18.04
11.84
C


ATOM
4684
CD2
LEU
B1333
−44.25
−36.425
−18.993
15.31
C


ATOM
4685
C
LEU
B1333
−43.949
−37.147
−14.136
17.56
C


ATOM
4686
O
LEU
B1333
−43.079
−37.842
−13.573
17.14
O


ATOM
4687
N
VAL
B1334
−44.455
−36.034
−13.593
17.51
N


ATOM
4688
CA
VAL
B1334
−43.955
−35.678
−12.272
18.47
C


ATOM
4689
CB
VAL
B1334
−44.143
−34.153
−11.829
18.11
C


ATOM
4690
CG1
VAL
B1334
−44.442
−33.243
−13.018
14.01
C


ATOM
4691
CG2
VAL
B1334
−45.126
−34.083
−10.693
15.6
C


ATOM
4692
C
VAL
B1334
−44.396
−36.63
−11.139
19.77
C


ATOM
4693
O
VAL
B1334
−43.644
−36.832
−10.142
19.19
O


ATOM
4694
N
SER
B1335
−45.588
−37.22
−11.291
19.42
N


ATOM
4695
CA
SER
B1335
−45.993
−38.174
−10.308
20.01
C


ATOM
4696
CB
SER
B1335
−47.422
−38.604
−10.5
19.55
C


ATOM
4697
OG
SER
B1335
−48.127
−37.893
−9.525
24.31
O


ATOM
4698
C
SER
B1335
−45.084
−39.35
−10.397
20.57
C


ATOM
4699
O
SER
B1335
−44.477
−39.799
−9.382
22.6
O


ATOM
4700
N
ARG
B1336
−44.932
−39.81
−11.615
19.14
N


ATOM
4701
CA
ARG
B1336
−44.274
−41.073
−11.816
20.87
C


ATOM
4702
CB
ARG
B1336
−44.554
−41.564
−13.257
21.65
C


ATOM
4703
CG
ARG
B1336
−43.906
−42.881
−13.563
25.26
C


ATOM
4704
CD
ARG
B1336
−44.784
−44.042
−13.136
30.89
C


ATOM
4705
NE
ARG
B1336
−43.944
−45.064
−12.524
34.5
N


ATOM
4706
CZ
ARG
B1336
−44.048
−45.462
−11.251
37.83
C


ATOM
4707
NH1
ARG
B1336
−43.176
−46.392
−10.831
34.4
N


ATOM
4708
NH2
ARG
B1336
−45.001
−44.926
−10.416
33
N


ATOM
4709
C
ARG
B1336
−42.772
−40.978
−11.488
19.91 
C


ATOM
4710
O
ARG
B1336
−42.178
−41.918
−10.906
20.62
O


ATOM
4711
N
ILE
B1337
−42.183
−39.828
−11.823
17.75
N


ATOM
4712
CA
ILE
B1337
−40.813
−39.639
−11.58
17.06
C


ATOM
4713
CB
ILE
B1337
−40.183
−38.583
−12.531
17.62
C


ATOM
4714
CG2
ILE
B1337
−38.69
−38.364
−12.157
16.92
C


ATOM
4715
CG1
ILE
B1337
−40.247
−39.011
−14.001
16.78
C


ATOM
4716
CD1
ILE
B1337
−40.004 
−37.848
−15.033
17.27
C


ATOM
4717
C
ILE
B1337
−40.514
−39.39
−10.072
17.05
C


ATOM
4718
O
ILE
B1337
−39.44
−39.766
−9.582
16.58
O


ATOM
4719
N
SER
B1338
−41.446
−38.791
−9.323
17.74
N


ATOM
4720
CA
SER
B1338
−41.214
−38.622
−7.839
19.11
C


ATOM
4721
CB
SER
B1338
−42.322
−37.796
−7.116
18.77
C


ATOM
4722
OG
SER
B1338
−42.68
−36.632
−7.87
21.59
O


ATOM
4723
C
SER
B1338
−41.086
−39.958
−7.155 
17.75 
C


ATOM
4724
O
SER
B1338
−40.175
−40.172
−6.406
18.2
O


ATOM
4725
N
ALA
B1339
−42.03
−40.827
−7.479
18.2
N


ATOM
4726
CA
ALA
B1339
−42.127
−42.207
−7.068
17.95
C


ATOM
4727
CB
ALA
B1339
−43.227
−42.836
−7.861
16.27
C


ATOM
4728
C
ALA
B1339
−40.84
−42.941
−7.32
19.39
C


ATOM
4729
O
ALA
B1339
−40.314
−43.655
−6.409
21.18
O


ATOM
4730
N
ILE
B1340
−40.301
−42.781
−8.552
20.07
N


ATOM
4731
CA
ILE
B1340
−39.065
−43.48
−8.95
17.93
C


ATOM
4732
CB
ILE
B1340
−38.853
−43.383
−10.432
17.93
C


ATOM
4733
CG2
ILE
B1340
−37.443
−43.926
−10.849
16.49
C


ATOM
4734
CG1
ILE
B1340
−39.964
−44.074
−11.175
17.37
C


ATOM
4735
CD1
ILE
B1340
−39.847
−44.016
−12.777
16.33
C


ATOM
4736
C
ILE
B1340
−37.884
−42.87
−8.179
18.75
C


ATOM
4737
O
ILE
B1340
−36.949
−43.573
−7.793
17.26
O


ATOM
4738
N
PHE
B1341
−37.965
−41.545
−7.969
20.47
N


ATOM
4739
CA
PHE
B1341
−36.935
−40.757
−7.283
20.98
C


ATOM
4740
CB
PHE
B1341
−37.206
−39.264
−7.419
19.62
C


ATOM
4741
CG
PHE
B1341
−36.215
−38.396
−6.69
17.4
C


ATOM
4742
CD1
PHE
B1341
−34.924
−38.216
−7.209
18.52
C


ATOM
4743
CD2
PHE
B1341
−36.562
−37.789
−5.463
15.18
C


ATOM
4744
CE1
PHE
B1341
−33.962
−37.381
−6.529
22.53
C


ATOM
4745
CE2
PHE
B1341
−35.657
−36.973
−4.732
19.9
C


ATOM
4746
CZ
PHE
B1341
−34.31
−36.737
−5.272
21.72
C


ATOM
4747
C
PHE
B1341
−36.898
−41.127
−5.827
23.05
C


ATOM
4748
O
PHE
B1341
−35.809
−41.317
−5.277
23.42
O


ATOM
4749
N
SER
B1342
−38.062
−41.212
−5.201
25.6
N


ATOM
4750
CA
SER
B1342
−38.149
−41.713
−3.819
31.43
C


ATOM
4751
CB
SER
B1342
−39.567
−41.807
−3.363
31.39
C


ATOM
4752
OG
SER
B1342
−39.717
−40.757
−2.434
36.05
O


ATOM
4753
C
SER
B1342
−37.516
−43.06
−3.501
34.23
C


ATOM
4754
O
SER
B1342
−36.693
−43.154
−2.57
35.16
O


ATOM
4755
N
THR
B1343
−37.901
−44.101
−4.257
36.83
N


ATOM
4756
CA
THR
B1343
−37.229
−45.397
−4.165
38.38
C


ATOM
4757
CB
THR
B1343
−37.554
−46.287
−5.308
38.54
C


ATOM
4758
OG1
THR
B1343
−36.597
−46.025
−6.353
38.96
O


ATOM
4759
CG2
THR
B1343
−38.995
−46.003
−5.763
37.89
C


ATOM
4760
C
THR
B1343
−35.742
−45.266
−4.224
39.74
C


ATOM
4761
O
THR
B1343
−35.032
−46.224
−3.938
41.03
O


ATOM
4762
N
PHE
B1344
−35.233
−44.1
−4.58
41.26
N


ATOM
4763
CA
PHE
B1344
−33.799
−44.038
−4.73
42.8
C


ATOM
4764
CB
PHE
B1344
−33.345
−43.216
−5.903
41.57
C


ATOM
4765
CG
PHE
B1344
−32.811
−44.036
−6.983
38.68
C


ATOM
4766
CD1
PHE
B1344
−33.674
−44.636
−7.897
39.26
C


ATOM
4767
CD2
PHE
B1344
−31.458
−44.289
−7.056
35.03
C


ATOM
4768
CE1
PHE
B1344
−33.166
−45.431
−8.921
37.52
C


ATOM
4769
CE2
PHE
B1344
−30.932
−45.052
−8.046
33.41
C


ATOM
4770
CZ
PHE
B1344
−31.769
−45.642
−8.984
38.56
C


ATOM
4771
C
PHE
B1344
−32.936
−43.789
−3.544
45.59
C


ATOM
4772
O
PHE
B1344
−33.206
−42.962
−2.646
45.42
O


ATOM
4773
N
ILE
B1345
−31.827
−44.505
−3.656
49.05
N


ATOM
4774
CA
ILE
B1345
−30.833
−44.778
−2.628
51.82
C


ATOM
4775
CB
ILE
B1345
−31.443
−44.651
−1.138
52.15
C


ATOM
4776
CG2
ILE
B1345
−32.243
−45.949
−0.677
53.65
C


ATOM
4777
CG1
ILE
B1345
−30.429
−44.02
−0.126
52.44
C


ATOM
4778
CD1
ILE
B1345
−29.161
−44.87
60.167
49.33
C


ATOM
4779
C
ILE
B1345
−30.383
−46.197
−3.124
53.09
C


ATOM
4780
O
ILE
B1345
−29.175
−46.436
−3.442
53.28
O


ATOM
4781
N
GLY
B1346
−31.38
−47.09
−3.271
53.8
N


ATOM
4782
CA
GLY
B1346
−31.227
−48.359
−3.998
54.24
C


ATOM
4783
C
GLY
B1346
−32.269
−48.514
−5.109
54.24
C


ATOM
4784
O
GLY
B1346
−32.572
−47.603
−5.915
53.17
O


ATOM
4785
OXT
GLY
B1346
−32.842
−49.608
−5.198
54.15
O


ATOM
4786
C18
M97
C1
−6.757
10.413
1.931
13.34
C


ATOM
4787
C17
M97
C1
−6.821
11.541
2.986
11.83
C


ATOM
4788
C16
M97
C1
−5.784
12.663
2.878
15.81
C


ATOM
4789
C15
M97
C1
−5.684
13.145
1.409
17.14
C


ATOM
4790
C23
M97
C1
−5.215
14.43
1.015
15.54
C


ATOM
4791
C22
M97
C1
−5.141
14.811
−0.321
12.44
C


ATOM
4792
C21
M97
C1
−5.545
13.904
−1.323
14.75
C


ATOM
4793
C20
M97
C1
−6.025
12.648
−0.947
16.78
C


ATOM
4794
C19
M97
C1
−6.1
12.29
0.385
17.2
C


ATOM
4795
N3
M97
C1
−6.631
10.999
0.557
13.75
N


ATOM
4796
C3
M97
C1
−6.844
10.562
−0.666
13.83
C


ATOM
4797
C2
M97
C1
−6.514
11.51
−1.566
17.04
C


ATOM
4798
C6
M97
C1
−6.692
11.372
−3.093
13.93
C


ATOM
4799
C8
M97
C1
−5.475
11.814
−3.914
12.39
C


ATOM
4800
O2
M97
C1
−4.314
11.482
−3.73
11.64
O


ATOM
4801
N2
M97
C1
−5.811
12.562
−4.949
13.09
N


ATOM
4802
C7
M97
C1
−7.135
12.751
−4.996
13.15
C


ATOM
4803
O1
M97
C1
−7.643
13.406
−5.899
12.05
O


ATOM
4804
C1
M97
C1
−7.819
12.181
−3.728
14.16
C


ATOM
4805
C4
M97
C1
−9.155
11.566
−3.893
16.46
C


ATOM
4806
C10
M97
C1
−10.106
11.501
−2.902
16.63
C


ATOM
4807
C11
M97
C1
−10.181
11.877
−1.578
21.54
C


ATOM
4808
C12
M97
C1
−11.335
11.655
−0.794
16.81
C


ATOM
4809
C13
M97
C1
−12.39
11.019
−1.396
15.57
C


ATOM
4810
C14
M97
C1
−12.336
10.641
−2.722
16.22
C


ATOM
4811
C9
M97
C1
−11.197
10.875
−3.485
17.96
C


ATOM
4812
N1
M97
C1
−10.896
10.615
−4.784
18.43
N


ATOM
4813
C5
M97
C1
−9.655
11.061
−5.036
19.08
C


ATOM
4814
C18
M97
D1
−27.796
−19.375
−23.523
24.48
C


ATOM
4815
C17
M97
D1
−27.404
−18.301
−24.565
25.28
C


ATOM
4816
C16
M97
D1
−28.222
−17.006
−24.512
22.55
C


ATOM
4817
C15
M97
D1
−28.24
−16.516
−23.076
22.61
C


ATOM
4818
C23
M97
D1
−28.488
−15.163
−22.754
23.09
C


ATOM
4819
C22
M97
D1
−28.498
−14.791
−21.391
24.77
C


ATOM
4820
C21
M97
D1
−28.295
−15.729
−20.363
22.55
C


ATOM
4821
C20
M97
D1
−28.099
−17.062
−20.721
19.7
C


ATOM
4822
C19
M97
D1
−28.082
−17.41
−22.029
19.61
C


ATOM
4823
N3
M97
D1
−27.855
−18.769
−22.162
22.53
N


ATOM
4824
C3
M97
D1
−27.736
−19.275
−20.961
22.1
C


ATOM
4825
C2
M97
D1
−27.884
−18.269
−20.099
21.74
C


ATOM
4826
C6
M97
D1
−27.783
−18.535
−18.611
22.97
C


ATOM
4827
C8
M97
D1
−28.6
−17.631
−17.729
21.97
C


ATOM
4828
O2
M97
D1
−29.818
−17.491
−17.8
24.31
O


ATOM
4829
N2
M97
D1
−27.842
−17.074
−16.78
24.76
N


ATOM
4830
C7
M97
D1
−26.556
−17.369
−16.9
22.86
C


ATOM
4831
O1
M97
D1
−25.701
−16.934
−16.141
24.63
O


ATOM
4832
C1
M97
D1
−26.415
−18.195
−18.118
26.09
C


ATOM
4833
C4
M97
D1
−25.204
−18.618
−18.914
28.08
C


ATOM
4834
C10
M97
D1
−24.147
−19.415
−18.721
27.23
C


ATOM
4835
C11
M97
D1
−23.744
−20.094
−17.651
29.15
C


ATOM
4836
C12
M97
D1
−22.572
−20.813
−17.843
30.82
C


ATOM
4837
C13
M97
D1
−21.838
−20.791
−19.03
29.97
C


ATOM
4838
C14
M97
D1
−22.247
−20.076
−20.127
28.69
C


ATOM
4839
C9
M97
D1
−23.408
−19.39
−19.928
30.21
C


ATOM
4840
N1
M97
D1
−24.007
−18.618
−20.83
132.6
N


ATOM
4841
C5
M97
D1
−25.078
−18.18
−20.18
133.7
C


ATOM
4842
O
HOH
Fl
−29.32
−45.647
−32.002
16.53
O


ATOM
4843
O
HOH
F5
6.241
−1.313
7.848
9.44
O


ATOM
4844
O
HOH
F6
9.31
−0.294
−12.45
10.96
O


ATOM
4845
O
HOH
F8
−0.518
−17.255
−13.443
12.19
O


ATOM
4846
O
HOH
F11
−41.781
−18.635
−8.479
18.73
O


ATOM
4847
O
HOH
F13
−7.464
−2.012
15.403
16.58
O


ATOM
4848
O
HOH
F15
14.609
−0.995
6.201
11.01
O


ATOM
4849
O
HOH
F16
8.312
34.844
14.609
21.07
O


ATOM
4850
O
HOH
F17
3.508
8.749
−10.788
15.51
O


ATOM
4851
O
HOH
F18
14.725
−4.454
5.272
30.25
O


ATOM
4852
O
HOH
F19
−13.905
−9.795
−22.444
15.68
O


ATOM
4853
O
HOH
F21
−42.866
−29.624
−28.883
28.13
O


ATOM
4854
O
HOH
F22
−26.774
−0.392
−19.528
11.42
O


ATOM
4855
O
HOH
F23
−11.848
−12.69
−13.164
37.75
O


ATOM
4856
O
HOH
F24
4.702
−18.668
−5.903
19.11
O


ATOM
4857
O
HOH
F25
−33.344
−32.268
−6.818
31.15
O


ATOM
4858
O
HOH
F26
−25.708
−43.353
−8.875
20.32
O


ATOM
4859
O
HOH
F29
−45.908
−39.581
−34.22
19.74
O


ATOM
4860
O
HOH
F30
−30.706
−12.15
−30.792
11.84
O


ATOM
4861
O
HOH
F31
−33.571
−22.557
−28.722
29.36
O


ATOM
4862
O
HOH
F33
−50.609
−28.235
−27.266
30.52
O


ATOM
4863
O
HOH
F34
−27.54
−39.356
−4.277
23.05
O


ATOM
4864
O
HOH
F38
−16.68
−38.138
−14.134
19.08
O


ATOM
4865
O
HOH
F41
−8.258
−22.143
−2.471
21.09
O


ATOM
4866
O
HOH
F42
−6.61
−0.884
3.132
4.31
O


ATOM
4867
O
HOH
F43
−37.744
−19.121
−10.97
9.19
O


ATOM
4868
O
HOH
F44
−13.126
9.645
−6.048
28.15
O


ATOM
4869
O
HOH
F47
−20.145
−18.005
−8.987
50.58
O


ATOM
4870
O
HOH
F48
10.711
2.092
12.972
21.72
O


ATOM
4871
O
HOH
F49
−36.132
−38.07
−31.15
16.14
O


ATOM
4872
O
HOH
F51
−35.488
−29.638
−28.278
11.04
O


ATOM
4873
O
HOH
F52
14.842
−11.981
10.718
30.87
O


ATOM
4874
O
HOH
F55
−35.382
−49.541
−30.387
26.91
O


ATOM
4875
O
HOH
F56
−11.404
−13.613
12.021
10.79
O


ATOM
4876
O
HOH
F59
0.123
−4.338
−14.067
16.42
O


ATOM
4877
O
HOH
F61
2.695
29
−0.436
14.27
O


ATOM
4878
O
HOH
F63
−17.953
−3.003
−15.671
12.17
O


ATOM
4879
O
HOH
F65
−36.272
−14.628
−12.624
12.14
O


ATOM
4880
O
HOH
F66
−37.039
−52.238
−39.018
10.87
O


ATOM
4881
O
HOH
F68
−1.256
−13.25
7.793
7.61
O


ATOM
4882
O
HOH
F69
13.93
−6.17
1.302
7.23
O


ATOM
4883
O
HOH
F74
−21.281
−26.8
−15.829
36.75
O


ATOM
4884
O
HOH
F75
−8.945
−12.697
−14.696
15.11
O


ATOM
4885
O
HOH
F78
−41.02
−15.364
−18.372
32.16
O


ATOM
4886
O
HOH
F79
2.29
10.714
−1.259
16.47
O


ATOM
4887
O
HOH
F80
−48.619
−49.393
−27.169
27.17
O


ATOM
4888
O
HOH
F81
−49.904
−38.791
−33.25
27.2
O


ATOM
4889
O
HOH
F82
−13.586
−12.029
−4.742
30.12
O


ATOM
4890
O
HOH
F84
15.912
−6.318
−3.476
24.03
O


ATOM
4891
O
HOH
F86
−8.824
20.746
3.879
17.29
O


ATOM
4892
O
HOH
F87
−0.697
−8.031
11.805
9.36
O


ATOM
4893
O
HOH
F89
−48.633
−6.161
−17.326
10.19
O


ATOM
4894
O
HOH
F90
−42.9
−45.555
−34.406
17.72
O


ATOM
4895
O
HOH
F92
11.987
−1.35
20.511
35.19
O


ATOM
4896
O
HOH
F93
−28.968
−46.992
−11.157
38.03
O


ATOM
4897
O
HOH
F94
19.165
5.56
−3.202
13.7
O


ATOM
4898
O
HOH
F95
−10.566
−5.79
−17.051
15.61
O


ATOM
4899
O
HOH
F98
−36.062
−17.343
−13.063
5.49
O


ATOM
4900
O
HOH
F99
−32.503
−51.224
−24.017
10.16
O


ATOM
4901
O
HOH
F103
9.945
0.105
2.08
15.57
O


ATOM
4902
O
HOH
F106
4.418
−17.639
13.148
16.93
O


ATOM
4903
O
HOH
F107
−45.986
−2.509
−16.086
15.03
O


ATOM
4904
O
HOH
F109
−2.683
−19.25
−13.776
28.45
O


ATOM
4905
O
HOH
F110
−4.254
−4.332
−13.533
18.93
O


ATOM
4906
O
HOH
F111
−11.1
6.177
−16.231
25.82
O


ATOM
4907
O
HOH
F113
−27.258
−24.151
−30.7
14.97
O


ATOM
4908
O
HOH
F118
−11.233
12.9
−14.378
51.8
O


ATOM
4909
O
HOH
F119
−40.043
−29.384
−26.812
7.78
O


ATOM
4910
O
HOH
F122
−27.638
−41.749
−41.794
20.81
O


ATOM
4911
O
HOH
F123
−37.295
−51.413
−19.137
29.17
O


ATOM
4912
O
HOH
F127
12.353
29.785
0.805
34.63
O


ATOM
4913
O
HOH
F132
−46.845
−25.3
−34.335
18.55
O


ATOM
4914
O
HOH
F133
−10.658
24.394
−8.533
13.92
O


ATOM
4915
O
HOH
F135
−27.625
−23.545
−23.649
23.5
O


ATOM
4916
O
HOH
F139
−7.482
−18.693
−10.139
26.8
O


ATOM
4917
O
HOH
F140
−37.308
3.619
−35.119
10.72
O


ATOM
4918
O
HOH
F141
−9.487
−12.65
7.885
27.37
O


ATOM
4919
O
HOH
F147
−14.473
−15.515
−13.357
28.23
O


ATOM
4920
O
HOH
F151
−49.253
−31.734
−19.766
12.77
O


ATOM
4921
O
HOH
F152
−33.874
−21.649
−26.009
35.39
O


ATOM
4922
O
HOH
F160
−27.074
−43.992
−33.171
26.02
O


ATOM
4923
O
HOH
F162
−1.216
−8.886
9.489
6.68
O


ATOM
4924
O
HOH
F163
−8.684
−9.212
−17.193
20.8
O


ATOM
4925
O
HOH
F164
−24.704
−27.369
−24.384
23.89
O


ATOM
4926
O
HOH
F165
10.661
−0.274
−9.633
19.75
O


ATOM
4927
O
HOH
F167
−39.405
−17
−10.792
13.52
O


ATOM
4928
O
HOH
F171
−19.563
−0.808
−17.608
25.97
O


ATOM
4929
O
HOH
F175
−1.316
6.842
6.302
30.22
O


ATOM
4930
O
HOH
F181
−23.672
−36.748
−6.006
33.39
O


ATOM
4931
O
HOH
F187
−19.483
18.366
1.47
18.85
O


ATOM
4932
O
HOH
F191
−20.833
−30.336
−23.71
17.88
O


ATOM
4933
O
HOH
F192
−23.256
−24.86
−6.405
25.34
O


ATOM
4934
O
HOH
F195
−27.943
−43.121
−7.194
24.93
O


ATOM
4935
O
HOH
F196
−9.437
−4.406
3.163
32.85
O


ATOM
4936
O
HOH
F199
−14.351
−15.223
−16.592
35.52
O


ATOM
4937
O
HOH
F201
−28.051
−20.14
−37.061
2.96
O


ATOM
4938
O
HOH
F204
13.399
−2.13
13.08
38.46
O


ATOM
4939
O
HOH
F206
−0.623
6.957
−15.231
43.14
O


ATOM
4940
O
HOH
F209
3.949
29.41
−7.507
9.37
O


ATOM
4941
O
HOH
F214
−4.368
13.84
−12.583
17.62
O


ATOM
4942
O
HOH
F216
−38.765
−22.875
−29.099
25.73
O


ATOM
4943
O
HOH
F220
4.401
7.618
−0.759
21.38
O


ATOM
4944
O
HOH
F224
−46.22
−27.713
−23.131
21.06
O


ATOM
4945
O
HOH
F232
−17.824
−0.269
1.213
29.39
O


ATOM
4946
O
HOH
F234
−41.265
−32.211
−31.685
23.51
O


ATOM
4947
O
HOH
F236
14.698
−0.179
1.827
20.96
O


ATOM
4948
O
HOH
F238
−16.579
11.275
−2.474
28.52
O


ATOM
4949
O
HOH
F239
−36.288
−36.794
−42.538
29.54
O


ATOM
4950
O
HOH
F243
−28.661
−43.161
−29.758
16.75
O


ATOM
4951
O
HOH
F244
−36.382
−42.158
−29.189
16.52
O


ATOM
4952
O
HOH
F245
−8.091
−23.484
0.658
15.9
O


ATOM
4953
O
HOH
F256
−47.173
−21.426
−26.921
17.64
O


ATOM
4954
O
HOH
F264
10.977
−5.747
10.557
16.36
O


ATOM
4955
O
HOH
F267
−36.06
1.427
−13.036
40.7
O


ATOM
4956
O
HOH
F268
11.515
6.152
5.718
11.46
O


ATOM
4957
O
HOH
F269
−6.05
34.979
5.439
23.66
O


ATOM
4958
O
HOH
F271
−8.98
−0.279
5.32
15.75
O


ATOM
4959
O
HOH
F276
2.974
11.07
9.919
22.17
O


ATOM
4960
O
HOH
F278
−14.111
−9.961
6.282
44.67
O


ATOM
4961
O
HOH
F279
−29.218
−45.75
−28.633
11.2
O


ATOM
4962
O
HOH
F282
−42.477
−21.253
−27.923
18.5
O


ATOM
4963
O
HOH
F283
−34.014
−4.394
2.354
12.22
O


ATOM
4964
O
HOH
F284
4.7
22.988
−7.778
23.08
O


ATOM
4965
O
HOH
F289
−8.366
−21.818
2.824
18.62
O


ATOM
4966
O
HOH
F290
1.692
9.464
29.595
34.19
O


ATOM
4967
O
HOH
F291
−23.192
−11.572
−29.113
40.34
O


ATOM
4968
O
HOH
F293
−48.105
−36.996
−38.885
30.74
O


ATOM
4969
O
HOH
F298
−24.065
−44.956
−29.789
44.17
O


ATOM
4970
O
HOH
F299
−17.055
−9.208
8.875
44.85
O


ATOM
4971
O
HOH
F310
−10.136
18.804
6.712
30.24
O


ATOM
4972
O
HOH
F311
−11.822
24.153
−6.297
18.14
O


ATOM
4973
O
HOH
F316
9.546
31.815
−11.844
9.61
O


ATOM
4974
O
HOH
F317
11.95
30.507
−11.564
11.26
O


ATOM
4975
O
HOH
F321
−6.987
10.303
−12.194
12.61
O


ATOM
4976
O
HOH
F323
−8.229
12.163
−14.579
17.55
O


ATOM
4977
O
HOH
F324
3.683
−0.89
5.686
18.78
O


ATOM
4978
O
HOH
F325
−11.488
−14.186
−3.45
20.66
O


ATOM
4979
O
HOH
F327
−11.968
−13.195
7.446
33.2
O


ATOM
4980
O
HOH
F328
−16.3
−13.463
9.956
22.62
O


ATOM
4981
O
HOH
F329
−9.272
−14.428
11.275
15.93
O


ATOM
4982
O
HOH
F330
−1.857
−22.856
−1.675
31.54
O


ATOM
4983
O
HOH
F331
11.811
−10.851
12.466
27.69
O


ATOM
4984
O
HOH
F332
15.961
−8.575
7.8
18.32
O


ATOM
4985
O
HOH
F333
18.235
−17.932
8.891
22.9
O


ATOM
4986
O
HOH
F340
−24.46
−9.744
−25.665
12.78
O


ATOM
4987
O
HOH
F342
−27.314
−21.134
−29.776
13.86
O


ATOM
4988
O
HOH
F348
−40.626
−30.693
−29.559
28.67
O


ATOM
4989
O
HOH
F351
−9.41
−15.753
7.013
14
O


ATOM
4990
O
HOH
F352
−32.049
−50.283
−33.663
35.95
O


ATOM
4991
O
HOH
F356
−18.866
−15.309
−30.177
24.26
O


ATOM
4992
O
HOH
F358
−33.287
−55.033
−37.052
9.53
O


ATOM
4993
O
HOH
F359
4.652
−3.504
10.226
33.1
O


ATOM
4994
O
HOH
F360
−31.099
−32.445
−33.508
5.43
O


ATOM
4995
O
HOH
F361
5.952
9.627
−8.466
18.68
O


ATOM
4996
O
HOH
F362
12.851
−5.168
−0.578
11.64
O


ATOM
4997
O
HOH
F363
−31.321
−33.548
−8.199
25.88
O


ATOM
4998
O
HOH
F365
−14.509
−15.416
−24.15
28.59
O


ATOM
4999
O
HOH
F368
−12.027
4.182
−4.641
5.68
O


ATOM
5000
O
HOH
F372
2.882
−3.106
−13.774
28.16
O


ATOM
5001
O
HOH
F373
−38.023
−25.397
−32.152
17.02
O


ATOM
5002
O
HOH
F374
11.155
−20.718
−4.4
29.01
O


ATOM
5003
O
HOH
F376
−10.556
7.527
−1.55
18.42
O


ATOM
5004
O
HOH
F377
−48.85
−18.397
−12.457
12.98
O


ATOM
5005
O
HOH
F380
−36.569
−37.246
−33.524
11.2
O


ATOM
5006
O
HOH
F381
−24.863
−41.265
−28.065
25.79
O


ATOM
5007
O
HOH
F383
−45.552
−0.183
−14.246
21.66
O


ATOM
5008
O
HOH
F384
4.701
−21.598
−7.352
26.64
O


ATOM
5009
O
HOH
F386
−0.6
−0.52
6.816
31.53
O


ATOM
5010
O
HOH
F387
−10.111
−2.953
5.26
17.96
O


ATOM
5011
O
HOH
F388
−25.049
−17.468
−7.969
32.9
O


ATOM
5012
O
HOH
F389
−26.332
−11.606
−6.498
36.6
O


ATOM
5013
O
HOH
F391
14.913
−6.481
8.487
36.2
O


ATOM
5014
O
HOH
F394
16.259
−15.826
−6.447
37.58
O


ATOM
5015
O
HOH
F395
−9.203
4.244
6.795
17.76
O


ATOM
5016
O
HOH
F396
−40.086
0.372
−8.964
21.08
O


ATOM
5017
O
HOH
F398
16.994
−6.858
0.059
42.45
O


ATOM
5018
O
HOH
F402
2.118
−1.406
8.674
16.11
O


ATOM
5019
O
HOH
F405
0.837
9.273
11.254
24.81
O


ATOM
5020
O
HOH
F407
3.045
12.282
−8.946
33.67
O


ATOM
5021
O
HOH
F410
−51.076
−26.098
−29.893
35.22
O


ATOM
5022
O
HOH
F413
5.628
−20.263
13.119
19.98
O


ATOM
5023
O
HOH
F414
−3.942
17.588
8.986
20.79
O


ATOM
5024
O
HOH
F415
−4.646
12.122
15.494
35.45
O


ATOM
5025
O
HOH
F420
−21.567
−21.045
−15.42
45.94
O


ATOM
5026
O
HOH
F421
−33.27
−1.351
−28.007
16.96
O


ATOM
5027
O
HOH
F422
−33.732
−14.336
−37.208
18.79
O


ATOM
5028
O
HOH
F423
−24.498
−22.642
−29.114
26.48
O


ATOM
5029
O
HOH
F427
−42.526
−46.274
−14.79
18.27
O


ATOM
5030
O
HOH
F430
−14.75
−31.131
−19.055
48.87
O


ATOM
5031
O
HOH
F431
−34.878
6.53
−28.368
19.91
O


ATOM
5032
O
HOH
F432
10.549
29.362
−2.166
24.44
O


ATOM
5033
O
HOH
F433
8.3
29.965
−3.709
42.01
O


ATOM
5034
O
HOH
F434
4.93
35.082
7.767
27.24
O


ATOM
5035
O
HOH
F435
7.01
38.01
9.004
21.31
O


ATOM
5036
O
HOH
F436
18.755
27.791
9.77
46.05
O


ATOM
5037
O
HOH
F438
0.35
28.842
15.624
13.72
O


ATOM
5038
O
HOH
F439
6.557
22.735
17.683
31.05
O


ATOM
5039
O
HOH
F440
3.297
0.092
−13.573
29.27
O


ATOM
5040
O
HOH
F441
−7.94
23.432
−18.434
28.66
O


ATOM
5041
O
HOH
F442
1.802
29.841
−11.164
42.98
O


ATOM
5042
O
HOH
F443
−50.163
−32.075
−16.975
13.52
O


ATOM
5043
O
HOH
F444
−50.324
−33.207
−22.394
34.24
O


ATOM
5044
O
HOH
F445
−30.405
−27.894
−41.835
20.26
O


ATOM
5045
O
HOH
F446
−42.528
−50.128
−39.155
34.7
O


ATOM
5046
O
HOH
F447
−6.122
−20.519
10.241
31.88
O


ATOM
5047
O
HOH
F448
−9.471
−17.911
15.198
29.11
O


ATOM
5048
O
HOH
F449
−10.256
8.058
1.039
22.58
O


ATOM
5049
O
HOH
F450
−10.084
8.041
6.965
35.26
O


ATOM
5050
O
HOH
F451
−8.258
10.019
15.224
14.39
O


ATOM
5051
O
HOH
F452
−3.132
9.777
17.396
43.71
O


ATOM
5052
O
HOH
F453
−7.844
6.196
15.354
25.77
O


ATOM
5053
O
HOH
F454
−33.488
−47.929
−40.055
17.2
O


ATOM
5054
O
HOH
F455
−32.976
−45.657
−40.842
24.75
O


ATOM
5055
O
HOH
F456
−15.149
9.534
2.929
44.29
O


ATOM
5056
O
HOH
F457
−16.433
16.612
−6.304
32
O


ATOM
5057
O
HOH
F458
−38.154
−3.576
−2.259
34.13
O


ATOM
5058
O
HOH
F459
−33.967
0.453
−7.339
31.91
O
















TABLE 1B





(SEQ ID NO: 2)
























ATOM
1
CB
LEU
1046 
−19.713
−2.925
−36.938
37.65
C


ATOM
2
CG
LEU
1046 
−19.834
−3.388
−35.494
38.45
C


ATOM
3
CD1
LEU
1046 
−20.915
−2.586
−34.807
37.79
C


ATOM
4
CD2
LEU
1046 
−20.107
−4.883
−35.426
38.03
C


ATOM
5
C
LEU
1046
−22.28
−3.028
−37.251
37.24
C


ATOM
6
O
LEU
1046 
−22.669
−1.886
−37.029
36.06
O


ATOM
7
N
LEU
1046
−20.8 
−2.523
−39.117
37.83
N


ATOM
8
CA
LEU
1046 
−20.858
−3.287
−37.783
38.05
C


ATOM
9
N
LEU
1047 
−22.803
−4.188
−36.833
37.34
N


ATOM
10
CA
LEU
1047 
−24.322
−4.334 
−36.88
37.41
C


ATOM
11
CB
LEU
1047 
−24.559
−5.846
−36.963
38.63
C


ATOM
12
CG
LEU
1047 
−24.045
−6.619
−38.197
39.63
C


ATOM
13
CD1
LEU
1047 
−23.493
−7.978
−37.765 
40.91
C


ATOM
14
CD2
LEU
1047 
−25.172
−6.793 
−39.21
40.19
C


ATOM
15
C
LEU
1047
−25.1 
−3.582
−35.917
36.45
C


ATOM
16
O
LEU
1047 
−25.898
−2.729
−36.286
36.58
O


ATOM
17
N
GLN
1048 
−24.943
−4.046
−34.699
36.14
N


ATOM
18
CA
GLN
1048 
−25.308
−3.208
−33.552
37.2
C


ATOM
19
CB
GLN
1048
−24.1 
−3.359
−32.547
38.59
C


ATOM
20
CG
GLN
1048 
−22.726
−3.016
−33.094
41.49
C


ATOM
21
CD
GLN
1048
−21.59
−3.712
−32.361
43.83
C


ATOM
22
OE1
GLN
1048 
−21.408 
−3.52
−31.158
44.72
O


ATOM
23
NE2
GLN
1048 
−20.825
−4.534
−33.079
42.9
N


ATOM
24
C
GLN
1048 
−25.331
−1.753
−33.995
35.99
C


ATOM
25
O
GLN
1048 
−26.367
−1.101
−33.978
35.9
O


ATOM
26
N
ASN
1049 
−24.192
−1.292 
−34.49
34.21
N


ATOM
27
CA
ASN
1049 
−24.188
0.042
−34.802
33.13
C


ATOM
28
CB
ASN
1049 
−22.763
0.474
−35.102
34.55
C


ATOM
29
CG
ASN
1049
−22.03
0.787
−33.852
36.88
C


ATOM
30
OD1
ASN
1049 
−22.593
1.274
−32.899
38.35
O


ATOM
31
ND2
ASN
1049 
−20.756
0.562
−33.862
36.72
N


ATOM
32
C
ASN
1049 
−25.042
0.484 
−35.87
31.5
C


ATOM
33
O
ASN
1049 
−24.714
1.503
−36.268
33.07
O


ATOM
34
N
THR
1050 
−26.135
−0.177
−36.286
29.28
N


ATOM
35
CA
THR
1050 
−27.071
0.242
−37.372
27.57
C


ATOM
36
CB
THR
1050 
−26.772
−0.569
−38.656
27.93
C


ATOM
37
OG1
THR
1050 
−26.853
−1.982
−38.404
28.31
O


ATOM
38
CG2
THR
1050 
−25.354
−0.265
−39.069
28.62
C


ATOM
39
C
THR
1050 
−28.501
−0.015
−36.874
26.39
C


ATOM
40
O
THR
1050
−29.511
0.174 
−37.56
26.33
O


ATOM
41
N
VAL
1051
−28.568
−0.357
−35.614
23.92
N


ATOM
42
CA
VAL
1051
−29.836
−0.634
−35.034
22.71
C


ATOM
43
CB
VAL
1051
−29.705
−1.748
−34.014
22.99
C


ATOM
44
CG1
VAL
1051
−31.041
−2.037
−33.406
21.99
C


ATOM
45
CG2
VAL
1051
−29.082
−2.987
−34.659
23.78
C


ATOM
46
C
VAL
1051
−30.375
0.589 
−34.295
22.22
C


ATOM
47
O
VAL
1051
−29.95
0.831 
−33.199
20.21
O


ATOM
48
N
HIS
1052
−31.251
1.366 
−34.82
22.87
N


ATOM
49
CA
HIS
1052
−31.674
2.419 
−33.928
24
C


ATOM
50
CB
HIS
1052
−31.576
3.704 
−34.653
24.15
C


ATOM
51
CG
HIS
1052
−32.273
4.827 
−33.985
23.62
C


ATOM
52
CD2
HIS
1052
−33.461
5.416 
−34.247
24.61
C


ATOM
53
ND1
HIS
1052
−31.722
5.51 
−32.926
25.74
N


ATOM
54
CE1
HIS
1052
−32.534
6.488 
−32.571
25.69
C


ATOM
55
NE2
HIS
1052
−33.596
6.453 
−33.358
27.01
N


ATOM
56
C
HIS
1052
−33.129
2.083 
−33.65
24.08
C


ATOM
57
O
HIS
1052
−33.725
1.402 
−34.453
25.06
O


ATOM
58
N
ILE
1053
−33.727
2.592 
−32.609
25.32
N


ATOM
59
CA
ILE
1053
−35.131
2.237 
−32.376
26.95
C


ATOM
60
CB
ILE
1053
−35.181
1.212 
−31.221
27.35
C


ATOM
61
CG2
ILE
1053
−36.585
1.044 
−30.766 
26.5
C


ATOM
62
CG1
ILE
1053
−34.506
−0.12 
−31.596
27.84
C


ATOM
63
CD
ILE
1053
−32.991
−0.116
−31.455
30.41
C


ATOM
64
C
ILE
1053
−35.828
3.54 
−31.879
27.08
C


ATOM
65
O
ILE
1053
−35.243
4.138 
−31.014
27.08
O


ATOM
66
N
ASP
1054
−36.982
3.996 
−32.351
27.49
N


ATOM
67
CA
ASP
1054
−37.546
5.236 
−31.77
27.84
C


ATOM
68
CB
ASP
1054
−38.199
6.114 
−32.815
28.33
C


ATOM
69
CG
ASP
1054
−38.818
7.383 
−32.249
28.99
C


ATOM
70
OD1
ASP
1054
−38.773
7.627 
−31.021
28.77
O


ATOM
71
OD2
ASP
1054
−39.366
8.145 
−33.064
30.36
O


ATOM
72
C
ASP
1054
−38.537
4.749 
−30.768
27.75
C


ATOM
73
O
ASP
1054
−39.568
4.12 
−31.051
28.21
O


ATOM
74
N
LEU
1055
−38.158
4.976 
−29.561
28.32
N


ATOM
75
CA
LEU
1055
−38.975
4.494 
−28.544
29.2
C


ATOM
76
CB
LEU
1055
−38.127
4.545 
−27.289
28.05
C


ATOM
77
CG
LEU
1055
−36.86
3.674 
−27.342
27.28
C


ATOM
78
CD1
LEU
1055
−36.032
3.941 
−26.098
27.69
C


ATOM
79
CD2
LEU
1055
−37.238
2.199 
−27.412
26.67
C


ATOM
80
C
LEU
1055
−40.331
5.239 
−28.441
30.11
C


ATOM
81
O
LEU
1055
−41.3
4.617 
−28.07 
30.04
O


ATOM
82
N
SER
1056
−40.451
6.507 
−28.822
30.85
N


ATOM
83
CA
SER
1056
−41.728
7.269 
−28.615
33.07
C


ATOM
84
CB
SER
1056
−41.442
8.729 
−28.747
32.67
C


ATOM
85
OG
SER
1056
−41.007
8.96 
−30.076
31.6
O


ATOM
86
C
SER
1056
−42.712
6.925 
−29.718
34.59
C


ATOM
87
O
SER
1056
−43.94 
7.153 
−29.689
35.04
O


ATOM
88
N
ALA
1057
−42.081
6.42 
−30.703
36.25
N


ATOM
89
CA
ALA
1057
−42.822
6.002 
−31.859
38.14
C


ATOM
90
CB
ALA
1057 
−41.819
5.716 
−32.996
36.82
C


ATOM
91
C
ALA
1057 
−43.573
4.697 
−31.555
39.49
C


ATOM
92
O
ALA
1057 
−44.274
4.161 
−32.415
40.68
O


ATOM
93
N
ILE
1058 
−43.475
4.255 
−30.311
40.19
N


ATOM
94
CA
ILE
1058 
−43.995
2.962 
−29.948
41.59
C


ATOM
95
CB
ILE
1058 
−42.872
2.192 
−29.127
42.24
C


ATOM
96
CG2
ILE
1058 
−42.904
2.642 
−27.671
45.17
C


ATOM
97
CG1
ILE
1058 
−43.068
0.676 
−29.213
43.34
C


ATOM
98
CD
ILE
1058 
−42.673
0.062 
−30.552
43.01
C


ATOM
99
C
ILE
1058 
−45.257
2.918 
−29.14
41.13
C


ATOM
100
O
ILE
1058 
−45.292
3.407 
−28.015
41.55
O


ATOM
101
N
ASP
1059 
−46.315
2.389 
−29.753
41.15
N


ATOM
102
CA
ASP
1059 
−47.605
2.129 
−29.055
41.81
C


ATOM
103
CB
ASP
1059 
−48.138
0.801 
−29.462
42.5
C


ATOM
104
CG
ASP
1059
−49.4
0.451 
−28.71
42.86
C


ATOM
105
OD1
ASP
1059 
−49.464
0.728 
−27.494
43.52
O


ATOM
106
OD2
ASP
1059 
−50.325
−0.113
−29.323
44.01
O


ATOM
107
C
ASP
1059 
−47.288
2.221 
−27.554
41.59
C


ATOM
108
O
ASP
1059 
−46.381
1.613 
−27.024
42.14
O


ATOM
109
N
PRO
1060
−48.13
2.869 
−26.869
41.04
N


ATOM
110
CD
PRO
1060 
−48.701
3.943 
−27.675
41.33
C


ATOM
111
CA
PRO
1060 
−48.061
3.174 
−25.457
41.53
C


ATOM
112
CB
PRO
1060 
−48.349
4.654 
−25.458
40.32
C


ATOM
113
CG
PRO
1060 
−49.253
4.76 
−26.709
40.85
C


ATOM
114
C
PRO
1060 
−48.658
2.397 
−24.392
41.35
C


ATOM
115
O
PRO
1060 
−48.591
2.565 
−23.203
42.29
O


ATOM
116
N
GLU
1061 
−49.145
1.297 
−24.822
41.69
N


ATOM
117
CA
GLU
1061 
−49.723
0.813 
−23.678
41.96
C


ATOM
118
CB
GLU
1061 
−51.163
0.879 
−23.965
43.79
C


ATOM
119
CG
GLU
1061
−51.39
0.487 
−25.385
47.3
C


ATOM
120
CD
GLU
1061 
−52.836
0.513 
−25.748
49.83
C


ATOM
121
OE1
GLU
1061 
−53.643
0.923 
−24.889
50.97
O


ATOM
122
OE2
GLU
1061 
−53.172
0.124 
−26.887
51.87
O


ATOM
123
C
GLU
1061 
−49.023
−0.456
−23.755
40.72
C


ATOM
124
O
GLU
1061 
−48.908
−1.181
−22.797
40
O


ATOM
125
N
LEU
1062
−48.49
−0.721
−24.936
39.26
N


ATOM
126
CA
LEU
1062 
−47.736
−1.936
−25.047
37.05
C


ATOM
127
CB
LEU
1062 
−47.144
−2.067
−26.447
36.62
C


ATOM
128
CG
LEU
1062 
−46.166
−3.232
−26.606
36.37
C


ATOM
129
CD1
LEU
1062 
−46.871
−4.543
−26.286
37.04
C


ATOM
130
CD2
LEU
1062 
−45.613
−3.252
−28.022
35.34
C


ATOM
131
C
LEU
1062
−46.61
−1.713
−24.034
36.08
C


ATOM
132
O
LEU
1062 
−46.172
−2.59 
−23.284
35
O


ATOM
133
N
VAL
1063 
−46.211
−0.472
−23.986
35.17
N


ATOM
134
CA
VAL
1063 
−45.136
−0.06 
−23.15
35.46
C


ATOM
135
CB
VAL
1063 
−44.642
1.236 
−23.725
35.44
C


ATOM
136
CG1
VAL
1063 
−43.706
1.89 
−22.788
35.6
C


ATOM
137
CG2
VAL
1063 
−43.997
0.967 
−25.086
35.93
C


ATOM
138
C
VAL
1063 
−45.523
0.057 
−21.678
35.67
C


ATOM
139
O
VAL
1063 
−44.712
−0.239
−20.794
35.29
O


ATOM
140 
N
GLN
1064 
−46.754
0.5 
−21.423
35.76
N


ATOM
141 
CA
GLN
1064 
−47.262
0.647 
−20.053
36.63
C


ATOM
142 
CB
GLN
1064 
−48.699
1.158 
−20.085
38.64
C


ATOM
143 
CG
GLN
1064 
−49.181
1.631 
−18.737
44.03
C


ATOM
144 
CD
GLN
1064 
−50.665
1.931 
−18.728
47.48
C


ATOM
145 
OE1
GLN
1064 
−51.319
1.924 
−19.775
49.46
O


ATOM
146 
NE2
GLN
1064 
−51.208
2.201 
−17.544
48.03
N


ATOM
147 
C
GLN
1064 
−47.177
−0.761
−19.454
35.07
C


ATOM
148 
O
GLN
1064 
−46.523
−0.982
−18.435
34.95
O


ATOM
149 
N
ALA
1065 
−47.864
−1.693
−20.097
32.4
N


ATOM
150 
CA
ALA
1065 
−47.798
−3.114
−19.773
30.99
C


ATOM
151 
CB
ALA
1065 
−48.238
−3.895
−21.008
29.54
C


ATOM
152 
C
ALA
1065
−46.37
−3.59 
−19.366
29.66
C


ATOM
153 
O
ALA
1065 
−46.137
−4
−18.23
31.42
O


ATOM
154 
N
VAL
1066 
−45.417
−3.545
−20.298
26.55
N


ATOM
155 
CA
VAL
1066 
−44.063
−4.031
−20.015
24.46
C


ATOM
156 
CB
VAL
1066
−43.31
−4.334
−21.353
23.5
C


ATOM
157 
CG1
VAL
1066 
−44.296
−4.837
−22.408
23.77
C


ATOM
158 
CG2
VAL
1066 
−42.598
−3.102
−21.852
22.22
C


ATOM
159 
C
VAL
1066
−43.16
−3.163
−19.111
23.52
C


ATOM
160 
O
VAL
1066 
−42.126
−3.645
−18.638
24.4
O


ATOM
161 
N
GLN
1067 
−43.544
−1.911
−18.848
22.41
N


ATOM
162 
CA
GLN
1067 
−42.703
−1.021
−18.038
21.71
C


ATOM
163 
CB
GLN
1067 
−43.417
0.277 
−17.642
23.75
C


ATOM
164 
CG
GLN
1067 
−42.446
1.315 
−17.06
27.36
C


ATOM
165 
CD
GLN
1067 
−41.496
1.888 
−18.115
28.42
C


ATOM
166 
OE1
GLN
1067 
−40.309
2.121 
−17.854
30.71
O


ATOM
167 
NE2
GLN
1067 
−42.022
2.126 
−19.308
28.25
N


ATOM
168 
C
GLN
1067 
−42.169
−1.645
−16.773
20.39
C


ATOM
169 
O
GLN
1067 
−41.027
−1.394
−16.392
17.45
O


ATOM
170 
N
HIS
1068 
−42.972
−2.464
−16.108
18.61
N


ATOM
171 
CA
HIS
1068 
−42.458
−3.041
−14.886
17.47
C


ATOM
172 
CB
HIS
1068 
−43.563
−3.74 
−14.101
16.08
C


ATOM
173 
CG
HIS
1068 
−44.015
−5.023
−14.704
16.78
C


ATOM
174 
CD2
HIS
1068 
−43.866 
−6.3 
−14.282
16.5
C


ATOM
175 
ND1
HIS
1068 
−44.741
−5.082
−15.874
16.21
N


ATOM
176 
CE1
HIS
1068 
−45.024
−6.344
−16.145
15.79
C


ATOM
177 
NE2
HIS
1068 
−44.504
−7.102
−15.194
17.99
N


ATOM
178 
C
HIS
1068 
−41.251
−3.967
−15.081
17.41
C


ATOM
179 
O
HIS
1068 
−40.582
−4.28 
−14.101
15.49
O


ATOM
180 
N
VAL
1069 
−40.949
−4.402
−16.31 
15.97
N


ATOM
181 
CA
VAL
1069
−39.75
−5.237
−16.509
15.14
C


ATOM
182 
CB
VAL
1069 
−39.978
−6.463
−17.444
14.83
C


ATOM
183 
CG1
VAL
1069 
−40.968
−7.409
−16.839
16.23
C


ATOM
184 
CG2
VAL
1069 
−40.429
−6.01 
−18.813
17.27
C


ATOM
185 
C
VAL
1069 
−38.579
−4.455
−17.106
16.95
C


ATOM
186 
O
VAL
1069 
−37.484
−5.005
−17.258
13.59
O


ATOM
187 
N
VAL
1070 
−38.802
−3.19 
−17.461
17.23
N


ATOM
188 
CA
VAL
1070 
−37.741
−2.37 
−18.048
19.93
C


ATOM
189 
CB
VAL
1070
−38.294
−1.133
−18.74
20.65
C


ATOM
190
CG1
VAL
1070
−37.135
−0.251
−19.247
22.41
C


ATOM
191
CG2
VAL
1070
−39.181
−1.565
−19.885
22.99
C


ATOM
192
C
VAL
1070
−36.783
−1.934
−16.969
20.17
C


ATOM
193
O
VAL
1070
−37.19 
−1.383
−15.954
19.99
O


ATOM
194
N
ILE
1071
−35.497
−2.152
−17.202
21.73
N


ATOM
195
CA
ILE
1071
−34.52 
−1.843
−16.175
24.48
C


ATOM
196
CB
ILE
1071
−33.326
−2.83 
−16.285
24.86
C


ATOM
197
CG2
ILE
1071
−32.302
−2.542
−15.218
25.75
C


ATOM
198
CG1
ILE
1071
−33.828
−4.283
−16.134
27.22
C


ATOM
199
CD
ILE
1071
−34.561
−4.632
−14.81
30.1
C


ATOM
200
C
ILE
1071
−34.02 
−0.401
−15.981
26.09
C


ATOM
201
O
ILE
1071
−33.915
0.054 
−14.842
29.19
O


ATOM
202
N
GLY
1072
−33.74
0.345 
−17.04
25.89
N


ATOM
203
CA
GLY
1072
−33.245
1.696 
−16.813
24.16
C


ATOM
204
C
GLY
1072
−31.743
1.564 
−16.874
24.08
C


ATOM
205
O
GLY
1072
−31.158
0.805 
−16.098
23.13
O


ATOM
206
N
PRO
1073
−31.075
2.312 
−17.755
24.22
N


ATOM
207
CD
PRO
1073
−31.504
3.335 
−18.725
23.18
C


ATOM
208
CA
PRO
1073
−29.626
2.111 
−17.78
24.27
C


ATOM
209
CB
PRO
1073
−29.194
2.872 
−19.033
24.61
C


ATOM
210
CG
PRO
1073
−30.194
3.967 
−19.142
24.35
C


ATOM
211
C
PRO
1073
−28.769
2.398 
−16.555
24.59
C


ATOM
212
O
PRO
1073
−27.782
1.708 
−16.346
24.13
O


ATOM
213
N
SER
1074
−29.118
3.376 
−15.734
24.35
N


ATOM
214
CA
SER
1074
−28.298
3.626 
−14.555
24.76
C


ATOM
215
CB
SER
1074
−28.922
4.721 
−13.681
27.55
C


ATOM
216
OG
SER
1074
−30.159
4.284 
−13.126
32.15
O


ATOM
217
C
SER
1074
−28.218
2.348 
−13.723
22.97
C


ATOM
218
O
SER
1074
−27.185
2.03 
−13.139
24.56
O


ATOM
219
N
SER
1075
−29.324
1.613 
−13.705
21.28
N


ATOM
220
CA
SER
1075
−29.494
0.399 
−12.907
19.44
C


ATOM
221
CB
SER
1075
−30.977
0.062 
−12.849
18.46
C


ATOM
222
OG
SER
1075
−31.684
1.089 
−12.195
14.27
O


ATOM
223
C
SER
1075
−28.732
−0.873
−13.249
20.54
C


ATOM
224
O
SER
1075
−28.633
−1.795
−12.429
21.36
O


ATOM
225
N
LEU
1076
−28.183
−0.923
−14.446
20.1
N


ATOM
226
CA
LEU
1076
−27.483
−2.104
−14.875
19.87
C


ATOM
227
CB
LEU
1076
−28.224
−2.699
−16.063
19.21
C


ATOM
228
CG
LEU
1076
−27.534
−3.89 
−16.707
19.12
C


ATOM
229
CD1
LEU
1076
−27.461
−5.021
−15.696
17.77
C


ATOM
230
CD2
LEU
1076
−28.302
−4.319
−17.948
19.82
C


ATOM
231
C
LEU
1076
−26.041
−1.87 
−15.285
20.54
C


ATOM
232
O
LEU
1076
−25.769
−0.986
−16.091 
22.3
O


ATOM
233
N
ILE
1077
−25.105
−2.632
−14.731
19.46
N


ATOM
234
CA
ILE
1077
−23.738
−2.495
−15.208
18.87
C


ATOM
235
CB
ILE
1077
−22.653
−2.504
−14.094
19.56
C


ATOM
236
CG2
ILE
1077
−21.285
−2.271
−14.737
19.59
C


ATOM
237
CG1
ILE
1077
−22.892
−1.405
−13.059
21.62
C


ATOM
238
CD
ILE
1077
−24.062
−1.664
−12.118
28.65
C


ATOM
239
C
ILE
1077
−23.51 
−3.766
−16.037
17.95
C


ATOM
240
O
ILE
1077
−23.793 
−4.863
−15.563
15.66
O


ATOM
241
N
VAL
1078
−23.053 
−3.637 
−17.28
17.31
N


ATOM
242
CA
VAL
1078
−22.745 
−4.842
−18.052
17.78
C


ATOM
243
CB
VAL
1078
−23.077 
−4.777
−19.553
18.44
C


ATOM
244
CG1
VAL
1078
−22.56 
−6.065
−20.228
18.64
C


ATOM
245
CG2
VAL
1078
−24.569 
−4.616
−19.782
17.46
C


ATOM
246
C
VAL
1078
−21.243 
−4.876
−17.998
19.43
C


ATOM
247
O
VAL
1078
−20.587 
−3.934
−18.433
19.77
O


ATOM
248
N
HIS
1079
−20.68 
−5.943
−17.467
20.51
N


ATOM
249
CA
HIS
1079
−19.24 
−6.009
−17.402
21.34
C


ATOM
250
CB
HIS
1079
−18.849 
−6.917 
−16.23
19.83
C


ATOM
251
CG
HIS
1079
−19.417 
−6.458
−14.919
19.74
C


ATOM
252
CD2
HIS
1079
−20.228 
−7.077
−14.027
19.88
C


ATOM
253
ND1
HIS
1079
−19.212 
−5.185
−14.427
20.23
N


ATOM
254
CE1
HIS
1079
−19.876 
−5.038
−13.293
18.18
C


ATOM
255
NE2
HIS
1079
−20.5
−6.172
−13.028
19.41
N


ATOM
256
C
HIS
1079
−18.73 
−6.499
−18.768
22.35
C


ATOM
257
O
HIS
1079
−18.699 
−7.702 
−19.04
21.87
O


ATOM
258
N
PHE
1080
−18.366 
−5.555
−19.639
23.27
N


ATOM
259
CA
PHE
1080
−17.898 
−5.913
−20.977
25.46
C


ATOM
260
CB
PHE
1080
−17.882 
−4.686
−21.918
27.46
C


ATOM
261
CG
PHE
1080
−19.259 
−4.25
−22.39
29.48
C


ATOM
262
CD1
PHE
1080
−20.027 
−5.062
−23.223
30.23
C


ATOM
263
CD2
PHE
1080
−19.798 
−3.04 
−21.968
30
C


ATOM
264
CE1
PHE
1080
−21.318 
−4.669
−23.622
31.49
C


ATOM
265
CE2
PHE
1080
−21.078 
−2.644 
−22.36
30.98
C


ATOM
266
CZ
PHE
1080
−21.838 
−3.459
−23.187
30.57
C


ATOM
267
C
PHE
1080
−16.536
−6.6 
−20.987
26.31
C


ATOM
268
O
PHE
1080
−16.179 
−7.225
−21.975
26.79
O


ATOM
269
N
ASN
1081
−15.765 
−6.508
−19.907
27.81
N


ATOM
270
CA
ASN
1081
−14.479 
−7.194
−19.918
29.51
C


ATOM
271
CB
ASN
1081
−13.346 
−6.286
−19.398
32.42
C


ATOM
272
CG
ASN
1081
−12.313 
−5.938
−20.504
36.54
C


ATOM
273
OD1
ASN
1081
−12.536 
−5.047 
−21.34
36.01
O


ATOM
274
ND2
ASN
1081
−11.193 
−6.663
−20.514
36.11
N


ATOM
275
C
ASN
1081
−14.538 
−8.517
−19.146
28.92
C


ATOM
276
O
ASN
1081
−13.544 
−8.976
−18.587
29.73
O


ATOM
277
N
GLU
1082
−15.714 
−9.14 
−19.149
27.42
N


ATOM
278
CA
GLU
1082
−15.91
−10.408
−18.464
27.47
C


ATOM
279
CB
GLU
1082
−16.04 
−10.16
−16.981
28.91
C


ATOM
280
CG
GLU
1082
−14.864
−10.669
−16.224
31.39
C


ATOM
281
CD
GLU
1082
−15.313
−11.523 
−15.08
33.01
C


ATOM
282
OE1
GLU
1082
−15.894
−10.968
−14.122
30.29
O


ATOM
283
OE2
GLU
1082
−15.11
−12.751 
−15.15
33.33
O


ATOM
284
C
GLU
1082
−17.11
−11.203
−18.964
26.21
C


ATOM
285
O
GLU
1082
−18.227
−11.076
−18.471
27.02
O


ATOM
286
N
VAL
1083
−16.846 
−12.06 
−19.93
24.63
N


ATOM
287
CA
VAL
1083
−17.86 
−12.87
−20.574
23.96
C


ATOM
288
CB
VAL
1083
−17.298
−13.188
−22
23.43
C


ATOM
289
CG1
VAL
1083
−18.161
−14.146
−22.766
23.66
C


ATOM
290
CG2
VAL
1083 
−17.164
−11.872
−22.762
24.22
C


ATOM
291
C
VAL
1083 
−18.239
−14.119
−19.748
22.62
C


ATOM
292
O
VAL
1083 
−17.357
−14.809
−19.245
22.61
O


ATOM
293
N
ILE
1084 
−19.539
−14.371
−19.543
21.85
N


ATOM
294
CA
ILE
1084
−19.95
−15.584 
−18.81
22.19
C


ATOM
295
CB
ILE
1084 
−21.503
−15.625
−18.472
23.79
C


ATOM
296
CG2
ILE
1084 
−21.863
−16.953
−17.767
24.46
C


ATOM
297
CG1
ILE
1084 
−21.889 
−14.48
−17.523
24.21
C


ATOM
298
CD
ILE
1084 
−23.311
−14.031
−17.657
27.1
C


ATOM
299
C
ILE
1084 
−19.588
−16.697 
−19.82
21.17
C


ATOM
300
O
ILE
1084 
−18.999
−17.715
−19.466
22
O


ATOM
301
N
GLY
1085 
−19.905
−16.471
−21.091
20.77
N


ATOM
302
CA
GLY
1085 
−19.577
−17.449
−22.115
21.09
C


ATOM
303
C
GLY
1085 
−20.052
−17.055 
−23.5
22.33
C


ATOM
304
O
GLY
1085 
−20.901
−16.179
−23.636
21.38
O


ATOM
305
N
ARG
1086 
−19.501
−17.678
−24.536
24.79
N


ATOM
306
CA
ARG
1086 
−19.944
−17.371
−25.886
27.33
C


ATOM
307
CB
ARG
1086 
−19.034
−16.315 
−26.53
30.23
C


ATOM
308
CG
ARG
1086
−17.68
−16.806
−26.973
34.24
C


ATOM
309
CD
ARG
1086 
−16.572
−15.889
−26.484
36.27
C


ATOM
310
NE
ARG
1086 
−16.649
−14.513
−26.972
38.68
N


ATOM
311
CZ
ARG
1086
−15.93 
−13.53
−26.443
40.82 
C


ATOM
312
NH1
ARG
1086 
−15.116
−13.806
−25.431
42.74
N


ATOM
313
NH2
ARG
1086 
−16.009 
−12.29
−26.908
40.02
N


ATOM
314
C
ARG
1086 
−20.039
−18.618
−26.755
26.1
C


ATOM
315
O
ARG
1086 
−19.714
−19.722
−26.323
26.61
O


ATOM
316
N
GLY
1087 
−20.526
−18.421 
−27.97
25.65
N


ATOM
317
CA
GLY
1087 
−20.693
−19.502
−28.918
24.38
C


ATOM
318
C
GLY
1087 
−21.688
−19
−29.939
24.55
C


ATOM
319
O
GLY
1087 
−21.875
−17.796
−30.112
23.97
O


ATOM
320
N
HIS
1088 
−22.325
−19.946
−30.604
25.2
N


ATOM
321
CA
HIS
1088 
−23.333 
−19.7 
−31.616
25.57
C


ATOM
322
CB
HIS
1088 
−23.894
−21.035
−32.012
28.7
C


ATOM
323
CG
HIS
1088 
−22.846
−21.938
−32.566
32.77
C


ATOM
324
CD2
HIS
1088 
−22.251
−21.968
−33.785
32.79
C


ATOM
325
ND1
HIS
1088 
−22.396
−23.074
−31.911
34.14
N


ATOM
326
CE1
HIS
1088 
−21.605
−23.783
−32.719
35.12 
C


ATOM
327
NE2
HIS
1088 
−21.517
−23.138
−33.868
34.26
N


ATOM
328
C
HIS
1088 
−24.476
−18.786
−31.172 
25.12 
C


ATOM
329
O
HIS
1088 
−25.102
−18.116
−31.997
24.17
O


ATOM
330
N
PHE
1089 
−24.776
−18.797
−29.875
23.19
N


ATOM
331
CA
PHE
1089 
−25.859
−17.976
−29.332
22.94
C


ATOM
332
CB
PHE
1089 
−26.286
−18.457
−27.929
22.43
C


ATOM
333
CG
PHE
1089 
−25.143
−18.641
−26.966
22.92
C


ATOM
334
CD1
PHE
1089 
−24.626
−19.908
−26.724
22.34
C


ATOM
335
CD2
PHE
1089 
−24.553
−17.545
−26.334
24.58 
C


ATOM
336
CE1
PHE
1089
−23.54
−20.084
−25.877
23.16 
C


ATOM
337
CE2
PHE
1089 
−23.462
−17.715
−25.482
22.08
C


ATOM
338
CZ
PHE
1089 
−22.955
−18.985
−25.257
21.68
C


ATOM
339
C
PHE
1089 
−25.351
−16.561
−29.248
22.27 
C


ATOM
340
O
PHE
1089 
−26.116
−15.601
−29.243
20.96
O


ATOM
341
N
GLY
1090 
−24.035
−16.452
−29.167
23.56
N


ATOM
342
CA
GLY
1090 
−23.423
−15.151 
−29.11
23.31
C


ATOM
343
C
GLY
1090
−22.48
−14.936
−27.958
23.5
C


ATOM
344
O
GLY
1090 
−21.532
−15.694
−27.727
24.61
O


ATOM
345
N
CYS
1091 
−22.778
−13.877
−27.225
21.88
N


ATOM
346
CA
CYS
1091 
−21.968
−13.472
−26.116 
21.85
C


ATOM
347
CB
CYS
1091 
−21.026
−12.375
−26.578
22.79
C


ATOM
348
SG
CYS
1091
−19.78
−12.017
−25.368
29.92
S


ATOM
349
C
CYS
1091 
−22.807
−12.981
−24.951
21.01
C


ATOM
350
O
CYS
1091 
−23.561
−12.013
−25.071
20.39
O


ATOM
351
N
VAL
1092
−22.66
−13.683 
−23.83
20.12
N


ATOM
352
CA
VAL
1092 
−23.357
−13.391
−22.586
17.5
C


ATOM
353
CB
VAL
1092 
−23.984
−14.676
−22.018
16.22
C


ATOM
354
CG1
VAL
1092 
−24.836
−14.367
−20.794
14.54
C


ATOM
355
CG2
VAL
1092 
−24.828
−15.333
−23.087
15.2
C


ATOM
356
C
VAL
1092 
−22.325
−12.833 
−21.61
16.82
C


ATOM
357
O
VAL
1092 
−21.296
−13.464
−21.335
16.7
O


ATOM
358
N
TYR
1093 
−22.593
−11.633
−21.109
15.42
N


ATOM
359
CA
TYR
1093 
−21.682
−10.994
−20.185
17.23
C


ATOM
360
CB
TYR
1093 
−21.427 
−9.531
−20.566 
17.62
C


ATOM
361
CG
TYR
1093 
−20.851 
−9.299
−21.945
20.58
C


ATOM
362
CD1
TYR
1093 
−21.686 
−9.105
−23.037
21.94
C


ATOM
363
CE1
TYR
1093 
−21.165 
−8.829
−24.305
24.31
C


ATOM
364
CD2
TYR
1093 
−19.466 
−9.224
−22.147
21.64
C


ATOM
365
CE2
TYR
1093 
−18.932 
−8.951
−23.409
23.55
C


ATOM
366
CZ
TYR
1093
−19.79 
−8.751
−24.484
25.26
C


ATOM
367
OH
TYR
1093 
−19.291 
−8.455
−25.738
26.62
O


ATOM
368
C
TYR
1093 
−22.211
−11.008
−18.773
18.22
C


ATOM
369
O
TYR
1093 
−23.396
−11.209
−18.521 
19.61
O


ATOM
370
N
HIS
1094 
−21.289
−10.793
−17.853
18.6
N


ATOM
371
CA
HIS
1094 
−21.604
−10.698
−16.452
18.83
C


ATOM
372
CB
HIS
1094 
−20.316
−10.789
−15.638
19.99
C


ATOM
373
CG
HIS
1094 
−19.836
−12.185
−15.394
21.1
C


ATOM
374
CD2
HIS
1094 
−18.704
−12.818
−15.783
22.5
C


ATOM
375
ND1
HIS
1094 
−20.491
−13.057
−14.551
21.79
N


ATOM
376
CE1
HIS
1094 
−19.777
−14.161
−14.421
21.06
C


ATOM
377
NE2
HIS
1094 
−18.687 
−14.04
−15.157
21.09
N


ATOM
378
C
HIS
1094 
−22.177 
−9.281
−16.328
18.78
C


ATOM
379
O
HIS
1094
−21.78 
−8.382
−17.073
18.3
O


ATOM
380
N
GLY
1095 
−23.116 
−9.099 
−15.41
19.1
N


ATOM
381
CA
GLY
1095
−23.7
−7.791
−15.188
19.67
C


ATOM
382
C
GLY
1095 
−24.024 
−7.631
−13.713
21.24
C


ATOM
383
O
GLY
1095 
−24.131 
−8.621
−12.986
19.08
O


ATOM
384
N
THR
1096 
−24.141 
−6.388
−13.259
23.02
N


ATOM
385
CA
THR
1096 
−24.501 
−6.095
−11.874
22.84
C


ATOM
386
CB
THR
1096 
−23.404 
−5.275 
−11.14
23.36
C


ATOM
387
OG1
THR
1096 
−22.428 
−6.166
−10.589
26.41
O


ATOM
388
CG2
THR
1096
−24.01 
−4.451
−10.016
24.26
C


ATOM
389
C
THR
1096 
−25.793 
−5.281 
−11.94
21.4
C


ATOM
390
O
THR
1096
−25.842 
−4.216
−12.559
20.93
O


ATOM
391
N
LEU
1097
−26.841 
−5.798
−11.314
21.53
N


ATOM
392
CA
LEU
1097
−28.141 
−5.141
−11.326
21.82
C


ATOM
393
CB
LEU
1097
−29.209 
−6.159
−11.758
20.06
C


ATOM
394
CG
LEU
1097
−30.646 
−5.76 
−12.111
19.25
C


ATOM
395
CD1
LEU
1097
−30.665 
−4.708
−13.216
18.42
C


ATOM
396
CD2
LEU
1097
−31.385 
−7.007
−12.565
16.83
C


ATOM
397
C
LEU
1097
−28.519 
−4.53
−9.981
21.19
C


ATOM
398
O
LEU
1097
−28.367 
−5.164 
−8.938
19.7
O


ATOM
399
N
LEU
1098
−28.996 
−3.286
−10.021
23.17
N


ATOM
400
CA
LEU
1098
−29.46 
−2.583 
−8.822
24.41
C


ATOM
401
CB
LEU
1098
−29.613 
−1.09
−9.083
26.16
C


ATOM
402
CG
LEU
1098
−28.496 
−0.161 
−8.629
29.18
C


ATOM
403
CD1
LEU
1098
−29.114
1.203
−8.341
28.63
C


ATOM
404
CD2
LEU
1098
−27.822 
−0.709 
−7.365
29.03
C


ATOM
405
C
LEU
1098
−30.837 
−3.144 
−8.541
24.65
C


ATOM
406
O
LEU
1098
−31.779 
−2.833 
−9.276
23.31
O


ATOM
407
N
ASP
1099
−30.973 
−3.96
−7.497
24.68
N


ATOM
408
CA
ASP
1099
−32.283 
−4.545 
−7.224
26.36
C


ATOM
409
CB
ASP
1099
−32.18 
−5.778 
−6.306
27.06
C


ATOM
410
CG
ASP
1099
−32.004 
−5.446 
−4.831
29.17
C


ATOM
411
OD1
ASP
1099
−31.643
−6.4
−4.128
31.65
O


ATOM
412
OD2
ASP
1099
−32.229 
−4.305 
−4.365
28.08
O


ATOM
413
C
ASP
1099
−33.244 
−3.518 
−6.686
27.55
C


ATOM
414
O
ASP
1099
−32.875 
−2.344 
−6.562
26.26
O


ATOM
415
N
ASN
1100
−34.477 
−3.923 
−6.374
29.32
N


ATOM
416
CA
ASN
1100
−35.391 
−2.909 
−5.913
30.82
C


ATOM
417
CB
ASN
1100
−36.817 
−3.375 
−5.712
28.63
C


ATOM
418
CG
ASN
1100
−37.784 
−2.203 
−5.776
27.15
C


ATOM
419
OD1
ASN
1100
−37.902 
−1.518 
−6.802
25.47
O


ATOM
420
ND2
ASN
1100
−38.459 
−1.946 
−4.667
25.33
N


ATOM
421
C
ASN
1100
−34.817 
−2.17
−4.731
34.06
C


ATOM
422
O
ASN
1100 
−34.99 
−0.959 
−4.698
33.4
O


ATOM
423
N
ASP
1101
−34.244 
−2.749 
−3.684
36.87
N


ATOM
424
CA
ASP
1101
−33.561 
−1.645 
−3.071
40.16
C


ATOM
425
CB
ASP
1101
−33.957 
−1.09
−1.753
42.43
C


ATOM
426
CG
ASP
1101
−33.365
0.343
−1.643
44.17
C


ATOM
427
OD1
ASP
1101
−33.676
1.142
−2.566
43.29
O


ATOM
428
OD2
ASP
1101
−32.573
0.673
−0.723
44.41
O


ATOM
429
C
ASP
1101
−32.097 
−1.555 
−3.027
40.36
C


ATOM
430
O
ASP
1101
−31.468 
−1.272 
−4.032
40.01
O


ATOM
431
N
GLY
1102
−31.538 
−1.723 
−1.849
40.9
N


ATOM
432
CA
GLY
1102
−30.121 
−1.537 
−1.771
40.87
C


ATOM
433
C
GLY
1102
−29.265 
−2.35
−2.702
39.17
C


ATOM
434
O
GLY
1102
−28.437 
−1.801 
−3.436
38.81
O


ATOM
435
N
LYS
1103
−29.541 
−3.645 
−2.757
37.87
N


ATOM
436
CA
LYS
1103
−28.614 
−4.503
−3.44
35.83
C


ATOM
437
CB
LYS
1103
−28.57 
−5.866 
−2.672
37.7
C


ATOM
438
CG
LYS
1103
−29.817 
−6.811 
−2.577
41.49
C


ATOM
439
CD
LYS
1103
−30.76 
−6.723 
−1.312
43.33
C


ATOM
440
CE
LYS
1103
−32.272 
−6.806 
−1.734
43.17
C


ATOM
441
NZ
LYS
1103
−33.348 
−7.174 
−0.746
44.65
N


ATOM
442
C
LYS
1103
−28.306 
−4.733 
−4.911
32.44
C


ATOM
443
O
LYS
1103
−29.144 
−4.908 
−5.808 
32.36
O


ATOM
444
N
LYS
1104
−26.985 
−4.671 
−5.06
29.44
N


ATOM
445
CA
LYS
1104
−26.201 
−4.881 
−6.257 
29.31
C


ATOM
446
CB
LYS
1104
−24.733 
−4.422 
−5.988
31.35
C


ATOM
447
CG
LYS
1104
−24.465 
−2.898 
−5.603
33.76
C


ATOM
448
CD
LYS
1104
−23.118 
−2.693 
−4.801
37.44
C


ATOM
449
CE
LYS
1104
−22.131 
−1.588 
−5.33
39.69
C


ATOM
450
NZ
LYS
1104
−22.349 
−0.137 
−4.967
39.76
N


ATOM
451
C
LYS
1104
−26.285 
−6.422 
−6.37
28.22
C


ATOM
452
O
LYS
1104
−25.698 
−7.139 
−5.554 
26.29
O


ATOM
453
N
ILE
1105
−27.052 
−6.91
−7.349
26.65
N


ATOM
454
CA
ILE
1105
−27.265 
−8.348 
−7.598
26.94
C


ATOM
455
CB
ILE
1105
−28.789 
−8.661 
−7.72
27.99
C


ATOM
456
CG2
ILE
1105
−29.026 
−9.839 
−8.673
30.38
C


ATOM
457
CG1
ILE
1105
−29.391 
−8.883 
−6.322
30.76
C


ATOM
458
CD
ILE
1105
−28.852
−10.101 
−5.536
35.19
C


ATOM
459
C
ILE
1105
−26.558 
−8.837 
−8.877
25.68
C


ATOM
460
O
ILE
1105
−26.505 
−8.118 
−9.874
24.13
O


ATOM
461
N
HIS
1106
−26.034 
−10.06 
−8.854
23.56
N


ATOM
462
CA
HIS
1106
−25.334
−10.602
−10.023
22.94
C


ATOM
463
CB
HIS
1106
−24.409
−11.758 
−9.615
24.08
C


ATOM
464
CG
HIS
1106
−23.469
−12.194
−10.699
27.15
C


ATOM
465
CD2
HIS
1106
−23.422
−11.885
−12.018
28.42
C


ATOM
466
ND1
HIS
1106
−22.378
−13.001
−10.458
27.68
N


ATOM
467
CE1
HIS
1106
−21.695
−13.161
−11.578
29.8
C


ATOM
468
NE2
HIS
1106
−22.307
−12.493 
−12.54
29.95
N


ATOM
469
C
HIS
1106
−26.296
−11.099 
−11.09
20.67
C


ATOM
470
O
HIS
1106
−27.245
−11.815
−10.798
21.19
O


ATOM
471
N
CYS
1107
−26.062
−10.724
−12.335
17.6
N


ATOM
472
CA
CYS
1107
−26.938
−11.208
−13.385
17.33
C


ATOM
473
CB
CYS
1107
−28.014
−10.171
−13.699
18.03
C


ATOM
474
SG
CYS
1107
−27.321 
−8.564
−14.194
19.36
S


ATOM
475
C
CYS
1107
−26.13
−11.512
−14.638
17.39
C


ATOM
476
O
CYS
1107
−24.931
−11.213
−14.715
17.99
O


ATOM
477
N
ALA
1108
−26.793
−12.125
−15.608
14.48
N


ATOM
478
CA
ALA
1108
−26.172
−12.458
−16.878
15.95
C


ATOM
479
CB
ALA
1108
−26.418 
−13.93
−17.204
15.75
C


ATOM
480
C
ALA
1108
−26.89 
−11.56
−17.883
15.24
C


ATOM
481
O
ALA
1108
−28.107
−11.399
−17.798
12.68
O


ATOM
482
N
VAL
1109
−26.177
−10.958
−18.827
15.61
N


ATOM
483
CA
VAL
1109
−26.885
−10.087 
−19.76
16.53
C


ATOM
484
CB
VAL
1109
−26.732 
−8.557
−19.371
18.81
C


ATOM
485
CG1
VAL
1109
−26.215 
−8.404
−17.944 
20.45
C


ATOM
486
CG2
VAL
1109
−25.815 
−7.839
−20.346
19.51
C


ATOM
487
C
VAL
1109
−26.504
−10.231
−21.227 
17.08
C


ATOM
488
O
VAL
1109
−25.378
−10.611
−21.561
17.04
O


ATOM
489
N
LYS
1110
−27.461 
−9.952
−22.107
17.38
N


ATOM
490
CA
LYS
1110 
−27.158 
−9.965
−23.534
17.22
C


ATOM
491
CB
LYS
1110 
−26.814
−11.372
−24.044
19.64
C


ATOM
492
CG
LYS
1110 
−27.959
−12.334
−24.212
18.31
C


ATOM
493
CD
LYS
1110 
−28.051
−12.821
−25.655
19.3
C


ATOM
494
CE
LYS
1110 
−26.738
−13.341
−26.235
20.56
C


ATOM
495
NZ
LYS
1110
−26.86
−13.284
−27.731 
20.37
N


ATOM
496
C
LYS
1110 
−28.156 
−9.305
−24.468
15.54
C


ATOM
497
O
LYS
1110 
−29.348 
−9.176
−24.183
14.09
O


ATOM
498
N
SER
1111
−27.58 
−8.874
−25.586
15.93
N


ATOM
499
CA
SER
1111 
−28.193 
−8.161
−26.691
16.27
C


ATOM
500
CB
SER
1111 
−27.094 
−7.361
−27.375
15.21
C


ATOM
501
OG
SER
1111 
−27.529 
−6.71 
−28.544
18.36
O


ATOM
502
C
SER
1111 
−28.889 
−9.092
−27.599
15.76
C


ATOM
503
O
SER
1111 
−28.454
−10.211
−27.947
12.53
O


ATOM
504
N
LEU
1112 
−30.098 
−8.685
−27.952 
17.34
N


ATOM
505
CA
LEU
1112 
−30.711 
−9.683
−28.742
20.62
C


ATOM
506
CB
LEU
1112 
−32.234 
−9.458
−28.562 
20.06
C


ATOM
507
CG
LEU
1112 
−32.642 
−9.744
−27.101
21.55
C


ATOM
508
CD1
LEU
1112 
−33.953 
−9.403
−26.868
19.7
C


ATOM
509
CD2
LEU
1112 
−32.411
−11.154
−26.774
19.53
C


ATOM
510
C
LEU
1112 
−30.167 
−9.375
−30.102
21.91
C


ATOM
511
O
LEU
1112 
−30.723 
−8.688
−30.799
23.49
O


ATOM
512
N
ASN
1113 
−29.063
−10.052
−30.556
22.86
N


ATOM
513
CA
ASN
1113 
−28.909 
−9.404 
−31.85
23.45
C


ATOM
514
CB
ASN
1113
−27.43 
−9.495
−32.245
23.43
C


ATOM
515
CG
ASN
1113 
−26.585 
−9.117 
−31.09
25.58
C


ATOM
516
OD1
ASN
1113 
−26.541 
−8.023 
−30.63
25.22
O


ATOM
517
ND2
ASN
1113 
−25.914
−10.072
−30.585
22.74
N


ATOM
518
C
ASN
1113 
−29.885 
−9.566
−33
22.92
C


ATOM
519
O
ASN
1113 
−29.831 
−8.839
−33.944
23.28
O


ATOM
520
N
ARG
1114 
−30.958
−10.381
−32.816 
21.82
N


ATOM
521
CA
ARG
1114 
−31.849 
−10.5 
−33.937
22.01
C


ATOM
522
CB
ARG
1114
−32.4 
−11.948
−33.913
22.1
C


ATOM
523
CG
ARG
1114
−31.25
−12.857
−34.102
25.83
C


ATOM
524
CD
ARG
1114 
−31.459
−14.259
−33.982
28.53
C


ATOM
525
NE
ARG
1114 
−32.736
−14.557
−34.514
30.33
N


ATOM
526
CZ
ARG
1114 
−33.501
−15.502 
−34.01
32.37
C


ATOM
527
NH1
ARG
1114 
−33.154
−16.204
−32.927
30.58
N


ATOM
528
NH2
ARG
1114 
−34.661
−15.652
−34.574
33.1
N


ATOM
529
C
ARG
1114 
−32.938 
−9.462
−33.984
21.79
C


ATOM
530
O
ARG
1114 
−33.683 
−9.45
−34.91
22.34
O


ATOM
531
N
ILE
1115 
−33.051 
−8.545 
−33.03
22.68
N


ATOM
532
CA
ILE
1115 
−34.107 
−7.541
−33.104
21.2
C


ATOM
533
CB
ILE
1115 
−34.741 
−7.354
−31.703 
24.03
C


ATOM
534
CG2
ILE
1115 
−35.642 
−6.144
−31.668
23.21
C


ATOM
535
CG1
ILE
1115 
−35.589 
−8.58 
−31.351
24.72
C


ATOM
536
CD
ILE
1115 
−35.868 
−8.729
−29.851
26.57
C


ATOM
537
C
ILE
1115 
−33.318 
−6.335
−33.548
21.28
C


ATOM
538
O
ILE
1115 
−32.489 
−5.821
−32.809
20.76
O


ATOM
539
N
THR
1116 
−33.595 
−5.909 
−34.77 
22.08
N


ATOM
540
CA
THR
1116
−32.856
−4.857
−35.452
23.07
C


ATOM
541
CB
THR
1116
−32.421
−5.438
−36.786
23.06
C


ATOM
542
OG1
THR
1116
−33.597
−5.795
−37.535
23.74 
O


ATOM
543
CG2
THR
1116
−31.615
−6.729
−36.558
24.03
C


ATOM
544
C
THR
1116
−33.622
−3.572
−35.704
23.05 
C


ATOM
545
O
THR
1116
−33.056
−2.585
−36.174
23.27
O


ATOM
546
N
ASP
1117 
−34.92
−3.61 
−35.44
22.99
N


ATOM
547
CA
ASP
1117
−35.759
−2.447
−35.643
24.43 
C


ATOM
548
CB
ASP
1117
−36.122
−2.292
−37.121
26.12
C


ATOM
549
CG
ASP
1117
−37.083
−3.345 
−37.6
28.5
C


ATOM
550
OD1
ASP
1117
−37.787
−3.933
−36.756
30.79 
O


ATOM
551
OD2
ASP
1117
−37.151
−3.569
−38.826
30.95
O


ATOM
552
C
ASP
1117
−37.002
−2.491
−34.764
23.72 
C


ATOM
553
O
ASP
1117
−37.291 
−3.5 
−34.122
23.98
O


ATOM
554
N
ILE
1118
−37.743
−1.388
−34.77 
24.56 
N


ATOM
555
CA
ILE
1118
−38.888
−1.211
−33.891
25.74
C


ATOM
556
CB
ILE
1118
−39.278
0.274 
−33.878
25.32 
C


ATOM
557
CG2
ILE
1118
−39.571
0.743 
−35.276
26.13
C


ATOM
558
CG1
ILE
1118
−40.435
0.497 
−32.915
24.98
C


ATOM
559
CD
ILE
1118
−40.733
1.964 
−32.613
28.73
C


ATOM
560
C
ILE
1118
−40.092
−2.113
−34.069
25.74 
C


ATOM
561
O
ILE
1118
−40.779
−2.448
−33.099
25.12
O


ATOM
562
N
GLY
1119
−40.346
−2.504
−35.307
25.89 
N


ATOM
563
CA
GLY
1119
−41.422
−3.437
−35.543
25.68
C


ATOM
564
C
GLY
1119
−41.012
−4.734
−34.844
25.67
C


ATOM
565
O
GLY
1119
−41.864
−5.425
−34.288
25.14
O


ATOM
566
N
GLU
1120
−39.715
−5.066
−34.85
23.75
N


ATOM
567
CA
GLU
1120
−39.226
−6.295
−34.212
23.95
C


ATOM
568
CB
GLU
1120
−37.817
−6.627
−34.706
24.69
C


ATOM
569
CG
GLU
1120
−37.823
−7.463
−35.977
25.41
C


ATOM
570
CD
GLU
1120
−36.543
−7.319
−36.777
27.56
C


ATOM
571
OE1
GLU
1120
−35.575
−6.731
−36.247
26.97
O


ATOM
572
OE2
GLU
1120
−36.499
−7.797
−37.934
28.81
O


ATOM
573
C
GLU
1120
−39.262
−6.176
−32.692
23.53 
C


ATOM
574
O
GLU
1120
−39.737
−7.076
−31.996
20.73
O


ATOM
575
N
VAL
1121
−38.759
−5.057
−32.192
22.95
N


ATOM
576
CA
VAL
1121
−38.797
−4.775
−30.769
24.45
C


ATOM
577
CB
VAL
1121
−38.396
−3.315
−30.51
24.85
C


ATOM
578
CG1
VAL
1121
−38.695
−2.929
−29.063
21.7
C


ATOM
579
CG2
VAL
1121
−36.933
−3.111
−30.857
23.7
C


ATOM
580
C
VAL
1121
−40.259
−4.934
−30.333
26.12
C


ATOM
581
O
VAL
1121
−40.567
−5.618
−29.349
26.27 
O


ATOM
582
N
SER
1122 
−41.16
−4.303
−31.084
26.23
N


ATOM
583
CA
SER
1122
−42.583
−4.322
−30.75
27.11
C


ATOM
584
CB
SER
1122
−43.374
−3.492
−31.766
28.38 
C


ATOM
585
OG
SER
1122
−44.763
−3.526
−31.482
32.31
O


ATOM
586
C
SER
1122
−43.171
−5.722
−30.644
26.65
C


ATOM
587
O
SER
1122
−43.865
−6.045
−29.677
25.95 
O


ATOM
588
N
GLN
1123
−42.893
−6.553
−31.641
26.43
N


ATOM
589
CA
GLN
1123 
−43.39
−7.919
−31.636
26.5
C


ATOM
590
CB
GLN
1123
−43.046 
−8.607 
−32.955
29.41
C


ATOM
591
CG
GLN
1123
−43.203
−10.123 
−32.919
33.88
C


ATOM
592
CD
GLN
1123
−43.393
−10.721 
−34.301
36.39
C


ATOM
593
OE1
GLN
1123
−42.587
−10.498 
−35.203
36.5
O


ATOM
594
NE2
GLN
1123
−44.467
−11.489 
−34.472
38.02
N


ATOM
595
C
GLN
1123
−42.801 
−8.714
−30.47
25.95
C


ATOM
596
O
GLN
1123
−43.454 
−9.597 
−29.918
24.87
O


ATOM
597
N
PHE
1124
−41.557 
−8.402 
−30.114
24.65
N


ATOM
598
CA
PHE
1124
−40.871 
−9.079 
−29.023
23.66
C


ATOM
599
CB
PHE
1124
−39.414 
−8.629 
−28.955
23.72
C


ATOM
600
CG
PHE
1124
−38.77
−8.86 
−27.618
23.58
C


ATOM
601
CD1
PHE
1124
−38.694 
−10.14 
−27.076
25.18
C


ATOM
602
CD2
PHE
1124
−38.24
−7.798 
−26.902
24
C


ATOM
603
CE1
PHE
1124
−38.097
−10.354 
−25.834
25.88
C


ATOM
604
CE2
PHE
1124
−37.642
−8
−25.662
25.31
C


ATOM
605
CZ
PHE
1124
−37.568 
−9.276 
−25.128
25.33
C


ATOM
606
C
PHE
1124
−41.544 
−8.749 
−27.715
24.78
C


ATOM
607
O
PHE
1124
−41.873 
−9.621
−26.92
26.5
O


ATOM
608
N
LEU
1125
−41.723 
−7.466 
−27.479
23.2
N


ATOM
609
CA
LEU
1125
−42.356 
−7.073 
−26.261
22.77
C


ATOM
610
CB
LEU
1125
−42.567 
−5.598 
−26.229
21.09
C


ATOM
611
CG
LEU
1125
−41.236 
−4.899 
−26.129
17.73
C


ATOM
612
CD1
LEU
1125
−41.631 
−3.496 
−26.146
19.09
C


ATOM
613
CD2
LEU
1125
−40.427 
−5.218 
−24.871
16.2
C


ATOM
614
C
LEU
1125
−43.682
−7.72 
−26.132
25.71
C


ATOM
615
O
LEU
1125
−44.116
−8.03 
−25.032
23.93
O


ATOM
616
N
THR
1126
−44.368 
−7.944 
−27.228
26.97
N


ATOM
617
CA
THR
1126
−45.639 
−8.549 
−26.998
30.56
C


ATOM
618
CB
THR
1126
−46.474
−8.47 
−28.349
30.39
C


ATOM
619
OG1
THR
1126
−47.089 
−7.172 
−28.448
31.21
O


ATOM
620
CG2
THR
1126
−47.536 
−9.509 
−28.425
32.25
C


ATOM
621
C
THR
1126
−45.308 
−9.955 
−26.367
32.6
C


ATOM
622
O
THR
1126
−46.214
−10.759 
−26.142
30.99
O


ATOM
623
N
GLU
1127
−44.006
−10.139 
−25.994
35.71
N


ATOM
624
CA
GLU
1127
−43.324
−11.363 
−25.421
37.11
C


ATOM
625
CB
GLU
1127
−42.663
−12.118 
−26.553
36.36
C


ATOM
626
CG
GLU
1127
−43.597
−12.481 
−27.631
39.29
C


ATOM
627
CD
GLU
1127
−44.476
−13.585 
−27.184
41.29
C


ATOM
628
OE1
GLU
1127
−44.087
−14.213 
−26.181
41.62
O


ATOM
629
OE2
GLU
1127
−45.523
−13.843 
−27.816
43.61
O


ATOM
630
C
GLU
1127
−42.227
−11.228 
−24.313
36.65
C


ATOM
631
O
GLU
1127
−41.449
−12.168 
−24.042
36.3
O


ATOM
632
N
GLY
1128
−42.13
−10.02 
−23.774
37.88
N


ATOM
633
CA
GLY
1128
−41.248 
−9.679 
−22.675
36.79
C


ATOM
634
C
GLY
1128
−42.463 
−9.503 
−21.803
36.28
C


ATOM
635
O
GLY
1128
−42.531 
−8.689
−20.88
34.64
O


ATOM
636
N
ILE
1129
−43.485
−10.238 
−22.251
36.52
N


ATOM
637
CA
ILE
1129
−44.786
−10.362 
−21.617
37.06
C


ATOM
638
CB
ILE
1129
−45.997
−10.386 
−22.653
35.43
C


ATOM
639
CG2
ILE
1129
−47.188
−11.204 
−22.111
33.75
C


ATOM
640
CG1
ILE
1129 
−46.554 
−8.978
−22.897
35.19
C


ATOM
641
CD
ILE
1129 
−46.993 
−8.179
−21.639 
36.58
C


ATOM
642
C
ILE
1129 
−44.562 
−11.78
−21.112 
38.14
C


ATOM
643
O
ILE
1129 
−43.906
−12.012
−20.096
40.02
O


ATOM
644
N
ILE
1130
−45.05
−12.697
−21.936 
39.77
N


ATOM
645
CA
ILE
1130 
−45.059 
−14.15
−21.818 
39.09
C


ATOM
646
CB
ILE
1130 
−45.827
−14.638
−23.165
37.23
C


ATOM
647
CG2
ILE
1130 
−46.725
−15.832
−22.942
35.01
C


ATOM
648
CG1
ILE
1130 
−46.834
−13.555
−23.613
36.25
C


ATOM
649
CD
ILE
1130 
−47.219
−13.572
−25.099
35.76
C


ATOM
650
C
ILE
1130 
−43.655
−14.881
−21.549
41.51
C


ATOM
651
O
ILE
1130 
−43.156 
−15.56
−22.452
39.43
O


ATOM
652
N
MET
1131 
−43.035
−14.698
−20.346
42.91
N


ATOM
653
CA
MET
1131 
−41.742
−15.349
−19.835 
44.95
C


ATOM
654
CB
MET
1131 
−40.472
−15.204
−20.764
46.01
C


ATOM
655
CG
MET
1131 
−39.274
−16.281 
−20.43
45.5
C


ATOM
656
SD
MET
1131 
−37.426
−16.086
−20.877
48.89
S


ATOM
657
CE
MET
1131 
−36.526
−17.834
−20.399
44.9
C


ATOM
658
C
MET
1131 
−41.305
−14.898
−18.397
45.24
C


ATOM
659
O
MET
1131 
−40.606
−15.644 
−17.7
46.07
O


ATOM
660
N
LYS
1132 
−41.711
−13.684
−17.992
45.8
N


ATOM
661
CA
LYS
1132 
−41.448
−13.047
−16.667
44.47
C


ATOM
662
CB
LYS
1132 
−41.153
−11.536
−16.863
44.62
C


ATOM
663
CG
LYS
1132 
−41.633
−10.562
−15.744
45.98
C


ATOM
664
CD
LYS
1132 
−40.704
−10.607
−14.528
47.24
C


ATOM
665
CE
LYS
1132 
−41.097 
−9.681
−13.372
48.16
C


ATOM
666
NZ
LYS
1132 
−39.906 
−9.52
−12.48
50.03
N


ATOM
667
C
LYS
1132 
−42.766
−13.202
−15.908
43.38
C


ATOM
668
O
LYS
1132 
−42.822
−13.535
−14.706
44.16
O


ATOM
669
N
ASP
1133
−43.81
−12.924 
−16.69
40.97
N


ATOM
670
CA
ASP
1133 
−45.216
−12.985
−16.338
37.24
C


ATOM
671
CB
ASP
1133 
−45.968
−11.948
−17.229
39.7
C


ATOM
672
CG
ASP
1133 
−45.378
−10.475
−17.104 
44.34
C


ATOM
673
OD1
ASP
1133 
−45.471 
−9.672
−18.073
46.2
O


ATOM
674
OD2
ASP
1133 
−44.832
−10.103
−16.036
45.51
O


ATOM
675
C
ASP
1133 
−45.599 
−14.51
−16.559
32.78
C


ATOM
676
O
ASP
1133 
−46.634
−14.894
−17.119
29.59
O


ATOM
677
N
PHE
1134 
−44.642
−15.327
−16.103
27.86
N


ATOM
678
CA
PHE
1134 
−44.601
−16.796
−16.002
22.57
C


ATOM
679
CB
PHE
1134 
−43.753
−17.483
−17.107 
22.44
C


ATOM
680
CG
PHE
1134 
−44.565
−18.066
−18.259
19.89
C


ATOM
681
CD1
PHE
1134 
−43.967
−18.296
−19.503 
16.65
C


ATOM
682
CD2
PHE
1134 
−45.934
−18.311
−18.126 
18.05
C


ATOM
683
CE1
PHE
1134 
−44.725
−18.745
−20.598
15.13
C


ATOM
684
CE2
PHE
1134 
−46.697
−18.762
−19.214
16.83
C


ATOM
685
CZ
PHE
1134 
−46.092
−18.973
−20.449 
16.75
C


ATOM
686
C
PHE
1134 
−43.795
−16.804
−14.689
19.23
C


ATOM
687
O
PHE
1134 
−42.732
−16.175
−14.607
15.87
O


ATOM
688
N
SER
1135 
−44.293
−17.468
−13.656
15.8
N


ATOM
689
CA
SER
1135 
−43.575
−17.473
−12.397
13.93
C


ATOM
690
CB
SER
1135 
−44.165
−16.454
−11.426
12.94
C


ATOM
691
OG
SER
1135 
−43.254
−16.177
−10.383 
15.88
O


ATOM
692
C
SER
1135 
−43.654
−18.829
−11.775 
12.54
C


ATOM
693
O
SER
1135 
−44.695
−19.221
−11.262
11.79
O


ATOM
694
N
HIS
1136 
−42.548
−19.547
−11.831 
11.97
N


ATOM
695
CA
HIS
1136 
−42.491
−20.859
−11.253
12.4
C


ATOM
696
CB
HIS
1136 
−43.068 
−21.88
−12.226
10.91
C


ATOM
697
CG
HIS
1136 
−43.199 
−23.24
−11.633
12.1
C


ATOM
698
CD2
HIS
1136 
−44.246
−23.858
−11.036
10.8
C


ATOM
699
ND1
HIS
1136 
−42.127
−24.097
−11.518 
10.52
N


ATOM
700
CE1
HIS
1136 
−42.506
−25.185
−10.872
11.14
C


ATOM
701
NE2
HIS
1136 
−43.786
−25.065
−10.569
11.88
N


ATOM
702
C
HIS
1136 
−41.034
−21.143
−10.917
13.17
C


ATOM
703
O
HIS
1136 
−40.127
−20.784 
−11.67
12.81
O


ATOM
704
N
PRO
1137
−40.79
−21.774 
−9.763
14.54
N


ATOM
705
CD
PRO
1137 
−41.762
−22.325 
−8.797
13.56
C


ATOM
706
CA
PRO
1137 
−39.414
−22.076 
−9.36
15.38
C


ATOM
707
CB
PRO
1137 
−39.597
−22.831 
−8.035
13.45
C


ATOM
708
CG
PRO
1137 
−40.974
−23.438 
−8.155
17.2
C


ATOM
709
C
PRO
1137 
−38.568
−22.842
−10.386 
15.05
C


ATOM
710
O
PRO
1137 
−37.334
−22.756
−10.366
14.8
O


ATOM
711
N
ASN
1138
−39.23
−23.571
−11.286
14.53
N


ATOM
712
CA
ASN
1138 
−38.546
−24.338
−12.328
13.54
C


ATOM
713
CB
ASN
1138 
−38.979
−25.801
−12.281 
11.91
C


ATOM
714
CG
ASN
1138 
−38.491
−26.491
−11.042
15.12
C


ATOM
715
OD1
ASN
1138 
−39.279
−26.876
−10.183
14.55
O


ATOM
716
ND2
ASN
1138 
−37.176
−26.639
−10.928
15.25
N


ATOM
717
C
ASN
1138 
−38.752
−23.804
−13.736 
12.76
C


ATOM
718
O
ASN
1138 
−38.733
−24.573
−14.699
13.13
O


ATOM
719
N
VAL
1139 
−38.967
−22.493
−13.836
14.58
N


ATOM
720
CA
VAL
1139 
−39.148
−21.797
−15.115
14.5
C


ATOM
721
CB
VAL
1139 
−40.634
−21.332
−15.343 
16.08
C


ATOM
722
CG1
VAL
1139 
−40.715
−20.404
−16.561
14.73
C


ATOM
723
CG2
VAL
1139 
−41.543
−22.544
−15.556
14.08
C


ATOM
724
C
VAL
1139 
−38.246 
−20.56
−15.074 
15.17
C


ATOM
725
O
VAL
1139 
−38.351
−19.736
−14.157
13.04
O


ATOM
726
N
LEU
1140 
−37.358
−20.427
−16.059
14.62
N


ATOM
727
CA
LEU
1140 
−36.445
−19.281
−16.098
13.44
C


ATOM
728
CB
LEU
1140 
−35.213 
−19.59
−16.962
12.31
C


ATOM
729
CG
LEU
1140 
−34.085
−18.546
−16.992
10.46
C


ATOM
730
CD1
LEU
1140 
−33.328
−18.594
−15.684 
13.12
C


ATOM
731
CD2
LEU
1140 
−33.128 
−18.82
−18.148
9.58
C


ATOM
732
C
LEU
1140 
−37.118
−18.024
−16.634
14.11
C


ATOM
733
O
LEU
1140 
−37.551
−17.962
−17.786
14.02
O


ATOM
734
N
SER
1141 
−37.201
−17.012
−15.791
15.03
N


ATOM
735
CA
SER
1141 
−37.794
−15.759
−16.214
17.47
C


ATOM
736
CB
SER
1141 
−38.961
−15.397
−15.302 
17.42
C


ATOM
737
OG
SER
1141 
−39.908
−16.448
−15.288
16.21
O


ATOM
738
C
SER
1141
−36.75
−14.654
−16.178
18.33
C


ATOM
739
O
SER
1141 
−35.783
−14.702
−15.405 
19.08
O


ATOM
740
N
LEU
1142 
−36.949
−13.664
−17.031
18.51
N


ATOM
741
CA
LEU
1142 
−36.046
−12.537
−17.079 
20.96
C


ATOM
742
CB
LEU
1142 
−36.333
−11.641
−18.288
24.4
C


ATOM
743
CG
LEU
1142 
−37.635
−11.494
−19.093
26.67
C


ATOM
744
CD1
LEU
1142 
−37.157
−11.596
−20.531 
28.07
C


ATOM
745
CD2
LEU
1142 
−38.723
−12.554 
−18.83
30.08
C


ATOM
746
C
LEU
1142 
−36.199
−11.719
−15.831
20.09
C


ATOM
747
O
LEU
1142 
−37.276
−11.671
−15.243
18.69
O


ATOM
748
N
LEU
1143 
−35.102
−11.099
−15.418 
19.75
N


ATOM
749
CA
LEU
1143 
−35.129
−10.217
−14.275 
18.51
C


ATOM
750
CB
LEU
1143 
−33.714
−10.014 
−13.7
20.09
C


ATOM
751
CG
LEU
1143 
−33.069
−11.105
−12.816
20.67
C


ATOM
752
CD1
LEU
1143 
−31.795
−10.548 
−12.2
19.71
C


ATOM
753
CD2
LEU
1143 
−34.021
−11.539
−11.693
20.92
C


ATOM
754
C
LEU
1143 
−35.662 
−8.929
−14.905
18.23
C


ATOM
755
O
LEU
1143 
−36.354 
−8.141
−14.258
18.44
O


ATOM
756
N
GLY
1144 
−35.359 
−8.731
−16.191
16.4
N


ATOM
757
CA
GLY
1144 
−35.837 
−7.543
−16.874
14.04
C


ATOM
758
C
GLY
1144 
−35.224 
−7.371
−18.245
15.5
C


ATOM
759
O
GLY
1144 
−34.485 
−8.226
−18.713
15.81
O


ATOM
760
N
ILE
1145 
−35.539 
−6.274
−18.911 
16.87
N


ATOM
761
CA
ILE
1145 
−34.972 
−6.031
−20.225
18.26
C


ATOM
762
CB
ILE
1145 
−35.981 
−6.403
−21.409
19.17
C


ATOM
763
CG2
ILE
1145 
−36.919 
−7.552
−21.014
19.39
C


ATOM
764
CG1
ILE
1145 
−36.829 
−5.188
−21.848
21.36
C


ATOM
765
CD
ILE
1145 
−37.787 
−4.592 
−20.8
25.83
C


ATOM
766
C
ILE
1145 
−34.699 
−4.549 
−20.34
18.79
C


ATOM
767
O
ILE
1145 
−35.295 
−3.764
−19.609
19.26
O


ATOM
768
N
CYS
1146 
−33.713 
−4.129 
−21.11 
21.57
N


ATOM
769
CA
CYS
1146 
−33.808 
−2.713
−21.347
24.57
C


ATOM
770
CB
CYS
1146 
−32.932 
−1.749
−20.568 
27.61
C


ATOM
771
SG
CYS
1146 
−33.831 
−0.088
−20.586
32.88
S


ATOM
772
C
CYS
1146 
−33.743 
−2.422
−22.789
23.95
C


ATOM
773
O
CYS
1146 
−33.051 
−3.059
−23.594 
24.57
O


ATOM
774
N
LEU
1147 
−34.617 
−1.474
−23.069 
23.64
N


ATOM
775
CA
LEU
1147 
−34.914 
−0.935
−24.363
23.73
C


ATOM
776
CB
LEU
1147 
−36.373 
−0.494
−24.408
23.23
C


ATOM
777
CG
LEU
1147 
−37.678 
−1.312
−24.387
24.45
C


ATOM
778
CD1
LEU
1147 
−37.461 
−2.649
−25.062
23.58
C


ATOM
779
CD2
LEU
1147 
−38.205 
−1.491
−22.981
24.44
C


ATOM
780
C
LEU
1147 
−34.067
0.269 
−24.673
23.59
C


ATOM
781
O
LEU
1147 
−34.394 
1.389 
−24.275
23.87
O


ATOM
782
N
ARG
1148 
−33.001
0.038 
−25.412
23.12
N


ATOM
783
CA
ARG
1148 
−32.106
1.095 
−25.808
22.97
C


ATOM
784
CB
ARG
1148 
−30.734 
0.495 
−25.988
23.4
C


ATOM
785
CG
ARG
1148
−30.35 
−0.366
−24.817
24.2
C


ATOM
786
CD
ARG
1148 
−28.914 
−0.697
−24.921 
21.72
C


ATOM
787
NE
ARG
1148 
−28.681 
−1.755
−25.884 
20.32
N


ATOM
788
CZ
ARG
1148 
−27.484 
−2.001
−26.385 
20.41
C


ATOM
789
NH1
ARG
1148 
−26.471 
−1.248
−25.996
19.37
N


ATOM
790
NH2
ARG
1148 
−27.284 
−2.999
−27.237 
19.66 
N


ATOM
791
C
ARG
1148 
−32.534
1.748
−27.12
22.97 
C


ATOM
792
O
ARG
1148 
−33.294
1.182 
−27.908 
21.03 
O


ATOM
793
N
SER
1149 
−32.069
2.956 
−27.361
23.25 
N


ATOM
794
CA
SER
1149 
−32.407 
3.517 
−28.637
23.55
C


ATOM
795
CB
SER
1149 
−32.661
4.995
−28.55 
24.41 
C


ATOM
796
OG
SER
1149 
−31.484
5.636 
−28.145
25.43
O


ATOM
797
C
SER
1149 
−31.292 
3.142 
−29.624 
23.14
C


ATOM
798
O
SER
1149 
−31.555
3.159 
−30.796
23.95 
O


ATOM
799
N
GLU
1150 
−30.052 
2.888 
−29.203
23.72 
N


ATOM
800
CA
GLU
1150 
−29.119
2.289
−30.16
25.39
C


ATOM
801
CB
GLU
1150 
−27.729
2.816 
−30.061
27.71 
C


ATOM
802
CG
GLU
1150 
−27.793 
4.064 
−29.446 
32.33
C


ATOM
803
CD
GLU
1150 
−27.698
5.005 
−30.524
35.64 
C


ATOM
804
OE1
GLU
1150 
−26.732
5.794 
−30.561
34.51
O


ATOM
805
OE2
GLU
1150 
−28.587
4.89 
−31.384
37
O


ATOM
806
C
GLU
1150 
−28.961
0.921 
−29.518
23.45
C


ATOM
807
O
GLU
1150
−28.64 
0.859 
−28.325 
21.36 
O


ATOM
808
N
GLY
1151 
−28.982 
−0.078
−30.413
22.51
N


ATOM
809
CA
GLY
1151 
−28.828 
−1.495
−30.147
21.13 
C


ATOM
810
C
GLY
1151 
−30.042 
−2.16 
−29.833
20.26
C


ATOM
811
O
GLY
1151 
−30.916 
−1.448
−29.502 
20.28
O


ATOM
812
N
SER
1152 
−30.155 
−3.445 
−30.24 
20.15 
N


ATOM
813
CA
SER
1152 
−31.201 
−4.317 
−29.94
19.17
C


ATOM
814
CB
SER
1152 
−30.704 
−5.674
−30.274
20.12 
C


ATOM
815
OG
SER
1152 
−29.814 
−5.608
−31.375
20.17
O


ATOM
816
C
SER
1152 
−31.474 
−4.253
−28.464
18.39
C


ATOM
817
O
SER
1152 
−30.637 
−3.799 
−27.66 
15.67 
O


ATOM
818
N
PRO
1153 
−32.619 
−4.743
−28.024 
18.17
N


ATOM
819
CD
PRO
1153 
−33.834 
−4.874
−28.851 
15.64 
C


ATOM
820
CA
PRO
1153 
−32.914 
−4.755
−26.603 
16.33
C


ATOM
821
CB
PRO
1153 
−34.306 
−5.346
−26.545 
18.14
C


ATOM
822
CG
PRO
1153 
−34.939 
−4.917
−27.824 
17.45
C


ATOM
823
C
PRO
1153 
−31.918 
−5.665
−25.921
17.54
C


ATOM
824
O
PRO
1153 
−31.433 
−6.614
−26.549 
17.31
O


ATOM
825
N
LEU
1154 
−31.624 
−5.412
−24.651 
16.29 
N


ATOM
826
CA
LEU
1154 
−30.743 
−6.284
−23.875 
16.17
C


ATOM
827
CB
LEU
1154 
−29.845 
−5.47 
−22.952 
16.61 
C


ATOM
828
CG
LEU
1154 
−28.429 
−5.058
−23.319 
16.57
C


ATOM
829
CD1
LEU
1154 
−28.235 
−4.914
−24.811 
15.54
C


ATOM
830
CD2
LEU
1154 
−28.161 
−3.773
−22.572 
15.34
C


ATOM
831
C
LEU
1154 
−31.663 
−7.095
−22.962
15.58 
C


ATOM
832
O
LEU
1154 
−32.679 
−6.569
−22.521
15.77
O


ATOM
833
N
VAL
1155 
−31.348 
−8.362
−22.703
14.14
N


ATOM
834
CA
VAL
1155 
−32.147 
−9.128
−21.742 
14.36
C


ATOM
835
CB
VAL
1155 
−32.666
−10.516
−22.236
16.13
C


ATOM
836
CG1
VAL
1155 
−34.096
−10.383
−22.707
17.55
C


ATOM
837
CG2
VAL
1155 
−31.778 
−11.09 
−23.31
14.8 
C


ATOM
838
C
VAL
1155
−31.24 
−9.405 
−20.56 
13.32
C


ATOM
839
O
VAL
1155 
−30.046 
−9.654
−20.728 
12.82 
O


ATOM
840
N
VAL
1156 
−31.817 
−9.344
−19.366 
13.23
N


ATOM
841
CA
VAL
1156 
−31.095 
−9.583
−18.123
13.25
C


ATOM
842
CB
VAL
1156 
−31.197 
−8.352 
−17.18
11.59
C


ATOM
843
CG1
VAL
1156 
−30.163 
−8.455
−16.064
9.84
C


ATOM
844
CG2
VAL
1156 
−31.001 
−7.072
−17.976
10.35
C


ATOM
845
C
VAL
1156 
−31.713
−10.806
−17.432 
13.41
C


ATOM
846
O
VAL
1156 
−32.897
−10.813
−17.102 
12.45
O


ATOM
847
N
LEU
1157 
−30.904
−11.839
−17.228
14.42
N


ATOM
848
CA
LEU
1157 
−31.358
−13.065
−16.587
14.54
C


ATOM
849
CB
LEU
1157 
−31.107
−14.235
−17.529
17.37
C


ATOM
850
CG
LEU
1157 
−32.159
−14.084
−18.616
17.45
C


ATOM
851
CD1
LEU
1157 
−31.523
−13.964 
−19.97 
15.68
C


ATOM
852
CD2
LEU
1157
−33.12
−15.235 
−18.51
14.04
C


ATOM
853
C
LEU
1157 
−30.666
−13.312
−15.263
15.03
C


ATOM
854
O
LEU
1157 
−29.591
−12.768
−15.021 
14.87
O


ATOM
855
N
PRO
1158
−31.29 
−14.11
−14.369 
15.01
N


ATOM
856
CD
PRO
1158 
−32.657
−14.659
−14.452 
14.36
C


ATOM
857
CA
PRO
1158 
−30.676
−14.411
−13.067
14.63
C


ATOM
858
CB
PRO
1158 
−31.664 
−15.38
−12.424
12.4
C


ATOM
859
CG
PRO
1158 
−32.975
−14.977
−13.006 
16.67
C


ATOM
860
C
PRO
1158 
−29.354
−15.117 
−13.36
14.38
C


ATOM
861
O
PRO
1158
−29.27
−15.852
−14.346
14.05
O


ATOM
862
N
TYR
1159 
−28.328
−14.908
−12.544 
14.53
N


ATOM
863
CA
TYR
1159 
−27.079
−15.618
−12.797 
16.89
C


ATOM
864
CB
TYR
1159 
−25.916
−15.097
−11.927 
17.44
C


ATOM
865
CG
TYR
1159 
−24.597
−15.847
−12.146
20.62
C


ATOM
866
CD1
TYR
1159
−24.05
−15.994
−13.426
19.72
C


ATOM
867
CE1
TYR
1159 
−22.843
−16.704
−13.627
21.21
C


ATOM
868
CD2
TYR
1159 
−23.906 
−16.42
−11.072
20.45
C


ATOM
869
CE2
TYR
1159 
−22.705
−17.124
−11.266 
19.01
C


ATOM
870
CZ
TYR
1159
−22.18
−17.266
−12.539
20.38
C


ATOM
871
OH
TYR
1159 
−21.009
−17.988
−12.714 
18.95
O


ATOM
872
C
TYR
1159 
−27.345
−17.084
−12.475 
16.92
C


ATOM
873
O
TYR
1159 
−27.794
−17.419
−11.377
17.08
O


ATOM
874
N
MET
1160 
−27.097
−17.939
−13.463
17.77
N


ATOM
875
CA
MET
1160 
−27.272
−19.382
−13.334
19.63
C


ATOM
876
CB
MET
1160 
−28.094
−19.903
−14.538
20.87
C


ATOM
877
CG
MET
1160
−29.59
−19.473
−14.517
23.25
C


ATOM
878
SD
MET
1160 
−30.392
−20
−12.946
26.21
S


ATOM
879
CE
MET
1160 
−31.976
−19.029
−12.819
25.57
C


ATOM
880
C
MET
1160 
−25.838
−19.959
−13.289
19.44
C


ATOM
881
O
MET
1160 
−25.262
−20.285
−14.323
19.44
O


ATOM
882
N
LYS
1161 
−25.283
−20.054 
−12.07 
20.74
N


ATOM
883
CA
LYS
1161 
−23.897
−20.517
−11.782 
21.83
C


ATOM
884
CB
LYS
1161 
−23.718
−20.814
−10.255
23.08
C


ATOM
885
CG
LYS
1161 
−22.277
−21.256
−9.7
26.14
C


ATOM
886
CD
LYS
1161 
−22.276 
−21.43 
−8.113
29.21
C


ATOM
887
CE
LYS
1161 
−21.135
−22.295 
−7.464
30.75
C


ATOM
888
NZ
LYS
1161 
−21.405
−22.621 
−5.992 
32.69
N


ATOM
889
C
LYS
1161 
−23.378
−21.704
−12.581 
21.45
C


ATOM
890
O
LYS
1161 
−22.233
−21.692
−13.029
22.38
O


ATOM
891
N
HIS
1162 
−24.209
−22.721
−12.768
21.1
N


ATOM
892
CA
HIS
1162
−23.77
−23.916
−13.475 
21.05
C


ATOM
893
CB
HIS
1162 
−24.271
−25.147
−12.729 
21.67
C


ATOM
894
CG
HIS
1162
−23.95 
−25.13
−11.267
23.58
C


ATOM
895
CD2
HIS
1162
−24.75
−24.981
−10.184
25.8
C


ATOM
896
ND1
HIS
1162 
−22.664
−25.242
−10.782
22.88
N


ATOM
897
CE1
HIS
1162 
−22.686
−25.164 
−9.461 
24.94
C


ATOM
898
NE2
HIS
1162
−23.94
−25.005 
−9.074
27.06
N


ATOM
899
C
HIS
1162 
−24.145
−24.003
−14.948 
20.46
C


ATOM
900
O
HIS
1162 
−23.893
−25.021
−15.601
20.52
O


ATOM
901
N
GLY
1163 
−24.748
−22.944
−15.473 
16.19
N


ATOM
902
CA
GLY
1163 
−25.101
−22.941
−16.879
15.75
C


ATOM
903
C
GLY
1163 
−26.153
−23.945
−17.287 
14.03
C


ATOM
904
O
GLY
1163 
−27.039
−24.295
−16.505
14.31
O


ATOM
905
N
ASP
1164 
−26.054
−24.402
−18.529
13.99
N


ATOM
906
CA
ASP
1164 
−27.003
−25.356
−19.055 
15.09
C


ATOM
907
CB
ASP
1164 
−26.891
−25.453
−20.586
17.44
C


ATOM
908
CG
ASP
1164 
−25.468
−25.264
−21.092
20.23
C


ATOM
909
OD1
ASP
1164 
−24.817
−24.255
−20.729 
26.07
O


ATOM
910
OD2
ASP
1164 
−25.007
−26.121
−21.872
21.73
O


ATOM
911
C
ASP
1164 
−26.853
−26.719
−18.399
15.19
C


ATOM
912
O
ASP
1164 
−25.765
−27.128
−17.969
11.3
O


ATOM
913
N
LEU
1165 
−27.979
−27.399 
−18.29
15.65
N


ATOM
914
CA
LEU
1165 
−28.022
−28.704
−17.674 
17.38
C


ATOM
915
CB
LEU
1165 
−29.472
−29.172
−17.594
19.29
C


ATOM
916
CG
LEU
1165 
−29.893
−30.157
−16.507 
23.06
C


ATOM
917
CD1
LEU
1165 
−29.794
−29.502
−15.132
24.16
C


ATOM
918
CD2
LEU
1165 
−31.336
−30.597
−16.783 
22.91
C


ATOM
919
C
LEU
1165 
−27.191
−29.661
−18.523
18.34
C


ATOM
920
O
LEU
1165 
−26.598
−30.599
−17.999 
16.81
O


ATOM
921
N
ARG
1166 
−27.115
−29.426
−19.828 
16.61
N


ATOM
922
CA
ARG
1166 
−26.328
−30.347
−20.631 
20.77
C


ATOM
923
CB
ARG
1166
−26.59
−30.209
−22.129
21.19
C


ATOM
924
CG
ARG
1166 
−25.748
−31.255
−22.956
29.35
C


ATOM
925
CD
ARG
1166 
−24.754
−30.446
−23.364 
33.96
C


ATOM
926
NE
ARG
1166 
−23.929
−30.501 
−24.55
41.69
N


ATOM
927
CZ
ARG
1166 
−23.013
−31.595
−24.116
43.95
C


ATOM
928
NH1
ARG
1166 
−22.272 
−31.74
−25.146
44.72
N


ATOM
929
NH2
ARG
1166 
−23.215
−32.382
−23.404 
44.74
N


ATOM
930
C
ARG
1166 
−24.826
−30.272
−20.398
19.99
C


ATOM
931
O
ARG
1166 
−24.174
−31.312 
−20.34
19.94
O


ATOM
932
N
ASN
1167 
−24.262
−29.069
−20.302
20.09
N


ATOM
933
CA
ASN
1167 
−22.826
−28.947
−20.049
19.35
C


ATOM
934
CB
ASN
1167
−22.35
−27.498
−20.026 
21.75
C


ATOM
935
CG
ASN
1167 
−22.323 
−26.86 
−21.38
26.57
C


ATOM
936
OD1
ASN
1167
−22.67 
−25.69
−21.512
29.34
O


ATOM
937
ND2
ASN
1167
−21.89
−27.601
−22.393
26.01
N


ATOM
938
C
ASN
1167 
−22.595
−29.437
−18.655 
19.05
C


ATOM
939
O
ASN
1167 
−21.566
−30.028
−18.345 
20.21
O


ATOM
940
N
PHE
1168 
−23.551
−29.154
−17.788
17
N


ATOM
941
CA
PHE
1168 
−23.364
−29.544
−16.419
16.81 
C


ATOM
942
CB
PHE
1168 
−24.575
−29.188
−15.577 
16.11
C


ATOM
943
CG
PHE
1168 
−24.368 
−29.47
−14.139
17.57
C


ATOM
944
CD1
PHE
1168 
−23.567
−28.633
−13.361 
17.68
C


ATOM
945
CD2
PHE
1168 
−24.888
−30.625
−13.572 
17.09
C


ATOM
946
CE1
PHE
1168 
−23.286
−28.954
−12.042
16.42
C


ATOM
947
CE2
PHE
1168 
−24.613
−30.953
−12.258
16.65
C


ATOM
948
CZ
PHE
1168 
−23.809
−30.118 
−11.49
16.79
C


ATOM
949
C
PHE
1168 
−23.054
−31.024
−16.257
17.57 
C


ATOM
950
O
PHE
1168 
−22.004
−31.379
−15.725
17.47
O


ATOM
951
N
ILE
1169 
−23.967
−31.872
−16.733
18.48
N


ATOM
952
CA
ILE
1169 
−23.849
−33.323
−16.618 
19.22 
C


ATOM
953
CB
ILE
1169 
−25.221
−33.994
−16.911 
18.85 
C


ATOM
954
CG2
ILE
1169 
−26.323
−33.291
−16.107 
20.15
C


ATOM
955
CG1
ILE
1169 
−25.562
−33.883
−18.398
19.02 
C


ATOM
956
CD
ILE
1169 
−26.743
−34.735
−18.851
21.26
C


ATOM
957
C
ILE
1169 
−22.742
−33.938 
−17.49 
20.6
C


ATOM
958
O
ILE
1169 
−22.254
−35.022
−17.203 
21.94
O


ATOM
959
N
ARG
1170 
−22.346
−33.234
−18.547
24.45
N


ATOM
960
CA
ARG
1170 
−21.269
−33.682
−19.438
27.69
C


ATOM
961
CB
ARG
1170 
−21.419
−32.978
−20.852
28.31 
C


ATOM
962
CG
ARG
1170 
−22.013
−33.766 
−22.12
33.76
C


ATOM
963
CD
ARG
1170 
−21.062
−33.577
−23.383
38.78 
C


ATOM
964
NE
ARG
1170 
−21.589
−33.737
−24.767 
44.17
N


ATOM
965
CZ
ARG
1170 
−21.776
−34.883
−25.421
45.25
C


ATOM
966
NH1
ARG
1170 
−21.509
−36.042
−24.837 
45.69 
N


ATOM
967
NH2
ARG
1170 
−22.158
−34.868
−26.699 
46.99
N


ATOM
968
C
ARG
1170 
−19.801 
−33.42 
−18.85
28.11 
C


ATOM
969
O
ARG
1170 
−18.863
−33.886
−19.461
28.96 
O


ATOM
970
N
ASN
1171 
−19.616
−32.761
−17.676
31.77
N


ATOM
971
CA
ASN
1171 
−18.278
−32.351
−17.071 
35.84 
C


ATOM
972
CB
ASN
1171
−18.34
−30.837
−16.751
35.9
C


ATOM
973
CG
ASN
1171 
−17.124
−30.291
−15.963 
36.69 
C


ATOM
974
OD1
ASN
1171 
−15.967 
−30.5 
−16.337 
38.54
O


ATOM
975
ND2
ASN
1171 
−17.402
−29.552
−14.892 
38.57
N


ATOM
976
C
ASN
1171 
−17.734 
−33.05
−15.837
38.26
C


ATOM
977
O
ASN
1171 
−18.335
−33.996 
−15.33 
37.47
O


ATOM
978
N
GLU
1172 
−16.634
−32.526
−15.299 
42.42 
N


ATOM
979
CA
GLU
1172 
−16.084 
−33.21
−14.185
44.62 
C


ATOM
980
CB
GLU
1172 
−14.662
−33.533 
−14.33
47.34 
C


ATOM
981
CG
GLU
1172 
−14.476
−34.899
−14.945
51.52
C


ATOM
982
CD
GLU
1172
−13 
−35.209
−15.021
54.32
C


ATOM
983
OE1
GLU
1172 
−12.209
−34.331
−14.607 
56.07
O


ATOM
984
OE2
GLU
1172 
−12.619
−36.306
−15.481
55.09
O


ATOM
985
C
GLU
1172 
−16.394
−32.813
−12.868
45.4
C


ATOM
986
O
GLU
1172 
−15.676
−32.606 
−11.9
45.64
O


ATOM
987
N
THR
1173
−17.5 
−33.46
−12.882 
45.94
N


ATOM
988
CA
THR
1173 
−18.303
−33.412
−11.801
45.89 
C


ATOM
989
CB
THR
1173
−18.9
−31.986
−11.806 
48.24 
C


ATOM
990
OG1
THR
1173 
−19.351
−31.627
−13.121 
51.69
O


ATOM
991
CG2
THR
1173 
−17.814
−30.958
−11.388
49.83
C


ATOM
992
C
THR
1173 
−19.225
−34.615
−12.011
44.29
C


ATOM
993
O
THR
1173 
−19.564
−34.981
−13.109
44.1
O


ATOM
994
N
HIS
1174 
−19.669
−35.201 
−10.93
42.7
N


ATOM
995
CA
HIS
1174 
−20.433
−36.472
−10.943
41.89
C


ATOM
996
CB
HIS
1174 
−19.872
−37.118 
−9.842
39.55
C


ATOM
997
CG
HIS
1174 
−18.497
−37.364
−10.145
37.93
C


ATOM
998
CD2
HIS
1174 
−18.032
−38.092
−11.169
36.9
C


ATOM
999
ND1
HIS
1174
−17.45
−36.607 
−9.675
37.27
N


ATOM
1000
CE1
HIS
1174 
−16.388
−36.875
−10.408
37.46
C


ATOM
1001
NE2
HIS
1174
−16.72
−37.767
−11.321
38.87
N


ATOM
1002
C
HIS
1174 
−21.626
−36.098
−10.522
43.19
C


ATOM
1003
O
HIS
1174 
−22.216
−36.764 
−9.624
40.83
O


ATOM
1004
N
ASN
1175 
−22.132 
−35.21
−11.301
45
N


ATOM
1005
CA
ASN
1175 
−22.901
−34.607
−10.372
46.48
C


ATOM
1006
CB
ASN
1175
−22.07
−33.389
−10.053
48.49
C


ATOM
1007
CG
ASN
1175 
−21.478
−33.586 
−8.735
50.32
C


ATOM
1008
OD1
ASN
1175 
−22.172
−33.645 
−7.717
50.43
O


ATOM
1009
ND2
ASN
1175 
−20.165
−33.807 
−8.744
52.85
N


ATOM
1010
C
ASN
1175 
−24.337
−34.512
−10.263
45.16
C


ATOM
1011
O
ASN
1175 
−24.947
−33.607 
−9.572
45.76
O


ATOM
1012
N
PRO
1176 
−24.862
−35.721
−10.584
42.63
N


ATOM
1013
CD
PRO
1176 
−25.399 
−35.28 
−11.89
42.59
C


ATOM
1014
CA
PRO
1176 
−24.501
−37.027
−11.106
39.43
C


ATOM
1015
CB
PRO
1176 
−23.589
−36.804
−12.308 
40.33
C


ATOM
1016
CG
PRO
1176 
−24.229
−35.822
−12.818
41.13
C


ATOM
1017
C
PRO
1176 
−24.454
−38.352
−10.571
35.88
C


ATOM
1018
O
PRO
1176 
−24.315
−39.218
−11.379
36.9
O


ATOM
1019
N
THR
1177 
−24.742
−38.551 
−9.294 
31.21
N


ATOM
1020
CA
THR
1177 
−25.219
−39.893 
−8.976
27.86
C


ATOM
1021
CB
THR
1177 
−25.691
−39.919 
−7.539
28.3
C


ATOM
1022
OG1
THR
1177 
−26.718
−38.926 
−7.34
28.69
O


ATOM
1023
CG2
THR
1177 
−24.519 
−39.58 
−6.658 
29.42
C


ATOM
1024
C
THR
1177 
−26.551
−39.987 
−9.875 
25.62
C


ATOM
1025
O
THR
1177 
−27.064
−38.967
−10.392 
24.15
O


ATOM
1026
N
VAL
1178 
−27.117 
−41.19
−10.018
23.06
N


ATOM
1027
CA
VAL
1178 
−28.349
−41.394
−10.787
20
C


ATOM
1028
CB
VAL
1178
−28.65
−42.913
−10.982 
21.95
C


ATOM
1029
CG1
VAL
1178 
−30.109
−43.124
−11.338
22.35
C


ATOM
1030
CG2
VAL
1178 
−27.774 
−43.49
−12.098 
21.65
C


ATOM
1031
C
VAL
1178 
−29.551
−40.708
−10.115
19.06
C


ATOM
1032
O
VAL
1178 
−30.457
−40.256
−10.801 
14.69
O


ATOM
1033
N
LYS
1179 
−29.555 
−40.61 
−8.784
17.59
N


ATOM
1034
CA
LYS
1179 
−30.674 
−39.95 
−8.098 
17.37
C


ATOM
1035
CB
LYS
1179 
−30.595
−40.091 
−6.573
15.86
C


ATOM
1036
CG
LYS
1179 
−31.893
−39.607 
−5.945
17.43
C


ATOM
1037
CD
LYS
1179 
−31.973
−39.615 
−4.431 
18.96
C


ATOM
1038
CE
LYS
1179 
−33.444
−39.433 
−4.033
19.52
C


ATOM
1039
NZ
LYS
1179 
−33.713
−39.473 
−2.586
23.06
N


ATOM
1040
C
LYS
1179 
−30.722
−38.466 
−8.432 
16.18
C


ATOM
1041
O
LYS
1179 
−31.795
−37.904 
−8.696
16
O


ATOM
1042
N
ASP
1180 
−29.545 
−37.85 
−8.368
16.29 
N


ATOM
1043
CA
ASP
1180 
−29.319 
−36.44 
−8.672
16.7
C


ATOM
1044
CB
ASP
1180
−27.8
−36.166 
−8.754
21.3 
C


ATOM
1045
CG
ASP
1180 
−27.093
−36.177 
−7.382 
24.33 
C


ATOM
1046
OD1
ASP
1180 
−25.843
−36.324 
−7.358 
24.63 
O


ATOM
1047
OD2
ASP
1180 
−27.766 
−36.02 
−6.34
25.45
O


ATOM
1048
C
ASP
1180 
−29.941
−36.166
−10.046
16.85
C


ATOM
1049
O
ASP
1180 
−30.788
−35.284
−10.204 
17.45
O


ATOM
1050
N
LEU
1181 
−29.495
−36.942
−11.031
14.01
N


ATOM
1051
CA
LEU
1181 
−29.948
−36.844
−12.417
15.35
C


ATOM
1052
CB
LEU
1181 
−29.241
−37.908
−13.252
12.86
C


ATOM
1053
CG
LEU
1181 
−28.102
−37.644
−14.236 
16.66 
C


ATOM
1054
CD1
LEU
1181 
−27.429
−36.281
−14.107 
14.78
C


ATOM
1055
CD2
LEU
1181 
−27.138
−38.797
−14.016
16.96 
C


ATOM
1056
C
LEU
1181 
−31.465
−36.989
−12.604
15.84
C


ATOM
1057
O
LEU
1181 
−32.057
−36.288
−13.425 
13.36
O


ATOM
1058
N
ILE
1182 
−32.083
−37.924
−11.884 
16.57 
N


ATOM
1059
CA
ILE
1182 
−33.535
−38.106
−11.971
18.12
C


ATOM
1060
CB
ILE
1182 
−34.009
−39.375
−11.205
19.44 
C


ATOM
1061
CG2
ILE
1182 
−35.549
−39.429
−11.179
18.44 
C


ATOM
1062
CG1
ILE
1182 
−33.477
−40.659
−11.866 
22.47 
C


ATOM
1063
CD
ILE
1182
−32.11
−40.629
−12.516
26.66
C


ATOM
1064
C
ILE
1182 
−34.088 
−36.87
−11.276 
17.03
C


ATOM
1065
O
ILE
1182 
−35.165
−36.364
−11.611
15.91 
O


ATOM
1066
N
GLY
1183 
−33.315
−36.388
−10.307
15.99
N


ATOM
1067
CA
GLY
1183 
−33.702
−35.204 
−9.562
17.43
C


ATOM
1068
C
GLY
1183 
−33.873
−34.015
−10.488 
17.32 
C


ATOM
1069
O
GLY
1183 
−34.833
−33.258 
−10.36
16.44
O


ATOM
1070
N
PHE
1184
−32.95
−33.843
−11.427 
17.05
N


ATOM
1071
CA
PHE
1184 
−33.052
−32.724
−12.357 
17.09 
C


ATOM
1072
CB
PHE
1184 
−31.749
−32.522
−13.141
18.5 
C


ATOM
1073
CG
PHE
1184 
−30.522
−32.379
−12.283
19.66 
C


ATOM
1074
CD1
PHE
1184 
−30.502
−31.544
−11.167 
20.39 
C


ATOM
1075
CD2
PHE
1184 
−29.367
−33.075
−12.616
22.04
C


ATOM
1076
CE1
PHE
1184 
−29.335
−31.414
−10.398 
22.54 
C


ATOM
1077
CE2
PHE
1184 
−28.208
−32.956
−11.865
23.06
C


ATOM
1078
CZ
PHE
1184 
−28.186
−32.127
−10.754 
23.72
C


ATOM
1079
C
PHE
1184 
−34.199
−32.938
−13.338
15.91
C


ATOM
1080
O
PHE
1184
−34.91
−31.994
−13.682 
15.75
O


ATOM
1081
N
GLY
1185 
−34.377
−34.172
−13.794 
14.93 
N


ATOM
1082
CA
GLY
1185 
−35.457
−34.458
−14.723
15.28 
C


ATOM
1083
C
GLY
1185 
−36.789
−34.122
−14.088
15.23 
C


ATOM
1084
O
GLY
1185 
−37.713
−33.646 
−14.75
12.8
O


ATOM
1085
N
LEU
1186 
−36.864
−34.366
−12.783 
14.32 
N


ATOM
1086
CA
LEU
1186 
−38.056
−34.098
−12.006 
14.34 
C


ATOM
1087
CB
LEU
1186
−37.88 
−34.62
−10.572
13.65
C


ATOM
1088
CG
LEU
1186 
−39.029
−34.398 
−9.581 
16.71
C


ATOM
1089
CD1
LEU
1186
−40.35
−34.885
−10.173
12.78
C


ATOM
1090
CD2
LEU
1186
−38.722
−35.145
−8.28
14.5
C


ATOM
1091
C
LEU
1186
−38.351
−32.601
−11.996
14.32
C


ATOM
1092
O
LEU
1186
−39.479
−32.196
−12.256
14.05
O


ATOM
1093
N
GLN
1187
−37.351 
−31.77 
−11.71
13.6
N


ATOM
1094
CA
GLN
1187
−37.605 
−30.34
−11.698
13.35
C


ATOM
1095
CB
GLN
1187
−36.387
−29.575
−11.206
14.52
C


ATOM
1096
CG
GLN
1187
−35.823 
−30.07 
−9.902
16.14
C


ATOM
1097
CD
GLN
1187
−34.745
−29.136
−9.4
18.91
C


ATOM
1098
OE1
GLN
1187
−35.02
−27.993 
−9.054
23.4
O


ATOM
1099
NE2
GLN
1187
−33.51
−29.609 
−9.375
19
N


ATOM
1100
C
GLN
1187
−38.004
−29.829
−13.081
11.58
C


ATOM
1101
O
GLN
1187
−38.696
−28.821
−13.194
13.07
O


ATOM
1102
N
VAL
1188
−37.576
−30.506
−14.138
11.09
N


ATOM
1103
CA
VAL
1188
−37.949
−30.071
−15.492
11.72
C


ATOM
1104
CB
VAL
1188
−37.075
−30.744
−16.577
9.94
C


ATOM
1105
CG1
VAL
1188
−37.652
−30.471
−17.966
11.58
C


ATOM
1106
CG2
VAL
1188
−35.659
−30.193
−16.495
9.54
C


ATOM
1107
C
VAL
1188
−39.418
−30.373
−15.781
11.54
C


ATOM
1108
O
VAL
1188
−40.106
−29.587
−16.419
12.41
O


ATOM
1109
N
ALA
1189
−39.894
−31.519
−15.304
14.27
N


ATOM
1110
CA
ALA
1189
−41.281
−31.913
−15.513
13.61
C


ATOM
1111
CB
ALA
1189
−41.481
−33.359 
−15.09
13.82
C


ATOM
1112
C
ALA
1189
−42.195
−31.007
−14.706
13.97
C


ATOM
1113
O
ALA
1189
−43.352 
−30.79
−15.072
16.38
O


ATOM
1114
N
LYS
1190
−41.674
−30.504
−13.593
12.74
N


ATOM
1115
CA
LYS
1190
−42.434
−29.617
−12.722
15.29
C


ATOM
1116
CB
LYS
1190
−41.708
−29.434
−11.399
14.89
C


ATOM
1117
CG
LYS
1190
−42.14
−30.477
−10.409
18.23
C


ATOM
1118
CD
LYS
1190
−41.278
−30.504 
−9.175
18.47
C


ATOM
1119
CE
LYS
1190
−41.793
−31.579 
−8.246
18.95
C


ATOM
1120
NZ
LYS
1190
−41.279 
−31.37 
−6.871
20.27
N


ATOM
1121
C
LYS
1190
−42.637
−28.279
−13.398
14.43
C


ATOM
1122
O
LYS
1190
−43.721
−27.703
−13.373
15.22
O


ATOM
1123
N
GLY
1191
−41.573
−27.782
−14.001
13.21
N


ATOM
1124
CA
GLY
1191
−41.666
−26.523
−14.706
12.63
C


ATOM
1125
C
GLY
1191
−42.579
−26.713
−15.895
12.4
C


ATOM
1126
O
GLY
1191
−43.406
−25.849
−16.174
12.86
O


ATOM
1127
N
MET
1192
−42.442 
−27.85
−16.582
12.14
N


ATOM
1128
CA
MET
1192
−43.271
−28.144
−17.741
11.6
C


ATOM
1129
CB
MET
1192
−42.701
−29.326
−18.541
10.64
C


ATOM
1130
CG
MET
1192
−41.421
−29.006
−19.336
13.7
C


ATOM
1131
SD
MET
1192
−41.513
−27.621
−20.534
17.92
S


ATOM
1132
CE
MET
1192
−42.921
−28.121
−21.647
20.8
C


ATOM
1133
C
MET
1192
−44.736
−28.383
−17.363
12.32
C


ATOM
1134
O
MET
1192
−45.624
−28.038
−18.147
13.61
O


ATOM
1135
N
LYS
1193
−44.993
−28.955
−16.181
11.86
N


ATOM
1136
CA
LYS
1193
−46.373
−29.158
−15.712
12.84
C


ATOM
1137
CB
LYS
1193
−46.395
−29.822
−14.301
13.93
C


ATOM
1138
CG
LYS
1193
−47.766
−29.826
−13.567
17.85
C


ATOM
1139
CD
LYS
1193
−47.72
−30.237
−12.045
23.67
C


ATOM
1140
CE
LYS
1193 
−46.391
−29.929 
−11.3
26.38 
C


ATOM
1141
NZ
LYS
1193 
−45.901
−28.542
−10.955
30.9
N


ATOM
1142
C
LYS
1193 
−46.955
−27.734
−15.649
12.03
C


ATOM
1143
O
LYS
1193 
−48.068
−27.479
−16.108
12.04 
O


ATOM
1144
N
TYR
1194
−46.18
−26.795
−15.112
12.64
N


ATOM
1145
CA
TYR
1194 
−46.647
−25.407
−14.997
12.34 
C


ATOM
1146
CB
TYR
1194 
−45.668
−24.591
−14.147
11.64 
C


ATOM
1147
CG
TYR
1194 
−45.962 
−23.1 
−14.065 
11.89 
C


ATOM
1148
CD1
TYR
1194 
−46.907 
−22.58
−13.167
12.34 
C


ATOM
1149
CE1
TYR
1194 
−47.178
−21.199
−13.125
13.81
C


ATOM
1150
CD2
TYR
1194 
−45.304
−22.208
−14.911 
12.87 
C


ATOM
1151
CE2
TYR
1194 
−45.572 
−20.84
−14.879
12.27
C


ATOM
1152
CZ
TYR
1194 
−46.502 
−20.34
−13.994
12.63
C


ATOM
1153
OH
TYR
1194 
−46.763
−18.991
−14.015
13.8
O


ATOM
1154
C
TYR
1194 
−46.863
−24.747
−16.369 
14.72
C


ATOM
1155
O
TYR
1194 
−47.966 
−24.29
−16.668 
13.67
O


ATOM
1156
N
LEU
1195 
−45.829
−24.707
−17.205 
14.63
N


ATOM
1157
CA
LEU
1195 
−45.961
−24.114
−18.53
14.48
C


ATOM
1158
CB
LEU
1195 
−44.659
−24.313
−19.327 
11.22
C


ATOM
1159
CG
LEU
1195 
−43.558
−23.232
−19.419
12.32
C


ATOM
1160
CD1
LEU
1195 
−43.924
−22.016
−18.591
11.57
C


ATOM
1161
CD2
LEU
1195 
−42.204
−23.817
−19
9.97
C


ATOM
1162
C
LEU
1195 
−47.153 
−24.75
−19.26
14.78
C


ATOM
1163
O
LEU
1195 
−48.011
−24.048
−19.799 
15.68
O


ATOM
1164
N
ALA
1196 
−47.226
−26.077
−19.255
15.59 
N


ATOM
1165
CA
ALA
1196 
−48.323 
−26.76
−19.931
17.53
C


ATOM
1166
CB
ALA
1196 
−48.122
−28.286
−19.882 
17.48 
C


ATOM
1167
C
ALA
1196
−49.71
−26.397
−19.395
17.02
C


ATOM
1168
O
ALA
1196
−50.7 
−26.616
−20.083
18.22
O


ATOM
1169
N
SER
1197 
−49.799
−25.859
−18.181
18.14 
N


ATOM
1170
CA
SER
1197 
−51.109
−25.484
−17.646
18.76 
C


ATOM
1171
CB
SER
1197 
−51.115
−25.544
−16.114 
19.04
C


ATOM
1172
OG
SER
1197
−50.19
−24.624
−15.551 
20.46
O


ATOM
1173
C
SER
1197
−51.49
−24.081
−18.123 
18.11 
C


ATOM
1174
O
SER
1197 
−52.665
−23.732
−18.177
20.7
O


ATOM
1175
N
LYS
1198 
−50.487 
−23.29
−18.48
18.69 
N


ATOM
1176
CA
LYS
1198 
−50.698
−21.937
−18.988
19.35 
C


ATOM
1177
CB
LYS
1198 
−49.478 
−21.06
−18.689
20.72
C


ATOM
1178
CG
LYS
1198 
−49.059
−21.106
−17.24
19.87
C


ATOM
1179
CD
LYS
1198 
−50.309
−21.238
−16.407
21.44
C


ATOM
1180
CE
LYS
1198 
−50.069
−21.004
−14.947
22.31 
C


ATOM
1181
NZ
LYS
1198
−51.33
−20.451
−14.393
23.65 
N


ATOM
1182
C
LYS
1198
−50.86
−22.094
−20.488
19.76
C


ATOM
1183
O
LYS
1198 
−50.899
−21.117
−21.234
20.25
O


ATOM
1184
N
LYS
1199 
−50.943
−23.356
−20.901
19.44 
N


ATOM
1185
CA
LYS
1199 
−51.079
−23.747
−22.302
21.24
C


ATOM
1186
CB
LYS
1199 
−52.326
−23.134
−22.952 
23.73
C


ATOM
1187
CG
LYS
1199 
−53.683
−23.601
−22.468
27.68
C


ATOM
1188
CD
LYS
1199 
−54.769
−22.601
−22.926
32.24
C


ATOM
1189
CE
LYS
1199 
−55.458
−22.948
−24.274
35.47 
C


ATOM
1190
NZ
LYS
1199 
−54.653
−22.791
−25.529
34.96
N


ATOM
1191
C
LYS
1199
−49.88
−23.276
−23.119 
21.02
C


ATOM
1192
O
LYS
1199 
−50.037
−22.907
−24.277
20.05
O


ATOM
1193
N
PHE
1200 
−48.687
−23.274
−22.546
18.53
N


ATOM
1194
CA
PHE
1200 
−47.542
−22.814
−23.312
18.34
C


ATOM
1195
CB
PHE
1200 
−46.658
−21.964
−22.404 
19.51
C


ATOM
1196
CG
PHE
1200 
−45.328 
−21.61
−22.982 
18.89
C


ATOM
1197
CD1
PHE
1200 
−44.242
−22.452
−22.793
19.96
C


ATOM
1198
CD2
PHE
1200 
−45.133
−20.398
−23.634
20.92
C


ATOM
1199
CE1
PHE
1200 
−42.977
−22.092 
−23.23
21.7
C


ATOM
1200
CE2
PHE
1200 
−43.865
−20.025 
−24.08
20.16
C


ATOM
1201
CZ
PHE
1200 
−42.786
−20.872
−23.876
20.78
C


ATOM
1202
C
PHE
1200 
−46.778
−23.969
−23.946
17.03 
C


ATOM
1203
O
PHE
1200 
−46.409 
−24.92
−23.282 
16.04
O


ATOM
1204
N
VAL
1201 
−46.575
−23.887
−25.253
17.46
N


ATOM
1205
CA
VAL
1201 
−45.868
−24.933
−25.977 
18.28
C


ATOM
1206
CB
VAL
1201 
−46.586
−25.227
−27.312
17.97
C


ATOM
1207
CG1
VAL
1201 
−45.917
−26.389
−28.045
16.62
C


ATOM
1208
CG2
VAL
1201 
−48.053
−25.553
−27.018
19.79 
C


ATOM
1209
C
VAL
1201 
−44.427
−24.474 
−26.19
17.03
C


ATOM
1210
O
VAL
1201 
−44.146
−23.552
−26.951
16.94
O


ATOM
1211
N
HIS
1202 
−43.516
−25.127
−25.484 
18.22 
N


ATOM
1212
CA
HIS
1202 
−42.117
−24.766 
−25.55
19.44
C


ATOM
1213
CB
HIS
1202 
−41.352
−25.573
−24.503
20.61
C


ATOM
1214
CG
HIS
1202 
−39.987
−25.039
−24.218
23.13 
C


ATOM
1215
CD2
HIS
1202 
−39.507
−24.329 
−23.17 
22.29
C


ATOM
1216
ND1
HIS
1202 
−38.938 
−25.18
−25.101
25.25
N


ATOM
1217
CE1
HIS
1202
−37.87
−24.579
−24.608
23.7
C


ATOM
1218
NE2
HIS
1202 
−38.189
−24.055
−23.438
24.81
N


ATOM
1219
C
HIS
1202
−41.5
−24.923
−26.946
19.79
C


ATOM
1220
O
HIS
1202 
−41.037
−23.946
−27.514 
19.21 
O


ATOM
1221
N
ARG
1203 
−41.491
−26.145
−27.484
21.16 
N


ATOM
1222
CA
ARG
1203 
−40.951
−26.456
−28.821
20.86 
C


ATOM
1223
CB
ARG
1203 
−41.293 
−25.36
−29.847
22.37 
C


ATOM
1224
CG
ARG
1203 
−42.756
−24.976
−29.983
27.08
C


ATOM
1225
CD
ARG
1203 
−42.888
−23.623
−30.689
30.84
C


ATOM
1226
NE
ARG
1203 
−42.868
−23.673
−32.153
36.66 
N


ATOM
1227
CZ
ARG
1203
−43.94
−23.521
−32.934 
38.15 
C


ATOM
1228
NH1
ARG
1203 
−45.139
−23.308
−32.399
37.56 
N


ATOM
1229
NH2
ARG
1203 
−43.811
−23.569
−34.258 
38.08 
N


ATOM
1230
C
ARG
1203 
−39.442
−26.705 
−28.93
20.03 
C


ATOM
1231
O
ARG
1203 
−38.962
−27.062
−30.001
20.19
O


ATOM
1232
N
ASP
1204
−38.68
−26.498
−27.866 
18.22
N


ATOM
1233
CA
ASP
1204 
−37.242
−26.727
−27.961 
17.39
C


ATOM
1234
CB
ASP
1204 
−36.519
−25.454
−28.397
18.69
C


ATOM
1235
CG
ASP
1204 
−35.059
−25.705
−28.756
20.08
C


ATOM
1236
OD1
ASP
1204 
−34.278
−24.736
−28.736
20.95
O


ATOM
1237
OD2
ASP
1204 
−34.697
−26.864
−29.063 
20.4
O


ATOM
1238
C
ASP
1204 
−36.713
−27.183
−26.617 
16.06
C


ATOM
1239
O
ASP
1204 
−35.627
−26.811
−26.194 
14.59
O


ATOM
1240
N
LEU
1205 
−37.524
−27.984
−25.947 
15.88
N


ATOM
1241
CA
LEU
1205 
−37.178
−28.529
−24.656
15.06
C


ATOM
1242
CB
LEU
1205
−38.41
−29.214
−24.078
15.7
C


ATOM
1243
CG
LEU
1205 
−38.336
−29.828
−22.689
16.1
C


ATOM
1244
CD1
LEU
1205 
−38.054
−28.738 
−21.67
17.91
C


ATOM
1245
CD2
LEU
1205 
−39.655
−30.512
−22.377
18.02
C


ATOM
1246
C
LEU
1205 
−36.067
−29.543 
−24.93
15.1
C


ATOM
1247
O
LEU
1205 
−36.226 
−30.41
−25.777
13.35
O


ATOM
1248
N
ALA
1206 
−34.944
−29.396
−24.234
13.57
N


ATOM
1249
CA
ALA
1206 
−33.775
−30.261
−24.359
12.02
C


ATOM
1250
CB
ALA
1206 
−33.038
−29.999
−25.683
12.69
C


ATOM
1251
C
ALA
1206 
−32.917
−29.824
−23.184
11.59
C


ATOM
1252
O
ALA
1206 
−33.116
−28.719
−22.665
11.21
O


ATOM
1253
N
ALA
1207 
−31.968
−30.648
−22.754
11.55
N


ATOM
1254
CA
ALA
1207 
−31.153 
−30.25
−21.606 
13.24
C


ATOM
1255
CB
ALA
1207 
−30.255
−31.394
−21.164
12.55
C


ATOM
1256
C
ALA
1207 
−30.324
−28.984
−21.838
13.57
C


ATOM
1257
O
ALA
1207 
−29.973 
−28.29
−20.884
12.7
O


ATOM
1258
N
ARG
1208 
−30.008 
−28.66
−23.087 
14.61
N


ATOM
1259
CA
ARG
1208 
−29.226
−27.451
−23.316
15.15
C


ATOM
1260
CB
ARG
1208
−28.74
−27.384
−24.759
15.13
C


ATOM
1261
CG
ARG
1208 
−29.829
−27.618
−25.745
15.45
C


ATOM
1262
CD
ARG
1208 
−29.409 
−27.3
−27.17 
14.22
C


ATOM
1263
NE
ARG
1208 
−30.574
−27.433
−28.039
16.17
N


ATOM
1264
CZ
ARG
1208 
−31.128
−28.598
−28.368
17.5
C


ATOM
1265
NH1
ARG
1208 
−30.616
−29.734
−27.913 
15.22
N


ATOM
1266
NH2
ARG
1208 
−32.211 
−28.63
−29.132
17.23
N


ATOM
1267
C
ARG
1208 
−30.094
−26.238
−23.004 
15.44
C


ATOM
1268
O
ARG
1208
−29.59
−25.126
−22.823
14.4
O


ATOM
1269
N
ASN
1209 
−31.402
−26.452
−22.915
15.58
N


ATOM
1270
CA
ASN
1209 
−32.323
−25.351 
−22.64
15.77
C


ATOM
1271
CB
ASN
1209 
−33.479
−25.394
−23.644
18.91
C


ATOM
1272
CG
ASN
1209
−33.06
−24.919
−25.021 
18.29
C


ATOM
1273
OD1
ASN
1209
−32.54
−23.817
−25.167
22.07
O


ATOM
1274
ND2
ASN
1209 
−33.282
−25.741 
−26.03
20.52
N


ATOM
1275
C
ASN
1209 
−32.869
−25.211
−21.218 
15.85
C


ATOM
1276
O
ASN
1209
−33.85
−24.493
−20.997 
14.98
O


ATOM
1277
N
CYS
1210 
−32.235
−25.897
−20.265 
14.98
N


ATOM
1278
CA
CYS
1210 
−32.605
−25.834
−18.848
13.93
C


ATOM
1279
CB
CYS
1210 
−32.902 
−27.23
−18.301 
14.01
C


ATOM
1280
SG
CYS
1210 
−34.181
−28.128
−19.141
18.21
S


ATOM
1281
C
CYS
1210 
−31.381
−25.299
−18.117
13.47
C


ATOM
1282
O
CYS
1210 
−30.281
−25.796
−18.337
14.75
O


ATOM
1283
N
MET
1211 
−31.542
−24.306
−17.251
11.84
N


ATOM
1284
CA
MET
1211 
−30.389
−23.777
−16.526
12.37
C


ATOM
1285
CB
MET
1211 
−30.373 
−22.25
−16.618
12.33
C


ATOM
1286
CG
MET
1211 
−30.417
−21.723 
−18.04
15.48
C


ATOM
1287
SD
MET
1211 
−28.921
−22.155
−18.986 
16.79
S


ATOM
1288
CE
MET
1211 
−29.629 
−22.57
−20.593 
17.49
C


ATOM
1289
C
MET
1211 
−30.355
−24.221
−15.051
13.11
C


ATOM
1290
O
MET
1211 
−31.405
−24.444
−14.433 
12.82
O


ATOM
1291
N
LEU
1212 
−29.138
−24.339
−14.515
14.5
N


ATOM
1292
CA
LEU
1212 
−28.858
−24.757
−13.126 
18.15
C


ATOM
1293
CB
LEU
1212 
−27.783
−25.854
−13.117
18.33 
C


ATOM
1294
CG
LEU
1212 
−28.063
−27.342
−12.907 
23.14
C


ATOM
1295
CD1
LEU
1212 
−26.759
−28.114
−12.725 
22.22
C


ATOM
1296
CD2
LEU
1212 
−28.895
−27.512
−11.67
22.5
C


ATOM
1297
C
LEU
1212 
−28.318
−23.607
−12.264 
18.5
C


ATOM
1298
O
LEU
1212 
−27.306
−23.003
−12.624
17.66 
O


ATOM
1299
N
ASP
1213 
−28.945 
−23.3 
−11.131
19.27
N


ATOM
1300
CA
ASP
1213 
−28.396
−22.225
−10.308
21.32
C


ATOM
1301
CB
ASP
1213 
−29.477
−21.318
−9.693
21.56
C


ATOM
1302
CG
ASP
1213 
−30.303
−22.006
−8.609
23.87
C


ATOM
1303
OD1
ASP
1213 
−29.909
−23.083
−8.098
22.69
O


ATOM
1304
OD2
ASP
1213 
−31.359
−21.435 
−8.26
23.31
O


ATOM
1305
C
ASP
1213 
−27.537
−22.792
−9.199
22.81
C


ATOM
1306
O
ASP
1213 
−27.369
−24.013
−9.088
21.8
O


ATOM
1307
N
GLU
1214 
−27.015
−21.875
−8.387
23.36
N


ATOM
1308
CA
GLU
1214
−26.15
−22.172
−7.263
25.25
C


ATOM
1309
CB
GLU
1214 
−25.713
−20.823
−6.591
27.38
C


ATOM
1310
CG
GLU
1214 
−26.765
−19.881
−5.826
31.52 
C


ATOM
1311
CD
GLU
1214 
−27.635
−18.892
−6.678
36.11
C


ATOM
1312
OE1
GLU
1214 
−28.537 
−19.36
−7.408
37.3
O


ATOM
1313
OE2
GLU
1214 
−27.447
−17.642
−6.592
38.7
O


ATOM
1314
C
GLU
1214 
−26.736
−23.199 
−6.26
25.42 
C


ATOM
1315
O
GLU
1214 
−25.992
−23.936
−5.608
25.26
O


ATOM
1316
N
LYS
1215 
−28.062
−23.282
−6.172
25.13 
N


ATOM
1317
CA
LYS
1215 
−28.709
−24.231
−5.258
25.77
C


ATOM
1318
CB
LYS
1215 
−29.843
−23.524
−4.475
28.21
C


ATOM
1319
CG
LYS
1215 
−29.356
−22.414 
−3.48
33.22
C


ATOM
1320
CD
LYS
1215 
−30.496
−21.715
−2.665
36.61
C


ATOM
1321
CE
LYS
1215 
−29.956
−20.614
−1.691
39.24
C


ATOM
1322
NZ
LYS
1215 
−30.983
−19.842
−0.882
40.6
N


ATOM
1323
C
LYS
1215
−29.23
−25.491
−5.998
25.36
C


ATOM
1324
O
LYS
1215 
−30.031
−26.261
−5.464
24.65 
O


ATOM
1325
N
PHE
1216 
−28.739
−25.682
−7.225
23.22 
N


ATOM
1326
CA
PHE
1216 
−29.075
−26.811
−8.091
21.85 
C


ATOM
1327
CB
PHE
1216 
−28.465
−28.108
−7.517
23.16 
C


ATOM
1328
CG
PHE
1216 
−26.958
−28.012
−7.263
24.21 
C


ATOM
1329
CD1
PHE
1216 
−26.463 
−27.77
−5.975
26.27 
C


ATOM
1330
CD2
PHE
1216 
−26.043
−28.113
−8.314
23.83 
C


ATOM
1331
CE1
PHE
1216 
−25.081
−27.629
−5.741
24.88 
C


ATOM
1332
CE2
PHE
1216 
−24.659
−27.972
−8.088
25.08
C


ATOM
1333
CZ
PHE
1216 
−24.183 
−27.73
−6.803
25.51
C


ATOM
1334
C
PHE
1216 
−30.569 
−26.93
−8.396
20.58
C


ATOM
1335
O
PHE
1216 
−31.144
−28.015 
−8.54
17.6
O


ATOM
1336
N
THR
1217 
−31.179
−25.759
−8.521
19.63
N


ATOM
1337
CA
THR
1217 
−32.576
−25.635
−8.871
17.9
C


ATOM
1338
CB
THR
1217 
−33.199 
−24.4 
−8.134
18.25 
C


ATOM
1339
OG1
THR
1217 
−33.309
−24.708
−6.736
22.27
O


ATOM
1340
CG2
THR
1217 
−34.587
−24.057 
−8.663 
18.17
C


ATOM
1341
C
THR
1217 
−32.473 
−25.47
−10.396 
16.93
C


ATOM
1342
O
THR
1217 
−31.649
−24.686
−10.886
16.95
O


ATOM
1343
N
VAL
1218 
−33.243
−26.282
−11.127
14.5
N


ATOM
1344
CA
VAL
1218 
−33.271 
−26.27
−12.593
12.8
C


ATOM
1345
CB
VAL
1218 
−33.428 
−27.71
−13.207
13.21
C


ATOM
1346
CG1
VAL
1218 
−33.421
−27.636
−14.734
9.72
C


ATOM
1347
CG2
VAL
1218 
−32.297
−28.638 
−12.73
11.3
C


ATOM
1348
C
VAL
1218 
−34.455
−25.437
−13.066
12.06
C


ATOM
1349
O
VAL
1218 
−35.546
−25.515
−12.503 
10.84
O


ATOM
1350
N
LYS
1219 
−34.229
−24.646
−14.107 
12.68
N


ATOM
1351
CA
LYS
1219 
−35.268 
−23.8 
−14.659
13.73
C


ATOM
1352
CB
LYS
1219 
−35.033
−22.337
−14.228 
13.19
C


ATOM
1353
CG
LYS
1219 
−34.861
−22.121
−12.692
17.83
C


ATOM
1354
CD
LYS
1219 
−35.229
−20.688
−12.283
21.91
C


ATOM
1355
CE
LYS
1219 
−35.232
−20.482
−10.768 
22.55
C


ATOM
1356
NZ
LYS
1219 
−33.871
−20.066
−10.367
26.09
N


ATOM
1357
C
LYS
1219 
−35.258 
−23.95
−16.187
13.7
C


ATOM
1358
O
LYS
1219 
−34.202
−23.854 
−16.83
14.06
O


ATOM
1359
N
VAL
1220 
−36.437
−24.224
−16.746
12.71
N


ATOM
1360
CA
VAL
1220 
−36.641
−24.392
−18.188
13.54
C


ATOM
1361
CB
VAL
1220 
−38.027
−25.056
−18.466
10.73
C


ATOM
1362
CG1
VAL
1220 
−38.189
−25.371
−19.946
12.56
C


ATOM
1363
CG2
VAL
1220 
−38.177
−26.319
−17.619
13.35
C


ATOM
1364
C
VAL
1220 
−36.617
−22.987
−18.794
13.96
C


ATOM
1365
O
VAL
1220 
−37.273
−22.079 
−18.28
13.77
O


ATOM
1366
N
ALA
1221 
−35.866
−22.814
−19.874
15.44
N


ATOM
1367
CA
ALA
1221 
−35.742
−21.521
−20.529 
17.32
C


ATOM
1368
CB
ALA
1221 
−34.291
−21.059
−20.472 
19.47
C


ATOM
1369
C
ALA
1221 
−36.193
−21.558
−21.967 
18.52
C


ATOM
1370
O
ALA
1221 
−36.144
−22.607
−22.622
17.22
O


ATOM
1371
N
ASP
1222 
−36.655
−20.409 
−22.44
19.34
N


ATOM
1372
CA
ASP
1222
−37.05
−20.259
−23.823 
20.45
C


ATOM
1373
C
ASP
1222 
−36.096
−19.138
−24.197
21.22
C


ATOM
1374
O
ASP
1222 
−36.346
−17.986
−23.881
20.31
O


ATOM
1375
CB
ASP
1222 
−38.513 
−19.79
−23.946
0
C


ATOM
1376
CG
ASP
1222 
−38.938 
−19.5 
−25.394
0
C


ATOM
1377
OD1
ASP
1222 
−38.028 
−19.47
−26.254
0
O


ATOM
1378
OD2
ASP
1222 
−40.162
−19.394
−25.634
0
O1−


ATOM
1379
N
PHE
1223 
−34.946
−19.467
−24.764
22.78
N


ATOM
1380
CA
PHE
1223 
−34.068
−18.376
−25.174
24.51
C


ATOM
1381
CB
PHE
1223 
−32.649 
−18.78
−25.064
23.52
C


ATOM
1382
CG
PHE
1223 
−32.181
−18.589 
−23.73
22.43
C


ATOM
1383
CD1
PHE
1223 
−32.106
−17.305
−23.205
22.25
C


ATOM
1384
CD2
PHE
1223 
−31.915
−19.675
−22.943
22.04
C


ATOM
1385
CE1
PHE
1223 
−31.767
−17.121
−21.898
23.44
C


ATOM
1386
CE2
PHE
1223 
−31.579
−19.511
−21.655
23.35
C


ATOM
1387
CZ
PHE
1223 
−31.497 
−18.23
−21.115 
21.72
C


ATOM
1388
C
PHE
1223 
−34.508
−18.133
−26.543
26.06
C


ATOM
1389
O
PHE
1223 
−35.441
−17.365
−26.738
27.77
O


ATOM
1390
N
GLY
1224 
−33.816
−18.621
−27.533
25.8
N


ATOM
1391
CA
GLY
1224 
−34.608
−18.551
−28.715 
26.02
C


ATOM
1392
C
GLY
1224 
−34.467
−17.321 
−29.46
24.52
C


ATOM
1393
O
GLY
1224 
−33.784
−17.447 
−30.43
26.4
O


ATOM
1394
N
LEU
1225 
−35.099
−16.199
−29.133 
23.41
N


ATOM
1395
CA
LEU
1225 
−34.742
−15.069
−29.965
22.22
C


ATOM
1396
CB
LEU
1225 
−35.724
−13.898
−29.921
24.33
C


ATOM
1397
CG
LEU
1225 
−35.597
−13.386
−31.376
24.95
C


ATOM
1398
CD1
LEU
1225
−36.22
−14.383
−32.359
27.59
C


ATOM
1399
CD2
LEU
1225 
−36.271
−12.083
−31.549
27.1
C


ATOM
1400
C
LEU
1225 
−33.399
−14.576
−29.482
21.21
C


ATOM
1401 
O
LEU
1225 
−32.701
−13.862
−30.192
23.15
O


ATOM
1402
N
ALA
1226 
−33.014
−14.967
−28.279
18.87
N


ATOM
1403 
CA
ALA
1226 
−31.743 
−14.53
−27.759
18.09
C


ATOM
1404
CB
ALA
1226 
−31.729
−14.712
−26.281
17.96
C


ATOM
1405
C
ALA
1226 
−30.563
−15.254
−28.404 
19.16
C


ATOM
1406
O
ALA
1226 
−29.424
−14.798
−28.296
19.43
O


ATOM
1407
N
ARG
1227 
−30.825
−16.383
−29.063
19.46
N


ATOM
1408
CA
ARG
1227 
−29.762
−17.127
−29.734
19.73
C


ATOM
1409
CB
ARG
1227 
−30.173
−18.589
−29.955
21.4
C


ATOM
1410 
CG
ARG
1227 
−29.913
−19.468
−28.749
21.1
C


ATOM
1411
CD
ARG
1227 
−30.775
−20.709
−28.773
24.1
C


ATOM
1412
NE
ARG
1227 
−30.764
−21.366
−27.479
24.33
N


ATOM
1413
CZ
ARG
1227 
−29.659
−21.795
−26.901
25.32
C


ATOM
1414
NH1
ARG
1227 
−28.485
−21.653
−27.513
23.64
N


ATOM
1415
NH2
ARG
1227 
−29.722
−22.259
−25.669
22.87
N


ATOM
1416
C
ARG
1227 
−29.502
−16.471
−31.081
19.24
C


ATOM
1417
O
ARG
1227 
−30.343
−16.548
−31.967 
19.55
O


ATOM
1418
N
ASP
1228 
−28.353
−15.814
−31.225
18.7
N


ATOM
1419
CA
ASP
1228 
−27.993
−15.164
−32.476
20.06
C


ATOM
1420
CB
ASP
1228 
−26.596
−14.543
−32.363 
22.84
C


ATOM
1421
CG
ASP
1228 
−26.564
−13.326 
−31.44
25.1
C


ATOM
1422
OD1
ASP
1228 
−27.649
−12.775
−31.148
28.18
O


ATOM
1423
OD2
ASP
1228 
−25.463
−12.912
−31.015
24.23
O


ATOM
1424 
C
ASP
1228 
−28.032
−16.191
−33.614
21.09
C


ATOM
1425
O
ASP
1228
−28.69
−15.971
−34.635
20.36
O


ATOM
1426
N
MET
1229 
−27.319
−17.303
−33.401
22.55
N


ATOM
1427
CA
MET
1229 
−27.226
−18.451
−34.317
25.14
C


ATOM
1428
CB
MET
1229 
−25.849 
−18.58
−34.936
26.88
C


ATOM
1429
CG
MET
1229 
−25.515 
−17.46
−35.798
31.32
C


ATOM
1430
SD
MET
1229 
−24.024 
−17.65
−36.705
35.03
S


ATOM
1431
CE
MET
1229 
−23.377
−16.183
−36.259
34.46
C


ATOM
1432
C
MET
1229 
−27.431
−19.769
−33.598
26.07
C


ATOM
1433
O
MET
1229 
−27.166
−19.877
−32.409
24.93
O


ATOM
1434
N
TYR
1230 
−27.867
−20.747
−34.392 
28.36
N


ATOM
1435
CA
TYR
1230 
−28.082
−22.125
−33.992
31.64
C


ATOM
1436
CB
TYR
1230 
−29.453
−22.541
−34.464
32.55
C


ATOM
1437 
CG
TYR
1230 
−30.516
−21.962
−33.652 
35.13
C


ATOM
1438 
CD1
TYR
1230 
−30.798
−20.603
−33.714
36.14
C


ATOM
1439 
CE1
TYR
1230 
−31.725
−20.077
−32.932
36.69
C


ATOM
1440
CD2
TYR
1230 
−31.171
−22.761
−32.768 
36.34
C


ATOM
1441
CE2
TYR
1230 
−32.087
−22.251
−31.994
37.04
C


ATOM
1442
CZ
TYR
1230 
−32.365
−20.915
−32.096
38.54
C


ATOM
1443
OH
TYR
1230 
−33.288
−20.428
−31.255
40.67
O


ATOM
1444
C
TYR
1230 
−27.115 
−23.13
−34.593 
33.96
C


ATOM
1445
O
TYR
1230 
−26.726
−22.999
−35.739 
31.96
O


ATOM
1446
N
ASP
1231 
−26.708
−24.121
−33.842 
37.48 
N


ATOM
1447
CA
ASP
1231 
−25.919
−25.139
−34.375
40.93
C


ATOM
1448
CB
ASP
1231
−24.61
−25.288
−33.497
44.37
C


ATOM
1449
CG
ASP
1231 
−23.925
−24.048
−33.276
48.97
C


ATOM
1450
OD1
ASP
1231 
−24.038
−23.129
−34.127 
52.21
O


ATOM
1451
OD2
ASP
1231 
−23.288
−23.979
−32.223
52.03
O


ATOM
1452
C
ASP
1231 
−26.456
−26.616
−34.314 
40.83
C


ATOM
1453
O
ASP
1231 
−27.297
−26.882
−33.463
42.4
O


ATOM
1454
N
LYS
1232 
−26.267
−27.085
−35.575
42.17
N


ATOM
1455
CA
LYS
1232 
−25.533
−28.505
−35.598
41.36
C


ATOM
1456
CB
LYS
1232 
−24.062
−27.847
−35.332 
43.03
C


ATOM
1457
CG
LYS
1232 
−23.742
−27.489
−33.868
42.47
C


ATOM
1458
CD
LYS
1232 
−22.298
−27.062
−33.676
44.85
C


ATOM
1459
CE
LYS
1232 
−22.066 
−26.5 
−32.281
45.67
C


ATOM
1460
NZ
LYS
1232
−22.63
−27.363
−31.219
45.92
N


ATOM
1461
C
LYS
1232 
−25.864
−29.353
−34.331
42.16
C


ATOM
1462
O
LYS
1232
−24.92
−29.911
−33.817 
42.14
O


ATOM
1463
N
GLU
1233
−27.06
−29.753
−34.739 
41.02
N


ATOM
1464
CA
GLU
1233 
−28.195
−29.943
−33.706 
38.27
C


ATOM
1465
CB
GLU
1233
−27.97
−29.831
−32.326
38.85
C


ATOM
1466
CG
GLU
1233 
−28.074
−28.876 
−31.65
39.43
C


ATOM
1467
CD
GLU
1233 
−27.167
−29.213
−30.633
40.62
C


ATOM
1468
OE1
GLU
1233 
−27.027
−30.394
−30.339
41.43
O


ATOM
1469
OE2
GLU
1233 
−26.558
−28.342
−30.077
40.48 
O


ATOM
1470
C
GLU
1233 
−29.459
−29.134
−34.191
36.4
C


ATOM
1471
O
GLU
1233 
−30.524
−29.669
−33.898
34.53 
O


ATOM
1472
N
TYR
1234 
−29.475
−28.188
−35.121
36.25
N


ATOM
1473
CA
TYR
1234 
−30.734
−27.685
−35.527
36.56
C


ATOM
1474
CB
TYR
1234 
−30.911
−26.216
−35.002 
33.99 
C


ATOM
1475
CG
TYR
1234 
−31.224
−25.972
−33.511
31.79
C


ATOM
1476
CD1
TYR
1234 
−30.212 
−25.93
−32.539
31.24
C


ATOM
1477
CE1
TYR
1234 
−30.517
−25.712
−31.174 
30.51
C


ATOM
1478
CD2
TYR
1234 
−32.541
−25.784
−33.081
30.83
C


ATOM
1479
CE2
TYR
1234
−32.85
−25.571 
−31.73 
31.34
C


ATOM
1480
CZ
TYR
1234
−31.84
−25.539
−30.786 
30.26
C


ATOM
1481
OH
TYR
1234 
−32.168
−25.366
−29.461
30.54
O


ATOM
1482
C
TYR
1234 
−30.732
−27.612
−37.001
38.61 
C


ATOM
1483
O
TYR
1234 
−29.768
−27.222
−37.647
38.99
O


ATOM
1484
N
TYR
1235 
−31.838 
−28.06
−37.605
40.77
N


ATOM
1485
CA
TYR
1235 
−31.738
−27.772
−38.957
42.64
C


ATOM
1486
CB
TYR
1235 
−31.678
−29.069
−39.669
46.84 
C


ATOM
1487
CG
TYR
1235 
−32.849
−29.778
−39.865
50.38
C


ATOM
1488
CD1
TYR
1235 
−34.004
−29.171
−39.769
53.12
C


ATOM
1489
CE1
TYR
1235 
−35.198
−29.749
−40.213
55.79 
C


ATOM
1490
CD2
TYR
1235 
−32.817
−31.021
−40.357
53.24 
C


ATOM
1491
CE2
TYR
1235
−34.04
−31.664
−40.801
55.03 
C


ATOM
1492
CZ
TYR
1235 
−35.279
−30.998
−40.743
55.74 
C


ATOM
1493
OH
TYR
1235 
−36.599
−31.478
−41.034
56.64 
O


ATOM
1494
C
TYR
1235 
−32.684
−26.594
−39.33
42.38
C


ATOM
1495
O
TYR
1235 
−33.349
−26.096
−38.446 
40.51
O


ATOM
1496
N
SER
1236 
−32.562
−26.056
−40.555
43.09
N


ATOM
1497
CA
SER
1236 
−33.212
−24.801
−41.007
45.87 
C


ATOM
1498
CB
SER
1236 
−32.195
−23.721
−41.381
45.81
C


ATOM
1499
OG
SER
1236 
−32.456
−22.403
−40.912 
46.19
O


ATOM
1500
C
SER
1236 
−33.855
−25.128
−42.242
46.98
C


ATOM
1501
O
SER
1236
−33.2 
−25.525
−43.229
46.05
O


ATOM
1502
N
VAL
1237 
−35.127 
−24.83
−42.112 
49.49
N


ATOM
1503
CA
VAL
1237 
−36.152
−25.135
−42.976
53.03
C


ATOM
1504
CB
VAL
1237 
−36.004
−26.282
−43.795
54.51
C


ATOM
1505
CG1
VAL
1237 
−37.535
−26.564
−44.634
55.14 
C


ATOM
1506
CG2
VAL
1237 
−34.579
−26.099
−44.653
55.8
C


ATOM
1507
C
VAL
1237 
−37.635
−25.216
−42.705 
53.76 
C


ATOM
1508
O
VAL
1237 
−38.019
−25.752
−41.647
56
O


ATOM
1509
N
HIS
1238 
−37.758
−23.997
−43.136
52.4
N


ATOM
1510
CA
HIS
1238 
−37.717
−23.906
−44.535 
51.91
C


ATOM
1511
CB
HIS
1238 
−38.465
−22.886
−45.254
54.35 
C


ATOM
1512
CG
HIS
1238 
−39.616
−23.437
−45.974
57.6
C


ATOM
1513
CD2
HIS
1238 
−40.346
−22.958
−47.004
58.86
C


ATOM
1514
ND1
HIS
1238 
−40.192
−24.626
−45.598
58.65
N


ATOM
1515
CE1
HIS
1238 
−41.237
−24.859
−46.368
60.01
C


ATOM
1516
NE2
HIS
1238 
−41.353
−23.862
−47.23
59.82 
N


ATOM
1517
C
HIS
1238 
−36.249
−23.225
−44.582
48.89 
C


ATOM
1518
O
HIS
1238 
−35.761
−22.506
−43.669
48.04
O


ATOM
1519
N
ASN
1239 
−35.594
−23.733
−45.588
45.16 
N


ATOM
1520
CA
ASN
1239 
−34.522
−23.154
−46.263
42.36 
C


ATOM
1521
CB
ASN
1239 
−34.461
−23.909
−47.567
39.19 
C


ATOM
1522
CG
ASN
1239 
−33.336
−24.794
−47.582 
36.67 
C


ATOM
1523
OD1
ASN
1239 
−32.361
−24.421
−47.049
32.64
O


ATOM
1524
ND2
ASN
1239 
−33.421
−25.953
−48.131
35.18 
N


ATOM
1525
C
ASN
1239 
−35.228
−21.819
−46.602
41.96
C


ATOM
1526
O
ASN
1239 
−34.606
−20.882
−47.041
40.93
O


ATOM
1527
N
LYS
1240 
−36.529
−21.728
−46.411
42.34 
N


ATOM
1528
CA
LYS
1240 
−37.182
−20.524
−46.813
43.5
C


ATOM
1529
CB
LYS
1240 
−38.236
−20.938
−47.786
45.68 
C


ATOM
1530
CG
LYS
1240 
−38.978
−19.876
−48.424
49.63
C


ATOM
1531
CD
LYS
1240 
−39.862
−20.598
−49.314
52.15
C


ATOM
1532
CE
LYS
1240 
−40.698 
−19.81
−50.23
53.54
C


ATOM
1533
NZ
LYS
1240 
−41.324
−20.804
−51.138
53.01 
N


ATOM
1534
C
LYS
1240
−37.69 
−19.72
−45.646
42.44 
C


ATOM
1535
O
LYS
1240 
−37.456
−18.534
−45.622
43.49
O


ATOM
1536
N
THR
1241 
−38.354
−20.336
−44.673
40.41
N


ATOM
1537
CA
THR
1241 
−38.785 
−19.59
−43.49
38.28
C


ATOM
1538
CB
THR
1241 
−39.811
−20.311
−42.655 
37.86 
C


ATOM
1539
OG1
THR
1241 
−39.215
−21.421
−41.969
35.48
O


ATOM
1540
CG2
THR
1241 
−40.791
−20.851
−43.504
37.56
C


ATOM
1541
C
THR
1241 
−37.666
−19.407
−42.501
37.63
C


ATOM
1542
O
THR
1241 
−37.766
−18.558 
−41.64
38.27
O


ATOM
1543
N
GLY
1242 
−36.621 
−20.22
−42.576
36.14
N


ATOM
1544
CA
GLY
1242 
−35.569
−20.096
−41.584
33.51
C


ATOM
1545
C
GLY
1242 
−35.945
−20.657
−40.222 
32.78
C


ATOM
1546
O
GLY
1242 
−35.296
−20.446
−39.216
32.4
O


ATOM
1547
N
ALA
1243 
−36.965
−21.453
−40.154
30.86
N


ATOM
1548
CA
ALA
1243 
−37.285
−21.872
−38.837
30.24
C


ATOM
1549
CB
ALA
1243 
−38.591
−22.411
−38.953
31.17
C


ATOM
1550
C
ALA
1243 
−36.196
−22.869 
−38.28
29.29
C


ATOM
1551
O
ALA
1243 
−35.507
−23.504
−39.074
28.68
O


ATOM
1552
N
LYS
1244 
−35.951
−22.972
−36.968
27.71
N


ATOM
1553
CA
LYS
1244 
−34.908
−23.918 
−36.53
27.48
C


ATOM
1554
CB
LYS
1244 
−33.923 
−23.33
−35.522
28.19
C


ATOM
1555
CG
LYS
1244 
−33.554
−21.899
−35.836
29.18
C


ATOM
1556
CD
LYS
1244 
−32.685
−21.772
−37.068 
30.21
C


ATOM
1557
CE
LYS
1244 
−32.757
−20.362
−37.658
34.05
C


ATOM
1558
NZ
LYS
1244
−33.43
−19.381
−36.754
35.34
N


ATOM
1559
C
LYS
1244 
−35.595
−25.092
−35.941
27.46
C


ATOM
1560
O
LYS
1244 
−36.579
−24.986
−35.212
27.05
O


ATOM
1561
N
LEU
1245 
−35.016
−26.227
−36.213
26.57
N


ATOM
1562
CA
LEU
1245 
−35.698 
−27.39
−35.828
25.63
C


ATOM
1563
CB
LEU
1245 
−36.319
−27.817
−37.122
26.81
C


ATOM
1564
CG
LEU
1245 
−37.185
−26.893
−37.928
27.54
C


ATOM
1565
CD1
LEU
1245 
−36.824
−27.236
−39.225 
29.71
C


ATOM
1566
CD2
LEU
1245 
−38.559
−27.221 
−37.86 
29.25
C


ATOM
1567
C
LEU
1245 
−34.862
−28.475 
−35.12
23.78
C


ATOM
1568
O
LEU
1245 
−33.954
−29.072
−35.711
24.46
O


ATOM
1569
N
PRO
1246 
−35.134
−28.688
−33.814
21.49
N


ATOM
1570
CD
PRO
1246 
−36.076
−27.899
−32.992
22.41
C


ATOM
1571
CA
PRO
1246
−34.45
−29.686
−32.982
20.52
C


ATOM
1572
CB
PRO
1246 
−34.893
−29.326
−31.563 
20.74
C


ATOM
1573
CG
PRO
1246
−36.27
−28.784
−31.769
22.45
C


ATOM
1574
C
PRO
1246 
−34.929
−31.054
−33.419
18.08
C


ATOM
1575
O
PRO
1246 
−35.579
−31.778
−32.663 
17.77
O


ATOM
1576
N
VAL
1247 
−34.609
−31.386
−34.664
17.04
N


ATOM
1577
CA
VAL
1247 
−35.005 
−32.65
−35.261
16.91
C


ATOM
1578
CB
VAL
1247 
−34.141
−33.039
−36.451
18.82
C


ATOM
1579
CG1
VAL
1247 
−34.435
−32.219
−37.548
17.47
C


ATOM
1580
CG2
VAL
1247 
−32.717
−32.843 
−36.16
22.1
C


ATOM
1581
C
VAL
1247 
−34.917
−33.816
−34.315
16.17
C


ATOM
1582
O
VAL
1247 
−35.866
−34.571
−34.161
15.61
O


ATOM
1583
N
LYS
1248 
−33.768
−33.966
−33.677
15.85
N


ATOM
1584
CA
LYS
1248 
−33.576
−35.092
−32.784 
14.63
C


ATOM
1585
CB
LYS
1248 
−32.092
−35.337
−32.625
17.18
C


ATOM
1586
CG
LYS
1248 
−31.533
−35.883
−33.913
19.71
C


ATOM
1587
CD
LYS
1248 
−30.083
−36.145
−33.764
22.1
C


ATOM
1588
CE
LYS
1248 
−29.479
−36.741
−34.994
23.2
C


ATOM
1589
NZ
LYS
1248 
−28.029
−36.572
−34.748
29.5
N


ATOM
1590
C
LYS
1248 
−34.291
−35.113
−31.44
15.45
C


ATOM
1591
O
LYS
1248 
−34.255
−36.141
−30.745
13.52
O


ATOM
1592
N
TRP
1249 
−34.935
−33.999
−31.079
12.34
N


ATOM
1593
CA
TRP
1249 
−35.734
−33.909
−29.855
12.07
C


ATOM
1594
CB
TRP
1249 
−35.377
−32.678
−29.002
11.94
C


ATOM
1595
CG
TRP
1249 
−34.121
−32.803
−28.185
11.75
C


ATOM
1596
CD2
TRP
1249 
−32.786
−32.749
−28.683
9.74
C


ATOM
1597
CE2
TRP
1249 
−31.921
−32.988
−27.594
11.73
C


ATOM
1598
CE3
TRP
1249 
−32.235
−32.534
−29.955
11.43
C


ATOM
1599
CD1
TRP
1249 
−34.021
−33.056
−26.836
10.88
C


ATOM
1600
NE1
TRP
1249 
−32.699
−33.171
−26.48
10.21
N


ATOM
1601
CZ2
TRP
1249 
−30.528
−33.017
−27.737
12.35
C


ATOM
1602
CZ3
TRP
1249
−30.85
−32.564
−30.102
9.5
C


ATOM
1603
CH2
TRP
1249 
−30.013
−32.804
−28.995
11.36
C


ATOM
1604
C
TRP
1249 
−37.187
−33.763
−30.288
13.69
C


ATOM
1605
O
TRP
1249 
−38.075
−33.743
−29.447
14.98
O


ATOM
1606
N
MET
1250 
−37.435
−33.665
−31.595
13.34
N


ATOM
1607
CA
MET
1250 
−38.799
−33.485
−32.102
13.11
C


ATOM
1608
CB
MET
1250 
−38.806 
−32.79
−33.475
11.56
C


ATOM
1609
CG
MET
1250 
−38.605
−31.283
−33.468
15.9
C


ATOM
1610
SD
MET
1250 
−38.179
−30.668
−35.141
17.57
S


ATOM
1611
CE
MET
1250 
−39.682
−31.196
−36.142
17.78
C


ATOM
1612
C
MET
1250 
−39.579
−34.772
−32.239
12.68
C


ATOM
1613
O
MET
1250 
−39.028
−35.823
−32.568
13.57
O


ATOM
1614
N
ALA
1251 
−40.884 
−34.68
−32.026
12.09
N


ATOM
1615
CA
ALA
1251 
−41.718
−35.859
−32.137
13.59
C


ATOM
1616
CB
ALA
1251 
−42.981
−35.663
−31.356
13.36
C


ATOM
1617
C
ALA
1251 
−42.044
−36.246
−33.58
16.39
C


ATOM
1618
O
ALA
1251 
−42.113
−35.397
−34.48 
14.98
O


ATOM
1619
N
LEU
1252 
−42.254
−37.548
−33.773
17.37
N


ATOM
1620
CA
LEU
1252 
−42.573 
−38.11
−35.074
17.41
C


ATOM
1621
CB
LEU
1252 
−43.224
−39.505
−34.909 
17.7
C


ATOM
1622
CG
LEU
1252 
−43.415
−40.392
−36.149
15.74
C


ATOM
1623
CD1
LEU
1252 
−42.258
−40.179
−37.122
14.12
C


ATOM
1624
CD2
LEU
1252 
−43.491
−41.858
−35.733
16.89
C


ATOM
1625
C
LEU
1252
−43.49 
−37.2 
−35.88
17.33
C


ATOM
1626 
O
LEU
1252 
−43.167 
−36.85
−37.008
16.45
O


ATOM
1627
N
GLU
1253 
−44.609 
−36.78
−35.293
18.42
N


ATOM
1628
CA
GLU
1253 
−45.558
−35.955
−36.034
20.38
C


ATOM
1629
CB
GLU
1253 
−46.936
−35.976
−35.347
22.08
C


ATOM
1630
CG
GLU
1253 
−47.116 
−35.11
−34.102
23.88
C


ATOM
1631
CD
GLU
1253 
−46.628
−35.757
−32.814
27.39
C


ATOM
1632 
OE1
GLU
1253 
−46.309
−36.965
−32.809
28.41
O


ATOM
1633
OE2
GLU
1253 
−46.575
−35.044
−31.791
29.51
O


ATOM
1634
C
GLU
1253 
−45.127
−34.518
−36.358
21.17
C


ATOM
1635
O
GLU
1253 
−45.629 
−33.92
−37.32
20.27
O


ATOM
1636
N
SER
1254 
−44.198
−33.972
−35.574
19.04
N


ATOM
1637 
CA
SER
1254 
−43.695 
−32.62
−35.817
20.94
C


ATOM
1638
CB
SER
1254
−42.98
−32.078
−34.573
17.59
C


ATOM
1639
OG
SER
1254 
−43.826
−32.137
−33.439
17.95
O


ATOM
1640
C
SER
1254 
−42.705 
−32.72
−36.971 
20.79
C


ATOM
1641
O
SER
1254 
−42.545
−31.793
−37.757 
21.89
O


ATOM
1642
N
LEU
1255 
−42.033
−33.858
−37.066
21.85
N


ATOM
1643
CA
LEU
1255 
−41.078
−34.054
−38.149 
23.75
C


ATOM
1644
CB
LEU
1255
−40.31
−35.356
−37.971 
22.37
C


ATOM
1645
CG
LEU
1255 
−39.313
−35.423
−36.82
21.95 
C


ATOM
1646
CD1
LEU
1255 
−38.573
−36.757
−36.904
22.01 
C


ATOM
1647
CD2
LEU
1255 
−38.337
−34.255
−36.903
20.85 
C


ATOM
1648
C
LEU
1255 
−41.833 
−34.1 
−39.466
25.17 
C


ATOM
1649
O
LEU
1255 
−41.315
−33.701
−40.51
25.31
O


ATOM
1650
N
GLN
1256
−43.06
−34.601
−39.397
26.07
N


ATOM
1651
CA
GLN
1256
−43.92
−34.717
−40.555
27.58
C


ATOM
1652
CB
GLN
1256 
−44.909
−35.877
−40.345
27.79
C


ATOM
1653
CG
GLN
1256 
−44.289
−37.284
−40.403
30.43
C


ATOM
1654
CD
GLN
1256 
−45.281
−38.364
−39.99
33.67
C


ATOM
1655
OE1
GLN
1256 
−45.421 
−39.39
−40.654
35.61
O


ATOM
1656
NE2
GLN
1256 
−45.972
−38.132
−38.88
34.01 
N


ATOM
1657
C
GLN
1256 
−44.657
−33.395
−40.834
27.62 
C


ATOM
1658
O
GLN
1256 
−44.562 
−32.87
−41.937
29.77
O


ATOM
1659
N
THR
1257 
−45.358
−32.837
−39.845
27.72
N


ATOM
1660
CA
THR
1257
−46.1 
−31.578
−40.036 
27.3
C


ATOM
1661
CB
THR
1257 
−47.357
−31.499
−39.114
26.41
C


ATOM
1662
OG1
THR
1257 
−46.963
−31.701
−37.75
26.82
O


ATOM
1663
CG2
THR
1257 
−48.414
−32.514
−39.521
25.55
C


ATOM
1664
C
THR
1257 
−45.381
−30.216
−39.847
27.61
C


ATOM
1665
O
THR
1257
−45.77
−29.234
−40.466 
27.07
O


ATOM
1666
N
GLN
1258 
−44.355
−30.167
−39
28.64 
N


ATOM
1667
CA
GLN
1258 
−43.603
−28.941
−38.626
29.71
C


ATOM
1668
CB
GLN
1258 
−43.165
−28.034
−39.826
30.88
C


ATOM
1669
CG
GLN
1258 
−41.693
−27.435
−39.662
34.29
C


ATOM
1670
CD
GLN
1258 
−41.388
−26.084
−40.38
35.42
C


ATOM
1671
OE1
GLN
1258
−41.11 
−25.07
−39.724
37.02
O


ATOM
1672
NE2
GLN
1258 
−41.413
−26.085
−41.712 
35.8
N


ATOM
1673
C
GLN
1258
−44.51
−28.144
−37.677 
28.89 
C


ATOM
1674
O
GLN
1258
−44.27
−26.967
−37.414
29.27
O


ATOM
1675
N
LYS
1259 
−45.553
−28.805
−37.168
28.49
N


ATOM
1676
CA
LYS
1259 
−46.496
−28.196
−36.221
28.29
C


ATOM
1677
CB
LYS
1259 
−47.963 
−28.4 
−36.727
28.96 
C


ATOM
1678
CG
LYS
1259 
−48.203 
−28.05
−38.258
31
C


ATOM
1679
CD
LYS
1259 
−49.257
−26.931
−38.585
32.59
C


ATOM
1680
CE
LYS
1259 
−50.617
−27.453
−39.126
33.31 
C


ATOM
1681
NZ
LYS
1259 
−51.559
−27.921
−38.065
36.13
N


ATOM
1682
C
LYS
1259 
−46.215
−28.858
−34.828 
26.44
C


ATOM
1683
O
LYS
1259
−46.07
−30.079
−34.741
26.47
O


ATOM
1684
N
PHE
1260 
−46.088
−28.045
−33.767
25.21
N


ATOM
1685
CA
PHE
1260 
−45.781
−28.507
−32.388
24.1
C


ATOM
1686
CB
PHE
1260 
−44.607
−27.704
−31.792
23.41
C


ATOM
1687
CG
PHE
1260 
−43.308
−27.831
−32.547
25.91
C


ATOM
1688
CD1
PHE
1260 
−43.116
−27.165
−33.758
27.41 
C


ATOM
1689
CD2
PHE
1260 
−42.265
−28.605
−32.036
27.23
C


ATOM
1690
CE1
PHE
1260 
−41.902
−27.269
−34.449
26.54
C


ATOM
1691
CE2
PHE
1260 
−41.049
−28.714
−32.721 
27.29
C


ATOM
1692
CZ
PHE
1260 
−40.871
−28.045
−33.927
26.57
C


ATOM
1693
C
PHE
1260 
−46.937
−28.426
−31.368 
22.89
C


ATOM
1694
O
PHE
1260 
−47.811
−27.568
−31.478
22.69
O


ATOM
1695
N
THR
1261 
−46.919
−29.294
−30.354
21.28
N


ATOM
1696
CA
THR
1261 
−47.968
−29.297
−29.325
21.08
C


ATOM
1697
CB
THR
1261 
−49.112
−30.269
−29.709
21.01
C


ATOM
1698
OG1
THR
1261
−48.76
−31.601
−29.316
21.47 
O


ATOM
1699
CG2
THR
1261 
−49.338
−30.256
−31.227
21.65 
C


ATOM
1700
C
THR
1261 
−47.389
−29.708
−27.957
20.48
C


ATOM
1701
O
THR
1261 
−46.199
−30.017
−27.857
17.26 
O


ATOM
1702
N
THR
1262 
−48.204
−29.707
−26.902
20.44 
N


ATOM
1703
CA
THR
1262 
−47.678
−30.099
−25.592
19.37
C


ATOM
1704
CB
THR
1262 
−48.688
−29.783
−24.445 
18.52 
C


ATOM
1705
OG1
THR
1262 
−48.865
−28.364
−24.364 
22.58 
O


ATOM
1706
CG2
THR
1262 
−48.153 
−30.24
−23.091
17.69 
C


ATOM
1707
C
THR
1262
−47.24
−31.571
−25.597
17.47
C


ATOM
1708
O
THR
1262 
−46.342
−31.946
−24.851
18.79
O


ATOM
1709
N
LYS
1263 
−47.834
−32.392 
−26.47 
19.24 
N


ATOM
1710
CA
LYS
1263 
−47.446
−33.809
−26.592
18.23
C


ATOM
1711
CB
LYS
1263 
−48.518
−34.637
−27.304
16.94
C


ATOM
1712
CG
LYS
1263 
−49.874
−34.561
−26.667
19.51 
C


ATOM
1713
CD
LYS
1263 
−49.769
−34.879
−25.188
23.06
C


ATOM
1714
CE
LYS
1263 
−51.108
−35.281
−24.587 
22.44
C


ATOM
1715
NZ
LYS
1263 
−50.893
−35.855
−23.223
24.48
N


ATOM
1716
C
LYS
1263
−46.14 
−33.96
−27.367
17.16
C


ATOM
1717
O
LYS
1263 
−45.417
−34.929 
−27.17
18.48
O


ATOM
1718
N
SER
1264 
−45.838
−33.039
−28.271
16.85
N


ATOM
1719
CA
SER
1264 
−44.569
−33.169
−28.971
17.48
C


ATOM
1720
CB
SER
1264 
−44.558
−32.344
−30.259
17.7
C


ATOM
1721
OG
SER
1264 
−44.882
−30.994
−30.001
18.83
O


ATOM
1722
C
SER
1264 
−43.496
−32.696
−27.968 
17.45
C


ATOM
1723
O
SER
1264 
−42.329
−33.071
−28.077
17.64 
O


ATOM
1724
N
ASP
1265 
−43.928
−31.889
−26.988
14.49
N


ATOM
1725
CA
ASP
1265 
−43.089
−31.368
−25.888 
14.77
C


ATOM
1726
CB
ASP
1265 
−43.831
−30.278
−25.093
16.44
C


ATOM
1727
CG
ASP
1265 
−43.451 
−28.85
−25.492
17.46
C


ATOM
1728
OD1
ASP
1265 
−42.537
−28.634
−26.318 
17.88
O


ATOM
1729
OD2
ASP
1265 
−44.092
−27.925
−24.949
18.78
O


ATOM
1730
C
ASP
1265 
−42.801
−32.522
−24.911
12.9 
C


ATOM
1731
O
ASP
1265 
−41.713
−32.626
−24.349 
13.55
O


ATOM
1732
N
VAL
1266 
−43.818 
−33.35
−24.681 
11.93
N


ATOM
1733
CA
VAL
1266 
−43.692
−34.515
−23.816
13.82
C


ATOM
1734
CB
VAL
1266 
−45.068
−35.254
−23.686
14.9
C


ATOM
1735
CG1
VAL
1266 
−44.876 
−36.7 
−23.246
10.56
C


ATOM
1736
CG2
VAL
1266 
−45.966
−34.507
−22.686
12.47
C


ATOM
1737
C
VAL
1266
−42.65
−35.397 
−24.52
14.39
C


ATOM
1738
O
VAL
1266 
−41.717
−35.906
−23.892
14.25 
O


ATOM
1739
N
TRP
1267 
−42.788 
−35.55
−25.835
14.88 
N


ATOM
1740
CA
TRP
1267 
−41.816
−36.352
−26.578
15.69
C


ATOM
1741
CB
TRP
1267 
−42.062
−36.328
−28.087
16.09
C


ATOM
1742
CG
TRP
1267 
−41.057
−37.186
−28.883
17.05
C


ATOM
1743
CD2
TRP
1267 
−41.368
−38.331
−29.682
17.26
C


ATOM
1744
CE2
TRP
1267 
−40.157
−38.801
−30.243
17.57
C


ATOM
1745
CE3
TRP
1267 
−42.556
−39.004
−29.981
17.76
C


ATOM
1746
CD1
TRP
1267 
−39.694 
−37.01
−28.986
17.69
C


ATOM
1747
NE1
TRP
1267 
−39.151 
−37.98
−29.804
18.08
N


ATOM
1748
CZ2
TRP
1267 
−40.107
−39.916
−31.087 
19.89
C


ATOM
1749
CZ3
TRP
1267 
−42.505
−40.112
−30.822
18.54
C


ATOM
1750
CH2
TRP
1267 
−41.289
−40.556
−31.362 
19.43
C


ATOM
1751
C
TRP
1267 
−40.411
−35.813
−26.332
16.62
C


ATOM
1752
O
TRP
1267 
−39.511
−36.586
−26.023
17.18
O


ATOM
1753
N
SER
1268 
−40.217
−34.501
−26.488
14.99
N


ATOM
1754
CA
SER
1268 
−38.891 
−33.91
−26.286
14.28
C


ATOM
1755
CB
SER
1268 
−38.876
−32.398
−26.566 
14.67
C


ATOM
1756
OG
SER
1268 
−39.424
−32.051
−27.825
19.01
O


ATOM
1757
C
SER
1268 
−38.408
−34.098
−24.858
12.79
C


ATOM
1758
O
SER
1268 
−37.216
−34.252 
−24.62 
12.21
O


ATOM
1759
N
PHE
1269 
−39.327
−34.039 
−23.9
10.34
N


ATOM
1760
CA
PHE
1269 
−38.932
−34.194
−22.512 
12.36
C


ATOM
1761
CB
PHE
1269
−40.12
−33.897 
−21.59
12.12
C


ATOM
1762
CG
PHE
1269
−39.85 
−34.2 
−20.149 
15.09
C


ATOM
1763
CD1
PHE
1269 
−39.046
−33.365
−19.372
14.94
C


ATOM
1764
CD2
PHE
1269 
−40.355
−35.363
−19.582
14.21
C


ATOM
1765
CE1
PHE
1269 
−38.751
−33.695
−18.053 
15.06
C


ATOM
1766
CE2
PHE
1269 
−40.063
−35.699
−18.267 
15.58
C


ATOM
1767
CZ
PHE
1269
−39.26
−34.863
−17.503
14.09
C


ATOM
1768
C
PHE
1269 
−38.371
−35.603
−22.286
11.45
C


ATOM
1769
O
PHE
1269 
−37.429
−35.791
−21.522 
14.03
O


ATOM
1770
N
GLY
1270 
−38.945
−36.591
−22.965
12.93
N


ATOM
1771
CA
GLY
1270 
−38.442
−37.947
−22.849 
13.38
C


ATOM
1772
C
GLY
1270 
−37.016
−38.029
−23.388 
12.82
C


ATOM
1773
O
GLY
1270 
−36.209
−38.804
−22.873
13.02
O


ATOM
1774
N
VAL
1271 
−36.702
−37.248
−24.428 
12.51
N


ATOM
1775
CA
VAL
1271
−35.34 
−37.23
−24.987
12.39
C


ATOM
1776
CB
VAL
1271 
−35.256
−36.469
−26.371
12.83
C


ATOM
1777
CG1
VAL
1271 
−33.818 
−36.39
−26.846 
14.09
C


ATOM
1778
CG2
VAL
1271 
−36.044
−37.203
−27.429
12.97
C


ATOM
1779
C
VAL
1271 
−34.414
−36.555 
−23.96
11.86
C


ATOM
1780
O
VAL
1271 
−33.262
−36.961 
−23.81 
13.66
O


ATOM
1781
N
LEU
1272 
−34.927
−35.537
−23.254
12.4
N


ATOM
1782
CA
LEU
1272 
−34.163
−34.832 
−22.21
11.28
C


ATOM
1783
CB
LEU
1272 
−34.961
−33.628
−21.648
12.83
C


ATOM
1784
CG
LEU
1272 
−34.465
−32.674
−20.527
12.7
C


ATOM
1785
CD1
LEU
1272 
−35.271
−31.379
−20.589
11.58
C


ATOM
1786
CD2
LEU
1272 
−34.622
−33.302
−19.134
16.29
C


ATOM
1787
C
LEU
1272 
−33.857
−35.824
−21.083
10.67
C


ATOM
1788
O
LEU
1272
−32.73
−35.884 
−20.59
9.63
O


ATOM
1789
N
LEU
1273 
−34.853
−36.612
−20.682
10.3
N


ATOM
1790
CA
LEU
1273 
−34.622 
−37.59 
−19.62
12.31
C


ATOM
1791 
CB
LEU
1273 
−35.879
−38.415
−19.343
13.07
C


ATOM
1792
CG
LEU
1273 
−37.038
−37.707
−18.634 
15.53
C


ATOM
1793
CD1
LEU
1273 
−38.259
−38.639
−18.597 
13.92
C


ATOM
1794
CD2
LEU
1273 
−36.605
−37.302
−17.236 
12.41
C


ATOM
1795 
C
LEU
1273 
−33.494
−38.518
−20.061
11.72
C


ATOM
1796 
O
LEU
1273 
−32.638
−38.887
−19.265
10.87
O


ATOM
1797
N
TRP
1274 
−33.508
−38.888 
−21.34
10.2
N


ATOM
1798
CA
TRP
1274 
−32.487
−39.765
−21.891
11.44
C


ATOM
1799
CB
TRP
1274 
−32.866 
−40.2 
−23.321
10.95
C


ATOM
1800
CG
TRP
1274 
−31.903 
−41.19 
−23.98 
10.98
C


ATOM
1801
CD2
TRP
1274 
−30.712
−40.861
−24.698
9.72
C


ATOM
1802 
CE2
TRP
1274 
−30.124
−42.072 
−25.12 
11.07
C


ATOM
1803
CE3
TRP
1274 
−30.083
−39.652
−25.024
13.5
C


ATOM
1804
CD1
TRP
1274 
−31.989
−42.562
−23.993
10.52
C


ATOM
1805 
NE1
TRP
1274 
−30.921
−43.096
−24.679
9.57
N


ATOM
1806
CZ2
TRP
1274
−28.93
−42.109
−25.858
13.29
C


ATOM
1807 
CZ3
TRP
1274 
−28.897
−39.688
−25.756
13.28
C


ATOM
1808 
CH2
TRP
1274 
−28.335 
−40.91
−26.166 
12.43
C


ATOM
1809
C
TRP
1274 
−31.104
−39.087
−21.867 
11.05
C


ATOM
1810
O
TRP
1274
−30.12
−39.746
−21.551 
10.69
O


ATOM
1811
N
GLU
1275 
−31.015 
−37.79
−22.184 
11.93
N


ATOM
1812
CA
GLU
1275 
−29.706
−37.111
−22.147
12.13
C


ATOM
1813
CB
GLU
1275 
−29.778
−35.657
−22.624
14.74
C


ATOM
1814
CG
GLU
1275 
−30.309
−35.362 
−24.01
18.02
C


ATOM
1815
CD
GLU
1275 
−30.436
−33.856
−24.191
20.57
C


ATOM
1816
OE1
GLU
1275 
−31.573
−33.324 
−24.15 
19.95
O


ATOM
1817 
OE2
GLU
1275 
−29.385
−33.197
−24.333 
21.55
O


ATOM
1818 
C
GLU
1275 
−29.203
−37.059
−20.694 
12.79
C


ATOM
1819 
O
GLU
1275 
−27.999
−37.121
−20.435
9.21
O


ATOM
1820
N
LEU
1276 
−30.139
−36.898
−19.759 
11.64
N


ATOM
1821
CA
LEU
1276
−29.83 
−36.83
−18.333
13.52
C


ATOM
1822 
CB
LEU
1276 
−31.128
−36.608
−17.524
13.33
C


ATOM
1823
CG
LEU
1276 
−31.604
−35.226
−17.028
12.41
C


ATOM
1824
CD1
LEU
1276 
−31.498
−34.247
−18.143
17.11
C


ATOM
1825
CD2
LEU
1276 
−33.046
−35.271
−16.511 
11.26
C


ATOM
1826
C
LEU
1276
−29.15
−38.125
−17.882
15.4
C


ATOM
1827
O
LEU
1276 
−28.046 
−38.11
−17.327
16.84
O


ATOM
1828
N
MET
1277 
−29.804
−39.249
−18.154 
14.23
N


ATOM
1829
CA
MET
1277 
−29.288
−40.553 
−17.76
16.99
C


ATOM
1830
CB
MET
1277 
−30.375
−41.605 
−17.97
17.95
C


ATOM
1831
CG
MET
1277
−31.64
−41.311
−17.168
21.05
C


ATOM
1832
SD
MET
1277 
−31.277
−41.118
−15.408
28.97
S


ATOM
1833
CE
MET
1277 
−30.177 
−42.52
−15.198 
24.12
C


ATOM
1834
C
MET
1277 
−27.986
−40.976
−18.442
16.88
C


ATOM
1835
O
MET
1277 
−27.249
−41.794
−17.902
17.63
O


ATOM
1836
N
THR
1278 
−27.703
−40.425 
−19.62 
16.09
N


ATOM
1837
CA
THR
1278 
−26.466
−40.753
−20.339
16.44
C


ATOM
1838 
CB
THR
1278 
−26.677
−40.824
−21.869
15.75
C


ATOM
1839 
OG1
THR
1278 
−27.275
−39.605
−22.322 
14.11
O


ATOM
1840
CG2
THR
1278
−27.55
−42.021
−22.261 
16.13
C


ATOM
1841
C
THR
1278 
−25.412
−39.675
−20.096
16.13
C


ATOM
1842
O
THR
1278 
−24.332
−39.707
−20.682
16.66 
O


ATOM
1843
N
ARG
1279 
−25.745
−38.744
−19.212
16.79 
N


ATOM
1844
CA
ARG
1279 
−24.908
−37.593
−18.881
17.42 
C


ATOM
1845
CB
ARG
1279 
−23.641
−37.996
−18.127
17.17
C


ATOM
1846
CG
ARG
1279 
−23.982
−38.325
−16.685 
19.24
C


ATOM
1847
CD
ARG
1279
−22.78
−38.507
−15.793
20.29
C


ATOM
1848
NE
ARG
1279 
−22.028
−37.264
−15.776
22.44
N


ATOM
1849
CZ
ARG
1279 
−20.833
−37.071
−15.228
24.32 
C


ATOM
1850
NH1
ARG
1279 
−20.181
−38.022
−14.565
25.1
N


ATOM
1851
NH2
ARG
1279 
−20.267
−35.895
−15.386
23.97
N


ATOM
1852
C
ARG
1279 
−24.534 
−36.77
−20.082 
17.7
C


ATOM
1853
O
ARG
1279 
−23.371
−36.456
−20.262 
21.43 
O


ATOM
1854
N
GLY
1280 
−25.503
−36.432
−20.924
15.97
N


ATOM
1855
CA
GLY
1280 
−25.186
−35.597
−22.068
16.82
C


ATOM
1856
C
GLY
1280 
−24.787
−36.224
−23.392
17.54
C


ATOM
1857
O
GLY
1280 
−24.189
−35.542
−24.221
16.85
O


ATOM
1858
N
ALA
1281 
−25.111
−37.498 
−23.6
17.75
N


ATOM
1859
CA
ALA
1281 
−24.802
−38.185
−24.853
17.82
C


ATOM
1860
CB
ALA
1281 
−25.111
−39.671
−24.708
16.36
C


ATOM
1861
C
ALA
1281 
−25.662
−37.587
−25.972
18.54
C


ATOM
1862
O
ALA
1281
−26.8 
−37.201
−25.727
18.61
O


ATOM
1863
N
PRO
1282 
−25.133
−37.482
−27.207
18.63
N


ATOM
1864
CD
PRO
1282 
−23.748
−37.732
−27.652
19.37
C


ATOM
1865
CA
PRO
1282 
−25.969
−36.916
−28.279
19.93
C


ATOM
1866
CB
PRO
1282 
−24.942
−36.503
−29.346
20.38
C


ATOM
1867
CG
PRO
1282 
−23.812
−37.491
−29.157 
19.28
C


ATOM
1868
C
PRO
1282 
−26.983
−37.973
−28.768
20.28
C


ATOM
1869
O
PRO
1282 
−26.594
−39.101
−29.08
20.76
O


ATOM
1870
N
PRO
1283
−28.29
−37.634
−28.852
20.54
N


ATOM
1871
CD
PRO
1283 
−28.977
−36.338
−28.822 
20.35 
C


ATOM
1872
CA
PRO
1283 
−29.214
−38.685
−29.314
21.42
C


ATOM
1873
CB
PRO
1283 
−30.604
−38.102
−29.052 
20.81 
C


ATOM
1874
CG
PRO
1283 
−30.371
−36.751
−28.434
21.83
C


ATOM
1875
C
PRO
1283 
−29.054
−39.061
−30.783
21.78
C


ATOM
1876
O
PRO
1283 
−28.764
−38.205
−31.615
22.56
O


ATOM
1877
N
TYR
1284 
−29.274
−40.337
−31.092 
20.5
N


ATOM
1878
CA
TYR
1284 
−29.159
−40.848
−32.46
21.94
C


ATOM
1879
CB
TYR
1284 
−30.292
−40.303
−33.317 
22.25
C


ATOM
1880
CG
TYR
1284 
−31.641
−40.352
−32.651
21.17
C


ATOM
1881
CD1
TYR
1284 
−32.432
−41.504
−32.706
20.04 
C


ATOM
1882
CE1
TYR
1284 
−33.676
−41.545
−32.084
18.05
C


ATOM
1883
CD2
TYR
1284 
−32.122
−39.247
−31.955 
19.85
C


ATOM
1884
CE2
TYR
1284 
−33.348
−39.277
−31.331
19.2
C


ATOM
1885
CZ
TYR
1284 
−34.125 
−40.42
−31.396
18.12
C


ATOM
1886
OH
TYR
1284 
−35.343
−40.403
−30.772
15.51 
O


ATOM
1887
C
TYR
1284
−27.85
−40.349
−33.034 
22.78 
C


ATOM
1888
O
TYR
1284 
−27.828
−39.743 
−34.1
20.74
O


ATOM
1889
N
PRO
1285 
−26.729
−40.632
−32.372
24.32 
N


ATOM
1890
CD
PRO
1285 
−26.367
−41.515
−31.248
25.4
C


ATOM
1891
CA
PRO
1285 
−25.535
−40.079
−33.002
26.46 
C


ATOM
1892
CB
PRO
1285
−24.43
−40.483
−32.031 
25.47
C


ATOM
1893
CG
PRO
1285 
−24.901
−41.795
−31.53
25.65
C


ATOM
1894
C
PRO
1285 
−25.149
−40.395
−34.446
28.83
C


ATOM
1895
O
PRO
1285
−24.72
−39.505
−35.186
28.91
O


ATOM
1896
N
ASP
1286 
−25.312
−41.639
−34.859
30.51
N


ATOM
1897
CA
ASP
1286 
−24.845
−42.035
−36.171 
34.63
C


ATOM
1898
CB
ASP
1286 
−24.278
−43.468
−35.991
37.19
C


ATOM
1899
CG
ASP
1286 
−22.867 
−43.46
−35.32
40.75 
C


ATOM
1900
OD1
ASP
1286 
−22.625 
−44.11
−34.265
42.38 
O


ATOM
1901
OD2
ASP
1286 
−21.982
−42.776
−35.881
42.78
O


ATOM
1902
C
ASP
1286 
−25.778
−41.846
−37.407
35.2
C


ATOM
1903
O
ASP
1286 
−25.432
−42.243
−38.535
35.64
O


ATOM
1904
N
VAL
1287 
−26.884
−41.115
−37.173
33.72 
N


ATOM
1905
CA
VAL
1287 
−27.987
−40.815
−38.126
33.27 
C


ATOM
1906
CB
VAL
1287 
−29.318
−41.221
−37.487
32.97 
C


ATOM
1907
CG1
VAL
1287
−29.1 
−42.389
−36.558
32.75 
C


ATOM
1908
CG2
VAL
1287 
−29.893
−40.035
−36.693
34.84
C


ATOM
1909
C
VAL
1287 
−28.233
−39.357
−38.616 
32.3
C


ATOM
1910
O
VAL
1287
−28.04 
−38.4 
−37.861
31.13
O


ATOM
1911
N
ASN
1288 
−28.724
−39.201
−39.852
30
N


ATOM
1912
CA
ASN
1288 
−29.047 
−37.87
−40.387
27.35
C


ATOM
1913
CB
ASN
1288 
−28.569
−37.722
−41.843 
25.1
C


ATOM
1914
CG
ASN
1288 
−29.298
−38.651
−42.807
23.58
C


ATOM
1915
OD1
ASN
1288 
−30.486
−38.905
−42.657 
20.67 
O


ATOM
1916
ND2
ASN
1288 
−28.586 
−39.14
−43.814
21.64 
N


ATOM
1917
C
ASN
1288 
−30.575
−37.662
−40.279
26.78 
C


ATOM
1918
O
ASN
1288 
−31.322
−38.629
−40.141
25.63
O


ATOM
1919
N
THR
1289 
−31.033
−36.412
−40.355
27.2
N


ATOM
1920
CA
THR
1289 
−32.457 
−36.08
−40.193
28.7
C


ATOM
1921
CB
THR
1289 
−32.638
−34.569
−40.092
29.7
C


ATOM
1922
OG1
THR
1289 
−32.974
−34.004
−41.359
32.14
O


ATOM
1923
CG2
THR
1289 
−31.363
−33.978
−39.679 
30.98 
C


ATOM
1924
C
THR
1289 
−33.422 
−36.64
−41.205
28.93 
C


ATOM
1925
O
THR
1289 
−34.637
−36.448
−41.092
29.84
O


ATOM
1926
N
PHE
1290 
−32.885
−37.331
−42.202
28.3
N


ATOM
1927
CA
PHE
1290 
−33.758
−37.948
−43.159
28.01
C


ATOM
1928
CB
PHE
1290
−33.15
−38.156
−44.519
28.4
C


ATOM
1929
CG
PHE
1290 
−34.013
−39.008
−45.375
30.93 
C


ATOM
1930
CD1
PHE
1290 
−35.181
−38.489
−45.906
30.67
C


ATOM
1931
CD2
PHE
1290 
−33.737
−40.355
−45.547
29.81
C


ATOM
1932
CE1
PHE
1290 
−36.058
−39.292
−46.589
32.06 
C


ATOM
1933
CE2
PHE
1290 
−34.615
−41.167
−46.231 
32.26 
C


ATOM
1934
CZ
PHE
1290 
−35.777
−40.635
−46.752
31.34
C


ATOM
1935
C
PHE
1290 
−34.152
−39.321
−42.675
27.78
C


ATOM
1936
O
PHE
1290 
−35.296
−39.718
−42.827
27.15
O


ATOM
1937
N
ASP
1291 
−33.237 
−40.09
−42.117
26.53
N


ATOM
1938
CA
ASP
1291 
−33.727 
−41.38
−41.705 
28.3
C


ATOM
1939
CB
ASP
1291 
−32.878
−42.484
−42.312
31.72
C


ATOM
1940
CG
ASP
1291
−31.43
−42.208
−42.173
34.91
C


ATOM
1941
OD1
ASP
1291 
−31.077
−41.644
−41.112
36.01 
O


ATOM
1942
OD2
ASP
1291 
−30.662
−42.549
−43.101
32.69 
O


ATOM
1943
C
ASP
1291 
−33.923
−41.575
−40.212
26.5
C


ATOM
1944
O
ASP
1291 
−34.187
−42.688
−39.761
25.11
O


ATOM
1945
N
ILE
1292 
−33.793
−40.505
−39.436 
24.99
N


ATOM
1946
CA
ILE
1292 
−34.075
−40.621
−38.016
24.84
C


ATOM
1947
CB
ILE
1292 
−33.607
−39.358
−37.223
25.08 
C


ATOM
1948
CG2
ILE
1292 
−34.193
−38.124 
−37.85
24.46 
C


ATOM
1949
CG1
ILE
1292 
−34.071
−39.404
−35.759
23.22 
C


ATOM
1950
CD
ILE
1292 
−34.253
−40.785
−35.155
25.97
C


ATOM
1951
C
ILE
1292
−35.61
−40.707
−38.075
24.13
C


ATOM
1952
O
ILE
1292 
−36.254
−41.303
−37.217
23.5
O


ATOM
1953
N
THR
1293 
−36.179
−40.143 
−39.14
23.68
N


ATOM
1954
CA
THR
1293 
−37.624
−40.139 
−39.33
24.12
C


ATOM
1955
CB
THR
1293 
−38.036
−39.061
−40.377
26.66
C


ATOM
1956
OG1
THR
1293 
−37.503
−37.787
−39.975 
28.33
O


ATOM
1957
CG2
THR
1293 
−39.558
−38.934
−40.463
27.13
C


ATOM
1958
C
THR
1293 
−38.115
−41.527
−39.741
24.12
C


ATOM
1959
O
THR
1293 
−39.176 
−41.98
−39.316
23.92
O


ATOM
1960
N
VAL
1294 
−37.323
−42.201
−40.559 
22.73 
N


ATOM
1961
CA
VAL
1294 
−37.638
−43.542
−40.998 
22.69 
C


ATOM
1962
CB
VAL
1294 
−36.657
−43.948
−42.108
23.12
C


ATOM
1963
CG1
VAL
1294 
−36.576
−45.413 
−42.18
23.01 
C


ATOM
1964
CG2
VAL
1294 
−37.084
−43.339
−43.438
23.05
C


ATOM
1965
C
VAL
1294
−37.51
−44.466 
−39.76
22.25 
C


ATOM
1966
O
VAL
1294 
−38.398
−45.284 
−39.49 
22.56
O


ATOM
1967
N
TYR
1295 
−36.405
−44.297
−39.017
20.41
N


ATOM
1968
CA
TYR
1295 
−36.074
−45.036
−37.775
19.13
C


ATOM
1969
CB
TYR
1295 
−34.786
−44.436
−37.133 
20.43
C


ATOM
1970
CG
TYR
1295 
−34.263
−45.004
−35.773
22.2
C


ATOM
1971
CD1
TYR
1295 
−33.174
−45.889
−35.729
22.09
C


ATOM
1972
CE1
TYR
1295 
−32.652
−46.373
−34.502 
22.58
C


ATOM
1973
CD2
TYR
1295 
−34.823
−44.609 
−34.54
21.45
C


ATOM
1974
CE2
TYR
1295 
−34.299
−45.093
−33.299
22.41
C


ATOM
1975
CZ
TYR
1295 
−33.216
−45.979
−33.302
22.9
C


ATOM
1976
OH
TYR
1295 
−32.719
−46.521
−32.132
23.86 
O


ATOM
1977
C
TYR
1295 
−37.238
−44.967
−36.781
17.02
C


ATOM
1978
O
TYR
1295 
−37.635
−45.987
−36.217
17.06
O


ATOM
1979
N
LEU
1296 
−37.768
−43.764
−36.557
15.78
N


ATOM
1980
CA
LEU
1296 
−38.892
−43.564
−35.636
15.62
C


ATOM
1981
CB
LEU
1296
−39.19
−42.069 
−35.44
13.27
C


ATOM
1982
CG
LEU
1296 
−38.167
−41.253
−34.648 
14.85
C


ATOM
1983
CD1
LEU
1296 
−38.665
−39.812 
−34.44 
13.49
C


ATOM
1984
CD2
LEU
1296 
−37.931
−41.928
−33.301
12.69 
C


ATOM
1985
C
LEU
1296 
−40.107
−44.233
−36.242
17.24
C


ATOM
1986
O
LEU
1296 
−40.917
−44.859
−35.547
17.7
O


ATOM
1987
N
LEU
1297 
−40.224
−44.085
−37.555
18.13
N


ATOM
1988
CA
LEU
1297 
−41.313 
−44.68
−38.292
20.85
C


ATOM
1989
CB
LEU
1297
−41.21
−44.288
−39.778
22.8
C


ATOM
1990
CG
LEU
1297 
−42.437
−43.505
−40.283
24.14
C


ATOM
1991
CD1
LEU
1297 
−43.187
−42.928
−39.098
26.68
C


ATOM
1992
CD2
LEU
1297 
−42.036
−42.403
−41.242
24.5
C


ATOM
1993
C
LEU
1297 
−41.316
−46.203
−38.086
21.11
C


ATOM
1994
O
LEU
1297 
−42.353
−46.759
−37.735
21.79
O


ATOM
1995
N
GLN
1298 
−40.167
−46.864
−38.265
21.59
N


ATOM
1996
CA
GLN
1298 
−40.059 
−48.32
−38.058
21.53
C


ATOM
1997
CB
GLN
1298 
−38.663
−48.825
−38.468 
22.02
C


ATOM
1998
CG
GLN
1298 
−38.339
−48.635
−39.955
22.67
C


ATOM
1999
CD
GLN
1298 
−36.856
−48.747
−40.277
25.11 
C


ATOM
2000
OE1
GLN
1298
−36.02
−48.914
−39.385
25.42
O


ATOM
2001
NE2
GLN
1298 
−36.522
−48.646
−41.566
27.23
N


ATOM
2002
C
GLN
1298 
−40.305
−48.629 
−36.58
21.21 
C


ATOM
2003
O
GLN
1298 
−40.241
−49.785
−36.143
23.95 
O


ATOM
2004
N
GLY
1299 
−40.571
−47.578 
−35.81
19.63
N


ATOM
2005
CA
GLY
1299 
−40.842
−47.739
−34.395
16.55
C


ATOM
2006
C
GLY
1299 
−39.635
−47.944
−33.491
16.17
C


ATOM
2007
O
GLY
1299 
−39.782
−48.481
−32.394
15.64
O


ATOM
2008
N
ARG
1300 
−38.453
−47.536
−33.944
15.6
N


ATOM
2009
CA
ARG
1300
−37.23
−47.663 
−33.15
14.57
C


ATOM
2010
CB
ARG
1300 
−35.987
−47.624
−34.061
13.21
C


ATOM
2011
CG
ARG
1300 
−35.606
−48.953
−34.696
12.55
C


ATOM
2012
CD
ARG
1300
−34.87
−48.794
−36.041
12.57 
C


ATOM
2013
NE
ARG
1300
−35.26
−49.892
−36.918 
14.36
N


ATOM
2014
CZ
ARG
1300 
−34.748
−51.118
−36.859
15.98
C


ATOM
2015
NH1
ARG
1300 
−33.792 
−51.41
−35.981
17.16
N


ATOM
2016
NH2
ARG
1300 
−35.251
−52.073
−37.624
12.34
N


ATOM
2017
C
ARG
1300 
−37.171
−46.474
−32.196
14.89
C


ATOM
2018
O
ARG
1300 
−37.633
−45.389
−32.536
14.23
O


ATOM
2019
N
ARG
1301 
−36.615
−46.663
−31.006
14.09
N


ATOM
2020
CA
ARG
1301 
−36.504
−45.548
−30.085
14.82
C


ATOM
2021
CB
ARG
1301 
−37.522
−45.684 
−28.96
15.03
C


ATOM
2022
CG
ARG
1301 
−38.961
−45.614
−29.449
16.03
C


ATOM
2023
CD
ARG
1301 
−39.267
−44.225
−30.023
16.85
C


ATOM
2024
NE
ARG
1301 
−40.663
−44.068
−30.429
17.41
N


ATOM
2025
CZ
ARG
1301 
−41.145
−44.345
−31.635
17.22
C


ATOM
2026
NH1
ARG
1301 
−40.354 
−44.8 
−32.598 
15.84
N


ATOM
2027
NH2
ARG
1301 
−42.435
−44.167
−31.876
21.38 
N


ATOM
2028
C
ARG
1301 
−35.097
−45.495
−29.524
15.64
C


ATOM
2029
O
ARG
1301 
−34.282
−46.375
−29.805 
15.79
O


ATOM
2030
N
LEU
1302 
−34.804
−44.455
−28.757
12.85 
N


ATOM
2031
CA
LEU
1302 
−33.493 
−44.32
−28.141
15.61
C


ATOM
2032
CB
LEU
1302
−33.38
−42.956
−27.437
15.94
C


ATOM
2033
CG
LEU
1302 
−33.299
−41.659 
−28.26 
12.87
C


ATOM
2034
CD1
LEU
1302 
−33.581
−40.444
−27.379
14
C


ATOM
2035
CD2
LEU
1302 
−31.927
−41.543
−28.882 
15.39
C


ATOM
2036
C
LEU
1302 
−33.409
−45.472
−27.131 
16.47 
C


ATOM
2037
O
LEU
1302 
−34.375
−45.735
−26.408
16.43 
O


ATOM
2038
N
LEU
1303 
−32.276
−46.168
−27.086
16.41 
N


ATOM
2039
CA
LEU
1303 
−32.143
−47.309
−26.187
18.6
C


ATOM
2040
CB
LEU
1303 
−31.037
−48.239
−26.727
19.3
C


ATOM
2041
CG
LEU
1303 
−31.469
−48.766
−28.121
22.94
C


ATOM
2042
CD1
LEU
1303 
−30.288
−49.341 
−28.91
22.68
C


ATOM
2043
CD2
LEU
1303 
−32.563
−49.818 
−27.95
19.49
C


ATOM
2044
C
LEU
1303 
−31.953
−46.931
−24.703 
18.49
C


ATOM
2045
O
LEU
1303 
−31.622
−45.788 
−24.38
17.75
O


ATOM
2046
N
GLN
1304 
−32.218
−47.876
−23.804
16.43
N


ATOM
2047
CA
GLN
1304 
−32.094
−47.608
−22.376 
17.47
C


ATOM
2048
CB
GLN
1304 
−32.686 
−48.76
−21.556
16.36
C


ATOM
2049
CG
GLN
1304 
−32.738
−48.413
−20.069
20
C


ATOM
2050
CD
GLN
1304 
−33.444
−49.453
−19.219
19.17
C


ATOM
2051
OE1
GLN
1304 
−33.769
−49.195 
−18.06
23.21
O


ATOM
2052
NE2
GLN
1304 
−33.674
−50.632 
−19.78
20.05
N


ATOM
2053
C
GLN
1304
−30.64
−47.385
−21.956
17.45
C


ATOM
2054
O
GLN
1304 
−29.788
−48.223
−22.207
18.13
O


ATOM
2055
N
PRO
1305 
−30.335
−46.245
−21.318
17.11
N


ATOM
2056
CD
PRO
1305 
−31.109
−44.993
−21.246
17.67
C


ATOM
2057
CA
PRO
1305 
−28.943
−46.017
−20.906
18.76
C


ATOM
2058
CB
PRO
1305 
−28.948
−44.557
−20.464
17.33
C


ATOM
2059
CG
PRO
1305 
−30.016
−43.951
−21.316
20.16
C


ATOM
2060
C
PRO
1305 
−28.493
−46.925
−19.762
19.88
C


ATOM
2061
O
PRO
1305 
−29.317 
−47.39
−18.987
17.37
O


ATOM
2062
N
GLU
1306 
−27.188
−47.169
−19.668
23.66
N


ATOM
2063
CA
GLU
1306 
−26.634
−47.978
−18.586 
28.01
C


ATOM
2064
CB
GLU
1306 
−25.106
−48.108
−18.749
29.98
C


ATOM
2065
CG
GLU
1306 
−24.401
−48.854
−17.605
34.82
C


ATOM
2066
CD
GLU
1306 
−22.979
−49.299
−17.948 
36.96
C


ATOM
2067
OE1
GLU
1306 
−22.688 
−50.51
−17.812
38.32
O


ATOM
2068
OE2
GLU
1306 
−22.154
−48.447
−18.346
37.25
O


ATOM
2069
C
GLU
1306 
−26.971
−47.185
−17.315
29.78
C


ATOM
2070
O
GLU
1306 
−26.886
−45.961
−17.323
32.55
O


ATOM
2071
N
TYR
1307 
−27.381
−47.857
−16.243
30.97
N


ATOM
2072
CA
TYR
1307 
−27.716
−47.179
−14.971
30.01
C


ATOM
2073
CB
TYR
1307 
−26.643 
−46.14
−14.567
31.8
C


ATOM
2074
CG
TYR
1307
−25.18
−46.581
−14.564
33.12
C


ATOM
2075
CD1
TYR
1307
−24.21
−45.814
−15.214
33.66
C


ATOM
2076
CE1
TYR
1307 
−22.866
−46.218
−15.262
34.33
C


ATOM
2077
CD2
TYR
1307 
−24.771
−47.765
−13.946
33.66
C


ATOM
2078
CE2
TYR
1307 
−23.429
−48.179
−13.986
34.02
C


ATOM
2079
CZ
TYR
1307 
−22.484
−47.406
−14.654
35.13
C


ATOM
2080
OH
TYR
1307 
−21.185
−47.867
−14.776
34.55
O


ATOM
2081
C
TYR
1307 
−29.076
−46.452
−14.918
28.96
C


ATOM
2082
O
TYR
1307 
−29.432
−45.895
−13.881
27.44
O


ATOM
2083
N
CYS
1308
−29.82
−46.405
−16.019
27.77
N


ATOM
2084
CA
CYS
1308 
−31.126
−45.744
−15.988
25.91
C


ATOM
2085
CB
CYS
1308
−31.56
−45.362
−17.409
25.12
C


ATOM
2086
SG
CYS
1308 
−33.321
−44.917
−17.596
24
S


ATOM
2087
C
CYS
1308 
−32.055
−46.804
−15.414
25.06
C


ATOM
2088
O
CYS
1308 
−31.968 
−47.96
−15.812
23.71
O


ATOM
2089
N
PRO
1309 
−32.952
−46.442
−14.477 
24.93
N


ATOM
2090
CD
PRO
1309 
−33.195 
−45.18
−13.761
25.38 
C


ATOM
2091
CA
PRO
1309 
−33.817
−47.503
−13.954 
23.94
C


ATOM
2092
CB
PRO
1309 
−34.344
−46.928
−12.635
25.11
C


ATOM
2093
CG
PRO
1309 
−33.496
−45.682
−12.386
26.23
C


ATOM
2094
C
PRO
1309 
−34.961
−47.871
−14.891
23.92
C


ATOM
2095
O
PRO
1309
−35.53
−47.017
−15.567
24.15
O


ATOM
2096
N
ASP
1310 
−35.291
−49.155
−14.902
22.35
N


ATOM
2097
CA
ASP
1310 
−36.365
−49.695 
−15.72 
22.11
C


ATOM
2098
CB
ASP
1310 
−36.698
−51.109 
−15.24 
25.28
C


ATOM
2099
CG
ASP
1310 
−35.592
−52.102
−15.553
27.4
C


ATOM
2100
OD1
ASP
1310 
−34.505
−51.668
−15.992
28.7
O


ATOM
2101
OD2
ASP
1310 
−35.806
−53.317
−15.357
28.25 
O


ATOM
2102
C
ASP
1310 
−37.632 
−48.84
−15.739
20.06 
C


ATOM
2103
O
ASP
1310 
−38.174
−48.544 
−16.8
18.79 
O


ATOM
2104
N
PRO
1311 
−38.142
−48.451
−14.562 
19.74
N


ATOM
2105
CD
PRO
1311 
−37.807
−48.805
−13.174 
18.73
C


ATOM
2106
CA
PRO
1311 
−39.351
−47.629
−14.602 
18.41
C


ATOM
2107
CB
PRO
1311 
−39.741
−47.517
−13.128
17.9
C


ATOM
2108
CG
PRO
1311 
−38.441
−47.673 
−12.42 
18.48
C


ATOM
2109
C
PRO
1311 
−39.143
−46.265
−15.261
16.43 
C


ATOM
2110
O
PRO
1311 
−40.071 
−45.71
−15.842
14.98
O


ATOM
2111
N
LEU
1312 
−37.935
−45.716
−15.191 
14.58
N


ATOM
2112
CA
LEU
1312
−37.73
−44.428
−15.824
13.14
C


ATOM
2113
CB
LEU
1312 
−36.413
−43.778
−15.407
13.51
C


ATOM
2114
CG
LEU
1312 
−36.337
−42.287
−15.754 
11.5
C


ATOM
2115
CD1
LEU
1312 
−37.488
−41.494
−15.114 
13.78
C


ATOM
2116
CD2
LEU
1312
−35.01 
−41.77
−15.254 
13.81
C


ATOM
2117
C
LEU
1312
−37.74 
−44.62
−17.316
13.15
C


ATOM
2118
O
LEU
1312 
−38.261
−43.785
−18.051 
11.21
O


ATOM
2119
N
TYR
1313 
−37.162
−45.722
−17.777
14.68
N


ATOM
2120
CA
TYR
1313 
−37.159
−45.972
−19.208
14.13
C


ATOM
2121
CB
TYR
1313 
−36.325
−47.198
−19.573
15.38 
C


ATOM
2122
CG
TYR
1313 
−36.105
−47.341
−21.075 
15.55
C


ATOM
2123
CD1
TYR
1313 
−35.638
−46.265
−21.841
17.29 
C


ATOM
2124
CE1
TYR
1313 
−35.407
−46.393
−23.216
16.45
C


ATOM
2125
CD2
TYR
1313 
−36.338
−48.552
−21.721
14.65
C


ATOM
2126
CE2
TYR
1313 
−36.111
−48.694
−23.088
17.53 
C


ATOM
2127
CZ
TYR
1313 
−35.644
−47.608
−23.832
16.76
C


ATOM
2128
OH
TYR
1313 
−35.418
−47.749 
−25.18
17.88
O


ATOM
2129
C
TYR
1313 
−38.591
−46.156
−19.687
14.31
C


ATOM
2130
O
TYR
1313 
−38.936
−45.653
−20.751
14.78
O


ATOM
2131
N
GLU
1314 
−39.421
−46.863
−18.913
15.45
N


ATOM
2132
CA
GLU
1314 
−40.832
−47.065
−19.287 
19.13
C


ATOM
2133
CB
GLU
1314 
−41.636
−47.741
−18.155
21.74 
C


ATOM
2134
CG
GLU
1314 
−42.374
−49.072
−18.498
30.22
C


ATOM
2135
CD
GLU
1314 
−43.763 
−48.91 
−19.15
35.3
C


ATOM
2136
OE1
GLU
1314 
−43.865
−48.965 
−20.4
38.8
O


ATOM
2137
OE2
GLU
1314
−44.76
−48.739
−18.411 
38.41
O


ATOM
2138
C
GLU
1314 
−41.414
−45.674 
−19.54
17.22 
C


ATOM
2139
O
GLU
1314 
−42.127
−45.461 
−20.52
17.96 
O


ATOM
2140
N
VAL
1315 
−41.111
−44.742
−18.635 
15.21
N


ATOM
2141
CA
VAL
1315 
−41.578
−43.359
−18.745
13.46
C


ATOM
2142
CB
VAL
1315 
−40.957 
−42.44
−17.656
14.51
C


ATOM
2143
CG1
VAL
1315 
−41.324
−40.976
−17.926 
13.39
C


ATOM
2144
CG2
VAL
1315 
−41.438
−42.857
−16.274 
12.16
C


ATOM
2145
C
VAL
1315 
−41.138
−42.819
−20.092
14.52
C


ATOM
2146
O
VAL
1315 
−41.951
−42.333
−20.887
10.37
O


ATOM
2147
N
MET
1316 
−39.834
−42.921
−20.333
14.75
N


ATOM
2148
CA
MET
1316 
−39.252
−42.436 
−21.57
17.75
C


ATOM
2149
CB
MET
1316 
−37.763
−42.803
−21.663
20.34
C


ATOM
2150
CG
MET
1316 
−36.819
−42.276
−20.559
19.79
C


ATOM
2151
SD
MET
1316 
−35.114
−42.567 
−21.17
21.6
S


ATOM
2152
CE
MET
1316 
−34.136
−42.746
−19.658
23.16
C


ATOM
2153
C
MET
1316 
−39.987 
−43.02 
−22.77
18.51
C


ATOM
2154
O
MET
1316
−40.42
−42.274
−23.651
19.69
O


ATOM
2155
N
LEU
1317 
−40.142
−44.345
−22.815
17.78
N


ATOM
2156
CA
LEU
1317 
−40.829
−44.956
−23.945
17.94
C


ATOM
2157
CB
LEU
1317 
−40.888
−46.473
−23.795
17.54
C


ATOM
2158
CG
LEU
1317 
−39.502
−47.099
−23.888
18.27
C


ATOM
2159
CD1
LEU
1317
−39.58
−48.542
−23.434
19.06
C


ATOM
2160
CD2
LEU
1317 
−38.961
−46.976
−25.315
18.11
C


ATOM
2161
C
LEU
1317 
−42.226
−44.399
−24.094
19.36
C


ATOM
2162
O
LEU
1317 
−42.676
−44.125
−25.206
19.4
O


ATOM
2163
N
LYS
1318 
−42.917 
−44.22
−22.976
18.7
N


ATOM
2164
CA
LYS
1318 
−44.268
−43.685
−23.029
20.42
C


ATOM
2165
CB
LYS
1318 
−44.879
−43.663
−21.625
21.8
C


ATOM
2166
CG
LYS
1318
−45.9 
−44.794
−21.389
26.1
C


ATOM
2167
CD
LYS
1318 
−46.046
−45.138
−19.905
26.99
C


ATOM
2168
CE
LYS
1318 
−47.177
−46.138
−19.636
30.43
C


ATOM
2169
NZ
LYS
1318 
−48.042
−45.717
−18.483
32.95
N


ATOM
2170
C
LYS
1318 
−44.284
−42.288
−23.657
20.66
C


ATOM
2171
O
LYS
1318 
−45.195
−41.942
−24.417
21.24
O


ATOM
2172
N
CYS
1319 
−43.268 
−41.49
−23.353 
18.11
N


ATOM
2173
CA
CYS
1319 
−43.188
−40.152
−23.918
16.47
C


ATOM
2174
CB
CYS
1319 
−41.964
−39.408
−23.386
15.37
C


ATOM
2175
SG
CYS
1319 
−42.114
−38.898
−21.672 
12.54
S


ATOM
2176
C
CYS
1319 
−43.074
−40.248
−25.422
18
C


ATOM
2177
O
CYS
1319 
−43.512 
−39.35
−26.139 
15.45
O


ATOM
2178
N
TRP
1320 
−42.489
−41.338
−25.911
18.62
N


ATOM
2179
CA
TRP
1320 
−42.323
−41.463
−27.348
19.38
C


ATOM
2180
CB
TRP
1320 
−40.935
−41.999
−27.689
17.86
C


ATOM
2181
CG
TRP
1320 
−39.797
−41.256 
−27.06 
16.31
C


ATOM
2182
CD2
TRP
1320 
−38.626 
−41.84
−26.488
16.1
C


ATOM
2183
CE2
TRP
1320 
−37.816
−40.782
−26.019
15.34
C


ATOM
2184
CE3
TRP
1320 
−38.182
−43.162
−26.327
14.66
C


ATOM
2185
CD1
TRP
1320 
−39.659
−39.902
−26.926
13.95
C


ATOM
2186
NE1
TRP
1320 
−38.471
−39.609
−26.299
14.46
N


ATOM
2187
CZ2
TRP
1320 
−36.587
−41.004
−25.396
16.01
C


ATOM
2188
CZ3
TRP
1320 
−36.967
−43.385
−25.714
13.39
C


ATOM
2189
CH2
TRP
1320 
−36.179
−42.311
−25.252
14.92
C


ATOM
2190
C
TRP
1320
−43.361
−42.293
−28.093
21.79
C


ATOM
2191
O
TRP
1320
−43.098
−42.741
−29.207
21.52
O


ATOM
2192 
N
HIS
1321
−44.534
−42.501
−27.508 
21.94
N


ATOM
2193 
CA
HIS
1321
−45.57
−43.266
−28.198
22.23
C


ATOM
2194
CB
HIS
1321
−46.832 
−43.3 
−27.343 
23.03
C


ATOM
2195
CG
HIS
1321
−47.853
−44.286
−27.811
24.08
C


ATOM
2196
CD2
HIS
1321
−48.285
−45.442
−27.259
24.79
C


ATOM
2197
ND1
HIS
1321
−48.555
−44.135
−28.986 
25.03
N


ATOM
2198
CE1
HIS
1321
−49.378
−45.157
−29.137 
24.27
C


ATOM
2199
NE2
HIS
1321
−49.233
−45.964
−28.103 
26.25
N


ATOM
2200
C
HIS
1321
−45.87 
−42.58
−29.538
22
C


ATOM
2201
O
HIS
1321
−45.966
−41.351
−29.602
19.88
O


ATOM
2202
N
PRO
1322
−46.016
−43.358 
−30.63
21.9
N


ATOM
2203
CD
PRO
1322
−45.801
−44.808
−30.784
22.07
C


ATOM
2204
CA
PRO
1322
−46.3 
−42.721
−31.926
22.49
C


ATOM
2205
CB
PRO
1322
−46.304
−43.905
−32.904
20.78
C


ATOM
2206
CG
PRO
1322
−46.567
−45.108
−32.037 
20.57
C


ATOM
2207
C
PRO
1322
−47.579
−41.918
−31.963
23.4
C


ATOM
2208
O
PRO
1322
−47.778
−41.017
−32.789 
22.39
O


ATOM
2209
N
LYS
1323
−48.405
−42.188 
−30.98
24.92
N


ATOM
2210
CA
LYS
1323
−49.697
−41.569
−30.918
25.96
C


ATOM
2211
CB
LYS
1323
−50.574
−42.739
−30.573
28.31
C


ATOM
2212
CG
LYS
1323
−51.827
−42.832
−31.242 
30.59
C


ATOM
2213
CD
LYS
1323
−51.727
−43.515
−32.566
32.35
C


ATOM
2214
CE
LYS
1323
−52.933
−44.485 
−32.88
34.1
C


ATOM
2215
NZ
LYS
1323
−52.65
−45.312
−34.124 
34.56
N


ATOM
2216
C
LYS
1323
−49.758
−40.444
−29.909
26.46
C


ATOM
2217
O
LYS
1323
−50.007
−40.667
−28.758
25.08
O


ATOM
2218
N
ALA
1324
−49.634
−39.187
−30.295
26.66
N


ATOM
2219 
CA
ALA
1324
−49.62
−38.088
−29.304
27.92
C


ATOM
2220
CB
ALA
1324
−49.95
−36.785
−29.987
25.6
C


ATOM
2221
C
ALA
1324
−50.446
−38.245
−28.055
28.17
C


ATOM
2222
O
ALA
1324
−50.036
−37.905
−26.931
27.6
O


ATOM
2223
N
GLU
1325
−51.686 
−38.71
−28.301
29.23
N


ATOM
2224
CA
GLU
1325
−52.504
−38.853
−27.162
29.6
C


ATOM
2225
CB
GLU
1325
−53.952
−38.627
−27.542
31.15
C


ATOM
2226
CG
GLU
1325
−54.643
−39.516
−28.214
34.14
C


ATOM
2227 
CD
GLU
1325
−54.089
−39.858
−29.564
37.11
C


ATOM
2228
OE1
GLU
1325
−53.647
−39.081
−30.455
37.72
O


ATOM
2229
OE2
GLU
1325
−54.189
−41.064
−29.758
38.5
O


ATOM
2230
C
GLU
1325
−52.362 
−40.01
−26.213
28.69
C


ATOM
2231
O
GLU
1325
−52.972
−39.871
−25.213
28.59
O


ATOM
2232 
N
MET
1326
−51.468
−40.993
−26.388
28.82
N


ATOM
2233
CA
MET
1326
−51.245
−42.047
−25.396
29.26
C


ATOM
2234
CB
MET
1326
−50.955
−43.396
−26.095
32.22
C


ATOM
2235
CG
MET
1326
−52.066
−44.064
−26.984 
38.68
C


ATOM
2236 
SD
MET
1326
−53.888
−43.928 
−26.71
45.38
S


ATOM
2237
CE
MET
1326
−54.572
−45.537
−27.685
43.56
C


ATOM
2238
C
MET
1326
−50.005
−41.619
−24.608
28
C


ATOM
2239
O
MET
1326
−49.463
−42.377
−23.802 
28.97
O


ATOM
2240
N
ARG
1327
−49.56
−40.394 
−24.86 
25.84
N


ATOM
2241
CA
ARG
1327
−48.4
−39.855
−24.179
23.95
C


ATOM
2242
CB
ARG
1327
−47.76
−38.751
−25.018
22.84
C


ATOM
2243
CG
ARG
1327 
−47.176
−39.309
−26.287
22.89
C


ATOM
2244
CD
ARG
1327 
−46.312 
−38.32
−27.012
21.37 
C


ATOM
2245
NE
ARG
1327 
−46.201
−38.754 
−28.39
19.79
N


ATOM
2246
CZ
ARG
1327 
−46.045
−37.934
−29.417
19
C


ATOM
2247
NH1
ARG
1327 
−45.971
−36.629
−29.214
17.36 
N


ATOM
2248
NH2
ARG
1327 
−45.993
−38.425
−30.647
17.81 
N


ATOM
2249
C
ARG
1327 
−48.784
−39.293
−22.835 
22.04
C


ATOM
2250
O
ARG
1327 
−49.876
−38.761
−22.666
21.25 
O


ATOM
2251
N
PRO
1328 
−47.899
−39.441
−21.854
21.95
N


ATOM
2252
CD
PRO
1328 
−46.644
−40.199
−21.724
22.8
C


ATOM
2253
CA
PRO
1328 
−48.266
−38.874
−20.605 
21.34
C


ATOM
2254
CB
PRO
1328 
−47.249
−39.534
−19.606
21.48
C


ATOM
2255
CG
PRO
1328 
−46.083
−39.682
−20.415
23.57
C


ATOM
2256
C
PRO
1328
−48.31 
−37.37
−20.508
20.97
C


ATOM
2257
O
PRO
1328 
−47.608
−36.705 
−21.26
21.32
O


ATOM
2258
N
SER
1329 
−49.152
−36.854 
−19.61
20.09 
N


ATOM
2259
CA
SER
1329 
−49.285
−35.419
−19.361
19.4
C


ATOM
2260
CB
SER
1329 
−50.552
−35.135
−18.548 
19.48 
C


ATOM
2261
OG
SER
1329 
−50.436
−35.663
−17.232
21.56
O


ATOM
2262
C
SER
1329 
−48.066 
−35.09
−18.518 
19.12 
C


ATOM
2263
O
SER
1329 
−47.354
−35.999
−18.093
18.4
O


ATOM
2264
N
PHE
1330
−47.8
−33.816
−18.259
19.43
N


ATOM
2265
CA
PHE
1330 
−46.627
−33.511
−17.447
19.52 
C


ATOM
2266
CB
PHE
1330 
−46.166
−32.066
−17.716
17.45 
C


ATOM
2267
CG
PHE
1330
−45.31
−31.927
−18.971
16.35
C


ATOM
2268
CD1
PHE
1330 
−44.005
−32.427
−18.999
16.41 
C


ATOM
2269
CD2
PHE
1330 
−45.809
−31.319
−20.124
16.49
C


ATOM
2270
CE1
PHE
1330 
−43.212 
−32.32
−20.152
15.43
C


ATOM
2271
CE2
PHE
1330 
−45.025 
−31.21 
−21.28
15.83 
C


ATOM
2272
CZ
PHE
1330 
−43.724
−31.711
−21.292 
16.39
C


ATOM
2273
C
PHE
1330 
−46.951
−33.816
−15.978
18.21
C


ATOM
2274
O
PHE
1330 
−46.066
−34.112
−15.172
17.21 
O


ATOM
2275
N
SER
1331 
−48.247
−33.808 
−15.67 
21.81 
N


ATOM
2276
CA
SER
1331 
−48.763
−34.137
−14.341
22.73
C


ATOM
2277
CB
SER
1331 
−50.291
−34.012
−14.318
25.32 
C


ATOM
2278
OG
SER
1331
−50.7
−32.663
−14.454
25.24
O


ATOM
2279
C
SER
1331 
−48.379
−35.581
−14.001
21.79
C


ATOM
2280
O
SER
1331 
−47.698
−35.816
−12.999
21
O


ATOM
2281
N
GLU
1332 
−48.824
−36.533
−14.831
23.52 
N


ATOM
2282
CA
GLU
1332 
−48.512 
−37.95
−14.628
24.89
C


ATOM
2283
CB
GLU
1332 
−49.171
−38.856
−15.729
29.5
C


ATOM
2284
CG
GLU
1332 
−48.682
−38.665 
−17.21 
37.98 
C


ATOM
2285
CD
GLU
1332 
−49.432
−39.536 
−18.28
43.96 
C


ATOM
2286
OE1
GLU
1332 
−50.339
−40.303
−17.982
45.97
O


ATOM
2287
OE2
GLU
1332 
−49.132 
−39.46
−19.444 
47.85
O


ATOM
2288
C
GLU
1332 
−46.981
−38.047
−14.635
22.38 
C


ATOM
2289
O
GLU
1332 
−46.393
−38.787
−13.855
23.87 
O


ATOM
2290
N
LEU
1333 
−46.327
−37.261
−15.481
20.18
N


ATOM
2291
CA
LEU
1333 
−44.875
−37.295
−15.507
18.89
C


ATOM
2292
CB
LEU
1333 
−44.318 
−36.39
−16.622
20.31
C


ATOM
2293
CG
LEU
1333 
−43.658
−37.081
−17.836
19.84
C


ATOM
2294
CD1
LEU
1333 
−44.137
−38.513
−17.983
21.18
C


ATOM
2295
CD2
LEU
1333 
−43.963 
−36.29
−19.091 
19.76
C


ATOM
2296
C
LEU
1333 
−44.292
−36.926
−14.138
18.06
C


ATOM
2297
O
LEU
1333 
−43.457 
−37.67
−13.629
17.4
O


ATOM
2298
N
VAL
1334 
−44.712
−35.829 
−13.5
16.42
N


ATOM
2299
CA
VAL
1334 
−44.101
−35.581
−12.195
14.44
C


ATOM
2300
CB
VAL
1334 
−44.155
−34.045
−11.723 
14.47
C


ATOM
2301
CG1
VAL
1334 
−44.851
−33.176
−12.744
12.5
C


ATOM
2302
CG2
VAL
1334 
−44.749
−33.899
−10.336 
13.35
C


ATOM
2303
C
VAL
1334 
−44.503
−36.562
−11.069
15.52
C


ATOM
2304
O
VAL
1334 
−43.676
−36.818 
−10.2
15.12
O


ATOM
2305
N
SER
1335 
−45.698
−37.161
−11.059
15.65
N


ATOM
2306
CA
SER
1335 
−45.927
−38.104 
−9.947
17.61
C


ATOM
2307
CB
SER
1335 
−47.396
−38.541 
−9.762 
19.13
C


ATOM
2308
OG
SER
1335
−48.28
−37.995
−10.714
21.27
O


ATOM
2309
C
SER
1335 
−45.104
−39.319 
−10.16 
16.26
C


ATOM
2310
O
SER
1335
−44.45
−39.844 
−9.265
15.18
O


ATOM
2311
N
ARG
1336 
−45.057
−39.739
−11.396 
16.43
N


ATOM
2312
CA
ARG
1336 
−44.326
−40.942
−11.638
19.04
C


ATOM
2313
CB
ARG
1336 
−44.461
−41.125
−13.056
23.11
C


ATOM
2314
CG
ARG
1336 
−44.507
−42.397
−13.484
26.63
C


ATOM
2315
CD
ARG
1336 
−45.813
−42.346
−14.321
29.99
C


ATOM
2316
NE
ARG
1336 
−45.664 
−41.73
−15.664
32.06
N


ATOM
2317
CZ
ARG
1336 
−45.635
−42.334
−16.856
31.45
C


ATOM
2318
NH1
ARG
1336 
−45.722
−43.613
−17.103
33.52
N


ATOM
2319
NH2
ARG
1336 
−45.423
−41.616 
−17.91
31.66
N


ATOM
2320
C
ARG
1336 
−42.905
−40.758
−11.309
20.68
C


ATOM
2321
O
ARG
1336 
−42.324
−41.569
−10.577
20.06
O


ATOM
2322
N
ILE
1337 
−42.301
−39.726
−11.874
19.97
N


ATOM
2323
CA
ILE
1337 
−40.913
−39.442
−11.613
19.1
C


ATOM
2324
CB
ILE
1337 
−40.414
−38.268
−12.509
19.3
C


ATOM
2325
CG2
ILE
1337 
−38.941
−37.989
−12.218
16.69
C


ATOM
2326
CG1
ILE
1337 
−40.561
−38.655
−13.993
18.86
C


ATOM
2327
CD
ILE
1337 
−40.445
−37.496
−14.979
19.36
C


ATOM
2328
C
ILE
1337 
−40.602
−39.176
−10.112 
18.87
C


ATOM
2329
O
ILE
1337 
−39.518
−39.543 
−9.663
18.78
O


ATOM
2330
N
SER
1338
−41.51
−38.572 
−9.332 
19.34
N


ATOM
2331
CA
SER
1338 
−41.229
−38.346 
−7.892 
20.11
C


ATOM
2332
CB
SER
1338 
−42.325
−37.541 
−7.183
20.76
C


ATOM
2333
OG
SER
1338
−42.75
−36.416 
−7.912 
24.23
O


ATOM
2334
C
SER
1338 
−41.226
−39.708 
−7.224
18.9
C


ATOM
2335
O
SER
1338 
−40.459
−39.975 
−6.294 
18.76
O


ATOM
2336
N
ALA
1339 
−42.151
−40.536 
−7.701
18.39
N


ATOM
2337
CA
ALA
1339 
−42.345
−41.896 
−7.23
18.01
C


ATOM
2338
CB
ALA
1339
−43.48
−42.548 
−8.012
17.08
C


ATOM
2339
C
ALA
1339 
−41.057
−42.677 
−7.427
19.89
C


ATOM
2340
O
ALA
1339 
−40.581
−43.341 
−6.509
22.03
O


ATOM
2341
N
ILE
1340 
−40.492
−42.583 
−8.63
20.82
N


ATOM
2342
CA
ILE
1340 
−39.253
−43.275 
−8.976
21.34
C


ATOM
2343
CB
ILE
1340 
−39.016
−43.206
−10.523
22.55
C


ATOM
2344
CG2
ILE
1340 
−37.663
−43.825
−10.888 
23.59
C


ATOM
2345
CG1
ILE
1340
−40.11
−43.985
−11.294
25.81
C


ATOM
2346
CD
ILE
1340 
−41.497
−44.205
−10.626
29.71
C


ATOM
2347
C
ILE
1340
−38.07
−42.658 
−8.21
21.59
C


ATOM
2348
O
ILE
1340 
−37.153
−43.365 
−7.79
18.89
O


ATOM
2349
N
PHE
1341 
−38.127
−41.339 
−8.007 
22.51
N


ATOM
2350
CA
PHE
1341 
−37.084
−40.571 
−7.312
23.12
C


ATOM
2351
CB
PHE
1341 
−37.366
−39.076 
−7.448
21.04
C


ATOM
2352
CG
PHE
1341 
−36.369
−38.216 
−6.741
18.35
C


ATOM
2353
CD1
PHE
1341 
−35.128
−37.965 
−7.31
17.9
C


ATOM
2354
CD2
PHE
1341 
−36.658
−37.671 
−5.494
18.97
C


ATOM
2355
CE1
PHE
1341 
−34.186
−37.181 
−6.652
18.18
C


ATOM
2356
CE2
PHE
1341 
−35.723
−36.886 
−4.825
18.68
C


ATOM
2357
CZ
PHE
1341 
−34.479 
−36.64 
−5.411
17.63
C


ATOM
2358
C
PHE
1341 
−36.941
−40.905 
−5.837
25.96
C


ATOM
2359
O
PHE
1341 
−35.867
−41.019 
−5.279 
24.76
O


ATOM
2360
N
SER
1342 
−38.107 
−41.03 
−5.204
28.8
N


ATOM
2361
CA
SER
1342 
−38.188
−41.346
−3.8
33.62
C


ATOM
2362
CB
SER
1342 
−39.589
−41.431 
−3.385
34.36
C


ATOM
2363
OG
SER
1342 
−39.895 
−40.25 
−2.726
37.13
O


ATOM
2364
C
SER
1342 
−37.681
−42.675 
−3.572
36.29
C


ATOM
2365
O
SER
1342 
−36.913
−42.931 
−2.739
36.94
O


ATOM
2366
N
THR
1343 
−38.255
−43.619 
−4.223
38.79
N


ATOM
2367
CA
THR
1343 
−38.007
−45.046 
−4.101 
42.78
C


ATOM
2368
CB
THR
1343 
−38.082 
−45.62 
−5.347
43.14
C


ATOM
2369
OG1
THR
1343 
−37.499
−44.974 
−6.327
45.03
O


ATOM
2370
CG2
THR
1343 
−39.089
−46.338 
−5.894 
42.28
C


ATOM
2371
C
THR
1343 
−36.447
−45.187 
−4.538
44.77
C


ATOM
2372
O
THR
1343 
−36.291
−46.076 
−5.408 
45.85
O


ATOM
2373
N
PHE
1344 
−35.516
−44.538 
−3.915
46.03
N


ATOM
2374
CA
PHE
1344 
−34.193
−44.422 
−4.598
47.65
C


ATOM
2375
CB
PHE
1344 
−34.478
−43.644 
−5.88
48.08
C


ATOM
2376
CG
PHE
1344
−33.55
−44.017 
−6.982
46.41
C


ATOM
2377
CD1
PHE
1344 
−34.002
−44.165 
−8.282
45.61
C


ATOM
2378
CD2
PHE
1344 
−32.205
−44.245 
−6.71
45.61
C


ATOM
2379
CE1
PHE
1344 
−33.134
−44.529 
−9.297
45.07
C


ATOM
2380
CE2
PHE
1344 
−31.332
−44.609 
−7.721
44.04
C


ATOM
2381
CZ
PHE
1344 
−31.798 
−44.75 
−9.016
44.55
C


ATOM
2382
C
PHE
1344 
−33.357
−43.599 
−3.602
49.92
C


ATOM
2383
O
PHE
1344 
−33.488
−42.376 
−3.477 
51.55
O


ATOM
2384
N
ILE
1345 
−32.396
−44.351 
−3.076
51.14
N


ATOM
2385
CA
ILE
1345 
−31.802
−43.901 
−1.816 
51.51
C


ATOM
2386
CB
ILE
1345 
−30.772
−44.991 
−1.309
51.18
C


ATOM
2387
CG2
ILE
1345 
−29.756
−44.342 
−0.398
49.1
C


ATOM
2388
CG1
ILE
1345 
−31.473
−46.176 
−0.598
51.89
C


ATOM
2389
CD
ILE
1345 
−32.276 
−45.84 
0.682
51.67
C


ATOM
2390
C
ILE
1345 
−31.323 
−42.476 
−1.708
52.76
C


ATOM
2391
O
ILE
1345 
−30.098 
−42.321 
−2.071
51.79
O


ATOM
2392
N
GLY
1346 
−32.172 
−41.554 
−1.404 
52.64
N


ATOM
2393
CA
GLY
1346 
−31.848 
−40.112 
−1.194
53.2
C


ATOM
2394
C
GLY
1346 
−30.478 
−40.01
−0.552
53.8
C


ATOM
2395
OT1
GLY
1346 
−30.041 
−41.005 
0.076
53.54
O


ATOM
2396
OXT
GLY
1346 
−29.834 
−38.946 
−0.669
53.44
O


TER
2397
GLY
346








HETATM
2398
C18
M97
1
−28.421 
−19.33 
−23.501
20.4
C


HETATM
2399
C17
M97
1
−28.05 
−18.355
−24.625 
22.33
C


HETATM
2400
C16
M97
1
−28.763 
−17.001
−24.516
20.81
C


HETATM
2401
C15
M97
1
−28.583 
−16.465
−23.104
21.33
C


HETATM
2402
C23
M97
1
−28.693 
−15.112
−22.776
21.71
C


HETATM
2403
C22
M97
1
−28.525 
−14.706
−21.456
23.83
C


HETATM
2404
C21
M97
1
−28.245 
−15.591
−20.427 
21.68
C


HETATM
2405
C20
M97
1
−28.13 
−16.961
−20.742
19.42
C


HETATM
2406
C19
M97
1
−28.303 
−17.326
−22.047
20.56
C


HETATM
2407
N3
M97
1
−28.175 
−18.712
−22.175 
21.67
N


HETATM
2408
C3
M97
1
−27.916 
−19.167
−20.955
17.66
C


HETATM
2409
C2
M97
1
−27.883 
−18.147
−20.082
18.09
C


HETATM
2410
C6
M97
1
−27.568 
−18.343
−18.599
16.61
C


HETATM
2411
C8
M97
1
−28.539
−17.7 
−17.605
18.67
C


HETATM
2412
O2
M97
1
−29.767 
−17.736
−17.726
19.12
O


HETATM
2413
N2
M97
1
−27.899 
−17.101
−16.607 
17.51
N


HETATM
2414
C7
M97
1
−26.579 
−17.132
−16.804
17.32
C


HETATM
2415
O1
M97
1
−25.745 
−16.754
−15.985
18.84
O


HETATM
2416
C1
M97
1
−26.241 
−17.726
−18.172
16.61
C


HETATM
2417
C4
M97
1
−25.08 
−18.719
−18.217
18.4
C


HETATM
2418
C10
M97
1
−24.374 
−18.961
−19.389
16.93
C


HETATM
2419
C11
M97
1
−24.497 
−18.49 
−20.685
19.11
C


HETATM
2420
C12
M97
1
−23.573 
−18.885
−21.641
19.55
C


HETATM
2421
C13
M97
1
−22.536 
−19.749
−21.281 
19.99
C


HETATM
2422
C14
M97
1
−22.425 
−20.218
−19.981
18.84
C


HETATM
2423
C9
M97
1
−23.349 
−19.826
−19.016
18.71
C


HETATM
2424
N1
M97
1
−23.479 
−20.067
−17.715
17.96
N


HETATM
2425
C5
M97
1
−24.523 
−19.402 
−17.22
18.43
C


HETATM
2426
O
HOH
1
−29.733 
−45.042
−32.394
23.71
O


HETATM
2427
O
HOH
11
−41.978 
−18.659 
−8.604
33.69
O


HETATM
2428
O
HOH
19
−14.344 
−9.842
−22.4
23.99
O


HETATM
2429
O
HOH
21
−43.049 
−29.657
−28.643
33.17
O


HETATM
2430
O
HOH
22
−27.163 
−0.128 
−19.346
37.35
O


HETATM
2431
O
HOH
23
−11.942 
−12.723
−13.277 
40.63
O


HETATM
2432
O
HOH
25
−33.037 
−32.588 
−8.01
24.8
O


HETATM
2433
O
HOH
26
−25.627 
−43.198 
−8.776
24.3
O


HETATM
2434
O
HOH
29
−46.913 
−39.523
−36.653
28
O


HETATM
2435
O
HOH
30
−30.849 
−12.281 
−30.69
21.24
O


HETATM
2436
O
HOH
31
−34.444 
−22.254
−29.224
14.19
O


HETATM
2437
O
HOH
33
−50.753 
−27.924
−27.093
26.45
O


HETATM
2438
O
HOH
34
−27.308 
−38.76
−4.252
35.8
O


HETATM
2439
O
HOH
38
−16.629 
−37.696
−14.044 
24.11
O


HETATM
2440
O
HOH
43
−37.896
−19.153
−11.112
20.78
O


HETATM
2441
O
HOH
45
−40.294
3.592 
−21.002
46.87
O


HETATM
2442
O
HOH
47
−19.865
−18.501
−9.486
42.76
O


HETATM
2443
O
HOH
49
−36.45
−37.969
−30.939
15.37
O


HETATM
2444
O
HOH
50
−29.817
−27.464
−2.853
38.04
O


HETATM
2445
O
HOH
51
−35.913
−29.539
−28.732 
15.99
O


HETATM
2446
O
HOH
55
−35.063
−49.437
−29.855
33.2
O


HETATM
2447
O
HOH
63
−17.108 
−3.162
−15.949 
31.66
O


HETATM
2448
O
HOH
65
−36.185
−14.548 
−12.6
24.69
O


HETATM
2449
O
HOH
66
−37.492
−51.897
−39.152
22.65
O


HETATM
2450
O
HOH
74
−21.385
−26.942
−16.186
40.62
O


HETATM
2451
O
HOH
77
−32.568
−48.216
−6.703
47.5
O


HETATM
2452
O
HOH
78
−40.231
−18.222
−13.28
21.62
O


HETATM
2453
O
HOH
80
−49.359
−48.928
−27.562
28.98
O


HETATM
2454
O
HOH
81
−50.28
−38.693
−33.409
34.22 
O


HETATM
2455
O
HOH
89
−48.667 
−5.949
−17.295 
35.77
O


HETATM
2456
O
HOH
90
−43.326 
−45.18
−33.961
31.65
O


HETATM
2457
O
HOH
93
−29.409
−47.043
−11.708 
31.44
O


HETATM
2458
O
HOH
95
−10.204 
−6.223
−17.26
18.06
O


HETATM
2459
O
HOH
96
−31.221 
−3.393
−19.944
22.32 
O


HETATM
2460
O
HOH
98
−36.257
−17.223
−13.142 
20.12
O


HETATM
2461
O
HOH
99
−33.234
−50.471
−24.546
20.45
O


HETATM
2462
O
HOH
107
−46.234 
−2.234
−15.955 
20.16
O


HETATM
2463
O
HOH
113
−27.073
−24.228
−30.542
26.4
O


HETATM
2464
O
HOH
119
−40.31 
−29.4 
−26.968 
12.91
O


HETATM
2465
O
HOH
122
−27.616
−41.457
−42.019
25.56 
O


HETATM
2466
O
HOH
123
−37.721
−50.822
−18.769 
37.76
O


HETATM
2467
O
HOH
128
−36.977
−26.973
−6.723
47.18 
O


HETATM
2468
O
HOH
132
−46.704
−25.042
−34.234 
25.99
O


HETATM
2469
O
HOH
135
−27.544
−24.241
−23.965 
30.92
O


HETATM
2470
O
HOH
140
−37.425
3.24 
−35.007
18.34 
O


HETATM
2471
O
HOH
143
−20.008
−12.815
−30.386 
40.51 
O


HETATM
2472
O
HOH
147
−14.407
−15.827
−13.914
30.48
O


HETATM
2473
O
HOH
151
−49.199
−31.854
−19.993 
33.45 
O


HETATM
2474
O
HOH
152
−33.758
−21.539
−26.003 
45.57
O


HETATM
2475
O
HOH
156
−21.439
−40.205
−36.699
50.64
O


HETATM
2476
O
HOH
160
−27.226
−43.392
−33.693
25.08 
O


HETATM
2477
O
HOH
164
−25.061
−26.966
−24.102 
22.64
O


HETATM
2478
O
HOH
167
−39.626 
−16.67
−10.802
34.02 
O


HETATM
2479
O
HOH
171
−19.142 
−1.168
−17.551
32.21 
O


HETATM
2480
O
HOH
172
−30.803 
−0.387
−20.702 
32.83 
O


HETATM
2481
O
HOH
176
−54.115
−25.794
−25.837 
53.46
O


HETATM
2482
O
HOH
181
−23.869
−36.686
−5.557
40.21
O


HETATM
2483
O
HOH
184
−29.269
−30.565
−24.802
22.28
O


HETATM
2484
O
HOH
189
−50.2 
−45.277
−19.345
38.58
O


HETATM
2485
O
HOH
191
−21.65
−29.789
−23.813
31.45
O


HETATM
2486
O
HOH
192
−23.062
−24.401
−6.237
35.26
O


HETATM
2487
O
HOH
194
−25.27
1.306 
−15.454
29.8
O


HETATM
2488
O
HOH
195
−28.159
−42.387
−7.202
22.48
O


HETATM
2489
O
HOH
199
−13.955
−14.842
−16.709
32.78
O


HETATM
2490
O
HOH
200
−36.82
−41.718 
0.531
50.12
O


HETATM
2491
O
HOH
201 
−28.644 
−20.12
−36.964 
18.87
O


HETATM
2492
O
HOH
203 
−50.477
−32.049
−17.177
24.64
O


HETATM
2493
O
HOH
216 
−39.142
−22.788
−29.507 
33.97
O


HETATM
2494
O
HOH
219
−47.47
−15.035
−20.201
35.71
O


HETATM
2495
O
HOH
224 
−46.506
−27.482
−23.402 
21.71
O


HETATM
2496
O
HOH
234 
−41.895
−31.848
−31.831
20.74
O


HETATM
2497
O
HOH
235 
−26.441
−19.233 
−9.527
33.45
O


HETATM
2498
O
HOH
239 
−37.357
−36.383
−42.714
31.76
O


HETATM
2499
O
HOH
240 
−31.471 
−4.986
0.652
22.91
O


HETATM
2500
O
HOH
243
−28.65
−42.512
−29.641 
22.84
O


HETATM
2501
O
HOH
244 
−36.603
−42.277
−29.106
19.94
O


HETATM
2502
O
HOH
248 
−29.027
−13.664
−10.124
31.23
O


HETATM
2503
O
HOH
249 
−40.094
−50.827
−15.065
43.7
O


HETATM
2504
O
HOH
251 
−23.436 
−42.81
−11.982
46.35
O


HETATM
2505
O
HOH
252 
−31.443
−12.916 
−9.468
43.08
O


HETATM
2506
O
HOH
253 
−45.124
−10.841
−28.548
57.83
O


HETATM
2507
O
HOH
256 
−47.989
−21.853
−27.175
28.06
O


HETATM
2508
O
HOH
257 
−44.346
−21.809
−29.799 
45.06
O


HETATM
2509
O
HOH
258 
−48.882
−41.587
−10.969
52.61
O


HETATM
2510
O
HOH
259 
−29.049
−34.816
−39.703
52.2
O


HETATM
2511
O
HOH
267 
−36.421
1.247 
−12.805
36
O


HETATM
2512
O
HOH
279 
−29.355
−45.223
−28.378
33.41
O


HETATM
2513
O
HOH
282 
−42.248
−20.932
−28.066 
29.16
O


HETATM
2514
O
HOH
283 
−33.773
−4.7
2.104
49.74
O


HETATM
2515
O
HOH
285 
−21.851
−38.325 
−6.435 
31.66
O


HETATM
2516
O
HOH
287
−26.26
−43.568
−28.371
25.76
O


HETATM
2517
O
HOH
291
−22.18
−11.552
−29.799
43.2
O


HETATM
2518
O
HOH
293 
−48.423
−37.306 
−38.97
42.54
O


HETATM
2519
O
HOH
298 
−24.451
−45.031
−29.768 
43.48
O


HETATM
2520
O
HOH
340 
−24.526 
−9.586 
−25.61
15.08
O


HETATM
2521
O
HOH
342 
−27.622
−21.226
−29.674 
29.04
O


HETATM
2522
O
HOH
348 
−40.859
−30.744
−29.704 
25.01
O


HETATM
2523
O
HOH
352 
−32.508
−49.493
−33.945
34.9
O


HETATM
2524
O
HOH
356 
−18.731
−15.159
−30.315 
33.75
O


HETATM
2525
O
HOH
358 
−34.046
−54.592
−37.088
20.7
O


HETATM
2526
O
HOH
360 
−31.208
−32.444
−33.609
20.04
O


HETATM
2527
O
HOH
363 
−30.618
−33.523 
−8.002
25.2
O


HETATM
2528
O
HOH
365 
−14.406
−16.156
−24.124
39.38
O


HETATM
2529
O
HOH
373 
−38.591
−25.485
−32.288
30.06
O


HETATM
2530
O
HOH
377 
−48.553 
−17.92
−12.222
37.86
O


HETATM
2531
O
HOH
380 
−36.774
−36.981
−33.348
22.77
O


HETATM
2532
O
HOH
381 
−24.808
−41.352
−28.041
28
O


HETATM
2533
O
HOH
388 
−24.856
−17.892 
−7.816
27.87
O


HETATM
2534
O
HOH
389 
−26.781
−11.754 
−6.859
37.48
O


HETATM
2535
O
HOH
390 
−26.698
−26.085
−28.658
43.43
O


HETATM
2536
O
HOH
396 
−39.993 
−0.244 
−8.176
44.09
O


HETATM
2537
O
HOH
399 
−22.572
−23.838
−19.334 
35.76
O


HETATM
2538
O
HOH
408 
−39.893
−27.132 
−7.517
28.65
O


HETATM
2539
O
HOH
410 
−51.294
−26.589
−30.152
36.54
O


HETATM
2540
O
HOH
416
−27.033 
−4.323
−31.352
40.18
O


HETATM
2541
O
HOH
418
−32.288
−20.615
−47.531
46.09 
O


HETATM
2542
O
HOH
420
−21.59
−20.992
−15.896
47.82
O


HETATM
2543
O
HOH
421
−33.255 
−1.487
−28.193 
15.19
O


HETATM
2544
O
HOH
422
−33.862
−14.639
−36.562 
39.85
O


HETATM
2545
O
HOH
423
−24.055
−22.398
−28.638
38.93
O


HETATM
2546
O
HOH
424
−23.254
−24.538
−37.285 
41.97 
O


HETATM
2547
O
HOH
425
−27.795 
−30.29
−26.912
29.38
O


HETATM
2548
O
HOH
426
−24.824
−29.707
−29.385
39.8
O


HETATM
2549
O
HOH
427
−42.553 
−46.3 
−15.041
21.97
O









The electronic representation of the c-Met structure was then displayed on a computer screen for visual inspection and analysis. All important motifs involved in c-Met ligand recognition and binding were identified, including those described above.
A three dimensional graphical representation of the c-Met binding pocket was then generated as part of an electronic representation of the ligand bound binding site. In an embodiment, the electronic representation of the binding pocket contains the coordinates of c-Met residues up to 6 Å from every atom of the ligand. This model contains twenty three amino acid residues (Table 4).
The structure coordinates of amino acid residues that constitute the binding pocket define the chemical environment of the ligand binding site, and thereby are useful in designing compounds that may interact with those residues.
The binding site amino acid residues are key residues for ligand binding. Alternatively, the binding site amino acid residues may be residues that are spatially related in the definition of the three-dimensional shape of the binding pocket. The amino acid residues may be contiguous or non-contiguous in the primary sequence.
The c-Met inhibition model is formed by three-dimensional coordinates of amino acid residues selected from the X-ray crystallographic structure of the complex of c-Met bound to the selective c-Met inhibitor as explained above. This model is mostly hydrophobic in nature. The only exception is c-Met hinge binding motif, which corresponds to the backbone amide of M1160 and the backbone carbonyl of P115.
Computer programs are also employed to estimate the attraction, repulsion, and steric hindrance of the ligand to the kinase inhibition model. Generally the tighter the fit between the inhibitor and c-Met at the molecular level and atomic level (e.g., the lower the steric hindrance, and/or the greater the attractive force), the more potent the potential drug will be because these properties are consistent with a tighter-binding constant.
To increase the likelihood of finding a suitable ligand, a set of seed molecules has been compiled. This set contains fragments that are modified to result in a molecule that tightly binds the model.
Alternatively, a potential ligand is obtained by screening a random chemical library. A ligand selected in this manner is then systematically modified by computer-modeling programs until one or more promising potential ligands are identified. Such analysis has been shown to be effective in the development of HIV protease inhibitors (Lam et al., Science 263:380-384 (1994); Wlodawer et al., Ann. Rev. Biochem. 62:543-585 (1993); Appelt, Perspectives in Drug Discovery and Design 1:23-48 (1993); Erickson, Perspectives in Drug Discovery and Design 1: 109-128 (1993). Such computer modeling allows the selection of a finite number of rational chemical modifications, as opposed to the countless number of essentially random chemical modifications that could be made, any of which any one might lead to a useful drug. Each chemical modification requires additional chemical steps, which while being reasonable for the synthesis of a finite number of compounds, quickly becomes overwhelming if all possible modifications needed to be synthesized. Thus, through the use of the structure coordinates disclosed herein and computer modeling, a large number of these compounds are rapidly screened on the computer monitor screen, and a few likely candidates are determined or identified without the laborious synthesis of untold numbers of compounds.
Once a potential ligand (agonist or antagonist) is identified, it is either selected from commercial libraries of compounds or synthesized de novo. As mentioned above, the de novo synthesis of one or even a relatively small group of specific compounds is reasonable in the art of drug design.
For all of the drug design strategies described herein further refinements to the structure of the drug are generally necessary and are made by the successive iterations of any and/or all of the steps provided by the aforementioned strategies.
Another aspect of the invention involves using the structure coordinates generated from the c-Met/inhibitor complex to generate a three-dimensional shape. This is achieved through the use of commercially available software that is capable of generating three-dimensional graphical representations of molecules or portions thereof from a set of structure coordinates.
The variations in coordinates discussed above may be generated because of mathematical manipulations of the c-Met/inhibitor complex structure coordinates. For example, the structure coordinates set forth in Table 1A or Table 1B could be manipulated by crystallographic permutations of the structure coordinates, fractionalization of the structure coordinates, integer additions or subtractions to sets of the structure coordinates, or combinations thereof.
Alternatively, modifications in the crystal structure due to mutations, additions, substitutions, and/or deletions of amino acids, or other changes in any of the components that make up the crystal also account for variations in structure coordinates. If such variations are within an acceptable standard error, as compared to the original coordinates, the resulting three-dimensional shape is considered to be the same. Thus, for example, a ligand that bound to the binding pocket of the c-Met kinase domain is also expected to bind to another binding pocket whose structure coordinates, when compared to those described, have a root mean square difference of equal to or less than about 1.5 Å, more preferably less than about 1.0 Å, and even more preferably, less than about 0.5 Å, from the backbone atoms.
Various computational analyses can be performed to analyze c-Met or other kinases or the kinase domains thereof. Such analyses may be carried out through the use of known software applications, such as ProMod, SWISS-MODEL (Swiss Institute of Bioinformatics), and the Molecular Similarity application of QUANTA (Accelrys, Inc., San Diego, Calif.). Programs, such as QUANTA permit comparisons between different structures, different conformations of the same structure, and different parts of the same structure. Comparison of structures using such computer software may involve the following steps: 1) loading the structures to be compared; 2) defining the atom equivalencies in the structures; 3) performing a fitting operation; and 4) analyzing the results. Each structure is identified by a name. One structure is identified as the target (i.e., the fixed structure) and all remaining structures are working structures (i.e., moving structures). Since atom equivalency with QUANTA is defined by user input, for the purpose of this invention, applicants define equivalent atoms as protein backbone atoms (N, Cα, C, and O) for all conserved residues between the two structures being compared. Only rigid fitting operations are also considered. When a rigid fitting method is used, the working structure is translated and rotated to obtain an optimum fit with the target structure. The fitting operation uses an algorithm that computes the optimum translation and rotation to be applied to the moving structure, such that the root mean square difference of the fit over the specified pairs of equivalent atoms is an absolute minimum. This number, given in angstroms (Å), is reported by software applications, such as QUANTA.
For the purpose of this invention, any c-Met molecule or molecular complex or kinase domain thereof that has a root mean square deviation of conserved residue backbone atoms (N, Cα, C, O) of less than about 1.5 Å, more preferably less than about 1.0 Å, and even more preferably less than about 0.5 Å, when superimposed on the relevant backbone atoms described by structure coordinates listed in Table 1A or Table 1B are considered equivalent.
The term “root mean square deviation” means the square root of the arithmetic mean of the squares of the deviations from the mean. It is a way to express the deviation or variation from a trend or object. For purposes of this invention, the “root mean square deviation” defines the variation in the backbone of a protein from the backbone of the c-Met or other kinases of the invention or the kinase domain portion thereof, as defined by the structure coordinates described herein.
3. Use of the C-Met Inhibition Model to Derive an Inhibition Model for Another Kinase
The c-Met inhibition model can be modified to construct a model for the inhibition of another kinase. This method is known as homology modeling. The model for the new kinase can be generated by replacing electronic representations of particular residues of the c-Met inhibition model with electronic representations of corresponding residues of the new kinase.
The new kinase is a kinase with a difference of at least one amino acid residue from the wild-type human c-Met. The another kinase can be a mutant c-Met protein, a paralog of c-Met protein, a family member or a related sequence (homologous) of c-Met, a kinase with at least 10% amino acid sequence identity or homology to c-Met, or a kinase with at least 30% nucleotide or amino acid sequence similarity to wild type c-Met.
There are several applications for this methodology.
3.1. Methodology to Derive an Inhibition Model for Another Kinase from the c-Met Inhibition Model
Typically, construction of such an inhibition model involves: performing sequence alignment between the amino acid sequence of other kinase against the amino acid sequence of c-Met, identifying conserved amino acid residues between c-Met and the kinase of interest, generating atomic coordinates of all conserved amino acids in the other kinase from the electronic representation of c-Met residues; generating conformations for the structurally variable residues in the other kinase; replacing the non-conserved residues of c-Met with residues from the other kinase structure; building side chain conformations; and refining and/or evaluating the structure.
This method is known as homology modeling. The method is accomplished using commercially available software. Non-limiting examples of such programs are MOE (CCG, Montreal, Canada), ICM (Molsoft, La Jolla, Calif.), and Insight II/Discover (Accelrys, Inc., San Diego, Calif.).
The success of homology models depends on the sequence alignment. Four motifs were selected to guide such an alignment: P-loop, salt-bridge, DFG-motif and the A-loop.
The geometry of the residues forming the kinase hinge is very important and differs from one kinase to the other. The hinge also assumes different conformations depending on the bound ligand. To optimize the shape and geometry of the model's binding pocket, fragments from known inhibitors were used. Those fragments were modified by attaching atomic groups suitable to complement the pocket.
Once the inhibition model is built, a three dimensional graphical representation of the binding pockets of c-Met paralogs, significant c-Met homologs, and/or other kinases is generated. The new kinase inhibition model is defined as an electronic representation of residues corresponding to the c-Met inhibition model.
The resulting pair-wise comparison of binding pocket residues provides a basis for evaluating similarities and differences in polarity and hydrophobicity, and therefore differences in the chemical environment, of the binding pockets of various kinases by using the inhibition model. This inhibitor model is important for drug design, e.g. designing inhibitors of c-Met paralogs, significant c-Met homologs, and/or other kinases. The kinase, for which an inhibitor is designed using the inhibitor model, can be any known kinase.
3.2. Similarity Assessment Method for Comparing Inhibition Models Derived for a Series of New Kinase Proteins.
To assess the similarity of inhibition models, a weighting system is applied. In one embodiment of the invention, residues are assigned the following weights:
2 critical for ligand binding residues
1 residue side chain lining the inhibition model
0.5 backbone atoms part of the inhibition model

    
    
        additions, deletions and changes in backbone flexibility, lack of residue
    
    


−1 alignment

    
    
        dramatic changes in size and/or polarity inside the inhibition model, lack of
    
    


−2 alignment of critical residues
The following illustrative examples demonstrate that the highest similarity assessment value of 25 is obtained when the system is applied to the c-Met protein. All other proteins are expected to score below the maximum of 25.







TABLE 2





(SEQ ID NOs. 11, 3, 4, 5, 6, 7, 8, and 9, respectively)
























C-MET

AXL

FLT-3

cKIT



PROTEIN
(SEQ ID NO: 11)
weight
(SEQ ID NO: 3)
weight
(SEQ ID NO: 4)
weight
(SEQ ID NO: 5)
weight






I_1084
2
L_542
1
L_616
1
L_595
1



G_1085
2
G_543
2
G_617
2
G_596
2



F_1089
2
F_547
2
F_621
2
F_600
2



V_1092
2
V_550
2
V_624
2
V_603
2



A_1108
1
A_565
1
A_642 
1
A_621
1



V_1109b
0.5
V_566
0.5
V_643
0.5
V_1109
0.5



K_1110b
0.5
K_567
0.5
K_644
0.5
K_623
0.5



L_1140
1
M_598
0.5
V_675
0.5
V_654
0.5



V_1155
1
V_618
1
L_689
0.5
I_669
0.5



L_1157
1
L_620
1
F_691
0.5
T_670
−2



P_1158
1
P_621
1
E_692
−1
E_671
−1



Y_1159b
0.5
F_622
0.5
Y_693
0.5
Y_672
0.5



M_1160
1
M_623
1
C_694
0.5
C_673
0.5



K_1161b
0.5
K_624
0.5
C_695
0.5
C_674
0.5



H_1162b
0.5
H_625
0.5
Y_696
0.5
Y_675
0.5



G_1163
0.5
G_626
0.5
G_697
0.5
G_676
0.5



D_1164
1
D_627
1
D_698
1
D_677
1



M_1211
1
M_679
1
L_818
0.5
L_799
0.5



A_1221
1
A_689
1
C_828
0.5
C_809
0.5



D_1222
1
D_690
1
D_629
1
D_810
1



F_1223
1
F_691
1
F_630
1
F_811
1



A_1226
1
S_694
−1
A_833
1
A_814
1



R_1227
2
K_695
1
R_834
2
R_815
2


Similarity assessment

25

20.5

19

17


value














IRK

cFMS

cABL

PIM1



PROTEIN
(SEQ ID NO: 6)
weight
(SEQ ID NO: 7)
weight
(SEQ ID NO: 8)
weight
(SEQ ID NO: 9)
weight






L_1002
1
L_588
1
L_266
1
L_44
1



G_1003
1
G_589
2
G_267
2
G_45
2



F_1007
2
F_593
2
Y_271
1
F_49
2



V_1010
2
V-596
2
V_274
2
V_52
2



A_1028
1
A_614
1
A_287
1
A_65
1



V_1029
0.5
V_615
0.5
V_288
0.5
I_66
0.5



K_1030
0.5
K_616
0.5
K_289
0.5
K_67
0.5



V_1060
0.5
V_647
0.5
V_317
0.5
V_103
1



V_1075
1
V_661
1
I_331
0.5
L_118
1



M_1076
0.5
T_663
−2
T_333
−2
L_120
1



E_1077
−1
E_664
−1
E_334
−1
E_121
−1



L_1078
0.5
Y_665
0.5
F_335
0.5
R_122
0.5



M_1079
1
C_666
0.5
M_336
1
P_123
−1









E_124
−1



A_1080
0.5
C_667
0.5
T_337
0.5
P_125
−1



H_1081
0.5
Y_668
0.5
Y_338
0.5
V_126
0.5



G_1082
0.5
G_669
0.5
G_339
0.5
Q_127
−1



D_1083
1
D_670
1
N_340
−2
D_128
1



M_1139
1
L_785
0.5
L_388
0.5
L_174
0.5



G_1149
−1
G_795
−1
A_398
1
I_185
1



D_1150
1
D_796
1
D_399
1
D_186
1



F_1151
1
F_797
1
F_400
1
F_187
1



T_1154
−1
A_800
1
S_403
−1
A_191
1



R_1155
2
R_801
2
R_404
2
L_192
−2


Similarity assessment

16

15.5

11.5

11.5


value

















Residues which constitute a unique hydrophobic interaction critical for binding c-Met to the selective c-Met inhibitor are allocated a maximum weight of 2. Those residues include 11084, G1085, F1089, V1092 and R1227.
Conserved residue substitutions, are assigned half of this maximum value (1) to take into account size changes. Residues such as alanine, valine, leucine and isoleucine are exchanged by conserved substitutions. Similarly, the following residue pairs constitute conservative substitutions: serine and threonine, asparagine and glutamic acid, phenylalanine and tyrosine, and asparagine and glutamine.
When residues contribute only their backbone atoms to the creation of the inhibition model a weight of 0.5 is assigned.
Two penalty levels have been assigned (one severe (−2), one moderate (−1)) to residues which are considered to contribute negatively to the similarity assessment relative to c-Met.
Determination of the similarity assessment provides a critical analysis of the target inhibition model for a kinase relative to the one described in this application for the selective c-Met inhibitor and c-Met.
The results of the similarity assessments indicate the expected selectivity of novel ligands identified with the inhibition model. In one embodiment of the invention, similarity assessment values above 90% of that of the selective c-Met inhibitor and c-Met (25) indicate the lowest level of compound selectivity; similarity assessment values between 90% and 50% are expected at the next level; and similarity assessment values below 50% indicate the highest level of selectivity.
These similarity assessments of various inhibition models are also critical in order to identify regions within the inhibition models that can be employed to ensure adequate complementarity between the inhibition model and ligand to overcome these differences, and therefore, lead to increased likelihood of success in the electronic screening or design process.
For instance, in the design process, the presence of a polar residue in place of a hydrophobic one may significantly alter the inhibitor's chemical environment. Modifications of the inhibitor to include a polar complementary atomic group within the inhibitory model will provide maximum electrostatic interactions with the inhibition model.
4. Use of the Inhibition Model for Ligand Screening (Enrichment), Fitting and Selection
The kinase inhibition model is used for ligand screening (enrichment), fitting, and selection.
The electronic representation of compounds and/or fragments is generated as described above. In one embodiment of the invention, electronic representations of compounds and/or fragments are assembled into electronic databases. In another embodiment of the invention, these databases include chemical entities' coordinates in any SMILES, mol, sdf, or mo12 formats.
Selected chemical entities or fragments may be positioned in a variety of orientations inside the inhibition model. Chemical entities come from different sources including, but not limited to, proprietary compound repositories, commercial data bases, or virtual data bases. Non-limiting exemplary sources of fragments include reagent data bases, de-novo design, etc.
The selected chemical entities or fragments are used to perform a fitting of the electronic representation of compounds and/or fragments and the inhibition model. The fitting is done manually or is computer assisted (docking). In one embodiment, docking programs used in the present invention are ICM (Molsoft, La Jolla, Calif.), FelxiDock (Tripos, St. Louis, Mo.), GRAM (Medical Univ. Of South Carolina), DOCK3.5 and 4.0 (Univ. Calif. San Francisco), Glide (Schrödinger, Portland, Oreg.), Gold (Cambridge Crystallographic Data Centre, UK), FLEX-X (Bi-oSolvelT GmbH, Germany); or AUTODOCK (Scripps Research Institute).
The results of the fitting operation are then analyzed to quantify the association between the chemical entity and the binding pocket. The quality of fitting of these entities to the inhibition model is evaluated either by using a scoring function, shape complementarity, or estimating the interaction energy.
Methods for evaluating the association of a chemical entity with the target include energy minimization and molecular dynamics with standard molecular mechanics force fields, such as CHARMM and AMBER.
Additional data is obtained using Free Energy Perturbations (FEP), to account for other energetic effects such as desolvation penalties. Information about the chemical interactions with the target are then used to elucidate chemical modifications that can enhance selectivity of binding of the compound
Potential binding compounds are identified based on favorable geometric fit and energetically favorable complementary interactions. Energetically favorable electrostatic interactions include attractive charge-charge, dipole-dipole and charge-dipole interactions between the target enzyme, and the small molecule.
The association with the binding pocket is further assessed by means of visual inspection followed by energy minimization and molecular dynamics. Examples of such programs include: MOE (CCG, Montreal, Canada), QUANTA/CHARMM (Accelrys, Inc., San Diego, Calif.); Gaussian (M. J. Frisch, Gaussian, Inc., Carnegie, Pa.); AMBER (P. A. Kollman, University of California at San Francisco); Jaguar (Schrödinger, Portland, Oreg.); SPARTAN (Wavefunction, Inc., Irvine, Calif.); Impact (Schrödinger, Portland, Oreg.); Insight II/Discover (Accelrys, Inc., San Diego, Calif.); MacroModel (Schrödinger, Portland, Oreg.); Maestro (Schrödinger, Portland, Oreg.); and DelPhi (Accelrys, Inc., San Diego, Calif.).
Once suitable fragments have been identified, they are connected into a single compound or complex on the three-dimensional image displayed on a computer screen in relation to all or a portion of the inhibition model.
5. Use of the Inhibition Model for Ligand Design
The design of compounds using the inhibition model includes calculation of non-covalent molecular interactions important in the compound's binding association including hydrogen bonding, van der Waals interactions, hydrophobic interactions and electrostatic interactions.
The compound's binding affinity to the inhibition model is further optimized by computational evaluation of the deformation energy of binding, i.e. the energy difference between bound and free states of the chemical entity.
Computer calculations may suggest more than one conformation similar in overall binding energy for a chemical entity. In these cases the deformation energy of binding is defined as the difference between the energy of the free entity and the average energy of the conformations observed when the inhibitor binds to the protein.
EXAMPLES
Examples are provided below to further illustrate different features of the present invention. The examples also illustrate useful methodology for practicing the invention. These examples do not limit the claimed invention.
Material and Methods
Expression and Purification of the cMet1 Kinase Domain
cDNA of full-length cMet purchased from Origen Technologies was used as template for PCR amplification. The DNA fragment encoding the kinase domain (1038-1346) was inserted into a Novagen vector pet28a between Nco1 and Sal1 sites. The primers were designed to contain a six-histidine tag to the N-terminus. In order to express dephosphorylated cMet kinase protein, a tyrosine phosphatase PTP1B (1-283) was sequentially ligated into the construct between SalI and NotI sites. A second ribosome binding site was incorporated in the PTP1B primer after the SalI site.
c-Met1 Protein Expression
The N-terminal His-tagged proteins were expressed in Circlegrow broth (Q-Biogen). The transformed E. Coli cell line BL21(DE3)RIL (Stratagene) was cultured to OD=0.8 at 37° C. and induced with 0.3 mM of IPTG for overnight at 12° C. The co-expressed protein was purified by metal-chelation chromatography followed by anion and cation columns. In a typical preparation 4 liters of cells were lysed by sonication in 140 ml buffer containing 20 mM MOPS pH 6.5, 200 mM NaCl, 7.5% glycerol, 0.1% Igepal, supplied with 1 mM PMSF. The supernatant was obtained by centrifugation at 50,000 g for 30 minutes and followed by incubation with 8 mL of Ni-NTA His Bind resin (Novagen) at 4° C. for one hour. A second step 50 ml wash buffer (with 100 mM NaCl and 5 mM imidazole) was applied after initial wash with the lysis buffer. Protein was eluted by 200 mM imidazole pH8.5, 100 mM NaCl and 7.5% glycerol and directly cleared by passing 10 ml QFF column. The salt concentration and the pH value of the protein flow through were adjusted to 50 mM and 7.5 by dilution, and then loaded to 1 ml SP FF column. The protein was further gel-filtered in an equilibrium buffer of 20 mM TrisHCl pH8.5, 150 mM NaCl, 7.5% glycerol and 2 mM DTT. The monomeric cMet protein was concentrated to 30 mg/ml for storage at −80° C.
c-Met1 Protein purification was performed as follows:
BL21(DE3)RIL cells were chilled on ice before being induced at 12° C. overnight at a density of OD600=1.
4-6 L cell pellets were then resuspended in 150 ml of 50 mM K2HPO4 pH 8.0, 200 mM NaCl, 7% Glycerol, 0.1% Igepal.=buffer A, +1.5 mM PMSF.
Cell suspensions were subsequently sonicated at 60% for 10 min, in cycles of 5 s on and 8 s off, and kept in ice.
Sonicated suspensions were centrifuged at 50,000×g for 30 min at 4° C. The resulting supernatants were transferred to 8 ml fresh nickle beads. This solution was rotated for 40 min at 4° C.
Supernatant liquid was allowed to drain off.
The nickel beads (which bound cMet1 protein) were resuspended twice with 50 ml of buffer A.
Nickel beads were then resuspended twice with 25 ml 50 mM K2HPO4, 100 mM NaCl, 7.5% Glycerol, 10 mM Imidazole (pH 8.5).
cMet1 protein was eluted from the nickel beads with 30 ml 200 mM Imidazole (pH8.5), 100 mM NaCl, 7.5% Glycerol.
The eluted flow-through directly drains to 10 ml QFF (in 100 mM NaCl).
(a) The first 2 ml of the flow through is not collected, but sent to waste.
(b) All remaining fractions are collected and concentrated down to  ̃500 ul for Gelfiltration in 20 mM TrisHCl pH 8.5, 150 mM NaCl, 7.5% Glycerol, 1 mM DTT. Peak elutes around 16 ml from a 24 ml superdex 200.
c-Met1 Crystallization, Data Collection and Structure Determination
The c-Met protein was diluted to 10 mg/ml by a buffer of 20 mM TrisHCl 8.5, 100 mM NC1 and 5% glycerol. The selective c-Met inhibitor was added to 1 mM from a 10 mM (50% DMSO) stock solution. 20 mM Li2SO4 was also included in the protein solution. Thin needle crystals were obtained at 4° C. by hanging drop methodology using 15% ethanol, 12% ethylene glycol, 100 mM imidazole pH8.5 as precipitant. Typically, 250 nL protein solution was mixed with an equal volume of reservoir solution and streak-seeding method was employed to reduce the crystal nucleus. The crystals were harvested after adding ethylene glycol to 30%. The triclinic crystal has unit cell dimension of a=53.22 Å, b=57.97 Å, c=64.93 Å, α=88.11°, β, 67.97°, γ=85.58°. There are two copies of c-Met polypeptide chain per asymmetric unit and the solvent content is 45%.
Diffraction images were collected at Cornell High Energy Synchrotron Source beamline A1 at 100 K with CCD detector. Raw data were reduced with DENZO and scaled and merged by using SCALEPACK on CHESS site. The complex structure was solved by molecular replacement using the program MOLREP implemented in CCP4. The Initial mode was ligand free c-Met kinase crystal structure (PDB code 2G15) from 1060-1346, excluding 1222-1239 (activation loop). With data up to 3 Å, a unique solution was found with correlation coefficient 0.34 versus 0.19 for the next highest peak. Structure refinement consisted of iterative cycles of modeling building in Coot, following by simulated annealing, minimization, and restrained B-factor refinement in CNX. The N-terminal and the A-loop amino acids were revealed during the refinement and built back to the electron density with different conformation from the initial model. Water molecules were added based on Fo-Fc maps (3σ) with density recapitulated in 2Fo-Fc maps (1σ). All waters satisfy the hydrogen-bonding criteria as implemented in the CNX programs Waterpick and Waterdelete. Non-crystallographic symmetry was not employed for the refinement though the two subunits are almost identical. In both subunits, the inhibitor conformation was unambiguously defined in the electron density and included for the refinement at late stage. Final rounds of improvement were performed in REFAC5 with TLS protocols to 2 Å and no σ cutoff. The finished model has continuous electron density from 1047 to 1346 but missing 1038-1046, and also contains 500 water molecules with a crystallographic R-value of 20.9% (Rfree=25.3%). The x-ray data and refinement statistics are summarized in Table 3.







TABLE 3







Data collection










Space group
P1



Cell dimensions a, b, c (Å)
53.22, 57.97, 64.93



Cell angles α, β, γ (deg)
88.11, 67.97, 85.58



Resolution (Å)
30.0-2.0



Unique reflections
38978



Completeness (2.07-2.00 Å)
84.8% (51.4%)



Rsym (2.07-2.00 Å)
11.0% (26%)



Mean I/σ(I)
6.9



Redundancy
1.8







Refinement










Intensity cutoff
0.0



Rcryst a
22.3%



Rfree a
24.6%



rmsd in bond length (Å)
0.009



rmsd in bond angle (°)
1.77



Average B factor (Å2)
23.00







a Rcrys and Rfree = (Σ|Fobs−Fcalc|)/(Σ|Fobs|). Rfree was calculated over a randomly selected 5% of the reflections not used in refinement. Parentheses indicate the outer resolution shell.






Example 1
The Structure of the c-Met1/Inhibitor Complex
The unphosphorylated c-Met kinase domain bound to the selective c-Met inhibitor follows the bi-lobal architecture with N-terminal domain mainly β-sheet connected through a hinge segment to the mainly α-helical C-terminal lobe. All of the residues of the kinase domain are well defined in the structure, including those from the activation loop and the nucleotide binding loop (P-loop). Residues of those loops have an average B-values less than 35 Å.
The selective c-Met inhibitor binds the interdomain cleft between the N- and G-lobes. The carbonyl group from the succinamide ring forms hydrogen bond with the backbone amide of M1160 and the N—H group forms hydrogen bonds with the backbone carbonyl of P1158. The indole ring is close to the ATP binding site opening while the tricyclic ring is bound deep inside the hydrophobic pocket. While the selective c-Met inhibitor binding mode is similar to the binding of many ATP competitive inhibitors, the kinase domain of c-Met bound to the selective c-Met inhibitor assumes an inactive conformation resembling that found in some receptor tyrosine kinases.
The activation loop is in the canonical, autoinhibitory conformation with a short anti-parallel strand observed in many inactive RTKs present in the structure. Two tyrosine residues Y1234 and Y1235 located in the A-loop of the kinase domain are responsible for c-Met catalytic activity. While Y1234 is exposed, Y1235 is sequestered into the active site occupying the site of the substrate tyrosine (FIG. 1). FIG. 1 shows the activation loop of the unphosphorylated c-Met bound to selective inhibitor AQ197 is shown in dark gray. The peptide substrate, as seen in the structure of the phosphorylated insulin receptor IRK in complex with ATP and a peptide (PDB entry 1IR3), is shown in lighter grey. FIG. 1 was generated by superimposing the catalytic segments of those two kinases. Similar orientation has been found for Y1162 in the inactive IRK (1IRK), Y842 of FLT3 (1RJB), Y823 in c-Kit (1T45), Y412 of c-Abl (2HYY) as well as Y823 of c-Kit (1T46) bound to Gleevec, and Y809 of cFMS bound to arylamides (2IOY) and quinolone (2IOV) series of inhibitors.
Y1235 of unphosphorylated c-Met bound to the selective c-Met inhibitor is held by a hydrogen bond network formed by catalytic loop (C-loop) N1204 and R1208, strictly conserved residues across the type III RTKs. Their hydrogen bond interactions correlate well with observed substrate preferences in active RTKs like IRK and c-Kit, where the corresponding Asp residue interacts with the attacking hydroxyl side chain of the substrate, while the arginine residue engages in hydrogen bonding interactions that orient asparagine (FIG. 2). FIG. 2 is a cartoon image of c-Met kinase domain. The activation loop is in the canonical, autoinhibitory conformation forming a typical short anti-parallel strand. This particular conformation has been observed in other inactive RTKs. While Y1235 is mimicking the substrate tyrosine residue Y1234 is exposed. Residues shown in sticks are labeled. Y1235 of c-Met bound to the selective c-Met inhibitor is sequestered by the hydrogen bond network formed by N1204 and R1208. These two residues are part of the catalytic loop (C-loop) and strictly conserved across the type III RTKs. The aromatic side chain of F1089 (sticks) stabilize the downfold of the loop by van de Waals contacts with the selective c-Met inhibitor. Similar specific conformations induced by small molecule fitting are present in the crystal structures of Abl bound to Gleevec and FGFR-1 bound to SU-5402 (PDB entry 1FGK). In the structure of the selective c-Met inhibitor bound to c-Met the conformation of the A-loop dramatically differs from those reported previously for the c-Met receptor kinase domain (Wang, W. et al. 2006. Proc. Natl. Acad. Sci. USA 103:3563-3568 (2006); Schiering, N. et al. 2003. Proc. Natl. Acad. Sci. USA 100:112654-12659). The wild type apo-c-Met reported by Wang et al. shows the activation loop in an open conformation, unsuitable for substrate binding, but does not block the ATP binding site. Y1234 is pulled closer to the N-terminal domain, making hydrogen bonds with E1127 an important catalytic residue as we explained above. The structure of mutant c-Met resolved by Schiering et al. was obtained from baculovirus cultures where the Y1194, Y1234 and Y1235 were mutated to prevent their phosphorylation during production. In this case the activation loop resembles the activated conformation.
Two different conformations of the DFG motif are known. In the activated kinases the DFG motif is in so-called ‘DFG-in’ conformation. This conformation permits Mg2+ ion ligation by asparagine residue and phenylalanine makes room for the ATP tucking itself away under the αC helix. In this case the kinase has the ability to bind the ATP productively. In the ‘DFG-out’ conformation which is exhibited by our structure the aspartic acid and the phenylalanine switched sides, with aspartic acid point away from where the ATP would bind and phenylalanine is situated in the approximated position of the ATP adenine moiety. Stabilization of this portion of the A-loop is provided in part by the tricyclic group of the selective c-Met inhibitor, which is making van der Waals interactions with phenylalanine residue from the DFG motif. This is why, although the hydroxyl group of the Y1235 is in position for phosphor-transfer, the DFG-out motif occludes the ATP binding site interfering with a possibility of cis-transfer.
The nucleotide binding loop, the P-loop is well ordered in the structure of c-Met bound to the selective c-Met inhibitor, where residues 11084 to G1087 form part of the β1 strand. In contrast, in the publicly available unbound c-Met these four residues are disordered. F1089 stabilizes the downfold of the loop by van de Waals contacts with the selective c-Met inhibitor (FIG. 2). Crystal structures of Abl and FGFR complexed with inhibitors STI-571 (2HYY) and SU-5402 (1FGI), respectively, adopt similar conformations induced by inhibitor fitting.
While there are common features shared by Gleevec bound to c-Abl and c-Met bound to the selective c-Met inhibitor, there is an important difference in the alignment of the lysine-glutamic acid pair. In phosphorylated kinases corresponding glutamic acid residue stabilizes the orientation of lysine residue after kinase activation. When Gleevec binds c-Abl the salt bridge is well preserved and forms part of the hydrogen bond network with the inhibitor. When the selective c-Met inhibitor binds c-Met, the ion pair is disrupted, residues K1110 and E1127 are 16 Å apart, accentuating the inactive nature of the c-Met kinase conformation in the presence of the selective c-Met inhibitor With respect to FIG. 4, strictly conserved Lys (β3) and Glu (αC) in active kinases form an ion pair necessary for stabilizing the phosphate group transfer. Unphosphorylated c-Met bound to AQ197 shows this salt bridge disrupted as a result of the conformational changes of the A-loop and the helix αC (magenta). In yellow, the αC structure of the active form of insuline receptor kinase. Catalytic important Glutamic acid residues are shown in sticks.
A similar situation to c-Abl is present in c-Kit bound to Gleevec, lysine-glutamic acid maintain salt bridge distance. c-Kit structure is remarkable in another way. The unphosphorylated apo-structure appears very similar to the structure in complex with Gleevec. This fact may confirm the overall belief that Gleevec recognizes and binds the canonical, autoinhibited kinase conformation.
Another receptor kinase cFMS bound to small molecule inhibitors is also in the canonical inactive conformation (Schubert, C. et al. 2007. J. Biol. Chem. 282:4094-4101). These inhibitors resemble the binding mode of Gleevec, but being small they do not reach the back pocket.
It is reasonable to suggest based on this description of the binding mode of the selective c-Met inhibitor bound to the non-phosphorylated form of c-Met, that the selective c-Met inhibitor binds a pre-existing pocket formed in the unphosphorylated c-Met, with the tricyclic moiety fitting perfectly between two phenylalanine residues F1089 from the P-loop and F1223 from the DFG motif. Both residues have their aromatic rings in van der Waals, hydrophobic contact with the selective c-Met inhibitor.
Example 1A
The Construction of the c-Met2 Inhibition Model
The three dimensional electronic representation of the ligand bound to c-Met was used. Twenty three residues of c-Met at distances up to 6 Å from every atom of the ligand were selected. The coordinates of these twenty three residues constitute the inhibition model of c-Met.
The amino acids of the inhibition model of c-Met derived from the structure of c-Met2 kinase domain are described herein and are defined by a set of structure coordinates set forth in Table 4.







TABLE 4





(SEQ ID NO: 11)
























ATOM
1
N
ILE
1084
−19.676
−14.451
−19.716
15.47
N


ATOM
2
CA
ILE
1084
−20.082
−15.696
−19.067
15.31
C


ATOM
3
CB
ILE
1084
−21.542
−15.681
−18.586
14.71
C


ATOM
4
CG1
ILE
1084
−21.729
−14.619
−17.505
14.37
C


ATOM
5
CD1
ILE
1084
−23.127
−14.461
−17.033
6.51
C


ATOM
6
CG2
ILE
1084
−21.928
−17.056
−18.067
14.52
C


ATOM
7
C
ILE
1084
−19.802
−16.886
−19.998
14.64
C


ATOM
8
O
ILE
1084
−19.178
−17.865
−19.589
14.54
O


ATOM
9
N
GLY
1085
−20.235
−16.777
−21.247
14.55
N


ATOM
10
CA
GLY
1085
−19.946
−17.782
−22.243
13.94
C


ATOM
11
C
GLY
1085
−20.087
−17.158
−23.592
14.69
C


ATOM
12
O
GLY
1085
−20.694
−16.104
−23.725
13.22
O


ATOM
13
N
PHE
1089
−24.836
−18.883
−30.097
15.3
N


ATOM
14
CA
PHE
1089
−25.9
−18.001
−29.571
13.53
C


ATOM
15
CB
PHE
1089
−26.393
−18.453
−28.156
12.25
C


ATOM
16
CG
PHE
1089
−25.281
−18.681
−27.155
12.52
C


ATOM
17
CD1
PHE
1089
−24.789
−19.972
−26.93
10.55
C


ATOM
18
CE1
PHE
1089
−23.728
−20.182
−26.026
10.53
C


ATOM
19
CZ
PHE
1089
−23.173
−19.124
−25.36
10.12
C


ATOM
20
CE2
PHE
1089
−23.625
−17.83
−25.583
9.89
C


ATOM
21
CD2
PHE
1089
−24.694
−17.613
−26.476
12.9
C


ATOM
22
C
PHE
1089
−25.449
−16.545
−29.503
13.39
C


ATOM
23
O
PHE
1089
−26.284
−15.658
−29.406
14.08
O


ATOM
24
N
VAL
1092
−22.639
−13.849
−23.919
12.22
N


ATOM
25
CA
VAL
1092
−23.38
−13.53
−22.701
10.83
C


ATOM
26
CB
VAL
1092
−24.097
−14.78
−22.141
10.23
C


ATOM
27
CG1
VAL
1092
−24.877
−14.441
−20.91
8.74
C


ATOM
28
CG2
VAL
1092
−24.998
−15.332
−23.184
11.17
C


ATOM
29
C
VAL
1092
−22.393
−12.944
−21.691
10.92
C


ATOM
30
O
VAL
1092
−21.402
−13.605
−21.364
9.96
O


ATOM
31
N
ALA
1108
−26.911
−12.095
−15.851
8.12
N


ATOM
32
CA
ALA
1108
−26.39
−12.461
−17.121
8.23
C


ATOM
33
CB
ALA
1108
−26.701
−13.958
−17.42
7.36
C


ATOM
34
C
ALA
1108
−27.054
−11.581
−18.146
7.48
C


ATOM
35
O
ALA
1108
−28.294
−11.377
−18.103
6.23
O


ATOM
36
N
VAL
1109
−26.262
−11.022
−19.053
6.4
N


ATOM
37
CA
VAL
1109
−26.871
−10.086
−19.974
7.09
C


ATOM
38
CB
VAL
1109
−26.761
−8.561
−19.567
7.99
C


ATOM
39
CG1
VAL
1109
−25.877
−8.259
−18.375
9.38
C


ATOM
40
CG2
VAL
1109
−26.627
−7.612
−20.741
7.64
C


ATOM
41
C
VAL
1109
−26.574
−10.363
−21.435
8.01
C


ATOM
42
O
VAL
1109
−25.47
−10.729
−21.79
5.65
O


ATOM
43
N
LYS
1110
−27.587
−10.221
−22.269
7.51
N


ATOM
44
CA
LYS
1110
−27.256
−10.294
−23.664
9.65
C


ATOM
45
CB
LYS
1110
−27.073
−11.731
−24.086
10.89
C


ATOM
46
CG
LYS
1110
−28.259
−12.478
−24.304
12.06
C


ATOM
47
CD
LYS
1110
−28.291
−12.786
−25.777
14.94
C


ATOM
48
CE
LYS
1110
−26.923
−13.196
−26.354
15.05
C


ATOM
49
NZ
LYS
1110
−27.04
−13.161
−27.915
11.9
N


ATOM
50
C
LYS
1110
−28.105
−9.473
−24.577
9.23
C


ATOM
51
O
LYS
1110
−29.287
−9.193
−24.318
8.86
O


ATOM
52
N
LEU
1140
−37.463
−20.519
−16.111
8.72
N


ATOM
53
CA
LEU
1140
−36.55
−19.367
−16.142
11.04
C


ATOM
54
CB
LEU
1140
−35.314
−19.688
−17
10.97
C


ATOM
55
CG
LEU
1140
−34.23
−18.646
−17.065
9.46
C


ATOM
56
CD1
LEU
1140
−33.609
−18.426
−15.69
8.34
C


ATOM
57
CD2
LEU
1140
−33.188
−19.076
−18.042
11.77
C


ATOM
58
C
LEU
1140
−37.252
−18.13
−16.69
12.97
C


ATOM
59
O
LEU
1140
−37.803
−18.148
−17.804
12.64
O


ATOM
60
N
VAL
1155
−31.611
−8.495
−22.98
8.16
N


ATOM
61
CA
VAL
1155
−32.323
−9.277
−21.923
8.76
C


ATOM
62
CB
VAL
1155
−32.814
−10.693
−22.353
9.39
C


ATOM
63
CG1
VAL
1155
−34.033
−10.582
−23.316
10.94
C


ATOM
64
CG2
VAL
1155
−31.728
−11.492
−22.993
8.74
C


ATOM
65
C
VAL
1155
−31.427
−9.427
−20.73
8.02
C


ATOM
66
O
VAL
1155
−30.209
−9.527
−20.889
7.13
O


ATOM
67
N
LEU
1157
−30.843
−11.847
−17.422
7.79
N


ATOM
68
CA
LEU
1157
−31.27
−13.118
−16.786
7.81
C


ATOM
69
CB
LEU
1157
−30.902
−14.33
−17.682
9.69
C


ATOM
70
CG
LEU
1157
−32.066
−14.227
−18.65
11.62
C


ATOM
71
CD1
LEU
1157
−31.674
−13.539
−19.933
11.32
C


ATOM
72
CD2
LEU
1157
−32.851
−15.474
−18.797
10.57
C


ATOM
73
C
LEU
1157
−30.661
−13.291
−15.419
8.75
C


ATOM
74
O
LEU
1157
−29.588
−12.733
−15.162
7.63
O


ATOM
75
N
PRO
1158
−31.285
−14.129
−14.552
9.58
N


ATOM
76
CA
PRO
1158
−30.573
−14.427
−13.309
10.72
C


ATOM
77
CB
PRO
1158
−31.566
−15.292
−12.497
10.18
C


ATOM
78
CG
PRO
1158
−32.788
−15.258
−13.187
11.04
C


ATOM
79
CD
PRO
1158
−32.545
−14.873
−14.637
9.45
C


ATOM
80
C
PRO
1158
−29.342
−15.228
−13.655
11.46
C


ATOM
81
O
PRO
1158
−29.302
−15.934
−14.683
11.52
O


ATOM
82
N
TYR
1159
−28.326
−15.091
−12.828
12.18
N


ATOM
83
CA
TYR
1159
−27.094
−15.799
−13.05
13.78
C


ATOM
84
CB
TYR
1159
−25.976
−15.173
−12.234
13.95
C


ATOM
85
CG
TYR
1159
−24.668
−15.894
−12.374
15.44
C


ATOM
86
CD1
TYR
1159
−23.973
−15.906
−13.604
15.19
C


ATOM
87
CE1
TYR
1159
−22.762
−16.583
−13.73
15.55
C


ATOM
88
CZ
TYR
1159
−22.229
−17.235
−12.622
15.73
C


ATOM
89
OH
TYR
1159
−21.025
−17.924
−12.718
18.54
O


ATOM
90
CE2
TYR
1159
−22.889
−17.225
−11.399
16.11
C


ATOM
91
CD2
TYR
1159
−24.099
−16.548
−11.276
14.98
C


ATOM
92
C
TYR
1159
−27.328
−17.25
−12.659
14.12
C


ATOM
93
O
TYR
1159
−27.868
−17.544
−11.573
13.85
O


ATOM
94
N
MET
1160
−26.977
−18.141
−13.575
13.76
N


ATOM
95
CA
MET
1160
−27.199
−19.572
−13.403
14.48
C


ATOM
96
CB
MET
1160
−28.079
−20.159
−14.542
14.71
C


ATOM
97
CG
MET
1160
−29.48
−19.592
−14.597
15.91
C


ATOM
98
SD
MET
1160
−30.533
−20.154
−13.195
20.68
S


ATOM
99
CE
MET
1160
−31.401
−18.698
−12.74
20.48
C


ATOM
100
C
MET
1160
−25.816
−20.14
−13.382
14.64
C


ATOM
101
O
MET
1160
−25.182
−20.283
−14.417
15.02
O


ATOM
102
N
LYS
1161
−25.314
−20.346
−12.167
15.21
N


ATOM
103
CA
LYS
1161
−23.952
−20.771
−11.91
14.1
C


ATOM
104
CB
LYS
1161
−23.758
−21.08
−10.427
15.12
C


ATOM
105
CG
LYS
1161
−22.333
−21.497
−10.095
17.53
C


ATOM
106
CD
LYS
1161
−22.188
−21.839
−8.613
24.97
C


ATOM
107
CE
LYS
1161
−20.714
−21.982
−8.207
26.67
C


ATOM
108
NZ
LYS
1161
−20.549
−21.583
−6.789
32.02
N


ATOM
109
C
LYS
1161
−23.518
−21.98
−12.746
13.45
C


ATOM
110
O
LYS
1161
−22.404
−22.006
−13.258
12.16
O


ATOM
111
N
HIS
1162
−24.38
−22.987
−12.865
12.66
N


ATOM
112
CA
HIS
1162
−23.979
−24.201
−13.569
12.84
C


ATOM
113
CB
HIS
1162
−24.427
−25.452
−12.815
11.85
C


ATOM
114
CG
HIS
1162
−23.908
−25.504
−11.426
13.4
C


ATOM
115
ND1
HIS
1162
−22.554
−25.561
−11.145
15.28
N


ATOM
116
CE1
HIS
1162
−22.385
−25.595
−9.838
16.31
C


ATOM
117
NE2
HIS
1162
−23.575
−25.537
−9.261
17.98
N


ATOM
118
CD2
HIS
1162
−24.542
−25.471
−10.232
14.71
C


ATOM
119
C
HIS
1162
−24.36
−24.282
−15.038
13.45
C


ATOM
120
O
HIS
1162
−24.234
−25.367
−15.634
14.09
O


ATOM
121
N
GLY
1163
−24.807
−23.162
−15.62
12.39
N


ATOM
122
CA
GLY
1163
−25.108
−23.113
−17.056
11.81
C


ATOM
123
C
GLY
1163
−26.195
−24.111
−17.397
11.37
C


ATOM
124
O
GLY
1163
−27.052
−24.405
−16.541
12.27
O


ATOM
125
N
ASP
1164
−26.16
−24.657
−18.612
10.58
N


ATOM
126
CA
ASP
1164
−27.202
−25.57
−19.037
11.05
C


ATOM
127
CB
ASP
1164
−27.395
−25.576
−20.566
10.73
C


ATOM
128
CG
ASP
1164
−26.214
−26.22
−21.317
14.82
C


ATOM
129
OD1
ASP
1164
−26.203
−27.447
−21.509
16.5
O


ATOM
130
OD2
ASP
1164
−25.324
−25.485
−21.76
16.71
O


ATOM
131
C
ASP
1164
−26.958
−26.97
−18.481
10.14
C


ATOM
132
O
ASP
1164
−25.836
−27.355
−18.139
9.32
O


ATOM
133
N
ASP
1211
−31.568
−24.508
−17.398
11.25
N


ATOM
134
CA
ASP
1211
−30.407
−23.962
−16.703
12.07
C


ATOM
135
CB
ASP
1211
−30.29
−22.425
−16.878
13.35
C


ATOM
136
CG
ASP
1211
−29.946
−21.986
−18.38
15.72
C


ATOM
137
OD1
ASP
1211
−28.869
−22.268
−19.063
3.34
O


ATOM
138
OD2
ASP
1211
−30.838
−21.298
−18.869
22.8
O


ATOM
139
C
ASP
1211
−30.314
−24.43
−15.238
11.76
C


ATOM
140
O
ASP
1211
−31.303
−24.781
−14.626
11.98
O


ATOM
141
N
ALA
1221
−35.874
−22.995
−19.798
9.64
N


ATOM
142
CA
ALA
1221
−35.638
−21.759
−20.538
11.43
C


ATOM
143
CB
ALA
1221
−34.165
−21.475
−20.605
12.72
C


ATOM
144
C
ALA
1221
−36.215
−21.756
−21.953
12.59
C


ATOM
145
O
ALA
1221
−36.317
−22.801
−22.617
11.05
O


ATOM
146
O
ASP
1222
−36.499
−18.098
−24.227
17.5
O


ATOM
147
N
ASP
1222
−36.5
−20.634
−22.356
20
N


ATOM
148
CA
ASP
1222
−36.941
−20.406
−23.727
20
C


ATOM
149
C
ASP
1222
−36.151
−19.273
−24.377
20
C


ATOM
150
CB
ASP
1222
−38.437
−20.091
−23.763
20
C


ATOM
151
CG
ASP
1222
−38.824
−18.99
−22.796
20
C


ATOM
152
OD1
ASP
1222
−37.994
−18.638
−21.932
20
O


ATOM
153
OD2
ASP
1222
−39.935
−18.418
−22.824
20
O


ATOM
154
N
PHE
1223
−35.113
−19.54
−24.88
16.19
N


ATOM
155
CA
PHE
1223
−34.306
−18.466
−25.34
17.32
C


ATOM
156
CB
PHE
1223
−32.818
−18.714
−25.181
16
C


ATOM
157
CG
PHE
1223
−32.355
−18.541
−23.754
11.65
C


ATOM
158
CD1
PHE
1223
−32.357
−17.286
−23.16
11.27
C


ATOM
159
CE1
PHE
1223
−31.94
−17.128
−21.826
15.53
C


ATOM
160
CZ
PHE
1223
−31.549
−18.252
−21.091
14.31
C


ATOM
161
CE2
PHE
1223
−31.558
−19.492
−21.689
14.38
C


ATOM
162
CD2
PHE
1223
−31.98
−19.622
−23.01
14.35
C


ATOM
163
C
PHE
1223
−34.816
−18.009
−26.7
20.29
C


ATOM
164
O
PHE
1223
−35.386
−16.886
−26.787
22.15
O


ATOM
165
N
ALA
1226
−32.985
−15.014
−28.359
16.83
N


ATOM
166
CA
ALA
1226
−31.681
−14.627
−27.816
15.78
C


ATOM
167
CB
ALA
1226
−31.656
−14.803
−26.309
15.05
C


ATOM
168
C
ALA
1226
−30.512
−15.38
−28.432
15.33
C


ATOM
169
O
ALA
1226
−29.385
−14.922
−28.31
14.85
O


ATOM
170
N
ARG
1227
−30.768
−16.534
−29.062
14.69
N


ATOM
171
CA
ARG
1227
−29.719
−17.245
−29.776
13.62
C


ATOM
172
CB
ARG
1227
−30.066
−18.729
−29.985
14.18
C


ATOM
173
CG
ARG
1227
−30.303
−19.5
−28.711
12.15
C


ATOM
174
CD
ARG
1227
−30.765
−20.926
−28.952
14.86
C


ATOM
175
NE
ARG
1227
−30.801
−21.623
−27.669
17.43
N


ATOM
176
CZ
ARG
1227
−29.719
−22.054
−27.024
18.53
C


ATOM
177
NH1
ARG
1227
−28.513
−21.933
−27.574
20.01
N


ATOM
178
NH2
ARG
1227
−29.843
−22.65
−25.851
19.76
N


ATOM
179
C
ARG
1227
−29.535
−16.57
−31.118
13.93
C


ATOM
180
O
ARG
1227
−30.445
−16.603
−31.947
14.89
O









Example 2
The Construction of the c-Abl Inhibition Model
A 3-dimensional model for the inhibition of c-Abl was created using the process described below.
The sequence alignment of c-Abl kinase and the amino acid sequence of c-Met was performed using MOE alignment tools. Care was taken to make sure that known kinase motifs: DFG motif, the hinge residues and the salt bridge residues were superposed.
The identification of conserved amino acid residues between c-Met and c-Abl, generation of atomic coordinates of all conserved amino acids in c-Abl from the electronic representation of c-Met residues; rotamer search of the structurally variable and replacement of non-conserved residues of c-Met with residues from c-Abl sequence; building of side chain conformations; and final refinement and evaluation of the c-Abl structure were carried out in an automated fashion using MOE homology tools.
Example 3
The Similarity Assessment of c-Abl Inhibition Model
From Table 2, it can be determined that the similarity assessment value is less than 50% for c-Abl. Three residues show negative weights: T333 (L1157), N340 (D1164), and S403 (A1226). The inhibition model will have a significant change in polarity factor.
L1157 is located deep into the c-Met inhibition model. This residue is one of several which confers c-Met its mainly hydrophobic nature. In this position, c-Abl model shows a T333, a highly polar residue. Therefore, the chemical environment of an inhibitor has changed dramatically. The selective c-Met inhibitor does not have any atomic group to make favorable electrostatic interactions with T333. N340 and S403 also lack favorable electrostatic interactions with the selective c-Met inhibitor. Thus, the selective c-Met inhibitor is not predicted to inhibit c-Abl.
The amino acids of the inhibition model of c-Abl derived from the c-Met inhibition model are described herein and are defined by a set of structure coordinates set forth in Table 5.







TABLE 5





(SEQ ID NO: 8)






















ATOM
N
LEU
266
−19.916
−14.441
−18.273
N


ATOM
CA
LEU
266
−20.814
−15.367
−18.929
C


ATOM
CB
LEU
266
−22.191
−14.827
−19.221
C


ATOM
C
LEU
266
−20.09
−16.157
−20.018
C


ATOM
O
LEU
266
−19.184
−16.942
−19.745
O


ATOM
CG
LEU
266
−23.209
−15.308
−18.209
C


ATOM
CD1
LEU
266
−22.892
−14.842
−16.81
C


ATOM
CD2
LEU
266
−24.581
−14.82
−18.593
C


ATOM
N
GLY
267
−20.417
−15.864
−21.327
N


ATOM
CA
GLY
267
−19.615
−16.503
−22.345
C


ATOM
C
GLY
267
−20.218
−16.526
−23.733
C


ATOM
O
GLY
267
−21.424
−16.638
−23.949
O


ATOM
N
TYR
271
−24.397
−19.744
−29.694
N


ATOM
CA
TYR
271
−25.559
−18.884
−29.522
C


ATOM
CB
TYR
271
−26.283
−19.182
−28.204
C


ATOM
C
TYR
271
−25.27
−17.375
−29.625
C


ATOM
O
TYR
271
−26.133
−16.521
−29.392
O


ATOM
CG
TYR
271
−25.398
−19.096
−26.995
C


ATOM
CD1
TYR
271
−24.792
−17.887
−26.648
C


ATOM
CD2
TYR
271
−25.102
−20.248
−26.264
C


ATOM
CE1
TYR
271
−23.869
−17.829
−25.616
C


ATOM
CE2
TYR
271
−24.179
−20.197
−25.219
C


ATOM
CZ
TYR
271
−23.557
−18.989
−24.92
C


ATOM
OH
TYR
271
−22.608
−18.958
−23.929
O


ATOM
N
VAL
274
−23.294
−14.153
−24.61
N


ATOM
CA
VAL
274
−24.16
−13.806
−23.491
C


ATOM
CB
VAL
274
−25.02
−14.966
−23.017
C


ATOM
C
VAL
274
−23.242
−13.359
−22.365
C


ATOM
O
VAL
274
−22.23
−13.983
−22.045
O


ATOM
CG1
VAL
274
−26.029
−14.498
−21.991
C


ATOM
CG2
VAL
274
−25.781
−15.575
−24.163
C


ATOM
N
ALA
287
−27.677
−12.533
−15.683
N


ATOM
CA
ALA
287
−27.163
−12.605
−17.031
C


ATOM
CB
ALA
287
−27.621
−13.873
−17.711
C


ATOM
C
ALA
287
−27.733
−11.415
−17.791
C


ATOM
O
ALA
287
−28.826
−10.907
−17.535
O


ATOM
N
VAL
288
−26.977
−11.03
−18.871
N


ATOM
CA
VAL
288
−27.516
−10.069
−19.803
C


ATOM
CB
VAL
288
−26.987
−8.657
−19.576
C


ATOM
C
VAL
288
−27.201
−10.557
−21.208
C


ATOM
O
VAL
288
−26.124
−11.023
−21.58
O


ATOM
CG1
VAL
288
−27.658
−7.659
−20.495
C


ATOM
CG2
VAL
288
−27.21
−8.185
−18.157
C


ATOM
N
LYS
289
−28.252
−10.312
−22.064
N


ATOM
CA
LYS
289
−28.041
−10.491
−23.48
C


ATOM
CB
LYS
289
−28.329
−11.881
−24.014
C


ATOM
C
LYS
289
−28.817
−9.471
−24.288
C


ATOM
O
LYS
289
−29.858
−8.937
−23.914
O


ATOM
CG
LYS
289
−27.284
−12.24
−25.052
C


ATOM
CD
LYS
289
−27.779
−13.297
−26.008
C


ATOM
CE
LYS
289
−26.677
−13.676
−26.976
C


ATOM
NZ
LYS
289
−27.262
−14.535
−28.044
N1+


ATOM
N
VAL
317
−36.3
−20.382
−15.116
N


ATOM
CA
VAL
317
−35.436
−19.216
−15.287
C


ATOM
CB
VAL
317
−34.28
−19.474
−16.244
C


ATOM
C
VAL
317
−36.337
−18.127
−15.852
C


ATOM
O
VAL
317
−37.128
−18.313
−16.773
O


ATOM
CG1
VAL
317
−33.439
−20.65
−15.809
C


ATOM
CG2
VAL
317
−33.373
−18.267
−16.334
C


ATOM
N
ILE
331
−32.2
−7.875
−22.796
N


ATOM
CA
ILE
331
−32.865
−8.817
−21.914
C


ATOM
CB
ILE
331
−33.299
−10.061
−22.683
C


ATOM
C
ILE
331
−31.906
−9.163
−20.783
C


ATOM
O
ILE
331
−30.744
−9.528
−20.955
O


ATOM
CG1
ILE
331
−34.398
−9.745
−23.684
C


ATOM
CG2
ILE
331
−33.763
−11.172
−21.764
C


ATOM
CD1
ILE
331
−35.654
−9.209
−23.03
C


ATOM
N
THR
333
−31.711
−11.403
−17.09
N


ATOM
CA
THR
333
−32.291
−12.558
−16.398
C


ATOM
CB
THR
333
−32.376
−13.8
−17.293
C


ATOM
C
THR
333
−31.371
−12.885
−15.243
C


ATOM
O
THR
333
−30.16
−12.687
−15.306
O


ATOM
OG1
THR
333
−31.099
−14.206
−17.797
O


ATOM
CG2
THR
333
−33.289
−13.577
−18.477
C


ATOM
N
GLU
334
−31.929
−13.562
−14.194
N


ATOM
CA
GLU
334
−31.049
−14.086
−13.162
C


ATOM
CB
GLU
334
−31.793
−14.548
−11.918
C


ATOM
C
GLU
334
−30.016
−15.113
−13.667
C


ATOM
O
GLU
334
−30.153
−15.806
−14.674
O


ATOM
CG
GLU
334
−32.718
−15.726
−12.155
C


ATOM
CD
GLU
334
−33.907
−15.472
−13.064
C


ATOM
OE1
GLU
334
−34.471
−16.519
−13.499
O1−


ATOM
OE2
GLU
334
−34.185
−14.264
−13.348
O


ATOM
N
PHE
335
−28.897
−15.174
−12.855
N


ATOM
CA
PHE
335
−27.724
−15.967
−13.224
C


ATOM
CB
PHE
335
−26.472
−15.304
−12.651
C


ATOM
C
PHE
335
−27.822
−17.389
−12.673
C


ATOM
O
PHE
335
−27.992
−17.648
−11.486
O


ATOM
CG
PHE
335
−25.147
−15.936
−12.949
C


ATOM
CD1
PHE
335
−24.88
−16.583
−14.156
C


ATOM
CD2
PHE
335
−24.145
−15.864
−11.983
C


ATOM
CE1
PHE
335
−23.637
−17.166
−14.389
C


ATOM
CE2
PHE
335
−22.898
−16.44
−12.214
C


ATOM
CZ
PHE
335
−22.645
−17.095
−13.416
C


ATOM
N
MET
336
−27.676
−18.363
−13.637
N


ATOM
CA
MET
336
−27.674
−19.773
−13.292
C


ATOM
CB
MET
336
−28.489
−20.582
−14.273
C


ATOM
C
MET
336
−26.24
−20.281
−13.223
C


ATOM
O
MET
336
−25.533
−20.558
−14.187
O


ATOM
CG
MET
336
−29.927
−20.877
−13.875
C


ATOM
SD
MET
336
−30.643
−20.004
−12.452
S


ATOM
CE
MET
336
−31.071
−18.464
−13.296
C


ATOM
N
THR
337
−25.767
−20.22
−11.937
N


ATOM
CA
THR
337
−24.346
−20.219
−11.611
C


ATOM
CB
THR
337
−24.222
−20.086
−10.094
C


ATOM
C
THR
337
−23.595
−21.487
−12.019
C


ATOM
O
THR
337
−22.386
−21.482
−12.227
O


ATOM
OG1
THR
337
−25.449
−19.587
−9.527
O


ATOM
CG2
THR
337
−23.079
−19.169
−9.723
C


ATOM
N
TYR
338
−24.343
−22.643
−11.985
N


ATOM
CA
TYR
338
−23.729
−23.934
−12.217
C


ATOM
CB
TYR
338
−24.416
−24.993
−11.379
C


ATOM
C
TYR
338
−23.762
−24.378
−13.682
C


ATOM
O
TYR
338
−23.383
−25.493
−14.026
O


ATOM
CG
TYR
338
−23.568
−25.565
−10.292
C


ATOM
CD1
TYR
338
−22.236
−25.927
−10.513
C


ATOM
CD2
TYR
338
−24.147
−25.802
−9.046
C


ATOM
CE1
TYR
338
−21.497
−26.545
−9.507
C


ATOM
CE2
TYR
338
−23.411
−26.411
−8.034
C


ATOM
CZ
TYR
338
−22.098
−26.795
−8.277
C


ATOM
OH
TYR
338
−21.418
−27.465
−7.287
O


ATOM
N
GLY
339
−24.173
−23.424
−14.591
N


ATOM
CA
GLY
339
−24.111
−23.721
−16.01
C


ATOM
C
GLY
339
−25.334
−24.505
−16.464
C


ATOM
O
GLY
339
−26.443
−24.373
−15.942
O


ATOM
N
ASN
340
−25.101
−25.257
−17.604
N


ATOM
CA
ASN
340
−26.191
−26.036 
−18.17
C


ATOM
CB
ASN
340
−26.524
−25.799
−19.634
C


ATOM
C
ASN
340
−26.198
−27.515
−17.8
C


ATOM
O
ASN
340
−25.188
−28.131
−17.466
O


ATOM
CG
ASN
340
−25.47
−26.41
−20.502
C


ATOM
OD1
ASN
340
−25.344
−27.622
−20.648
O


ATOM
ND2
ASN
340
−24.639
−25.481
−21.052
N


ATOM
N
LEU
388
−30.765
−24.965
−17.173
N


ATOM
CA
LEU
388
−29.637
−24.46
−16.404
C


ATOM
CB
LEU
388
−29.54
−22.942
−16.453
C


ATOM
C
LEU
388
−29.728
−24.852
−14.933
C


ATOM
O
LEU
388
−30.785
−25.113
−14.356
O


ATOM
CG
LEU
388
−29.205
−22.298
−17.782
C


ATOM
CD1
LEU
388
−28.098
−23.005
−18.523
C


ATOM
CD2
LEU
388
−30.424
−22.172
−18.658
C


ATOM
N
ALA
398
−35.889
−22.88
−19.129
N


ATOM
CA
ALA
398
−36.044
−21.552
−19.7
C


ATOM
CB
ALA
398
−34.943
−20.618
−19.251
C


ATOM
C
ALA
398
−36.046
−21.615
−21.211
C


ATOM
O
ALA
398
−35.39
−22.427
−21.854
O


ATOM
N
ASP
399
−36.893
−20.694
−21.784
N


ATOM
CA
ASP
399
−36.858
−20.444
−23.21
C


ATOM
CB
ASP
399
−38.239
−20.251
−23.829
C


ATOM
C
ASP
399
−35.954
−19.212
−23.354
C


ATOM
O
ASP
399
−35.733
−18.392
−22.468
O


ATOM
CG
ASP
399
−38.247
−20.184
−25.363
C


ATOM
OD1
ASP
399
−37.116
−20.365
−25.93
O


ATOM
OD2
ASP
399
−39.369
−19.86
−25.882
O1−


ATOM
N
PHE
400
−35.483
−19.083
−24.627
N


ATOM
CA
PHE
400
−34.56
−18.038
−24.992
C


ATOM
CB
PHE
400
−33.141
−18.571
−25.139
C


ATOM
C
PHE
400
−34.97
−17.332
−26.27
C


ATOM
O
PHE
400
−34.492
−16.233
−26.549
O


ATOM
CG
PHE
400
−32.584
−19.079
−23.847
C


ATOM
CD1
PHE
400
−32.179
−20.407
−23.749
C


ATOM
CE1
PHE
400
−31.711
−20.913
−22.54
C


ATOM
CZ
PHE
400
−31.651
−20.091
−21.42
C


ATOM
CE2
PHE
400
−32.052
−18.762
−21.512
C


ATOM
CD2
PHE
400
−32.512
−18.255
−22.723
C


ATOM
N
GLY
401
−35.767
−18.029
−27.165
N


ATOM
CA
GLY
401
−36.219
−17.353
−28.371
C


ATOM
C
GLY
401
−35.078
−16.919
−29.288
C


ATOM
O
GLY
401
−34.093
−17.609
−29.541
0


ATOM
N
SER
403
−32.943
−14.891
−28.539
N


ATOM
CA
SER
403
−31.691
−14.692
−27.847
C


ATOM
CB
SER
403
−31.925
−14.71
−26.353
C


ATOM
C
SER
403
−30.655
−15.749
−28.247
C


ATOM
O
SER
403
−29.448
−15.589
−28.049
O


ATOM
OG
SER
403
−31.052
−13.781
−25.724
O


ATOM
N
ARG
404
−31.161
−16.939
−28.747
N


ATOM
CA
ARG
404
−30.26
−17.923
−29.325
C


ATOM
C
ARG
404
−30.241
−17.654
−30.824
C


ATOM
O
ARG
404
−31.151
−17.963
−31.589
O


ATOM
CB
ARG
404
−30.647
−19.349
−28.982
C


ATOM
CG
ARG
404
−30.039
−19.673
−27.637
C


ATOM
CD
ARG
404
−30.267
−21.085
−27.152
C


ATOM
NE
ARG
404
−29.692
−21.2
−25.81
N1+


ATOM
CZ
ARG
404
−28.984
−22.31
−25.348
C


ATOM
NH1
ARG
404
−28.74
−23.394
−26.179
N


ATOM
NH2
ARG
404
−28.465
−22.29
−24.064
N









Example 4
The Use of c-Abl Inhibition Model in the Fitting and Optimization of a Small Molecular Template
N-(4-methyl-3-(4-(pyridin-3-yl)pyrimidin-2-ylamino)phenyl)nicotinamide, which is known as a c-Abl inhibitor (Schindler et al, 2000) was placed inside the c-Abl inhibition model.
Docking and optimization against the c-Abl inhibition model was performed. The docking procedure was carried out using ICM software. A conformation in which the pyridine ring and the hinge residues were in close proximity was selected. Further optimization was carried out using MOE energy minimization tools
Hydrogen bonds between the pyridine and the critical amino group of the hinge from M336 and the compound's amino group and T333 were identified. The presence of these hydrogen bonds is in agreement with experimental X-ray crystallographic data for the complex c-Abl kinase/Gleevec.
The overall protein-ligand interaction energy was negative (−68 kcal/mol), as it is calculated using MOE energy calculation tools, indicating a high probability of interaction.
(−)-trans-3-(5,6-dihydro-4H-pyrrolo[3,2,1-ij]quinolin-1-yl)-4(1H-indol-3-yl)pyrrolidine-2,5-dione, the selective c-Met inhibitor, was also docked in the c-Abl inhibition model where the pyrrolidine carbonyl ring makes a hydrogen bonds with the amino group of M336.
Further energy optimization using MOE tools was carried out. Two hydrogen bonds where observed between the pyrrolidine ring and hinge residues M336 and E334. Although the overall interaction energy is negative (−50 kcal/mol), a lack of feature complementarity between the selective c-Met inhibitor and c-Abl inhibitor model is clearly observed.
The hydrophobic tricyclic ring is placed in a polar region of the c-Abl inhibition model. Additionally no interactions between the selective c-Met inhibitor and a critical residue in c-Abl T333 are observed. N340 and 5403 will also lack favorable electrostatic interactions with the selective c-Met inhibitor. Taken together, it is expected that the selective c-Met inhibitor does not bind to the inactive form of c-Abl kinase. This conclusion is consistent with the observation that the selective c-Met inhibitor does not inhibit the activity of c-Abl effectively, while it inhibits the activity of c-Met effectively (WO 2006/086484 A1).
Example 5
The Construction of FGFR-2 Inhibition Model
A 3-dimensional inhibition model of FGFR-2 was created using the process.
The sequence alignment of FGFR-2 kinase and the amino acid sequence of c-Met were performed using MOE alignment tools. Known kinase motifs: the P-loop F492, the DFG motif (644-646), the hinge residue A567, the salt bridge K517-E534, and tyrosine residues Y656 and Y657 in the A-loop, residues which are phosphorylated upon activation, were superposed.
The identification of conserved amino acid residues between c-Met and FGFR-2; generation of atomic coordinates of all conserved amino acids in FGFR-2 from the electronic representation of c-Met residues; rotamer search of the structurally variable and replacement of non-conserved residues of c-Met with residues from FGFR-2 sequence; building of side chain conformations; and final refinement and evaluation of the FGFR-2 structure was carried out in an automated fashion using MOE homology tools.
Example 6
The Similarity Assessment of FGFR2 Inhibition Model
The FGFR-2 model is 78% similar to c-Met1 (Table 6). One residue shows negative weights: E565 (P1158). The inhibition model has no significant changes in polarity factor. The only differences are in size: 1548 (L1140), gate keeper V564 (L1157), hinge residue A567 (M1160), and L633 (M1211).
Although, the FGFR-2 binding pocket is 78% similar, the presence of a smaller gate keeper residue V564, hinge residue (A567) and L633, results in a larger binding site.







TABLE 6







(SEQ ID NOs. 11 and 12, respectively)














CMET

FGFR-2





(SEQ ID

(SEQ ID




PROTEIN
NO: 11)
weight
NO: 12)
weight


















I_1084
2
L_487
1




G_1085
2
G_488
2




F_1089
2
F_492
2




V_1092
2
V_495
2




A_1108
1
A_515
1




V_1109b
0.5
V_516b
0.5




K_1110b
0.5
K_517
0.5




L_1140
1
I_548
0.5




V_1155
1
V_562
1




L_1157
1
V_564
0.5




P_1158
1
E_565
−1




Y_1159b
0.5
Y_566b
0.5




M_1160b
1
A_567
0.5




K_1161b
0.5
S_568
0.5




H_1162b
0.5
K_569
0.5




G_1163
0.5
G_570
0.5




D_1164
1
N_571
0.5




M_1211
1
L_633
0.5




A_1221
1
A_643
1




D_1222
1
D_644
1




F_1223
1
F_645
1




A_1226
1
A_648
1




R_1227
2
R_649
2



Similarity







assessmet







value

25

19.5










The amino acids of the inhibition model of FGFR-2 derived from the c-Met inhibition model are described herein and are defined by a set of structure coordinates set forth in Table 7.







TABLE 7





(SEQ ID NO: 13)























ATOM
1
N
LEU
487
−15.283
−12.748
−21.3
N


ATOM
2
CA
LEU
487
−15.06
−13.48
−22.53
C


ATOM
3
CB
LEU
487
−13.576
−13.545
−22.839
C


ATOM
4
C
LEU
487
−15.629
−14.889
−22.364
C


ATOM
5
O
LEU
487
−15.735
−15.456
−21.281
O


ATOM
6
CG
LEU
487
−13.279
−13.768
−24.307
C


ATOM
7
CD1
LEU
487
−13.885
−12.686
−25.169
C


ATOM
8
CD2
LEU
487
−11.787
−13.812
−24.52
C


ATOM
9
N
GLY
488
−15.929
−15.472
−23.57
N


ATOM
10
CA
GLY
488
−16.524
−16.79
−23.653
C


ATOM
11
C
GLY
488
−16.466
−17.181
−25.116
C


ATOM
12
O
GLY
488
−15.582
−16.783
−25.867
O


ATOM
13
N
PHE
492
−23.749
−19.863
−29.63
N


ATOM
14
CA
PHE
492
−25.002
−19.22
−29.231
C


ATOM
15
CB
PHE
492
−25.587
−19.86
−27.979
C


ATOM
16
C
PHE
492
−25.001
−17.689
−29.085
C


ATOM
17
O
PHE
492
−26.019
−17.067
−28.781
O


ATOM
18
CG
PHE
492
−24.719
−19.956
−26.759
C


ATOM
19
CD1
PHE
492
−24.804
−21.1
−25.968
C


ATOM
20
CD2
PHE
492
−23.836
−18.942
−26.382
C


ATOM
21
CE1
PHE
492
−24.02
−21.234
−24.825
C


ATOM
22
CE2
PHE
492
−23.048
−19.07
−25.241
C


ATOM
23
CZ
PHE
492
−23.141
−20.219
−24.461
C


ATOM
24
N
GLY
493
−23.77
−17.113
−29.309
N


ATOM
25
CA
GLY
493
−23.455
−15.731
−29.017
C


ATOM
26
C
GLY
493
−22.503
−15.689
−27.832
C


ATOM
27
O
GLY
493
−21.708
−16.582
−27.563
O


ATOM
28
N
GLN
494
−22.526
−14.481
−27.17
N


ATOM
29
CA
GLN
494
−21.732
−14.296
−25.963
C


ATOM
30
CB
GLN
494
−21.048
−12.945
−26.027
C


ATOM
31
C
GLN
494
−22.718
−14.31
−24.793
C


ATOM
32
O
GLN
494
−23.886
−13.945
−24.911
O


ATOM
33
CG
GLN
494
−20.061
−12.71
−24.903
C


ATOM
34
CD
GLN
494
−19.703
−11.252
−24.848
C


ATOM
35
OE1
GLN
494
−20.153
−10.395
−25.598
O


ATOM
36
NE2
GLN
494
−18.807
−10.945
−23.868
N


ATOM
37
N
VAL
495
−22.162
−14.629
−23.575
N


ATOM
38
CA
VAL
495
−22.939
−14.409
−22.373
C


ATOM
39
CB
VAL
495
−22.86
−15.58
−21.402
C


ATOM
40
C
VAL
495
−22.459
−13.103
−21.75
C


ATOM
41
O
VAL
495
−21.278
−12.855
−21.519
O


ATOM
42
CG1
VAL
495
−21.452
−15.945
−20.985
C


ATOM
43
CG2
VAL
495
−23.702
−15.34
−20.173
C


ATOM
44
N
VAL
496
−23.484
−12.248
−21.413
N


ATOM
45
CA
VAL
496
−23.179
−11.07
−20.645
C


ATOM
46
CB
VAL
496
−22.851
−9.761
−21.324
C


ATOM
47
C
VAL
496
−23.249
−11.167
−19.14
C


ATOM
48
O
VAL
496
−24.216
−11.678
−18.581
O


ATOM
49
CG1
VAL
496
−23.894
−9.375
−22.346
C


ATOM
50
CG2
VAL
496
−21.48
−9.77
−21.952
C


ATOM
51
N
VAL
514
−25.883
−11.411
−12.079
N


ATOM
52
CA
VAL
514
−26.859
−11.989
−12.989
C


ATOM
53
CB
VAL
514
−28.229
−11.335
−12.845
C


ATOM
54
C
VAL
514
−26.37
−11.928
−14.442
C


ATOM
55
O
VAL
514
−25.251
−11.529
−14.762
O


ATOM
56
CG1
VAL
514
−28.19
−9.827
−12.937
C


ATOM
57
CG2
VAL
514
−28.95
−11.778
−11.595
C


ATOM
58
N
ALA
515
−27.267
−12.383
−15.386
N


ATOM
59
CA
ALA
515
−26.791
−12.451
−16.749
C


ATOM
60
CB
ALA
515
−26.728
−13.861
−17.274
C


ATOM
61
C
ALA
515
−27.514
−11.523
−17.703
C


ATOM
62
O
ALA
515
−28.703
−11.235
−17.586
O


ATOM
63
N
VAL
516
−26.711
−11.107
−18.744
N


ATOM
64
CA
VAL
516
−27.23
−10.248
−19.791
C


ATOM
65
CB
VAL
516
−26.383
−8.987
−19.971
C


ATOM
66
C
VAL
516
−27.215
−10.994
−21.123
C


ATOM
67
O
VAL
516
−26.31
−11.744
−21.483
O


ATOM
68
CG1
VAL
516
−27.079
−7.964
−20.836
C


ATOM
69
CG2
VAL
516
−26.019
−8.316
−18.674
C


ATOM
70
N
LYS
517
−28.253
−10.572
−21.928
N


ATOM
71
CA
LYS
517
−28.249
−10.726
−23.368
C


ATOM
72
CB
LYS
517
−27.776
−11.986
−24.071
C


ATOM
73
C
LYS
517
−28.797
−9.577
−24.194
C


ATOM
74
O
LYS
517
−29.796
−8.954
−23.846
O


ATOM
75
CG
LYS
517
−28.92
−12.668
−24.793
C


ATOM
76
CD
LYS
517
−28.518
−13.807
−25.713
C


ATOM
77
CE
LYS
517
−27.58
−13.411
−26.843
C


ATOM
78
NZ
LYS
517
−27.474
−14.567
−27.763
N1+


ATOM
79
N
ILE
548
−36.281
−20.184
−15.458
N


ATOM
80
CA
ILE
548
−35.436
−19.031
−15.752
C


ATOM
81
CB
ILE
548
−34.664
−19.219
−17.06
C


ATOM
82
C
ILE
548
−36.408
−17.853
−15.822
C


ATOM
83
O
ILE
548
−37.458
−17.886
−16.452
O


ATOM
84
CG1
ILE
548
−33.392
−20.028
−16.883
C


ATOM
85
CG2
ILE
548
−34.252
−17.907
−17.69
C


ATOM
86
CD1
ILE
548
−33.627
−21.413
−16.336
C


ATOM
87
N
VAL
562
−31.795
−7.739
−22.294
N


ATOM
88
CA
VAL
562
−32.342
−8.134
−21.014
C


ATOM
89
CB
VAL
562
−33.499
−9.124
−21.117
C


ATOM
90
C
VAL
562
−31.274
−8.662
−20.068
C


ATOM
91
O
VAL
562
−30.216
−9.164
−20.451
O


ATOM
92
CG1
VAL
562
−34.749
−8.496
−21.679
C


ATOM
93
CG2
VAL
562
−33.149
−10.372
−21.896
C


ATOM
94
N
VAL
564
−31.237
−11.518
−16.699
N


ATOM
95
CA
VAL
564
−31.896
−12.694
−16.127
C


ATOM
96
CB
VAL
564
−32.086
−13.727
−17.235
C


ATOM
97
C
VAL
564
−31.098
−13.219
−14.919
C


ATOM
98
O
VAL
564
−29.92
−12.905
−14.743
O


ATOM
99
CG1
VAL
564
−32.973
−14.887
−16.875
C


ATOM
100
CG2
VAL
564
−30.789
−14.232
−17.825
C


ATOM
101
N
GLU
565
−31.782
−14.111
−14.099
N


ATOM
102
CA
GLU
565
−31.085
−14.734
−12.973
C


ATOM
103
CB
GLU
565
−31.992
−15.005
−11.782
C


ATOM
104
C
GLU
565
−29.941
−15.717
−13.297
C


ATOM
105
O
GLU
565
−29.737
−16.147
−14.431
O


ATOM
106
CG
GLU
565
−32.392
−16.452
−11.541
C


ATOM
107
CD
GLU
565
−31.43
−17.186
−10.607
C


ATOM
108
OE1
GLU
565
−31.684
−18.423
−10.464
O1−


ATOM
109
OE2
GLU
565
−30.465
−16.501
−10.16
O


ATOM
110
N
TYR
566
−29.152
−16.054
−12.215
N


ATOM
111
CA
TYR
566
−27.823
−16.588
−12.406
C


ATOM
112
CB
TYR
566
−26.781
−15.718
−11.724
C


ATOM
113
C
TYR
566
−27.641
−18.044
−11.99
C


ATOM
114
O
TYR
566
−28.024
−18.531
−10.93
O


ATOM
115
CG
TYR
566
−25.444
−15.789
−12.391
C


ATOM
116
CD1
TYR
566
−25.275
−15.305
−13.689
C


ATOM
117
CE1
TYR
566
−24.024
−15.355
−14.299
C


ATOM
118
CD2
TYR
566
−24.353
−16.321
−11.703
C


ATOM
119
CE2
TYR
566
−23.098
−16.379
−12.308
C


ATOM
120
CZ
TYR
566
−22.945
−15.891
−13.6
C


ATOM
121
OH
TYR
566
−21.693
−15.924
−14.174
O


ATOM
122
N
ALA
567
−26.891
−18.744
−12.906
N


ATOM
123
CA
ALA
567
−26.494
−20.101
−12.647
C


ATOM
124
CB
ALA
567
−26.697
−20.945
−13.884
C


ATOM
125
C
ALA
567
−25.023
−20.106
−12.297
C


ATOM
126
O
ALA
567
−24.142
−19.656
−13.025
O


ATOM
127
N
SER
568
−24.777
−20.692
−11.076
N


ATOM
128
CA
SER
568
−23.392
−20.872
−10.669
C


ATOM
129
CB
SER
568
−23.287
−21.156
−9.18
C


ATOM
130
C
SER
568
−22.779
−22.049
−11.436
C


ATOM
131
O
SER
568
−21.589
−22.069
−11.739
O


ATOM
132
OG
SER
568
−23.589
−19.986
−8.424
O


ATOM
133
N
LYS
569
−23.612
−23.14
−11.637
N


ATOM
134
CA
LYS
569
−23.125
−24.243
−12.446
C


ATOM
135
CB
LYS
569
−23.916
−25.503
−12.162
C


ATOM
136
C
LYS
569
−23.157
−23.937
−13.939
C


ATOM
137
O
LYS
569
−22.249
−24.312
−14.674
O


ATOM
138
CG
LYS
569
−23.179
−26.423
−11.212
C


ATOM
139
CD
LYS
569
−21.753
−26.645
−11.661
C


ATOM
140
CE
LYS
569
−21.016
−27.517
−10.675
C


ATOM
141
NZ
LYS
569
−19.648
−27.708
−11.215
N1+


ATOM
142
N
GLY
570
−24.319
−23.373
−14.413
N


ATOM
143
CA
GLY
570
−24.453
−23.038
−15.812
C


ATOM
144
C
GLY
570
−25.524
−23.921
−16.407
C


ATOM
145
O
GLY
570
−26.559
−24.245
−15.824
O


ATOM
146
N
ASN
571
−25.286
−24.249
−17.721
N


ATOM
147
CA
ASN
571
−26.274
−25.077
−18.386
C


ATOM
148
CB
ASN
571
−26.321
−24.743
−19.86
C


ATOM
149
C
ASN
571
−26.109
−26.524
−17.918
C


ATOM
150
O
ASN
571
−25.024
−27.043
−17.664
O


ATOM
151
CG
ASN
571
−25.797
−25.724
−20.862
C


ATOM
152
OD1
ASN
571
−25.578
−26.912
−20.665
O


ATOM
153
N D2
ASN
571
−25.585
−25.128
−22.072
N


ATOM
154
N
LEU
633
−31.139
−24.989
−17.022
N


ATOM
155
CA
LEU
633
−30.144
−24.369
−16.179
C


ATOM
156
CB
LEU
633
−30.509
−22.921
−15.923
C


ATOM
157
C
LEU
633
−29.959
−25.091
−14.857
C


ATOM
158
O
LEU
633
−30.903
−25.516
−14.191
O


ATOM
159
CG
LEU
633
−29.311
−21.997
−15.935
C


ATOM
160
CD1
LEU
633
−28.592
−22.042
−17.263
C


ATOM
161
CD2
LEU
633
−29.768
−20.585
−15.665
C


ATOM
162
N
ALA
643
−36.35
−23.324
−19.23
N


ATOM
163
CA
ALA
643
−36.544
−22.152
−20.052
C


ATOM
164
CB
ALA
643
−35.423
−21.153
−19.88
C


ATOM
165
C
ALA
643
−36.674
−22.565
−21.505
C


ATOM
166
O
ALA
643
−36.305
−23.66
−21.933
O


ATOM
167
N
ASP
644
−37.2
−21.581
−22.31
N


ATOM
168
CA
ASP
644
−37.014
−21.613
−23.75
C


ATOM
169
C
ASP
644
−35.623
−20.964
−23.979
C


ATOM
170
O
ASP
644
−34.857
−20.648
−23.073
O


ATOM
171
CB
ASP
644
−38.16
−20.848
−24.389
C


ATOM
172
CG
ASP
644
−38.22
−20.841
−25.905
C


ATOM
173
OD1
ASP
644
−37.259
−21.446
−26.484
O


ATOM
174
OD2
ASP
644
−39.176
−20.165
−26.375
O1−


ATOM
175
N
PHE
645
−35.297
−20.757
−25.29
N


ATOM
176
CA
PHE
645
−34.1
−20.044
−25.673
C


ATOM
177
CB
PHE
645
−32.96
−21.008
−25.921
C


ATOM
178
C
PHE
645
−34.416
−19.213
−26.908
C


ATOM
179
O
PHE
645
−34.014
−18.058
−27.023
O


ATOM
180
CG
PHE
645
−31.717
−20.552
−25.231
C


ATOM
181
CD1
PHE
645
−31.097
−19.35
−25.573
C


ATOM
182
CD2
PHE
645
−31.156
−21.354
−24.239
C


ATOM
183
CE1
PHE
645
−29.924
−18.956
−24.935
C


ATOM
184
CE2
PHE
645
−29.98
−20.965
−23.603
C


ATOM
185
CZ
PHE
645
−29.366
−19.766
−23.952
C


ATOM
186
N
GLY
646
−35.072
−19.861
−27.936
N


ATOM
187
CA
GLY
646
−35.65
−19.091
−29.017
C


ATOM
188
C
GLY
646
−34.659
−18.179
−29.727
C


ATOM
189
O
GLY
646
−33.522
−18.494
−30.065
O


ATOM
190
N
ALA
648
−33.161
−15.84
−28.383
N


ATOM
191
CA
ALA
648
−32.005
−15.478
−27.595
C


ATOM
192
CB
ALA
648
−32.175
−15.893
−26.152
C


ATOM
193
C
ALA
648
−30.73
−16.122
−28.147
C


ATOM
194
O
ALA
648
−29.621
−15.677
−27.855
O


ATOM
195
N
ARG
649
−30.876
−17.281
−28.889
N


ATOM
196
CA
ARG
649
−29.696
−17.894
−29.479
C


ATOM
197
CB
ARG
649
−29.859
−19.371
−29.767
C


ATOM
198
C
ARG
649
−29.344
−17.17
−30.777
C


ATOM
199
O
ARG
649
−30.151
−16.969
−31.678
O


ATOM
200
CG
ARG
649
−29.749
−20.201
−28.508
C


ATOM
201
CD
ARG
649
−29.878
−21.666
−28.861
C


ATOM
202
NE
ARG
649
−30.114
−22.502
−27.687
N1+


ATOM
203
CZ
ARG
649
−29.201
−22.79
−26.717
C


ATOM
204
NH1
ARG
649
−27.944
−22.278
−26.724
N


ATOM
205
NH2
ARG
649
−29.564
−23.67
−25.761
N









Example 7
The Use of FGFR-2 Inhibition Model in the Fitting and Optimization of a Small Molecular Template
Virtual screening of ArQule's collection of kinase inhibitors was carried out using the described FGFR-2 inhibition model. Additional filters were applied for compound selection: molecular weight between 250 and 350, number of hetero atoms less or equal 5, number of hydrogen bonds donors less or equal 3, AlogP less than 5.
Docking and optimization against the FGFR-2 inhibition model was performed. The docking procedure was carried out using ICM software. Further optimization was carried out using MOE energy minimization tools.
ARQ13194808, a racemic mixture of two enantiomers, was identified from this virtual screening (MW 342, logP 4.17). Individual enantiomers were optimized in the model binding site. A single enantiomer was determined to have a preferential binding interaction.
Hydrogen bonds between the pyridine and the critical amino and carbonyl groups of the hinge residue A567 were identified. The fused benzene ring makes aromatic interactions with the F492 from the P-loop.
The overall protein-ligand interaction energy was negative (−40 kcal/mol) and the compounds energy was low (37 kcal/mol) just 3 kcal/mol above the energy minimum in the absence of the protein, as it is calculated using MOE energy calculation tools, indicating a high probability of interaction.
Based on the analysis of these results, ARQ13194808 could be selected as a starting point for designing a FGFR-2 kinase inhibitor.
(−)-trans-3-(5,6-dihydro-4H-pyrrolo[3,2,1-ij]quinolin-1-yl)-4(1H-indol-3-yl)pyrrolidine-2,5-dione, the selective c-Met inhibitor, was also docked in the FGFR-2 inhibition model. A docking pose, where the pyrrolidine carbonyl ring was making hydrogen bonds with the amino group of A567, was selected.
Further energy optimization using MOE tools was carried out. Two hydrogen bonds where observed between the pyrrolidine ring and hinge residue A567. The overall interaction energy is negative (−37 kcal/mol) and the compound's energy is equal to 51 kcal/mol, which is 5 kcal/mol above the energy minimum in the absence of the protein.
Example 8
Cloning, Expression and Purification of c-Met2
As used herein, the c-Met protein of Table 1A is related to the cMet1 protein. cMet1 contains a mutation at residue position 1166, a substitution of glutamine for arginine. Wild type cMet, which has the same sequence as cMet2 of the present application, contains an arginine residue at position 1166. cMet1 contains a glutamine residue at position 1166. Tables 1B and 4, relate to the cMet2 protein. Table 1B provides the complete sequence and atomic structure of the cMet2/the selective cMet inhibitor complex.
The DNA fragment encoding the kinase domain (1038-1346) of cMet was PCR amplified using full length human cDNA with primers designed to contain a non-cleavable N-terminus 6×His tag. The resulting DNA fragment was inserted into pET28a vector between NcoI and SalI sites. A bicistronic form of this vector was designed for co-expression with phosphatase by sequentially inserting the PTP1B gene (1-283) between Sal1 and Not1 sites. A second ribosome binding site was incorporated into the PTP1B primer after the Sal1 site. The construct generated initially contained a random mutation in cMet gene at position 1166 (Arginine to Glutamine), which was corrected to the wild-type form using site-directed mutagenesis kit (Stratagene). All constructs and mutants were verified by sequencing the entire coding region from both 5′ and 3′ directions. Plasmids were transformed into E. Coli strain BL21 (DE3)-RILP cells. The culture was grown at 25° C. in 2×YT medium up to an A600 of 0.6 when overexpression of cMet protein was induced with 0.25 mM IPTG at 12° C. The incubation continued at 12° C. for 16 h before harvesting. Frozen cell pastes suspended in lysis buffer (50 mM Tris pH 8.5, 150 mM NaCl, 0.01% 2-mercapto ethanol, 30 mM imidazole, 1 mM PMSF, 100 μg/ml lysozyme, 10 μg/ml DNAase-1) were lysed by using Branson 450D sonifier on ice at 60% power. The lysate was clarified by centrifugation at 30,000×g at 4° C. for 45 min, and the supernatant loaded onto a 10 ml Ni-Chelating Sepharose column (GE Healthcare). The column washed with 25 mM Tris pH 8.5, 100 mM NaCl, 0.01% 2-mercapto ethanol, 30 mM imidazole, pH 8.5 and the unphosphorylated cMet was eluted with 500 mM imidazole in the same buffer. cMet protein was further purified with an anion exchange column, Fast Trap QFF 5 ml column (GE Healthcare), after dialysis with 25 mM Tris pH 8.5 and 10% glycerol. Eluted protein was concentrated to 20 mg/ml and stored at −80° C. in buffer composed of 25 mM Tris pH 8.5, 100 mM NaCl, 0.1% 2-mercaptoethanol and 10% glycerol.
Crystallization of cMet2 in Complex with the Selective c-Met Inhibitor
Co-crystals of unphosphorylated cMet kinase domain and the selective c-Met inhibitor were grown by the hanging drop vapor diffusion method at 4° C. using a drop size of 1 μl from 12% ethanol, 14% ethylene glycol and 0.1M imidazole buffer, pH 8.5. For cMet/the selective c-Met inhibitor complex preparation, 10 mM the selective c-Met inhibitor solution was prepared in 50% DMSO/water, diluted to 1.2 mM with buffer solution (25 mM Tris pH 8.5, 100 mM NaCl), and immediately mixed in equal volumes with cMet (20 mg/ml). The complex was incubated on ice for 30 min and centrifuged at 13,000×g prior to crystallization. Large single crystals suitable for data collection were obtained after microseeding from thin needle-like clusters generated from initial screening. Crystals were harvested into a cryoprotected solution of 12% ethanol, 20% ethylene glycol, 10% glycerol and 0.1M imidazole buffer, pH 8.5, and flash-frozen in liquid nitrogen. X-ray diffraction data were collected at beamline X29 of the National Synchrotron Light Source (Brookhaven, N.Y.) on a CCD detector under cryogenic temperature. The diffraction data was integrated, processed and scaled using HKL2000 at NSLS site. The crystals belong to P1 space group with unit cell dimension of a=53.47 Å, b=58.67 Å, c=64.96 Å, α=88.41, β=68.10, γ=85.52, and contain two molecules of cMet in the asymmetric unit with solvent content of 46%.
The structure was determined by molecular replacement utilizing MOLREP as implemented in CCP4 package. The atomic coordinates of the published cMet structure 2G15 was used as search model and the activation and p-loop residues were deleted from the model. The initial electron density map for the selective c-Met inhibitor, P-loop and activation loop regions were well resolved, leaving no ambiguities for the binding mode of the inhibitor. Structure refinement consisted of iterative cycles of model building in Coot, followed by simulated annealing, B-factor minimization, and restrained B-factor refinement in CNX. The residues for activation loop, P-loop and the N-terminal regions different from the initial model were built during the refinement process. The selective c-Met inhibitor conformation was identical in both copies of cMet and was built during the final stages of refinement. Water molecules were added based on Fo-Fc maps (3σ) with density recapitulated in 2Fo-Fc maps (1σ). All waters satisfy the hydrogen-bonding criteria as implemented in the CNX programs Waterpick and Waterdelete. Final rounds of refinement were performed using REFMAC5 restrained refinement protocol. The final model consists of two copies of cMet with residues from 1046 to 1346, two selective c-Met inhibitor molecules and 600 hundred water molecules with crystallographic R value of 19.8% (Rfree=25.9%). The data collection and refinement statistics are summarized in Table 8.







TABLE 8





Diffraction data and refinement statistics







Data collection










Space group
P1



Cell dimensions a, b, c (Å)
53.47, 58.67, 64.96



Cell angles α, β, γ (deg)
88.41, 68.10, 85.52



Resolution (Å)
50.0-1.93



Unique reflections
47320



Completeness
93% (96%)



Rsym 
0.102 (0.28)



Mean I/σ(I)
6.9



Redundancy
2







Refinement










Ra
0.198



Rfree
0.259



RMSD Bond distance (Å)
0.018



RMSD Bond angle (deg)
1.951







aR and Rfree = (Σ|Fobs−Fcalc|)/(Σ|Fobs|). Rfree was calculated over randomly chosen 5% of the reflections not used in refinement. Parentheses indicate the outer resolution shell.






Other embodiments are within the following claims. While several embodiments have been shown and described, various modifications may be made without departing from the spirit and scope of the present invention.

## Claims

1. A crystal comprising a ligand complexed with a wild type c-Met kinase domain of SEQ ID NO: 2, wherein the crystal is in space group P1 and having unit cell dimension of a=53.47 Å, b=58.67 Å, c=64.96 Å, α=88.41°, β=68.10° and γ=85.52°.

2. The crystal of claim 1, wherein the crystal diffracts X-rays and the diffraction pattern is solved to produce the three-dimensional structure defined by the atomic coordinates from Table 1B.

3. The crystal of claim 1 wherein the ligand is a selective inhibitor of a wild type c-Met.

4. The crystal of claim 3 wherein the inhibitor is (−)-trans-3-(5,6-dihydro-4H-pyrrolo[3,2,1-ij]quinolin-1-yl)-4(1H-indol-3-yl)pyrrolidine-2,5-dione.