METHODS RELATED TO A STRUCTURE OF HIGH-AFFINITY HUMAN PD-1/PD-L2 COMPLEX

Variants of human PD-1 comprising one or more of amino acid substitutions in residues corresponding to N74, T76 and A132 of SEQ ID NO:1 are described. Also described are structures, obtained using X-ray crystallography, of the human PD-1/PD-L2 complex and mutant PD-1 variants. The structures of human PD-1 described in the present disclosure are useful in drug discovery, including small-molecule drug discovery. Accordingly, methods of using the structures in drug discovery are also described.

Skip to: Description  ·  Claims  · Patent History  ·  Patent History
Description
CROSS REFERENCE TO RELATED APPLICATIONS

This application is a continuation of U.S. patent application Ser. No. 16/786,409, filed Feb. 10, 2020, which claims the benefit of U.S. Provisional Application No. 62/904,515, filed Sep. 23, 2019, and U.S. Provisional Application No. 62/907,335, filed Sep. 27, 2019. All of the foregoing applications are incorporated by reference in their entirety herein.

STATEMENT AS TO RIGHTS TO INVENTIONS MADE UNDER FEDERALLY SPONSORED RESEARCH AND DEVELOPMENT

This invention was made with Government support under Contracts DA043893 and GM103393 awarded by the National Institutes of Health and DE-AC02-76F00515 awarded by the U.S. Department of Energy. The government has certain rights in the invention.

BACKGROUND

Immune checkpoint blockade of programmed death 1 (PD-1) and its ligand 1 (PD-L1) has dramatically increased progression-free survival for many cancers (1-3). For example, a monoclonal antibody (mAb) drug, pembrolizumab (Keytruda®), received regulatory approval for use in patients with microsatellite instability-high (MSI-H) or mismatch repair deficient (dMMR) solid tumors (4, 5). While mAb drugs inhibiting immune checkpoints are highly useful in oncology, there is a desire for other types of inhibitors of immune checkpoints, such as small-molecules. Small-molecule drugs targeting PD-1 may lead to increases in efficacy and safety of cancer treatment, as well to improved access to cancer treatments.

SUMMARY

Other than mAbs, compounds targeting human PD-1 so far have been out of reach. Development of human PD-1-binding drugs is hindered by the fact that the ligand-binding surface of human PD-1 is generally flat, lacking identifiable binding pockets that can serve as drug targets during computational screening of small molecule libraries and computational drug modelling efforts. Only a small cavity forms when human PD-1 binds one of its in-vivo ligands, PD-L1. The small volume of the PD-L1 binding cavity in human PD-1 prevents its use for computational modelling of PD-1 interactions with its ligands. While it is known that, in murine PD-1, the PD-L1-binding cavity extends upon binding of a different in-vivo ligand, PD-L2, the cavity of murine PD-1 cannot provide a structural model due to low sequence similarity between human and murine PD-1 proteins. As described in more detail further in the present disclosure, the inventors were able to design a substituted variant of human PD-1 that binds PD-L2 with an affinity that is two orders of magnitude higher than that of the wild-type protein, and to crystallize and, using X-ray crystallography, determine to high resolution the structures of the human PD-1 variant and the complex of the human PD-1 variant with PD-L2. As a result, a prominent pocket on the ligand-binding surface of human PD-1 was identified. The structure of the PD-L2 binding pocket of human PD-1 is described in the present disclosure. The structure of the PD-L2 binding pocket of human PD-1 is useful, for example, in the drug discovery, design and optimization methods, such as, but not limited to, the methods that involve computational (in silico) screening of small molecule libraries for candidate small molecules capable of binding to of the PD-L2 binding pocket of human PD-1, the methods that involve computational identification of ligands capable of interacting with the PD-L2 binding pocket of human PD-1, and any methods that involve computational docking of ligands to the PD-L2 binding pocket of human PD-1. Such methods are included among the embodiments of the present invention and are described in the present disclosure.

The terms “invention,” “the invention,” “this invention” and “the present invention,” as used in this document, are intended to refer broadly to all of the subject matter of this patent application and the claims below. Statements containing these terms should be understood not to limit the subject matter described herein or to limit the meaning or scope of the patent claims below. Covered embodiments of the invention are defined by the claims, not this summary. This summary is a high-level overview of various aspects of the invention and introduces some of the concepts that are described and illustrated in the present document and the accompanying figures. This summary is not intended to identify key or essential features of the claimed subject matter, nor is it intended to be used in isolation to determine the scope of the claimed subject matter. The subject matter should be understood by reference to appropriate portions of the entire specification, any or all figures and each claim. Some of the exemplary embodiments of the present invention are discussed below.

Included among the embodiments of the present invention are proteins comprising a ligand binding pocket with a three-dimensional structure corresponding to a structure of PD-L2 binding pocket of a variant of human PD-1 with one or more of amino acid substitutions in residues corresponding to N74, T76 or A132 of SEQ ID NO:1. A variant of human PD-1 can further comprises amino acid substitutions removing one or more N-linked glycosylation sites. In a protein according to the embodiments of the present invention, the one or more of the amino acid substitutions are two or three amino acid substitutions. The amino acid substitutions can be N74G, T76P or A132V. The amino acid substitutions can be N74G, T76P, A132V or A132L. A protein according to the embodiments of the present invention can comprise amino acid substitutions N74G, T76P and A132L. A protein according to the embodiments of the present invention amino acid substitutions N74G and A132V. A protein according to the embodiments of the present invention can be a variant of human PD-1. In a protein according to the embodiments of the present invention, the PD-L2 binding pocket of the variant of human PD-1 can include bound PD-L2. In a protein according to the embodiments of the present invention, a ligand binding pocket can form upon binding of a non-PD-L2 ligand to the protein. The non-PD-L2 ligand can be a small-molecule ligand. In a protein according to the embodiments of the present invention, a binding pocket can exist in the absence of a bound ligand. Embodiments of the present invention encompass crystal forms of the proteins described in the present disclosure.

Also included among the embodiments of the present invention are variants of human PD-1, wherein the variant of human PD-1 comprising one or more of amino acid substitutions in residues corresponding to N74, T76 and A132 of SEQ ID NO:1. A variant of human PD-1 can be in crystal form. A variant of human PD-1 according to the embodiments of the present invention can include two or three amino acid substitutions. The amino acid substitutions can be N74G, T76P or A132V. In an exemplary embodiment, a variant of human PD-1 includes amino acid substitutions N74G, T76P and A132L. In another exemplary embodiment, a variant of human PD-1 includes amino acid substitutions N74G and A132V. A variant of human PD-1 can further include amino acid substitutions removing one or more N-linked glycosylation sites. A variant of human PD-1 can be capable of binding PD-L2 or be bound to PD-L2.

Also included among the embodiments of the present invention are methods for identifying a small molecule capable of binding to PD-L2 binding pocket of human PD-1. A method according to the embodiments of the present invention can comprise the steps of: I) screening small molecule libraries using in silico docking for candidate small molecules that are identified based on a docking score being above a threshold for binding to a binding pocket with a three-dimensional structure corresponding to a structure of the PD-L2 binding pocket of human PD-1; and II) evaluating the candidate small molecules identified in step (I) through one or more in vitro or in vivo assays for their ability to bind to surface residues of the PD-L2 binding pocket of human PD-1 to thereby identify the small molecule capable of binding to the PD-L2 binding pocket of human PD-1. In a method, the candidate small molecules can be identified as binding with the PD-L2 binding pocket of human PD-1 via the docking score that includes one or more interactions of (a) to (k): a) the candidate small molecules interact via hydrogen bonds with one or more amino acid residues in the PD-L2 binding pocket of human PD-1; b) the candidate small molecules interact via hydrogen bonds with the PD-L2 binding pocket of human PD-1; c) the candidate small molecules interact via ionic interactions with one or more amino acid residues in the PD-L2 binding pocket of human PD-1; d) the candidate small molecules interact via ionic interactions with the PD-L2 binding pocket of human PD-1; e) the candidate small molecules interact via one or more water molecules with one or more amino acid residues in the PD-L2 binding pocket of human PD-1; f) the candidate small molecules interact via one or more water molecules with the PD-L2 binding pocket of human PD-1; g) the candidate small molecules interact via π-π interactions with one or more amino acid residues in the in the PD-L2 binding pocket of human PD-1; h) the candidate small molecules interact via van der Waals interactions to one or more amino acid residues in the in the PD-L2 binding pocket of human PD-1; i) the candidate small molecules interact via van der Waals interactions with the PD-L2 binding pocket of human PD-1; j) the candidate small molecules interact via steric interactions to one or more amino acid residues in the in the PD-L2 binding pocket of human PD-1; k) the candidate small molecules interact via steric interactions with the PD-L2 binding pocket of human PD-1. In some embodiments, the candidate small molecules are not endogenous ligands of human PD-1. In some embodiments, the candidate small molecules have 1, 2, 3, 4, 5, 6, 7, 8, 9, 10 or 11 of the interactions (a)-(k). In some embodiments, the candidate small molecules bind via 1-20 hydrogen bonds to one or more amino acid residues in the PD-L2 binding pocket of human PD-1. In some embodiments, the candidate small molecules bind via 1-20 hydrogen bonds to the PD-L2 binding pocket of human PD-1. In some embodiments, the candidate small molecules bind via 1-20 water molecules in the PD-L2 binding pocket of human PD-1. In some embodiments, the candidate small molecules bind via 1-20 water molecules to one or more amino acid residues in the PD-L2 binding pocket of human PD-1. In some embodiments, a model of the structure of the PD-L2 binding pocket of human PD-1 is computationally derived from crystallographic data. In some embodiments, model of the PD-L2 binding pocket of human PD-1 is computationally derived from crystallographic data obtained using crystals of a variant of human PD-1 according to the embodiments of the present invention and described elsewhere in the present disclosure. In some embodiments of the methods, in silico docking comprises computational docking three-dimensional structures of small molecules from the small molecule libraries onto surface exposed amino acid residues of the model of the PD-L2 binding pocket of human PD-1. In some embodiments, the surface exposed amino acid residues comprise one or more amino acids corresponding to F63, V64, N66, Y68, E84, L122, I126, I134 or E136 of SEQ ID NO:1. In some embodiments, the computational docking comprises sampling, scoring, and binning of docking scores of a plurality of docked orientations of the small molecules relative to the model of the PD-L2 binding pocket of human PD-1. In some embodiments, the computation docking further comprising assigning a distance cutoff to match atoms of the small molecules to exposed atoms of the PD-L2 binding pocket of human PD-1. The exposed atoms can include one or more of CB of F63, CE1 of F63, CD1 of F63, CE1 of F63, CG2 of V64, CG2 of V64, O of V64, ND2 of N66, ND2 of N66, CE1 of Y68, OH of Y68, OE1 of E84, OE2 of E84, OE2 of E84, OE1 of E84, OE2 of E84, OE1 of E84, CD1 of L122, CG2 of I126, CD1 of I126, CD1 of I126, CG2 of I126, CD1 of I126, CB of I134, CG1 of I134, CG1 of I134, CD1 of I134, CD1 of I134, OE2 of E136, OE2 of E136 or OE2 of E136, wherein numbering of amino acids containing the exposed atoms is based on SEQ ID NO:1. In some embodiments, the scoring comprises determining, for complexes of the small molecules and the PD-L2 binding pocket of human PD-1, one or more of binding forces, configurational entropy, local minimal in Gibbs free energy landscape, or energy barriers between the local minima of the Gibbs free energy landscape, or combinations of two or more thereof.

Also described herein and included among the embodiments of the present invention are in silico method of identifying a compound that binds to PD-L2 binding pocket of human PD-1. The methods can comprise the steps of: (a) receiving, by a computer system, information on a three-dimensional structure of PD-L2 binding pocket of human PD-1 comprising a plurality of amino acids; (b) receiving, by the computer system, information on a three-dimensional structure of a candidate compound; (c) using the computer system and the information received into the computer system in steps (a) and (b), performing one or more of molecular dynamic simulations, kinetic Monte Carlo (KMC) simulations, direct simulations Monte Carlo (DSMC), or density functional theory (DFT) simulations to determine if the candidate compound binds to the PD-L2 binding pocket of human PD-1, thereby identifying the compound that binds to PD-L2 binding pocket of human PD-1. In the above methods, the three-dimensional structure of the PD-L2 binding pocket of human PD-1 can be computationally derived from crystallographic data. The crystallographic data can be obtained using crystals of a variant of human PD-1 according to the embodiments of the present invention and described elsewhere in the present disclosure. In a method according to the embodiments of the present invention, step (c) can include computational docking of small molecules from small molecule libraries onto surface exposed amino acid residues of the three-dimensional structure of the PD-L2 binding pocket of human PD-1. The surface exposed amino acid residues can include one or more amino acids corresponding to F63, V64, N66, Y68, E84, L122, I126, I134 or E136 of SEQ ID NO:1. In a method according to the embodiments of the present invention, step (c) can include determining, using the computer system, a docking score of the candidate compound to the PD-L2 binding pocket of human PD-1. The determining of the docking score can include sampling, scoring and binning of docking scores of a plurality of docked orientations of the small molecules relative to the model of the PD-L2 binding pocket of human PD-1, and assigning a distance cutoff to match atoms of the small molecules to exposed atoms of the PD-L2 binding pocket of human PD-1. The exposed atoms can include one or more of CB of F63, CE1 of F63, CD1 of F63, CE1 of F63, CG2 of V64, CG2 of V64, O of V64, ND2 of N66, ND2 of N66, CE1 of Y68, OH of Y68, OE1 of E84, OE2 of E84, OE2 of E84, OE1 of E84, OE2 of E84, OE1 of E84, CD1 of L122, CG2 of I126, CD1 of I126, CD1 of I126, CG2 of I126, CD1 of I126, CB of I134, CG1 of I134, CG1 of I134, CD1 of I134, CD1 of I134, OE2 of E136, OE2 of E136 or OE2 of E136, wherein numbering of amino acids containing the exposed atoms is based on SEQ ID NO:1. In a method according to the embodiments of the present invention, step (c) can include determining, for the complexes of the compound and the PD-L2 binding pocket of human PD-1, one or more of binding forces, configurational entropy, local minimal in Gibbs free energy landscape or energy barriers between the local minima of the Gibbs free energy landscape, or combinations of two or more thereof.

Also included among the embodiments of the present invention are methods for identifying interactions between a ligand and a PD-L2 binding pocket of human PD-1. A method according to the embodiments of the present invention cam comprise the steps of: (a) receiving, by a computer system, test ligand molecular data corresponding to a test ligand that is a candidate drug; (b) receiving, by the computer system, protein molecular data corresponding to a three-dimensional structure of PD-L2 binding pocket of human PD-1; (c) calculating an interaction score between the PD-L2 binding pocket of human PD-1 and the candidate drug. In A method according to the embodiments of the present invention can further comprise a step of comparing the interaction score to a threshold score to determine whether or not an interaction exists between the PD-L2 binding pocket of human PD-1 and the candidate drug. An interaction score can be determined for each of a plurality of test ligands, including the test ligand, and the method can further comprise the steps of: determining a ranking the plurality of the interactions scores; and comparing the ranking of the test ligand to a threshold to determine whether or not an interaction exists between the PD-L2 binding pocket of human PD-1 and the candidate drug. In a method according to the embodiments of the present invention, step (c) can include performing one or more of molecular dynamic simulations, kinetic Monte Carlo (KMC) simulations, direct simulations Monte Carlo (DSMC), or density functional theory (DFT) simulations, or combinations of two or more thereof. In a method according to the embodiments of the present invention, step (c) can include determining, for the complexes of the test ligand and the PD-L2 binding pocket of human PD-1, one or more of binding forces, configurational entropy, local minimal in Gibbs free energy landscape, or energy barriers between the local minima of the Gibbs free energy landscape. In a method according to the embodiments of the present invention, the three-dimensional structure of the PD-L2 binding pocket of human PD-1 is computationally derived from crystallographic data. The crystallographic data can be obtained using crystals of a variant of human PD-1 according to the embodiments of the present invention and described elsewhere in the present disclosure. In a method according to the embodiments of the present invention, step (c) can include computational docking of small molecules from the small molecule libraries onto surface exposed amino acid residues of the model of the PD-L2 binding pocket of human PD-1. The surface exposed amino acid residues can comprise one or more amino acids corresponding to F63, V64, N66, Y68, E84, L122, I126, I134 or E136 of SEQ ID NO:1. In a method according to the embodiments of the present invention, step (c) can include determining, using the computer system, a docking score of the candidate compound to the PD-L2 binding pocket of human PD-1. The determining of the docking score can include sampling, scoring and binning of docking scores of a plurality of docked orientations of the small molecules relative to the model of the PD-L2 binding pocket of human PD-1, and assigning a distance cutoff to match atoms of the small molecules to exposed atoms of the PD-L2 binding pocket of human PD-1. The exposed atoms can include one or more of CB of F63, CE1 of F63, CD1 of F63, CE1 of F63, CG2 of V64, CG2 of V64, O of V64, ND2 of N66, ND2 of N66, CE1 of Y68, OH of Y68, OE1 of E84, OE2 of E84, OE2 of E84, OE1 of E84, OE2 of E84, OE1 of E84, CD1 of L122, CG2 of I126, CD1 of I126, CD1 of I126, CG2 of I126, CD1 of I126, CB of I134, CG1 of I134, CG1 of I134, CD1 of I134, CD1 of I134, OE2 of E136, OE2 of E136 or OE2 of E136, wherein numbering of amino acids containing the exposed atoms is based on SEQ ID NO:1.

In some embodiments of the methods described in the present disclosure, a candidate compound, such as a candidate small molecule, can be a candidate anti-cancer drug. The methods can therefore include testing the candidate anti-cancer drug in an in vitro or in vivo assay to determine its anti-cancer efficacy. The methods can also include determining toxicity of the candidate anti-cancer drug. The methods can also include determining if the candidate anti-cancer drug has an off-target effect. The toxicity or the off-target effect can be determined by an in vitro assay, by an in vivo assay, in silico, or by a combination of two or more thereof. The methods can also include optimizing the candidate anti-cancer drug. For example, the candidate anti-cancer drug can be optimized to one or more of: reduce an off-target effect, reduce toxicity, increase or decrease binding affinity for the PD-L2 binding pocket of human PD-1, decrease binding affinity for the PD-L2 binding pocket of human PD-1. Also included among the embodiments of the present invention are computer products comprising a non-transitory computer readable medium storing a plurality of instructions that when executed control a computer system to identity protein-drug interactions by performing the methods according to the embodiments of the present invention.

BRIEF DESCRIPTION OF THE FIGURES

FIGS. 1A and 1B schematically illustrates the X-ray crystal structure of the human PD-1/PD-L2 complex. FIG. 1A shows a space-filling and ribbon diagram overlay of the human PD-1N74G T76P A132V (dark grey)/PD-L2IgV (light grey)), showing the overall architecture of the human PD-1/PD-L2 complex. FIG. 1B shows a ribbon diagram of a ˜180° rotation view of the ribbon diagram shown in FIG. 1A. Substitutions of N74G, T76P, and A132V are labeled and their sidechains are indicated with sticks. The β-sheets on the interacting faces of each protein are labeled.

FIGS. 2A, 2B and 2C schematically illustrate the formation of a prominent pocket in human PD-1 upon binding PD-L2. FIGS. 2A and 2B show the close-up views of space-filling models of apo-human PD-1N74G T76P A132V (FIG. 2A), and human PD-L2-bound human PD-1N74G T76P A132V overlaid with pocket-residues in sticks (FIG. 2B). The pocket shown in FIG. 2B adopts a funnel-shaped architecture (left: entrance, and right: end) with a volume measured as 130 Å3. FIG. 2C shows a space-filling models of pockets of human PD-L2-bound human PD-1N74G T76P A132V with a ribbon diagram of the PG of PD-L2. The PD-L2 interacting-residues are overlaid in sticks and labeled with an L2 subscript. A 130 Å3 funnel-shaped pocket (left, entrance; right, exit) when human PD-1 binds PD-L2

FIGS. 3A and 3B schematically illustrate a model for conformational coupling for PD-L2 binding to PD-1. Schematic cartoon model shown in FIG. 3A is that of human PD-1 with a flat interface (left) in equilibrium with the PD-L2-bound conformation in the absence of PD-L2 (middle). Schematic cartoon model shown in FIG. 3B is that of the PD-1 loop variant with increased population of the PD-L2-bound conformations in the absence of PD-L2. For clarity, only two of the states in the conformational ensembles are depicted in the schematic cartoon models. Crosses indicate the loop substitutions. Binding of PD-L2 stabilizes the bound conformation of PD-1 (right).

FIGS. 4A and 4B show ribbon diagrams schematically illustrating human PD-1/PD-L2 binding interface. FIGS. 4A and 4B show ribbon diagrams of human PD-1/PD-L2 interface overlaid with interacting residues in sticks. ˜180° rotation between views shown in FIGS. 4A and 4B.

FIGS. 5A, 5B, 5C and 5D show ribbon diagrams schematically illustrating human PD-1/PD-L2 binding interface. FIGS. 5A and 5B show close-up ribbon diagrams of the localizations of the loop substitutions overlaid in sticks of the mutated G74, P76 (FIG. 5A), and V132 (FIG. 5B) in the human PD-1/PD-L2 structure. The PD-L2 residues are overlaid in sticks and labeled with an L2 subscript. P76 of the CC′ loop of PD-1 localizes in between sidechains of Y112L2 and Y114L2. V132 of the FG loop localizes to a groove of T56L2 S58L2 I103L2 and I105L2. FIGS. 5C and 5D show close-up ribbon diagrams of the localizations of the loop substitutions overlaid in sticks of N74, T76 (FIG. 5C), and A132 (FIG. 5D) in the human PD-1/PD-L1 structure (PDB: 4ZQK). The PD-L1 residues are overlaid in sticks and labeled with an L1 subscript. Compared to PD-L2, the corresponding Y114L2 is substituted by R125L1. A132 of the FG loop localizes to a groove of I54L1, Y56L1, Q66L1, and M115L1 in PD-L1.

FIG. 6 is a schematic illustration of a system for performing exemplary methods according to the embodiments of the present invention.

 DETAILED DESCRIPTION

PD-1 is a receptor expressed by T cells, B cells, and monocytes, and is a potent regulator of immune responses (16). PD-1 is an attractive target for anti-cancer pharmaceuticals. PD-1 has two known protein ligands in vivo, PD-L1 and PD-L2, which bind to the same region on the surface of PD-1. It would be desirable to identify other ligands, including, but not limited to small molecule compounds, that would bind to this region of human PD-1 and interfere with its binding to PD-L1 and/or PD-L2. Such ligands, once identified, may be used as lead compounds for drug development and tested for potential biological activity, such as anti-cancer activity, by suitable in vitro and/or in vivo assays. However, it is currently impossible to identify in silico the ligands that would specifically and efficiently bind to PD-1 ligand-binding site, because the PD-1 ligand-binding site lacks a defined binding pocket in the absence of its in vivo ligands. Although the structure of human PD-1/PD-L1 complex has been determined, and a model of PD-L1 binding cavity of human PD-1 exists, the volume of PD-1 binding cavity in the above model is too small for the model to be used effectively in computational studies of PD-1/ligand interactions. As a consequence, until the discoveries described in the present disclosure, effective computational of PD-1/ligand interactions were intractable, making it impossible, for example, to pre-select a reasonable number of lead ligands, such as small-molecule compounds for further testing with in vitro and/or in vivo assays for PD-1 signaling in order to identify biologically active ligands that can be used as drug candidates in pre-clinical and/or clinical testing. The absence of a model of binding PD-1/PD-L1 binding cavity also prevented in silico rational drug design and optimization studies.

The available structures of murine PD-1/PD-L1 and PD-1/PD-L2 complexes showed that a modest binding cavity was formed upon PD-L1 binding, and the cavity extended to a volume suitable for small-molecule ligands only upon PD-L2 binding to murine PD-1. However, the model of the structure of murine PD-1/PD-L2 complex is unsuitable for human drug development due to low sequence similarity between the human and murine PD-1 proteins. Since human PD-1 protein has a very mobile structure, all the multiple previous attempts to crystalize human PD-1/PD-L2 complex and determine the structure of PD-1 ligand binding pocket failed. As described in the present disclosure, the inventors were able to stabilize the structure of PD-1/PD-L2 complex by mutating several residues in two mobile loops (CC′ and FG) of PD-1, which increased the affinity of PD-1 for PD-L2. The inventors were then able to crystallize the PD-1/PD-L2 complex and determine the structure of the PD-L2 binding pocket. The model of the structure of human PD-1/PD-L2 binding pocket can now be used for drug discovery and development. One non-limiting example of the drug discovery and development process in which the structure of human PD-1/PD-L2 binding pocket can be used, is a process that involves computational screening of compounds to identify PD-1 ligands (“leads”). In the above process, screened compounds can be small molecules. For example, libraries of small compounds (small-molecule libraries) can be computationally screed according to various procedures, some of which are described in the present disclosure, to identify candidate small molecules capable of binding to a PD-L2 binding pocket of human PD-1. Based on the results of the computational screening, potential leads can be tested by appropriate in vitro and/or in vivo testing to identify the compounds that affect PD-1 signaling. Another non-limiting example in which the structure of human PD-1/PD-L2 binding pocket can be used is a process that involves computational design and testing of candidate ligands (“leads”), which can subsequently be tested by appropriate in vitro and/or in vivo testing to identify the compounds that affect PD-1 signaling. Prior to the determination of the structure, described in the present disclosure, of human PD-1/PD-L2 binding pocket, it was impossible to identify computationally (in silico) the leads for subsequent in vitro and/or in vivo testing identify the compounds that affect PD-1 signaling. Although in vitro and/or in vivo testing without prior in silico lead identification was theoretically possible, it was, in practice, unworkable due to the high costs (including monetary, time, labor and animal lives required for the testing) that would be required to test large numbers of essentially randomly selected compounds with low probability of success. The discoveries described in the present disclosure permit carrying out the processes related to drug discovery, such as, but not limited to, screening of small molecules and rational drug design, in which in vitro and/or in vivo testing of lead compounds can be implement practically and effectively due to the now available capability to perform the initial steps of lead screening and/or design computationally, thereby drastically reducing the number of the leads that need to be tested in vitro and/or in vivo to identify biologically active PD-1 ligands that can serve as drug candidates in subsequent pre-clinical and clinical testing.

An exemplary amino acid sequence of human PD-1  (SEQ ID NO: 1), UniProt database entry Q15116         10         20         30         40  MQIPQAPWPV VWAVLQLGWR PGWFLDSPDR PWNPPTFSPA          50         60         70         80  LLVVTEGDNA TFTCSFSNTS ESFVLNWYRM SPSNQTDKLA          90        100        110        120  AFPEDRSQPG QDCRFRVTQL PNGRDFHMSV VRARRNDSGT         130        140        150        160  YLCGAISLAP KAQIKESLRA ELRVTERRAE VPTAHPSPSP         170        180        190        200 RPAGOFQTLV VGVVGGLLGS LVLLVWVLAV ICSRAARGTI        210        220        230        240  GARRTGQPLK EDPSAVPVFS VDYGELDFQW REKTPEPPVP         250        260        270        280 CVPEQTEYAT IVFPSGMGTS SPARRGSADG PRSAQPLRPE DGHCSWPL

An exemplary amino acid sequence of human PD-1 protein is shown as SEQ ID NO:1. The present disclosure describes, among other things, structures of the human triple-mutant PD-1/PD-L2 complex and the apo triple-mutant PD-1 variant obtained using X-ray crystallography at 2.0 Å and 1.2 Å resolution, respectively. The structures described in the present disclosure revealed that binding of PD-L2 to human PD-1 was accompanied by formation of a prominent pocket in human PD-1, as well as substantial conformational changes of the CC′ and FG loops. The structure of human apo triple-mutant PD-1 revealed that the CC′ loop adopted the ligand-bound conformation, providing support for allostery between the loop and pocket. The structures of human PD-1/PD-L2 described in the present disclosure are useful for design and discovery of small-molecule PD-1 inhibitors. While mAb drugs inhibiting immune checkpoints, such as pembrolizumab, are highly useful in oncology, small-molecule inhibitors of immune checkpoints are highly desirable. Small molecule inhibitors are expected to penetrate more effectively than mAbs in the tumor microenvironment, which can enhance their efficacy (6). In addition, if penetration into the brain is desired, small molecule inhibitors can be effective (7, 8). Also, there are rare but severe immune-related side effects of checkpoint inhibition that call for immediate drug discontinuation (9, 10). Since mAbs have long half-lives in the body (typically, weeks) (11), the treatment of such severe immune-related side effects is primarily supportive. Small-molecule checkpoint inhibitors can offer the potential for convenient dosing (e.g., once a day), while allowing for prompt drug removal, if desired (12). Small-molecule immune checkpoint inhibitors can facilitate treatment of cancers in low- and middle-income countries by reducing production costs and eliminating the need for refrigeration during transportation and storage, as compared to mAbs (13). Despite substantial efforts, currently there are no well-characterized small-molecule ligands for PD-1 (14, 15).

In vivo, PD-1 binds two distinct ligands, PD-L1 (also known as B7-H1 or CD274) and PD-L2 (also known as B7-DC) (16). The ligand-binding surface of human PD-1 is generally flat, lacking pockets considered suitable for binding small molecules (16). However, upon binding to PD-L1, a modest cavity forms on the ligand binding surface of PD-1 (17). A similar cavity is formed in murine PD-1 upon binding PD-L1 (18). When murine PD-1 binds PD-L2 (19), this cavity extends to a volume comparable to that occupied by established small-molecule inhibitors (20, 21). Unfortunately, currently available structure of murine PD-1/PD-L2 complex is insufficient to provide a structural model for the analogous pocket in the human PD-1/PD-L2 complex, as the human and murine PD-1 proteins share sequence identities of only about 63% (22). Although the structure of murine PD-1/PD-L2 complex was determined over a decade ago, the structure of the human complex has not yet been obtained due to various difficulties. Previous attempts to obtain diffraction-quality crystals of human PD-1/PD-L2 complex were unsuccessful.

The inventors realized that formation of cavities on the ligand-binding surface of PD-1 is accompanied by changes in the structures of the CC′ and FG loops. The inventors further realized that substitutions in these loops can have an allosteric effect on the conformations of PD-1 in the pocket region and alter its affinity for PD-L2. Using deep-mutational scanning (24) and yeast-surface display (25), the CC′ and FG loop variants of human PD-1 with enhanced PD-L2 binding were selected. A triple-mutant PD-1 was identified that binds PD-L2 with nanomolar affinity and is amenable to crystallization, both alone and as a complex. The formation of a prominent pocket in human PD-1 upon binding PD-L2 revealed by the X-ray crystal structures described in the present disclosure supports the notion of allostery between the pocket and the CC′ and FG loops. The pocket identified in human PD-1 can serve as a template for virtual drug discovery (26) and opens up additional avenues for the discovery of small-molecule PD-1 inhibitors.

The prominent pocket formed in human PD-1 upon binding PD-L2 has a volume of 130 Å3, comparable to those pockets that bind small-molecule drugs (20, 21, 35). The structure of the pocket in human PD-1 described in the present disclosure is quite distinct from the corresponding pocket in murine PD-1 when bound to PD-L2 (19). The pocket in human PD-1 described in the present disclosure represents an attractive drug target. It is envisioned that a small molecule binding to PD-1 contacting all or many of the residues that form the pocket, particularly F63, V64, N66, Y68, E84, L122, G124, I126, I134, and E136 in a conformation similar to that formed in the complex with PD-L2, as illustrated in FIG. 2B. The structure of human PD-1/PD-L2 complex is useful for virtual drug screening to identify potential lead compounds (see e.g., (26)). In addition, the structures of the indole and phenyl rings and neighboring sidechains of PD-L2 when bound to the pocket, as illustrated in FIG. 2C, are useful for the design of fragment-based screening scaffolds (36, 37).

Conformational changes in the CC′ and FG loops can be coupled to formation of pockets in the ligand-binding interface of PD-1 (FIG. 3). In this model, PD-1 exists in an ensemble of conformations in the absence of ligands, populating predominantly structures containing a flat ligand-binding face (K1<1). PD-1 molecules with a pre-formed pocket have a higher affinity for PD-L2 (i.e., K3>K2). Thermodynamics dictates that K1K3=K2K4, so K4>K1. In this model, the PD-1 loop variants studied here increase K1, and lead to a higher proportion of apo-PD-1 in the PD-L2-bound conformation. The increased association constants (kon) for binding ligands by the mutant PD-1s, as compared to wild-type PD-1 support this model. Such kinetic properties are consistent with an increase fraction of unliganded mutant PD-1 molecules that are in a ligand-bound conformation as compared to wild-type PD-1 (38, 39). In addition, the CC′ loop shifts toward the PD-L2-bound conformation in the apo-PD-1 triple and double mutants. While there are only minimal changes in the pocket of human PD-1, as illustrated in FIG. 2A, the pocket residues and a neighboring FG loop have substantial crystal contacts in the lattice that likely interfere with conformational changes. Such coupling can stabilize the pocket in the absence of a ligand, for example, if the two loops were held in their PD-L2-bound conformations with antibodies or aptamers. Thus, the structures of human PD-1 described in the present disclosure are useful in drug development, such as, but not limited, to small-molecule drug discovery, such as by high-throughput screening (40, 41), and rational drug design. The structures described in the present disclosure can be used to discover, design and/or optimize PD-1 ligands, including small-molecule ligands, and can also be used in the discovery of allosteric regulators of PD-1 activity.

Terms and Concepts

A number of terms and concepts are discussed below. They are intended to facilitate the understanding of various embodiments of the invention in conjunction with the rest of the present document and the accompanying figures. These terms and concepts may be further clarified and understood based on the accepted conventions in the fields of the present invention. the description provided throughout the present document and/or the accompanying figures. Some other terms can be explicitly or implicitly defined in other sections of this document and in the accompanying figures, and may be used and understood based on the accepted conventions in the fields of the present invention, the description provided throughout the present document and/or the accompanying figures. The terms not explicitly defined can also be defined and understood based on the accepted conventions in the fields of the present invention and interpreted in the context of the present document and/or the accompanying figures.

Further, unless otherwise required by context, singular terms shall include pluralities and plural terms shall include the singular. Generally, nomenclatures used in connection with, and techniques of, cell and tissue culture, molecular biology, immunology, microbiology, genetics and protein and nucleic acid chemistry are those well-known and commonly used. Known methods and techniques are generally performed according to conventional methods well known and as described in various general and more specific references that are discussed throughout the present disclosure, unless otherwise indicated. For example, enzymatic reactions and purification techniques are performed according to manufacturer's specifications, as commonly accomplished. The nomenclatures used in connection with the laboratory procedures and techniques described in the present disclosure are those well-known and commonly used.

As used herein, the terms “a”, “an”, and “the” can refer to one or more unless specifically noted otherwise.

The use of the term “or” is used to mean “and/or” unless explicitly indicated to refer to alternatives only or the alternatives are mutually exclusive, although the disclosure supports a definition that refers to only alternatives and “and/or.” As used herein “another” can mean at least a second or more.

As used herein, the amino acid residues are abbreviated as follows: alanine (Ala; A), asparagine (Asn; N), aspartic acid (Asp; D), arginine (Arg; R), cysteine (Cys; C), glutamic acid (Glu; E), glutamine (Gln; Q), glycine (Gly; G), histidine (His; H), isoleucine (Ile), leucine (Leu), lysine (Lys; K), methionine (Met; M), phenylalanine (Phe; F), proline (Pro; P), serine (Ser; S), threonine (Thr; T), tryptophan (Trp; W), tyrosine (Tyr; Y), and valine (Val; V). In the broadest sense, the naturally occurring amino acids can be divided into groups based upon the chemical characteristic of the side chain of the respective amino acids. By “hydrophobic” amino acid is meant either His, Leu, Met, Phe, Trp, Tyr, Val, Ala, Cys or Pro. By “hydrophilic” amino acid is meant either Gly, Asn, Gln, Ser, Thr, Asp, Glu, Lys, Arg or His. This grouping of amino acids can be further sub-classed as follows: by “uncharged hydrophilic” amino acid is meant either Ser, Thr, Asn or Gln. By “acidic” amino acid is meant either Glu or Asp. By “basic” amino acid is meant either Lys, Arg or His.

The term “variant,” when used in the present disclosure in reference to a protein or a polypeptide, encompasses homologues, variants, isoforms, fragments, mutants, modified forms and other variations of the protein, polypeptide or amino acid sequences described in this document. The term “homologous,” “homologues” and other related terms used in this document in reference to various amino acid, are intended to describe a degree of sequence similarity among amino acid sequences, calculated according to an accepted procedure. Homologous sequences may be at least 60%, 65%, 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% 99% or 100% homologous. As used herein, “percent homology” of two amino acid sequences is determined using the algorithm of Karlin and Altschul, which is incorporated into the NBLAST and XBLAST programs, available for public use through the website of the National Institutes of Health (U.S.A.). To obtain gapped alignments for comparison purposes, Gapped BLAST is utilized. When utilizing BLAST and Gapped BLAST programs, the default parameters of the respective programs (e.g.,)(BLAST and NBLAST) are used. “Percent homology” may be used in this document to describe fragments, variants or isoforms of amino acids sequences, but other ways of describing fragments, variants or isoforms may be employed alternatively to or in conjunction with homology.

The term “ligand” and the related terms used in the present disclosure refer to a compound or compounds that form a complex with PD-1 protein. The term “ligand” encompassess all compounds, regardless of their size or origin. For example, inorganic molecules, organic molecules, small molecules, biological molecules, non-biological molecules are all encompassed by the term “ligand.”

The term “interaction” and the related terms refer to a type of physical or chemical interaction of one or more molecular subsets with itself (intramolecular) or other molecular subsets (intermolecular) or with components of an environment (environmental). Interaction types may be either enthalpic or entropic in nature and may reflect either nonbonded or bonded interactions. Examples of nonbonded interaction types include, but are not limited to, electrostatic interactions, van der Waals (or dispersion) interactions between time-varying dipole moments (often related to steric complementarity), short range repulsion between overlapping atomic orbitals, hydrogen bonding, interactions involved with metal ion coordination, or interactions with one or more ordered or structural waters. Other examples of nonbonded interaction types may also include one or more solvation effects such as electrostatic desolvation (including self-reaction field polarization effects, solvent screening in a dielectric medium or interactions with a solvent-based ionic atmosphere), the hydrophobic effect, cavitation energy, and surface tension. Examples of bonded interactions include, but are not limited to, the intramolecular strain associated with distortions of equilibrium bond lengths, angles, torsions, etc., or the energy gap between cis-trans modes or the energy differential associated with changes in chirality of one or more chiral center. Examples of entropic-based interactions include the loss of conformational entropy of molecular subsets (including loss of rotameric entropy for protein side chains) upon binding or the favorable entropy gain obtained by the release of one or more ordered waters. Other more exotic interaction types may include π-π stacking, charge transfer, or other quantum mechanical phenomena.

The term “hydrogen-bonding,” “hydrogen bonds,” and related terms relate to a partially electrostatic attraction between a hydrogen (H) which is bound to a more electronegative atom such as nitrogen (N) or oxygen (O) and another adjacent atom bearing a lone pair of electrons. For example, when it is stated that the nitrogen acts as a “hydrogen bond donor” it means that a hydrogen (H) bound to a nitrogen (N) is donated by the nitrogen as it electrostatically attracted to or accepted by an adjacent atom bearing a lone pair of electrons such as an oxygen. Similarly, when it is stated that an oxygen acts as a “hydrogen bond acceptor,” it means that a hydrogen (H) bound to a more electronegative atom such as nitrogen (N) is electrostatically attracted to or “accepted by” an adjacent atom such as oxygen bearing a lone pair of electrons. Sometimes the hydrogen bonded atoms are called out without explicitly stating the origin and presence of an intermediate hydrogen atom. The term “hydrogen bonding” is used wherever LigPlot Plus software predicts a hydrogen bonding interaction using its algorithm and applied parameters of 3.35 Å for maximum distance between hydrogen bond donor and acceptor. Not all hydrogen bonds may actually be in place simultaneously; this is evident for atoms that are shown to form 4 putative hydrogen bonds, where however, at any given time only 3 hydrogen bonds are chemically possible. In general, although crystal structures such as the co-crystal structural information herein does not directly show or detect hydrogen bonding, the software used to describe the co-crystal does predict such H-bonding exists. Therefore, throughout the disclosure when a H-bond is present and described, it may be said to be “predicted” by software to be present.

The term “ionic bonding” and related terms include a type of chemical bond that involves the electrostatic attraction between oppositely charged ions, and is the primary interaction occurring in ionic compounds.

The term “van der Waals interaction” and related terms include weak, short-range electrostatic attractive forces between uncharged molecules, arising from the interaction of permanent or transient electric dipole moments.

The term “π-π interaction or π-π stacking” and related terms include attractive, noncovalent interactions between aromatic rings that are oriented either roughly parallel or roughly perpendicular (such as in “edge-face” interactions) to each other, since they contain 7C bonds.

The term “steric interactions,” “steric effects” and the related terms describe molecular and/or atomic interactions that may arise in a number of ways. Steric effects are described, for example, in (48). For example, steric effects may result from repulsions between valence electrons or nonbonded atoms, leading to in an increase in the energy of the system. In the formation of a ligand-receptor complex, any group of atoms that is in van der Waals contact with the receptor or the biomolecule can be or is involved in the binding event. If a ligand binding pocket can adjust to any ligand, then no steric effect will be observed. If, however, the binding pocket has limited conformational flexibility, and this flexibility is not equivalent in all directions, then a steric effect will be observed. The steric effect will be dependent on conformational states, and the minimal steric interaction principle will probably be observed. This principle states that a substituent whose steric effect is conformationally variable will prefer a conformation that minimizes steric repulsions and will give rise to the smallest steric strain.

The term “binding site” and related terms refer to an area on the protein wherein a small molecule can interact with such as a region, which can be located on the surface or interior of the protein molecule. The term “pocket,” “binding pocket” or related terms can refer to a cavity on the surface or in the interior of a protein molecule that possesses suitable properties for binding a ligand. Amino acid and other residues (such as co-factors) around a pocket determine its physicochemical characteristics. Residues outside the binding site can also have a long-range effect on the properties of the binding pocket. Binding pocket can have a concave surface presenting amino acid residues in a suitable configuration for binding low molecular weight compounds (which can be referred to as “small molecules”). The mobility of a protein molecule can permit opening, closing, and adaptation of binding pockets to regulate binding processes. The influence of protein flexibility on binding pockets can vary from small changes to an already existent pocket to the formation of a completely new pocket. Pockets and binding sites are described, for example, in (47).

Typically, a set of appropriate molecular descriptors describing each distinct configuration will be used to distinguish one configuration from another. Molecular descriptors may include, but are not limited to, a) chemical descriptors (e.g., element, atom type, chemical group, residue, bond type, hybridization state, ionization state, tautomeric state, chirality, stereochemistry, protonation, hydrogen bond donor or acceptor capacity, aromaticity, etc.); b) physical descriptors (e.g., charge, both formal and partial, mass, polarizability, ionization energy, characteristic size parameters, such as van der Waals [vdW] radii, vdW well depths, hydrophobicity, hydrogen bonding potential parameters, solubility, equilibrium bond parameters relating bond energies to bond geometries, etc.); c) geometrical descriptors (e.g., atomic coordinates, bond vectors, bond lengths, bond angles, bond torsions, suitable structural descriptors for rings, descriptors for molecular surfaces and volumes, such as solvent accessible surfaces and solvent-excluded volumes, etc.); and d) environmental descriptors (e.g., temperature, pH, ionic strength, pressure, etc.). Chemical descriptors may be assigned based on application of one or more rules or concepts of organic (or inorganic, if appropriate) chemistry to represent chemical structures that must at least stipulate basic structural information such as element type and bond connectivity (i.e., minimally which nonhydrogen atoms are connected to one another) but may also contain some form of coordinate information. Such chemical structures may be stored and received in a number of different data representations. One common example of data representation, though many others are also possible, is that of a PDB file. Examples of currently available software programs that can be used to assign chemical descriptors include SYBYL™ from Tripos, Chimera™ from UCSF, and WhatIf′ (for proteins), etc. Correct assignment of chemical descriptors may also include additional input regarding chiral centers and stereochemistry or even environmental factors, such as expected pH as related to assignment of ionization states.

The term “affinity formulation” and the related term refer to the energy model used to calculate approximate quantitative values for a given interaction type for a configuration associated with a molecular combination. Typically, there may be many different affinity formulations for a given interaction type from which to choose. The choice of affinity formulation may affect the amount of error associated with the quantitative approximation of a given interaction type. The choice of affinity formulation may also involve very different levels of modeling sophistication and hence computational complexity. A given affinity formulation may require one or more molecular descriptors for evaluation. Two different affinity formulations for a given interaction type may require a very different set of molecular descriptors, while others may share multiple molecular descriptors in common. For example, electrostatic interactions may be modeled according to an affinity formulation involving the use of a modified form of Coulomb's law with distance-dependent dielectric function as applied to a set of partial charges assigned to atomic centers in each molecular subset via use of a suitable force field. In another example, both electrostatic and electrostatic desolvation interactions may be modeled according to an affinity formulation involving a solution of the Poisson-Boltzmann equation (linear or nonlinear) along with an assumption of point charges embedded in solute spherical cavities with size defined by van der Waal radius of each atom and the solute spheres placed in a homogeneous dielectric medium representing water with and possibly containing an ionic atmosphere. Alternatively, electrostatic interactions may be modeled based on quantum-mechanical solution of electronic ground states for each molecular subset. In most scenarios the modified Coulomb with distance-dependent dielectric formulation will be cheaper to compute but less accurate than a Poisson-Boltzmann-based formulation let alone a full quantum-mechanical solution. As further examples, van der Waals interactions may be modeled according to an affinity formulation based on use of a generalized Lennard-Jones potential or alternatively based on a steric complementarity. Hydrogen-bonding interactions may be modeled according to an affinity formulation based on use of a 12-10 Lennard-Jones potential with an angular weighting function or by rescaling of partial charges and van der Waals radii of hydrogen bond donor and acceptor atoms such as that found in the Amber force field. The hydrophobic effect may be modeled according to an affinity formulation based on the fragmental volume approach or the solvent accessible surface area-based formalism. Intramolecular strain associated with dihedral changes may be modeled according to an affinity formulation based on use of Pitzer potentials or by inverse Gaussian torsional constraints. As yet another example, instead of using a Poisson Boltzmann-based formulation, electrostatic desolvation for a configuration may be modeled via an affinity formulation based on use of a variant of the Generalized Born approximation.

The term “computation strategy” herein refers to the computational technique used to quantitatively evaluate a given affinity formulation for one or more interaction types. The choice of computation strategy may be influenced by the available computational systems, apparatus, means and/or methods, the available memory capacity, and/or computing time constraints. As an example of different computational strategies for the same affinity formulation, consider the electrostatic interaction for target-ligand combination, for which a modified Coulombic affinity formulation with distance-dependent dielectric may be computed according to a computation strategy involving direct summation of pair-wise calculation between all possible pairs of partial charges across the protein and ligand. For a ligand with 100 atoms and a protein with 3000 atoms, this would entail the calculation of 300 K intermolecular distances let alone the number of distinct intramolecular pairs. An alternative computation strategy is to instead utilize a probe grid map approximation, whereby an electrostatic potential function associated with source charges on the protein is evaluated and stored on 3-D grid for coordinate locations enclosing the protein. Then for each ligand charge a corresponding electrostatic potential value is accessed from memory (or other storage) and the direct product of the charge and the potential is then accumulated over all charges in the ligand. This may significantly reduce computational effort especially in the context of screening a molecule library where many molecular combinations may feature the same target protein but different ligands. Of course, the probe grid map approximation may require significant storage in order to reduce numerical errors related to variation of the potential function. Moreover, such an approximation is only suitable when the source charges of the protein do not change positions between different configurations. An alternative for a target protein featuring a flexible binding pocket, may be to use a hybrid computation strategy involving the use of the pair-wise strategy for the portion of the protein containing mobile source charges and the probe grid map strategy for the remainder of the protein. In general, various different computation strategies may be applied to other affinity formulations for other interaction types. On the other hand, the choice of computation strategy may be limited by the nature of the affinity formulation or interaction type in question. For example, it is unlikely that one would a strategy appropriate for evaluation of intermolecular electrostatics interactions to instead compute intramolecular strain components involving bonded interactions. Other types of computational strategies exist than those based on pair-wise (e.g., interactions between pairs of atoms) or map or potential field (e.g., interactions of an atom with a potential field) calculations. For example, the evaluation of a Generalized Born solvation model based on the calculation of either volume integrals over the solvent excluded volume or on the calculation of surface integrals on the solvent accessible surface area. As yet another example, various formulations of bonded interactions may be evaluated according to a computation strategy featuring traversal of an appropriate data structure containing relevant coordinate and bond descriptors.

An “affinity function” is a composition of affinity components each of which corresponds to a combination of an interaction type, an affinity formulation, and a computation strategy. An affinity component may represent interactions for the whole or parts of one or more molecular subsets. An affinity function may contain multiple affinity components relating to the same interaction type. For example, two affinity components may represent the same interaction type but differ in either their affinity formulation and/or their computation strategy. Each distinct molecular configuration for a given molecular combination may produce different quantitative results for an affinity component and hence for the corresponding affinity function. In one embodiment, the analysis of a molecular combination may be based on determination of the configuration with the best value for the affinity function. In other embodiments, multiple favorable values for the affinity function corresponding to molecular configurations associated with one or more potential binding modes may be considered. In yet another embodiment, multiple affinity functions may be computed on one or more configurations of a molecular combination and some decision or action based on their joint consideration, such as for example the scenario of consensus scoring of a small finite number of configurations for each molecular combination explored in the course of screening a molecule library against a target molecule.

The terms “about” and “approximately” as used herein shall generally mean an acceptable degree of error for the quantity measured given the nature or precision of the measurements. Typical, exemplary degrees of error are within 20 percent (%); preferably, within 10%; and more preferably, within 5% of a given value or range of values. Any reference to “about X” specifically indicates at least the values X, 0.95X, 0.96X, 0.97X, 0.98X, 0.99X, 1.01X, 1.02X, 1.03X, 1.04X, and 1.05X. Thus, “about X” is intended to teach and provide written support for a claim limitation of, e.g., “0.98X.” Alternatively, in biological systems, the terms “about” and “approximately” may mean values that are within an order of magnitude, preferably within 5-fold, and more preferably within 2-fold of a given value. Numerical quantities given herein are approximate unless stated otherwise, meaning that the term “about” or “approximately” can be inferred when not expressly stated. When “about” is applied to the beginning of a numerical range, it applies to both ends of the range.

As used herein, the terms “small molecule,” “small organic molecule” and “small inorganic molecule” includes molecules (either organic, organometallic, or inorganic), organic molecules, and inorganic molecules, respectively, which have a molecular weight of more than about 50 Da and less than about 2500 Da. Small organic (for example) molecules may be less than about 2000 Da, between about 100 Da to about 1000 Da, or between about 100 Da to about 600 Da, or between about 200 Da to about 500 Da.

Drug Design and Discovery

Drug design and discovery processes (which can also be referred to as “drug development”) can be divided into the following subprocesses: (1) target validation; (2) lead generation/optimization; (3) preclinical testing; and (4) clinical trials and approval. Target validation includes determination of one or more targets that have disease relevance. Results of the target validation phase might include a determination that the presence or action of the target molecule in an organism causes or influences some effect that initiates, exacerbates, or contributes to a disease for which a cure or treatment is sought. In some cases a natural binder or substrate for the target may also be determined via experimental methods. In the context of the present disclosure, a target is human PD-1 protein, with the examples of disease relevance being cancer start and/or progression, with or without treatment, some exemplary types of cancers being solid tumors and blood cancers, including metastatic cancer and cancers with high microsatellite instability and mismatch-repair deficient cancers. The types of cancers that may be relevant in the context of the present disclosure include, but are not limited to, colorectal cancer, gastrointestinal cancer, including stomach and esophageal cancer, endometrial cancer, breast cancer, prostate cancer, prostate cancer, bladder cancer, thyroid cancer, melanoma, lung cancer, head and neck cancer, including head and neck squamous cell carcinoma, or lymphoma, including Hodgkin lymphoma. Another examples of disease relevance are inherited disorders that lead to increased cancer predisposition, such as the syndromes that include mismatch repair deficiency and/or microsatellite instability, for example, Lynch syndrome.

Lead generation typically involves the identification of lead compounds, i.e., ligands, that can bind to the target molecule and that may alter the effects of the target through either activation, deactivation, catalysis, or inhibition of the function of the target, in which case the lead would be a viewed as a suitable candidate ligand to be used in the drug application process. In the context of the present disclosure, initial leads can be compounds that are identified in silico as being able to bind to a PD-L2 binding pocket of human PD-1 and determined to exert biological activity by in vitro and/or in vivo testing. Lead optimization involves the chemical and structural refinement of lead candidates into drug precursors in order to improve binding affinity to the desired target (human PD-1 in the context of the present disclosure), increase selectivity, and also to address basic issues of toxicity, solubility, and metabolism. Together lead generation and lead optimization can result in one or more chemically distinct leads for further consideration. In preclinical testing, biochemical assays and animal models are used to test the selected leads for various pharmacokinetic factors related to drug absorption, distribution, metabolism, excretion, toxicity, side effects, and required dosages. After the preclinical testing period, clinical trials and approval take place, during which the drug candidates are tested on human subjects for safety and efficacy.

A number of laboratory methods exist for measuring or estimating affinity between a target molecule and a ligand. Often the target might be first isolated and then mixed with the ligand in vitro and the molecular interaction assessed experimentally such as in the myriad biochemical and functional assays associated with high throughput screening. However, such methods are most useful where the target is simple to isolate, the ligand is simple to manufacture and the molecular interaction easily measured, but is more problematic when the target cannot be easily isolated, isolation interferes with the biological process or disease pathway, the ligand is difficult to synthesize in sufficient quantity, or where the particular target or ligand is not well characterized ahead of time. In the latter case, many thousands or millions of experiments might be needed for all possible combinations of the target and ligands, making the use of laboratory methods unfeasible.

While a number of attempts have been made to resolve this bottleneck by first using specialized knowledge of various chemical and biological properties of the target (or even related targets such as protein family members) and/or one or more already known natural binders or substrates to the target, to reduce the number of combinations required for lab processing, this is still impractical and too expensive in most cases. Instead of actually combining molecules in a laboratory setting and measuring experimental results, another approach is to use computers to simulate or characterize molecular interactions between two or more molecules (i.e., molecular combinations modeled in silico). The use of computational methods to assess molecular combinations and interactions is usually associated with one or more stages of rational drug design, whether structure-based, ligand-based, or both.

Computational Methods

Rational drug design can use structural information about drug targets (structure-based) and/or their natural ligands (ligand-based) as a basis for the design of effective lead candidate generation and optimization. In the context of the present disclosure, PD-L2 binding pocket of human PD-1 can serve as a drug target in the drug design process. In some cases, natural ligands PD-L1 and/or PD-L2 can serve as a basis for generating lead candidates. Structure-based rational drug design can utilize a three-dimensional model of the structure for the target. For target proteins or nucleic acids, such structures may be the result of X-ray crystallography/NMR or other measurement procedures or may result from homology modeling, analysis of protein motifs and conserved domains, and/or computational modeling of protein folding or the nucleic acid equivalent.

In the context of the present disclosure, the structure of the target can be a three-dimensional model of the PD-L2 binding pocket of human PD-1 that is computationally derived (generated) from the structures of the PD-L2 binding pocket of human PD-1 described in the present disclosure. For example, the three-dimensional model of the PD-L2 binding pocket of human PD-1 can be computationally derived from atomic coordinates, provided elsewhere in the present disclosure, corresponding to crystals of a variant of human PD-1 comprising amino acid substitutions, such as substitutions in one or more of the residues (for example, each of the residues) corresponding to N74, T76 or A132 of SEQ ID NO:1. In some examples, in addition of a three-dimensional model of the PD-L2 binding pocket of human PD-1 that is computationally derived (generated) from the structures of the PD-L2 binding pocket of human PD-1 described in the present disclosure, structure-based in silico design, testing and/or optimization of human PD-1 ligands can also employ a three-dimensional model of human apo-PD-1 (meaning PD-1 without a ligand) that lacks a PD-2 binding pocket in a process that models formation of the PD-2 binding pocket and ligand-binding. The structure of a ligand may be computationally generated based on natural in vivo ligands, such as PD-1 and/or PD-2, or previously identified ligands. The ligand structure may instead be constructed ab initio from a known 2-D chemical representation using fundamental physics and chemistry principles, for example, when the ligand is not a biopolymer.

Rational drug design may incorporate the use of any of a number of computational components ranging from computational modeling of target-ligand molecular interactions and combinations to lead optimization to computational prediction of desired drug-like biological properties. The use of computational modeling in the context of rational drug design has been largely motivated by a desire both to reduce the required time and to improve the focus and efficiency of drug research and development, by avoiding often time consuming and costly efforts in biological “wet” lab testing and the like.

Computational modeling of target-ligand molecular combinations in the context of lead generation may involve the large-scale in silico screening of compound libraries, such as small-molecule libraries (i.e., library screening), whether the libraries are virtually generated and stored as one or more compound structural databases or constructed via combinatorial chemistry and organic synthesis, using computational methods to rank a selected subset of ligands based on computational prediction of bioactivity (or an equivalent measure) with respect to the intended target molecule.

In the context of the present disclosure, the target molecule is PD-1, and the structure of the target employed in the library screening can be a three-dimensional model of the PD-L2 binding pocket of human PD-1 that is computationally derived (generated) from the structures of the PD-L2 binding pocket of human PD-1 described in the present disclosure. For example, the three-dimensional model of the PD-L2 binding pocket of human PD-1 can be computationally derived from atomic coordinates, provided elsewhere in the present disclosure, corresponding to crystals of a variant of human PD-1 comprising amino acid substitutions, such as substitutions in one or more of the residues (for example, each of the residues) corresponding to N74, T76 or A132 of SEQ ID NO:1. In some examples, in addition of a three-dimensional model of the PD-L2 binding pocket of human PD-1 that is computationally derived (generated) from the structures of the PD-L2 binding pocket of human PD-1 described in the present disclosure, computational library screending of human PD-1 ligands can also employ a three-dimensional model of human apo-PD-1 (meaning PD-1 without a ligand) that lacks a PD-2 binding pocket in a process that models formation of the PD-2 binding pocket and ligand-binding.

Fragment-based drug discovery (FBDD), discussed, for example, in (114) and (115), is another tool for discovering leads for drug development. FBDD first identifies starting points: low-molecular-weight ligands (˜150 Da) (fragments) that bind to a target, for example, human PD-1. The fragments may bind to the target with the very low affinity. The identified fragments may be them grown or combined to produce leads with higher affinity. The three-dimensional binding mode of the fragments may be determined in silico and/or experimentally, using X-ray crystallography or NMR spectroscopy, and is used to facilitate their optimization into leads with higher activity. FBLD can be combined with screening.

Various terms and concepts are employed in computational modeling. For example, “binding mode” refers to the 3-D molecular structure of a potential molecular complex in a bound state at or near a minimum of the binding energy (i.e., maximum of the binding affinity), where the term “binding energy” (sometimes interchanged with “binding free energy” or with its conceptually antipodal counterpart “binding affinity”) refers to the change in free energy of a molecular system upon formation of a potential molecular complex, i.e., the transition from an unbound to a (potential) bound state for the ligand and target. The term “system pose” is also sometimes used to refer to the binding mode. Here the term free energy generally refers to both enthalpic and entropic effects as the result of physical interactions between the constituent atoms and bonds of the molecules between themselves (i.e., both intermolecular and intramolecular interactions) and with their surrounding environment. Examples of the free energy are the Gibbs free energy encountered in the canonical or grand canonical ensembles of equilibrium statistical mechanics.

In general, the optimal binding free energy of a given target-ligand pair directly correlates to the likelihood of combination or formation of a potential molecular complex between the two molecules in chemical equilibrium, though, in truth, the binding free energy describes an ensemble of (putative) complexed structures and not one single binding mode. However, in computational modeling, it is usually assumed that the change in free energy is dominated by a single structure corresponding to a minimal energy. This is certainly true for tight binders (pK ˜0.1 to 10 nanomolar) but questionable for weak ones (pK ˜10 to 100 micromolar). The dominating structure is usually taken to be the binding mode. In some cases, it may be necessary to consider more than one alternative binding mode when the associated system states are nearly degenerate in terms of energy.

Binding affinity is of direct interest to drug discovery and rational drug design because the interaction of two molecules, such as a protein that is part of a biological process or pathway and a drug candidate sought for targeting a modification of the biological process or pathway, often helps indicate how well the drug candidate will serve its purpose. Furthermore, where the binding mode is determinable, the action of the drug on the target can be better understood. Such understanding may be useful when, for example, it is desirable to further modify one or more characteristics of the ligand so as to improve its potency (with respect to the target), binding specificity (with respect to other target biopolymers), or other chemical and metabolic properties.

When computationally modeling the nature and/or likelihood of a potential molecular combination for a given target-ligand pair, the actual computational prediction of binding mode and affinity is customarily accomplished in two parts: (a) “docking”, in which the computational system attempts to predict the optimal binding mode for the ligand and the target and (b) “scoring”, in which the computational system attempts to refine the estimate of the binding affinity associated with the computed binding mode. During library screening, scoring may also be used to predict a relative binding affinity for one ligand vs. another ligand with respect to the target molecule and thereby rank prioritize the ligands or assign a probability for binding.

Docking may involve a search or function optimization algorithm, whether deterministic or stochastic in nature, with the intent to find one or more system poses that have favorable affinity. Scoring may involve a more refined estimation of an affinity function, where the affinity is represented in terms of a combination of one or more empirical, molecular-mechanics-based, quantum mechanics-based, or knowledge-based expressions, i.e., a scoring function. Individuals scoring functions may themselves be combined to form a more robust consensus-scoring scheme using a variety of formulations. In practice, there are many different docking strategies and scoring schemes employed in the context of today's computational drug design.

Whatever the choice of computational method there are inherent trade-offs between the computational complexity of both the underlying molecular models and the intrinsic numerical algorithms, and the amount of computing resources (time, number of CPUs, number of simulations) that must be allocated to process each molecular combination. For example, while highly sophisticated molecular dynamics simulations (MD) of the two molecules surrounded by explicit water molecules and evolved over trillions of time steps may lead to higher accuracy in modeling the potential molecular combination, the resultant computational cost (i.e., time and computing power) is so enormous that such simulations are intractable for use with more than just a few molecular combinations. On the other hand, the use of more primitive models for representing molecular interactions, in conjunction with multiple, and often error-prone, modeling shortcuts and approximations, may result in more acceptable computational cost, but will decrease modeling accuracy and predictive power.

Methods and concepts related to computational aspects of drug discovery and drug design are described in the publications summarized below. The process of high throughput docking and scoring and its applications are discussed in (46) and (49). A general approach to the design, docking, and virtual screening of multiple combinatorial libraries against a family of proteins is described in (50). The use of multiple computers to accelerate virtual screening of a large ligand library against a specific target by assigning groups of ligands to specific computers is described in (51). A number of examples of software tools are used to perform docking simulations. These methods involve a wide range of computational techniques, including use of a) rigid-body pattern-matching algorithms, either based on surface correlations, use of geometric hashing, pose clustering, or graph pattern-matching; b) fragmental-based methods, including incremental construction or ‘place and join’ operators; c) stochastic optimization methods including use of Monte Carlo, simulated annealing, or genetic (or memetic) algorithms; d) molecular dynamics simulations or e) hybrids strategies derived thereof.

The earliest docking software tool was a graph-based rigid-body pattern-matching algorithm called DOCK, developed at UCSF back in 1982 (v1.0), with more recent versions including extensions to include incremental construction. Other examples of graph-based pattern-matching algorithms are described in include CLIX (which in turn uses GRID), FLOG and LIGIN. The above and other software tools are described in (52-56). Other rigid-body pattern-matching docking software tools are described in (57-60) and include the shape-based correlation methods of FTDOCK and HEX, the geometric hashing and the pose clustering. In general, rigid-body pattern-matching algorithms assume that both the target and ligand are rigid (i.e., not flexible) and hence may be appropriate for docking small, rigid molecules (or molecular fragments) to a simple protein with a well-defined, nearly rigid active site. Thus, this class of docking tools may be suitable for de novo ligand design, combinatorial library design, or straightforward rigid-body screening of a molecule library containing multiple conformers per ligand. Incremental construction based docking software tools include FlexX (61, 62) from Tripos (licensed from EMBL), Hammerhead (63), DOCK v4.0 (as an option), and the nongreedy, backtracking algorithm of (64). Programs using incremental construction in the context of de novo ligand design include LUDI (65) (from Accelrys) and GrowMol (66_. Docking software tools also include the tools based on ‘place and join’ strategies (67).

Incremental construction algorithms may be used to model docking of flexible ligands to a rigid target molecule with a well-characterized active site. They may be used when screening a library of flexible ligands against one or more targets. They are often comparatively less compute intensive, yet consequently less accurate, than many of their stochastic optimization based competitors. Incremental construction algorithms often employ one or more scoring functions to evaluate and rank different system poses encountered during computations. For example, FlexX was extended to FlexE (68) to attempt to account for partial flexibility of the target molecule's active site via use of user-defined ensembles of certain active site rotamers. Computational docking software tools based on stochastic optimization (69) are described in (70-72) and include ICM (from MolSoft), GLIDE (from Schrodinger), and LigandFit (from Accelrys), all based on modified Monte Carlo techniques, as well as AutoDock v.2.5 (from Scripps Institute) based on simulated annealing. Other software tools based on genetic or memetic algorithms are described in (73-76) and include GOLD, DARWIN, and AutoDock v.3.0 (also from Scripps).

Stochastic optimization-based methods may be used to model docking of flexible ligands to a target molecule. They generally use a molecular-mechanics-based formulation of the affinity function and employ various strategies to search for one or more favorable system energy minima. They are often more computer intensive, yet also more robust, than their incremental construction competitors. As they are stochastic in nature, different runs or simulations may often result in different predictions. Traditionally most docking software tools using stochastic optimization assume the target to be nearly rigid (i.e., hydrogen bond donor and acceptor groups in the active site may rotate), since otherwise the combinatorial complexity increases rapidly making the problem difficult to robustly solve in reasonable time.

Molecular dynamics simulations have also been used in the context of computational modeling of target-ligand combinations. This includes the implementations presented in (77) and (71) (along with Monte Carlo). In principle, molecular dynamics simulations may be able to model protein flexibility to an arbitrary degree. On the other hand, they may also require evaluation of many fine-grained, time steps and are thus often very time-consuming (one order of hours or even days per target-ligand combination). They also often require user interaction for selection of valid trajectories. Use of molecular dynamics simulations in lead discovery can be more suited to local minimization of predicted complexes featuring a small number of promising lead candidates. Hybrid methods may involve use of rigid-body pattern-matching techniques for fast screening of selected low-energy ligand conformations, followed by Monte Carlo torsional optimization of surviving poses, and finally even molecular dynamics refinement of a few choice ligand structures in combination with a (potentially) flexible protein active site. An example of this type of docking software strategy is (78).

There are a number of examples of scoring functions implemented in software and used to estimate target-ligand affinity, rank prioritize different ligands as per a library screen, or rank intermediate docking poses in order to predict binding modes. Scoring functions traditionally fall into three distinct categories: a) empirical scoring functions, b) molecular-mechanics-based expressions, or I knowledge-based scoring functions or hybrid schemes derived thereof. Empirically derived scoring functions (as applied to target-ligand combinations) were first inspired by the linear free-energy relationships often utilized in QSAR studies. An early example is that of Böhm et al. (65, 79) (used in LUDI). Other empirical scoring functions are described in (80-84) and include SCORE (used in FlexX), ChemScore, PLP, Fresno, and GlideScore v.2.0+(modified form of ChemScore, used by GLIDE).

In general, empirical scoring functions comprise the bulk of scoring functions used today, especially in the context of large compound library screening. The basic premise is to calibrate a linear combination of empirical energy models, each multiplied by an associated numerical weight and each representing one of a set of interaction components represented in a (so-called) ‘master scoring equation’, where said equation attempts to well approximate the binding free energy of a molecular combination. The numerical weight factors may be obtained by fitting to experimental binding free energy data composed for a training set of target-ligand complexes. Molecular-mechanics-based scoring functions were first developed for use in molecular modeling in the context of molecular mechanics force fields like AMBER, OPLS, MMFF, and CHARMM (described in (85-89)). Examples of molecular-mechanics-based scoring functions include both the chemical and energy-based scoring functions of DOCK v.4.0 (based on AMBER), the objective functions used in GOLD, AutoDock v.3.0 (with empirical weights), and FLOG. In general, molecular-mechanics-based scoring functions may closely resemble the objective functions utilized by many stochastic optimization-based docking programs. Such functions typically require atomic (or chemical group) level parameterization of various attributes (e.g., charge, mass, van der Waals radii, bond equilibrium constants, etc.) based on one or more molecular mechanics force fields (e.g., AMBER, MMFF, OPLS, etc.). In some cases, the relevant parameters for the ligand may also be assigned based on usage of other molecular modeling software packages, e.g., ligand partial charges assigned via use of MOPAC (90), AMPAC (91) or AMSOL (92). They may also include intramolecular interactions (i.e., self-energy of molecules), as well as long range interactions such as electrostatics. In some cases, the combination of energy terms may again be accomplished via numerical weights optimized for reproduction of test ligand-target complexes.

Knowledge-based scoring functions were first inspired by the potential of mean force statistical mechanics methods for modeling liquids. Examples include DrugScore, PMF and BLEEP (93-95). In general, knowledge-based scoring functions do not require partitioning of the affinity function. However, they do require usage of a large database of 3-D structures of relevant molecular complexes. There is also usually no need for regression against a data set of molecular complexes with known experimental binding affinities. These methods are based on the underlying assumption that the more favorable an interaction is between two atoms, at a given distance, the more frequent its occurrence relative to expectations in a bulk, disordered medium. These schemes are sometimes referred to as ‘inverse Boltzmann’ schemes, but in fact the presence of local, optimized structures in macromolecules and protein folds means that distance-dependent pair-wise preference distributions need not be strictly Boltzmann. It is also possible to introduce the concept of singlet preferences based on other molecular descriptors, e.g., solvent accessible surface area for approximation of solvation effects. Hybrid scoring functions may be a mixture of one or more scoring functions of distinct type. One example is VALIDATE (96), which is a molecular-mechanics/empirical hybrid function. Other combinations of scoring functions may include the concept of consensus scoring in which multiple functions may be evaluated for each molecular combination and some form of ‘consensus’ decision is made based on a set of rules or statistical criteria, e.g., states that occur in the top 10% rank list of each scoring function (intersection-based), states that have a high mean rank (average-based), etc. A useful review discussion of consensus scoring can be found in (97). Various file formats exist for the digital representation of structural and chemical information for both target proteins and compounds as related to structural databases. Examples include the pdb, mol2 (from Tripos), and the SMILES formats.

A discussion on the calculation of total electrostatic energies involved in the formation of a potential molecular complex can be found in (98). Computational solutions of electrostatic potentials in the classical regime range from simpler formulations, like those involving distance-dependent dielectric functions, to more complex formulations, like those involving solution of the Poisson-Boltzmann equation (99, 100), a second order, generally nonlinear, elliptic partial differential equation. Other classical formalisms that attempt to model electrostatic desolvation include those based on the Generalized Born solvation model (101, 102), methods that involve representation of reaction field effects via additional solvent accessible or fragmental volume terms (103-105), or explicit representation of solvent in the context of molecular dynamics simulations (106-108). A lengthy review of full quantum mechanical treatment of electrostatics interactions can be found in (109).

FIG. 6 illustrates a modeling system 100 for the analysis of molecular combinations according to embodiments of the present disclosure. As shown, a configuration modeler 102 receives one or more input configuration records 106, including both the identities of and molecular descriptors for input structures for one or more molecular subsets from an input molecular combination database 104. The configuration modeler 102 comprises a configuration data transformation engine 108, an affinity calculator 109, and descriptor data storage 120. Results from the configuration modeler 102 are output as configuration results records 111 to a results database (DB) 110. Modeling system 100 may be used to determine or characterize one or more molecular combinations. In some embodiments, this may include, but is not limited to, prediction of likelihood of formation of a potential molecular complex, or a proxy thereof, the estimation of the binding affinity or binding energy between molecular subsets in an environment, the prediction of the binding mode (or even additional alternative modes) for the molecular combination, or the rank prioritization of a collection of molecular subsets (e.g., ligands) based on predicted bioactivity with a target molecular subset, and would therefore also include usage associated with computational target-ligand docking and scoring.

In a typical operation, many molecular combinations, each featuring many different molecular configurations, may be modeled. Since the total possible number of configurations may be enormous, the modeling system may sample a subset of configurations during the modeling procedure, though the sampling subset may still be very large (e.g., millions or billions of configurations per combination) and the selection strategy for configuration sampling is specified by one or more search and/or optimization techniques (e.g., steepest descent, conjugate gradient, modified Newton's methods, Monte Carlo, simulated annealing, genetic or memetic algorithms, brute force sampling, pattern matching, incremental construction, fragment place-and-join, etc.). An affinity function is evaluated for each visited configuration and the results for one or more configurations recorded in a storage medium.

The molecular combination may then be assessed by examination of the set of configuration results including the corresponding computed affinity function values. Once the cycle of computation is complete for one molecular combination, modeling of the next molecular combination may ensue. Alternatively, in some embodiments of the modeling system 100, multiple molecular combinations may be modeled in parallel as opposed to in sequence. Likewise, in some embodiments, during modeling of a molecular combination, more than one configuration may be processed in parallel as opposed to in sequence.

In one embodiment, modeling system 100 may be implemented on a dedicated microprocessor, ASIC, or FPGA. In another embodiment, modeling system 100 may be implemented on an electronic or system board featuring multiple microprocessors, ASICs, or FPGAs. In yet another embodiment, modeling system 100 may be implemented on or across multiple boards housed in one or more electronic devices. In yet another embodiment, modeling system 100 may be implemented across multiple devices containing one or more microprocessors, ASICs, or FPGAs on one or more electronic boards and the devices connected across a network.

In some embodiments, modeling system 100 may also include one or more storage media devices for the storage of various, required data elements used in or produced by the analysis. Alternatively, in some other embodiments, some or all of the storage media devices may be externally located but networked or otherwise connected to the modeling system 100. Examples of external storage media devices may include one or more database servers or file systems. In some embodiments involving implementations featuring one or more boards, the modeling system 100 may also include one or more software processing components in order to assist the computational process. Alternatively, in some other embodiments, some or all of the software processing components may be externally located but networked or otherwise connected to the modeling system 100.

In some embodiments, results records from database 110 may be further subjected to a configuration selector 112 during which one or more molecular configurations may be selected based on various selection criteria and then resubmitted to the configuration modeler 102 (possibly under different operational conditions) for further scrutiny (i.e., a feedback cycle). In such embodiments, the molecular configurations are transmitted as inputs to the configuration modeler 102 in the form of selected configuration records 114. In another embodiment, the configuration selector 112 may also send instructions to the configuration data transformation engine on how to construct one or more new configurations to be subsequently modeled by configuration modeler 102. For example, if the configuration modeler modeled ten target-ligand configurations for a given target-ligand pair (the target, in the context of the present disclosure, can be a PD-L2 binding pocket of human PD-1, and the ligand is a test ligand capable of interacting with the PD-L2 binding pocket of human PD-1), and two of the configurations had substantially higher estimated affinity than the other eight, then the configuration selector 112 may generate instructions for the configuration data transformation engine on how to construct further additional configurations (i.e., both target and ligand poses) that are structurally similar to the top two high-scoring configurations, which are then subsequently processed by the remainder of the configuration modeler 102. In some embodiments, the transmitted instructions may relate to construction from the resubmitted configurations whereas in other cases they relate to construction from the original input reference configuration(s).

In some embodiments, once analysis of a molecular combination is completed (i.e., all desired configurations assessed) a combination postprocessor 116 may be used to select one or more configuration results records from database 110 in order to generate one or more qualitative or quantitative measures for the combination, such as a combination score, a combination summary, a combination grade, etc., and the resultant combination measures are then stored in a combination results database 118. In one embodiment, the combination measure may reflect the configuration record stored in database 110 with the best observed affinity. In another embodiment, multiple high affinity configurations are submitted to the combination postprocessor 116 and a set of combination measures written to the combination results database 118. In another embodiment, the selection of multiple configurations for use by the combination postprocessor 116 may involve one or more thresholds or other decision-based criteria.

In a further embodiment, the selected configurations are also chosen based on criteria involving structural diversity or, alternatively, structural similarity (e.g., consideration of mutual rmsd of configurations, use of structure-based clustering or niching strategies, etc.). In yet another embodiment, the combination measures output to the combination results database 118 are based on various statistical analysis of a sampling of possibly a large number of configuration results records stored in database 110. In other embodiment the selection sampling itself may be based on statistical methods (e.g., principal component analysis, multidimensional clustering, multivariate regression, etc.) or on pattern-matching methods (e.g., neural networks, support vector machines, etc.)

In yet another embodiment, the combination results records stored in database 118 may not only include the relevant combination measures, but may also include some or all of the various configuration records selected by the combination postprocessor 116 in order to construct a given combination measure. For example, combination results records stored in database 118 may include representations of the predicted binding mode or of other alternative, high affinity (possibly structurally diverse) modes for the molecular combination. In another embodiment, the combination postprocessor 116 may be applied dynamically (i.e., on-the-fly) to the configuration results database 110 in conjunction with the analysis of the molecular combination as configuration results records become available. In yet another embodiment, the combination postprocessor 116 may be used to rank different configurations in order to store a sorted list of either all or a subset of the configurations stored in database 110 that are associated with the combination in question. In yet other embodiments, once the final combination results records, reflecting the complete analysis of the molecular combination by the configuration modeler 102, have been stored in database 118, some or all of the configuration records in database 110 may be removed or deleted in order to conserve storage in the context of a library screen involving possibly many different molecular combinations. Alternatively, some form of garbage collection or equivalent may be used in other embodiments to dynamically remove poor affinity configuration records from database 110.

In one embodiment, the molecular combination record database 104 may comprise one or more molecule records databases (e.g., flat file, relational, object oriented, etc.) or file systems and the configuration modeler 102 receives an input molecule record corresponding to an input structure for each molecular subset of the combination, and possibly a set of environmental descriptors for an associated environment. In another embodiment, when modeling target protein-ligand molecular combinations, the molecular combination record database 104 is replaced by an input target record database and an input ligand (or drug candidate) record database. In a further embodiment, the input target molecular records may be based on that are experimentally derived (e.g., X-ray crystallography, NMR, etc.), energy minimized, and/or model-built structures. In another embodiment, the input ligand molecular records may reflect energy minimized or randomized 3-D structures or other 3-D structures converted from a 2-D chemical representation, or even a sampling of low energy conformers of the ligand in isolation. In yet another embodiment, the input ligand molecular records may correspond to naturally existing compounds or even to virtually generated compounds, which may or may not be synthesizable.

In one embodiment the configuration data transformation engine 108 may transform one or more input molecular configurations into one or more other new configurations by application of various geometrical operators characterized by sets of geometrical descriptors. Transformation of molecular configurations into newer variants may be accomplished by one or more unary operations (i.e., acting on one input configuration, such as the mutation operator in a genetic algorithm), binary operations (i.e., acting on two input configurations, such as a binary crossover in a genetic algorithm), other n-ary operations (i.e., acting on a plurality of input configurations, such as a transform operator based on a population of configurations), or a combination thereof. In another embodiment, the transformation of molecular configurations into newer variants may result in multiple new configurations from one configuration, such as, for example, the construction of a suitable (often randomized) initial population for use in a genetic algorithm. In some embodiments, the configuration data transformation engine 108 may be able to construct ab initio one or more entirely new configurations without the requirement of input geometrical descriptors from an input molecular combination database 104, though other types of molecular descriptors may still be needed.

As already discussed, in some embodiments, the set of configurations generated via transformation during the course of an analysis of a molecular combination may be determined according to a schedule or sampling scheme specified by one or more search and/or optimization techniques used to drive the modeling processes of the configuration modeler 102. In some embodiments, the search strategy or optimization technique may be an iterative process whereby one or more configurations are generated from one or more input configurations, then affinities are calculated for each configuration, decisions are made based on affinity and/or structure, and all or part of the new set of configurations are used as input seeds for the next iteration; the process continuing until a specified number of iterations are completed configuration modeler 102 or some other convergence criteria satisfied. In such embodiments, the input configuration records 106 obtained or derived from data in the input molecular combination database 104, may serve only to initiate (or also possibly reset) the iterative process (i.e., prime the pump). For example, in the context of the present disclosure, the input target molecular records may be based on atomic coordinates of PD-L2 binding pocket of human PD-1 included in the present disclosure, which are determined from co-crystals of a variant of human PD-1 with PD-L2 ligand. In one example, the variant of human PD-1 is a variant comprising amino acid substitutions in one or more of (such as in each) of residues corresponding to N74, T76 or A132 of SEQ ID NO:1,

In some embodiments, the search strategy or optimization technique may be stochastic in nature meaning that the set of configurations visited during analysis of a molecular combination may involve some random component and thus be possibly different between different runs of the configuration modeler 102 as applied to the same molecular combination. Here the term run refers to two different initiations of (possibly iterative) cycles of computation for analysis of the same molecular combination. In some embodiments, the combination postprocessor 116 may then base its results or decisions on configuration results records stored in database 110 but obtained from different runs. In some embodiments, the configuration data transformation engine 108 may produce new configurations sequentially, such as a new possible state associated with a given iteration of a Monte Carlo-based technique, and feed them to the affinity calculator 109 in a sequential manner. In other embodiments, the configuration data transformation engine 108 may produce multiple new configurations in parallel, such as a population associated with a given iteration of a genetic algorithm, and submit them in parallel to the affinity calculator 109. In other embodiments, the configuration data transformation engine 108 may not generate additional configurations and instead the configuration modeler 102 may operate solely on one or more input configuration records from the input molecular combination database 104, such as for example in some usages of modeling system 100 related to scoring of a set of known molecular configurations. In such embodiments, the configuration data modeler 102 may not include a search or optimization strategy and instead be used to perform affinity calculations on an enumerated set of input configuration records.

In some embodiments, various descriptor data related to the configurations of a given molecular combination may be stored or cached in one or more components of a descriptor data storage 120 via one or more storage (or memory) allocation means, structure or apparatus for efficient access and storage during the cycle of computations performed by the configuration modeler 102. In one embodiment, the descriptor data storage 120 may contain chemical or physical descriptors assigned to atoms, bonds, groups, residues, etc. in each of the molecular subsets or may even also contain environmental descriptors. In another embodiment, the descriptor data common to all configurations for a given molecular combination is compactly represented via a storage allocation means in one or more lookup tables. For example, often many physical and chemical descriptors may be identical for different configurations of a combination whereas one or more geometric descriptors are not. In yet another embodiment, the descriptor data storage 120 may also contain relevant geometric descriptors for the configurations arranged in one or more storage formats via a prescribed storage allocation means. As examples, such formats may involve, but are not limited to, records analogous to pdb or mol2 file formats. Additional examples include various data structures such as those associated with the molecular representation partitioning shown in Ahuja I. As a further example, perhaps stored descriptors for atoms and bonds may represent individual nodes in one or more lists or arrays, or may alternatively be attached, respectively, to nodes and edges of a tree or directed graph.

The whole or parts of the input configuration records 106, and, if applicable, selected configuration records 114 chosen by configuration selector 112, may be converted to data representations used in the storage allocation means of the descriptor data storage 120. Data constructs contained in the descriptor data storage 120 may be either read (i.e., accessed) for use by the configuration data transformation engine 108 or the affinity calculator 109 and may be written either at the inception of or during the execution of a cycle of computation by the configuration modeler 102. The layout and access patterns for the associated descriptor data storage 120 will likely depend on the needs of the affinity calculator 109 as well as the configuration data transformation engine 108.

The affinity calculator 109 may comprise one or more processing (i.e., affinity) engines, where each affinity engine may be dedicated to performing calculations related to one or more affinity components as defined previously in regard to interaction types, affinity formulations, and computation strategies. In some embodiments, different affinity engines are assigned to each unique affinity component. In other embodiments, one or more affinity engines may compute multiple affinity components according to similarity of processing requirements. In yet other embodiments, different affinity engines may be grouped or otherwise arranged together to take advantage of common subsets of required input data in order to improve any caching scheme and/or to reduce the number of, the bandwidth requirements for, or the routing requirements for various associated data paths.

For example, in one embodiment, affinity components for both the electrostatic and van der Waals interactions involving field-based computation strategies utilizing stored pregenerated probe grid maps, may be computed on the same affinity engine, where said engine requires access to both types of probe grid maps in storage and to various numerical parameters used in evaluating the affinity formulation for the two different interactions. As another example, affinity components for both the hydrogen bonding and van der Waals interactions using affinity formulations featuring generalized Lennard-Jones potentials computed according to a pair-based computation strategy may be computed on the same affinity engine. In an alternative embodiment, the same two affinity components may be computed using two different affinity engines but grouped together in order to share common input data such as that relating to spatial coordinates and a subset of relevant chemical or physical descriptors.

In Vitro and In Vivo Methods

The methods related to drug design and discovery described in the present disclosure can include determining biological activity (including presence, absence or amount of biological activity, which can be also referred of “efficacy,” of a candidate compound or molecule (which can be, but is not limited to, a small molecule) identified and/or designed by computational (in silico) methods in an in vitro biological assay or in vivo in a subject (such as a model animal, for example, a wild-type animal, a laboratory-bred animal, or a transgenic animal model). The methods disclosed in the present disclosure can also include validating or confirming in silico predicted activities of a ligand, for example, in silico binding of the ligand to PD-1 conformation of the target protein, with the results of an in vitro biological assay, and/or with the results of an in vivo study in an animal model.

One assay in vitro platform suitable for evaluation of the ability of candidate compounds to block PD-1 interaction with its in vivo ligands is described in (116). The platform uses fluorescence-base transcriptional reporters based on the human Jurkat T cell line in conjunction with engineered T cell stimulator cell lines for investigating immune checkpoint signaling pathways, including PD-1 activity. A PD-1:PD-L2 cell-based inhibitor screening assay kit for conducting is a bioluminescent cell-based assay that can be used to screen and profile inhibitors of the PD-1:PD-L2 interaction is available from BPS Bioscience (San Diego, Calif.). In the above assay, as described in the assay data sheet, PD-1/NFAT Reporter/Jurkat T cells are used as effector cells; HEK293 cells over-expressing PD-L2 and an engineered T cell receptor (TCR) activator by transient transfection are used as target cells. When the cells are co-cultivated, TCR complexes on effector cells are activated by TCR activator on target cells, resulting in expression of the NFAT luciferase reporter. However, PD-1 and PD-L2 binding prevents TCR activation and suppresses the NFAT-responsive luciferase activity. In both scenarios, this inhibition can be specifically reversed by anti-PD-1 antibodies. This interaction also can be blocked by anti-PD-L2 antibodies. These neutralizing antibodies block PD-1 signaling and promote T cell activation, resulting in reactivation of the NFAT-responsive luciferase reporter. Another example of an in vitro assay suitable for evaluation of the ability of candidade compounds to block PD-1 interaction with its ligand in vitro is competition ELISA described in (117). As described in (117), the assay measures the amount of biotin tagged PD-1 that is able to bind to the wells coated with PD-L1. Similarly, PD-L2 can be used as an in vivo ligand. An example of an in vitro assay for testing biological activity of candidate compounds, also described in (117), is an assay testing the ability of candidate compounds to promote T cell function. As described in (117), the production of IL-2 by peripheral blood mononuclear cells (PBMCs) pre-treated with PD-1/PD-L1 antagonists (or inhibitors): neutralizing mAbs or candidate compounds before stimulation with Staphylococcal enterotoxin B (SEB) for 72 hours. PBMCs include the cells that express/up-regulate both PD-1 (T cells) and PD-L1 (T cells, APCs) upon stimulation. In this assay, cytokine levels from cell culture supernatants would indicate that stimulated T cells treated with a-PD-1/PD-L1 antagonist produced significantly higher concentrations of IL-2 compared to untreated and stimulated cells, with the cells pre-treated by neutralizing mAbs serving as a positive control. Some other in vitro assays suitable for evaluating biologica activity of candidate compounds are described in (118). In one assay, PBMC from normal healthy donors are seeded at 1×105 cells/well and stimulated with SEB in the presence of candidate compounds. IL-2 secretion by PMBC is measured by ELISA on day 3 after the stimulation. In another assay, mixed lymphocyte response is assessed by co-culturing 1×105 cells CD4+ T cells with allogeneic monocyte-derived dendritic cells (DC) at a ratio of 10:1 (T:DC) in flat-bottom 96-well microtiter plates. CD4+ T cells and DC are incubated for 6 days in the presence or absence of a candidate compound. Culture supernatants are harvested on day 5 for ELISA analysis of IFN-γ secretion. One more assay measures nonspecific T cell activation. In this assay, candidate compounds are mixed with samples of heparinized fresh human whole blood to measure cytokine release. After a 4-hour incubation at 37° C., the cells are pelleted, and the plasma fraction collected for measurement of IFN-γ, TNF-α, IL-2, IL-4, IL-6, and IL-10 using a cytokine cytometric bead array assay. Studies of potential anti-cancer effects of candidate compounds can also be performed in vitro in tumor-derived cell ilnes, such as D4m melanoma lines.

In vivo assays can be performed using animals, such as mice, with chemically induced or implanted tumors. Examples of in vivo assays using mouse models are described in (118). MC38 tumor cells are cultured in DMEM and implanted subcutaneously into female C57/Bl6 mice or B6.129S7-Ifngtm1Ts/J C57BL/6 mice. CT26 tumor cells are cultured in DMEM and implanted subcutaneously in female BALB/c mice. Tumor measurements are made 2-3 times weekly using an electronic caliper. Candidate compounds are administered to mice intraperitoneally on days 7, 10, and 13. For T-cell depletion studies, 500 μg of depleting antibodies for CD4 (GK1.5) or CD8 (53.6.72; BioXCell, W. Lebanon, N.H.) are administered on day 7. following subcutaneous implantation of MC38 tumor cells in the hind flank. The efficiency of CD4+ or CD8+ T cell depletion (>90%) is confirmed by FACS analysis of blood samples collected four days after administration of the depleting antibodies. Mice are sacrificed at the study termination or pre-determined endpoints. For immune response monitoring, tumors are harvested and processed using cell disruptors. The cell suspensions are clarified, pelleted, resuspended buffer or media, and counted. Cells are incubated with anti-CD16/32 mAb 24G.2 (BioXCell) to reduce background FcγR binding and then stained with antibodies specific for CD8, CD4, and CD45. Cells are also stained with the a fixable viability. For intracellular staining (ICS), cell samples are fixed, permeabilized, and stained with antibodies specific for FoxP3, Ki67, CTLA-4, IFN-γ, and TNF-α CT26 tumor antigen-specific CD8+ T cells are identified using AH-1 MHC class I tetramers. Ex vivo AH-1 peptide stimulation is performed by culturing tumor or splenic cells with 2 μM AH-1 peptide (MBL) in the presence of brefeldin-A for 4 hours at 37° C. Ex vivo cytokine staining is performed by fixing and staining cells as described above, directly after tissue harvest. Samples are analyzed on FACS flow cytometers. Cytokine assays of harvested tumor cells can also be performed using bead-bays cytokine arrays. Immunohistochemical studies of tumor sections can also be performed according to established procedures.

Any of the methods described in the present disclosure can further comprise determining the toxicity of the ligand in an in vitro, in vivo or in silico assay. As used in the present disclosure, toxicity refers to a harmful effect on a cell or organism. For example, and not to be limiting, the cardiotoxicity or neurotoxicity of a compound can be determined. In vitro methods for assessing cardiotoxicity are known in the art. For example, electrophysiology measurements can be performed in cells, including, for example single cardiac cells. The effect of one or more compounds can be assessed in cell lines that express the human ether-a-go-go related gene (hERG1) or in cells transfected with hERG1. The hERG safety assay from Cyprotex (Watertown, Mass.) can also be used. Cardiotoxicity can also be measured in vivo by conducting an electrocardiogram (ECG) in a subject (e.g., a wild type animal or transgenic animal) expressing hERG1 after administering the compound to the animal. In vitro cytotoxicity panels can also be used to measure toxicity in individual cells. For example, assays that measure nuclear size, mitochondrial membrane potential, intracellular calcium, membrane permeability and/or cell number can be used. See, for example, the ADME-Tox panel available from EuroFins PanLabs, Inc. (Redmond, Wash.). In this assay, all five parameters are measured. Intracellular calcium and membrane permeability will increase in the presence of a cytotoxic compound. Conversely, nuclear size, cell number and mitochondrial membrane potential will decrease in the presence of a cytotoxic compound.

Genotoxicity studies can also be performed to identify mutagenic compounds. Gene mutations can be detected in bacteria, where they cause a change in growth requirements. The Ames test, which is conducted using Salmonella typhimurium is a widely used bacterial assay for the identification of compounds that can produce gene mutations, and it shows high predictive value with rodent carcinogenicity tests. Micronucleus assays can also be used to identify mutagenic compounds. Micronucleus formation is a hallmark of genotoxicity. Micronuclei are chromatin-containing bodies that represent fragments or even whole chromosomes that were not incorporated into a daughter cell nucleus at mitosis. The purpose of the assay is to detect those agents that induce chromosome damage leading to the induction of micronuclei in interphase cells. Assays that measure Cytochrome p450 (CYP) inhibition, CYP induction or drug transporter inhibition can also be performed.

Any of the methods provided in the present disclosure can further comprise determining if a candidate compound or molecule has an adverse drug reaction (ADR) or off-target effect in an in vitro, in vivo or in silico assay. It should be noted that off-target effects may be desirable or undesirable effects. In silico methods for determining off-target effects are known in the art. See, for example (110-112). In vitro assays for assessing off-target effects are also known in the art. See (113) for a review of in vitro assays that can identify undesirable off-target activity. Any of the methods provided herein can further comprise optimizing the ligand. A candidate compound or molecule can be modified or optimized for certain properties. For example, a candidate compound or molecule can be modified to reduce its toxicity, to reduce an undesirable off-target effect, to increase the binding affinity to a target protein, to decrease the binding affinity to a target protein, to increase a desirable off-target activity or to decrease an off-target activity.

Computer Systems

Any of the computer systems mentioned in the present disclosure may utilize any suitable number of subsystems. In some embodiments, a computer system includes a single computer apparatus, where the subsystems can be the components of the computer apparatus. In other embodiments, a computer system can include multiple computer apparatuses, each being a subsystem, with internal components. The subsystems can be interconnected via a system bus. Additional subsystems such as a printer, keyboard, storage device(s), monitor, which is coupled to display adapter, and others are shown. Peripherals and input/output (I/O) devices, which couple to I/O controller, can be connected to the computer system by any number of means known in the art, such as serial port. For example, serial port or external interface (e.g. Ethernet, Wi-Fi, etc.) can be used to connect computer system to a wide area network such as the Internet, a mouse input device, or a scanner. The interconnection via system bus allows the central processor to communicate with each subsystem and to control the execution of instructions from system memory or the storage device(s) (e.g., a fixed disk, such as a hard drive or optical disk), as well as the exchange of information between subsystems. The system memory and/or the storage device(s) may embody a computer readable medium. Any of the data mentioned herein can be output from one component to another component and can be output to the user.

A computer system can include a plurality of the same components or subsystems, e.g., connected together by external interface or by an internal interface. In some embodiments, computer systems, subsystem, or apparatuses can communicate over a network. In such instances, one computer can be considered a client and another computer a server, where each can be part of a same computer system. A client and a server can each include multiple systems, subsystems, or components.

It should be understood that any of the embodiments of the present invention can be implemented in the form of control logic using hardware (e.g. an application specific integrated circuit or field programmable gate array) and/or using computer software with a generally programmable processor in a modular or integrated manner. As user herein, a processor includes a multi-core processor on a same integrated chip, or multiple processing units on a single circuit board or networked. Based on the disclosure and teachings provided herein, a person of ordinary skill in the art will know and appreciate other ways and/or methods to implement embodiments of the present invention using hardware and a combination of hardware and software.

Any of the software components or functions described in this application may be implemented as software code to be executed by a processor using any suitable computer language such as, for example, Java, C++ or Perl using, for example, conventional or object-oriented techniques. The software code may be stored as a series of instructions or commands on a computer readable medium for storage and/or transmission, suitable media include random access memory (RAM), a read only memory (ROM), a magnetic medium such as a hard-drive or a floppy disk, or an optical medium such as a compact disk (CD) or DVD (digital versatile disk), flash memory, and the like. The computer readable medium may be any combination of such storage or transmission devices.

Such programs may also be encoded and transmitted using carrier signals adapted for transmission via wired, optical, and/or wireless networks conforming to a variety of protocols, including the Internet. As such, a computer readable medium according to an embodiment of the present invention may be created using a data signal encoded with such programs. Computer readable media encoded with the program code may be packaged with a compatible device or provided separately from other devices (e.g., via Internet download). Any such computer readable medium may reside on or within a single computer product (e.g. a hard drive, a CD, or an entire computer system), and may be present on or within different computer products within a system or network. A computer system may include a monitor, printer, or other suitable display for providing any of the results mentioned herein to a user.

The methods described herein may be totally or partially performed with a computer system including one or more processors, which can be configured to perform the steps. Thus, embodiments can be directed to computer systems configured to perform the steps of any of the methods described herein, potentially with different components performing a respective steps or a respective group of steps. Although presented as numbered steps, steps of methods herein can be performed at a same time or in a different order. Additionally, portions of these steps may be used with portions of other steps from other methods. Also, all or portions of a step may be optional. Additionally, any of the steps of any of the methods can be performed with modules, circuits, or other means for performing these steps.

EXAMPLES

The following examples are offered to illustrate, but not to limit the claimed invention.

Example 1: Materials and Methods

A. Yeast-Surface Display

Deep mutational scanning of the CC′ and FG loops of human PD-1 was performed using a previously described PCR-based method (24). The PD-1 loop variant libraries were constructed using the Saccharomyces cerevisiae EBY100 strain. MACS and FACS experiments were performed using recombinant human PD-L2-Fc or PD-L1-Fc proteins. The yeast strains and plasmids used in the study are summarized in Table 1.

TABLE 1 Plasmids and yeast strain. Yeast Strain (45) Genotype EBY100 MATa AGA1::PGAL1-AGA1::URA3 ura3-52 trp1 leu2Δ200 his3Δ200 pep4Δ::HIS3 prb1Δ1.6R can1 GAL Plasmid Description pST892 pRS414 PGAL1-AGA2-PD-1(P21-E150) pST992 pRS414 PGAL1-AGA2-PD-1(P21-E150) N74G pST993 pRS414 PGAL1-AGA2-PD-1(P21-E150) T76P pST995 pRS414 PGAL1-AGA2-PD-1(P21-E150) A132V pST1013 pRS414 PGAL1-AGA2-PD-1(P21-E150) N74G T76P A132V pST1132 pET23d PD-1(N33-E150)-StrepII C93S N74G T76P A132V pST1167 pET23d PD-1(N33-E150)-StrepII C93S T76P A132V pST971 pADD2 PD-L1-Fc pST972 pADD2 PD-L2-Fc pST980 pADD2 Fc pST981 pADD2 PD-1-Fc pST982 pADD2 PD-1-Fc N74G pST983 pADD2 PD-1-Fc T76P pST985 pADD2 PD-1-Fc A132V pST1008 pADD2 PD-1-Fc N74G A132V pST1009 pADD2 PD-1-Fc T76P A132V pST1010 pADD2 PD-1-Fc N74G T76P A132V pST739 pADD2 PD-L1-His6 pST700 pADD2 PD-L2-His6 pST963 pADD2 PD-1-Fc C93S pST964 pADD2 PD-1-Fc C93S CC′ loop-mutant (S71G P72G S73G N74G Q75G T76G D77G) pST965 pADD2 PD-1-Fc C93S FG loop-mutant (L128G A129G P130G K131G A132G Q133G) pST966 pADD2 PD-1-Fc C93S Pocket-mutant (Y68A I126A I134A E136A) pST1195 pADD2 PD-1(N33-E150)-Ctag C93S N74G T76P A132V N49S N58S N116D pST1228 pADD2 PD-1(N33-E150)-Ctag N49D N58D N74D N116D pST1207 pADD2 PD-L2(M1-Y123) N37D N64D pST1249 pADD2 PD-1-Fc V64E pST1250 pADD2 PD-1-Fc N66A pST1251 pADD2 PD-1-Fc Y68A pST1252 pADD2 PD-1-Fc Q75A pST1253 pADD2 PD-1-Fc I126D pST1254 pADD2 PD-1-Fc I134D pST1255 pADD2 PD-1-Fc E136A pST1262 pADD2 PD-L2-His6 I103D pST1263 pADD2 PD-L2-His6 I105D pST1266 pADD2 PD-L2-His6 Y112A pST1267 pADD2 PD-L2-His6 Y114A

B. Bio-Layer Interferometry

BLI was performed on an Octet RED96® system at 30° C. in a buffer of 150 mM NaCl, 20 mM HEPES:NaOH pH 7.4, 0.1% BSA and 0.05% Tween 20. The human PD-1-Fc proteins were loaded onto anti-human IgG Fc capture (AHC) biosensors, associated in defined concentrations of human PD-L2-His6 or PD-L1-His6 proteins, and then dissociated in buffer.

TABLE 2 Crystallographic data collection and refinement statistics. PD1N74G T76P A132V/ PD-L2Igv Apo-PD1N74G T76P A132V Apo-PD1T76P A132V Wavelength (Å) 0.978 0.978 0.978 Resolution 37.5-1.99 36.5-1.18 36.5-1.42 range (2.06-1.99) (1.23-1.18) (1.48-1.42) (Å) Space group P 21 21 21 P 32 2 1 P 32 2 1 Unit cell 41.3 67.8 89.7 46.2 46.2 89.3 46.2 46.2 89.4 90 90 90 90 90 120 90 90 120 Total reflections 185797 (11081) 400313 (24984) 171335 (11683) Unique 17750 (1645) 36661 (3544) 21301 (2090) reflections Multiplicity 10.4 (6.7) 10.9 (7.0) 8.0 (5.6) Completeness 98.6 (90.6) 99.7 (98.8) 99.7 (98.2) (%) Mean I/sigma(I) 16.1 (2.28) 28.5 (2.79) 23.3 (2.40) Wilson B-factor 35.8 16.7 21.9 Rmerge 0.139 (0.723) 0.0521 (0.539) 0.0903 (1.03) CC1/2 0.992 (0.780) 0.999 (0.856) 0.998 (0.769) CC* 0.998 (0.936) 1.00 (0.960) 0.999 (0.932) Rwork 0.196 (0.292) 0.154 (0.192) 0.158 (0.193) Rfree 0.226 (0.339) 0.164 (0.233) 0.189 (0.263) Number of non- 1782 1156 1143 hydrogen atoms macromolecules 1654 1001 1056 water 127 144 82 Protein residues 210 112 116 RMS(bonds) (Å) 0.013 0.009 0.016 RMS(angles) (°) 1.48 1.35 1.60 Ramachandran 99 100 99 favored (%) Ramachandran 0 0 0 outliers (%) Clashscore 8.32 0.99 5.66 Average B- 50.8 23.4 30.3 factor macromolecules 50.6 21.1 30.9 solvent 53.8 38.2 39.1 Statistics for the highest-resolution shell are shown in parentheses.

C. Protein Crystallization and X-Ray Crystallography

The human apo-PD-1N74G T76P A132V and human apo-PD-1T76P A132V proteins were over-expressed in and refolded from the inclusion bodies of Escherichia coli BL21(DE3) cells. The human apo-PD-1N74G T76P A132V protein was crystallized in 100 mM NaCl, 100 mM Tris:HCl pH 8.0, 27% (w/v) PEG-MME 5,000. The human apo-PD-1T76P A132V protein was crystallized in 100 mM NaCl, 100 mM Tris:HCl pH 8.0, 36% (w/v) PEG 3,350. The human PD-1N74G T76P A132V and human PD-L2IgV protein complex was produced using the human Expi293F cell line. The complex was crystallized in 200 mM magnesium acetate, 10% (w/v) PEG 8000. All X-ray diffraction data were collected at the SSRL beam lines 12-2 or 14-1, and processed using HKL-3000 (42). Molecular replacement, refinement and density modification were performed in Phenix (43) and model building in Coot (44). The crystallographic data collection and refinement statistics are summarized in Table 2.

Example 2: Engineering Human PD-1 Loop Variants with Enhanced PD-L2 Affinity

Substantial earlier efforts (23) to crystalize the human PD-1/PD-L2 complex were unsuccessful. Previous studies (16, 17, 19) indicated that the PD-1 ligand-binding interface comprises a hydrophobic core, the CC′ loop and the FG loop, and that formation of a complex with ligands results in loop movement and pocket formation in the hydrophobic core. In the present study, it was conceived that mutations in these two loops of PD-1 were coupled to pocket formation and may alter the affinity for PD-L2. It was then experimentally confirmed that poly-glycine mutants of these loops in human PD-1 significantly decreased its affinities for PD-L2 (data not shown). The binding of sensor-loaded PD-1, the glycine-loop-mutants and the pocket mutant to 1.9 μM PD-L2 (left) and 17 μM PD-L1 (right) was measured using biolayer interferometry. Corresponding PD-1-Fc proteins were loaded onto anti-human IgG Fc capture (AHC) biosensors. Association was monitored for 2 min and dissociation for 2 min. Since the present study was particularly interested in the structure of the PD-1 pocket when bound to PD-L2, the residues in the hydrophobic core were maintained, and directed evolution was performed exclusively in the CC′ loop (residues 70-78) and the FG loop (residues 127-133) of human PD-1. Deep mutational scanning (24, 27) was used to construct loop-variant libraries with trinucleotides encoding each of 20 residues at each position. Next, yeast-surface display (25) was used with a recombinant human PD-L2-human Fc fusion protein as the selection agent. After two rounds of selection using magnetic- and fluorescent-activated cell sorting (MACS and FACS), human PD-1 loop-variant clones with single-residue substitutions were isolated (data not shown). Substitutions at two residues were identified in the CC′ loop (N74G and T76P), and at one residue in the FG loop (A132V, A132L). In contrast, when the same yeast library was used for section with PD-L1-Fc, only the A132 substitutions were isolated as high-affinity variants (data not shown). This result suggested that the N74G and T76P variants were PD-L2-binding specific. PD-1T76P was chosen as a template to generate a second PD-1 loop variant library and selected for further enhancement of PD-L2 binding. As a result, a PD-1 triple mutant was obtained, which contained all three substitutions identified from the first library, N74G, T76P and A132V.

Example 3: PD-1 Loop Variants Showed Increased Binding Affinity and Association Kinetics for PD-L2 and PD-L1

To validate the enhanced affinity of PD-1 loop variants, human PD-1 and the loop variants, as well as human PD-L2 and PD-L1 ectodomain proteins, were recombinantly expressed and purified. Using bio-layer interferometry (BLI), the binding of PD-L2 to wild-type PD-1 and the variants was compared (data not shown). The binding of sensor-loaded PD-1 and the loop variants to 190 nM PD-L2 and 1.1 μM PD-L1 was measured using biolayer interferometry. Corresponding PD-1-Fc proteins were loaded on anti-human IgG Fc capture (AHC) biosensors. Association was monitored for 2 min and dissociation for 2 min. Fitting of binding curves was performed in Graphpad Prism 8 software using built-in equations of “Receptor binding—kinetics” models. Means and standard deviations were calculated from 3-4 independent experiments. Wild-type PD-1 bound PD-L2 with a KD of 500 nM. The variants all exhibited increased PD-L2 affinity, with KD of 170 nM for N74G, 12 nM for T76P, and 69 nM for A132V. Remarkably, the PD-1 triple mutant had a KD of 2.6 nM, exhibiting a ˜200-fold increase in PD-L2 binding affinity. Table 3 summarizes the binding affinity (KD) and kinetic parameters (association constant kon, dissociation constant koff) for the PD-1 loop variants binding to PD-L2 or PD-L1. Fitting of binding curves was performed in Graphpad Prism 8 using built-in equations of “Receptor binding—kinetics” models. Means and standard deviations were calculated from 3-4 independent experiments. The triple-mutant also showed substantially increased affinity for PD-L1. The A132V mutant showed increased affinity for PD-L1, consistent with previous reports (19, 23, 28, 29), but the N74G and T76P single mutants had minor effects. Thus, a human PD-1 triple-mutant exhibited potent binding affinity enhancement for both PD-L1 and PD-L2. Kinetic measurements of binding of the ligands by PD-1 with BLI also permitted the determination of association constants (kon). Compared to wild-type PD-1, all loop variants showed increased kon for binding PD-L2. The PD-1 triple mutant showed a 3-fold increase of kon for PD-L2, and 14-fold for PD-L1. These results suggested that these amino acid substitutions in the loops stabilized the ligand-bound state among the conformational ensembles of apo-PD-1 (17, 19).

TABLE 3 Binding affinity (KD) and kinetic parameters (association constant kon, dissociation constant koff) for the PD-1 loop variants binding to PD-L2 or PD-L1. Binding hPD-L2 Binding hPD-L1 KD kon koff KD kon koff hPD-1 (nM) (105/M · s) (10−2/s) (nM) (105/M · s) (10−2/s) Wild-Type 500 ± 82  1.8 ± 0.44 8.4 ± 0.50  4,100 ± 110  0.36 ± 0.025  15 ± 1.4  N74G 170 ± 24  2.9 ± 0.39 4.7 ± 0.07 20,000 ± 430 0.097 ± 0.026  17 ± 3.0  T76P  12 ± 5.4 5.0 ± 0.96 0.56 ± 0.11   2,700 ± 290  0.42 ± 0.024  11 ± 1.3  A132V  69 ± 9.6 4.8 ± 0.76 3.3 ± 0.47   90 ± 23  5.3 ± 0.52 4.7 ± 0.73  N74G T76P  2.6 ± 0.62 5.8 ± 0.74 0.14 ± 0.01    72 ± 20  5.2 ± 0.80 3.6 ± 0.41  A132V N74G T76P 92 ± 1.3 3.5 ± 0.25 0.32 ± 0.03   2,700 ± 130  0.33 ± 0.020  89 ± 0.080 N74G 22 ± 4.9 4.5 ± 0.41 0.96 ± 0.12    94 ± 23  5.2 ± 0.85 4.7 ± 0.35  A132V T76P  2.6 ± 0.29 5.5 ± 0.18 0.14 ± 0.010   82 ± 18  4.8 ± 0.69 3.9 ± 0.28  A132V

Example 4: X-Ray Crystal Structure of the Human PD-1/PD-L2 Complex

The human PD-1/PD-L2 complex was crystallized using the PD-1 triple mutant. Site-directed mutagenesis was used to remove all N-linked glycosylation sites in each protein in an effort to aid crystallization, as illustrated by the protein sequences summarized in Table 4. Co-expression of the PD-1 triple mutant and the PD-L2 IgV domain yielded a stable and 1:1 stoichiometric complex, which was purified. The crystals of the human PD-1N74G T76P A132V/PD-L2IgV complex were successfully obtained, and a 2.0 Å resolution structure of the complex by X-ray crystallography was determined. The structure is illustrated, for example, in FIG. 1A. The crystal contained one PD-1/PD-L2 complex per asymmetric unit, with space group P 21 21 21. The crystallographic data collection and refinement statistics are summarized in Table 2. The human PD-1/PD-L2 complex adopted an architecture similar to the previously determined murine PD-1/PD-L2 complex (19) with a Ca root-mean-square deviation (R.M.S.D.) of 3.8 Å.

TABLE 4 Amino acid sequences. Plasmid Amino acid sequence (Parent) pST1132 (pET23d) pST1167 (pET23d) >PD-1_N74G_T76P_A132V pST1195 MGWSCIILFLVATATGVHSNPPTFSPALLVVTEGDSATFTCSFSSTSESFVL (pADD2) NWYRMSPSGQPDKLAAFPEDRSQPGQDSRFRVTQLPNGRDFHMSVVRA RRDDSGTYLCGAISLAPKVQIKESLRAELRVTERRAEPEA (SEQ ID NO: 4) >PD-L2_IgV pST1207 MIFLLLMLSLELQLHQIAALFTVTVPKELYIIEHGSDVTLECNFDTGSHVNL (pADD2) GAITASLQKVEDDTSPHRERATLLEEQLPLGKASFHIPQVQVRDEGQYQ CIIIYGVAWDYKYLTLKVKASY (SEQ ID NO: 5) Signal sequence, C-tag

The structure of human PD-1/PD-L2 complex revealed that human PD-1/PD-L2 interface was formed by the front β-sheets of both IgV domains, as illustrated in FIG. 1B, burying 1,840 Å2 (14% of the total) of solvent-accessible surface area. In the interface, notable interacting residues included the three highly conserved aromatics W110L2, Y112L2 and Y114L2 from PG of the PD-L2 IgV domain. The sidechains of these residues pointed into the center of the PD-1 ligand-binding surface, as illustrated in FIGS. 4A and 4B. To validate the interactions observed at the PD-1/PD-L2 interface, site-directed mutagenesis on several PD-1 and PD-L2 interfacial residues was performed. Using BLI, reduced binding of PD-1 interface mutants to PD-L2, and PD-L2 interface mutants to PD-1 was observed. The observed reduced binding was consistent with the structure of human PD-1/PD-L2 complex. The high-affinity loop substitutions of PD-1 localized to the interface, as illustrated in FIG. 1B. Among them, T76P and A132V made additional contacts to PD-L2, likely contributing to the increase in affinity, as illustrated in FIG. 5.

Example 5: X-Ray Crystal Structures of Human Apo-PD-1 Loop Variants

To assist analyses of the conformational change of PD-1 associated with PD-L2 binding, two human apo-PD-1 loop variants (see Table 4 for the amino acid sequences) were crystallized and their X-ray crystal structures were determined at 1.2 Å and 1.4 Å resolution, for PD-1N74G T76P A132V and PD-1T76P A132V respectively. Crystals of both variants contain a single PD-1 molecule per asymmetric unit, with space group P 32 2 1 (see Table 2 for crystallographic data collection and refinement statistics). Both PD-1 variants were well-defined by the electron density maps with a notable exception of the CC′ loop discussed further below. Superimposing the apo and PD-L2-bound PD-1N74G T76P A132V structures resulted in a Cα R.M.S.D. of 1.6 Å. The C′D loop of PD-1 (residues 83-92) was previously known to be a major part of the pembrolizumab epitope (30-32). This loop was not previously resolved in structures of human PD-1 without pembrolizumab (17, 23, 33), but it was clearly in both apo-PD-1 structures described in the present disclosure. The results of the structure determination indicated that the conformation of the loop changed significantly upon antibody binding.

Example 6: Formation of a Prominent Pocket in Human PD-1 Upon Binding PD-L2, with Human PD-1 Pocket Having Architecture Distinct from that of Murine PD-1 Pocket

The structures of the human PD-1/PD-L2 complex and apo-PD-1 variants described in the present disclosure permitted the examination of formation of human PD-1 pocket in the PD-1/PD-L2 interface. Although human apo-PD-1 has a flat ligand-binding interface, as illustrated in FIG. 2A, the structures described in the present disclosure revealed that there were rearrangements in this interface upon binding of PD-L2. These rearrangements involved residues in βC (F63, V64, N66, Y68), βF (L122, G124, I126), βG (I134, E136) and the C′D loop (E84) forming a deep and extended pocket (illustrated in FIG. 2B), accommodating PD-L2 sidechains including the aromatic residues W110L2 and Y112L2, as illustrated in FIG. 2C. Each of these residues in PD-1 is within 4.4 Å of a PD-L2 residue (Table 5).

TABLE 5 A list of atoms from PD-L2 residues within 6.0 Å distance of the PD-1 pocket residues shown in FIG. 2B. Distance measurements were generated by COCOMAPS. PD-1 PD-L2 Distance Residue Number Atom Residue Number Atom (Å) βC Phe 63 CB Trp 110 NE1 4.7 Phe 63 CE1 Ile 105 CG2 4.2 Phe 63 CD1 Val 108 O 4.0 Phe 63 CE1 Gly 107 O 4.2 Val 64 CG2 Ala 109 N 4.1 Val 64 CG2 Val 108 O 3.0 Val 64 O Trp 110 NE1 3.0 Asn 66 ND2 Asp 111 CA 4.4 Asn 66 ND2 Trp 110 O 2.9 Tyr 68 CE1 Lys 113 NZ 5.3 Tyr 68 OH Trp 110 CZ3 3.5 C′D loop Glu 84 OE1 Ala 109 CB 3.4 Glu 84 OE2 Phe 21 N 3.0 Glu 84 OE2 Thr 22 N 6.0 Glu 84 OE1 Trp 110 N 4.6 Glu 84 OE2 Leu 20 CD2 3.2 Glu 84 OE1 Val 108 O 5.5 βF Leu 122 CD1 Tyr 112 OH 4.3 Ile 126 CG2 Val 108 O 5.7 Ile 126 CD1 Ile 104 O 5.8 Ile 126 CD1 Ile 103 CG2 3.8 Ile 126 CG2 Trp 110 NE1 3.5 Ile 126 CD1 Ile 105 CD1 3.5 βG Ile 134 CB Gln 101 NE2 4.0 Ile 134 CG1 Tyr 112 CG 3.9 Ile 134 CG1 Ile 103 CD1 3.7 Ile 134 CD1 Trp 110 CZ3 3.4 Ile 134 CD1 Asp 111 O 5.6 Glu 136 OE2 Tyr 114 OH 2.6 Glu 136 OE2 Gln 101 NE2 4.4 Glu 136 OE2 Tyr 112 OH 2.6

Comparison of the PD-1 pockets in the human and murine PD-1/PD-L2 complexes demonstrated striking differences in pocket geometries. Human PD-1 pocket adopted an open, funnel-shaped architecture. Compared to murine PD-1 pocket, human PD-1 pocket has a wider entrance and a narrower exit (illustrated in FIG. 2B). The structured described in the present disclosure revealed that distinct pocket geometries arise from at least two considerations. First, human PD-1 was revealed to employ a different subset of interfacial residues to form the pocket, as compared to murine PD-1. Human PD-1 lacks an ordered PC″ strand, and thus the open pocket in human PD-1 is formed by rearranging residues F63, V64 and E84. In contrast, murine PD-1 pocket is closed with sidechains of A81 and S83 forming a boundary. Second, several sequence variations exist among the residues that form the pocket. For example, V64 and Y68 in human PD-1 are substituted with M64 and N68 in murine PD-1, respectively. To quantitatively evaluate the pocket dimensions, pocket volumes were measured using POCASA 1.1 (34). Human and murine PD-1 pockets were measured to have volumes of 130 Å3 and 154 Å3, respectively. Notably, these pockets were comparable in size to other protein cavities with established small-molecule inhibitors (20, 21, 35).

The structure of human PD-1/PD-L2 described in the present disclosure was compared with the previously determined human PD-1/PD-L1 structure (17). Superimposing the two structures resulted in a Ca R.M.S.D. of 1.5 Å for PD-1 residues. Binding PD-L1 triggered formation a much smaller cavity in human PD-1, as compared to binding of PD-L2, with the cavity having a measured volume of 40 Å3. PD-L1 lacks a large aromatic sidechain corresponding to W110L2, so the PD-1 rearrangement was revealed to involve only a small subset of the interfacial residues to accommodate the sidechain of Y123L1, corresponding to PD-L2 residue Y112L2. These results showed that the core of the human PD-1 interface had remarkable structural plasticity and the ability to form pockets with varied dimensions, permitting the interactions with different PD-1 ligands.

Example 7: The CC′ Loop in the Triple-Mutant PD-1 Adopts a Ligand-Bound Conformation in the Absence of Ligand

Conformational changes in the CC′ and FG loops upon binding of PD-L2 to human PD-1 were observed (data not shown). Earlier studies showed that the CC′ loop underwent a substantial conformational change when human PD-1 binds PD-L1 (17, 33). This CC′ loop conformational change was even larger in the human PD-1/PD-L2 structure described in the present disclosure. Strikingly, in the absence of ligands, the CC′ loop conformations of the PD-1 triple and double mutants resembled that of the ligand-bound conformations. For example, a 4.8 Å shift was observed between the Ca of T76 and P76 in the PD-1 triple mutant of apo-PD-1. When the triple-mutant PD-1 bound PD-L2, the sidechain of P76 maintained the same conformation. An increased population of the ligand-bound conformations in the mutant apo-PD-1 proteins was consistent with increased association constants (kon) of the PD-1 variants.

In contrast, the conformations of the FG loop were the same in all three apo-PD-1 structures (one with an A132L substitution in the FG loop (23) and the triple and double mutants described in the present disclosure. Upon binding PD-L1 (17), there were no significant conformational changes in the FG loop. There was, however, a substantial shift in the FG loop conformation upon binding PD-L2.

Example 8: Structural plasticity of the human PD-1 ligand-binding interface

To further investigate how the loop changes were associated with pocket formation, the apo and PD-L2-bound structures of the human triple-mutant PD-1 were superimposed (data not shown). Upon binding PD-L2, a large conformational change I in the PD-1 ligand-binding interface. A three-residue shortening of βC was observed, and βC and βF moved apart to create a deep cleft. The rearrangements that I in the pocket propagated to the edge of the FG loop, resulting in a remarkable 8.2 Å lateral shift. The overall change was less dramatic in murine PD-1. The closed architecture of the murine pocket did not require flipping of residues E84 and F63, as seen in human PD-1, and there was no secondary structure change of βC in murine PD-1. Taken together, the results described in the present disclosure provide a structural basis for systematic rearrangements at the human PD-1 ligand-binding interface coupling pocket formation and changes in the loops of PD-1 when it binds PD-L2.

Example 9: Coordinates and Structure Factors

The atomic coordinates and structure factors for human PD-1N74G T76P A132V/PD-L2IgV complex, human apo-PD-1N74G T76P A132V and apo-PD-1T76P A132V is included as Tables 6-8, respectively, which are found in an Appendix.

REFERENCE TO A SEQUENCE LISTING SUBMITTED AS A TEXT FILE VIA EFS-WEB

The official copy of the sequence listing is submitted electronically via EFS-Web as an ASCII formatted sequence listing with a file named 103182-1163588-003620US_Seq_Listing.txt, created on Apr. 23, 2020, and having a size of 7 kilobytes, which is filed concurrently with the specification. The sequence listing contained in this ASCII formatted document is part of the specification and is herein incorporated by reference in its entirety.

REFERENCES CITED IN THIS DISCLOSURE

  • 1. D. J. Byun, J. D. Wolchok, L. M. Rosenberg, M. Girotra, Cancer immunotherapy—immune checkpoint blockade and associated endocrinopathies. Nat Rev Endocrinol 10.1038/nrendo.2016.205 (2017).
  • 2. H. Borghaei et al., Nivolumab versus Docetaxel in Advanced Nonsquamous Non-Small-Cell Lung Cancer. N Engl J Med 373, 1627-1639 (2015).
  • 3. C. Robert et al., Pembrolizumab versus Ipilimumab in Advanced Melanoma. N Engl J Med 372, 2521-2532 (2015).
  • 4. L. Marcus, S. J. Lemery, P. Keegan, R. Pazdur, FDA Approval Summary: Pembrolizumab for the Treatment of Microsatellite Instability-High Solid Tumors. Clin. Cancer. Res. 25, 3753-3758 (2019).
  • 5. D. T. Le et al., Mismatch repair deficiency predicts response of solid tumors to PD-1 blockade. Science 357, 409-413 (2017).
  • 6. A. I. Minchinton, I. F. Tannock, Drug penetration in solid tumours. Nat. Rev. Cancer 6, 583-592 (2006).
  • 7. E. A. Neuwelt et al., Engaging neuroscience to advance translational research in brain barrier biology. Nat. Rev. Neurosci. 12, 169-182 (2011).
  • 8. J. L. Mikitsh, A. M. Chacko, Pathways for small molecule delivery to the central nervous system across the blood-brain barrier. Perspect Medicin Chem 6, 11-24 (2014).
  • 9. A. Shimabukuro-Vornhagen et al., Cytokine release syndrome. J Immunother Cancer 6, 56 (2018).
  • 10. A. Sindel et al., Hematopoietic stem cell mobilization following PD-1 blockade: Cytokine release syndrome after transplantation managed with ascorbic acid. Eur J Haematol 103, 134-136 (2019).
  • 11. R. J. Keizer, A. D. Huitema, J. H. Schellens, J. H. Beijnen, Clinical pharmacokinetics of therapeutic monoclonal antibodies. Clin Pharmacokinet 49, 493-507 (2010).
  • 12. G. R. Jang, R. Z. Harris, D. T. Lau, Pharmacokinetics and its role in small molecule drug discovery research. Med Res Rev 21, 382-396 (2001).
  • 13. J. K. Liu, The history of monoclonal antibody development—Progress, remaining challenges and future innovations. Ann Med Surg (Loud) 3, 113-116 (2014).
  • 14. K. Guzik et al., Small-Molecule Inhibitors of the Programmed Cell Death-1/Programmed Death-Ligand 1 (PD-1/PD-L1) Interaction via Transiently Induced Protein States and Dimerization of PD-L1. J. Med. Chem. 60, 5857-5867 (2017).
  • 15. P. Jiao et al., Small molecules as PD-1/PD-L1 pathway modulators for cancer immunotherapy. Curr. Pharm. Des. 10.2174/1381612824666181112114958 (2018).
  • 16. X. Cheng et al., Structure and interactions of the human programmed cell death 1 receptor. The Journal of biological chemistry 288, 11771-11785 (2013).
  • 17. K. M. Zak et al., Structure of the Complex of Human Programmed Death 1, PD-1, and Its Ligand PD-L1. Structure 23, 2341-2348 (2015).
  • 18. D. Y. Lin et al., The PD-1/PD-L1 complex resembles the antigen-binding Fv domains of antibodies and T cell receptors. Proceedings of the National Academy of Sciences of the United States of America 105, 3011-3016 (2008).
  • 19. E. Lazar-Molnar et al., Crystal structure of the complex between programmed death-1 (PD-1) and its ligand PD-L2. Proceedings of the National Academy of Sciences of the United States of America 105, 10483-10488 (2008).
  • 20. A. J. Souers et al., ABT-199, a potent and selective BCL-2 inhibitor, achieves antitumor activity while sparing platelets. Nat. Med. 19, 202-208 (2013).
  • 21. C. Tovar et al., MDM2 small-molecule antagonist RG7112 activates p53 signaling and regresses human tumors in preclinical cancer models. Cancer Res. 73, 2587-2597 (2013).
  • 22. X. Zhang et al., Structural and functional analysis of the costimulatory receptor programmed death-1. Immunity 20, 337-347 (2004).
  • 23. E. Lazar-Molnar et al., Structure-guided development of a high-affinity human Programmed Cell Death-1: Implications for tumor immunotherapy. EBioMedicine 17, 30-44 (2017).
  • 24. J. D. Bloom, An experimentally determined evolutionary model dramatically improves phylogenetic fit. Mol. Biol. Evol. 31, 1956-1978 (2014).
  • 25. G. Chao et al., Isolating and engineering human antibodies using yeast surface display. Nat Protoc 1, 755-768 (2006).
  • 26. J. Lyu et al., Ultra-large library docking for discovering new chemotypes. Nature 566, 224-229 (2019).
  • 27. D. M. Fowler, S. Fields, Deep mutational scanning: a new style of protein science. Nat. Methods 11, 801-807 (2014).
  • 28. R. L. Maute et al., Engineering high-affinity PD-1 variants for optimized immunotherapy and immuno-PET imaging. Proceedings of the National Academy of Sciences of the United States of America 112, E6506-6514 (2015).
  • 29. Y. Li et al., High-affinity PD-1 molecules deliver improved interaction with PD-L1 and PD-L2. Cancer Sci. 109, 2435-2445 (2018).
  • 30. J. Y. Lee et al., Structural basis of checkpoint blockade by monoclonal antibodies in cancer immunotherapy. Nat Commun 7, 13354 (2016).
  • 31. S. Horita et al., High-resolution crystal structure of the therapeutic antibody pembrolizumab bound to the human PD-1. Sci Rep 6, 35297 (2016).
  • 32. Z. Na et al., Structural basis for blocking PD-1-mediated immune suppression by therapeutic antibody pembrolizumab. Cell Res. 27, 147-150 (2017).
  • 33. R. Pascolutti et al., Structure and Dynamics of PD-L1 and an Ultra-High-Affinity PD-1 Receptor Mutant. Structure 24, 1719-1728 (2016).
  • 34. J. Yu, Y. Zhou, I. Tanaka, M. Yao, Roll: a new algorithm for the detection of protein pockets and cavities with a rolling probe sphere. Bioinformatics 26, 46-52 (2010).
  • 35. M. R. Arkin, Y. Tang, J. A. Wells, Small-molecule inhibitors of protein-protein interactions: progressing toward the reality. Chem. Biol. 21, 1102-1114 (2014).
  • 36. C. Corbi-Verge, P. M. Kim, Motif mediated protein-protein interactions as drug targets. Cell Commun Signal 14, 8 (2016).
  • 37. A. E. Modell, S. L. Blosser, P. S. Arora, Systematic Targeting of Protein-Protein Interactions. Trends Pharmacol. Sci. 37, 702-713 (2016).
  • 38. I. H. Moal, P. A. Bates, Kinetic rate constant prediction supports the conformational selection mechanism of protein binding. PLoS Comput Biol 8, e1002351 (2012).
  • 39. K. G. Daniels, Y. Suo, T. G. Oas, Conformational kinetics reveals affinities of protein conformational states. Proceedings of the National Academy of Sciences of the United States of America 112, 9352-9357 (2015).
  • 40. M. J. Caulfield et al., Small molecule mimetics of an HIV-1 gp41 fusion intermediate as vaccine leads. The Journal of biological chemistry 285, 40604-40611 (2010).
  • 41. S. Eyrisch, V. Helms, Transient pockets on protein surfaces involved in protein-protein interaction. J Med. Chem. 50, 3457-3464 (2007).
  • 42. W. Minor, M. Cymborowski, Z. Otwinowski, M. Chruszcz, HKL-3000: the integration of data reduction and structure solution—from diffraction images to an initial model in minutes. Acta crystallographica. Section D, Biological crystallography 62, 859-866 (2006).
  • 43. P. D. Adams et al., PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr., Sect. D: Biol. Crystallogr. 66, 213-221 (2010).
  • 44. G. E. Palade, Studies on the endoplasmic reticulum. II. Simple dispositions in cells in situ. J Biophys Biochem Cytol 1, 567-582 (1955).
  • 45. E. T. Boder, K. D. Wittrup, Yeast surface display for screening combinatorial polypeptide libraries. Nat. Biotechnol. 15, 553-557 (1997).
  • 46. J. Lyu et al., Ultra-large library docking for discovering new chemotypes. Nature 566, 224-229 (2019)
  • 47. A. Stank et al., Protein Binding Pocket Dynamics. Acc. Chem. Res. 49, 809-815 (2016)
  • 48. P. Wipf et al. in The Practice of Medicinal Chemistry (Fourth Edition), Chapter 11, C. Wermuth et al., Eds, Academic Press, 4th edition, pages 279-299 (2015)
  • 49. R. Abagyan and M. Totrov, High-throughput docking for lead generation, Current Opinion in Chemical Biology, Vol. 5, 375-382 (2001).
  • 50. M. L. Lamb et al., Design, docking, and evaluation of multiple libraries against multiple targets, Proteins, Vol. 42, 296-318 (2001).
  • 51. B. Waszkowycz et al. Large-scale virtual screening for discovering leads in the postgenomic era, IBM Systems Journal, Vol. 40, No. 2 (2001).
  • 52. B. K. Shoichet et al. Molecular docking using shape descriptors, J Comp Chem, Vol. 13 No. 3, 380-397 (1992).
  • 53. T. J. A. Ewing et al. Critical Evaluation of Search Algorithms for Automated Molecular Docking and Database Screening, J. Computational Chemistry, Vol. 18 No. 9, 1175-1189 (1997).
  • 54. Kastenholz, M. A. et al. GRID/CPCA: A new computational tool to design selective ligands, J. Medicinal Chemistry, Vol. 43, 3033-3044 (2000).
  • 55. Miller, M. D. et al. FLOG: a system to select ‘quasi-flexible’ ligands complementary to a receptor of known three-dimensional structure, J. Computer Aided Molecular Design, Vol. 8 No. 2, 153-174 (1994).
  • 56. Sobolev, V. et al. Molecular docking using surface complementarity, Proteins, Vol. 25, 120-129 (1996).
  • 57. Aloy, P. et al. Modeling Protein Docking using Shape Complementarity, Electrostatics and Biochemical Information, Proteins: Structure, Function, and Genetics, Vol. 33, 535-549 (1998).
  • 58. Ritchie, D. W. and Kemp. G. J. L., Fast Computation, Rotation, and Comparison of Low Resolution Spherical Harmonic Molecular Surfaces, Proteins: Structure, Function, and Genetics, Vol. 39, 178-194 (2000).
  • 59. Fischer, D. et al. Surface motifs by a computer vision technique: searches, detection, and implications for protein-ligand recognition, Proteins, Vol. 16, 278-292 (1993).
  • 60. Rarey, M. et al. Placement of medium-sized molecular fragments into active sites of proteins, J. Computer-Aided Molecular Design, Vol. 10, 41-54 (1996).
  • 61. Kramer, B. et al. Evaluation of the FlexX incremental construction algorithm for protein-ligand docking, Proteins, Vol. 37, 228-241 (1999).
  • 62. Rarey, M. et al. A Fast Flexible Docking Method Using An Incremental Construction Algorithm, J. Mol. Biol., Vol. 261, 470-489 (1996).
  • 63. Welch, W. et al. Hammerhead: Fast, fully automated docking of flexible ligands to protein binding sites, Chemical Biology, Vol. 3, 449-462 (1996).
  • 64. Leach, A. R., Kuntz, I.D., Conformational Analysis of Flexible Ligands in Macromolecular Receptor Sites, J. Comp. Chem., Vol. 13, 730-748 (1992).
  • 65. Bohm, H. J., The computer program LUDI: a new method for the de novo design of enzyme inhibitors, J. Computer-Aided Molecular Design, Vol. 6, 61-78 (1992).
  • 66. Bohacek, R. S. and McMartin, C., Multiple Highly Diverse Structures Complementary to Enzyme Binding Sites: Results of Extensive Application of a de Novo Design Method Incorporating Combinatorial Growth, J. American Chemical Society, Vol. 116, 5560-5571 (1994).
  • 67. DesJarlais, R. L. et al. Docking Flexible Ligands to Macromolecular Receptors by Molecular Shape, J. Med. Chem., Vol. 29, 2149-2153 (1986).
  • 68. Claussen, H. et al. FlexE: Efficient Molecular Docking Considering Protein Structure Variations, J Molecular Biology, Vol. 308, 377-395 (2001).
  • 69. Abagyan, R. A. et al. Biased probability Monte Carlo conformational searches and electrostatic calculations for peptides and proteins, J Comp. Chem., Vol. 15, 488-506 (1994).
  • 70. Halgren, T. A. et al. Glide: a new approach for rapid, accurate docking and scoring. 2.
  • Enrichment factors in database screening, J Med Chem., Vol. 47 No. 7, 1750-1759, (2004). 71. Luty, B. A. et al. Molecular Mechanics/Grid Method for the Evaluation of Ligand-Receptor Interactions, J. Comp. Chem., Vol. 16, 454-464 (1995).
  • 72. Goodsell et al. Automated Docking of Substrates to Proteins by Simulated Annealing, Proteins: Structure, Function, and Genetics, Vol. 8, 195-202 (1990).
  • 73. Jones, G. et al. Molecular Recognition of Receptor Sites using a Genetic Algorithm with a Description of Desolvation, J Mol. Biol., Vol. 245, 43-53 (1995).
  • 74. Jones, G. et al. Development and Validation of a Genetic Algorithm for Flexible Docking, Mol. Biol., Vol. 267, 727-748 (1997).
  • 75. Taylor, J. S. and Burnett, R. M., Proteins, Vol. 41, 173-191 (2000).
  • 76. Morris, G. M. et al. Automated Docking Using a Lamarckian Genetic Algorithm and an Empirical Binding Free Energy Function, J Comp. Chem., Vol. 19, 1639-1662 (1998).
  • 77. Di Nola, A. et al. Molecular Dynamics Simulation of the Docking of Substrates to Proteins, Proteins, Vol. 19, 174-182 (1994).
  • 78. Wang, J. et al. Proteins, Vol. 36, 1-19 (1999).
  • 79. Bohm, H.J., The Development of a simple empirical scoring function to estimate the binding constant for a protein-ligand complex of known three-dimensional structure, J Comput-Aided Mol. Des., Vol. 8, 243-256 (1994).
  • 80. Wang, R. et al. A new empirical method for estimating the binding affinity of a protein-ligand complex., J Molecular Modeling, Vol. 4, 379 (1998).
  • 81. Eldridge, M. D. et al. Empirical scoring functions: I. The development of a fast empirical scoring function to estimate the binding affinity of ligands in receptor complexes, J. Computer-Aided Molecular Design, Vol. 11, 425-445 (1997).
  • 82. Gelhaar, D. K. et al. In Rational Drug Design: Novel Methodology and Practical Applications, Parrill, L., Reddy, M. R., Ed.; American Chemical Society: Washington, D.C., pp. 292-311 (1999).
  • 83. Rognan D. et al. J. Medicinal Chemistry, Vol. 42, 4650-4658 (1999).
  • 84. Halgren, T. A. et al. Glide: a new approach for rapid, accurate docking and scoring. 2. Enrichment factors in database screening, J Med Chem., Vol. 47 No. 7, 1750-1759 (2004).
  • 85. Pearlman, D. A. et al. AMBER 4.1, University of California, San Francisco (1995).
  • 86. Cornell, W. D. et al. A second-generation force field for the simulation of proteins, nucleic acids, and organic molecules, J. American Chemical Society, Vol. 117, 5179-5197 (1995).
  • 87. Jorgensen, W. L., & Tirado-Rives, J American Chemical Society, Vol. 110, 1657-1666 (1988).
  • 88. Halgren, T. A., Merck Molecular Force Field. I. Basis, Form, Scope, Parameterization, and Performance of MMFF94, J. Comp. Chem., Vol. 17, 490-519 (1996).
  • 89. Brooks, B. R. et al. CHARMM: A Program for Macromolecular Energy, Minimization, and Dynamics Calculations, J. Comp. Chem., Vol. 4, 187-217 (1983).
  • 90. Stewart, J. J. P., Quantum Chemistry Program Exchange, Vol. 10:86 (1990).
  • 91. Liotard, D. A. et al. Quantum Chemistry Program Exchange—no. 506, QCPE Bulletin, Vol. 9: 123 (1989).
  • 92. AMSOL-version 6.5.1 by G. D. Hawkins et al. University of Minnesota, Minneapolis (1997).
  • 93. Gohlke, H. et al. Knowledge-based Scoring Function to Predict Protein-Ligand Interactions, J Mol. Biol., Vol. 295, 337-356 (2000).
  • 94. Muegge, I. and Martin, Y. C., A general and fast scoring function for protein-ligand interactions—a simplified potential approach., J. Med. Chem., Vol. 42, 791-804 (1999).
  • 95. Mitchell, J. B. O. et al. BLEEP—Potential of Mean Force Describing Protein-Ligand Interactions II. Calculation of Binding Energies and Comparison with Experimental Data, J. Comp. Chem., Vol. 20, 1165-1176 (1999).
  • 96. Head, R. D. et al. VALIDATE: A New Method for Receptor-Based Prediction of Binding Affinities of Novel Ligand, J. American Chemical Society, Vol. 118, 3959-3969 (1996).
  • 97. Bissantz, C. et al. Protein-based virtual screening of chemical databases. 1. Evaluation of different docking/scoring combinations, J Med Chem, Vol. 43, 4759-4767 (2000).
  • 98. Gilson, M. K., and Honig, B., Calculation of the Total Electrostatic Energy of a Macromolecular System: Solvation Energies, Binding Energies, and Conformational Analysis, Proteins, Vol. 4, 7-18 (1988).
  • 99. Mehler, E. L. and Solmajer, T., Electrostatic effects in proteins: comparison of dielectric and charge models Protein Engineering, Vol. 4, 903-910 (1991).
  • 99. Hoist, M. et al. Adaptive Multilevel Finite Element Solution of the Poisson-Boltzmann Equations I. Algorithms and Examples, J Comp. Chem., Vol. 21, No. 15, 1319-1342 (2000).
  • 100. Nicholls, A., and Honig, B., A Rapid Finite Difference Algorithm, Utilizing Successive Over-Relaxation to Solve Poisson-Boltzmann Equation, J Comp. Chem., Vol. 12, No. 4, 435-445 (1991)
  • 101. Still, W. C. et al. A General Treatment of Solvation for Molecular Mechanics, J. Am. Chem. Soc., Vol. 112, 6127-6129 (1990).
  • 102. Ghosh, A. et al. A Generalized Born Model Based on Surface Integral Formulation, J. Physical Chemistry B., Vol. 102, 10983-10 (1988).
  • 103. Eisenberg, D., and McLachlan, A. D., Solvation Energy in Protein Folding and Binding, Nature, Vol. 31, 3086 (1986).
  • 104. Privalov, P. L., and Makhatadze, G. I., Contribution of hydration to protein folding thermodynamics, J Mol. Bio., Vol. 232, 660-679 (1993).
  • 105. Stouten, P. F. W. et al. An effective solvation term based on atomic occupancies for use in protein simulations, Molecular Simulation, Vol. 10, No. 2-6, 97-120 (1993).
  • 106. Bash, P. et al. Free Energy Calculation by Computer Simulation, Science, Vol. 236, 564 (1987).
  • 107. Jorgensen, W. L. et al. Relative Partition Coefficients for Organic Solutes from Fluid Simulations, J Phys. Chem., Vol. 94, 1683-1686 (1990).
  • 108. Jackson, R. M. Rapid Refinement of Protein Interfaces Incorporating Solvation: Application to the Docking Problem, J Mol. Biol., Vol. 276, 265-285 (1998).
  • 109. Labanowski and J. Andzelm, editors, Density Functional Methods in Chemistry, Springer-Verlag, New York (1991).
  • 110. LaBute et al. Adverse Drug Reaction Prediction Using Scores Produced by Large-Scale Drug-Protein Target Docking on High-Performance Computing Machines, PloS One 9(9): e106298 (2014)
  • 111. Wang et al. TargetHunter: An In Silico Target Identification Tool for Predicting Therapeutic Potential of Small Organic Molecules Based on Chemogenic Database, The AAPS Journal 15(2): 395-406 (2013)
  • 112. Keiser, M. J. (2015) In Silico Prediction of Drug Side Effects, in Antitargets and Drug Safety (eds L. Urbán, V. F. Patel and R. J. Vaz), Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim, Germany.
  • 113. Bowes et al. Reducing safety-related drug attrition: The use of in vitro pharmacological profiling, Nature Review Drug Discovery 11:909 (2012)
  • 114. Erlanson D.A. (2011) Introduction to Fragment-Based Drug Discovery. In: Davies T., Hyvönen M. (eds) Fragment-Based Drug Discovery and X-Ray Crystallography. Topics in Current Chemistry, vol 317. Springer, Berlin, Heidelberg
  • 115. Murray, C., Rees, D. The rise of fragment-based drug discovery. Nature Chem. 1:187-192 (2009)
  • 116. Jutz et al. A cellular platform for the evaluation of immune checkpoint molecules. Oncotarget 8(39):64892-64906 (2017)
  • 117. Ganesan, A. et al. Comprehensive in vitro characterization of PD-L1 small molecule inhibitors. Sci Rep 9:12392 (2019)
  • 118. Selby et al. Preclinical Development of Ipilimumab and Nivolumab Combination Immunotherapy: Mouse Tumor Models, In Vitro Functional Studies, and Cynomolgus Macaque Toxicology. PLoS One September 9; 11(9):e0161779 (2016)

In the foregoing description, numerous specific details are set forth to provide a more thorough understanding of the present invention. However, it will be apparent to one of skill in the art that the invention described in this disclosure may be practiced without one or more of these specific details. In other instances, well-known features and procedures well known to those skilled in the art have not been described in order to avoid obscuring the invention. Embodiments of the disclosure have been described for illustrative and not restrictive purposes. Although the present invention is described primarily with reference to specific embodiments, it is also envisioned that other embodiments will become apparent to those skilled in the art upon reading the present disclosure, and it is intended that such embodiments be contained within the present inventive methods. Accordingly, the present disclosure is not limited to the embodiments described above or depicted in the drawings, and various embodiments and modifications can be made without departing from the scope of the claims below. All publications, patents, and patent applications cited herein are hereby incorporated by reference in their entirety for all purposes.

APPENDIX

TABLE 6 Atomic coordinates and structure factors for the human PD 1N74G T76P A132V/PD-L2IgV complex (based on a PDB file). CRYST1 41.291   67.798   89.701  90.00  90.00  90.00 P 21 21 21 SCALE1   0.024218  0.000000  0.000000     0.00000 SCALE2   0.000000  0.014750  0.000000     0.00000 SCALE3   0.000000  0.000000  0.011148     0.00000 ATOM 1 O ASN A 33 −21.189 −9.931 21.441 1.00101.06 O ANISOU 1 O ASN A 33 12153 12425 13822 −1086 −350 −3162 O ATOM 2 N ASN A 33 −24.027 −9.539 19.170 1.00111.31 N ANISOU 2 N ASN A 33 12657 14221 15414 −1189 −1298 −4138 N ATOM 3 CA ASN A 33 −23.199 −10.217 20.160 1.00108.35 C ANISOU 3 CA ASN A 33 12515 13486 15165 −1354 −857 −3959 C ATOM 4 C ASN A 33 −21.841 −9.544 20.469 1.00 99.06 C ANISOU 4 C ASN A 33 11702 12421 13515 −1050 −713 −3465 C ATOM 5 CB ASN A 33 −22.990 −11.673 19.738 1.00117.04 C ANISOU 5 CB ASN A 33 13811 14236 16424 −1494 −767 −4198 C ATOM 6 CG ASN A 33 −24.293 −12.464 19.739 1.00126.13 C ANISOU 6 CG ASN A 33 14633 15208 18082 −1793 −735 −4454 C ATOM 7 OD1 ASN A 33 −25.348 −11.936 20.099 1.00128.87 O ANISOU 7 OD1 ASN A 33 14584 15691 18689 −1896 −755 −4480 O ATOM 8 ND2 ASN A 33 −24.230 −13.727 19.323 1.00130.65 M ANISOU 8 ND2 ASN A 33 15361 15477 18804 −1918 −674 −4657 N ATOM 9 N PRO A 34 −21.406 −8.542 19.665 1.00 83.38 N ANISOU 9 N PRO A 34 9812 10792 11076 −746 −988 −3389 N ATOM 10 C PRO A 34 −21.072 −6.991 21.522 1.00 57.91 C ANISOU 10 C PRO A 34 6522 7668 7811 −674 −635 −2704 C ATOM 11 O PRO A 34 −22.283 −6.799 21.518 1.00 57.97 O ANISOU 11 O PRO A 34 6198 7745 8083 −806 −767 −2918 O ATOM 12 CA PRO A 34 −20.437 −7.630 20.294 1.00 70.58 C ANISOU 12 CA PRO A 34 8364 9278 9176 −553 −802 −2919 C ATOM 13 CB PRO A 34 −20.177 −6.572 19.220 1.00 71.52 C ANISOU 13 CB PRO A 34 8581 9745 8847 −265 −1094 −2905 C ATOM 14 CG PRO A 34 −20.529 −7.209 17.951 1.00 75.86 C ANISOU 14 CG PRO A 34 9187 10337 9300 −230 −1392 −3325 C ATOM 15 CD PRO A 34 −21.520 −8.309 18.213 1.00 81.93 C ANISOU 15 CD PRO A 34 9694 10865 10569 −546 −1405 −3685 C ATOM 16 N PRO A 35 −20.283 −6.644 22.545 1.00 49.94 N ANISOU 16 N PRO A 35 5665 6595 6714 −610 −366 −2322 N ATOM 17 CA PRO A 35 −20.963 −6.060 23.705 1.00 46.59 C ANISOU 17 CA PRO A 35 5050 6163 6489 −715 −199 −2154 C ATOM 18 C PRO A 35 −21.633 −4.748 23.352 1.00 47.39 C ANISOU 18 C PRO A 35 4920 6581 6503 −599 −450 −2180 C ATOM 19 O PRO A 35 −21.251 −4.083 22.386 1.00 41.97 O ANISOU 19 O PRO A 35 4329 6117 5500 −383 −706 −2188 O ATOM 20 CB PRO A 35 −19.832 −5.808 24.717 1.00 41.10 C ANISOU 20 CB PRO A 35 4615 5394 5608 −589 39 −1769 C ATOM 21 CG PRO A 35 −18.623 −6.495 24.148 1.00 40.77 C ANISOU 21 CG PRO A 35 4843 5271 5375 −457 29 −1764 C ATOM 22 CD PRO A 35 −18.821 −6.534 22.664 1.00 43.69 C ANISOU 22 CD PRO A 35 5171 5801 5628 −408 −251 −2054 C ATOM 23 N THR A 36 −22.653 −4.389 24.121 1.00 49.01 N ANISOU 23 N THR A 36 4845 6786 6990 −727 −350 −2192 N ATOM 24 CA THR A 36 −23.241 −3.073 23.972 1.00 48.00 C ANISOU 24 CA THR A 36 4516 6929 6791 −572 −557 −2174 C ATOM 25 C THR A 36 −22.754 −2.242 25.152 1.00 42.95 C ANISOU 25 C THR A 36 4003 6277 6041 −501 −306 −1810 C ATOM 26 O THR A 36 −22.334 −2.781 26.167 1.00 39.95 O ANISOU 26 O THR A 36 3776 5686 5717 −606 13 −1640 O ATOM 27 CB THR A 36 −24.757 −3.132 23.911 1.00 51.22 C ANISOU 27 CB THR A 36 4462 7389 7610 −717 −665 −2501 C ATOM 28 OG1 THR A 36 −25.245 −3.728 25.112 1.00 56.97 O ANISOU 28 OG1 THR A 36 5059 7872 8715 −994 −241 −2467 O ATOM 29 CG2 THR A 36 −25.219 −3.968 22.694 1.00 54.62 C ANISOU 29 CG2 THR A 36 4758 7844 8152 −780 −988 −2933 C ATOM 30 N PHE A 37 −22.799 −0.928 25.006 1.00 42.88 N ANISOU 30 N PHE A 37 3965 6475 5852 −298 −465 −1702 N ATOM 31 CA PHE A 37 −22.126 −0.050 25.939 1.00 42.42 C ANISOU 31 CA PHE A 37 4075 6413 5630 −202 −289 −1391 C ATOM 32 C PHE A 37 −22.893 1.261 25.947 1.00 43.95 C ANISOU 32 C PHE A 37 4087 6775 5837 −57 −425 −1388 C ATOM 33 O PHE A 37 −23.025 1.900 24.898 1.00 43.18 O ANISOU 33 O PHE A 37 3989 6838 5580 128 −724 −1452 O ATOM 34 CB PHE A 37 −20.673 0.141 25.507 1.00 42.11 C ANISOU 34 CB PHE A 37 4355 6392 5252 −63 −327 −1214 C ATOM 35 CG PHE A 37 −19.811 0.814 26.536 1.00 41.18 C ANISOU 35 CG PHE A 37 4397 6235 5015 −4 −154 −952 C ATOM 36 CD1 PHE A 37 −19.221 2.030 26.261 1.00 42.27 C ANISOU 36 CD1 PHE A 37 4629 6481 4950 150 −239 −820 C ATOM 37 CD2 PHE A 37 −19.587 0.220 27.768 1.00 39.98 C ANISOU 37 CD2 PHE A 37 4326 5917 4945 −94 90 −852 C ATOM 38 CE1 PHE A 37 −18.391 2.647 27.184 1.00 39.97 C ANISOU 38 CE1 PHE A 37 4453 6149 4585 185 −114 −641 C ATOM 39 CE2 PHE A 37 −18.790 0.825 28.704 1.00 39.54 C ANISOU 39 CE2 PHE A 37 4422 5847 4755 −9 179 −662 C ATOM 40 CZ PHE A 37 −18.181 2.046 28.408 1.00 39.80 C ANISOU 40 CZ PHE A 37 4487 6004 4630 118 61 −581 C ATOM 41 O SER A 38 −23.717 3.063 29.391 1.00 42.91 O ANISOU 41 O SER A 38 3867 6531 5906 −53 229 −1042 O ATOM 42 N SER A 38 −23.442 1.646 27.100 1.00 40.45 N ANISOU 42 N SER A 38 3518 6284 5567 −112 −201 −1320 N ATOM 43 C SER A 38 −24.207 3.590 28.388 1.00 44.20 C ANISOU 43 C SER A 38 3858 6843 6092 71 −62 −1170 C ATOM 44 CA SER A 38 −24.375 2.769 27.105 1.00 42.20 C ANISOU 44 CA SER A 38 3507 6648 5881 31 −322 −1378 C ATOM 45 CB SER A 38 −25.818 2.250 26.963 1.00 50.60 C ANISOU 45 CB SER A 38 4116 7750 7359 −93 −360 −1699 C ATOM 46 OG SER A 38 −26.193 1.570 28.143 1.00 51.89 O ANISOU 46 OG SER A 38 4187 7736 7794 −340 64 −1692 O ATOM 47 N PRO A 39 −24.609 4.877 28.364 1.00 42.13 N ANISOU 47 N PRO A 39 3528 6683 5798 273 −180 −1144 N ATOM 48 CA PRO A 39 −25.211 5.580 27.221 1.00 42.61 C ANISOU 48 CA PRO A 39 3445 6902 5841 496 −547 −1267 C ATOM 49 C PRO A 39 −24.159 6.005 26.227 1.00 41.21 C ANISOU 49 C PRO A 39 3616 6748 5293 648 −752 −1117 C ATOM 50 O PRO A 39 −22.966 6.034 26.577 1.00 36.56 O ANISOU 50 O PRO A 39 3314 6062 4514 586 −589 −919 O ATOM 51 CB PRO A 39 −25.884 6.792 27.873 1.00 46.77 C ANISOU 51 CB PRO A 39 3852 7454 6464 665 −493 −1239 C ATOM 52 CG PRO A 39 −25.040 7.075 29.062 1.00 42.57 C ANISOU 52 CG PRO A 39 3592 6784 5798 588 −179 −1020 C ATOM 53 CD PRO A 39 −24.573 5.719 29.574 1.00 42.15 C ANISOU 53 CD PRO A 39 3613 6626 5775 324 53 −1004 C ATOM 54 N ALA A 40 −24.571 6.315 25.007 1.00 42.34 N ANISOU 54 N ALA A 40 3740 7017 5330 854 −1096 −1221 N ATOM 55 CA ALA A 40 −23.631 6.754 23.977 1.00 40.44 C ANISOU 55 CA ALA A 40 3882 6782 4703 1015 −1234 −1063 C ATOM 56 C ALA A 40 −22.950 8.050 24.389 1.00 43.29 C ANISOU 56 C ALA A 40 4504 7037 4906 1125 −1089 −793 C ATOM 57 O ALA A 40 −21.808 8.304 23.985 1.00 40.86 O ANISOU 57 O ALA A 40 4518 6657 4352 1126 −1001 −615 O ATOM 58 CB ALA A 40 −24.360 6.931 22.585 1.00 41.32 C ANISOU 58 CB ALA A 40 3983 7050 4666 1292 −1663 −1228 C ATOM 59 N LEU A 41 −23.659 8.869 25.171 1.00 43.52 N ANISOU 59 N LEU A 41 4381 7045 5109 1209 −1043 −791 N ATOM 60 CA LEU A 41 −23.142 10.151 25.660 1.00 39.16 C ANISOU 60 CA LEU A 41 4059 6358 4462 1305 −908 −583 C ATOM 61 C LEU A 41 −23.457 10.291 27.152 1.00 38.91 C ANISOU 61 C LEU A 41 3854 6267 4662 1189 −666 −613 C ATOM 62 O LEU A 41 −24.600 10.380 27.538 1.00 39.67 O ANISOU 62 O LEU A 41 3664 6426 4984 1260 −685 −758 O ATOM 63 CB LEU A 41 −23.756 11.330 24.892 1.00 38.46 C ANISOU 63 CB LEU A 41 4078 6270 4264 1656 −1144 −540 C ATOM 64 CG LEU A 41 −23.569 12.725 25.539 1.00 39.47 C ANISOU 64 CG LEU A 41 4385 6217 4396 1769 −999 −380 C ATOM 65 CD1 LEU A 41 −22.083 13.004 25.798 1.00 37.63 C ANISOU 65 CD1 LEU A 41 4466 5809 4024 1575 −744 −188 C ATOM 66 CD2 LEU A 41 −24.107 13.816 24.629 1.00 42.71 C ANISOU 66 CD2 LEU A 41 4987 6584 4658 2157 −1239 −304 C ATOM 67 N LEU A 42 −22.431 10.308 27.976 1.00 36.39 N ANISOU 67 N LEU A 42 3711 5835 4280 1029 −440 −495 N ATOM 68 C LEU A 42 −21.992 11.678 29.943 1.00 36.30 C ANISOU 68 C LEU A 42 3859 5627 4308 1020 −140 −412 C ATOM 69 O LEU A 42 −20.832 11.976 29.667 1.00 36.38 O ANISOU 69 O LEU A 42 4090 5552 4180 965 −138 −305 O ATOM 70 CD1 LEU A 42 −23.306 9.093 32.109 1.00 39.82 C ANISOU 70 CD1 LEU A 42 3913 6159 5059 669 340 −626 C ATOM 71 CD2 LEU A 42 −21.099 7.841 32.101 1.00 38.26 C ANISOU 71 CD2 LEU A 42 4087 5884 4564 480 317 −463 C ATOM 72 CA LEU A 42 −22.585 10.372 29.435 1.00 38.27 C ANISOU 72 CA LEU A 42 3882 6014 4643 937 −206 −517 C ATOM 73 CB LEU A 42 −21.878 9.183 30.087 1.00 35.67 C ANISOU 73 CB LEU A 42 3598 5665 4290 711 −42 −506 C ATOM 74 CG LEU A 42 −21.882 9.100 31.625 1.00 38.22 C ANISOU 74 CG LEU A 42 3964 5918 4638 640 207 −504 C ATOM 75 N VAL A 43 −22.774 12.474 30.652 1.00 36.07 N ANISOU 75 N VAL A 43 3759 5559 4388 1144 −70 −467 N ATOM 76 CA VAL A 43 −22.306 13.784 31.082 1.00 34.96 C ANISOU 76 CA VAL A 43 3841 5251 4191 1233 −22 −404 C ATOM 77 C VAL A 43 −22.431 13.835 32.595 1.00 38.56 C ANISOU 77 C VAL A 43 4295 5671 4684 1178 191 −488 C ATOM 78 O VAL A 43 −23.509 13.615 33.130 1.00 41.78 O ANISOU 78 O VAL A 43 4501 6149 5225 1233 305 −591 O ATOM 79 CB VAL A 43 −23.109 14.943 30.444 1.00 40.48 C ANISOU 79 CB VAL A 43 4551 5888 4941 1519 −154 −392 C ATOM 80 CG1 VAL A 43 −22.628 16.281 30.961 1.00 42.09 C ANISOU 80 CG1 VAL A 43 5013 5859 5122 1586 −64 −342 C ATOM 81 CG2 VAL A 43 −23.057 14.897 28.893 1.00 49.38 C ANISOU 81 CG2 VAL A 43 5760 7054 5947 1638 −385 −297 C ATOM 82 N AVAL A 44 −21.318 14.134 33.267 0.42 35.68 N ANISOU 82 N AVAL A 44 4155 5200 4203 1079 247 −464 N ATOM 83 CA AVAL A 44 −21.217 14.103 34.730 0.42 36.28 C ANISOU 83 CA AVAL A 44 4322 5249 4215 1047 409 −550 C ATOM 84 C AVAL A 44 −20.440 15.329 35.240 0.42 36.32 C ANISOU 84 C AVAL A 44 4553 5078 4168 1075 384 −598 C ATOM 85 O AVAL A 44 −19.559 15.832 34.545 0.42 35.50 O ANISOU 85 O AVAL A 44 4537 4873 4079 1014 279 −544 O ATOM 86 CB AVAL A 44 −20.505 12.809 35.201 0.42 34.79 C ANISOU 86 CB AVAL A 44 4180 5136 3901 888 448 −527 C ATOM 87 CG1 AVAL A 44 −20.607 12.646 36.701 0.42 33.76 C ANISOU 87 CG1 AVAL A 44 4201 4991 3638 913 623 −596 C ATOM 88 CG2 AVAL A 44 −21.054 11.565 34.460 0.42 31.56 C ANISOU 88 CG2 AVAL A 44 3570 4844 3576 811 455 −487 C ATOM 89 N BVAL A 44 −21.316 14.072 33.280 0.58 35.37 N ANISOU 89 N BVAL A 44 4111 5167 4162 1073 250 −465 N ATOM 90 CA BVAL A 44 −21.332 14.226 34.738 0.58 36.42 C ANISOU 90 CA BVAL A 44 4334 5259 4245 1068 414 −556 C ATOM 91 C BVAL A 44 −20.605 15.488 35.171 0.58 36.63 C ANISOU 91 C BVAL A 44 4583 5106 4229 1104 386 −599 C ATOM 92 O BVAL A 44 −19.922 16.151 34.390 0.58 36.08 O ANISOU 92 O BVAL A 44 4601 4918 4188 1079 284 −538 O ATOM 93 CB BVAL A 44 −20.682 13.028 35.471 0.58 34.57 C ANISOU 93 CB BVAL A 44 4169 5093 3874 919 484 −551 C ATOM 94 CG1 BVAL A 44 −21.524 11.767 35.297 0.58 35.02 C ANISOU 94 CG1 BVAL A 44 4033 5264 4010 857 594 −536 C ATOM 95 CG2 BVAL A 44 −19.221 12.801 34.983 0.58 27.21 C ANISOU 95 CG2 BVAL A 44 3335 4141 2864 801 324 −498 C ATOM 96 N THR A 45 −20.768 15.811 36.435 1.00 34.64 N ANISOU 96 N THR A 45 4440 4813 3909 1156 506 −717 N ATOM 97 CA THR A 45 −20.067 16.938 37.036 1.00 36.77 C ANISOU 97 CA THR A 45 4925 4904 4143 1172 468 −826 C ATOM 98 C THR A 45 −18.768 16.431 37.670 1.00 36.41 C ANISOU 98 C THR A 45 4999 4887 3946 1028 370 −891 C ATOM 99 O THR A 45 −18.772 15.336 38.250 1.00 33.44 O ANISOU 99 O THR A 45 4636 4652 3418 1012 414 −875 O ATOM 100 CB THR A 45 −20.967 17.609 38.085 1.00 41.43 C ANISOU 100 CB THR A 45 5593 5436 4711 1347 632 −965 C ATOM 101 OG1 THR A 45 −22.164 18.071 37.437 1.00 45.85 O ANISOU 101 OG1 THR A 45 5982 5982 5455 1518 688 −927 O ATOM 102 CG2 THR A 45 −20.263 18.784 38.730 1.00 44.32 C ANISOU 102 CG2 THR A 45 6199 5594 5046 1361 576 −1128 C ATOM 103 O GLU A 46 −17.203 17.173 40.282 1.00 35.69 O ANISOU 103 O GLU A 46 5349 4697 3515 1064 187 −1336 O ATOM 104 N GLU A 46 −17.671 17.189 37.556 1.00 36.77 N ANISOU 104 N GLU A 46 5126 4790 4055 932 243 −974 N ATOM 105 CA GLU A 46 −16.377 16.733 38.083 1.00 37.14 C ANISOU 105 CA GLU A 46 5209 4887 4016 816 89 −1085 C ATOM 106 C GLU A 46 −16.540 16.439 39.577 1.00 33.91 C ANISOU 106 C GLU A 46 4985 4553 3347 942 88 −1229 C ATOM 107 CB GLU A 46 −15.248 17.762 37.839 1.00 39.17 C ANISOU 107 CB GLU A 46 5470 4949 4462 671 −17 −1225 C ATOM 108 CG GLU A 46 −15.494 19.109 38.450 1.00 38.50 C ANISOU 108 CG GLU A 46 5546 4642 4441 728 13 −1404 C ATOM 109 CD GLU A 46 −14.355 20.145 38.300 1.00 40.05 C ANISOU 109 CD GLU A 46 5742 4592 4884 535 −60 −1590 C ATOM 110 OE1 GLU A 46 −13.161 19.822 37.993 1.00 38.37 O ANISOU 110 OE1 GLU A 46 5370 4411 4797 344 −165 −1654 O ATOM 111 OE2 GLU A 46 −14.689 21.330 38.582 1.00 42.07 O ANISOU 111 OE2 GLU A 46 6151 4599 5236 577 5 −1707 O ATOM 112 O GLY A 47 −17.059 13.117 42.652 1.00 45.08 O ANISOU 112 O GLY A 47 7024 6323 3782 1302 306 −1114 O ATOM 113 N GLY A 47 −15.983 15.325 40.039 1.00 33.51 N ANISOU 113 N GLY A 47 4973 4649 3110 947 −4 −1218 N ATOM 114 CA GLY A 47 −16.123 14.964 41.449 1.00 37.77 C ANISOU 114 CA GLY A 47 5781 5249 3320 1110 8 −1316 C ATOM 115 C GLY A 47 −17.164 13.870 41.684 1.00 40.08 C ANISOU 115 C GLY A 47 6137 5634 3458 1185 277 −1123 C ATOM 116 N ASP A 48 −18.159 13.780 40.804 1.00 34.49 N ANISOU 116 N ASP A 48 5210 4928 2969 1124 473 −980 N ATOM 117 C ASP A 48 −18.742 11.428 40.192 1.00 38.54 C ANISOU 117 C ASP A 48 5587 5571 3484 1015 689 −686 C ATOM 118 O ASP A 48 −17.794 11.428 39.395 1.00 35.78 O ANISOU 118 O ASP A 48 5124 5237 3232 934 449 −682 O ATOM 119 CA ASP A 48 −19.192 12.736 40.854 1.00 35.42 C ANISOU 119 CA ASP A 48 5286 5111 3062 1128 753 −833 C ATOM 120 CB ASP A 48 −20.477 13.224 40.160 1.00 37.20 C ANISOU 120 CB ASP A 48 5246 5325 3563 1127 930 −811 C ATOM 121 CG ASP A 48 −21.252 14.265 40.987 1.00 46.36 C ANISOU 121 CG ASP A 48 6505 6417 4694 1282 1109 −947 C ATOM 122 OD1 ASP A 48 −21.051 14.335 42.208 1.00 48.98 O ANISOU 122 OD1 ASP A 48 7142 6725 4742 1381 1193 −1035 O ATOM 123 OD2 ASP A 48 −22.073 15.008 40.414 1.00 52.93 O ANISOU 123 OD2 ASP A 48 7129 7215 5766 1341 1158 −975 O ATOM 124 N SER A 49 −19.431 10.318 40.466 1.00 32.69 N ANISOU 124 N SER A 49 4887 4844 2689 998 941 −574 N ATOM 125 C SER A 49 −19.742 9.092 38.380 1.00 32.87 C ANISOU 125 C SER A 49 4455 4928 3105 760 888 −433 C ATOM 126 O SER A 49 −20.806 9.666 38.207 1.00 34.32 O ANISOU 126 O SER A 49 4463 5122 3456 772 1017 −482 O ATOM 127 CA SER A 49 −19.084 9.069 39.765 1.00 31.28 C ANISOU 127 CA SER A 49 4624 4688 2574 888 896 −451 C ATOM 128 CB SER A 49 −19.533 7.822 40.557 1.00 33.21 C ANISOU 128 CB SER A 49 5094 4870 2656 899 1194 −335 C ATOM 129 OG SER A 49 −19.073 7.830 41.924 1.00 35.52 O ANISOU 129 OG SER A 49 5816 5123 2557 1084 1217 −339 O ATOM 130 N ALA A 50 −19.101 8.457 37.415 1.00 35.34 N ANISOU 130 N ALA A 50 4665 5271 3493 672 720 −383 N ATOM 131 CA ALA A 50 −19.630 8.328 36.067 1.00 36.09 C ANISOU 131 CA ALA A 50 4474 5413 3823 582 668 −378 C ATOM 132 C ALA A 50 −19.755 6.854 35.794 1.00 36.46 C ANISOU 132 C ALA A 50 4496 5444 3914 475 758 −326 C ATOM 133 O ALA A 50 −18.745 6.164 35.806 1.00 38.85 O ANISOU 133 O ALA A 50 4939 5722 4099 474 664 −276 O ATOM 134 CB ALA A 50 −18.676 8.986 35.051 1.00 34.05 C ANISOU 134 CB ALA A 50 4166 5179 3591 577 413 −380 C ATOM 135 N THR A 51 −20.957 6.374 35.498 1.00 33.68 N ANISOU 135 N THR A 51 3937 5093 3766 388 925 −365 N ATOM 136 C THR A 51 −21.693 4.597 33.930 1.00 38.22 C ANISOU 136 C THR A 51 4188 5665 4668 152 914 −450 C ATOM 137 O THR A 51 −22.772 5.027 33.536 1.00 37.82 O ANISOU 137 O THR A 51 3852 5687 4831 145 914 −567 O ATOM 138 CA THR A 51 −21.147 4.951 35.318 1.00 34.30 C ANISOU 138 CA THR A 51 4003 5100 3928 252 1054 −343 C ATOM 139 CB THR A 51 −22.070 4.393 36.412 1.00 40.09 C ANISOU 139 CB THR A 51 4808 5718 4707 187 1460 −324 C ATOM 140 OG1 THR A 51 −21.456 4.623 37.686 1.00 38.41 O ANISOU 140 OG1 THR A 51 4979 5445 4172 326 1554 −223 O ATOM 141 CG2 THR A 51 −22.268 2.904 36.231 1.00 44.07 C ANISOU 141 CG2 THR A 51 5327 6080 5337 16 1639 −300 C ATOM 142 N PHE A 52 −20.900 3.841 33.168 1.00 37.06 N ANISOU 142 N PHE A 52 4101 5505 4475 111 763 −431 N ATOM 143 CA PHE A 52 −21.390 3.213 31.950 1.00 39.21 C ANISOU 143 CA PHE A 52 4149 5816 4932 13 647 −558 C ATOM 144 C PHE A 52 −21.939 1.820 32.235 1.00 41.84 C ANISOU 144 C PHE A 52 4460 5992 5447 −171 888 −609 C ATOM 145 O PHE A 52 −21.616 1.231 33.245 1.00 45.01 O ANISOU 145 O PHE A 52 5114 6236 5753 −192 1125 −485 O ATOM 146 CB PHE A 52 −20.281 3.086 30.937 1.00 35.29 C ANISOU 146 CB PHE A 52 3750 5368 4290 65 408 −535 C ATOM 147 CG PHE A 52 −19.824 4.378 30.340 1.00 38.05 C ANISOU 147 CG PHE A 52 4108 5833 4516 201 209 −500 C ATOM 148 CD1 PHE A 52 −18.606 4.943 30.725 1.00 36.80 C ANISOU 148 CD1 PHE A 52 4132 5658 4191 270 185 −394 C ATOM 149 CD2 PHE A 52 −20.556 4.982 29.322 1.00 36.63 C ANISOU 149 CD2 PHE A 52 3765 5760 4394 267 37 −585 C ATOM 150 CE1 PHE A 52 −18.144 6.108 30.127 1.00 36.62 C ANISOU 150 CE1 PHE A 52 4133 5685 4097 351 65 −360 C ATOM 151 CE2 PHE A 52 −20.112 6.148 28.716 1.00 37.10 C ANISOU 151 CE2 PHE A 52 3912 5868 4314 403 −102 −514 C ATOM 152 CZ PHE A 52 −18.896 6.713 29.108 1.00 36.59 C AMISOU 152 CZ PHE A 52 4036 5748 4118 419 −53 −394 C ATOM 153 N THR A 53 −22.748 1.276 31.333 1.00 39.44 N ANISOU 153 N THR A 53 3879 5708 5397 −297 821 −800 N ATOM 154 C THR A 53 −22.712 −0.899 30.219 1.00 38.09 C ANISOU 154 C THR A 53 3685 5337 5451 −553 804 −1002 C ATOM 155 O THR A 53 −23.034 −0.500 29.090 1.00 41.35 O ANISOU 155 O THR A 53 3880 5930 5903 −502 498 −1175 O ATOM 156 CA THR A 53 −23.129 −0.114 31.453 1.00 35.98 C ANISOU 156 CA THR A 53 3431 5072 5169 −511 1045 −874 C ATOM 157 CB THR A 53 −24.658 −0.264 31.662 1.00 41.97 C ANISOU 157 CB THR A 53 3813 5802 6333 −697 1266 −1071 C ATOM 158 OG1 THR A 53 −25.048 0.459 32.838 1.00 42.98 O ANISOU 158 OG1 THR A 53 3977 5926 6428 −642 1545 −957 O ATOM 159 CG2 THR A 53 −25.014 −1.723 31.818 1.00 43.33 C ANISOU 159 CG2 THR A 53 3994 5703 6767 −968 1562 −1150 C ATOM 160 N CYS A 54 −21.967 −1.986 30.437 1.00 39.25 N ANISOU 160 N CYS A 54 4109 5276 5530 −603 932 −916 N ATOM 161 C CYS A 54 −22.428 −4.162 29.455 1.00 47.40 C ANISOU 161 C CYS A 54 5072 5992 6945 −921 1009 −1224 C ATOM 162 O CYS A 54 −22.680 −4.677 30.538 1.00 49.13 O ANISOU 162 O CYS A 54 5437 5968 7261 −1034 1389 −1098 O ATOM 163 CA ACYS A 54 −21.571 −2.912 29.378 0.99 42.45 C ANISOU 163 CA ACYS A 54 4541 5624 5963 −649 771 −1055 C ATOM 164 CB ACYS A 54 −20.083 −3.283 29.482 0.99 43.81 C ANISOU 164 CB ACYS A 54 5068 5723 5853 −488 737 −875 C ATOM 165 SG ACYS A 54 −19.492 −4.434 28.153 0.99 51.80 S ANISOU 165 SG ACYS A 54 6149 6654 6877 −504 573 −1060 S ATOM 166 CA BCYS A 54 −21.592 −2.892 29.365 0.01 42.20 C ANISOU 166 CA BCYS A 54 4502 5598 5935 −649 767 −1059 C ATOM 167 CB BCYS A 54 −20.100 −3.223 29.426 0.01 41.78 C ANISOU 167 CB BCYS A 54 4797 5483 5596 −485 720 −882 C ATOM 168 SG BCYS A 54 −19.491 −4.198 28.028 0.01 51.66 S ANISOU 168 SG BCYS A 54 6099 6696 6832 −482 525 −1066 S ATOM 169 N ASER A 55 −22.887 −4.644 28.302 0.55 46.27 N ANISOU 169 N ASER A 55 4706 5883 6990 −1029 800 −1524 N ATOM 170 C ASER A 55 −23.086 −6.877 27.331 0.55 46.64 C ANISOU 170 C ASER A 55 4787 5528 7407 −1346 853 −1905 C ATOM 171 O ASER A 55 −22.757 −6.576 26.176 0.55 43.82 O ANISOU 171 O ASER A 55 4385 5398 6868 −1198 471 −2053 O ATOM 172 CA ASER A 55 −23.718 −5.838 28.244 0.55 47.01 C ANISOU 172 CA ASER A 55 4658 5712 7491 −1331 1000 −1760 C ATOM 173 CB ASER A 55 −25.117 −5.493 27.743 0.55 49.65 C ANISOU 173 CB ASER A 55 4460 6207 8197 −1481 862 −2106 C ATOM 174 OG ASER A 55 −25.628 −4.354 28.408 0.55 49.97 O ANISOU 174 OG ASER A 55 4323 6429 8233 −1391 931 −1992 O ATOM 175 N BSER A 55 −22.862 −4.658 28.301 0.45 46.12 N ANISOU 175 N BSER A 55 4696 5861 6967 −1027 800 −1521 N ATOM 176 C BSER A 55 −23.106 −6.885 27.321 0.45 46.61 C ANISOU 176 C BSER A 55 4777 5523 7410 −1350 852 −1911 C ATOM 177 O BSER A 55 −22.812 −6.600 26.155 0.45 44.13 O ANISOU 177 O BSER A 55 4408 5434 6924 −1209 469 −2070 O ATOM 178 CA BSER A 55 −23.709 −5.836 28.244 0.45 47.03 C ANISOU 178 CA BSER A 55 4663 5714 7491 −1329 999 −1758 C ATOM 179 CB BSER A 55 −25.109 −5.458 27.768 0.45 49.61 C ANISOU 179 CB BSER A 55 4458 6207 8185 −1475 865 −2096 C ATOM 180 OG BSER A 55 −25.938 −6.599 27.686 0.45 54.16 O ANISOU 180 OG BSER A 55 4827 6518 9233 −1814 1062 −2384 O ATOM 181 N PHE A 56 −22.928 −8.095 27.842 1.00 47.19 N ANISOU 181 N PHE A 56 5097 5204 7630 −1505 1179 −1858 N ATOM 182 CA PHE A 56 −22.288 −9.167 27.092 1.00 48.37 C ANISOU 182 CA PHE A 56 5459 5160 7759 −1504 1091 −1990 C ATOM 183 C PHE A 56 −22.551 −10.508 27.737 1.00 54.27 C ANISOU 183 C PHE A 56 6407 5399 8815 −1754 1519 −1985 C ATOM 184 O PHE A 56 −22.617 −10.614 28.958 1.00 57.38 O ANISOU 184 O PHE A 56 7007 5574 9220 −1791 1912 −1702 O ATOM 185 CB PHE A 56 −20.765 −8.963 27.002 1.00 47.95 C ANISOU 185 CB PHE A 56 5764 5200 7254 −1162 953 −1737 C ATOM 186 CG PHE A 56 −20.063 −10.061 26.251 1.00 52.72 C ANISOU 186 CG PHE A 56 6591 5604 7836 −1121 892 −1877 C ATOM 187 CD1 PHE A 56 −20.131 −10.121 24.858 1.00 53.31 C ANISOU 187 CD1 PHE A 56 6526 5850 7881 −1108 568 −2208 C ATOM 188 CD2 PHE A 56 −19.369 −11.049 26.923 1.00 55.03 C ANISOU 188 CD2 PHE A 56 7266 5524 8118 −1064 1153 −1692 C ATOM 189 CE1 PHE A 56 −19.516 −11.143 24.153 1.00 53.35 C ANISOU 189 CE1 PHE A 56 6747 5661 7860 −1063 533 −2371 C ATOM 190 CE2 PHE A 56 −18.747 −12.081 26.223 1.00 54.15 C ANISOU 190 CE2 PHE A 56 7360 5202 8013 −1004 1108 −1843 C ATOM 191 CZ PHE A 56 −18.820 −12.128 24.834 1.00 53.49 C ANISOU 191 CZ PHE A 56 7113 5295 7915 −1016 811 −2194 C ATOM 192 O SER A 57 −22.499 −13.749 25.210 1.00 72.55 O ANISOU 192 O SER A 57 8875 7001 11689 −2134 1303 −2927 O ATOM 193 N SER A 57 −22.674 −11.540 26.917 1.00 54.77 N ANISOU 193 N SER A 57 6463 5247 9102 −1911 1458 −2295 N ATOM 194 CA SER A 57 −22.829 −12.886 27.431 1.00 63.73 C ANISOU 194 CA SER A 57 7850 5826 10539 −2148 1879 −2293 C ATOM 195 C SER A 57 −22.294 −13.895 26.421 1.00 71.20 C ANISOU 195 C SER A 57 8967 6581 11506 −2129 1702 −2552 C ATOM 196 CB SER A 57 −24.298 −13.167 27.764 1.00 68.64 C ANISOU 196 CB SER A 57 8099 6250 11730 −2592 2191 −2530 C ATOM 197 OG SER A 57 −24.534 −14.557 27.873 1.00 78.92 O ANISOU 197 OG SER A 57 9591 7002 13395 −2873 2543 −2647 O ATOM 198 O SER A 58 −21.133 −17.551 27.921 1.00 86.40 O ANISOU 198 O SER A 58 12282 6804 13742 −2219 2780 −2141 O ATOM 199 N SER A 58 −21.588 −14.902 26.927 1.00 73.98 N ANISOU 199 N SER A 58 9798 6487 11823 −2063 1989 −2348 N ATOM 200 CA SER A 58 −21.089 −15.994 26.099 1.00 79.23 C ANISOU 200 CA SER A 58 10678 6876 12549 −2044 1902 −2588 C ATOM 201 C SER A 58 −21.439 −17.315 26.751 1.00 87.23 C ANISOU 201 C SER A 58 11995 7205 13944 −2313 2401 −2561 C ATOM 202 CB SER A 58 −19.575 −15.903 25.883 1.00 76.07 C ANISOU 202 CB SER A 58 10618 6615 11669 −1576 1701 −2367 C ATOM 203 OG SER A 58 −19.115 −17.077 25.231 1.00 79.00 O ANISOU 203 OG SER A 58 11243 6641 12130 −1549 1704 −2583 O ATOM 204 O THR A 59 −21.514 −21.565 27.024 1.00113.78 O ANISOU 204 O THR A 59 16241 9103 17886 −2570 3157 −2540 O ATOM 205 N THR A 59 −22.082 −18.183 25.987 1.00 93.91 N ANISOU 205 N THR A 59 12655 7925 15103 −2548 2333 −2921 N ATOM 206 CA THR A 59 −22.535 −19.440 26.546 1.00104.73 C ANISOU 206 CA THR A 59 14226 8803 16762 −2751 2750 −2828 C ATOM 207 C THR A 59 −21.433 −20.491 26.426 1.00108.86 C ANISOU 207 C THR A 59 15299 8944 17121 −2500 2791 −2713 C ATOM 208 CB THR A 59 −23.845 −19.923 25.856 1.00111.67 C ANISOU 208 CB THR A 59 14615 9721 18095 −3124 2675 −3272 C ATOM 209 OG1 THR A 59 −23.725 −19.805 24.431 1.00110.73 O ANISOU 209 OG1 THR A 59 14272 9905 17893 −3047 2126 −3697 O ATOM 210 CG2 THR A 59 −25.025 −19.076 26.309 1.00111.67 C ANISOU 210 CG2 THR A 59 14111 10000 18317 −3340 2773 −3308 C ATOM 211 O SER A 60 −17.034 −21.457 25.544 1.00105.57 O ANISOU 211 O SER A 60 16118 8287 15707 −1109 2327 −2423 O ATOM 212 N SER A 60 −20.368 −20.119 25.742 1.00105.90 N ANISOU 212 N SER A 60 15046 8775 16417 −2167 2444 −2780 N ATOM 213 CA SER A 60 −19.374 −21.076 25.319 1.00108.06 C ANISOU 213 CA SER A 60 15719 8778 16561 −1902 2388 −2794 C ATOM 214 C SER A 60 −17.946 −20.659 25.648 1.00103.18 C ANISOU 214 C SER A 60 15460 8223 15519 −1403 2326 −2495 C ATOM 215 CB SER A 60 −19.519 −21.353 23.828 1.00110.78 C ANISOU 215 CB SER A 60 15824 9308 16959 −1964 1999 −3305 C ATOM 216 OG SER A 60 −19.036 −20.278 23.081 1.00105.77 O ANISOU 216 OG SER A 60 15004 9180 16003 −1749 1626 −3450 O ATOM 217 O GLU A 61 −17.288 −17.552 28.110 1.00105.37 O ANISOU 217 O GLU A 61 15623 9428 14984 −894 2287 −1470 O ATOM 218 N GLU A 61 −17.732 −19.423 26.087 1.00101.10 N ANISOU 218 N GLU A 61 15056 8364 14993 −1256 2228 −2276 N ATOM 219 CA GLU A 61 −16.380 −18.983 26.441 1.00 99.80 C ANISOU 219 CA GLU A 61 15101 8438 14381 −737 2074 −1939 C ATOM 220 C GLU A 61 −16.329 −18.195 27.763 1.00110.21 C ANISOU 220 C GLU A 61 16494 9894 15488 −613 2196 −1484 C ATOM 221 CB GLU A 61 −15.745 −18.199 25.285 1.00 88.19 C ANISOU 221 CB GLU A 61 13328 7535 12644 −533 1648 −2152 C ATOM 222 CG GLU A 61 −15.563 −18.990 23.998 1.00 88.07 C ANISOU 222 CG GLU A 61 13343 7401 12718 −543 1520 −2582 C ATOM 223 CD GLU A 61 −15.206 −18.134 22.787 1.00 81.57 C ANISOU 223 CD GLU A 61 12233 7146 11616 −409 1157 −2812 C ATOM 224 OE1 GLU A 61 −15.937 −17.199 22.472 1.00 78.07 O ANISOU 224 OE1 GLU A 61 11450 7080 11134 −587 980 −2905 O ATOM 225 OE2 GLU A 61 −14.193 −18.404 22.143 1.00 79.38 O ANISOU 225 OE2 GLU A 61 12090 6921 11150 −107 1073 −2897 O ATOM 226 O SER A 62 −15.732 −15.486 30.530 1.00127.79 O ANISOU 226 O SER A 62 18744 12881 16928 −112 2130 −561 O ATOM 227 N SER A 62 −15.219 −18.284 28.492 1.00125.02 N ANISOU 227 N SER A 62 18722 11712 17068 −171 2184 −1149 N ATOM 228 CA SER A 62 −15.046 −17.641 29.791 1.00129.26 C ANISOU 228 CA SER A 62 19419 12347 17347 16 2262 −739 C ATOM 229 C SER A 62 −15.107 −16.138 29.693 1.00124.89 C ANISOU 229 C SER A 62 18419 12425 16608 8 1993 −742 C ATOM 230 CB SER A 62 −13.707 −18.050 30.419 1.00135.84 C ANISOU 230 CB SER A 62 20679 13045 17889 566 2173 −466 C ATOM 231 OG SER A 62 −12.551 −17.631 29.699 1.00136.69 O ANISOU 231 OG SER A 62 20556 13552 17829 896 1791 −596 O ATOM 232 O PHE A 63 −14.740 −13.234 29.854 1.00 61.43 O ANISOU 232 O PHE A 63 9730 5483 8128 171 1496 −622 O ATOM 233 N PHE A 63 −14.458 −15.574 28.685 1.00102.45 N ANISOU 233 N PHE A 63 15274 9998 13655 142 1648 −941 N ATOM 234 CA PHE A 63 −13.242 −14.818 28.870 1.00 79.01 C ANISOU 234 CA PHE A 63 12253 7389 10377 537 1386 −795 C ATOM 235 C PHE A 63 −13.602 −13.572 29.706 1.00 64.66 C ANISOU 235 C PHE A 63 10280 5883 8405 492 1354 −596 C ATOM 236 CB PHE A 63 −12.700 −14.368 27.512 1.00 71.68 C ANISOU 236 CB PHE A 63 10997 6833 9406 586 1124 −1072 C ATOM 237 CG PHE A 63 −11.889 −15.407 26.766 1.00 72.15 C ANISOU 237 CG PHE A 63 11220 6682 9514 791 1107 −1248 C ATOM 238 CD1 PHE A 63 −10.580 −15.687 27.120 1.00 70.21 C ANISOU 238 CD1 PHE A 63 11126 6406 9142 1226 1031 −1124 C ATOM 239 CD2 PHE A 63 −12.410 −16.057 25.675 1.00 69.52 C ANISOU 239 CD2 PHE A 63 10855 6206 9352 574 1137 −1578 C ATOM 240 CE1 PHE A 63 −9.830 −16.614 26.421 1.00 68.61 C ANISOU 240 CE1 PHE A 63 11049 6018 9001 1444 1031 −1304 C ATOM 241 CE2 PHE A 63 −11.666 −16.984 24.981 1.00 68.87 C ANISOU 241 CE2 PHE A 63 10939 5928 9300 777 1135 −1762 C ATOM 242 CZ PHE A 63 −10.376 −17.259 25.352 1.00 68.06 C ANISOU 242 CZ PHE A 63 10989 5785 9085 1215 1102 −1616 C ATOM 243 N VAL A 64 −12.598 −12.935 30.267 1.00 56.73 N ANISOU 243 N VAL A 64 9293 5116 7147 829 1163 −427 N ATOM 244 CA VAL A 64 −12.707 −11.657 30.951 1.00 48.70 C ANISOU 244 CA VAL A 64 8115 4430 5958 837 1068 −289 C ATOM 245 C VAL A 64 −13.228 −10.536 30.047 1.00 44.29 C ANISOU 245 C VAL A 64 7102 4266 5459 590 941 −474 C ATOM 246 O VAL A 64 −13.023 −10.556 28.861 1.00 42.88 O ANISOU 246 O VAL A 64 6730 4219 5344 547 826 −690 O ATOM 247 CB VAL A 64 −11.309 −11.250 31.437 1.00 48.17 C ANISOU 247 CB VAL A 64 8077 4563 5664 1259 807 −187 C ATOM 248 CG1 VAL A 64 −11.286 −9.875 32.026 1.00 40.43 C ANISOU 248 CG1 VAL A 64 6905 3933 4525 1269 667 −110 C ATOM 249 CG2 VAL A 64 −10.763 −12.254 32.413 1.00 52.29 C ANISOU 249 CG2 VAL A 64 9080 4725 6063 1597 860 14 C ATOM 250 N LEU A 65 −13.931 −9.578 30.638 1.00 38.97 N ANISOU 250 N LEU A 65 6309 3757 4739 458 976 −382 N ATOM 251 C LEU A 65 −13.665 −7.212 30.233 1.00 35.26 C ANISOU 251 C LEU A 65 5342 3954 4103 467 653 −426 C ATOM 252 O LEU A 65 −13.419 −6.944 31.392 1.00 35.04 O ANISOU 252 O LEU A 65 5476 3902 3936 608 670 −251 O ATOM 253 CA LEU A 65 −14.485 −8.458 29.913 1.00 36.70 C ANISOU 253 CA LEU A 65 5644 3811 4490 274 852 −520 C ATOM 254 CB LEU A 65 −15.953 −8.259 30.306 1.00 42.15 C ANISOU 254 CB LEU A 65 6242 4432 5341 −19 1053 −526 C ATOM 255 CG LEU A 65 −16.781 −7.263 29.499 1.00 46.09 C ANISOU 255 CG LEU A 65 6352 5231 5929 −199 917 −701 C ATOM 256 CD1 LEU A 65 −17.018 −7.821 28.091 1.00 50.52 C ANISOU 256 CD1 LEU A 65 6769 5795 6630 −316 793 −988 C ATOM 257 CD2 LEU A 65 −18.118 −6.981 30.199 1.00 49.54 C ANISOU 257 CD2 LEU A 65 6673 5611 6537 −422 1135 −684 C ATOM 258 N ASN A 66 −13.269 −6.442 29.222 1.00 34.31 N ANISOU 258 N ASN A 66 4965 4115 3957 469 480 −552 N ATOM 259 CA ASN A 66 −12.354 −5.314 29.436 1.00 34.32 C ANISOU 259 CA ASN A 66 4839 4375 3828 622 326 −495 C ATOM 260 C ASN A 66 −12.989 −3.969 29.200 1.00 34.62 C ANISOU 260 C ASN A 66 4666 4641 3846 481 279 −504 C ATOM 261 O ASN A 66 −13.823 −3.813 28.315 1.00 34.81 O ANISOU 261 O ASN A 66 4572 4723 3932 323 279 −611 O ATOM 262 CB ASN A 66 −11.123 −5.394 28.516 1.00 36.02 C ANISOU 262 CB ASN A 66 4949 4704 4034 768 230 −607 C ATOM 263 CG ASN A 66 −10.152 −6.502 28.893 1.00 37.61 C ANISOU 263 CG ASN A 66 5319 4723 4247 1016 219 −596 C ATOM 264 OD1 ASN A 66 −10.355 −7.237 29.860 1.00 38.67 O ANISOU 264 OD1 ASN A 66 5714 4621 4357 1103 272 −476 O ATOM 265 ND2 ASN A 66 −9.086 −6.631 28.104 1.00 36.89 N ANISOU 265 ND2 ASN A 66 5099 4727 4188 1153 175 −719 N ATOM 266 N TRP A 67 −12.559 −2.981 29.971 1.00 31.20 N ANISOU 266 N TRP A 67 4196 4333 3325 567 207 −415 N ATOM 267 CA TRP A 67 −13.016 −1.624 29.765 1.00 29.46 C ANISOU 267 CA TRP A 67 3806 4298 3090 470 164 −417 C ATOM 268 C TRP A 67 −11.857 −0.754 29.256 1.00 31.37 C ANISOU 268 C TRP A 67 3907 4708 3306 545 66 −455 C ATOM 269 O TRP A 67 −10.777 −0.796 29.848 1.00 30.79 O ANISOU 269 O TRP A 67 3831 4642 3224 689 −6 −454 O ATOM 270 CB TRP A 67 −13.580 −1.100 31.086 1.00 31.97 C ANISOU 270 CB TRP A 67 4207 4587 3354 473 210 −312 C ATOM 271 CG TRP A 67 −14.127 0.260 31.040 1.00 30.78 C ANISOU 271 CG TRP A 67 3913 4579 3202 400 181 −315 C ATOM 272 CD1 TRP A 67 −14.596 0.919 29.956 1.00 30.81 C ANISOU 272 CD1 TRP A 67 3757 4693 3255 314 141 −377 C ATOM 273 CD2 TRP A 67 −14.258 1.152 32.150 1.00 31.04 C ANISOU 273 CD2 TRP A 67 3996 4641 3158 447 181 −257 C ATOM 274 NE1 TRP A 67 −14.995 2.177 30.312 1.00 32.30 N ANISOU 274 NE1 TRP A 67 3886 4959 3427 309 123 −346 N ATOM 275 CE2 TRP A 67 −14.794 2.341 31.661 1.00 30.40 C ANISOU 275 CE2 TRP A 67 3760 4670 3122 375 154 −287 C ATOM 276 CE3 TRP A 67 −13.981 1.047 33.511 1.00 37.56 C ANISOU 276 CE3 TRP A 67 5025 5400 3848 573 191 −188 C ATOM 277 CZ2 TRP A 67 −15.068 3.424 32.484 1.00 36.15 C ANISOU 277 CZ2 TRP A 67 4503 5428 3805 404 157 −266 C ATOM 278 CZ3 TRP A 67 −14.259 2.134 34.335 1.00 39.10 C ANISOU 278 CZ3 TRP A 67 5243 5650 3962 600 184 −181 C ATOM 279 CH2 TRP A 67 −14.789 3.304 33.816 1.00 35.93 C ANISOU 279 CH2 TRP A 67 4657 5345 3650 504 175 −228 C ATOM 280 N TYR A 68 −12.092 0.033 28.195 1.00 32.47 N ANISOU 280 N TYR A 68 3934 4965 3439 458 68 −494 N ATOM 281 CA TYR A 68 −11.053 0.818 27.488 1.00 31.88 C ANISOU 281 CA TYR A 68 3751 5001 3359 483 77 −522 C ATOM 282 C TYR A 68 −11.368 2.284 27.359 1.00 31.80 C ANISOU 282 C TYR A 68 3691 5066 3327 412 82 −469 C ATOM 283 O TYR A 68 −12.529 2.676 27.178 1.00 34.10 O ANISOU 283 O TYR A 68 4016 5366 3575 362 59 −437 O ATOM 284 CB TYR A 68 −10.824 0.310 26.034 1.00 31.12 C ANISOU 284 CB TYR A 68 3677 4932 3215 485 147 −604 C ATOM 285 CG TYR A 68 −10.124 −0.996 26.010 1.00 31.07 C ANISOU 285 CG TYR A 68 3703 4844 3256 585 169 −682 C ATOM 286 CD1 TYR A 68 −8.733 −1.067 26.222 1.00 28.94 C ANISOU 286 CD1 TYR A 68 3318 4601 3075 704 191 −725 C ATOM 287 CD2 TYR A 68 −10.824 −2.170 25.840 1.00 31.06 C ANISOU 287 CD2 TYR A 68 3827 4717 3256 570 163 −739 C ATOM 288 CE1 TYR A 68 −8.089 −2.276 26.238 1.00 28.27 C ANISOU 288 CE1 TYR A 68 3267 4430 3046 851 193 −801 C ATOM 289 CE2 TYR A 68 −10.171 −3.401 25.833 1.00 30.90 C ANISOU 289 CE2 TYR A 68 3881 4572 3289 687 193 −808 C ATOM 290 CZ TYR A 68 −8.803 −3.439 26.046 1.00 36.07 C ANISOU 290 CZ TYR A 68 4440 5264 4000 851 201 −828 C ATOM 291 OH TYR A 68 −8.150 −4.656 26.061 1.00 38.03 O ANISOU 291 OH TYR A 68 4762 5378 4309 1020 215 −900 O ATOM 292 N ARG A 69 −10.317 3.088 27.402 1.00 30.18 N ANISOU 292 N ARG A 69 3387 4897 3184 413 117 −480 N ATOM 293 CA ARG A 69 −10.379 4.472 26.952 1.00 29.68 C ANISOU 293 CA ARG A 69 3313 4849 3115 338 188 −429 C ATOM 294 C ARG A 69 −9.518 4.606 25.689 1.00 34.40 C ANISOU 294 C ARG A 69 3900 5467 3704 316 367 −445 C ATOM 295 O ARG A 69 −8.414 4.044 25.619 1.00 34.43 O ANISOU 295 O ARG A 69 3780 5489 3813 343 433 −535 O ATOM 296 CB ARG A 69 −9.907 5.431 28.044 1.00 31.56 C ANISOU 296 CB ARG A 69 3459 5064 3468 309 140 −449 C ATOM 297 CG ARG A 69 −9.783 6.861 27.573 1.00 32.21 C ANISOU 297 CG ARG A 69 3547 5097 3596 214 258 −406 C ATOM 298 CD ARG A 69 −9.533 7.841 28.706 1.00 33.39 C ANISOU 298 CD ARG A 69 3626 5193 3867 171 185 −466 C ATOM 299 NE ARG A 69 −9.475 9.212 28.219 1.00 36.21 N ANISOU 299 NE ARG A 69 4027 5439 4292 67 333 −418 N ATOM 300 CZ ARG A 69 −9.163 10.246 28.984 1.00 37.74 C ANISOU 300 CZ ARG A 69 4167 5541 4630 −6 311 −498 C ATOM 301 NH1 ARG A 69 −8.866 10.038 30.260 1.00 38.48 N ANISOU 301 NH1 ARG A 69 4163 5683 4776 37 112 −644 N ATOM 302 NH2 ARG A 69 −9.107 11.469 28.476 1.00 42.52 N ANISOU 302 NH2 ARG A 69 4853 5987 5316 −110 487 −441 N ATOM 303 O MET A 70 −8.955 7.844 23.711 1.00 47.21 O ANISOU 303 O MET A 70 5776 6908 5253 138 894 −202 O ATOM 304 N MET A 70 −10.048 5.287 24.671 1.00 32.95 N ANISOU 304 N MET A 70 3867 5275 3376 299 454 −360 N ATOM 305 C MET A 70 −8.472 6.749 23.422 1.00 42.54 C ANISOU 305 C MET A 70 5109 6400 4656 178 911 −292 C ATOM 306 CA MET A 70 −9.328 5.482 23.416 1.00 35.38 C ANISOU 306 CA MET A 70 4257 5580 3604 293 688 −341 C ATOM 307 CB MET A 70 −10.323 5.537 22.245 1.00 40.35 C ANISOU 307 CB MET A 70 5159 6234 3938 381 659 −270 C ATOM 308 CG MET A 70 −11.330 4.408 22.281 1.00 41.35 C ANISOU 308 CG MET A 70 5295 6424 3992 447 420 −365 C ATOM 309 SD MET A 70 −10.548 2.775 22.405 1.00 54.68 S ANISOU 309 SD MET A 70 6876 8119 5782 460 446 −523 S ATOM 310 CE MET A 70 −9.805 2.752 20.772 1.00 43.48 C ANISOU 310 CE MET A 70 5649 6733 4138 527 692 −543 C ATOM 311 O SER A 71 −7.451 8.318 20.978 1.00 59.66 O ANISOU 311 O SER A 71 7686 8372 6610 90 1653 −64 O ATOM 312 N SER A 71 −7.195 6.587 23.106 1.00 43.34 N ANISOU 312 N SER A 71 5057 6500 4911 120 1141 −375 N ATOM 313 CA SER A 71 −6.247 7.690 22.992 1.00 53.52 C ANISOU 313 CA SER A 71 6243 7679 6414 −40 1431 −371 C ATOM 314 C SER A 71 −6.567 8.617 21.806 1.00 66.57 C ANISOU 314 C SER A 71 8248 9206 7841 −61 1719 −173 C ATOM 315 CB SER A 71 −4.834 7.130 22.839 1.00 52.34 C ANISOU 315 CB SER A 71 5792 7577 6517 −83 1633 −544 C ATOM 316 OG SER A 71 −4.674 6.627 21.526 1.00 59.64 O ANISOU 316 OG SER A 71 6909 8523 7229 −19 1904 −497 O ATOM 317 O PRO A 72 −6.525 9.773 18.325 1.00 95.84 O ANISOU 317 O PRO A 72 12964 12663 10790 60 2601 276 O ATOM 318 N PRO A 72 −5.854 9.755 21.722 1.00 85.13 N ANISOU 318 N PRO A 72 10565 11384 10397 −239 2035 −136 N ATOM 319 CA PRO A 72 −5.928 10.573 20.502 1.00 91.13 C ANISOU 319 CA PRO A 72 11721 11975 10928 −247 2412 81 C ATOM 320 C PRO A 72 −5.691 9.766 19.231 1.00 90.80 C ANISOU 320 C PRO A 72 11890 12020 10591 −128 2638 115 C ATOM 321 CB PRO A 72 −4.796 11.586 20.698 1.00 98.04 C ANISOU 321 CB PRO A 72 12398 12640 12211 −525 2807 33 C ATOM 322 CG PRO A 72 −4.708 11.739 22.182 1.00 95.56 C ANISOU 322 CG PRO A 72 11699 12362 12246 −615 2464 −167 C ATOM 323 CD PRO A 72 −4.993 10.379 22.747 1.00 88.12 C ANISOU 323 CD PRO A 72 10576 11685 11220 −438 2055 −300 C ATOM 324 O SER A 73 −4.904 6.347 16.821 1.00 76.70 O ANISOU 324 O SER A 73 10310 10631 8200 269 2882 −164 O ATOM 325 N SER A 73 −4.565 9.059 19.193 1.00 83.79 N ANISOU 325 N SER A 73 10685 11210 9939 −205 2838 −65 N ATOM 326 CA SER A 73 −4.163 8.283 18.024 1.00 78.73 C ANISOU 326 CA SER A 73 10215 10641 9058 −99 3119 −75 C ATOM 327 C SER A 73 −5.060 7.068 17.802 1.00 72.65 C ANISOU 327 C SER A 73 9599 10053 7950 143 2724 −129 C ATOM 328 CB SER A 73 −2.701 7.842 18.154 1.00 80.04 C ANISOU 328 CB SER A 73 9920 10844 9646 −228 3418 −297 C ATOM 329 OG SER A 73 −2.503 6.917 19.209 1.00 79.23 O ANISOU 329 OG SER A 73 9394 10900 9808 −172 3026 −525 O ATOM 330 O GLY A 74 −7.182 3.421 18.845 1.00 53.62 O ANISOU 330 O GLY A 74 7049 7995 5330 523 1520 −514 O ATOM 331 N GLY A 74 −5.998 6.840 18.712 1.00 63.68 N ANISOU 331 N GLY A 74 8376 8982 6836 195 2241 −156 N ATOM 332 CA GLY A 74 −6.962 5.771 18.545 1.00 58.59 C ANISOU 332 CA GLY A 74 7860 8467 5936 373 1884 −221 C ATOM 333 C GLY A 74 −6.554 4.437 19.146 1.00 55.08 C ANISOU 333 C GLY A 74 7116 8116 5697 402 1725 −430 C ATOM 334 O GLN A 75 −6.241 3.875 22.804 1.00 32.68 O ANISOU 334 O GLN A 75 3522 5304 3593 322 1088 −630 O ATOM 335 N GLN A 75 −5.515 4.431 19.989 1.00 50.13 N ANISOU 335 N GLN A 75 6112 7481 5455 306 1800 −532 N ATOM 336 CA GLN A 75 −5.137 3.235 20.725 1.00 40.00 C ANISOU 336 CA GLN A 75 4572 6260 4365 387 1600 −706 C ATOM 337 C GLN A 75 −5.999 2.984 21.970 1.00 36.89 C ANISOU 337 C GLN A 75 4130 5867 4020 409 1194 −694 C ATOM 338 CB GLN A 75 −3.654 3.295 21.149 1.00 37.80 C ANISOU 338 CB GLN A 75 3888 5994 4479 336 1785 −855 C ATOM 339 CG GLN A 75 −2.682 3.317 19.972 1.00 44.26 C ANISOU 339 CG GLN A 75 4693 6811 5314 316 2263 −908 C ATOM 340 CD GLN A 75 −2.576 1.971 19.248 1.00 43.08 C ANISOU 340 CD GLN A 75 4658 6715 4995 508 2302 −1021 C ATOM 341 OE1 GLN A 75 −3.222 0.976 19.626 1.00 41.84 O ANISOU 341 OE1 GLN A 75 4587 6571 4739 641 1965 −1065 O ATOM 342 NE2 GLN A 75 −1.768 1.940 18.211 1.00 46.53 N ANISOU 342 NE2 GLN A 75 5116 7155 5408 515 2751 −1076 N ATOM 343 O PRO A 76 −5.406 0.521 24.557 1.00 37.77 O ANISOU 343 O PRO A 76 3591 5966 4793 196 728 −1132 O ATOM 344 N PRO A 76 −6.422 1.736 22.147 1.00 30.84 N ANISOU 344 N PRO A 76 3281 5135 3301 54 1119 −1031 N ATOM 345 C PRO A 76 −6.357 1.294 24.577 1.00 35.24 C ANISOU 345 C PRO A 76 3458 5690 4240 151 679 −982 C ATOM 346 CA PRO A 76 −7.232 1.459 23.333 1.00 30.42 C ANISOU 346 CA PRO A 76 3141 5108 3309 121 781 −933 C ATOM 347 CB PRO A 76 −7.946 0.154 22.962 1.00 31.30 C ANISOU 347 CB PRO A 76 3327 5215 3350 194 650 −986 C ATOM 348 CG PRO A 76 −6.932 −0.540 22.084 1.00 33.08 C ANISOU 348 CG PRO A 76 3512 5402 3656 197 886 −1172 C ATOM 349 CD PRO A 76 −6.275 0.554 21.276 1.00 32.29 C ANISOU 349 CD PRO A 76 3521 5302 3444 98 1207 −1181 C ATOM 350 O ASP A 77 −7.847 1.613 28.260 1.00 29.72 O ANISOU 350 O ASP A 77 2760 4992 3541 246 36 −690 O ATOM 351 N ASP A 77 −6.668 2.024 25.650 1.00 34.03 N ANISOU 351 N ASP A 77 3276 5553 4100 142 519 −874 N ATOM 352 CA ASP A 77 −5.895 1.902 26.904 1.00 39.25 C ANISOU 352 CA ASP A 77 3721 6186 5006 193 347 −924 C ATOM 353 C ASP A 77 −6.736 1.173 27.933 1.00 32.62 C ANISOU 353 C ASP A 77 2972 5332 4090 278 84 −818 C ATOM 354 CB ASP A 77 −5.489 3.270 27.443 1.00 44.76 C ANISOU 354 CB ASP A 77 4346 6890 5771 112 372 −918 C ATOM 355 CG ASP A 77 −4.729 3.177 28.779 1.00 56.00 C ANISOU 355 CG ASP A 77 5576 8287 7414 182 118 −996 C ATOM 356 OD1 ASP A 77 −3.911 2.250 28.952 1.00 58.46 O ANISOU 356 OD1 ASP A 77 5712 8554 7946 282 11 −1119 O ATOM 357 OD2 ASP A 77 −4.958 4.027 29.673 1.00 59.65 O ANISOU 357 OD2 ASP A 77 6079 8761 7824 155 −3 −945 O ATOM 358 N LYS A 78 −6.225 0.054 28.436 1.00 32.49 N ANISOU 358 N LYS A 78 2871 5247 4228 389 −65 −874 N ATOM 359 C LYS A 78 −7.209 −0.178 30.657 1.00 32.62 C ANISOU 359 C LYS A 78 3126 5201 4065 467 −413 −660 C ATOM 360 O LYS A 78 −6.217 0.020 31.342 1.00 30.01 O ANISOU 360 O LYS A 78 2687 4851 3864 534 −572 −730 O ATOM 361 CA LYS A 78 −7.050 −0.806 29.285 1.00 33.85 C ANISOU 361 CA LYS A 78 3199 5358 4305 457 −246 −756 C ATOM 362 CB LYS A 78 −6.411 −2.184 29.403 1.00 33.16 C ANISOU 362 CB LYS A 78 3048 5153 4398 589 −358 −828 C ATOM 363 CG LYS A 78 −7.229 −3.242 30.122 1.00 31.84 C ANISOU 363 CG LYS A 78 3086 4866 4145 647 −481 −699 C ATOM 364 CD LYS A 78 −6.474 −4.570 30.085 1.00 32.88 C ANISOU 364 CD LYS A 78 3156 4848 4491 794 −584 −780 C ATOM 365 CE LYS A 78 −7.005 −5.641 31.017 1.00 33.31 C ANISOU 365 CE LYS A 78 3450 4718 4488 875 −726 −633 C ATOM 366 NZ LYS A 78 −6.195 −6.917 30.919 1.00 33.02 N ANISOU 366 NZ LYS A 78 3352 4499 4694 1045 −844 −716 N ATOM 367 O LEU A 79 −8.418 −0.148 34.601 1.00 31.04 O ANISOU 367 O LEU A 79 3565 4844 3383 566 −818 −339 O ATOM 368 N LEU A 79 −8.437 0.118 31.059 1.00 32.65 N ANISOU 368 N LEU A 79 3312 5218 3874 407 −384 −532 N ATOM 369 CA LEU A 79 −8.678 0.740 32.377 1.00 33.94 C ANISOU 369 CA LEU A 79 3605 5375 3916 406 −492 −454 C ATOM 370 C LEU A 79 −8.924 −0.274 33.483 1.00 31.65 C ANISOU 370 C LEU A 79 3529 4962 3534 490 −628 −357 C ATOM 371 CB LEU A 79 −9.898 1.660 32.324 1.00 30.79 C ANISOU 371 CB LEU A 79 3291 5029 3380 298 −348 −384 C ATOM 372 CG LEU A 79 −9.903 2.724 31.243 1.00 30.97 C ANISOU 372 CG LEU A 79 3204 5133 3430 224 −214 −429 C ATOM 373 CD1 LEU A 79 −11.303 3.320 31.137 1.00 32.39 C ANISOU 373 CD1 LEU A 79 3471 5326 3510 166 −127 −360 C ATOM 374 CD2 LEU A 79 −8.840 3.789 31.495 1.00 34.87 C ANISOU 374 CD2 LEU A 79 3590 5654 4006 201 −237 −504 C ATOM 375 N ALA A 80 −9.795 −1.232 33.195 1.00 34.83 N ANISOU 375 N ALA A 80 4027 5287 3919 469 −523 −293 N ATOM 376 CA ALA A 80 −10.134 −2.232 34.190 1.00 40.96 C ANISOU 376 CA ALA A 80 5062 5899 4602 523 −578 −175 C ATOM 377 C ALA A 80 −10.776 −3.367 33.470 1.00 39.77 C ANISOU 377 C ALA A 80 4905 5650 4555 491 −453 −173 C ATOM 378 O ALA A 80 −10.981 −3.297 32.252 1.00 37.25 O ANISOU 378 O ALA A 80 4395 5414 4343 436 −359 −275 O ATOM 379 CB ALA A 80 −11.075 −1.667 35.252 1.00 42.76 C ANISOU 379 CB ALA A 80 5526 6106 4614 444 −478 −70 C ATOM 380 N ALA A 81 −11.136 −4.390 34.231 1.00 39.22 N ANISOU 380 N ALA A 81 5080 5386 4436 518 −444 −60 N ATOM 381 CA ALA A 81 −11.687 −5.618 33.665 1.00 41.75 C ANISOU 381 CA ALA A 81 5408 5558 4897 485 −330 −70 C ATOM 382 C ALA A 81 −12.448 −6.422 34.713 1.00 44.08 C ANISOU 382 C ALA A 81 6036 5614 5098 443 −207 90 C ATOM 383 O ALA A 81 −12.228 −6.265 35.907 1.00 42.96 O ANISOU 383 O ALA A 81 6181 5398 4743 500 −273 225 O ATOM 384 CB ALA A 81 −10.589 −6.460 33.080 1.00 37.41 C ANISOU 384 CB ALA A 81 4746 4947 4521 628 −485 −155 C ATOM 385 O PHE A 82 −14.190 −9.841 33.411 1.00 51.73 O ANISOU 385 O PHE A 82 7018 6009 6628 243 194 −10 O ATOM 386 N PHE A 82 −13.322 −7.304 34.255 1.00 44.49 N ANISOU 386 N PHE A 82 6073 5526 5305 339 −21 64 N ATOM 387 CA PHE A 82 −13.965 −8.242 35.162 1.00 48.69 C ANISOU 387 CA PHE A 82 6931 5770 5798 281 155 213 C ATOM 388 C PHE A 82 −13.919 −9.645 34.599 1.00 49.92 C ANISOU 388 C PHE A 82 7081 5704 6180 301 171 175 C ATOM 389 CB PHE A 82 −15.417 −7.847 35.426 1.00 49.60 C ANISOU 389 CB PHE A 82 7043 5868 5933 64 482 205 C ATOM 390 CG PHE A 82 −16.100 −8.707 36.469 1.00 55.78 C ANISOU 390 CG PHE A 82 8203 6329 6663 −34 763 364 C ATOM 391 CD1 PHE A 82 −16.133 −8.310 37.798 1.00 58.59 C ANISOU 391 CD1 PHE A 82 8950 6613 6700 −31 863 537 C ATOM 392 CD2 PHE A 82 −16.690 −9.915 36.124 1.00 57.19 C ANISOU 392 CD2 PHE A 82 8379 6255 7096 −137 948 333 C ATOM 393 CE1 PHE A 82 −16.756 −9.094 38.761 1.00 63.12 C ANISOU 393 CE1 PHE A 82 9945 6861 7176 −133 1182 701 C ATOM 394 CE2 PHE A 82 −17.307 −10.707 37.092 1.00 60.47 C ANISOU 394 CE2 PHE A 82 9175 6329 7470 −251 1269 493 C ATOM 395 CZ PHE A 82 −17.342 −10.292 38.400 1.00 64.04 C ANISOU 395 CZ PHE A 82 10052 6708 7573 −251 1404 687 C ATOM 396 O PRO A 83 −10.824 −11.071 35.880 1.00 70.44 O ANISOU 396 O PRO A 83 10150 7959 8655 908 −555 407 O ATOM 397 N PRO A 83 −13.547 −10.620 35.434 1.00 50.73 N ANISOU 397 N PRO A 83 7539 5519 6217 399 137 346 N ATOM 398 CA PRO A 83 −12.933 −10.360 36.747 1.00 59.77 C ANISOU 398 CA PRO A 83 9070 6597 7045 538 −15 549 C ATOM 399 C PRO A 83 −11.414 −10.265 36.604 1.00 71.30 C ANISOU 399 C PRO A 83 10422 8151 8519 801 −437 500 C ATOM 400 CB PRO A 83 −13.336 −11.579 37.573 1.00 55.89 C ANISOU 400 CB PRO A 83 9045 5698 6492 523 154 756 C ATOM 401 CG PRO A 83 −13.416 −12.704 36.555 1.00 54.35 C ANISOU 401 CG PRO A 83 8641 5346 6662 501 203 634 C ATOM 402 CD PRO A 83 −13.806 −12.056 35.213 1.00 50.88 C ANISOU 402 CD PRO A 83 7664 5219 6449 375 250 358 C ATOM 403 O GLU A 84 −9.846 −7.331 38.624 1.00 93.91 O ANISOU 403 O GLU A 84 13474 11462 10745 1028 −1025 536 O ATOM 404 N GLU A 84 −10.796 −9.240 37.163 1.00 79.85 N ANISOU 404 N GLU A 84 11520 9415 9402 890 −647 509 N ATOM 405 CA GLU A 84 −9.342 −9.165 37.219 1.00 88.54 C ANISOU 405 CA GLU A 84 12514 10566 10563 1141 −1061 443 C ATOM 406 C GLU A 84 −9.012 −8.145 38.305 1.00 96.12 C ANISOU 406 C GLU A 84 13673 11632 11214 1200 −1253 504 C ATOM 407 CB GLU A 84 −8.794 −8.768 35.834 1.00 84.53 C ANISOU 407 CB GLU A 84 11464 10289 10363 1127 −1077 189 C ATOM 408 CG GLU A 84 −7.375 −9.199 35.485 1.00 83.91 C ANISOU 408 CG GLU A 84 11162 10177 10544 1360 −1385 53 C ATOM 409 CD GLU A 84 −6.919 −8.727 34.103 1.00 78.72 C ANISOU 409 CD GLU A 84 10019 9740 10152 1300 −1284 −201 C ATOM 410 OE1 GLU A 84 −7.648 −8.910 33.136 1.00 73.30 O ANISOU 410 OE1 GLU A 84 9226 9100 9526 1146 −1017 −267 O ATOM 411 OE2 GLU A 84 −5.822 −8.178 33.992 1.00 77.18 O ANISOU 411 OE2 GLU A 84 9566 9657 10103 1405 −1468 −345 O ATOM 412 O ASP A 85 −5.447 −6.546 38.532 1.00105.79 O ANISOU 412 O ASP A 85 14234 13193 12770 1683 −2317 70 O ATOM 413 N ASP A 85 −7.812 −8.194 38.876 1.00101.42 N ANISOU 413 N ASP A 85 14415 12260 11861 1452 −1686 493 N ATOM 414 CA ASP A 85 −7.353 −7.205 39.837 1.00104.52 C ANISOU 414 CA ASP A 85 14956 12764 11993 1527 −1946 489 C ATOM 415 C ASP A 85 −6.391 −6.187 39.242 1.00103.99 C ANISOU 415 C ASP A 85 14369 12960 12182 1557 −2142 230 C ATOM 416 O ARG A 86 −5.966 −1.524 38.587 1.00 81.91 O ANISOU 416 O ARG A 86 10691 10927 9503 1148 −1973 −272 O ATOM 417 N ARG A 86 −6.632 −4.911 39.534 1.00 99.94 N ANISOU 417 N ARG A 86 13820 12644 11510 1431 −2076 174 N ATOM 418 CA ARG A 86 −5.743 −3.851 39.096 1.00 91.73 C ANISOU 418 CA ARG A 86 12336 11817 10703 1431 −2229 −64 C ATOM 419 C ARG A 86 −6.503 −2.634 38.613 1.00 84.28 C ANISOU 419 C ARG A 86 11220 11080 9721 1183 −1884 −116 C ATOM 420 N SER A 93 −8.138 2.009 43.366 1.00 62.39 N ANISOU 420 N SER A 93 9731 8513 5459 921 −1892 −158 N ATOM 421 CA SER A 93 −8.283 2.182 41.930 1.00 59.24 C ANISOU 421 CA SER A 93 8804 8223 5482 800 −1655 −210 C ATOM 422 C SER A 93 −9.359 3.245 41.598 1.00 53.78 C ANISOU 422 C SER A 93 8004 7623 4809 593 −1249 −236 C ATOM 423 O SER A 93 −10.355 3.408 42.297 1.00 56.09 O ANISOU 423 O SER A 93 8612 7862 4840 515 −1000 −162 O ATOM 424 CB SER A 93 −8.603 0.834 41.254 1.00 63.80 C ANISOU 424 CB SER A 93 9362 8701 6180 824 −1522 −61 C ATOM 425 OG SER A 93 −8.517 0.910 39.826 1.00 63.73 O ANISOU 425 OG SER A 93 8872 8793 6549 747 −1377 −140 O ATOM 426 N ARG A 94 −9.109 3.992 40.535 1.00 47.65 N ANISOU 426 N ARG A 94 6787 6963 4355 515 −1183 −353 N ATOM 427 CA ARG A 94 −9.997 5.038 40.074 1.00 42.51 C ANISOU 427 CA ARG A 94 5999 6379 3775 360 −870 −382 C ATOM 428 C ARG A 94 −11.170 4.474 39.284 1.00 38.15 C ANISOU 428 C ARG A 94 5386 5806 3303 279 −550 −264 C ATOM 429 O ARG A 94 −12.161 5.167 39.059 1.00 36.17 O ANISOU 429 O ARG A 94 5078 5574 3089 177 −299 −272 O ATOM 430 CB ARG A 94 −9.238 6.017 39.169 1.00 46.10 C ANISOU 430 CB ARG A 94 6060 6925 4530 313 −918 −528 C ATOM 431 CG ARG A 94 −8.134 6.831 39.814 1.00 49.99 C ANISOU 431 CG ARG A 94 6502 7435 5059 348 −1200 −710 C ATOM 432 CD ARG A 94 −7.832 8.045 38.925 1.00 49.21 C ANISOU 432 CD ARG A 94 6068 7382 5249 229 −1067 −829 C ATOM 433 NE ARG A 94 −9.059 8.832 38.797 1.00 48.07 N ANISOU 433 NE ARG A 94 6008 7234 5023 126 −767 −763 N ATOM 434 CZ ARG A 94 −9.591 9.248 37.649 1.00 45.03 C ANISOU 434 CZ ARG A 94 5453 6860 4796 51 −528 −705 C ATOM 435 NH1 ARG A 94 −8.978 8.974 36.508 1.00 43.52 N ANISOU 435 NH1 ARG A 94 5035 6692 4809 43 −507 −702 N ATOM 436 NH2 ARG A 94 −10.754 9.925 37.653 1.00 38.80 N ANISOU 436 NH2 ARG A 94 4743 6046 3955 −3 −314 −661 N ATOM 437 N PHE A 95 −10.991 3.245 38.797 1.00 34.87 N ANISOU 437 N PHE A 95 4941 5344 2965 336 −596 −188 N ATOM 438 C PHE A 95 −12.497 1.332 38.539 1.00 45.78 C ANISOU 438 C PHE A 95 6511 6544 4341 280 −267 8 C ATOM 439 O PHE A 95 −11.806 0.608 39.261 1.00 52.15 O ANISOU 439 O PHE A 95 7561 7254 4998 394 −465 73 O ATOM 440 CA PHE A 95 −11.919 2.562 37.902 1.00 36.87 C ANISOU 440 CA PHE A 95 5087 5572 3350 270 −363 −120 C ATOM 441 CB PHE A 95 −11.207 2.223 36.594 1.00 38.04 C ANISOU 441 CB PHE A 95 4930 5782 3743 305 −453 −175 C ATOM 442 CG PHE A 95 −10.579 3.417 35.987 1.00 37.70 C ANISOU 442 CG PHE A 95 4647 5850 3827 276 −489 −287 C ATOM 443 CD1 PHE A 95 −11.371 4.420 35.468 1.00 35.57 C ANISOU 443 CD1 PHE A 95 4291 5631 3592 182 −309 −299 C ATOM 444 CD2 PHE A 95 −9.220 3.606 36.044 1.00 40.96 C ANISOU 444 CD2 PHE A 95 4933 6288 4343 342 −702 −389 C ATOM 445 CE1 PHE A 95 −10.807 5.564 34.972 1.00 36.43 C ANISOU 445 CE1 PHE A 95 4242 5799 3803 146 −312 −378 C ATOM 446 CE2 PHE A 95 −8.657 4.743 35.525 1.00 43.70 C ANISOU 446 CE2 PHE A 95 5068 6702 4836 281 −673 −499 C ATOM 447 CZ PHE A 95 −9.456 5.726 35.000 1.00 37.86 C ANISOU 447 CZ PHE A 95 4300 5995 4090 178 −465 −476 C ATOM 448 N ARG A 96 −13.797 1.131 38.335 1.00 45.58 N ANISOU 448 N ARG A 96 6476 6465 4376 162 39 38 N ATOM 449 C ARG A 96 −15.410 −0.696 38.041 1.00 41.36 C ANISOU 449 C ARG A 96 6013 5688 4013 28 430 132 C ATOM 450 O ARG A 96 −16.194 −0.061 37.315 1.00 38.73 O ANISOU 450 O ARG A 96 5398 5442 3875 −52 548 30 O ATOM 451 CG ARG A 96 −15.844 −0.632 40.971 1.00 54.23 C ANISOU 451 CG ARG A 96 8553 7059 4995 −12 726 320 C ATOM 452 CD ARG A 96 −16.399 −0.130 42.282 1.00 57.72 C ANISOU 452 CD ARG A 96 9392 7414 5123 −82 988 347 C ATOM 453 NE ARG A 96 −15.412 0.657 43.024 1.00 57.44 N ANISOU 453 NE ARG A 96 9576 7472 4775 46 675 325 N ATOM 454 CZ ARG A 96 −15.718 1.404 44.086 1.00 59.25 C ANISOU 454 CZ ARG A 96 10125 7681 4707 6 831 291 C ATOM 455 NH1 ARG A 96 −16.974 1.466 44.508 1.00 59.90 N ANISOU 455 NH1 ARG A 96 10323 7651 4787 −161 1337 278 N ATOM 456 NH2 ARG A 96 −14.783 2.095 44.722 1.00 57.32 N ANISOU 456 NH2 ARG A 96 10065 7518 4196 126 494 236 N ATOM 457 CA ARG A 96 −14.455 0.018 38.978 1.00 45.36 C ANISOU 457 CA ARG A 96 6737 6249 4248 126 222 154 C ATOM 458 CB ARG A 96 −15.188 0.486 40.220 1.00 47.55 C ANISOU 458 CB ARG A 96 7338 6448 4282 49 463 186 C ATOM 459 N VAL A 97 −15.324 −2.019 38.054 1.00 41.24 N ANISOU 459 N VAL A 97 6136 5511 4022 50 437 215 N ATOM 460 CA VAL A 97 −16.192 −2.869 37.233 1.00 42.09 C ANISOU 460 CA VAL A 97 6059 5530 4405 −49 616 170 C ATOM 461 C VAL A 97 −16.885 −3.879 38.095 1.00 42.31 C ANISOU 461 C VAL A 97 6407 5288 4380 −141 901 283 C ATOM 462 O VAL A 97 −16.224 −4.614 38.825 1.00 42.00 O ANISOU 462 O VAL A 97 6731 5095 4133 −49 812 432 O ATOM 463 CB VAL A 97 −15.419 −3.653 36.135 1.00 44.71 C ANISOU 463 CB VAL A 97 6204 5884 4900 45 390 126 C ATOM 464 CGI VAL A 97 −16.412 −4.406 35.254 1.00 42.83 C ANISOU 464 CGI VAL A 97 5764 5565 4945 −69 554 31 C ATOM 465 CG2 VAL A 97 −14.603 −2.718 35.298 1.00 43.88 C ANISOU 465 CG2 VAL A 97 5838 6010 4824 125 166 27 C ATOM 466 N THR A 98 −18.208 −3.924 38.008 1.00 42.14 N ANISOU 466 N THR A 98 6256 5186 4570 −318 1242 204 N ATOM 467 CA THR A 98 −18.983 −4.827 38.844 1.00 49.46 C ANISOU 467 CA THR A 98 7480 5821 5490 −456 1623 295 C ATOM 468 C THR A 98 −20.077 −5.496 38.016 1.00 52.20 C ANISOU 468 C THR A 98 7489 6060 6284 −618 1840 143 C ATOM 469 O THR A 98 −20.599 −4.901 37.074 1.00 54.32 O ANISOU 469 O THR A 98 7319 6495 6824 −644 1762 −49 O ATOM 470 CB THR A 98 −19.631 −4.080 40.028 1.00 58.99 C ANISOU 470 CB THR A 98 8940 6979 6494 −557 1958 323 C ATOM 471 OG1 THR A 98 −20.489 −3.058 39.511 1.00 62.76 O ANISOU 471 OG1 THR A 98 8990 7613 7242 −639 2062 121 O ATOM 472 CG2 THR A 98 −18.575 −3.426 40.916 1.00 59.23 C ANISOU 472 CG2 THR A 98 9339 7102 6063 −398 1712 442 C ATOM 473 N GLN A 99 −20.420 −6.728 38.362 1.00 53.29 N ANISOU 473 N GLN A 99 7844 5900 6505 −719 2090 222 N ATOM 474 CA GLN A 99 −21.403 −7.497 37.602 1.00 53.42 C ANISOU 474 CA GLN A 99 7534 5774 6989 −885 2282 48 C ATOM 475 C GLN A 99 −22.780 −7.377 38.229 1.00 55.44 C ANISOU 475 C GLN A 99 7738 5854 7471 −1128 2810 −44 C ATOM 476 O GLN A 99 −22.952 −7.666 39.397 1.00 57.95 O ANISOU 476 O GLN A 99 8497 5942 7578 −1220 3183 118 O ATOM 477 CB GLN A 99 −20.981 −8.964 37.522 1.00 56.06 C ANISOU 477 CB GLN A 99 8092 5843 7366 −873 2271 154 C ATOM 478 CG GLN A 99 −21.942 −9.864 36.745 1.00 59.38 C ANISOU 478 CG GLN A 99 8186 6081 8293 −1056 2456 −52 C ATOM 479 CD GLN A 99 −21.483 −11.304 36.736 1.00 64.04 C ANISOU 479 CD GLN A 99 9038 6371 8923 −1041 2463 61 C ATOM 480 OE1 GLN A 99 −21.051 −11.827 37.765 1.00 68.35 O ANISOU 480 OE1 GLN A 99 10112 6676 9180 −1007 2604 326 O ATOM 481 NE2 GLN A 99 −21.558 −11.952 35.573 1.00 62.25 N ANISOU 481 NE2 GLN A 99 8480 6141 9033 −1049 2290 −142 N ATOM 482 N LEU A 100 −23.765 −6.946 37.457 1.00 55.90 N ANISOU 482 N LEU A 100 7269 6004 7965 −1224 2846 −317 N ATOM 483 CA LEU A 100 −25.113 −6.745 38.005 1.00 58.90 C ANISOU 483 CA LEU A 100 7493 6221 8666 −1453 3357 −468 C ATOM 484 C LEU A 100 −25.831 −8.087 38.182 1.00 62.43 C ANISOU 484 C LEU A 100 7979 6289 9454 −1686 3777 −508 C ATOM 485 O LEU A 100 −25.315 −9.123 37.762 1.00 63.47 O ANISOU 485 O LEU A 100 8222 6304 9589 −1652 3615 −436 O ATOM 486 CB LEU A 100 −25.916 −5.798 37.109 1.00 61.88 C ANISOU 486 CB LEU A 100 7258 6808 9444 −1440 3187 −771 C ATOM 487 CG LEU A 100 −25.262 −4.440 36.827 1.00 63.14 C ANISOU 487 CG LEU A 100 7370 7305 9315 −1222 2791 −736 C ATOM 488 CD1 LEU A 100 −26.349 −3.487 36.371 1.00 65.89 C ANISOU 488 CD1 LEU A 100 7214 7745 10077 −1244 2793 −1012 C ATOM 489 CD2 LEU A 100 −24.507 −3.876 38.044 1.00 63.96 C ANISOU 489 CD2 LEU A 100 7978 7438 8887 −1160 2904 −495 C ATOM 490 O PRO A 101 −27.903 −11.467 38.073 1.00 77.58 O ANISOU 490 O PRO A 101 9745 7331 12400 −2107 4498 −829 O ATOM 491 N PRO A 101 −26.998 −8.089 38.852 1.00 66.52 N ANISOU 491 N PRO A 101 8452 6627 10197 −1814 4163 −645 N ATOM 492 C PRO A 101 −28.000 −10.246 37.963 1.00 74.24 C ANISOU 492 C PRO A 101 9103 7180 11926 −2027 4335 −909 C ATOM 493 CA PRO A 101 −27.619 −9.381 39.164 1.00 71.13 C ANISOU 493 CA PRO A 101 9160 6854 11011 −1959 4495 −678 C ATOM 494 CB PRO A 101 −28.874 −8.972 39.943 1.00 72.61 C ANISOU 494 CB PRO A 101 9271 6918 11397 −2046 4872 −864 C ATOM 495 CG PRO A 101 −28.472 −7.708 40.646 1.00 69.54 C ANISOU 495 CG PRO A 101 9105 6730 10587 −1939 4821 −743 C ATOM 496 CD PRO A 101 −27.603 −6.992 39.639 1.00 66.07 C ANISOU 496 CD PRO A 101 8408 6638 10058 −1794 4325 −716 C ATOM 497 O ASN A 102 −28.008 −12.069 34.150 1.00 76.70 O ANISOU 497 O ASN A 102 8301 7562 13278 −2029 3360 −1550 O ATOM 498 N ASN A 102 −28.412 −9.654 36.845 1.00 72.16 N ANISOU 498 N ASN A 102 8259 7146 12013 −1974 3988 −1194 N ATOM 499 CA ASN A 102 −28.873 −10.474 35.718 1.00 74.38 C ANISOU 499 CA ASN A 102 8131 7361 12767 −2016 3786 −1463 C ATOM 500 C ASN A 102 −27.755 −11.252 35.028 1.00 72.75 C ANISOU 500 C ASN A 102 8053 7146 12444 −1997 3527 −1340 C ATOM 501 CB ASN A 102 −29.622 −9.613 34.692 1.00 73.03 C ANISOU 501 CB ASN A 102 7381 7429 12936 −1911 3398 −1800 C ATOM 502 CG ASN A 102 −28.748 −8.569 34.030 1.00 67.03 C ANISOU 502 CG ASN A 102 6538 7032 11899 −1741 2943 −1730 C ATOM 503 OD1 ASN A 102 −27.529 −8.716 33.929 1.00 65.91 O ANISOU 503 OD1 ASN A 102 6652 6982 11409 −1693 2809 −1509 O ATOM 504 ND2 ASN A 102 −29.376 −7.496 33.567 1.00 65.25 N ANISOU 504 ND2 ASN A 102 5980 6996 11814 −1616 2682 −1920 N ATOM 505 O GLY A 103 −23.588 −11.472 33.355 1.00 65.17 O ANISOU 505 O GLY A 103 7716 6751 10295 −1280 2165 −859 O ATOM 506 N GLY A 103 −26.517 −10.982 35.423 1.00 68.04 N ANISOU 506 N GLY A 103 7885 6653 11314 −1866 3410 −1016 N ATOM 507 CA GLY A 103 −25.378 −11.725 34.914 1.00 66.51 C ANISOU 507 CA GLY A 103 7927 6472 10871 −1695 3055 −877 C ATOM 508 C GLY A 103 −24.757 −11.190 33.634 1.00 63.73 C ANISOU 508 C GLY A 103 7303 6488 10424 −1467 2454 −1007 C ATOM 509 O ARG A 104 −23.992 −8.098 30.518 1.00 45.47 O ANISOU 509 O ARG A 104 4270 5255 7753 −916 1100 −1362 O ATOM 510 N ARG A 104 −25.507 −10.424 32.845 1.00 61.46 N ANISOU 510 N ARG A 104 6543 6405 10403 −1469 2266 −1287 N ATOM 511 CA ARG A 104 −24.982 −10.018 31.532 1.00 57.81 C ANISOU 511 CA ARG A 104 5889 6246 9831 −1266 1723 −1414 C ATOM 512 C ARG A 104 −24.679 −8.532 31.439 1.00 49.81 C ANISOU 512 C ARG A 104 4838 5564 8523 −1097 1491 −1347 C ATOM 513 CB ARG A 104 −25.945 −10.422 30.421 1.00 61.80 C ANISOU 513 CB ARG A 104 5941 6714 10826 −1348 1548 −1803 C ATOM 514 CG ARG A 104 −27.335 −9.902 30.613 1.00 63.43 C ANISOU 514 CG ARG A 104 5740 6868 11494 −1496 1721 −2044 C ATOM 515 CD ARG A 104 −28.260 −10.382 29.518 1.00 68.74 C ANISOU 515 CD ARG A 104 6012 7497 12610 −1509 1457 −2432 C ATOM 516 NE ARG A 104 −29.649 −10.078 29.856 1.00 72.02 N ANISOU 516 NE ARG A 104 6188 7812 13364 −1529 1629 −2601 N ATOM 517 CZ ARG A 104 −30.163 −8.862 29.752 1.00 73.38 C ANISOU 517 CZ ARG A 104 6194 8158 13530 −1395 1449 −2663 C ATOM 518 NH1 ARG A 104 −29.395 −7.868 29.311 1.00 71.31 N ANISOU 518 NH1 ARG A 104 5996 8189 12911 −1228 1106 −2547 N ATOM 519 NH2 ARG A 104 −31.430 −8.637 30.089 1.00 75.78 N ANISOU 519 NH2 ARG A 104 6273 8321 14198 −1422 1623 −2850 N ATOM 520 N ASP A 105 −25.148 −7.763 32.418 1.00 49.77 N ANISOU 520 N ASP A 105 4861 5547 8503 −1163 1771 −1269 N ATOM 521 CA ASP A 105 −24.821 −6.340 32.496 1.00 50.67 C ANISOU 521 CA ASP A 105 4984 5932 8337 −1012 1598 −1187 C ATOM 522 C ASP A 105 −23.700 −6.076 33.526 1.00 49.16 C ANISOU 522 C ASP A 105 5259 5773 7648 −932 1688 −863 C ATOM 523 O ASP A 105 −23.596 −6.782 34.541 1.00 50.64 O ANISOU 523 O ASP A 105 5765 5733 7742 −1028 2007 −704 O ATOM 524 CB ASP A 105 −26.081 −5.509 32.845 1.00 54.34 C ANISOU 524 CB ASP A 105 5135 6377 9135 −1108 1803 −1363 C ATOM 525 CG ASP A 105 −27.136 −5.539 31.735 1.00 61.72 C ANISOU 525 CG ASP A 105 5557 7321 10571 −1124 1569 −1719 C ATOM 526 OD1 ASP A 105 −26.763 −5.703 30.557 1.00 61.59 O ANISOU 526 OD1 ASP A 105 5475 7438 10487 −994 1138 −1801 O ATOM 527 OD2 ASP A 105 −28.346 −5.412 32.035 1.00 68.95 O ANISOU 527 OD2 ASP A 105 6194 8097 11906 −1233 1783 −1918 O ATOM 528 N PHE A 106 −22.867 −5.072 33.238 1.00 46.08 N ANISOU 528 N PHE A 106 4920 5643 6947 −754 1393 −779 N ATOM 529 CA PHE A 106 −21.722 −4.683 34.075 1.00 40.91 C ANISOU 529 CA PHE A 106 4637 5054 5855 −651 1371 −531 C ATOM 530 C PHE A 106 −21.691 −3.186 34.224 1.00 43.39 C ANISOU 530 C PHE A 106 4886 5568 6031 −578 1290 −530 C ATOM 531 O PHE A 106 −21.726 −2.466 33.217 1.00 45.14 O ANISOU 531 O PHE A 106 4866 5967 6317 −491 1031 −638 O ATOM 532 CB PHE A 106 −20.381 −5.153 33.475 1.00 32.17 C ANISOU 532 CB PHE A 106 3655 4030 4539 −497 1061 −444 C ATOM 533 CG PHE A 106 −20.295 −6.618 33.342 1.00 38.54 C ANISOU 533 CG PHE A 106 4551 4619 5475 −542 1121 −441 C ATOM 534 CD1 PHE A 106 −20.886 −7.256 32.262 1.00 38.88 C ANISOU 534 CD1 PHE A 106 4321 4622 5830 −599 1051 −654 C ATOM 535 CD2 PHE A 106 −19.694 −7.379 34.326 1.00 38.77 C ANISOU 535 CD2 PHE A 106 4958 4451 5322 −525 1238 −236 C ATOM 536 CE1 PHE A 106 −20.834 −8.640 32.144 1.00 42.56 C ANISOU 536 CE1 PHE A 106 4868 4853 6451 −653 1125 −672 C ATOM 537 CE2 PHE A 106 −19.654 −8.780 34.229 1.00 43.16 C ANISOU 537 CE2 PHE A 106 5622 4751 6026 −564 1311 −223 C ATOM 538 CZ PHE A 106 −20.229 −9.405 33.136 1.00 44.62 C ANISOU 538 CZ PHE A 106 5506 4895 6553 −639 1274 −447 C ATOM 539 N HIS A 107 −21.624 −2.700 35.458 1.00 41.04 N ANISOU 539 N HIS A 107 4842 5228 5525 −607 1508 −410 N ATOM 540 CA HIS A 107 −21.315 −1.283 35.652 1.00 39.78 C ANISOU 540 CA HIS A 107 4676 5251 5186 −519 1398 −396 C ATOM 541 C HIS A 107 −19.800 −1.019 35.544 1.00 38.66 C ANISOU 541 C HIS A 107 4718 5256 4716 −365 1087 −264 C ATOM 542 O HIS A 107 −19.000 −1.639 36.229 1.00 36.62 O ANISOU 542 O HIS A 107 4762 4920 4231 −328 1071 −124 O ATOM 543 CB HIS A 107 −21.857 −0.791 37.005 1.00 45.04 C ANISOU 543 CB HIS A 107 5542 5817 5756 −613 1758 −366 C ATOM 544 CG HIS A 107 −23.304 −0.412 36.967 1.00 52.22 C ANISOU 544 CG HIS A 107 6133 6652 7055 −732 2030 −565 C ATOM 545 ND1 HIS A 107 −24.039 −0.144 38.101 1.00 57.47 N ANISOU 545 ND1 HIS A 107 6925 7179 7734 −858 2468 −595 N ATOM 546 CD2 HIS A 107 −24.157 −0.270 35.923 1.00 53.31 C ANISOU 546 CD2 HIS A 107 5824 6825 7608 −733 1914 −770 C ATOM 547 CE1 HIS A 107 −25.278 0.164 37.756 1.00 59.47 C ANISOU 547 CE1 HIS A 107 6762 7382 8452 −935 2631 −826 C ATOM 548 NE2 HIS A 107 −25.382 0.071 36.445 1.00 58.49 N ANISOU 548 NE2 HIS A 107 6283 7358 8582 −853 2266 −935 N ATOM 549 O MET A 108 −18.599 2.672 34.310 1.00 33.12 O ANISOU 549 O MET A 108 3728 5027 3831 −130 580 −335 O ATOM 550 N MET A 108 −19.427 −0.102 34.659 1.00 33.60 N ANISOU 550 N MET A 108 3887 4802 4079 −272 841 −320 N ATOM 551 C MET A 108 −18.015 1.814 34.977 1.00 34.87 C ANISOU 551 C MET A 108 4154 5185 3912 −137 608 −251 C ATOM 552 CA AMET A 108 −18.042 0.349 34.555 0.73 34.55 C ANISOU 552 CA AMET A 108 4112 5051 3964 −155 605 −240 C ATOM 553 CB AMET A 108 −17.519 0.142 33.130 0.73 33.13 C ANISOU 553 CB AMET A 108 3759 4971 3856 −84 382 −296 C ATOM 554 CG AMET A 108 −17.668 −1.320 32.722 0.73 35.17 C ANISOU 554 CG AMET A 108 4009 5115 4238 −109 396 −322 C ATOM 555 SD AMET A 108 −17.063 −1.780 31.097 0.73 41.12 S ANISOU 555 SD AMET A 108 4624 5959 5042 −33 182 −419 S ATOM 556 CE AMET A 108 −16.695 −3.545 31.344 0.73 39.78 C ANISOU 556 CE AMET A 108 4560 5588 4966 −54 243 −404 C ATOM 557 CA BMET A 108 −18.045 0.370 34.532 0.27 34.11 C ANISOU 557 CA BMET A 108 4051 4998 3911 −154 602 −242 C ATOM 558 CB BMET A 108 −17.529 0.269 33.093 0.27 32.64 C ANISOU 558 CB BMET A 108 3686 4922 3793 −82 376 −300 C ATOM 559 CG BMET A 108 −16.988 −1.085 32.705 0.27 33.74 C ANISOU 559 CG BMET A 108 3870 4991 3960 −57 312 −289 C ATOM 560 SD BMET A 108 −18.292 −2.298 32.503 0.27 36.80 S ANISOU 560 SD BMET A 108 4168 5202 4612 −172 475 −377 S ATOM 561 CE BMET A 108 −17.355 −3.671 31.842 0.27 39.03 C ANISOU 561 CE BMET A 108 4504 5420 4907 −106 344 −380 C ATOM 562 O SER A 109 −15.198 3.453 37.319 1.00 31.33 O ANISOU 562 O SER A 109 4228 4847 2831 9 300 −140 O ATOM 563 N SER A 109 −17.376 2.088 36.105 1.00 31.74 N ANISOU 563 N SER A 109 4006 4772 3280 −121 623 −177 N ATOM 564 CA SER A 109 −17.480 3.418 36.689 1.00 32.08 C ANISOU 564 CA SER A 109 4079 4865 3245 −126 672 −215 C ATOM 565 C SER A 109 −16.148 4.084 36.863 1.00 33.21 C ANISOU 565 C SER A 109 4297 5103 3219 −47 444 −198 C ATOM 566 CB SER A 109 −18.167 3.348 38.071 1.00 34.28 C ANISOU 566 CB SER A 109 4614 5017 3394 −206 959 −201 C ATOM 567 OG SER A 109 −19.447 2.783 37.973 1.00 37.08 O ANISOU 567 OG SER A 109 4855 5256 3979 −309 1234 −253 O ATOM 568 N VAL A 110 −16.090 5.356 36.493 1.00 33.21 N ANISOU 568 N VAL A 110 4159 5179 3281 −40 403 −262 N ATOM 569 CA VAL A 110 −15.059 6.250 36.993 1.00 32.83 C ANISOU 569 CA VAL A 110 4187 5180 3109 −9 267 −291 C ATOM 570 C VAL A 110 −15.515 6.692 38.402 1.00 31.69 C ANISOU 570 C VAL A 110 4285 4970 2785 −45 411 −322 C ATOM 571 O VAL A 110 −16.566 7.332 38.524 1.00 31.03 O ANISOU 571 O VAL A 110 4148 4849 2795 −95 621 −378 O ATOM 572 CB VAL A 110 −14.891 7.481 36.132 1.00 31.93 C ANISOU 572 CB VAL A 110 3878 5121 3131 −7 224 −343 C ATOM 573 CG1 VAL A 110 −13.708 8.297 36.685 1.00 30.11 C ANISOU 573 CG1 VAL A 110 3700 4916 2825 0 88 −404 C ATOM 574 CG2 VAL A 110 −14.666 7.099 34.658 1.00 32.57 C ANISOU 574 CG2 VAL A 110 3786 5250 3340 19 149 −314 C ATOM 575 O VAL A 111 −16.511 8.389 41.679 1.00 32.39 O ANISOU 575 O VAL A 111 5032 4905 2370 −142 835 −507 O ATOM 576 N VAL A 111 −14.781 6.326 39.444 1.00 32.38 N ANISOU 576 N VAL A 111 4652 5031 2621 −9 298 −298 N ATOM 577 C VAL A 111 −15.453 7.977 41.167 1.00 35.58 C ANISOU 577 C VAL A 111 5362 5376 2779 −76 532 −451 C ATOM 578 CA VAL A 111 −15.310 6.506 40.807 1.00 33.76 C ANISOU 578 CA VAL A 111 5162 5121 2544 −46 476 −315 C ATOM 579 CB VAL A 111 −14.469 5.762 41.825 1.00 37.11 C ANISOU 579 CB VAL A 111 5969 5494 2637 32 282 −249 C ATOM 580 CG1 VAL A 111 −14.921 6.093 43.267 1.00 40.92 C ANISOU 580 CG1 VAL A 111 6892 5888 2768 −1 461 −276 C ATOM 581 CG2 VAL A 111 −14.570 4.247 41.545 1.00 35.93 C ANISOU 581 CG2 VAL A 111 5890 5260 2502 55 302 −102 C ATOM 582 N ARG A 112 −14.443 8.777 40.844 1.00 32.56 N ANISOU 582 N ARG A 112 4839 5070 2464 −38 281 −525 N ATOM 583 CA ARG A 112 −14.539 10.227 41.027 1.00 34.44 C ANISOU 583 CA ARG A 112 5013 5304 2769 −73 331 −662 C ATOM 584 C ARG A 112 −14.057 10.952 39.757 1.00 34.54 C ANISOU 584 C ARG A 112 4686 5362 3075 −74 227 −678 C ATOM 585 O ARG A 112 −12.860 11.079 39.525 1.00 35.15 O ANISOU 585 O ARG A 112 4680 5480 3194 −56 2 −715 O ATOM 586 CB ARG A 112 −13.717 10.687 42.248 1.00 37.82 C ANISOU 586 CB ARG A 112 5716 5724 2930 −51 151 −779 C ATOM 587 CG ARG A 112 −14.139 10.079 43.565 1.00 46.73 C ANISOU 587 CG ARG A 112 7297 6785 3674 −43 262 −755 C ATOM 588 CD ARG A 112 −13.240 10.515 44.766 1.00 45.63 C ANISOU 588 CD ARG A 112 7488 6640 3209 10 −9 −890 C ATOM 589 NE ARG A 112 −13.762 9.942 46.011 1.00 55.86 N ANISOU 589 NE ARG A 112 9318 7846 4060 17 150 −844 N ATOM 590 CZ ARG A 112 −14.514 10.599 46.896 1.00 60.76 C ANISOU 590 CZ ARG A 112 10157 8401 4527 −45 436 −941 C ATOM 591 NH1 ARG A 112 −14.833 11.875 46.696 1.00 60.00 N ANISOU 591 NH1 ARG A 112 9880 8312 4606 −109 574 −1126 N ATOM 592 NH2 ARG A 112 −14.941 9.983 47.992 1.00 67.02 N ANISOU 592 NH2 ARG A 112 11291 9100 5072 −41 584 −843 N ATOM 593 N ALA A 113 −14.986 11.437 38.942 1.00 30.42 N ANISOU 593 N ALA A 113 3981 4812 2766 −90 393 −658 N ATOM 594 CA ALA A 113 −14.627 11.937 37.609 1.00 26.49 C ANISOU 594 CA ALA A 113 3251 4331 2482 −80 317 −622 C ATOM 595 C ALA A 113 −13.811 13.207 37.688 1.00 29.11 C ANISOU 595 C ALA A 113 3553 4625 2884 −112 252 −720 C ATOM 596 O ALA A 113 −14.085 14.072 38.505 1.00 33.62 O ANISOU 596 O ALA A 113 4215 5132 3428 −135 322 −829 O ATOM 597 CB ALA A 113 −15.876 12.171 36.792 1.00 30.39 C ANISOU 597 CB ALA A 113 3611 4780 3156 −54 448 −583 C ATOM 598 CD ARG A 114 −8.699 12.801 38.038 1.00 45.78 C ANISOU 598 CD ARG A 114 5351 6839 5205 −155 −473 −1057 C ATOM 599 NE ARG A 114 −8.314 12.206 39.314 1.00 53.81 N ANISOU 599 NE ARG A 114 6543 7886 6017 −71 −746 −1141 N ATOM 600 CZ ARG A 114 −7.175 11.557 39.538 1.00 58.39 C ANISOU 600 CZ ARG A 114 7026 8491 6667 −2 −1035 −1235 C ATOM 601 NH1 ARG A 114 −6.287 11.407 38.555 1.00 55.66 N ANISOU 601 NH1 ARG A 114 6362 8150 6635 −30 −1029 −1279 N ATOM 602 NH2 ARG A 114 −6.925 11.071 40.752 1.00 59.80 N ANISOU 602 NH2 ARG A 114 7445 8674 6602 105 −1327 −1294 N ATOM 603 N ARG A 114 −12.758 13.277 36.876 1.00 30.88 N ANISOU 603 N ARG A 114 3651 4871 3209 −129 144 −703 N ATOM 604 CA ARG A 114 −11.941 14.474 36.732 1.00 32.62 C ANISOU 604 CA ARG A 114 3799 5021 3572 −192 129 −797 C ATOM 605 C ARG A 114 −12.187 15.053 35.347 1.00 30.47 C ANISOU 605 C ARG A 114 3444 4678 3455 −198 246 −688 C ATOM 606 O ARG A 114 −12.519 14.310 34.425 1.00 32.29 O ANISOU 606 O ARG A 114 3649 4958 3663 −152 256 −566 O ATOM 607 CB ARG A 114 −10.439 14.159 36.875 1.00 34.69 C ANISOU 607 CB ARG A 114 3969 5328 3885 −225 −45 −894 C ATOM 608 CG ARG A 114 −10.057 13.492 38.183 1.00 39.36 C ANISOU 608 CG ARG A 114 4690 5977 4288 −177 −254 −988 C ATOM 609 N ARG A 115 −12.018 16.363 35.192 1.00 32.26 N ANISOU 609 N ARG A 115 3667 4770 3819 −249 325 −734 N ATOM 610 C ARG A 115 −11.336 16.174 32.824 1.00 36.23 C ANISOU 610 C ARG A 115 4126 5234 4406 −273 442 −525 C ATOM 611 O ARG A 115 −11.831 15.953 31.714 1.00 33.03 O ANISOU 611 O ARG A 115 3793 4818 3939 −214 480 −380 O ATOM 612 CA ARG A 115 −12.139 16.972 33.872 1.00 33.33 C ANISOU 612 CA ARG A 115 3809 4797 4056 −247 432 −605 C ATOM 613 CB ARG A 115 −11.680 18.437 33.886 1.00 34.75 C ANISOU 613 CB ARG A 115 4010 4786 4408 −333 536 −672 C ATOM 614 CG ARG A 115 −12.572 19.384 34.677 1.00 37.98 C ANISOU 614 CG ARG A 115 4485 5081 4866 −293 564 −749 C ATOM 615 CD ARG A 115 −14.011 19.486 34.099 1.00 35.98 C ANISOU 615 CD ARG A 115 4289 4770 4613 −147 581 −615 C ATOM 616 NE ARG A 115 −14.013 19.699 32.657 1.00 33.90 N ANISOU 616 NE ARG A 115 4106 4414 4363 −104 601 −427 N ATOM 617 CZ ARG A 115 −13.806 20.873 32.063 1.00 34.28 C ANISOU 617 CZ ARG A 115 4271 4234 4519 −123 695 −359 C ATOM 618 NH1 ARG A 115 −13.591 21.975 32.769 1.00 34.88 N ANISOU 618 NH1 ARG A 115 4351 4147 4755 −190 777 −483 N ATOM 619 NH2 ARG A 115 −13.829 20.949 30.751 1.00 38.97 N ANISOU 619 NH2 ARG A 115 5021 4741 5044 −72 713 −165 N ATOM 620 N ASP A 116 −10.117 15.720 33.153 1.00 26.58 N ANISOU 620 N ASP A 116 2781 4076 3242 −345 394 −638 N ATOM 621 CA ASP A 116 −9.325 15.073 32.133 1.00 31.95 C ANISOU 621 CA ASP A 116 3391 4792 3957 −376 461 −597 C ATOM 622 C ASP A 116 −9.781 13.654 31.856 1.00 33.78 C ANISOU 622 C ASP A 116 3635 5166 4035 −277 367 −518 C ATOM 623 O ASP A 116 −9.182 12.990 31.032 1.00 35.83 O ANISOU 623 O ASP A 116 3844 5461 4309 −288 423 −502 O ATOM 624 CB ASP A 116 −7.823 15.076 32.491 1.00 40.25 C ANISOU 624 CB ASP A 116 4236 5838 5220 −479 444 −785 C ATOM 625 CG ASP A 116 −7.576 14.572 33.906 1.00 52.12 C ANISOU 625 CG ASP A 116 5673 7435 6693 −429 176 −934 C ATOM 626 OD1 ASP A 116 −7.538 15.407 34.824 1.00 60.35 O ANISOU 626 OD1 ASP A 116 6735 8420 7777 −465 107 −1058 O ATOM 627 OD2 ASP A 116 −7.470 13.350 34.106 1.00 56.75 O ANISOU 627 OD2 ASP A 116 6236 8135 7189 −343 29 −923 O ATOM 628 N ASP A 117 −10.848 13.181 32.497 1.00 31.31 N ANISOU 628 N ASP A 117 3388 4911 3596 −192 265 −483 N ATOM 629 CA ASP A 117 −11.400 11.886 32.101 1.00 29.12 C ANISOU 629 CA ASP A 117 3125 4727 3212 −116 210 −408 C ATOM 630 C ASP A 117 −12.318 11.994 30.876 1.00 33.46 C ANISOU 630 C ASP A 117 3755 5245 3713 −63 260 −291 C ATOM 631 O ASP A 117 −12.712 10.976 30.321 1.00 32.02 O ANISOU 631 O ASP A 117 3575 5126 3465 −11 212 −254 O ATOM 632 CB ASP A 117 −12.208 11.248 33.214 1.00 26.65 C ANISOU 632 CB ASP A 117 2858 4458 2810 −69 133 −423 C ATOM 633 CG ASP A 117 −11.366 10.735 34.351 1.00 31.91 C ANISOU 633 CG ASP A 117 3529 5162 3433 −74 12 −511 C ATOM 634 OD1 ASP A 117 −10.331 10.057 34.115 1.00 30.96 O ANISOU 634 OD1 ASP A 117 3322 5080 3363 −66 −73 −545 O ATOM 635 OD2 ASP A 117 −11.774 11.000 35.513 1.00 32.13 O ANISOU 635 OD2 ASP A 117 3668 5171 3369 −72 −7 −557 O ATOM 636 N SER A 118 −12.708 13.210 30.495 1.00 31.63 N ANISOU 636 N SER A 118 3606 4899 3513 −59 321 −242 N ATOM 637 CA SER A 118 −13.559 13.367 29.316 1.00 29.70 C ANISOU 637 CA SER A 118 3482 4605 3200 30 294 −130 C ATOM 638 C SER A 118 −12.893 12.718 28.096 1.00 30.75 C ANISOU 638 C SER A 118 3693 4774 3216 17 343 −80 C ATOM 639 O SER A 118 −11.706 12.912 27.844 1.00 34.08 O ANISOU 639 O SER A 118 4114 5169 3665 −83 497 −102 O ATOM 640 CB SER A 118 −13.838 14.831 29.007 1.00 27.79 C ANISOU 640 CB SER A 118 3367 4188 3003 50 346 −65 C ATOM 641 OG SER A 118 −14.514 15.469 30.040 1.00 34.25 O ANISOU 641 OG SER A 118 4118 4955 3942 73 323 −133 O ATOM 642 N GLY A 119 −13.659 11.936 27.362 1.00 29.88 N ANISOU 642 N GLY A 119 3635 4716 3000 109 226 −46 N ATOM 643 CA GLY A 119 −13.121 11.261 26.199 1.00 32.11 C ANISOU 643 CA GLY A 119 4030 5034 3137 105 276 −24 C ATOM 644 C GLY A 119 −13.982 10.127 25.708 1.00 33.96 C ANISOU 644 C GLY A 119 4259 5350 3295 198 101 −52 C ATOM 645 O GLY A 119 −15.163 10.001 26.056 1.00 32.98 O ANISOU 645 O GLY A 119 4053 5230 3247 275 −65 −76 O ATOM 646 N THR A 120 −13.345 9.252 24.949 1.00 34.08 N ANISOU 646 N THR A 120 4327 5419 3203 177 162 −85 N ATOM 647 CA THR A 120 −14.018 8.170 24.270 1.00 34.03 C ANISOU 647 CA THR A 120 4350 5470 3109 252 7 −136 C ATOM 648 C THR A 120 −13.763 6.833 24.941 1.00 33.41 C ANISOU 648 C THR A 120 4063 5471 3160 214 5 −239 C ATOM 649 O THR A 120 −12.618 6.521 25.251 1.00 31.96 O ANISOU 649 O THR A 120 3802 5306 3034 147 148 −274 O ATOM 650 CB THR A 120 −13.526 8.140 22.829 1.00 36.48 C ANISOU 650 CB THR A 120 4941 5757 3162 266 93 −111 C ATOM 651 OG1 THR A 120 −13.789 9.425 22.269 1.00 40.75 O ANISOU 651 OG1 THR A 120 5743 6183 3558 312 91 20 O ATOM 652 CG2 THR A 120 −14.193 7.034 22.024 1.00 37.74 C ANISOU 652 CG2 THR A 120 5166 5972 3203 348 −95 −199 C ATOM 653 N TYR A 121 −14.811 6.041 25.156 1.00 30.08 N ANISOU 653 N TYR A 121 3544 5069 2816 260 −156 −297 N ATOM 654 CA TYR A 121 −14.681 4.788 25.921 1.00 31.48 C ANISOU 654 CA TYR A 121 3565 5273 3125 222 −143 −366 C ATOM 655 C TYR A 121 −15.399 3.651 25.236 1.00 34.73 C ANISOU 655 C TYR A 121 3963 5686 3546 257 −263 −463 C ATOM 656 O TYR A 121 −16.335 3.882 24.477 1.00 35.79 O ANISOU 656 O TYR A 121 4151 5811 3638 321 −422 −498 O ATOM 657 CB TYR A 121 −15.259 4.917 27.338 1.00 27.88 C ANISOU 657 CB TYR A 121 2984 4790 2820 193 −137 −350 C ATOM 658 CG TYR A 121 −14.530 5.881 28.248 1.00 31.05 C ANISOU 658 CG TYR A 121 3388 5185 3225 152 −45 −296 C ATOM 659 CD1 TYR A 121 −14.680 7.250 28.116 1.00 30.61 C ANISOU 659 CD1 TYR A 121 3388 5096 3146 160 −27 −248 C ATOM 660 CD2 TYR A 121 −13.652 5.403 29.227 1.00 30.66 C ANISOU 660 CD2 TYR A 121 3300 5142 3207 119 −7 −306 C ATOM 661 CE1 TYR A 121 −13.969 8.141 28.981 1.00 31.39 C ANISOU 661 CE1 TYR A 121 3478 5174 3275 108 55 −235 C ATOM 662 CE2 TYR A 121 −12.963 6.259 30.074 1.00 31.36 C ANISOU 662 CE2 TYR A 121 3385 5224 3306 87 25 −298 C ATOM 663 CZ TYR A 121 −13.115 7.627 29.946 1.00 33.17 C ANISOU 663 CZ TYR A 121 3645 5426 3532 69 69 −274 C ATOM 664 OH TYR A 121 −12.391 8.481 30.783 1.00 30.39 O ANISOU 664 OH TYR A 121 3278 5052 3214 24 95 −302 O ATOM 665 N LEU A 122 −15.008 2.416 25.547 1.00 33.30 N ANISOU 665 N LEU A 122 3708 5497 3447 227 −221 −522 N ATOM 666 CA LEU A 122 −15.722 1.266 24.992 1.00 33.83 C ANISOU 666 CA LEU A 122 3743 5537 3572 241 −324 −642 C ATOM 667 C LEU A 122 −15.420 0.064 25.855 1.00 34.53 C ANISOU 667 C LEU A 122 3743 5563 3814 197 −249 −660 C ATOM 668 O LEU A 122 −14.543 0.116 26.716 1.00 34.68 O ANISOU 668 O LEU A 122 3756 5574 3846 186 −160 −584 O ATOM 669 CB LEU A 122 −15.329 0.991 23.507 1.00 31.64 C ANISOU 669 CB LEU A 122 3627 5294 3100 286 −363 −725 C ATOM 670 CG LEU A 122 −13.854 0.666 23.152 1.00 35.53 C ANISOU 670 CG LEU A 122 4187 5803 3509 270 −175 −739 C ATOM 671 CD1 LEU A 122 −13.530 −0.773 23.469 1.00 39.44 C ANISOU 671 CD1 LEU A 122 4571 6245 4168 260 −149 −835 C ATOM 672 CD2 LEU A 122 −13.542 0.895 21.632 1.00 38.46 C ANISOU 672 CD2 LEU A 122 4809 6201 3602 303 −138 −795 C ATOM 673 N CYS A 123 −16.177 −1.000 25.631 1.00 36.76 N ANISOU 673 N CYS A 123 3967 5779 4221 180 −308 −769 N ATOM 674 C CYS A 123 −15.651 −3.318 25.200 1.00 38.24 C ANISOU 674 C CYS A 123 4149 5830 4549 170 −277 −932 C ATOM 675 O CYS A 123 −16.195 −3.249 24.091 1.00 39.11 O ANISOU 675 O CYS A 123 4285 5985 4590 190 −397 −1057 O ATOM 676 CA ACYS A 123 −16.015 −2.293 26.278 0.37 37.02 C ANISOU 676 CA ACYS A 123 3963 5699 4404 142 −236 −787 C ATOM 677 CB ACYS A 123 −17.318 −2.658 27.004 0.37 36.61 C ANISOU 677 CB ACYS A 123 3809 5537 4563 63 −203 −812 C ATOM 678 SG ACYS A 123 −17.513 −4.322 27.676 0.37 53.19 S ANISOU 678 SG ACYS A 123 5910 7424 6875 −13 −82 −838 S ATOM 679 CA BCYS A 123 −15.830 −2.261 26.262 0.63 37.27 C ANISOU 679 CA BCYS A 123 4006 5739 4416 149 −230 −779 C ATOM 680 CB BCYS A 123 −16.860 −2.692 27.308 0.63 37.76 C ANISOU 680 CB BCYS A 123 3996 5681 4672 71 −165 −760 C ATOM 681 SG BCYS A 123 −18.515 −3.004 26.705 0.63 35.46 S ANISOU 681 SG BCYS A 123 3540 5331 4604 16 −255 −945 S ATOM 682 N GLY A 124 −14.776 −4.266 25.514 1.00 37.42 N ANISOU 682 N GLY A 124 4060 5645 4513 187 −203 −930 N ATOM 683 CA GLY A 124 −14.397 −5.246 24.534 1.00 36.38 C ANISOU 683 CA GLY A 124 3954 5473 4396 217 −212 −1090 C ATOM 684 C GLY A 124 −14.460 −6.623 25.131 1.00 37.42 C ANISOU 684 C GLY A 124 4059 5412 4748 199 −176 −1114 C ATOM 685 O GLY A 124 −14.205 −6.808 26.332 1.00 35.35 O ANISOU 685 O GLV A 124 3817 5055 4561 202 −124 −966 O ATOM 686 N ALA A 125 −14.842 −7.564 24.281 1.00 38.76 N ANISOU 686 N ALA A 125 4222 5506 5000 183 −214 −1303 N ATOM 687 CA ALA A 125 −14.786 −8.987 24.558 1.00 41.58 C ANISOU 687 CA ALA A 125 4575 5643 5579 172 −167 −1364 C ATOM 688 C ALA A 125 −13.855 −9.645 23.550 1.00 42.84 C ANISOU 688 C ALA A 125 4770 5794 5714 251 −151 −1537 C ATOM 689 O ALA A 125 −13.607 −9.107 22.475 1.00 44.02 O ANISOU 689 O ALA A 125 4968 6099 5661 278 −169 −1650 O ATOM 690 CB ALA A 125 −16.163 −9.611 24.469 1.00 38.43 C ANISOU 690 CB ALA A 125 4104 5116 5381 56 −198 −1490 C ATOM 691 N ILE A 126 −13.410 −10.846 23.867 1.00 42.53 N ANISOU 691 N ILE A 126 4736 5545 5878 287 −102 −1569 N ATOM 692 CA ILE A 126 −12.572 −11.585 22.954 1.00 43.11 C ANISOU 692 CA ILE A 126 4820 5572 5986 365 −59 −1769 C ATOM 693 C ILE A 126 −13.172 −12.966 22.678 1.00 49.76 C ANISOU 693 C ILE A 126 5671 6179 7058 318 −67 −1946 C ATOM 694 O ILE A 126 −13.793 −13.568 23.550 1.00 51.93 O ANISOU 694 O ILE A 126 5947 6249 7534 254 −54 −1847 O ATOM 695 CB ILE A 126 −11.154 −11.691 23.537 1.00 40.17 C ANISOU 695 CB ILE A 126 4410 5150 5702 499 −3 −1677 C ATOM 696 CG1 ILE A 126 −10.201 −12.425 22.605 1.00 39.61 C ANISOU 696 CG1 ILE A 126 4307 5019 5723 589 88 −1914 C ATOM 697 CG2 ILE A 126 −11.171 −12.364 24.888 1.00 40.17 C ANISOU 697 CG2 ILE A 126 4449 4920 5893 536 −48 −1486 C ATOM 698 CD1 ILE A 126 −8.743 −12.233 23.089 1.00 40.14 C ANISOU 698 CD1 ILE A 126 4255 5080 5916 731 126 −1863 C ATOM 699 O SER A 127 −11.610 −14.784 19.717 1.00 48.68 O ANISOU 699 O SER A 127 5634 5942 6922 469 100 −2684 O ATOM 700 N SER A 127 −13.017 −13.466 21.456 1.00 48.94 N ANISOU 700 N SER A 127 5596 6082 6918 335 −63 −2221 N ATOM 701 CA SER A 127 −13.480 −14.813 21.156 1.00 48.02 C ANISOU 701 CA SER A 127 5480 5719 7048 292 −70 −2429 C ATOM 702 C SER A 127 −12.411 −15.475 20.345 1.00 46.45 C ANISOU 702 C SER A 127 5317 5464 6866 402 25 −2641 C ATOM 703 CB SER A 127 −14.814 −14.817 20.392 1.00 52.12 C ANISOU 703 CB SER A 127 5987 6280 7537 167 −213 −2643 C ATOM 704 OG SER A 127 −15.130 −16.132 19.910 1.00 55.10 O ANISOU 704 OG SER A 127 6359 6419 8158 122 −220 −2915 O ATOM 705 O LEU A 128 −11.302 −18.686 17.482 1.00 56.68 O ANISOU 705 O LEU A 128 6761 6307 8470 526 255 −3664 O ATOM 706 N LEU A 128 −12.389 −16.807 20.365 1.00 45.63 N ANISOU 706 N LEU A 128 5210 5071 7057 413 59 −2781 N ATOM 707 CA LEU A 128 −11.432 −17.574 19.587 1.00 50.69 C ANISOU 707 CA LEU A 128 5868 5615 7777 522 168 −3030 C ATOM 708 C LEU A 128 −12.022 −18.091 18.290 1.00 54.19 C ANISOU 708 C LEU A 128 6397 6055 8137 450 135 −3403 C ATOM 709 CB LEU A 128 −10.913 −18.771 20.383 1.00 55.08 C ANISOU 709 CB LEU A 128 6391 5812 8727 618 211 −2972 C ATOM 710 CG LEU A 128 −10.604 −18.636 21.865 1.00 57.74 C ANISOU 710 CG LEU A 128 6718 6035 9187 691 167 −2603 C ATOM 711 CD1 LEU A 128 −9.963 −19.929 22.338 1.00 59.13 C ANISOU 711 CD1 LEU A 128 6919 5825 9723 835 181 −2606 C ATOM 712 CD2 LEU A 128 −9.691 −17.450 22.101 1.00 59.48 C ANISOU 712 CD2 LEU A 128 6863 6526 9212 787 163 −2454 C ATOM 713 O ALA A 129 −15.233 −16.529 16.493 1.00 56.84 O ANISOU 713 O ALA A 129 6879 6854 7862 176 −454 −3736 O ATOM 714 N ALA A 129 −13.328 −17.916 18.091 1.00 52.57 N ANISOU 714 N ALA A 129 6204 5899 7872 310 −34 −3465 N ATOM 715 CA ALA A 129 −13.937 −18.518 16.910 1.00 55.45 C ANISOU 715 CA ALA A 129 6650 6228 8191 251 −137 −3858 C ATOM 716 C ALA A 129 −14.595 −17.469 16.007 1.00 55.57 C ANISOU 716 C ALA A 129 6784 6547 7783 220 −332 −3951 C ATOM 717 CB ALA A 129 −14.932 −19.588 17.318 1.00 55.07 C ANISOU 717 CB ALA A 129 6492 5871 8559 121 −210 −3968 C ATOM 718 O PRO A 130 −11.448 −19.471 13.748 1.00 62.27 O ANISOU 718 O PRO A 130 7964 7184 8513 475 311 −4479 O ATOM 719 N PRO A 130 −14.426 −17.619 14.683 1.00 56.85 N ANISOU 719 N PRO A 130 7155 6795 7652 256 −360 −4231 N ATOM 720 CA PRO A 130 −13.710 −18.721 14.014 1.00 60.20 C ANISOU 720 CA PRO A 130 7668 7059 8147 298 −191 −4422 C ATOM 721 C PRO A 130 −12.193 −18.547 14.088 1.00 58.25 C ANISOU 721 C PRO A 130 7443 6837 7850 421 133 −4347 C ATOM 722 CB PRO A 130 −14.202 −18.630 12.563 1.00 62.12 C ANISOU 722 CB PRO A 130 8186 7438 7979 280 −352 −4607 C ATOM 723 CG PRO A 130 −14.444 −17.171 12.361 1.00 60.39 C ANISOU 723 CG PRO A 130 8108 7501 7338 301 −469 −4433 C ATOM 724 CD PRO A 130 −14.910 −16.613 13.719 1.00 59.38 C ANISOU 724 CD PRO A 130 7693 7383 7484 264 −550 −4223 C ATOM 725 O LYS A 131 −11.300 −15.554 16.330 1.00 59.86 O ANISOU 725 O LYS A 131 7402 7459 7883 486 240 −3482 O ATOM 726 N LYS A 131 −11.759 −17.368 14.537 1.00 57.89 N ANISOU 726 N LYS A 131 7376 6989 7632 462 205 −4141 N ATOM 727 CA LYS A 131 −10.335 −17.076 14.762 1.00 59.58 C ANISOU 727 CA LYS A 131 7524 7230 7883 567 506 −4047 C ATOM 728 C LYS A 131 −10.259 −16.071 15.913 1.00 57.87 C ANISOU 728 C LYS A 131 7154 7128 7704 567 460 −3648 C ATOM 729 CB LYS A 131 −9.665 −16.538 13.480 1.00 62.67 C ANISOU 729 CB LYS A 131 8177 7795 7840 575 718 −4113 C ATOM 730 CG LYS A 131 −10.155 −15.149 13.018 1.00 61.10 C ANISOU 730 CG LYS A 131 8212 7865 7140 528 629 −3979 C ATOM 731 CD LYS A 131 −9.798 −14.887 11.540 1.00 63.14 C ANISOU 731 CD LYS A 131 8875 8197 6919 527 799 −4074 C ATOM 732 O VAL A 132 −8.961 −12.998 16.012 1.00 52.94 O ANISOU 732 O VAL A 132 6589 7007 6520 574 743 −3200 O ATOM 733 N VAL A 132 −9.069 −15.798 16.456 1.00 51.31 N ANISOU 733 N VAL A 132 6178 6296 7022 656 649 −3513 N ATOM 734 CA VAL A 132 −8.993 −14.830 17.559 1.00 51.06 C ANISOU 734 CA VAL A 132 6020 6371 7009 655 576 −3157 C ATOM 735 C VAL A 132 −9.424 −13.453 17.057 1.00 50.05 C ANISOU 735 C VAL A 132 6051 6520 6445 577 556 −3058 C ATOM 736 CB VAL A 132 −7.577 −14.722 18.174 1.00 50.08 C ANISOU 736 CB VAL A 132 5689 6201 7139 777 736 −3080 C ATOM 737 CG1 VAL A 132 −7.606 −13.755 19.261 1.00 44.23 C ANISOU 737 CG1 VAL A 132 4857 5567 6383 767 618 −2756 C ATOM 738 CG2 VAL A 132 −7.112 −16.054 18.714 1.00 52.93 C ANISOU 738 CG2 VAL A 132 5912 6257 7942 899 707 −3155 C ATOM 739 O GLN A 133 −11.827 −11.260 19.557 1.00 42.56 O ANISOU 739 O GLN A 133 4962 5790 5419 412 48 −2311 O ATOM 740 N GLN A 133 −10.306 −12.793 17.797 1.00 50.48 N ANISOU 740 N GLN A 133 6077 6651 6454 518 353 −2816 N ATOM 741 CA GLN A 133 −10.848 −11.494 17.401 1.00 51.28 C ANISOU 741 CA GLN A 133 6326 6977 6182 465 281 −2707 C ATOM 742 C GLN A 133 −11.280 −10.702 18.625 1.00 45.41 C ANISOU 742 C GLN A 133 5448 6283 5522 435 159 −2398 C ATOM 743 CB GLN A 133 −12.049 −11.658 16.444 1.00 56.21 C ANISOU 743 CB GLN A 133 7142 7636 6579 419 64 −2896 C ATOM 744 CG GLN A 133 −13.107 −12.636 16.960 1.00 60.12 C ANISOU 744 CG GLN A 133 7489 7958 7396 364 −146 −2967 C ATOM 745 CD GLN A 133 −14.469 −12.447 16.306 1.00 64.69 C ANISOU 74b CD GLN A 133 81bb 8b99 782b 314 −446 −3111 C ATOM 746 OE1 GLN A 133 −14.932 −11.313 16.133 1.00 66.19 O ANISOU 746 OE1 GLN A 133 8431 8960 7759 323 −582 −2992 O ATOM 747 NE2 GLN A 133 −15.126 −13.562 15.948 1.00 63.73 N ANISOU 747 NE2 GLN A 133 7997 8317 7901 269 −577 −3387 N ATOM 748 O ILE a 134 −13.112 −7.866 17.928 1.00 50.86 O ANISOU 748 O ILE A 134 6434 7355 5534 367 −170 −2151 O ATOM 749 N ILE A 134 −10.992 −9.410 18.645 1.00 45.08 N ANISOU 749 N ILE A 134 5455 6410 5265 428 217 −2237 N ATOM 750 CA ILE A 134 −11.589 −8.546 19.648 1.00 44.28 C ANISOU 750 CA ILE A 134 5271 6370 5185 393 87 −1984 C ATOM 751 C ILE A 134 −12.957 −8.130 19.126 1.00 46.76 C ANISOU 751 C ILE A 134 5698 6757 5313 350 −133 −2017 C ATOM 752 CB ILE A 134 −10.754 −7.328 19.923 1.00 40.89 C ANISOU 752 CB ILE A 134 4828 6059 4649 400 224 −1820 C ATOM 753 CG1 ILE A 134 −9.348 −7.767 20.348 1.00 43.21 C ANISOU 753 CG1 ILE A 134 4956 6274 5189 459 402 −1854 C ATOM 754 CG2 ILE A 134 −11.402 −6.433 21.016 1.00 36.69 C ANISOU 754 CG2 ILE A 134 4220 5578 4141 366 91 −1580 C ATOM 755 CD1 ILE A 134 −9.316 −8.758 21.521 1.00 40.56 C ANISOU 755 CD1 ILE A 134 4460 5766 5184 514 282 −1793 C ATOM 756 N LYS A 135 −13.956 −8.112 19.997 1.00 44.24 N ANISOU 756 N LYS A 135 5244 6392 5174 302 −283 −1916 N ATOM 757 CA LYS A 135 −15.235 −7.512 19.616 1.00 43.24 C ANISOU 757 CA LYS A 135 5150 6337 4943 280 −513 −1948 C ATOM 758 C LYS A 135 −15.394 −6.245 20.420 1.00 39.05 C ANISOU 758 C LYS A 135 4567 5897 4375 274 −510 −1704 C ATOM 759 O LYS A 135 −15.603 −6.312 21.639 1.00 39.58 O ANISOU 759 O LYS A 135 4476 5893 4668 228 −460 −1570 O ATOM 760 CB LYS A 135 −16.413 −8.467 19.857 1.00 47.69 C ANISOU 760 CB LYS A 135 5555 6755 5809 211 −663 −2097 C ATOM 761 CG LYS A 135 −16.470 −9.670 18.898 1.00 52.49 C ANISOU 761 CG LYS A 135 6226 7265 6453 210 −723 −2397 C ATOM 762 CD LYS A 135 −17.638 −10.592 19.225 1.00 56.02 C ANISOU 762 CD LYS A 135 6474 7533 7277 110 −842 −2557 C ATOM 763 N GLU A 136 −15.268 −5.097 19.758 1.00 35.71 N ANISOU 763 N GLU A 136 4315 5604 3648 321 −542 −1643 N ATOM 764 C GLU A 136 −16.836 −3.422 20.476 1.00 35.76 C ANISOU 764 C GLU A 136 4211 5679 3699 328 −791 −1458 C ATOM 765 O GLU A 136 −17.523 −3.626 19.487 1.00 36.05 O ANISOU 765 O GLU A 136 4339 5722 3638 375 −1018 −1629 O ATOM 766 CG GLU A 136 −13.022 −2.978 19.626 1.00 47.50 C ANISOU 766 CG GLU A 136 6035 7254 4759 340 −111 −1346 C ATOM 767 CD GLU A 136 −12.323 −1.796 18.915 1.00 50.24 C ANISOU 767 CD GLU A 136 6617 7659 4811 339 69 −1261 C ATOM 768 OE1 GLU A 136 −13.023 −1.028 18.212 1.00 51.42 O ANISOU 768 OE1 GLU A 136 7008 7840 4688 379 −73 −1216 O ATOM 769 OE2 GLU A 136 −11.084 −1.617 19.056 1.00 46.12 O ANISOU 769 OE2 GLU A 136 6042 7130 4352 302 350 −1244 O ATOM 770 CA GLU A 136 −15.370 −3.823 20.467 1.00 32.90 C ANISOU 770 CA GLU A 136 3922 5315 3262 319 −530 −1425 C ATOM 771 CB GLU A 136 −14.548 −2.728 19.798 1.00 36.80 C ANISOU 771 CB GLU A 136 4642 5903 3439 355 −411 −1331 C ATOM 772 N SER A 137 −17.314 −2.834 21.561 1.00 34.32 N ANISOU 772 N SER A 137 3863 5483 3694 294 −772 −1323 N ATOM 773 CA SER A 137 −18.638 −2.222 21.521 1.00 38.59 C ANISOU 773 CA SER A 137 4305 6025 4334 321 −999 −1366 C ATOM 774 C SER A 137 −18.560 −0.969 20.651 1.00 40.09 C ANISOU 774 C SER A 137 4731 6301 4199 432 −1135 −1291 C ATOM 775 O SER A 137 −17.484 −0.502 20.322 1.00 38.35 O ANISOU 775 O SER A 137 4726 6132 3715 445 −971 −1176 O ATOM 776 CB SER A 137 −19.102 −1.851 22.919 1.00 36.52 C ANISOU 776 CB SER A 137 3832 5714 4331 253 −877 −1250 C ATOM 777 OG SER A 137 −18.306 −0.795 23.461 1.00 32.93 O ANISOU 777 OG SER A 137 3470 5322 3720 268 −732 −1043 O ATOM 778 N LEU A 138 −19.698 −0.397 20.310 1.00 37.05 N ANISOU 778 N LEU A 138 4306 5910 3863 513 −1424 −1356 N ATOM 779 CA LEU A 138 −19.717 0.977 19.829 1.00 40.16 C ANISOU 779 CA LEU A 138 4919 6338 4000 628 −1541 −1220 C ATOM 780 C LEU A 138 −19.149 1.894 20.899 1.00 40.98 C ANISOU 780 C LEU A 138 4966 6448 4158 572 −1274 −999 C ATOM 781 O LEU A 138 −19.180 1.586 22.119 1.00 41.48 O ANISOU 781 O LEU A 138 4779 6486 4496 471 −1096 −975 O ATOM 782 CB LEU A 138 −21.136 1.413 19.436 1.00 45.42 C ANISOU 782 CB LEU A 138 5489 6966 4802 756 −1952 −1345 C ATOM 783 CG LEU A 138 −21.800 0.509 18.404 1.00 46.57 C ANISOU 783 CG LEU A 138 5667 7073 4955 804 −2246 −1583 C ATOM 784 CD1 LEU A 138 −23.325 0.761 18.372 1.00 51.66 C ANISOU 784 CD1 LEU A 138 6055 7602 5970 875 −2531 −1696 C ATOM 785 CD2 LEU A 138 −21.176 0.757 17.058 1.00 48.44 C ANISOU 785 CD2 LEU A 138 6391 7320 4693 888 −2292 −1506 C ATOM 786 N ARG A 139 −18.577 3.002 20.447 1.00 39.20 N ANISOU 786 N ARG A 139 5011 6236 3647 630 −1227 −841 N ATOM 787 CA ARG A 139 −17.828 3.873 21.349 1.00 38.07 C ANISOU 787 CA ARG A 139 4839 6091 3534 562 −962 −659 C ATOM 788 C ARG A 139 −18.773 4.900 21.947 1.00 40.93 C ANISOU 788 C ARG A 139 5073 6402 4075 621 −1088 −606 C ATOM 789 O ARG A 139 −19.701 5.352 21.287 1.00 45.61 O ANISOU 789 O ARG A 139 5732 6955 4645 756 −1383 −648 O ATOM 790 CB ARG A 139 −16.666 4.523 20.601 1.00 40.39 C ANISOU 790 CB ARG A 139 5463 6388 3495 558 −773 −537 C ATOM 791 CG ARG A 139 −15.742 3.453 20.037 1.00 42.66 C ANISOU 791 CG ARG A 139 5833 6715 3662 500 −607 −633 C ATOM 792 CD ARG A 139 −14.610 3.975 19.153 1.00 49.30 C ANISOU 792 CD ARG A 139 7004 7539 4190 475 −351 −558 C ATOM 793 NE ARG A 139 −13.801 2.853 18.672 1.00 51.57 N ANISOU 793 NE ARG A 139 7311 7854 4429 425 −175 −698 N ATOM 794 CZ ARG A 139 −12.568 2.973 18.197 1.00 53.58 C ANISOU 794 CZ ARG A 139 7712 8092 4555 355 170 −694 C ATOM 795 NH1 ARG A 139 −12.024 4.186 18.126 1.00 54.33 N ANISOU 795 NH1 ARG A 139 7963 8133 4549 310 379 −544 N ATOM 796 NH2 ARG A 139 −11.890 1.888 17.787 1.00 50.34 N ANISOU 796 NH2 ARG A 139 7280 7694 4154 324 329 −857 N ATOM 797 O ALA A 140 −17.363 7.181 24.502 1.00 38.21 O ANISOU 797 O ALA A 140 4612 6008 3900 452 −545 −297 O ATOM 798 N ALA A 140 −18.559 5.233 23.210 1.00 38.22 N ANISOU 798 N ALA A 140 4551 6051 3921 535 −887 −538 N ATOM 799 CA ALA A 140 −19.432 6.168 23.915 1.00 41.12 C ANISOU 799 CA ALA A 140 4771 6358 4493 576 −944 −518 C ATOM 800 C ALA A 140 −18.578 7.326 24.374 1.00 39.26 C ANISOU 800 C ALA A 140 4659 6101 4155 542 −750 −358 C ATOM 801 CB ALA A 140 −20.095 5.506 25.096 1.00 41.31 C ANISOU 801 CB ALA A 140 4490 6366 4841 488 −848 −618 C ATOM 802 N AGLU A 141 −19.200 8.466 24.639 0.50 36.77 N ANISOU 802 N AGLU A 141 4324 5707 3940 614 −817 −317 N ATOM 803 CA AGLU A 141 −18.442 9.641 25.026 0.50 36.21 C ANISOU 803 CA AGLU A 141 4375 5584 3799 578 −642 −186 C ATOM 804 C AGLU A 141 −18.774 10.053 26.448 0.50 33.98 C ANISOU 804 C AGLU A 141 3878 5275 3757 520 −514 −225 C ATOM 805 O AGLU A 141 −19.945 10.089 26.836 0.50 35.04 O ANISOU 805 O AGLU A 141 3823 5368 4124 577 −605 −321 O ATOM 806 CB AGLU A 141 −18.706 10.783 24.041 0.50 41.97 C ANISOU 806 CB AGLU A 141 5367 6198 4383 718 −797 −80 C ATOM 807 CG AGLU A 141 −18.197 10.453 22.638 0.50 45.67 C ANISOU 807 CG AGLU A 141 6163 6679 4511 759 −858 −22 C ATOM 808 CD AGLU A 141 −18.398 11.563 21.623 0.50 57.19 C ANISOU 808 CD AGLU A 141 7998 7990 5742 907 −1004 121 C ATOM 809 OE1 AGLU A 141 −18.821 12.678 22.013 0.50 60.61 O ANISOU 809 OE1 AGLU A 141 8423 8295 6312 977 −1047 189 O ATOM 810 OE2 AGLU A 141 −18.127 11.316 20.424 0.50 61.11 O ANISOU 810 OE2 AGLU A 141 8838 8479 5904 959 −1068 167 O ATOM 811 N BGLU A 141 −19.168 8.494 24.587 0.50 36.84 N ANISOU 811 N BGLU A 141 4347 5715 3935 617 −819 −312 N ATOM 812 CA BGLU A 141 −18.335 9.591 25.040 0.50 35.54 C ANISOU 812 CA BGLU A 141 4295 5507 3703 566 −623 −183 C ATOM 813 C BGLU A 141 −18.746 10.015 26.432 0.50 33.89 C ANISOU 813 C BGLU A 141 3869 5267 3740 518 −513 −225 C ATOM 814 O BGLU A 141 −19.930 10.007 26.787 0.50 34.96 O ANISOU 814 O BGLU A 141 3814 5363 4105 575 −610 −323 O ATOM 815 CB BGLU A 141 −18.364 10.772 24.056 0.50 41.41 C ANISOU 815 CB BGLU A 141 5328 6137 4269 683 −729 −60 C ATOM 816 CG BGLU A 141 −19.536 11.698 24.125 0.50 47.62 C ANISOU 816 CG BGLU A 141 6062 6803 5229 836 −941 −67 C ATOM 817 CD BGLU A 141 −19.258 13.048 23.449 0.50 56.78 C ANISOU 817 CD BGLU A 141 7561 7802 6211 926 −962 107 C ATOM 818 OE1 BGLU A 141 −18.106 13.256 23.009 0.50 58.96 O ANISOU 818 OE1 BGLU A 141 8096 8063 6242 829 −744 226 O ATOM 819 OE2 BGLU A 141 −20.179 13.897 23.354 0.50 58.94 O ANISOU 819 OE2 BGLU A 141 7841 7939 6615 1093 −1178 118 O ATOM 820 N LEU A 142 −17.737 10.328 27.232 1.00 29.18 N ANISOU 820 N LEU A 142 3293 4686 3107 405 −299 −179 N ATOM 821 CA LEU A 142 −17.913 10.860 28.578 1.00 28.20 C ANISOU 821 CA LEU A 142 3052 4529 3134 352 −174 −218 C ATOM 822 C LEU A 142 −17.525 12.349 28.559 1.00 28.54 C ANISOU 822 C LEU A 142 3219 4465 3162 365 −120 −147 C ATOM 823 O LEU A 142 −16.449 12.707 28.054 1.00 29.52 O ANISOU 823 O LEU A 142 3492 4573 3150 314 −43 −69 O ATOM 824 CB LEU A 142 −17.031 10.075 29.583 1.00 30.01 C ANISOU 824 CB LEU A 142 3243 4839 3321 230 −31 −245 C ATOM 825 CG LEU A 142 −16.923 10.660 31.001 1.00 31.30 C ANISOU 825 CG LEU A 142 3384 4972 3537 169 95 −286 C ATOM 826 CD1 LEU A 142 −18.279 10.680 31.645 1.00 31.83 C ANISOU 826 CD1 LEU A 142 3340 4987 3768 194 140 −366 C ATOM 827 CD2 LEU A 142 −15.922 9.878 31.925 1.00 26.31 C ANISOU 827 CD2 LEU A 142 2782 4408 2809 88 150 −302 C ATOM 828 N ARG A 143 −18.380 13.214 29.091 1.00 27.94 N ANISOU 828 N ARG A 143 3072 4290 3255 423 −129 −189 N ATOM 829 C ARG A 143 −18.148 14.943 30.693 1.00 31.81 C ANISOU 829 C ARG A 143 3555 4636 3896 352 89 −254 C ATOM 830 O ARG A 143 −19.211 14.743 31.289 1.00 30.81 O ANISOU 830 O ARG A 143 3277 4500 3929 392 102 −359 O ATOM 831 CA ARG A 143 −18.016 14.621 29.220 1.00 29.12 C ANISOU 831 CA ARG A 143 3334 4306 3426 425 −58 −137 C ATOM 832 CB ARG A 143 −18.900 15.598 28.399 1.00 32.20 C ANISOU 832 CB ARG A 143 3811 4527 3894 599 −225 −78 C ATOM 833 CG ARG A 143 −18.742 15.605 26.851 1.00 72.08 C ANISOU 833 CG ARG A 143 9122 9534 8730 699 −389 67 C ATOM 834 CD ARG A 143 −17.356 16.075 26.328 1.00 68.54 C ANISOU 834 CD ARG A 143 8941 9034 8068 584 −195 203 C ATOM 835 NE ARG A 143 −16.472 14.925 26.184 1.00 65.66 N ANISOU 835 NE ARG A 143 8544 8841 7564 460 −92 175 N ATOM 836 CZ ARG A 143 −16.127 14.364 25.035 1.00 65.27 C ANISOU 836 CZ ARG A 143 8688 8827 7286 478 −117 241 C ATOM 837 NH1 ARG A 143 −16.527 14.865 23.871 1.00 68.09 N ANISOU 837 NH1 ARG A 143 9353 9060 7458 612 −251 364 N ATOM 838 NH2 ARG A 143 −15.356 13.300 25.059 1.00 64.84 N ANISOU 838 NH2 ARG A 143 8549 8916 7173 372 −12 179 N ATOM 839 N VAL A 144 −17.054 15.426 31.274 1.00 31.58 N ANISOU 839 N VAL A 144 3595 4599 3804 239 213 −261 N ATOM 840 CA VAL A 144 −17.060 15.813 32.671 1.00 33.73 C ANISOU 840 CA VAL A 144 3825 4856 4136 173 329 −387 C ATOM 841 C VAL A 144 −17.126 17.330 32.681 1.00 35.73 C ANISOU 841 C VAL A 144 4139 4924 4514 200 374 −398 C ATOM 842 O VAL A 144 −16.283 17.992 32.061 1.00 34.95 O ANISOU 842 O VAL A 144 4149 4740 4391 160 390 −319 O ATOM 843 CB VAL A 144 −15.810 15.300 33.407 1.00 30.37 C ANISOU 843 CB VAL A 144 3428 4536 3576 49 366 −432 C ATOM 844 CG1 VAL A 144 −15.869 15.688 34.866 1.00 25.47 C ANISOU 844 CG1 VAL A 144 2836 3895 2948 −1 447 −573 C ATOM 845 CG2 VAL A 144 −15.731 13.767 33.277 1.00 28.73 C ANISOU 845 CG2 VAL A 144 3184 4472 3260 46 309 −400 C ATOM 846 N THR A 145 −18.123 17.885 33.363 1.00 34.70 N ANISOU 846 N THR A 145 3940 4703 4543 260 428 −504 N ATOM 847 CA THR A 145 −18.271 19.329 33.386 1.00 38.67 C ANISOU 847 CA THR A 145 4497 4997 5201 305 467 −528 C ATOM 848 C THR A 145 −17.688 19.973 34.650 1.00 39.11 C ANISOU 848 C THR A 145 4590 5015 5255 185 613 −685 C ATOM 849 O THR A 145 −17.593 19.345 35.698 1.00 40.05 O ANISOU 849 O THR A 145 4697 5258 5261 110 680 −801 O ATOM 850 CB THR A 145 −19.746 19.728 33.225 1.00 43.79 C ANISOU 850 CB THR A 145 5026 5519 6092 479 414 −577 C ATOM 851 OG1 THR A 145 −20.542 19.124 34.250 1.00 47.54 O ANISOU 851 OG1 THR A 145 5341 6073 6648 456 543 −746 O ATOM 852 CG2 THR A 145 −20.265 19.255 31.844 1.00 47.11 C ANISOU 852 CG2 THR A 145 5442 5947 6510 624 181 −436 C ATOM 853 O GLU A 146 −19.018 22.626 36.400 1.00 48.08 O ANISOU 853 O GLU A 146 5715 5721 6833 266 891 −1062 O ATOM 854 N GLU A 146 −17.281 21.223 34.522 1.00 34.62 N ANISOU 854 N GLU A 146 4105 4254 4794 168 651 −689 N ATOM 855 CA GLU A 146 −16.800 22.005 35.653 1.00 37.67 C ANISOU 855 CA GLU A 146 4528 4567 5218 64 762 −877 C ATOM 856 C GLU A 146 −17.894 22.193 36.709 1.00 44.41 C ANISOU 856 C GLU A 146 5330 5388 6154 123 875 −1060 C ATOM 857 CB GLU A 146 −16.275 23.353 35.133 1.00 39.38 C ANISOU 857 CB GLU A 146 4838 4529 5596 37 801 −838 C ATOM 858 CG GLU A 146 −15.174 24.083 35.976 1.00 46.35 C ANISOU 858 CG GLU A 146 5752 5338 6518 −137 877 −1024 C ATOM 859 CD GLU A 146 −14.011 23.192 36.426 1.00 44.09 C ANISOU 859 CD GLU A 146 5419 5271 6062 −276 806 −1099 C ATOM 860 OE1 GLU A 146 −13.718 22.203 35.738 1.00 38.29 O ANISOU 860 OE1 GLU A 146 4648 4689 5212 −270 741 −954 O ATOM 861 OE2 GLU A 146 −13.404 23.480 37.506 1.00 35.48 O ANISOU 861 OE2 GLU A 146 4331 4190 4959 −377 788 −1326 O ATOM 862 O ARG A 147 −17.523 24.215 39.276 1.00 46.46 O ANISOU 862 O ARG A 147 5768 5400 6486 −29 1145 −1593 O ATOM 863 N ARG A 147 −17.589 21.856 37.962 1.00 43.22 N ANISOU 863 N ARG A 147 5237 5346 5838 23 953 −1230 N ATOM 864 CA ARG A 147 −18.543 22.093 39.030 1.00 40.73 C ANISOU 864 CA ARG A 147 4929 4980 5565 51 1138 −1426 C ATOM 865 C ARG A 147 −18.561 23.575 39.319 1.00 45.72 C ANISOU 865 C ARG A 147 5598 5376 6399 61 1215 −1572 C ATOM 866 CB ARG A 147 −18.188 21.304 40.289 1.00 39.75 C ANISOU 866 CB ARG A 147 4961 5017 5124 −51 1203 −1547 C ATOM 867 CG ARG A 147 −19.242 21.450 41.419 1.00 53.91 C ANISOU 867 CG ARG A 147 6821 6751 6912 −41 1484 −1753 C ATOM 868 CD ARG A 147 −18.911 20.580 42.645 1.00 55.20 C ANISOU 868 CD ARG A 147 7249 7055 6670 −133 1556 −1833 C ATOM 869 NE ARG A 147 −18.748 19.158 42.308 1.00 55.18 N ANISOU 869 NE ARG A 147 7248 7220 6499 −143 1464 −1643 N ATOM 870 CZ ARG A 147 −19.726 18.247 42.335 1.00 53.32 C ANISOU 870 CZ ARG A 147 6961 7013 6285 −132 1657 −1595 C ATOM 871 NH1 ARG A 147 −20.956 18.606 42.660 1.00 58.92 N ANISOU 871 NH1 ARG A 147 7576 7604 7208 −110 1962 −1734 N ATOM 872 NH2 ARG A 147 −19.483 16.976 42.010 1.00 45.09 N ANISOU 872 NH2 ARG A 147 5932 6097 5102 −148 1559 −1428 N ATOM 873 O ARG A 148 −18.922 25.010 42.085 1.00 64.66 O ANISOU 873 O ARG A 148 8258 7587 8722 −40 1601 −2179 O ATOM 874 N ARG A 148 −19.729 24.139 39.611 1.00 49.33 N ANISOU 874 N ARG A 148 5976 5683 7083 164 1374 −1698 N ATOM 875 CA ARG A 148 −19.797 25.572 39.908 1.00 59.43 C ANISOU 875 CA ARG A 148 7292 6703 8586 188 1458 −1856 C ATOM 876 C ARG A 148 −19.120 25.893 41.249 1.00 66.19 C ANISOU 876 C ARG A 148 8334 7582 9233 40 1562 −2110 C ATOM 877 CB ARG A 148 −21.254 26.062 39.925 1.00 61.22 C ANISOU 877 CB ARG A 148 7352 6751 9156 359 1602 −1966 C ATOM 878 O ALA A 149 −19.341 27.591 44.936 1.00 90.72 O ANISOU 878 O ALA A 149 11937 10471 12064 −125 2082 −3022 O ATOM 879 N ALA A 149 −18.741 27.151 41.441 1.00 73.74 N ANISOU 879 N ALA A 149 9350 8315 10355 10 1584 −2250 N ATOM 880 CA ALA A 149 −18.303 27.606 42.757 1.00 81.09 C ANISOU 880 CA ALA A 149 10459 9228 11124 −104 1675 −2557 C ATOM 881 C ALA A 149 −19.497 27.637 43.712 1.00 86.57 C ANISOU 881 C ALA A 149 11190 9887 11817 −40 1966 −2779 C ATOM 882 CB ALA A 149 −17.646 28.978 42.661 1.00 84.53 C ANISOU 882 CB ALA A 149 10924 9396 11799 −162 1641 −2676 C TER ATOM 883 O LEU B 20 −1.649 −5.434 33.856 1.00 58.08 O ANISOU 883 O LEU B 20 7988 9726 4354 1942 402 750 O ATOM 884 N LEU B 20 −3.012 −5.202 36.329 1.00 62.51 N ANISOU 884 N LEU B 20 9807 9782 4160 2346 1138 760 N ATOM 885 CA LEU B 20 −3.676 −5.607 35.106 1.00 58.15 C ANISOU 885 CA LEU B 20 8804 8611 4682 2971 1236 992 C ATOM 886 C LEU B 20 −2.682 −6.066 34.062 1.00 56.80 C ANISOU 886 C LEU B 20 7765 9094 4723 2746 714 1049 C ATOM 887 CB LEU B 20 −4.487 −4.469 34.521 1.00 62.55 C ANISOU 887 CB LEU B 20 10141 8069 5557 2835 1708 751 C ATOM 888 CG LEU B 20 −5.846 −4.191 35.138 1.00 71.78 C ANISOU 888 CG LEU B 20 12027 8200 7048 3362 2409 907 C ATOM 889 CD1 LEU B 20 −6.577 −3.220 34.232 1.00 73.47 C ANISOU 889 CD1 LEU B 20 12506 7590 7818 3013 2649 929 C ATOM 890 CD2 LEU B 20 −6.627 −5.482 35.330 1.00 70.22 C ANISOU 890 CD2 LEU B 20 10977 8255 7449 3520 2121 1346 C ATOM 891 N PHE B 21 −3.008 −7.160 33.393 1.00 52.83 N ANISOU 891 N PHE B 21 6487 8553 5033 3417 684 1415 N ATOM 892 CA PHE B 21 −2.252 −7.576 32.236 1.00 49.20 C ANISOU 892 CA PHE B 21 5469 8298 4926 2899 406 1312 C ATOM 893 C PHE B 21 −2.431 −6.524 31.140 1.00 45.14 C ANISOU 893 C PHE B 21 5281 7328 4542 2877 401 1134 C ATOM 894 O PHE B 21 −3.572 −6.224 30.766 1.00 41.12 O ANISOU 894 O PHE B 21 5200 5942 4480 2791 684 1034 O ATOM 895 CB PHE B 21 −2.720 −8.955 31.778 1.00 45.59 C ANISOU 895 CB PHE B 21 4890 7268 5164 2397 452 1215 C ATOM 896 CG PHE B 21 −2.020 −9.444 30.541 1.00 44.10 C ANISOU 896 CG PHE B 21 4442 7169 5145 2128 355 1205 C ATOM 897 CD1 PHE B 21 −0.744 −9.943 30.619 1.00 47.89 C ANISOU 897 CD1 PHE B 21 4549 8169 5478 1984 244 1336 C ATOM 898 CD2 PHE B 21 −2.637 −9.366 29.306 1.00 47.32 C ANISOU 898 CD2 PHE B 21 4991 7151 5836 2001 390 1102 C ATOM 899 CE1 PHE B 21 −0.084 −10.378 29.501 1.00 50.70 C ANISOU 899 CE1 PHE B 21 4757 8513 5995 1768 221 1360 C ATOM 900 CE2 PHE B 21 −1.982 −9.802 28.164 1.00 45.35 C ANISOU 900 CE2 PHE B 21 4563 6948 5722 1794 315 1081 C ATOM 901 CZ PHE B 21 −0.700 −10.310 28.263 1.00 46.66 C ANISOU 901 CZ PHE B 21 4431 7530 5766 1695 253 1205 C ATOM 902 N THR B 22 −1.327 −5.933 30.650 1.00 45.73 N ANISOU 902 N THR B 22 5337 7801 4237 2149 103 874 N ATOM 903 CA THR B 22 −1.426 −4.916 29.583 1.00 42.62 C ANISOU 903 CA THR B 22 5349 6854 3992 1799 187 587 C ATOM 904 C THR B 22 −0.482 −5.153 28.398 1.00 41.92 C ANISOU 904 C THR B 22 4707 7116 4103 1531 −132 581 C ATOM 905 O THR B 22 0.589 −5.754 28.538 1.00 39.02 O ANISOU 905 O THR B 22 3771 7487 3567 1326 −435 709 O ATOM 906 CB THR B 22 −1.122 −3.507 30.104 1.00 47.30 C ANISOU 906 CB THR B 22 6763 7288 3921 1074 338 142 C ATOM 907 OG1 THR B 22 0.190 −3.506 30.667 1.00 50.41 O ANISOU 907 OG1 THR B 22 6942 8564 3648 444 −62 0 O ATOM 908 CG2 THR B 22 −2.154 −3.066 31.181 1.00 49.21 C ANISOU 908 CG2 THR B 22 7764 6949 3984 1273 836 100 C ATOM 909 N VAL B 23 −0.885 −4.639 27.248 1.00 35.34 N ANISOU 909 N VAL B 23 4057 5738 3634 1526 −19 490 N ATOM 910 CA VAL B 23 −0.111 −4.746 26.005 1.00 33.17 C ANISOU 910 CA VAL B 23 3403 5644 3557 1286 −233 458 C ATOM 911 C VAL B 23 0.206 −3.352 25.560 1.00 35.04 C ANISOU 911 C VAL B 23 4186 5587 3543 737 −146 120 C ATOM 912 O VAL B 23 −0.678 −2.487 25.619 1.00 35.02 O ANISOU 912 O VAL B 23 4758 4964 3583 793 202 41 O ATOM 913 CB VAL B 23 −0.906 −5.507 24.908 1.00 42.34 C ANISOU 913 CB VAL B 23 4319 6393 5376 1655 −158 633 C ATOM 914 CG1 VAL B 23 −0.344 −5.249 23.495 1.00 38.71 C ANISOU 914 CG1 VAL B 23 3720 5942 5047 1427 −273 557 C ATOM 915 CG2 VAL B 23 −0.913 −7.010 25.247 1.00 38.47 C ANISOU 915 CG2 VAL B 23 3718 5765 5135 1412 −155 591 C ATOM 916 N THR B 24 1.462 −3.101 25.174 1.00 35.92 N ANISOU 916 N THR B 24 4108 6094 3445 219 −382 −36 N ATOM 917 CA THR B 24 1.863 −1.787 24.655 1.00 38.14 C ANISOU 917 CA THR B 24 4840 6085 3568 −291 −254 −370 C ATOM 918 C THR B 24 2.542 −1.884 23.277 1.00 40.73 C ANISOU 918 C THR B 24 4833 6443 4201 −378 −389 −329 C ATOM 919 O THR B 24 3.043 −2.944 22.917 1.00 43.51 O ANISOU 919 O THR B 24 4608 7161 4762 −229 −607 −95 O ATOM 920 CB THR B 24 2.827 −1.091 25.595 1.00 46.28 C ANISOU 920 CB THR B 24 6103 7498 3985 −979 −360 −693 C ATOM 921 OG1 THR B 24 3.982 −1.911 25.769 1.00 46.89 O ANISOU 921 OG1 THR B 24 5526 8343 3949 −1168 −801 −505 O ATOM 922 CG2 THR B 24 2.174 −0.857 26.957 1.00 47.29 C ANISOU 922 CG2 THR B 24 6720 7552 3697 −995 −155 −807 C ATOM 923 N VAL B 25 2.549 −0.793 22.514 1.00 38.94 N ANISOU 923 N VAL B 25 4973 5795 4028 −599 −173 −525 N ATOM 924 CA VAL B 25 3.189 −0.797 21.197 1.00 40.66 C ANISOU 924 CA VAL B 25 4953 5998 4498 −675 −254 −492 C ATOM 925 C VAL B 25 4.116 0.374 21.098 1.00 49.10 C ANISOU 925 C VAL B 25 6279 7003 5372 −1232 −160 −817 C ATOM 926 O VAL B 25 3.672 1.509 20.933 1.00 53.14 O ANISOU 926 O VAL B 25 7264 7039 5889 −1327 220 −994 O ATOM 927 CB VAL B 25 2.183 −0.710 20.021 1.00 54.36 C ANISOU 927 CB VAL B 25 6786 7270 6597 −287 −66 −305 C ATOM 928 CG1 VAL B 25 2.906 −0.596 18.712 1.00 59.16 C ANISOU 928 CG1 VAL B 25 7254 7870 7356 −425 −110 −312 C ATOM 929 CG2 VAL B 25 1.237 −1.924 20.019 1.00 51.02 C ANISOU 929 CG2 VAL B 25 6067 6894 6423 228 −170 −4 C ATOM 930 N PRO B 26 5.421 0.113 21.192 1.00 53.75 N ANISOU 930 N PRO B 26 6517 8048 5857 −1601 −448 −851 N ATOM 931 CA PRO B 26 6.367 1.232 21.186 1.00 57.08 C ANISOU 931 CA PRO B 26 7149 8423 6116 −2184 −379 −1185 C ATOM 932 C PRO B 26 6.514 1.805 19.778 1.00 52.07 C ANISOU 932 C PRO B 26 6595 7343 5848 −2093 −141 −1199 C ATOM 933 O PRO B 26 6.907 2.947 19.616 1.00 54.90 O ANISOU 933 O PRO B 26 7244 7429 6186 −2431 115 −1491 O ATOM 934 CB PRO B 26 7.667 0.604 21.707 1.00 62.67 C ANISOU 934 CB PRO B 26 7328 9804 6678 −2553 −816 −1057 C ATOM 935 CG PRO B 26 7.572 −0.819 21.361 1.00 61.18 C ANISOU 935 CG PRO B 26 6596 9851 6797 −2078 −975 −596 C ATOM 936 CD PRO B 26 6.089 −1.191 21.326 1.00 56.87 C ANISOU 936 CD PRO B 26 6271 8989 6349 −1508 −781 −528 C ATOM 937 N LYS B 27 6.116 1.044 18.770 1.00 48.04 N ANISOU 937 N LYS B 27 5864 6737 5653 −1640 −169 −897 N ATOM 938 CA LYS B 27 6.121 1.574 17.418 1.00 47.65 C ANISOU 938 CA LYS B 27 5936 6300 5870 −1525 61 −871 C ATOM 939 C LYS B 27 4.809 1.202 16.758 1.00 43.30 C ANISOU 939 C LYS B 27 5455 5533 5462 −1033 155 −615 C ATOM 940 O LYS B 27 4.538 0.025 16.564 1.00 43.91 O ANISOU 940 O LYS B 27 5241 5816 5625 −784 −54 −405 O ATOM 941 CB LYS B 27 7.325 1.029 16.652 1.00 50.64 C ANISOU 941 CB LYS B 27 5951 6835 6454 −1637 −97 −757 C ATOM 942 CG LYS B 27 7.419 1.471 15.203 1.00 53.14 C ANISOU 942 CG LYS B 27 6406 6777 7009 −1504 141 −711 C ATOM 943 CD LYS B 27 8.634 0.840 14.533 1.00 55.35 C ANISOU 943 CD LYS B 27 6369 7136 7526 −1609 60 −568 C ATOM 944 CE LYS B 27 8.934 1.499 13.201 1.00 58.42 C ANISOU 944 CE LYS B 27 6965 7121 8110 −1542 342 −576 C ATOM 945 NZ LYS B 27 9.728 0.608 12.336 1.00 59.37 N ANISOU 945 NZ LYS B 27 6870 7211 8476 −1508 360 −358 N ATOM 946 N GLU B 28 3.974 2.184 16.430 1.00 40.82 N ANISOU 946 N GLU B 28 5487 4813 5209 −909 504 −590 N ATOM 947 CA GLU B 28 2.655 1.841 15.917 1.00 44.01 C ANISOU 947 CA GLU B 28 5894 5079 5749 −480 535 −249 C ATOM 948 C GLU B 28 2.562 1.849 14.390 1.00 44.43 C ANISOU 948 C GLU B 28 5880 5066 5936 −338 548 −30 C ATOM 949 O GLU B 28 1.615 1.293 13.833 1.00 45.11 O ANISOU 949 O GLU B 28 5867 5193 6081 −68 428 267 O ATOM 950 CB GLU B 28 1.585 2.760 16.502 1.00 51.11 C ANISOU 950 CB GLU B 28 7137 5585 6696 −364 941 −155 C ATOM 951 CG GLU B 28 1.802 4.241 16.332 1.00 60.68 C ANISOU 951 CG GLU B 28 8673 6401 7982 −569 1478 −281 C ATOM 952 CD GLU B 28 0.794 5.079 17.152 1.00 65.46 C ANISOU 952 CD GLU B 28 9655 6542 8676 −503 2034 −191 C ATOM 953 OE1 GLU B 28 −0.050 4.488 17.874 1.00 56.50 O ANISOU 953 OE1 GLU B 28 8540 5398 7530 −281 1942 −26 O ATOM 954 OE2 GLU B 28 0.852 6.332 17.068 1.00 74.70 O ANISOU 954 OE2 GLU B 28 11104 7297 9982 −661 2649 −268 O ATOM 955 N LEU B 29 3.545 2.447 13.721 1.00 40.79 N ANISOU 955 N LEU B 29 5469 4524 5507 −541 680 −170 N ATOM 956 CA LEU B 29 3.527 2.546 12.267 1.00 39.31 C ANISOU 956 CA LEU B 29 5277 4273 5386 −420 738 34 C ATOM 957 C LEU B 29 4.800 1.981 11.631 1.00 38.09 C ANISOU 957 C LEU B 29 4989 4230 5254 −597 609 −105 C ATOM 958 O LEU B 29 5.900 2.392 11.950 1.00 37.80 O ANISOU 958 O LEU B 29 4942 4128 5293 −841 690 −327 O ATOM 959 CB LEU B 29 3.346 3.999 11.835 1.00 44.93 C ANISOU 959 CB LEU B 29 6213 4638 6222 −380 1213 125 C ATOM 960 CG LEU B 29 3.402 4.281 10.336 1.00 47.96 C ANISOU 960 CG LEU B 29 6598 4986 6640 −245 1322 377 C ATOM 961 CD1 LEU B 29 2.344 3.481 9.572 1.00 46.93 C ANISOU 961 CD1 LEU B 29 6352 5112 6365 −38 1026 764 C ATOM 962 CD2 LEU B 29 3.175 5.756 10.142 1.00 53.43 C ANISOU 962 CD2 LEU B 29 7440 5327 7536 −155 1903 524 C ATOM 963 N TYR B 30 4.617 1.027 10.726 1.00 33.10 N ANISOU 963 N TYR B 30 4264 3738 4576 −502 446 46 N ATOM 964 CA TYR B 30 5.703 0.406 10.010 1.00 35.59 C ANISOU 964 CA TYR B 30 4508 4057 4957 −645 452 −17 C ATOM 965 C TYR B 30 5.574 0.797 8.541 1.00 39.60 C ANISOU 965 C TYR B 30 5235 4430 5381 −573 612 125 C ATOM 966 O TYR B 30 4.509 0.663 7.931 1.00 38.67 O ANISOU 966 O TYR B 30 5181 4438 5073 −445 519 331 O ATOM 967 CB TYR B 30 5.648 −1.106 10.169 1.00 32.27 C ANISOU 967 CB TYR B 30 3850 3864 4547 −653 272 10 C ATOM 968 CG TYR B 30 5.931 −1.620 11.574 1.00 34.35 C ANISOU 968 CG TYR B 30 3821 4331 4899 −698 133 −47 C ATOM 969 CD1 TYR B 30 7.171 −2.148 11.892 1.00 35.46 C ANISOU 969 CD1 TYR B 30 3693 4550 5229 −883 164 −35 C ATOM 970 CD2 TYR B 30 4.953 −1.572 12.573 1.00 37.16 C ANISOU 970 CD2 TYR B 30 4152 4806 5163 −546 −4 −35 C ATOM 971 CE1 TYR B 30 7.450 −2.613 13.160 1.00 40.40 C ANISOU 971 CE1 TYR B 30 3990 5466 5892 −936 13 6 C ATOM 972 CE2 TYR B 30 5.208 −2.046 13.861 1.00 35.61 C ANISOU 972 CE2 TYR B 30 3706 4844 4981 −580 −129 −64 C ATOM 973 CZ TYR B 30 6.450 −2.574 14.151 1.00 38.84 C ANISOU 973 CZ TYR B 30 3807 5431 5519 −781 −147 −33 C ATOM 974 OH TYR B 30 6.709 −3.064 15.417 1.00 37.39 O ANISOU 974 OH TYR B 30 3310 5586 5310 −820 −296 32 O ATOM 975 N ILE B 31 6.653 1.290 7.973 1.00 38.79 N ANISOU 975 N ILE B 31 5228 4095 5417 −660 843 54 N ATOM 976 CA ILE B 31 6.641 1.686 6.582 1.00 38.51 C ANISOU 976 CA ILE B 31 5420 3930 5283 −572 1037 201 C ATOM 977 C ILE B 31 7.670 0.824 5.868 1.00 43.88 C ANISOU 977 C ILE B 31 6155 4480 6037 −718 1141 139 C ATOM 978 O ILE B 31 8.849 0.939 6.117 1.00 46.53 O ANISOU 978 O ILE B 31 6412 4584 6683 −819 1298 50 O ATOM 979 CB ILE B 31 6.948 3.171 6.442 1.00 43.79 C ANISOU 979 CB ILE B 31 6191 4319 6127 −471 1377 219 C ATOM 980 CG1 ILE B 31 5.761 3.992 6.965 1.00 47.95 C ANISOU 980 CG1 ILE B 31 6704 4902 6612 −311 1439 382 C ATOM 981 CG2 ILE B 31 7.230 3.528 5.005 1.00 44.84 C ANISOU 981 CG2 ILE B 31 6529 4303 6205 −354 1627 386 C ATOM 982 CD1 ILE B 31 6.084 5.446 7.279 1.00 51.11 C ANISOU 982 CD1 ILE B 31 7166 4964 7288 −275 1906 310 C ATOM 983 N ILE B 32 7.220 −0.089 5.020 1.00 42.96 N ANISOU 983 N ILE B 32 6170 4495 5659 −773 1086 201 N ATOM 984 CA ILE B 32 8.123 −1.097 4.462 1.00 43.12 C ANISOU 984 CA ILE B 32 6274 4325 5785 −954 1307 135 C ATOM 985 C ILE B 32 8.120 −1.054 2.932 1.00 45.07 C ANISOU 985 C ILE B 32 6939 4453 5734 −1000 1523 193 C ATOM 986 O ILE B 32 7.065 −0.878 2.312 1.00 46.79 O ANISOU 986 O ILE B 32 7302 4963 5514 −980 1335 297 O ATOM 987 CB ILE B 32 7.717 −2.501 4.951 1.00 41.14 C ANISOU 987 CB ILE B 32 5827 4288 5515 −1080 1183 72 C ATOM 988 CG1 ILE B 32 7.667 −2.509 6.493 1.00 43.57 C ANISOU 988 CG1 ILE B 32 5728 4772 6053 −1001 956 58 C ATOM 989 CG2 ILE B 32 8.670 −3.556 4.425 1.00 42.51 C ANISOU 989 CG2 ILE B 32 6073 4181 5900 −1278 1587 50 C ATOM 990 CD1 ILE B 32 8.978 −2.111 7.138 1.00 47.81 C ANISOU 990 CD1 ILE B 32 6066 5123 6975 −1063 1081 74 C ATOM 991 O GLU B 33 8.893 −3.626 0.909 1.00 51.23 O ANISOU 991 O GLU B 33 8407 4825 6234 −1618 2264 −19 O ATOM 992 N GLU B 33 9.292 −1.206 2.329 1.00 47.25 N ANISOU 992 N GLU B 33 7398 4311 6243 −1071 1922 181 N ATOM 993 CA GLU B 33 9.390 −1.266 0.878 1.00 51.43 C ANISOU 993 CA GLU B 33 8403 4680 6459 −1144 2198 214 C ATOM 994 C GLU B 33 8.730 −2.523 0.355 1.00 48.95 C ANISOU 994 C GLU B 33 8293 4581 5724 −1451 2169 92 C ATOM 995 CB GLU B 33 10.842 −1.217 0.416 1.00 59.64 C ANISOU 995 CB GLU B 33 9507 5260 7894 −1047 2594 200 C ATOM 996 CG GLU B 33 11.622 −0.080 0.998 1.00 64.78 C ANISOU 996 CG GLU B 33 9851 5788 8976 −786 2570 246 C ATOM 997 CD GLU B 33 12.555 0.549 0.001 1.00 77.49 C ANISOU 997 CD GLU B 33 11587 7179 10676 −562 2848 268 C ATOM 998 OE1 GLU B 33 12.894 −0.122 −1.006 1.00 81.94 O ANISOU 998 OE1 GLU B 33 12412 7654 11067 −592 3069 227 O ATOM 999 OE2 GLU B 33 12.942 1.724 0.223 1.00 82.24 O ANISOU 999 OE2 GLU B 33 12025 7703 11520 −371 2889 301 O ATOM 1000 O HIS B 34 9.374 −4.436 −2.071 1.00 42.45 O ANISOU 1000 O HIS B 34 4652 7423 4053 −463 507 −501 O ATOM 1001 N HIS B 34 7.929 −2.334 −0.676 1.00 44.67 N ANISOU 1001 N HIS B 34 4623 8075 4274 780 −88 192 N ATOM 1002 CA HIS B 34 7.298 −3.433 −1.384 1.00 48.78 C ANISOU 1002 CA HIS B 34 4864 9335 4335 137 25 −163 C ATOM 1003 C HIS B 34 8.246 −4.623 −1.634 1.00 46.34 C ANISOU 1003 C HIS B 34 4848 8489 4270 −488 387 −595 C ATOM 1004 CB HIS B 34 6.763 −2.935 −2.722 1.00 56.08 C ANISOU 1004 CB HIS B 34 5459 11213 4636 123 −114 92 C ATOM 1005 CG HIS B 34 5.878 −3.927 −3.392 1.00 62.90 C ANISOU 1005 CG HIS B 34 5962 13061 4875 −595 −58 −263 C ATOM 1006 ND1 HIS B 34 6.324 −4.763 −4.393 1.00 71.37 N ANISOU 1006 ND1 HIS B 34 7164 14274 5678 −1324 195 −654 N ATOM 1007 CD2 HIS B 34 4.589 −4.264 −3.159 1.00 65.10 C ANISOU 1007 CD2 HIS B 34 5777 14207 4749 −770 −177 −330 C ATOM 1008 CE1 HIS B 34 5.331 −5.549 −4.777 1.00 78.01 C ANISOU 1008 CE1 HIS B 34 7651 16034 5954 −1968 221 −976 C ATOM 1009 NE2 HIS B 34 4.271 −5.272 −4.038 1.00 75.05 N ANISOU 1009 NE2 HIS B 34 6884 16089 5542 −1636 −19 −762 N ATOM 1010 N GLY B 35 7.778 −5.843 −1.370 1.00 46.16 N ANISOU 1010 N GLY B 35 4738 8627 4175 −1038 626 −1040 N ATOM 1011 CA GLY B 35 8.616 −7.019 −1.521 1.00 47.19 C ANISOU 1011 CA GLY B 35 5155 8160 4617 −1588 1113 −1416 C ATOM 1012 C GLY B 35 9.688 −7.266 −0.438 1.00 41.02 C ANISOU 1012 C GLY B 35 4676 6302 4608 −1363 1285 −1304 C ATOM 1013 O GLY B 35 10.420 −8.245 −0.528 1.00 44.43 O ANISOU 1013 O GLY B 35 5308 6190 5382 −1739 1764 −1503 O ATOM 1014 N ASER B 36 9.775 −6.418 0.582 0.24 37.94 N ANISOU 1014 N ASER B 36 4308 5630 4477 −791 948 −970 N ATOM 1015 CA ASER B 36 10.718 −6.697 1.668 0.24 36.07 C ANISOU 1015 CA ASER B 36 4282 4558 4867 −669 1060 −836 C ATOM 1016 C ASER B 36 10.004 −7.122 2.951 0.24 35.38 C ANISOU 1016 C ASER B 36 4068 4524 4852 −627 1018 −928 C ATOM 1017 O ASER B 36 8.863 −6.733 3.201 0.24 34.94 O ANISOU 1017 O ASER B 36 3804 5040 4432 −465 778 −975 O ATOM 1018 CB ASER B 36 11.613 −5.488 1.941 0.24 36.35 C ANISOU 1018 CB ASER B 36 4513 4132 5166 −189 767 −419 C ATOM 1019 OG ASER B 36 10.858 −4.361 2.329 0.24 37.10 O ANISOU 1019 OG ASER B 36 4540 4548 5009 255 394 −261 O ATOM 1020 N BSER B 36 9.786 −6.394 0.564 0.76 37.11 N ANISOU 1020 N BSER B 36 4205 5526 4370 −784 943 −963 N ATOM 1021 CA BSER B 36 10.704 −6.653 1.676 0.76 36.59 C ANISOU 1021 CA BSER B 36 4346 4632 4925 −652 1044 −827 C ATOM 1022 C BSER B 36 9.953 −7.316 2.830 0.76 36.23 C ANISOU 1022 C BSER B 36 4160 4670 4935 −717 1084 −989 C ATOM 1023 O BSER B 36 8.724 −7.301 2.850 0.76 35.46 O ANISOU 1023 O BSER B 36 3817 5235 4422 −745 954 −1152 O ATOM 1024 CB BSER B 36 11.383 −5.364 2.150 0.76 36.69 C ANISOU 1024 CB BSER B 36 4526 4252 5163 −119 695 −414 C ATOM 1025 OG BSER B 36 12.329 −4.899 1.186 0.76 39.16 O ANISOU 1025 OG BSER B 36 5002 4309 5570 −86 739 −235 O ATOM 1026 N ASP B 37 10.698 −7.923 3.754 1.00 36.58 N ANISOU 1026 N ASP B 37 4318 4092 5487 −747 1282 −890 N ATOM 1027 CA ASP B 37 10.130 −8.523 4.984 1.00 37.16 C ANISOU 1027 CA ASP B 37 4280 4172 5669 −761 1328 −962 C ATOM 1028 C ASP B 37 9.856 −7.496 6.085 1.00 35.60 C ANISOU 1028 C ASP B 37 4103 4009 5414 −299 877 −735 C ATOM 1029 O ASP B 37 10.470 −6.457 6.119 1.00 36.66 O ANISOU 1029 O ASP B 37 4403 3919 5608 −4 611 −480 O ATOM 1030 CB ASP B 37 11.083 −9.583 5.575 1.00 38.44 C ANISOU 1030 CB ASP B 37 4514 3691 6402 −937 1751 −826 C ATOM 1031 CG ASP B 37 11.277 −10.783 4.673 1.00 43.73 C ANISOU 1031 CG ASP B 37 5311 4367 6939 −1103 2102 −1054 C ATOM 1032 OD1 ASP B 37 10.839 −10.752 3.517 1.00 44.18 O ANISOU 1032 OD1 ASP B 37 5386 4702 6697 −1423 2215 −1364 O ATOM 1033 OD2 ASP B 37 11.841 −11.788 5.126 1.00 44.73 O ANISOU 1033 OD2 ASP B 37 5497 4257 7241 −937 2273 −951 O ATOM 1034 N VAL B 38 8.970 −7.814 7.024 1.00 35.97 N ANISOU 1034 N VAL B 38 4016 4286 5364 −273 854 −848 N ATOM 1035 CA VAL B 38 8.783 −6.937 8.176 1.00 33.62 C ANISOU 1035 CA VAL B 38 3808 3936 5033 106 532 −670 C ATOM 1036 C VAL B 38 8.447 −7.770 9.404 1.00 34.40 C ANISOU 1036 C VAL B 38 3822 3988 5259 4 666 −717 C ATOM 1037 O VAL B 38 7.878 −8.855 9.295 1.00 34.50 O ANISOU 1037 O VAL B 38 3648 4186 5275 −284 971 −943 O ATOM 1038 CB VAL B 38 7.692 −5.892 7.944 1.00 33.86 C ANISOU 1038 CB VAL B 38 3754 4465 4644 444 285 −697 C ATOM 1039 CG1 VAL B 38 6.288 −6.541 7.830 1.00 36.65 C ANISOU 1039 CG1 VAL B 38 3763 5477 4684 297 391 −950 C ATOM 1040 CG2 VAL B 38 7.674 −4.885 9.085 1.00 37.72 C ANISOU 1040 CG2 VAL B 38 4457 4732 5143 817 73 −536 C ATOM 1041 N THR B 39 8.856 −7.279 10.564 1.00 37.67 N ANISOU 1041 N THR B 39 4392 4152 5770 189 471 −504 N ATOM 1042 CA THR B 39 8.531 −7.921 11.831 1.00 36.24 C ANISOU 1042 CA THR B 39 4139 3981 5649 135 553 −488 C ATOM 1043 C THR B 39 7.718 −6.941 12.674 1.00 34.97 C ANISOU 1043 C THR B 39 4090 4029 5168 437 300 −542 C ATOM 1044 O THR B 39 8.221 −5.906 13.110 1.00 38.33 O ANISOU 1044 O THR B 39 4781 4243 5538 597 71 −409 O ATOM 1045 CB THR B 39 9.795 −8.354 12.590 1.00 43.86 C ANISOU 1045 CB THR B 39 5159 4530 6978 9 595 −129 C ATOM 1046 OG1 THR B 39 10.460 −9.401 11.863 1.00 42.54 O ANISOU 1046 OG1 THR B 39 4869 4111 7184 −230 984 −42 O ATOM 1047 CG2 THR B 39 9.413 −8.872 13.954 1.00 47.38 C ANISOU 1047 CG2 THR B 39 5524 5071 7406 −11 636 −55 C ATOM 1048 N LEU B 40 6.435 −7.223 12.841 1.00 30.76 N ANISOU 1048 N LEU B 40 3364 3903 4419 494 392 −753 N ATOM 1049 CA LEU B 40 5.551 −6.330 13.601 1.00 32.50 C ANISOU 1049 CA LEU B 40 3676 4308 4365 823 262 −790 C ATOM 1050 C LEU B 40 5.532 −6.811 15.075 1.00 37.02 C ANISOU 1050 C LEU B 40 4311 4781 4973 743 313 −755 C ATOM 1051 O LEU B 40 5.585 −8.017 15.341 1.00 37.31 O ANISOU 1051 O LEU B 40 4157 4829 5192 491 514 −751 O ATOM 1052 CB LEU B 40 4.139 −6.329 13.019 1.00 36.32 C ANISOU 1052 CB LEU B 40 3850 5363 4588 960 332 −947 C ATOM 1053 CG LEU B 40 4.041 −6.109 11.490 1.00 45.78 C ANISOU 1053 CG LEU B 40 4870 6857 5668 941 294 −955 C ATOM 1054 CD1 LEU B 40 2.646 −6.421 10.967 1.00 48.96 C ANISOU 1054 CD1 LEU B 40 4836 7996 5770 915 358 −1076 C ATOM 1055 CD2 LEU B 40 4.397 −4.681 11.142 1.00 47.82 C ANISOU 1055 CD2 LEU B 40 5366 6934 5870 1330 119 −745 C ATOM 1056 N GLU B 41 5.446 −5.880 16.017 1.00 34.50 N ANISOU 1056 N GLU B 41 4277 4359 4474 938 190 −728 N ATOM 1057 CA GLU B 41 5.673 −6.243 17.410 1.00 36.14 C ANISOU 1057 CA GLU B 41 4590 4488 4653 793 193 −654 C ATOM 1058 C GLU B 41 4.801 −5.494 18.382 1.00 35.37 C ANISOU 1058 C GLU B 41 4708 4481 4250 1017 225 −788 C ATOM 1059 O GLU B 41 4.434 −4.331 18.165 1.00 35.79 O ANISOU 1059 O GLU B 41 4988 4460 4152 1301 225 −869 O ATOM 1060 CB GLU B 41 7.139 −6.005 17.773 1.00 41.04 C ANISOU 1060 CB GLU B 41 5426 4789 5379 563 0 −408 C ATOM 1061 CG GLU B 41 8.104 −6.958 17.074 1.00 49.77 C ANISOU 1061 CG GLU B 41 6292 5756 6863 340 67 −177 C ATOM 1062 CD GLU B 41 9.578 −6.630 17.356 1.00 57.67 C ANISOU 1062 CD GLU B 41 7427 6508 7977 137 −147 157 C ATOM 1063 OE1 GLU B 41 9.882 −5.449 17.648 1.00 58.68 O ANISOU 1063 OE1 GLU B 41 7885 6534 7876 145 −375 107 O ATOM 1064 OE2 GLU B 41 10.424 −7.551 17.289 1.00 61.84 O ANISOU 1064 OE2 GLU B 41 7721 6940 8834 −43 −41 490 O ATOM 1065 N CYS B 42 4.458 −6.166 19.469 1.00 31.20 N ANISOU 1065 N CYS B 42 4119 4085 3653 909 321 −784 N ATOM 1066 CA CYS B 42 3.902 −5.459 20.588 1.00 33.63 C ANISOU 1066 CA CYS B 42 4725 4400 3653 1037 373 −897 C ATOM 1067 C CYS B 42 4.404 −6.176 21.834 1.00 34.18 C ANISOU 1067 C CYS B 42 4815 4520 3653 725 339 −747 C ATOM 1068 O CYS B 42 4.823 −7.349 21.766 1.00 35.93 O ANISOU 1068 O CYS B 42 4713 4812 4127 531 371 −536 O ATOM 1069 CB CYS B 42 2.349 −5.381 20.534 1.00 47.34 C ANISOU 1069 CB CYS B 42 6285 6418 5283 1388 612 −1061 C ATOM 1070 SG CYS B 42 1.472 −6.981 20.617 1.00 54.11 S ANISOU 1070 SG CYS B 42 6605 7676 6276 1269 806 −1080 S ATOM 1071 N ASN B 43 4.430 −5.438 22.940 1.00 36.79 N ANISOU 1071 N ASN B 43 5539 4802 3638 656 315 −828 N ATOM 1072 CA ASN B 43 5.008 −5.917 24.168 1.00 38.29 C ANISOU 1072 CA ASN B 43 5777 5131 3642 310 222 −640 C ATOM 1073 C ASN B 43 3.931 −6.211 25.187 1.00 44.90 C ANISOU 1073 C ASN B 43 6626 6187 4245 411 453 −764 C ATOM 1074 O ASN B 43 2.837 −5.661 25.112 1.00 41.32 O ANISOU 1074 O ASN B 43 6294 5706 3700 736 677 −1032 O ATOM 1075 CB ASN B 43 5.969 −4.877 24.742 1.00 48.08 C ANISOU 1075 CB ASN B 43 7481 6232 4553 −12 3 −660 C ATOM 1076 CG ASN B 43 7.024 −4.462 23.739 1.00 50.32 C ANISOU 1076 CG ASN B 43 7775 6275 5068 −102 −212 −541 C ATOM 1077 OD1 ASN B 43 7.325 −3.290 23.587 1.00 57.91 O ANISOU 1077 OD1 ASN B 43 9149 6978 5877 −149 −254 −733 O ATOM 1078 ND2 ASN B 43 7.574 −5.423 23.044 1.00 44.09 N ANISOU 1078 ND2 ASN B 43 6554 5525 4673 −124 −277 −232 N ATOM 1079 O PHE B 44 5.112 −7.564 28.721 1.00 52.80 O ANISOU 1079 O PHE B 44 7615 7986 4459 −503 239 −56 O ATOM 1080 N PHE B 44 4.234 −7.060 26.162 1.00 43.33 N ANISOU 1080 N PHE B 44 6281 6226 3957 159 428 −510 N ATOM 1081 CA PHE B 44 3.262 −7.240 27.227 1.00 45.35 C ANISOU 1081 CA PHE B 44 6609 6685 3936 233 653 −629 C ATOM 1082 C PHE B 44 3.932 −7.209 28.581 1.00 53.45 C ANISOU 1082 C PHE B 44 7849 7939 4521 −174 505 −446 C ATOM 1083 CB PHE B 44 2.460 −8.525 27.017 1.00 44.67 C ANISOU 1083 CB PHE B 44 6024 6763 4187 413 903 −530 C ATOM 1084 CG PHE B 44 3.297 −9.747 26.877 1.00 48.05 C ANISOU 1084 CG PHE B 44 6052 7242 4965 211 877 −101 C ATOM 1085 CD1 PHE B 44 3.613 −10.508 27.985 1.00 53.57 C ANISOU 1085 CD1 PHE B 44 6616 8174 5564 25 918 270 C ATOM 1086 CD2 PHE B 44 3.765 −10.146 25.622 1.00 52.78 C ANISOU 1086 CD2 PHE B 44 6404 7647 6004 224 877 −29 C ATOM 1087 CE1 PHE B 44 4.386 −11.648 27.858 1.00 56.93 C ANISOU 1087 CE1 PHE B 44 6641 8603 6387 −90 1000 768 C ATOM 1088 CE2 PHE B 44 4.537 −11.288 25.478 1.00 52.65 C ANISOU 1088 CE2 PHE B 44 6042 7584 6377 72 989 391 C ATOM 1089 CZ PHE B 44 4.850 −12.041 26.609 1.00 55.11 C ANISOU 1089 CZ PHE B 44 6196 8093 6649 −57 1072 822 C ATOM 1090 O ASP B 45 1.640 −7.122 32.030 1.00 76.11 O ANISOU 1090 O ASP B 45 11338 11369 6213 −211 1171 −855 O ATOM 1091 N ASP B 45 3.155 −6.759 29.566 1.00 60.34 N ANISOU 1091 N ASP B 45 9058 8898 4972 −159 700 −704 N ATOM 1092 CA ASP B 45 3.655 −6.433 30.889 1.00 69.25 C ANISOU 1092 CA ASP B 45 10529 10277 5505 −614 586 −666 C ATOM 1093 C ASP B 45 2.883 −7.200 31.942 1.00 78.36 C ANISOU 1093 C ASP B 45 11552 11755 6468 −573 812 −569 C ATOM 1094 CB ASP B 45 3.554 −4.929 31.156 1.00 71.36 C ANISOU 1094 CB ASP B 45 11510 10264 5339 −742 692 −1162 C ATOM 1095 O THR B 46 5.354 −8.573 34.718 1.00128.01 O ANISOU 1095 O THR B 46 19514 15362 13762 −1288 753 −976 O ATOM 1096 N THR B 46 3.654 −7.942 32.725 1.00117.53 N ANISOU 1096 N THR B 46 18518 13246 12891 −716 857 −1346 N ATOM 1097 CA THR B 46 3.159 −8.792 33.785 1.00122.03 C ANISOU 1097 CA THR B 46 18844 14174 13349 −633 1011 −1350 C ATOM 1098 C THR B 46 4.152 −8.726 34.941 1.00125.08 C ANISOU 1098 C THR B 46 19190 14916 13418 −1019 900 −1209 C ATOM 1099 CB THR B 46 2.995 −10.241 33.306 1.00124.30 C ANISOU 1099 CB THR B 46 18746 14629 13853 −407 1185 −1043 C ATOM 1100 OG1 THR B 46 4.257 −10.735 32.850 1.00124.51 O ANISOU 1100 OG1 THR B 46 18550 14813 13946 −597 1092 −637 O ATOM 1101 CG2 THR B 46 1.990 −10.313 32.155 1.00123.96 C ANISOU 1101 CG2 THR B 46 18739 14229 14130 −13 1291 −1192 C ATOM 1102 O GLY B 47 5.089 −10.155 39.186 1.00120.05 O ANISOU 1102 O GLY B 47 18382 15439 11790 −1710 814 −934 O ATOM 1103 N GLY B 47 3.658 −8.837 36.170 1.00125.72 N ANISOU 1103 N GLY B 47 19292 15218 13255 −1067 970 −1377 N ATOM 1104 CA GLY B 47 4.515 −8.742 37.342 1.00122.62 C ANISOU 1104 CA GLY B 47 18916 15139 12537 −1426 842 −1269 C ATOM 1105 C GLY B 47 4.897 −10.072 37.975 1.00116.92 C ANISOU 1105 C GLY B 47 17915 14796 11712 −1485 867 −929 C ATOM 1106 O SER B 48 5.763 −12.937 35.410 1.00 98.98 O ANISOU 1106 O SER B 48 14774 12605 10229 −991 934 −28 O ATOM 1107 N SER B 48 4.995 −11.095 37.155 1.00112.19 N ANISOU 1107 N SER B 48 17038 14218 11371 −1287 925 −643 N ATOM 1108 CA SER B 48 5.372 −12.390 37.667 1.00107.95 C ANISOU 1108 CA SER B 48 16268 13993 10755 −1315 894 −313 C ATOM 1109 C SER B 48 6.014 −13.170 36.570 1.00104.79 C ANISOU 1109 C SER B 48 15547 13588 10680 −1173 842 14 C ATOM 1110 CB SER B 48 4.136 −13.109 38.185 1.00103.44 C ANISOU 1110 CB SER B 48 15726 13493 10082 −1158 1140 −433 C ATOM 1111 O HIS B 49 5.643 −15.491 35.257 1.00110.33 O ANISOU 1111 O HIS B 49 15713 14352 11854 −677 1012 489 O ATOM 1112 N HIS B 49 6.807 −14.142 36.949 1.00106.08 N ANISOU 1112 N HIS B 49 15492 14016 10799 −1247 678 326 N ATOM 1113 CA HIS B 49 7.725 −14.723 36.032 1.00109.44 C ANISOU 1113 CA HIS B 49 15581 14485 11516 −1189 558 591 C ATOM 1114 C HIS B 49 6.799 −15.237 34.976 1.00109.74 C ANISOU 1114 C HIS B 49 15515 14332 11849 −845 808 610 C ATOM 1115 CB HIS B 49 8.432 −15.892 36.690 1.00111.32 C ANISOU 1115 CB HIS B 49 15610 15015 11670 −1226 328 883 C ATOM 1116 O VAL B 50 6.870 −17.628 32.146 1.00100.44 O ANISOU 1116 O VAL B 50 13531 13068 11562 −202 992 1166 O ATOM 1117 N VAL B 50 7.253 −15.286 33.737 1.00108.29 N ANISOU 1117 N VAL B 50 15126 14033 11987 −761 815 711 N ATOM 1118 CA VAL B 50 6.320 −15.373 32.640 1.00103.91 C ANISOU 1118 CA VAL B 50 14573 13208 11701 −462 1049 650 C ATOM 1119 C VAL B 50 6.006 −16.830 32.475 1.00100.58 C ANISOU 1119 C VAL B 50 13867 12923 11427 −203 1127 904 C ATOM 1120 CB VAL B 50 6.881 −14.791 31.330 1.00102.46 C ANISOU 1120 CB VAL B 50 14355 12807 11769 −517 1040 645 C ATOM 1121 O ASN B 51 3.504 −20.481 32.483 1.00 88.57 O ANISOU 1121 O ASN B 51 12002 11577 10076 573 1613 1295 O ATOM 1122 N ASN B 51 4.760 −17.172 32.721 1.00 99.47 N ANISOU 1122 N ASN B 51 13835 12720 11240 11 1339 792 N ATOM 1123 CA ASN B 51 4.456 −18.463 33.287 1.00 96.35 C ANISOU 1123 CA ASN B 51 13313 12537 10760 111 1373 993 C ATOM 1124 C ASN B 51 4.031 −19.417 32.210 1.00 91.66 C ANISOU 1124 C ASN B 51 12464 11860 10504 439 1523 1164 C ATOM 1125 CB ASN B 51 3.376 −18.330 34.345 1.00 96.71 C ANISOU 1125 CB ASN B 51 13633 12621 10492 66 1543 740 C ATOM 1126 O LEU B 52 4.971 −19.273 28.248 1.00 85.97 O ANISOU 1126 O LEU B 52 11233 10645 10785 772 1611 1388 O ATOM 1127 N LEU B 52 4.222 −18.995 30.969 1.00 90.63 N ANISOU 1127 N LEU B 52 12236 11516 10683 545 1559 1148 N ATOM 1128 CA LEU B 52 3.307 −19.377 29.924 1.00 88.19 C ANISOU 1128 CA LEU B 52 11845 10996 10666 882 1789 1126 C ATOM 1129 C LEU B 52 4.058 −19.906 28.728 1.00 86.56 C ANISOU 1129 C LEU B 52 11328 10766 10794 968 1736 1386 C ATOM 1130 CB LEU B 52 2.465 −18.176 29.546 1.00 87.40 C ANISOU 1130 CB LEU B 52 12047 10564 10597 956 1908 749 C ATOM 1131 O GLY B 53 0.462 −22.179 27.767 1.00 86.95 O ANISOU 1131 O GLY B 53 11206 10585 11247 1953 2471 1307 O ATOM 1132 N GLY B 53 3.656 −21.059 28.230 1.00 84.58 N ANISOU 1132 N GLY B 53 10839 10549 10747 1240 1849 1579 N ATOM 1133 CA GLY B 53 2.529 −21.119 27.340 1.00 84.37 C ANISOU 1133 CA GLY B 53 10850 10259 10948 1555 2095 1462 C ATOM 1134 C GLY B 53 1.215 −21.273 28.051 1.00 85.94 C ANISOU 1134 C GLY B 53 11213 10451 10989 1700 2294 1243 C ATOM 1135 O ALA B 54 −1.678 −17.977 28.102 1.00 71.58 O ANISOU 1135 O ALA B 54 10269 7822 9106 1969 2529 −144 O ATOM 1136 N ALA B 54 0.926 −20.332 28.932 1.00 83.82 N ANISOU 1136 N ALA B 54 11232 10166 10448 1525 2279 944 N ATOM 1137 CA ALA B 54 −0.398 −19.766 29.090 1.00 77.01 C ANISOU 1137 CA ALA B 54 10581 9123 9555 1680 2477 521 C ATOM 1138 C ALA B 54 −0.627 −18.587 28.134 1.00 71.62 C ANISOU 1138 C ALA B 54 10094 8043 9075 1795 2434 260 C ATOM 1139 CB ALA B 54 −0.604 −19.342 30.530 1.00 76.88 C ANISOU 1139 CB ALA B 54 10777 9291 9144 1426 2475 290 C ATOM 1140 N ILE B 55 0.376 −18.272 27.353 1.00 67.24 N ANISOU 1140 N ILE B 55 9520 7385 8645 1680 2273 468 N ATOM 1141 CA ILE B 55 0.261 −17.136 26.461 1.00 66.95 C ANISOU 1141 CA ILE B 55 9762 6940 8736 1717 2194 252 C ATOM 1142 C ILE B 55 −0.165 −17.553 25.067 1.00 67.05 C ANISOU 1142 C ILE B 55 9688 6686 9103 2023 2285 333 C ATOM 1143 O ILE B 55 0.413 −18.453 24.466 1.00 66.51 O ANISOU 1143 O ILE B 55 9325 6746 9200 2041 2320 679 O ATOM 1144 CB ILE B 55 1.564 −16.359 26.360 1.00 67.80 C ANISOU 1144 CB ILE B 55 9989 7041 8732 1340 1982 365 C ATOM 1145 CG1 ILE B 55 1.631 −15.346 27.493 1.00 72.90 C ANISOU 1145 CG1 ILE B 55 10914 7730 9053 1096 1865 103 C ATOM 1146 CG2 ILE B 55 1.631 −15.601 25.034 1.00 65.66 C ANISOU 1146 CG2 ILE B 55 9961 6339 8646 1360 1918 298 C ATOM 1147 CD1 ILE B 55 2.955 −14.685 27.623 1.00 76.41 C ANISOU 1147 CD1 ILE B 55 11438 8252 9345 687 1670 213 C ATOM 1148 N THR B 56 −1.217 −16.911 24.585 1.00 47.66 N ANISOU 1148 N THR B 56 8634 4154 5321 642 2450 802 N ATOM 1149 CA THR B 56 −1.536 −16.897 23.172 1.00 51.32 C ANISOU 1149 CA THR B 56 8646 4778 6076 310 2315 562 C ATOM 1150 C THR B 56 −1.153 −15.501 22.668 1.00 49.38 C ANISOU 1150 C THR B 56 7913 5043 5808 283 1829 539 C ATOM 1151 O THR B 56 −1.229 −14.530 23.418 1.00 51.68 O ANISOU 1151 O THR B 56 8163 5456 6019 328 1732 629 O ATOM 1152 CB THR B 56 −3.043 −17.190 22.918 1.00 71.03 C ANISOU 1152 CB THR B 56 11004 7017 8969 −160 2661 363 C ATOM 1153 OG1 THR B 56 −3.392 −18.445 23.501 1.00 74.68 O ANISOU 1153 OG1 THR B 56 11963 6931 9481 −162 3206 391 O ATOM 1154 CG2 THR B 56 −3.354 −17.244 21.424 1.00 70.90 C ANISOU 1154 CG2 THR B 56 10553 7209 9177 −477 2444 84 C ATOM 1155 N ALA B 57 −0.700 −15.387 21.427 1.00 41.89 N ANISOU 1155 N ALA B 57 6653 4356 4905 224 1567 422 N ATOM 1156 CA ALA B 57 −0.611 −14.082 20.809 1.00 33.93 C ANISOU 1156 CA ALA B 57 5202 3751 3940 128 1222 392 C ATOM 1157 C ALA B 57 −1.081 −14.236 19.399 1.00 35.37 C ANISOU 1157 C ALA B 57 5115 4048 4278 −121 1144 196 C ATOM 1158 O ALA B 57 −0.800 −15.244 18.771 1.00 38.28 O ANISOU 1158 O ALA B 57 5632 4294 4616 −113 1231 91 O ATOM 1159 CB ALA B 57 0.857 −13.530 20.835 1.00 36.33 C ANISOU 1159 CB ALA B 57 5430 4344 4029 426 919 505 C ATOM 1160 N SER B 58 −1.749 −13.224 18.873 1.00 35.97 N ANISOU 1160 N SER B 58 4823 4361 4482 −305 969 149 N ATOM 1161 CA SER B 58 −2.133 −13.252 17.472 1.00 38.71 C ANISOU 1161 CA SER B 58 4923 4898 4886 −483 804 −26 C ATOM 1162 C SER B 58 −2.071 −11.861 16.920 1.00 37.40 C ANISOU 1162 C SER B 58 4439 5079 4693 −447 534 63 C ATOM 1163 O SER B 58 −2.246 −10.867 17.651 1.00 35.31 O ANISOU 1163 O SER B 58 4080 4849 4486 −405 533 201 O ATOM 1164 CB SER B 58 −3.550 −13.819 17.295 1.00 53.43 C ANISOU 1164 CB SER B 58 6670 6615 7014 −815 939 −237 C ATOM 1165 OG SER B 58 −3.592 −15.182 17.691 1.00 64.20 O ANISOU 1165 OG SER B 58 8381 7587 8426 −884 1266 −339 O ATOM 1166 N LEU B 59 −1.827 −11.788 15.617 1.00 32.74 N ANISOU 1166 N LEU B 59 3739 4711 3990 −452 346 −16 N ATOM 1167 CA LEU B 59 −1.876 −10.533 14.926 1.00 33.05 C ANISOU 1167 CA LEU B 59 3528 5044 3984 −404 137 82 C ATOM 1168 C LEU B 59 −3.023 −10.604 13.914 1.00 43.26 C ANISOU 1168 C LEU B 59 4615 6503 5320 −573 −36 −80 C ATOM 1169 O LEU B 59 −2.955 −11.349 12.937 1.00 47.27 O ANISOU 1169 O LEU B 59 5211 7069 5679 −635 −123 −265 O ATOM 1170 CB LEU B 59 −0.544 −10.237 14.247 1.00 35.74 C ANISOU 1170 CB LEU B 59 3937 5528 4113 −214 79 168 C ATOM 1171 CG LEU B 59 −0.479 −8.825 13.679 1.00 36.52 C ANISOU 1171 CG LEU B 59 3849 5853 4173 −142 −37 322 C ATOM 1172 CD1 LEU B 59 −0.232 −7.796 14.759 1.00 35.91 C ANISOU 1172 CD1 LEU B 59 3705 5716 4223 −100 31 481 C ATOM 1173 CD2 LEU B 59 0.580 −8.796 12.670 1.00 39.62 C ANISOU 1173 CD2 LEU B 59 4320 6366 4367 −13 −33 350 C ATOM 1174 N GLN B 60 −4.081 −9.846 14.153 1.00 39.57 N ANISOU 1174 N GLN B 60 3869 6119 5047 −635 −96 −28 N ATOM 1175 CA GLN B 60 −5.260 −9.955 13.305 1.00 44.90 C ANISOU 1175 CA GLN B 60 4262 6996 5803 −782 −315 −200 C ATOM 1176 C GLN B 60 −5.456 −8.737 12.424 1.00 42.61 C ANISOU 1176 C GLN B 60 3772 7041 5378 −591 −578 −38 C ATOM 1177 O GLN B 60 −5.641 −7.623 12.914 1.00 38.62 O ANISOU 1177 O GLN B 60 3138 6547 4989 −453 −519 192 O ATOM 1178 CB GLN B 60 −6.487 −10.178 14.165 1.00 46.57 C ANISOU 1178 CB GLN B 60 4236 7057 6401 −985 −165 −284 C ATOM 1179 CG GLN B 60 −6.467 −11.510 14.903 1.00 54.37 C ANISOU 1179 CG GLN B 60 5469 7672 7519 −1191 144 −457 C ATOM 1180 CD GLN B 60 −6.650 −12.710 13.974 1.00 64.33 C ANISOU 1180 CD GLN B 60 6785 8929 8728 −1425 48 −798 C ATOM 1181 OE1 GLN B 60 −7.229 −12.588 12.885 1.00 71.72 O ANISOU 1181 OE1 GLN B 60 7460 10177 9613 −1514 −290 −971 O ATOM 1182 NE2 GLN B 60 −6.177 −13.874 14.408 1.00 63.52 N ANISOU 1182 NE2 GLN B 60 7052 8463 8617 −1509 346 −901 N ATOM 1183 N LYS B 61 −5.452 −8.952 11.110 1.00 42.99 N ANISOU 1183 N LYS B 61 3842 7340 5154 −565 −847 −157 N ATOM 1184 CA LYS B 61 −5.655 −7.833 10.207 1.00 38.43 C ANISOU 1184 CA LYS B 61 3146 7075 4380 −323 −1088 32 C ATOM 1185 C LYS B 61 −7.097 −7.330 10.336 1.00 41.13 C ANISOU 1185 C LYS B 61 3039 7593 4995 −332 −1270 42 C ATOM 1186 O LYS B 61 −8.078 −8.102 10.326 1.00 44.45 O ANISOU 1186 O LYS B 61 3189 8076 5623 −575 −1409 −238 O ATOM 1187 CB LYS B 61 −5.309 −8.216 8.759 1.00 49.92 C ANISOU 1187 CB LYS B 61 4809 8762 5395 −256 −1328 −97 C ATOM 1188 CG LYS B 61 −5.010 −7.020 7.886 1.00 50.07 C ANISOU 1188 CG LYS B 61 4916 9005 5104 83 −1430 198 C ATOM 1189 CD LYS B 61 −4.664 −7.435 6.472 1.00 54.24 C ANISOU 1189 CD LYS B 61 5734 9743 5130 171 −1626 72 C ATOM 1190 CE LYS B 61 −4.271 −6.245 5.603 1.00 51.21 C ANISOU 1190 CE LYS B 61 5538 9521 4396 545 −1630 414 C ATOM 1191 NZ LYS B 61 −5.303 −5.218 5.441 1.00 50.86 N ANISOU 1191 NZ LYS B 61 5226 9714 4385 773 −1875 630 N ATOM 1192 N VAL B 62 −7.245 −6.020 10.449 1.00 43.87 N ANISOU 1192 N VAL B 62 3278 8008 5381 −66 −1244 358 N ATOM 1193 CA VAL B 62 −8.584 −5.457 10.571 1.00 44.83 C ANISOU 1193 CA VAL B 62 2946 8300 5787 7 −1387 416 C ATOM 1194 C VAL B 62 −9.384 −5.557 9.276 1.00 52.62 C ANISOU 1194 C VAL B 62 3716 9701 6577 102 −1875 291 C ATOM 1195 O VAL B 62 −10.520 −6.015 9.299 1.00 56.68 O ANISOU 1195 O VAL B 62 3886 10258 7390 −61 −2037 64 O ATOM 1196 CB VAL B 62 −8.555 −3.977 11.004 1.00 43.44 C ANISOU 1196 CB VAL B 62 2763 8040 5703 315 −1187 803 C ATOM 1197 CG1 VAL B 62 −9.985 −3.405 10.995 1.00 50.36 C ANISOU 1197 CG1 VAL B 62 3205 9057 6874 462 −1319 858 C ATOM 1198 CG2 VAL B 62 −7.969 −3.849 12.397 1.00 41.17 C ANISOU 1198 CG2 VAL B 62 2669 7343 5631 192 −748 861 C ATOM 1199 O GLU B 63 −11.560 −5.909 5.991 1.00 92.29 O ANISOU 1199 O GLU B 63 8497 15454 11114 309 −3144 −98 O ATOM 1200 N GLU B 63 −8.803 −5.127 8.156 1.00 55.98 N ANISOU 1200 N GLU B 63 4451 10290 6529 363 −2045 425 N ATOM 1201 CA GLU B 63 −9.603 −4.907 6.931 1.00 70.47 C ANISOU 1201 CA GLU B 63 6241 12377 8157 552 −2458 383 C ATOM 1202 C GLU B 63 −10.460 −6.093 6.519 1.00 84.42 C ANISOU 1202 C GLU B 63 7778 14280 10017 235 −2803 −52 C ATOM 1203 CB GLU B 63 −8.716 −4.535 5.741 1.00 70.62 C ANISOU 1203 CB GLU B 63 6742 12504 7587 822 −2525 542 C ATOM 1204 O ASP B 64 −12.942 −8.390 5.647 1.00112.02 O ANISOU 1204 O ASP B 64 10559 18045 13960 −535 −3581 −975 O ATOM 1205 N ASP B 64 −9.955 −7.301 6.751 1.00 85.46 N ANISOU 1205 N ASP B 64 8028 14318 10126 −125 −2707 −370 N ATOM 1206 CA ASP B 64 −10.612 −8.517 6.258 1.00 97.58 C ANISOU 1206 CA ASP B 64 9451 15923 11702 −478 −2979 −827 C ATOM 1207 C ASP B 64 −12.114 −8.618 6.540 1.00104.54 C ANISOU 1207 C ASP B 64 9782 16839 13100 −645 −3152 −952 C ATOM 1208 CB ASP B 64 −9.906 −9.717 6.848 1.00 97.62 C ANISOU 1208 CB ASP B 64 9637 15696 11759 −859 −2687 −1128 C ATOM 1209 CG ASP B 64 −8.446 −9.708 6.546 1.00 95.55 C ANISOU 1209 CG ASP B 64 9892 15387 11024 −701 −2511 −1008 C ATOM 1210 OD1 ASP B 64 −8.067 −9.230 5.456 1.00 98.14 O ANISOU 1210 OD1 ASP B 64 10490 15933 10866 −411 −2716 −880 O ATOM 1211 OD2 ASP B 64 −7.672 −10.145 7.407 1.00 91.84 O ANISOU 1211 OD2 ASP B 64 9661 14510 10724 −811 −2073 −967 O ATOM 1212 O PRO B 68 −7.396 −14.242 5.894 1.00100.74 O ANISOU 1212 O PRO B 68 11578 15240 11460 −1752 −2074 −2335 O ATOM 1213 N PRO B 68 −10.494 −14.729 5.787 1.00116.51 N ANISOU 1213 N PRO B 68 12523 17506 14238 −2372 −2688 −2893 N ATOM 1214 CA PRO B 68 −9.523 −14.470 4.739 1.00115.35 C ANISOU 1214 CA PRO B 68 12851 17560 13416 −2073 −2862 −2825 C ATOM 1215 C PRO B 68 −8.097 −14.880 5.116 1.00108.70 C ANISOU 1215 C PRO B 68 12519 16424 12358 −2030 −2399 −2785 C ATOM 1216 CB PRO B 68 −9.677 −12.976 4.532 1.00114.27 C ANISOU 1216 CB PRO B 68 12501 17767 13148 −1604 −3110 −2344 C ATOM 1217 CG PRO B 68 −11.141 −12.739 4.750 1.00118.30 C ANISOU 1217 CG PRO B 68 12431 18385 14134 −1717 −3353 −2358 C ATOM 1218 CD PRO B 68 −11.641 −13.810 5.677 1.00119.42 C ANISOU 1218 CD PRO B 68 12368 18178 14830 −2207 −3038 −2678 C ATOM 1219 O HIS B 69 −6.646 −18.953 4.114 1.00120.78 O ANISOU 1219 O HIS B 69 15599 16807 13485 −2796 −1566 −3991 O ATOM 1220 N HIS B 69 −7.700 −16.015 4.583 1.00111.88 N ANISOU 1220 N HIS B 69 13358 16609 12542 −2250 −2284 −3167 N ATOM 1221 CA HIS B 69 −7.040 −16.999 5.387 1.00110.83 C ANISOU 1221 CA HIS B 69 13567 15888 12656 −2396 −1698 −3209 C ATOM 1222 C HIS B 69 −6.190 −17.916 4.549 1.00115.95 C ANISOU 1222 C HIS B 69 14844 16336 12877 −2402 −1536 −3468 C ATOM 1223 CB HIS B 69 −8.037 −17.782 6.242 1.00112.06 C ANISOU 1223 CB HIS B 69 13413 15751 13414 −2880 −1520 −3510 C ATOM 1224 CG HIS B 69 −9.089 −18.535 5.473 1.00118.11 C ANISOU 1224 CG HIS B 69 14038 16580 14259 −3248 −1819 −3981 C ATOM 1225 ND1 HIS B 69 −10.171 −17.934 4.866 1.00121.55 N ANISOU 1225 ND1 HIS B 69 14012 17446 14725 −3209 −2368 −3968 N ATOM 1226 CD2 HIS B 69 −9.249 −19.866 5.280 1.00122.49 C ANISOU 1226 CD2 HIS B 69 14879 16737 14925 −3601 −1596 −4383 C ATOM 1227 CE1 HIS B 69 −10.923 −18.855 4.298 1.00128.90 C ANISOU 1227 CE1 HIS B 69 14932 18293 15752 −3555 −2524 −4379 C ATOM 1228 NE2 HIS B 69 −10.395 −20.036 4.551 1.00129.64 N ANISOU 1228 NE2 HIS B 69 15468 17881 15909 −3808 −2049 −4641 N ATOM 1229 O ARG B 70 −2.018 −17.873 6.287 1.00105.31 O ANISOU 1229 O ARG B 70 14427 14088 11496 −1298 −121 −2287 O ATOM 1230 N ARG B 70 −4.961 −17.523 4.284 1.00114.04 N ANISOU 1230 N ARG B 70 14970 16073 12286 −1979 −1341 −3127 N ATOM 1231 CA ARG B 70 −3.823 −18.258 4.776 1.00112.98 C ANISOU 1231 CA ARG B 70 15269 15450 12207 −1852 −776 −3017 C ATOM 1232 C ARG B 70 −3.127 −17.515 5.909 1.00105.58 C ANISOU 1232 C ARG B 70 14169 14414 11531 −1529 −516 −2474 C ATOM 1233 CB ARG B 70 −2.849 −18.564 3.641 1.00116.54 C ANISOU 1233 CB ARG B 70 16265 15900 12115 −1636 −671 −3100 C ATOM 1234 O GLU B 71 −1.608 −16.244 8.152 1.00 77.81 O ANISOU 1234 O GLU B 71 10423 10689 8452 −950 −46 −1552 O ATOM 1235 N GLU B 71 −3.768 −16.540 6.535 1.00100.31 N ANISOU 1235 N GLU B 71 13034 13965 11113 −1512 −718 −2239 N ATOM 1236 CA GLU B 71 −3.183 −15.221 6.679 1.00 89.47 C ANISOU 1236 CA GLU B 71 11517 12824 9652 −1140 −770 −1774 C ATOM 1237 C GLU B 71 −1.882 −15.275 7.487 1.00 76.87 C ANISOU 1237 C GLU B 71 10116 10939 8152 −881 −351 −1470 C ATOM 1238 CB GLU B 71 −4.171 −14.252 7.336 1.00 87.85 C ANISOU 1238 CB GLU B 71 10806 12820 9753 −1183 −988 −1602 C ATOM 1239 CG GLU B 71 −4.728 −13.148 6.430 1.00 86.37 C ANISOU 1239 CG GLU B 71 10390 13114 9313 −1029 −1427 −1504 C ATOM 1240 CD GLU B 71 −6.011 −12.568 6.958 1.00 82.99 C ANISOU 1240 CD GLU B 71 9429 12859 9243 −1144 −1655 −1477 C ATOM 1241 OE1 GLU B 71 −6.432 −11.492 6.577 1.00 80.10 O ANISOU 1241 OE1 GLU B 71 8830 12828 8777 −928 −1933 −1270 O ATOM 1242 OE2 GLU B 71 −6.615 −13.201 7.802 1.00 85.14 O ANISOU 1242 OE2 GLU B 71 9521 12900 9928 −1433 −1502 −1647 O ATOM 1243 O ARG B 72 2.482 −14.256 7.485 1.00 46.67 O ANISOU 1243 O ARG B 72 6633 7026 4076 123 399 −640 O ATOM 1244 N ARG B 72 −1.063 −14.245 7.308 1.00 65.86 N ANISOU 1244 N ARG B 72 8690 9726 6609 −570 −346 −1135 N ATOM 1245 CA ARG B 72 0.265 −14.288 6.735 1.00 54.71 C ANISOU 1245 CA ARG B 72 7564 8277 4947 −301 −115 −1017 C ATOM 1246 C ARG B 72 1.361 −13.956 7.725 1.00 46.15 C ANISOU 1246 C ARG B 72 6391 7051 4092 −79 151 −704 C ATOM 1247 CB ARG B 72 0.379 −13.231 5.652 1.00 51.55 C ANISOU 1247 CB ARG B 72 7171 8213 4203 −125 −288 −871 C ATOM 1248 CG ARG B 72 0.167 −13.674 4.224 1.00 53.12 C ANISOU 1248 CG ARG B 72 7705 8556 3923 −145 −427 −1139 C ATOM 1249 CD ARG B 72 0.600 −12.558 3.286 1.00 51.88 C ANISOU 1249 CD ARG B 72 7649 8661 3403 142 −455 −874 C ATOM 1250 NE ARG B 72 1.905 −12.824 2.745 1.00 55.84 N ANISOU 1250 NE ARG B 72 8491 9016 3709 352 −47 −805 N ATOM 1251 CZ ARG B 72 2.778 −11.923 2.381 1.00 55.87 C ANISOU 1251 CZ ARG B 72 8540 9076 3614 611 193 −489 C ATOM 1252 NH1 ARG B 72 3.904 −12.320 1.907 1.00 61.32 N ANISOU 1252 NH1 ARG B 72 9502 9614 4184 774 601 −473 N ATOM 1253 NH2 ARG B 72 2.540 −10.650 2.465 1.00 58.36 N ANISOU 1253 NH2 ARG B 72 8641 9563 3969 707 81 −196 N ATOM 1254 N ALA B 73 1.033 −13.313 8.822 1.00 41.84 N ANISOU 1254 N ALA B 73 5561 6508 3830 −110 88 −527 N ATOM 1255 CA ALA B 73 2.039 −12.903 9.774 1.00 39.81 C ANISOU 1255 CA ALA B 73 5200 6174 3751 82 255 −270 C ATOM 1256 C ALA B 73 2.232 −13.993 10.778 1.00 45.23 C ANISOU 1256 C ALA B 73 6027 6555 4605 91 438 −325 C ATOM 1257 O ALA B 73 1.299 −14.386 11.438 1.00 45.12 O ANISOU 1257 O ALA B 73 6010 6393 4740 −96 421 −421 O ATOM 1258 CB ALA B 73 1.632 −11.633 10.453 1.00 39.35 C ANISOU 1258 CB ALA B 73 4845 6248 3858 58 115 −70 C ATOM 1259 N THR B 74 3.442 −14.487 10.903 1.00 34.99 N ANISOU 1259 N THR B 74 4850 5150 3293 337 646 −247 N ATOM 1260 CA THR B 74 3.656 −15.619 11.770 1.00 37.57 C ANISOU 1260 CA THR B 74 5387 5165 3725 427 843 −269 C ATOM 1261 C THR B 74 4.344 −15.226 13.081 1.00 37.02 C ANISOU 1261 C THR B 74 5163 5105 3797 644 826 −23 C ATOM 1262 O THR B 74 5.317 −14.477 13.082 1.00 37.96 O ANISOU 1262 O THR B 74 5052 5433 3937 818 769 128 O ATOM 1263 CB THR B 74 4.468 −16.687 11.072 1.00 43.56 C ANISOU 1263 CB THR B 74 6441 5748 4361 612 1106 −364 C ATOM 1264 OG1 THR B 74 3.836 −16.981 9.830 1.00 49.20 O ANISOU 1264 OG1 THR B 74 7337 6480 4878 394 1083 −634 O ATOM 1265 CG2 THR B 74 4.494 −17.946 11.920 1.00 45.70 C ANISOU 1265 CG2 THR B 74 7009 5626 4728 713 1352 −385 C ATOM 1266 N LEU B 75 3.835 −15.758 14.182 1.00 34.30 N ANISOU 1266 N LEU B 75 4964 4527 3541 620 889 −5 N ATOM 1267 CA LEU B 75 4.362 −15.463 15.521 1.00 33.45 C ANISOU 1267 CA LEU B 75 4797 4426 3485 835 836 204 C ATOM 1268 C LEU B 75 5.764 −16.055 15.671 1.00 35.36 C ANISOU 1268 C LEU B 75 5091 4659 3685 1245 925 324 C ATOM 1269 O LEU B 75 5.977 −17.199 15.310 1.00 38.87 O ANISOU 1269 O LEU B 75 5820 4860 4089 1381 1166 268 O ATOM 1270 CB LEU B 75 3.444 −16.027 16.606 1.00 34.03 C ANISOU 1270 CB LEU B 75 5124 4199 3608 748 964 207 C ATOM 1271 CG LEU B 75 3.881 −15.838 18.067 1.00 36.37 C ANISOU 1271 CG LEU B 75 5490 4473 3855 998 914 414 C ATOM 1272 CD1 LEU B 75 3.922 −14.351 18.444 1.00 31.54 C ANISOU 1272 CD1 LEU B 75 4543 4172 3269 910 638 477 C ATOM 1273 CD2 LEU B 75 2.986 −16.634 19.025 1.00 38.85 C ANISOU 1273 CD2 LEU B 75 6187 4396 4179 949 1176 431 C ATOM 1274 N LEU B 76 6.695 −15.274 16.214 1.00 34.81 N ANISOU 1274 N LEU B 76 4730 4847 3649 1435 735 470 N ATOM 1275 CA LEU B 76 8.029 −15.802 16.587 1.00 37.41 C ANISOU 1275 CA LEU B 76 5010 5224 3980 1872 753 601 C ATOM 1276 C LEU B 76 8.068 −16.133 18.089 1.00 41.31 C ANISOU 1276 C LEU B 76 5685 5625 4385 2111 654 743 C ATOM 1277 O LEU B 76 8.232 −15.251 18.927 1.00 40.95 O ANISOU 1277 O LEU B 76 5441 5795 4324 2097 383 794 O ATOM 1278 CB LEU B 76 9.110 −14.785 16.219 1.00 37.28 C ANISOU 1278 CB LEU B 76 4503 5576 4087 1923 594 635 C ATOM 1279 CG LEU B 76 9.029 −14.252 14.777 1.00 42.18 C ANISOU 1279 CG LEU B 76 4998 6287 4741 1694 718 536 C ATOM 1280 CD1 LEU B 76 10.035 −13.122 14.567 1.00 39.49 C ANISOU 1280 CD1 LEU B 76 4180 6255 4570 1694 631 584 C ATOM 1281 CD2 LEU B 76 9.197 −15.374 13.688 1.00 38.51 C ANISOU 1281 CD2 LEU B 76 4814 5625 4195 1822 1036 458 C ATOM 1282 N GLU B 77 7.837 −17.393 18.425 1.00 39.69 N ANISOU 1282 N GLU B 77 4778 5378 4924 1296 363 625 N ATOM 1283 CA GLU B 77 7.582 −17.774 19.811 1.00 44.60 C ANISOU 1283 CA GLU B 77 5477 6106 5362 1498 410 791 C ATOM 1284 C GLU B 77 8.796 −17.544 20.715 1.00 45.19 C ANISOU 1284 C GLU B 77 5476 6439 5256 1685 181 920 C ATOM 1285 O GLU B 77 8.660 −17.279 21.907 1.00 50.57 O ANISOU 1285 O GLU B 77 6241 7303 5670 1821 74 971 O ATOM 1286 CB GLU B 77 7.165 −19.248 19.893 1.00 53.70 C ANISOU 1286 CB GLU B 77 6705 7051 6646 1605 766 988 C ATOM 1287 CG GLU B 77 5.752 −19.535 19.448 1.00 60.50 C ANISOU 1287 CG GLU B 77 7642 7685 7661 1442 969 884 C ATOM 1288 CD GLU B 77 5.413 −21.020 19.487 1.00 69.41 C ANISOU 1288 CD GLU B 77 8826 8562 8985 1522 1338 1059 C ATOM 1289 OE1 GLU B 77 6.328 −21.864 19.283 1.00 71.22 O ANISOU 1289 OE1 GLU B 77 9036 8718 9305 1636 1471 1204 O ATOM 1290 OE2 GLU B 77 4.226 −21.339 19.734 1.00 71.86 O ANISOU 1290 OE2 GLU B 77 9184 8725 9396 1475 1521 1065 O ATOM 1291 N GLU B 78 9.979 −17.635 20.132 1.00 43.81 N ANISOU 1291 N GLU B 78 5142 6279 5226 1691 102 975 N ATOM 1292 CA GLU B 78 11.199 −17.584 20.904 1.00 49.48 C ANISOU 1292 CA GLU B 78 5724 7232 5845 1865 −125 1140 C ATOM 1293 C GLU B 78 11.365 −16.221 21.569 1.00 52.51 C ANISOU 1293 C GLU B 78 6084 7858 6011 1793 −512 944 C ATOM 1294 O GLU B 78 12.129 −16.083 22.505 1.00 56.31 O ANISOU 1294 O GLU B 78 6500 8583 6313 1928 −767 1039 O ATOM 1295 CB GLU B 78 12.406 −17.900 20.023 1.00 49.92 C ANISOU 1295 CB GLU B 78 5573 7213 6183 1872 −96 1247 C ATOM 1296 CG GLU B 78 12.947 −16.717 19.222 1.00 50.53 C ANISOU 1296 CG GLU B 78 5498 7306 6396 1674 −312 1035 C ATOM 1297 CD GLU B 78 12.175 −16.483 17.911 1.00 50.44 C ANISOU 1297 CD GLU B 78 5589 7055 6520 1461 −123 828 C ATOM 1298 OE1 GLU B 78 11.111 −17.143 17.702 1.00 49.57 O ANISOU 1298 OE1 GLU B 78 5663 6787 6385 1430 115 802 O ATOM 1299 OE2 GLU B 78 12.624 −15.622 17.113 1.00 46.37 O ANISOU 1299 OE2 GLU B 78 4963 6517 6139 1328 −223 699 O ATOM 1300 N GLN B 79 10.655 −15.206 21.103 1.00 49.31 N ANISOU 1300 N GLN B 79 5732 7386 5619 1580 −564 668 N ATOM 1301 CA GLN B 79 10.848 −13.899 21.717 1.00 54.81 C ANISOU 1301 CA GLN B 79 6416 8265 6144 1502 −894 461 C ATOM 1302 C GLN B 79 9.832 −13.573 22.824 1.00 51.84 C ANISOU 1302 C GLN B 79 6290 7972 5437 1563 −887 380 C ATOM 1303 O GLN B 79 9.952 −12.548 23.510 1.00 50.98 O ANISOU 1303 O GLN B 79 6233 8009 5127 1520 −1140 193 O ATOM 1304 CB GLN B 79 10.857 −12.834 20.623 1.00 64.12 C ANISOU 1304 CB GLN B 79 7485 9325 7551 1261 −952 231 C ATOM 1305 CG GLN B 79 12.236 −12.808 19.927 1.00 71.51 C ANISOU 1305 CG GLN B 79 8155 10262 8754 1237 −1060 304 C ATOM 1306 CD GLN B 79 12.219 −12.131 18.588 1.00 75.16 C ANISOU 1306 CD GLN B 79 8532 10547 9479 1051 −979 170 C ATOM 1307 OE1 GLN B 79 11.348 −11.304 18.305 1.00 75.81 O ANISOU 1307 OE1 GLN B 79 8707 10563 9535 913 −961 −20 O ATOM 1308 NE2 GLN B 79 13.186 −12.481 17.740 1.00 77.35 N ANISOU 1308 NE2 GLN B 79 8634 10739 10016 1067 −901 296 N ATOM 1309 N LEU B 80 8.870 −14.465 23.035 1.00 49.02 N ANISOU 1309 N LEU B 80 6090 7501 5034 1671 −577 525 N ATOM 1310 CA LEU B 80 7.907 −14.277 24.108 1.00 51.73 C ANISOU 1310 CA LEU B 80 6675 7895 5085 1773 −492 506 C ATOM 1311 C LEU B 80 8.547 −14.120 25.503 1.00 55.40 C ANISOU 1311 C LEU B 80 7257 8653 5139 1971 −739 557 C ATOM 1312 O LEU B 80 8.093 −13.287 26.285 1.00 56.56 O ANISOU 1312 O LEU B 80 7598 8886 5005 1972 −825 386 O ATOM 1313 CB LEU B 80 6.910 −15.428 24.115 1.00 50.36 C ANISOU 1313 CB LEU B 80 6604 7532 5000 1878 −91 711 C ATOM 1314 CG LEU B 80 5.920 −15.352 22.953 1.00 48.15 C ANISOU 1314 CG LEU B 80 6266 6987 5041 1656 104 593 C ATOM 1315 CD1 LEU B 80 5.095 −16.625 22.877 1.00 51.51 C ANISOU 1315 CD1 LEU B 80 6739 7201 5631 1727 475 791 C ATOM 1316 CD2 LEU B 80 5.013 −14.117 23.041 1.00 44.05 C ANISOU 1316 CD2 LEU B 80 5818 6449 4469 1525 62 373 C ATOM 1317 N PRO B 81 9.599 −14.902 25.824 1.00 58.66 N ANISOU 1317 N PRO B 81 7562 9223 5503 2144 −855 794 N ATOM 1318 CA PRO B 81 10.204 −14.675 27.148 1.00 62.15 C ANISOU 1318 CA PRO B 81 8116 9988 5509 2323 −1161 831 C ATOM 1319 C PRO B 81 10.839 −13.287 27.307 1.00 63.28 C ANISOU 1319 C PRO B 81 8200 10292 5553 2132 −1607 496 C ATOM 1320 O PRO B 81 11.115 −12.879 28.430 1.00 65.62 O ANISOU 1320 O PRO B 81 8658 10843 5434 2227 −1883 422 O ATOM 1321 CB PRO B 81 11.286 −15.758 27.241 1.00 65.57 C ANISOU 1321 CB PRO B 81 8359 10546 6008 2527 −1216 1180 C ATOM 1322 CG PRO B 81 10.900 −16.781 26.236 1.00 63.57 C ANISOU 1322 CG PRO B 81 8019 9984 6149 2519 −790 1356 C ATOM 1323 CD PRO B 81 10.182 −16.078 25.148 1.00 60.09 C ANISOU 1323 CD PRO B 81 7558 9299 5974 2223 −686 1063 C ATOM 1324 N LEU B 82 11.072 −12.585 26.201 1.00 62.19 N ANISOU 1324 N LEU B 82 7846 9999 5783 1870 −1667 298 N ATOM 1325 CA LEU B 82 11.525 −11.189 26.246 1.00 65.18 C ANISOU 1325 CA LEU B 82 8163 10447 6155 1656 −2014 −43 C ATOM 1326 C LEU B 82 10.360 −10.223 26.447 1.00 61.76 C ANISOU 1326 C LEU B 82 7990 9888 5589 1545 −1879 −321 C ATOM 1327 O LEU B 82 10.544 −9.011 26.413 1.00 62.06 O ANISOU 1327 O LEU B 82 8007 9912 5662 1354 −2080 −625 O ATOM 1328 CB LEU B 82 12.276 −10.803 24.961 1.00 66.50 C ANISOU 1328 CB LEU B 82 7986 10475 6805 1446 −2081 −103 C ATOM 1329 CG LEU B 82 13.649 −11.418 24.722 1.00 71.74 C ANISOU 1329 CG LEU B 82 8331 11249 7678 1515 −2261 126 C ATOM 1330 CD1 LEU B 82 14.531 −10.423 23.985 1.00 74.30 C ANISOU 1330 CD1 LEU B 82 8354 11514 8360 1282 −2484 −56 C ATOM 1331 CD2 LEU B 82 14.270 −11.826 26.055 1.00 76.78 C ANISOU 1331 CD2 LEU B 82 9014 12217 7941 1724 −2566 269 C ATOM 1332 N GLY B 83 9.162 −10.765 26.628 1.00 57.80 N ANISOU 1332 N GLY B 83 7708 9265 4987 1666 −1507 −202 N ATOM 1333 CA GLY B 83 7.969 −9.942 26.760 1.00 52.94 C ANISOU 1333 CA GLY B 83 7308 8497 4309 1588 −1308 −403 C ATOM 1334 C GLY B 83 7.471 −9.300 25.469 1.00 49.05 C ANISOU 1334 C GLY B 83 6645 7753 4239 1351 −1170 −532 C ATOM 1335 O GLY B 83 6.804 −8.269 25.501 1.00 43.27 O ANISOU 1335 O GLY B 83 6015 6912 3512 1244 −1106 −744 O ATOM 1336 N LYS B 84 7.776 −9.906 24.331 1.00 41.11 N ANISOU 1336 N LYS B 84 5397 6648 3573 1284 −1104 −393 N ATOM 1337 C LYS B 84 6.620 −10.405 22.248 1.00 40.66 C ANISOU 1337 C LYS B 84 5158 6226 4065 1101 −700 −291 C ATOM 1338 O LYS B 84 6.992 −11.577 22.219 1.00 39.22 O ANISOU 1338 O LYS B 84 4943 6063 3896 1215 −630 −87 O ATOM 1339 CA LYS B 84 7.350 −9.358 23.055 1.00 45.90 C ANISOU 1339 CA LYS B 84 5858 7048 4532 1083 −992 −487 C ATOM 1340 CB LYS B 84 8.524 −8.860 22.197 1.00 53.74 C ANISOU 1340 CB LYS B 84 6590 8049 5780 937 −1214 −567 C ATOM 1341 CG LYS B 84 9.560 −8.016 22.877 1.00 65.52 C ANISOU 1341 CG LYS B 84 8027 9698 7171 889 −1563 −745 C ATOM 1342 CD LYS B 84 10.240 −7.076 21.866 1.00 69.89 C ANISOU 1342 CD LYS B 84 8328 10143 8083 687 −1668 −879 C ATOM 1343 CE LYS B 84 11.012 −7.826 20.787 1.00 69.93 C ANISOU 1343 CE LYS B 84 8093 10097 8379 694 −1612 −673 C ATOM 1344 NZ LYS B 84 12.040 −8.704 21.395 1.00 73.12 N ANISOU 1344 NZ LYS B 84 8402 10686 8695 838 −1789 −497 N ATOM 1345 N ALA B 85 5.593 −9.945 21.572 1.00 33.88 N ANISOU 1345 N ALA B 85 4293 5201 3377 979 −539 −357 N ATOM 1346 CA ALA B 85 4.914 −10.732 20.581 1.00 33.81 C ANISOU 1346 CA ALA B 85 4215 5034 3596 924 −334 −238 C ATOM 1347 C ALA B 85 5.343 −10.155 19.238 1.00 33.43 C ANISOU 1347 C ALA B 85 3995 4924 3782 750 −429 −331 C ATOM 1348 O ALA B 85 5.006 −8.999 18.917 1.00 34.59 O ANISOU 1348 O ALA B 85 4106 5032 4005 640 −471 −465 O ATOM 1349 CB ALA B 85 3.397 −10.645 20.783 1.00 31.76 C ANISOU 1349 CB ALA B 85 4043 4651 3372 919 −106 −215 C ATOM 1350 N SER B 86 6.131 −10.940 18.503 1.00 34.85 N ANISOU 1350 N SER B 86 4084 5085 4070 749 −433 −242 N ATOM 1351 CA SER B 86 6.682 −10.528 17.217 1.00 33.15 C ANISOU 1351 CA SER B 86 3738 4810 4049 625 −483 −294 C ATOM 1352 C SER B 86 6.126 −11.391 16.148 1.00 31.01 C ANISOU 1352 C SER B 86 3489 4402 3892 567 −315 −230 C ATOM 1353 O SER B 86 6.130 −12.622 16.269 1.00 32.28 O ANISOU 1353 O SER B 86 3707 4513 4046 641 −186 −116 O ATOM 1354 CB SER B 86 8.216 −10.643 17.180 1.00 35.86 C ANISOU 1354 CB SER B 86 3957 5228 4442 677 −612 −249 C ATOM 1355 OG SER B 86 8.796 −9.895 18.223 1.00 40.58 O ANISOU 1355 OG SER B 86 4523 5970 4927 710 −828 −332 O ATOM 1356 N PHE B 87 5.726 −10.742 15.070 1.00 31.21 N ANISOU 1356 N PHE B 87 3473 4363 4024 436 −321 −303 N ATOM 1357 CA PHE B 87 5.101 −11.404 13.940 1.00 27.28 C ANISOU 1357 CA PHE B 87 3015 3752 3596 346 −217 −288 C ATOM 1358 C PHE B 87 5.822 −11.039 12.654 1.00 32.24 C ANISOU 1358 C PHE B 87 3606 4351 4291 290 −238 −315 C ATOM 1359 O PHE B 87 5.979 −9.865 12.330 1.00 34.68 O ANISOU 1359 O PHE B 87 3837 4693 4645 252 −317 −360 O ATOM 1360 CB PHE B 87 3.625 −10.991 13.834 1.00 25.29 C ANISOU 1360 CB PHE B 87 2761 3469 3378 253 −206 −318 C ATOM 1361 CG PHE B 87 2.820 −11.332 15.064 1.00 28.39 C ANISOU 1361 CG PHE B 87 3197 3857 3733 325 −120 −267 C ATOM 1362 CD1 PHE B 87 2.136 −12.538 15.156 1.00 29.94 C ANISOU 1362 CD1 PHE B 87 3439 3952 3984 321 20 −195 C ATOM 1363 CD2 PHE B 87 2.747 −10.437 16.121 1.00 30.93 C ANISOU 1363 CD2 PHE B 87 3529 4251 3971 398 −152 −295 C ATOM 1364 CE1 PHE B 87 1.368 −12.851 16.304 1.00 31.78 C ANISOU 1364 CE1 PHE B 87 3711 4159 4206 412 154 −110 C ATOM 1365 CE2 PHE B 87 2.011 −10.745 17.276 1.00 32.26 C ANISOU 1365 CE2 PHE B 87 3779 4408 4070 496 −28 −231 C ATOM 1366 CZ PHE B 87 1.315 −11.956 17.348 1.00 32.61 C ANISOU 1366 CZ PHE B 87 3850 4352 4188 513 138 −119 C ATOM 1367 N HIS B 88 6.279 −12.026 11.918 1.00 28.66 N ANISOU 1367 N HIS B 88 3223 3813 3852 298 −129 −279 N ATOM 1368 CA HIS B 88 7.042 −11.797 10.715 1.00 30.79 C ANISOU 1368 CA HIS B 88 3501 4038 4160 282 −90 −282 C ATOM 1369 C HIS B 88 6.187 −11.988 9.487 1.00 34.45 C ANISOU 1369 C HIS B 88 4088 4439 4562 165 −63 −345 C ATOM 1370 O HIS B 88 5.472 −12.936 9.382 1.00 31.09 O ANISOU 1370 O HIS B 88 3765 3945 4104 105 −14 −381 O ATOM 1371 CB HIS B 88 8.250 −12.701 10.701 1.00 31.36 C ANISOU 1371 CB HIS B 88 3585 4046 4286 393 42 −191 C ATOM 1372 CG HIS B 88 9.123 −12.589 9.498 1.00 37.07 C ANISOU 1372 CG HIS B 88 4334 4688 5064 411 156 −164 C ATOM 1373 ND1 HIS B 88 8.888 −13.313 8.359 1.00 39.72 N ANISOU 1373 ND1 HIS B 88 4870 4900 5324 368 309 −206 N ATOM 1374 CD2 HIS B 88 10.272 −11.918 9.282 1.00 35.70 C ANISOU 1374 CD2 HIS B 88 4022 4519 5023 477 168 −94 C ATOM 1375 CE1 HIS B 88 9.832 −13.072 7.483 1.00 42.00 C ANISOU 1375 CE1 HIS B 88 5172 5124 5660 430 436 −152 C ATOM 1376 NE2 HIS B 88 10.691 −12.234 8.020 1.00 39.53 N ANISOU 1376 NE2 HIS B 88 4634 4879 5506 498 365 −67 N ATOM 1377 N ILE B 89 6.258 −11.028 8.585 1.00 31.70 N ANISOU 1377 N ILE B 89 3721 4121 4204 133 −106 −356 N ATOM 1378 CA ILE B 89 5.730 −11.176 7.254 1.00 30.60 C ANISOU 1378 CA ILE B 89 3723 3952 3950 52 −99 −400 C ATOM 1379 C ILE B 89 6.807 −11.086 6.194 1.00 31.44 C ANISOU 1379 C ILE B 89 3921 4002 4024 124 37 −361 C ATOM 1380 O ILE B 89 7.513 −10.135 6.075 1.00 31.62 O ANISOU 1380 O ILE B 89 3834 4044 4135 192 60 −290 O ATOM 1381 CB ILE B 89 4.631 −10.161 6.916 1.00 34.20 C ANISOU 1381 CB ILE B 89 4109 4503 4382 −27 −250 −401 C ATOM 1382 CG1 ILE B 89 3.588 −10.098 8.013 1.00 35.29 C ANISOU 1382 CG1 ILE B 89 4134 4676 4598 −72 −334 −408 C ATOM 1383 CG2 ILE B 89 3.975 −10.522 5.603 1.00 35.86 C ANISOU 1383 CG2 ILE B 89 4479 4720 4427 −119 −301 −449 C ATOM 1384 CD1 ILE B 89 2.793 −8.834 8.010 1.00 36.18 C ANISOU 1384 CD1 ILE B 89 4112 4865 4768 −94 −430 −361 C ATOM 1385 O PRO B 90 6.262 −11.581 2.730 1.00 37.74 O ANISOU 1385 O PRO B 90 5291 4752 4295 38 122 −478 O ATOM 1386 N PRO B 90 6.858 −12.201 5.391 1.00 33.41 N ANISOU 1386 N PRO B 90 4399 4147 4150 100 159 −420 N ATOM 1387 CA PRO B 90 7.860 −12.159 4.332 1.00 36.58 C ANISOU 1387 CA PRO B 90 4932 4469 4496 192 346 −374 C ATOM 1388 C PRO B 90 7.382 −11.436 3.079 1.00 38.46 C ANISOU 1388 C PRO B 90 5296 4775 4540 161 289 −386 C ATOM 1389 CB PRO B 90 8.115 −13.622 4.069 1.00 38.28 C ANISOU 1389 CB PRO B 90 5368 4524 4653 194 534 −441 C ATOM 1390 CG PRO B 90 6.803 −14.214 4.176 1.00 39.61 C ANISOU 1390 CG PRO B 90 5614 4707 4728 28 380 −584 C ATOM 1391 CD PRO B 90 6.176 −13.565 5.324 1.00 32.57 C ANISOU 1391 CD PRO B 90 4465 3944 3968 1 190 −535 C ATOM 1392 O GLN B 91 5.747 −10.014 0.390 1.00 37.38 O ANISOU 1392 O GLN B 91 5459 4900 3845 91 24 −371 O ATOM 1393 N GLN B 91 8.237 −10.663 2.439 1.00 37.21 N ANISOU 1393 N GLN B 91 5130 4599 4409 280 427 −270 N ATOM 1394 CA GLN B 91 7.973 −10.168 1.108 1.00 37.62 C ANISOU 1394 CA GLN B 91 5371 4697 4225 302 445 −245 C ATOM 1395 C GLN B 91 6.620 −9.500 1.003 1.00 37.27 C ANISOU 1395 C GLN B 91 5263 4826 4071 194 163 −266 C ATOM 1396 CB GLN B 91 8.170 −11.243 0.051 1.00 41.56 C ANISOU 1396 CB GLN B 91 6247 5092 4452 312 611 −342 C ATOM 1397 CG GLN B 91 9.581 −11.768 0.003 1.00 50.35 C ANISOU 1397 CG GLN B 91 7413 6010 5706 463 961 −262 C ATOM 1398 CD GLN B 91 9.836 −12.792 −1.076 1.00 63.63 C ANISOU 1398 CD GLN B 91 9513 7546 7117 496 1198 −361 C ATOM 1399 OE1 GLN B 91 8.967 −13.177 −1.807 1.00 69.50 O ANISOU 1399 OE1 GLN B 91 10533 8340 7533 383 1069 −528 O ATOM 1400 NE2 GLN B 91 11.053 −13.224 −1.167 1.00 68.09 N ANISOU 1400 NE2 GLN B 91 10119 7920 7832 650 1549 −258 N ATOM 1401 N VAL B 92 6.439 −8.404 1.708 1.00 35.54 N ANISOU 1401 N VAL B 92 4766 4674 4064 206 74 −174 N ATOM 1402 CA VAL B 92 5.139 −7.812 1.852 1.00 34.02 C ANISOU 1402 CA VAL B 92 4458 4618 3849 117 −161 −166 C ATOM 1403 C VAL B 92 4.561 −7.375 0.522 1.00 35.12 C ANISOU 1403 C VAL B 92 4743 4873 3729 136 −239 −93 C ATOM 1404 O VAL B 92 5.243 −6.929 −0.328 1.00 33.80 O ANISOU 1404 O VAL B 92 4686 4686 3471 263 −78 12 O ATOM 1405 CB VAL B 92 5.149 −6.613 2.800 1.00 34.52 C ANISOU 1405 CB VAL B 92 4230 4693 4194 150 −177 −79 C ATOM 1406 CG1 VAL B 92 5.715 −6.978 4.144 1.00 35.55 C ANISOU 1406 CG1 VAL B 92 4236 4749 4523 140 −145 −152 C ATOM 1407 CG2 VAL B 92 5.943 −5.496 2.215 1.00 38.30 C ANISOU 1407 CG2 VAL B 92 4653 5132 4767 279 −14 70 C ATOM 1408 N GLN B 93 3.267 −7.530 0.392 1.00 36.05 N ANISOU 1408 N GLN B 93 4844 5115 3736 13 −492 −135 N ATOM 1409 CA GLN B 93 2.515 −7.217 −0.816 1.00 36.76 C ANISOU 1409 CA GLN B 93 5055 5367 3545 10 −659 −67 C ATOM 1410 C GLN B 93 1.576 −6.059 −0.492 1.00 38.51 C ANISOU 1410 C GLN B 93 4982 5707 3942 21 −803 109 C ATOM 1411 O GLN B 93 1.367 −5.724 0.689 1.00 37.05 O ANISOU 1411 O GLN B 93 4551 5463 4063 −6 −784 117 O ATOM 1412 CB GLN B 93 1.721 −8.447 −1.287 1.00 39.53 C ANISOU 1412 CB GLN B 93 5606 5766 3650 −171 −880 −268 C ATOM 1413 CG GLN B 93 2.574 −9.701 −1.673 1.00 48.34 C ANISOU 1413 CG GLN B 93 7058 6723 4584 −188 −700 −464 C ATOM 1414 CD GLN B 93 1.739 −10.982 −1.845 1.00 47.61 C ANISOU 1414 CD GLN B 93 7120 6614 4357 −412 −902 −712 C ATOM 1415 OE1 GLN B 93 0.552 −10.924 −2.161 1.00 44.52 O ANISOU 1415 OE1 GLN B 93 6657 6375 3883 −552 −1225 −739 O ATOM 1416 NE2 GLN B 93 2.356 −12.143 −1.601 1.00 46.87 N ANISOU 1416 NE2 GLN B 93 7204 6315 4288 −450 −706 −883 N ATOM 1417 N VAL B 94 1.024 −5.438 −1.530 1.00 37.85 N ANISOU 1417 N VAL B 94 4938 5788 3656 79 −927 263 N ATOM 1418 CA VAL B 94 −0.031 −4.450 −1.384 1.00 42.05 C ANISOU 1418 CA VAL B 94 5193 6444 4339 94 −1078 461 C ATOM 1419 C VAL B 94 −1.129 −4.946 −0.416 1.00 42.32 C ANISOU 1419 C VAL B 94 5012 6482 4585 −84 −1275 368 C ATOM 1420 O VAL B 94 −1.591 −4.191 0.425 1.00 39.68 O ANISOU 1420 O VAL B 94 4407 6114 4555 −58 −1231 482 O ATOM 1421 CB VAL B 94 −0.653 −4.094 −2.768 1.00 45.84 C ANISOU 1421 CB VAL B 94 5783 7152 4481 157 −1276 629 C ATOM 1422 CG1 VAL B 94 −1.864 −3.240 −2.599 1.00 44.44 C ANISOU 1422 CG1 VAL B 94 5285 7109 4489 164 −1458 853 C ATOM 1423 CG2 VAL B 94 0.372 −3.384 −3.650 1.00 43.42 C ANISOU 1423 CG2 VAL B 94 5660 6826 4013 384 −1010 796 C ATOM 1424 N ARG B 95 −1.523 −6.215 −0.516 1.00 38.35 N ANISOU 1424 N ARG B 95 4638 5989 3946 −259 −1450 160 N ATOM 1425 CA ARG B 95 −2.574 −6.735 0.361 1.00 42.00 C ANISOU 1425 CA ARG B 95 4885 6428 4647 −422 −1601 95 C ATOM 1426 C ARG B 95 −2.225 −6.737 1.860 1.00 40.15 C ANISOU 1426 C ARG B 95 4510 6014 4732 −399 −1374 53 C ATOM 1427 O ARG B 95 −3.117 −6.889 2.702 1.00 43.99 O ANISOU 1427 O ARG B 95 4790 6469 5456 −479 −1427 67 O ATOM 1428 CB ARG B 95 −2.953 −8.163 −0.031 1.00 40.54 C ANISOU 1428 CB ARG B 95 4875 6235 4294 −628 −1791 −145 C ATOM 1429 CG ARG B 95 −1.852 −9.233 0.131 1.00 38.83 C ANISOU 1429 CG ARG B 95 4942 5834 3979 −644 −1575 −372 C ATOM 1430 CD ARG B 95 −2.483 −10.588 −0.172 1.00 46.45 C ANISOU 1430 CD ARG B 95 6034 6757 4858 −875 −1763 −609 C ATOM 1431 NE ARG B 95 −1.572 −11.724 −0.327 1.00 50.98 N ANISOU 1431 NE ARG B 95 6929 7151 5292 −904 −1570 −832 N ATOM 1432 CZ ARG B 95 −1.718 −12.889 0.308 1.00 53.62 C ANISOU 1432 CZ ARG B 95 7276 7302 5793 −1040 −1504 −1002 C ATOM 1433 NH1 ARG B 95 −0.882 −13.893 0.075 1.00 50.51 N ANISOU 1433 NH1 ARG B 95 7183 6731 5277 −1046 −1299 −1182 N ATOM 1434 NH2 ARG B 95 −2.719 −13.054 1.167 1.00 57.43 N ANISOU 1434 NH2 ARG B 95 7470 7760 6591 −1155 −1608 −970 N ATOM 1435 N ASP B 96 −0.944 −6.609 2.195 1.00 35.98 N ANISOU 1435 N ASP B 96 4093 5370 4207 −289 −1129 8 N ATOM 1436 CA ASP B 96 −0.544 −6.602 3.624 1.00 36.54 C ANISOU 1436 CA ASP B 96 4055 5305 4525 −261 −957 −40 C ATOM 1437 C ASP B 96 −0.744 −5.239 4.281 1.00 40.24 C ANISOU 1437 C ASP B 96 4303 5763 5223 −164 −869 108 C ATOM 1438 O ASP B 96 −0.668 −5.109 5.517 1.00 36.55 O ANISOU 1438 O ASP B 96 3748 5205 4935 −149 −763 66 O ATOM 1439 CB ASP B 96 0.928 −7.027 3.778 1.00 32.01 C ANISOU 1439 CB ASP B 96 3647 4620 3894 −191 −765 −139 C ATOM 1440 CG ASP B 96 1.187 −8.461 3.290 1.00 37.69 C ANISOU 1440 CG ASP B 96 4602 5290 4427 −274 −775 −296 C ATOM 1441 OD1 ASP B 96 0.476 −9.407 3.724 1.00 35.26 O ANISOU 1441 OD1 ASP B 96 4287 4946 4165 −398 −853 −394 O ATOM 1442 OD2 ASP B 96 2.091 −8.643 2.443 1.00 38.06 O ANISOU 1442 OD2 ASP B 96 4850 5309 4301 −209 −670 −316 O ATOM 1443 N GLU B 97 −0.944 −4.219 3.455 1.00 43.03 N ANISOU 1443 N GLU B 97 4596 6198 5554 −86 −890 281 N ATOM 1444 CA GLU B 97 −1.061 −2.847 3.944 1.00 41.46 C ANISOU 1444 CA GLU B 97 4207 5950 5595 17 −755 426 C ATOM 1445 C GLU B 97 −2.360 −2.700 4.709 1.00 36.02 C ANISOU 1445 C GLU B 97 3315 5263 5109 −30 −810 494 C ATOM 1446 O GLU B 97 −3.407 −3.174 4.270 1.00 38.79 O ANISOU 1446 O GLU B 97 3593 5720 5424 −111 −1006 558 O ATOM 1447 CB GLU B 97 −1.015 −1.802 2.794 1.00 43.33 C ANISOU 1447 CB GLU B 97 4422 6263 5779 139 −728 646 C ATOM 1448 CG GLU B 97 −0.911 −0.348 3.330 1.00 57.97 C ANISOU 1448 CG GLU B 97 6096 7996 7933 251 −511 777 C ATOM 1449 CD GLU B 97 −0.720 0.742 2.260 1.00 59.34 C ANISOU 1449 CD GLU B 97 6241 8199 8106 403 −405 1026 C ATOM 1450 OE1 GLU B 97 0.391 0.848 1.670 1.00 55.03 O ANISOU 1450 OE1 GLU B 97 5828 7606 7474 475 −275 1022 O ATOM 1451 OE2 GLU B 97 −1.679 1.523 2.039 1.00 62.85 O ANISOU 1451 OE2 GLU B 97 6514 8698 8669 471 −418 1257 O ATOM 1452 N GLY B 98 −2.291 −2.059 5.869 1.00 42.74 N ANISOU 1452 N GLY B 98 5399 7196 3643 28 −802 992 N ATOM 1453 CA GLY B 98 −3.497 −1.734 6.603 1.00 40.83 C ANISOU 1453 CA GLY B 98 4890 7044 3580 220 −1011 1094 C ATOM 1454 C GLY B 98 −3.244 −1.824 8.103 1.00 39.89 C ANISOU 1454 C GLY B 98 4757 6465 3934 312 −878 888 C ATOM 1455 O GLY B 98 −2.102 −1.907 8.561 1.00 38.24 O ANISOU 1455 O GLY B 98 4711 5897 3920 280 −674 756 O ATOM 1456 N GLN B 99 −4.341 −1.837 8.848 1.00 39.23 N ANISOU 1456 N GLN B 99 4445 6464 3996 412 −1000 865 N ATOM 1457 C GLN B 99 −4.461 −3.303 10.792 1.00 34.54 C ANISOU 1457 C GLN B 99 3822 5575 3727 257 −826 343 C ATOM 1458 O GLN B 99 −5.124 −4.128 10.161 1.00 37.11 O ANISOU 1458 O GLN B 99 4057 6225 3818 38 −902 212 O ATOM 1459 CA GLN B 99 −4.321 −1.868 10.293 1.00 40.04 C ANISOU 1459 CA GLN B 99 4522 6229 4462 500 −889 696 C ATOM 1460 CB GLN B 99 −5.458 −0.990 10.841 1.00 46.09 C ANISOU 1460 CB GLN B 99 5052 7017 5444 770 −973 888 C ATOM 1461 CG GLN B 99 −5.293 −0.610 12.270 1.00 53.11 C ANISOU 1461 CG GLN B 99 5973 7526 6680 884 −807 749 C ATOM 1462 CD GLN B 99 −6.473 0.184 12.768 1.00 62.24 C ANISOU 1462 CD GLN B 99 6894 8682 8072 1143 −812 895 C ATOM 1463 OE1 GLN B 99 −7.618 −0.141 12.465 1.00 63.39 O ANISOU 1463 OE1 GLN B 99 6767 9183 8136 1165 −964 966 O ATOM 1464 NE2 GLN B 99 −6.202 1.235 13.536 1.00 66.04 N ANISOU 1464 NE2 GLN B 99 7455 8769 8868 1322 −615 912 N ATOM 1465 N TYR B 100 −3.827 −3.578 11.926 1.00 31.25 N ANISOU 1465 N TYR B 100 3498 4841 3535 283 −671 201 N ATOM 1466 CA TYR B 100 −3.766 −4.904 12.533 1.00 31.65 C ANISOU 1466 CA TYR B 100 3590 4824 3611 121 −534 −41 C ATOM 1467 C TYR B 100 −4.054 −4.734 14.015 1.00 34.48 C ANISOU 1467 C TYR B 100 3892 5032 4177 259 −489 −62 C ATOM 1468 O TYR B 100 −3.684 −3.709 14.576 1.00 32.70 O ANISOU 1468 O TYR B 100 3680 4666 4077 426 −502 23 O ATOM 1469 CB TYR B 100 −2.371 −5.534 12.374 1.00 29.13 C ANISOU 1469 CB TYR B 100 3465 4298 3306 47 −352 −115 C ATOM 1470 CG TYR B 100 −1.989 −5.952 10.938 1.00 29.04 C ANISOU 1470 CG TYR B 100 3561 4408 3065 −148 −291 −178 C ATOM 1471 CD1 TYR B 100 −2.038 −7.280 10.549 1.00 26.45 C ANISOU 1472 CD1 TYR B 100 3309 4079 2662 −391 −100 −424 C ATOM 1472 CD2 TYR B 100 −1.535 −5.013 10.023 1.00 29.08 C ANISOU 1472 CD2 TYR B 100 3618 4490 2939 −101 −361 −4 C ATOM 1473 CE1 TYR B 100 −1.684 −7.671 9.238 1.00 31.66 C ANISOU 1473 CE1 TYR B 100 4093 4863 3074 −618 8 −558 C ATOM 1474 CE2 TYR B 100 −1.164 −5.390 8.733 1.00 31.74 C ANISOU 1474 CE2 TYR B 100 4079 4978 3002 −298 −275 −71 C ATOM 1475 CZ TYR B 100 −1.245 −6.719 8.357 1.00 33.45 C ANISOU 1475 CZ TYR B 100 4369 5234 3108 −567 −96 −376 C ATOM 1476 OH TYR B 100 −0.902 −7.081 7.081 1.00 36.51 O ANISOU 1476 OH TYR B 100 4900 5788 3186 −805 31 −509 O ATOM 1477 N GLN B 101 −4.684 −5.715 14.649 1.00 36.18 N ANISOU 1477 N GLN B 101 4063 5265 4420 159 −392 −196 N ATOM 1478 C GLN B 101 −3.656 −6.753 16.637 1.00 31.33 C ANISOU 1478 C GLN B 101 3622 4343 3938 242 −128 −216 C ATOM 1479 O GLN B 101 −3.618 −7.931 16.239 1.00 33.85 O ANISOU 1479 O GLN B 101 4007 4596 4258 100 33 −283 O ATOM 1480 CA GLN B 101 −4.710 −5.780 16.126 1.00 32.90 C ANISOU 1480 CA GLN B 101 3661 4713 4126 263 −290 −212 C ATOM 1481 CB GLN B 101 −6.098 −6.212 16.648 1.00 29.75 C ANISOU 1481 CB GLN B 101 3103 4429 3771 198 −231 −294 C ATOM 1482 CG GLN B 101 −7.218 −5.282 16.242 1.00 35.27 C ANISOU 1482 CG GLN B 101 3556 5336 4511 280 −385 −238 C ATOM 1483 CD GLN B 101 −8.606 −5.895 16.366 1.00 43.66 C ANISOU 1483 CD GLN B 101 4374 6601 5613 142 −342 −345 C ATOM 1484 OE1 GLN B 101 −8.820 −7.073 16.071 1.00 47.85 O ANISOU 1484 OE1 GLN B 101 4912 7182 6085 −126 −243 −502 O ATOM 1485 NE2 GLN B 101 −9.554 −5.085 16.807 1.00 41.56 N ANISOU 1485 NE2 GLN B 101 3875 6427 5489 311 −366 −282 N ATOM 1486 N CYS B 102 −2.806 −6.273 17.537 1.00 28.72 N ANISOU 1486 N CYS B 102 3336 3950 3627 381 −147 −145 N ATOM 1487 CA CYS B 102 −1.849 −7.136 18.208 1.00 30.40 C ANISOU 1487 CA CYS B 102 3625 4084 3840 434 −31 −59 C ATOM 1488 C CYS B 102 −2.483 −7.620 19.485 1.00 35.08 C ANISOU 1488 C CYS B 102 4225 4714 4390 473 69 −20 C ATOM 1489 O CYS B 102 −2.691 −6.804 20.371 1.00 35.21 O ANISOU 1489 O CYS B 102 4207 4840 4330 530 −10 −52 O ATOM 1490 CB CYS B 102 −0.567 −6.361 18.511 1.00 31.66 C ANISOU 1490 CB CYS B 102 3762 4278 3989 526 −147 −4 C ATOM 1491 SG CYS B 102 0.908 −7.387 18.669 1.00 52.31 S ANISOU 1491 SG CYS B 102 6371 6851 6655 627 −45 174 S ATOM 1492 N ILE B 103 −2.786 −8.919 19.595 1.00 33.75 N ANISOU 1492 N ILE B 103 4122 4429 4274 426 297 33 N ATOM 1493 CA ILE B 103 −3.660 −9.415 20.674 1.00 34.24 C ANISOU 1493 CA ILE B 103 4202 4506 4302 423 456 77 C ATOM 1494 C ILE B 103 −2.896 −10.420 21.490 1.00 38.10 C ANISOU 1494 C ILE B 103 4799 4905 4774 566 638 347 C ATOM 1495 O ILE B 103 −2.285 −11.339 20.955 1.00 38.66 O ANISOU 1495 O ILE B 103 4936 4761 4994 590 814 446 O ATOM 1496 CB ILE B 103 −4.962 −10.076 20.135 1.00 37.37 C ANISOU 1496 CB ILE B 103 4555 4831 4813 202 631 −87 C ATOM 1497 CG1 ILE B 103 −5.729 −9.100 19.243 1.00 38.13 C ANISOU 1497 CG1 ILE B 103 4476 5105 4906 109 407 −271 C ATOM 1498 CG2 ILE B 103 −5.864 −10.591 21.266 1.00 39.83 C ANISOU 1498 CG2 ILE B 103 4878 5132 5121 177 859 −39 C ATOM 1499 CD1 ILE B 103 −6.847 −9.744 18.430 1.00 40.86 C ANISOU 1499 CD1 ILE B 103 4699 5507 5320 −160 495 −461 C ATOM 1500 N ILE B 104 −2.876 −10.223 22.795 1.00 34.98 N ANISOU 1500 N ILE B 104 4418 4687 4185 682 613 491 N ATOM 1501 CA ILE B 104 −2.132 −11.140 23.620 1.00 36.61 C ANISOU 1501 CA ILE B 104 4699 4890 4323 874 750 852 C ATOM 1502 C ILE B 104 −3.049 −11.596 24.749 1.00 38.22 C ANISOU 1502 C ILE B 104 4995 5137 4390 867 969 972 C ATOM 1503 O ILE B 104 −3.690 −10.777 25.418 1.00 38.53 O ANISOU 1503 O ILE B 104 5008 5401 4229 799 877 813 O ATOM 1504 CB ILE B 104 −0.826 −10.487 24.135 1.00 38.06 C ANISOU 1504 CB ILE B 104 4778 5385 4297 1038 456 990 C ATOM 1505 CGI ILE B 104 −0.063 −9.851 22.953 1.00 38.30 C ANISOU 1505 CGI ILE B 104 4708 5354 4489 988 278 811 C ATOM 1506 CG2 ILE B 104 0.029 −11.508 24.881 1.00 37.06 C ANISOU 1506 CG2 ILE B 104 4657 5319 4106 1303 563 1465 C ATOM 1507 CD1 ILE B 104 1.276 −9.246 23.299 1.00 44.53 C ANISOU 1507 CD1 ILE B 104 5339 6433 5148 1090 18 898 C ATOM 1508 N ILE B 105 −3.131 −12.915 24.894 1.00 39.09 N ANISOU 1508 N ILE B 105 5228 4974 4652 927 1328 1240 N ATOM 1509 CA ILE B 105 −3.963 −13.578 25.867 1.00 43.63 C ANISOU 1509 CA ILE B 105 5924 5501 5153 915 1645 1419 C ATOM 1510 C ILE B 105 −3.053 −14.276 26.871 1.00 47.53 C ANISOU 1510 C ILE B 105 6506 6090 5464 1236 1733 1983 C ATOM 1511 O ILE B 105 −2.060 −14.924 26.481 1.00 46.72 O ANISOU 1511 O ILE B 105 6395 5808 5549 1444 1794 2260 O ATOM 1512 CB ILE B 105 −4.883 −14.630 25.228 1.00 48.68 C ANISOU 1512 CB ILE B 105 6643 5691 6160 693 2084 1298 C ATOM 1513 CG1 ILE B 105 −5.767 −14.013 24.149 1.00 51.06 C ANISOU 1513 CG1 ILE B 105 6790 6007 6603 382 1946 786 C ATOM 1514 CG2 ILE B 105 −5.727 −15.315 26.301 1.00 51.55 C ANISOU 1514 CG2 ILE B 105 7139 5978 6471 667 2474 1511 C ATOM 1515 CD1 ILE B 105 −6.645 −15.048 23.441 1.00 56.20 C ANISOU 1515 CD1 ILE B 105 7466 6306 7580 70 2343 578 C ATOM 1516 O TYR B 106 −4.196 −14.555 31.052 1.00 60.34 O ANISOU 1516 O TYR B 106 8479 8599 5850 1435 2087 2804 O ATOM 1517 N TYR B 106 −3.396 −14.143 28.146 1.00 48.76 N ANISOU 1517 N TYR B 106 6730 6551 5247 1290 1755 2172 N ATOM 1518 CA TYR B 106 −2.626 −14.729 29.242 1.00 56.60 C ANISOU 1518 CA TYR B 106 7788 7781 5938 1608 1792 2776 C ATOM 1519 C TYR B 106 −3.608 −15.297 30.250 1.00 59.64 C ANISOU 1519 C TYR B 106 8370 8137 6152 1570 2181 2993 C ATOM 1520 CB TYR B 106 −1.716 −13.671 29.879 1.00 59.27 C ANISOU 1520 CB TYR B 106 7966 8773 5783 1693 1275 2768 C ATOM 1521 CG TYR B 106 −0.729 −14.164 30.926 1.00 65.71 C ANISOU 1521 CG TYR B 106 8700 9952 6313 1961 1129 3252 C ATOM 1522 CD1 TYR B 106 0.158 −15.195 30.643 1.00 68.62 C ANISOU 1522 CD1 TYR B 106 8969 10069 7035 2227 1233 3613 C ATOM 1523 CD2 TYR B 106 −0.635 −13.547 32.169 1.00 69.13 C ANISOU 1523 CD2 TYR B 106 9104 10975 6186 1889 870 3215 C ATOM 1524 CE1 TYR B 106 1.080 −15.631 31.579 1.00 75.75 C ANISOU 1524 CE1 TYR B 106 9719 11324 7737 2455 1084 3997 C ATOM 1525 CE2 TYR B 106 0.299 −13.986 33.124 1.00 76.21 C ANISOU 1525 CE2 TYR B 106 9873 12235 6849 2075 691 3585 C ATOM 1526 CZ TYR B 106 1.151 −15.030 32.810 1.00 79.07 C ANISOU 1526 CZ TYR B 106 10106 12363 7573 2379 793 4004 C ATOM 1527 OH TYR B 106 2.091 −15.488 33.707 1.00 86.71 O ANISOU 1527 OH TYR B 106 10904 13718 8325 2600 639 4414 O ATOM 1528 O GLY B 107 −6.517 −17.060 29.267 1.00 65.57 O ANISOU 1528 O GLY B 107 9341 7677 7894 922 3346 2502 O ATOM 1529 N GLY B 107 −3.818 −16.608 30.194 1.00 62.02 N ANISOU 1529 N GLY B 107 8782 7944 6838 1627 2591 3225 N ATOM 1530 CA GLY B 107 −4.861 −17.221 31.004 1.00 64.59 C ANISOU 1530 CA GLY B 107 9263 8129 7149 1511 2959 3290 C ATOM 1531 C GLY B 107 −6.211 −16.799 30.443 1.00 65.16 C ANISOU 1531 C GLY B 107 9335 8024 7397 1117 3180 2789 C ATOM 1532 O VAL B 108 −9.096 −13.411 30.140 1.00 59.94 O ANISOU 1532 O VAL B 108 8195 8022 6559 389 2796 1233 O ATOM 1533 N VAL B 108 −7.020 −16.134 31.262 1.00 63.74 N ANISOU 1533 N VAL B 108 9165 8177 6877 976 3181 2633 N ATOM 1534 CA VAL B 108 −8.264 −15.567 30.764 1.00 60.51 C ANISOU 1534 CA VAL B 108 8638 7701 6652 641 3327 2116 C ATOM 1535 C VAL B 108 −8.163 −14.048 30.627 1.00 57.38 C ANISOU 1535 C VAL B 108 8051 7719 6031 605 2819 1686 C ATOM 1536 CB VAL B 108 −9.485 −15.931 31.653 1.00 66.32 C ANISOU 1536 CB VAL B 108 9432 8396 7370 456 3685 2073 C ATOM 1537 CGI VAL B 108 −9.923 −17.362 31.384 1.00 70.30 C ANISOU 1537 CGI VAL B 108 10020 8342 8347 347 4087 2182 C ATOM 1538 CG2 VAL B 108 −9.194 −15.701 33.143 1.00 68.15 C ANISOU 1538 CG2 VAL B 108 9811 9069 7015 619 3596 2371 C ATOM 1539 N ALA B 109 −7.027 −13.488 31.028 1.00 51.92 N ANISOU 1539 N ALA B 109 7375 7394 4959 815 2435 1841 N ATOM 1540 CA ALA B 109 −6.759 −12.069 30.868 1.00 47.80 C ANISOU 1540 CA ALA B 109 6703 7187 4273 764 2005 1433 C ATOM 1541 C ALA B 109 −6.228 −11.758 29.465 1.00 47.65 C ANISOU 1541 C ALA B 109 6523 6958 4623 754 1718 1220 C ATOM 1542 O ALA B 109 −5.648 −12.625 28.797 1.00 50.58 O ANISOU 1542 O ALA B 109 6918 7061 5241 844 1771 1447 O ATOM 1543 CB ALA B 109 −5.781 −11.604 31.904 1.00 50.21 C ANISOU 1543 CB ALA B 109 7068 8014 3997 904 1738 1621 C ATOM 1544 N TRP B 110 −6.409 −10.520 29.014 1.00 40.75 N ANISOU 1544 N TRP B 110 5503 6183 3796 653 1463 801 N ATOM 1545 CA TRP B 110 −5.962 −10.158 27.670 1.00 35.45 C ANISOU 1545 CA TRP B 110 4699 5341 3430 637 1214 627 C ATOM 1546 C TRP B 110 −5.938 −8.649 27.468 1.00 33.56 C ANISOU 1546 C TRP B 110 4343 5251 3159 591 948 271 C ATOM 1547 O TRP B 110 −6.520 −7.889 28.251 1.00 34.91 O ANISOU 1547 O TRP B 110 4517 5579 3168 539 1019 74 O ATOM 1548 CB TRP B 110 −6.876 −10.806 26.630 1.00 37.60 C ANISOU 1548 CB TRP B 110 4896 5279 4111 484 1415 507 C ATOM 1549 CG TRP B 110 −8.307 −10.389 26.811 1.00 36.45 C ANISOU 1549 CG TRP B 110 4623 5165 4061 331 1575 248 C ATOM 1550 CD1 TRP B 110 −9.220 −10.921 27.674 1.00 41.65 C ANISOU 1550 CD1 TRP B 110 5329 5816 4681 252 1936 305 C ATOM 1551 CD2 TRP B 110 −8.972 −9.323 26.131 1.00 35.59 C ANISOU 1551 CD2 TRP B 110 4289 5110 4125 273 1406 −65 C ATOM 1552 NE1 TRP B 110 −10.427 −10.269 27.556 1.00 41.88 N ANISOU 1552 NE1 TRP B 110 5138 5901 4875 134 2002 8 N ATOM 1553 CE2 TRP B 110 −10.306 −9.291 26.605 1.00 39.69 C ANISOU 1553 CE2 TRP B 110 4679 5663 4737 171 1671 −196 C ATOM 1554 CE3 TRP B 110 −8.583 −8.427 25.122 1.00 33.97 C ANISOU 1554 CE3 TRP B 110 3964 4914 4027 316 1088 −202 C ATOM 1555 CZ2 TRP B 110 −11.249 −8.363 26.138 1.00 38.06 C ANISOU 1555 CZ2 TRP B 110 4188 5524 4747 156 1604 −437 C ATOM 1556 CZ3 TRP B 110 −9.513 −7.513 24.665 1.00 35.12 C ANISOU 1556 CZ3 TRP B 110 3875 5109 4359 305 1028 −403 C ATOM 1557 CH2 TRP B 110 −10.833 −7.486 25.168 1.00 34.32 C ANISOU 1557 CH2 TRP B 110 3608 5061 4371 245 1273 −509 C ATOM 1558 N ASP B 111 −5.268 −8.223 26.403 1.00 34.63 N ANISOU 1558 N ASP B 111 4391 5293 3473 606 704 190 N ATOM 1559 CA ASP B 111 −5.205 −6.818 26.016 1.00 33.87 C ANISOU 1559 CA ASP B 111 4200 5229 3440 573 509 −99 C ATOM 1560 C ASP B 111 −4.785 −6.784 24.538 1.00 33.04 C ANISOU 1560 C ASP B 111 4014 4936 3602 574 351 −101 C ATOM 1561 O ASP B 111 −4.424 −7.808 23.980 1.00 34.78 O ANISOU 1561 O ASP B 111 4267 5039 3908 584 395 69 O ATOM 1562 CB ASP B 111 −4.225 −6.034 26.905 1.00 34.02 C ANISOU 1562 CB ASP B 111 4265 5522 3138 575 348 −173 C ATOM 1563 CG ASP B 111 −4.444 −4.517 26.845 1.00 36.61 C ANISOU 1563 CG ASP B 111 4546 5809 3555 498 313 −538 C ATOM 1564 OD1 ASP B 111 −3.551 −3.755 27.285 1.00 36.03 O ANISOU 1564 OD1 ASP B 111 4489 5904 3297 422 181 −695 O ATOM 1565 OD2 ASP B 111 −5.501 −4.071 26.361 1.00 35.08 O ANISOU 1565 OD2 ASP B 111 4278 5412 3639 509 440 −666 O ATOM 1566 N TYR B 112 −4.871 −5.625 23.909 1.00 35.61 N ANISOU 1566 N TYR B 112 4255 5211 4064 564 224 −286 N ATOM 1567 CA TYR B 112 −4.484 −5.480 22.509 1.00 32.86 C ANISOU 1567 CA TYR B 112 3851 4734 3900 560 84 −266 C ATOM 1568 C TYR B 112 −4.129 −4.035 22.174 1.00 32.50 C ANISOU 1568 C TYR B 112 3770 4640 3938 585 −36 −395 C ATOM 1569 O TYR B 112 −4.454 −3.114 22.942 1.00 30.73 O ANISOU 1569 O TYR B 112 3549 4426 3702 592 35 −557 O ATOM 1570 CB TYR B 112 −5.615 −5.973 21.578 1.00 33.54 C ANISOU 1570 CB TYR B 112 3829 4756 4157 494 146 −277 C ATOM 1571 CG TYR B 112 −6.837 −5.066 21.496 1.00 34.88 C ANISOU 1571 CG TYR B 112 3828 4961 4465 529 160 −386 C ATOM 1572 CD1 TYR B 112 −7.158 −4.385 20.311 1.00 32.29 C ANISOU 1572 CD1 TYR B 112 3357 4636 4275 570 15 −363 C ATOM 1573 CD2 TYR B 112 −7.649 −4.849 22.616 1.00 35.84 C ANISOU 1573 CD2 TYR B 112 3915 5126 4576 552 341 −473 C ATOM 1574 CE1 TYR B 112 −8.287 −3.538 20.242 1.00 34.35 C ANISOU 1574 CE1 TYR B 112 3405 4938 4710 680 38 −377 C ATOM 1575 CE2 TYR B 112 −8.743 −4.013 22.562 1.00 36.31 C ANISOU 1575 CE2 TYR B 112 3778 5191 4828 632 404 −553 C ATOM 1576 CZ TYR B 112 −9.078 −3.365 21.361 1.00 36.45 C ANISOU 1576 CZ TYR B 112 3611 5206 5034 719 245 −481 C ATOM 1577 OH TYR B 112 −10.201 −2.530 21.315 1.00 35.18 O ANISOU 1577 OH TYR B 112 3195 5059 5112 872 322 −480 O ATOM 1578 N LYS B 113 −3.441 −3.849 21.039 1.00 28.94 N ANISOU 1578 N LYS B 113 3311 4103 3583 583 −155 −334 N ATOM 1579 CA LYS B 113 −3.166 −2.526 20.496 1.00 26.59 C ANISOU 1579 CA LYS B 113 2995 3686 3421 607 −209 −396 C ATOM 1580 C LYS B 113 −3.337 −2.586 18.969 1.00 31.07 C ANISOU 1580 C LYS B 113 3521 4198 4086 624 −283 −259 C ATOM 1581 O LYS B 113 −3.412 −3.676 18.397 1.00 29.01 O ANISOU 1581 O LYS B 113 3261 4003 3757 562 −296 −195 O ATOM 1582 CB LYS B 113 −1.756 −2.070 20.860 1.00 28.04 C ANISOU 1582 CB LYS B 113 3227 3886 3541 539 −268 −467 C ATOM 1583 CG LYS B 113 −1.579 −1.710 22.400 1.00 32.02 C ANISOU 1583 CG LYS B 113 3757 4547 3862 467 −227 −666 C ATOM 1584 CD LYS B 113 −2.429 −0.535 22.774 1.00 34.30 C ANISOU 1584 CD LYS B 113 4066 4678 4288 467 −62 −880 C ATOM 1585 CE LYS B 113 −2.374 −0.238 24.298 1.00 35.99 C ANISOU 1585 CE LYS B 113 4339 5083 4255 340 29 −1150 C ATOM 1586 NZ LYS B 113 −3.056 −1.333 25.025 1.00 36.79 N ANISOU 1586 NZ LYS B 113 4455 5395 4128 392 66 −1031 N ATOM 1587 N TYR B 114 −3.385 −1.431 18.321 1.00 31.27 N ANISOU 1587 N TYR B 114 3528 4101 4254 693 −296 −215 N ATOM 1588 CA TYR B 114 −3.408 −1.389 16.859 1.00 30.07 C ANISOU 1588 CA TYR B 114 3354 3967 4102 708 −382 −39 C ATOM 1589 C TYR B 114 −1.996 −1.114 16.351 1.00 33.63 C ANISOU 1589 C TYR B 114 3918 4310 4549 641 −380 −14 C ATOM 1590 O TYR B 114 −1.247 −0.378 17.002 1.00 29.21 O ANISOU 1590 O TYR B 114 3399 3616 4082 614 −316 −120 O ATOM 1591 CB TYR B 114 −4.371 −0.313 16.372 1.00 33.29 C ANISOU 1591 CB TYR B 114 3652 4326 4668 881 −378 112 C ATOM 1592 CG TYR B 114 −5.850 −0.705 16.509 1.00 37.98 C ANISOU 1592 CG TYR B 114 4036 5118 5276 946 −410 133 C ATOM 1593 CD1 TYR B 114 −6.430 −1.596 15.617 1.00 40.03 C ANISOU 1593 CD1 TYR B 114 4174 5667 5369 848 −553 197 C ATOM 1594 CD2 TYR B 114 −6.656 −0.159 17.501 1.00 37.64 C ANISOU 1594 CD2 TYR B 114 3898 4988 5418 1069 −266 51 C ATOM 1595 CE1 TYR B 114 −7.775 −1.958 15.710 1.00 42.70 C ANISOU 1595 CE1 TYR B 114 4255 6236 5734 855 −587 188 C ATOM 1596 CE2 TYR B 114 −8.007 −0.528 17.628 1.00 40.31 C ANISOU 1596 CE2 TYR B 114 3988 5524 5805 1121 −268 69 C ATOM 1597 CZ TYR B 114 −8.558 −1.443 16.734 1.00 43.63 C ANISOU 1597 CZ TYR B 114 4245 6263 6069 1005 −445 141 C ATOM 1598 OH TYR B 114 −9.903 −1.819 16.804 1.00 47.57 O ANISOU 1598 OH TYR B 114 4431 7015 6630 1003 −457 132 O ATOM 1599 N LEU B 115 −1.647 −1.747 15.224 1.00 31.19 N ANISOU 1599 N LEU B 115 3646 4083 4124 572 −422 80 N ATOM 1600 CA LEU B 115 −0.421 −1.507 14.463 1.00 33.70 C ANISOU 1600 CA LEU B 115 4049 4313 4441 510 −378 135 C ATOM 1601 C LEU B 115 −0.811 −1.213 13.026 1.00 35.12 C ANISOU 1601 C LEU B 115 4259 4574 4510 523 −413 329 C ATOM 1602 O LEU B 115 −1.764 −1.810 12.523 1.00 32.02 O ANISOU 1602 O LEU B 115 3807 4405 3955 499 −506 356 O ATOM 1603 CB LEU B 115 0.497 −2.735 14.480 1.00 36.04 C ANISOU 1603 CB LEU B 115 4372 4655 4667 413 −327 60 C ATOM 1604 CG LEU B 115 1.133 −3.203 15.772 1.00 40.21 C ANISOU 1604 CG LEU B 115 4845 5193 5238 428 −315 −28 C ATOM 1605 CD1 LEU B 115 1.877 −4.523 15.615 1.00 35.56 C ANISOU 1605 CD1 LEU B 115 4259 4618 4634 416 −218 2 C ATOM 1606 CD2 LEU B 115 2.050 −2.102 16.264 1.00 44.19 C ANISOU 1606 CD2 LEU B 115 5303 5637 5850 399 −325 −90 C ATOM 1607 N THR B 116 −0.082 −0.333 12.349 1.00 36.33 N ANISOU 1607 N THR B 116 4495 4590 4719 533 −335 464 N ATOM 1608 CA THR B 116 −0.366 −0.074 10.942 1.00 37.35 C ANISOU 1608 CA THR B 116 4677 4856 4658 551 −365 711 C ATOM 1609 C THR B 116 0.857 −0.407 10.095 1.00 38.10 C ANISOU 1609 C THR B 116 4902 4932 4641 396 −232 696 C ATOM 1610 O THR B 116 1.973 −0.056 10.449 1.00 34.51 O ANISOU 1610 O THR B 116 4474 4255 4383 349 −89 623 O ATOM 1611 CB THR B 116 −0.786 1.391 10.692 1.00 44.84 C ANISOU 1611 CB THR B 116 5628 5641 5768 756 −321 1009 C ATOM 1612 OG1 THR B 116 −2.013 1.658 11.383 1.00 50.90 O ANISOU 1612 OG1 THR B 116 6240 6436 6662 931 −404 1033 O ATOM 1613 CG2 THR B 116 −1.028 1.639 9.181 1.00 40.61 C ANISOU 1613 CG2 THR B 116 5148 5331 4953 803 −373 1364 C ATOM 1614 N LEU B 117 0.625 −1.103 8.978 1.00 36.95 N ANISOU 1614 N LEU B 117 4814 5057 4168 286 −264 728 N ATOM 1615 CA LEU B 117 1.677 −1.385 8.033 1.00 35.28 C ANISOU 1615 CA LEU B 117 4743 4843 3817 137 −81 713 C ATOM 1616 C LEU B 117 1.396 −0.640 6.758 1.00 33.83 C ANISOU 1616 C LEU B 117 4661 4842 3350 162 −98 1032 C ATOM 1617 O LEU B 117 0.330 −0.776 6.187 1.00 38.44 O ANISOU 1617 O LEU B 117 5195 5783 3625 171 −295 1147 O ATOM 1618 CB LEU B 117 1.787 −2.875 7.759 1.00 35.26 C ANISOU 1618 CB LEU B 117 4775 4980 3642 −55 −6 435 C ATOM 1619 CG LEU B 117 2.755 −3.382 6.693 1.00 37.15 C ANISOU 1619 CG LEU B 117 5167 5236 3711 −233 250 349 C ATOM 1620 CD1 LEU B 117 4.210 −2.932 6.918 1.00 37.68 C ANISOU 1620 CD1 LEU B 117 5230 5007 4081 −192 476 382 C ATOM 1621 CD2 LEU B 117 2.638 −4.874 6.787 1.00 39.90 C ANISOU 1621 CD2 LEU B 117 5528 5608 4023 −386 368 29 C ATOM 1622 N ALYS B 118 2.356 0.171 6.333 0.51 35.23 N ANISOU 1622 N ALYS B 118 4956 4803 3627 168 111 1199 N ATOM 1623 CA ALYS B 118 2.270 0.879 5.061 0.51 41.08 C ANISOU 1623 CA ALYS B 118 5839 5699 4071 198 162 1573 C ATOM 1624 C ALYS B 118 3.351 0.347 4.119 0.51 44.17 C ANISOU 1624 C ALYS B 118 6399 6147 4238 −35 422 1462 C ATOM 1625 O ALYS B 118 4.494 0.128 4.517 0.51 43.43 O ANISOU 1625 O ALYS B 118 6294 5774 4434 −128 653 1243 O ATOM 1626 CB ALYS B 118 2.416 2.392 5.262 0.51 43.62 C ANISOU 1626 CB ALYS B 118 6195 5654 4725 403 292 1920 C ATOM 1627 CG ALYS B 118 1.184 3.054 5.870 0.51 44.10 C ANISOU 1627 CG ALYS B 118 6114 5684 4959 680 101 2122 C ATOM 1628 N BLYS B 118 2.377 0.154 6.339 0.49 35.20 N ANISOU 1628 N BLYS B 118 4953 4797 3626 165 114 1192 N ATOM 1629 CA BLYS B 118 2.341 0.913 5.091 0.49 41.26 C ANISOU 1629 CA BLYS B 118 5865 5695 4119 198 178 1570 C ATOM 1630 C BLYS B 118 3.371 0.329 4.119 0.49 44.12 C ANISOU 1630 C BLYS B 118 6393 6139 4232 −39 427 1455 C ATOM 1631 O BLYS B 118 4.509 0.060 4.501 0.49 43.29 O ANISOU 1631 O BLYS B 118 6277 5765 4405 −138 656 1227 O ATOM 1632 CB BLYS B 118 2.632 2.398 5.356 0.49 43.61 C ANISOU 1632 CB BLYS B 118 6199 5589 4781 380 335 1876 C ATOM 1633 CG BLYS B 118 2.546 3.294 4.131 0.49 47.86 C ANISOU 1633 CG BLYS B 118 6903 6203 5081 483 444 2389 C ATOM 1634 N VAL B 119 2.968 0.118 2.873 1.00 45.61 N ANISOU 1634 N VAL B 119 6707 6742 3879 −135 386 1603 N ATOM 1635 CA VAL B 119 3.862 −0.469 1.880 1.00 51.10 C ANISOU 1635 CA VAL B 119 7590 7546 4278 −387 673 1452 C ATOM 1636 C VAL B 119 4.182 0.580 0.832 1.00 54.41 C ANISOU 1636 C VAL B 119 8200 8020 4451 −343 836 1914 C ATOM 1637 O VAL B 119 3.282 0.984 0.111 1.00 59.47 O ANISOU 1637 O VAL B 119 8880 9065 4651 −255 621 2278 O ATOM 1638 CB VAL B 119 3.201 −1.712 1.242 1.00 52.68 C ANISOU 1638 CB VAL B 119 7824 8227 3964 −636 564 1144 C ATOM 1639 CG1 VAL B 119 4.074 −2.326 0.208 1.00 57.21 C ANISOU 1639 CG1 VAL B 119 8619 8899 4221 −916 925 931 C ATOM 1640 CG2 VAL B 119 2.873 −2.739 2.334 1.00 48.97 C ANISOU 1640 CG2 VAL B 119 7186 7613 3806 −666 474 734 C ATOM 1641 N LYS B 120 5.404 1.102 0.809 1.00 57.03 N ANISOU 1641 N LYS B 120 8615 7960 5094 −377 1205 1956 N ATOM 1642 C LYS B 120 6.414 1.226 −1.478 1.00 66.76 C ANISOU 1642 C LYS B 120 10283 9533 5550 −672 1734 2224 C ATOM 1643 O LYS B 120 6.823 0.105 −1.364 1.00 66.57 O ANISOU 1643 O LYS B 120 10220 9531 5543 −866 1845 1734 O ATOM 1644 CA LYS B 120 5.932 1.965 −0.264 1.00 64.53 C ANISOU 1644 CA LYS B 120 9793 8905 5822 −396 1494 2364 C ATOM 1645 CB LYS B 120 7.161 2.723 0.183 1.00 69.57 C ANISOU 1645 CB LYS B 120 10412 8975 7048 −413 1872 2372 C ATOM 1646 CG LYS B 120 7.195 3.214 1.594 1.00 67.42 C ANISOU 1646 CG LYS B 120 9915 8276 7426 −286 1772 2241 C ATOM 1647 CD LYS B 120 8.585 3.689 1.930 1.00 69.90 C ANISOU 1647 CD LYS B 120 10160 8159 8240 −439 2159 2098 C ATOM 1648 CE LYS B 120 9.624 2.639 1.621 1.00 71.34 C ANISOU 1648 CE LYS B 120 10279 8451 8374 −655 2382 1744 C ATOM 1649 NZ LYS B 120 10.830 2.828 2.455 1.00 72.38 N ANISOU 1649 NZ LYS B 120 10146 8260 9096 −770 2583 1482 N ATOM 1650 O ALA B 121 8.913 2.828 −3.416 1.00 77.21 O ANISOU 1650 O ALA B 121 11983 10459 6895 −908 2779 2744 O ATOM 1651 N ALA B 121 6.461 1.886 −2.630 1.00 69.76 N ANISOU 1651 N ALA B 121 10901 10137 5469 −684 1889 2666 N ATOM 1652 CA ALA B 121 7.093 1.309 −3.806 1.00 75.66 C ANISOU 1652 CA ALA B 121 11823 11181 5741 −951 2189 2499 C ATOM 1653 C ALA B 121 8.553 1.752 −3.897 1.00 76.62 C ANISOU 1653 C ALA B 121 11952 10834 6325 −1041 2680 2465 C ATOM 1654 CB ALA B 121 6.347 1.704 −5.038 1.00 84.92 C ANISOU 1654 CB ALA B 121 13224 12772 6271 −818 2038 2848 C TER HETATM 1655 MG MG C 1 −12.423 21.789 37.851 1.00 10.21 Mg TER HETATM 1656 O HOH S 1 −11.900 7.714 39.918 1.00 36.82 O HETATM 1657 O HOH S 2 5.380 −1.733 18.078 1.00 42.03 O HETATM 1658 O HOH S 3 −3.752 −1.172 27.706 1.00 30.61 O HETATM 1659 O HOH S 4 −10.403 9.535 25.067 1.00 36.60 O HETATM 1660 O HOH S 5 −10.109 8.110 32.307 1.00 33.09 O HETATM 1661 O HOH S 6 −8.230 −8.835 30.592 1.00 36.54 O HETATM 1662 O HOH S 7 −6.450 −3.897 7.581 1.00 43.31 O HETATM 1663 O HOH S 8 −11.226 17.652 37.643 1.00 41.73 O HETATM 1664 O HOH S 9 11.006 −5.310 10.589 1.00 41.18 O HETATM 1665 O HOH S 10 6.936 −13.148 20.077 1.00 42.17 O HETATM 1666 O HOH S 11 −7.618 7.364 31.834 1.00 35.02 O HETATM 1667 O HOH S 12 −23.200 −0.301 40.120 1.00 39.37 O HETATM 1668 O HOH S 13 −10.349 11.123 41.000 1.00 42.33 O HETATM 1669 O HOH S 14 −8.911 −19.801 17.605 1.00 54.02 O HETATM 1670 O HOH S 15 −12.611 15.391 40.612 1.00 39.82 O HETATM 1671 O HOH 5 16 −18.344 3.513 17.529 1.00 40.36 O HETATM 1672 O HOH S 17 −14.904 13.729 44.439 1.00 43.93 O HETATM 1673 O HOH S 18 −7.828 10.805 33.107 1.00 47.89 O HETATM 1674 O HOH S 19 −23.034 14.524 38.000 1.00 40.79 O HETATM 1675 O HOH S 20 −23.090 8.084 36.258 1.00 44.88 O HETATM 1676 O HOH S 21 −22.806 9.951 40.206 1.00 54.76 O HETATM 1677 O HOH S 22 0.813 1.581 23.702 1.00 57.37 O HETATM 1678 O HOH S 23 11.708 −14.287 3.627 1.00 52.01 O HETATM 1679 O HOH S 24 −14.338 −11.481 26.493 1.00 44.42 O HETATM 1680 O HOH S 25 9.131 −3.175 16.236 1.00 42.13 O HETATM 1681 O HOH S 26 −1.105 2.064 14.167 1.00 60.92 O HETATM 1682 O HOH S 27 11.909 −5.197 −1.529 1.00 51.43 O HETATM 1683 O HOH S 28 13.293 −15.900 14.555 1.00 39.68 O HETATM 1684 O HOH S 29 7.650 −19.522 16.191 1.00 43.67 O HETATM 1685 O HOH S 30 1.348 −17.126 14.225 1.00 42.61 O HETATM 1686 O HOH S 31 −14.905 23.868 39.927 1.00 45.13 O HETATM 1687 O HOH S 32 −10.080 14.900 28.889 1.00 37.23 O HETATM 1688 O HOH S 33 −8.426 −10.736 11.463 1.00 55.62 O HETATM 1689 O HOH S 34 −18.847 0.126 38.624 1.00 43.58 O HETATM 1690 O HOH S 35 −15.672 0.253 18.397 1.00 44.41 O HETATM 1691 O HOH S 36 13.643 −7.930 3.769 1.00 42.90 O HETATM 1692 O HOH S 37 −10.654 −8.957 15.970 1.00 47.50 O HETATM 1693 O HOH S 38 −21.135 −14.442 22.657 1.00 54.40 O HETATM 1694 O HOH S 39 −21.281 20.925 35.993 1.00 50.08 O HETATM 1695 O HOH S 40 −13.418 17.631 41.547 1.00 50.58 O HETATM 1696 O HOH S 41 −27.329 5.575 24.313 1.00 59.43 O HETATM 1697 O HOH S 42 −14.776 −4.993 16.979 1.00 49.61 O HETATM 1698 O HOH S 43 −0.676 −9.652 6.203 1.00 43.69 O HETATM 1699 O HOH S 44 −25.252 −1.782 28.133 1.00 54.09 O HETATM 1700 O HOH S 45 −22.083 −2.141 20.937 1.00 41.28 O HETATM 1701 O HOH S 46 6.716 −24.401 18.382 1.00 56.79 O HETATM 1702 O HOH S 47 −19.242 −7.960 40.741 1.00 55.27 O HETATM 1703 O HOH S 48 −24.885 3.029 32.595 1.00 47.29 O HETATM 1704 O HOH S 49 −6.222 1.301 35.492 1.00 47.37 O HETATM 1705 O HOH S 50 −6.853 −1.015 7.397 1.00 54.42 O HETATM 1706 O HOH S 51 −9.238 3.184 16.875 1.00 56.84 O HETATM 1707 O HOH S 52 5.516 −14.125 0.045 1.00 59.28 O HETATM 1708 O HOH S 53 −9.526 11.881 25.225 1.00 51.94 O HETATM 1709 O HOH S 54 −3.550 2.482 14.129 1.00 55.95 O HETATM 1710 O HOH S 55 −17.418 22.428 31.944 1.00 40.14 O HETATM 1711 O HOH S 56 −4.486 −3.749 1.719 1.00 45.17 O HETATM 1712 O HOH S 57 5.103 4.636 14.892 1.00 66.66 O HETATM 1713 O HOH S 58 −23.492 −0.094 22.392 1.00 47.19 O HETATM 1714 O HOH S 59 −26.738 3.100 30.515 1.00 57.55 O HETATM 1715 O HOH S 60 −24.686 10.560 35.917 1.00 46.11 O HETATM 1716 O HOH S 61 13.398 −18.359 23.686 1.00 51.45 O HETATM 1717 O HOH S 62 −21.258 −0.014 40.488 1.00 59.28 O HETATM 1718 O HOH S 63 −21.450 9.546 21.544 1.00 44.60 O HETATM 1719 O HOH S 64 −15.980 19.531 42.414 1.00 54.58 O HETATM 1720 O HOH S 65 −26.583 9.077 25.046 1.00 67.01 O HETATM 1721 O HOH S 66 −25.031 6.323 34.427 1.00 49.13 O HETATM 1722 O HOH S 67 4.323 −19.716 14.727 1.00 60.95 O HETATM 1723 O HOH S 68 9.220 2.118 9.552 1.00 49.01 O HETATM 1724 O HOH S 69 −26.836 7.978 32.921 1.00 49.25 O HETATM 1725 O HOH S 70 −23.972 −5.676 19.453 1.00 56.39 O HETATM 1726 O HOH S 71 14.673 −7.560 1.360 1.00 55.30 O HETATM 1727 O HOH S 72 −6.648 −17.237 15.642 1.00 53.29 O HETATM 1728 O HOH S 73 0.200 −17.959 20.530 1.00 49.36 O HETATM 1729 O HOH S 74 12.672 −11.935 1.844 1.00 53.58 O HETATM 1730 O HOH S 75 −5.701 13.730 36.592 1.00 58.09 O HETATM 1731 O HOH S 76 −5.766 −19.056 27.135 1.00 51.70 O HETATM 1732 O HOH S 77 −25.610 11.969 30.497 1.00 45.95 O HETATM 1733 O HOH S 78 10.560 −2.550 −4.237 1.00 57.19 O HETATM 1734 O HOH S 79 −25.261 12.245 34.406 1.00 52.54 O HETATM 1735 O HOH S 80 6.500 −27.035 18.000 1.00 50.83 O HETATM 1736 O HOH S 81 −12.866 −16.068 33.587 1.00 63.38 O HETATM 1737 O HOH S 82 −6.248 8.367 35.809 1.00 44.88 O HETATM 1738 O HOH S 83 13.594 −2.415 −2.493 1.00 62.89 O HETATM 1739 O HOH S 85 1.990 −6.171 −4.313 1.00 46.07 O HETATM 1740 O HOH S 86 −6.321 6.088 29.395 1.00 43.19 O HETATM 1741 O HOH S 87 −5.277 −11.712 9.904 1.00 41.48 O HETATM 1742 O HOH S 88 −0.692 −21.465 15.484 1.00 65.91 O HETATM 1743 O HOH S 89 −10.486 8.212 42.653 1.00 58.03 O HETATM 1744 O HOH S 90 −9.955 −4.337 37.118 1.00 56.18 O HETATM 1745 O HOH S 91 3.767 −23.040 34.067 1.00 59.96 O HETATM 1746 O HOH S 92 0.653 −0.503 30.031 1.00 51.73 O HETATM 1747 O HOH S 93 −18.336 −14.096 21.741 1.00 59.29 O HETATM 1748 O HOH S 94 3.479 −25.209 38.916 1.00 63.56 O HETATM 1749 O HOH S 95 −26.605 10.470 22.549 1.00 52.94 O HETATM 1750 O HOH S 96 −12.820 14.810 43.469 1.00 60.93 O HETATM 1751 O HOH S 97 −11.877 −22.060 17.397 1.00 57.27 O HETATM 1752 O HOH S 98 −11.511 −6.158 13.611 1.00 61.64 O HETATM 1753 O HOH S 99 −6.402 3.744 38.398 1.00 58.98 O HETATM 1754 O HOH S 100 −12.627 −6.523 39.220 1.00 65.30 O HETATM 1755 O HOH S 101 −24.129 −11.311 39.009 1.00 73.80 O HETATM 1756 O HOH S 102 −3.142 −18.704 9.848 1.00 65.08 O HETATM 1757 O HOH S 103 7.671 −5.745 27.881 1.00 60.74 O HETATM 1758 O HOH S 104 −0.042 2.480 25.710 1.00 60.35 O HETATM 1759 O HOH S 105 −4.587 −10.265 34.955 1.00 61.56 O HETATM 1760 O HOH S 106 −24.323 5.290 19.367 1.00 61.98 O HETATM 1761 O HOH S 107 −25.459 7.824 19.064 1.00 67.53 O HETATM 1762 O HOH S 108 −24.758 1.839 41.011 1.00 71.29 O HETATM 1763 O HOH S 109 5.609 −12.232 −2.646 1.00 69.92 O HETATM 1764 O HOH S 110 −22.882 16.125 43.554 1.00 63.16 O HETATM 1765 O HOH S 112 −16.657 12.218 48.606 1.00 69.31 O HETATM 1766 O HOH S 113 −24.809 15.560 34.889 1.00 69.17 O HETATM 1767 O HOH S 114 −17.404 6.366 16.634 1.00 62.38 O HETATM 1768 O HOH S 115 14.658 −12.079 2.681 1.00 67.54 O HETATM 1769 O HOH S 116 13.040 −9.195 13.096 1.00 55.34 O HETATM 1770 O HOH S 118 −16.739 11.026 49.721 1.00 69.52 O HETATM 1771 O HOH S 119 −12.669 6.257 18.282 1.00 61.46 O HETATM 1772 O HOH S 120 12.775 −6.171 14.964 1.00 65.93 O HETATM 1773 O HOH S 122 11.291 −2.217 13.161 1.00 63.39 O HETATM 1774 O HOH S 123 −11.161 −2.151 14.499 1.00 68.03 O HETATM 1775 O HOH S 124 −8.793 2.192 14.011 1.00 73.70 O HETATM 1776 O HOH S 125 −11.481 −15.730 36.023 1.00 71.36 O HETATM 1777 O HOH S 126 −5.104 1.400 43.064 1.00 68.56 O HETATM 1778 O HOH S 127 3.229 −28.600 36.834 1.00 78.22 O HETATM 1779 O HOH S 128 5.055 −12.031 −1.300 1.00 69.82 O HETATM 1780 O HOH S 130 −16.498 18.765 29.401 1.00 57.18 O HETATM 1781 O HOH S 131 −27.516 8.450 17.962 1.00 79.87 O HETATM 1782 O HOH S 132 1.844 8.012 23.188 1.00 76.81 O TER END

TABLE 7 Atomic coordinates and structure factors for human apo-PD-1N74G T76P A132V (based on a PDB file). CRYST1  46.172   46.172   89.270  90.00  90.00 120.00 P 32 2 1 SCALE1    0.021658  0.012504  0.000000     0.00000 SCALE2    0.000000  0.025009  0.000000     0.00000 SCALE3    0.000000  0.000000  0.011202     0.00000 ATOM 1 O MET A 32 79.830 72.727 114.713 1.00 33.51 O ANISOU 1 O MET A 32 4442 4896 3394 −702 −1149 301 O ATOM 2 N MET A 32 78.909 75.195 115.710 1.00 37.88 N ANISOU 2 N MET A 32 5485 5060 3848 −66 −935 −491 N ATOM 3 C MET A 32 78.636 72.854 114.996 1.00 31.86 C ANISOU 3 C MET A 32 4346 4552 3207 −68 −941 −549 C ATOM 4 CA AMET A 32 77.995 74.240 115.087 0.49 30.75 C ANISOU 4 CA AMET A 32 4520 4029 3135 44 −1085 −722 C ATOM 5 CB AMET A 32 77.560 74.735 113.696 0.49 32.29 C ANISOU 5 CB AMET A 32 4539 4040 3688 −153 −1019 −383 C ATOM 6 CG AMET A 32 76.475 73.892 113.023 0.49 29.96 C ANISOU 6 CG AMET A 32 4316 3395 3674 −172 −944 −240 C ATOM 7 SD AMET A 32 75.859 74.568 111.459 0.49 25.76 S ANISOU 7 SD AMET A 32 3894 2513 3382 −170 −830 42 S ATOM 8 CE AMET A 32 77.360 74.632 110.485 0.49 24.73 C ANISOU 8 CE AMET A 32 3990 2249 3158 −46 −746 −0 C ATOM 9 CA BMET A 32 77.988 74.230 115.126 0.51 31.28 C ANISOU 9 CA BMET A 32 4697 4033 3155 190 −922 −701 C ATOM 10 CB BMET A 32 77.504 74.711 113.760 0.51 34.88 C ANISOU 10 CB BMET A 32 5128 4374 3750 550 −604 −347 C ATOM 11 CG BMET A 32 78.611 74.790 112.734 0.51 29.06 C ANISOU 11 CG BMET A 32 4499 3462 3079 949 −286 −26 C ATOM 12 SD BMET A 32 78.032 75.208 111.094 0.51 22.29 S ANISOU 12 SD BMET A 32 3320 2568 2581 −86 −682 98 S ATOM 13 CE BMET A 32 76.765 73.972 110.841 0.51 21.47 C ANISOU 13 CE BMET A 32 3037 2508 2612 −312 −458 −483 C ATOM 14 N ASN A 33 77.838 71.825 115.236 1.00 27.27 N ANISOU 14 N ASN A 33 3793 3937 2629 415 −354 −960 N ATOM 15 CA ASN A 33 78.278 70.448 115.106 1.00 25.75 C ANISOU 15 CA ASN A 33 3582 3665 2536 −312 −207 −1117 C ATOM 16 C ASN A 33 77.907 69.965 113.725 1.00 22.88 C ANISOU 16 C ASN A 33 2433 3822 2438 444 −531 −1185 C ATOM 17 O ASN A 33 76.936 70.447 113.146 1.00 27.75 O ANISOU 17 O ASN A 33 2891 4625 3026 1444 −982 −1681 O ATOM 18 CB ASN A 33 77.529 69.583 116.118 1.00 30.67 C ANISOU 18 CB ASN A 33 4226 4744 2683 −940 184 −1015 C ATOM 19 CG ASN A 33 77.341 70.278 117.443 1.00 34.68 C ANISOU 19 CG ASN A 33 4200 5911 3064 −76 292 −796 C ATOM 20 OD1 ASN A 33 76.219 70.417 117.946 1.00 37.76 O ANISOU 20 OD1 ASN A 33 4804 6206 3335 −264 280 −880 O ATOM 21 ND2 ASN A 33 78.440 70.734 118.016 1.00 29.13 N ANISOU 21 ND2 ASN A 33 3681 5301 2088 595 −673 −893 N ATOM 22 N PRO A 34 78.655 68.998 113.179 1.00 18.36 N ANISOU 22 N PRO A 34 1952 2987 2038 257 −510 −597 N ATOM 23 C PRO A 34 76.953 67.611 112.049 1.00 15.80 C ANISOU 23 C PRO A 34 1875 2665 1462 379 −368 −360 C ATOM 24 O PRO A 34 76.706 67.033 113.102 1.00 18.22 O ANISOU 24 O PRO A 34 2174 3378 1372 68 −220 30 O ATOM 25 CA APRO A 34 78.235 68.417 111.903 0.47 16.78 C ANISOU 25 CA APRO A 34 1807 2637 1930 289 −434 −220 C ATOM 26 CB APRO A 34 79.384 67.461 111.555 0.47 19.28 C ANISOU 26 CB APRO A 34 2070 2646 2609 16 −131 −137 C ATOM 27 CG APRO A 34 80.526 67.879 112.418 0.47 16.73 C ANISOU 27 CG APRO A 34 1848 2450 2059 82 −671 −184 C ATOM 28 CD APRO A 34 79.925 68.430 113.662 0.47 17.94 C ANISOU 28 CD APRO A 34 1726 3066 2023 172 −701 −345 C ATOM 29 CA BPRO A 34 78.196 68.473 111.896 0.53 16.26 C ANISOU 29 CA BPRO A 34 1714 2648 1817 420 −357 −563 C ATOM 30 CB BPRO A 34 79.373 67.613 111.430 0.53 19.36 C ANISOU 30 CB BPRO A 34 2073 2908 2374 459 −177 −544 C ATOM 31 CG BPRO A 34 80.037 67.196 112.684 0.53 21.73 C ANISOU 31 CG BPRO A 34 2467 3366 2422 687 −363 −378 C ATOM 32 CD BPRO A 34 79.900 68.354 113.632 0.53 21.39 C ANISOU 32 CD BPRO A 34 2149 3605 2373 528 −424 −408 C ATOM 33 N PRO A 35 76.153 67.545 110.992 1.00 14.87 N ANISOU 33 N PRO A 35 1860 2567 1222 320 −286 −531 N ATOM 34 CA PRO A 35 75.029 66.611 110.996 1.00 15.01 C ANISOU 34 CA PRO A 35 1992 2294 1417 421 −354 −385 C ATOM 35 C PRO A 35 75.547 65.175 110.811 1.00 14.70 C ANISOU 35 C PRO A 35 1862 2629 1094 194 −229 −323 C ATOM 36 O PRO A 35 76.677 64.987 110.362 1.00 15.42 O ANISOU 36 O PRO A 35 1899 2377 1584 386 −97 −146 O ATOM 37 CB PRO A 35 74.232 67.048 109.767 1.00 16.89 C ANISOU 37 CB PRO A 35 2063 2934 1420 365 −287 −270 C ATOM 38 CG PRO A 35 75.269 67.639 108.845 1.00 17.84 C ANISOU 38 CG PRO A 35 2804 2536 1438 746 −662 −274 C ATOM 39 CD PRO A 35 76.296 68.267 109.713 1.00 16.05 C ANISOU 39 CD PRO A 35 2802 2289 1009 546 −449 −215 C ATOM 40 N THR A 36 74.718 64.185 111.117 1.00 15.08 N ANISOU 40 N THR A 36 2017 2363 1351 225 −228 −344 N ATOM 41 CA THR A 36 75.023 62.793 110.803 1.00 16.35 C ANISOU 41 CA THR A 36 2124 2588 1502 246 −309 −222 C ATOM 42 C THR A 36 74.028 62.296 109.759 1.00 15.16 C ANISOU 42 C THR A 36 1801 2402 1557 206 −204 −398 C ATOM 43 O THR A 36 72.916 62.814 109.646 1.00 18.63 O ANISOU 43 O THR A 36 2032 3001 2046 688 −368 −1001 O ATOM 44 CB THR A 36 74.965 61.892 112.042 1.00 20.81 C ANISOU 44 CB THR A 36 2401 3485 2019 275 −138 105 C ATOM 45 OG1 THR A 36 73.631 61.886 112.555 1.00 24.03 O ANISOU 45 OG1 THR A 36 3055 3856 2219 497 207 636 O ATOM 46 CG2 THR A 36 75.933 62.383 113.114 1.00 20.93 C ANISOU 46 CG2 THR A 36 2980 3430 1543 429 −566 −172 C ATOM 47 N PHE A 37 74.431 61.308 108.976 1.00 14.36 N ANISOU 47 N PHE A 37 2089 2035 1331 309 −60 −217 N ATOM 48 CA PHE A 37 73.640 60.887 107.830 1.00 13.70 C ANISOU 48 CA PHE A 37 2134 1944 1126 100 −174 −165 C ATOM 49 C PHE A 37 73.624 59.369 107.792 1.00 14.15 C ANISOU 49 C PHE A 37 2000 2138 1240 407 −90 −88 C ATOM 50 O PHE A 37 74.684 58.740 107.782 1.00 17.72 O ANISOU 50 O PHE A 37 2211 2296 2225 259 84 −36 O ATOM 51 CB PHE A 37 74.274 61.468 106.576 1.00 14.18 C ANISOU 51 CB PHE A 37 2209 2159 1019 39 −98 −76 C ATOM 52 CG PHE A 37 73.369 61.532 105.387 1.00 14.61 C ANISOU 52 CG PHE A 37 2445 1869 1238 −149 50 −21 C ATOM 53 CD1 PHE A 37 73.812 61.078 104.163 1.00 19.33 C ANISOU 53 CD1 PHE A 37 3032 3221 1090 −913 193 −167 C ATOM 54 CD2 PHE A 37 72.111 62.105 105.465 1.00 17.12 C ANISOU 54 CD2 PHE A 37 2497 2187 1820 −100 −524 −2 C ATOM 55 CE1 PHE A 37 73.010 61.163 103.046 1.00 23.99 C ANISOU 55 CE1 PHE A 37 3414 4289 1414 −1415 108 90 C ATOM 56 CE2 PHE A 37 71.308 62.201 104.347 1.00 19.30 C ANISOU 56 CE2 PHE A 37 2914 2529 1892 −612 −721 455 C ATOM 57 CZ PHE A 37 71.765 61.734 103.141 1.00 21.04 C ANISOU 57 CZ PHE A 37 2905 3608 1483 −1397 −469 732 C ATOM 58 O SER A 38 70.289 57.574 106.613 1.00 15.97 O ANISOU 58 O SER A 38 2359 2030 1679 215 −282 −3 O ATOM 59 N SER A 38 72.431 58.785 107.767 1.00 14.16 N ANISOU 59 N SER A 38 2349 1917 1113 58 −180 −60 N ATOM 60 C SER A 38 71.160 56.826 107.016 1.00 14.91 C ANISOU 60 C SER A 38 2287 2034 1342 −75 −143 61 C ATOM 61 CA ASER A 38 72.288 57.343 107.907 0.56 15.15 C ANISOU 61 CA ASER A 38 2420 2246 1091 304 −249 23 C ATOM 62 CB ASER A 38 72.023 56.979 109.374 0.56 20.63 C ANISOU 62 CB ASER A 38 3585 2419 1836 181 3 16 C ATOM 63 OG ASER A 38 70.756 57.451 109.795 0.56 21.87 O ANISOU 63 OG ASER A 38 4075 2401 1835 −72 389 78 O ATOM 64 CA BSER A 38 72.260 57.348 107.941 0.16 15.76 C ANISOU 64 CA BSER A 38 2456 2292 1239 113 −273 11 C ATOM 65 CB BSER A 38 71.909 57.057 109.408 0.16 17.69 C ANISOU 65 CB BSER A 38 2714 2621 1285 139 −331 −33 C ATOM 66 OG BSER A 38 71.329 55.775 109.576 0.16 16.34 O ANISOU 66 OG BSER A 38 2597 2720 890 117 −526 0 O ATOM 67 CA CSER A 38 72.263 57.344 107.930 0.28 15.41 C ANISOU 67 CA CSER A 38 2481 2242 1132 167 −273 15 C ATOM 68 CB CSER A 38 71.896 57.020 109.381 0.28 17.88 C ANISOU 68 CB CSER A 38 3115 2347 1332 −64 −223 −42 C ATOM 69 OG CSER A 38 72.827 57.580 110.283 0.28 17.98 O ANISOU 69 OG CSER A 38 3241 2377 1212 −387 −254 133 O ATOM 70 N PRO A 39 71.197 55.524 106.669 1.00 16.19 N ANISOU 70 N PRO A 39 2436 1977 1737 65 −316 85 N ATOM 71 CA PRO A 39 72.243 54.535 106.948 1.00 16.60 C ANISOU 71 CA PRO A 39 2454 1838 2014 41 −99 41 C ATOM 72 C PRO A 39 73.419 54.778 106.016 1.00 15.97 C ANISOU 72 C PRO A 39 2658 1744 1666 131 −207 245 C ATOM 73 O PRO A 39 73.264 55.425 104.971 1.00 16.75 O ANISOU 73 O PRO A 39 2523 2165 1675 191 −88 230 O ATOM 74 CB PRO A 39 71.571 53.210 106.600 1.00 19.16 C ANISOU 74 CB PRO A 39 3181 1904 2195 26 −121 227 C ATOM 75 CG PRO A 39 70.626 53.561 105.537 1.00 19.50 C ANISOU 75 CG PRO A 39 3343 1919 2148 −173 −550 30 C ATOM 76 CD PRO A 39 70.094 54.929 105.892 1.00 18.31 C ANISOU 76 CD PRO A 39 2901 2007 2050 −155 −387 170 C ATOM 77 N ALA A 40 74.581 54.258 106.377 1.00 16.67 N ANISOU 77 N ALA A 40 2629 2178 1525 335 −190 183 N ATOM 78 CA ALA A 40 75.768 54.444 105.561 1.00 16.37 C ANISOU 78 CA ALA A 40 2306 2449 1465 144 −236 −117 C ATOM 79 C ALA A 40 75.627 53.797 104.190 1.00 15.01 C ANISOU 79 C ALA A 40 2233 2025 1446 215 −251 236 C ATOM 80 O ALA A 40 76.222 54.262 103.222 1.00 15.34 O ANISOU 80 O ALA A 40 2262 2060 1505 −20 −202 134 O ATOM 81 CB ALA A 40 76.990 53.897 106.276 1.00 20.28 C ANISOU 81 CB ALA A 40 2826 3357 1522 643 −539 −171 C ATOM 82 N LEU A 41 74.855 52.717 104.120 1.00 15.59 N ANISOU 82 N LEU A 41 2571 2135 1218 360 −160 −76 N ATOM 83 CA LEU A 41 74.588 52.042 102.856 1.00 15.63 C ANISOU 83 CA LEU A 41 2477 2052 1411 62 −23 116 C ATOM 84 C LEU A 41 73.105 51.734 102.800 1.00 14.98 C ANISOU 84 C LEU A 41 2489 1902 1299 64 −72 11 C ATOM 85 O LEU A 41 72.569 51.088 103.699 1.00 18.14 O ANISOU 85 O LEU A 41 2947 2224 1719 36 −31 345 O ATOM 86 CB LEU A 41 75.385 50.742 102.740 1.00 16.61 C ANISOU 86 CB LEU A 41 2618 2152 1540 286 −109 −298 C ATOM 87 CG LEU A 41 75.066 49.870 101.518 1.00 18.17 C ANISOU 87 CG LEU A 41 2906 2231 1768 387 −18 −173 C ATOM 88 CD1 LEU A 41 75.352 50.581 100.207 1.00 18.57 C ANISOU 88 CD1 LEU A 41 2888 2659 1508 −9 232 −249 C ATOM 89 CD2 LEU A 41 75.842 48.564 101.591 1.00 20.17 C ANISOU 89 CD2 LEU A 41 3236 2167 2259 336 121 −279 C ATOM 90 N LEU A 42 72.452 52.211 101.750 1.00 14.97 N ANISOU 90 N LEU A 42 2285 2045 1357 139 8 −66 N ATOM 91 C LEU A 42 70.899 51.271 100.172 1.00 14.15 C ANISOU 91 C LEU A 42 1938 2233 1205 97 48 87 C ATOM 92 O LEU A 42 71.321 51.808 99.151 1.00 15.43 O ANISOU 92 O LEU A 42 2382 2214 1268 −9 151 −67 O ATOM 93 CD1 LEU A 42 68.105 52.322 102.336 1.00 24.90 C ANISOU 93 CD1 LEU A 42 2747 4393 2320 341 253 409 C ATOM 94 CD2 LEU A 42 68.209 54.656 101.428 1.00 23.22 C ANISOU 94 CD2 LEU A 42 2935 3807 2082 1510 −20 −37 C ATOM 95 CA LEU A 42 71.040 51.961 101.525 1.00 15.55 C ANISOU 95 CA LEU A 42 2344 2269 1296 392 147 156 C ATOM 96 CB LEU A 42 70.285 53.287 101.519 1.00 17.74 C ANISOU 96 CB LEU A 42 2446 2867 1427 690 −24 −381 C ATOM 97 CG LEU A 42 68.772 53.247 101.324 1.00 19.78 C ANISOU 97 CG LEU A 42 2418 3446 1654 505 −170 185 C ATOM 98 N VAL A 43 70.315 50.078 100.172 1.00 15.80 N ANISOU 98 N VAL A 43 2433 2143 1428 71 101 162 N ATOM 99 CA VAL A 43 70.124 49.313 98.949 1.00 16.71 C ANISOU 99 CA VAL A 43 2287 1993 2069 −25 33 5 C ATOM 100 C VAL A 43 68.630 49.186 98.706 1.00 16.06 C ANISOU 100 C VAL A 43 2498 1838 1768 −45 78 291 C ATOM 101 O VAL A 43 67.887 48.701 99.568 1.00 19.81 O ANISOU 101 O VAL A 43 2835 2613 2078 −283 −37 558 O ATOM 102 CB VAL A 43 70.750 47.902 99.057 1.00 19.48 C ANISOU 102 CB VAL A 43 2787 2163 2452 227 −314 −188 C ATOM 103 CG1 VAL A 43 70.563 47.128 97.749 1.00 22.59 C ANISOU 103 CG1 VAL A 43 3225 2444 2913 70 −423 −342 C ATOM 104 CG2 VAL A 43 72.217 48.010 99.427 1.00 20.81 C ANISOU 104 CG2 VAL A 43 2974 2305 2628 409 −228 156 C ATOM 105 N VAL A 44 68.188 49.625 97.535 1.00 15.96 N ANISOU 105 N VAL A 44 2101 2113 1849 −158 −56 66 N ATOM 106 CA VAL A 44 66.786 49.525 97.156 1.00 16.74 C ANISOU 106 CA VAL A 44 2428 1970 1962 −130 69 −14 C ATOM 107 C VAL A 44 66.691 49.006 95.727 1.00 16.45 C ANISOU 107 C VAL A 44 2440 1820 1990 −201 −140 −306 C ATOM 108 O VAL A 44 67.665 49.018 94.985 1.00 19.18 O ANISOU 108 O VAL A 44 2609 2599 2079 −243 181 −421 O ATOM 109 CB VAL A 44 66.044 50.886 97.255 1.00 17.02 C ANISOU 109 CB VAL A 44 2823 2239 1406 229 12 −137 C ATOM 110 CG1 VAL A 44 66.197 51.487 98.646 1.00 17.74 C ANISOU 110 CG1 VAL A 44 2799 2493 1450 −41 108 −102 C ATOM 111 CG2 VAL A 44 66.530 51.855 96.190 1.00 17.52 C ANISOU 111 CG2 VAL A 44 3101 1940 1617 −142 2 35 C ATOM 112 N ATHR A 45 65.497 48.571 95.351 0.71 16.45 N ANISOU 112 N ATHR A 45 2256 1846 2150 −433 −9 −362 N ATOM 113 CA ATHR A 45 65.228 48.128 93.991 0.71 18.16 C ANISOU 113 CA ATHR A 45 2516 2138 2248 −655 −58 −612 C ATOM 114 C ATHR A 45 64.713 49.293 93.160 0.71 17.67 C ANISOU 114 C ATHR A 45 2553 2219 1944 −325 −54 −749 C ATOM 115 O ATHR A 45 63.957 50.122 93.664 0.71 15.17 O ANISOU 115 O ATHR A 45 2130 1995 1638 −252 −15 −517 O ATOM 116 CB ATHR A 45 64.179 47.003 93.993 0.71 23.21 C ANISOU 116 CB ATHR A 45 3391 2475 2951 −714 −299 −438 C ATOM 117 OG1 ATHR A 45 64.605 45.975 94.892 0.71 24.08 O ANISOU 117 OG1 ATHR A 45 3734 2170 3248 −460 −132 −208 O ATOM 118 CG2 ATHR A 45 64.002 46.410 92.594 0.71 22.72 C ANISOU 118 CG2 ATHR A 45 3321 2345 2966 −575 −443 −535 C ATOM 119 N BTHR A 45 65.522 48.507 95.349 0.29 19.88 N ANISOU 119 N BTHR A 45 2704 2333 2518 −233 −162 −303 N ATOM 120 CA BTHR A 45 65.315 48.117 93.963 0.29 21.66 C ANISOU 120 CA BTHR A 45 2882 2599 2751 −272 −188 −417 C ATOM 121 C BTHR A 45 64.831 49.328 93.188 0.29 19.03 C ANISOU 121 C BTHR A 45 2370 2457 2404 −478 −15 −488 C ATOM 122 O BTHR A 45 64.225 50.234 93.760 0.29 25.66 O ANISOU 122 O BTHR A 45 3197 3384 3168 −379 219 −258 O ATOM 123 CB BTHR A 45 64.294 46.973 93.820 0.29 25.92 C ANISOU 123 CB BTHR A 45 3398 3210 3241 −149 −347 −434 C ATOM 124 OG1 BTHR A 45 63.092 47.308 94.522 0.29 27.14 O ANISOU 124 OG1 BTHR A 45 3544 3390 3377 −241 −219 −550 O ATOM 125 CG2 BTHR A 45 64.858 45.679 94.381 0.29 25.55 C ANISOU 125 CG2 BTHR A 45 3258 3145 3303 −81 −414 −354 C ATOM 126 N AGLU A 46 65.114 49.353 91.891 0.71 17.63 N ANISOU 126 N AGLU A 46 2589 2242 1868 −98 −13 −582 N ATOM 127 C AGLU A 46 63.082 50.480 91.088 0.71 16.75 C ANISOU 127 C AGLU A 46 2581 2539 1245 −614 −77 −562 C ATOM 128 O AGLU A 46 62.386 49.461 91.045 0.71 18.68 O ANISOU 128 O AGLU A 46 2753 2659 1685 −631 −213 −575 O ATOM 129 CD AGLU A 46 65.212 48.836 87.533 0.71 33.06 C ANISOU 129 CD AGLU A 46 5116 4718 2725 −733 −70 −1224 C ATOM 130 OE1 AGLU A 46 65.296 49.890 86.867 0.71 36.61 O ANISOU 130 OE1 AGLU A 46 5669 5242 2997 −929 −172 −1456 O ATOM 131 OE2 AGLU A 46 65.450 47.707 87.057 0.71 33.49 O ANISOU 131 OE2 AGLU A 46 5216 5046 2462 −129 64 −1320 O ATOM 132 CG AGLU A 46 64.794 48.925 88.984 0.71 26.90 C ANISOU 132 CG AGLU A 46 4032 3916 2271 −762 −109 −1017 C ATOM 133 CA AGLU A 46 64.605 50.416 91.037 0.71 18.78 C ANISOU 133 CA AGLU A 46 2648 2748 1739 −235 95 −535 C ATOM 134 CB AGLU A 46 65.105 50.263 89.599 0.71 23.48 C ANISOU 134 CB AGLU A 46 3012 3787 2124 −371 −57 −714 C ATOM 135 N BGLU A 46 65.079 49.332 91.912 0.29 19.95 N ANISOU 135 N BGLU A 46 2619 2589 2373 −318 102 −529 N ATOM 136 C BGLU A 46 63.075 50.471 91.126 0.29 18.27 C ANISOU 136 C BGLU A 46 2602 2552 1786 −566 57 −502 C ATOM 137 O BGLU A 46 62.393 49.480 91.117 0.29 21.67 O ANISOU 137 O BGLU A 46 3051 2850 2334 −445 85 −432 O ATOM 138 CD BGLU A 46 65.685 50.905 87.353 0.29 29.27 C ANISOU 138 CD BGLU A 46 4288 4449 2384 17 217 −1220 C ATOM 139 OE1 BGLU A 46 65.554 49.697 86.977 0.29 28.44 O ANISOU 139 OE1 BGLU A 46 4611 4037 2157 −159 2 −1571 O ATOM 140 OE2 BGLU A 46 66.221 51.892 86.715 0.29 26.39 O ANISOU 140 OE2 BGLU A 46 3311 4592 2124 −1012 230 −1032 O ATOM 141 CG BGLU A 46 65.103 51.196 88.740 0.29 28.25 C ANISOU 141 CG BGLU A 46 4004 4129 2599 3 459 −877 C ATOM 142 CA BGLU A 46 64.579 50.340 91.043 0.29 19.89 C ANISOU 142 CA BGLU A 46 2644 2768 2147 −376 277 −573 C ATOM 143 CB BGLU A 46 65.003 50.000 89.611 0.29 22.64 C ANISOU 143 CB BGLU A 46 2924 3355 2324 −393 506 −676 C ATOM 144 N GLY A 47 62.578 51.700 91.211 1.00 16.83 N ANISOU 144 N GLY A 47 2563 2385 1445 −516 −94 −315 N ATOM 145 CA GLY A 47 61.157 51.931 91.349 1.00 17.00 C ANISOU 145 CA GLY A 47 2295 2743 1422 −102 −326 −304 C ATOM 146 C GLY A 47 60.739 52.183 92.791 1.00 16.71 C ANISOU 146 C GLY A 47 2189 2753 1406 −346 −282 −90 C ATOM 147 O GLY A 47 59.705 52.807 93.037 1.00 17.82 O ANISOU 147 O GLY A 47 2076 2916 1780 −261 −343 −48 O ATOM 148 N ASP A 48 61.524 51.706 93.758 1.00 16.20 N ANISOU 148 N ASP A 48 2414 2424 1317 −142 −195 −254 N ATOM 149 C ASP A 48 61.540 53.383 95.542 1.00 14.98 C ANISOU 149 C ASP A 48 2004 2400 1289 −423 −86 −322 C ATOM 150 O ASP A 48 62.274 54.085 94.853 1.00 17.23 O ANISOU 150 O ASP A 48 2320 2516 1711 −587 296 −202 O ATOM 151 OD1 ASP A 48 60.858 49.221 95.553 1.00 25.99 O ANISOU 151 OD1 ASP A 48 4034 2673 3167 −827 839 −366 O ATOM 152 OD2 ASP A 48 62.827 48.965 96.533 1.00 27.11 O ANISOU 152 OD2 ASP A 48 3064 3221 4017 −880 939 −583 O ATOM 153 CG ASP A 48 61.916 49.675 96.039 1.00 28.36 C ANISOU 153 CG ASP A 48 3675 3712 3391 25 908 −239 C ATOM 154 CA ASP A 48 61.227 51.956 95.169 1.00 14.96 C ANISOU 154 CA ASP A 48 2268 2050 1366 −318 −298 −133 C ATOM 155 CB ASP A 48 62.146 51.150 96.088 1.00 21.71 C ANISOU 155 CB ASP A 48 3615 2510 2123 360 15 −122 C ATOM 156 N ASN A 49 61.035 53.812 96.688 1.00 14.25 N ANISOU 156 N ASN A 49 1950 2081 1382 −420 −76 −203 N ATOM 157 C ASN A 49 62.763 54.746 98.109 1.00 14.83 C ANISOU 157 C ASN A 49 2202 1989 1443 −229 −206 31 C ATOM 158 O ASN A 49 63.021 53.609 98.464 1.00 16.68 O ANISOU 158 O ASN A 49 2375 2165 1796 −386 −391 32 O ATOM 159 CA AASN A 49 61.504 55.031 97.329 0.79 14.54 C ANISOU 159 CA AASN A 49 2109 2039 1375 −330 −232 −311 C ATOM 160 OD1 AASN A 49 59.174 56.327 96.449 0.79 18.64 O ANISOU 160 OD1 AASN A 49 2021 2630 2431 −267 −296 86 O ATOM 161 ND2 AASN A 49 58.033 55.612 98.245 0.79 17.53 N ANISOU 161 ND2 AASN A 49 2076 2453 2134 461 −141 −505 N ATOM 162 CB AASN A 49 60.441 55.544 98.287 0.79 18.02 C ANISOU 162 CB AASN A 49 2691 2333 1825 −31 −47 −586 C ATOM 163 CG AASN A 49 59.158 55.870 97.589 0.79 17.41 C ANISOU 163 CG AASN A 49 2051 2395 2170 −29 −278 −365 C ATOM 164 CA BASN A 49 61.547 55.049 97.237 0.21 15.93 C ANISOU 164 CA BASN A 49 2103 2270 1679 −379 −37 −79 C ATOM 165 OD1 BASN A 49 60.303 54.472 99.874 0.21 12.57 O ANISOU 165 OD1 BASN A 49 1619 2027 1132 −354 262 256 O ATOM 166 ND2 BASN A 49 58.372 55.043 98.869 0.21 11.68 N ANISOU 166 ND2 BASN A 49 1088 2516 833 144 −71 206 N ATOM 167 CB BASN A 49 60.459 55.868 97.951 0.21 15.89 C ANISOU 167 CB BASN A 49 1964 2391 1683 −2 243 150 C ATOM 168 CG BASN A 49 59.702 55.068 98.984 0.21 13.93 C ANISOU 168 CG BASN A 49 1668 2210 1414 −76 247 166 C ATOM 169 N ALA A 50 63.545 55.770 98.395 1.00 14.97 N ANISOU 169 N ALA A 50 2221 1884 1584 −223 −509 −146 N ATOM 170 CA ALA A 50 64.733 55.609 99.215 1.00 15.39 C ANISOU 170 CA ALA A 50 2057 2050 1739 75 −572 −316 C ATOM 171 C ALA A 50 64.804 56.796 100.149 1.00 13.56 C ANISOU 171 C ALA A 50 1987 1839 1326 −116 −460 −25 C ATOM 172 O ALA A 50 64.684 57.940 99.717 1.00 16.01 O ANISOU 172 O ALA A 50 2995 1848 1241 20 −628 −15 O ATOM 173 CB ALA A 50 65.971 55.565 98.362 1.00 17.18 C ANISOU 173 CB ALA A 50 2215 2124 2188 142 −393 −543 C ATOM 174 N THR A 51 65.032 56.531 101.430 1.00 12.96 N ANISOU 174 N THR A 51 1948 1665 1312 −147 −223 −37 N ATOM 175 C THR A 51 66.290 57.466 103.330 1.00 12.69 C ANISOU 175 C THR A 51 1967 1768 1086 66 −112 57 C ATOM 176 O THR A 51 66.484 56.453 103.997 1.00 14.73 O ANISOU 176 O THR A 51 2193 1930 1475 −249 −319 98 O ATOM 177 CA THR A 51 65.076 57.587 102.423 1.00 13.04 C ANISOU 177 CA THR A 51 1772 1928 1254 −72 −84 −74 C ATOM 178 CB THR A 51 63.795 57.569 103.296 1.00 16.11 C ANISOU 178 CB THR A 51 1860 2543 1719 −171 −49 −138 C ATOM 179 OG1 THR A 51 62.661 57.803 102.460 1.00 17.62 O ANISOU 179 OG1 THR A 51 1895 2845 1956 −9 50 49 O ATOM 180 CG2 THR A 51 63.856 58.646 104.369 1.00 17.63 C ANISOU 180 CG2 THR A 51 2141 2903 1654 −42 311 −439 C ATOM 181 N PHE A 52 67.099 58.517 103.341 1.00 12.45 N ANISOU 181 N PHE A 52 1755 1780 1196 −46 −94 −77 N ATOM 182 CA PHE A 52 68.149 58.690 104.333 1.00 12.35 C ANISOU 182 CA PHE A 52 1693 1780 1220 −87 −117 −170 C ATOM 183 C PHE A 52 67.637 59.574 105.461 1.00 11.78 C ANISOU 183 C PHE A 52 1775 1819 883 −47 88 −103 C ATOM 184 O PHE A 52 66.713 60.363 105.272 1.00 13.68 O ANISOU 184 O PHE A 52 1862 1996 1339 171 49 −54 O ATOM 185 CB PHE A 52 69.362 59.373 103.707 1.00 13.20 C ANISOU 185 CB PHE A 52 1674 2082 1259 −74 36 −193 C ATOM 186 CG PHE A 52 70.060 58.558 102.656 1.00 13.65 C ANISOU 186 CG PHE A 52 1859 2063 1265 101 −80 −294 C ATOM 187 CD1 PHE A 52 69.867 58.808 101.304 1.00 15.96 C ANISOU 187 CD1 PHE A 52 2344 2424 1297 450 −110 −262 C ATOM 188 CD2 PHE A 52 70.960 57.571 103.022 1.00 13.80 C ANISOU 188 CD2 PHE A 52 2050 1952 1242 55 36 −380 C ATOM 189 CE1 PHE A 52 70.550 58.070 100.353 1.00 19.56 C ANISOU 189 CE1 PHE A 52 2890 3357 1187 1033 −244 −404 C ATOM 190 CE2 PHE A 52 71.627 56.830 102.065 1.00 15.86 C ANISOU 190 CE2 PHE A 52 2309 2450 1266 185 −126 −442 C ATOM 191 CZ PHE A 52 71.424 57.083 100.741 1.00 19.49 C ANISOU 191 CZ PHE A 52 2993 3185 1230 972 −96 −537 C ATOM 192 N THR A 53 68.267 59.457 106.624 1.00 13.11 N ANISOU 192 N THR A 53 2050 2005 927 −107 −0 −249 N ATOM 193 C THR A 53 69.175 61.189 108.078 1.00 13.81 C ANISOU 193 C THR A 53 2110 2108 1027 154 153 −327 C ATOM 194 O THR A 53 70.271 60.665 108.336 1.00 14.96 O ANISOU 194 O THR A 53 2204 2189 1291 268 −121 −186 O ATOM 195 CA THR A 53 67.961 60.342 107.741 1.00 14.27 C ANISOU 195 CA THR A 53 2236 2258 928 −320 144 −150 C ATOM 196 CB THR A 53 67.523 59.561 108.986 1.00 17.46 C ANISOU 196 CB THR A 53 2645 2908 1081 −531 119 −197 C ATOM 197 OG1 THR A 53 66.366 58.783 108.662 1.00 19.30 O ANISOU 197 OG1 THR A 53 2767 2883 1685 −568 468 −5 O ATOM 198 CG2 THR A 53 67.179 60.511 110.122 1.00 19.57 C ANISOU 198 CG2 THR A 53 3268 2842 1325 −217 518 −202 C ATOM 199 N CYS A 54 68.980 62.502 108.044 1.00 14.25 N ANISOU 199 N CYS A 54 1903 2111 1400 24 72 −436 N ATOM 200 C CYS A 54 69.602 63.910 109.883 1.00 15.35 C ANISOU 200 C CYS A 54 1932 2469 1432 93 −224 −449 C ATOM 201 O CYS A 54 68.469 64.334 110.093 1.00 18.07 O ANISOU 201 O CYS A 54 1863 3055 1949 414 −68 −659 O ATOM 202 CA ACYS A 54 69.994 63.454 108.488 0.71 15.23 C ANISOU 202 CA ACYS A 54 1763 2153 1872 −72 −154 −232 C ATOM 203 CB ACYS A 54 70.071 64.655 107.530 0.71 16.71 C ANISOU 203 CB ACYS A 54 1744 2158 2448 −209 −168 −78 C ATOM 204 SG ACYS A 54 71.243 65.962 107.970 0.71 20.97 S ANISOU 204 SG ACYS A 54 2659 2312 2996 50 −627 −398 S ATOM 205 CA BCYS A 54 69.994 63.439 108.493 0.29 15.64 C ANISOU 205 CA BCYS A 54 1955 2443 1545 60 −10 −399 C ATOM 206 CB BCYS A 54 70.075 64.624 107.534 0.29 14.54 C ANISOU 206 CB BCYS A 54 1615 2621 1290 266 242 −351 C ATOM 207 SG BCYS A 54 71.443 65.750 107.821 0.29 13.09 S ANISOU 207 SG BCYS A 54 1527 2428 1017 −145 345 −322 S ATOM 208 N SER A 55 70.526 63.806 110.831 1.00 15.37 N ANISOU 208 N SER A 55 1956 2468 1416 46 5 −417 N ATOM 209 C SER A 55 71.142 65.460 112.496 1.00 16.48 C ANISOU 209 C SER A 55 1830 3049 1382 24 125 −573 C ATOM 210 O SER A 55 72.350 65.437 112.281 1.00 17.81 O ANISOU 210 O SER A 55 1932 2900 1934 159 −87 −946 O ATOM 211 CA ASER A 55 70.266 64.254 112.192 0.78 15.56 C ANISOU 211 CA ASER A 55 2144 2606 1164 7 −121 −405 C ATOM 212 CB ASER A 55 70.518 63.126 113.188 0.78 19.67 C ANISOU 212 CB ASER A 55 2608 3009 1855 −145 229 −201 C ATOM 213 OG ASER A 55 69.698 62.006 112.896 0.78 21.82 O ANISOU 213 OG ASER A 55 3024 3035 2229 57 171 −66 O ATOM 214 CA BSER A 55 70.282 64.241 112.201 0.22 20.24 C ANISOU 214 CA BSER A 55 2673 3100 1917 113 135 −321 C ATOM 215 CB BSER A 55 70.607 63.112 113.178 0.22 25.20 C ANISOU 215 CB BSER A 55 3703 3356 2516 254 323 24 C ATOM 216 OG BSER A 55 70.412 63.518 114.520 0.22 23.63 O ANISOU 216 OG BSER A 55 3875 2988 2116 1127 401 391 O ATOM 217 N PHE A 56 70.531 66.530 112.985 1.00 15.78 N ANISOU 217 N PHE A 56 2052 2746 1197 228 47 −380 N ATOM 218 CA PHE A 56 71.276 67.759 113.197 1.00 14.92 C ANISOU 218 CA PHE A 56 2201 2450 1019 72 91 −351 C ATOM 219 C PHE A 56 70.784 68.461 114.429 1.00 17.96 C ANISOU 219 C PHE A 56 2383 2975 1468 236 46 −328 C ATOM 220 O PHE A 56 69.590 68.729 114.551 1.00 19.12 O ANISOU 220 O PHE A 56 2334 2899 2034 347 318 −520 O ATOM 221 CB PHE A 56 71.130 68.693 111.994 1.00 17.02 C ANISOU 221 CB PHE A 56 2329 2970 1168 306 −88 −170 C ATOM 222 CG PHE A 56 71.801 70.029 112.177 1.00 15.82 C ANISOU 222 CG PHE A 56 2302 2580 1128 340 −120 −92 C ATOM 223 CD1 PHE A 56 73.177 70.112 112.330 1.00 16.84 C ANISOU 223 CD1 PHE A 56 2452 2880 1068 404 −23 −167 C ATOM 224 CD2 PHE A 56 71.055 71.201 112.196 1.00 18.24 C ANISOU 224 CD2 PHE A 56 2931 2790 1208 698 −216 −242 C ATOM 225 CE1 PHE A 56 73.799 71.336 112.489 1.00 18.09 C ANISOU 225 CE1 PHE A 56 2671 2660 1543 254 −135 33 C ATOM 226 CE2 PHE A 56 71.672 72.424 112.350 1.00 18.75 C ANISOU 226 CE2 PHE A 56 3314 2594 1215 992 −146 47 C ATOM 227 CZ PHE A 56 73.044 72.498 112.499 1.00 19.20 C ANISOU 227 CZ PHE A 56 2868 2945 1483 769 −282 209 C ATOM 228 O SER A 57 72.963 71.288 116.247 1.00 28.67 O ANISOU 228 O SER A 57 4434 4296 2164 −383 −224 −589 O ATOM 229 N SER A 57 71.717 68.753 115.329 1.00 18.02 N ANISOU 229 N SER A 57 2800 2847 1201 188 −7 −553 N ATOM 230 C SER A 57 71.786 70.943 116.340 1.00 23.95 C ANISOU 230 C SER A 57 3948 3464 1686 −163 413 −550 C ATOM 231 CA ASER A 57 71.423 69.491 116.554 0.77 22.72 C ANISOU 231 CA ASER A 57 4043 2959 1631 −461 30 −474 C ATOM 232 CB ASER A 57 72.223 68.928 117.732 0.77 30.41 C ANISOU 232 CB ASER A 57 5609 3756 2191 474 327 −332 C ATOM 233 OG ASER A 57 71.849 67.590 118.015 0.77 34.14 O ANISOU 233 OG ASER A 57 6172 4402 2398 991 1022 349 O ATOM 234 CA BSER A 57 71.420 69.486 116.550 0.23 23.72 C ANISOU 234 CA BSER A 57 3848 3512 1653 84 94 −637 C ATOM 235 CB BSER A 57 72.202 68.908 117.731 0.23 23.65 C ANISOU 235 CB BSER A 57 4045 3455 1488 84 −21 −1017 C ATOM 236 OG BSER A 57 73.594 68.900 117.466 0.23 28.42 O ANISOU 236 OG BSER A 57 4828 4290 1681 482 −25 −918 O ATOM 237 O ASN A 58 71.189 73.518 118.344 1.00 27.11 O ANISOU 237 O ASN A 58 5348 3155 1798 104 864 119 O ATOM 238 N ASN A 58 70.768 71.791 116.263 1.00 24.93 N ANISOU 238 N ASN A 58 3932 3386 2153 284 553 −276 N ATOM 239 C ASN A 58 71.354 73.991 117.220 1.00 23.37 C ANISOU 239 C ASN A 58 3886 3066 1928 −258 482 −469 C ATOM 240 CG ASN A 58 68.497 73.622 116.272 1.00 31.16 C ANISOU 240 CG ASN A 58 5146 3958 2735 1225 93 −339 C ATOM 241 ND2 ASN A 58 67.605 74.596 116.245 1.00 31.49 N ANISOU 241 ND2 ASN A 58 5592 3808 2565 763 50 −124 N ATOM 242 CA ASN A 58 70.970 73.202 115.979 1.00 24.89 C ANISOU 242 CA ASN A 58 4103 3002 2353 77 363 −317 C ATOM 243 CB ASN A 58 69.700 73.793 115.373 1.00 27.45 C ANISOU 243 CB ASN A 58 4410 3654 2366 886 364 −69 C ATOM 244 O THR A 59 69.822 76.582 117.228 1.00 26.47 O ANISOU 244 O THR A 59 3897 4075 2086 −1292 108 100 O ATOM 245 N THR A 59 71.881 75.192 117.011 1.00 22.79 N ANISOU 245 N THR A 59 4037 2360 2261 114 694 −58 N ATOM 246 CA THR A 59 72.007 76.168 118.077 1.00 24.12 C ANISOU 246 CA THR A 59 4022 2483 2661 152 127 127 C ATOM 247 C THR A 59 70.733 76.974 117.958 1.00 19.72 C ANISOU 247 C THR A 59 3618 2271 1605 −534 396 56 C ATOM 248 CB THR A 59 73.225 77.093 117.891 1.00 26.52 C ANISOU 248 CB THR A 59 3290 3353 3436 71 −94 377 C ATOM 249 OG1 THR A 59 73.068 77.870 116.696 1.00 24.62 O ANISOU 249 OG1 THR A 59 3011 2918 3424 131 388 426 O ATOM 250 N SER A 60 70.659 78.091 118.656 1.00 23.62 N ANISOU 250 N SER A 60 4120 3135 1719 228 275 266 N ATOM 251 C SER A 60 69.462 79.724 117.267 1.00 24.75 C ANISOU 251 C SER A 60 3898 3733 1775 879 −15 362 C ATOM 252 O SER A 60 68.482 80.399 116.961 1.00 28.56 O ANISOU 252 O SER A 60 3860 4779 2210 1292 −166 218 O ATOM 253 CA ASER A 60 69.477 78.931 118.566 0.91 29.40 C ANISOU 253 CA ASER A 60 4487 4650 2035 1254 49 231 C ATOM 254 CB ASER A 60 69.417 79.880 119.760 0.91 34.07 C ANISOU 254 CB ASER A 60 5625 5190 2128 1589 57 −218 C ATOM 255 OG ASER A 60 70.576 80.690 119.801 0.91 37.81 O ANISOU 255 OG ASER A 60 6811 5070 2486 1709 −350 −846 O ATOM 256 CA BSER A 60 69.495 78.964 118.584 0.09 26.73 C ANISOU 256 CA BSER A 60 4577 3723 1857 980 101 224 C ATOM 257 CB BSER A 60 69.509 79.968 119.738 0.09 29.68 C ANISOU 257 CB BSER A 60 5463 3900 1913 1377 73 6 C ATOM 258 OG BSER A 60 69.485 79.315 120.993 0.09 31.59 O ANISOU 258 OG BSER A 60 5970 4055 1977 1408 12 −150 O ATOM 259 O GLU A 61 69.922 78.569 113.979 1.00 17.86 O ANISOU 259 O GLU A 61 3074 2315 1398 262 −62 −145 O ATOM 260 N GLU A 61 70.541 79.620 116.497 1.00 20.99 N ANISOU 260 N GLU A 61 3855 2731 1388 240 −25 71 N ATOM 261 CA GLU A 61 70.682 80.431 115.297 1.00 22.03 C ANISOU 261 CA GLU A 61 4064 3020 1286 325 −243 −275 C ATOM 262 C GLU A 61 70.069 79.789 114.059 1.00 17.74 C ANISOU 262 C GLU A 61 3292 2150 1298 203 −150 −12 C ATOM 263 CB GLU A 61 72.154 80.747 115.040 1.00 24.81 C ANISOU 263 CB GLU A 61 4484 3178 1763 −889 −577 −100 C ATOM 264 CG GLU A 61 72.879 81.390 116.212 1.00 33.93 C ANISOU 264 CG GLU A 61 6075 3794 3025 −353 −757 77 C ATOM 265 CD GLU A 61 72.273 82.716 116.634 1.00 37.67 C ANISOU 265 CD GLU A 61 6657 4334 3321 234 −1045 278 C ATOM 266 OE1 GLU A 61 71.806 83.471 115.757 1.00 38.90 O ANISOU 266 OE1 GLU A 61 7305 3901 3575 48 −1107 129 O ATOM 267 N SER A 62 69.721 80.633 113.095 1.00 18.16 N ANISOU 267 N SER A 62 3209 2204 1488 428 −98 −51 N ATOM 268 C SER A 62 70.110 79.264 111.090 1.00 14.71 C ANISOU 268 C SER A 62 2356 2015 1219 150 5 −155 C ATOM 269 O SER A 62 71.315 79.448 111.147 1.00 15.97 O ANISOU 269 O SER A 62 2723 2245 1101 106 89 −133 O ATOM 270 CA ASER A 62 69.160 80.196 111.815 0.84 17.43 C ANISOU 270 CA ASER A 62 3105 2302 1217 519 −145 −350 C ATOM 271 CB ASER A 62 68.895 81.411 110.920 0.84 20.15 C ANISOU 271 CB ASER A 62 3728 2145 1786 558 84 166 C ATOM 272 OG ASER A 62 68.170 82.409 111.607 0.84 22.31 O ANISOU 272 OG ASER A 62 3725 2681 2070 549 133 184 O ATOM 273 CA BSER A 62 69.143 80.170 111.842 0.16 17.49 C ANISOU 273 CA BSER A 62 2955 2302 1390 589 −90 −341 C ATOM 274 CB BSER A 62 68.752 81.362 110.966 0.16 18.11 C ANISOU 274 CB BSER A 62 3065 2452 1364 1104 −73 −581 C ATOM 275 OG BSER A 62 69.863 82.206 110.724 0.16 20.38 O ANISOU 275 OG BSER A 62 3356 2821 1568 1249 51 −638 O ATOM 276 N PHE A 63 69.559 78.286 110.382 1.00 14.78 N ANISOU 276 N PHE A 63 2556 1904 1155 149 −15 −152 N ATOM 277 CA PHE A 63 70.374 77.366 109.612 1.00 13.93 C ANISOU 277 CA PHE A 63 2492 1811 989 305 −72 −44 C ATOM 278 C PHE A 63 69.632 76.896 108.376 1.00 13.38 C ANISOU 278 C PHE A 63 2341 1838 903 306 7 78 C ATOM 279 O PHE A 63 68.421 77.053 108.270 1.00 14.28 O ANISOU 279 O PHE A 63 2286 2024 1115 481 −106 37 O ATOM 280 CB PHE A 63 70.785 76.151 110.449 1.00 15.23 C ANISOU 280 CB PHE A 63 2609 1969 1207 −50 −307 57 C ATOM 281 CG PHE A 63 69.633 75.271 110.865 1.00 14.79 C ANISOU 281 CG PHE A 63 2488 2036 1097 138 −282 −4 C ATOM 282 CD1 PHE A 63 69.309 74.123 110.149 1.00 15.78 C ANISOU 282 CD1 PHE A 63 2928 1697 1370 180 −222 237 C ATOM 283 CD2 PHE A 63 68.898 75.570 112.005 1.00 16.83 C ANISOU 283 CD2 PHE A 63 2847 2287 1261 11 −267 148 C ATOM 284 CE1 PHE A 63 68.257 73.305 110.549 1.00 16.54 C ANISOU 284 CE1 PHE A 63 3050 1963 1271 −3 33 −29 C ATOM 285 CE2 PHE A 63 67.846 74.762 112.403 1.00 18.09 C ANISOU 285 CE2 PHE A 63 2936 2408 1528 −214 127 21 C ATOM 286 CZ PHE A 63 67.529 73.623 111.672 1.00 18.05 C ANISOU 286 CZ PHE A 63 3212 2134 1513 −102 172 111 C ATOM 287 N VAL A 64 70.387 76.321 107.449 1.00 13.89 N ANISOU 287 N VAL A 64 2374 1895 1010 58 47 −203 N ATOM 288 CA VAL A 64 69.842 75.618 106.293 1.00 13.59 C ANISOU 288 CA VAL A 64 2410 1726 1029 122 23 −66 C ATOM 289 C VAL A 64 70.497 74.244 106.268 1.00 12.85 C ANISOU 289 C VAL A 64 1989 1701 1191 50 −17 −70 C ATOM 290 O VAL A 64 71.683 74.104 106.576 1.00 14.71 O ANISOU 290 O VAL A 64 1853 1840 1898 25 −186 −210 O ATOM 291 CB VAL A 64 70.160 76.379 104.979 1.00 15.12 C ANISOU 291 CB VAL A 64 2695 2026 1022 254 −124 −25 C ATOM 292 CG1 VAL A 64 69.871 75.536 103.725 1.00 17.25 C ANISOU 292 CG1 VAL A 64 3344 2244 966 69 66 −56 C ATOM 293 CG2 VAL A 64 69.387 77.690 104.961 1.00 16.93 C ANISOU 293 CG2 VAL A 64 3099 1948 1385 291 17 −32 C ATOM 294 N LEU A 65 69.709 73.230 105.941 1.00 13.31 N ANISOU 294 N LEU A 65 1854 1781 1422 68 −105 −12 N ATOM 295 C LEU A 65 70.026 71.455 104.347 1.00 14.47 C ANISOU 295 C LEU A 65 1918 1888 1692 375 −298 −235 C ATOM 296 O LEU A 65 68.898 71.352 103.873 1.00 17.15 O ANISOU 296 O LEU A 65 2053 2382 2080 402 −545 −622 O ATOM 297 CA ALEU A 65 70.221 71.884 105.802 0.73 13.54 C ANISOU 297 CA ALEU A 65 1945 1514 1686 26 −65 33 C ATOM 298 CB ALEU A 65 69.452 70.978 106.760 0.73 16.36 C ANISOU 298 CB ALEU A 65 2096 1694 2425 114 −107 411 C ATOM 299 CG ALEU A 65 70.018 69.616 107.123 0.73 17.07 C ANISOU 299 CG ALEU A 65 1843 2185 2458 15 290 105 C ATOM 300 CD1 ALEU A 65 71.343 69.787 107.861 0.73 17.78 C ANISOU 300 CD1 ALEU A 65 1801 2494 2460 14 −263 515 C ATOM 301 CD2 ALEU A 65 69.029 68.890 107.989 0.73 18.56 C ANISOU 301 CD2 ALEU A 65 2107 2515 2431 −227 372 212 C ATOM 302 CA BLEU A 65 70.206 71.869 105.784 0.27 16.45 C ANISOU 302 CA BLEU A 65 2203 2063 1984 84 −176 −18 C ATOM 303 CB BLEU A 65 69.407 70.899 106.641 0.27 19.74 C ANISOU 303 CB BLEU A 65 2579 2463 2458 144 −233 152 C ATOM 304 CG BLEU A 65 69.630 70.897 108.141 0.27 17.01 C ANISOU 304 CG BLEU A 65 2026 2263 2174 −162 −201 59 C ATOM 305 CD1 BLEU A 65 69.071 69.622 108.692 0.27 14.06 C ANISOU 305 CD1 BLEU A 65 1786 1776 1779 −382 −127 354 C ATOM 306 CD2 BLEU A 65 71.087 70.997 108.451 0.27 13.64 C ANISOU 306 CD2 BLEU A 65 1756 1684 1743 −256 45 97 C ATOM 307 N ASN A 66 71.133 71.229 103.651 1.00 14.31 N ANISOU 307 N ASN A 66 1991 1772 1674 206 −314 −424 N ATOM 308 CA ASN A 66 71.105 70.858 102.249 1.00 15.36 C ANISOU 308 CA ASN A 66 2298 1848 1689 290 −272 −387 C ATOM 309 C ASN A 66 71.382 69.361 102.106 1.00 14.40 C ANISOU 309 C ASN A 66 1958 1893 1620 429 −324 −227 C ATOM 310 O ASN A 66 72.203 68.783 102.842 1.00 16.44 O ANISOU 310 O ASN A 66 2291 2094 1862 406 −601 −403 O ATOM 311 CB ASN A 66 72.175 71.616 101.467 1.00 17.15 C ANISOU 311 CB ASN A 66 2706 1917 1891 287 −81 −163 C ATOM 312 CG ASN A 66 71.791 73.042 101.133 1.00 18.64 C ANISOU 312 CG ASN A 66 3139 1723 2220 102 −338 −95 C ATOM 313 OD1 ASN A 66 70.624 73.420 101.153 1.00 20.60 O ANISOU 313 OD1 ASN A 66 3423 2061 2342 712 −486 −88 O ATOM 314 ND2 ASN A 66 72.793 73.835 100.790 1.00 21.57 N ANISOU 314 ND2 ASN A 66 3650 1939 2606 5 −455 −177 N ATOM 315 N TRP A 67 70.722 68.738 101.138 1.00 12.75 N ANISOU 315 N TRP A 67 1839 1829 1177 182 −127 −220 N ATOM 316 CA TRP A 67 71.006 67.362 100.746 1.00 12.34 C ANISOU 316 CA TRP A 67 1935 1769 983 336 85 4 C ATOM 317 C TRP A 67 71.748 67.412 99.428 1.00 12.12 C ANISOU 317 C TRP A 67 1745 1726 1132 38 −118 −121 C ATOM 318 O TRP A 67 71.255 68.022 98.487 1.00 12.76 O ANISOU 318 O TRP A 67 1765 1909 1173 40 −90 97 O ATOM 319 CB TRP A 67 69.687 66.619 100.566 1.00 12.68 C ANISOU 319 CB TRP A 67 1649 1773 1396 −95 44 −48 C ATOM 320 CG TRP A 67 69.816 65.171 100.211 1.00 11.92 C ANISOU 320 CG TRP A 67 1671 2022 836 43 34 5 C ATOM 321 CD1 TRP A 67 70.914 64.362 100.346 1.00 13.13 C ANISOU 321 CD1 TRP A 67 1850 1870 1269 −3 −103 −134 C ATOM 322 CD2 TRP A 67 68.780 64.353 99.670 1.00 11.88 C ANISOU 322 CD2 TRP A 67 1715 1951 848 3 217 75 C ATOM 323 NE1 TRP A 67 70.614 63.082 99.912 1.00 12.66 N ANISOU 323 NE1 TRP A 67 1567 2116 1129 −51 157 −68 N ATOM 324 CE2 TRP A 67 69.313 63.058 99.494 1.00 11.56 C ANISOU 324 CE2 TRP A 67 1601 2028 763 −78 283 −48 C ATOM 325 CE3 TRP A 67 67.443 64.590 99.334 1.00 13.96 C ANISOU 325 CE3 TRP A 67 1526 2406 1370 −12 75 149 C ATOM 326 CZ2 TRP A 67 68.545 62.004 99.001 1.00 13.02 C ANISOU 326 CZ2 TRP A 67 1706 2270 971 −215 253 −82 C ATOM 327 CZ3 TRP A 67 66.687 63.547 98.857 1.00 14.78 C ANISOU 327 CZ3 TRP A 67 1737 2393 1484 −350 −53 101 C ATOM 328 CH2 TRP A 67 67.240 62.277 98.680 1.00 14.74 C ANISOU 328 CH2 TRP A 67 1988 2096 1519 −57 −105 −40 C ATOM 329 N TYR A 68 72.924 66.784 99.370 1.00 12.48 N ANISOU 329 N TYR A 68 1803 1913 1027 133 118 −62 N ATOM 330 CA TYR A 68 73.749 66.782 98.173 1.00 13.15 C ANISOU 330 CA TYR A 68 2092 1608 1295 −25 24 −8 C ATOM 331 C TYR A 68 73.969 65.385 97.631 1.00 12.46 C ANISOU 331 C TYR A 68 1801 1927 1008 105 167 −18 C ATOM 332 O TYR A 68 74.116 64.411 98.386 1.00 13.68 O ANISOU 332 O TYR A 68 2142 2007 1049 282 −33 39 O ATOM 333 CB TYR A 68 75.143 67.323 98.478 1.00 15.77 C ANISOU 333 CB TYR A 68 2074 2117 1802 −148 286 −228 C ATOM 334 CG TYR A 68 75.178 68.725 99.014 1.00 15.67 C ANISOU 334 CG TYR A 68 2062 2014 1878 −115 −125 −226 C ATOM 335 CD1 TYR A 68 75.113 69.821 98.166 1.00 17.48 C ANISOU 335 CD1 TYR A 68 2477 2023 2140 −49 −324 232 C ATOM 336 CD2 TYR A 68 75.288 68.955 100.372 1.00 18.50 C ANISOU 336 CD2 TYR A 68 2933 2221 1875 183 −251 −541 C ATOM 337 CE1 TYR A 68 75.175 71.111 98.659 1.00 19.19 C ANISOU 337 CE1 TYR A 68 2777 1944 2571 −58 −346 −164 C ATOM 338 CE2 TYR A 68 75.348 70.238 100.873 1.00 21.38 C ANISOU 338 CE2 TYR A 68 3262 2316 2547 −13 −230 −261 C ATOM 339 CZ TYR A 68 75.294 71.308 100.011 1.00 19.89 C ANISOU 339 CZ TYR A 68 2755 1961 2842 −64 −353 −521 C ATOM 340 OH TYR A 68 75.357 72.575 100.515 1.00 25.60 O ANISOU 340 OH TYR A 68 3976 2269 3481 419 −449 −816 O ATOM 341 N ARG A 69 74.047 65.292 96.309 1.00 13.12 N ANISOU 341 N ARG A 69 1946 1920 1120 27 134 −12 N ATOM 342 CA ARG A 69 74.641 64.137 95.662 1.00 13.65 C ANISOU 342 CA ARG A 69 2058 2055 1073 −134 188 −182 C ATOM 343 C ARG A 69 76.071 64.515 95.332 1.00 15.57 C ANISOU 343 C ARG A 69 2385 1745 1788 −99 292 85 C ATOM 344 O ARG A 69 76.319 65.587 94.782 1.00 17.91 O ANISOU 344 O ARG A 69 2389 2222 2193 −37 486 148 O ATOM 345 CB ARG A 69 73.878 63.763 94.406 1.00 15.79 C ANISOU 345 CB ARG A 69 2497 2444 1061 −107 199 −400 C ATOM 346 CG ARG A 69 74.444 62.548 93.739 1.00 18.45 C ANISOU 346 CG ARG A 69 2955 2486 1571 134 −4 −437 C ATOM 347 CD ARG A 69 73.515 62.067 92.657 1.00 20.16 C ANISOU 347 CD ARG A 69 3537 2681 1443 −116 −15 −668 C ATOM 348 NE ARG A 69 74.000 60.832 92.066 1.00 22.13 N ANISOU 348 NE ARG A 69 3985 3058 1364 207 37 −248 N ATOM 349 CZ ARG A 69 73.401 60.204 91.056 1.00 20.16 C ANISOU 349 CZ ARG A 69 4133 2458 1069 −241 106 −1 C ATOM 350 NH1 ARG A 69 72.297 60.705 90.521 1.00 24.37 N ANISOU 350 NH1 ARG A 69 4156 3285 1817 −776 398 −325 N ATOM 351 NH2 ARG A 69 73.922 59.100 90.559 1.00 25.49 N ANISOU 351 NH2 ARG A 69 5407 2586 1692 156 20 145 N ATOM 352 O MET A 70 78.519 62.145 93.955 1.00 26.67 O ANISOU 352 O MET A 70 3096 3335 3703 −118 826 −479 O ATOM 353 N MET A 70 77.005 63.634 95.676 1.00 16.93 N ANISOU 353 N MET A 70 2006 1914 2513 15 292 −133 N ATOM 354 C MET A 70 79.055 63.153 94.403 1.00 24.24 C ANISOU 354 C MET A 70 2963 2574 3672 42 501 42 C ATOM 355 CA AMET A 70 78.443 63.891 95.587 0.74 19.88 C ANISOU 355 CA AMET A 70 2329 2256 2967 244 −102 64 C ATOM 356 CB AMET A 70 79.155 63.453 96.880 0.74 18.43 C ANISOU 356 CB AMET A 70 2519 1941 2543 176 −335 133 C ATOM 357 CG AMET A 70 78.608 64.127 98.134 0.74 19.82 C ANISOU 357 CG AMET A 70 2393 2745 2395 −235 −82 −231 C ATOM 358 SD AMET A 70 78.836 65.908 98.115 0.74 19.75 S ANISOU 358 SD AMET A 70 2392 2996 2117 19 95 −115 S ATOM 359 CE AMET A 70 80.624 65.982 98.207 0.74 23.24 C ANISOU 359 CE AMET A 70 2813 3622 2394 −88 133 −425 C ATOM 360 CA BMET A 70 78.408 63.972 95.506 0.26 25.11 C ANISOU 360 CA BMET A 70 2866 2847 3829 41 410 −103 C ATOM 361 CB BMET A 70 79.172 63.793 96.817 0.26 32.43 C ANISOU 361 CB BMET A 70 3612 3793 4915 33 576 −150 C ATOM 362 CG BMET A 70 80.538 64.448 96.821 0.26 38.99 C ANISOU 362 CG BMET A 70 4371 4666 5779 124 765 −201 C ATOM 363 SD BMET A 70 80.492 66.247 96.836 0.26 41.31 S ANISOU 363 SD BMET A 70 4516 5319 5860 755 920 −426 S ATOM 364 CE BMET A 70 79.803 66.560 98.459 0.26 39.32 C ANISOU 364 CE BMET A 70 4138 4795 6006 163 1008 −422 C ATOM 365 O GLN A 75 79.533 67.314 93.156 1.00 59.81 O ANISOU 365 O GLN A 75 5496 6775 10454 −367 3926 570 O ATOM 366 N GLN A 75 82.467 67.453 93.351 1.00 65.58 N ANISOU 366 N GLN A 75 6279 7002 11637 −69 3815 −22 N ATOM 367 CA GLN A 75 81.558 68.591 93.278 1.00 64.14 C ANISOU 367 CA GLN A 75 6119 6868 11382 −99 3743 161 C ATOM 368 C GLN A 75 80.156 68.203 93.734 1.00 61.67 C ANISOU 368 C GLN A 75 5856 6752 10823 −38 3546 338 C ATOM 369 CB GLN A 75 81.512 69.152 91.856 1.00 69.11 C ANISOU 369 CB GLN A 75 6803 7535 11921 435 3706 68 C ATOM 370 O PRO A 76 77.317 70.261 93.947 1.00 37.41 O ANISOU 370 O PRO A 76 4445 2739 7031 −487 1773 1170 O ATOM 371 N PRO A 76 79.659 68.865 94.784 1.00 47.65 N ANISOU 371 N PRO A 76 4178 4699 9229 −429 2977 379 N ATOM 372 C PRO A 76 77.209 69.141 94.450 1.00 34.74 C ANISOU 372 C PRO A 76 3765 2706 6728 −488 2096 632 C ATOM 373 CA PRO A 76 78.326 68.582 95.323 1.00 41.79 C ANISOU 373 CA PRO A 76 3727 3934 8216 −348 2638 391 C ATOM 374 CB PRO A 76 78.341 69.304 96.672 1.00 48.42 C ANISOU 374 CB PRO A 76 4224 5386 8785 205 2965 611 C ATOM 375 CG PRO A 76 79.296 70.429 96.478 1.00 51.38 C ANISOU 375 CG PRO A 76 4505 5874 9144 453 3196 784 C ATOM 376 CD PRO A 76 80.361 69.905 95.557 1.00 51.62 C ANISOU 376 CD PRO A 76 4374 5909 9329 579 3152 626 C ATOM 377 O ASP A 77 73.450 67.872 95.183 1.00 17.09 O ANISOU 377 O ASP A 77 2573 1931 1989 −78 179 418 O ATOM 378 N ASP A 77 76.148 68.364 94.274 1.00 27.61 N ANISOU 378 N ASP A 77 3182 2248 5058 −51 2019 303 N ATOM 379 CA ASP A 77 74.960 68.844 93.585 1.00 25.29 C ANISOU 379 CA ASP A 77 3260 2429 3921 108 1406 651 C ATOM 380 C ASP A 77 73.819 68.890 94.596 1.00 19.12 C ANISOU 380 C ASP A 77 2645 1864 2756 −154 388 395 C ATOM 381 CB ASP A 77 74.587 67.934 92.417 1.00 33.66 C ANISOU 381 CB ASP A 77 4555 3599 4635 53 1470 606 C ATOM 382 CG ASP A 77 73.296 68.361 91.738 1.00 39.65 C ANISOU 382 CG ASP A 77 5496 4491 5077 −212 1645 670 C ATOM 383 OD2 ASP A 77 72.636 67.506 91.111 1.00 43.65 O ANISOU 383 OD2 ASP A 77 5964 5343 5278 −604 1573 886 O ATOM 384 N LYS A 78 73.265 70.077 94.812 1.00 18.13 N ANISOU 384 N LYS A 78 2656 2021 2211 −292 128 738 N ATOM 385 C LYS A 78 70.900 69.679 95.252 1.00 17.91 C ANISOU 385 C LYS A 78 2582 2405 1820 110 −120 778 C ATOM 386 O LYS A 78 70.459 70.061 94.175 1.00 23.29 O ANISOU 386 O LYS A 78 3262 3409 2177 −475 −462 1288 O ATOM 387 CD LYS A 78 70.844 73.246 97.792 1.00 31.36 C ANISOU 387 CD LYS A 78 5027 3368 3521 167 147 139 C ATOM 388 CE LYS A 78 70.602 74.229 96.682 1.00 36.57 C ANISOU 388 CE LYS A 78 5609 4344 3941 9 135 −87 C ATOM 389 CA LYS A 78 72.205 70.235 95.798 1.00 18.66 C ANISOU 389 CA LYS A 78 2733 1988 2368 −187 219 468 C ATOM 390 CB LYS A 78 72.024 71.697 96.202 1.00 20.26 C ANISOU 390 CB LYS A 78 2983 2140 2575 −67 194 403 C ATOM 391 CG LYS A 78 70.942 71.840 97.253 1.00 23.00 C ANISOU 391 CG LYS A 78 3743 2305 2690 17 188 328 C ATOM 392 N LEU A 79 70.300 68.761 95.995 1.00 14.93 N ANISOU 392 N LEU A 79 2193 2021 1459 60 11 346 N ATOM 393 CA LEU A 79 69.061 68.106 95.585 1.00 14.87 C ANISOU 393 CA LEU A 79 2146 2203 1299 80 −138 17 C ATOM 394 C LEU A 79 67.813 68.749 96.155 1.00 15.07 C ANISOU 394 C LEU A 79 2034 2226 1466 197 −275 −45 C ATOM 395 O LEU A 79 66.782 68.816 95.495 1.00 17.12 O ANISOU 395 O LEU A 79 2255 2712 1537 228 −311 11 O ATOM 396 CB LEU A 79 69.085 66.648 96.040 1.00 15.38 C ANISOU 396 CB LEU A 79 2206 2080 1556 238 145 −62 C ATOM 397 CG LEU A 79 70.270 65.839 95.514 1.00 15.34 C ANISOU 397 CG LEU A 79 2239 2083 1505 70 32 8 C ATOM 398 CD1 LEU A 79 70.353 64.513 96.244 1.00 16.98 C ANISOU 398 CD1 LEU A 79 2645 1939 1867 38 426 −10 C ATOM 399 CD2 LEU A 79 70.165 65.634 94.019 1.00 18.66 C ANISOU 399 CD2 LEU A 79 2815 3182 1095 460 48 −201 C ATOM 400 N ALA A 80 67.907 69.182 97.401 1.00 15.22 N ANISOU 400 N ALA A 80 2270 2164 1350 219 −209 −35 N ATOM 401 CA ALA A 80 66.769 69.690 98.152 1.00 14.17 C ANISOU 401 CA ALA A 80 1958 2196 1229 123 −92 −176 C ATOM 402 C ALA A 80 67.304 70.274 99.444 1.00 13.34 C ANISOU 402 C ALA A 80 1931 1846 1290 167 −139 151 C ATOM 403 O ALA A 80 68.460 70.050 99.797 1.00 14.84 O ANISOU 403 O ALA A 80 2009 2141 1489 297 −266 −77 O ATOM 404 CB ALA A 80 65.763 68.572 98.437 1.00 17.46 C ANISOU 404 CB ALA A 80 2376 2541 1717 −366 2 −212 C ATOM 405 N ALA A 81 66.476 71.050 100.129 1.00 14.26 N ANISOU 405 N ALA A 81 1911 1978 1529 347 −270 −112 N ATOM 406 CA ALA A 81 66.912 71.740 101.333 1.00 15.46 C ANISOU 406 CA ALA A 81 2038 2197 1641 −10 −151 −273 C ATOM 407 C ALA A 81 65.792 71.876 102.346 1.00 13.84 C ANISOU 407 C ALA A 81 1708 1729 1820 230 −67 11 C ATOM 408 O ALA A 81 64.607 71.836 101.996 1.00 14.92 O ANISOU 408 O ALA A 81 1770 2029 1870 55 −148 −141 O ATOM 409 CB ALA A 81 67.444 73.129 100.979 1.00 19.24 C ANISOU 409 CB ALA A 81 2786 2332 2194 −609 230 −380 C ATOM 410 O PHE A 82 67.093 73.937 105.446 1.00 17.78 O ANISOU 410 O PHE A 82 1865 2618 2271 447 −361 −609 O ATOM 411 N PHE A 82 66.194 72.068 103.599 1.00 14.65 N ANISOU 411 N PHE A 82 2045 2056 1468 294 −98 −213 N ATOM 412 CA PHE A 82 65.325 72.541 104.665 1.00 15.78 C ANISOU 412 CA PHE A 82 2180 1991 1827 128 −46 −218 C ATOM 413 C PHE A 82 65.901 73.845 105.213 1.00 15.26 C ANISOU 413 C PHE A 82 2013 2063 1722 386 −47 −247 C ATOM 414 CB PHE A 82 65.234 71.552 105.828 1.00 17.84 C ANISOU 414 CB PHE A 82 2955 2220 1603 557 −3 151 C ATOM 415 CG PHE A 82 64.555 72.136 107.043 1.00 17.96 C ANISOU 415 CG PHE A 82 3276 2085 1465 469 −43 138 C ATOM 416 CD1 PHE A 82 63.187 72.065 107.164 1.00 20.00 C ANISOU 416 CD1 PHE A 82 2822 2710 2069 −17 230 445 C ATOM 417 CD2 PHE A 82 65.277 72.803 108.032 1.00 20.15 C ANISOU 417 CD2 PHE A 82 4186 2211 1258 819 −276 −34 C ATOM 418 CE1 PHE A 82 62.546 72.627 108.257 1.00 20.60 C ANISOU 418 CE1 PHE A 82 3319 2722 1785 298 551 94 C ATOM 419 CE2 PHE A 82 64.641 73.377 109.121 1.00 21.22 C ANISOU 419 CE2 PHE A 82 4330 1975 1759 257 8 264 C ATOM 420 CZ PHE A 82 63.275 73.276 109.236 1.00 21.54 C ANISOU 420 CZ PHE A 82 3444 2628 2110 138 374 212 C ATOM 421 O APRO A 83 64.534 75.084 102.806 0.78 17.31 O ANISOU 421 O APRO A 83 2881 2017 1681 −373 95 −57 O ATOM 422 N APRO A 83 65.057 74.863 105.424 0.78 13.97 N ANISOU 422 N APRO A 83 1879 1971 1456 265 26 18 N ATOM 423 CA APRO A 83 63.649 74.965 105.036 0.78 14.86 C ANISOU 423 CA APRO A 83 2040 2040 1566 477 6 −17 C ATOM 424 C APRO A 83 63.534 74.923 103.518 0.78 15.20 C ANISOU 424 C APRO A 83 2282 1663 1830 −51 0 91 C ATOM 425 CB APRO A 83 63.245 76.357 105.547 0.78 17.53 C ANISOU 425 CB APRO A 83 2598 2308 1753 749 −85 −356 C ATOM 426 CG APRO A 83 64.219 76.672 106.610 0.78 19.00 C ANISOU 426 CG APRO A 83 2894 2303 2023 780 −236 −334 C ATOM 427 CD APRO A 83 65.509 76.055 106.161 0.78 16.76 C ANISOU 427 CD APRO A 83 2557 2022 1790 498 −384 −407 C ATOM 428 O BPRO A 83 64.504 75.290 102.883 0.22 16.75 O ANISOU 428 O BPRO A 83 2733 2012 1618 429 −43 747 O ATOM 429 N BPRO A 83 65.052 74.862 105.416 0.22 19.74 N ANISOU 429 N BPRO A 83 2486 2470 2545 100 85 13 N ATOM 430 CA BPRO A 83 63.634 74.855 105.058 0.22 20.73 C ANISOU 430 CA BPRO A 83 2647 2668 2563 256 1 190 C ATOM 431 C BPRO A 83 63.513 74.970 103.550 0.22 20.60 C ANISOU 431 C BPRO A 83 2844 2629 2354 123 −151 511 C ATOM 432 CB BPRO A 83 63.107 76.121 105.731 0.22 21.65 C ANISOU 432 CB BPRO A 83 2699 2693 2834 91 139 153 C ATOM 433 CG BPRO A 83 64.268 77.037 105.735 0.22 19.42 C ANISOU 433 CG BPRO A 83 2355 2419 2605 124 166 236 C ATOM 434 CD BPRO A 83 65.477 76.166 105.954 0.22 17.84 C ANISOU 434 CD BPRO A 83 2283 2088 2407 −41 259 152 C ATOM 435 O GLU A 84 62.190 77.212 101.837 1.00 23.62 O ANISOU 435 O GLU A 84 3166 3247 2561 −336 −386 1188 O ATOM 436 N GLU A 84 62.333 74.688 103.015 1.00 19.02 N ANISOU 436 N GLU A 84 2551 2553 2124 −411 −461 633 N ATOM 437 C GLU A 84 62.522 76.236 101.167 1.00 23.36 C ANISOU 437 C GLU A 84 3268 3027 2579 −822 −552 684 C ATOM 438 CA AGLU A 84 62.118 74.820 101.583 0.78 22.42 C ANISOU 438 CA AGLU A 84 3205 3051 2263 −774 −859 684 C ATOM 439 CB AGLU A 84 60.665 74.546 101.218 0.78 26.82 C ANISOU 439 CB AGLU A 84 3306 4177 2706 −1277 −1119 711 C ATOM 440 CG AGLU A 84 60.416 74.454 99.721 0.78 31.73 C ANISOU 440 CG AGLU A 84 3984 4919 3152 −1016 −1297 512 C ATOM 441 CA BGLU A 84 62.129 74.823 101.582 0.22 23.88 C ANISOU 441 CA BGLU A 84 3269 3142 2660 −325 −468 620 C ATOM 442 CB BGLU A 84 60.685 74.506 101.189 0.22 28.06 C ANISOU 442 CB BGLU A 84 3669 3804 3189 206 −366 532 C ATOM 443 CG BGLU A 84 59.638 75.324 101.920 0.22 24.44 C ANISOU 443 CG BGLU A 84 3119 3391 2774 862 −219 455 C ATOM 444 O ASP A 85 61.949 78.209 98.274 1.00 25.20 O ANISOU 444 O ASP A 85 3930 3398 2248 −53 −857 48 O ATOM 445 N ASP A 85 63.268 76.331 100.081 1.00 21.43 N ANISOU 445 N ASP A 85 3677 2558 1909 −557 −542 607 N ATOM 446 C ASP A 85 62.725 78.547 99.165 1.00 21.13 C ANISOU 446 C ASP A 85 3274 2668 2086 −480 −587 278 C ATOM 447 CG ASP A 85 65.361 78.608 97.908 1.00 22.45 C ANISOU 447 CG ASP A 85 3991 2525 2014 −834 −400 −112 C ATOM 448 OD1 ASP A 85 65.532 79.599 98.641 1.00 20.09 O ANISOU 448 OD1 ASP A 85 2992 2515 2125 −310 −400 42 O ATOM 449 OD2 ASP A 85 65.626 78.606 96.696 1.00 28.08 O ANISOU 449 OD2 ASP A 85 5417 3188 2066 −1047 29 −280 O ATOM 450 CA AASP A 85 63.823 77.599 99.639 0.50 21.48 C ANISOU 450 CA AASP A 85 3594 2559 2009 −607 −498 404 C ATOM 451 CB AASP A 85 64.821 77.340 98.512 0.50 22.67 C ANISOU 451 CB AASP A 85 3962 2620 2032 −713 −443 111 C ATOM 452 CA BASP A 85 63.823 77.599 99.639 0.50 21.47 C ANISOU 452 CA BASP A 85 3593 2557 2008 −606 −497 405 C ATOM 453 CB BASP A 85 64.821 77.340 98.512 0.50 22.69 C ANISOU 453 CB BASP A 85 3964 2622 2034 −714 −442 113 C ATOM 454 O ARG A 86 61.763 82.988 98.452 1.00 22.95 O ANISOU 454 O ARG A 86 2562 2977 3179 −9 −100 682 O ATOM 455 N ARG A 86 62.665 79.733 99.766 1.00 20.17 N ANISOU 455 N ARG A 86 2853 2802 2009 −407 −366 458 N ATOM 456 CA ARG A 86 61.711 80.764 99.362 1.00 20.70 C ANISOU 456 CA ARG A 86 2371 3069 2423 −796 70 134 C ATOM 457 C ARG A 86 62.392 81.958 98.685 1.00 20.61 C ANISOU 457 C ARG A 86 2465 2787 2577 −296 −394 292 C ATOM 458 CB ARG A 86 60.891 81.237 100.561 1.00 26.57 C ANISOU 458 CB ARG A 86 3126 3810 3159 −519 363 443 C ATOM 459 CG ARG A 86 59.936 80.187 101.095 1.00 28.39 C ANISOU 459 CG ARG A 86 3490 3724 3573 −743 369 492 C ATOM 460 CD ARG A 86 58.831 79.901 100.093 1.00 31.18 C ANISOU 460 CD ARG A 86 3877 4040 3929 −1020 436 425 C ATOM 461 O SER A 87 64.635 83.665 95.428 1.00 20.78 O ANISOU 461 O SER A 87 3764 2006 2125 −347 −216 27 O ATOM 462 N SER A 87 63.678 81.824 98.373 1.00 17.97 N ANISOU 462 N SER A 87 2511 2503 1812 −510 −166 −102 N ATOM 463 CA SER A 87 64.399 82.880 97.670 1.00 17.63 C ANISOU 463 CA SER A 87 2430 2367 1901 −463 4 −332 C ATOM 464 C SER A 87 64.296 82.740 96.160 1.00 17.95 C ANISOU 464 C SER A 87 2911 1944 1967 −267 −225 −86 C ATOM 465 CB SER A 87 65.876 82.882 98.068 1.00 17.44 C ANISOU 465 CB SER A 87 2583 2262 1780 −372 125 −606 C ATOM 466 OG SER A 87 66.572 81.799 97.475 1.00 17.39 O ANISOU 466 OG SER A 87 2815 2448 1346 −305 −12 −237 O ATOM 467 O GLN A 88 61.787 80.040 95.023 1.00 20.77 O ANISOU 467 O GLN A 88 3440 2502 1950 −582 −513 267 O ATOM 468 N GLN A 88 63.852 81.572 95.705 1.00 18.09 N ANISOU 468 N GLN A 88 2977 2093 1805 −272 −409 42 N ATOM 469 CA GLN A 88 63.696 81.272 94.289 1.00 19.08 C ANISOU 469 CA GLN A 88 3031 2430 1788 −132 −535 −12 C ATOM 470 C GLN A 88 62.354 80.595 94.076 1.00 19.03 C ANISOU 470 C GLN A 88 3191 2241 1801 −454 −468 355 C ATOM 471 CB GLN A 88 64.812 80.326 93.837 1.00 20.35 C ANISOU 471 CB GLN A 88 2830 3218 1684 −3 −456 −330 C ATOM 472 CG GLN A 88 66.212 80.903 93.946 1.00 22.21 C ANISOU 472 CG GLN A 88 3071 3837 1530 −58 −336 −146 C ATOM 473 CD GLN A 88 66.479 81.994 92.928 1.00 23.77 C ANISOU 473 CD GLN A 88 3083 4614 1336 55 −482 −412 C ATOM 474 OE1 GLN A 88 65.631 82.310 92.087 1.00 28.49 O ANISOU 474 OE1 GLN A 88 3633 5636 1555 −355 −399 475 O ATOM 475 NE2 GLN A 88 67.671 82.572 92.993 1.00 24.25 N ANISOU 475 NE2 GLN A 88 2930 4646 1637 −287 −219 −420 N ATOM 476 O PRO A 89 61.745 77.831 92.863 1.00 25.02 O ANISOU 476 O PRO A 89 4635 2982 1888 −1212 −947 440 O ATOM 477 N PRO A 89 61.852 80.600 92.827 1.00 21.31 N ANISOU 477 N PRO A 89 3510 2583 2004 −597 −717 541 N ATOM 478 CA PRO A 89 60.590 79.906 92.557 1.00 23.52 C ANISOU 478 CA PRO A 89 3804 3239 1893 −1177 −974 676 C ATOM 479 C PRO A 89 60.665 78.422 92.888 1.00 26.08 C ANISOU 479 C PRO A 89 4289 3537 2084 −1006 −978 478 C ATOM 480 CB PRO A 89 60.410 80.072 91.047 1.00 25.55 C ANISOU 480 CB PRO A 89 4076 3659 1971 −856 −1060 627 C ATOM 481 CG PRO A 89 61.262 81.200 90.662 1.00 25.71 C ANISOU 481 CG PRO A 89 4079 3550 2141 −1092 −950 630 C ATOM 482 CD PRO A 89 62.413 81.216 91.614 1.00 21.71 C ANISOU 482 CD PRO A 89 3670 2839 1738 −419 −612 884 C ATOM 483 O GLY A 90 59.812 76.050 91.128 1.00 30.52 O ANISOU 483 O GLY A 90 5742 3916 1938 −1347 −515 151 O ATOM 484 N GLY A 90 59.515 77.833 93.186 1.00 26.56 N ANISOU 484 N GLY A 90 4633 3065 2395 −1226 −554 414 N ATOM 485 CA GLY A 90 59.443 76.416 93.473 1.00 28.69 C ANISOU 485 CA GLY A 90 5254 3596 2052 −1124 −258 209 C ATOM 486 C GLY A 90 59.880 75.596 92.278 1.00 27.73 C ANISOU 486 C GLY A 90 5532 3423 1582 −1150 −191 296 C ATOM 487 O GLN A 91 60.118 71.649 92.899 1.00 36.65 O ANISOU 487 O GLN A 91 7341 4045 2540 −647 −838 −23 O ATOM 488 N GLN A 91 60.346 74.387 92.555 1.00 30.58 N ANISOU 488 N GLN A 91 6500 3296 1822 −339 −451 −108 N ATOM 489 CA GLN A 91 60.777 73.483 91.507 1.00 32.88 C ANISOU 489 CA GLN A 91 6550 3649 2294 −431 −957 −253 C ATOM 490 C GLN A 91 60.198 72.101 91.759 1.00 35.00 C ANISOU 490 C GLN A 91 6948 3585 2767 −337 −981 83 C ATOM 491 CB GLN A 91 62.305 73.415 91.450 1.00 37.68 C ANISOU 491 CB GLN A 91 6800 4675 2842 −139 −1191 58 C ATOM 492 O ASP A 92 61.544 69.405 90.352 1.00 38.12 O ANISOU 492 O ASP A 92 6240 3836 4407 521 −84 2149 O ATOM 493 N ASP A 92 59.775 71.443 90.688 1.00 32.54 N ANISOU 493 N ASP A 92 6408 2878 3078 −125 −1248 −106 N ATOM 494 CA ASP A 92 59.289 70.075 90.779 1.00 33.32 C ANISOU 494 CA ASP A 92 6009 2884 3766 291 −1087 238 C ATOM 495 C ASP A 92 60.488 69.159 90.930 1.00 33.55 C ANISOU 495 C ASP A 92 5699 3030 4018 −227 −662 1287 C ATOM 496 CB ASP A 92 58.495 69.702 89.530 1.00 35.93 C ANISOU 496 CB ASP A 92 6034 3526 4091 988 −1266 −315 C ATOM 497 CG ASP A 92 57.367 70.670 89.253 1.00 39.20 C ANISOU 497 CG ASP A 92 6283 4264 4349 1570 −1146 −250 C ATOM 498 OD1 ASP A 92 57.594 71.644 88.503 1.00 40.93 O ANISOU 498 OD1 ASP A 92 6607 4537 4406 1865 −994 −332 O ATOM 499 N SER A 93 60.331 68.095 91.704 1.00 31.37 N ANISOU 499 N SER A 93 5045 3069 3807 −406 −1308 977 N ATOM 500 CA SER A 93 61.484 67.293 92.067 1.00 29.30 C ANISOU 500 CA SER A 93 4388 3190 3555 −688 −1461 996 C ATOM 501 C SER A 93 61.095 65.911 92.569 1.00 26.29 C ANISOU 501 C SER A 93 3690 3021 3277 −553 −841 720 C ATOM 502 O SER A 93 60.028 65.746 93.153 1.00 28.27 O ANISOU 502 O SER A 93 3223 3405 4113 319 −267 910 O ATOM 503 CB SER A 93 62.265 68.024 93.157 1.00 33.85 C ANISOU 503 CB SER A 93 5574 3390 3898 −1246 −1329 860 C ATOM 504 OG SER A 93 63.428 67.315 93.509 1.00 32.62 O ANISOU 504 OG SER A 93 5489 3552 3354 −1242 −1481 1245 O ATOM 505 N ARG A 94 61.963 64.926 92.342 1.00 20.30 N ANISOU 505 N ARG A 94 3048 2960 1704 −444 −480 450 N ATOM 506 CA ARG A 94 61.815 63.616 92.977 1.00 17.72 C ANISOU 506 CA ARG A 94 2618 2603 1514 −456 −264 284 C ATOM 507 C ARG A 94 62.415 63.607 94.374 1.00 15.29 C ANISOU 507 C ARG A 94 2054 2523 1233 −370 −64 327 C ATOM 508 O ARG A 94 62.303 62.615 95.078 1.00 17.63 O ANISOU 508 O ARG A 94 2799 2200 1700 −251 −196 418 O ATOM 509 CB ARG A 94 62.489 62.507 92.154 1.00 19.40 C ANISOU 509 CB ARG A 94 2916 2914 1541 177 −230 −45 C ATOM 510 CG ARG A 94 61.767 62.182 90.868 1.00 20.14 C ANISOU 510 CG ARG A 94 2701 3291 1660 −101 −596 396 C ATOM 511 CD ARG A 94 62.369 60.974 90.166 1.00 21.38 C ANISOU 511 CD ARG A 94 2991 3172 1961 131 −257 257 C ATOM 512 NE ARG A 94 63.783 61.189 89.899 1.00 19.16 N ANISOU 512 NE ARG A 94 2513 3131 1636 282 98 213 N ATOM 513 CZ ARG A 94 64.774 60.418 90.323 1.00 16.67 C ANISOU 513 CZ ARG A 94 2308 2686 1339 97 −15 55 C ATOM 514 NH1 ARG A 94 64.532 59.314 91.014 1.00 18.26 N ANISOU 514 NH1 ARG A 94 2371 3039 1528 −139 −16 269 N ATOM 515 NH2 ARG A 94 66.019 60.752 90.022 1.00 17.67 N ANISOU 515 NH2 ARG A 94 2506 2575 1632 −145 79 81 N ATOM 516 N PHE A 95 63.042 64.712 94.767 1.00 15.48 N ANISOU 516 N PHE A 95 2362 2305 1217 −366 −227 307 N ATOM 517 C PHE A 95 63.115 65.661 97.029 1.00 16.60 C ANISOU 517 C PHE A 95 2787 2168 1352 −19 56 166 C ATOM 518 O PHE A 95 62.652 66.756 96.706 1.00 21.26 O ANISOU 518 O PHE A 95 4079 2218 1783 440 −147 155 O ATOM 519 CA APHE A 95 63.802 64.764 96.008 0.60 15.40 C ANISOU 519 CA APHE A 95 2374 2299 1177 −447 −5 95 C ATOM 520 CB APHE A 95 65.241 65.225 95.738 0.60 17.70 C ANISOU 520 CB APHE A 95 2505 3070 1152 −728 −107 100 C ATOM 521 CG APHE A 95 66.005 64.304 94.818 0.60 17.06 C ANISOU 521 CG APHE A 95 2251 3242 987 −813 130 53 C ATOM 522 CD1 APHE A 95 66.807 63.294 95.328 0.60 17.27 C ANISOU 522 CD1 APHE A 95 2597 2718 1246 −1015 141 −247 C ATOM 523 CD2 APHE A 95 65.905 64.434 93.440 0.60 20.26 C ANISOU 523 CD2 APHE A 95 2394 4067 1236 −571 330 140 C ATOM 524 CE1 APHE A 95 67.501 62.438 94.481 0.60 17.41 C ANISOU 524 CE1 APHE A 95 2279 3093 1244 −940 −186 −347 C ATOM 525 CE2 APHE A 95 66.596 63.582 92.593 0.60 21.17 C ANISOU 525 CE2 APHE A 95 2329 4064 1650 −693 184 74 C ATOM 526 CZ APHE A 95 67.390 62.582 93.113 0.60 20.82 C ANISOU 526 CZ APHE A 95 2461 3930 1519 −763 98 −117 C ATOM 527 CA BPHE A 95 63.803 64.784 96.013 0.40 16.16 C ANISOU 527 CA BPHE A 95 2520 2210 1411 −371 67 144 C ATOM 528 CB BPHE A 95 65.197 65.343 95.753 0.40 17.84 C ANISOU 528 CB BPHE A 95 2637 2532 1608 −594 232 4 C ATOM 529 CG BPHE A 95 65.877 64.703 94.598 0.40 16.16 C ANISOU 529 CG BPHE A 95 2311 2590 1238 −798 417 −95 C ATOM 530 CD1 BPHE A 95 66.381 63.420 94.708 0.40 18.96 C ANISOU 530 CD1 BPHE A 95 2670 3203 1332 −218 432 −455 C ATOM 531 CD2 BPHE A 95 65.990 65.366 93.389 0.40 19.75 C ANISOU 531 CD2 BPHE A 95 2728 2891 1885 −726 169 −115 C ATOM 532 CE1 BPHE A 95 66.998 62.811 93.634 0.40 17.68 C ANISOU 532 CE1 BPHE A 95 2183 3157 1377 −1008 407 −220 C ATOM 533 CE2 BPHE A 95 66.610 64.764 92.313 0.40 20.84 C ANISOU 533 CE2 BPHE A 95 2649 3464 1804 −666 39 −127 C ATOM 534 CZ BPHE A 95 67.115 63.486 92.435 0.40 20.23 C ANISOU 534 CZ BPHE A 95 2400 3543 1744 −520 130 −205 C ATOM 535 N ARG A 96 63.058 65.186 98.264 1.00 15.57 N ANISOU 535 N ARG A 96 1877 2794 1246 141 43 160 N ATOM 536 C ARG A 96 63.220 65.897 100.582 1.00 15.94 C ANISOU 536 C ARG A 96 2303 2502 1250 282 324 −96 C ATOM 537 O ARG A 96 63.883 64.905 100.880 1.00 15.74 O ANISOU 537 O ARG A 96 2571 1970 1438 402 −38 −83 O ATOM 538 CG AARG A 96 60.052 65.904 100.483 0.74 32.33 C ANISOU 538 CG AARG A 96 3554 5716 3016 736 −21 140 C ATOM 539 CD AARG A 96 58.847 65.011 100.784 0.74 36.28 C ANISOU 539 CD AARG A 96 3912 5949 3924 −79 −103 −10 C ATOM 540 NE AARG A 96 57.943 64.855 99.646 0.74 34.69 N ANISOU 540 NE AARG A 96 3628 5549 4004 −469 258 307 N ATOM 541 CZ AARG A 96 56.791 64.189 99.693 0.74 35.88 C ANISOU 541 CZ AARG A 96 3718 5640 4274 −391 252 499 C ATOM 542 NH1 AARG A 96 56.400 63.611 100.823 0.74 30.40 N ANISOU 542 NH1 AARG A 96 3104 4637 3810 −282 554 836 N ATOM 543 NH2 AARG A 96 56.028 64.100 98.611 0.74 41.38 N ANISOU 543 NH2 AARG A 96 4540 6283 4901 −253 164 525 N ATOM 544 CA AARG A 96 62.362 65.896 99.317 0.74 19.49 C ANISOU 544 CA AARG A 96 2563 3664 1178 1066 222 56 C ATOM 545 CB AARG A 96 61.021 65.190 99.577 0.74 24.85 C ANISOU 545 CB AARG A 96 2264 5235 1942 1177 −175 −196 C ATOM 546 CG BARG A 96 60.088 65.290 98.485 0.26 30.44 C ANISOU 546 CG BARG A 96 3116 5402 3047 504 −45 56 C ATOM 547 CD BARG A 96 58.797 64.585 98.906 0.26 36.84 C ANISOU 547 CD BARG A 96 3987 6035 3975 316 17 116 C ATOM 548 NE BARG A 96 57.772 64.582 97.864 0.26 37.27 N ANISOU 548 NE BARG A 96 4071 5829 4260 −192 −48 152 N ATOM 549 CZ BARG A 96 56.614 63.931 97.958 0.26 37.23 C ANISOU 549 CZ BARG A 96 4054 5704 4388 −379 −16 259 C ATOM 550 NH1 BARG A 96 56.331 63.225 99.046 0.26 32.06 N ANISOU 550 NH1 BARG A 96 3381 4903 3897 −797 119 344 N ATOM 551 NH2 BARG A 96 55.737 63.986 96.963 0.26 39.77 N ANISOU 551 NH2 BARG A 96 4382 6063 4667 −215 −67 258 N ATOM 552 CA BARG A 96 62.462 65.896 99.317 0.26 19.09 C ANISOU 552 CA BARG A 96 2389 3427 1436 655 153 22 C ATOM 553 CB BARG A 96 61.121 65.190 99.577 0.26 26.16 C ANISOU 553 CB BARG A 96 2800 4814 2326 776 −32 −87 C ATOM 554 N VAL A 97 63.208 67.013 101.311 1.00 16.57 N ANISOU 554 N VAL A 97 2509 2406 1379 657 448 463 N ATOM 555 CA VAL A 97 63.741 67.064 102.662 1.00 15.24 C ANISOU 555 CA VAL A 97 2030 2151 1611 315 690 232 C ATOM 556 C VAL A 97 62.600 67.464 103.566 1.00 15.96 C ANISOU 556 C VAL A 97 2173 1951 1940 99 564 −94 C ATOM 557 O VAL A 97 61.918 68.460 103.320 1.00 17.51 O ANISOU 557 O VAL A 97 2300 2147 2206 502 494 106 O ATOM 558 CB VAL A 97 64.897 68.070 102.850 1.00 16.53 C ANISOU 558 CB VAL A 97 2032 2122 2125 147 563 216 C ATOM 559 CG1 VAL A 97 65.341 68.085 104.307 1.00 18.83 C ANISOU 559 CG1 VAL A 97 2266 2364 2526 −305 626 −540 C ATOM 560 CG2 VAL A 97 66.068 67.715 101.960 1.00 17.60 C ANISOU 560 CG2 VAL A 97 1986 2366 2335 175 453 398 C ATOM 561 N ATHR A 98 62.352 66.673 104.602 0.48 15.93 N ANISOU 561 N ATHR A 98 1793 2361 1897 −631 158 −349 N ATOM 562 CA ATHR A 98 61.291 66.993 105.553 0.48 22.15 C ANISOU 562 CA ATHR A 98 2567 3200 2648 −365 144 −387 C ATOM 563 C ATHR A 98 61.769 66.857 106.982 0.48 17.38 C ANISOU 563 C ATHR A 98 1729 3166 1707 61 309 −547 C ATOM 564 O ATHR A 98 62.313 65.826 107.373 0.48 19.03 O ANISOU 564 O ATHR A 98 2103 3872 1254 348 172 −428 O ATOM 565 CB ATHR A 98 60.077 66.065 105.408 0.48 21.66 C ANISOU 565 CB ATHR A 98 2887 2550 2793 −654 72 −204 C ATOM 566 OG1 ATHR A 98 60.494 64.707 105.595 0.48 21.51 O ANISOU 566 OG1 ATHR A 98 2728 2805 2641 −502 627 563 O ATOM 567 CG2 ATHR A 98 59.430 66.225 104.051 0.48 21.26 C ANISOU 567 CG2 ATHR A 98 2704 2440 2935 −493 −414 −49 C ATOM 568 N BTHR A 98 62.398 66.700 104.623 0.52 13.91 N ANISOU 568 N BTHR A 98 1623 2373 1290 590 627 142 N ATOM 569 CA BTHR A 98 61.323 66.996 105.538 0.52 14.20 C ANISOU 569 CA BTHR A 98 1773 2260 1365 172 587 245 C ATOM 570 C BTHR A 98 61.861 66.907 106.954 0.52 14.38 C ANISOU 570 C BTHR A 98 1555 2283 1627 89 636 −66 C ATOM 571 O BTHR A 98 62.591 65.981 107.291 0.52 17.26 O ANISOU 571 O BTHR A 98 2643 2172 1741 1137 460 243 O ATOM 572 CB BTHR A 98 60.157 66.020 105.321 0.52 16.05 C ANISOU 572 CB BTHR A 98 1919 3050 1131 96 521 66 C ATOM 573 OG1 BTHR A 98 59.816 65.993 103.927 0.52 17.77 O ANISOU 573 OG1 BTHR A 98 2067 3177 1509 92 36 −18 O ATOM 574 CG2 BTHR A 98 58.944 66.439 106.132 0.52 17.76 C ANISOU 574 CG2 BTHR A 98 1974 3490 1282 −250 465 19 C ATOM 575 N GLN A 99 61.522 67.891 107.773 1.00 16.48 N ANISOU 575 N GLN A 99 1987 2588 1687 231 214 −483 N ATOM 576 CA GLN A 99 61.857 67.853 109.172 1.00 15.12 C ANISOU 576 CA GLN A 99 1907 2066 1770 −125 375 −261 C ATOM 577 C GLN A 99 60.842 66.993 109.896 1.00 16.11 C ANISOU 577 C GLN A 99 1777 2258 2087 80 114 −346 C ATOM 578 O GLN A 99 59.647 67.216 109.763 1.00 18.16 O ANISOU 578 O GLN A 99 1838 2472 2591 −32 284 −379 O ATOM 579 CB GLN A 99 61.834 69.257 109.738 1.00 16.41 C ANISOU 579 CB GLN A 99 2386 2191 1657 −188 379 −423 C ATOM 580 CG GLN A 99 62.258 69.318 111.172 1.00 17.42 C ANISOU 580 CG GLN A 99 2535 2335 1751 −417 218 −300 C ATOM 581 CD GLN A 99 62.333 70.741 111.658 1.00 19.11 C ANISOU 581 CD GLN A 99 2949 2372 1939 136 276 −149 C ATOM 582 OE1 GLN A 99 61.439 71.545 111.383 1.00 21.45 O ANISOU 582 OE1 GLN A 99 3307 2763 2080 548 242 −130 O ATOM 583 NE2 GLN A 99 63.410 71.074 112.362 1.00 20.48 N ANISOU 583 NE2 GLN A 99 3155 2423 2201 −377 120 −401 N ATOM 584 N LEU A 100 61.301 66.004 110.655 1.00 15.04 N ANISOU 584 N LEU A 100 1871 2386 1459 −205 531 −266 N ATOM 585 CA LEU A 100 60.383 65.158 111.409 1.00 16.78 C ANISOU 585 CA LEU A 100 2203 2488 1684 −457 440 −398 C ATOM 586 C LEU A 100 59.901 65.913 112.646 1.00 17.14 C ANISOU 586 C LEU A 100 2145 2711 1657 −639 604 −720 C ATOM 587 O LEU A 100 60.516 66.901 113.061 1.00 18.94 O ANISOU 587 O LEU A 100 2393 2806 1999 −577 627 −691 O ATOM 588 CB LEU A 100 61.066 63.850 111.790 1.00 17.20 C ANISOU 588 CB LEU A 100 2408 2341 1785 −370 582 −186 C ATOM 589 CG LEU A 100 61.464 62.989 110.584 1.00 20.20 C ANISOU 589 CG LEU A 100 2679 2491 2504 −374 69 −754 C ATOM 590 CD1 LEU A 100 62.072 61.676 111.039 1.00 24.69 C ANISOU 590 CD1 LEU A 100 3217 2849 3315 −237 44 −306 C ATOM 591 CD2 LEU A 100 60.296 62.745 109.648 1.00 24.32 C ANISOU 591 CD2 LEU A 100 3287 3342 2610 337 −381 −985 C ATOM 592 O PRO A 101 58.879 67.123 116.438 1.00 28.28 O ANISOU 592 O PRO A 101 3373 4523 2848 −683 778 −1915 O ATOM 593 N PRO A 101 58.788 65.471 113.241 1.00 18.27 N ANISOU 593 N PRO A 101 2137 2770 2034 −574 700 −584 N ATOM 594 C PRO A 101 59.154 66.304 115.582 1.00 23.89 C ANISOU 594 C PRO A 101 2816 3818 2444 −1282 989 −1029 C ATOM 595 CA PRO A 101 58.231 66.199 114.382 1.00 21.55 C ANISOU 595 CA PRO A 101 2293 3662 2233 −815 984 −1149 C ATOM 596 CB PRO A 101 56.990 65.386 114.730 1.00 24.55 C ANISOU 596 CB PRO A 101 2332 4634 2363 −1116 884 −1196 C ATOM 597 CG PRO A 101 56.555 64.838 113.423 1.00 23.37 C ANISOU 597 CG PRO A 101 2468 3806 2607 −1008 918 −1023 C ATOM 598 CD PRO A 101 57.829 64.490 112.709 1.00 19.04 C ANISOU 598 CD PRO A 101 2120 3111 2003 −968 748 −801 C ATOM 599 O ASN A 102 62.906 67.290 117.402 1.00 21.80 O ANISOU 599 O ASN A 102 3401 3297 1586 −840 52 −564 O ATOM 600 N ASN A 102 60.227 65.534 115.661 1.00 22.60 N ANISOU 600 N ASN A 102 2582 4131 1874 −1060 613 −989 N ATOM 601 CA ASN A 102 61.164 65.749 116.763 1.00 22.20 C ANISOU 601 CA ASN A 102 2926 3793 1718 −970 330 −576 C ATOM 602 C ASN A 102 62.156 66.893 116.510 1.00 19.28 C ANISOU 602 C ASN A 102 2628 3282 1418 −849 292 −265 C ATOM 603 CB ASN A 102 61.876 64.453 117.168 1.00 22.66 C ANISOU 603 CB ASN A 102 3580 3404 1626 39 777 239 C ATOM 604 CG ASN A 102 62.942 64.015 116.171 1.00 26.42 C ANISOU 604 CG ASN A 102 4159 3706 2172 80 875 387 C ATOM 605 OD1 ASN A 102 63.103 64.589 115.091 1.00 25.28 O ANISOU 605 OD1 ASN A 102 3760 4004 1841 −237 1014 215 O ATOM 606 ND2 ASN A 102 63.680 62.975 116.540 1.00 31.94 N ANISOU 606 ND2 ASN A 102 4324 4873 2939 938 1039 494 N ATOM 607 O GLY A 103 65.039 68.934 113.819 1.00 22.76 O ANISOU 607 O GLY A 103 2323 3746 2580 −626 396 638 O ATOM 608 N GLY A 103 62.147 67.435 115.297 1.00 18.77 N ANISOU 608 N GLY A 103 2325 2931 1877 −439 312 −559 N ATOM 609 CA GLY A 103 62.990 68.571 114.963 1.00 19.17 C ANISOU 609 CA GLY A 103 2196 2956 2132 −591 318 −542 C ATOM 610 C GLY A 103 64.439 68.256 114.648 1.00 18.04 C ANISOU 610 C GLY A 103 2428 2448 1978 −426 101 −524 C ATOM 611 O ARG A 104 67.673 66.097 113.234 1.00 17.80 O ANISOU 611 O ARG A 104 2167 3047 1550 −143 135 −284 O ATOM 612 N ARG A 104 64.987 67.225 115.281 1.00 18.37 N ANISOU 612 N ARG A 104 2522 2933 1523 −215 349 −197 N ATOM 613 CA ARG A 104 66.385 66.830 115.106 1.00 19.14 C ANISOU 613 CA ARG A 104 2564 3213 1496 −84 83 −183 C ATOM 614 C ARG A 104 66.619 66.005 113.853 1.00 17.14 C ANISOU 614 C ARG A 104 2167 2919 1425 −338 159 −126 C ATOM 615 CB ARG A 104 66.836 66.009 116.312 1.00 26.16 C ANISOU 615 CB ARG A 104 3444 4974 1523 883 −139 62 C ATOM 616 CG ARG A 104 68.186 65.337 116.143 1.00 32.58 C ANISOU 616 CG ARG A 104 4231 6092 2055 1415 −467 249 C ATOM 617 CD ARG A 104 68.456 64.357 117.264 1.00 43.56 C ANISOU 617 CD ARG A 104 5603 7615 3334 1456 −429 598 C ATOM 618 NE ARG A 104 67.465 63.285 117.299 1.00 50.09 N ANISOU 618 NE ARG A 104 6396 8712 3925 1615 −537 468 N ATOM 619 CZ ARG A 104 67.672 62.059 116.832 1.00 52.21 C ANISOU 619 CZ ARG A 104 6792 8990 4056 1621 −521 386 C ATOM 620 NH1 ARG A 104 68.840 61.739 116.289 1.00 52.44 N ANISOU 620 NH1 ARG A 104 6927 9017 3982 1539 −468 439 N ATOM 621 NH2 ARG A 104 66.709 61.149 116.908 1.00 50.96 N ANISOU 621 NH2 ARG A 104 6677 8757 3929 1701 −569 575 N ATOM 622 N ASP A 105 65.656 65.158 113.516 1.00 17.04 N ANISOU 622 N ASP A 105 2326 3181 967 −339 202 −316 N ATOM 623 CA ASP A 105 65.801 64.283 112.363 1.00 15.90 C ANISOU 623 CA ASP A 105 2141 2691 1210 −349 224 −29 C ATOM 624 C ASP A 105 65.086 64.831 111.154 1.00 14.57 C ANISOU 624 C ASP A 105 1894 2359 1284 −205 173 −121 C ATOM 625 O ASP A 105 64.027 65.455 111.280 1.00 15.84 O ANISOU 625 O ASP A 105 1716 2919 1383 64 311 −209 O ATOM 626 CB ASP A 105 65.272 62.886 112.675 1.00 17.68 C ANISOU 626 CB ASP A 105 2521 2919 1278 −111 150 −39 C ATOM 627 CG ASP A 105 66.041 62.212 113.790 1.00 23.87 C ANISOU 627 CG ASP A 105 2847 4344 1878 −120 171 467 C ATOM 628 OD1 ASP A 105 67.270 62.424 113.898 1.00 25.21 O ANISOU 628 OD1 ASP A 105 3180 4770 1626 −9 49 616 O ATOM 629 OD2 ASP A 105 65.407 61.466 114.560 1.00 28.54 O ANISOU 629 OD2 ASP A 105 3737 4506 2600 −286 99 1368 O ATOM 630 N PHE A 106 65.675 64.566 109.987 1.00 13.84 N ANISOU 630 N PHE A 106 1942 2274 1040 −176 299 −381 N ATOM 631 CA PHE A 106 65.158 65.007 108.704 1.00 14.06 C ANISOU 631 CA PHE A 106 1954 2333 1055 −259 212 −306 C ATOM 632 C PHE A 106 65.202 63.831 107.744 1.00 14.26 C ANISOU 632 C PHE A 106 1884 2333 1203 −243 67 −317 C ATOM 633 O PHE A 106 66.201 63.118 107.676 1.00 17.69 O ANISOU 633 O PHE A 106 1819 2691 2212 389 −136 −752 O ATOM 634 CB PHE A 106 66.001 66.154 108.130 1.00 14.75 C ANISOU 634 CB PHE A 106 1894 2273 1436 26 278 −69 C ATOM 635 CG PHE A 106 66.058 67.372 109.018 1.00 14.13 C ANISOU 635 CG PHE A 106 1766 2134 1467 −60 325 −145 C ATOM 636 CD1 PHE A 106 66.865 67.385 110.154 1.00 14.24 C ANISOU 636 CD1 PHE A 106 1939 1908 1562 −177 434 −147 C ATOM 637 CD2 PHE A 106 65.325 68.513 108.716 1.00 15.05 C ANISOU 637 CD2 PHE A 106 1755 2257 1704 75 410 41 C ATOM 638 CE1 PHE A 106 66.915 68.485 110.984 1.00 15.99 C ANISOU 638 CE1 PHE A 106 2097 2131 1847 −151 213 100 C ATOM 639 CE2 PHE A 106 65.389 69.634 109.535 1.00 16.71 C ANISOU 639 CE2 PHE A 106 2220 2274 1854 −6 355 24 C ATOM 640 CZ PHE A 106 66.175 69.622 110.670 1.00 16.88 C ANISOU 640 CZ PHE A 106 2135 2293 1985 −167 324 −67 C ATOM 641 N HIS A 107 64.121 63.616 107.042 1.00 13.17 N ANISOU 641 N HIS A 107 1842 2409 754 −134 257 −121 N ATOM 642 CA HIS A 107 64.111 62.630 105.973 1.00 13.61 C ANISOU 642 CA HIS A 107 1835 2337 999 −219 324 69 C ATOM 643 C HIS A 107 64.532 63.257 104.650 1.00 12.32 C ANISOU 643 C HIS A 107 1682 1767 1232 110 285 −75 C ATOM 644 O HIS A 107 63.992 64.239 104.243 1.00 14.37 O ANISOU 644 O HIS A 107 1939 2092 1427 184 381 47 O ATOM 645 CB HIS A 107 62.735 62.005 105.804 1.00 15.09 C ANISOU 645 CB HIS A 107 1914 2649 1172 −367 537 −41 C ATOM 646 CG HIS A 107 62.480 60.891 106.751 1.00 16.86 C ANISOU 646 CG HIS A 107 1996 2904 1507 −597 512 −303 C ATOM 647 ND1 HIS A 107 61.253 60.282 106.871 1.00 22.25 N ANISOU 647 ND1 HIS A 107 2596 3704 2152 −792 577 217 N ATOM 648 CD2 HIS A 107 63.305 60.260 107.602 1.00 17.79 C ANISOU 648 CD2 HIS A 107 2702 2552 1506 −266 543 396 C ATOM 649 CE1 HIS A 107 61.343 59.331 107.776 1.00 22.80 C ANISOU 649 CE1 HIS A 107 3308 2978 2376 −745 389 402 C ATOM 650 NE2 HIS A 107 62.569 59.298 108.240 1.00 20.29 N ANISOU 650 NE2 HIS A 107 2887 2781 2041 −632 392 104 N ATOM 651 O MET A 108 66.111 60.745 101.834 1.00 12.41 O ANISOU 651 O MET A 108 1913 1779 1024 6 −185 −42 O ATOM 652 N MET A 108 65.500 62.599 104.024 1.00 11.99 N ANISOU 652 N MET A 108 1573 1911 1071 −34 168 −23 N ATOM 653 C MET A 108 65.531 61.837 101.785 1.00 11.86 C ANISOU 653 C MET A 108 1543 1703 1260 −138 −35 93 C ATOM 654 CA AMET A 108 65.897 62.991 102.694 0.31 9.98 C ANISOU 654 CA AMET A 108 1420 1693 679 −182 283 −218 C ATOM 655 CB AMET A 108 67.369 63.364 102.695 0.31 11.01 C ANISOU 655 CB AMET A 108 1856 1622 707 313 128 −219 C ATOM 656 CG AMET A 108 67.561 64.586 103.573 0.31 11.16 C ANISOU 656 CG AMET A 108 1792 1815 632 31 238 −218 C ATOM 657 SD AMET A 108 69.236 65.170 103.793 0.31 11.68 S ANISOU 657 SD AMET A 108 1560 1813 1066 −148 50 −117 S ATOM 658 CE AMET A 108 68.935 66.784 104.501 0.31 13.36 C ANISOU 658 CE AMET A 108 2340 1343 1394 −257 392 7 C ATOM 659 CA BMET A 108 65.980 62.961 102.697 0.69 11.74 C ANISOU 659 CA BMET A 108 1508 1929 1025 −99 145 −18 C ATOM 660 CB BMET A 108 67.510 63.017 102.703 0.69 11.36 C ANISOU 660 CB BMET A 108 1464 1919 932 −137 −15 −0 C ATOM 661 CG BMET A 108 1819 1851 1401 0.69 13.35 C ANISOU 661 CG BMET A 108 67.708 64.851 104.737 −14 −68 −164 C ATOM 662 SD BMET A 108 2055 2065 1219 0.69 14.05 S ANISOU 662 SD BMET A 108 68.668 66.359 104.858 −165 155 −93 S ATOM 663 CE BMET A 108 2166 1900 1404 0.69 14.40 C ANISOU 663 CE BMET A 108 63.524 62.347 98.368 −477 −52 −276 C ATOM 664 O ASER A 109 63.524 62.347 98.368 0.46 13.09 O ANISOU 664 O ASER A 109 1510 1702 1761 −64 −206 550 O ATOM 665 N ASER A 109 64.481 62.066 101.006 0.46 13.22 N ANISOU 665 N ASER A 109 1401 2243 1378 −596 −76 297 N ATOM 666 CA ASER A 109 63.814 60.982 100.313 0.46 14.19 C ANISOU 666 CA ASER A 109 1532 2199 1660 −729 −387 316 C ATOM 667 C ASER A 109 63.777 61.232 98.823 0.46 15.86 C ANISOU 667 C ASER A 109 1881 2209 1935 −293 −523 315 C ATOM 668 CB ASER A 109 62.384 60.835 100.825 0.46 18.88 C ANISOU 668 CB ASER A 109 1932 3045 2197 −918 −420 384 C ATOM 669 OG ASER A 109 61.627 61.981 100.489 0.46 23.42 O ANISOU 669 OG ASER A 109 2235 4129 2534 −848 −302 383 O ATOM 670 O BSER A 109 63.893 62.301 98.210 0.54 14.06 O ANISOU 670 O BSER A 109 1871 2436 1035 −354 −16 −34 O ATOM 671 N BSER A 109 64.488 62.079 100.993 0.54 12.36 N ANISOU 671 N BSER A 109 1967 1671 1056 320 −262 −67 N ATOM 672 CA BSER A 109 63.865 61.002 100.229 0.54 13.66 C ANISOU 672 CA BSER A 109 2146 1688 1357 −49 −261 −97 C ATOM 673 C BSER A 109 63.959 61.185 98.719 0.54 12.08 C ANISOU 673 C BSER A 109 1760 1787 1043 −554 −173 82 C ATOM 674 CB BSER A 109 62.395 60.845 100.629 0.54 15.41 C ANISOU 674 CB BSER A 109 2028 2475 1351 −126 −44 530 C ATOM 675 OG BSER A 109 62.275 60.525 102.005 0.54 14.24 O ANISOU 675 OG BSER A 109 1704 2365 1343 −572 −47 288 O ATOM 676 N AVAL A 110 64.025 60.178 98.063 0.46 14.13 N ANISOU 676 N AVAL A 110 2189 1495 1685 −252 −781 −248 N ATOM 677 CA AVAL A 110 63.842 60.235 96.629 0.46 13.87 C ANISOU 677 CA AVAL A 110 1818 1975 1475 −693 −507 −150 C ATOM 678 C AVAL A 110 62.783 59.221 96.233 0.46 16.24 C ANISOU 678 C AVAL A 110 2276 2379 1515 −186 −521 −271 C ATOM 679 O AVAL A 110 62.760 58.086 96.710 0.46 15.75 O ANISOU 679 O AVAL A 110 2184 2287 1512 −353 −623 −124 O ATOM 680 CB AVAL A 110 65.153 59.981 95.871 0.46 14.17 C ANISOU 680 CB AVAL A 110 1908 1950 1528 −628 −360 −91 C ATOM 681 CG1 AVAL A 110 65.725 58.620 96.231 0.46 15.64 C ANISOU 681 CG1 AVAL A 110 1827 2141 1976 33 −239 −186 C ATOM 682 CG2 AVAL A 110 64.935 60.110 94.367 0.46 14.09 C ANISOU 682 CG2 AVAL A 110 2312 1705 1339 −763 −445 −16 C ATOM 683 N BVAL A 110 64.107 60.064 98.020 0.54 16.27 N ANISOU 683 N BVAL A 110 2723 2252 1207 −353 −393 40 N ATOM 684 CA BVAL A 110 63.987 60.007 96.570 0.54 17.67 C ANISOU 684 CA BVAL A 110 3012 2291 1409 22 −458 211 C ATOM 685 C BVAL A 110 62.749 59.177 96.257 0.54 15.31 C ANISOU 685 C BVAL A 110 2567 2018 1230 −464 −274 200 C ATOM 686 O BVAL A 110 62.572 58.100 96.821 0.54 16.94 O ANISOU 686 O BVAL A 110 2820 2028 1589 −420 −467 90 O ATOM 687 CB BVAL A 110 65.197 59.286 95.926 0.54 18.85 C ANISOU 687 CB BVAL A 110 3031 2399 1733 −1070 −352 −34 C ATOM 688 CG1 BVAL A 110 65.085 59.302 94.408 0.54 20.93 C ANISOU 688 CG1 BVAL A 110 3622 2405 1925 −873 48 306 C ATOM 689 CG2 BVAL A 110 66.514 59.895 96.374 0.54 27.75 C ANISOU 689 CG2 BVAL A 110 4208 3504 2832 −400 −383 −73 C ATOM 690 O VAL A 111 61.952 58.746 92.749 1.00 16.30 O ANISOU 690 O VAL A 111 2339 2657 1196 −449 −226 −114 O ATOM 691 N VAL A 111 61.893 59.655 95.359 1.00 14.94 N ANISOU 691 N VAL A 111 1920 2579 1175 −404 −188 111 N ATOM 692 C VAL A 111 61.218 58.161 93.547 1.00 15.49 C ANISOU 692 C VAL A 111 1886 2665 1332 −439 −234 293 C ATOM 693 CA AVAL A 111 60.815 58.816 94.868 0.20 16.52 C ANISOU 693 CA AVAL A 111 1946 2767 1565 −566 −386 51 C ATOM 694 CB AVAL A 111 59.507 59.636 94.710 0.20 17.33 C ANISOU 694 CB AVAL A 111 1923 2957 1705 −241 −956 −331 C ATOM 695 CG1 AVAL A 111 59.563 60.531 93.482 0.20 17.31 C ANISOU 695 CG1 AVAL A 111 1995 2786 1794 212 −1057 −308 C ATOM 696 CG2 AVAL A 111 58.298 58.729 94.641 0.20 21.58 C ANISOU 696 CG2 AVAL A 111 2345 3687 2167 −367 −934 −421 C ATOM 697 CA BVAL A 111 60.826 58.804 94.863 0.80 16.66 C ANISOU 697 CA BVAL A 111 1976 3204 1148 −368 226 118 C ATOM 698 CB BVAL A 111 59.496 59.550 94.714 0.80 23.34 C ANISOU 698 CB BVAL A 111 2542 4811 1516 36 405 −152 C ATOM 699 CG1 BVAL A 111 58.921 59.840 96.071 0.80 24.86 C ANISOU 699 CG1 BVAL A 111 2781 5029 1638 670 286 −652 C ATOM 700 CG2 BVAL A 111 59.686 60.837 93.958 0.80 28.83 C ANISOU 700 CG2 BVAL A 111 3727 5261 1965 846 414 19 C ATOM 701 N ARG A 112 60.737 56.940 93.346 1.00 17.54 N ANISOU 701 N ARG A 112 1933 2425 2304 −250 −66 57 N ATOM 702 CA ARG A 112 60.950 56.185 92.126 1.00 20.77 C ANISOU 702 CA ARG A 112 2284 3024 2584 −132 −533 −363 C ATOM 703 C ARG A 112 62.422 56.147 91.753 1.00 16.79 C ANISOU 703 C ARG A 112 1871 2671 1837 −501 −302 48 C ATOM 704 O ARG A 112 62.837 56.635 90.691 1.00 19.07 O ANISOU 704 O ARG A 112 2796 2615 1834 −85 −473 −36 O ATOM 705 CB ARG A 112 60.115 56.765 90.994 1.00 21.77 C ANISOU 705 CB ARG A 112 2242 3200 2831 −32 −822 −806 C ATOM 706 CG ARG A 112 59.864 55.757 89.898 1.00 29.72 C ANISOU 706 CG ARG A 112 3768 3934 3592 518 −937 −878 C ATOM 707 CD ARG A 112 58.893 56.257 88.855 1.00 27.60 C ANISOU 707 CD ARG A 112 3707 3393 3389 −461 −924 −563 C ATOM 708 NE ARG A 112 58.584 55.192 87.912 1.00 27.35 N ANISOU 708 NE ARG A 112 3366 3631 3394 −952 −705 236 N ATOM 709 CZ ARG A 112 57.782 55.334 86.867 1.00 24.16 C ANISOU 709 CZ ARG A 112 2973 3152 3055 −1031 −555 768 C ATOM 710 NH1 ARG A 112 57.218 56.510 86.619 1.00 25.29 N ANISOU 710 NH1 ARG A 112 2961 3236 3412 −420 −598 748 N ATOM 711 NH2 ARG A 112 57.556 54.303 86.065 1.00 26.18 N ANISOU 711 NH2 ARG A 112 3477 3147 3323 −911 −800 374 N ATOM 712 N ALA A 113 63.213 55.581 92.651 1.00 16.27 N ANISOU 712 N ALA A 113 2134 2413 1635 −181 −171 190 N ATOM 713 CA ALA A 113 64.651 55.489 92.474 1.00 14.95 C ANISOU 713 CA ALA A 113 1739 2638 1304 −351 60 −50 C ATOM 714 C ALA A 113 64.989 54.748 91.191 1.00 16.73 C ANISOU 714 C ALA A 113 2521 2389 1445 −300 −83 −84 C ATOM 715 O ALA A 113 64.373 53.740 90.856 1.00 17.71 O ANISOU 715 O ALA A 113 2456 2409 1864 −287 86 −300 O ATOM 716 CB ALA A 113 65.248 54.781 93.645 1.00 16.82 C ANISOU 716 CB ALA A 113 2237 2998 1155 −96 −120 283 C ATOM 717 CD AARG A 114 66.096 58.022 87.181 0.47 22.28 C ANISOU 717 CD AARG A 114 4380 2235 1851 586 −454 157 C ATOM 718 NE AARG A 114 66.807 59.283 87.375 0.47 29.21 N ANISOU 718 NE AARG A 114 5121 3878 2099 561 −435 −201 N ATOM 719 CZ AARG A 114 66.843 60.280 86.494 0.47 29.18 C ANISOU 719 CZ AARG A 114 4935 4185 1969 858 −468 −157 C ATOM 720 NH1 AARG A 114 66.210 60.173 85.334 0.47 29.51 N ANISOU 720 NH1 AARG A 114 4913 4547 1753 313 −347 −156 N ATOM 721 NH2 AARG A 114 67.522 61.386 86.774 0.47 28.86 N ANISOU 721 NH2 AARG A 114 4808 4083 2075 829 −48 558 N ATOM 722 N AARG A 114 65.946 55.280 90.442 0.47 16.78 N ANISOU 722 N AARG A 114 2381 2769 1224 −787 270 −73 N ATOM 723 CA AARG A 114 66.390 54.651 89.200 0.47 19.86 C ANISOU 723 CA AARG A 114 2775 3432 1339 −871 146 −279 C ATOM 724 C AARG A 114 67.841 54.207 89.358 0.47 19.32 C ANISOU 724 C AARG A 114 2730 3222 1387 −997 295 −279 C ATOM 725 O AARG A 114 68.543 54.707 90.237 0.47 16.91 O ANISOU 725 O AARG A 114 2646 2777 1005 −1122 254 −149 O ATOM 726 CB AARG A 114 66.215 55.607 88.011 0.47 23.44 C ANISOU 726 CB AARG A 114 3530 3302 2075 −1037 −16 3 C ATOM 727 CG AARG A 114 66.342 57.080 88.367 0.47 23.11 C ANISOU 727 CG AARG A 114 4394 2386 2001 231 −111 141 C ATOM 728 CD BARG A 114 65.114 56.925 86.490 0.53 29.64 C ANISOU 728 CD BARG A 114 3805 3936 3521 −303 449 68 C ATOM 729 NE BARG A 114 66.154 57.921 86.261 0.53 32.49 N ANISOU 729 NE BARG A 114 4232 4250 3861 −576 603 147 N ATOM 730 CZ BARG A 114 66.103 59.153 86.745 0.53 32.81 C ANISOU 730 CZ BARG A 114 3897 4956 3612 −1041 762 −157 C ATOM 731 NH1 BARG A 114 65.074 59.522 87.485 0.53 39.73 N ANISOU 731 NH1 BARG A 114 4650 6253 4193 −258 742 −234 N ATOM 732 NH2 BARG A 114 67.081 60.011 86.501 0.53 25.77 N ANISOU 732 NH2 BARG A 114 2917 4047 2826 −1934 578 −651 N ATOM 733 N BARG A 114 66.001 55.255 90.500 0.53 16.92 N ANISOU 733 N BARG A 114 2241 2872 1315 139 77 −334 N ATOM 734 CA BARG A 114 66.468 54.674 89.253 0.53 17.25 C ANISOU 734 CA BARG A 114 2322 3159 1073 476 214 −544 C ATOM 735 C BARG A 114 67.857 54.110 89.449 0.53 16.74 C ANISOU 735 C BARG A 114 2648 2541 1171 561 63 −720 C ATOM 736 O BARG A 114 68.547 54.452 90.410 0.53 17.00 O ANISOU 736 O BARG A 114 2578 2603 1279 390 −260 −456 O ATOM 737 CB BARG A 114 66.513 55.740 88.170 0.53 20.12 C ANISOU 737 CB BARG A 114 2607 3562 1477 550 368 −166 C ATOM 738 CG BARG A 114 65.175 56.371 87.896 0.53 25.17 C ANISOU 738 CG BARG A 114 3311 3704 2547 563 254 −46 C ATOM 739 N ARG A 115 68.281 53.258 88.526 1.00 19.29 N ANISOU 739 N ARG A 115 2678 3110 1540 −304 184 −771 N ATOM 740 C ARG A 115 70.647 53.879 88.645 1.00 16.53 C ANISOU 740 C ARG A 115 2755 2243 1284 −43 −86 −389 C ATOM 741 O ARG A 115 71.625 53.814 89.385 1.00 16.80 O ANISOU 741 O ARG A 115 2692 2558 1135 112 −127 −273 O ATOM 742 CA ARG A 115 69.646 52.739 88.581 1.00 18.24 C ANISOU 742 CA ARG A 115 2510 2720 1702 5 242 −904 C ATOM 743 CB ARG A 115 69.929 51.864 87.361 1.00 23.65 C ANISOU 743 CB ARG A 115 3131 3699 2158 292 46 −1078 C ATOM 744 N AASN A 116 70.383 54.934 87.887 0.36 15.37 N ANISOU 744 N AASN A 116 2565 2465 809 −172 −236 −368 N ATOM 745 CA AASN A 116 71.305 56.057 87.815 0.36 16.82 C ANISOU 745 CA AASN A 116 2921 2698 770 59 −152 −155 C ATOM 746 C AASN A 116 71.206 57.040 88.995 0.36 18.02 C ANISOU 746 C AASN A 116 2819 2812 1218 −441 126 −54 C ATOM 747 O AASN A 116 71.856 58.087 88.973 0.36 24.62 O ANISOU 747 O AASN A 116 3748 3859 1746 −150 506 47 O ATOM 748 CB AASN A 116 71.164 56.762 86.468 0.36 21.29 C ANISOU 748 CB AASN A 116 3591 3452 1045 549 −189 14 C ATOM 749 CG AASN A 116 69.749 57.111 86.163 0.36 21.89 C ANISOU 749 CG AASN A 116 3534 3523 1262 896 −478 77 C ATOM 750 OD1 AASN A 116 69.040 57.593 87.031 0.36 21.41 O ANISOU 750 OD1 AASN A 116 3203 3596 1336 1271 −19 439 O ATOM 751 ND2 AASN A 116 69.310 56.843 84.942 0.36 23.62 N ANISOU 751 ND2 AASN A 116 3873 3279 1823 192 −720 −107 N ATOM 752 N BASN A 116 70.353 54.916 87.869 0.64 17.08 N ANISOU 752 N BASN A 116 2786 2699 1005 −88 59 −187 N ATOM 753 CA BASN A 116 71.208 56.094 87.775 0.64 15.60 C ANISOU 753 CA BASN A 116 2635 2608 687 43 70 −37 C ATOM 754 C BASN A 116 71.256 56.972 89.038 0.64 13.42 C ANISOU 754 C BASN A 116 2121 2074 903 27 412 5 C ATOM 755 O BASN A 116 71.996 57.902 89.081 0.64 16.21 O ANISOU 755 O BASN A 116 2371 2484 1303 −334 600 −90 O ATOM 756 CB BASN A 116 70.812 57.080 86.651 0.64 22.22 C ANISOU 756 CB BASN A 116 3469 3707 1266 −333 −266 87 C ATOM 757 CG BASN A 116 70.430 56.447 85.356 0.64 25.18 C ANISOU 757 CG BASN A 116 4094 3742 1733 61 −123 279 C ATOM 758 OD1 BASN A 116 71.115 56.674 84.383 0.64 25.75 O ANISOU 758 OD1 BASN A 116 3866 4047 1872 604 417 344 O ATOM 759 ND2 BASN A 116 69.305 55.736 85.307 0.64 22.01 N ANISOU 759 ND2 BASN A 116 3700 3679 984 3 −225 247 N ATOM 760 N ASP A 117 70.398 56.707 90.008 1.00 14.41 N ANISOU 760 N ASP A 117 2158 2458 859 6 −56 −46 N ATOM 761 CA ASP A 117 70.468 57.377 91.314 1.00 13.50 C ANISOU 761 CA ASP A 117 1970 2283 875 42 −32 −109 C ATOM 762 C ASP A 117 71.553 56.760 92.202 1.00 14.25 C ANISOU 762 C ASP A 117 1941 2161 1311 −89 95 −272 C ATOM 763 O ASP A 117 71.884 57.308 93.253 1.00 14.60 O ANISOU 763 O ASP A 117 2149 2316 1084 −47 −48 −425 O ATOM 764 CB ASP A 117 69.129 57.312 92.034 1.00 14.55 C ANISOU 764 CB ASP A 117 1989 2329 1212 42 117 −107 C ATOM 765 CG ASP A 117 68.074 58.194 91.396 1.00 14.39 C ANISOU 765 CG ASP A 117 2112 2028 1329 −159 176 −115 C ATOM 766 OD1 ASP A 117 68.389 59.322 90.957 1.00 16.30 O ANISOU 766 OD1 ASP A 117 2380 2449 1365 −26 −72 −54 O ATOM 767 OD2 ASP A 117 66.908 57.774 91.385 1.00 17.53 O ANISOU 767 OD2 ASP A 117 2155 2599 1906 −237 −77 −95 O ATOM 768 N SER A 118 72.099 55.613 91.813 1.00 13.49 N ANISOU 768 N SER A 118 1842 2339 944 −93 6 −177 N ATOM 769 CA SER A 118 73.164 55.007 92.598 1.00 13.65 C ANISOU 769 CA SER A 118 1990 2268 927 −214 6 −237 C ATOM 770 C SER A 118 74.331 55.971 92.703 1.00 12.92 C ANISOU 770 C SER A 118 2080 2062 765 28 36 −149 C ATOM 771 O SER A 118 74.718 56.591 91.719 1.00 15.69 O ANISOU 771 O SER A 118 2329 2706 927 −261 170 −129 O ATOM 772 CB SER A 118 73.639 53.703 91.961 1.00 14.99 C ANISOU 772 CB SER A 118 2105 2183 1407 −208 95 −430 C ATOM 773 OG SER A 118 72.591 52.757 91.905 1.00 15.64 O ANISOU 773 OG SER A 118 2312 2256 1373 −173 160 −360 O ATOM 774 N GLY A 119 74.885 56.101 93.900 1.00 12.77 N ANISOU 774 N GLY A 119 1890 2033 929 84 21 −288 N ATOM 775 CA GLY A 119 75.997 57.014 94.099 1.00 13.83 C ANISOU 775 CA GLY A 119 1890 2380 986 −233 14 −398 C ATOM 776 C GLY A 119 76.126 57.368 95.558 1.00 12.67 C ANISOU 776 C GLY A 119 1542 2194 1077 125 199 −49 C ATOM 777 O GLY A 119 75.591 56.685 96.421 1.00 14.12 O ANISOU 777 O GLY A 119 2112 2263 989 −113 −31 −249 O ATOM 778 N THR A 120 76.858 58.434 95.841 1.00 13.23 N ANISOU 778 N THR A 120 1669 2124 1236 14 152 −166 N ATOM 779 CA THR A 120 77.013 58.848 97.225 1.00 13.66 C ANISOU 779 CA THR A 120 1751 2209 1232 352 −268 −518 C ATOM 780 C THR A 120 76.419 60.219 97.444 1.00 12.85 C ANISOU 780 C THR A 120 1865 1759 1259 12 −232 −14 C ATOM 781 O THR A 120 76.339 61.058 96.542 1.00 13.74 O ANISOU 781 O THR A 120 1899 2053 1268 162 233 −168 O ATOM 782 CB THR A 120 78.435 58.821 97.752 1.00 18.06 C ANISOU 782 CB THR A 120 2271 2318 2275 492 27 −383 C ATOM 783 OG1 THR A 120 79.208 59.751 97.008 1.00 18.48 O ANISOU 783 OG1 THR A 120 2013 2529 2480 132 414 118 O ATOM 784 CG2 THR A 120 79.016 57.434 97.676 1.00 20.53 C ANISOU 784 CG2 THR A 120 2335 2792 2672 680 −247 −548 C ATOM 785 N TYR A 121 75.985 60.404 98.674 1.00 12.14 N ANISOU 785 N TYR A 121 1649 2006 958 63 32 −140 N ATOM 786 CA TYR A 121 75.174 61.527 99.065 1.00 12.31 C ANISOU 786 CA TYR A 121 1697 2116 865 343 20 −277 C ATOM 787 C TYR A 121 75.660 61.997 100.427 1.00 12.33 C ANISOU 787 C TYR A 121 1797 1900 990 179 73 178 C ATOM 788 O TYR A 121 76.284 61.230 101.167 1.00 13.90 O ANISOU 788 O TYR A 121 2072 1916 1294 214 −362 −104 O ATOM 789 CB TYR A 121 73.709 61.089 99.184 1.00 13.05 C ANISOU 789 CB TYR A 121 1660 2354 945 100 2 −139 C ATOM 789 CG TYR A 121 73.073 60.674 97.880 1.00 11.72 C ANISOU 790 CG TYR A 121 1673 1953 827 98 89 −65 C ATOM 791 CD1 TYR A 121 73.308 59.416 97.319 1.00 13.22 C ANISOU 791 CD1 TYR A 121 1739 2157 1128 24 169 68 C ATOM 792 CD2 TYR A 121 72.231 61.542 97.208 1.00 13.26 C ANISOU 792 CD2 TYR A 121 1977 2118 944 348 −95 −79 C ATOM 793 CE1 TYR A 121 72.739 59.051 96.108 1.00 13.76 C ANISOU 793 CE1 TYR A 121 1746 2072 1410 −86 90 −5 C ATOM 794 CE2 TYR A 121 71.631 61.180 96.020 1.00 14.01 C ANISOU 794 CE2 TYR A 121 2416 2145 761 257 −268 −233 C ATOM 795 CZ TYR A 121 71.888 59.940 95.475 1.00 13.00 C ANISOU 795 CZ TYR A 121 2198 1939 802 36 42 10 C ATOM 796 OH TYR A 121 71.300 59.627 94.271 1.00 14.81 O ANISOU 796 OH TYR A 121 2323 2303 1000 145 −199 −175 O ATOM 797 N LEU A 122 75.333 63.226 100.794 1.00 13.07 N ANISOU 797 N LEU A 122 1854 2115 997 277 −6 −236 N ATOM 798 CA LEU A 122 75.613 63.680 102.146 1.00 13.79 C ANISOU 798 CA LEU A 122 1625 2261 1355 437 −160 −259 C ATOM 799 C LEU A 122 74.654 64.803 102.494 1.00 12.48 C ANISOU 799 C LEU A 122 1496 2110 1135 199 −134 −51 C ATOM 800 O LEU A 122 73.943 65.314 101.631 1.00 13.74 O ANISOU 800 O LEU A 122 1851 2278 1093 439 −119 −42 O ATOM 801 CB LEU A 122 77.067 64.116 102.333 1.00 16.34 C ANISOU 801 CB LEU A 122 1875 2279 2056 136 −83 −216 C ATOM 802 CG LEU A 122 77.649 65.347 101.648 1.00 20.27 C ANISOU 802 CG LEU A 122 2556 2935 2209 351 769 23 C ATOM 803 CD1 LEU A 122 77.256 66.677 102.284 1.00 23.23 C ANISOU 803 CD1 LEU A 122 3633 2394 2800 −118 −62 −81 C ATOM 804 CD2 LEU A 122 79.158 65.205 101.742 1.00 24.56 C ANISOU 804 CD2 LEU A 122 2716 3908 2710 203 452 −623 C ATOM 805 N CYS A 123 74.639 65.163 103.769 1.00 12.47 N ANISOU 805 N CYS A 123 1827 1792 1119 216 −110 −148 N ATOM 806 C CYS A 123 74.842 67.350 104.740 1.00 13.20 C ANISOU 806 C CYS A 123 1597 1955 1463 95 −204 −288 C ATOM 807 O CYS A 123 75.865 67.021 105.363 1.00 16.98 O ANISOU 807 O CYS A 123 1948 2177 2327 43 −675 −251 O ATOM 808 CA ACYS A 123 73.860 66.264 104.293 0.35 12.80 C ANISOU 808 CA ACYS A 123 1553 1897 1413 −5 −276 −173 C ATOM 809 CB ACYS A 123 73.080 65.736 105.492 0.35 16.64 C ANISOU 809 CB ACYS A 123 2030 2679 1614 375 −92 −583 C ATOM 810 SG ACYS A 123 72.063 66.905 106.359 0.35 19.14 S ANISOU 810 SG ACYS A 123 1808 3384 2080 388 −212 −661 S ATOM 811 CA BCYS A 123 73.888 66.342 104.155 0.65 12.35 C ANISOU 811 CA BCYS A 123 1942 1522 1230 361 15 −270 C ATOM 812 CB BCYS A 123 72.694 66.057 105.078 0.65 13.85 C ANISOU 812 CB BCYS A 123 1967 1926 1369 342 113 −135 C ATOM 813 SG BCYS A 123 73.068 65.330 106.668 0.65 14.15 S ANISOU 813 SG BCYS A 123 2056 2123 1198 132 −170 −279 S ATOM 814 N GLY A 124 74.546 68.611 104.471 1.00 13.98 N ANISOU 814 N GLY A 124 1932 1679 1699 68 −247 −399 N ATOM 815 CA GLY A 124 75.409 69.685 104.912 1.00 15.36 C ANISOU 815 CA GLY A 124 1979 1824 2033 149 −131 −384 C ATOM 816 C GLY A 124 74.597 70.727 105.640 1.00 14.07 C ANISOU 816 C GLY A 124 1920 1640 1786 112 −70 −99 C ATOM 817 O GLY A 124 73.558 71.153 105.141 1.00 16.05 O ANISOU 817 O GLY A 124 2049 2285 1762 432 −319 −359 O ATOM 818 N ALA A 125 75.056 71.118 106.823 1.00 14.15 N ANISOU 818 N ALA A 125 1956 1798 1621 −21 −295 −273 N ATOM 819 CA ALA A 125 74.405 72.152 107.612 1.00 15.07 C ANISOU 819 CA ALA A 125 2232 1776 1717 72 −71 −359 C ATOM 820 C ALA A 125 75.128 73.467 107.417 1.00 14.80 C ANISOU 820 C ALA A 125 2075 1672 1875 −27 −158 −353 C ATOM 821 O ALA A 125 76.351 73.524 107.514 1.00 17.95 O ANISOU 821 O ALA A 125 2024 1995 2802 −176 −410 −185 O ATOM 822 CB ALA A 125 74.405 71.776 109.087 1.00 17.33 C ANISOU 822 CB ALA A 125 2696 2349 1539 −105 −220 −144 C ATOM 823 N ILE A 126 74.369 74.517 107.143 1.00 14.25 N ANISOU 823 N ILE A 126 2188 1679 1547 −111 −76 −237 N ATOM 824 CA ILE A 126 74.917 75.850 106.988 1.00 14.83 C ANISOU 824 CA ILE A 126 2188 1996 1452 −8 −211 −135 C ATOM 825 C ILE A 126 74.382 76.719 108.098 1.00 15.65 C ANISOU 825 C ILE A 126 2310 1888 1749 27 −271 −137 C ATOM 826 O ILE A 126 73.171 76.924 108.203 1.00 15.71 O ANISOU 826 O ILE A 126 2271 2056 1644 −23 1 −290 O ATOM 827 CB ILE A 126 74.489 76.464 105.651 1.00 16.21 C ANISOU 827 CB ILE A 126 2431 2163 1566 −85 −47 85 C ATOM 828 CG1 ILE A 126 74.933 75.566 104.496 1.00 19.33 C ANISOU 828 CG1 ILE A 126 2837 3063 1445 53 −65 −255 C ATOM 829 CG2 ILE A 126 75.095 77.838 105.490 1.00 18.36 C ANISOU 829 CG2 ILE A 126 2881 2294 1801 −127 −215 152 C ATOM 830 CD1 ILE A 126 74.276 75.888 103.175 1.00 24.69 C ANISOU 830 CD1 ILE A 126 3413 4262 1705 −205 −124 −445 C ATOM 831 N SER A 127 75.275 77.201 108.948 1.00 16.52 N ANISOU 831 N SER A 127 2502 1703 2073 77 −398 −385 N ATOM 832 C SER A 127 74.814 79.540 109.297 1.00 19.59 C ANISOU 832 C SER A 127 2975 1877 2592 −60 65 −491 C ATOM 833 O SER A 127 75.710 79.923 108.535 1.00 22.57 O ANISOU 833 O SER A 127 2996 2333 3247 −467 230 −553 O ATOM 834 CA ASER A 127 74.905 78.177 109.959 0.45 20.72 C ANISOU 834 CA ASER A 127 3014 2320 2538 79 −393 −382 C ATOM 835 CB ASER A 127 75.953 78.222 111.068 0.45 21.55 C ANISOU 835 CB ASER A 127 2952 2825 2411 −478 −634 −91 C ATOM 836 OG ASER A 127 77.183 78.726 110.573 0.45 21.36 O ANISOU 836 OG ASER A 127 3177 2582 2356 −502 −724 −36 O ATOM 837 CA BSER A 127 74.877 78.170 109.951 0.55 17.42 C ANISOU 837 CA BSER A 127 2728 1958 1934 328 −604 −768 C ATOM 838 CB BSER A 127 75.847 78.178 111.134 0.55 23.22 C ANISOU 838 CB BSER A 127 3309 3423 2093 28 −862 −1064 C ATOM 839 OG BSER A 127 75.401 79.056 112.153 0.55 27.03 O ANISOU 839 OG BSER A 127 3908 4035 2329 294 −832 −1451 O ATOM 840 O LEU A 128 74.050 83.859 109.583 1.00 26.89 O ANISOU 840 O LEU A 128 4259 2209 3748 −286 −696 −18 O ATOM 841 N LEU A 128 73.745 80.271 109.581 1.00 19.17 N ANISOU 841 N LEU A 128 3119 1801 2364 45 −196 −380 N ATOM 842 CA LEU A 128 73.585 81.582 108.994 1.00 21.02 C ANISOU 842 CA LEU A 128 3686 1656 2646 −11 33 −217 C ATOM 843 C LEU A 128 74.001 82.694 109.962 1.00 24.21 C ANISOU 843 C LEU A 128 4035 1901 3263 31 −36 −130 C ATOM 844 CB LEU A 128 72.150 81.757 108.525 1.00 19.79 C ANISOU 844 CB LEU A 128 3864 1670 1983 116 −2 −101 C ATOM 845 CG LEU A 128 71.735 80.768 107.437 1.00 19.99 C ANISOU 845 CG LEU A 128 3926 2051 1617 296 187 320 C ATOM 846 CD1 LEU A 128 70.253 80.928 107.162 1.00 22.41 C ANISOU 846 CD1 LEU A 128 4228 2414 1875 −136 −290 −42 C ATOM 847 CD2 LEU A 128 72.556 80.951 106.161 1.00 24.98 C ANISOU 847 CD2 LEU A 128 4312 3193 1986 597 103 378 C ATOM 848 N ALA A 129 74.328 82.313 111.197 1.00 24.94 N ANISOU 848 N ALA A 129 3926 2291 3261 −307 −73 −713 N ATOM 849 CA ALA A 129 74.789 83.235 112.234 1.00 30.35 C ANISOU 849 CA ALA A 129 4517 3113 3902 −95 −405 −882 C ATOM 850 C ALA A 129 75.338 82.423 113.412 1.00 30.47 C ANISOU 850 C ALA A 129 4703 2926 3947 −673 −840 −737 C ATOM 851 O ALA A 129 74.948 81.274 113.604 1.00 34.23 O ANISOU 851 O ALA A 129 4945 3845 4217 −1048 −331 −432 O ATOM 852 CB ALA A 129 73.648 84.129 112.687 1.00 31.92 C ANISOU 852 CB ALA A 129 4856 3348 3925 216 −175 −959 C ATOM 853 O PRO A 130 78.183 85.428 112.388 1.00 47.91 O ANISOU 853 O PRO A 130 8160 3729 6314 −716 −868 −970 O ATOM 854 N PRO A 130 76.258 83.005 114.203 1.00 40.27 N ANISOU 854 N PRO A 130 6003 4354 4945 −1014 −1393 −1001 N ATOM 855 CA PRO A 130 76.865 84.334 114.057 1.00 39.87 C ANISOU 855 CA PRO A 130 6281 3919 4950 −991 −1368 −1609 C ATOM 856 C PRO A 130 77.898 84.367 112.937 1.00 48.18 C ANISOU 856 C PRO A 130 7481 4483 6342 −757 −1106 −1180 C ATOM 857 CB PRO A 130 77.542 84.555 115.411 1.00 44.09 C ANISOU 857 CB PRO A 130 6803 4743 5204 −614 −1648 −1698 C ATOM 858 CG PRO A 130 77.852 83.187 115.894 1.00 42.21 C ANISOU 858 CG PRO A 130 6661 4386 4989 −755 −1733 −1537 C ATOM 859 CD PRO A 130 76.714 82.330 115.431 1.00 40.64 C ANISOU 859 CD PRO A 130 6069 4508 4865 −1218 −1748 −1134 C ATOM 860 O LYS A 131 78.197 81.120 110.815 1.00 43.67 O ANISOU 860 O LYS A 131 5793 4637 6164 −1021 −1211 −610 O ATOM 861 N LYS A 131 78.451 83.207 112.606 1.00 43.55 N ANISOU 861 N LYS A 131 6157 4263 6129 −1307 −1163 −860 N ATOM 862 CA LYS A 131 79.371 83.097 111.485 1.00 47.77 C ANISOU 862 CA LYS A 131 6227 5224 6700 −898 −1163 −802 C ATOM 863 C LYS A 131 78.793 82.136 110.458 1.00 39.78 C ANISOU 863 C LYS A 131 5208 4011 5894 −779 −1179 −607 C ATOM 864 CB LYS A 131 80.743 82.611 111.953 1.00 49.12 C ANISOU 864 CB LYS A 131 6057 5704 6901 −1072 −1087 −814 C ATOM 865 N VAL A 132 78.955 82.465 109.184 1.00 29.62 N ANISOU 865 N VAL A 132 3527 2782 4945 −791 −1052 −86 N ATOM 866 CA VAL A 132 78.487 81.597 108.118 1.00 26.03 C ANISOU 866 CA VAL A 132 3039 2262 4590 −524 −1158 439 C ATOM 867 C VAL A 132 79.498 80.490 107.882 1.00 26.40 C ANISOU 867 C VAL A 132 2871 2419 4740 −606 −794 146 C ATOM 868 O VAL A 132 80.650 80.738 107.549 1.00 29.54 O ANISOU 868 O VAL A 132 3043 2876 5305 −520 −479 284 O ATOM 869 CB VAL A 132 78.262 82.379 106.820 1.00 29.44 C ANISOU 869 CB VAL A 132 3636 2818 4731 −703 −1156 929 C ATOM 870 CG1 VAL A 132 77.820 81.442 105.711 1.00 31.93 C ANISOU 870 CG1 VAL A 132 3690 3734 4707 −852 −1452 549 C ATOM 871 CG2 VAL A 132 77.241 83.470 107.044 1.00 31.15 C ANISOU 871 CG2 VAL A 132 3843 3001 4990 −573 −1332 831 C ATOM 872 N GLN A 133 79.062 79.256 108.071 1.00 26.20 N ANISOU 872 N GLN A 133 3052 2153 4751 −297 −670 179 N ATOM 873 C GLN A 133 79.098 76.911 107.453 1.00 24.80 C ANISOU 873 C GLN A 133 2769 2063 4592 −230 −91 241 C ATOM 874 O GLN A 133 77.906 76.834 107.762 1.00 23.24 O ANISOU 874 O GLN A 133 2322 2217 4290 −271 −459 −90 O ATOM 875 CA AGLN A 133 79.931 78.106 107.886 0.69 28.66 C ANISOU 875 CA AGLN A 133 3201 2799 4888 −652 −726 −38 C ATOM 876 CB AGLN A 133 80.646 77.767 109.185 0.69 31.24 C ANISOU 876 CB AGLN A 133 3488 3566 4815 −655 −1347 −395 C ATOM 877 CA BGLN A 133 79.931 78.107 107.879 0.31 28.06 C ANISOU 877 CA BGLN A 133 3161 2591 4911 −449 −575 61 C ATOM 878 CB BGLN A 133 80.664 77.771 109.170 0.31 32.24 C ANISOU 878 CB BGLN A 133 3663 3346 5240 −395 −864 −130 C ATOM 879 N ILE A 134 79.719 75.990 106.725 1.00 25.56 N ANISOU 879 N ILE A 134 2608 2544 4560 −243 412 634 N ATOM 880 C ILE A 134 79.831 73.576 107.058 1.00 22.31 C ANISOU 880 C ILE A 134 1851 2611 4015 24 212 173 C ATOM 881 O ILE A 134 81.066 73.563 107.084 1.00 25.41 O ANISOU 881 O ILE A 134 2126 2823 4707 −55 80 144 O ATOM 882 CA AILE A 134 79.070 74.729 106.407 0.61 22.23 C ANISOU 882 CA AILE A 134 2349 2093 4005 483 270 516 C ATOM 883 CB AILE A 134 78.897 74.493 104.868 0.61 21.09 C ATOM 884 CG1 AILE A 134 78.105 73.198 104.615 0.61 26.12 C ATOM 885 CG2 AILE A 134 80.249 74.520 104.143 0.61 35.37 C ATOM 886 CA BILE A 134 79.170 74.729 106.407 0.39 26.87 C ANISOU 886 CA BILE A 134 2726 2858 4624 175 328 426 C ATOM 887 CB BILE A 134 78.997 74.493 104.868 0.39 31.21 C ATOM 888 CG1 BILE A 134 78.152 73.232 104.616 0.39 30.26 C ATOM 889 CG2 BILE A 134 80.354 74.458 104.152 0.39 36.57 C ATOM 890 N LYS A 135 79.090 72.643 107.643 1.00 18.71 N ANISOU 890 N LYS A 135 1937 1951 3223 −26 −60 −126 N ATOM 891 CA LYS A 135 79.656 71.392 108.134 1.00 18.47 C ANISOU 891 CA LYS A 135 1975 1983 3061 25 −475 −353 C ATOM 892 C LYS A 135 78.904 70.226 107.520 1.00 17.52 C ANISOU 892 C LYS A 135 1889 2114 2653 −83 −452 −74 C ATOM 893 O LYS A 135 77.673 70.175 107.528 1.00 17.94 O ANISOU 893 O LYS A 135 1825 2409 2581 22 −235 −450 O ATOM 894 CB LYS A 135 79.598 71.319 109.651 1.00 23.31 C ANISOU 894 CB LYS A 135 3256 2166 3434 252 −959 −545 C ATOM 895 CG LYS A 135 80.420 72.422 110.286 1.00 26.16 C ANISOU 895 CG LYS A 135 4007 2174 3757 194 −1292 −625 C ATOM 896 CD LYS A 135 80.870 72.094 111.685 1.00 30.44 C ANISOU 896 CD LYS A 135 4405 2633 4529 −286 −1440 −164 C ATOM 897 CE LYS A 135 81.737 73.215 112.251 1.00 32.34 C ANISOU 897 CE LYS A 135 4531 2907 4851 −524 −1232 −376 C ATOM 898 NZ LYS A 135 83.078 73.310 111.606 1.00 39.32 N ANISOU 898 NZ LYS A 135 5621 3854 5462 −714 −1056 −345 N ATOM 899 N GLU A 136 79.667 69.288 106.988 1.00 17.58 N ANISOU 899 N GLU A 136 1777 2026 2878 28 −374 −303 N ATOM 900 C GLU A 136 79.100 66.903 107.098 1.00 15.56 C ANISOU 900 C GLU A 136 1660 2035 2217 209 −278 −364 C ATOM 901 O GLU A 136 79.993 66.668 107.928 1.00 16.23 O ANISOU 901 O GLU A 136 1688 2211 2267 47 −253 −457 O ATOM 902 CG GLU A 136 79.894 69.110 104.011 1.00 28.51 C ANISOU 902 CG GLU A 136 3684 3470 3677 −363 198 251 C ATOM 903 CD GLU A 136 80.612 68.863 102.687 1.00 44.23 C ANISOU 903 CD GLU A 136 5616 6070 5121 48 272 387 C ATOM 904 OE1 GLU A 136 81.467 67.953 102.618 1.00 36.65 O ANISOU 904 OE1 GLU A 136 4507 5310 4107 −769 586 271 O ATOM 905 OE2 GLU A 136 80.319 69.587 101.706 1.00 45.57 O ANISOU 905 OE2 GLU A 136 5976 6342 4998 545 182 735 O ATOM 906 CA AGLU A 136 79.120 68.163 106.258 0.61 16.88 C ANISOU 906 CA AGLU A 136 2038 1873 2502 −93 −289 −334 C ATOM 907 CB AGLU A 136 79.941 67.923 104.978 0.61 21.37 C ANISOU 907 CB AGLU A 136 2741 2372 3007 −109 112 69 C ATOM 908 CA BGLU A 136 79.220 68.163 106.258 0.39 19.72 C ANISOU 908 CA BGLU A 136 2280 2374 2840 136 −355 −389 C ATOM 909 CB BGLU A 136 80.041 67.923 104.978 0.39 22.35 C ANISOU 909 CB BGLU A 136 2709 2566 3218 −73 −31 −90 C ATOM 910 N SER A 137 78.092 66.072 106.850 1.00 14.12 N ANISOU 910 N SER A 137 1608 1959 1800 56 −141 −371 N ATOM 911 CA SER A 137 78.086 64.714 107.351 1.00 13.81 C ANISOU 911 CA SER A 137 1707 1907 1633 136 −165 −296 C ATOM 912 C SER A 137 79.127 63.892 106.609 1.00 13.49 C ANISOU 912 C SER A 137 1695 2031 1399 253 −116 −298 C ATOM 913 O SER A 137 79.708 64.344 105.623 1.00 14.99 O ANISOU 913 O SER A 137 1909 2105 1680 270 20 −148 O ATOM 914 CB SER A 137 76.711 64.083 107.133 1.00 13.13 C ANISOU 914 CB SER A 137 1602 2025 1361 137 −190 −270 C ATOM 915 OG SER A 137 76.471 63.847 105.750 1.00 13.22 O ANISOU 915 OG SER A 137 1692 1979 1352 26 −263 −172 O ATOM 916 N LEU A 138 79.340 62.664 107.059 1.00 13.53 N ANISOU 916 N LEU A 138 1676 2005 1460 327 −297 −425 N ATOM 917 CA LEU A 138 80.035 61.714 106.213 1.00 14.24 C ANISOU 917 CA LEU A 138 1922 1972 1516 345 −315 −321 C ATOM 918 C LEU A 138 79.096 61.317 105.080 1.00 13.40 C ANISOU 918 C LEU A 138 1652 2005 1434 235 −335 −269 C ATOM 919 O LEU A 138 77.875 61.524 105.145 1.00 14.30 O ANISOU 919 O LEU A 138 1817 2122 1494 274 −360 −319 O ATOM 920 CB LEU A 138 80.430 60.481 107.007 1.00 15.80 C ANISOU 920 CB LEU A 138 2268 2188 1548 557 −333 −332 C ATOM 921 CG LEU A 138 81.395 60.733 108.163 1.00 17.06 C ANISOU 921 CG LEU A 138 2453 2817 1212 870 −564 −528 C ATOM 922 CD1 LEU A 138 81.776 59.401 108.778 1.00 22.22 C ANISOU 922 CD1 LEU A 138 3158 3685 1601 1653 −461 −182 C ATOM 923 CD2 LEU A 138 82.634 61.495 107.697 1.00 19.04 C ANISOU 923 CD2 LEU A 138 2123 3312 1801 659 −792 −780 C ATOM 924 N ARG A 139 79.644 60.724 104.032 1.00 14.60 N ANISOU 924 N ARG A 139 2136 2119 1294 329 −230 −295 N ATOM 925 CA ARG A 139 78.795 60.288 102.933 1.00 14.78 C ANISOU 925 CA ARG A 139 2456 2108 1053 201 −586 −331 C ATOM 926 C ARG A 139 77.970 59.050 103.285 1.00 16.19 C ANISOU 926 C ARG A 139 2699 2019 1434 268 −584 200 C ATOM 927 O ARG A 139 78.311 58.281 104.183 1.00 16.93 O ANISOU 927 O ARG A 139 2311 2414 1707 −14 −378 52 O ATOM 928 CB ARG A 139 79.635 60.000 101.710 1.00 18.11 C ANISOU 928 CB ARG A 139 2650 2549 1680 −83 −374 −173 C ATOM 929 CG ARG A 139 80.251 61.234 101.155 1.00 17.94 C ANISOU 929 CG ARG A 139 2309 2926 1581 −390 −144 −183 C ATOM 930 CD ARG A 139 80.614 61.028 99.730 1.00 21.55 C ANISOU 930 CD ARG A 139 2839 3023 2326 −472 17 227 C ATOM 931 NE ARG A 139 81.616 61.985 99.309 1.00 22.47 N ANISOU 931 NE ARG A 139 2570 3298 2671 −402 −180 505 N ATOM 932 CZ ARG A 139 82.194 61.959 98.117 1.00 22.50 C ANISOU 932 CZ ARG A 139 2436 3488 2625 279 −251 866 C ATOM 933 NH1 ARG A 139 81.837 61.044 97.228 1.00 22.91 N ANISOU 933 NH1 ARG A 139 2377 3500 2828 −194 −313 473 N ATOM 934 NH2 ARG A 139 83.116 62.852 97.815 1.00 24.34 N ANISOU 934 NH2 ARG A 139 2374 3639 3234 −246 −141 1211 N ATOM 935 O ALA A 140 76.007 57.992 100.187 1.00 17.70 O ANISOU 935 O ALA A 140 3352 2154 1218 −358 −525 123 O ATOM 936 N ALA A 140 76.871 58.868 102.569 1.00 15.86 N ANISOU 936 N ALA A 140 2543 2147 1338 −129 −583 −48 N ATOM 937 CA ALA A 140 76.141 57.605 102.569 1.00 15.81 C ANISOU 937 CA ALA A 140 2719 2111 1178 −343 −537 −18 C ATOM 938 C ALA A 140 76.020 57.162 101.107 1.00 15.57 C ANISOU 938 C ALA A 140 2655 2130 1130 −309 −530 183 C ATOM 939 CB ALA A 140 74.763 57.759 103.228 1.00 19.34 C ANISOU 939 CB ALA A 140 2752 2958 1639 −312 82 16 C ATOM 940 N GLU A 141 75.941 55.854 100.890 1.00 15.45 N ANISOU 940 N GLU A 141 2633 1949 1289 −211 −309 77 N ATOM 941 CA GLU A 141 75.813 55.314 99.547 1.00 14.01 C ANISOU 941 CA GLU A 141 2012 2090 1223 −201 −299 6 C ATOM 942 C GLU A 141 74.410 54.795 99.307 1.00 13.38 C ANISOU 942 C GLU A 141 2188 1940 957 70 110 −156 C ATOM 943 O GLU A 141 73.837 54.097 100.154 1.00 14.64 O ANISOU 943 O GLU A 141 2244 2108 1210 −51 −126 50 O ATOM 944 CB GLU A 141 76.798 54.169 99.341 1.00 16.38 C ANISOU 944 CB GLU A 141 2246 2333 1645 −93 −204 −101 C ATOM 945 CG GLU A 141 76.706 53.581 97.942 1.00 17.79 C ANISOU 945 CG GLU A 141 2312 2375 2073 154 39 16 C ATOM 946 CD GLU A 141 77.665 52.434 97.689 1.00 21.05 C ANISOU 946 CD GLU A 141 2654 3015 2328 415 61 61 C ATOM 947 OE1 GLU A 141 78.469 52.088 98.591 1.00 22.81 O ANISOU 947 OE1 GLU A 141 2687 3419 2559 582 314 447 O ATOM 948 OE2 GLU A 141 77.605 51.865 96.575 1.00 23.73 O ANISOU 948 OE2 GLU A 141 3387 3338 2291 1202 63 −157 O ATOM 949 N LEU A 142 73.873 55.128 98.137 1.00 13.02 N ANISOU 949 N LEU A 142 2153 1950 843 49 −49 −99 N ATOM 950 CA LEU A 142 72.638 54.531 97.646 1.00 12.97 C ANISOU 950 CA LEU A 142 1770 2037 1121 −35 −95 −217 C ATOM 951 C LEU A 142 73.008 53.568 96.527 1.00 13.06 C ANISOU 951 C LEU A 142 1915 2054 995 −58 −41 −220 C ATOM 952 O LEU A 142 73.721 53.935 95.576 1.00 13.51 O ANISOU 952 O LEU A 142 1906 2100 1129 20 158 −202 O ATOM 953 CB LEU A 142 71.707 55.606 97.081 1.00 13.82 C ANISOU 953 CB LEU A 142 1990 2088 1172 84 −48 −81 C ATOM 954 CG LEU A 142 70.372 55.113 96.536 1.00 14.05 C ANISOU 954 CG LEU A 142 1902 2215 1221 224 −69 −132 C ATOM 955 CD1 LEU A 142 69.555 54.431 97.625 1.00 16.79 C ANISOU 955 CD1 LEU A 142 1992 2857 1529 −108 −4 284 C ATOM 956 CD2 LEU A 142 69.624 56.273 95.925 1.00 16.01 C ANISOU 956 CD2 LEU A 142 2119 2684 1279 183 69 −42 C ATOM 957 N ARG A 143 72.535 52.333 96.640 1.00 13.93 N ANISOU 957 N ARG A 143 2025 1842 1425 −68 110 −290 N ATOM 958 C ARG A 143 71.301 50.970 95.115 1.00 15.63 C ANISOU 958 C ARG A 143 2586 1922 1429 −182 56 −480 C ATOM 959 O ARG A 143 70.501 50.481 95.904 1.00 18.86 O ANISOU 959 O ARG A 143 2882 2606 1677 −675 169 −149 O ATOM 960 NE AARG A 143 76.173 48.875 96.563 0.56 26.47 N ANISOU 960 NE AARG A 143 3900 3059 3097 1060 401 −324 N ATOM 961 CZ AARG A 143 76.907 48.245 97.477 0.56 26.76 C ANISOU 961 CZ AARG A 143 3819 3240 3108 1146 410 −587 C ATOM 962 NH1 AARG A 143 76.641 46.982 97.785 0.56 29.91 N ANISOU 962 NH1 AARG A 143 4282 3270 3813 131 416 −626 N ATOM 963 NH2 AARG A 143 77.902 48.877 98.091 0.56 23.26 N ANISOU 963 NH2 AARG A 143 2922 2838 3077 1182 419 −81 N ATOM 964 CA AARG A 143 72.701 51.346 95.591 0.56 16.10 C ANISOU 964 CA AARG A 143 2593 1914 1609 328 138 −517 C ATOM 965 CB AARG A 143 73.431 50.126 96.155 0.56 20.95 C ANISOU 965 CB AARG A 143 3481 2306 2173 904 196 −369 C ATOM 966 CG AARG A 143 74.183 49.296 95.137 0.56 25.33 C ANISOU 966 CG AARG A 143 3915 2740 2969 341 −45 −547 C ATOM 967 CD AARG A 143 75.064 48.263 95.831 0.56 27.18 C ANISOU 967 CD AARG A 143 3894 2973 3461 402 193 −424 C ATOM 968 NE CARG A 143 76.869 49.400 97.299 0.44 20.33 N ANISOU 968 NE CARG A 143 2868 2365 2490 775 479 −119 N ATOM 969 CZ CARG A 143 77.606 48.570 98.026 0.44 24.33 C ANISOU 969 CZ CARG A 143 3292 2620 3332 337 473 187 C ATOM 970 NH1 CARG A 143 77.159 47.352 98.307 0.44 21.51 N ANISOU 970 NH1 CARG A 143 3104 2243 2825 1002 411 78 N ATOM 971 NH2 CARG A 143 78.787 48.965 98.476 0.44 23.17 N ANISOU 971 NH2 CARG A 143 2551 3234 3017 674 477 235 N ATOM 972 CA CARG A 143 72.679 51.360 95.567 0.44 14.97 C ANISOU 972 CA CARG A 143 2398 1662 1628 −371 315 −12 C ATOM 973 CB CARG A 143 73.411 50.112 96.038 0.44 20.30 C ANISOU 973 CB CARG A 143 3094 2282 2337 −62 284 19 C ATOM 974 CG CARG A 143 74.849 50.352 96.335 0.44 16.25 C ANISOU 974 CG CARG A 143 2165 2118 1891 −280 2 −532 C ATOM 975 CD CARG A 143 75.552 49.084 96.761 0.44 19.96 C ANISOU 975 CD CARG A 143 2984 2306 2293 442 486 −89 C ATOM 976 N VAL A 144 71.016 51.207 93.839 1.00 16.24 N ANISOU 976 N VAL A 144 2443 2419 1308 −39 −58 −366 N ATOM 977 CA VAL A 144 69.711 50.890 93.283 1.00 16.83 C ANISOU 977 CA VAL A 144 2617 2290 1486 −102 67 −376 C ATOM 978 C VAL A 144 69.870 49.716 92.337 1.00 21.07 C ANISOU 978 C VAL A 144 3173 2891 1942 −272 455 −634 C ATOM 979 O VAL A 144 70.539 49.817 91.310 1.00 23.65 O ANISOU 979 O VAL A 144 3734 3326 1926 −242 526 −790 O ATOM 980 CB VAL A 144 69.090 52.086 92.538 1.00 17.74 C ANISOU 980 CB VAL A 144 2482 2715 1544 −276 −194 −399 C ATOM 981 CG1 VAL A 144 67.705 51.735 92.050 1.00 19.38 C ANISOU 981 CG1 VAL A 144 2640 3148 1575 −493 −170 −236 C ATOM 982 CG2 VAL A 144 69.047 53.325 93.425 1.00 16.94 C ANISOU 982 CG2 VAL A 144 2808 2199 1430 −393 3 −259 C ATOM 983 N THR A 145 69.248 48.600 92.692 1.00 20.56 N ANISOU 983 N THR A 145 3128 2306 2378 −198 374 −729 N ATOM 984 CA THR A 145 69.463 47.344 91.988 1.00 23.95 C ANISOU 984 CA THR A 145 3461 2672 2967 74 163 −1190 C ATOM 985 C THR A 145 68.383 47.081 90.944 1.00 24.55 C ANISOU 985 C THR A 145 3347 2667 3314 −173 205 −1226 C ATOM 986 O THR A 145 67.292 47.641 91.000 1.00 23.35 O ANISOU 986 O THR A 145 2959 2847 3065 −151 132 −1264 O ATOM 987 CB THR A 145 69.520 46.177 92.981 1.00 28.34 C ANISOU 987 CB THR A 145 4479 2827 3462 617 205 −970 C ATOM 988 OG1 THR A 145 68.280 46.098 93.694 1.00 31.62 O ANISOU 988 OG1 THR A 145 5383 2817 3813 387 876 −577 O ATOM 989 CG2 THR A 145 70.646 46.394 93.983 1.00 32.13 C ANISOU 989 CG2 THR A 145 5294 3342 3571 787 −281 −1033 C ATOM 990 O GLU A 146 66.589 44.315 90.220 1.00 33.08 O ANISOU 990 O GLU A 146 4148 3633 4789 −465 −94 −1525 O ATOM 991 N GLU A 146 68.693 46.214 89.990 1.00 27.38 N ANISOU 991 N GLU A 146 3510 3446 3447 −49 327 −1807 N ATOM 992 CA GLU A 146 67.774 45.933 88.888 1.00 29.06 C ANISOU 992 CA GLU A 146 3956 3533 3552 −317 −30 −2047 C ATOM 993 C GLU A 146 66.524 45.170 89.335 1.00 31.40 C ANISOU 993 C GLU A 146 3972 3678 4281 −948 3 −1685 C ATOM 994 CB GLU A 146 68.491 45.165 87.773 1.00 34.51 C ANISOU 994 CB GLU A 146 4684 4966 3460 218 −200 −2294 C ATOM 995 O ARG A 147 64.818 43.038 87.503 1.00 41.53 O ANISOU 995 O ARG A 147 5166 4974 5640 −391 −426 −2644 O ATOM 996 N ARG A 147 65.387 45.494 88.721 1.00 31.67 N ANISOU 996 N ARG A 147 3749 3888 4395 −951 −11 −1878 N ATOM 997 CA ARG A 147 64.134 44.785 88.980 1.00 38.10 C ANISOU 997 CA ARG A 147 4634 4509 5332 −659 −204 −1893 C ATOM 998 C ARG A 147 64.241 43.330 88.547 1.00 39.30 C ANISOU 998 C ARG A 147 4756 4756 5420 −415 −287 −2397 C ATOM 999 CB ARG A 147 62.968 45.453 88.242 1.00 44.93 C ANISOU 999 CB ARG A 147 5572 5478 6021 −342 −499 −1680 C ATOM 1000 CG ARG A 147 62.252 46.530 89.042 1.00 49.71 C ANISOU 1000 CG ARG A 147 6135 6192 6560 −208 −730 −1375 C ATOM 1001 CD ARG A 147 61.567 47.538 88.129 1.00 50.17 C ANISOU 1001 CD ARG A 147 5985 6479 6597 −346 −933 −1156 C TER HETATM 1002 CL CL B 1 77.677 61.025 109.310 1.00 24.26 Cl TER HETATM 1003 CL A CL B 2 60.106 72.005 104.718 0.43 31.83 Cl HETATM 1004 CL B CL B 2 60.046 74.655 105.285 0.57 28.96 Cl TER HETATM 1005 O HOH S 1 57.430 67.141 118.746 1.00 21.21 O HETATM 1006 O HOH S 2 82.586 60.395 103.902 1.00 20.60 O HETATM 1007 O HOH S 3 78.817 63.491 111.081 1.00 22.60 O HETATM 1008 O HOH S 4 76.145 52.923 94.493 1.00 21.32 O HETATM 1009 O HOH S 5 67.052 80.545 100.696 1.00 22.45 O HETATM 1010 O HOH S 6 66.272 79.354 102.896 1.00 19.65 O HETATM 1011 O HOH S 7 71.389 60.172 110.959 1.00 26.91 O HETATM 1012 O HOH S 8 66.515 56.646 106.896 1.00 22.37 O HETATM 1013 O HOH S 9 64.255 53.753 102.197 1.00 22.29 O HETATM 1014 O HOH S 10 62.264 71.138 103.203 1.00 22.77 O HETATM 1015 O HOH S 11 63.607 79.682 102.525 1.00 24.56 O HETATM 1016 O HOH S 12 67.408 70.442 114.015 1.00 22.97 O HETATM 1017 O AHOH S 13 69.436 75.663 100.041 0.74 20.55 O HETATM 1018 O BHOH S 13 67.843 77.110 100.058 0.26 21.75 O HETATM 1019 O HOH S 14 76.851 60.191 93.207 1.00 24.68 O HETATM 1020 O HOH S 15 70.133 61.148 92.264 1.00 27.30 O HETATM 1021 O HOH S 17 58.782 55.203 94.319 1.00 24.40 O HETATM 1022 O AHOH S 18 59.915 70.158 106.713 0.61 20.66 O HETATM 1023 O BHOH S 18 59.452 69.640 106.872 0.39 27.64 O HETATM 1024 O HOH S 19 63.847 71.353 98.727 1.00 25.28 O HETATM 1025 O HOH S 20 65.339 53.944 104.582 1.00 26.63 O HETATM 1026 O HOH S 21 69.516 48.688 102.677 1.00 30.33 O HETATM 1027 O HOH S 22 62.920 51.874 100.481 1.00 27.87 O HETATM 1028 O HOH S 23 65.379 76.411 95.129 1.00 30.76 O HETATM 1029 O HOH S 24 70.432 71.724 120.013 1.00 29.49 O HETATM 1030 O HOH S 25 61.940 55.413 101.581 1.00 26.88 O HETATM 1031 O HOH S 26 76.093 85.628 109.892 1.00 30.88 O HETATM 1032 O HOH S 27 80.576 57.162 105.547 1.00 30.06 O HETATM 1033 O HOH S 28 74.611 52.689 108.918 1.00 31.81 O HETATM 1034 O HOH S 29 61.819 69.297 100.027 1.00 31.23 O HETATM 1035 O HOH S 30 77.221 58.625 106.967 1.00 26.29 O HETATM 1036 O HOH S 31 77.910 65.513 114.947 1.00 33.77 O HETATM 1037 O HOH S 32 59.000 52.395 88.751 1.00 25.46 O HETATM 1038 O HOH S 34 74.269 72.547 93.457 1.00 31.68 O HETATM 1039 O HOH S 35 59.962 61.995 102.948 1.00 30.48 O HETATM 1040 O HOH S 36 78.949 51.959 101.310 1.00 29.60 O HETATM 1041 O HOH S 37 60.418 77.661 103.825 1.00 32.54 O HETATM 1042 O HOH S 38 64.337 73.857 98.445 1.00 36.83 O HETATM 1043 O HOH S 39 70.282 50.025 105.056 1.00 38.23 O HETATM 1044 O HOH S 40 67.330 45.766 96.409 1.00 36.46 O HETATM 1045 O HOH S 41 66.498 68.443 92.773 1.00 42.28 O HETATM 1046 O HOH S 42 57.480 64.464 118.550 1.00 43.50 O HETATM 1047 O HOH S 43 63.919 55.879 107.942 1.00 48.40 O HETATM 1048 O HOH S 44 82.271 65.080 106.284 1.00 51.88 O HETATM 1049 O HOH S 45 67.906 70.564 118.415 1.00 35.59 O HETATM 1050 O HOH S 46 59.675 62.503 114.914 1.00 42.35 O HETATM 1051 O HOH S 47 84.504 75.303 113.293 1.00 44.45 O HETATM 1052 O HOH S 48 69.227 60.073 88.487 1.00 25.89 O HETATM 1053 O HOH S 49 56.407 56.257 94.519 1.00 29.48 O HETATM 1054 O HOH S 50 75.972 87.073 112.546 1.00 45.01 O HETATM 1055 O HOH S 51 61.016 73.535 95.375 1.00 42.26 O HETATM 1056 O HOH S 52 73.061 77.907 112.924 1.00 33.56 O HETATM 1057 O HOH S 53 82.470 82.777 106.828 1.00 53.02 O HETATM 1058 O AHOH S 54 79.436 59.161 94.370 0.51 24.61 O HETATM 1059 O BHOH S 54 81.256 59.211 95.031 0.49 27.92 O HETATM 1060 O HOH S 56 55.642 58.691 92.932 1.00 47.56 O HETATM 1061 O HOH S 57 75.933 64.200 116.451 1.00 42.90 O HETATM 1062 O HOH S 58 61.360 64.040 102.879 1.00 21.86 O HETATM 1063 O HOH S 59 70.389 63.369 90.940 1.00 26.53 O HETATM 1064 O HOH S 60 78.757 54.411 102.685 1.00 27.01 O HETATM 1065 O HOH S 61 57.378 65.660 109.331 1.00 23.47 O HETATM 1066 O HOH S 62 79.929 56.310 100.932 1.00 26.39 O HETATM 1067 O HOH S 63 74.661 50.940 106.612 1.00 28.90 O HETATM 1068 O HOH S 64 57.806 52.236 91.089 1.00 33.66 O HETATM 1069 O HOH S 65 64.127 69.714 95.525 1.00 39.44 O HETATM 1070 O HOH S 66 57.817 49.353 90.926 1.00 43.07 O HETATM 1071 O HOH S 67 82.662 76.748 106.385 1.00 42.18 O HETATM 1072 O HOH S 68 59.754 48.914 92.942 1.00 43.66 O HETATM 1073 O HOH S 69 65.932 58.157 83.638 1.00 25.25 O HETATM 1074 O HOH S 70 83.553 67.550 106.500 1.00 36.13 O HETATM 1075 O HOH S 71 79.130 49.647 103.301 1.00 44.50 O HETATM 1076 O HOH S 72 74.424 67.532 114.823 1.00 26.09 O HETATM 1077 O AHOH S 73 65.707 82.659 89.714 0.59 33.77 O HETATM 1078 O BHOH S 73 64.853 83.970 90.636 0.41 21.68 O HETATM 1079 O HOH S 74 60.223 59.329 113.439 1.00 48.46 O HETATM 1080 O HOH S 75 78.431 45.755 100.061 1.00 52.89 O HETATM 1081 O HOH S 76 71.873 78.026 121.604 1.00 44.28 O HETATM 1082 O HOH S 77 59.163 52.192 98.563 1.00 21.31 O HETATM 1083 O HOH S 78 71.545 76.150 114.323 1.00 23.97 O HETATM 1084 O HOH S 79 77.047 54.056 91.965 1.00 28.71 O HETATM 1085 O HOH S 80 55.960 64.395 120.883 1.00 34.79 O HETATM 1086 O HOH S 81 57.096 79.709 93.763 1.00 45.83 O HETATM 1087 O HOH S 82 59.224 68.879 102.307 1.00 36.88 O HETATM 1088 O HOH S 83 75.095 78.893 115.129 1.00 45.56 O HETATM 1089 O HOH S 84 82.002 64.491 104.242 1.00 37.55 O HETATM 1090 O HOH S 86 83.627 62.767 104.076 1.00 32.57 O HETATM 1091 O HOH S 87 62.350 77.030 95.671 1.00 34.75 O HETATM 1092 O HOH S 88 72.529 65.140 91.039 1.00 38.63 O HETATM 1093 O HOH S 89 62.629 54.150 105.575 1.00 49.04 O HETATM 1094 O HOH S 90 63.207 49.381 99.368 1.00 31.86 O HETATM 1095 O HOH S 91 73.193 53.654 83.945 1.00 40.40 O HETATM 1096 O HOH S 92 76.565 43.643 93.769 1.00 51.00 O HETATM 1097 O HOH S 93 73.894 44.922 93.694 1.00 51.33 O HETATM 1098 O HOH S 94 82.395 64.135 100.901 1.00 37.20 O HETATM 1099 O HOH S 95 68.694 54.383 85.476 1.00 38.52 O HETATM 1100 O HOH S 96 75.745 50.591 92.570 1.00 38.51 O HETATM 1101 O HOH S 97 57.196 74.069 89.690 1.00 44.43 O HETATM 1102 O HOH S 98 58.823 71.444 109.216 1.00 43.89 O HETATM 1103 O AHOH S 99 65.419 54.387 84.501 0.54 33.13 O HETATM 1104 O BHOH S 99 66.459 52.602 86.126 0.46 25.24 O HETATM 1105 O HOH S 100 72.132 53.131 110.463 1.00 47.44 O HETATM 1106 O HOH S 102 60.149 84.733 99.929 1.00 41.38 O HETATM 1107 O HOH S 103 67.196 55.553 83.544 1.00 47.80 O HETATM 1108 O HOH S 104 78.913 45.418 95.016 1.00 57.07 O HETATM 1109 O HOH S 105 78.173 65.188 92.355 1.00 40.00 O HETATM 1110 O HOH S 106 71.615 52.024 84.401 1.00 52.57 O HETATM 1111 O HOH S 107 77.280 77.678 115.428 1.00 48.55 O HETATM 1112 O HOH S 108 71.512 43.089 92.230 1.00 56.65 O HETATM 1113 O HOH S 110 80.509 47.126 95.603 1.00 54.92 O HETATM 1114 O HOH S 111 80.259 71.593 99.980 1.00 63.90 O HETATM 1115 O HOH S 112 68.918 57.671 112.722 1.00 53.96 O HETATM 1116 O HOH S 113 70.300 83.442 113.613 1.00 29.88 O HETATM 1117 O AHOH S 114 66.795 76.702 101.785 0.74 23.82 O HETATM 1118 O BHOH S 114 66.370 77.010 102.388 0.26 24.19 O HETATM 1119 O AHOH S 115 59.053 62.549 106.127 0.60 19.44 O HETATM 1120 O BHOH S 115 57.247 65.452 103.361 0.40 15.82 O HETATM 1121 O HOH S 116 60.861 62.614 97.618 1.00 30.80 O HETATM 1122 O HOH S 117 61.573 56.997 117.632 1.00 51.95 O HETATM 1123 O HOH S 118 81.074 84.577 108.313 1.00 46.27 O HETATM 1124 O HOH S 119 73.428 55.743 81.859 1.00 34.45 O HETATM 1125 O HOH S 120 82.654 69.742 107.083 1.00 38.65 O HETATM 1126 O HOH S 122 62.374 69.829 96.978 1.00 48.84 O HETATM 1127 O HOH S 123 58.386 70.671 111.363 1.00 56.98 O HETATM 1128 O HOH S 124 78.972 58.166 91.940 1.00 52.15 O HETATM 1129 O HOH S 125 80.430 64.535 90.804 1.00 48.85 O HETATM 1130 O HOH S 126 71.469 44.836 90.528 1.00 43.98 O HETATM 1131 O HOH S 127 75.978 56.855 109.467 1.00 44.00 O HETATM 1132 O HOH S 128 70.323 59.333 116.131 1.00 57.81 O HETATM 1133 O HOH S 129 77.256 62.535 90.718 1.00 52.58 O HETATM 1134 O HOH S 130 74.334 45.315 96.792 1.00 51.31 O HETATM 1135 O HOH S 131 83.259 66.794 103.808 1.00 50.92 O HETATM 1136 O HOH S 132 59.345 79.745 96.552 1.00 47.19 O HETATM 1137 O HOH S 133 61.610 58.979 116.361 1.00 48.36 O HETATM 1138 O HOH S 134 63.162 59.836 118.024 1.00 55.93 O HETATM 1139 O HOH S 135 76.936 43.553 96.830 1.00 61.58 O HETATM 1140 O HOH S 136 57.386 68.014 92.618 1.00 49.32 O HETATM 1141 O HOH S 137 83.138 74.599 115.308 1.00 50.48 O HETATM 1142 O HOH S 138 84.189 82.738 109.005 1.00 57.05 O HETATM 1143 O HOH S 139 68.404 50.713 106.175 1.00 50.11 O HETATM 1144 O HOH S 140 65.546 48.441 100.909 1.00 45.80 O HETATM 1145 O HOH S 141 68.393 66.857 91.161 1.00 62.36 O HETATM 1146 O HOH S 142 67.813 76.089 93.906 1.00 51.02 O HETATM 1147 O HOH S 143 82.920 66.297 100.638 1.00 61.00 O HETATM 1148 O AHOH S 145 58.793 64.590 96.018 0.57 51.09 O HETATM 1149 O BHOH S 145 52.539 62.260 96.275 0.43 51.51 O HETATM 1150 O HOH S 146 61.132 37.910 86.642 1.00 63.11 O HETATM 1151 O HOH S 147 78.019 80.100 113.163 1.00 56.94 O HETATM 1152 O HOH S 148 68.878 66.327 88.863 1.00 61.15 O HETATM 1153 O HOH S 149 71.524 48.875 88.987 1.00 53.48 O HETATM 1154 O HOH S 150 62.915 37.379 84.940 1.00 65.99 O HETATM 1155 O AHOH S 151 64.070 58.203 110.138 0.55 27.19 O TER HETATM 1156 O BHOH S 151 68.424 55.667 109.016 0.55 36.34 O TER END

TABLE 8 Atomic coordinates and structure factors for human apo-PD-1T76P A132V (based on a PDB file). CRYST1 46.199  46.199  89.407  90.00  90.00  120.00  P  32  2  1 SCALE1 0.021645  0.012497  0.000000  0.00000 SCALE2 0.000000  0.024994  0.000000  0.00000 SCALE3 0.000000  0.000000  0.011185  0.00000 ATOM 1 O MET A 32 −33.514 7.432 25.524 1.00 47.58 O ANISOU 1 O MET A 32 5753 7175 5152 −154 1784 723 O ATOM 2 N MET A 32 −32.396 5.090 26.810 1.00 52.12 N ANISOU 2 N MET A 32 7042 7125 5636 902 705 156 N ATOM 3 C MET A 32 −32.333 7.387 25.888 1.00 46.44 C ANISOU 3 C MET A 32 5888 6742 5015 461 1457 1051 C ATOM 4 CA AMET A 32 −31.611 6.036 26.020 0.44 47.31 C ANISOU 4 CA AMET A 32 6303 6386 5287 645 1240 552 C ATOM 5 CB AMET A 32 −31.295 5.439 24.632 0.44 46.23 C ANISOU 5 CB AMET A 32 6247 5879 5438 798 1190 194 C ATOM 6 CG AMET A 32 −30.328 6.255 23.780 0.44 41.86 C ANISOU 6 CG AMET A 32 5742 4789 5375 307 1475 53 C ATOM 7 SD AMET A 32 −29.839 5.507 22.193 0.44 37.67 S ANISOU 7 SD AMET A 32 5243 3605 5463 −669 1423 −221 S ATOM 8 CE AMET A 32 −31.424 5.296 21.385 0.44 36.56 C ANISOU 8 CE AMET A 32 5475 3025 5390 −623 1237 −248 C ATOM 9 CA BMET A 32 −31.593 6.066 26.090 0.56 48.41 C ANISOU 9 CA BMET A 32 6455 6487 5453 676 1273 841 C ATOM 10 CB BMET A 32 −31.144 5.510 24.741 0.56 49.97 C ANISOU 10 CB BMET A 32 6754 6243 5990 1043 1250 908 C ATOM 11 CG BMET A 32 −32.295 5.139 23.844 0.56 48.60 C ANISOU 11 CG BMET A 32 6773 5415 6276 982 1591 1293 C ATOM 12 SD BMET A 32 −31.726 4.762 22.201 0.56 46.23 S ANISOU 12 SD BMET A 32 6431 4509 6625 638 2362 1816 S ATOM 13 CE BMET A 32 −30.808 6.252 21.804 0.56 45.84 C ANISOU 13 CE BMET A 32 6576 4482 6358 127 2259 2483 C ATOM 14 N ASN A 33 −31.627 8.474 26.165 1.00 39.88 N ANISOU 14 N ASN A 33 5292 5645 4214 563 1175 2037 N ATOM 15 CA ASN A 33 −32.157 9.804 25.947 1.00 42.03 C ANISOU 15 CA ASN A 33 5949 6351 3667 1269 1131 1849 C ATOM 16 C ASN A 33 −31.669 10.277 24.596 1.00 33.44 C ANISOU 16 C ASN A 33 3743 5808 3156 1482 1232 1757 C ATOM 17 O ASN A 33 −30.602 9.874 24.145 1.00 35.26 O ANISOU 17 O ASN A 33 3938 5705 3755 1651 995 1962 O ATOM 18 CB ASN A 33 −31.672 10.756 27.036 1.00 46.78 C ANISOU 18 CB ASN A 33 7351 6823 3600 1245 1354 2231 C ATOM 19 CG ASN A 33 −32.138 10.334 28.401 1.00 55.32 C ANISOU 19 CG ASN A 33 9094 7638 4285 1888 1346 2061 C ATOM 20 OD1 ASN A 33 −33.140 10.836 28.916 1.00 58.96 O ANISOU 20 OD1 ASN A 33 9496 8239 4667 2705 2288 2012 O ATOM 21 ND2 ASN A 33 −31.444 9.374 28.977 1.00 57.08 N ANISOU 21 ND2 ASN A 33 9752 7825 4112 1789 537 2233 N ATOM 22 N PRO A 34 −32.450 11.127 23.928 1.00 25.03 N ANISOU 22 N PRO A 34 2563 4178 2769 511 766 754 N ATOM 23 C PRO A 34 −30.767 12.498 22.759 1.00 21.81 C ANISOU 23 C PRO A 34 1958 4072 2255 672 314 156 C ATOM 24 O PRO A 34 −30.547 13.154 23.783 1.00 25.42 O ANISOU 24 O PRO A 34 3358 4404 1898 286 435 166 O ATOM 25 CA APRO A 34 −32.035 11.666 22.632 0.47 23.20 C ANISOU 25 CA APRO A 34 2253 3858 2704 79 394 137 C ATOM 26 CB APRO A 34 −33.204 12.576 22.249 0.47 23.74 C ANISOU 26 CB APRO A 34 2223 3997 2800 −347 −25 64 C ATOM 27 CG APRO A 34 −34.359 12.136 23.140 0.47 24.04 C ANISOU 27 CG APRO A 34 2277 4132 2727 −649 −35 −148 C ATOM 28 CD APRO A 34 −33.715 11.706 24.399 0.47 25.77 C ANISOU 28 CD APRO A 34 2344 4530 2916 −52 245 562 C ATOM 29 CA BPRO A 34 −31.987 11.604 22.628 0.53 22.93 C ANISOU 29 CA BPRO A 34 2143 3873 2696 330 575 228 C ATOM 30 CB BPRO A 34 −33.181 12.399 22.103 0.53 23.06 C ANISOU 30 CB BPRO A 34 1926 4133 2700 387 514 289 C ATOM 31 CG BPRO A 34 −33.935 12.807 23.325 0.53 22.86 C ANISOU 31 CG BPRO A 34 2147 3935 2602 661 553 349 C ATOM 32 CD BPRO A 34 −33.765 11.673 24.290 0.53 25.43 C ANISOU 32 CD BPRO A 34 2311 4493 2857 779 527 773 C ATOM 33 N PRO A 35 −29.938 12.498 21.729 1.00 18.67 N ANISOU 33 N PRO A 35 2177 3152 1765 659 538 514 N ATOM 34 CA PRO A 35 −28.824 13.447 21.691 1.00 17.89 C ANISOU 34 CA PRO A 35 2092 2784 1920 −166 392 682 C ATOM 35 C PRO A 35 −29.335 14.871 21.506 1.00 19.21 C ANISOU 35 C PRO A 35 2469 3182 1647 472 −69 509 C ATOM 36 O PRO A 35 −30.457 15.077 21.047 1.00 20.66 O ANISOU 36 O PRO A 35 2705 3371 1774 517 −35 145 O ATOM 37 CB PRO A 35 −28.018 12.989 20.464 1.00 20.77 C ANISOU 37 CB PRO A 35 1994 4010 1888 71 280 288 C ATOM 38 CG PRO A 35 −29.057 12.343 19.594 1.00 23.62 C ANISOU 38 CG PRO A 35 3977 2987 2012 495 867 158 C ATOM 39 CD PRO A 35 −30.036 11.693 20.498 1.00 22.34 C ANISOU 39 CD PRO A 35 3666 3393 1428 777 545 64 C ATOM 40 N THR A 36 −28.516 15.850 21.856 1.00 19.79 N ANISOU 40 N THR A 36 2357 3543 1620 225 228 410 N ATOM 41 CA THR A 36 −28.836 17.243 21.504 1.00 21.34 C ANISOU 41 CA THR A 36 2300 3727 2082 407 53 429 C ATOM 42 C THR A 36 −27.853 17.747 20.457 1.00 19.81 C ANISOU 42 C THR A 36 1755 3785 1985 13 128 444 C ATOM 43 O THR A 36 −26.730 17.247 20.388 1.00 23.78 O ANISOU 43 O THR A 36 2094 4251 2690 641 492 1409 O ATOM 44 CB THR A 36 −28.811 18.190 22.717 1.00 25.11 C ANISOU 44 CB THR A 36 2832 4606 2102 22 −29 −329 C ATOM 45 OG1 THR A 36 −27.491 18.194 23.256 1.00 30.33 O ANISOU 45 OG1 THR A 36 3601 5178 2745 627 −419 −1114 O ATOM 46 CG2 THR A 36 −29.768 17.710 23.787 1.00 25.12 C ANISOU 46 CG2 THR A 36 3469 3857 2218 79 447 −9 C ATOM 47 N PHE A 37 −28.262 18.714 19.642 1.00 19.41 N ANISOU 47 N PHE A 37 3220 2748 1406 414 49 18 N ATOM 48 CA PHE A 37 −27.460 19.111 18.485 1.00 17.96 C ANISOU 48 CA PHE A 37 2894 2853 1076 380 153 127 C ATOM 49 C PHE A 37 −27.464 20.626 18.460 1.00 20.12 C ANISOU 49 C PHE A 37 2929 2759 1958 430 284 78 C ATOM 50 O PHE A 37 −28.532 21.236 18.445 1.00 22.81 O ANISOU 50 O PHE A 37 3082 3060 2526 280 63 70 O ATOM 51 CB PHE A 37 −28.117 18.528 17.240 1.00 18.94 C ANISOU 51 CB PHE A 37 2712 3275 1211 161 105 −184 C ATOM 52 CG PHE A 37 −27.218 18.477 16.055 1.00 18.45 C ANISOU 52 CG PHE A 37 2760 2794 1458 −185 −46 −236 C ATOM 53 CD1 PHE A 37 −27.657 18.932 14.828 1.00 24.25 C ANISOU 53 CD1 PHE A 37 3367 4312 1533 −7.41 −281 189 C ATOM 54 CD2 PHE A 37 −25.976 17.884 16.154 1.00 20.07 C ANISOU 54 CD2 PHE A 37 3020 2550 2055 150 591 210 C ATOM 55 CE1 PHE A 37 −26.816 18.847 13.735 1.00 27.38 C ANISOU 55 CE1 PHE A 37 3908 4736 1760 −1156 −240 −120 C ATOM 56 CE2 PHE A 37 −25.151 17.761 15.061 1.00 24.03 C ANISOU 56 CE2 PHE A 37 3724 3298 2107 −381 532 −362 C ATOM 57 CZ PHE A 37 −25.565 18.241 13.859 1.00 26.10 C ANISOU 57 CZ PHE A 37 3415 4685 1817 −1535 193 −572 C ATOM 58 O SER A 38 −24.150 22.452 17.292 1.00 20.42 O ANISOU 58 O SER A 38 2994 2559 2205 256 293 60 O ATOM 59 N SER A 38 −26.280 21.221 18.458 1.00 18.09 N ANISOU 59 N SER A 38 2679 2283 1912 −222 210 332 N ATOM 60 C SER A 38 −25.018 23.195 17.712 1.00 18.62 C ANISOU 60 C SER A 38 2903 2295 1875 −52 224 238 C ATOM 61 CA ASER A 38 −26.143 22.663 18.613 0.45 19.87 C ANISOU 61 CA ASER A 38 3356 2275 1916 −154 391 125 C ATOM 62 CB ASER A 38 −25.872 23.028 20.086 0.45 23.68 C ANISOU 62 CB ASER A 38 3879 2993 2125 −261 −58 22 C ATOM 63 OG ASER A 38 −24.580 22.611 20.489 0.45 24.63 O ANISOU 63 OG ASER A 38 4337 2956 2063 −162 −417 −203 O ATOM 64 CA BSER A 38 −26.112 22.655 18.650 0.26 19.74 C ANISOU 64 CA BSER A 38 3038 2548 1916 −150 363 360 C ATOM 65 CB BSER A 38 −25.745 22.911 20.119 0.26 22.39 C ANISOU 65 CB BSER A 38 3098 3325 2086 −431 119 447 C ATOM 66 OG BSER A 38 −25.301 24.234 20.343 0.26 22.99 O ANISOU 66 OG BSER A 38 3212 3455 2068 −700 63 275 O ATOM 67 CA CSER A 38 −26.119 22.663 18.631 0.28 19.53 C ANISOU 67 CA CSER A 38 3234 2412 1776 52 444 165 C ATOM 68 CB CSER A 38 −25.755 22.986 20.087 0.28 21.98 C ANISOU 68 CB CSER A 38 3700 2978 1674 309 311 −6 C ATOM 69 OG CSER A 38 −26.670 22.392 20.982 0.28 21.91 O ANISOU 69 OG CSER A 38 3954 3054 1317 802 561 −208 O ATOM 70 N PRO A 39 −25.057 24.483 17.380 1.00 19.87 N ANISOU 70 N PRO A 39 2776 2564 2212 −238 114 144 N ATOM 71 CA PRO A 39 −26.117 25.474 17.640 1.00 20.67 C ANISOU 71 CA PRO A 39 2909 2582 2364 435 218 −148 C ATOM 72 C PRO A 39 −27.289 25.226 16.687 1.00 20.46 C ANISOU 72 C PRO A 39 3004 3038 1733 −76 185 −423 C ATOM 73 O PRO A 39 −27.126 24.581 15.640 1.00 21.86 O ANISOU 73 O PRO A 39 3387 3020 1898 −105 103 −514 O ATOM 74 CB PRO A 39 −25.441 26.808 17.293 1.00 23.73 C ANISOU 74 CB PRO A 39 4010 2378 2631 191 16 −199 C ATOM 75 CG PRO A 39 −24.458 26.432 16.236 1.00 23.37 C ANISOU 75 CG PRO A 39 3339 2298 3242 −45 396 −90 C ATOM 76 CD PRO A 39 −23.982 25.040 16.550 1.00 21.23 C ANISOU 76 CD PRO A 39 3038 2343 2687 −326 280 49 C ATOM 77 N ALA A 40 −28.462 25.717 17.025 1.00 21.41 N ANISOU 77 N ALA A 40 3090 2992 2051 74 43 33 N ATOM 78 CA ALA A 40 −29.634 25.478 16.198 1.00 21.40 C ANISOU 78 CA ALA A 40 3191 3174 1768 −425 257 −190 C ATOM 79 C ALA A 40 −29.502 26.162 14.825 1.00 20.53 C ANISOU 79 C ALA A 40 3396 2723 1680 84 217 −581 C ATOM 80 O ALA A 40 −30.052 25.679 13.847 1.00 19.65 O ANISOU 80 O ALA A 40 3053 2723 1689 −157 342 −385 O ATOM 81 CB ALA A 40 −30.898 25.935 16.937 1.00 27.12 C ANISOU 81 CB ALA A 40 3481 4477 2347 779 453 −68 C ATOM 82 N LEU A 41 −28.763 27.265 14.773 1.00 22.38 N ANISOU 82 N LEU A 41 3710 3141 1654 471 98 151 N ATOM 83 CA LEU A 41 −28.443 27.908 13.502 1.00 20.19 C ANISOU 83 CA LEU A 41 3380 2378 1914 293 −187 −52 C ATOM 84 C LEU A 41 −26.971 28.250 13.448 1.00 21.56 C ANISOU 84 C LEU A 41 3473 2921 1796 −102 −124 −301 C ATOM 85 O LEU A 41 −26.451 28.944 14.326 1.00 24.54 O ANISOU 85 O LEU A 41 3684 3336 2304 −143 390 −630 O ATOM 86 CB LEU A 41 −29.258 29.194 13.339 1.00 21.12 C ANISOU 86 CB LEU A 41 3244 2777 2006 303 189 393 C ATOM 87 CG LEU A 41 −28.938 30.068 12.099 1.00 23.28 C ANISOU 87 CG LEU A 41 3860 2574 2411 255 142 243 C ATOM 88 CD1 LEU A 41 −29.214 29.331 10.782 1.00 22.84 C ANISOU 88 CD1 LEU A 41 3378 3307 1993 46 −395 190 C ATOM 89 CD2 LEU A 41 −29.664 31.402 12.148 1.00 26.07 C ANISOU 89 CD2 LEU A 41 4385 2593 2927 435 −414 −23 C ATOM 90 N LEU A 42 −26.292 27.748 12.415 1.00 19.00 N ANISOU 90 N LEU A 42 2746 2694 1778 43 −86 −24 N ATOM 91 C LEU A 42 −24.733 28.730 10.839 1.00 19.27 C ANISOU 91 C LEU A 42 3071 2391 1858 −30 386 91 C ATOM 92 O LEU A 42 −25.161 28.204 9.803 1.00 20.72 O ANISOU 92 O LEU A 42 3025 3024 1824 −33 −265 −161 O ATOM 93 CD1 LEU A 42 −21.882 27.647 12.991 1.00 32.06 C ANISOU 93 CD1 LEU A 42 3249 5651 3281 159 −669 −369 C ATOM 94 CD2 LEU A 42 −22.065 25.304 12.149 1.00 30.38 C ANISOU 94 CD2 LEU A 42 4172 4881 2490 1858 −365 −173 C ATOM 95 CA LEU A 42 −24.879 28.019 12.178 1.00 19.23 C ANISOU 95 CA LEU A 42 2674 2722 1910 −63 50 −111 C ATOM 96 CB LEU A 42 −24.106 26.710 12.170 1.00 24.94 C ANISOU 96 CB LEU A 42 3435 3581 2460 1004 −1 −442 C ATOM 97 CG LEU A 42 −22.587 26.731 11.994 1.00 26.64 C ANISOU 97 CG LEU A 42 3177 4266 2680 613 −258 −318 C ATOM 98 N VAL A 43 −24.175 29.933 10.855 1.00 21.69 N ANISOU 98 N VAL A 43 3097 2560 2585 303 −126 298 N ATOM 99 CA VAL A 43 −23.993 30.701 9.631 1.00 21.50 C ANISOU 99 CA VAL A 43 3240 2071 2859 309 −528 26 C ATOM 100 C VAL A 43 −22.515 30.842 9.375 1.00 23.88 C ANISOU 100 C VAL A 43 3547 2558 2970 79 −270 −433 C ATOM 101 O VAL A 43 −21.786 31.299 10.246 1.00 27.58 O ANISOU 101 O VAL A 43 3650 3699 3130 −529 44 −732 O ATOM 102 CB VAL A 43 −24.603 32.105 9.755 1.00 24.41 C ANISOU 102 CB VAL A 43 3490 2727 3057 67 −103 393 C ATOM 103 CG1 VAL A 43 −24.418 32.878 8.433 1.00 28.27 C ANISOU 103 CG1 VAL A 43 4208 3064 3470 359 149 648 C ATOM 104 CG2 VAL A 43 −26.086 32.003 10.153 1.00 26.73 C ANISOU 104 CG2 VAL A 43 3574 3309 3273 208 −309 160 C ATOM 105 N VAL A 44 −22.061 30.408 8.202 1.00 22.26 N ANISOU 105 N VAL A 44 2961 2776 2722 −42 15 −314 N ATOM 106 CA VAL A 44 −20.646 30.481 7.852 1.00 22.76 C ANISOU 106 CA VAL A 44 3092 2816 2738 −41 156 372 C ATOM 107 C VAL A 44 −20.518 31.005 6.429 1.00 22.60 C ANISOU 107 C VAL A 44 3086 2715 2787 −371 97 749 C ATOM 108 O VAL A 44 −21.487 31.009 5.672 1.00 25.09 O ANISOU 108 O VAL A 44 2954 3568 3012 −243 −511 683 O ATOM 109 CB VAL A 44 −19.925 29.101 7.961 1.00 23.66 C ANISOU 109 CB VAL A 44 4296 2293 2401 −43 −172 129 C ATOM 110 CG1 VAL A 44 −20.102 28.511 9.353 1.00 26.79 C ANISOU 110 CG1 VAL A 44 4403 3453 2323 818 95 707 C ATOM 111 CG2 VAL A 44 −20.436 28.119 6.934 1.00 25.41 C ANISOU 111 CG2 VAL A 44 5020 2275 2361 207 −247 −241 C ATOM 112 N ATHR A 45 −19.312 31.451 6.082 0.58 25.11 N ANISOU 112 N ATHR A 45 3256 3112 3171 −605 −172 717 N ATOM 113 CA ATHR A 45 −19.022 31.961 4.750 0.58 25.13 C ANISOU 113 CA ATHR A 45 3571 2435 3544 −764 −39 944 C ATOM 114 C ATHR A 45 −18.455 30.817 3.929 0.58 24.21 C ANISOU 114 C ATHR A 45 3450 2534 3215 −477 −241 1296 C ATOM 115 O ATHR A 45 −17.655 30.031 4.438 0.58 24.40 O ANISOU 115 O ATHR A 45 3271 2757 3244 −61 −186 1292 O ATOM 116 CB ATHR A 45 −17.985 33.107 4.811 0.58 28.30 C ANISOU 116 CB ATHR A 45 3785 2904 4064 −784 119 573 C ATOM 117 OG1 ATHR A 45 −18.391 34.091 5.777 0.58 28.86 O ANISOU 117 OG1 ATHR A 45 3705 3125 4136 −168 −215 267 O ATOM 118 CG2 ATHR A 45 −17.808 33.770 3.434 0.58 28.67 C ANISOU 118 CG2 ATHR A 45 3993 2608 4291 −921 443 934 C ATOM 119 N BTHR A 45 −19.334 31.461 6.031 0.42 25.74 N ANISOU 119 N BTHR A 45 3408 3262 3109 −824 −52 714 N ATOM 120 CA BTHR A 45 −19.164 31.872 4.635 0.42 27.81 C ANISOU 120 CA BTHR A 45 3803 3292 3471 −805 −84 727 C ATOM 121 C BTHR A 45 −18.582 30.727 3.818 0.42 27.25 C ANISOU 121 C BTHR A 45 3384 3840 3129 −927 −111 905 C ATOM 122 O BTHR A 45 −17.925 29.842 4.364 0.42 26.31 O ANISOU 122 O BTHR A 45 3026 4011 2958 −1147 190 1007 O ATOM 123 CB BTHR A 45 −18.283 33.130 4.482 0.42 32.37 C ANISOU 123 CB BTHR A 45 4524 3726 4047 4 −302 577 C ATOM 124 OG1 BTHR A 45 −16.997 32.889 5.056 0.42 34.11 O ANISOU 124 OG1 BTHR A 45 4492 4153 4315 −255 −560 698 O ATOM 125 CG2 BTHR A 45 −18.910 34.313 5.179 0.42 32.09 C ANISOU 125 CG2 BTHR A 45 4916 3070 4206 1119 −745 508 C ATOM 126 N AGLU A 46 −18.870 30.713 2.670 0.58 26.06 N ANISOU 126 N AGLU A 46 3778 3222 2902 −39 −388 1324 N ATOM 127 C AGLU A 46 −16.838 29.567 1.855 0.58 25.90 C ANISOU 127 C AGLU A 46 3479 3836 2524 −702 −163 827 C ATOM 128 O AGLU A 46 −16.135 30.581 1.892 0.58 24.57 O ANISOU 128 O AGLU A 46 3633 2839 2865 −583 43 527 O ATOM 129 CD AGLU A 46 −18.932 31.333 −1.730 0.58 42.11 C ANISOU 129 CD AGLU A 46 6661 6106 3233 315 −229 1203 C ATOM 130 OE1 AGLU A 46 −19.035 30.320 −2.456 0.58 42.51 O ANISOU 130 OE1 AGLU A 46 6736 5977 3440 −1097 −212 1386 O ATOM 131 OE2 AGLU A 46 −19.252 32.478 −2.116 0.58 45.21 O ANISOU 131 OE2 AGLU A 46 7058 7012 3107 1316 −353 1088 O ATOM 132 CG AGLU A 46 −18.386 31.159 −0.311 0.58 38.08 C ANISOU 132 CG AGLU A 46 5954 5336 3177 734 −119 1403 C ATOM 133 CA AGLU A 46 −18.363 29.665 1.789 0.58 27.90 C ANISOU 133 CA AGLU A 46 3813 4040 2749 −117 −369 1042 C ATOM 134 CB AGLU A 46 −18.847 29.875 0.337 0.58 33.23 C ANISOU 134 CB AGLU A 46 5094 4514 3017 548 −126 1301 C ATOM 135 N BGLU A 46 −18.830 30.742 2.512 0.42 28.35 N ANISOU 135 N BGLU A 46 3447 4309 3015 −878 −506 814 N ATOM 136 C BGLU A 46 −16.824 29.565 1.756 0.42 26.37 C ANISOU 136 C BGLU A 46 3221 4440 2359 −1078 −338 1036 C ATOM 137 O BGLU A 46 −16.109 30.569 1.737 0.42 27.79 O ANISOU 137 O BGLU A 46 3360 4830 2370 −668 −244 1392 O ATOM 138 CD BGLU A 46 −19.653 28.824 −1.999 0.42 39.10 C ANISOU 138 CD BGLU A 46 5062 6154 3642 −529 −737 2020 C ATOM 139 OE1 BGLU A 46 −19.810 29.987 −2.432 0.42 43.16 O ANISOU 139 OE1 BGLU A 46 5577 6957 3867 −574 −804 2120 O ATOM 140 OE2 BGLU A 46 −20.039 27.807 −2.633 0.42 34.63 O ANISOU 140 OE2 BGLU A 46 4088 5406 3663 −1665 −247 2168 O ATOM 141 CG BGLU A 46 −18.964 28.633 −0.642 0.42 39.17 C ANISOU 141 CG BGLU A 46 5385 6075 3422 −47 −875 1363 C ATOM 142 CA BGLU A 46 −18.343 29.683 1.634 0.42 29.14 C ANISOU 142 CA BGLU A 46 3532 4723 2818 −1023 −588 924 C ATOM 143 CB BGLU A 46 −18.778 29.926 0.169 0.42 34.14 C ANISOU 143 CB BGLU A 46 4742 5118 3112 −313 −740 1260 C ATOM 144 N GLY A 47 −16.336 28.339 1.924 1.00 25.60 N ANISOU 144 N GLY A 47 3084 4465 2176 −480 149 925 N ATOM 145 CA GLY A 47 −14.915 28.127 2.064 1.00 24.50 C ANISOU 145 CA GLY A 47 2722 4641 1947 59 158 734 C ATOM 146 C GLY A 47 −14.499 27.850 3.507 1.00 22.87 C ANISOU 146 C GLY A 47 2501 4179 2009 −622 −248 478 C ATOM 147 O GLY A 47 −13.474 27.227 3.731 1.00 26.21 O ANISOU 147 O GLY A 47 2651 4800 2509 −426 −145 611 O ATOM 148 N AASP A 48 −15.297 28.310 4.467 0.65 22.60 N ANISOU 148 N AASP A 48 2947 3607 2032 −245 208 1095 N ATOM 149 C AASP A 48 −15.371 26.667 6.310 0.65 19.68 C ANISOU 149 C AASP A 48 2497 2927 2053 −392 −28 254 C ATOM 150 O AASP A 48 −16.083 25.950 5.636 0.65 24.35 O ANISOU 150 O AASP A 48 2970 3949 2332 −442 −778 262 O ATOM 151 CA AASP A 48 −14.985 28.074 5.870 0.65 19.93 C ANISOU 151 CA AASP A 48 2687 2951 1937 17 −248 434 C ATOM 152 CB AASP A 48 −15.719 29.071 6.760 0.65 25.63 C ANISOU 152 CB AASP A 48 4691 2791 2258 538 −271 −200 C ATOM 153 CG AASP A 48 −15.232 30.504 6.568 0.65 33.29 C ANISOU 153 CG AASP A 48 6202 3260 3187 2073 −1021 −390 C ATOM 154 OD1 AASP A 48 −14.173 30.702 5.938 0.65 35.52 O ANISOU 154 OD1 AASP A 48 6471 3105 3919 430 −1652 −118 O ATOM 155 OD2 AASP A 48 −15.912 31.432 7.051 0.65 45.53 O ANISOU 155 OD2 AASP A 48 8640 4673 3987 2824 −1288 −403 O ATOM 156 N BASP A 48 −15.274 28.336 4.479 0.35 24.42 N ANISOU 156 N BASP A 48 3254 3720 2303 −168 17 354 N ATOM 157 C BASP A 48 −15.365 26.720 6.323 0.35 21.83 C ANISOU 157 C BASP A 48 3011 3003 2280 −573 213 358 C ATOM 158 O BASP A 48 −16.116 26.047 5.635 0.35 23.09 O ANISOU 158 O BASP A 48 3478 2705 2590 −1134 157 732 O ATOM 159 CA BASP A 48 −14.962 28.126 5.901 0.35 24.28 C ANISOU 159 CA BASP A 48 3535 3277 2414 −138 −13 269 C ATOM 160 CB BASP A 48 −15.712 29.142 6.774 0.35 30.12 C ANISOU 160 CB BASP A 48 5048 3562 2833 816 −62 −91 C ATOM 161 CG BASP A 48 −15.222 29.166 8.234 0.35 35.60 C ANISOU 161 CG BASP A 48 6143 3960 3422 2179 −268 −357 C ATOM 162 OD1 BASP A 48 −14.143 28.607 8.536 0.35 34.05 O ANISOU 162 OD1 BASP A 48 6160 3242 3535 1756 −524 −86 O ATOM 163 OD2 BASP A 48 −15.915 29.764 9.089 0.35 42.66 O ANISOU 163 OD2 BASP A 48 7123 5095 3992 3325 −485 −999 O ATOM 164 N ASN A 49 −14.861 26.256 7.459 1.00 19.71 N ANISOU 164 N ASN A 49 2473 3228 1789 −28 216 335 N ATOM 165 C ASN A 49 −16.593 25.293 8.848 1.00 20.19 C ANISOU 165 C ASN A 49 2582 3254 1837 −123 256 108 C ATOM 166 O ASN A 49 −16.840 26.429 9.225 1.00 22.09 O ANISOU 166 O ASN A 49 3074 3224 2094 −385 501 408 O ATOM 167 CA AASN A 49 −15.329 25.021 8.074 0.76 17.58 C ANISOU 167 CA AASN A 49 2115 2662 1901 −42 172 459 C ATOM 168 OD1 AASN A 49 −13.020 23.767 7.187 0.76 23.75 O ANISOU 168 OD1 AASN A 49 2516 3564 2942 −206 597 −187 O ATOM 169 ND2 AASN A 49 −11.865 24.326 9.020 0.76 23.19 N ANISOU 169 ND2 AASN A 49 2680 3748 2386 689 −29 720 N ATOM 170 CB AASN A 49 −14.264 24.499 9.038 0.76 21.43 C ANISOU 170 CB AASN A 49 2486 3403 2253 41 131 568 C ATOM 171 CG AASN A 49 −12.992 24.156 8.341 0.76 21.57 C ANISOU 171 CG AASN A 49 2632 3126 2437 356 422 348 C ATOM 172 CA BASN A 49 −15.375 25.006 7.983 0.24 18.26 C ANISOU 172 CA BASN A 49 2329 2832 1776 −81 −12 57 C ATOM 173 OD1 BASN A 49 −14.105 25.588 10.650 0.24 21.94 O ANISOU 173 OD1 BASN A 49 2934 3450 1953 −231 −787 522 O ATOM 174 ND2 BASN A 49 −12.206 25.064 9.582 0.24 17.39 N ANISOU 174 ND2 BASN A 49 2074 2345 2188 −48 −287 89 N ATOM 175 CB BASN A 49 −14.298 24.194 8.722 0.24 18.84 C ANISOU 175 CB BASN A 49 2475 2796 1889 221 −437 −372 C ATOM 176 CG BASN A 49 −13.527 25.017 9.736 0.24 18.35 C ANISOU 176 CG BASN A 49 2388 2573 2010 −227 −387 39 C ATOM 177 N ALA A 50 −17.380 24.264 9.102 1.00 18.96 N ANISOU 177 N ALA A 50 2511 2545 2150 −300 582 292 N ATOM 178 CA ALA A 50 −18.563 24.443 9.937 1.00 19.41 C ANISOU 178 CA ALA A 50 2594 2643 2139 −84 745 412 C ATOM 179 C ALA A 50 −18.640 23.264 10.885 1.00 19.32 C ANISOU 179 C ALA A 50 3052 2436 1852 −375 368 123 C ATOM 180 O ALA A 50 −18.538 22.132 10.451 1.00 20.58 O ANISOU 180 O ALA A 50 3728 2504 1588 5 658 134 O ATOM 181 CB ALA A 50 −19.835 24.519 9.080 1.00 23.14 C ANISOU 181 CB ALA A 50 2801 3481 2508 195 465 356 C ATOM 182 N THR A 51 −18.863 23.529 12.175 1.00 18.79 N ANISOU 182 N THR A 51 2429 2755 1957 −135 371 292 N ATOM 183 C THR A 51 −20.128 22.564 14.065 1.00 17.40 C ANISOU 183 C THR A 51 2125 2905 1580 −119 356 300 C ATOM 184 O THR A 51 −20.348 23.586 14.698 1.00 20.69 O ANISOU 184 O THR A 51 2698 3083 2079 −112 364 −1 O ATOM 185 CA THR A 51 −18.895 22.465 13.181 1.00 17.49 C ANISOU 185 CA THR A 51 2041 2661 1945 −284 −64 319 C ATOM 186 CB THR A 51 −17.628 22.488 14.066 1.00 20.21 C ANISOU 186 CB THR A 51 2247 3169 2264 −264 28 320 C ATOM 187 OG1 THR A 51 −16.486 22.283 13.220 1.00 23.51 O ANISOU 187 OG1 THR A 51 2846 3604 2483 −156 293 −54 O ATOM 188 CG2 THR A 51 −17.676 21.392 15.127 1.00 21.96 C ANISOU 188 CG2 THR A 51 2415 3488 2441 −371 −175 598 C ATOM 189 N PHE A 52 −20.931 21.503 14.086 1.00 16.27 N ANISOU 189 N PHE A 52 1851 2837 1495 −235 164 342 N ATOM 190 CA PHE A 52 −22.002 21.329 15.059 1.00 16.43 C ANISOU 190 CA PHE A 52 2151 2445 1649 −23 −92 376 C ATOM 191 C PHE A 52 −21.490 20.450 16.172 1.00 15.77 C ANISOU 191 C PHE A 52 2256 2291 1446 −14 −10 157 C ATOM 192 O PHE A 52 −20.551 19.675 16.001 1.00 17.77 O ANISOU 192 O PHE A 52 2550 2478 1723 112 −47 76 O ATOM 193 CB PHE A 52 −23.204 20.629 14.445 1.00 16.69 C ANISOU 193 CB PHE A 52 2105 2370 1866 −148 −361 68 C ATOM 194 CG PHE A 52 −23.901 21.418 13.371 1.00 18.07 C ANISOU 194 CG PHE A 52 2395 2885 1587 86 37 420 C ATOM 195 CD1 PHE A 52 −23.722 21.120 12.023 1.00 22.08 C ANISOU 195 CD1 PHE A 52 3299 3379 1712 205 100 473 C ATOM 196 CD2 PHE A 52 −24.789 22.434 13.710 1.00 17.47 C ANISOU 196 CD2 PHE A 52 2173 2461 2005 133 −169 530 C ATOM 197 CE1 PHE A 52 −24.438 21.817 11.058 1.00 24.07 C ANISOU 197 CE1 PHE A 52 3755 3513 1878 892 438 397 C ATOM 198 CE2 PHE A 52 −25.480 23.128 12.740 1.00 20.34 C ANISOU 198 CE2 PHE A 52 2935 3235 1559 257 −68 375 C ATOM 199 CZ PHE A 52 −25.294 22.828 11.416 1.00 23.73 C ANISOU 199 CZ PHE A 52 3538 4003 1476 816 161 449 C ATOM 200 N THR A 53 −22.125 20.574 17.331 1.00 17.89 N ANISOU 200 N THR A 53 2557 2970 1270 13 89 198 N ATOM 201 C THR A 53 −23.014 18.850 18.804 1.00 18.88 C ANISOU 201 C THR A 53 2732 2876 1567 72 318 259 C ATOM 202 O THR A 53 −24.093 19.370 19.067 1.00 19.29 O ANISOU 202 O THR A 53 2312 3063 1954 218 162 115 O ATOM 203 CA THR A 53 −21.804 19.691 18.449 1.00 18.70 C ANISOU 203 CA THR A 53 2888 3065 1151 −231 −149 124 C ATOM 204 CB THR A 53 −21.351 20.487 19.689 1.00 21.27 C ANISOU 204 CB THR A 53 3213 3309 1559 −398 −242 222 C ATOM 205 OG1 THR A 53 −20.186 21.244 19.354 1.00 24.52 O ANISOU 205 OG1 THR A 53 3505 3697 2116 −735 −349 74 O ATOM 206 CG2 THR A 53 −20.976 19.556 20.870 1.00 25.04 C ANISOU 206 CG2 THR A 53 3909 3789 1814 −80 −436 330 C ATOM 207 N CYS A 54 −22.827 17.541 18.773 1.00 18.66 N ANISOU 207 N CYS A 54 1992 3186 1912 −41 −36 824 N ATOM 208 C CYS A 54 −23.446 16.119 20.618 1.00 20.94 C ANISOU 208 C CYS A 54 2377 3427 2154 208 309 660 C ATOM 209 O CYS A 54 −22.325 15.686 20.813 1.00 23.39 O ANISOU 209 O CYS A 54 2485 4082 2319 598 276 800 O ATOM 210 CA ACYS A 54 −23.832 16.589 19.223 0.75 19.79 C ANISOU 210 CA ACYS A 54 2285 3111 2122 −99 359 40 C ATOM 211 CB ACYS A 54 −23.847 15.385 18.261 0.75 21.16 C ANISOU 211 CB ACYS A 54 2873 2464 2703 −89 497 18 C ATOM 212 SG ACYS A 54 −25.000 14.041 18.736 0.75 28.05 S ANISOU 212 SG ACYS A 54 4084 2849 3723 424 1078 251 S ATOM 213 CA BCYS A 54 −23.835 16.610 19.228 0.25 18.74 C ANISOU 213 CA BCYS A 54 1898 3297 1923 −31 −58 700 C ATOM 214 CB BCYS A 54 −23.911 15.442 18.254 0.25 16.94 C ANISOU 214 CB BCYS A 54 1583 3121 1734 −62 −584 873 C ATOM 215 SG BCYS A 54 −25.284 14.348 18.558 0.25 18.10 S ANISOU 215 SG BCYS A 54 1810 3267 1801 −176 −839 636 S ATOM 216 N SER A 55 −24.380 16.202 21.571 1.00 20.54 N ANISOU 216 N SER A 55 2347 3805 1654 6 −15 433 N ATOM 217 C SER A 55 −24.972 14.568 23.249 1.00 21.69 C ANISOU 217 C SER A 55 2217 4285 1739 −527 −182 643 C ATOM 218 O SER A 55 −26.183 14.575 23.015 1.00 23.95 O ANISOU 218 O SER A 55 2356 4217 2526 147 −76 1094 O ATOM 219 CA ASER A 55 −24.117 15.779 22.947 0.63 20.27 C ANISOU 219 CA ASER A 55 2377 3968 1357 −156 393 15 C ATOM 220 CB ASER A 55 −24.425 16.882 23.963 0.63 23.07 C ANISOU 220 CB ASER A 55 3136 3939 1690 −281 376 322 C ATOM 221 OG ASER A 55 −23.611 18.004 23.698 0.63 26.53 O ANISOU 221 OG ASER A 55 3951 3913 2215 −100 46 94 O ATOM 222 CA BSER A 55 −24.131 15.798 22.946 0.37 23.08 C ANISOU 222 CA BSER A 55 2792 4282 1695 66 −60 120 C ATOM 223 CB BSER A 55 −24.510 16.927 23.900 0.37 29.58 C ANISOU 223 CB BSER A 55 3989 5163 2086 773 −291 −52 C ATOM 224 OG BSER A 55 −24.154 16.607 25.227 0.37 34.88 O ANISOU 224 OG BSER A 55 4949 5865 2438 1337 −645 −542 O ATOM 225 N PHE A 56 −24.339 13.511 23.746 1.00 21.58 N ANISOU 225 N PHE A 56 2556 3987 1657 −17 45 600 N ATOM 226 CA PHE A 56 −25.072 12.276 23.950 1.00 21.23 C ANISOU 226 CA PHE A 56 2336 3971 1761 333 280 301 C ATOM 227 C PHE A 56 −24.508 11.559 25.143 1.00 25.58 C ANISOU 227 C PHE A 56 2957 4462 2299 261 24 783 C ATOM 228 O PHE A 56 −23.326 11.259 25.199 1.00 25.38 O ANISOU 228 O PHE A 56 3152 3768 2725 161 −591 622 O ATOM 229 CB PHE A 56 −24.960 11.368 22.717 1.00 22.98 C ANISOU 229 CB PHE A 56 2926 3682 2124 552 481 138 C ATOM 230 CG PHE A 56 −25.627 10.038 22.891 1.00 22.10 C ANISOU 230 CG PHE A 56 3154 3462 1780 632 214 220 C ATOM 231 CD1 PHE A 56 −27.007 9.955 23.047 1.00 23.78 C ANISOU 231 CD1 PHE A 56 3384 3856 1796 281 284 430 C ATOM 232 CD2 PHE A 56 −24.882 8.871 22.925 1.00 24.70 C ANISOU 232 CD2 PHE A 56 3554 3699 2133 600 60 −299 C ATOM 233 CE1 PHE A 56 −27.640 8.713 23.207 1.00 24.74 C ANISOU 233 CE1 PHE A 56 3504 3764 2131 767 −109 76 C ATOM 234 CE2 PHE A 56 −25.491 7.628 23.078 1.00 26.53 C ANISOU 234 CE2 PHE A 56 3852 4022 2208 992 −36 −175 C ATOM 235 CZ PHE A 56 −26.883 7.536 23.229 1.00 25.80 C ANISOU 235 CZ PHE A 56 3682 4125 1995 578 193 −96 C ATOM 236 O SER A 57 −26.560 8.805 27.017 1.00 36.59 O ANISOU 236 O SER A 57 5426 4898 3580 169 −254 1075 O ATOM 237 N SER A 57 −25.383 11.315 26.086 1.00 28.19 N ANISOU 237 N SER A 57 4093 4177 2440 344 255 1314 N ATOM 238 C SER A 57 −25.423 8.949 27.327 1.00 36.44 C ANISOU 238 C SER A 57 5525 5136 3183 674 −531 202 C ATOM 239 CA ASER A 57 −24.962 10.572 27.3030 0.58 36.34 C ANISOU 239 CA ASER A 57 559 4910 3041 1279 97 635 C ATOM 240 CB ASER A 57 −25.645 11.205 28.517 0.58 42.64 C ANISOU 240 CB ASER A 57 7399 5326 3475 2220 −87 −24 C ATOM 241 OG ASER A 57 −25.300 12.576 28.633 0.58 42.98 O ANISOU 241 OG ASER A 57 7946 4967 3418 2929 −295 −828 O ATOM 242 CA BSER A 57 −24.949 10.568 27.290 0.42 35.14 C ANISOU 242 CA BSER A 57 5347 5149 2856 796 146 1299 C ATOM 243 CB BSER A 57 −25.602 11.204 28.507 0.42 38.96 C ANISOU 243 CB BSER A 57 5926 5936 2940 812 261 1992 C ATOM 244 OG BSER A 57 −27.006 11.149 28.390 0.42 39.13 O ANISOU 244 OG BSER A 57 5539 6401 2928 529 101 2149 O ATOM 245 O ASN A 58 −25.004 6.449 28.983 1.00 37.84 O ANISOU 245 O ASN A 58 7229 3929 3219 530 −1977 −322 O ATOM 246 N ASN A 58 −24.459 8.132 26.972 1.00 38.69 N ANISOU 246 N ASN A 58 5983 5713 3006 427 −1083 −553 N ATOM 247 C ASN A 58 −25.150 5.985 27.899 1.00 34.43 C ANISOU 247 C ASN A 58 5486 4363 3232 −156 −1779 167 C ATOM 248 CA ASN A 58 −24.736 6.753 26.676 1.00 38.79 C ANISOU 248 CA ASN A 58 5811 5443 3484 350 −1094 −320 C ATOM 249 CB ASN A 58 −23.578 6.060 26.021 1.00 39.67 C ANISOU 249 CB ASN A 58 5592 5720 3763 −274 −579 −39 C ATOM 250 CG ASN A 58 −22.264 6.397 26.642 1.00 44.41 C ANISOU 250 CG ASN A 58 6590 6063 4220 834 −341 464 C ATOM 251 OD1 ASN A 58 −21.874 7.520 26.681 1.00 46.73 O ANISOU 251 OD1 ASN A 58 6786 6306 4662 683 −157 427 O ATOM 252 ND2 ASN A 58 −21.554 5.399 27.060 1.00 42.66 N ANISOU 252 ND2 ASN A 58 6985 5339 3884 884 −572 1128 N ATOM 253 O THR A 59 −23.731 3.373 28.098 1.00 33.37 O ATOM 254 N THR A 59 −25.762 4.855 27.658 1.00 33.61 N ATOM 255 CA THR A 59 −25.970 3.807 28.608 1.00 35.90 C ATOM 256 C THR A 59 −24.703 3.042 28.699 1.00 27.20 C ATOM 257 CB THR A 59 −27.142 2.896 28.200 1.00 48.98 C ATOM 258 OG1 THR A 59 −26.898 2.353 26.898 1.00 48.93 O ATOM 259 CG2 THR A 59 −28.411 3.713 28.006 1.00 56.40 C ATOM 260 N SER A 60 −24.739 1.978 29.446 1.00 36.19 N ANISOU 260 N SER A 60 6165 4140 3447 1065 −1646 −687 N ATOM 261 C SER A 60 −23.125 0.606 27.786 1.00 41.91 C ANISOU 261 C SER A 60 6752 5724 3448 1045 −285 41 C ATOM 262 O SER A 60 −22.334 −0.279 27.866 1.00 46.82 O ANISOU 262 O SER A 60 7408 6950 3430 1055 −761 678 O ATOM 263 CA SER A 60 −23.429 1.195 29.347 1.00 40.15 C ANISOU 263 CA SER A 60 6058 5185 4012 1849 −1000 −139 C ATOM 264 CB SER A 60 −23.436 0.031 30.340 1.00 46.31 C ATOM 265 OG SER A 60 −23.462 0.500 31.676 1.00 87.22 O ATOM 266 O GLU A 61 −23.745 1.380 24.715 1.00 28.36 O ANISOU 266 O GLU A 61 4989 3780 2008 −311 −244 −68 O ATOM 267 N GLU A 61 −24.292 0.450 27.204 1.00 35.39 N ANISOU 267 N GLU A 61 6241 4573 2632 −468 426 164 N ATOM 268 CA GLU A 61 −24.403 −0.421 26.068 1.00 36.09 C ANISOU 268 CA GLU A 61 6984 4145 2586 −495 636 171 C ATOM 269 C GLU A 61 −23.851 0.206 24.811 1.00 32.43 C ANISOU 269 C GLU A 61 6059 3869 2392 −29 −216 −33 C ATOM 270 CB GLU A 61 −25.820 −0.873 25.884 1.00 40.27 C ANISOU 270 CB GLU A 61 7762 4520 3019 −1470 1112 216 C ATOM 271 CG GLU A 61 −26.306 −1.785 27.011 1.00 48.39 C ANISOU 271 CG GLU A 61 9067 5656 3663 −678 1691 90 C ATOM 272 CD GLU A 61 −25.289 −2.840 27.427 1.00 57.83 C ANISOU 272 CD GLU A 61 10504 6967 4500 499 1573 −288 C ATOM 273 OE1 GLU A 61 −25.136 −3.818 26.707 1.00 59.54 O ANISOU 273 OE1 GLU A 61 10799 6776 5049 1045 1544 −545 O ATOM 274 OE2 GLU A 61 −24.642 −2.731 28.479 1.00 63.24 O ANISOU 274 OE2 GLU A 61 11063 8024 4941 691 1232 −304 O ATOM 275 N SER A 62 −23.496 0.642 23.870 1.00 30.03 N ANISOU 275 N SER A 62 5078 3885 2447 284 −7 115 N ATOM 276 C SER A 62 −23.900 0.717 21.863 1.00 22.91 C ANISOU 276 C SER A 62 4253 2375 2078 −125 −59 101 C ATOM 277 O SER A 62 −25.111 0.522 21.914 1.00 25.03 O ANISOU 277 O SER A 62 4593 2868 2049 −233 −12 393 O ATOM 278 CA ASER A 62 −22.952 −0.209 22.583 0.75 25.32 C ANISOU 278 CA ASER A 62 5079 2247 2295 77 −257 158 C ATOM 279 CB ASER A 62 −22.746 −1.426 21.685 0.75 26.51 C ANISOU 279 CB ASER A 62 5064 2376 2634 443 −433 −94 C ATOM 280 OG ASER A 62 −21.953 −2.396 22.324 0.75 29.08 O ANISOU 280 OG ASER A 62 5016 3192 2839 188 −50 206 O ATOM 281 CA BSER A 62 −22.931 −0.187 22.609 0.25 28.34 C ANISOU 281 CA BSER A 62 5058 3443 2268 127 −70 291 C ATOM 282 CB BSER A 62 −22.584 −1.386 21.735 0.25 31.99 C ANISOU 282 CB BSER A 62 5478 4302 2374 124 −145 506 C ATOM 283 OG BSER A 62 −23.730 −2.188 21.532 0.25 34.84 O ANISOU 283 OG BSER A 62 5926 4950 2362 44 −120 901 O ATOM 284 N PHE A 63 −23.349 1.690 21.144 1.00 20.93 N ANISOU 284 N PHE A 63 3727 2789 1438 332 −270 10 N ATOM 285 CA PHE A 63 −24.170 2.619 20.363 1.00 19.10 C ANISOU 285 CA PHE A 63 3155 2539 1564 192 58 215 C ATOM 286 C PHE A 63 −23.412 3.072 19.118 1.00 19.71 C ANISOU 286 C PHE A 63 3196 2796 1495 138 −75 −93 C ATOM 287 O PHE A 63 −22.211 2.936 19.019 1.00 21.47 O ANISOU 287 O PHE A 63 3340 3181 1638 627 −68 −94 O ATOM 288 CB PHE A 63 −24.592 3.847 21.194 1.00 21.69 C ANISOU 288 CB PHE A 63 3646 2488 2107 −141 280 −553 C ATOM 289 CG PHE A 63 −23.452 4.731 21.596 1.00 21.93 C ANISOU 289 CG PHE A 63 3665 2561 2107 251 428 −15 C ATOM 290 CD1 PHE A 63 −23.135 5.853 20.855 1.00 20.38 C ANISOU 290 CD1 PHE A 63 3111 2473 2159 201 −187 −281 C ATOM 291 CD2 PHE A 63 −22.696 4.447 22.743 1.00 24.22 C ANISOU 291 CD2 PHE A 63 3884 3142 2176 221 136 −15 C ATOM 292 CE1 PHE A 63 −22.108 6.695 21.237 1.00 22.60 C ANISOU 292 CE1 PHE A 63 3640 2966 1979 220 202 −195 C ATOM 293 CE2 PHE A 63 −21.644 5.282 23.126 1.00 22.98 C ANISOU 293 CE2 PHE A 63 3654 3102 1976 155 −161 225 C ATOM 294 CZ PHE A 63 −21.355 6.421 22.356 1.00 25.17 C ANISOU 294 CZ PHE A 63 4351 3336 1877 22 −227 48 C ATOM 295 N VAL A 64 −24.155 3.623 18.176 1.00 19.04 N ANISOU 295 N VAL A 64 2901 2997 1335 −41 −103 203 N ATOM 296 CA VAL A 64 −23.607 4.315 17.020 1.00 19.45 C ANISOU 296 CA VAL A 64 3380 2611 1397 326 −0 291 C ATOM 297 C VAL A 64 −24.264 5.706 16.999 1.00 17.21 C ANISOU 297 C VAL A 64 2355 2399 1784 −395 164 493 C ATOM 298 O VAL A 64 −25.468 5.838 17.267 1.00 20.34 O ANISOU 298 O VAL A 64 2595 2706 2427 −183 182 351 O ATOM 299 CB VAL A 64 −23.972 3.535 15.734 1.00 20.05 C ANISOU 299 CB VAL A 64 3554 2403 1662 188 475 521 C ATOM 300 CG1 VAL A 64 −23.750 4.384 14.483 1.00 24.84 C ANISOU 300 CG1 VAL A 64 4319 3151 1967 −111 −23 −122 C ATOM 301 CG2 VAL A 64 −23.155 2.243 15.695 1.00 22.81 C ANISOU 301 CG2 VAL A 64 4007 2486 2173 738 11 409 C ATOM 302 N LEU A 65 −23.492 6.731 16.689 1.00 17.65 N ANISOU 302 N LEU A 65 2470 2373 1863 114 95 105 N ATOM 303 C LEU A 65 −23.834 8.496 15.056 1.00 19.14 C ANISOU 303 C LEU A 65 2278 2980 2017 348 144 266 C ATOM 304 O LEU A 65 −22.710 8.616 14.599 1.00 23.52 O ANISOU 304 O LEU A 65 2717 3486 2734 757 626 920 O ATOM 305 CA ALEU A 65 −24.017 8.077 16.523 0.76 17.01 C ANISOU 305 CA ALEU A 65 2800 1911 1753 436 −139 −203 C ATOM 306 CB ALEU A 65 −23.258 9.010 17.462 0.76 23.38 C ANISOU 306 CB ALEU A 65 3087 2789 3008 178 −24 −483 C ATOM 307 CG ALEU A 65 −23.842 10.358 17.829 0.76 23.41 C ANISOU 307 CG ALEU A 65 2650 2853 3390 −90 39 −451 C ATOM 308 CD1 ALEU A 65 −25.206 10.222 18.515 0.76 22.26 C ANISOU 308 CD1 ALEU A 65 2225 3066 3169 −116 554 −278 C ATOM 309 CD2 ALEU A 65 −22.858 11.045 18.720 0.76 23.52 C ANISOU 309 CD2 ALEU A 65 2641 3172 3125 −323 −612 −143 C ATOM 310 CA BLEU A 65 −24.025 8.078 16.488 0.24 17.60 C ANISOU 310 CA BLEU A 65 2218 2502 1966 −16 136 341 C ATOM 311 CB BLEU A 65 −23.296 9.093 17.346 0.24 19.59 C ANISOU 311 CB BLEU A 65 2146 2886 2411 50 24 192 C ATOM 312 CG BLEU A 65 −23.572 9.048 18.831 0.24 17.01 C ANISOU 312 CG BLEU A 65 1590 2505 2367 −539 −304 270 C ATOM 313 CD1 BLEU A 65 −22.802 10.157 19.470 0.24 15.56 C ANISOU 313 CD1 BLEU A 65 1608 2000 2302 −462 −786 −460 C ATOM 314 CD2 BLEU A 65 −25.032 9.207 19.115 0.24 17.29 C ANISOU 314 CD2 BLEU A 65 2374 1904 2291 −503 −207 729 C ATOM 315 N ASN A 66 −24.937 8.717 14.358 1.00 19.50 N ANISOU 315 N ASN A 66 2956 2476 1978 262 −53 496 N ATOM 316 CA ASN A 66 −24.916 9.075 12.942 1.00 20.34 C ANISOU 316 CA ASN A 66 2925 2622 2181 332 −27 324 C ATOM 317 C ASN A 66 −25.205 10.582 12.804 1.00 18.94 C ANISOU 317 C ASN A 66 2394 2820 1983 371 282 367 C ATOM 318 O ASN A 66 −26.039 11.159 13.526 1.00 21.81 O ANISOU 318 O ASN A 66 2874 3062 2353 703 577 367 O ATOM 319 CB ASN A 66 −26.012 8.323 12.218 1.00 21.72 C ANISOU 319 CB ASN A 66 3495 2328 2432 68 −46 78 C ATOM 320 CG ASN A 66 −25.629 6.885 11.859 1.00 24.63 C ANISOU 320 CG ASN A 66 3679 2649 3031 −234 9 183 C ATOM 321 OD1 ASN A 66 −24.464 6.506 11.844 1.00 28.62 O ANISOU 321 OD1 ASN A 66 4225 3368 3281 867 382 392 O ATOM 322 ND2 ASN A 66 −26.628 6.094 11.512 1.00 26.30 N ANISOU 322 ND2 ASN A 66 3996 2551 3447 −249 244 −93 N ATOM 323 N TRP A 67 −24.527 11.210 11.857 1.00 16.96 N ANISOU 323 N TRP A 67 2219 2551 1675 403 139 202 N ATOM 324 CA TRP A 67 −24.821 12.582 11.466 1.00 17.35 C ANISOU 324 CA TRP A 67 2648 2322 1622 296 −487 80 C ATOM 325 C TRP A 67 −25.559 12.535 10.139 1.00 16.02 C ANISOU 325 C TRP A 67 2057 2340 1690 −132 188 −137 C ATOM 326 O TRP A 67 −25.044 11.953 9.193 1.00 17.52 O ANISOU 326 O TRP A 67 2341 2772 1542 192 20 −102 O ATOM 327 CB TRP A 67 −23.506 13.345 11.289 1.00 16.70 C ANISOU 327 CB TRP A 67 2291 2264 1791 −158 −88 −202 C ATOM 328 CG TRP A 67 −23.644 14.788 10.913 1.00 15.50 C ANISOU 328 CG TRP A 67 1895 2429 1566 −32 −158 −93 C ATOM 329 CD1 TRP A 67 −24.733 15.597 11.062 1.00 16.72 C ANISOU 329 CD1 TRP A 67 2197 2528 1627 539 −206 319 C ATOM 330 CD2 TRP A 67 −22.605 15.614 10.379 1.00 15.69 C ANISOU 330 CD2 TRP A 67 1896 2652 1416 −242 −150 −334 C ATOM 331 NE1 TRP A 67 −24.447 16.880 10.638 1.00 16.73 N ANISOU 331 NE1 TRP A 67 2145 2701 1512 −36 135 245 N ATOM 332 CE2 TRP A 67 −23.145 16.912 10.195 1.00 15.97 C ANISOU 332 CE2 TRP A 67 2002 2561 1506 −0 34 −116 C ATOM 333 CE3 TRP A 67 −21.264 15.382 10.059 1.00 18.33 C ANISOU 333 CE3 TRP A 67 1627 3525 1813 −201 87 −270 C ATOM 334 CZ2 TRP A 67 −22.385 17.979 9.710 1.00 17.25 C ANISOU 334 CZ2 TRP A 67 2052 2871 1631 −217 −404 −7 C ATOM 335 CZ3 TRP A 67 −20.503 16.435 9.554 1.00 18.98 C ANISOU 335 CZ3 TRP A 67 2015 3430 1766 −354 48 66 C ATOM 336 CH2 TRP A 67 −21.066 17.716 9.382 1.00 19.49 C ANISOU 336 CH2 TRP A 67 2459 2964 1984 −57 −77 37 C ATOM 337 N TYR A 68 −26.733 13.148 10.084 1.00 17.60 N ANISOU 337 N TYR A 68 2239 2803 1645 360 −334 196 N ATOM 338 CA TYR A 68 −27.535 13.132 8.865 1.00 18.83 C ANISOU 338 CA TYR A 68 2361 2956 1838 151 −193 160 C ATOM 339 C TYR A 68 −27.775 14.520 8.312 1.00 17.36 C ANISOU 339 C TYR A 68 2348 2705 1542 685 −246 369 C ATOM 340 O TYR A 68 −27.945 15.487 9.058 1.00 19.44 O ANISOU 340 O TYR A 68 2880 2839 1669 786 212 34 O ATOM 341 CB TYR A 68 −28.939 12.583 9.158 1.00 22.37 C ANISOU 341 CB TYR A 68 2629 3311 2558 −208 −229 −62 C ATOM 342 CG TYR A 68 −28.966 11.176 9.662 1.00 21.28 C ANISOU 342 CG TYR A 68 2607 2830 2649 −131 −166 262 C ATOM 343 CD1 TYR A 68 −28.924 10.112 8.809 1.00 22.93 C ANISOU 343 CD1 TYR A 68 3237 2732 2745 −556 −122 40 C ATOM 344 CD2 TYR A 68 −29.104 10.914 11.020 1.00 25.46 C ANISOU 344 CD2 TYR A 68 4086 3081 2507 341 −14 572 C ATOM 345 CE1 TYR A 68 −28.987 8.803 9.267 1.00 25.28 C ANISOU 345 CE1 TYR A 68 3736 2842 3027 −353 −31 504 C ATOM 346 CE2 TYR A 68 −29.160 9.597 11.489 1.00 28.99 C ANISOU 346 CE2 TYR A 68 4540 3390 3085 673 187 212 C ATOM 347 CZ TYR A 68 −29.114 8.555 10.593 1.00 26.96 C ANISOU 347 CZ TYR A 68 3934 2885 3423 −365 55 342 C ATOM 348 OH TYR A 68 −29.187 7.260 11.023 1.00 32.87 O ANISOU 348 OH TYR A 68 5410 3215 3862 −257 148 377 O ATOM 349 N ARG A 69 −27.843 14.606 6.988 1.00 18.39 N ANISOU 349 N ARG A 69 2680 2776 1532 30 −79 388 N ATOM 350 CA ARG A 69 −28.398 15.774 6.357 1.00 19.02 C ANISOU 350 CA ARG A 69 3074 2452 1703 −487 −332 534 C ATOM 351 C ARG A 69 −29.832 15.410 6.025 1.00 19.80 C ANISOU 351 C ARG A 69 3020 2443 2061 −149 −557 −543 C ATOM 352 O ARG A 69 −30.102 14.356 5.461 1.00 24.21 O ANISOU 352 O ARG A 69 3236 3098 2867 119 −495 −783 O ATOM 353 CB ARG A 69 −27.645 16.133 5.082 1.00 22.34 C ANISOU 353 CB ARG A 69 3564 3429 1495 −177 −56 808 C ATOM 354 CG ARG A 69 −28.133 17.419 4.475 1.00 22.49 C ANISOU 354 CG ARG A 69 3915 3021 1607 −379 −19 799 C ATOM 355 CD ARG A 69 −27.252 17.890 3.388 1.00 26.43 C ANISOU 355 CD ARG A 69 4548 3361 2133 −82 137 1257 C ATOM 356 NE ARG A 69 −27.785 19.116 2.803 1.00 24.93 N ANISOU 356 NE ARG A 69 4181 3495 1796 −267 218 766 N ATOM 357 CZ ARG A 69 −27.190 19.754 1.795 1.00 24.72 C ANISOU 357 CZ ARG A 69 4062 3413 1916 −360 −424 −63 C ATOM 358 NH1 ARG A 69 −26.063 19.279 1.278 1.00 27.53 N ANISOU 358 NH1 ARG A 69 3709 4627 2123 −390 −768 378 N ATOM 359 NH2 ARG A 69 −27.710 20.843 1.314 1.00 28.19 N ANISOU 359 NH2 ARG A 69 5033 3694 1984 327 −385 −535 N ATOM 360 O AMET A 70 −34.121 16.404 5.088 0.63 32.94 O ANISOU 360 O AMET A 70 3794 4565 4158 1047 173 127 O ATOM 361 N AMET A 70 −30.757 16.279 6.435 0.63 21.29 N ANISOU 361 N AMET A 70 2374 3135 2579 639 45 −106 N ATOM 362 C AMET A 70 −32.961 16.726 5.350 0.63 29.17 C ANISOU 362 C AMET A 70 3071 4239 3774 218 −765 −262 C ATOM 363 CA AMET A 70 −32.204 16.001 6.427 0.63 25.67 C ANISOU 363 CA AMET A 70 2819 3863 3072 282 2 −344 C ATOM 364 CB AMET A 70 −32.865 16.415 7.762 0.63 25.85 C ANISOU 364 CB AMET A 70 3156 4084 2580 1193 587 −592 C ATOM 365 CG AMET A 70 −32.334 15.641 8.925 0.63 26.62 C ANISOU 365 CG AMET A 70 3310 4024 2779 29 −95 202 C ATOM 366 SD AMET A 70 −32.681 13.886 8.816 0.63 25.57 S ANISOU 366 SD AMET A 70 2915 3735 3064 55 −215 −27 S ATOM 367 CE AMET A 70 −34.457 13.866 9.003 0.63 29.39 C ANISOU 367 CE AMET A 70 2985 4948 3233 −294 −572 658 C ATOM 368 O BMET A 70 −33.686 16.135 4.423 0.37 32.05 O ANISOU 368 O BMET A 70 2704 5080 4392 −853 −1724 −463 O ATOM 369 N BMET A 70 −30.758 16.278 6.387 0.37 23.82 N ANISOU 369 N BMET A 70 2725 3374 2950 −718 −775 −187 N ATOM 370 C BMET A 70 −32.797 16.669 5.100 0.37 30.69 C ANISOU 370 C BMET A 70 2651 4926 4083 −738 −1707 −367 C ATOM 371 CA BMET A 70 −32.161 15.941 6.264 0.37 29.71 C ANISOU 371 CA BMET A 70 3118 4533 3638 −766 −1059 −301 C ATOM 372 CB BMET A 70 −32.899 16.289 7.556 0.37 36.52 C ANISOU 372 CB BMET A 70 4116 5976 3784 375 −401 105 C ATOM 373 CG BMET A 70 −34.246 15.651 7.647 0.37 41.35 C ANISOU 373 CG BMET A 70 4953 6816 3944 939 158 630 C ATOM 374 SD BMET A 70 −34.206 13.870 7.553 0.37 46.65 S ANISOU 374 SD BMET A 70 5683 7766 4278 1347 404 1179 S ATOM 375 CE BMET A 70 −34.938 13.419 9.126 0.37 46.19 C ANISOU 375 CE BMET A 70 5849 7281 4419 894 302 1210 C ATOM 376 O SER A 71 −30.690 19.786 3.772 1.00 27.87 O ANISOU 376 O SER A 71 3431 3577 3579 197 −867 105 O ATOM 377 N SER A 71 −32.347 17.894 4.866 1.00 30.43 N ANISOU 377 N SER A 71 2656 4721 4183 −120 −889 675 N ATOM 378 CA SER A 71 −32.842 18.692 3.756 1.00 33.99 C ANISOU 378 CA SER A 71 3005 5737 4173 913 −732 199 C ATOM 379 C SER A 71 −31.687 19.460 3.105 1.00 36.17 C ANISOU 379 C SER A 71 4376 4900 4466 3 −579 938 C ATOM 380 CB SER A 71 −33.940 19.655 4.231 1.00 33.85 C ANISOU 380 CB SER A 71 3149 5270 4443 496 −513 −653 C ATOM 381 OG SER A 71 −33.405 20.647 5.095 1.00 37.20 O ANISOU 381 OG SER A 71 4259 5515 4360 425 −571 −1173 O ATOM 382 O PRO A 72 −31.622 17.247 0.700 1.00 79.55 O ANISOU 382 O PRO A 72 9807 8972 11447 1413 −611 524 O ATOM 383 N PRO A 72 −31.930 19.711 1.760 1.00 46.66 N ANISOU 383 N PRO A 72 5155 6766 5809 500 −1637 509 N ATOM 384 CA PRO A 72 −32.981 19.189 0.882 1.00 58.56 C ANISOU 384 CA PRO A 72 6438 7948 7865 408 −1909 548 C ATOM 385 C PRO A 72 −32.715 17.754 0.447 1.00 87.61 C ANISOU 385 C PRO A 72 10558 10867 11864 353 −1260 528 C ATOM 386 CB PRO A 72 −32.915 20.123 −0.328 1.00 53.01 C ANISOU 386 CB PRO A 72 5911 7859 6373 1210 −1816 605 C ATOM 387 CG PRO A 72 −31.500 20.589 −0.359 1.00 49.25 C ANISOU 387 CG PRO A 72 5060 8210 5441 1261 −1901 497 C ATOM 388 CD PRO A 72 −31.074 20.698 1.078 1.00 45.71 C ANISOU 388 CD PRO A 72 4769 7373 5224 1151 −2036 1113 C ATOM 389 O SER A 73 −35.496 14.835 −0.740 1.00 89.31 O ATOM 390 N SER A 73 −33.794 17.016 0.435 1.00 131.36 N ATOM 391 CA SER A 73 −33.763 15.579 0.767 1.00 69.01 C ATOM 392 C SER A 73 −34.364 14.639 −0.297 1.00 88.91 C ATOM 393 O ASN A 74 −35.006 10.928 1.253 1.00 97.59 O ATOM 394 N ASN A 74 −33.596 13.625 −0.696 1.00 67.36 N ATOM 395 CA ASN A 74 −33.885 12.194 −0.474 1.00 83.94 C ATOM 396 C ASN A 74 −34.163 11.781 0.974 1.00 112.13 C ATOM 397 CB ASN A 74 −32.760 11.330 −1.052 1.00 81.23 C ATOM 398 O GLN A 75 −34.797 11.983 4.041 1.00 94.95 O ATOM 399 N GLN A 75 −33.428 12.412 1.877 1.00 116.23 N ATOM 400 CA GLN A 75 −32.670 11.842 2.945 1.00 75.15 C ATOM 401 C GLN A 75 −33.646 11.547 4.049 1.00 75.49 C ATOM 402 CB GLN A 75 −31.602 12.823 3.431 1.00 109.74 C ATOM 403 O PRO A 76 −30.775 9.537 4.735 1.00 40.28 O ANISOU 403 O PRO A 76 5352 3506 6447 −351 −1585 −514 O ATOM 404 N PRO A 76 −33.150 10.791 5.002 1.00 52.61 N ANISOU 404 N PRO A 76 5675 6045 8269 −2909 −1848 886 N ATOM 405 C PRO A 76 −30.795 10.728 5.056 1.00 37.46 C ANISOU 405 C PRO A 76 4497 3555 6180 −813 −1791 203 C ATOM 406 CA PRO A 76 −32.015 11.328 5.738 1.00 43.47 C ANISOU 406 CA PRO A 76 4563 4769 7184 −1137 −2010 455 C ATOM 407 CB PRO A 76 −32.198 10.727 7.124 1.00 46.18 C ANISOU 407 CB PRO A 76 4663 5522 7363 −1010 −1800 415 C ATOM 408 CG PRO A 76 −33.667 10.501 7.230 1.00 46.93 C ANISOU 408 CG PRO A 76 4916 5399 7517 −1582 −1827 169 C ATOM 409 CD PRO A 76 −34.113 10.107 5.879 1.00 50.47 C ANISOU 409 CD PRO A 76 5055 6224 7896 −1723 −1718 791 C ATOM 410 O ASP A 77 −27.188 12.018 5.842 1.00 21.14 O ANISOU 410 O ASP A 77 3066 2646 2322 −21 −356 −317 O ATOM 411 N ASP A 77 −29.798 11.547 4.798 1.00 31.79 N ANISOU 411 N ASP A 77 3417 3780 4881 −876 −1752 458 N ATOM 412 CA ASP A 77 −28.597 11.075 4.152 1.00 30.39 C ANISOU 412 CA ASP A 77 4217 3630 3700 −629 −1385 −166 C ATOM 413 C ASP A 77 −27.530 10.999 5.228 1.00 23.84 C ANISOU 413 C ASP A 77 3427 2890 2741 −879 −888 −334 C ATOM 414 CB ASP A 77 −28.181 12.097 3.081 1.00 35.59 C ANISOU 414 CB ASP A 77 6033 4101 3390 74 −1396 384 C ATOM 415 CG ASP A 77 −26.901 11.701 2.348 1.00 48.11 C ANISOU 415 CG ASP A 77 8332 5760 4188 895 −446 914 C ATOM 416 OD1 ASP A 77 −26.453 10.541 2.501 1.00 55.44 O ANISOU 416 OD1 ASP A 77 9101 7301 4661 458 563 1016 O ATOM 417 OD2 ASP A 77 −26.349 12.536 1.593 1.00 54.64 O ANISOU 417 OD2 ASP A 77 9396 7230 4135 1159 −444 445 O ATOM 418 N LYS A 78 −26.998 9.808 5.468 1.00 25.64 N ANISOU 418 N LYS A 78 3532 3634 2576 126 −286 −255 N ATOM 419 C LYS A 78 −24.626 10.301 5.958 1.00 23.36 C ANISOU 419 C LYS A 78 2636 3525 2716 −313 468 −1003 C ATOM 420 O LYS A 78 −24.109 9.901 4.898 1.00 31.31 O ANISOU 420 O LYS A 78 4100 4572 3224 −682 800 −1583 O ATOM 421 CA LYS A 78 −25.946 9.693 6.469 1.00 23.80 C ANISOU 421 CA LYS A 78 3170 3080 2793 −2 −441 −378 C ATOM 422 CB LYS A 78 −25.731 8.250 6.874 1.00 25.49 C ANISOU 422 CB LYS A 78 3701 3222 2761 284 −676 −87 C ATOM 423 CG LYS A 78 −24.649 8.164 7.922 1.00 28.34 C ANISOU 423 CG LYS A 78 4370 3575 2822 728 −689 268 C ATOM 424 CD LYS A 78 −24.572 6.804 8.517 1.00 39.89 C ANISOU 424 CD LYS A 78 6575 5112 3471 1388 98 457 C ATOM 425 CE LYS A 78 −24.293 5.814 7.461 1.00 45.57 C ANISOU 425 CE LYS A 78 7602 6017 3697 1619 654 818 C ATOM 426 NZ LYS A 78 −24.459 4.455 7.998 1.00 51.10 N ANISOU 426 NZ LYS A 78 8393 6831 4191 1793 956 1085 N ATOM 427 N LEU A 79 −24.051 11.246 6.690 1.00 19.32 N ANISOU 427 N LEU A 79 2214 3018 2108 80 −181 −403 N ATOM 428 CA LEU A 79 −22.807 11.898 6.278 1.00 19.20 C ANISOU 428 CA LEU A 79 2316 3162 1817 286 149 14 C ATOM 429 C LEU A 79 −21.560 11.234 6.852 1.00 19.69 C ANISOU 429 C LEU A 79 2365 3348 1767 −30 308 30 C ATOM 430 O LEU A 79 −20.502 11.174 6.211 1.00 22.91 O ANISOU 430 O LEU A 79 3000 3571 2132 266 439 206 O ATOM 431 CB LEU A 79 −22.820 13.370 6.738 1.00 19.24 C ANISOU 431 CB LEU A 79 2652 2849 1809 176 −144 232 C ATOM 432 CG LEU A 79 −24.040 14.149 6.242 1.00 19.55 C ANISOU 432 CG LEU A 79 2696 3082 1649 397 −173 25 C ATOM 433 CD1 LEU A 79 −24.103 15.506 6.919 1.00 21.97 C ANISOU 433 CD1 LEU A 79 3347 2831 2170 151 −435 −207 C ATOM 434 CD2 LEU A 79 −23.963 14.287 4.723 1.00 22.99 C ANISOU 434 CD2 LEU A 79 3157 4106 1471 546 −249 555 C ATOM 435 N ALA A 80 −21.674 10.793 8.105 1.00 19.24 N ANISOU 435 N ALA A 80 2934 2922 1453 460 212 114 N ATOM 436 CA ALA A 80 −20.524 10.293 8.859 1.00 18.60 C ANISOU 436 CA ALA A 80 2440 2818 1808 114 130 401 C ATOM 437 C ALA A 80 −21.066 9.699 10.160 1.00 17.43 C ANISOU 437 C ALA A 80 2430 2390 1801 119 401 112 C ATOM 438 O ALA A 80 −22.223 9.940 10.515 1.00 19.11 O ANISOU 438 O ALA A 80 2218 3148 1896 203 398 199 O ATOM 439 CB ALA A 80 −19.538 11.430 9.164 1.00 22.26 C ANISOU 439 CB ALA A 80 2913 2941 2604 −517 −136 62 C ATOM 440 N ALA A 81 −20.252 8.903 10.835 1.00 19.05 N ANISOU 440 N ALA A 81 2646 2780 1811 354 22 295 N ATOM 441 CA ALA A 81 −20.665 8.235 12.060 1.00 18.68 C ANISOU 441 CA ALA A 81 2603 2499 1995 −195 −337 275 C ATOM 442 C ALA A 81 −19.569 8.109 13.064 1.00 18.56 C ANISOU 442 C ALA A 81 2328 2498 2226 464 −121 −470 C ATOM 443 O ALA A 81 −18.392 8.136 12.709 1.00 20.25 O ANISOU 443 O ALA A 81 2360 2812 2520 444 95 −61 O ATOM 444 CB ALA A 81 −21.214 6.815 11.744 1.00 22.23 C ANISOU 444 CB ALA A 81 2855 3182 2411 −451 −528 108 C ATOM 445 O PHE A 82 −20.846 6.014 16.222 1.00 24.81 O ANISOU 445 O PHE A 82 2317 3708 3401 502 170 861 O ATOM 446 N PHE A 82 −19.975 7.934 14.324 1.00 20.32 N ANISOU 446 N PHE A 82 2866 2887 1968 203 5 321 N ATOM 447 CA PHE A 82 −19.108 7.430 15.394 1.00 21.19 C ANISOU 447 CA PHE A 82 2782 3210 2058 33 −356 258 C ATOM 448 C PHE A 82 −19.669 6.106 15.940 1.00 20.15 C ANISOU 448 C PHE A 82 2405 2780 2471 143 −253 528 C ATOM 449 CB PHE A 82 −19.022 8.415 16.566 1.00 23.16 C ANISOU 449 CB PHE A 82 3374 3419 2009 345 −510 −481 C ATOM 450 CG PHE A 82 −18.336 7.822 17.765 1.00 26.29 C ANISOU 450 CG PHE A 82 4301 3361 2328 518 −828 −708 C ATOM 451 CD1 PHE A 82 −16.977 7.856 17.858 1.00 30.38 C ANISOU 451 CD1 PHE A 82 4339 4414 2790 440 −802 −988 C ATOM 452 CD2 PHE A 82 −19.065 7.164 18.763 1.00 29.00 C ANISOU 452 CD2 PHE A 82 5248 3373 2397 1517 −321 −378 C ATOM 453 CE1 PHE A 82 −16.326 7.262 18.968 1.00 30.08 C ANISOU 453 CE1 PHE A 82 4657 4169 2602 3 −1011 88 C ATOM 454 CE2 PHE A 82 −18.440 6.561 19.858 1.00 28.43 C ANISOU 454 CE2 PHE A 82 5143 3059 2599 480 −438 287 C ATOM 455 CZ PHE A 82 −17.061 6.612 19.966 1.00 29.77 C ANISOU 455 CZ PHE A 82 5102 3359 2851 282 −1108 −171 C ATOM 456 O APRO A 83 −18.301 4.853 13.522 0.74 22.74 O ANISOU 456 O APRO A 83 3313 2768 2560 −197 −53 −17 O ATOM 457 N APRO A 83 −18.825 5.082 16.116 0.74 20.63 N ANISOU 457 N APRO A 83 2773 2904 2161 501 −83 −14 N ATOM 458 CA APRO A 83 −17.417 4.993 15.738 0.74 20.86 C ANISOU 458 CA APRO A 83 2663 2991 2270 968 −83 −17 C ATOM 459 C APRO A 83 −17.295 5.045 14.227 0.74 21.23 C ANISOU 459 C APRO A 83 3178 2409 2480 81 −222 −207 C ATOM 460 CB APRO A 83 −17.012 3.600 16.225 0.74 24.70 C ANISOU 460 CB APRO A 83 2927 3578 2880 984 183 477 C ATOM 461 CG APRO A 83 −17.986 3.279 17.346 0.74 25.48 C ANISOU 461 CG APRO A 83 3095 3505 3080 936 146 430 C ATOM 462 CD APRO A 83 −19.279 3.899 16.873 0.74 23.74 C ANISOU 462 CD APRO A 83 2911 3352 2757 531 −66 −88 C ATOM 463 O BPRO A 83 −18.283 4.761 13.573 0.26 25.54 O ANISOU 463 O BPRO A 83 3539 3224 2940 315 168 −293 O ATOM 464 N BPRO A 83 −18.817 5.081 16.099 0.26 21.32 N ANISOU 464 N BPRO A 83 2579 2907 2614 399 19 407 N ATOM 465 CA BPRO A 83 −17.402 5.136 15.751 0.26 21.83 C ANISOU 465 CA BPRO A 83 2732 2779 2785 312 208 282 C ATOM 466 C BPRO A 83 −17.287 5.047 14.248 0.26 24.04 C ANISOU 466 C BPRO A 83 3306 2902 2928 86 232 −180 C ATOM 467 CB BPRO A 83 −16.853 3.860 16.375 0.26 21.48 C ANISOU 467 CB BPRO A 83 2478 2675 3007 134 419 675 C ATOM 468 CG BPRO A 83 −17.978 2.899 16.235 0.26 20.85 C ANISOU 468 CG BPRO A 83 2249 2720 2954 454 273 542 C ATOM 469 CD BPRO A 83 −19.222 3.723 16.508 0.26 22.96 C ANISOU 469 CD BPRO A 83 2468 3434 2823 672 85 553 C ATOM 470 O GLU A 84 −15.904 2.794 12.572 1.00 31.21 O ANISOU 470 O GLU A 84 5278 3198 3384 40 173 −865 O ATOM 471 N GLU A 84 −16.099 5.317 13.736 1.00 25.49 N ANISOU 471 N GLU A 84 3646 2948 3092 −310 526 −426 N ATOM 472 C GLU A 84 −16.263 3.779 11.906 1.00 29.82 C ANISOU 472 C GLU A 84 4641 3545 3145 −386 401 −385 C ATOM 473 CA AGLU A 84 −15.885 5.205 12.307 0.62 29.77 C ANISOU 473 CA AGLU A 84 4113 3950 3248 −726 570 −493 C ATOM 474 CB AGLU A 84 −14.443 5.525 11.930 0.62 34.81 C ANISOU 474 CB AGLU A 84 4402 5228 3598 −1155 667 −774 C ATOM 475 CG AGLU A 84 −14.202 5.621 10.418 0.62 36.28 C ANISOU 475 CG AGLU A 84 4818 5426 3540 −1112 892 −907 C ATOM 476 CA BGLU A 84 −15.858 5.187 12.313 0.38 29.16 C ANISOU 476 CA BGLU A 84 4058 3758 3262 −442 446 −377 C ATOM 477 CB BGLU A 84 −14.388 5.452 11.991 0.38 31.91 C ANISOU 477 CB BGLU A 84 3976 4556 3593 −654 324 −452 C ATOM 478 CG BGLU A 84 −13.396 4.609 12.783 0.38 32.68 C ANISOU 478 CG BGLU A 84 3860 4904 3652 −430 219 −573 C ATOM 479 O ASP A 85 −15.707 1.834 9.028 1.00 37.07 O ANISOU 479 O ASP A 85 5502 5657 2927 −142 1140 −325 O ATOM 480 N ASP A 85 −17.040 3.687 10.843 1.00 31.28 N ANISOU 480 N ASP A 85 5268 3841 2777 −285 697 −454 N ATOM 481 C ASP A 85 −16.503 1.479 9.902 1.00 30.78 C ANISOU 481 C ASP A 85 4808 4235 2652 −522 569 −729 C ATOM 482 CG ASP A 85 −19.192 1.391 8.726 1.00 34.55 C ANISOU 482 CG ASP A 85 5916 4574 2639 −961 362 52 C ATOM 483 OD1 ASP A 85 −19.395 0.418 9.473 1.00 32.78 O ANISOU 483 OD1 ASP A 85 5362 4018 3077 −631 438 421 O ATOM 484 OD2 ASP A 85 −19.435 1.358 7.512 1.00 40.60 O ANISOU 484 OD2 ASP A 85 7698 5108 2620 −820 135 −409 O ATOM 485 CA AASP A 85 −17.599 2.422 10.405 0.50 31.21 C ANISOU 485 CA AASP A 85 5137 4219 2502 −567 529 −338 C ATOM 486 CB AASP A 85 −18.641 2.672 9.311 0.50 32.81 C ANISOU 486 CB AASP A 85 5417 4407 2641 −1074 290 17 C ATOM 487 CA BASP A 85 −17.599 2.422 10.405 0.50 31.20 C ANISOU 487 CA BASP A 85 5136 4218 2502 −568 530 −337 C ATOM 488 CB BASP A 85 −18.641 2.672 9.312 0.50 32.80 C ANISOU 488 CB BASP A 85 5416 4405 2641 −1077 293 19 C ATOM 489 O ARG A 86 −15.612 −2.973 9.130 1.00 35.85 O ANISOU 489 O ARG A 86 4572 3850 5200 −92 1205 −1072 O ATOM 490 N ARG A 86 −16.469 0.268 10.450 1.00 31.26 N ANISOU 490 N ARG A 86 4426 4480 2973 −240 676 −542 N ATOM 491 CA ARG A 86 −15.518 −0.743 10.004 1.00 32.86 C ANISOU 491 CA ARG A 86 4019 4586 3880 −1057 656 −628 C ATOM 492 C ARG A 86 −16.226 −1.913 9.330 1.00 32.39 C ANISOU 492 C ARG A 86 4418 3495 4394 −119 958 −886 C ATOM 493 CB ARG A 86 −14.680 −1.233 11.193 1.00 36.58 C ANISOU 493 CB ARG A 86 4355 5051 4492 −631 198 −603 C ATOM 494 CG ARG A 86 −13.757 −0.165 11.776 1.00 36.27 C ANISOU 494 CG ARG A 86 4656 4401 4726 −706 79 −1212 C ATOM 495 CD ARG A 86 −12.555 0.089 10.855 1.00 40.36 C ANISOU 495 CD ARG A 86 5035 5109 5192 −394 −322 −579 C ATOM 496 O SER A 87 −18.498 −3.594 6.042 1.00 34.51 O ANISOU 496 O SER A 87 5952 4009 3153 −80 258 305 O ATOM 497 N SER A 87 −17.511 −1.747 8.990 1.00 29.93 N ANISOU 497 N SER A 87 4223 3507 3643 −1038 1047 −242 N ATOM 498 CA SER A 87 −18.261 −2.819 8.303 1.00 29.09 C ANISOU 498 CA SER A 87 4311 3704 3038 −945 1119 −49 C ATOM 499 C SER A 87 −18.165 −2.667 6.793 1.00 31.24 C ANISOU 499 C SER A 87 5281 3609 2981 −760 779 60 C ATOM 500 CB SER A 87 −19.738 −2.847 8.710 1.00 28.40 C ANISOU 500 CB SER A 87 4171 3559 3062 −542 515 225 C ATOM 501 OG SER A 87 −20.450 −1.741 8.163 1.00 29.67 O ANISOU 501 OG SER A 87 4864 3795 2613 −369 −195 280 O ATOM 502 O GLN A 88 −15.661 0.062 5.677 1.00 35.65 O ANISOU 502 O GLN A 88 6338 4381 2827 −906 966 −716 O ATOM 503 N GLN A 88 −17.702 −1.503 6.360 1.00 28.54 N ANISOU 503 N GLN A 88 4855 3292 2697 −490 284 −173 N ATOM 504 CA GLN A 88 −17.569 −1.182 4.955 1.00 33.90 C ANISOU 504 CA GLN A 88 5221 4806 2853 −735 461 −496 C ATOM 505 C GLN A 88 −16.255 −0.470 4.727 1.00 35.45 C ANISOU 505 C GLN A 88 6005 4772 2694 −847 1039 −941 C ATOM 506 CB GLN A 88 −18.736 −0.289 4.509 1.00 31.31 C ANISOU 506 CB GLN A 88 4696 4584 2618 −922 227 −129 C ATOM 507 CG GLN A 88 −20.088 −0.968 4.655 1.00 32.64 C ANISOU 507 CG GLN A 88 4902 5292 2209 −592 648 −553 C ATOM 508 CD GLN A 88 −20.315 −2.105 3.658 1.00 36.25 C ANISOU 508 CD GLN A 88 5163 6336 2274 44 1289 −836 C ATOM 509 OE1 GLN A 88 −19.440 −2.450 2.834 1.00 40.67 O ANISOU 509 OE1 GLN A 88 5517 7444 2491 −712 808 −1367 O ATOM 510 NE2 GLN A 88 −21.519 −2.675 3.702 1.00 37.45 N ANISOU 510 NE2 GLN A 88 5002 6422 2807 −432 1077 −245 N ATOM 511 O PRO A 89 −15.707 2.257 3.519 1.00 42.39 O ANISOU 511 O PRO A 89 8235 4472 3399 −2054 790 −754 O ATOM 512 N PRO A 89 −15.788 −0.445 3.466 1.00 38.38 N ANISOU 512 N PRO A 89 6933 4791 2859 −1271 1577 −970 N ATOM 513 CA PRO A 89 −14.520 0.240 3.197 1.00 39.05 C ANISOU 513 CA PRO A 89 7344 4358 3135 −2106 1680 −255 C ATOM 514 C PRO A 89 −14.615 1.695 3.563 1.00 42.25 C ANISOU 514 C PRO A 89 8056 4672 3324 −2041 1306 −204 C ATOM 515 CB PRO A 89 −14.369 0.107 1.690 1.00 41.99 C ANISOU 515 CB PRO A 89 7688 5350 2916 −1511 1804 −188 C ATOM 516 CG PRO A 89 −15.213 −0.987 1.288 1.00 40.12 C ANISOU 516 CG PRO A 89 7391 4717 3135 −2191 1758 −122 C ATOM 517 CD PRO A 89 −16.325 −1.098 2.253 1.00 38.08 C ANISOU 517 CD PRO A 89 7289 4438 2741 −1610 1452 −1034 C ATOM 518 O GLY A 90 −13.766 4.053 1.897 1.00 50.07 O ANISOU 518 O GLY A 90 10806 4730 3490 −2299 1756 −696 O ATOM 519 N GLY A 90 −13.485 2.286 3.931 1.00 42.62 N ANISOU 519 N GLY A 90 8318 4368 3507 −2948 881 −564 N ATOM 520 CA GLY A 90 −13.440 3.699 4.250 1.00 46.50 C ANISOU 520 CA GLY A 90 9190 4754 3723 −2602 1105 −750 C ATOM 521 C GLY A 90 −13.821 4.527 3.038 1.00 49.51 C ANISOU 521 C GLY A 90 10315 4774 3723 −2032 1501 −566 C ATOM 522 O GLN A 91 −14.348 8.633 3.531 1.00 60.25 O ANISOU 522 O GLN A 91 12188 6000 4707 834 2151 46 O ATOM 523 N GLN A 91 −14.219 5.764 3.280 1.00 53.64 N ANISOU 523 N GLN A 91 11363 4889 4127 −731 1334 −315 N ATOM 524 CA GLN A 91 −14.641 6.655 2.210 1.00 54.13 C ANISOU 524 CA GLN A 91 11631 4667 4269 −384 1697 72 C ATOM 525 C GLN A 91 −14.110 8.062 2.466 1.00 57.56 C ANISOU 525 C GLN A 91 11791 5314 4767 288 1902 13 C ATOM 526 CB GLN A 91 −16.171 6.675 2.114 1.00 54.49 C ANISOU 526 CB GLN A 91 11546 4962 4196 −620 1607 −216 C ATOM 527 O ASP A 92 −14.923 10.911 0.914 1.00 56.66 O ANISOU 527 O ASP A 92 10373 5142 6015 1649 1210 −1660 O ATOM 528 N ASP A 92 −13.383 8.609 1.493 1.00 56.97 N ANISOU 528 N ASP A 92 11008 5464 5176 405 1970 251 N ATOM 529 CA ASP A 92 −12.820 9.957 1.599 1.00 55.51 C ANISOU 529 CA ASP A 92 10188 5341 5561 897 1707 −75 C ATOM 530 C ASP A 92 −13.592 10.985 1.684 1.00 53.27 C ANISOU 530 C ASP A 92 9661 4871 5709 1006 1477 −905 C ATOM 531 CB ASP A 92 −11.903 10.241 0.402 1.00 55.64 C ANISOU 531 CB ASP A 92 9800 5659 5681 505 1879 291 C ATOM 532 N SER A 93 −13.835 11.935 2.614 1.00 42.80 N ANISOU 532 N SER A 93 8122 2599 5540 451 1585 −868 N ATOM 533 CA SER A 93 −14.985 12.746 2.983 1.00 38.50 C ANISOU 533 CA SER A 93 6693 3361 4575 −257 1960 −1003 C ATOM 534 C SER A 93 −14.678 14.152 3.484 1.00 31.06 C ANISOU 534 C SER A 93 5067 2890 3853 148 1312 −950 C ATOM 535 O SER A 93 −13.716 14.353 4.234 1.00 37.92 O ANISOU 535 O SER A 93 4552 5039 4817 1141 1078 −92 O ATOM 536 CB SER A 93 −15.759 12.030 4.074 1.00 40.18 C ANISOU 536 CB SER A 93 6953 3882 4430 −772 1532 −1274 C ATOM 537 OG SER A 93 −16.999 12.656 4.233 1.00 38.36 O ANISOU 537 OG SER A 93 6253 4256 4067 −1358 1677 −1700 O ATOM 538 N ARG A 94 −15.533 15.114 3.121 1.00 27.17 N ANISOU 538 N ARG A 94 4597 3294 2431 −235 1036 −346 N ATOM 539 CA ARG A 94 −15.488 16.429 3.758 1.00 22.75 C ANISOU 539 CA ARG A 94 3400 3348 1895 −369 479 −28 C ATOM 540 C ARG A 94 −16.160 16.421 5.124 1.00 21.09 C ANISOU 540 C ARG A 94 2696 3597 1722 −432 270 −341 C ATOM 541 O ARG A 94 −16.126 17.410 5.789 1.00 21.86 O ANISOU 541 O ARG A 94 3236 3180 1890 −422 260 −138 O ATOM 542 CB ARG A 94 −16.186 17.502 2.898 1.00 26.10 C ANISOU 542 CB ARG A 94 3701 4157 2061 75 305 801 C ATOM 543 CG ARG A 94 −15.485 17.813 1.611 1.00 26.03 C ANISOU 543 CG ARG A 94 3195 4624 2073 239 224 739 C ATOM 544 CD ARG A 94 −16.125 19.020 0.916 1.00 27.51 C ANISOU 544 CD ARG A 94 3149 5362 1943 867 355 1021 C ATOM 545 NE ARG A 94 −17.533 18.761 0.637 1.00 28.02 N ANISOU 545 NE ARG A 94 2666 5611 2368 699 −110 17 N ATOM 546 CZ ARG A 94 −18.538 19.539 1.029 1.00 22.60 C ANISOU 546 CZ ARG A 94 2360 4470 1758 −60 −197 −95 C ATOM 547 NH1 ARG A 94 −18.303 20.671 1.684 1.00 24.22 N ANISOU 547 NH1 ARG A 94 2892 4712 1599 −407 78 −113 N ATOM 548 NH2 ARG A 94 −19.772 19.195 0.736 1.00 24.78 N ANISOU 548 NH2 ARG A 94 3273 4014 2128 826 −108 4 N ATOM 549 N PHE A 95 −16.784 15.314 5.504 1.00 20.85 N ANISOU 549 N PHE A 95 3394 3074 1455 −671 239 −286 N ATOM 550 C PHE A 95 −16.870 14.368 7.755 1.00 20.58 C ANISOU 550 C PHE A 95 3213 2963 1642 −63 189 308 C ATOM 551 O PHE A 95 −16.363 13.284 7.425 1.00 27.39 O ANISOU 551 O PHE A 95 4832 3034 2540 613 −91 −57 O ATOM 552 CA APHE A 95 −17.561 15.263 6.743 0.55 21.28 C ANISOU 552 CA APHE A 95 3251 3465 1371 −530 −183 71 C ATOM 553 CB APHE A 95 −19.004 14.812 6.473 0.55 23.58 C ANISOU 553 CB APHE A 95 3538 3900 1522 −836 −314 327 C ATOM 554 CG APHE A 95 −19.756 15.729 5.534 0.55 22.19 C ANISOU 554 CG APHE A 95 3107 3868 1455 −1493 −413 267 C ATOM 555 CD1 APHE A 95 −20.546 16.758 6.027 0.55 23.63 C ANISOU 555 CD1 APHE A 95 3583 3884 1511 −1279 −394 578 C ATOM 556 CD2 APHE A 95 −19.674 15.570 4.153 0.55 21.24 C ANISOU 556 CD2 APHE A 95 3457 3320 1295 −603 −166 755 C ATOM 557 CE1 APHE A 95 −21.240 17.593 5.167 0.55 23.61 C ANISOU 557 CE1 APHE A 95 3405 4028 1538 −1275 −145 274 C ATOM 558 CE2 APHE A 95 −20.359 16.411 3.305 0.55 23.20 C ANISOU 558 CE2 APHE A 95 3257 4020 1537 −6 126 −279 C ATOM 559 CZ APHE A 95 −21.133 17.421 3.813 0.55 23.09 C ANISOU 559 CZ APHE A 95 3297 3912 1564 −470 344 300 C ATOM 560 CA BPHE A 95 −17.576 15.217 6.740 0.45 20.30 C ANISOU 560 CA BPHE A 95 3171 3054 1490 −552 −106 87 C ATOM 561 CB BPHE A 95 −18.920 14.561 6.465 0.45 20.68 C ANISOU 561 CB BPHE A 95 3409 2749 1699 −615 −266 317 C ATOM 562 CG BPHE A 95 −19.626 15.135 5.294 0.45 18.61 C ANISOU 562 CG BPHE A 95 3166 2357 1548 −265 123 395 C ATOM 563 CD1 BPHE A 95 −20.183 16.403 5.364 0.45 21.97 C ANISOU 563 CD1 BPHE A 95 3051 3751 1548 349 80 454 C ATOM 564 CD2 BPHE A 95 −19.710 14.433 4.103 0.45 17.20 C ANISOU 564 CD2 BPHE A 95 2668 1958 1908 214 218 −3 C ATOM 565 CE1 BPHE A 95 −20.830 16.948 4.285 0.45 23.41 C ANISOU 565 CE1 BPHE A 95 2539 4629 1725 176 24 7 C ATOM 566 CE2 BPHE A 95 −20.366 14.968 3.028 0.45 21.95 C ANISOU 566 CE2 BPHE A 95 2908 3552 1878 642 −123 −403 C ATOM 567 CZ BPHE A 95 −20.919 16.229 3.113 0.45 22.35 C ANISOU 567 CZ BPHE A 95 1954 4668 1869 695 80 −603 C ATOM 568 N ARG A 96 −16.837 14.841 8.989 1.00 20.91 N ANISOU 568 N ARG A 96 2695 3730 1522 31 −61 49 N ATOM 569 C ARG A 96 −16.991 14.137 11.313 1.00 20.35 C ANISOU 569 C ARG A 96 3091 3020 1619 557 19 −272 C ATOM 570 O ARG A 96 −17.652 15.132 11.602 1.00 19.34 O ANISOU 570 O ARG A 96 3037 2624 1688 576 26 −56 O ATOM 571 CG AARG A 96 −13.712 14.155 11.035 0.72 34.13 C ANISOU 571 CG AARG A 96 3860 6297 2809 430 −336 −523 C ATOM 572 CD AARG A 96 −12.525 15.090 11.345 0.72 33.69 C ANISOU 572 CD AARG A 96 3252 6072 3478 −719 −259 −531 C ATOM 573 NE AARG A 96 −11.631 15.298 10.206 0.72 39.09 N ANISOU 573 NE AARG A 96 3882 6644 4327 −119 −187 −749 N ATOM 574 CZ AARG A 96 −10.517 16.027 10.235 0.72 39.28 C ANISOU 574 CZ AARG A 96 4140 6177 4610 136 1 −920 C ATOM 575 NH1 AARG A 96 −10.139 16.648 11.343 0.72 33.42 N ANISOU 575 NH1 AARG A 96 3843 4424 4431 39 −444 −1393 N ATOM 576 NH2 AARG A 96 −9.778 16.137 9.135 0.72 43.24 N ANISOU 576 NH2 AARG A 96 4516 6840 5072 381 −52 −980 N ATOM 577 CA AARG A 96 −16.128 14.141 10.048 0.72 22.82 C ANISOU 577 CA AARG A 96 3065 3917 1688 450 −384 −300 C ATOM 578 CB AARG A 96 −14.820 14.911 10.328 0.72 29.51 C ANISOU 578 CB AARG A 96 3200 5515 2496 424 −371 93 C ATOM 579 CG BARG A 96 −13.801 14.649 9.198 0.28 32.35 C ANISOU 579 CG BARG A 96 3511 5486 3296 15 73 −304 C ATOM 580 CD BARG A 96 −12.553 15.474 9.471 0.28 36.70 C ANISOU 580 CD BARG A 96 4017 6152 3776 540 −44 −530 C ATOM 581 NE BARG A 96 −11.775 15.718 8.259 0.28 38.49 N ANISOU 581 NE BARG A 96 4175 6296 4153 497 223 −803 N ATOM 582 CZ BARG A 96 −10.693 16.488 8.217 0.28 40.96 C ANISOU 582 CZ BARG A 96 4857 6214 4492 632 227 −780 C ATOM 583 NH1 BARG A 96 −10.267 17.088 9.321 0.28 41.22 N ANISOU 583 NH1 BARG A 96 4986 5983 4694 555 −2 −1069 N ATOM 584 NH2 BARG A 96 −10.037 16.658 7.075 0.28 41.24 N ANISOU 584 NH2 BARG A 96 4866 6121 4683 730 413 −642 N ATOM 585 CA BARG A 96 −16.159 14.110 10.049 0.28 22.57 C ANISOU 585 CA BARG A 96 2951 3775 1849 348 −93 −144 C ATOM 586 CB BARG A 96 −14.787 14.729 10.345 0.28 28.08 C ANISOU 586 CB BARG A 96 3086 4920 2663 293 −61 38 C ATOM 587 N VAL A 97 −16.968 13.015 12.034 1.00 21.53 N ANISOU 587 N VAL A 97 3316 3008 1855 361 −527 −109 N ATOM 588 CA VAL A 97 −17.528 12.949 13.376 1.00 18.82 C ANISOU 588 CA VAL A 97 2335 2566 2248 227 −656 −4 C ATOM 589 C VAL A 97 −16.381 12.558 14.291 1.00 20.67 C ANISOU 589 C VAL A 97 2449 2946 2459 −110 −456 201 C ATOM 590 O VAL A 97 −15.705 11.549 14.075 1.00 23.93 O ANISOU 590 O VAL A 97 3100 3292 2701 727 −620 −4 O ATOM 591 CB VAL A 97 −18.722 11.960 13.549 1.00 21.64 C ANISOU 591 CB VAL A 97 2515 3010 2698 65 −360 −128 C ATOM 592 CG1 VAL A 97 −19.173 11.964 15.005 1.00 24.40 C ANISOU 592 CG1 VAL A 97 3154 3368 2749 109 −322 991 C ATOM 593 CG2 VAL A 97 −19.888 12.325 12.655 1.00 23.05 C ANISOU 593 CG2 VAL A 97 2578 3365 2813 370 −474 −497 C ATOM 594 N ATHR A 98 −16.102 13.405 15.274 0.54 20.12 N ANISOU 594 N ATHR A 98 2232 3211 2204 −431 −432 105 N ATOM 595 CA ATHR A 98 −15.090 13.072 16.277 0.54 23.91 C ANISOU 595 CA ATHR A 98 2780 3858 2446 −609 −506 197 C ATOM 596 C ATHR A 98 −15.677 13.128 17.668 0.54 20.84 C ANISOU 596 C ATHR A 98 2301 3649 1969 −728 −365 516 C ATOM 597 O ATHR A 98 −16.453 14.036 17.988 0.54 21.61 O ANISOU 597 O ATHR A 98 3168 3407 1634 8 6 604 O ATOM 598 CB ATHR A 98 −13.891 14.036 16.259 0.54 30.22 C ANISOU 598 CB ATHR A 98 3569 4953 2961 −106 −562 534 C ATOM 599 OG1 ATHR A 98 −14.350 15.381 16.455 0.54 31.33 O ANISOU 599 OG1 ATHR A 98 3048 5642 3213 −215 −587 412 O ATOM 600 CG2 ATHR A 98 −13.113 13.920 14.954 0.54 35.29 C ANISOU 600 CG2 ATHR A 98 4475 5671 3265 313 −244 479 C ATOM 601 N BTHR A 98 −16.176 13.363 15.321 0.46 20.09 N ANISOU 601 N BTHR A 98 2038 3530 2064 549 −436 247 N ATOM 602 CA BTHR A 98 −15.106 13.085 16.263 0.46 21.23 C ANISOU 602 CA BTHR A 98 2135 3849 2082 592 −449 245 C ATOM 603 C BTHR A 98 −15.562 13.201 17.705 0.46 20.15 C ANISOU 603 C BTHR A 98 1803 3948 1904 292 −759 385 C ATOM 604 O BTHR A 98 −16.137 14.222 18.094 0.46 22.84 O ANISOU 604 O BTHR A 98 2486 4261 1932 1126 −694 205 O ATOM 605 CB BTHR A 98 −13.952 14.043 16.045 0.46 21.40 C ANISOU 605 CB BTHR A 98 2109 4039 1983 579 −109 323 C ATOM 606 OG1 BTHR A 98 −13.601 14.042 14.653 0.46 20.44 O ANISOU 606 OG1 BTHR A 98 1921 3731 2112 −352 334 −338 O ATOM 607 CG2 BTHR A 98 −12.775 13.615 16.893 0.46 20.00 C ANISOU 607 CG2 BTHR A 98 1665 4186 1747 384 5 507 C ATOM 608 N GLN A 99 −15.287 12.166 18.500 1.00 21.57 N ANISOU 608 N GLN A 99 2526 3886 1782 291 −239 647 N ATOM 609 CA GLN A 99 −15.642 12.176 19.911 1.00 19.60 C ANISOU 609 CA GLN A 99 2407 2987 2054 100 −73 555 C ATOM 610 C GLN A 99 −14.627 13.036 20.635 1.00 21.13 C ANISOU 610 C GLN A 99 2168 3429 2433 −383 −373 769 C ATOM 611 O GLN A 99 −13.413 12.849 20.481 1.00 25.72 O ANISOU 611 O GLN A 99 2265 4660 2845 205 −90 871 O ATOM 612 CB GLN A 99 −15.627 10.763 20.468 1.00 23.32 C ANISOU 612 CB GLN A 99 3448 3354 2060 84 −398 944 C ATOM 613 CG GLN A 99 −16.121 10.657 21.911 1.00 24.29 C ANISOU 613 CG GLN A 99 3681 3235 2315 −359 −790 792 C ATOM 614 CD GLN A 99 −16.120 9.241 22.387 1.00 24.87 C ANISOU 614 CD GLN A 99 3340 3395 2714 −104 −658 541 C ATOM 615 OE1 GLN A 99 −15.155 8.499 22.151 1.00 27.40 O ANISOU 615 OE1 GLN A 99 3662 3771 2979 721 −481 14 O ATOM 616 NE2 GLN A 99 −17.202 8.830 23.046 1.00 24.83 N ANISOU 616 NE2 GLN A 99 3350 3346 2738 −410 −466 473 N ATOM 617 N LEU A 100 −15.108 13.989 21.424 1.00 20.35 N ANISOU 617 N LEU A 100 2427 3424 1881 −315 −846 702 N ATOM 618 CA LEU A 100 −14.218 14.855 22.193 1.00 22.12 C ANISOU 618 CA LEU A 100 2509 3354 2543 −587 −923 929 C ATOM 619 C LEU A 100 −13.757 14.099 23.439 1.00 25.22 C ANISOU 619 C LEU A 100 2833 3977 2774 −1314 −1036 1650 C ATOM 620 O LEU A 100 −14.376 13.116 23.851 1.00 27.84 O ANISOU 620 O LEU A 100 3004 4776 2798 −1252 −1055 1755 O ATOM 621 CB LEU A 100 −14.954 16.148 22.564 1.00 22.18 C ANISOU 621 CB LEU A 100 3310 2550 2569 −116 −841 571 C ATOM 622 CG LEU A 100 −15.310 16.980 21.323 1.00 28.57 C ANISOU 622 CG LEU A 100 3537 3836 3484 −505 −141 1220 C ATOM 623 CD1 LEU A 100 −15.964 18.295 21.711 1.00 32.10 C ANISOU 623 CD1 LEU A 100 3875 4438 3882 −661 −249 677 C ATOM 624 CD2 LEU A 100 −14.102 17.260 20.439 1.00 31.65 C ANISOU 624 CD2 LEU A 100 4243 4262 3519 8 165 1410 C ATOM 625 O PRO A 101 −12.823 12.888 27.227 1.00 42.12 O ANISOU 625 O PRO A 101 4341 7516 4147 −2276 −1438 2756 O ATOM 626 N PRO A 101 −12.641 14.524 24.022 1.00 27.37 N ANISOU 626 N PRO A 101 3025 4492 2883 −1042 −851 1757 N ATOM 627 C PRO A 101 −13.061 13.728 26.355 1.00 34.13 C ANISOU 627 C PRO A 101 3698 6095 3173 −1859 −1291 1925 C ATOM 628 CA PRO A 101 −12.108 13.796 25.173 1.00 30.26 C ANISOU 628 CA PRO A 101 3072 4929 3498 −1719 −1295 2197 C ATOM 629 CB PRO A 101 −10.870 14.603 25.543 1.00 31.58 C ANISOU 629 CB PRO A 101 2962 5358 3680 −1735 −1316 1898 C ATOM 630 CG PRO A 101 −10.423 15.192 24.260 1.00 32.58 C ANISOU 630 CG PRO A 101 3238 5486 3656 −1126 −1249 2046 C ATOM 631 CD PRO A 101 −11.707 15.540 23.537 1.00 29.39 C ANISOU 631 CD PRO A 101 2928 4828 3412 −1714 −1259 1811 C ATOM 632 O ASN A 102 −16.801 12.781 28.200 1.00 35.02 O ANISOU 632 O ASN A 102 4270 6614 2423 −1745 −851 1252 O ATOM 633 N ASN A 102 −14.091 14.557 26.448 1.00 32.58 N ANISOU 633 N ASN A 102 4022 5777 2581 −2080 −1029 1493 N ATOM 634 CA ASN A 102 −15.065 14.346 27.553 1.00 32.70 C ANISOU 634 CA ASN A 102 4343 5858 2224 −1815 −549 1207 C ATOM 635 C ASN A 102 −16.057 13.180 27.305 1.00 29.34 C ANISOU 635 C ASN A 102 3349 5361 2439 −1440 −802 1599 C ATOM 636 CB ASN A 102 −15.768 15.655 27.921 1.00 35.06 C ANISOU 636 CB ASN A 102 4712 6095 2516 −1470 −1263 −197 C ATOM 637 CG ASN A 102 −16.865 16.039 26.954 1.00 35.49 C ANISOU 637 CG ASN A 102 5449 5336 2698 −1224 −1270 −897 C ATOM 638 OD1 ASN A 102 −17.007 15.447 25.897 1.00 33.75 O ANISOU 638 OD1 ASN A 102 5435 4761 2628 −1602 −1374 −353 O ATOM 639 ND2 ASN A 102 −17.654 17.043 27.322 1.00 41.24 N ANISOU 639 ND2 ASN A 102 6179 6153 3335 −152 −997 −218 N ATOM 640 O GLY A 103 −18.907 11.008 24.825 1.00 32.45 O ANISOU 640 O GLY A 103 3152 4883 4296 −845 −1333 240 O ATOM 641 N GLY A 103 −16.123 12.691 26.101 1.00 28.97 N ANISOU 641 N GLY A 103 3350 5204 2454 −710 −1037 1402 N ATOM 642 CA GLY A 103 −16.834 11.481 25.790 1.00 28.79 C ANISOU 642 CA GLY A 103 3333 4748 2858 −1476 −931 1338 C ATOM 643 C GLY A 103 −18.305 11.747 25.543 1.00 27.31 C ANISOU 643 C GLY A 103 3375 4064 2938 −1613 −1087 838 C ATOM 644 O ARG A 104 −21.504 13.994 24.086 1.00 22.07 O ANISOU 644 O ARG A 104 2425 3656 2303 −471 −456 432 O ATOM 645 N ARG A 104 −18.832 12.829 26.061 1.00 25.93 N ANISOU 645 N ARG A 104 3342 4210 2300 −646 −963 1045 N ATOM 646 CA ARG A 104 −20.201 13.227 25.880 1.00 25.73 C ANISOU 646 CA ARG A 104 3272 4683 1820 3 −922 241 C ATOM 647 C ARG A 104 −20.466 14.039 24.630 1.00 20.90 C ANISOU 647 C ARG A 104 2015 3732 2192 −400 −783 59 C ATOM 648 CB ARG A 104 −20.638 14.047 27.057 1.00 34.48 C ANISOU 648 CB ARG A 104 4973 6038 2089 1169 −12 106 C ATOM 649 CG ARG A 104 −22.086 14.384 27.026 1.00 41.42 C ANISOU 649 CG ARG A 104 5706 7086 2946 1174 501 −347 C ATOM 650 CD ARG A 104 −22.418 15.373 28.120 1.00 50.96 C ANISOU 650 CD ARG A 104 7134 7926 4304 1794 370 −841 C ATOM 651 NE ARG A 104 −21.389 16.386 28.246 1.00 60.36 N ANISOU 651 NE ARG A 104 8381 9038 5516 2806 225 −656 N ATOM 652 CZ ARG A 104 −21.471 17.644 27.836 1.00 63.89 C ANISOU 652 CZ ARG A 104 9252 8929 6093 2909 102 −250 C ATOM 653 NH1 ARG A 104 −22.552 18.085 27.225 1.00 63.72 N ANISOU 653 NH1 ARG A 104 9360 8710 6140 2947 131 −275 N ATOM 654 NH2 ARG A 104 −20.455 18.452 28.023 1.00 64.81 N ANISOU 654 NH2 ARG A 104 9606 8608 6413 2804 38 −321 N ATOM 655 N ASP A 105 −19.496 14.812 24.225 1.00 22.13 N ANISOU 655 N ASP A 105 2712 3885 1812 −265 −418 210 N ATOM 656 CA ASP A 105 −19.652 15.717 23.118 1.00 20.37 C ANISOU 656 CA ASP A 105 2627 3149 1964 −635 −551 381 C ATOM 657 C ASP A 105 −18.933 15.183 21.907 1.00 21.30 C ANISOU 657 C ASP A 105 2468 3720 1905 129 −110 114 C ATOM 658 O ASP A 105 −17.963 14.536 22.015 1.00 21.58 O ANISOU 658 O ASP A 105 2488 3988 1722 −86 −104 72 O ATOM 659 CB ASP A 105 −19.119 17.092 23.438 1.00 23.74 C ANISOU 659 CB ASP A 105 3191 3859 1971 −172 −224 −50 C ATOM 660 CG ASP A 105 −19.880 17.763 24.535 1.00 33.60 C ANISOU 660 CG ASP A 105 4328 5776 2664 −93 −275 −1112 C ATOM 661 OD1 ASP A 105 −21.065 17.547 24.681 1.00 34.44 O ANISOU 661 OD1 ASP A 105 4145 6321 2618 −284 −44 −1308 O ATOM 662 OD2 ASP A 105 −19.246 18.521 25.249 1.00 36.25 O ANISOU 662 OD2 ASP A 105 4728 5484 3562 −707 −265 −1489 O ATOM 663 N PHE A 106 −19.524 15.439 20.753 1.00 18.18 N ANISOU 663 N PHE A 106 2548 2696 1663 −538 −167 160 N ATOM 664 CA PHE A 106 −18.981 15.003 19.480 1.00 16.83 C ANISOU 664 CA PHE A 106 2415 2448 1531 −17 −266 248 C ATOM 665 C PHE A 106 −19.004 16.178 18.503 1.00 17.57 C ANISOU 665 C PHE A 106 1991 3059 1628 317 −319 255 C ATOM 666 O PHE A 106 −19.997 16.918 18.426 1.00 21.23 O ANISOU 666 O PHE A 106 2094 3402 2570 650 177 799 O ATOM 667 CB PHE A 106 −19.860 13.889 18.898 1.00 18.71 C ANISOU 667 CB PHE A 106 2259 3046 1805 61 −264 169 C ATOM 668 CG PHE A 106 −19.914 12.664 19.743 1.00 17.88 C ANISOU 668 CG PHE A 106 2132 2838 1822 105 −385 207 C ATOM 669 CD1 PHE A 106 −20.717 12.626 20.877 1.00 17.86 C ANISOU 669 CD1 PHE A 106 2273 2774 1740 −120 −307 213 C ATOM 670 CD2 PHE A 106 −19.146 11.549 19.421 1.00 19.49 C ANISOU 670 CD2 PHE A 106 2447 3221 1738 38 −412 243 C ATOM 671 CE1 PHE A 106 −20.742 11.505 21.683 1.00 19.36 C ANISOU 671 CE1 PHE A 106 2906 2398 2052 252 −233 −87 C ATOM 672 CE2 PHE A 106 −19.206 10.404 20.208 1.00 21.47 C ANISOU 672 CE2 PHE A 106 2787 3543 1827 9 −16 302 C ATOM 673 CZ PHE A 106 −19.981 10.391 21.342 1.00 20.27 C ANISOU 673 CZ PHE A 106 2985 2821 1895 −217 −336 217 C ATOM 674 N HIS A 107 −17.915 16.375 17.784 1.00 18.11 N ANISOU 674 N HIS A 107 2115 3526 1239 −191 −153 240 N ATOM 675 CA HIS A 107 −17.931 17.405 16.726 1.00 17.62 C ANISOU 675 CA HIS A 107 2317 3059 1319 −395 −451 134 C ATOM 676 C HIS A 107 −18.349 16.772 15.406 1.00 15.55 C ANISOU 676 C HIS A 107 2321 2421 1167 −278 −594 86 C ATOM 677 O HIS A 107 −17.791 15.750 15.006 1.00 19.06 O ANISOU 677 O HIS A 107 2768 2785 1689 358 −295 −121 O ATOM 678 CB HIS A 107 −16.580 18.074 16.555 1.00 19.06 C ANISOU 678 CB HIS A 107 2110 3144 1988 −846 −495 −173 C ATOM 679 CG HIS A 107 −16.336 19.176 17.532 1.00 20.90 C ANISOU 679 CG HIS A 107 2843 3071 2025 −955 −969 328 C ATOM 680 ND1 HIS A 107 −15.112 19.792 17.646 1.00 27.80 N ANISOU 680 ND1 HIS A 107 2976 4887 2700 −1398 −945 −352 N ATOM 681 CD2 HIS A 107 −17.164 19.809 18.400 1.00 22.85 C ANISOU 681 CD2 HIS A 107 3497 3272 1913 −257 −644 −76 C ATOM 682 CE1 HIS A 107 −15.182 20.740 18.564 1.00 27.90 C ANISOU 682 CE1 HIS A 107 3576 4309 2715 −871 −706 −930 C ATOM 683 NE2 HIS A 107 −16.417 20.773 19.037 1.00 25.61 N ANISOU 683 NE2 HIS A 107 3042 3935 2753 −1004 −432 −349 N ATOM 684 O MET A 108 −19.925 19.263 12.576 1.00 16.89 O ANISOU 684 O MET A 108 2706 2461 1251 −158 26 35 O ATOM 685 N MET A 108 −19.309 17.413 14.767 1.00 15.87 N ANISOU 685 N MET A 108 2301 2680 1049 −419 −400 230 N ATOM 686 C MET A 108 −19.344 18.168 12.511 1.00 15.57 C ANISOU 686 C MET A 108 2717 2119 1078 −523 4 −128 C ATOM 687 CA AMET A 108 −19.700 17.022 13.431 0.32 16.16 C ANISOU 687 CA AMET A 108 2600 2353 1187 13 −255 80 C ATOM 688 CB AMET A 108 −21.169 16.659 13.433 0.32 15.94 C ANISOU 688 CB AMET A 108 3022 1636 1398 −223 −93 −407 C ATOM 689 CG AMET A 108 −21.353 15.400 14.247 0.32 17.02 C ANISOU 689 CG AMET A 108 2499 2421 1547 −480 49 −142 C ATOM 690 SD AMET A 108 −23.038 14.856 14.506 0.32 16.64 S ANISOU 690 SD AMET A 108 2135 2566 1621 −97 11 25 S ATOM 691 CE AMET A 108 −22.785 13.224 15.205 0.32 15.65 C ANISOU 691 CE AMET A 108 2774 1318 1854 −329 −281 154 C ATOM 692 CA BMET A 108 −19.777 17.045 13.417 0.68 15.05 C ANISOU 692 CA BMET A 108 1659 2843 1218 −474 −213 226 C ATOM 693 CB BMET A 108 −21.303 16.993 13.391 0.68 16.38 C ANISOU 693 CB BMET A 108 1378 3382 1463 −501 174 454 C ATOM 694 CG BMET A 108 −21.875 15.650 13.763 0.68 20.01 C ANISOU 694 CG BMET A 108 2285 3439 1878 61 −154 863 C ATOM 695 SD BMET A 108 −21.507 15.184 15.465 0.68 19.52 S ANISOU 695 SD BMET A 108 2548 3053 1817 −242 −231 86 S ATOM 696 CE BMET A 108 −22.409 13.651 15.637 0.68 20.51 C ANISOU 696 CE BMET A 108 2629 2942 2221 −671 −220 14 C ATOM 697 O ASER A 109 −17.267 17.696 9.029 0.43 18.50 O ANISOU 697 O ASER A 109 1959 3313 1756 234 142 −1063 O ATOM 698 N ASER A 109 −18.333 17.924 11.681 0.43 15.96 N ANISOU 698 N ASER A 109 2243 2294 1526 −857 355 −225 N ATOM 699 CA ASER A 109 −17.667 19.024 10.994 0.43 19.35 C ANISOU 699 CA ASER A 109 2447 2967 1938 −715 95 −670 C ATOM 700 C ASER A 109 −17.594 18.792 9.493 0.43 19.29 C ANISOU 700 C ASER A 109 2177 3504 1650 −318 151 −805 C ATOM 701 CB ASER A 109 −16.239 19.196 11.523 0.43 23.72 C ANISOU 701 CB ASER A 109 2616 3962 2433 114 −62 −1036 C ATOM 702 OG ASER A 109 −15.449 18.066 11.206 0.43 24.87 O ANISOU 702 OG ASER A 109 2232 4522 2694 −77 142 −378 O ATOM 703 O BSER A 109 −17.755 17.712 8.903 0.57 16.58 O ANISOU 703 O BSER A 109 2228 2680 1393 −326 36 357 O ATOM 704 N BSER A 109 −18.310 17.930 11.700 0.57 17.42 N ANISOU 704 N BSER A 109 2651 3054 915 132 261 432 N ATOM 705 CA BSER A 109 −17.720 19.036 10.931 0.57 18.10 C ANISOU 705 CA BSER A 109 2316 3142 1420 −340 18 333 C ATOM 706 C BSER A 109 −17.807 18.844 9.413 0.57 17.35 C ANISOU 706 C BSER A 109 2279 2987 1328 −363 158 232 C ATOM 707 CB BSER A 109 −16.233 19.249 11.301 0.57 18.35 C ANISOU 707 CB BSER A 109 1707 3539 1728 −560 −117 −304 C ATOM 708 OG BSER A 109 −16.081 19.537 12.694 0.57 18.43 O ANISOU 708 OG BSER A 109 2119 3280 1604 −671 −282 −272 O ATOM 709 N AVAL A 110 −17.879 19.848 8.749 0.43 20.22 N ANISOU 709 N AVAL A 110 2646 3467 1570 −274 344 −416 N ATOM 710 CA AVAL A 110 −17.685 19.820 7.311 0.43 18.67 C ANISOU 710 CA AVAL A 110 2544 3062 1489 −282 353 −386 C ATOM 711 C AVAL A 110 −16.617 20.829 6.918 0.43 19.25 C ANISOU 711 C AVAL A 110 2525 3225 1565 −86 198 −393 C ATOM 712 O AVAL A 110 −16.610 21.971 7.371 0.43 21.11 O ANISOU 712 O AVAL A 110 2862 3304 1853 −113 355 −451 O ATOM 713 CB AVAL A 110 −18.994 20.089 6.540 0.43 18.48 C ANISOU 713 CB AVAL A 110 2217 3191 1614 −484 317 −311 C ATOM 714 CG1 AVAL A 110 −19.556 21.453 6.936 0.43 17.24 C ANISOU 714 CG1 AVAL A 110 1865 2994 1691 261 25 −350 C ATOM 715 CG2 AVAL A 110 −18.767 19.987 5.022 0.43 18.66 C ANISOU 715 CG2 AVAL A 110 3126 2446 1519 −907 508 −173 C ATOM 716 N BVAL A 110 −17.948 19.974 8.727 0.57 20.02 N ANISOU 716 N BVAL A 110 3350 2884 1373 −535 −10 617 N ATOM 717 CA BVAL A 110 −17.806 20.049 7.276 0.57 20.16 C ANISOU 717 CA BVAL A 110 3309 2772 1578 −634 −7 637 C ATOM 718 C BVAL A 110 −16.551 20.862 6.975 0.57 19.46 C ANISOU 718 C BVAL A 110 3030 2682 1682 −618 345 461 C ATOM 719 O BVAL A 110 −16.337 21.905 7.575 0.57 22.31 O ANISOU 719 O BVAL A 110 3588 2840 2047 −704 622 378 O ATOM 720 CB BVAL A 110 −19.015 20.766 6.604 0.57 24.08 C ANISOU 720 CB BVAL A 110 3663 3351 2136 −1178 −128 1214 C ATOM 721 CG1 BVAL A 110 −18.845 20.824 5.080 0.57 25.54 C ANISOU 721 CG1 BVAL A 110 3902 3935 1869 −723 −823 696 C ATOM 722 CG2 BVAL A 110 −20.331 20.085 6.959 0.57 30.09 C ANISOU 722 CG2 BVAL A 110 4574 4134 2725 −626 279 1349 C ATOM 723 O VAL A 111 −15.710 21.304 3.526 1.00 22.48 O ANISOU 723 O VAL A 111 3203 3547 1793 −452 306 67 O ATOM 724 N VAL A 111 −15.694 20.388 6.082 1.00 20.45 N ANISOU 724 N VAL A 111 2564 3535 1670 −208 209 89 N ATOM 725 C VAL A 111 −14.992 21.904 4.327 1.00 22.78 C ANISOU 725 C VAL A 111 2511 3946 2197 −572 238 99 C ATOM 726 CA VAL A 111 −14.614 21.254 5.641 1.00 21.42 C ANISOU 726 CA VAL A 111 2591 3604 1944 65 −166 −44 C ATOM 727 CB VAL A 111 −13.256 20.545 5.502 1.00 28.54 C ANISOU 727 CB VAL A 111 3359 5341 2143 776 −361 122 C ATOM 728 CG1 VAL A 111 −12.765 20.131 6.855 1.00 34.74 C ANISOU 728 CG1 VAL A 111 3942 6915 2341 1505 −240 1042 C ATOM 729 CG2 VAL A 111 −13.344 19.356 4.616 1.00 32.15 C ANISOU 729 CG2 VAL A 111 4741 4959 2514 1243 −217 140 C ATOM 730 N AARG A 112 −14.502 23.123 4.130 0.64 25.50 N ANISOU 730 N AARG A 112 2338 4648 2704 560 57 482 N ATOM 731 CA AARG A 112 −14.716 23.863 2.899 0.64 28.16 C ANISOU 731 CA AARG A 112 3096 4660 2946 224 75 807 C ATOM 732 C AARG A 112 −16.189 23.863 2.517 0.64 25.69 C ANISOU 732 C AARG A 112 2940 4205 2614 −321 −431 69 C ATOM 733 O AARG A 112 −16.599 23.293 1.497 0.64 28.17 O ANISOU 733 O AARG A 112 3662 4575 2464 36 172 −354 O ATOM 734 CB AARG A 112 −13.881 23.264 1.784 0.64 32.74 C ANISOU 734 CB AARG A 112 3520 5668 3251 772 812 1196 C ATOM 735 CG AARG A 112 −13.672 24.222 0.641 0.64 37.11 C ANISOU 735 CG AARG A 112 4357 6186 3556 1108 1203 1445 C ATOM 736 CD AARG A 112 −12.668 23.673 −0.347 0.64 37.95 C ANISOU 736 CD AARG A 112 4603 5884 3933 499 1346 1205 C ATOM 737 NE AARG A 112 −12.339 24.695 −1.313 0.64 35.79 N ANISOU 737 NE AARG A 112 4011 5560 4028 −410 928 336 N ATOM 738 CZ AARG A 112 −11.469 24.535 −2.294 0.64 35.41 C ANISOU 738 CZ AARG A 112 3566 5629 4259 −1251 877 138 C ATOM 739 NH1 AARG A 112 −10.841 23.380 −2.456 0.64 34.82 N ANISOU 739 NH1 AARG A 112 3635 5291 4303 −780 384 68 N ATOM 740 NH2 AARG A 112 −11.251 25.535 −3.121 0.64 37.00 N ANISOU 740 NH2 AARG A 112 3619 5713 4724 −1464 953 −112 N ATOM 741 N BARG A 112 −14.507 23.128 4.129 0.36 25.39 N ANISOU 741 N BARG A 112 2625 4291 2730 266 157 616 N ATOM 742 CA BARG A 112 −14.706 23.887 2.896 0.36 26.81 C ANISOU 742 CA BARG A 112 2991 4095 3103 −24 272 1219 C ATOM 743 C BARG A 112 −16.169 23.948 2.474 0.36 24.08 C ANISOU 743 C BARG A 112 2848 3479 2824 −25 125 1085 C ATOM 744 O BARG A 112 −16.539 23.526 1.376 0.36 23.44 O ANISOU 744 O BARG A 112 2813 3230 2863 461 906 1647 O ATOM 745 CB BARG A 112 −13.827 23.325 1.781 0.36 31.96 C ANISOU 745 CB BARG A 112 3389 5114 3642 279 443 1177 C ATOM 746 CG BARG A 112 −12.347 23.407 2.107 0.36 35.35 C ANISOU 746 CG BARG A 112 3724 5528 4178 41 550 1210 C ATOM 747 CD BARG A 112 −11.473 23.126 0.904 0.36 39.31 C ANISOU 747 CD BARG A 112 4401 5838 4698 −159 544 1152 C ATOM 748 NE BARG A 112 −10.076 22.971 1.297 0.36 44.00 N ANISOU 748 NE BARG A 112 5216 6419 5084 84 425 1034 N ATOM 749 CZ BARG A 112 −9.106 22.587 0.475 0.36 45.80 C ANISOU 749 CZ BARG A 112 5444 6610 5349 −368 486 970 C ATOM 750 NH1 BARG A 112 −9.375 22.314 −0.794 0.36 47.53 N ANISOU 750 NH1 BARG A 112 5679 7004 5376 −200 445 828 N ATOM 751 NH2 BARG A 112 −7.866 22.467 0.926 0.36 45.03 N ANISOU 751 NH2 BARG A 112 5455 6153 5501 −891 469 1060 N ATOM 752 N ALA A 113 −16.999 24.471 3.367 1.00 23.98 N ANISOU 752 N ALA A 113 3000 3452 2658 130 −457 328 N ATOM 753 CA ALA A 113 −18.430 24.526 3.155 1.00 20.94 C ANISOU 753 CA ALA A 113 2416 3494 2046 −164 −422 331 C ATOM 754 C ALA A 113 −18.747 25.291 1.880 1.00 22.40 C ANISOU 754 C ALA A 113 3228 3217 2067 −533 −46 587 C ATOM 755 O ALA A 113 −18.148 26.310 1.575 1.00 25.47 O ANISOU 755 O ALA A 113 3626 3522 2531 −263 −590 849 O ATOM 756 CB ALA A 113 −19.075 25.220 4.378 1.00 24.76 C ANISOU 756 CB ALA A 113 3029 4434 1945 109 −90 −62 C ATOM 757 CD AARG A 114 −19.822 22.063 −2.196 0.44 27.73 C ANISOU 757 CD AARG A 114 4602 4367 1567 −229 528 927 C ATOM 758 NE AARG A 114 −20.565 20.821 −1.977 0.44 33.50 N ANISOU 758 NE AARG A 114 5210 5529 1988 984 468 594 N ATOM 759 CZ AARG A 114 −20.512 19.732 −2.743 0.44 33.12 C ANISOU 759 CZ AARG A 114 4858 5683 2042 1930 559 798 C ATOM 760 NH1 AARG A 114 −19.738 19.691 −3.834 0.44 35.33 N ANISOU 760 NH1 AARG A 114 5422 5657 2345 2434 940 848 N ATOM 761 NH2 AARG A 114 −21.248 18.668 −2.416 0.44 30.86 N ANISOU 761 NH2 AARG A 114 3689 6042 1995 1766 −568 −101 N ATOM 762 N AARG A 114 −19.681 24.763 1.110 0.44 23.54 N ANISOU 762 N AARG A 114 3330 3855 1757 −888 −497 392 N ATOM 763 CA AARG A 114 −20.120 25.419 −0.113 0.44 25.85 C ANISOU 763 CA AARG A 114 3684 4464 1673 −514 −616 420 C ATOM 764 C AARG A 114 −21.587 25.822 0.037 0.44 23.92 C ANISOU 764 C AARG A 114 3674 3849 1565 −455 −670 680 C ATOM 765 O AARG A 114 −22.282 25.310 0.928 0.44 23.09 O ANISOU 765 O AARG A 114 4106 3262 1404 −838 −675 192 O ATOM 766 CB AARG A 114 −19.886 24.498 −1.311 0.44 25.68 C ANISOU 766 CB AARG A 114 3957 4334 1468 −1066 −593 217 C ATOM 767 CG AARG A 114 −20.049 23.017 −0.997 0.44 28.12 C ANISOU 767 CG AARG A 114 4700 4662 1320 72 −71 616 C ATOM 768 CD BARG A 114 −18.772 23.074 −2.774 0.56 35.82 C ANISOU 768 CD BARG A 114 4056 5852 3704 117 −126 2051 C ATOM 769 NE BARG A 114 −19.944 22.277 −3.109 0.56 40.47 N ANISOU 769 NE BARG A 114 4804 5911 4662 55 −389 1775 N ATOM 770 CZ BARG A 114 −20.098 21.011 −2.753 0.56 42.83 C ANISOU 770 CZ BARG A 114 4566 6379 5328 −456 −1164 1126 C ATOM 771 NH1 BARG A 114 −19.143 20.408 −2.079 0.56 41.08 N ANISOU 771 NH1 BARG A 114 3605 6549 5453 −1102 −2126 551 N ATOM 772 NH2 BARG A 114 −21.198 20.343 −3.085 0.56 40.75 N ANISOU 772 NH2 BARG A 114 4003 5819 5660 −1974 −1102 1134 N ATOM 773 N BARG A 114 −19.723 24.767 1.160 0.56 22.89 N ANISOU 773 N BARG A 114 2520 4204 1973 −596 −310 454 N ATOM 774 CA BARG A 114 −20.196 25.345 −0.083 0.56 25.25 C ANISOU 774 CA BARG A 114 2633 4796 2163 340 −129 872 C ATOM 775 C BARG A 114 −21.603 25.887 0.108 0.56 22.44 C ANISOU 775 C BARG A 114 2802 3977 1749 456 −196 1011 C ATOM 776 O BARG A 114 −22.282 25.517 1.077 0.56 22.28 O ANISOU 776 O BARG A 114 2878 3893 1695 601 343 649 O ATOM 777 CB BARG A 114 −20.206 24.270 −1.151 0.56 29.98 C ANISOU 777 CB BARG A 114 3322 5573 2495 800 −78 1057 C ATOM 778 CG BARG A 114 −18.866 23.604 −1.360 0.56 31.95 C ANISOU 778 CG BARG A 114 3493 5722 2925 46 57 1221 C ATOM 779 N ARG A 115 −22.046 26.749 −0.807 1.00 25.34 N ANISOU 779 N ARG A 115 3540 4070 2019 −88 −539 1193 N ATOM 780 C ARG A 115 −24.377 26.091 −0.682 1.00 23.08 C ANISOU 780 C ARG A 115 3190 4041 1539 265 323 1049 C ATOM 781 O ARG A 115 −25.342 26.113 0.082 1.00 21.35 O ANISOU 781 O ARG A 115 2940 3726 1447 140 188 409 O ATOM 782 CA ARG A 115 −23.407 27.257 −0.729 1.00 27.28 C ANISOU 782 CA ARG A 115 4054 4056 2257 409 −360 1570 C ATOM 783 CB ARG A 115 −23.724 28.110 −1.967 1.00 32.91 C ATOM 784 CG ARG A 115 −25.218 28.462 −2.136 1.00 41.29 C ATOM 785 CD ARG A 115 −25.569 28.978 −3.572 1.00 61.63 C ATOM 786 NE ARG A 115 −25.270 27.958 −4.585 1.00 78.38 N ATOM 787 CZ ARG A 115 −24.270 28.027 −5.466 1.00 72.47 C ATOM 788 NH1 ARG A 115 −23.472 29.092 −5.502 1.00 76.77 N ATOM 789 NH2 ARG A 115 −24.071 27.031 −6.324 1.00 56.40 N ATOM 790 N AASN A 116 −24.118 25.053 −1.459 1.00 22.62 N ANISOU 790 N AASN A 116 3265 3968 1361 477 −142 510 N ATOM 791 CA AASN A 116 −25.047 23.934 −1.529 0.41 21.78 C ANISOU 791 CA AASN A 116 3351 3780 1144 774 57 −138 C ATOM 792 C AASN A 116 −24.921 22.945 −0.356 0.41 21.02 C ANISOU 792 C AASN A 116 3012 3710 1263 656 −173 −174 C ATOM 793 O AASN A 116 −25.539 21.881 −0.376 0.41 23.29 O ANISOU 793 O AASN A 116 2655 4542 1652 1467 −582 −538 O ATOM 794 CB AASN A 116 −24.913 23.237 −2.880 0.41 22.43 C ANISOU 794 CB AASN A 116 3493 3705 1323 1047 −478 −446 C ATOM 795 CG AASN A 116 −23.485 22.930 −3.205 0.41 25.26 C ANISOU 795 CG AASN A 116 3882 4220 1494 1347 −291 −558 C ATOM 796 OD1 AASN A 116 −22.717 22.625 −2.299 0.41 26.45 O ANISOU 796 OD1 AASN A 116 3529 4711 1810 897 −662 −673 O ATOM 797 ND2 AASN A 116 −23.101 23.017 −4.479 0.41 28.74 N ANISOU 797 ND2 AASN A 116 4690 4144 2084 1089 686 −736 N ATOM 798 N BASN A 116 −24.061 25.048 −1.446 0.59 22.74 N ANISOU 798 N BASN A 116 3178 3893 1569 883 −283 821 N ATOM 799 CA BASN A 116 −24.905 23.864 −1.578 0.59 23.94 C ANISOU 799 CA BASN A 116 3529 3995 1571 978 210 258 C ATOM 800 C BASN A 116 −25.030 23.066 −0.288 0.59 22.23 C ANISOU 800 C BASN A 116 3261 3740 1447 339 −21 150 C ATOM 801 O BASN A 116 −25.939 22.250 −0.154 0.59 23.73 O ANISOU 801 O BASN A 116 3117 4220 1678 77 68 221 O ATOM 802 CB BASN A 116 −24.371 22.942 −2.679 0.59 27.67 C ANISOU 802 CB BASN A 116 4242 4299 1972 1422 −53 185 C ATOM 803 CG BASN A 116 −24.010 23.681 −3.939 0.59 31.37 C ANISOU 803 CG BASN A 116 4600 5105 2215 1349 272 242 C ATOM 804 OD1 BASN A 116 −22.977 24.379 −4.004 0.59 35.05 O ANISOU 804 OD1 BASN A 116 5288 6005 2023 1324 736 732 O ATOM 805 ND2 BASN A 116 −24.850 23.519 −4.975 0.59 29.76 N ANISOU 805 ND2 BASN A 116 3851 4866 2590 1526 −90 463 N ATOM 806 N ASP A 117 −24.126 23.295 0.664 1.00 18.63 N ANISOU 806 N ASP A 117 2614 3385 1081 348 192 244 N ATOM 807 CA ASP A 117 −24.216 22.614 1.978 1.00 17.28 C ANISOU 807 CA ASP A 117 2064 3061 1440 234 −11 463 C ATOM 808 C ASP A 117 −25.308 23.206 2.871 1.00 17.99 C ANISOU 808 C ASP A 117 2199 3074 1563 −202 −177 182 C ATOM 809 O ASP A 117 −25.651 22.625 3.923 1.00 19.33 O ANISOU 809 O ASP A 117 2538 3209 1595 280 160 127 O ATOM 810 CB ASP A 117 −22.882 22.714 2.707 1.00 19.14 C ANISOU 810 CB ASP A 117 1982 3815 1475 316 −173 286 C ATOM 811 CG ASP A 117 −21.810 21.821 2.075 1.00 19.54 C ANISOU 811 CG ASP A 117 2536 2972 1916 −9 170 274 C ATOM 812 OD1 ASP A 117 −22.099 20.687 1.618 1.00 21.93 O ANISOU 812 OD1 ASP A 117 2784 3055 2494 193 −92 218 O ATOM 813 OD2 ASP A 117 −20.654 22.257 2.042 1.00 24.17 O ANISOU 813 OD2 ASP A 117 2760 4075 2348 −325 102 183 O ATOM 814 N SER A 118 −25.855 24.355 2.497 1.00 18.44 N ANISOU 814 N SER A 118 2710 2940 1356 107 91 301 N ATOM 815 CA SER A 118 −26.961 24.934 3.248 1.00 19.24 C ANISOU 815 CA SER A 118 2740 3090 1480 123 161 578 C ATOM 816 C SER A 118 −28.119 23.962 3.352 1.00 17.34 C ANISOU 816 C SER A 118 2236 2841 1513 −195 149 411 C ATOM 817 O SER A 118 −28.515 23.319 2.387 1.00 21.21 O ANISOU 817 O SER A 118 2561 3719 1780 −7 −135 61 O ATOM 818 CB SER A 118 −27.435 26.240 2.609 1.00 19.56 C ANISOU 818 CB SER A 118 2643 2969 1821 473 211 257 C ATOM 819 OG SER A 118 −26.407 27.208 2.561 1.00 21.23 O ANISOU 819 OG SER A 118 2741 3282 2043 −67 −164 262 O ATOM 820 N GLY A 119 −28.681 23.830 4.541 1.00 18.54 N ANISOU 820 N GLY A 119 2190 3450 1404 151 216 858 N ATOM 821 CA GLY A 119 −29.787 22.912 4.726 1.00 17.86 C ANISOU 821 CA GLY A 119 2272 3347 1168 −389 142 704 C ATOM 822 C GLY A 119 −29.940 22.538 6.187 1.00 16.48 C ANISOU 822 C GLY A 119 1791 3008 1462 162 −290 376 C ATOM 823 O GLY A 119 −29.411 23.231 7.047 1.00 17.68 O ANISOU 823 O GLY A 119 2467 2930 1320 −127 −151 322 O ATOM 824 N THR A 120 −30.652 1.455 6.460 1.00 16.96 N ANISOU 824 N THR A 120 2339 2589 1515 133 50 324 N ATOM 825 CA THR A 120 −30.846 21.038 7.844 1.00 17.39 C ANISOU 825 CA THR A 120 2261 2752 1596 363 11 412 C ATOM 826 C THR A 120 −30.229 19.704 8.108 1.00 17.16 C ANISOU 826 C THR A 120 2518 2569 1433 598 188 356 C ATOM 827 O THR A 120 −30.087 18.854 7.204 1.00 18.43 O ANISOU 827 O THR A 120 2501 2862 1640 293 −322 136 O ATOM 828 CB THR A 120 −32.295 21.080 8.322 1.00 22.74 C ANISOU 828 CB THR A 120 2508 3475 2658 1017 −502 139 C ATOM 829 OG1 THR A 120 −33.067 20.130 7.605 1.00 25.67 O ANISOU 829 OG1 THR A 120 2845 3744 3164 458 −375 −510 O ATOM 830 CG2 THR A 120 −32.866 22.453 8.114 1.00 25.50 C ANISOU 830 CG2 THR A 120 2512 3674 3501 577 384 939 C ATOM 831 N TYR A 121 −29.785 19.560 9.357 1.00 15.89 N ANISOU 831 N TYR A 121 2154 2671 1212 48 −246 588 N ATOM 832 CA TYR A 121 −28.971 18.442 9.782 1.00 16.03 C ANISOU 832 CA TYR A 121 2230 2669 1190 126 −244 476 C ATOM 833 C TYR A 121 −29.457 17.963 11.142 1.00 17.45 C ANISOU 833 C TYR A 121 2751 2650 1229 −26 −107 157 C ATOM 834 O TYR A 121 −30.094 18.715 11.871 1.00 18.74 O ANISOU 834 O TYR A 121 2581 3114 1427 −4 32 −32 O ATOM 835 CB TYR A 121 −27.505 18.867 9.909 1.00 17.02 C ANISOU 835 CB TYR A 121 2030 3297 1142 −152 7 84 C ATOM 836 CG TYR A 121 −26.862 19.284 8.595 1.00 16.99 C ANISOU 836 CG TYR A 121 1923 3330 1202 303 −58 −27 C ATOM 837 CD1 TYR A 121 −27.122 20.526 8.025 1.00 16.94 C ANISOU 837 CD1 TYR A 121 2175 2999 1261 81 −6 91 C ATOM 838 CD2 TYR A 121 −25.990 18.431 7.953 1.00 18.72 C ANISOU 838 CD2 TYR A 121 2084 3636 1394 597 20 3 C ATOM 839 CE1 TYR A 121 −26.535 20.894 6.783 1.00 17.26 C ANISOU 839 CE1 TYR A 121 2223 2814 1521 192 −68 174 C ATOM 840 CE2 TYR A 121 −25.396 18.786 6.753 1.00 19.09 C ANISOU 840 CE2 TYR A 121 2817 3101 1335 803 93 136 C ATOM 841 CZ TYR A 121 −25.658 20.002 6.196 1.00 18.53 C ANISOU 841 CZ TYR A 121 2973 3026 1040 892 218 291 C ATOM 842 OH TYR A 121 −25.073 20.311 4.976 1.00 20.02 O ANISOU 842 OH TYR A 121 3173 3044 1390 410 120 244 O ATOM 843 N LEU A 122 −29.151 16.732 11.481 1.00 17.79 N ANISOU 843 N LEU A 122 2426 2656 1679 300 99 258 N ATOM 844 CA LEU A 122 −29.436 16.259 12.829 1.00 18.38 C ANISOU 844 CA LEU A 122 2257 2876 1850 383 151 362 C ATOM 845 C LEU A 122 −28.480 15.143 13.165 1.00 17.50 C ANISOU 845 C LEU A 122 2241 2673 1738 488 72 83 C ATOM 846 O LEU A 122 −27.747 14.642 12.323 1.00 18.44 O ANISOU 846 O LEU A 122 2330 3142 1533 367 83 22 O ATOM 847 CB LEU A 122 −30.899 15.832 13.022 1.00 21.09 C ANISOU 847 CB LEU A 122 2899 2911 2203 −122 97 −92 C ATOM 848 CG LEU A 122 −31.446 14.572 12.301 1.00 24.97 C ANISOU 848 CG LEU A 122 2912 3526 3050 762 −893 −350 C ATOM 849 CD1 LEU A 122 −30.992 13.195 12.875 1.00 28.68 C ANISOU 849 CD1 LEU A 122 4278 2844 3777 −171 −455 −198 C ATOM 850 CD2 LEU A 122 −32.977 14.605 12.377 1.00 30.20 C ANISOU 850 CD2 LEU A 122 2868 5067 3539 −50 77 824 C ATOM 851 N CYS A 123 −28.460 14.772 14.435 1.00 16.93 N ANISOU 851 N CYS A 123 2292 2385 1757 459 93 276 N ATOM 852 C CYS A 123 −28.643 12.568 15.416 1.00 17.97 C ANISOU 852 C CYS A 123 1816 2736 2277 −65 303 37 C ATOM 853 O CYS A 123 −29.644 12.887 16.062 1.00 22.06 O ANISOU 853 O CYS A 123 2319 3083 2978 100 651 228 O ATOM 854 CA ACYS A 123 −27.673 13.661 14.942 0.31 19.10 C ANISOU 854 CA ACYS A 123 2057 3008 2190 −6 122 39 C ATOM 855 CB ACYS A 123 −26.847 14.215 16.103 0.31 21.57 C ANISOU 855 CB ACYS A 123 2243 3416 2539 306 −33 −437 C ATOM 856 SG ACYS A 123 −25.899 13.084 17.129 0.31 25.01 S ANISOU 856 SG ACYS A 123 2756 4044 2703 677 343 464 S ATOM 857 CA BCYS A 123 −27.706 13.581 14.809 0.69 18.12 C ANISOU 857 CA BCYS A 123 2473 2531 1880 208 −102 260 C ATOM 858 CB BCYS A 123 −26.510 13.901 15.718 0.69 20.42 C ANISOU 858 CB BCYS A 123 3173 3100 1485 820 −676 149 C ATOM 859 SG BCYS A 123 −26.883 14.651 17.349 0.69 20.60 S ANISOU 859 SG BCYS A 123 2693 3083 2053 279 165 300 S ATOM 860 N GLY A 124 −28.353 11.317 15.140 1.00 18.85 N ANISOU 860 N GLY A 124 2602 2364 2197 341 27 219 N ATOM 861 CA GLY A 124 −29.211 10.233 15.570 1.00 21.70 C ANISOU 861 CA GLY A 124 2982 2486 2776 54 161 780 C ATOM 862 C GLY A 124 −28.392 9.209 16.333 1.00 19.89 C ANISOU 862 C GLY A 124 2817 2321 2418 202 −132 44 C ATOM 863 O GLY A 124 −27.320 8.802 15.878 1.00 21.28 O ANISOU 863 O GLY A 124 2637 3036 2413 337 167 453 O ATOM 864 N ALA A 125 −28.854 8.849 17.529 1.00 19.97 N ANISOU 864 N ALA A 125 2743 2795 2051 174 198 573 N ATOM 865 CA ALA A 125 −28.199 7.823 18.311 1.00 19.04 C ANISOU 865 CA ALA A 125 2651 2461 2121 −104 232 384 C ATOM 866 C ALA A 125 −28.897 6.474 18.131 1.00 20.41 C ANISOU 866 C ALA A 125 2524 2715 2516 −849 237 283 C ATOM 867 O ALA A 125 −30.107 6.391 18.227 1.00 22.93 O ANISOU 867 O ALA A 125 2463 2991 3260 −482 402 210 O ATOM 868 CB ALA A 125 −28.199 8.206 19.825 1.00 22.31 C ANISOU 868 CB ALA A 125 3434 3137 1907 148 409 112 C ATOM 869 N ILE A 126 −28.134 5.431 17.849 1.00 2 1.28 N ANISOU 869 N ILE A 126 3331 2307 2448 333 229 −23 N ATOM 870 CA ILE A 126 −28.689 4.102 17.708 1.00 21.03 C ANISOU 870 CA ILE A 126 2812 2984 2196 232 149 104 C ATOM 871 C ILE A 126 −28.141 3.249 18.823 1.00 20.32 C ANISOU 871 C ILE A 126 2948 2533 2241 81 381 −141 C ATOM 872 O ILE A 126 −26.929 3.053 18.932 1.00 21.41 O ANISOU 872 O ILE A 126 3035 2745 2354 236 304 359 O ATOM 873 CB ILE A 126 −28.299 3.468 16.357 1.00 21.73 C ANISOU 873 CB ILE A 126 2778 2998 2480 −196 −64 −74 C ATOM 874 CG1 ILE A 126 −28.776 4.372 15.225 1.00 28.07 C ANISOU 874 CG1 ILE A 126 3806 4420 2439 863 −34 −111 C ATOM 875 CG2 ILE A 126 −28.936 2.091 16.234 1.00 23.65 C ANISOU 875 CG2 ILE A 126 3280 2829 2876 427 198 −128 C ATOM 876 CD1 ILE A 126 −28.124 4.074 13.911 1.00 32.06 C ANISOU 876 CD1 ILE A 126 4119 5593 2470 1068 160 48 C ATOM 877 N SER A 127 −29.021 2.786 19.704 1.00 24.52 N ANISOU 877 N SER A 127 3469 2702 3148 134 942 513 N ATOM 878 C SER A 127 −28.562 0.439 20.099 1.00 26.97 C ANISOU 878 C SER A 127 3918 2809 3522 −161 486 365 C ATOM 879 O SER A 127 −29.476 0.016 19.372 1.00 30.64 O ANISOU 879 O SER A 127 4144 3088 4412 −524 −127 480 O ATOM 880 CA ASER A 127 −28.644 1.821 20.727 0.54 27.12 C ANISOU 880 CA ASER A 127 4183 2766 3354 −53 1116 866 C ATOM 881 CB ASER A 127 −29.680 1.805 21.850 0.54 30.65 C ANISOU 881 CB ASER A 127 4362 3651 3631 −97 1372 780 C ATOM 882 OG ASER A 127 −30.912 1.290 21.378 0.54 33.96 O ANISOU 882 OG ASER A 127 5028 4137 3738 695 1611 696 O ATOM 883 CA BSER A 127 −28.625 1.827 20.718 0.46 27.29 C ANISOU 883 CA BSER A 127 4288 2833 3249 67 1037 923 C ATOM 884 CB BSER A 127 −29.607 1.847 21.886 0.46 31.44 C ANISOU 884 CB BSER A 127 4819 3848 3277 387 1211 1189 C ATOM 885 OG BSER A 127 −29.173 0.977 22.908 0.46 33.58 O ANISOU 885 OG BSER A 127 5560 4055 3145 879 1354 1535 O ATOM 886 O LEU A 128 −27.899 −3.841 20.248 1.00 40.42 O ANISOU 886 O LEU A 128 6912 3312 5132 −4 1784 999 O ATOM 887 N LEU A 128 −27.490 −0.275 20.368 1.00 26.79 N ANISOU 887 N LEU A 128 43.71 2658 3149 562 905 370 N ATOM 888 CA LEU A 128 −27.366 −1.581 19.753 1.00 29.51 C ANISOU 888 CA LEU A 128 5014 2643 3556 242 573 395 C ATOM 889 C LEU A 128 −27.806 −2.701 20.682 1.00 37.60 C ANISOU 889 C LEU A 128 6003 3639 4645 441 1078 830 C ATOM 890 CB LEU A 128 −25.945 −1.775 19.240 1.00 26.66 C ANISOU 890 CB LEU A 128 4851 2415 2863 599 348 48 C ATOM 891 CG LEU A 128 −25.549 −0.733 18.186 1.00 25.31 C ANISOU 891 CG LEU A 128 4167 2838 2613 −13 88 −245 C ATOM 892 CD1 LEU A 128 −24.029 −0.823 17.921 1.00 29.58 C ANISOU 892 CD1 LEU A 128 4757 3555 2926 −46 66 −64 C ATOM 893 CD2 LEU A 128 −26.332 −0.928 16.881 1.00 30.47 C ANISOU 893 CD2 LEU A 128 4623 4166 2786 563 −133 −25 C ATOM 894 N ALA A 129 −28.110 −2.354 21.936 1.00 39.39 N ANISOU 894 N ALA A 129 5889 4067 5009 −75 1006 1586 N ATOM 895 CA ALA A 129 −28.617 −3.302 22.925 1.00 45.02 C ANISOU 895 CA ALA A 129 6382 5149 5573 81 1339 1287 C ATOM 896 C ALA A 129 −29.217 −2.550 24.109 1.00 47.61 C ANISOU 896 C ALA A 129 7091 5023 5976 −1056 2079 1526 C ATOM 897 O ALA A 129 −28.877 −1.393 24.334 1.00 50.07 O ANISOU 897 O ALA A 129 7454 5518 6050 −1216 2171 1360 O ATOM 898 CB ALA A 129 −27.500 −4.215 23.394 1.00 46.58 C ANISOU 898 CB ALA A 129 6533 5557 5608 790 693 916 C ATOM 899 O PRO A 130 −31.975 −5.426 22.814 1.00 58.16 O ANISOU 899 O PRO A 130 9589 4988 7521 −1059 1676 −700 O ATOM 900 N PRO A 130 −30.127 −3.187 24.870 1.00 52.97 N ANISOU 900 N PRO A 130 7755 6077 6294 −1043 2279 1376 N ATOM 901 CA PRO A 130 −30.751 −4.501 24.659 1.00 54.02 C ANISOU 901 CA PRO A 130 8326 5681 6519 −793 2163 1694 C ATOM 902 C PRO A 130 −31.774 −4.442 23.525 1.00 58.13 C ANISOU 902 C PRO A 130 8882 6003 7202 −388 1678 266 C ATOM 903 CB PRO A 130 −31.454 −4.770 25.994 1.00 55.97 C ANISOU 903 CB PRO A 130 8309 6714 6242 −233 2603 2153 C ATOM 904 CG PRO A 130 −31.716 −3.407 26.554 1.00 55.32 C ANISOU 904 CG PRO A 130 7997 7025 5998 −482 3053 2247 C ATOM 905 CD PRO A 130 −30.534 −2.585 26.153 1.00 56.05 C ANISOU 905 CD PRO A 130 8015 6969 6310 −691 2524 1488 C ATOM 906 O LYS A 131 −32.225 −1.083 21.638 1.00 53.26 O ANISOU 906 O LYS A 131 7211 6036 6988 −1277 1642 719 O ATOM 907 N LYS A 131 −32.408 −3.286 23.360 1.00 58.14 N ANISOU 907 N LYS A 131 8041 6758 7291 −26 1292 353 N ATOM 908 CA LYS A 131 −33.371 −3.084 22.292 1.00 55.65 C ANISOU 908 CA LYS A 131 7022 6953 7171 −240 1321 445 C ATOM 909 C LYS A 131 −32.764 −2.133 21.279 1.00 51.15 C ANISOU 909 C LYS A 131 6744 5717 6973 −589 1260 252 C ATOM 910 CB LYS A 131 −34.670 −2.498 22.848 1.00 57.23 C ANISOU 910 CB LYS A 131 6610 7844 7290 −149 1166 209 C ATOM 911 N VAL A 132 −32.830 −2.501 20.006 1.00 40.79 N ANISOU 911 N VAL A 132 5203 3596 6701 −1585 1163 −67 N ATOM 912 CA VAL A 132 −32.317 −1.621 18.981 1.00 37.12 C ANISOU 912 CA VAL A 132 4764 2788 6552 −1002 756 −133 C ATOM 913 C VAL A 132 −33.320 −0.516 18.763 1.00 38.89 C ANISOU 913 C VAL A 132 4436 3429 6910 −1212 628 33 C ATOM 914 O VAL A 132 −34.480 −0.768 18.473 1.00 41.35 O ANISOU 914 O VAL A 132 4698 3917 7096 −1001 409 −245 O ATOM 915 CB VAL A 132 −32.025 −2.372 17.695 1.00 37.20 C ANISOU 915 CB VAL A 132 4556 3156 6421 −1074 845 220 C ATOM 916 CG1 VAL A 132 −31.490 −1.421 16.657 1.00 40.18 C ANISOU 916 CG1 VAL A 132 4267 4807 6192 −1019 938 592 C ATOM 917 CG2 VAL A 132 −31.042 −3.488 17.975 1.00 38.97 C ANISOU 917 CG2 VAL A 132 4858 3617 6334 −244 731 −674 C ATOM 918 N AGLN A 133 −32.866 0.712 18.932 0.57 36.67 N ANISOU 918 N AGLN A 133 4276 2779 6877 −882 1224 287 N ATOM 919 C AGLN A 133 −32.869 3.051 18.267 0.57 35.25 C ANISOU 919 C AGLN A 133 3895 2804 6695 −519 842 −196 C ATOM 920 O AGLN A 133 −31.672 3.115 18.576 0.57 31.91 O ANISOU 920 O AGLN A 133 3376 2180 6569 −290 1780 −88 O ATOM 921 CA AGLN A 133 −33.709 1.867 18.676 0.57 39.15 C ANISOU 921 CA AGLN A 133 4417 3492 6967 −647 1210 218 C ATOM 922 CB AGLN A 133 −34.528 2.228 19.907 0.57 42.37 C ANISOU 922 CB AGLN A 133 5048 3932 7118 −1063 1864 671 C ATOM 923 CG AGLN A 133 −33.711 2.526 21.140 0.57 44.27 C ANISOU 923 CG AGLN A 133 5475 4046 7297 −1184 2221 777 C ATOM 924 CD AGLN A 133 −34.593 2.758 22.350 0.57 50.66 C ANISOU 924 CD AGLN A 133 6319 5437 7492 −495 2498 616 C ATOM 925 OE1 AGLN A 133 −35.753 3.146 22.211 0.57 53.00 O ANISOU 925 OE1 AGLN A 133 6654 5903 7579 38 2804 382 O ATOM 926 NE2 AGLN A 133 −34.055 2.508 23.541 0.57 52.31 N ANISOU 926 NE2 AGLN A 133 6680 5778 7418 −349 2559 744 N ATOM 927 N BGLN A 133 −32.871 0.721 18.930 0.43 39.44 N ANISOU 927 N BGLN A 133 4607 3384 6993 −681 767 68 N ATOM 928 C BGLN A 133 −32.931 3.130 18.406 0.43 38.26 C ANISOU 928 C BGLN A 133 4343 3358 6834 −461 155 −235 C ATOM 929 O BGLN A 133 −31.807 3.308 18.880 0.43 38.96 O ANISOU 929 O BGLN A 133 4650 3298 6857 71 138 −37 O ATOM 930 CA BGLN A 133 −33.736 1.888 18.769 0.43 42.20 C ANISOU 930 CA BGLN A 133 4877 4053 7102 −322 644 −21 C ATOM 931 CB BGLN A 133 −34.542 2.142 20.045 0.43 47.47 C ANISOU 931 CB BGLN A 133 5710 4986 7340 −23 1096 59 C ATOM 932 CG BGLN A 133 −35.879 1.407 20.097 0.43 50.82 C ANISOU 932 CG BGLN A 133 6207 5567 7535 53 1489 79 C ATOM 933 CD BGLN A 133 −36.420 1.276 21.505 0.43 53.36 C ANISOU 933 CD BGLN A 133 6601 6038 7635 −66 1892 261 C ATOM 934 OE1 BGLN A 133 −35.849 1.816 22.452 0.43 54.60 O ANISOU 934 OE1 BGLN A 133 6745 6345 7658 208 2223 567 O ATOM 935 NE2 BGLN A 133 −37.523 0.550 21.652 0.43 55.35 N ANISOU 935 NE2 BGLN A 133 6841 6460 7729 −86 1819 24 N ATOM 936 N ILE A 134 −33.504 3.978 17.552 1.00 35.40 N ANISOU 936 N ILE A 134 3349 3611 6491 −583 −106 −910 N ATOM 937 C ILE A 134 −33.613 6.410 17.820 1.00 30.98 C ANISOU 937 C ILE A 134 2294 3924 5551 −178 341 −304 C ATOM 938 O ILE A 134 −34.846 6.473 17.819 1.00 32.63 O ANISOU 938 O ILE A 134 2501 3638 6258 −262 79 −693 O ATOM 939 CA AILE A 134 −32.875 5.234 17.194 0.68 34.85 C ANISOU 939 CA AILE A 134 3516 3823 5902 448 151 −865 C ATOM 940 CB AILE A 134 −32.704 5.418 15.648 0.68 37.88 C ANISOU 940 CB AILE A 134 3748 4645 6000 −417 −218 −447 C ATOM 941 CG1 AILE A 134 −31.927 6.709 15.348 0.68 39.75 C ANISOU 941 CG1 AILE A 134 4153 5038 5913 600 −109 −476 C ATOM 942 CG2 AILE A 134 −34.046 5.375 14.924 0.68 40.75 C ANISOU 942 CG2 AILE A 134 3975 5387 6121 −861 −445 −310 C ATOM 943 CA BILE A 134 −32.879 5.233 17.187 0.32 35.26 C ANISOU 943 CA BILE A 134 3339 4032 6026 184 −4 −733 C ATOM 944 CB BILE A 134 −32.760 5.408 15.643 0.32 38.10 C ANISOU 944 CB BILE A 134 3678 4648 6149 −72 −404 −621 C ATOM 945 CG1 BILE A 134 −32.110 6.754 15.301 0.32 40.22 C ANISOU 945 CG1 BILE A 134 4090 5057 6135 734 −370 −550 C ATOM 946 CG2 BILE A 134 −34.114 5.246 14.962 0.32 39.37 C ANISOU 946 CG2 BILE A 134 3826 4906 6226 −498 −624 −652 C ATOM 947 N LYS A 135 −32.845 7.328 18.382 1.00 26.14 N ANISOU 947 N LYS A 135 2711 3294 3926 −126 215 −318 N ATOM 948 CA LYS A 135 −33.411 8.562 18.892 1.00 24.68 C ANISOU 948 CA LYS A 135 3001 2979 3397 84 1008 32 C ATOM 949 C LYS A 135 −32.685 9.739 18.266 1.00 21.47 C ANISOU 949 C LYS A 135 2178 3288 2691 −290 820 252 C ATOM 950 O LYS A 135 −31.451 9.807 18.273 1.00 22.71 O ANISOU 950 O LYS A 135 2266 3535 2827 131 432 381 O ATOM 951 CB LYS A 135 −33.316 8.607 20.405 1.00 28.39 C ANISOU 951 CB LYS A 135 4369 2783 3635 −212 1253 49 C ATOM 952 CG LYS A 135 −34.219 7.555 21.038 1.00 33.42 C ANISOU 952 CG LYS A 135 5709 2756 4233 −385 1258 336 C ATOM 953 CD LYS A 135 −34.517 7.852 22.465 1.00 38.61 C ANISOU 953 CD LYS A 135 6454 3325 4891 −534 1238 −352 C ATOM 954 CE LYS A 135 −35.348 6.754 23.117 1.00 42.65 C ANISOU 954 CE LYS A 135 6800 4003 5403 −1287 528 −101 C ATOM 955 NZ LYS A 135 −36.471 6.331 22.237 1.00 48.04 N ANISOU 955 NZ LYS A 135 7318 5307 5628 −1522 511 −62 N ATOM 956 N GLU A 136 −33.462 10.652 17.695 1.00 23.35 N ANISOU 956 N GLU A 136 2991 2826 3053 197 385 578 N ATOM 957 C GLU A 136 −32.906 13.034 17.760 1.00 19.67 C ANISOU 957 C GLU A 136 2080 2737 2657 137 103 279 C ATOM 958 O GLU A 136 −33.805 13.251 18.574 1.00 21.83 O ANISOU 958 O GLU A 136 2419 3222 2653 161 571 314 O ATOM 959 CG GLU A 136 −33.689 10.893 14.658 1.00 31.99 C ANISOU 959 CG GLU A 136 4476 4059 3618 −668 −265 −348 C ATOM 960 CD GLU A 136 −34.524 11.190 13.402 1.00 47.16 C ANISOU 960 CD GLU A 136 6277 6971 4669 −88 138 −1110 C ATOM 961 OE1 GLU A 136 −35.431 12.063 13.467 1.00 50.70 O ANISOU 961 OE1 GLU A 136 6225 8062 4976 −713 −80 −1367 O ATOM 962 OE2 GLU A 136 −34.258 10.562 12.340 1.00 53.59 O ANISOU 962 OE2 GLU A 136 7551 7600 5212 716 362 −1417 O ATOM 963 CA AGLU A 136 −32.917 11.772 16.948 0.69 21.12 C ANISOU 963 CA AGLU A 136 3045 2312 2666 70 18 486 C ATOM 964 CB AGLU A 136 −33.740 12.028 15.672 0.69 25.77 C ANISOU 964 CB AGLU A 136 3767 3151 2875 −18 −244 −72 C ATOM 965 CA BGLU A 136 −32.915 11.768 16.942 0.31 22.97 C ANISOU 965 CA BGLU A 136 2977 2834 2917 −0 114 290 C ATOM 966 CB BGLU A 136 −33.739 12.020 15.671 0.31 27.38 C ANISOU 966 CB BGLU A 136 3759 3459 3184 −182 −117 −98 C ATOM 967 N SER A 137 −31.903 13.876 17.520 1.00 18.53 N ANISOU 967 N SER A 137 2157 2736 2147 −146 57 275 N ATOM 968 CA SER A 137 −31.894 15.241 18.028 1.00 17.46 C ANISOU 968 CA SER A 137 1863 2622 2149 159 −2 400 C ATOM 969 C SER A 137 −32.933 16.055 17.267 1.00 16.92 C ANISOU 969 C SER A 137 1849 2709 1870 397 416 289 C ATOM 970 O SER A 137 −33.534 15.580 16.290 1.00 20.16 O ANISOU 970 O SER A 137 2638 3004 2018 131 −138 235 O ATOM 971 CB SER A 137 −30.514 15.894 17.838 1.00 16.92 C ANISOU 971 CB SER A 137 2290 2353 1784 −490 238 202 C ATOM 972 OG SER A 137 −30.254 16.113 16.431 1.00 17.57 O ANISOU 972 OG SER A 137 2494 2424 1757 −31 353 32 O ATOM 973 N LEU A 138 −33.172 17.271 17.739 1.00 18.35 N ANISOU 973 N LEU A 138 2290 2564 2116 515 272 621 N ATOM 974 CA LEU A 138 −33.828 18.251 16.914 1.00 18.04 C ANISOU 974 CA LEU A 138 2178 2637 2038 176 20 313 C ATOM 975 C LEU A 138 −32.914 18.642 15.747 1.00 19.17 C ANISOU 975 C LEU A 138 2523 2480 2280 528 579 785 C ATOM 976 O LEU A 138 −31.705 18.434 15.790 1.00 19.07 O ANISOU 976 O LEU A 138 2245 2967 2036 426 381 312 O ATOM 977 CB LEU A 138 −34.196 19.465 17.730 1.00 19.59 C ANISOU 977 CB LEU A 138 2591 3074 1780 302 355 −25 C ATOM 978 CG LEU A 138 −35.195 19.212 18.866 1.00 20.19 C ANISOU 978 CG LEU A 138 2813 2946 1912 245 387 −11 C ATOM 979 CD1 LEU A 138 −35.592 20.544 19.485 1.00 26.06 C ANISOU 979 CD1 LEU A 138 3684 4248 1970 1112 267 −273 C ATOM 980 CD2 LEU A 138 −36.419 18.476 18.367 1.00 23.97 C ANISOU 980 CD2 LEU A 138 2422 4374 2313 401 261 461 C ATOM 981 N ARG A 139 −33.483 19.218 14.708 1.00 19.80 N ANISOU 981 N ARG A 139 2752 2550 2223 277 521 523 N ATOM 982 CA ARG A 139 −32.644 19.650 13.588 1.00 20.06 C ANISOU 982 CA ARG A 139 2831 2913 1878 −152 293 367 C ATOM 983 C ARG A 139 −31.837 20.911 13.925 1.00 20.13 C ANISOU 983 C ARG A 139 3273 2290 2087 23 633 −40 C ATOM 984 O ARG A 139 −32.163 21.662 14.850 1.00 23.90 O ANISOU 984 O ARG A 139 3342 3477 2260 86 854 −51 O ATOM 985 CB ARG A 139 −33.507 19.924 12.370 1.00 21.52 C ANISOU 985 CB ARG A 139 3053 3147 1976 −344 153 −71 C ATOM 986 CG ARG A 139 −34.110 18.684 11.839 1.00 24.33 C ANISOU 986 CG ARG A 139 2966 3883 2397 −538 256 188 C ATOM 987 CD ARG A 139 −34.509 18.902 10.447 1.00 29.17 C ANISOU 987 CD ARG A 139 3901 3995 3188 −1108 453 134 C ATOM 988 NE ARG A 139 −35.479 17.914 10.030 1.00 28.32 N ANISOU 988 NE ARG A 139 2642 4736 3380 −476 559 −548 N ATOM 989 CZ ARG A 139 −36.055 17.941 8.832 1.00 36.30 C ANISOU 989 CZ ARG A 139 3771 5894 4128 650 −37 −1418 C ATOM 990 NH1 ARG A 139 −35.687 18.866 7.943 1.00 33.63 N ANISOU 990 NH1 ARG A 139 3087 5737 3955 498 −139 −1344 N ATOM 991 NH2 ARG A 139 −36.967 17.037 8.516 1.00 36.48 N ANISOU 991 NH2 ARG A 139 3088 5936 4838 −687 164 −1380 N ATOM 992 O ALA A 140 −29.878 21.986 10.818 1.00 21.57 O ANISOU 992 O ALA A 140 3842 2652 1699 −483 500 −200 O ATOM 993 N ALA A 140 −30.737 21.106 13.216 1.00 20.72 N ANISOU 993 N ALA A 140 3539 2563 1771 −190 850 463 N ATOM 994 CA ALA A 140 −30.049 22.393 13.202 1.00 20.38 C ANISOU 994 CA ALA A 140 3678 2583 1482 −461 536 373 C ATOM 995 C ALA A 140 −29.896 22.818 11.744 1.00 20.49 C ANISOU 995 C ALA A 140 3429 2891 1465 −588 534 108 C ATOM 996 CB ALA A 140 −28.687 22.287 13.876 1.00 24.02 C ANISOU 996 CB ALA A 140 3761 3710 1654 −424 −54 139 C ATOM 997 N GLU A 141 −29.788 24.114 11.535 1.00 19.80 N ANISOU 997 N GLU A 141 3092 3005 1425 −56 194 55 N ATOM 998 CA GLU A 141 −29.666 24.651 10.179 1.00 17.45 C ANISOU 998 CA GLU A 141 2487 2728 1416 −40 185 83 C ATOM 999 C GLU A 141 −28.270 25.175 9.950 1.00 18.20 C ANISOU 999 C GLU A 141 2746 2916 1252 273 −84 −213 C ATOM 1000 O GLU A 141 −27.708 25.887 10.793 1.00 20.22 O ANISOU 1000 O GLU A 141 2999 3297 1386 2 205 60 O ATOM 1001 CB GLU A 141 −30.640 25.818 10.000 1.00 18.96 C ANISOU 1001 CB GLU A 141 2515 2785 1905 −114 387 163 C ATOM 1002 CG GLU A 141 −30.542 26.399 8.583 1.00 20.36 C ANISOU 1002 CG GLU A 141 2437 3058 2242 59 124 455 C ATOM 1003 CD GLU A 141 −31.480 27.549 8.318 1.00 25.04 C ANISOU 1003 CD GLU A 141 2830 3962 2722 283 261 507 C ATOM 1004 OE1 GLU A 141 −32.339 27.854 9.197 1.00 30.41 O ANISOU 1004 OE1 GLU A 141 3420 4737 3396 651 470 −34 O ATOM 1005 OE2 GLU A 141 −31.355 28.152 7.203 1.00 28.36 O ANISOU 1005 OE2 GLU A 141 3788 3932 3057 622 339 760 O ATOM 1006 N LEU A 142 −27.723 24.838 8.779 1.00 17.25 N ANISOU 1006 N LEU A 142 2428 2903 1224 −28 8 20 N ATOM 1007 CA LEU A 142 −26.477 25.425 8.309 1.00 17.05 C ANISOU 1007 CA LEU A 142 2050 2819 1609 −3 150 187 C ATOM 1008 C LEU A 142 −26.850 26.402 7.199 1.00 17.92 C ANISOU 1008 C LEU A 142 2317 3003 1489 −45 −177 187 C ATOM 1009 O LEU A 142 −27.535 26.028 6.236 1.00 18.25 O ANISOU 1009 O LEU A 142 2423 3093 1417 −12 −204 76 O ATOM 1010 CB LEU A 142 −25.520 24.366 7.721 1.00 17.75 C ANISOU 1010 CB LEU A 142 2189 2903 1652 274 278 224 C ATOM 1011 CG LEU A 142 −24.203 24.876 7.162 1.00 19.28 C ANISOU 1011 CG LEU A 142 2133 3338 1853 341 −77 −68 C ATOM 1012 CD1 LEU A 142 −23.364 25.550 8.276 1.00 21.27 C ANISOU 1012 CD1 LEU A 142 2296 3665 2121 −352 −75 −323 C ATOM 1013 CD2 LEU A 142 −23.431 23.706 6.578 1.00 21.29 C ANISOU 1013 CD2 LEU A 142 2604 3900 1587 701 201 137 C ATOM 1014 N ARG A 143 −26.389 27.641 7.317 1.00 20.55 N ANISOU 1014 N ARG A 143 2698 3139 1972 182 −273 545 N ATOM 1015 C ARG A 143 −25.145 29.038 5.782 1.00 20.92 C ANISOU 1015 C ARG A 143 2770 3069 2111 −89 −273 655 C ATOM 1016 O ARG A 143 −24.344 29.518 6.553 1.00 24.40 O ANISOU 1016 O ARG A 143 3181 3810 2281 −673 −356 244 O ATOM 1017 NE AARG A 143 −29.995 31.156 7.319 0.69 30.85 N ANISOU 1017 NE AARG A 143 2933 4351 4438 846 −382 −3 N ATOM 1018 CZ AARG A 143 −30.815 31.764 8.171 0.69 31.56 C ANISOU 1018 CZ AARG A 143 3699 3581 4713 967 −552 −151 C ATOM 1019 NH1 AARG A 143 −30.637 33.043 8.479 0.69 33.62 N ANISOU 1019 NH1 AARG A 143 4960 2737 5075 1080 −393 −97 N ATOM 1020 NH2 AARG A 143 −31.832 31.096 8.713 0.69 31.37 N ANISOU 1020 NH2 AARG A 143 3013 4083 4824 500 −391 −477 N ATOM 1021 CA AARG A 143 −26.553 28.643 6.270 0.69 21.57 C ANISOU 1021 CA AARG A 143 2407 3379 2410 −139 −321 135 C ATOM 1022 CB AARG A 143 −27.307 29.837 6.872 0.69 29.36 C ANISOU 1022 CB AARG A 143 3895 4148 3112 897 −360 −316 C ATOM 1023 CG AARG A 143 −27.972 30.786 5.904 0.69 30.72 C ANISOU 1023 CG AARG A 143 3611 4398 3664 412 −422 −299 C ATOM 1024 CD AARG A 143 −28.854 31.796 6.660 0.69 30.46 C ANISOU 1024 CD AARG A 143 3105 4349 4119 86 −230 180 C ATOM 1025 NE CARG A 143 −30.663 30.715 7.848 0.31 20.97 N ANISOU 1025 NE CARG A 143 2566 3151 2251 −254 −644 172 N ATOM 1026 CZ CARG A 143 −31.351 31.490 8.681 0.31 27.40 C ANISOU 1026 CZ CARG A 143 4013 3541 2855 810 −474 −120 C ATOM 1027 NH1 CARG A 143 −30.839 32.633 9.124 0.31 29.22 N ANISOU 1027 NH1 CARG A 143 5046 3171 2886 1020 −304 −41 N ATOM 1028 NH2 CARG A 143 −32.555 31.110 9.086 0.31 28.81 N ANISOU 1028 NH2 CARG A 143 3897 3792 3258 901 −412 −397 N ATOM 1029 CA CARG A 143 −26.519 28.633 6.242 0.31 20.29 C ANISOU 1029 CA CARG A 143 2537 3077 2097 465 −114 353 C ATOM 1030 CB CARG A 143 −27.229 29.889 6.718 0.31 22.01 C ANISOU 1030 CB CARG A 143 3063 3108 2192 1484 185 −60 C ATOM 1031 CG CARG A 143 −28.685 29.718 6.887 0.31 19.17 C ANISOU 1031 CG CARG A 143 2125 3077 2080 1098 162 148 C ATOM 1032 CD CARG A 143 −29.329 31.003 7.345 0.31 21.56 C ANISOU 1032 CD CARG A 143 2765 3212 2216 962 −641 229 C ATOM 1033 N VAL A 144 −24.856 28.813 4.510 1.00 21.88 N ANISOU 1033 N VAL A 144 3090 3346 1878 34 −90 738 N ATOM 1034 CA VAL A 144 −23.532 29.112 3.969 1.00 23.28 C ANISOU 1034 CA VAL A 144 3527 3129 2190 264 105 541 C ATOM 1035 C VAL A 144 −23.701 30.284 3.029 1.00 26.54 C ANISOU 1035 C VAL A 144 3981 3196 2907 −54 −637 803 C ATOM 1036 O VAL A 144 −24.371 30.151 1.992 1.00 29.52 O ANISOU 1036 O VAL A 144 4547 3893 2776 −172 −996 849 O ATOM 1037 CB VAL A 144 −22.907 27.892 3.234 1.00 23.48 C ANISOU 1037 CB VAL A 144 3236 3542 2145 −559 −121 429 C ATOM 1038 CG1 VAL A 144 −21.504 28.239 2.773 1.00 26.07 C ANISOU 1038 CG1 VAL A 144 3304 4245 2355 −565 415 374 C ATOM 1039 CG2 VAL A 144 −22.856 26.660 4.153 1.00 22.88 C ANISOU 1039 CG2 VAL A 144 3579 3353 1760 −117 −111 317 C ATOM 1040 N THR A 145 −23.087 31.409 3.391 1.00 28.09 N ANISOU 1040 N THR A 145 3919 2960 3793 −182 −570 1683 N ATOM 1041 CA THR A 145 −23.256 32.681 2.691 1.00 33.03 C ANISOU 1041 CA THR A 145 4297 3816 4436 −421 −291 1965 C ATOM 1042 C THR A 145 −22.169 32.932 1.643 1.00 34.34 C ANISOU 1042 C THR A 145 4694 3753 4599 −398 −357 2439 C ATOM 1043 O THR A 145 −21.069 32.371 1.705 1.00 35.97 O ANISOU 1043 O THR A 145 4824 4201 4640 −28 −1138 2306 O ATOM 1044 CB THR A 145 −23.298 33.869 3.684 1.00 39.34 C ANISOU 1044 CB THR A 145 5615 4258 5072 929 557 1765 C ATOM 1045 OG1 THR A 145 −22.067 33.952 4.418 1.00 45.47 O ANISOU 1045 OG1 THR A 145 6704 5069 5502 2029 253 1472 O ATOM 1046 CG2 THR A 145 −24.447 33.694 4.671 1.00 42.22 C ANISOU 1046 CG2 THR A 145 6522 4211 5308 1062 1015 1722 C ATOM 1047 O GLU A 146 −20.501 35.700 1.021 1.00 44.40 O ANISOU 1047 O GLU A 146 5976 4884 6011 −564 264 1951 O ATOM 1048 N GLU A 146 −22.476 33.813 0.697 1.00 39.17 N ANISOU 1048 N GLU A 146 4997 4905 4980 161 −113 2870 N ATOM 1049 CA GLU A 146 −21.570 34.106 −0.406 1.00 44.14 C ANISOU 1049 CA GLU A 146 5590 6091 5091 8 475 3151 C ATOM 1050 C GLU A 146 −20.372 34.889 0.104 1.00 45.57 C ANISOU 1050 C GLU A 146 5795 5759 5761 −390 414 2913 C ATOM 1051 CB GLU A 146 −22.306 34.911 −1.483 1.00 47.51 C ANISOU 1051 CB GLU A 146 6071 7138 4841 307 517 3122 C ATOM 1052 O ARG A 147 −18.730 37.060 −1.694 1.00 54.70 O ANISOU 1052 O ARG A 147 6744 6771 7270 −518 244 2924 O ATOM 1053 N ARG A 147 −19.204 34.634 −0.478 1.00 47.61 N ANISOU 1053 N ARG A 147 5793 5843 6454 −1135 292 3100 N ATOM 1054 CA ARG A 147 −17.999 35.381 −0.129 1.00 52.50 C ANISOU 1054 CA ARG A 147 6324 6550 7072 −725 236 2577 C ATOM 1055 C ARG A 147 −18.043 36.799 −0.704 1.00 53.81 C ANISOU 1055 C ARG A 147 6575 6666 7205 −494 135 2875 C ATOM 1056 CB ARG A 147 −16.741 34.649 −0.615 1.00 54.71 C ANISOU 1056 CB ARG A 147 6524 6912 7350 −466 422 2352 C TER HETATM 1057 CL CL B 1 −31.532 18.967 19.982 0.00 22.75 Cl HETATM 1058 CL A CL B 2 −14.013 7.942 15.373 0.41 43.02 Cl HETATM 1059 CL B CL B 2 −13.877 5.390 15.959 0.59 36.08 Cl TER HETATM 1060 O HOH S 1 −11.320 12.933 29.488 1.00 24.25 O HETATM 1061 O HOH S 2 −29.963 27.082 5.173 1.00 26.06 O HETATM 1062 O HOH S 3 −36.398 19.602 14.615 1.00 26.46 O HETATM 1063 O HOH S 4 −25.179 19.890 21.690 1.00 31.16 O HETATM 1064 O HOH S 5 −20.377 23.391 17.674 1.00 27.55 O HETATM 1065 O HOH S 6 −32.642 16.478 21.774 1.00 29.02 O HETATM 1066 O HOH S 7 −20.800 −0.588 11.468 1.00 28.91 O HETATM 1067 O HOH S 8 −21.210 9.475 24.802 1.00 31.01 O HETATM 1068 O HOH S 9 −23.269 4.299 10.683 1.00 32.96 O HETATM 1069 O HOH S 10 −15.168 16.008 13.610 1.00 30.12 O HETATM 1070 O HOH S 11 −23.000 19.897 −0.770 1.00 32.33 O HETATM 1071 O HOH S 12 −16.053 8.925 14.002 1.00 28.30 O HETATM 1072 O HOH S 13 −31.058 21.412 17.451 1.00 34.49 O HETATM 1073 O HOH S 14 −11.148 17.070 13.522 1.00 35.55 O HETATM 1074 O HOH S 15 −13.606 9.894 17.437 1.00 33.67 O HETATM 1075 O HOH S 16 −17.334 0.330 13.286 1.00 29.83 O HETATM 1076 O HOH S 17 −23.530 18.918 3.248 1.00 32.42 O HETATM 1077 O HOH S 18 −25.398 3.755 25.094 1.00 37.41 O HETATM 1078 O HOH S 19 −12.444 24.646 5.144 1.00 32.56 O HETATM 1079 O HOH S 20 −23.990 −3.579 24.355 1.00 38.71 O HETATM 1080 O HOH S 21 −28.227 12.362 25.591 1.00 36.43 O HETATM 1081 O HOH S 22 −35.754 15.422 14.773 1.00 40.39 O HETATM 1082 O HOH S 23 −15.728 24.696 12.356 1.00 32.84 O HETATM 1083 O HOH S 24 −24.219 16.690 1.736 1.00 32.43 O HETATM 1084 O HOH S 25 −15.646 10.746 10.757 1.00 38.67 O HETATM 1085 O HOH S 26 −14.652 17.508 8.417 1.00 33.75 O HETATM 1086 O HOH S 27 −17.545 8.522 9.523 1.00 33.84 O HETATM 1087 O AHOH S 28 −12.876 17.475 17.095 0.54 26.63 O HETATM 1088 O BHOH S 28 −11.123 14.550 14.203 0.46 25.57 O HETATM 1089 O HOH S 29 −11.145 14.343 20.129 1.00 30.72 O HETATM 1090 O HOH S 30 −13.826 17.975 13.783 1.00 36.95 O HETATM 1091 O HOH S 31 −28.657 26.959 19.793 1.00 39.40 O HETATM 1092 O HOH S 32 −14.087 2.338 14.701 1.00 42.49 O HETATM 1093 O HOH S 33 −16.594 28.407 10.975 1.00 41.30 O HETATM 1094 O HOH S 34 −36.440 10.244 17.770 1.00 48.54 O HETATM 1095 O HOH S 35 −19.238 26.131 15.375 1.00 35.22 O HETATM 1096 O HOH S 36 −24.391 30.001 15.634 1.00 45.39 O HETATM 1097 O HOH S 37 −10.294 23.547 5.439 1.00 33.79 O HETATM 1098 O HOH S 38 −20.262 11.381 3.588 1.00 40.36 O HETATM 1099 O HOH S 39 −9.566 21.361 3.724 1.00 45.76 O HETATM 1100 O HOH S 40 −31.839 14.557 25.618 1.00 39.31 O HETATM 1101 O HOH S 41 −28.573 29.123 17.160 1.00 34.87 O HETATM 1102 O HOH S 42 −17.837 21.890 21.041 1.00 39.71 O HETATM 1103 O HOH S 43 −23.508 31.272 13.390 1.00 38.35 O HETATM 1104 O HOH S 44 −14.232 23.031 15.160 1.00 45.86 O HETATM 1105 O HOH S 45 −32.842 28.036 11.832 1.00 37.47 O HETATM 1106 O HOH S 46 −20.017 0.581 13.613 1.00 26.90 O HETATM 1107 O HOH S 47 −30.924 26.051 2.727 1.00 33.41 O HETATM 1108 O HOH S 48 −17.972 6.069 9.248 1.00 44.79 O HETATM 1109 O HOH S 49 −31.615 24.043 1.750 1.00 39.50 O HETATM 1110 O HOH S 50 −32.977 22.499 3.078 1.00 43.12 O HETATM 1111 O HOH S 51 −37.283 19.091 5.781 1.00 50.59 O HETATM 1112 O HOH S 52 −16.505 25.687 16.469 1.00 47.70 O HETATM 1113 O HOH S 53 −17.987 10.202 6.094 1.00 44.99 O HETATM 1114 O HOH S 54 −25.817 27.114 21.137 1.00 54.54 O HETATM 1115 O HOH S 55 −19.634 31.262 12.044 1.00 51.44 O HETATM 1116 O HOH S 56 −19.282 3.533 5.922 1.00 44.19 O HETATM 1117 O HOH S 57 −18.140 26.304 12.964 1.00 28.65 O HETATM 1118 O HOH S 58 −20.503 16.347 −0.676 1.00 39.93 O HETATM 1119 O HOH S 59 −20.668 28.377 16.271 1.00 54.96 O HETATM 1120 O AHOH S 60 −13.046 27.984 9.370 0.58 25.01 O HETATM 1121 O BHOH S 60 −17.607 32.024 8.445 0.42 30.47 O HETATM 1122 O HOH S 61 −12.651 27.445 −0.487 1.00 44.24 O HETATM 1123 O HOH S 62 −10.636 16.383 18.094 1.00 34.27 O HETATM 1124 O HOH S 63 −19.658 21.740 −5.664 1.00 34.16 O HETATM 1125 O HOH S 64 −21.399 34.434 7.059 1.00 50.31 O HETATM 1126 O HOH S 65 −29.754 22.788 20.357 1.00 47.87 O HETATM 1127 O HOH S 66 −29.614 29.358 3.092 1.00 46.67 O HETATM 1128 O HOH S 67 −9.725 11.812 27.805 1.00 45.85 O HETATM 1129 O HOH S 68 −32.790 9.593 10.674 1.00 54.56 O HETATM 1130 O HOH S 69 −27.077 26.307 −5.229 1.00 51.00 O HETATM 1131 O HOH S 70 −20.474 3.201 12.726 1.00 34.09 O HETATM 1132 O HOH S 71 −34.490 8.897 10.790 1.00 57.99 O HETATM 1133 O HOH S 72 −21.449 2.801 11.173 1.00 50.05 O HETATM 1134 O HOH S 73 −11.337 14.501 2.400 1.00 50.53 O HETATM 1135 O HOH S 74 −32.632 25.721 13.366 1.00 31.98 O HETATM 1136 O HOH S 75 −24.586 8.104 30.871 1.00 45.09 O HETATM 1137 O HOH S 76 −27.903 7.346 4.005 1.00 41.45 O HETATM 1138 O HOH S 77 −34.626 12.432 27.946 1.00 48.67 O HETATM 1139 O HOH S 78 −36.301 15.543 11.735 1.00 43.02 O HETATM 1140 O HOH S 79 −28.138 14.618 25.444 1.00 51.79 O HETATM 1141 O HOH S 80 −22.311 31.191 −7.395 1.00 60.17 O HETATM 1142 O HOH S 81 −34.346 −5.046 19.179 1.00 53.46 O HETATM 1143 O HOH S 82 −22.182 24.418 19.827 1.00 48.28 O TER END

Claims

1. An in silico method of identifying a compound that binds to PD-L2 binding pocket of human PD-1, the method comprising:

(a) receiving, by a computer system, information on a three-dimensional structure of PD-L2 binding pocket of human PD-1 comprising a plurality of amino acids;
(b) receiving, by the computer system, information on a three-dimensional structure of a candidate compound;
(c) using the computer system and the information received into the computer system in steps (a) and (b), performing one or more of molecular dynamic simulations, kinetic Monte Carlo (KMC) simulations, direct simulations Monte Carlo (DSMC), or density functional theory (DFT) simulations to determine if the candidate compound binds to the PD-L2 binding pocket of human PD-1, thereby identifying the compound that binds to PD-L2 binding pocket of human PD-1.

2. A protein comprising a ligand binding pocket with a three-dimensional structure corresponding to a structure of PD-L2 binding pocket of a variant of human PD-1 with one or more of amino acid substitutions in residues corresponding to N74, T76 or A132 of SEQ ID NO:1.

3. A variant of human PD-1 comprising one or more of amino acid substitutions in residues corresponding to N74, T76 and A132 of SEQ ID NO:1.

Patent History
Publication number: 20210088528
Type: Application
Filed: Apr 28, 2020
Publication Date: Mar 25, 2021
Inventors: Shaogeng Tang (Stanford, CA), Peter S. Kim (Stanford, CA)
Application Number: 16/861,058
Classifications
International Classification: G01N 33/68 (20060101); G16C 20/30 (20060101); G16C 20/64 (20060101);