US20060069019A1

US20060069019A1 - Crystal structure of the complex of hepatocyte growth factor beta chain with Met receptor and methods of use

Info

Publication number: US20060069019A1
Application number: US11/124,607
Authority: US
Inventors: Christian Wiesmann; Jennifer Stamos
Original assignee: Genentech Inc
Current assignee: Genentech Inc
Priority date: 2004-05-06
Filing date: 2005-05-06
Publication date: 2006-03-30
Also published as: WO2005108424A1; US20110012894A1; US7754458B2; US20080293923A1

Abstract

The disclosure provides a crystal structure of a complex of the HGF β-chain with am extracellular fragment of the Met receptor, as well as use of the crystal structure in the design, identification, and selection of ligands that modulate the Met Receptor and the interaction of HGF with the Met receptor.

Description

CROSS REFERENCE TO RELATED APPLICATIONS

This application claims the benefit of 35 U.S.C. § 119(e) to U.S. Ser. No. 60/568,865 filed May 6, 2004, which application is hereby incorporated by reference.

BACKGROUND

The receptor tyrosine kinase Met, and its ligand, hepatocyte growth factor (HGF, also called scatter factor), have been implicated in promoting invasive growth of many tumor types due to inappropriate activation of Met function (Jankowski et al., 2003; Nardone et al., 2003; Trusolino and Comoglio, 2002; Birchmeier et al., 2003). This activation can arise from a variety of sources, but in each case the Met receptor activates signaling cascades that normally function to organize groups of cells into branching, tubular structures that are present in a variety of organs (Montesano et al., 1992; Sonnenberg et al., 1993; Rosen et al., 1994; Trusolino and Comoglio, 2002; Zhang and Vande Woude, 2003). The Met receptor plays a unique role during development as a master switch, which can stimulate proliferation and motility necessary for the full program of growth and scattering of cells. Its role in the invasiveness of many cancers makes it an attractive target for therapeutics (Ma et al., 2003). However, many questions remain about how the ligand, HGF, binds to Met and induces its tyrosine kinase cascade and thus leads to a biological response.
The Met receptor is part of a larger family of growth factor receptors with identical domain architecture that includes the Ron and Sea receptors (Monsin et al., 1992, Huff et al., 1993). The extracellular portions of Met family members are composed of three domain types. The N-terminal 500 residues fold into a Sema domain, which shares sequence homology with domains found in the Semaphorin and plexin families of neural development proteins (Winburg et al., 1998). As reported recently, Sema domains form a 7-bladed β-propeller structure (Antipenkov et al., 2003, Love et al., 2003). Met undergoes proteolytic cleavage within the Sema domain during normal processing, although the role for this remains unclear since cells that are unable to cleave Met show normal levels of Met activation upon ligand binding (Komada et al., 1993). A PSI domain, a small domain spanning about 50 residues and containing 4 disulfide bonds, follows the Sema domain. In addition to the Met receptor family, PSI domains are also found in the plexins, Semaphorins and integrins, hence its name (Bork et al., 1999). In Met, the PSI domain is connected via 4 IPT domains to the transmembrane helix and the kinase domain in the intracellular portion of the receptor. IPT domains are related to immunoglobulin-like domains and are named after their presence in plexins and transcription factors (Takagi et al., 1995).
HGF is a large growth factor of 728 residues that is produced as an inactive single-chain precursor which is proteolytically processed to form the biologically active disulfide-linked α/β-heterodimer (Nakamura et al., 1989; Hartmann et al., 1992; Kataoka et al., 2003). The α-chain folds into an N-terminal domain (N-domain) followed by 4 Kringle domains. The β-chain starts with residue Val495 and is homologous to the protease domain of chymotrypsin like serine proteases, which, like HGF, are activated by a proteolytic cleavage event (Perona and Craig, 1995; Hedstrom 2002). However, no protease activity has been demonstrated for HGF β-chain (Lokker et al., 1992) consistent with the absence of the key serine and histidine residues that are part of the ‘catalytic triad’ Asp[c102]-His[c57]-Ser[c195] ([chymotrypsinogen numbering]) required for catalytic activity in serine proteases.
Comparisons of the biologically active, two-chain HGF, and the inactive single-chain HGF precursor on the Met receptor have shown that both forms of HGF bind Met with similar affinity, but only the cleaved, mature form of HGF is able to activate Met (Lokker et al., 1992). In addition, various C-terminally truncated fragments of the α-chain (termed NK1, NK2, or NK4 depending on the number of Kringle domains retained) bind Met; in many cases they act as potent antagonists of Met receptor function (Cioce et al., 1996; Chan et al., 1991; Date et al., 1997). Studies involving the cross-linking of Met receptors by a variety of specific antibodies to its extracellular domain have demonstrated that simple dimerization of Met is sufficient for activation (Prat et al., 1998). Based on these characteristics, the fundamental mechanism for Met dimerization remains unclear.
Currently, there is no detailed structural information about HGF β-chain complexed with Met receptor. A completely solved crystal structure of the HGF β-chain complexed with Met receptor is needed, for example, for assays for Met-ligand (e.g., HGF β-chain) interaction and function, modeling the structure-function relationship of Met and other molecules, diagnostic assays for mutation-induced pathologies, and rational design of agents useful in modulating Met or HGF activity or activation.

SUMMARY

In some embodiments, the present disclosure provides a crystalline form of hepatocyte growth factor beta chain (HGF β) complexed with Met receptor, and the structural coordinates of the crystal. Coordinates of a crystal structure solved by molecular replacement are listed in Table 2. In some embodiments, HGF β comprises an amino acid sequence of SEQ ID NO: 1 or conservative substitutions thereof and the Met receptor comprises an amino acid sequence of SEQ ID NO:3 or conservative substitutions thereof.
In some embodiments, the disclosure provides a crystal structure of HGF β complexed with Met receptor, as well as use of the crystal structure to model Met receptor activity when complexed with HGF β. This use of the structure includes: modeling the interaction of ligands with the Met receptor; activation and inhibition of Met receptor; and the rational design of modulators of Met receptor activity. For example, these modulators include ligands that interact with Met receptor and modulate Met receptor activities, such as cell migration, HGF β binding to Met, and Met phosphorylation and signaling.
In other embodiments, the amino acid residues that form the binding site for the Met receptor on HGF β are identified and are useful, for example, in methods to model the structure of HGF binding site and to identify agents that can bind or fit into the binding site. In addition, the amino acid positions that form the binding site for HGF β on Met have been identified and are useful, for example, in methods to model the structure of the Met ligand binding site and to identify other agents that can bind or fit into the binding site.

BRIEF DESCRIPTION OF FIGURES

FIG. 1A shows a superposition representation of HGF β-chain (grey) and plasmin. The plasmin α chain is shown as a thin dark line. Selected side-chains of HGF β and plasmin are shown as sticks. They include the residues of the catalytic triad in serine proteases (His[c57], Asp[c102], and Ser[c195]) and the respective residues in the catalytically inactive HGF β-chain (Gln534, Asp578 and Tyr673), the N-terminal Val495 (V495; Val16 in plasmin) and Asp672 (D672; Asp194 in plasmin). After maturation, the N-terminus of Val495 of HGF is inserted into the core of the protein. The N-terminal amine forms a salt bridge with the side-chain of Asp672 and thus rearranges the loops that carry the catalytic triad. The numbering system with a lower case c is that of the chymotyrpsinogen numbering system.
FIG. 1B shows the same superposition of FIG. 1A rotated 180° around the y-axis. The surface of HGF β-chain is grey. Cysteines 561 (C561) and 604 (C604) in HGF β-chain and the Asp598 (D598) are shown. The α-chain of plasmin follows a groove that is also present on the HGF surface. The distance requirements for the formation of the disulfide bond between the α- and the β-chain analogous to plasmin and MSP are not satisfied. The two cysteines on the plasmin α-chain are shown as stick stubs.
FIG. 1C shows the sequence alignment of selected regions of HGF, MSP, and plasmin. (SEQ ID NOs:7-9) The alignment shows the Cys residues that are present in the a and β chain of HGF. The Cys at position 487 in the α chain of HGF is conserved when compared with MSP and plasmin. However, the Cys residues in the β chain of HGF are not at conserved positions, but are found at positions 561 and 604. A disulfide bond between amino acid residues at 487 in the α chain and the cysteine residue at 604 in the β chain may be formed. However, given the location of cysteine 561 in the three-dimensional structure, this residue could also form a disulfide bond with amino acid residue 487 in the α chain. Asterisks indicate amino acid residues that are conserved when the three sequences are compared and dots indicate amino acids that are conservative substitutions.
FIGS. 2A-C show representations of the complex of Met and HGF β-chain. FIGS. 2A and 2B show ribbon representations with HGF β-chain.
FIG. 2A provides a view onto the ‘top’ side of the propeller. The numbers in the center refer to the blades. The β-strands in blade 1 are labeled A, B, C, and D. Disordered residues in the represented model are indicated with dotted lines and the dotted line associated numbers refer to the last and first amino acid residues present in the model.
FIG. 2B provides a side view of the same complex of FIG. 2A. Note that the loops on the top face of the propeller are longer than the ones on the bottom face. All figures were made using Pymol (DeLano, 2002).
FIG. 2C provides a surface representation of the Met Sema domain and an associated HGF β-chain represented as a gray ribbon. The left panel of FIG. 2C captures the complex in the same view as FIG. 2A and shows approximate molecular dimensions. The right panel of FIG. 2C is a view towards the bottom of the propeller and indicates a proteolysis site.
FIG. 3 shows sequence alignment of the Sema domains of human Met receptor (Met_h) (SEQ ID NO:10), human Sema4D (hSema4d) (SEQ ID NO:11), and mouse Sema3A (mSema3a) (SEQ ID NO:12). The secondary structure elements depicted refer to the Met structure. The structural elements identified as A1, B1, C1, etc. refer to β sheets that form the blades 1-7 of the propeller of the human Met receptor. For example, A1, B1, C1 and D1 identify the amino acids that form propellor blade 1 of the Met Sema domain. The amino acids forming other blades of the propeller are also identified. The boxes indicate structural equivalent positions between Met and Sema4D. The coordinates of the Sema3A structure were unavailable. Dots above the amino acid residues indicate these residues contact HGF β. Residues in the dimer interface of Sema4D are shaded. Cysteines engaged in disulfide bonds are marked with letters A to G and those with same letter form a disulfide bond. Residues that are disordered in the represented structure are shown in italics.
FIG. 4A shows a superposition representation of Met and Sema4D. Note the structural similarities within the β-propellers and the differences in the insertions. The topology of the PSI domains in both structures is identical, but the relative orientation in comparison to the Sema domains is rather different.
FIGS. 4B and 4C shows two different views of a model of a potential Met-dimer based on the dimer of Sema4D and the superposition shown in FIG. 4A. The interface between the two molecules forming the Sema4D dimer is large and buries approximately 2,500 Å². If this dimerization interface were present on Met, the respective interface in Met would be much smaller due to the different conformation of the loops that correspond to the loops forming the dimer interface in Sema4D. Also shown are two HGF β molecules. Residues shown as spheres represent Cys604 (C604) and Cys561 (C561), which are potential disulfide partners of Cys487 in the α-chain of HGF.
FIG. 5A shows an open-book surface representation view of the Met-HGF complex interface. Atoms of an amino acid residues of HGF β (shown on the left) that are closer than about 4.7 Å to an atom of an amino acid of Met include Y513, K516, R533, Q534, P537, Y673, E670, Y619, D578, R647, P693, C669, V692, C697, E656, G694, G696, R695, I699, K649, and R702. Atoms of an amino acid residues of Met (shown on the right) closer than about 4.7 Å to an atom of an amino acid residues of HGF β include R218, K220, E221, T222, L229, T230, E167, D190, R191, F192, K223, Y126, D127, D128, H148, S286, and Y125. Contact residues are labeled. HGF is on the left side and Met is on the right side. The three underlined amino acid residue numbers indicate the residues that form the catalytic triad in serine proteases.
FIG. 5B shows differences in binding mode between a HGF:Met complex (left) and a trypsin:BPTI (pdb 2PTC) complex (right). Orientations of HGF and trypsin are similar to the view in FIG. 1. Contact residues of Met are shown as sticks. The numbers refer to Met residues. Contact residues of BPTI are also shown as sticks and the “P” number labels refer to BPTI residues.
FIG. 6 shows a view of the ‘S 1-pocket’ of HGF β. Selected numbered residues that form the ‘S1 pocket’ of HGF are shown as sticks with gray carbons. Glu221 (E221) of Met is shown. The dotted lines indicate potential hydrogen bonds between HGF β and Met amino acid residues.
FIGS. 7A and 7B show two different views of two crystallographically related HGF β-chain:Met complexes that may represent a portion of the active signaling complex. Residues 495:499 of both HGF β-chains are shown in stick representation to indicate the position of the HGF β-chain N-termini. Two cysteines (C604 and C561) shown as spheres, are candidates for the formation of the disulfide bond with Cys487 in the HGF α-chain.
FIG. 8 shows a schematic diagram for Met signaling. FIG. 8A shows the domain structure of Met. FIG. 8B shows a complex of Met with HGF in its uncleaved, immature form. High affinity binding of HGF to Met is established via the N and the K1 domains. FIGS. 8C and 8D show examples of maturation of HGF where the α- and β-chains remain connected via a single disulfide bond (—S—S—) between two cysteines (shown as —C≡C—). Maturation of HGF further leads to rearrangements in its activation domain and to an increased affinity of the HGF β-chain to the Sema domain of Met. FIG. 8C shows a 2:1 model where the α- and β-chains of HGF bind to different Met receptor molecules. FIG. 8D shows a 2:2 model where the α- and β-chains of HGF bind to the same Met receptor molecule to form stable 1:1 complexes. Maturation of HGF creates a new binding interface in the β-chain and allows the formation of a weak 2:2 Met:HGF complex. Such complexes may be stabilized via heparin or other co-receptors.

DETAILED DESCRIPTION

A. Abbreviations:

- (Å) Ångström
- (AA or aa) Amino acid; Amino acids are represented by single letter code or three letter code
- PSI domain is a small domain, which follows the Sema domain of Met, and spans about 50 residues and contains 4 disulfide bonds
- trypsin:BPTI (pdb 2PTC) is trypsin complexed with bovine pancreatic trypsin inhibitor
- MSP is macrophage stimulating protein
- NK1 is a region of the α-chain of a HGF variant, see U.S. Pat. No. 5,849,689.

B. Definitions:
The following definitions are used herein, unless specifically or contextually indicated otherwise:
The term “hepatocyte growth factor” or “HGF”, as used herein, refers, unless specifically or contextually indicated otherwise, to any native or variant (whether native or synthetic) HGF polypeptide that is capable of binding to Met and/or activating the HGF/Met signaling pathway under conditions that permit such process to occur, for example, conditions that allow for the formation of the two chain form. The term “wild type HGF sequence” generally refers to an amino acid sequence found in a naturally occurring HGF and includes naturally occurring truncated or secreted forms, variant forms (e.g. alternatively spliced forms) and naturally occurring allelic variants.
“HGF β” or “HGF β-chain”, “HGF-beta” or variations thereof, refers to any HGF β chain having the conformation that is adopted by wild type HGF β chain upon conversion of wild type HGF protein from a single chain form to a 2 chain form (i.e., α and β chain). In some embodiments, the conversion results at least in part from cleavage between residue 494 and residue 495 of the wild type HGF protein. In some embodiments, the conformation refers specifically to the conformation of the activation domain of the protease-like domain in the β chain. In some embodiments, the conformation refers even more specifically to the conformation of the active site of the protease-like domain in the HGF β chain. Generally, adoption of the conformation reveals a Met binding site, as described herein. HGF β includes variants of wild type HGF β, for example, a variant comprising an amino acid sequence of SEQ ID NO:1. The HGF β chain may be isolated from a variety of sources such as human tissue or prepared by recombinant or synthetic methods. One embodiment of HGF β chain comprises an amino acid sequence of SEQ ID NO:1 in Table 4. Another embodiment of HGF βchain comprises an amino acid sequence of SEQ ID NO:14 in Table 8.
“HGF β variant” as used herein refers to polypeptide that has a different sequence than a reference polypeptide. In some embodiments, the reference polypeptide is a HGF β polypeptide comprising SEQ ID NO:1 in Table 4. In some embodiments, a variant has at least 80% amino acid sequence identity with the HGF β amino acid sequence of Table 4 (SEQ ID NO:1) or Table 8 (SEQ ID NO:14). The variants include those polypeptides that have substitutions, additions or deletions. The variants also include those polypeptides that have at least one conservative amino acid substitutions, preferably all of the substitutions are conservative. In some embodiments, the HGF β variant has about 1-25 conservative amino amino acid substitutions, more preferably about 1-20 conservative amino acids substitutions, more preferably about 1-10 conservative amino acid substitions, more preferably about 1-5 conservative amino acid substitutions, and more preferably about 1-2 conservative amino acid substitutions. In some embodiments, the variants have the biological activity of binding to the Met receptor and/or activating it. In other embodiments, the variant can bind to the Met receptor but not activate it.
Ordinarily, a HGF β variant polypeptide will have at least 80% sequence identity, more preferably will have at least 81% sequence identity, more preferably will have at least 82% sequence identity, more preferably will have at least 83% sequence identity, more preferably will have at least 84% sequence identity; more preferably will have at least 85% sequence identity, more preferably will have at least 86% sequence identity, more preferably will have at least 87% sequence identity, more preferably will have at least 88% sequence identity, more preferably will have at least 89% sequence identity, more preferably will have at least 90% sequence identity, more preferably will have at least 91% sequence identity, more preferably will have at least 92% sequence identity, more preferably will have at least 93% sequence identity, more preferably will have at least 94% sequence identity, more preferably will have at least 95% sequence identity, more preferably will have at least 96% sequence identity, more preferably will have at least 96% sequence identity, more preferably will have at least 97% sequence identity, more preferably will have at least 98% sequence identity, more preferably will have at least 99% sequence identity with a HGF β polypeptide having an amino acid sequence comprising SEQ ID NO: 1 or SEQ ID NO:14.
The term “Met receptor” or “Met”, as used herein, refers to any native or variant (whether native or synthetic) Met polypeptide that is capable of binding to and/or being activated by HGF. The term “wild-type Met receptor” generally refers to a polypeptide comprising an amino acid sequence found in a naturally occurring Met receptor and includes naturally occurring truncated or secreted forms, variant forms (e.g. alternatively spliced forms) and naturally occurring allelic variants. The “Met Sema domain” comprises the N terminal 500 amino acid residues of a wild type Met receptor. A PSI domain follows the Sema domain and comprises 50 amino acid residues and has 4 disulfide bonds. Following the PSI domain are four IPT domains. IPT domains are related to immunoglobulin like domains. An embodiment of the Met receptor comprises an amino acid sequence of SEQ ID NO:2 as shown in Table 5. An embodiment of the extracellular fragment including the Sema domain of the Met receptor comprises an amino acid sequence of SEQ ID NO:3 as shown in Table 6 or comprises an amino acid sequence of SEQ ID NO:10 as shown in FIG. 3.
The term “Met receptor variant”, as used herein, refers to a polypeptide that has a different sequence than a reference polypeptide, whereine the reference polypeptide is the Met receptor that comprises an amino acid sequence of SEQ ID NO:2 or the extracellular fragment of the Met receptor that comprises an amino acid sequence of SEQ ID NO:3. Another embodiment of an extracellular fragment of the Met receptor comprises an amino acid sequence of SEQ ID NO:10 as shown in FIG. 3. An extracellular fragment of Met receptor comprising a sequence of SEQ ID NO:3 has amino acid substitutions at positions 304-308 of wild type sequence to insert a thrombin cleavage site. Variants include those polypeptides that have substitutions, deletions, and/or deletions. Variants also include those polypeptides that have at least one conservative amino acid substitution, preferably, all of the substitutions are conservative. In some embodiments, the Met receptor variant has about 1-25 conservative amino amino acid substitutions, more preferably about 1-20 conservative amino acids substitutions, more preferably about 1-10 conservative amino acid substitions, more preferably about 1-5 conservative amino acid substitutions, and more preferably about 1-2 conservative amino acid substitutions. In some embodiments, the variant has the biological activity of binding to HGF, but not becoming activated.
Ordinarily, a Met receptor variant will have at least 80% sequence identity to a polypeptide having SEQ ID NO:3 In some embodiments, Met receptor polypeptide variants have at least 80% sequence identity, more preferably 81% sequence identity, more preferably 82% sequence identity, more preferably 83% sequence identity, more preferably 84% sequence identity, more preferably 85% sequence identity, more preferably 86% sequence identity, more preferably 87% sequence identity, more preferably 88% sequence identity, more preferably 89% sequence identity, more preferably 90% sequence identity, more preferably 91% sequence identity, more preferably 92% sequence identity, more preferably 93% sequence identity, more preferably 94% sequence identity, more preferably 95% sequence identity, more preferably 96% sequence identity, more preferably 97% sequence identity, more preferably 98% sequence identity, more preferably 99% sequence identity or greater, to a polypeptide having a sequence of SEQ ID NO:2 or SEQ ID NO:3.
The term “binding site,” as used herein, refers to a region of a molecule or molecular complex that, as a result of its shape, distribution of electrostatic charge and/or distribution of nonpolar regions, favorably associates with a ligand. Thus, a binding site may include or consist of features such as cavities, surfaces, or interfaces between domains. Ligands that may associate with a binding site include, but are not limited to, cofactors, substrates, receptors, agonists, and antagonists. The term binding site includes a functional binding site and/or a structural binding site. A structural binding site includes “in contact” amino acid residues as determined from examination of a three-dimensional structure. “Contact” can be determined using Van der Waals radii of atoms or by proximity sufficient to exclude solvent, typically water, from the space between the ligand and the molecule or molecular complex. Some of the “in contact” amino acid residues may not cause any change in a biochemical assay, a cell-based assay, or an in vivo assay used to define a functional binding site but may contribute to the formation of a three dimensional structure. A functional binding site includes amino acid residues that are identified as binding site residues based upon loss or gain of function, for example, loss of binding to ligand upon mutation of the residue. In some embodiments, the amino acid residues of a functional binding site are a subset of the amino acid residues of the structural binding site.
The term “HGF β structural binding site” includes all or a portion of a molecule or molecular complex whose shape is sufficiently similar to at least a portion of a binding site on HGF β for Met as to be expected to bind Met or related structural analogs of Met. A structurally equivalent ligand binding site is defined by a root mean square deviation from the structure coordinates of the backbone atoms of the amino acids that make up binding sites in HGF β for Met of at most about 0.70 Å, preferably about 0.5 Å. In some embodiments, a structural binding site for the Met receptor on HGF β comprises, consists essentially of, or consists of at least one amino acid residue corresponding to a residue 513, 516, 533, 534, 536, 537, 539, 578, 619, 647, 649, 656, 668 to 670, 673, 692 to 697, 699, 702, 705 or 707 or mixtures thereof. Numbering of amino acids is that of the native receptor.
The term “Met structural binding site” includes all, or a portion of, a molecule whose shape is sufficiently similar to the binding site on Met for HGF β to be expected to bind HGF β or structural analogs of HGF β. A structurally equivalent “Met binding site” is defined by root mean square deviation from the structure coordinates of the amino acids that make up the binding sites in Met of at most about 0.70 Å, preferably about 0.5 Å. In some embodiments, a structural binding site for HGF β on the Met receptor comprises, consists essentially of, or consists of at least one amino acid residue corresponding to a residue 124-128, 148, 167, 190-192, 218, 220 to 224, 227, 229 to 230, 286 or 414 or mixtures thereof. Numbering of amino acids is that of the native receptor.
The term “a blade of a propeller” refers to a structural feature of the Met receptor. A blade is formed by four antiparallel strands with strand A in the center of the blade followed by strands B and C, and with strand D forming the outermost strand of the blade. The 7 blades are arranged in a circular fashion, with the N terminal strand forming strand D of the last blade. The AB and CD loops of each blade of the Met Sema domain form the flat bottom face of the propeller and the BC and DA loops form the top face of the propeller. In some embodiments, each of the blades of the propeller of the human Met receptor comprise the amino acid sequence as identified in FIG. 3.
“Crystal” as used herein, refers to one form of a solid state of matter in which atoms are arranged in a pattern that repeats periodically in three-dimensions, typically forming a lattice.
“Complementary or complement” as used herein, means the fit or relationship between two molecules that permits interaction, including for example, space, charge, three-dimensional configuration, and the like.
The term “corresponding” or “corresponds” refers to an amino acid residue or amino acid sequence that is found at the same positions or positions in a sequence when the amino acid position or sequences are aligned with a reference sequence. In some embodiments, the reference sequence is the extracellular fragment of the Met receptor comprising a sequence of SEQ D NO:3. It will be appreciated that when the amino acid position or sequence is aligned with the reference sequence the numbering of the amino acids may differ from that of the reference sequence or a different numbering system may be utilized.
“Heavy atom derivative”, as used herein, means a derivative produced by chemically modifying a crystal with a heavy atom such as Hg, Au, or a halogen.
“Structural homolog” of Met receptor as used herein refers to a protein that contains one or more amino acid substitutions, deletions, additions, or rearrangements with respect to the amino acid sequence of Met receptor, but that, when folded into its native conformation, exhibits or is reasonably expected to exhibit at least a portion of the tertiary (three-dimensional) structure of the Met receptor. In some embodiments, a portion of the three dimensional structure refers to structural domains of the Met receptor including the Sema domain, PSI domain, IPT domains, transmembrane domain and/or intracellular domain, and combinations thereof. For example, structurally homologous molecules of Met receptor include Met receptor variants, preferably variants with one or more conservative amino acid substitutions. In some embodiments, a Met receptor variant has only conservative amino acid substitutions. Homolog tertiary structure can be probed, measured, or confirmed by known analytic or diagnostic methods, for example, X-ray, NMR, circular dichroism, a panel of monoclonal antibodies that recognize native Met receptor, and like techniques. For example, structurally homologous molecules can have substitutions, deletions or additions of one or more contiguous or noncontiguous amino acids, such as a loop or a domain. Structurally homologous molecules also include “modified” Met receptor molecules that have been chemically or enzymatically derivatized at one or more constituent amino acid, including side chain modifications, backbone modifications, and N- and C-terminal modifications including acetylation, hydroxylation, methylation, amidation, and the attachment of carbohydrate or lipid moieties, cofactors, and like modifications.
“Ligand”, as used herein, refers to an agent and/or compound that associates with a binding site on a molecule, for example, Met and/or HGF β binding sites, and may be an antagonist or agonist of Met or HGF β activity. Ligands include molecules that mimic HGF β binding to Met and in some embodiments, are not capable of activating HGF β/Met signalling pathway.
“Compound” refers to molecule that associates with the Met or the HGF β or a pharmaceutically acceptable salt, ester, amide, prodrug, isomer, or metabolite, thereof. “Pharmaceutically acceptable salt” refers to a formulation of a compound that does not compromise the biological activity and properties of the compound. Pharmaceutical salts can be obtained by reacting a binding-active compound of the disclosure with inorganic or organic acids such as hydrochloric acid, hydrobromic acid, sulfuric acid, nitric acid, phosphoric acid, methanesulfonic acid, ethanesulfonic acid, p-toluenesulfonic acid, salicylic acid and the like. “Prodrug” refers to an agent that is converted into the parent drug in vivo. Prodrugs are often useful because, in some situations, they may be easier to administer than the parent drug. They may, for instance, be bioavailable by oral administration whereas the parent is not. The prodrug may also have improved solubility in pharmaceutical compositions over the parent drug. An example, without limitation, of a prodrug would be a compound of the present invention which is administered as an ester (the “prodrug”) to facilitate transport across a cell membrane where water solubility is detrimental to mobility but which then is metabolically hydrolyzed to the carboxylic acid, the active entity, once inside the cell where water solubility is beneficial. A further example of a prodrug might be a short peptide (polyaminoacid) bonded to an acid group wherein the peptide is metabolized to yield the active moiety.
“Molecular complex”, as used herein, refers to a combination of bound substrate or ligand with polypeptide, such as HGF β bound to Met, or a ligand bound to HGF β or Met.
“Machine-readable data storage medium”, as used herein, means a data storage material encoded with machine-readable data, wherein a machine programmed with instructions for using such data and is capable of displaying data in the desired format, for example, a graphical three-dimensional representation of molecules or molecular complexes.
“Scalable,” as used herein, means the increasing or decreasing of distances between coordinates (configuration of points) by a scalar factor while keeping the angles essentially the same.
“Space group symmetry”, as used herein, means the whole symmetry of the crystal that combines the translational symmetry of a crystalline lattice with the point group symmetry. A space group is designated by a capital letter identifying the lattice type (P, A, F, etc.) followed by the point group symbol in which the rotation and reflection elements are extended to include screw axes and glide planes. Note that the point group symmetry for a given space group can be determined by removing the cell centering symbol of the space group and replacing all screw axes by similar rotation axes and replacing all glide planes with mirror planes. The point group symmetry for a space group describes the true symmetry of its reciprocal lattice.
“Unit cell”, as used herein, means the atoms in a crystal that are arranged in a regular repeating pattern, in which the smallest repeating unit is called the unit cell. The entire structure can be reconstructed from knowledge of the unit cell, which is characterized by three lengths (a, b and c) and three angles (α, β and γ). The quantities a and b are the lengths of the sides of the base of the cell and γ is the angle between these two sides. The quantity c is the height of the unit cell. The angles α and β describe the angles between the base and the vertical sides of the unit cell.
“X-ray diffraction pattern” means the pattern obtained from X-ray scattering of the periodic assembly of molecules or atoms in a crystal. X-ray crystallography is a technique that exploits the fact that X-rays are diffracted by crystals. X-rays have the proper wavelength (in the Angstrom (Å) range, approximately 10-8 cm) to be scattered by the electron cloud of an atom of comparable size. Based on the diffraction pattern obtained from X-ray scattering of the periodic assembly of molecules or atoms in the crystal, the electron density can be reconstructed. Additional phase information can be extracted either from the diffraction data or from supplementing diffraction experiments to complete the reconstruction (the phase problem in crystallography). A model is then progressively built into the experimental electron density, refined against the data to produce an accurate molecular structure.
X-ray structure coordinates define a unique configuration of points in space. Those of skill in the art understand that a set of structure coordinates for a protein or a protein/ligand complex, or a portion thereof, define a relative set of points that, in turn, define a configuration in three dimensions. A similar or identical configuration can be defined by an entirely different set of coordinates, provided the distances and angles between coordinates remain essentially the same. In addition, a configuration of points can be defined by increasing or decreasing the distances between coordinates by a scalar factor, while keeping the angles essentially the same.
“Crystal structure” generally refers to the three-dimensional or lattice spacing arrangement of repeating atomic or molecular units in a crystalline material. The crystal structure of a crystalline material can be determined by X-ray crystallographic methods, see for example, “Principles of Protein X-Ray Crystallography,” by Jan Drenth, Springer Advanced Texts in Chemistry, Springer Verlag; 2nd ed., February 1999, ISBN: 0387985875, and “Introduction to Macromolecular Crystallography,” by Alexander McPherson, Wiley-Liss, Oct. 18, 2002, ISBN: 0471251224.
C. Modes for Carrying out the Invention:
The present disclosure thus includes a crystalline form and a crystal structure of hepatocyte growth factor beta-chain (HGF β) complexed with Met receptor (HGF β:Met) and methods of using the HGF β:Met crystal structure and structural coordinates to identify homologous proteins and to design or identify agents that can modulate the function of HGF, Met, and/or HGF β:Met complex. In some embodiments, the crystalline form of HGF β complexed with Met receptor diffracts X-rays for a determination of atomic coordinates to a resolution of 5 Å or better. The present disclosure also includes the three-dimensional configuration of points derived from the structure coordinates of at least a portion of an extracellular fragment of a Met receptor molecule or molecular complex, as well as structurally equivalent configurations, as described below. The three-dimensional configuration includes points derived from structure coordinates representing the locations of a plurality of the amino acids defining the Met binding site for HGF β, the blades of the propeller, and the PSI domain.
In some embodiments, the three-dimensional configuration includes points derived from structure coordinates representing the locations of the backbone atoms of a plurality of amino acids defining the Met or HGF β:Met complex binding site. Alternatively, the three-dimensional configuration includes points derived from structure coordinates representing the locations of the side chain and the backbone atoms (other than hydrogens) of a plurality of the amino acids defining the Met or HGF β:Met complex binding site including the Met binding site for HGF β and the HGF β binding site for Met.
The disclosure also includes the three-dimensional configuration of points identifying other structural features of an extracellular fragment of the Met receptor. Those other structural features include the blades of the propeller structure and PSI domain. A plurality of amino acid residues have been identified as contributing to these structural features of Met receptor. In some embodiments, the amino acid residues comprise those identified as corresponding to structural features as shown in FIG. 3.
Likewise, the disclosure also includes the scalable three-dimensional configuration of points derived from structure coordinates of molecules or molecular complexes that are structurally homologous to HGF β:Met complex or extracellular fragment of the Met receptor including the Sema domain, as well as structurally equivalent configurations. Structurally homologous molecules or molecular complexes are defined below. Advantageously, structurally homologous molecules can be identified using the structure coordinates of the HGF β:Met complex or extracellular fragment of the Met receptor according to a method of the disclosure.
The configurations of points in space derived from structure coordinates according to the disclosure can be visualized as, for example, a holographic image, a stereodiagram, a model, or a computer-displayed image, and the disclosure thus includes such images, diagrams or models.
The crystal structure and structural coordinates can be used in methods, for example, for obtaining structural information of a related molecule, and for identifying and designing agents that modulate Met or HGF β:Met complex activity.
The coordinates of the present disclosure have been deposited in the RCSB Protein Data Bank under accession code: PDBISHY.
1. Met and HGF β Polypeptides, Polynucleotides and Variants Thereof
The present disclosure includes a description of HGF β and an extracellular fragment of Met including the Sema domain of the Met receptor.
The present disclosure includes a description of hepatocyte growth factor and/or portions thereof. Hepatocyte growth factor comprises a 69 kDa alpha chain and 34 kDa beta chain. HGF is secreted as a single chain precursor form (scHGF). The 69 kDa alpha chain comprise a N terminal finger domain and four kringle domains (K1-K4). A representative amino acid sequence of human HGF β chain is shown in Table 4 (SEQ ID NO: 1). The sequence of Table 4 has one amino acid change from wild type shown in Table 8; the cysteine at amino acid position 604 is changed to a serine. It would be expected that a wild type HGF β would have an equivalent crystal structure. The amino acid numbering of the HGF β chain is based on the numbering of the single chain precursor form. Numbers in brackets or preceeded by a lower case c represent a numbering system based on reference to chymotrypsinogen.
The Met receptor is a tyrosine kinase and is part of a larger family of growth factor receptors with domain architecture similar to the Ron and Sea receptors. The extracellular portion of the Met receptor comprises N-terminal 500 amino acids that fold into a Sema domain. A PSI domain follows the Sema domain and comprises about 50 amino acids and has 4 disulfide bonds. The PSI domain is connected to the transmembrane domain and extracellular kinase domain by 4 IPT domains. IPT domains are immunoglobulin-like domains and are located C terminal to the PSI domain. Met becomes activated upon binding of a ligand, such as HGF β, the receptor is phosphorylated and cells expressing activated Met are stimulated to migrate, proliferate and/or differentiate. Crosslinking of Met receptors to form dimers also activates the Met receptor. A representative example of an amino acid sequence of a Met receptor is shown in Table 5 and comprises an amino acid sequence of SEQ ID NO:2. A representative example of a sequence of an extracellular portion of the Met receptor including the Sema domain and the PSI domain is shown in Table 6 and comprises an amino acid sequence of SEQ ID NO:3. The extracellular fragment of the Met receptor having a sequence of SEQ ID NO:3 differs from wild type in that amino acids at positions 304 to 308 have been substituted to include a thrombin cleavage site. Another embodiment of an extracellular fragment of Met is provided in FIG. 3 and comprises an amino acid sequence of SEQ ID NO:10. The numbering system of Met receptor is that of the Swiss Prot database as shown in Table 6.
Native or wild-type HGF, HGFα HGF β, or Met receptor polypeptides are those polypeptides that have a sequence of a polypeptide obtained from nature. Native or wild-type polypeptides include naturally occurring variants, secreted or truncated forms. Some domains of HGF and/or the Met receptor are known. Several isoforms of HGF are known such as isoform 1, isoform 2, isoform 3, isoform 4, and isoform 5. Representative sequences can be found at GenBank Accession Numbers NM_—000601, NM_—001010931, NM_—001010932, NM_—001010933, NM_—001010934, and NP_—000592.
The present disclosure also includes a polypeptide comprising, consisting essentially of, or consisting of a portion or fragment of the Met receptor. The polypeptide fragment includes amino acid residues from any of amino acid 1 to 25 residues to amino acid position 567 or residues corresponding to those positions. In some embodiments, the polypeptide portion has the ability to bind to ligand HGF. The polypeptide portion may also be fused to heterologous polypeptide, such as a peptide tag. Preferably, the fusion polypeptide retains the ability to bind a ligand, such as HGF.
The disclosure also provides a polypeptide comprising, consisting essentially of, or consisting of a portion or fragment of the Met receptor starting at amino acid residue 124 and ending at any one of amino acid residues 230 to 286 or residues corresponding to these residues. This polypeptide includes the amino acid residues that contact the HGF β ligand and preferably, the polypeptide has the ability to bind to a ligand such as HGF β. The polypeptide portion or fragment may be fused to a heterologous polypeptide. Preferably, the fusion protein can bind to a ligand, such as HGF β.
The present disclosure also includes variants of the Met receptor. Variants include those polypeptides that have amino acid substitutions, deletions, and additions. Amino acid substitutions can be made for example to replace cysteines and eliminate formation of disulfide bonds. Amino acid substitutions can also be made to change proteolytic cleavage sites. The variants also include those polypeptides that have at least one conservative amino acid substitution. In some embodiments a variant only has conservative amino acid substitutions. In some embodiments, the Met receptor variant has about 1-25 conservative amino acid substitutions, more preferably about 1-20 conservative amino acids substitutions, more preferably about 1-10 conservative amino acid substitutions, more preferably about 1-5 conservative amino acid substitutions, and more preferably about 1-2 conservative amino acid substitutions. In some embodiments, a Met receptor variant has at least 90% sequence identity to an extracellular domain fragment of the Met receptor, such as SEQ ID NO:3, and has changes at amino acids other than those associated with the binding site for HGF β on Met, preferably the amino acid changes are only conservative substitutions. Other variants can be made at the Met binding site for HGF β. In other embodiments, the variants of the Met receptor bind HGF β bind with the same or higher affinity than the wild type Met receptor.
Fusion Proteins
A Met receptor, variant or structural homolog or portions thereof, may be fused to a heterologous polypeptide or compound. The heterologous polypeptide is a polypeptide that has a different function than that of the Met receptor. Examples of heterologous polypeptide include polypeptides that may act as carriers, may extend half life, may act as epitope tags, may provide ways to detect or purify the fusion protein. Heterologous polypeptides include KLH, albumin, salvage receptor binding epitopes, immunoglobulin constant regions, and peptide tags. Peptide tags useful for detection or purification include FLAG, gD protein, polyhistidine tags, hemagluthinin from influenza virus, T7 tag, S tag, Strep tag, chloramiphenicol acetyl transferase, biotin, glutathione-S transferase, green fluorescent protein and maltose binding protein. Compounds that can be combined with the Met receptor, variants or structural homolog or portions thereof, include radioactive labels, protecting groups, and carbohydrate or lipid moieties.
Polynucleotides, Vectors and Host Cells
Variants of a Met receptor or extracellular fragment thereof can be prepared by introducing appropriate nucleotide changes into DNA encoding Met or the extracellular fragment, or by synthesis of the desired polypeptide variants. HGF β chain variants can be prepared by introducing appropriate nucleotide changes into DNA encoding HGF β or by synthesis of the desired polypeptide variants. Variants can be made using standard methods.
Amino acid substitutions, include one or more conservative amino acid substitutions. The term “conservative” amino acid substitution as used herein refers to an amino acid substitution which substitutes a functionally equivalent amino acid. Conservative amino acid changes result in silent changes in the amino acid sequence of the resulting polypeptide. For example, one or more amino acids of a similar polarity act as functional equivalents and result in a silent alteration within the amino acid sequence of the peptide. In general, substitutions within a group can be considered conservative with respect to structure and function. However, the skilled artisan will recognize that the role of a particular residue is determined by its context within the three-dimensional structure of the molecule in which it occurs. For example, Cys residues may occur in the oxidized (disulfide) form, which is less polar than the reduced (thiol) form. The long aliphatic portion of the Arg side chain can constitute a feature of its structural or functional role, and this may be best conserved by substitution of a nonpolar, rather than another basic residue. Also, it will be recognized that side chains containing aromatic groups (Trp, Tyr, and Phe) can participate in ionic-aromatic or “cation-pi” interactions. In these cases, substitution of one of these side chains with a member of the acidic or uncharged polar group may be conservative with respect to structure and function. Residues such as Pro, Gly, and Cys (disulfide form) can have direct effects on the main chain conformation, and often may not be substituted without structural distortions.

Amino acid substitutions can be the result of replacing one amino acid with another amino acid having similar structural and/or chemical properties, such as the replacement of a leucine with a serine, i.e., conservative amino acid replacements. Examples of conservative substitutions are shown in Table 9. The variation allowed can be determined by systematically making insertions, deletions or substitutions of amino acids in the sequence and testing the resulting variants for activity exhibited by the native sequence.

TABLE 9


Original		Preferred
Residue	Exemplary Substitutions	Substitutions

Ala (A)	Val; Leu; Ile	Val

Arg (R)	Lys; Gln; Asn	Lys

Asn (N)	Gln; His; Asp, Lys; Arg	Gln

Asp (D)	Glu; Asn	Glu

Cys (C)	Ser; Ala	Ser

Gln (Q)	Asn; Glu	Asn

Glu (E)	Asp; Gln	Asp

Gly ()	Ala	Ala

His (H)	Asn; Gln; Lys; Arg	Arg

Ile (I)	Leu; Val; Met; Ala; Phe;	Leu
	Norleucine

Leu (L)	Norleucine; Ile; Val; Met;	Ile
	Ala; Phe

Lys (K)	Arg; Gln; Asn	Arg

Met (M)	Leu; Phe; Ile	Leu

Phe (F)	Trp; Leu; Val; Ile; Ala; Tyr	Tyr

Pro (P)	Ala	Ala

Ser (S)	Thr	Thr

Thr (T)	Val; Ser	Ser

Trp (W)	Tyr; Phe	Tyr

Tyr (Y)	Trp; Phe; Thr; Ser	Phe

Val (V)	Ile; Leu; Met; Phe; Ala;	Leu
	Norleucine

Polynucleotide sequences encoding the polypeptides described herein can be obtained using standard recombinant techniques. Desired polynucleotide sequences may be isolated and sequenced from appropriate source cells. Alternatively, polynucleotides can be synthesized using nucleotide synthesizer or PCR techniques. Once obtained, sequences encoding the polypeptides or variant polypeptides are inserted into a recombinant vector capable of replicating and expressing heterologous polynucleotides in a host cell. Many vectors that are available and known in the art can be used for the purpose of the present invention. Selection of an appropriate vector will depend mainly on the size of the nucleic acids to be inserted into the vector and the particular host cell to be transformed with the vector. Each vector contains various components, depending on its function (amplification or expression of heterologous polynucleotide, or both) and its compatibility with the particular host cell in which it resides. The vector components generally include, but are not limited to: an origin of replication (in particular when the vector is inserted into a prokaryotic cell), a selection marker gene, a promoter, a ribosome binding site (RBS), a signal sequence, the heterologous nucleic acid insert and a transcription termination sequence.
In general, plasmid vectors containing replicon and control sequences, which are derived from a species compatible with the host cell are used in connection with these hosts. The vector ordinarily carries a replication site, as well as marking sequences, which are capable of providing phenotypic selection in transformed cells. For example, E. coli is typically transformed using pBR322, a plasmid derived from an E. coli species. pBR322 contains genes encoding ampicillin (Amp) and tetracycline (Tet) resistance and thus provides easy means for identifying transformed cells. pBR322, its derivatives, or other microbial plasmids or bacteriophage may also contain, or be modified to contain, promoters which can be used by the microbial organism for expression of endogenous proteins.
In addition, phage vectors containing replicon and control sequences that are compatible with the host microorganism can be used as transforming vectors in connection with these hosts. For example, bacteriophage such as λGEM™-11 may be utilized in making a recombinant vector which can be used to transform susceptible host cells such as E. coli LE392.
Either constitutive or inducible promoters can be used in the present invention, in accordance with the needs of a particular situation, which can be ascertained by one skilled in the art. A large number of promoters recognized by a variety of potential host cells are well known. The selected promoter can be operably linked to cistron DNA encoding a polypeptide described herein by removing the promoter from the source DNA via restriction enzyme digestion and inserting the isolated promoter sequence into the vector of choice. Both the native promoter sequence and many heterologous promoters may be used to direct amplification and/or expression of the target genes. However, heterologous promoters are preferred, as they generally permit greater transcription and higher yields of expressed target gene as compared to the native target polypeptide promoter.
Promoters suitable for use with prokaryotic hosts include the PhoA promoter, the β-galactamase and lactose promoter systems, a tryptophan (trp) promoter system and hybrid promoters such as the tac or the trc promoter. However, other promoters that are functional in bacteria (such as other known bacterial or phage promoters) are suitable as well. Their nucleotide sequences have been published, thereby enabling a skilled worker operably to ligate them to cistrons encoding the polypeptides or variant polypeptides (Siebenlist et al. (1980) Cell 20: 269) using linkers or adaptors to supply any required restriction sites.
In embodiments, each cistron within a recombinant vector comprises a secretion signal sequence component that directs translocation of the expressed polypeptides across a membrane. In general, the signal sequence may be a component of the vector, or it may be a part of the polypeptide encoding DNA that is inserted into the vector. The signal sequence selected for the purpose of this invention should be one that is recognized and processed (i.e. cleaved by a signal peptidase) by the host cell. For prokaryotic host cells that do not recognize and process the signal sequences native to the heterologous polypeptides, the signal sequence is substituted by a prokaryotic signal sequence selected, for example, from the group consisting of the alkaline phosphatase, penicillinase, Ipp, or heat-stable enterotoxin II (STII) leaders, LamB, PhoE, PelB, OmpA and MBP.
Prokaryotic host cells suitable for expressing polypeptides include Archaebacteria and Eubacteria, such as Gram-negative or Gram-positive organisms. Examples of useful bacteria include Escherichia (e.g., E. coli), Bacilli (e.g., B. subtilis), Enterobacteria, Pseudomonas species (e.g., P. aeruginosa), Salmonella typhimurium, Serratia marcescans, Klebsiella, Proteus, Shigella, Rhizobia, Vitreoscilla, or Paracoccus. Preferably, gram-negative cells are used. Preferably the host cell should secrete minimal amounts of proteolytic enzymes, and additional protease inhibitors may desirably be incorporated in the cell culture.
Besides prokaryotic host cells, eukaryotic host cell systems are also well established in the art. Examples of invertebrate cells include insect cells such as Drosophila S2 and Spodoptera Sf9, as well as plants and plant cells. Examples of useful mammalian host cell lines include Chinese hamster ovary (CHO) and COS cells. More specific examples include monkey kidney CVI line transformed by SV40 (COS-7, ATCC CRL 1651); Chinese hamster ovary cells/-DHFR(CHO, Urlaub and Chasin, Proc. Natl. Acad. Sci. USA, 77:4216 (1980)); mouse sertoli cells (TM4, Mather, Biol. Reprod., 23:243-251 (1980)); and mouse mammary tumor (MMT 060562, ATCC CCL51).
Polypeptide Production
Host cells are transformed or transfected with the above-described expression vectors and cultured in conventional nutrient media modified as appropriate for inducing promoters, selecting transformants, or amplifying the genes encoding the desired sequences.
Transfection refers to the taking up of an expression vector by a host cell whether or not any coding sequences are in fact expressed. Numerous methods of transfection are known to the ordinarily skilled artisan, for example, CaPO₄precipitation and electroporation. Successful transfection is generally recognized when any indication of the operation of this vector occurs within the host cell.
Transformation means introducing DNA into the prokaryotic host so that the DNA is replicable, either as an extrachromosomal element or by chromosomal integrant. Depending on the host cell used, transformation is done using standard techniques appropriate to such cells. The calcium treatment employing calcium chloride is generally used for bacterial cells that contain substantial cell-wall barriers. Another method for transformation employs polyethylene glycol/DMSO. Yet another technique used is electroporation.
Prokaryotic cells used to produce the polypeptides of the invention are grown in media known in the art and suitable for culture of the selected host cells. Examples of suitable media include luria broth (LB) plus necessary nutrient supplements. In preferred embodiments, the media also contains a selection agent, chosen based on the construction of the expression vector, to selectively permit growth of prokaryotic cells containing the expression vector. For example, ampicillin is added to media for growth of cells expressing ampicillin resistant gene.
Any necessary supplements besides carbon, nitrogen, and inorganic phosphate sources may also be included at appropriate concentrations introduced alone or as a mixture with another supplement or medium such as a complex nitrogen source. Optionally the culture medium may contain one or more reducing agents selected from the group consisting of glutathione, cysteine, cystamine, thioglycollate, dithioerythritol and dithiothreitol.
The prokaryotic host cells are cultured at suitable temperatures. For E. coli growth, for example, the preferred temperature ranges from about 20° C. to about 39° C., more preferably from about 25° C. to about 37° C., even more preferably at about 30° C. The pH of the medium may be any pH ranging from about 5 to about 9, depending mainly on the host organism. For E. coli, the pH is preferably from about 6.8 to about 7.4, and more preferably about 7.0.
If an inducible promoter is used in the expression vector, protein expression is induced under conditions suitable for the activation of the promoter. For example, if a PhoA promoter is used for controlling transcription, the transformed host cells may be cultured in a phosphate-limiting medium for induction. A variety of other inducers may be used, according to the vector construct employed, as is known in the art.
Eukaryotic host cells are cultured under conditions suitable for expression of the HGF and/or Met receptor polypeptides. The host cells used to produce the polypeptides may be cultured in a variety of media. Commercially available media such as Ham's F10 (Sigma), Minimal Essential Medium ((MEM), (Sigma), RPMI-1640 (Sigma), and Dulbecco's Modified Eagle's Medium ((DMEM), Sigma) are suitable for culturing the host cells. In addition, any of the media described in one or more of Ham et al., 1979, Meth. Enz. 58:44, Barnes et al., 1980, Anal. Biochem. 102: 255, U.S. Pat. No. 4,767,704, U.S. Pat. No. 4,657,866, U.S. Pat. No. 4,927,762, U.S. Pat. No. 4,560,655, or U.S. Pat. No. 5,122,469, WO 90/103430, WO 87/00195, and U.S. Pat. No. Re. 30,985 may be used as culture media for the host cells. Any of these media may be supplemented as necessary with hormones and/or other growth factors (such as insulin, transferrin, or epidermal growth factor), salts (such as sodium chloride, calcium, magnesium, and phosphate), buffers (such as HEPES™), nucleotides (such as adenosine and thymidine), antibiotics (such as GENTAMYCIN™), trace elements (defined as inorganic compounds usually present at final concentrations in the micromolar range), and glucose or an equivalent energy source. Other supplements may also be included at appropriate concentrations that would be known to those skilled in the art. The culture conditions, such as temperature, pH, and the like, are those previously used with the host cell selected for expression, and will be apparent to the ordinarily skilled artisan.
Polypeptides described herein expressed in a host cell may be secreted into and/or recovered from the periplasm of the host cells. Protein recovery typically involves disrupting the microorganism, generally by such means as osmotic shock, sonication or lysis. Once cells are disrupted, cell debris or whole cells may be removed by centrifugation or filtration. The proteins may be further purified, for example, by affinity resin chromatography. Alternatively, proteins can be transported into the culture media and isolated there from. Cells may be removed from the culture and the culture supernatant being filtered and concentrated for further purification of the proteins produced. The expressed polypeptides can be further isolated and identified using commonly known methods such as fractionation on immunoaffinity or ion-exchange columns; ethanol precipitation; reverse phase HPLC; chromatography on silica or on a cation exchange resin such as DEAE; chromatofocusing; SDS-PAGE; ammonium sulfate precipitation; gel filtration using, for example, Sephadex G-75; hydrophobic affinity resins, ligand affinity using a suitable antigen immobilized on a matrix and Western blot assay.
Polypeptides that are produced may be purified to obtain preparations that are substantially homogeneous for further assays and uses. Standard protein purification methods known in the art can be employed. The following procedures are exemplary of suitable purification procedures: fractionation on immunoaffinity or ion-exchange columns, ethanol precipitation, reverse phase HPLC, chromatography on silica or on a cation-exchange resin such as DEAE, chromatofocusing, SDS-PAGE, ammonium sulfate precipitation, and gel filtration using, for example, Sephadex G-75.
2. Crystals and Crystal Structures
The present disclosure provides crystals of and a crystal structure of HGF β chain cocrystalized with a fragment of the Met receptor. In some embodiments, the Met receptor fragment includes the Sema and PSI domain. The crystals were formed by contacting a mixture of purified HGF β chain and the Met receptor extracellular fragment with a precipitant in a buffer. In some embodiments, the crystal of a HGF β and a Met receptor can be diffracted by X-rays to determine atomic coordinates to a resolution of 5 Å or better. In some embodiments, the precipitant was 12-15% polyethylene glycol 10,000. In some embodiments, the crystals are formed from a HGF β comprising SEQ ID NO:1 and a Met receptor fragment comprising SEQ ID NO:3.
The resulting crystals diffracted to 3.2 Å resolution (Table 1) and have one (1) full complex containing one Met fragment and a single HGF β-chain in the asymmetric unit. The structure was refined to an R-value of 20.9% (Rfree 27.0%) with good geometry. Of the 628 non-glycine and non-proline residues, 97.6% have their main-chain torsion angles in the ‘most-favored’ or the ‘additionally allowed’ regions of the Ramachandran plot (Laskowski et al., 1993). The refined model includes residues 495 to 722 of HGF and residues 40 to 301, 311 to 377, 382 to 400, and 414 to 564 of Met. Although a number of glycosylation sites displayed electron density, none of the sugars were modeled into the structure.
In a specific embodiment, the structure of HGF β complexed with a Met receptor extracellular fragment (HGF β:Met) was solved by molecular replacement with the program AMORE (NAVAZC 1994) using the crystal structure of HGF β chain alone as search model (coordinates for HGF β can be found in the RCSB Protein Data Bank under accession code: PDB1UX3). The crystals belonged to space group P2₁P2₁P with cell parameters of a=137.1 Å, b=186.4 Å and c=66.7 Å and contained 1 complex of Met: HGF β chain in the asymmetric unit.
Each of the constituent amino acids in HGF β:Met is defined by a set of structural coordinates as set forth in Table 2. The coordinates and structure factors of the present disclosure have been deposited by the RCSB Protein Data Bank under Accession Code: PDB 1SHY.
The term “structure coordinates” refers to Cartesian coordinates derived from mathematical equations related to the patterns obtained on diffraction of a monochromatic beam of X-rays by the atoms (scattering centers) of a Met receptor or Met: HGF β in crystal form. The diffraction data are used to calculate an electron density map of the repeating unit of the crystal. The electron density maps are then used to establish the positions of the individual atoms of the Met receptor or protein/ligand complex.
Slight variations in structure coordinates can be generated by mathematically manipulating the Met receptor or Met: HGF β complex structure coordinates. For example, the structure coordinates as set forth in Table 2 could be manipulated by crystallographic permutations of the structure coordinates, fractionalization of the structure coordinates, integer additions or subtractions to sets of the structure coordinates, inversion of the structure coordinates, or any combination of the above. Alternatively, modifications in the crystal structure due to mutations, additions, substitutions, deletions, and combinations thereof, of amino acids, or other changes in any of the components that make up the crystal, could also yield variations in structure coordinates. Such slight variations in the individual coordinates will have little effect on overall shape. If such variations are within an acceptable standard error as compared to the original coordinates, the resulting three-dimensional shape is considered to be structurally equivalent. Structural equivalence is described in more detail below.
It should be noted that slight variations in individual structure coordinates of the HGF β:Met would not be expected to significantly alter the nature of chemical entities such as ligands that could associate with a binding site or other structural features of HGF β or Met. In this context, the phrase “associating with” refers to a condition of proximity between a ligand, or portions thereof, and a HGF β or Met molecule or portions thereof. The association may be non-covalent, wherein the juxtaposition is energetically favored by hydrogen bonding, van der Waals forces, and/or electrostatic interactions, or it may be covalent.
HGF β Chain Structure
The β-chain of HGF shares close to 40% sequence identity with the protease domain of plasmin, a trypsin-like serine protease. Structurally, these enzymes can be described as globular proteins composed of two antiparallel β-barrel domains (FIG. 1A). Both of the β-barrels share the same general topology and are formed by six antiparallel β-strands, with the N-terminal four strands folding into a Greek key motif, followed by two strands that form a hairpin. HGF, like serine proteases, is expressed as a zymogen-like precursor. For serine proteases, structural studies have shown that insertion of the N-terminus resulting from the maturation process leads to allosteric rearrangments within the binding site for the protease substrate (Perona and Craig, 1995; Hedstrom 2002). In serine proteases, the newly formed N-terminus forms a salt bridge with a nearby aspartate, which leads to the formation of the oxyanion hole via the backbone NH's of two neighboring residues and the creation of a part of the S1 pocket (FIG. 1). The ‘activated’ form of the HGF β-chain, as seen in the structure presented here, is similar to the mature form of serine proteases: superposition with plasmin (pdb-code IBML) yields an rmsd of about 1.3 Å for 212 C_α, pairs. Superposition between HGF β-chain and plasminogen (pdb-code 1QRZ) reveal differences in their ‘activation domain’ (Freer et al., 1970) and only 198 C_α pairs can be aligned well.
As with serine proteases, the N-terminal amine of HGF β, Val495, is inserted into the core of the C-terminal β-barrel and forms a salt bridge with the carboxyl group of Asp672, which corresponds to Asp[c 194] in plasmin, presumably leading to similar rearrangements, which have been characterized in serine proteases. The region in HGF corresponding to this so-called ‘activation domain’, i.e., the loops that undergo conformational changes in serine proteases (Freer et al., 1970; Huber and Bode, 1978), form part of the binding surface with Met.
After maturation, the α- and β-chains of HGF remain connected via a disulfide bond. Based on alignments of the kringle domains K1 to K4 of HGF α chain and macrophage stimulating protein (MSP), the two cysteine residues responsible for the formation of this disulfide bond were identified as Cys487 on the α-chain of HGF and Cys604 on the β-chain (Donate et al., 1994). The crystal structure, however, raises the possibility of an alternative cysteine residue as the anchor for the HGF α-chain. The HGF β-chain has two (2) cysteine residues that do not have partners for the formation of disulfide bridges within the β-chain. Neither is conserved in plasmin or MSP and both are located on the periphery of the protein and are at least partially solvent exposed; either could be potential partners for the formation of a disulfide bond with the α-chain while the other remains unpaired. The superposition of the plasmin structure that contains part of the α-chain (FIG. 1B), and the HGF β-chain structure presented here, shows that the distance between the C-terminus of the plasmin α-chain and Cys604 of the HGF β-chain is 27 Å and thus only slightly shorter than the respective distance between the plasmin α-chain C-terminus and Cys561 (33 Å) (FIG. 1B). In addition, the sequence alignment between plasmin, MSP, and HGF (FIG. 1C) shows that the α-chain cysteine forming the disulfide bond in plasmin and MSP is 13 and 15 residues away from the cleavage site in those proteins respectively, but there are only 7 residues in HGF to span the distance from Cys487 to the cleavage site. Therefore, due to distance requirements, the C-terminus of the HGF α-chain cannot follow the same path on the surface of the β-chain as it does in plasmin or MSP. Regardless of the position of the disulfide bond between the alpha and beta chain, the overall structure or the structural model of the Met receptor or Met: HGF β complex is not impacted.
Met Stucture
The analysis of crystal structure of the Sema domain of Met shows that it forms 7-bladed β-propeller with a diameter of a little more than 50 Å. The overall shape of the domain resembles a funnel with an inner diameter of about 25 Å between main chain atoms at the wide portion and 10 Å in the narrowest part (FIG. 2). Generally, in β-propellers, each of the blades is formed by 4 antiparallel β-strands with strand A in the center of the propeller followed by strands B and C, and with strand D forming the outermost strand of the blade. The blades are arranged in a circular fashion, with the N-terminal strand forming strand D of the last blade, thus closing the propeller and stabilizing the overall structure (FIG. 2A). The AB and CD loops of each blade of the Met Sema domain form the relatively flat ‘bottom’ face, and the generally longer BC and DA loops form the ‘top’ face of the propeller (FIG. 2B). In Met, the position of the 6th and the 7th blade are off-center, with blade 7 being closer to the center of the barrel and blade 6 more distant. This gives the domain an overall oval shape.
The β-propeller of the Met Sema domain is structurally most closely related to the recently reported crystal structures of Sema4D (Love et al., 2003) and Sema3A (Antipenkov et al., 2003). With the exception of the D-strands in blades 3 and 5, the core of Sema4D and the Met Sema domain align well (FIGS. 3 and 4) and the superposition of residues 40 to 519 with the Sema domain of Sema4D results in an rmsd of 1.6 Å for 303 atom pairs (FIG. 4). The residues that form strand D5 in Sema4A are hydrogen bonded to strand D4 in Met, thus the 4th blade of Met contains an extra strand while blade 5 is missing its strand D. While the core of both proteins align well, the loops contain a number of insertions or deletions and generally adopt very different conformations. For example, the Sema domains of Met and of Sema4D both have an insert of about 20 residues following strand D1. In Met, these residues form a short antiparallel two-stranded β-sheet, while Sema4D has an α-helix (FIGS. 3 and 4). Of the 24 loops that connect the various strands, only 3 have no insertions or deletions when comparing Met with Sema4D or Sema3A (FIG. 3). Interestingly, both the Semaphorins and the Met receptor have their largest insertion between strands C5 and A6; however, these inserts are not related in structure or sequence to each other. In Sema3A, this insert is involved in dimer formation and has been shown to be important for neuropilin binding (Antipenko et al., 2003). In the Met Sema domain, some of the residues within the insert are disordered and not included in our model (see FIG. 2). The function of the insert in Met is not known but its proximity to the HGF β-chain binding site, discussed below, suggests that it might be involved in binding to the α-chain of HGF.
The loop containing the cleavage site between the α- and β-chain of Met connects strand D4 to A5; it is disordered in the electron density. After processing of native Met, the α-chain, which forms the N-terminal 4 blades of the Sema domain, and the β-chain remain connected via at least 2 disulfide bonds. One disulfide bond is formed between residues Cys298 on strand D4 and Cys363 on C5, and the second is formed between Cys282 (D3) and Cys409. This last cysteine is positioned in a disordered region of the insert after blade 4. The electron density does not allow tracing of the main chain in this area but there is sufficient density in the area of the Sγ position to suggest that the disulfide bond is at least partially formed. With the exception of the N-terminal Cys26, which is disordered in the presently disclosed crystal structure and has no potential partner in the construct that was used for crystallization, all cysteine residues are engaged in disulfide bonds. It is unclear if Cys26 remains unpaired in the context of full length Met receptor or if it forms a disulfide bond with another cysteine that resides in the IPT domains. Besides the two disulfide bonds that covalently connect the α- and β-chain of the Sema domain, the domain is stabilized by 5 additional disulfide bridges formed between Cys95-Cys101, Cys98-Cys159, Cys133-Cys141, Cys172-Cys175, and Cys385-Cys397 (FIG. 3).
The surface of the Met Sema domain appears to be mostly negatively charged, especially in the center of the bottom face of the Sema domain (FIG. 2C). This surface, which is formed by a 20 residue insertion after strand D in the first blade and includes the rather irregular area of strand D in the third blade, shows clusters of acidic residues. Monomeric, full length Met was shown to bind to heparin (Gherardi et al., 2003). In the presently disclosed structure there are no dominant positively charged patches within the Met Sema domain; however, two arginines are located in the vicinity of the disordered furin-cleavage site. Together with the 6 positively charged residues that reside in this loop, these arginines could constitute a potential heparin binding site.
The last strand of the Sema domain (C7) is followed immediately by the PSI domain. This domain, with dimensions of about 20×15 Å, contains four (4) disulfide bridges and is not an integral part of the Sema domain but rather an independent structural module. The small core of the domain is formed by a helix and a short two-stranded antiparallel β-sheet that are connected via a disulfide bond and sandwich the side-chain of Trp540. Superposition of this domain with the PSI domain of Sema4D results in an rmsd of 1.6 Å for 41 C_α pairs. The relative orientation between the Sema and the PSI domains in the Met and the Sema4D structures, however, is different and requires a rotation of about 40° for superposition.
Th Interface Between the HGF β-Chain and Met
The HGF β-chain binds to the Sema domain of Met at the bottom face of the propeller, and forms contacts with residues that protrude from blades 2 and 3 (FIGS. 2 and 3). This is unlike other β-propeller containing receptors, such as the integrins, which bind their ligands utilizing the top face of the propeller (Xiong et al., 2002). Other Sema domain containing proteins, such as Sema3A and Sema4D, are also postulated to bind ligands using the top face (Antipenko et al., 2003; Love et al., 2003).
The interface between HGF β-chain and Met buries a total of 1770 Å²of solvent accessible surface and is dominated by polar or charge-charge interactions. The volume of the cavity of the pocket that is blocked by Met on the surface of HGF β is about 380 cubic angstroms as determined by placing a number of atoms at the entrance of the pocket to close the pocket and using the program GRASP (available from Columbia University at ihonigts@columbia/edu) to calculate the volume of the resulting cavity.
Of the 20 HGF β residues that have more that 10 Å²buried in the interface, 6 are positively charged, 3 carry negative charges, and 3 are aromatic. The positively charged amino acids include K516, R533, R647, R695, K649, and R702. The negatively charged amino acids include E656, E670, and D578. The aromatic amino acids include Y513, Y673, and Y619. (See Table 3).
Even more dramatic, of the 18 residues contributing more than 10 Å²of buried surface to the interface on the Met receptor, 6 carry negative charges, 4 are positively charged and 3 are aromatic. The positively charged amino acid residues include H148, R191, R218, and K223. The negatively charged amino acids include D127, D128, E168, E221, and D224. The aromatic amino acids include Y125, Y126, and F192. The combined buried surface of the hydrophobic residues Ala, Val, Leu, Ile, Met and Phe amounts to a mere 145 Å², while the charged residues Asp, Glu, Lys, Arg, and His are responsible for more than 1,000 Å²of buried surface. The resolution of the presently disclosed structure does not permit a detailed discussion of hydrogen bonds; however, the position of the side chains suggest the presence of at least 7 charged interactions between Met and the HGF β-chain. In some embodiments, variants of HGF beta or Met receptor may be designed to preserve and/or strengthen these charge charge interactions. In other embodiments, small molecules may be designed to mimic the charge-charge interaction of either the HGF β binding site for Met or the Met binding site for HGF β. (See Table 3).
On HGF, the residues analogous to those responsible for substrate binding and catalysis in the related serine proteases form most of the interactions with Met. Serine proteases bind linear peptides to their recognition site and form hydrogen bonds to main chain atoms to position a specific peptide bond for proteolytic cleavage. In contrast, the HGF β-chain binds to a series of protruding polar side chains from Met that comprise amino acid residues from 3 separate loops (FIG. 5B). The first of these loops includes residues 124-128 of Met and connects strands A2 and B2 of Met. This loop contains two tyrosines that are in the core of the binding interface and pack against Arg695 of HGF β. The second loop of Met that contacts HGF β-chain includes residues Asp190, Arg191, and Phe192 and connects A3 and B3. Asp190 of Met forms charged interactions with Arg533 of HGF. The side chain of Arg191 of Met packs against Val692 and Pro693 of HGF with its hydrophobic portion and in the presently disclosed model is in hydrogen bonding distance to the side chains of Glu656 and Asp578 with its guanidinium group. This Asp578 corresponds to aspartic acid [c102] in the catalytic triad of the related serine proteases. Furthermore, the backbone of this loop forms hydrophilic interactions with Gln534, the residue homologous to the histidine [c57] of the protease catalytic triad.
The third segment contributing to the interface also includes strand D in the third blade of the propeller, an area that deviates from the classical ‘propeller fold’. Strand D is interrupted and has a short helical insert within its strand. This unusual conformation presents a number of residues towards the surface of the HGF β-chain. The most prominent interaction formed by this loop involves Glu221 which extends its side chain towards what would be the S1 binding site in serine proteases (FIGS. 5 and 6). The carboxylate of Glu221 forms an extensive network of polar interactions with the side chain of Tyr673 (corresponding to the serine [c 195] of the catalytic triad in proteases), as well as the backbone amides of Gly694 and Gly696 (FIG. 6); however, unlike in serine proteases, where the S1 pocket is filled by the specificity determining P1 residue, it does not penetrate deeply into the S1 pocket. As a result of the exchange of Ser to Tyr in position 673 [c195], the entrance of the S1 pocket is much smaller than in the related proteases. Thus, Glu221 projects towards the entrance of the S1 pocket from a different angle when compared to a complex between trypsin and bovine pancreatic trypsin inhibitor (BPTI) and does not fill the pocket (FIG. 6). Therefore, a large cavity, presumably filled with a number of water molecules, remains in HGF β-chain.
Comparison of HGF β-Chain Unbound and Bound to Met
The structures of the HGF β-chain bound to Met and HGF β in its unbound state, as disclosed in application U.S. Ser. No. 60/569,301, filed May 6, 2004, which is hereby incorporated by reference, are very similar and superimpose with an rmsd of less than 0.8 Å for 218 C_α-pairs. The only significant differences between the two structures involve residues that are close to the Met binding interface. The backbone of residues 645 to 651 is disordered in unliganded HGF β but well defined in the structure of the complex, where it adopts a conformation that is commonly observed in serine proteases (FIG. 1). The side chains of the basic residues Arg647 and Lys649 are not well defined in the electron density but project towards the Met binding interface and, in presently disclosed model, participate in the formation of the complex. Arg695 also undergoes a change in conformation upon Met binding. This residue, located in the center of the receptor binding interface, packs against Tyr125 of Met, and its backbone forms part of the S1 pocket. In the structure of unliganded HGF β, the conformation of the backbone in this area is different, and the side chain of Arg695 projects toward the disordered region of the structure. It is conceivable that the binding event alters the position of Arg695, which in turn allows residues 645 to 651 to adopt a more stable conformation. The tunnel or void identified in the crystal structure of HGFβ, is also seen in the cocrystal.
3. Structurally Equivalent Crystal Structures
Various computational analyses can be used to determine whether a molecule or portions of the molecule defining structure features are “structurally equivalent,” defined in terms of its three-dimensional structure, to all or part of a Met receptor or HGF β:Met complex or its ligand binding sites. Such analyses may be carried out in current software applications, such as the Molecular Similarity application of QUANTA (Molecular Simulations Inc., San Diego, Calif.), Version 4.1, and as described in the accompanying User's Guide.
The Molecular Similarity application permits comparisons between different structures, different conformations of the same structure, and different parts of the same structure. A procedure used in Molecular Similarity to compare structures comprises: 1) loading the structures to be compared; 2) defining the atom equivalences in these structures; 3) performing a fitting operation; and 4) analyzing the results.
One structure is identified as the target (i.e., the fixed structure); all remaining structures are working structures (i.e., moving structures). Since atom equivalency within QUANTA is defined by user input, for the purpose of this disclosure equivalent atoms are defined as protein backbone atoms (N, Cα, C, and O) for all conserved residues between the two structures being compared. A conserved residue is defined as a residue that is structurally or functionally equivalent. Only rigid fitting operations are considered.
When a rigid fitting method is used, the working structure is translated and rotated to obtain an optimum fit with the target structure. The fitting operation uses an algorithm that computes the optimum translation and rotation to be applied to the moving structure, such that the root mean square difference of the fit over the specified pairs of equivalent atom is an absolute minimum. This number, given in Angstroms, is reported by QUANTA.
Structurally equivalent crystal structures have portions of the two molecules that are substantially identical, within an acceptable margin of error. The margin of error can be calculated by methods known to those of skill in the art. In some embodiments, any molecule or molecular complex or any portion thereof, that has a root mean square deviation of conserved residue backbone atoms (N, Cα, C, O) of less than about 0.70 Å, preferably 0.5 Å. For example, structurally equivalent molecules or molecular complexes are those that are defined by the entire set of structure coordinates listed in Table 2±a root mean square deviation from the conserved backbone atoms of those amino acids of not more than 0.70 Å, preferably 0.5 Å. The term “root mean square deviation” means the square root of the arithmetic mean of the squares of the deviations. It is a way to express the deviation or variation from a trend or object. For purposes of this disclosure, the “root mean square deviation” defines the variation in the backbone of a protein from the backbone of HGF β:Met complex (as defined by the structure coordinates of the complex as described herein) or a defining structural feature thereof.
4. Structurally Homologous Molecules, Molecular Complexes, and Crystal Structures
Structure coordinates can be used to aid in obtaining structural information about another crystallized molecule or molecular complex. The method of the disclosure allows determination of at least a portion of the three-dimensional structure of molecules or molecular complexes that contain one or more structural features that are similar to structural features of at least a portion of Met receptor or HGF β:Met complex. These molecules are referred to herein as “structurally homologous” to Met receptor or HGF β:Met. Similar structural features can include, for example, regions of amino acid identity, conserved active site or binding site motifs, and similarly arranged secondary structural elements (e.g. binding sites for HGF β, PSI domain, IPT domain, and propellor blades of the Sema domain).
Optionally, structural homology is determined by aligning the residues of the two amino acid sequences to optimize the number of identical amino acids along the lengths of their sequences; gaps in either or both sequences are permitted in making the alignment in order to optimize the number of identical amino acids, although the amino acids in each sequence must nonetheless remain in their proper order. Two amino acid sequences are compared using the BLAST program, version 2.0.9, of the BLAST 2 search algorithm, as described by Tatusova et al. (56), and available at http:www.ncbi.nlm.nih.gov/BLAST/. Preferably, the default values for all BLAST 2 search parameters are used, including matrix=BLOSUM62; open gap penalty=11, extension gap penalty=1, gap x_dropoff=50, expect=10, wordsize=3, and filter on. In the comparison of two amino acid sequences using the BLAST search algorithm, structural similarity is referred to as “identity.”
In some embodiments, a structurally homologous molecule is a protein that has an amino acid sequence sharing at least 80% identity with a native or recombinant amino acid sequence of Met, preferably an extracellular fragment of the Met receptor comprising a sequence of SEQ ID NO:3 or SEQ ID NO:10. An extracellular fragment of Met receptor comprising a sequence of SEQ ID NO:3 has amino acid substitutions at positions 304-308 to insert a thrombin cleavage site. In some embodiments, a Met receptor has a sequence of SEQ ID NO:3 and the structurally homologous molecule is a variant that has a % sequence identity to SEQ ID NO: 3 of at least 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88%, 89%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% or greater. In some embodiments, the Met receptor variant or structurally homologous molecule has one or more conservative amino acid substitutions, preferably only conservative amino acid substitutions and retains the structure of the binding site for HGF β. In some embodiments, the Met receptor variant has about 1-25 conservative amino amino acid substitutions, more preferably about 1-20 conservative amino acids substitutions, more preferably about 1-10 conservative amino acid substitions, more preferably about 1-5 conservative amino acid substitutions, and more preferably about 1-2 conservative amino acid substitutions. Preferably, the variant retains at least one or more domains such as the binding site for HGF β. More preferably, a protein that is structurally homologous to Met includes at least one contiguous stretch of at least 50 amino acids that shares at least 80% amino acid sequence identity with the analogous portion of the native or recombinant Met. Methods for generating structural information about the structurally homologous molecule or molecular complex are well known and include, for example, molecular replacement techniques.
Therefore, in another embodiment this disclosure provides a method of utilizing molecular replacement to obtain structural information about a molecule or molecular complex whose structure is unknown comprising:

- (a) generating an X-ray diffraction pattern from a crystallized molecule or molecular complex of unknown or incompletely known structure; and/or
- (b) applying at least a portion of the structural coordinates of the Met receptor or HGF β:Met complex complex to the X-ray diffraction pattern to generate a three-dimensional electron density map of the molecule or molecular complex whose structure is unknown or incompletely known.

By using molecular replacement, all or part of the structure coordinates of the Met receptor and/or HGF β:Met complex as provided by this disclosure can be used to determine the unsolved structure of a crystallized molecule or molecular complex more quickly and efficiently than attempting to determine such information ab initio. Coordinates of structural features of the Met receptor can be utilized including the Sema domain, PSI domain and the binding site for HGF β.
Molecular replacement can provide an accurate estimation of the phases for an unknown or incompletely known structure. Phases are one factor in equations that are used to solve crystal structures, and this factor cannot be determined directly. Obtaining accurate values for the phases, by methods other than molecular replacement, can be a time-consuming process that involves iterative cycles of approximations and refinements and greatly hinders the solution of crystal structures. However, when the crystal structure of a protein containing at least a structurally homologous portion has been solved, molecular replacement using the known structure provide a useful estimate of the phases for the unknown or incompletely known structure.
Thus, this method involves generating a preliminary model of a molecule or molecular complex whose structure coordinates are unknown, by orienting and positioning the relevant portion of the Met receptor and/or HGF β:Met complex within the unit cell of the crystal of the unknown molecule or molecular complex. This orientation or positioning is conducted so as best to account for the observed X-ray diffraction pattern of the crystal of the molecule or molecular complex whose structure is unknown. Phases can then be calculated from this model and combined with the observed X-ray diffraction pattern amplitudes to generate an electron density map of the structure. This map, in turn, can be subjected to established and well-known model building and structure refinement techniques to provide a final, accurate structure of the unknown crystallized molecule or molecular complex (see for example, Lattman, 1985. Methods in Enzymology 115:55-77).
Structural information about a portion of any crystallized molecule or molecular complex that is sufficiently structurally homologous to a portion of the Met receptor and/or HGF β:Met can be resolved by this method. In addition to a molecule that shares one or more structural features with the Met receptor, such as the Sema domain, and/or HGF β:Met as described above, a molecule that has similar bioactivity, such as the same catalytic activity, substrate specificity or ligand binding activity as the Met receptor and/or HGF β:Met, may also be sufficiently structurally homologous to a portion of the Met receptor and/or HGF β:Met to permit use of the structure coordinates of HGF β:Met to solve its crystal structure or identify structural features that are similar to those identified in the Met receptor described herein. It will be appreciated that amino acid residues in the structurally homologous molecule identified as corresponding to the Met receptor structural feature may have different amino acid numbering.
In one embodiment of the disclosure, the method of molecular replacement is utilized to obtain structural information about a molecule or molecular complex, wherein the molecule or molecular complex includes at least one HGF β:Met or Met receptor subunit or homolog. In the context of the present disclosure, a “structural homolog” of the Met receptor or HGF β:Met is a protein that contains one or more amino acid substitutions, deletions, additions, or rearrangements with respect to the amino acid sequence of HGF β:Met complex or Met receptor, but that, when folded into its native conformation, exhibits or is reasonably expected to exhibit at least a portion of the tertiary (three-dimensional) structure of at least a portion of the Met receptor and/or HGF β:Met complex. A portion of the Met receptor includes the Sema domain, PSI domain, IPT domains, and binding site for HGF β and combinations thereof.
For example, structurally homologous molecules can contain deletions or additions of one or more contiguous or noncontiguous amino acids, such as a loop or a domain. Structurally homologous molecules also include “modified” extracellular fragment of the Met receptor and/or HGF β:Met molecules that have been chemically or enzymatically derivatized at one or more constituent amino acid, including side chain modifications, backbone modifications, and N- and C-terminal modifications including acetylation, hydroxylation, methylation, amidation, and the attachment of carbohydrate or lipid moieties, cofactors, and like modifications. It will be appreciated that amino acid residues in the structurally homologous molecule identified as corresponding to extracellular fragment of the Met receptor or other structural feature of the Sema domain of the Met receptor may have different amino acid numbering.
A heavy atom derivative of HGF β:Met is also included as a HGF β:Met homolog. The term “heavy atom derivative” refers to derivatives of HGF β:Met produced by chemically modifying a crystal of HGF β or Met or both. In practice, a crystal is soaked in a solution containing heavy metal atom salts, or organometallic compounds, e.g., lead chloride, gold thiomalate, thiomersal or uranyl acetate, which can diffuse through the crystal and bind to the surface of the protein. The location(s) of the bound heavy metal atom(s) can be determined by X-ray diffraction analysis of the soaked crystal. This information, in turn, is used to generate the phase information used to construct three-dimensional structure of the protein (Blundell, et al., 1976, Protein Crystallography, Academic Press, San Diego, Calif.).
The structure coordinates of HGF β:Met provided by this disclosure are particularly useful in solving the structure of Met variants. Variants may be prepared, for example, by expression of Met cDNA previously altered in its coding sequence by oligonucleotide-directed mutagenesis as described herein. Variants may also be generated by site-specific incorporation of unnatural amino acids into Met proteins using known biosynthetic methods (Noren, et al., 1989, Science 244:182-88). In this method, the codon encoding the amino acid of interest in wild-type Met is replaced by a “blank” nonsense codon, TAG, using oligonucleotide-directed mutagenesis. A suppressor tRNA directed against this codon is then chemically aminoacylated in vitro with the desired unnatural amino acid. The aminoacylated tRNA is then added to an in vitro translation system to yield a mutant Met with the site-specific incorporated unnatural amino acid.
The structure coordinates of HGF β:Met are also particularly useful to solve or model the structure of crystals of HGF β, Met, HGF β variants, Met variants, or Met homologs or HGF β homologs which are co-complexed with a variety of ligands. HGF β is an inhibitor of full length HGF and can be used to identify or design other like inhibitors. This approach enables the determination of the optimal sites for interaction between ligand entities, including candidate HGF β or Met ligands. Potential sites for modification within the various binding sites of the molecule can also be identified. This information provides an additional tool for determining more efficient binding interactions, for example, increased hydrophobic or polar interactions, between Met and a ligand. For example, high-resolution X-ray diffraction data collected from crystals exposed to different types of solvent allows the determination of where each type of solvent molecule resides. Small molecules that bind tightly to those sites can then be designed and synthesized and tested for their Met affinity, such as inhibition activity.
In another embodiment, homology modeling can be conducted using the structural coordinates of HGF β and/or the Met receptor and a program designed to generate models of structures, such as Protein Explorer, Swiss Model, or RASMOL. The programs can provide a structural model of a homolog or variant of HGF β and/or Met by providing the structural coordinates such as provided in Table 2 and an alignment of the sequences.
All of the complexes referred to above may be studied using well-known X-ray diffraction techniques and may be refined versus 1.5-3.5 Å resolution X-ray data to an R-factor of about 0.30 or less using computer software, such as X-PLOR (Yale University, distributed by Molecular Simulations, Inc.)(see for example, Blundell, et al. 1976. Protein Crystallography, Academic Press, San Diego, Calif., and Methods in Enzymology, Vol. 114 & 115, H. W. Wyckoff et al., eds., Academic Press (1985)). This information may thus be used to optimize known Met modulators, and more importantly, to design new Met modulators.
The disclosure also includes the unique three-dimensional configuration defined by a set of points defined by the structure coordinates for a molecule or molecular complex structurally homologous to an extracellular fragment of the Met receptor or HGF β:Met complex as determined using the method of the present disclosure, structurally equivalent configurations, and magnetic storage media including such set of structure coordinates.
4. Homology Modeling
Using homology modeling, a computer model of a HGF β:Met complex or Met receptor homolog can be built or refined without crystallizing the homolog. First, a preliminary model of the homolog is created by sequence alignment with HGF β:Met or an extracellular fragment of Met, secondary structure prediction, the screening of structural libraries, or any combination of those techniques. Computational software may be used to carry out the sequence alignments and the secondary structure predictions. Programs available for such an analysis include Protein Explorer (eg available at molvissdsc.edu.protexpl.frontdoor.htm), Swiss Model (eg available at swissmodel.expasy.org) and RASMOL.Structural incoherences, e.g., structural fragments around insertions and deletions, can be modeled by screening a structural library for peptides of the desired length and with a suitable conformation. For prediction of the side chain conformation, a side chain rotamer library may be employed. If the homolog has been crystallized, the final homology model can be used to solve the crystal structure of the homolog by molecular replacement, as described above. Next, the preliminary model is subjected to energy minimization to yield an energy-minimized model. The energy-minimized model may contain regions where stereochemistry restraints are violated, in which case such regions are remodeled to obtain a final homology model. The homology model is positioned according to the results of molecular replacement, and subjected to further refinement including molecular dynamics calculations.
6. Methods for Identification of Modulators of HGF β:Met
Potent and selective ligands that modulate activity (antagonists and agonists) are identified using the three-dimensional model of the Met binding site for HGF β and/or other structural features produced using the coordinates of a cocrystal of HGF β with Met or a fragment thereof, such as provided in Table 2. Using this model, ligands that interact with the Met binding site for HGF β are identified, and the result of the interactions is modeled. In some embodiments, agents identified as candidate molecules for modulating the activity of HGF, Met and/or HGF β:Met can be screened against known bioassays. For example, the ability of an agent to inhibit the anti-apoptotic effects of Met can be measured using assays known in the art, or for example, the assays disclosed in the Examples. Using the modeling information and the assays described, one can identify agents that possess HGF, Met and/or HGF β:Met-modulating properties.
The methods of the disclosure also include methods of identifying molecules that mimic HGF β binding to a ligand (such as the Met receptor) or Met receptor binding to HGF β or both, but do not activate the HGF/Met signaling pathway. HGF β is an inhibitor of full length HGF and can be used to identify or design other like inhibitors. These molecules can be identified using the three-dimensional model of HGF β:Met complex using the coordinates of Tables 7 and 2.
In another embodiment, a candidate modulator can be identified using a biological assay such as binding to HGF and/or HGF β, modulating Met phosporylation or modulating HGF induced cell migration. The candidate modulator can then serve as a model to design similar agents and/or to modify the candidate modulator for example, to improve characteristics such as binding to HGF β or Met receptor. Design or modification of candidate modulators can be accomplished using the crystal structure coordinates and available software.
Binding Site and Other Structural Features
Applicants' disclosure provides information inter alia about the shape and structure of the structural binding site of Met for HGF β in the presence or absence of a modulator. Binding sites are of significant utility in fields such as drug discovery. The association of natural ligands or substrates with the binding sites of their corresponding receptors or enzymes is the basis of many biological mechanisms of action. Similarly, many drugs exert their biological effects through association with the binding sites of receptors and enzymes. Such associations may occur with all or any part of the binding site. An understanding of such associations helps lead to the design of drugs having more favorable associations with their target, and thus improved biological effects. Therefore, this information is valuable in designing potential modulators of HGF, Met and/or HGF β:Met binding sites, as discussed in more detail below.
The amino acid constituents of a Met or HGF β:Met binding site as defined herein are positioned in three dimensions. In one aspect, the structure coordinates defining a binding site of Met or HGF β:Met include structure coordinates of all atoms in the constituent amino acids; in another aspect, the structure coordinates of a binding site include structure coordinates of just the backbone atoms of the constituent atoms.
In some embodiments, the HGF β structural binding site for Met, for example, includes the amino acids highlighted in FIG. 5A as well as those identified in Table 3. In some embodiments, the amino acid residues identified in the HGF β binding site for Met comprise, consist essentially of, or consist of at least one or more or all amino acid residue corresponding to residues 513, 516, 533, 534, 537, 578, 619, 647, 649, 656, 669, 670, 673, 692, 693, 694, 695, 696, 697, 699 or 702 or mixtures thereof. In some embodiments, the amino acid residues identified in the HGF β binding site for Met comprise, consist essentially of, or consist of at least one or more or all amino acid residue corresponding to residues Y513, K516, R533, Q 534, P537, D 578, Y619, R647, K 649, E656, C669, E670, Y673, V692, P693, G694, R695, G 696, C697, 1699 or R702 or mixtures thereof, or conservative amino acid substitutions thereof. The cocrystalization studies indicate that amino acids residues 645 to 651 are better ordered in the HGF β:Met complex and further indicate that K649 contacts the Met receptor. In other embodiments, the amino acid residues identified in the HGF β binding site for Met comprise, consist essentially of, or consist of at least one or more or all amino acid residue corresponding to residues Y513, K516, R533, Q534, F536, P537, S538, R539, D578, Y619, R647, K649, E656, P668, C669, E670, Y673, V692, P693, G694, R695, C696, C697, 1699, R702 or mixtures thereof or conservative amino acid substitutions thereof. These residues may participate in polar or nonpolar interactions with charged residues on Met.
The term “Met structural binding site” includes all or a portion of a molecule or molecular complex whose shape is sufficiently similar to at least a portion of a binding site of Met for HGF β as to be expected to bind HGF β or related structural analogs. A structurally equivalent ligand binding site is defined by a root mean square deviation from the structure coordinates of the backbone atoms of the amino acids that make up binding sites in Met of at most about 0.70 Å, preferably about 0.5 Å. In some embodiments, the Met structural binding site for HGF β, for example, includes the amino acids highlighted in FIG. 5B as well as those identified in Table 3. In some embodiments, a structural binding site for HGF β on the Met receptor comprises, consists essentially of, or consists of at least one or more or all amino acid residues corresponding to residues 124-128, 148, 167, 190-192, 218, 220 to 223, 229 to 230, or 286, 414 or mixtures thereof. In some embodiments, a structural binding site for HGF β on the Met receptor comprises, consists essentially of, or consists of at least one or more or all amino acid residue corresponding to residues T124, Y125, Y126, D127, D128, H148, E 167, E168, D190, R191, F192, R218, K220, E221, T222, K223, D224, M227, L229, T230, I284, S286, D414, or mixtures thereof or conservative substitutions thereof. These residues may participate in polar interactions with charged residues on HGF β.
The binding site of HGF β or Met may be defined by those amino acids whose backbone atoms are situated within about 5 Å of one or more constituent atoms of a bound substrate or ligand. In yet another alternative, the binding site for HGF β on Met receptor can be defined by those amino acids whose backbone atoms are situated within a sphere centered on the coordinates representing the alpha carbon atom of amino acid E221 on the Met receptor, the sphere having a radius of about 5-6 Å, for example 5.8 Å.
Other structural features include the blades of the propellor of the Sema domain of the Met receptor and those that define the void in the center of the propellor, as well as the domains of the Met receptor including PSI and IPT domains. Amino acid residues that form these structural features can be found in FIG. 3.
Rational Drug Design
Computational techniques can be used to screen, identify, select, design ligands, and combinations thereof, capable of associating with Met or structurally homologous molecules. Candidate modulators of HGF, HGF β and/or Met may be identified using functional assays, such as binding to HGF β or Met, and novel modulators designed based on the structure of the candidate molecules so identified. Knowledge of the structure coordinates for Met or HGF β:Met permits, for example, the design, the identification of synthetic compounds, and like processes, and the design, the identification of other molecules and like processes, that have a shape complementary to the conformation of the Met and/or HGF β binding sites. In particular, computational techniques can be used to identify or design ligands, such as agonists and/or antagonists, that associate with a Met and/or HGF β binding site. Antagonists may bind to or interfere with all or a portion of an active site of Met, and can be competitive, non-competitive, or uncompetitive inhibitors. Once identified and screened for biological activity, these agonists, antagonists, and combinations thereof, may be used therapeutically and/or prophylactically, for example, to block Met activity and thus prevent the onset and/or further progression of diseases associated with Met activity. Structure-activity data for analogues of ligands that bind to or interfere with Met binding sites and/or HGF β binding sites can also be obtained computationally.
In some embodiments, an antagonist or agonist may be a molecule that mimics either HGF β or the Met receptor such that it binds to either the Met receptor or HGF β or both. HGF β is an inhibitor of full length HGF and can be used to identify or design other like inhibitors. In some embodiments, if the molecule is an antagonist, it binds to either receptor or both but does not activate the Met receptor. As the structural information provided herein indicates that the interaction of the HGF β with the Met receptor includes charge-charge interactions, in some embodiments, agonists or antagonists can be designed to include components that preserve and/or strengthen the charge charge interactions. Such antagonists or agonists would include components that are able to interact, for example, hydrogen bond with the charged amino acids found in either the HGF β or Met receptor binding site or both. In some embodiments, for HGF β, antagonist or agonist molecules are designed or selected that can interact with at least one or more or all amino acid residues that comprise, consist essentially of, or consist of amino acid residues corresponding to amino acid residues Y513, K516, R533, Y619, R647, R695, K649, R702, E656, E670, Y673, or D578 or mixtures thereof. In some embodiments, for the Met receptor, antagonist or agonist molecules are designed or selected that can interact with at least one or more or all amino acid residues that comprise, consist essentially of, or consist of amino acid residues corresponding to amino acid residues Y125, Y126, H148, R191, R218, K223, D127, D128, E168, F192, E221, or D224 or mixtures thereof.
In other embodiments, another criteria that may be utilized in the design of modulators is whether the modulator can fit into the binding site cavity on HGF β that is blocked by Met. The volume of that cavity is about 380 cubic angstroms. The volume of the cavity can be determined by placing atoms in the entrance of the pocket close to the surface and using a program like GRASP to calculate the volume of those atoms.
Data stored in a machine-readable storage medium that is capable of displaying a graphical three-dimensional representation of the structure of Met or a structurally homologous molecule or molecular complex, as identified herein, or portions thereof may thus be advantageously used for drug discovery. The structure coordinates of the ligand are used to generate a three-dimensional image that can be computationally fit to the three-dimensional image of Met, HGF β:Met complex, or a structurally homologous molecule. The three-dimensional molecular structure encoded by the data in the data storage medium can then be computationally evaluated for its ability to associate with ligands. When the molecular structures encoded by the data is displayed in a graphical three-dimensional representation on a computer screen, the protein structure can also be visually inspected for potential association with ligands.
One embodiment of the method of drug design involves evaluating the potential association of a candidate ligand with Met, such as HGF β, or a structurally homologous molecule or homologous complex, particularly with a binding site on the Met receptor. The method of drug design thus includes computationally evaluating the potential of a selected ligand to associate with any of the molecules or molecular complexes set forth above. This method includes the steps of: (a) employing computational means, for example, such as a programmable computer including the appropriate software known in the art or as disclosed herein, to perform a fitting operation between the selected ligand and a ligand binding site or a pocket nearby the ligand binding site of the molecule or molecular complex; and (b) analyzing the results of the fitting operation to quantify the association between the ligand and the ligand binding site. Optionally, the method further comprises analyzing the ability of the selected ligand to interact with charged amino acids in either the HGF β and/or Met receptor binding sites. Other structural features of the Met receptor and/or HGF β:Met complex can also be analyzed in the same manner.
In another embodiment, the method of drug design involves computer-assisted design of ligand that associate with Met, HGF β:Met, its homologs, or portions thereof. Ligands can be designed in a step-wise fashion, one fragment at a time, or may be designed as a whole or de novo. Ligands can be designed based on the structure of molecules that can modulate at least one biological function of HGF β or Met.
In some embodiments, to be a viable drug candidate, the ligand identified or designed according to the method must be capable of structurally associating with at least part of a Met binding site and/or HGF β binding site, and must be able, sterically and energetically, to assume a conformation that allows it to associate with the Met binding site and/or HGF β binding site. Non-covalent molecular interactions important in this association include hydrogen bonding, van der Waals interactions, hydrophobic interactions, and/or electrostatic interactions. In some embodiments, agents may contact at least one amino acid position in the Met binding site for HGF β. Conformational considerations include the overall three-dimensional structure and orientation of the ligand in relation to the ligand binding site, and the spacing between various functional groups of a ligand that directly interact with the Met binding site and/or HGF β binding site or homologs thereof.
Optionally, the potential binding of a ligand to a Met binding site and/or HGF β binding site is analyzed using computer modeling techniques prior to the actual synthesis and testing of the ligand. If these computational experiments suggest insufficient interaction and association between it and the Met binding site, and/or HGF β binding site testing of the ligand is obviated. However, if computer modeling indicates a strong interaction, the molecule may then be synthesized and tested for its ability to bind to or interfere with a Met binding site and/or HGF β binding site. Binding assays to determine if a compound actually modulates with Met activity can also be performed and are well known in the art.
Several methods can be used to screen ligands or fragments for the ability to associate with a Met binding site and/or HGF β binding site. This process may begin by visual inspection of, for example, a Met binding site and/or HGF β binding site on the computer screen based on the Met or HGF β:Met structure coordinates or other coordinates which define a similar shape generated from the machine-readable storage medium. Selected ligands may then be positioned in a variety of orientations, or docked, within the binding site. Docking may be accomplished using software such as QUANTA and SYBYL, followed by energy minimization and molecular dynamics with standard molecular mechanics force fields, such as CHARMM and AMBER.
Specialized computer programs may also assist in the process of selecting ligands. Examples include GRID (Hubbard, S. 1999. Nature Struct. Biol. 6:711-4); MCSS (Miranker, et al. 1991. Proteins 11:29-34) available from Molecular Simulations, San Diego, Calif.; AUTODOCK (Goodsell, et al. 1990. Proteins 8:195-202) available from Scripps Research Institute, La Jolla, Calif.; and DOCK (Kuntz, et al. 1982. J. Mol. Biol. 161:269-88) available from University of California, San Francisco, Calif.
For example, an examination of the structure of HGF β shows a tunnel or void formed by amino acid residues 634, 660-670, 673, 691 and 693-706. A molecule with an indole ring can fit within this void as determined by manual docking
Met binding ligands can be designed to fit a Met binding site and/or HGF β binding site, optionally as defined by the binding of a known modulator or one identified as modulating the activity of HGF β or Met. Examples of tyrosine kinase inhibitor compounds are disclosed in U.S. Pat. No. 6,696,463. There are many ligand design methods including, without limitation, LUDI (Bohm, 1992. J. Comput. Aided Molec. Design 6:61-78) available from Molecular Simulations Inc., San Diego, Calif.; LEGEND (Nishibata, Y., and Itai, A. 1993. J. Med. Chem. 36:2921-8) available from Molecular Simulations Inc., San Diego, Calif.; LeapFrog, available from Tripos Associates, St. Louis, Mo.; and SPROUT (Gillet, et al. 1993. J. Comput. Aided Mol. Design 7:127-53) available from the University of Leeds, UK.
Once a compound has been designed or selected by the above methods, the efficiency with which that ligand may bind to or interfere with a Met binding site and/or HGF β binding site may be tested and optimized by computational evaluation. For example, an effective Met binding site ligand and/or HGF β binding site should preferably demonstrate a relatively small difference in energy between its bound and free states (i.e., a small deformation energy of binding). Thus, an efficient Met binding site ligand should preferably be designed with a deformation energy of binding of not greater than about 10 to about 15 kcal/mole, such as about 12 kcal/mole, preferably not greater than about 8 to about 12 kcal/mole, such as about 10 kcal/mole, and more preferably not greater than about 5 to about 10 kcal/mole, such as about 7 kcal/mole. Met binding site and/or HGF β binding site ligands may interact with the binding site in more than one conformation that is similar in overall binding energy. In those cases, the deformation energy of binding is taken to be the difference between the free energy of the ligand and the average energy of the conformations observed when the ligand binds to the protein.
A ligand designed or selected as binding to or interfering with a Met binding site and/or HGF β binding site may be further computationally optimized so that in its bound state it would preferably lack repulsive electrostatic interaction with the target enzyme and with the surrounding water molecules. Such non-complementary electrostatic interactions include repulsive charge-charge, dipole-dipole, and charge-dipole interactions.
Specific computer software is available to evaluate compound deformation energy and electrostatic interactions. Examples of programs designed for such uses include: Gaussian 94, revision C (M. J. Frisch, Gaussian, Inc., Pittsburgh, Pa.); AMBER, version 4.1 (P. A. Kollman, University of California at San Francisco,); QUANTA/CHARMM (Molecular Simulations, Inc., San Diego, Calif.); Insight II/Discover (Molecular Simulations, Inc., San Diego, Calif.); DelPhi (Molecular Simulations, Inc., San Diego, Calif.); and AMSOL (Quantum Chemistry Program Exchange, Indiana University). These programs can be implemented, for instance, using a Silicon Graphics workstation, such as an Indigo2 with IMPACT graphics. Other hardware systems and software packages will be known to those skilled in the art.
Another approach encompassed by this disclosure is the computational screening of small molecule databases for ligands or compounds that can bind in whole, or in part, to a Met binding site and/or HGF β binding site. In this screening, the quality of fit of such ligands to the binding site may be judged either by shape complementarity or by estimated interaction energy (Meng, et al., 1992. J. Comp. Chem., 13:505-24). In addition, these small molecule databases can be screened for the ability to interact with the charged amino acids in the Met binding site and/or HGF β binding site as identified herein.
A compound that is identified or designed as a result of any of these methods can be obtained (or synthesized) and tested for its biological activity, for example, binding and/or inhibition of HGF and/or Met activity.
Another method involves assessing agents that are antagonists or agonists of the Met receptor. A method comprises applying at least a portion of the crystallography coordinates of a cocrystal of HGF β and Met, such as provided in Tables 7 and/or 2 to a computer algorithm that generates a three-dimensional model of HGF β:Met complex or the Met receptor suitable for designing molecules that are antagonists or agonists and searching a molecular structure database to identify potential antagonists or agonists. In some embodiments, a portion of the structural coordinates of a cocrystal of HGF β and Met, such as provided in Tables 7 and/or 2 that define a structural feature, for example, binding site for HGF β, may be utilized. The method may further comprise synthesizing or obtaining the agonist or antagonist and contacting the agonist or antagonist with the Met receptor and/or HGF β and selecting the antagonist or agonist that modulates the Met receptor and/or HGF β activity compared to a control without the agonist or antagonists and/or selecting the antagonist or agonist that binds to the Met receptor and/or HGF β. Activities of HGF and/or the Met receptor include phosphorylation of Met, stimulation of cell proliferation, and stimulation of cell migration.
A compound that is identified or designed as a result of any of these methods can be obtained (or synthesized) and tested for its biological activity, for example, binding to HGF β and/or Met receptor and/or modulation of HGF, HGF β and/or Met activity. Other modulators of the Met receptor include, for example, monoclonal antibodies directed against the Met receptor, peptide(s) that can modulate Met receptor function, or small-molecule compounds, such as organic and inorganic molecules, which can be identified with methods of the present disclosure.
7. Machine-Readable Storage Media
Transformation of the structure coordinates for all or a portion of Met or the HGF β:Met complex or one of its ligand binding sites, for structurally homologous molecules as defined below, or for the structural equivalents of any of these molecules or molecular complexes as defined above, into three-dimensional graphical representations of the molecule or complex can be conveniently achieved through the use of commercially-available software.
The disclosure thus further provides a machine-readable storage medium including a data storage material encoded with machine-readable data wherein a machine programmed with instructions for using said data displays a graphical three-dimensional representation of any of the molecule or molecular complexes of this disclosure that have been described above. In a preferred embodiment, the machine-readable data storage medium includes a data storage material encoded with machine-readable data wherein a machine programmed with instructions for using the abovementioned data displays a graphical three-dimensional representation of a molecule or molecular complex including all or any parts of a Met, Met ligand binding site, or Met-like ligand binding site, HGF β, HGF β binding site, or HGFβ: Met complex as defined above. In another preferred embodiment, the machine-readable data storage medium includes a data storage material encoded with machine readable data wherein a machine programmed with instructions for using the data displays a graphical three-dimensional representation of a molecule or molecular complex ±a root mean square deviation from the atoms of the amino acids of not more than 0.05 Å.
In an alternative embodiment, the machine-readable data storage medium includes a data storage material encoded with a first set of machine readable data which includes the Fourier transform of structure coordinates, and wherein a machine programmed with instructions for using the data is combined with a second set of machine readable data including the X-ray diffraction pattern of a molecule or molecular complex to determine at least a portion of the structure coordinates corresponding to the second set of machine readable data.
For example, a system for reading a data storage medium may include a computer including a central processing unit (“CPU”), a working memory which may be, for example, RAM (random access memory) or “core” memory, mass storage memory (such as one or more disk drives or CD-ROM drives), one or more display devices (e.g., cathode-ray tube (“CRT”) displays, light emitting diode (“LED”) displays, liquid crystal displays (“LCDs”), electroluminescent displays, vacuum fluorescent displays, field emission displays (“FEDs”), plasma displays, projection panels, etc.), one or more user input devices (e.g., keyboards, microphones, mice, track balls, touch pads, etc.), one or more input lines, and one or more output lines, all of which are interconnected by a conventional bidirectional system bus. The system may be a stand-alone computer, or may be networked (e.g., through local area networks, wide area networks, intranets, extranets, or the internet) to other systems (e.g., computers, hosts, servers, etc.). The system may also include additional computer controlled devices such as consumer electronics and appliances.
Input hardware may be coupled to the computer by input lines and may be implemented in a variety of ways. Machine-readable data of this disclosure may be inputted via the use of a modem or modems connected by a telephone line or dedicated data line. Alternatively or additionally, the input hardware may include CD-ROM drives or disk drives. In conjunction with a display terminal, a keyboard may also be used as an input device.
Output hardware may be coupled to the computer by output lines and may similarly be implemented by conventional devices. By way of example, the output hardware may include a display device for displaying a graphical representation of a binding site of this disclosure using a program such as QUANTA as described herein. Output hardware might also include a printer, so that hard copy output may be produced, or a disk drive, to store system output for later use.
In operation, a CPU coordinates the use of the various input and output devices, coordinates data accesses from mass storage devices, accesses to and from working memory, and determines the sequence of data processing steps. A number of programs may be used to process the machine-readable data of this disclosure. Such programs are discussed in reference to the computational methods of drug discovery as described herein. References to components of the hardware system are included as appropriate throughout the following description of the data storage medium.
Machine-readable storage devices useful in the present disclosure include, but are not limited to, magnetic devices, electrical devices, optical devices, and combinations thereof. Examples of such data storage devices include, but are not limited to, hard disk devices, CD devices, digital video disk devices, floppy disk devices, removable hard disk devices, magneto-optic disk devices, magnetic tape devices, flash memory devices, bubble memory devices, holographic storage devices, and any other mass storage peripheral device. It should be understood that these storage devices include necessary hardware (e.g., drives, controllers, power supplies, etc.) as well as any necessary media (e.g., disks, flash cards, etc.) to enable the storage of data.
8. Therapeutic Use
HGF, Met, and/or HGF β:Met complex modulator compounds obtained by methods of the invention are useful in a variety of therapeutic settings. For example, Met antagonists designed or identified using the crystal structure of an extracellular fragment of Met or HGF β:Met complex can be used to treat disorders or conditions, where inhibition or prevention of Met binding or activity is indicated.
Likewise, Met agonists designed or identified using the crystal structure of the HGF β:Met complex or an extracellular fragment of Met can be used to treat disorders or conditions, where induction or stimulation of Met activity is indicated.
An indication can be, for example, inhibition or stimulation of Met phosphorylation and the concomitant activation of a complex set of intracellular pathways that lead to cell growth, differentiation, and migration in a variety of cell types. The ability of HGF to stimulate mitogenesis, cell motility, and matrix invasion gives it and the Met receptor a central role in angiogenensis, tumorogenesis and tissue regeneration. Another indication can be, for example, in inhibition or stimulation of embryonic development. Still another indication can be, for example, in inhibition or stimulation of tissue regeneration. Another indication can be, for example, in inhibition of angiogenesis, mitogenesis and/or vasculogenesis. Expression of HGF has been associated with thyroid cancer, colon cancer, lymphoma, prostate cancer, and multiple myeloma. Yet another indication can be, for example, in inhibition or stimulation of the HGF/Met signaling pathway. Still yet another indication can be, for example, in inhibition of invasive tumor growth and metastasis.
Met and/or HGF β:Met complex antagonists are also useful as chemosensitizing agents, useful in combination with other chemotherapeutic drugs, in particular, drugs that induce apoptosis. Examples of other chemotherapeutic drugs that can be used in combination with chemosensitizing Met inhibitors include topoisomerase I inhibitors (e.g., camptothesin or topotecan), topoisomerase II inhibitors (e.g., daunomycin and etoposide), alkylating agents (e.g., cyclophosphamide, melphalan and BCNU), tubulin-directed agents (e.g., taxol and vinblastine), and biological agents (e.g., antibodies such as anti CD20 antibody, IDEC 8, immunotoxins, and cytokines). Examples of other chemotherapeutic drugs that can be used in combination with chemosensitizing HGF β inhibitors include topoisomerase I inhibitors (e.g., camptothecin or topotecan), topoisomerase II inhibitors (e.g., daunomycin and etoposide), alkylating agents (e.g., cyclophosphamide, melphalan and BCNU), tubulin-directed agents (e.g., taxol and vinblastine), and biological agents (e.g., antibodies such as anti CD20 antibody, IDEC 8, anti-VEGF antibody, immunotoxins, and cytokines). Other examples of chemotherapeutic agents include alkylating agents such as thiotepa and CYTOXAN® cyclosphosphamide; alkyl sulfonates such as busulfan, improsulfan and piposulfan; aziridines such as benzodopa, carboquone, meturedopa, and uredopa; ethylenimines and methylamelamines including altretamine, triethylenemelamine, trietylenephosphoramide, triethiylenethiophosphoramide and trimethylolomelamine; acetogenins (especially bullatacin and bullatacinone); a camptothecin (including the synthetic analogue topotecan); bryostatin; callystatin; CC-1065 (including its adozelesin, carzelesin and bizelesin synthetic analogues); cryptophycins (particularly cryptophycin I and cryptophycin 8); dolastatin; duocarmycin (including the synthetic analogues, KW-2189 and CBI-TMI); eleutherobin; pancratistatin; a sarcodictyin; spongistatin; nitrogen mustards such as chlorambucil, chlornaphazine, cholophosphamide, estramustine, ifosfamide, mechlorethamine, mechlorethamine oxide hydrochloride, melphalan, novembichin, phenesterine, prednimustine, trofosfamide, uracil mustard; nitrosureas such as carmustine, chlorozotocin, fotemustine, lomustine, nimustine, and ranimnustine; antibiotics such as the enediyne antibiotics (e.g., calicheamicin, especially calicheamicin gamma1I and calicheamicin omegaI1 (see, e.g., Agnew, Chem Intl. Ed. Engl., 33: 183-186 (1994)); dynemicin, including dynemicin A; bisphosphonates, such as clodronate; an esperamicin; as well as neocarzinostatin chromophore and related chromoprotein enediyne antibiotic chromophores), aclacinomysins, actinomycin, authramycin, azaserine, bleomycins, cactinomycin, carabicin, carminomycin, carzinophilin, chromomycinis, dactinomycin, daunorubicin, detorubicin, 6-diazo-5-oxo-L-norleucine, ADRIAMYCIN® doxorubicin (including morpholino-doxorubicin, cyanomorpholino-doxorubicin, 2-pyrrolino-doxorubicin and deoxydoxorubicin), epirubicin, esorubicin, idarubicin, marcellomycin, mitomycins such as mitomycin C, mycophenolic acid, nogalamycin, olivomycins, peplomycin, potfiromycin, puromycin, quelamycin, rodorubicin, streptonigrin, streptozocin, tubercidin, ubenimex, zinostatin, zorubicin; anti-metabolites such as methotrexate and 5-fluorouracil (5-FU); folic acid analogues such as denopterin, methotrexate, pteropterin, trimetrexate; purine analogs such as fludarabine, 6-mercaptopurine, thiamiprine, thioguanine; pyrimidine analogs such as ancitabine, azacitidine, 6-azauridine, carmofur, cytarabine, dideoxyuridine, doxifluridine, enocitabine, floxuridine; androgens such as calusterone, dromostanolone propionate, epitiostanol, mepitiostane, testolactone; anti-adrenals such as aminoglutethimide, mitotane, trilostane; folic acid replenisher such as frolinic acid; aceglatone; aldophosphamide glycoside; aminolevulinic acid; eniluracil; amsacrine; bestrabucil; bisantrene; edatraxate; defofamine; demecolcine; diaziquone; elformithine; elliptinium acetate; an epothilone; etoglucid; gallium nitrate; hydroxyurea; lentinan; lonidainine; maytansinoids such as maytansine and ansamitocins; mitoguazone; mitoxantrone; mopidanmol; nitraerine; pentostatin; phenamet; pirarubicin; losoxantrone; podophyllinic acid; 2-ethylhydrazide; procarbazine; PSK® polysaccharide complex (JHS Natural Products, Eugene, Oreg.); razoxane; rhizoxin; sizofiran; spirogermanium; tenuazonic acid; triaziquone; 2,2′,2″-trichlorotriethylamine; trichothecenes (especially T-2 toxin, verracurin A, roridin A and anguidine); urethan; vindesine; dacarbazine; mannomustine; mitobronitol; mitolactol; pipobroman; gacytosine; arabinoside (“Ara-C”); cyclophosphamide; thiotepa; taxoids, e.g., TAXOL® paclitaxel (Bristol-Myers Squibb Oncology, Princeton, N.J.), ABRAXANE™ Cremophor-free, albumin-engineered nanoparticle formulation of paclitaxel (American Pharmaceutical Partners, Schaumberg, Ill.), and TAXOTERE® doxetaxel (Rhône-Poulenc Rorer, Antony, France); chloranbucil; GEMZAR® gemcitabine; 6-thioguanine; mercaptopurine; methotrexate; platinum analogs such as cisplatin and carboplatin; vinblastine; platinum; etoposide (VP-16); ifosfamide; mitoxantrone; vincristine; NAVELBINE® vinorelbine; novantrone; teniposide; edatrexate; daunomycin; aminopterin; xeloda; ibandronate; CPT-11; topoisomerase inhibitor RFS 2000; difluorometlhylornithine (DMFO); retinoids such as retinoic acid; capecitabine; and pharmaceutically acceptable salts, acids or derivatives of any of the above.
Also included in the definition of “chemotherapeutic agent” above are anti-hormonal agents that act to regulate or inhibit hormone action on tumors such as anti-estrogens and selective estrogen receptor modulators (SERMs), including, for example, tamoxifen (including NOLVADEX® tamoxifen), raloxifene, droloxifene, 4-hydroxytamoxifen, trioxifene, keoxifene, LY117018, onapristone, and FARESTON toremifene; aromatase inhibitors that inhibit the enzyme aromatase, which regulates estrogen production in the adrenal glands, such as, for example, 4(5)-imidazoles, aminoglutethimide, MEGASE® megestrol acetate, AROMASIN® exemestane, formestanie, fadrozole, RIVISOR® vorozole, FEMARA® letrozole, and ARIMIDEX® anastrozole; and anti-androgens such as flutamide, nilutamide, bicalutamide, leuprolide, and goserelin; as well as troxacitabine (a 1,3-dioxolane nucleoside cytosine analog); antisense oligonucleotides, particularly those which inhibit expression of genes in signaling pathways implicated in abherant cell proliferation, such as, for example, PKC-alpha, Ralf and H-Ras; ribozymes such as a VEGF expression inhibitor (e.g., ANGIOZYME® ribozyme) and a HER2 expression inhibitor; vaccines such as gene therapy vaccines, for example, ALLOVECTIN® vaccine, LEUVECTIN™ vaccine, and VAXID® vaccine; PROLEUKIN® rIL-2; LURTOTECAN® topoisomerase 1 inhibitor; ABARELIX® rmRH; and pharmaceutically acceptable salts, acids or derivatives of any of the above.
9. Other Uses
The HGF β chain, or variants thereof, form cocrystals with the Met receptor in accord with the methods described herein. The crystals also are useful to store and/or deliver HGF β-chain or Met receptor molecules. HGF β is useful as an inhibitor of full length HGF and can be used to identify or design other like inhibitors. HGF β:Met complex may be useful as a standards in assays including diagnostic assays. Crystals can be prepared and used to store HGF β-chain Met receptor complexes for later use.
A variety of methods are known to those of skill in the art for formation of crystals. In some embodiments, for crystals prepared for storage, the crystal size and structure does not have to be so uniform or homogenous as for X-ray diffraction. In other embodiments, the crystals effectively diffract x-rays to a resolution of 5 Å or better. Typically, a purified polypeptide is contacted with a precipitant in the presence of a buffer. Precipitants include salts, polymers, or organic molecules. Organic precipitants include isopropanol, ethanol, hexanediol, and 2-methyl-2,4-pentanediol. Polymeric precipitants include polyethylene glycol and polyamines. Salts used include ammonium sulfate, sodium citrate, sodium acetate, ammonium dichloride, sodium chloride and magnesium formate. Many buffers can be utilized and are known to those of skill in the art.
In some cases, crystals can be cross-linked to one another. Such cross-linking may enhance the stability of the crystal. Methods of cross-linking crystals are know to those of skill in the art and have been described, for example, in U.S. Pat. No. 5,849,296.
The crystals can be maintained in crystallization solution, they can be dried, or combined with other carriers and/or other ingredients to form compositions and formulations. In some embodiments, the crystals can be combined with a polymeric carrier for stability and sustained release. Formulations of crystals of proteins, such as enzymes, receptors, antibodies, and like molecules, or fragments thereof, can include at least one ingredient or excipient. Ingredient or expedients are known to those of skill in the art and include acidifying agents, aerosol propellants, alcohol denaturants, alkalizing agents, anti-caking agents, antifoaming agents, microbial preservatives, anti-antioxidants, buffering agents, lubricants, chelating agents, colors, desiccants, emulsifying agents, filtering aids, flavors and perfumes, humectants, ointments, plasticizers, solvents (e.g. oils or organic), sorbents, carbon dioxide sorbents, stiffening agents, suppository bases, suspending or viscosity increasing agents, sweetening agents, tablet binders, table or capsule diluents, tablet disintegrants, tablet or capsule lubricants, tonicity agent, flavored or sweetened vehicles, oleaginous vehicles, solid carrier vehicles, water repelling agent, and wetting or solubilizing agents.
In some embodiments, the ingredients enhance storage stability. In other embodiments, the ingredient or excipient is preferably selected from the group consisting of albumin, sucrose, trehalose, lactitol, gelatin, and hydroxyproyl-β-cyclodextran.
All publications, patents, and patent documents are incorporated by reference herein, as though individually incorporated by reference. The disclosure has been described with reference to various specific and preferred embodiments and techniques. However, it should be understood that many variations and modifications can be made while remaining within the spirit and scope of the disclosure.

EXAMPLE 1

Protein Expression and Purification

For crystallization, we used a construct of the Met receptor that contained residues 25 to 567 and an additional C-terminal (His)₈-tag. In addition, the cleavage site after residue Arg308, present in the Met receptor family but not in the Sema domain of the Semaphorins or plexins, was replaced with a thrombin cleavable site. This exchange (residues 304 to 308 were exchanged from KRKKR (SEQ ID NO:4) to LVPRG (SEQ ID NO:5)) was introduced since native Met expressed in insect cells was partially cleaved and not homogeneous. Mutation of the cleavage site allowed for the production of homogeneous protein that depending on treatment with thrombin was cleaved or uncleaved. The complex presented here was obtained with the unprocessed, single chain Met.
The HGF β-chain protein used for crystallization begins with residue Val495 (the N-terminal residue obtained after maturation of single chain HGF), and has one alteration from the natural sequence: in full length, mature HGF, the α- and β-chains are covalently tethered by a disulfide bridge putatively formed between Cys487 and Cys604 (Donate et al., 1994). In order to prevent artificial dimerization of HGF β-chains during purification and crystallization, Cys604 was replaced with serine. (SEQ ID NO:1) The complex of the HGF β-chain and the Met fragment was formed in solution, purified using size exclusion chromatography and set up for crystallization trials.
Materials and Methods
The cDNA for the full length Met receptor was kindly provided by D. Wickramasinghe. PCR was carried out on the region encoding residues 25-567 of the Met receptor. A 2-step overlapping PCR scheme was used to introduce the thrombin cleavage site (LVPRG) (SEQ ID NO:5) and remove the native sequence (KRKKR) (SEQ ID NO:4). An N-terminal primer added overlapping sequence with the C-terminus of the insect cell secretion signal present in the pAcGP67A vector (BD Biosciences). A C-terminal primer contained coding sequence for (His)₈and a NotI restriction site added directly onto the C-terminus. For placement into the pAcGP67A vector, an additional PCR was carried out on the coding region for the insect cell secretion signal, with additional overlapping sequence from the N-terminus of our Met construct. A final PCR was done to directly fuse the C-terminus of the secretion signal to the N-terminus of our Met construct. This PCR product, as well as pAcGP67A, were digested with SpeI and NotI. Insert was combined with vector at a 3:1 ratio, ligated, and transformed into XL-1 Blue cells (Stratagene).
Purified plasmid DNA (pAcGP67A plus Met Sema and PSI domain) was transfected into Sf9 insect cells according to the manufacturer's protocol (BD Biosciences). Viral stock was amplified 3 times before use in protein expression. For expression, IL of Hi5 insect cells growing in ESF 921 media (Protein Expression, LLC) at a density of 5×10⁵cells/mL were infected with 10 mL of viral stock from the 3^rdamplification and incubated at 27° C. for 72 hours. Cells were then removed from the supernatant by centrifugation at 3000 g for 15 minutes. 1 mM of NiCl₂, 5 mM of CaCl₂, and 50 mM Tris pH 8.0 were added to the supernatant. The supernatant was then filtered through a 0.2 μm vacuum filter. Supernatant was applied to a 2 mL Ni-NTA column (Qiagen) by gravity flow, followed by 20 mL of wash buffer (50 mM Tris pH 8.0, 500 mM NaCl, 5 mM imidazole). Protein was eluted with a buffer containing 50 mM Tris 8.0, 300 mM NaCl, 250 mM imidazole. Fractions containing Met were identified by SDS-PAGE analysis and pooled, concentrated to 500 μL, and loaded onto a Superdex S-75 gel filtration column (Amersham Biosciences) equilibrated with 50 mM Tris 8.0, 500 mM NaCl. The final yield for Met (Sema and PSI domain) was approximately 0.25 mg/L of insect cell supernatant.
The amino acid sequence of an extracellular fragment of Met is shown in Table 6. (SEQ ID NO:3). Another embodiment of an extracellular fragment of Met comprises an amino acid sequence of SEQ ID NO:10 and is shown in FIG. 3.
HGF β proteins were expressed in insect cells using baculovirus secretion vector pAcGP67 (Pharmingen, San Diego, Calif.). All constructs contained a His₆tag at the carboxy terminus and were purified to homogeneity (>95% purity) by Ni NTA metal chelate and gel filtration chromatography. For wildtype HGF β, a cDNA fragment encoding the HGF β-chain from residues Val495 [c16] to Ser728 [c250] was cloned by PCR such that Val495 [c16] was inserted immediately after the secretion signal sequence. Site-directed mutagenesis was carried out using QuikChange™ (Stratagene, La Jolla, Calif.) with oligonucleotide 5′CCTAATTATGGATCCACAATTCCTG3′ (SEQ ID NO:6) to make HGF β containing a Cys604 to Ser mutation (HGF β). The cysteine was not altered in this construct to allow putative disulfide formation between Cys487 and Cys604. Wildtype HGF β (SEQ ID NO:14) refers to the native sequence and HGF β (SEQ ID NO:1) refers to the C604S mutant. Numbering is as follows: full length HGF sequence starting with MWV . . . as numbers 1-3 [chymotrypsinogen numbering is shown in the brackets]. It will be readily apparent that the numbering of amino acids in other isoforms of HGF β may be different than that of the HGF β numbering disclosed herein. The disclosure provides sequential numbering based on sequence only. In embodiments, an isoform may have structural “differences”, for example, if it carries insertion(s) or deletion(s) relative to the HGF β reference sequence. The chymotrypsinogen numbering convention may be useful for comparision to workers in the field.
The amino acid sequence of a HGF β is shown in Table 4 (SEQ ID NO:1) and Table 8 (SEQ ID NO:14).
Baculovirus vectors containing the desired inserts were transfected into Spodoptera frugiperda (Sf9) cells on plates in TNM-FH media via the Baculogold™ Expression System according to manufacturer's instructions (Pharmingen, San Diego, Calif.). After 2-4 rounds of virus amplification, 10 mL of viral stock was used to infect 1 L of High Five™ cells (Invitrogen, San Diego, Calif.) in suspension at 5×10⁵cells/mL in TNM-FH media. Cultures were incubated at 27° C. for 72 h before harvesting the culture media by centrifugation at 8,000×g for 15 min. Cell culture media was applied to a 4 mL Ni-NTA agarose column (Qiagen, Valencia, Calif.). After washing with 4 column volumes of 50 mM Tris.HCl, pH 8.0, 500 mM NaCl, 5 mM imidazole, HGF β proteins were eluted with 50 mM Tris HCl pH 8.0, 500 mM NaCl, 500 mM imidazole. The eluate was pooled and applied to a Superdex™-200 column (Amersham Biosciences, Piscataway, N.J.) equilibrated in 10 mM HEPES pH 7.2, 150 mM NaCl, 5 mM CaCl₂. Protein peaks were collected and concentrated using a Centriprep™ YM-10 (Millipore, Bedford, Mass.). Fractions were analyzed by 12% SDS-PAGE stained with Coomassie blue.
Met was combined with HGF β-chain in a 1:1.5 ratio and concentrated for loading onto a Superdex S-200 gel filtration column (Amersham Biosciences) equilibrated with 10 mM Tris 8.0, 250 mM NaCl. Elution fractions were assayed with SDS-PAGE, and those containing the complex were pooled. Buffer exchange into 10 mM Tris 8.0, 125 mM NaCl was carried out, and the complex was then concentrated to 10 mg/mL for crystallization trials. Although crystals grew without deglycosylation, diffraction was enhanced after deglycosylating the Met protein. For this, Met, previously purified using Nickel chromatography as described above, was mixed with a combination of PNGase F (Roche) and Endoglycosidase A (Roche) at 1:100 enzyme:Met concentration and incubated at room temperature for 3 hours. Met was then combined with HGF β-chain, concentrated, and loaded onto a gel filtration column as described above for the non-deglcosylated material.

EXAMPLE 2

Crystallization, Data Collection and Refinement

Met/HGF β-chain crystallized at 19° C. in 4 μL hanging drops in a 1:1 ratio of protein to mother liquor, suspended over mother liquor (12-15% PEG 10,000, Tris pH 8.0). Crystals grew to approximately 100 μm×200 μm×200 μm in 3 to 7 days. For data collection, crystals were placed in a solution of mother liquor containing 25% xylitol for 30 seconds, and then flash frozen in liquid N₂.

Data were collected at CHESS beamline A1 to 3.2 Å resolution and processed using the HKL package (Otwinowski et al., 1997). The crystals belonged to space group P2 ₁2₁2 with cell parameters of a=137.1 Å, b=186.4 Å, and c=66.7 Å and contained 1 complex of Met:HGF β-chain in the asymmetric unit and thus have a solvent content of about 75%. The structure was solved by molecular replacement with the program AMoRe (Navaza 1994), with the crystal structure of HGF β-chain alone (structural coordinates available at RCS Protein Databank, Accession No: PDBIUX3) as a search model. Using data from 8 Å to 4 Å yielded a clear solution in the rotation and translation functions and the best solution was subjected to rigid body refinement in program Refmac (CCP4, 1994). Solvent flattening, which due to the high crystal solvent content led to dramatic improvements in the quality of the phases, yielded maps that were of sufficient quality to recognize the β-propeller of the Sema domain and allowed for building the Met receptor without the use of any additional models. Subsequent rounds of model building with program 0 (Jones et al., 1991) and further refinement with program Refmac resulted in the final model with an Rfree and Rcryst of 27.0% and 20.9%, respectively, for all data between 30 Å and 3.2 Å.

TABLE 1


Data Collection and Refinement Statistics for a 1:1 complex of
the HGF β-chain with the Sema domain of the Met Receptor.

Data Collection

Resolution (Å)	50-3.2 (3.3-3.2)^a
R_sym ^b	0.058 (0.586)^a
Number of observations	98,834
Unique reflections	28,312
Completeness (%)	99.4 (100.0)^a
Refinement
Resolution (Å)	30-3.2
Number of reflections	26830
Final R^c, R_free(F > 0)	0.209, 0.270
Number of residues	727
Number of solvent	0
molecules
Number of non-H	5728
atoms
Rmsd bonds (Å)	0.013
Rmsd angles (°)	1.6
Space Group	P2	₁2₁2

^aNumbers in parentheses refer to the highest resolution shell.
^bR_sym= Σ\|I − <I>\|/ΣI. <I> is the average intensity of symmetry related observations of a unique reflection.
^cR = Σ\|F₀− F_c\|/ΣF_o. R_freeis calculated as R, but for 5% of the reflections excluded from all refinement.

Results

The crystal structure of HGFβ: Met was analyzed to identify amino acid positions involved in binding and/or activation of the Met receptor by HGF β.
Structure of HGF β
The α-chain of HGF shares close to 40% sequence identity with the protease domain of plasmin, a trypsin-like serine protease. Structurally, these enzymes can be described as globular proteins composed of two antiparallel β-barrel domains (FIG. 1A). Both of the β-barrels share the same general topology and are formed by six antiparallel β-strands, with the N-terminal four strands folding into a Greek key motif, followed by two strands that form a hairpin. HGF, like serine proteases, is expressed as a zymogen-like precursor. For serine proteases, structural studies have shown that insertion of the N-terminus resulting from the maturation process leads to allosteric rearrangments within the binding site for the protease substrate (Perona and Craig, 1995; Hedstrom 2002). In serine proteases, the newly formed N-terminus forms a salt bridge with a nearby aspartate, which leads to the formation of the oxyanion hole via the backbone NH's of two neighboring residues and the creation of a part of the S1 pocket (FIG. 1). The ‘activated’ form of the HGF β-chain, as seen in the structure presented here, is very similar to the mature form of serine proteases: superposition with plasmin (pdb-code 1 BML) yields an rmsd of about 1.3 Å for 212 C_α pairs. Superposition between HGF β-chain and plasminogen (pdb-code 1QRZ) reveal differences in their ‘activation domain’ (Freer et al., 1970) and only 198 C_α pairs can be aligned well.
As with serine proteases, the N-terminal amine of Val495 is inserted into the core of the C-terminal β-barrel and forms a salt bridge with the carboxyl group of Asp672, which corresponds to Asp 194 in plasmin, presumably leading to similar rearrangements, which have been characterized in serine proteases. The region in HGF corresponding to this so-called ‘activation domain’, i.e., the loops that undergo conformational changes in serine proteases (Freer et al., 1970; Huber and Bode, 1978), forms part of the binding surface with Met, discussed below. Therefore, proper display of the residues that interact with Met requires maturation of HGF.
After maturation, the α- and β-chains of HGF remain connected via a disulfide bond. Based on alignments of the kringle domains K1 to K4 of HGF and macrophage stimulating protein (MSP), the two cysteine residues responsible for the formation of this disulfide bond were identified as Cys487 on the α-chain of HGF and Cys604 on the β-chain (Donate et al., 1994). The crystal structure, however, raises the possibility of an alternative cysteine residue as the anchor for the HGF α-chain. The HGF β-chain has two (2) cysteine residues that do not have partners for the formation of disulfide bridges within the β-chain. Neither is conserved in plasmin or MSP and both are located on the periphery of the protein and are at least partially solvent exposed; either could be potential partners for the formation of a disulfide bond with the α-chain while the other remains unpaired. The superposition of the plasmin structure that contains part of the α-chain (FIG. 1B), and the HGF β-chain structure presented here, shows that the distance between the C-terminus of the plasmin β-chain and Cys604 of the HGF β-chain is 27 Å and thus only slightly shorter than the respective distance between the plasmin α-chain C-terminus and Cys561 (33 Å) (FIG. 1B). In addition, the sequence alignment between plasmin, MSP, and HGF (FIG. 1C) shows that the α-chain cysteine forming the disulfide bond in plasmin and MSP is 13 and 15 residues away from the cleavage site in those proteins respectively, but there are only 7 residues in HGF to span the distance from Cys487 to the cleavage site. Therefore, due to distance requirements, the C-terminus of the HGF α-chain cannot follow the same path on the surface of the β-chain as it does in plasmin or MSP. Continuing work seeks to clarify which of the two free cysteine residues in HGF β forms the disulfide bond with the α-chain of HGF.
Met Stucture
The Sema domain of Met forms 7-bladed β-propeller with a diameter of a little more than 50 Å. The overall shape of the domain resembles a funnel with an inner diameter of about 25 Å between main chain atoms at the wide portion and 10 Å in the narrowest part (FIG. 2). Generally, in β-propellers, each of the blades is formed by 4 antiparallel β-strands with strand A in the center of the propeller followed by strands B and C, and with strand D forming the outermost strand of the blade. The blades are arranged in a circular fashion, with the N-terminal strand forming strand D of the last blade, thus closing the propeller and stabilizing the overall structure (FIG. 2A). The AB and CD loops of each blade of the Met Sema domain form the relatively flat ‘bottom’ face, and the generally longer BC and DA loops form the ‘top’ face of the propeller (FIG. 2B). In Met, the position of the 6th and the 7th blade are off-center, with blade 7 being closer to the center of the barrel and blade 6 more distant. This gives the domain an overall oval shape.
The β-propeller of the Met Sema domain is structurally most closely related to the recently reported crystal structures of Sema4D (Love et al., 2003) and Sema3A (Antipenkov et al., 2003). With the exception of the D-strands in blades 3 and 5, the core of Sema4D and the Met Sema domain align well (FIGS. 3 and 4) and the superposition of residues 40 to 519 with the Sema domain of Sema4D results in an rmsd of 1.6 Å for 303 atom pairs (FIG. 4). The residues that form strand D5 in Sema4A are hydrogen bonding to strand D4 in Met, thus the 4th blade of Met contains an extra strand while blade 5 is missing its strand D. While the core of both proteins align well, the loops contain a number of insertions or deletions and generally adopt very different conformations. For example, the Sema domains of Met and of Sema4D both have an insert of about 20 residues following strand D1. In Met, these residues form a short antiparallel two-stranded β-sheet, while Sema4D has an α-helix (FIGS. 3 and 4). Of the 24 loops that connect the various strands, only 3 have no insertions or deletions when comparing Met with Sema4D or Sema3A (FIG. 3). Interestingly, both the Semaphorins and the Met receptor have their largest insertion between strands C5 and A6; however, these inserts are not related in structure or sequence to each other. In Sema3A, this insert is involved in dimer formation and has been shown to be important for neuropilin binding (Antipenko et al., 2003). In the Met Sema domain, some of the residues within the insert are disordered and not included in our model (see FIG. 2). The function of the insert in Met is not known but its proximity to the HGF β-chain binding site, discussed below, suggests that it might be involved in binding to the α-chain of HGF.
The loop containing the cleavage site between the α- and β-chain of Met connects strand D4 to A5; it is disordered in the electron density. After processing of native Met, the α-chain, which forms the N-terminal 4 blades of the Sema domain, and the β-chain remain connected via at least 2 disulfide bonds. One disulfide bond is formed between residues Cys298 on strand D4 and Cys363 on C5, and the second is formed between Cys282 (D3) and Cys409. This last cysteine is positioned in a disordered region of the insert after blade 4. The electron density does not allow tracing of the main chain in this area but there is sufficient density in the area of the Sγ position to suggest that the disulfide bond is at least partially formed. With the exception of the N-terminal Cys26, which is disordered in the presently disclosed crystal structure and has no potential partner in the construct that was used for crystallization, all cysteine residues are engaged in disulfide bonds. It is unclear if Cys26 remains unpaired in the context of full length Met receptor or if it forms a disulfide bond with another cysteine that resides in the IPT domains. Besides the two disulfide bonds that covalently connect the α- and β-chain of the Sema domain, the domain is stabilized by 5 additional disulfide bridges formed between Cys95-Cys101, Cys98-Cys159, Cys133-Cys141, Cys172-Cys175, and Cys385-Cys397 (FIG. 3).
The surface of the Met Sema domain appears to be mostly negatively charged, especially in the center of the bottom face of the Sema domain (FIG. 2C). This surface, which is formed by a 20 residue insertion after strand D in the first blade and includes the rather irregular area of strand D in the third blade, shows clusters of acidic residues. Monomeric, full length Met was shown to bind to heparin (Gherardi et al., 2003). In presently disclosed structure there are no dominant positively charged patches within the Met Sema domain; however, two arginines are located in the vicinity of the disordered furin-cleavage site. Together with the 6 positively charged residues that reside in this loop, these arginines could constitute a potential heparin binding site.
The last strand of the Sema domain (C7) is followed immediately by the PSI domain. This domain, with dimensions of about 20×15 Å, contains four (4) disulfide bridges and is not an integral part of the Sema domain but rather an independent structural module. The small core of the domain is formed by a helix and a short two-stranded antiparallel β-sheet that are connected via a disulfide bond and sandwich the side-chain of Trp540. Superposition of this domain with the PSI domain of Sema4D results in an rmsd of 1.6 Å for 41 Ca pairs. The relative orientation between the Sema and the PSI domains in the Met and the Sema4D structures, however, is different and requires a rotation of about 40° for superposition.
The interface Between the HGF β-Chain and Met
The HGF β-chain binds to the Sema domain of Met at the bottom face of the propeller, and forms contacts with residues that protrude from blades 2 and 3 (FIGS. 2 and 3). This is unlike other β-propeller containing receptors, such as the integrins, which bind their ligands utilizing the top face of the propeller (Xiong et al., 2002). Other Sema domain containing proteins, such as Sema3A and Sema4D, are also postulated to bind ligands using the top face (Antipenko et al., 2003; Love et al., 2003).
The interface between HGF β-chain and Met buries a total of 1770 Å²of solvent accessible surface and is dominated by polar or charge-charge interactions. Of the 20 HGF residues that have more that 10 Å²buried in the interface, 6 are positively charged, 3 carry negative charges, and 3 are aromatic. Even more dramatic, of the 18 residues contributing more than 10 Å²of buried surface to the interface on the Met side, 6 carry negative charges, 4 are positively charged and 3 are aromatic. The combined buried surface of the hydrophobic residues Ala, Val, Leu, Ile, Met and Phe amounts to a mere 145 Å², while the charged residues Asp, Glu, Lys, Arg, and His are responsible for more than 1,000 Å²of buried surface. The resolution of the presently disclosed structure does not permit a detailed discussion of hydrogen bonds; however, the position of the side chains suggest the presence of at least 7 charged interactions between Met and the HGF β-chain. (See Table 3)
On HGF, the residues analogous to those responsible for substrate binding and catalysis in the related serine proteases form most of the interactions with Met. Serine proteases bind linear peptides to their recognition site and form hydrogen bonds to main chain atoms to position a specific peptide bond for proteolytic cleavage. In contrast, the HGF β-chain binds to a series of protruding polar side chains from Met that originate mainly from 3 separate loops (FIG. 5B). The first of these loops includes residues 124-128 and connects strands A2 and B2 of Met. This loop contains two tyrosines that are in the core of the binding interface and pack against Arg695 of HGF. The second loop of Met that contacts HGF β-chain contains residues Asp190, Arg191, and Phe192 and connects A3 and B3. Asp190 of Met forms charged interactions with Arg533 of HGF. The side chain of Arg191 of Met packs against Val692 and Pro693 of HGF with its hydrophobic portion and in the presently disclosed model is in hydrogen bonding distance to the side chains of Glu656 and Asp578 with its guanidinium group. This Asp578 corresponds to aspartic acid [c102] in the catalytic triad of the related serine proteases. Furthermore, the backbone of this loop forms hydrophilic interactions with Gln534, the residue homologous to the histidine [c57] of the protease catalytic triad.
The third segment contributing to the interface also includes strand D in the third blade of the propeller, an area that deviates from the classical ‘propeller fold’. Strand D is interrupted and has a short helical insert within its strand. This unusual conformation presents a number of residues towards the surface of the HGF β-chain. The most prominent interaction formed by this loop involves Glu221 which extends its side chain towards what would be the S1 binding site in serine proteases (FIGS. 5 and 6). The carboxylate of Glu221 forms an extensive network of polar interactions with the side chain of Tyr673 (corresponding to the serine [c195] of the catalytic triad in proteases), as well as the backbone amides of Gly694 and Gly696 (FIG. 6); however, unlike in serine proteases, where the S1 pocket is filled by the specificity determining P1 residue, it does not penetrate deeply into the S1 pocket. As a result of the exchange of Ser to Tyr in position 673 [c195], the entrance of the S8 pocket is much smaller than in the related proteases. Thus, Glu221 projects towards the entrance of the S1 pocket from a different angle when compared to a complex between trypsin and bovine pancreatic trypsin inhibitor (BPTI) and does not fill the pocket (FIG. 6). Therefore, a large cavity, presumably filled with a number of water molecules, remains in HGF β-chain.
Comparison of HGF β-Chain Unbound and Bound to Met
The structures of the HGF β-chain bound to Met and in its unbound state, as disclosed in application U.S. Ser. No. 60/569,301 filed May 6, 2004, which application is hereby incorporated by reference, are very similar and superimpose with an rmsd of less than 0.8 Å for 218 C_α-pairs. The only significant differences between the two structures involve residues that are close to the Met binding interface. The backbone of residues 645 to 651 is disordered in unliganded HGF β but well defined in the structure of the complex, where it adopts a conformation that is commonly observed in serine proteases (FIG. 1). The side chains of the basic residues Arg647 and Lys649 are not well defined in the electron density but project towards the Met binding interface and, in presently disclosed model, participate in the formation of the complex. Arg695 also undergoes a change in conformation upon Met binding. This residue, located in the center of the receptor binding interface, packs against Tyr125 of Met, and its backbone forms part of the S1 pocket. In the structure of unliganded HGF β, the conformation of the backbone in this area is different, and the side chain of Arg695 projects toward the disordered region of the structure. It is conceivable that the binding event alters the position of Arg695, which in turn allows residues 645 to 651 to adopt a more stable conformation.
Models for Receptor Activation
In embodiments, a model for HGF mediated Met receptor activation is provided. Little is known about the signaling complex itself, and details of this interaction, such as the stoichiometry between ligand and receptor, have been elusive.
The presently disclosed structure shows unambiguously how Met binds to the β-chain of HGF. However, the exact role this interaction might play in Met activation remains uncertain. Two general models of how HGF can lead to Met dimerization have been suggested (Miller and Leonard, 1998). One of these models, follows the growth hormone paradigm (de Vos et al, 1994) where one HGF molecule binds to two different Met receptors with different affinities to form the 2:1 signaling complex. The other model suggests that two 1:1 complexes of Met and HGF are dimerized either via heparin or an alternative mechanism to form stable 2:2 complexes.
In the present disclosure, complexes of HGF β-chain and the Sema domain of Met were purified from the individual components via size exclusion chromatography. This clearly showed that HGF β and the N-terminal 564 residues of Met form a stable 1:1 complex. If Met activation via HGF indeed entails a 2:1 complex, the present disclosure characterizes the low affinity binding interaction between HGF and Met. The high affinity binding interaction involves the α-chain of HGF, in particular the NK1 domains (Lokker et al., 1992), and a previously uncharacterized binding site on Met. This model is in good agreement with the notion that single chain HGF is able to bind Met via its high affinity binding site which is contained in its N-terminal portion, yet unable to signal. For signaling, maturation of HGF is required. This leads to rearrangements in the activation domain of HGF β, the formation of the low affinity binding site and possibly allows for a reorientation of the β-chain of HGF relative to its α-chain. This model could also be valid for the closely related Ron/MSP system. Like HGF, single chain MSP can bind to its receptor Ron, but is only able to signal in its matured 2-chain form. Interestingly and in contrast to HGF, the high affinity binding site in MSP is contained within its β-chain while the low affinity binding site is harbored by its α-chain (Danilkovitch et al., 1999).
Recent studies employing analytical ultracentrifugation and light scattering experiments indicate that mature HGF and the Met ectodomain form 1:1 complexes that can be stabilized with heparin to form a 1:1:1 complex (Gherardi et al., 2003). However, in those experiments no higher order complexes or aggregates could be detected.
The present disclosure shows that the low affinity interaction between HGF β and Met is sufficient for 1:1 complex formation. The absence of 2:1 complexes in Gherardi et al, (2003), suggest two possible scenarios. Firstly, it is possible that the high and low affinity binding sites on the receptor overlap. In this case, at a 1:1 molar ratio of ligand and receptor, all high affinity binding sites on the receptor are occupied and none of the low affinity binding sites available thus preventing the formation of 2:1 complexes. An alternative explanation for the absence of 2:1 complexes is that α- and β-chain of a single HGF molecule bind to the same Met receptor and form stable 1:1 complexes. These 1:1 complexes only associate very weakly and require the juxtamembrane or intracellular portion of the receptors or need additional molecules or co-receptors for the assembly of 2:2 or higher order signaling complexes.
Recent crystal structures of dimeric Sema4D and Sema3A have demonstrated how these Sema domains dimerize. Antipenko A, Himanen J P, van Leyen K, Nardi-Dei V, Lesniak J, Barton W A, Rajashankar Kr, Lu M, Hoemme C, Puschel A W, Nikolov D B (2003) Structure of the Semaphorin-3A receptor binding module. Neuron 39:589-598 and Love C A, Harlos K, Mavaddat N, Davis S J, Stuart D I, Jones E Y, Esnouf R M (2003). The ligand-binding face of the Semaphorins revealed by the high-resolution crystal structure of Sema4D. Nat. Struct. Biol. 10:843-848.
In Sema4D, dimerization of the Sema domains is mediated by four loops that protrude from the core of the propeller. Three of these loops connect strands B4-C4, D4-A5, and B5-C5, and the fourth is part of the insert that follows the 5th blade of the propeller (FIG. 3). In the present crystal structure the interface observed in the Semaphorin structures is not present. The superposition of the complex described here and the dimer of Sema4D shows that none of the regions relevant for dimerization in Sema4D are conserved in the Met structure (FIG. 4B). Thus, it is unlikely that the Met dimerization follows the Semaphorin paradigm. However, since the loop connecting D4-A5 contains the furin cleavage site that was altered in the present construct, the possibility that the dimer seen in Sema4D is similar in the Met receptor system cannot be excluded. A number of characteristics of Met speak against this model. As discussed above, cleavage of Met at the furin cleavage site is not required for signaling. Therefore, it seems unlikely that this loop is involved in crucial interactions in the signaling complex. Furthermore, if Met were to dimerize similarly to the Semaphorins, the β-chains of HGF would be more than 70 Å apart from each other and lie on opposite sides of the Sema domain. Thus, they could not participate in the stabilization of a 2:2 complex, yet it is known that maturation of HGF and the presence of the HGF β-chain are required for the formation of a signaling complex.
A different model for a 2:2 signaling complex is suggested by the crystal packing of the 1:1 complexes in the disclosed crystal structure where two HGF β-chains form a symmetric interface with about 1250 Å²of total buried surface (FIG. 7). This interface is formed via interactions from 3 loops: the strand immediately following the N-terminus, residues 619-630, and residues 662-665. These 3 loops are part of the so-called ‘activation domain’ in the related serine proteases and rearrange upon zymogen maturation (Huber and Bode, 1978). As the surface engaged in this interface can only be present if full length HGF is properly cleaved and in its matured form, this dimer can only form after maturation which explains the requirement of HGF maturation for proper signaling. In this model, the C-termini of the Met receptor Sema domains are separated by about 110 Å, a gap that could be easily spanned by the PSI and the 4 IPT domains of the two receptors that connect the Sema domains to the transmembrane helix. Interestingly, while HGF β-chain/β-chain interactions are clearly weak, no oligomers were detected during size exclusion chromatography of the complex and the HGF β-chain is monomeric in solution (data not shown), the same interface is also present in crystals containing only the HGF β-chain and that were derived under different crystallization conditions, see application U.S. Ser. No. 60/569,301 filed May 6, 2004.
Based on these observations we propose a model in which the α-chain of HGF provides the initial binding event for HGF to Met (FIG. 8). The large, negatively charged patches in the center of the ‘bottom’ of the Sema domain propeller may represent a potential binding site for the HGF α-chain, allowing for interaction with the positively charged surface region of the NK1 domain (Lokker et al., 1992, Ultsch et al., 1998). Before cleavage of single-chain HGF, the protease-like domain of HGF would be unavailable for binding to Met. Once cleavage occurs, the N-terminus of the newly formed β-chain inserts into the protein and leads to rearrangements in the ‘activation domain’ creating the Met binding site on HGF β-chain. Now the HGF β-chain can bind to Met, which positions the α-chain dimerization surface for contact with a neighboring HGF/Met complex. The presence of heparin sulfate proteoglycans may serve to strengthen these interactions.

The 2:2 model is supported by the stoichiometry studies mentioned above which show no dimerization of complexes in solution (Gherardi et al., 2003), indicating that the 2:2 complex formation must be very weak. Also, the fact that the α-chain alone (NK4) is not able to mediate dimerization, but instead acts as an antagonist in vivo (Date et al., 1997), further highlights the potential role for the HGF β-chain in dimerization. The disclosed structure of Met lacks the IPT domains, and their role in the signaling of the Met/HGF complex is still unclear. A crystal structure of the full length Met in complex with full length, activated HGF could further resolve these issues.

TABLE 2


Atomic Coordinates of Hepatocyte Growth Factor Beta Chain with Met Receptor

	Amino Acid					Temp
Atom Number	Residue	X	Y	Z	Occ.	Factor	Atom Type

ATOM	1	N	VAL	A	495	3.648	8.257	25.688	1.00	34.05	A	N
ATOM	2	CA	VAL	A	495	2.510	8.343	24.730	1.00	31.80	A	C
ATOM	3	CB	VAL	A	495	2.999	8.054	23.335	1.00	34.93	A	C
ATOM	4	CG1	VAL	A	495	1.840	7.978	22.370	1.00	33.34	A	C
ATOM	5	CG2	VAL	A	495	4.062	9.062	22.921	1.00	39.47	A	C
ATOM	6	C	VAL	A	495	1.486	7.274	25.046	1.00	36.19	A	C
ATOM	7	O	VAL	A	495	1.814	6.071	25.187	1.00	35.83	A	O
ATOM	8	N	VAL	A	496	0.231	7.684	25.129	1.00	39.53	A	N
ATOM	9	CA	VAL	A	496	−0.796	6.708	25.480	1.00	41.32	A	C
ATOM	10	CB	VAL	A	496	−1.903	7.308	26.306	1.00	39.20	A	C
ATOM	11	CG1	VAL	A	496	−3.011	6.306	26.467	1.00	36.02	A	C
ATOM	12	CG2	VAL	A	496	−1.334	7.729	27.656	1.00	40.39	A	C
ATOM	13	C	VAL	A	496	−1.329	5.988	24.255	1.00	41.88	A	C
ATOM	14	O	VAL	A	496	−1.609	6.606	23.213	1.00	43.50	A	O
ATOM	15	N	ASN	A	497	−1.427	4.670	24.399	1.00	35.06	A	N
ATOM	16	CA	ASN	A	497	−1.803	3.780	23.313	1.00	31.56	A	C
ATOM	17	CB	ASN	A	497	−3.300	3.842	23.067	1.00	25.35	A	C
ATOM	18	CG	ASN	A	497	−4.046	3.020	24.063	1.00	34.07	A	C
ATOM	19	OD1	ASN	A	497	−3.513	2.045	24.585	1.00	39.84	A	O
ATOM	20	ND2	ASN	A	497	−5.271	3.395	24.356	1.00	41.50	A	N
ATOM	21	C	ASN	A	497	−0.960	3.807	22.021	1.00	33.76	A	C
ATOM	22	O	ASN	A	497	−1.488	3.849	20.916	1.00	37.21	A	O
ATOM	23	N	GLY	A	498	0.362	3.773	22.177	1.00	34.65	A	N
ATOM	24	CA	GLY	A	498	1.265	3.585	21.052	1.00	32.53	A	C
ATOM	25	C	GLY	A	498	2.206	2.425	21.294	1.00	32.73	A	C
ATOM	26	O	GLY	A	498	2.168	1.802	22.361	1.00	38.63	A	O
ATOM	27	N	ILE	A	499	3.058	2.128	20.318	1.00	30.60	A	N
ATOM	28	CA	ILE	A	499	3.983	0.994	20.458	1.00	28.08	A	C
ATOM	29	CB	ILE	A	499	3.766	−0.081	19.357	1.00	26.10	A	C
ATOM	30	CG1	ILE	A	499	4.267	0.409	18.011	1.00	30.80	A	C
ATOM	31	CD1	ILE	A	499	3.730	−0.420	16.858	1.00	41.02	A	C
ATOM	32	CG2	ILE	A	499	2.318	−0.445	19.244	1.00	24.14	A	C
ATOM	33	C	ILE	A	499	5.452	1.407	20.532	1.00	26.32	A	C
ATOM	34	O	ILE	A	499	5.821	2.539	20.200	1.00	29.62	A	O
ATOM	35	N	PRO	A	500	6.286	0.494	21.002	1.00	22.97	A	N
ATOM	36	CA	PRO	A	500	7.734	0.707	20.994	1.00	25.27	A	C
ATOM	37	CB	PRO	A	500	8.269	−0.630	21.510	1.00	28.37	A	C
ATOM	38	CG	PRO	A	500	7.119	−1.233	22.318	1.00	23.04	A	C
ATOM	39	CD	PRO	A	500	5.906	−0.804	21.591	1.00	20.18	A	C
ATOM	40	C	PRO	A	500	8.229	0.950	19.570	1.00	29.77	A	C
ATOM	41	O	PRO	A	500	7.752	0.311	18.614	1.00	30.70	A	O
ATOM	42	N	THR	A	501	9.166	1.877	19.409	1.00	32.11	A	N
ATOM	43	CA	THR	A	501	9.764	2.076	18.087	1.00	32.08	A	C
ATOM	44	CB	THR	A	501	10.433	3.459	17.931	1.00	30.15	A	C
ATOM	45	OG1	THR	A	501	11.565	3.581	18.811	1.00	26.33	A	O
ATOM	46	CG2	THR	A	501	9.475	4.579	18.353	1.00	29.78	A	C
ATOM	47	C	THR	A	501	10.770	0.977	17.841	1.00	36.15	A	C
ATOM	48	O	THR	A	501	11.510	0.597	18.752	1.00	36.54	A	O
ATOM	49	N	ARG	A	502	10.788	0.467	16.611	1.00	40.43	A	N
ATOM	50	CA	ARG	A	502	11.698	−0.612	16.235	1.00	36.95	A	C
ATOM	51	CB	ARG	A	502	11.661	−0.825	14.734	1.00	32.79	A	C
ATOM	52	CG	ARG	A	502	11.170	−2.173	14.365	1.00	39.24	A	C
ATOM	53	CD	ARG	A	502	10.928	−2.361	12.889	1.00	51.53	A	C
ATOM	54	NE	ARG	A	502	9.667	−1.765	12.471	1.00	59.18	A	N
ATOM	55	CZ	ARG	A	502	9.564	−0.590	11.871	1.00	65.00	A	C
ATOM	56	NH1	ARG	A	502	10.659	0.119	11.596	1.00	67.56	A	N
ATOM	57	NH2	ARG	A	502	8.366	−0.127	11.529	1.00	68.74	A	N
ATOM	58	C	ARG	A	502	13.127	−0.356	16.708	1.00	41.11	A	C
ATOM	59	O	ARG	A	502	13.750	−1.205	17.321	1.00	46.19	A	O
ATOM	60	N	THR	A	503	13.630	0.838	16.449	1.00	45.57	A	N
ATOM	61	CA	THR	A	503	14.999	1.186	16.776	1.00	49.27	A	C
ATOM	62	CB	THR	A	503	15.864	1.002	15.524	1.00	56.77	A	C
ATOM	63	OG1	THR	A	503	17.186	1.495	15.774	1.00	62.39	A	O
ATOM	64	CG2	THR	A	503	15.321	1.860	14.324	1.00	56.70	A	C
ATOM	65	C	THR	A	503	14.952	2.638	17.208	1.00	48.38	A	C
ATOM	66	O	THR	A	503	13.856	3.193	17.333	1.00	51.69	A	O
ATOM	67	N	ASN	A	504	16.091	3.286	17.427	1.00	43.12	A	N
ATOM	68	CA	ASN	A	504	15.971	4.699	17.763	1.00	45.81	A	C
ATOM	69	CB	ASN	A	504	17.002	5.205	18.793	1.00	51.99	A	C
ATOM	70	CG	ASN	A	504	18.415	5.244	18.278	1.00	52.58	A	C
ATOM	71	OD1	ASN	A	504	19.003	6.329	18.154	1.00	53.21	A	O
ATOM	72	ND2	ASN	A	504	19.003	4.069	18.055	1.00	51.18	A	N
ATOM	73	C	ASN	A	504	15.719	5.618	16.573	1.00	40.80	A	C
ATOM	74	O	ASN	A	504	15.688	5.153	15.447	1.00	38.18	A	O
ATOM	75	N	ILE	A	505	15.469	6.899	16.847	1.00	41.30	A	N
ATOM	76	CA	ILE	A	505	15.003	7.857	15.840	1.00	39.57	A	C
ATOM	77	CB	ILE	A	505	13.530	8.190	16.087	1.00	35.88	A	C
ATOM	78	CG1	ILE	A	505	12.662	6.955	15.901	1.00	30.11	A	C
ATOM	79	CD1	ILE	A	505	11.804	6.992	14.674	1.00	31.81	A	C
ATOM	80	CG2	ILE	A	505	13.099	9.344	15.213	1.00	36.92	A	C
ATOM	81	C	ILE	A	505	15.840	9.139	15.865	1.00	43.61	A	C
ATOM	82	O	ILE	A	505	16.022	9.761	16.915	1.00	54.35	A	O
ATOM	83	N	GLY	A	506	16.315	9.549	14.700	1.00	42.54	A	N
ATOM	84	CA	GLY	A	506	17.426	10.484	14.611	1.00	43.52	A	C
ATOM	85	C	GLY	A	506	17.219	11.885	15.135	1.00	39.59	A	C
ATOM	86	O	GLY	A	506	18.144	12.485	15.658	1.00	38.26	A	O
ATOM	87	N	TRP	A	507	16.004	12.393	14.992	1.00	39.65	A	N
ATOM	88	CA	TRP	A	507	15.683	13.773	15.324	1.00	43.96	A	C
ATOM	89	CB	TRP	A	507	14.541	14.257	14.448	1.00	46.87	A	C
ATOM	90	CG	TRP	A	507	13.981	13.179	13.606	1.00	50.10	A	C
ATOM	91	CD1	TRP	A	507	14.613	12.518	12.578	1.00	56.98	A	C
ATOM	92	NE1	TRP	A	507	13.784	11.566	12.031	1.00	52.84	A	N
ATOM	93	CE2	TRP	A	507	12.593	11.603	12.691	1.00	47.24	A	C
ATOM	94	CD2	TRP	A	507	12.694	12.613	13.703	1.00	46.13	A	C
ATOM	95	CE3	TRP	A	507	11.602	12.850	14.525	1.00	44.57	A	C
ATOM	96	CZ3	TRP	A	507	10.465	12.090	14.329	1.00	53.59	A	C
ATOM	97	CH2	TRP	A	507	10.401	11.087	13.315	1.00	52.29	A	C
ATOM	98	CZ2	TRP	A	507	11.459	10.842	12.490	1.00	46.18	A	C
ATOM	99	C	TRP	A	507	15.247	13.868	16.763	1.00	47.81	A	C
ATOM	100	O	TRP	A	507	15.144	14.975	17.322	1.00	49.41	A	O
ATOM	101	N	MET	A	508	14.978	12.706	17.356	1.00	43.74	A	N
ATOM	102	CA	MET	A	508	14.458	12.667	18.700	1.00	42.90	A	C
ATOM	103	CB	MET	A	508	13.918	11.277	19.029	1.00	45.76	A	C
ATOM	104	CG	MET	A	508	12.426	11.074	18.763	1.00	46.01	A	C
ATOM	105	SD	MET	A	508	11.392	12.550	18.899	1.00	46.79	A	S
ATOM	106	CE	MET	A	508	10.964	12.526	20.590	1.00	46.16	A	C
ATOM	107	C	MET	A	508	15.517	13.118	19.703	1.00	43.48	A	C
ATOM	108	O	MET	A	508	16.665	12.640	19.687	1.00	45.57	A	O
ATOM	109	N	VAL	A	509	15.101	14.062	20.546	1.00	39.27	A	N
ATOM	110	CA	VAL	A	509	15.898	14.649	21.612	1.00	35.93	A	C
ATOM	111	CB	VAL	A	509	16.175	16.141	21.318	1.00	34.18	A	C
ATOM	112	CG1	VAL	A	509	16.950	16.819	22.451	1.00	30.42	A	C
ATOM	113	CG2	VAL	A	509	16.885	16.315	19.968	1.00	35.44	A	C
ATOM	114	C	VAL	A	509	15.097	14.554	22.915	1.00	41.47	A	C
ATOM	115	O	VAL	A	509	13.904	14.930	22.976	1.00	40.48	A	O
ATOM	116	N	SER	A	510	15.743	14.049	23.960	1.00	41.97	A	N
ATOM	117	CA	SER	A	510	15.151	14.100	25.290	1.00	40.20	A	C
ATOM	118	CB	SER	A	510	15.345	12.786	26.045	1.00	40.31	A	C
ATOM	119	OG	SER	A	510	15.428	12.979	27.448	1.00	41.82	A	O
ATOM	120	C	SER	A	510	15.799	15.267	26.009	1.00	40.83	A	C
ATOM	121	O	SER	A	510	17.030	15.344	26.089	1.00	37.61	A	O
ATOM	122	N	LEU	A	511	14.950	16.195	26.466	1.00	42.88	A	N
ATOM	123	CA	LEU	A	511	15.348	17.347	27.263	1.00	40.77	A	C
ATOM	124	CB	LEU	A	511	14.337	18.478	27.124	1.00	38.22	A	C
ATOM	125	CG	LEU	A	511	14.830	19.924	27.325	1.00	41.51	A	C
ATOM	126	CD1	LEU	A	511	14.024	20.711	28.358	1.00	39.28	A	C
ATOM	127	CD2	LEU	A	511	16.300	19.998	27.665	1.00	43.86	A	C
ATOM	128	C	LEU	A	511	15.325	16.888	28.686	1.00	43.00	A	C
ATOM	129	O	LEU	A	511	14.362	16.246	29.100	1.00	42.35	A	O
ATOM	130	N	ARG	A	512	16.376	17.208	29.435	1.00	43.58	A	N
ATOM	131	CA	ARG	A	512	16.405	16.838	30.838	1.00	48.38	A	C
ATOM	132	CB	ARG	A	512	17.401	15.722	31.112	1.00	53.42	A	C
ATOM	133	CG	ARG	A	512	18.088	15.190	29.906	1.00	61.05	A	C
ATOM	134	CD	ARG	A	512	17.820	13.739	29.651	1.00	68.73	A	C
ATOM	135	NE	ARG	A	512	18.355	12.882	30.700	1.00	73.03	A	N
ATOM	136	CZ	ARG	A	512	17.944	11.640	30.889	1.00	78.60	A	C
ATOM	137	NH1	ARG	A	512	18.477	10.916	31.875	1.00	82.59	A	N
ATOM	138	NH2	ARG	A	512	16.990	11.128	30.092	1.00	73.30	A	N
ATOM	139	C	ARG	A	512	16.676	17.990	31.769	1.00	50.34	A	C
ATOM	140	O	ARG	A	512	17.745	18.598	31.723	1.00	51.89	A	O
ATOM	141	N	TYR	A	513	15.683	18.266	32.613	1.00	50.28	A	N
ATOM	142	CA	TYR	A	513	15.767	19.236	33.692	1.00	51.88	A	C
ATOM	143	CB	TYR	A	513	14.419	19.913	33.875	1.00	51.30	A	C
ATOM	144	CG	TYR	A	513	14.306	20.769	35.110	1.00	57.87	A	C
ATOM	145	CD1	TYR	A	513	14.988	21.981	35.210	1.00	62.28	A	C
ATOM	146	CE1	TYR	A	513	14.875	22.779	36.339	1.00	65.67	A	C
ATOM	147	CZ	TYR	A	513	14.064	22.369	37.383	1.00	70.03	A	C
ATOM	148	OH	TYR	A	513	13.945	23.147	38.514	1.00	75.63	A	O
ATOM	149	CE2	TYR	A	513	13.376	21.170	37.304	1.00	67.53	A	C
ATOM	150	CD2	TYR	A	513	13.502	20.380	36.168	1.00	61.73	A	C
ATOM	151	C	TYR	A	513	16.155	18.512	34.968	1.00	55.13	A	C
ATOM	152	O	TYR	A	513	15.646	17.428	35.241	1.00	58.26	A	O
ATOM	153	N	ARG	A	514	17.056	19.112	35.745	1.00	56.46	A	N
ATOM	154	CA	ARG	A	514	17.542	18.520	36.991	1.00	55.86	A	C
ATOM	155	CB	ARG	A	514	16.650	18.929	38.173	1.00	57.14	A	C
ATOM	156	CG	ARG	A	514	16.811	20.378	38.602	1.00	64.13	A	C
ATOM	157	CD	ARG	A	514	16.260	20.721	39.982	1.00	68.04	A	C
ATOM	158	NE	ARG	A	514	17.340	21.090	40.889	1.00	72.92	A	N
ATOM	159	CZ	ARG	A	514	17.856	20.278	41.810	1.00	78.47	A	C
ATOM	160	NH1	ARG	A	514	17.375	19.047	41.963	1.00	78.38	A	N
ATOM	161	NH2	ARG	A	514	18.857	20.697	42.585	1.00	81.64	A	N
ATOM	162	C	ARG	A	514	17.654	16.995	36.907	1.00	54.80	A	C
ATOM	163	O	ARG	A	514	17.101	16.283	37.738	1.00	57.67	A	O
ATOM	164	N	ASN	A	515	18.330	16.506	35.872	1.00	52.97	A	N
ATOM	165	CA	ASN	A	515	18.721	15.090	35.760	1.00	55.78	A	C
ATOM	166	CB	ASN	A	515	19.449	14.624	37.012	1.00	57.23	A	C
ATOM	167	CG	ASN	A	515	20.867	15.102	37.031	1.00	62.81	A	C
ATOM	168	OD1	ASN	A	515	21.654	14.754	36.143	1.00	63.04	A	O
ATOM	169	ND2	ASN	A	515	21.203	15.942	38.010	1.00	65.31	A	N
ATOM	170	C	ASN	A	515	17.721	14.030	35.280	1.00	57.34	A	C
ATOM	171	O	ASN	A	515	18.139	13.003	34.716	1.00	59.88	A	O
ATOM	172	N	LYS	A	516	16.427	14.270	35.478	1.00	53.97	A	N
ATOM	173	CA	LYS	A	516	15.409	13.383	34.924	1.00	52.63	A	C
ATOM	174	CB	LYS	A	516	14.329	13.081	35.980	1.00	59.60	A	C
ATOM	175	CG	LYS	A	516	13.107	13.990	36.034	1.00	71.77	A	C
ATOM	176	CD	LYS	A	516	11.887	13.206	36.610	1.00	80.27	A	C
ATOM	177	CE	LYS	A	516	10.558	13.533	35.874	1.00	85.92	A	C
ATOM	178	NZ	LYS	A	516	9.889	12.372	35.163	1.00	85.07	A	N
ATOM	179	C	LYS	A	516	14.866	13.943	33.600	1.00	48.79	A	C
ATOM	180	O	LYS	A	516	14.991	15.139	33.364	1.00	50.31	A	O
ATOM	181	N	HIS	A	517	14.308	13.100	32.724	1.00	44.58	A	N
ATOM	182	CA	HIS	A	517	13.729	13.590	31.451	1.00	41.66	A	C
ATOM	183	CB	HIS	A	517	13.611	12.474	30.402	1.00	45.12	A	C
ATOM	184	CG	HIS	A	517	12.438	12.613	29.463	1.00	40.15	A	C
ATOM	185	ND1	HIS	A	517	12.534	13.226	28.231	1.00	42.52	A	N
ATOM	186	CE1	HIS	A	517	11.364	13.175	27.618	1.00	38.84	A	C
ATOM	187	NE2	HIS	A	517	10.515	12.548	28.405	1.00	35.65	A	N
ATOM	188	CD2	HIS	A	517	11.163	12.175	29.558	1.00	35.82	A	C
ATOM	189	C	HIS	A	517	12.383	14.244	31.644	1.00	39.70	A	C
ATOM	190	O	HIS	A	517	11.574	13.779	32.439	1.00	43.99	A	O
ATOM	191	N	ILE	A	518	12.134	15.282	30.859	1.00	36.76	A	N
ATOM	192	CA	ILE	A	518	10.999	16.168	31.062	1.00	33.32	A	C
ATOM	193	CB	ILE	A	518	11.511	17.479	31.710	1.00	30.15	A	C
ATOM	194	CG1	ILE	A	518	10.367	18.337	32.228	1.00	33.32	A	C
ATOM	195	CD1	ILE	A	518	10.804	19.711	32.739	1.00	30.08	A	C
ATOM	196	CG2	ILE	A	518	12.299	18.295	30.718	1.00	29.73	A	C
ATOM	197	C	ILE	A	518	10.206	16.482	29.784	1.00	33.64	A	C
ATOM	198	O	ILE	A	518	9.082	16.954	29.868	1.00	36.86	A	O
ATOM	199	N	CYS	A	519	10.787	16.235	28.610	1.00	36.15	A	N
ATOM	200	CA	CYS	A	519	10.261	16.799	27.363	1.00	37.62	A	C
ATOM	201	CB	CYS	A	519	10.465	18.305	27.357	1.00	43.78	A	C
ATOM	202	SG	CYS	A	519	8.955	19.198	27.665	1.00	53.07	A	S
ATOM	203	C	CYS	A	519	10.962	16.269	26.145	1.00	36.96	A	C
ATOM	204	O	CYS	A	519	12.135	15.923	26.215	1.00	44.22	A	O
ATOM	205	N	GLY	A	520	10.256	16.252	25.018	1.00	33.67	A	N
ATOM	206	CA	GLY	A	520	10.824	15.825	23.750	1.00	31.07	A	C
ATOM	207	C	GLY	A	520	11.312	16.997	22.941	1.00	35.19	A	C
ATOM	208	O	GLY	A	520	11.103	18.162	23.307	1.00	38.25	A	O
ATOM	209	N	GLY	A	521	11.975	16.699	21.835	1.00	36.29	A	N
ATOM	210	CA	GLY	A	521	12.538	17.749	21.002	1.00	37.32	A	C
ATOM	211	C	GLY	A	521	12.990	17.241	19.652	1.00	38.07	A	C
ATOM	212	O	GLY	A	521	13.538	16.142	19.526	1.00	38.85	A	O
ATOM	213	N	SER	A	522	12.745	18.041	18.626	1.00	38.93	A	N
ATOM	214	CA	SER	A	522	13.114	17.658	17.271	1.00	34.80	A	C
ATOM	215	CB	SER	A	522	11.988	17.977	16.271	1.00	33.89	A	C
ATOM	216	OG	SER	A	522	10.701	18.060	16.889	1.00	33.28	A	O
ATOM	217	C	SER	A	522	14.398	18.400	16.935	1.00	34.35	A	C
ATOM	218	O	SER	A	522	14.491	19.626	17.102	1.00	32.30	A	O
ATOM	219	N	LEU	A	523	15.407	17.643	16.521	1.00	34.26	A	N
ATOM	220	CA	LEU	A	523	16.674	18.234	16.113	1.00	34.02	A	C
ATOM	221	CB	LEU	A	523	17.818	17.221	16.278	1.00	30.65	A	C
ATOM	222	CG	LEU	A	523	19.200	17.502	15.672	1.00	30.72	A	C
ATOM	223	CD1	LEU	A	523	19.812	18.751	16.258	1.00	34.42	A	C
ATOM	224	CD2	LEU	A	523	20.155	16.338	15.864	1.00	25.93	A	C
ATOM	225	C	LEU	A	523	16.510	18.722	14.666	1.00	35.12	A	C
ATOM	226	O	LEU	A	523	16.286	17.928	13.748	1.00	34.62	A	O
ATOM	227	N	ILE	A	524	16.576	20.033	14.468	1.00	34.63	A	N
ATOM	228	CA	ILE	A	524	16.254	20.582	13.157	1.00	35.75	A	C
ATOM	229	CB	ILE	A	524	15.155	21.663	13.218	1.00	35.51	A	C
ATOM	230	CG1	ILE	A	524	15.564	22.814	14.117	1.00	33.46	A	C
ATOM	231	CD1	ILE	A	524	14.971	24.098	13.673	1.00	34.02	A	C
ATOM	232	CG2	ILE	A	524	13.846	21.071	13.687	1.00	37.56	A	C
ATOM	233	C	ILE	A	524	17.466	21.070	12.400	1.00	37.14	A	C
ATOM	234	O	ILE	A	524	17.416	21.204	11.178	1.00	40.12	A	O
ATOM	235	N	LYS	A	525	18.533	21.369	13.128	1.00	37.43	A	N
ATOM	236	CA	LYS	A	525	19.843	21.598	12.527	1.00	38.70	A	C
ATOM	237	CB	LYS	A	525	19.997	23.024	11.995	1.00	40.01	A	C
ATOM	238	CG	LYS	A	525	19.923	23.104	10.465	1.00	48.89	A	C
ATOM	239	CD	LYS	A	525	20.464	24.447	9.928	1.00	58.25	A	C
ATOM	240	CE	LYS	A	525	20.461	24.504	8.394	1.00	60.68	A	C
ATOM	241	NZ	LYS	A	525	19.090	24.706	7.818	1.00	59.37	A	N
ATOM	242	C	LYS	A	525	20.889	21.270	13.568	1.00	38.37	A	C
ATOM	243	O	LYS	A	525	20.575	21.202	14.761	1.00	40.24	A	O
ATOM	244	N	GLU	A	526	22.123	21.071	13.111	1.00	36.22	A	N
ATOM	245	CA	GLU	A	526	23.226	20.562	13.931	1.00	38.49	A	C
ATOM	246	CB	GLU	A	526	24.544	20.747	13.178	1.00	41.99	A	C
ATOM	247	CG	GLU	A	526	24.727	19.735	12.053	1.00	49.92	A	C
ATOM	248	CD	GLU	A	526	24.503	20.305	10.651	1.00	55.90	A	C
ATOM	249	OE1	GLU	A	526	23.479	20.986	10.403	1.00	57.40	A	O
ATOM	250	OE2	GLU	A	526	25.358	20.049	9.772	1.00	59.44	A	O
ATOM	251	C	GLU	A	526	23.323	21.129	15.364	1.00	39.56	A	C
ATOM	252	O	GLU	A	526	23.780	20.444	16.288	1.00	36.08	A	O
ATOM	253	N	SER	A	527	22.866	22.369	15.535	1.00	41.92	A	N
ATOM	254	CA	SER	A	527	22.946	23.089	16.806	1.00	39.39	A	C
ATOM	255	CB	SER	A	527	23.880	24.303	16.657	1.00	37.58	A	C
ATOM	256	OG	SER	A	527	25.194	24.021	17.132	1.00	37.03	A	O
ATOM	257	C	SER	A	527	21.582	23.541	17.361	1.00	38.77	A	C
ATOM	258	O	SER	A	527	21.530	24.361	18.296	1.00	40.76	A	O
ATOM	259	N	TRP	A	528	20.485	23.011	16.810	1.00	33.24	A	N
ATOM	260	CA	TRP	A	528	19.160	23.515	17.178	1.00	30.57	A	C
ATOM	261	CB	TRP	A	528	18.646	24.492	16.140	1.00	29.10	A	C
ATOM	262	CG	TRP	A	528	19.412	25.747	16.114	1.00	31.01	A	C
ATOM	263	CD1	TRP	A	528	20.396	26.075	15.243	1.00	30.54	A	C
ATOM	264	NE1	TRP	A	528	20.886	27.325	15.527	1.00	29.07	A	N
ATOM	265	CE2	TRP	A	528	20.215	27.832	16.605	1.00	26.11	A	C
ATOM	266	CD2	TRP	A	528	19.278	26.860	17.004	1.00	30.79	A	C
ATOM	267	CE3	TRP	A	528	18.454	27.142	18.096	1.00	32.09	A	C
ATOM	268	CZ3	TRP	A	528	18.605	28.371	18.744	1.00	30.15	A	C
ATOM	269	CH2	TRP	A	528	19.549	29.310	18.312	1.00	19.71	A	C
ATOM	270	CZ2	TRP	A	528	20.350	29.059	17.249	1.00	21.17	A	C
ATOM	271	C	TRP	A	528	18.106	22.467	17.401	1.00	32.06	A	C
ATOM	272	O	TRP	A	528	17.775	21.697	16.500	1.00	37.40	A	O
ATOM	273	N	VAL	A	529	17.560	22.457	18.606	1.00	29.15	A	N
ATOM	274	CA	VAL	A	529	16.450	21.588	18.887	1.00	34.38	A	C
ATOM	275	CB	VAL	A	529	16.653	20.814	20.191	1.00	39.86	A	C
ATOM	276	CG1	VAL	A	529	15.491	19.858	20.418	1.00	45.49	A	C
ATOM	277	CG2	VAL	A	529	17.945	20.047	20.156	1.00	40.27	A	C
ATOM	278	C	VAL	A	529	15.207	22.443	18.991	1.00	36.13	A	C
ATOM	279	O	VAL	A	529	15.154	23.375	19.803	1.00	35.20	A	O
ATOM	280	N	LEU	A	530	14.216	22.136	18.156	1.00	37.62	A	N
ATOM	281	CA	LEU	A	530	12.910	22.785	18.251	1.00	36.57	A	C
ATOM	282	CB	LEU	A	530	12.191	22.760	16.909	1.00	31.08	A	C
ATOM	283	CG	LEU	A	530	10.770	23.313	16.984	1.00	29.72	A	C
ATOM	284	CD1	LEU	A	530	10.777	24.824	16.970	1.00	28.98	A	C
ATOM	285	CD2	LEU	A	530	9.943	22.788	15.847	1.00	30.51	A	C
ATOM	286	C	LEU	A	530	12.054	22.101	19.312	1.00	38.92	A	C
ATOM	287	O	LEU	A	530	11.896	20.871	19.298	1.00	44.45	A	O
ATOM	288	N	THR	A	531	11.496	22.891	20.224	1.00	34.89	A	N
ATOM	289	CA	THR	A	531	10.706	22.315	21.313	1.00	36.51	A	C
ATOM	290	CB	THR	A	531	11.655	21.749	22.382	1.00	29.03	A	C
ATOM	291	OG1	THR	A	531	10.884	21.120	23.415	1.00	26.10	A	O
ATOM	292	CG2	THR	A	531	12.405	22.866	23.059	1.00	23.72	A	C
ATOM	293	C	THR	A	531	9.608	23.230	21.905	1.00	40.20	A	C
ATOM	294	O	THR	A	531	9.405	24.338	21.426	1.00	47.18	A	O
ATOM	295	N	ALA	A	532	8.885	22.770	22.921	1.00	39.47	A	N
ATOM	296	CA	ALA	A	532	7.810	23.588	23.496	1.00	42.64	A	C
ATOM	297	CB	ALA	A	532	6.606	22.751	23.803	1.00	47.31	A	C
ATOM	298	C	ALA	A	532	8.217	24.384	24.736	1.00	42.64	A	C
ATOM	299	O	ALA	A	532	9.181	24.041	25.423	1.00	38.19	A	O
ATOM	300	N	ARG	A	533	7.464	25.443	25.024	1.00	44.00	A	N
ATOM	301	CA	ARG	A	533	7.873	26.378	26.058	1.00	44.35	A	C
ATOM	302	CB	ARG	A	533	7.242	27.761	25.892	1.00	46.20	A	C
ATOM	303	CG	ARG	A	533	5.867	27.917	26.489	1.00	53.50	A	C
ATOM	304	CD	ARG	A	533	5.162	29.162	26.000	1.00	63.95	A	C
ATOM	305	NE	ARG	A	533	4.710	30.013	27.094	1.00	71.05	A	N
ATOM	306	CZ	ARG	A	533	5.460	30.932	27.695	1.00	73.73	A	C
ATOM	307	NH1	ARG	A	533	4.948	31.652	28.685	1.00	74.71	A	N
ATOM	308	NH2	ARG	A	533	6.718	31.133	27.315	1.00	74.31	A	N
ATOM	309	C	ARG	A	533	7.573	25.802	27.401	1.00	46.11	A	C
ATOM	310	O	ARG	A	533	8.343	25.999	28.329	1.00	56.79	A	O
ATOM	311	N	GLN	A	534	6.477	25.062	27.497	1.00	40.40	A	N
ATOM	312	CA	GLN	A	534	6.120	24.373	28.719	1.00	38.80	A	C
ATOM	313	CB	GLN	A	534	4.852	23.532	28.507	1.00	42.02	A	C
ATOM	314	CG	GLN	A	534	3.522	24.276	28.352	1.00	40.73	A	C
ATOM	315	CD	GLN	A	534	3.303	24.893	26.973	1.00	42.20	A	C
ATOM	316	OE1	GLN	A	534	2.382	25.697	26.801	1.00	40.04	A	O
ATOM	317	NE2	GLN	A	534	4.151	24.539	25.997	1.00	44.63	A	N
ATOM	318	C	GLN	A	534	7.238	23.435	29.169	1.00	40.36	A	C
ATOM	319	O	GLN	A	534	7.039	22.646	30.069	1.00	45.68	A	O
ATOM	320	N	CYS	A	535	8.408	23.503	28.548	1.00	42.90	A	N
ATOM	321	CA	CYS	A	535	9.492	22.585	28.896	1.00	45.34	A	C
ATOM	322	CB	CYS	A	535	10.138	22.036	27.640	1.00	45.96	A	C
ATOM	323	SG	CYS	A	535	8.973	21.017	26.756	1.00	51.38	A	S
ATOM	324	C	CYS	A	535	10.574	23.134	29.799	1.00	47.11	A	C
ATOM	325	O	CYS	A	535	11.520	22.425	30.108	1.00	52.64	A	O
ATOM	326	N	PHE	A	536	10.444	24.381	30.231	1.00	46.54	A	N
ATOM	327	CA	PHE	A	536	11.521	25.032	30.969	1.00	40.70	A	C
ATOM	328	CB	PHE	A	536	12.183	26.086	30.082	1.00	41.52	A	C
ATOM	329	CG	PHE	A	536	12.679	25.541	28.778	1.00	43.07	A	C
ATOM	330	CD1	PHE	A	536	13.919	24.898	28.705	1.00	45.52	A	C
ATOM	331	CE1	PHE	A	536	14.376	24.359	27.504	1.00	44.59	A	C
ATOM	332	CZ	PHE	A	536	13.592	24.472	26.365	1.00	41.06	A	C
ATOM	333	CE2	PHE	A	536	12.356	25.121	26.437	1.00	39.09	A	C
ATOM	334	CD2	PHE	A	536	11.905	25.641	27.632	1.00	37.71	A	C
ATOM	335	C	PHE	A	536	11.056	25.645	32.287	1.00	38.93	A	C
ATOM	336	O	PHE	A	536	10.680	26.792	32.339	1.00	42.14	A	O
ATOM	337	N	PRO	A	537	11.082	24.878	33.358	1.00	38.38	A	N
ATOM	338	CA	PRO	A	537	10.711	25.394	34.678	1.00	39.14	A	C
ATOM	339	CB	PRO	A	537	10.728	24.140	35.541	1.00	44.43	A	C
ATOM	340	CG	PRO	A	537	10.593	23.029	34.540	1.00	45.79	A	C
ATOM	341	CD	PRO	A	537	11.452	23.457	33.402	1.00	41.04	A	C
ATOM	342	C	PRO	A	537	11.721	26.396	35.212	1.00	38.67	A	C
ATOM	343	O	PRO	A	537	11.316	27.387	35.777	1.00	38.75	A	O
ATOM	344	N	SER	A	538	13.008	26.119	35.038	1.00	43.61	A	N
ATOM	345	CA	SER	A	538	14.095	26.998	35.444	1.00	47.01	A	C
ATOM	346	CB	SER	A	538	15.383	26.191	35.550	1.00	50.27	A	C
ATOM	347	OG	SER	A	538	15.968	26.280	36.836	1.00	54.13	A	O
ATOM	348	C	SER	A	538	14.328	28.032	34.382	1.00	53.40	A	C
ATOM	349	O	SER	A	538	13.931	27.838	33.240	1.00	56.52	A	O
ATOM	350	N	ARG	A	539	14.985	29.129	34.750	1.00	59.84	A	N
ATOM	351	CA	ARG	A	539	15.570	30.015	33.749	1.00	62.13	A	C
ATOM	352	CB	ARG	A	539	15.334	31.495	34.072	1.00	65.44	A	C
ATOM	353	CG	ARG	A	539	14.786	32.357	32.897	1.00	73.11	A	C
ATOM	354	CD	ARG	A	539	14.232	31.582	31.648	1.00	79.75	A	C
ATOM	355	NE	ARG	A	539	12.759	31.550	31.546	1.00	83.84	A	N
ATOM	356	CZ	ARG	A	539	11.977	32.568	31.138	1.00	85.20	A	C
ATOM	357	NH1	ARG	A	539	10.659	32.419	31.094	1.00	85.44	A	N
ATOM	358	NH2	ARG	A	539	12.495	33.737	30.779	1.00	86.16	A	N
ATOM	359	C	ARG	A	539	17.050	29.702	33.622	1.00	61.46	A	C
ATOM	360	O	ARG	A	539	17.637	29.908	32.574	1.00	63.21	A	O
ATOM	361	N	ASP	A	540	17.639	29.175	34.689	1.00	63.93	A	N
ATOM	362	CA	ASP	A	540	19.062	28.855	34.718	1.00	68.12	A	C
ATOM	363	CB	ASP	A	540	19.509	28.615	36.169	1.00	74.68	A	C
ATOM	364	CG	ASP	A	540	20.922	28.049	36.270	1.00	82.15	A	C
ATOM	365	OD1	ASP	A	540	21.708	28.200	35.302	1.00	83.45	A	O
ATOM	366	OD2	ASP	A	540	21.335	27.438	37.285	1.00	86.19	A	O
ATOM	367	C	ASP	A	540	19.348	27.629	33.854	1.00	66.59	A	C
ATOM	368	O	ASP	A	540	18.929	26.525	34.204	1.00	71.11	A	O
ATOM	369	N	LEU	A	541	20.070	27.816	32.745	1.00	60.72	A	N
ATOM	370	CA	LEU	A	541	20.310	26.722	31.782	1.00	53.13	A	C
ATOM	371	CB	LEU	A	541	20.669	27.244	30.378	1.00	49.17	A	C
ATOM	372	CG	LEU	A	541	19.815	28.280	29.630	1.00	44.30	A	C
ATOM	373	CD1	LEU	A	541	20.286	28.383	28.185	1.00	41.68	A	C
ATOM	374	CD2	LEU	A	541	18.297	28.033	29.700	1.00	38.17	A	C
ATOM	375	C	LEU	A	541	21.360	25.712	32.243	1.00	49.37	A	C
ATOM	376	O	LEU	A	541	21.642	24.741	31.526	1.00	46.25	A	O
ATOM	377	N	LYS	A	542	21.933	25.952	33.425	1.00	47.11	A	N
ATOM	378	CA	LYS	A	542	22.772	24.973	34.106	1.00	51.16	A	C
ATOM	379	CB	LYS	A	542	23.253	25.528	35.450	1.00	55.37	A	C
ATOM	380	CG	LYS	A	542	24.763	25.754	35.545	1.00	63.15	A	C
ATOM	381	CD	LYS	A	542	25.122	27.183	35.986	1.00	65.17	A	C
ATOM	382	CE	LYS	A	542	26.207	27.795	35.097	1.00	64.91	A	C
ATOM	383	NZ	LYS	A	542	26.907	28.922	35.774	1.00	66.28	A	N
ATOM	384	C	LYS	A	542	21.985	23.678	34.333	1.00	53.42	A	C
ATOM	385	O	LYS	A	542	22.470	22.578	34.054	1.00	53.95	A	O
ATOM	386	N	ASP	A	543	20.751	23.830	34.808	1.00	53.44	A	N
ATOM	387	CA	ASP	A	543	19.910	22.711	35.212	1.00	52.87	A	C
ATOM	388	CB	ASP	A	543	18.650	23.231	35.887	1.00	56.38	A	C
ATOM	389	CG	ASP	A	543	18.942	23.964	37.176	1.00	60.48	A	C
ATOM	390	OD1	ASP	A	543	19.775	23.488	37.994	1.00	58.01	A	O
ATOM	391	OD2	ASP	A	543	18.364	25.033	37.450	1.00	65.01	A	O
ATOM	392	C	ASP	A	543	19.512	21.753	34.099	1.00	50.26	A	C
ATOM	393	O	ASP	A	543	19.065	20.637	34.380	1.00	54.20	A	O
ATOM	394	N	TYR	A	544	19.672	22.174	32.848	1.00	43.23	A	N
ATOM	395	CA	TYR	A	544	19.286	21.330	31.722	1.00	38.63	A	C
ATOM	396	CB	TYR	A	544	18.477	22.116	30.716	1.00	29.69	A	C
ATOM	397	CG	TYR	A	544	17.306	22.885	31.238	1.00	27.52	A	C
ATOM	398	CD1	TYR	A	544	16.008	22.363	31.143	1.00	30.21	A	C
ATOM	399	CE1	TYR	A	544	14.893	23.090	31.571	1.00	24.62	A	C
ATOM	400	CZ	TYR	A	544	15.086	24.348	32.080	1.00	24.13	A	C
ATOM	401	OH	TYR	A	544	14.019	25.055	32.497	1.00	28.35	A	O
ATOM	402	CE2	TYR	A	544	16.350	24.900	32.182	1.00	25.18	A	C
ATOM	403	CD2	TYR	A	544	17.461	24.166	31.746	1.00	25.99	A	C
ATOM	404	C	TYR	A	544	20.452	20.632	30.985	1.00	42.29	A	C
ATOM	405	O	TYR	A	544	21.630	20.955	31.192	1.00	44.90	A	O
ATOM	406	N	GLU	A	545	20.083	19.710	30.093	1.00	40.12	A	N
ATOM	407	CA	GLU	A	545	20.994	18.824	29.378	1.00	40.44	A	C
ATOM	408	CB	GLU	A	545	21.542	17.790	30.359	1.00	46.13	A	C
ATOM	409	CG	GLU	A	545	22.580	16.830	29.811	1.00	54.99	A	C
ATOM	410	CD	GLU	A	545	23.458	16.255	30.913	1.00	62.86	A	C
ATOM	411	OE1	GLU	A	545	23.387	15.028	31.148	1.00	65.66	A	O
ATOM	412	OE2	GLU	A	545	24.223	17.026	31.549	1.00	65.70	A	O
ATOM	413	C	GLU	A	545	20.178	18.124	28.273	1.00	42.84	A	C
ATOM	414	O	GLU	A	545	19.017	17.735	28.495	1.00	47.57	A	O
ATOM	415	N	ALA	A	546	20.758	17.977	27.084	1.00	37.78	A	N
ATOM	416	CA	ALA	A	546	20.041	17.392	25.952	1.00	31.25	A	C
ATOM	417	CB	ALA	A	546	19.925	18.396	24.825	1.00	23.18	A	C
ATOM	418	C	ALA	A	546	20.722	16.119	25.469	1.00	34.99	A	C
ATOM	419	O	ALA	A	546	21.838	16.161	24.959	1.00	37.39	A	O
ATOM	420	N	TRP	A	547	20.044	14.988	25.633	1.00	38.48	A	N
ATOM	421	CA	TRP	A	547	20.576	13.704	25.201	1.00	40.47	A	C
ATOM	422	CB	TRP	A	547	20.082	12.616	26.117	1.00	40.48	A	C
ATOM	423	CG	TRP	A	547	20.618	12.697	27.487	1.00	41.31	A	C
ATOM	424	CD1	TRP	A	547	21.048	13.810	28.139	1.00	42.51	A	C
ATOM	425	NE1	TRP	A	547	21.456	13.480	29.407	1.00	45.89	A	N
ATOM	426	CE2	TRP	A	547	21.294	12.130	29.586	1.00	44.69	A	C
ATOM	427	CD2	TRP	A	547	20.771	11.610	28.398	1.00	41.64	A	C
ATOM	428	CE3	TRP	A	547	20.515	10.237	28.327	1.00	43.81	A	C
ATOM	429	CZ3	TRP	A	547	20.779	9.448	29.421	1.00	44.52	A	C
ATOM	430	CH2	TRP	A	547	21.301	9.992	30.585	1.00	46.82	A	C
ATOM	431	CZ2	TRP	A	547	21.567	11.330	30.691	1.00	48.64	A	C
ATOM	432	C	TRP	A	547	20.109	13.385	23.805	1.00	44.57	A	C
ATOM	433	O	TRP	A	547	18.922	13.531	23.508	1.00	50.42	A	O
ATOM	434	N	LEU	A	548	21.037	12.934	22.963	1.00	43.65	A	N
ATOM	435	CA	LEU	A	548	20.772	12.711	21.544	1.00	45.06	A	C
ATOM	436	CB	LEU	A	548	21.617	13.658	20.693	1.00	41.86	A	C
ATOM	437	CG	LEU	A	548	21.288	15.146	20.522	1.00	39.52	A	C
ATOM	438	CD1	LEU	A	548	20.574	15.345	19.210	1.00	40.81	A	C
ATOM	439	CD2	LEU	A	548	20.487	15.769	21.662	1.00	33.92	A	C
ATOM	440	C	LEU	A	548	21.096	11.278	21.163	1.00	51.45	A	C
ATOM	441	O	LEU	A	548	21.915	10.626	21.816	1.00	51.74	A	O
ATOM	442	N	GLY	A	549	20.455	10.797	20.099	1.00	58.34	A	N
ATOM	443	CA	GLY	A	549	20.631	9.427	19.628	1.00	59.49	A	C
ATOM	444	C	GLY	A	549	20.411	8.354	20.685	1.00	58.01	A	C
ATOM	445	O	GLY	A	549	21.236	7.461	20.851	1.00	56.69	A	O
ATOM	446	N	ILE	A	550	19.306	8.457	21.417	1.00	57.21	A	N
ATOM	447	CA	ILE	A	550	18.940	7.433	22.391	1.00	56.71	A	C
ATOM	448	CB	ILE	A	550	18.836	8.022	23.803	1.00	53.72	A	C
ATOM	449	CG1	ILE	A	550	17.671	8.994	23.892	1.00	52.36	A	C
ATOM	450	CD1	ILE	A	550	17.114	9.109	25.269	1.00	53.68	A	C
ATOM	451	CG2	ILE	A	550	20.107	8.729	24.165	1.00	55.94	A	C
ATOM	452	C	ILE	A	550	17.637	6.729	22.001	1.00	59.34	A	C
ATOM	453	O	ILE	A	550	16.900	7.194	21.116	1.00	66.68	A	O
ATOM	454	N	HIS	A	551	17.373	5.604	22.658	1.00	51.80	A	N
ATOM	455	CA	HIS	A	551	16.178	4.818	22.424	1.00	43.88	A	C
ATOM	456	CB	HIS	A	551	16.541	3.483	21.800	1.00	40.60	A	C
ATOM	457	CG	HIS	A	551	15.387	2.764	21.175	1.00	40.32	A	C
ATOM	458	ND1	HIS	A	551	15.490	1.472	20.698	1.00	39.93	A	N
ATOM	459	CE1	HIS	A	551	14.326	1.097	20.200	1.00	39.40	A	C
ATOM	460	NE2	HIS	A	551	13.473	2.098	20.331	1.00	39.45	A	N
ATOM	461	CD2	HIS	A	551	14.112	3.154	20.935	1.00	39.43	A	C
ATOM	462	C	HIS	A	551	15.542	4.583	23.769	1.00	47.12	A	C
ATOM	463	O	HIS	A	551	14.323	4.661	23.893	1.00	53.18	A	O
ATOM	464	N	ASP	A	552	16.369	4.283	24.775	1.00	44.11	A	N
ATOM	465	CA	ASP	A	552	15.895	4.157	26.149	1.00	39.32	A	C
ATOM	466	CB	ASP	A	552	16.705	3.135	26.934	1.00	38.59	A	C
ATOM	467	CG	ASP	A	552	16.098	2.862	28.304	1.00	44.48	A	C
ATOM	468	OD1	ASP	A	552	16.576	3.424	29.316	1.00	42.47	A	O
ATOM	469	OD2	ASP	A	552	15.104	2.118	28.459	1.00	48.70	A	O
ATOM	470	C	ASP	A	552	15.955	5.494	26.879	1.00	36.72	A	C
ATOM	471	O	ASP	A	552	17.018	6.031	27.078	1.00	37.41	A	O
ATOM	472	N	VAL	A	553	14.810	6.017	27.295	1.00	35.32	A	N
ATOM	473	CA	VAL	A	553	14.755	7.260	28.051	1.00	35.91	A	C
ATOM	474	CB	VAL	A	553	13.381	7.424	28.755	1.00	32.99	A	C
ATOM	475	CG1	VAL	A	553	13.321	6.616	30.034	1.00	30.23	A	C
ATOM	476	CG2	VAL	A	553	13.042	8.903	28.997	1.00	26.91	A	C
ATOM	477	C	VAL	A	553	15.918	7.438	29.046	1.00	43.64	A	C
ATOM	478	O	VAL	A	553	16.364	8.568	29.276	1.00	52.45	A	O
ATOM	479	N	HIS	A	554	16.410	6.335	29.617	1.00	45.61	A	N
ATOM	480	CA	HIS	A	554	17.535	6.367	30.556	1.00	46.89	A	C
ATOM	481	CB	HIS	A	554	17.284	5.408	31.719	1.00	46.90	A	C
ATOM	482	CG	HIS	A	554	16.199	5.845	32.644	1.00	49.56	A	C
ATOM	483	ND1	HIS	A	554	14.981	5.208	32.711	1.00	52.02	A	N
ATOM	484	CE1	HIS	A	554	14.223	5.794	33.621	1.00	53.44	A	C
ATOM	485	NE2	HIS	A	554	14.909	6.789	34.151	1.00	56.69	A	N
ATOM	486	CD2	HIS	A	554	16.150	6.842	33.557	1.00	55.35	A	C
ATOM	487	C	HIS	A	554	18.850	5.985	29.883	1.00	46.94	A	C
ATOM	488	O	HIS	A	554	19.847	5.737	30.543	1.00	51.15	A	O
ATOM	489	N	GLY	A	555	18.845	5.900	28.566	1.00	48.30	A	N
ATOM	490	CA	GLY	A	555	20.049	5.588	27.816	1.00	50.65	A	C
ATOM	491	C	GLY	A	555	20.513	4.149	27.921	1.00	51.26	A	C
ATOM	492	O	GLY	A	555	21.633	3.828	27.492	1.00	54.15	A	O
ATOM	493	N	ARG	A	556	19.652	3.282	28.455	1.00	46.93	A	N
ATOM	494	CA	ARG	A	556	20.066	1.933	28.834	1.00	45.09	A	C
ATOM	495	CB	ARG	A	556	18.970	1.222	29.613	1.00	40.39	A	C
ATOM	496	CG	ARG	A	556	18.843	1.746	31.027	1.00	42.37	A	C
ATOM	497	CD	ARG	A	556	17.875	0.969	31.916	1.00	49.31	A	C
ATOM	498	NE	ARG	A	556	16.603	1.668	32.122	1.00	51.71	A	N
ATOM	499	CZ	ARG	A	556	15.444	1.287	31.602	1.00	54.36	A	C
ATOM	500	NH1	ARG	A	556	14.331	1.974	31.849	1.00	54.30	A	N
ATOM	501	NH2	ARG	A	556	15.393	0.207	30.832	1.00	59.72	A	N
ATOM	502	C	ARG	A	556	20.646	1.069	27.701	1.00	48.74	A	C
ATOM	503	O	ARG	A	556	21.717	0.463	27.859	1.00	51.93	A	O
ATOM	504	N	GLY	A	557	19.984	1.025	26.555	1.00	49.49	A	N
ATOM	505	CA	GLY	A	557	20.560	0.286	25.441	1.00	53.98	A	C
ATOM	506	C	GLY	A	557	21.794	0.931	24.810	1.00	54.64	A	C
ATOM	507	O	GLY	A	557	22.660	0.250	24.246	1.00	47.61	A	O
ATOM	508	N	ASP	A	558	21.882	2.253	24.935	1.00	59.36	A	N
ATOM	509	CA	ASP	A	558	22.565	3.049	23.925	1.00	64.13	A	C
ATOM	510	CB	ASP	A	558	21.577	4.015	23.225	1.00	64.08	A	C
ATOM	511	CG	ASP	A	558	20.132	3.875	23.724	1.00	63.54	A	C
ATOM	512	OD1	ASP	A	558	19.724	4.707	24.567	1.00	63.63	A	O
ATOM	513	OD2	ASP	A	558	19.331	2.988	23.327	1.00	60.19	A	O
ATOM	514	C	ASP	A	558	23.806	3.784	24.411	1.00	69.82	A	C
ATOM	515	O	ASP	A	558	23.799	5.010	24.542	1.00	73.90	A	O
ATOM	516	N	GLU	A	559	24.878	3.038	24.658	1.00	72.43	A	N
ATOM	517	CA	GLU	A	559	26.152	3.646	25.038	1.00	70.11	A	C
ATOM	518	CB	GLU	A	559	27.004	2.694	25.886	1.00	74.85	A	C
ATOM	519	CG	GLU	A	559	26.470	1.263	26.010	1.00	82.18	A	C
ATOM	520	CD	GLU	A	559	25.396	1.091	27.089	1.00	85.89	A	C
ATOM	521	OE1	GLU	A	559	25.367	1.875	28.068	1.00	86.56	A	O
ATOM	522	OE2	GLU	A	559	24.568	0.160	26.956	1.00	86.27	A	O
ATOM	523	C	GLU	A	559	26.870	4.047	23.766	1.00	65.20	A	C
ATOM	524	O	GLU	A	559	27.501	5.090	23.699	1.00	62.09	A	O
ATOM	525	N	LYS	A	560	26.716	3.229	22.737	1.00	66.52	A	N
ATOM	526	CA	LYS	A	560	27.395	3.455	21.473	1.00	70.54	A	C
ATOM	527	CB	LYS	A	560	27.572	2.128	20.719	1.00	78.87	A	C
ATOM	528	CG	LYS	A	560	29.014	1.865	20.249	1.00	86.89	A	C
ATOM	529	CD	LYS	A	560	29.280	0.382	19.952	1.00	91.41	A	C
ATOM	530	CE	LYS	A	560	29.837	0.176	18.530	1.00	94.26	A	C
ATOM	531	NZ	LYS	A	560	31.286	−0.214	18.490	1.00	93.72	A	N
ATOM	532	C	LYS	A	560	26.745	4.512	20.569	1.00	68.03	A	C
ATOM	533	O	LYS	A	560	27.231	4.742	19.460	1.00	69.10	A	O
ATOM	534	N	CYS	A	561	25.665	5.153	21.023	1.00	65.42	A	N
ATOM	535	CA	CYS	A	561	25.006	6.189	20.206	1.00	63.80	A	C
ATOM	536	CB	CYS	A	561	23.696	5.687	19.592	1.00	65.05	A	C
ATOM	537	SG	CYS	A	561	23.114	4.077	20.148	1.00	71.04	A	S
ATOM	538	C	CYS	A	561	24.779	7.541	20.900	1.00	60.62	A	C
ATOM	539	O	CYS	A	561	24.883	8.606	20.261	1.00	59.98	A	O
ATOM	540	N	LYS	A	562	24.471	7.479	22.195	1.00	55.53	A	N
ATOM	541	CA	LYS	A	562	24.241	8.649	23.053	1.00	51.59	A	C
ATOM	542	CB	LYS	A	562	24.284	8.204	24.517	1.00	50.33	A	C
ATOM	543	CG	LYS	A	562	23.663	9.172	25.506	1.00	50.06	A	C
ATOM	544	CD	LYS	A	562	23.388	8.476	26.829	1.00	49.50	A	C
ATOM	545	CE	LYS	A	562	24.453	8.784	27.862	1.00	50.51	A	C
ATOM	546	NZ	LYS	A	562	23.950	8.466	29.219	1.00	51.61	A	N
ATOM	547	C	LYS	A	562	25.199	9.842	22.855	1.00	48.90	A	C
ATOM	548	O	LYS	A	562	26.406	9.678	22.719	1.00	48.37	A	O
ATOM	549	N	GLN	A	563	24.635	11.041	22.856	1.00	47.04	A	N
ATOM	550	CA	GLN	A	563	25.396	12.278	22.799	1.00	43.96	A	C
ATOM	551	CB	GLN	A	563	25.290	12.881	21.402	1.00	41.41	A	C
ATOM	552	CG	GLN	A	563	26.214	12.301	20.363	1.00	43.30	A	C
ATOM	553	CD	GLN	A	563	26.240	13.135	19.075	1.00	47.28	A	C
ATOM	554	OE1	GLN	A	563	26.723	14.289	19.053	1.00	48.43	A	O
ATOM	555	NE2	GLN	A	563	25.730	12.549	17.997	1.00	45.76	A	N
ATOM	556	C	GLN	A	563	24.738	13.231	23.792	1.00	45.34	A	C
ATOM	557	O	GLN	A	563	23.577	13.604	23.597	1.00	49.13	A	O
ATOM	558	N	VAL	A	564	25.436	13.621	24.857	1.00	41.21	A	N
ATOM	559	CA	VAL	A	564	24.840	14.595	25.780	1.00	39.36	A	C
ATOM	560	CB	VAL	A	564	24.832	14.133	27.272	1.00	39.41	A	C
ATOM	561	CG1	VAL	A	564	24.330	12.699	27.395	1.00	37.33	A	C
ATOM	562	CG2	VAL	A	564	26.203	14.301	27.936	1.00	44.32	A	C
ATOM	563	C	VAL	A	564	25.437	15.988	25.614	1.00	38.92	A	C
ATOM	564	O	VAL	A	564	26.659	16.162	25.656	1.00	44.75	A	O
ATOM	565	N	LEU	A	565	24.567	16.972	25.414	1.00	34.38	A	N
ATOM	566	CA	LEU	A	565	25.001	18.338	25.159	1.00	34.56	A	C
ATOM	567	CB	LEU	A	565	24.632	18.727	23.738	1.00	35.95	A	C
ATOM	568	CG	LEU	A	565	25.329	17.895	22.669	1.00	42.59	A	C
ATOM	569	CD1	LEU	A	565	24.769	18.194	21.290	1.00	45.02	A	C
ATOM	570	CD2	LEU	A	565	26.853	18.128	22.703	1.00	48.14	A	C
ATOM	571	C	LEU	A	565	24.384	19.323	26.131	1.00	34.92	A	C
ATOM	572	O	LEU	A	565	23.209	19.217	26.442	1.00	39.73	A	O
ATOM	573	N	ASN	A	566	25.169	20.281	26.610	1.00	35.34	A	N
ATOM	574	CA	ASN	A	566	24.633	21.358	27.443	1.00	39.72	A	C
ATOM	575	CB	ASN	A	566	25.761	22.065	28.194	1.00	47.83	A	C
ATOM	576	CG	ASN	A	566	26.303	21.245	29.356	1.00	54.40	A	C
ATOM	577	OD1	ASN	A	566	25.550	20.864	30.252	1.00	57.20	A	O
ATOM	578	ND2	ASN	A	566	27.620	20.980	29.353	1.00	55.33	A	N
ATOM	579	C	ASN	A	566	23.839	22.362	26.601	1.00	38.42	A	C
ATOM	580	O	ASN	A	566	24.045	22.464	25.398	1.00	40.20	A	O
ATOM	581	N	VAL	A	567	22.928	23.099	27.217	1.00	37.71	A	N
ATOM	582	CA	VAL	A	567	22.124	24.045	26.456	1.00	42.36	A	C
ATOM	583	CB	VAL	A	567	20.658	24.000	26.886	1.00	44.62	A	C
ATOM	584	CG1	VAL	A	567	19.933	25.232	26.408	1.00	45.19	A	C
ATOM	585	CG2	VAL	A	567	19.974	22.736	26.339	1.00	47.75	A	C
ATOM	586	C	VAL	A	567	22.662	25.460	26.616	1.00	48.80	A	C
ATOM	587	O	VAL	A	567	22.792	25.953	27.742	1.00	56.77	A	O
ATOM	588	N	SER	A	568	22.958	26.118	25.496	1.00	47.82	A	N
ATOM	589	CA	SER	A	568	23.579	27.444	25.531	1.00	45.87	A	C
ATOM	590	CB	SER	A	568	24.660	27.547	24.465	1.00	48.47	A	C
ATOM	591	OG	SER	A	568	24.078	27.925	23.233	1.00	53.38	A	O
ATOM	592	C	SER	A	568	22.613	28.622	25.378	1.00	42.18	A	C
ATOM	593	O	SER	A	568	22.913	29.727	25.817	1.00	43.85	A	O
ATOM	594	N	GLN	A	569	21.471	28.397	24.745	1.00	38.76	A	N
ATOM	595	CA	GLN	A	569	20.524	29.476	24.495	1.00	39.06	A	C
ATOM	596	CB	GLN	A	569	20.852	30.165	23.176	1.00	45.06	A	C
ATOM	597	CG	GLN	A	569	21.818	31.327	23.243	1.00	50.32	A	C
ATOM	598	CD	GLN	A	569	22.452	31.614	21.888	1.00	51.10	A	C
ATOM	599	OE1	GLN	A	569	23.693	31.665	21.757	1.00	48.40	A	O
ATOM	600	NE2	GLN	A	569	21.603	31.787	20.870	1.00	49.35	A	N
ATOM	601	C	GLN	A	569	19.086	28.985	24.391	1.00	37.54	A	C
ATOM	602	O	GLN	A	569	18.804	27.889	23.871	1.00	34.48	A	O
ATOM	603	N	LEU	A	570	18.175	29.826	24.855	1.00	33.79	A	N
ATOM	604	CA	LEU	A	570	16.754	29.603	24.661	1.00	34.68	A	C
ATOM	605	CB	LEU	A	570	16.050	29.567	26.008	1.00	31.54	A	C
ATOM	606	CG	LEU	A	570	15.741	28.169	26.504	1.00	38.19	A	C
ATOM	607	CD1	LEU	A	570	16.987	27.329	26.642	1.00	37.37	A	C
ATOM	608	CD2	LEU	A	570	15.009	28.238	27.826	1.00	43.38	A	C
ATOM	609	C	LEU	A	570	16.227	30.764	23.838	1.00	39.24	A	C
ATOM	610	O	LEU	A	570	16.413	31.928	24.209	1.00	46.68	A	O
ATOM	611	N	VAL	A	571	15.605	30.490	22.700	1.00	36.53	A	N
ATOM	612	CA	VAL	A	571	15.016	31.598	21.971	1.00	31.35	A	C
ATOM	613	CB	VAL	A	571	15.680	31.835	20.589	1.00	26.55	A	C
ATOM	614	CG1	VAL	A	571	15.038	33.029	19.908	1.00	25.85	A	C
ATOM	615	CG2	VAL	A	571	17.181	32.066	20.725	1.00	16.87	A	C
ATOM	616	C	VAL	A	571	13.541	31.310	21.851	1.00	32.50	A	C
ATOM	617	O	VAL	A	571	13.157	30.403	21.118	1.00	37.07	A	O
ATOM	618	N	TYR	A	572	12.726	32.048	22.602	1.00	34.10	A	N
ATOM	619	CA	TYR	A	572	11.272	31.849	22.600	1.00	40.89	A	C
ATOM	620	CB	TYR	A	572	10.615	32.516	23.822	1.00	39.82	A	C
ATOM	621	CG	TYR	A	572	10.908	31.851	25.151	1.00	42.43	A	C
ATOM	622	CD1	TYR	A	572	12.195	31.865	25.682	1.00	47.25	A	C
ATOM	623	CE1	TYR	A	572	12.481	31.252	26.903	1.00	47.44	A	C
ATOM	624	CZ	TYR	A	572	11.466	30.625	27.612	1.00	47.09	A	C
ATOM	625	OH	TYR	A	572	11.778	30.030	28.819	1.00	49.58	A	O
ATOM	626	CE2	TYR	A	572	10.167	30.603	27.113	1.00	44.22	A	C
ATOM	627	CD2	TYR	A	572	9.898	31.216	25.886	1.00	43.00	A	C
ATOM	628	C	TYR	A	572	10.692	32.432	21.307	1.00	46.28	A	C
ATOM	629	O	TYR	A	572	11.125	33.505	20.854	1.00	48.74	A	O
ATOM	630	N	GLY	A	573	9.727	31.731	20.710	1.00	43.96	A	N
ATOM	631	CA	GLY	A	573	9.081	32.215	19.500	1.00	44.58	A	C
ATOM	632	C	GLY	A	573	7.976	33.201	19.824	1.00	47.16	A	C
ATOM	633	O	GLY	A	573	7.668	33.398	20.991	1.00	48.67	A	O
ATOM	634	N	PRO	A	574	7.371	33.793	18.793	1.00	47.15	A	N
ATOM	635	CA	PRO	A	574	6.301	34.802	18.916	1.00	48.36	A	C
ATOM	636	CB	PRO	A	574	5.575	34.658	17.599	1.00	44.73	A	C
ATOM	637	CG	PRO	A	574	6.678	34.358	16.654	1.00	47.04	A	C
ATOM	638	CD	PRO	A	574	7.703	33.524	17.384	1.00	45.01	A	C
ATOM	639	C	PRO	A	574	5.298	34.620	20.045	1.00	55.13	A	C
ATOM	640	O	PRO	A	574	5.043	33.489	20.451	1.00	58.51	A	O
ATOM	641	N	GLU	A	575	4.714	35.728	20.501	1.00	63.03	A	N
ATOM	642	CA	GLU	A	575	3.846	35.761	21.684	1.00	72.31	A	C
ATOM	643	CB	GLU	A	575	3.172	37.131	21.825	1.00	82.86	A	C
ATOM	644	CG	GLU	A	575	2.901	37.549	23.272	1.00	96.88	A	C
ATOM	645	CD	GLU	A	575	1.466	38.025	23.498	1.00	106.66	A	C
ATOM	646	OE1	GLU	A	575	1.117	39.114	22.971	1.00	110.29	A	O
ATOM	647	OE2	GLU	A	575	0.686	37.317	24.198	1.00	108.80	A	O
ATOM	648	C	GLU	A	575	2.803	34.646	21.752	1.00	73.37	A	C
ATOM	649	O	GLU	A	575	2.685	33.953	22.773	1.00	75.73	A	O
ATOM	650	N	GLY	A	576	2.055	34.466	20.669	1.00	72.32	A	N
ATOM	651	CA	GLY	A	576	1.073	33.397	20.599	1.00	72.86	A	C
ATOM	652	C	GLY	A	576	1.612	31.997	20.886	1.00	69.25	A	C
ATOM	653	O	GLY	A	576	1.072	31.285	21.730	1.00	71.38	A	O
ATOM	654	N	SER	A	577	2.688	31.626	20.194	1.00	64.77	A	N
ATOM	655	CA	SER	A	577	3.167	30.247	20.118	1.00	59.78	A	C
ATOM	656	CB	SER	A	577	4.297	30.122	19.078	1.00	55.51	A	C
ATOM	657	OG	SER	A	577	5.485	30.795	19.464	1.00	45.00	A	O
ATOM	658	C	SER	A	577	3.665	29.720	21.443	1.00	61.46	A	C
ATOM	659	O	SER	A	577	3.946	30.494	22.368	1.00	65.82	A	O
ATOM	660	N	ASP	A	578	3.774	28.397	21.530	1.00	54.85	A	N
ATOM	661	CA	ASP	A	578	4.485	27.800	22.638	1.00	47.81	A	C
ATOM	662	CB	ASP	A	578	3.616	26.766	23.371	1.00	50.27	A	C
ATOM	663	CG	ASP	A	578	2.324	27.373	23.933	1.00	53.63	A	C
ATOM	664	OD1	ASP	A	578	2.383	28.234	24.849	1.00	52.49	A	O
ATOM	665	OD2	ASP	A	578	1.197	27.053	23.501	1.00	56.11	A	O
ATOM	666	C	ASP	A	578	5.784	27.212	22.119	1.00	43.41	A	C
ATOM	667	O	ASP	A	578	6.335	26.294	22.707	1.00	47.68	A	O
ATOM	668	N	LEU	A	579	6.273	27.751	21.010	1.00	39.96	A	N
ATOM	669	CA	LEU	A	579	7.542	27.309	20.438	1.00	43.17	A	C
ATOM	670	CB	LEU	A	579	7.651	27.727	18.968	1.00	40.90	A	C
ATOM	671	CG	LEU	A	579	6.831	26.942	17.947	1.00	43.06	A	C
ATOM	672	CD1	LEU	A	579	7.406	27.120	16.571	1.00	39.25	A	C
ATOM	673	CD2	LEU	A	579	6.717	25.446	18.311	1.00	45.29	A	C
ATOM	674	C	LEU	A	579	8.716	27.910	21.188	1.00	47.30	A	C
ATOM	675	O	LEU	A	579	8.645	29.065	21.622	1.00	57.38	A	O
ATOM	676	N	VAL	A	580	9.794	27.142	21.342	1.00	41.85	A	N
ATOM	677	CA	VAL	A	580	11.087	27.720	21.722	1.00	39.69	A	C
ATOM	678	CB	VAL	A	580	11.323	27.831	23.266	1.00	38.42	A	C
ATOM	679	CG1	VAL	A	580	10.460	26.871	24.001	1.00	37.78	A	C
ATOM	680	CG2	VAL	A	580	12.810	27.613	23.628	1.00	38.21	A	C
ATOM	681	C	VAL	A	580	12.200	26.952	21.057	1.00	37.51	A	C
ATOM	682	O	VAL	A	580	12.176	25.729	21.030	1.00	40.20	A	O
ATOM	683	N	LEU	A	581	13.159	27.691	20.511	1.00	35.83	A	N
ATOM	684	CA	LEU	A	581	14.315	27.111	19.859	1.00	35.33	A	C
ATOM	685	CB	LEU	A	581	14.664	27.906	18.605	1.00	34.56	A	C
ATOM	686	CG	LEU	A	581	13.805	27.569	17.393	1.00	34.36	A	C
ATOM	687	CD1	LEU	A	581	13.948	28.631	16.319	1.00	34.77	A	C
ATOM	688	CD2	LEU	A	581	14.208	26.222	16.862	1.00	34.20	A	C
ATOM	689	C	LEU	A	581	15.503	27.060	20.806	1.00	36.62	A	C
ATOM	690	O	LEU	A	581	15.945	28.092	21.337	1.00	37.07	A	O
ATOM	691	N	MET	A	582	16.014	25.847	20.991	1.00	33.93	A	N
ATOM	692	CA	MET	A	582	17.113	25.569	21.898	1.00	36.12	A	C
ATOM	693	CB	MET	A	582	16.844	24.225	22.551	1.00	37.17	A	C
ATOM	694	CG	MET	A	582	17.334	24.040	23.963	1.00	38.27	A	C
ATOM	695	SD	MET	A	582	16.405	22.691	24.755	1.00	44.57	A	S
ATOM	696	CE	MET	A	582	16.599	21.366	23.601	1.00	41.92	A	C
ATOM	697	C	MET	A	582	18.433	25.486	21.139	1.00	39.39	A	C
ATOM	698	O	MET	A	582	18.565	24.668	20.220	1.00	41.71	A	O
ATOM	699	N	LYS	A	583	19.406	26.320	21.516	1.00	40.97	A	N
ATOM	700	CA	LYS	A	583	20.788	26.203	21.001	1.00	40.86	A	C
ATOM	701	CB	LYS	A	583	21.488	27.576	20.892	1.00	37.40	A	C
ATOM	702	CG	LYS	A	583	22.197	27.812	19.560	1.00	39.18	A	C
ATOM	703	CD	LYS	A	583	23.728	27.624	19.622	1.00	42.16	A	C
ATOM	704	CE	LYS	A	583	24.496	28.615	18.693	1.00	39.55	A	C
ATOM	705	NZ	LYS	A	583	25.333	29.620	19.428	1.00	34.06	A	N
ATOM	706	C	LYS	A	583	21.601	25.311	21.925	1.00	39.35	A	C
ATOM	707	O	LYS	A	583	21.647	25.552	23.140	1.00	42.05	A	O
ATOM	708	N	LEU	A	584	22.238	24.284	21.377	1.00	34.24	A	N
ATOM	709	CA	LEU	A	584	23.117	23.471	22.213	1.00	38.37	A	C
ATOM	710	CB	LEU	A	584	22.919	21.977	21.963	1.00	35.18	A	C
ATOM	711	CG	LEU	A	584	22.189	21.527	20.706	1.00	32.63	A	C
ATOM	712	CD1	LEU	A	584	23.174	21.472	19.551	1.00	33.30	A	C
ATOM	713	CD2	LEU	A	584	21.544	20.166	20.929	1.00	25.36	A	C
ATOM	714	C	LEU	A	584	24.591	23.883	22.092	1.00	43.10	A	C
ATOM	715	O	LEU	A	584	25.049	24.272	21.014	1.00	46.68	A	O
ATOM	716	N	ALA	A	585	25.317	23.809	23.208	1.00	46.13	A	N
ATOM	717	CA	ALA	A	585	26.678	24.344	23.300	1.00	53.33	A	C
ATOM	718	CB	ALA	A	585	27.050	24.598	24.763	1.00	54.74	A	C
ATOM	719	C	ALA	A	585	27.723	23.449	22.628	1.00	57.39	A	C
ATOM	720	O	ALA	A	585	28.535	22.822	23.311	1.00	62.76	A	O
ATOM	721	N	ARG	A	586	27.717	23.444	21.294	1.00	55.41	A	N
ATOM	722	CA	ARG	A	586	28.465	22.506	20.456	1.00	53.60	A	C
ATOM	723	CB	ARG	A	586	29.282	21.491	21.273	1.00	60.66	A	C
ATOM	724	CG	ARG	A	586	29.413	20.068	20.657	1.00	69.53	A	C
ATOM	725	CD	ARG	A	586	30.358	19.105	21.403	1.00	77.97	A	C
ATOM	726	NE	ARG	A	586	31.213	19.811	22.367	1.00	86.84	A	N
ATOM	727	CZ	ARG	A	586	31.276	19.544	23.671	1.00	90.03	A	C
ATOM	728	NH1	ARG	A	586	30.543	18.561	24.187	1.00	92.95	A	N
ATOM	729	NH2	ARG	A	586	32.074	20.259	24.461	1.00	88.53	A	N
ATOM	730	C	ARG	A	586	27.416	21.776	19.669	1.00	50.51	A	C
ATOM	731	O	ARG	A	586	26.431	21.325	20.260	1.00	51.03	A	O
ATOM	732	N	PRO	A	587	27.602	21.660	18.351	1.00	48.26	A	N
ATOM	733	CA	PRO	A	587	26.690	20.896	17.504	1.00	51.39	A	C
ATOM	734	CB	PRO	A	587	27.310	21.057	16.113	1.00	46.83	A	C
ATOM	735	CG	PRO	A	587	27.984	22.297	16.190	1.00	43.63	A	C
ATOM	736	CD	PRO	A	587	28.665	22.255	17.536	1.00	46.48	A	C
ATOM	737	C	PRO	A	587	26.627	19.418	17.865	1.00	53.08	A	C
ATOM	738	O	PRO	A	587	27.610	18.847	18.349	1.00	58.56	A	O
ATOM	739	N	ALA	A	588	25.466	18.819	17.639	1.00	48.21	A	N
ATOM	740	CA	ALA	A	588	25.363	17.377	17.609	1.00	51.17	A	C
ATOM	741	CB	ALA	A	588	23.919	16.960	17.465	1.00	56.53	A	C
ATOM	742	C	ALA	A	588	26.166	16.883	16.422	1.00	52.04	A	C
ATOM	743	O	ALA	A	588	26.262	17.561	15.389	1.00	52.47	A	O
ATOM	744	N	VAL	A	589	26.760	15.709	16.576	1.00	52.26	A	N
ATOM	745	CA	VAL	A	589	27.524	15.106	15.496	1.00	51.82	A	C
ATOM	746	CB	VAL	A	589	28.839	14.523	16.031	1.00	52.02	A	C
ATOM	747	CG1	VAL	A	589	29.159	13.154	15.413	1.00	52.14	A	C
ATOM	748	CG2	VAL	A	589	29.965	15.527	15.798	1.00	55.27	A	C
ATOM	749	C	VAL	A	589	26.626	14.065	14.848	1.00	49.96	A	C
ATOM	750	O	VAL	A	589	26.070	13.211	15.540	1.00	48.25	A	O
ATOM	751	N	LEU	A	590	26.451	14.151	13.532	1.00	47.38	A	N
ATOM	752	CA	LEU	A	590	25.423	13.340	12.883	1.00	45.62	A	C
ATOM	753	CB	LEU	A	590	24.685	14.125	11.789	1.00	41.44	A	C
ATOM	754	CG	LEU	A	590	24.303	15.586	12.053	1.00	40.18	A	C
ATOM	755	CD1	LEU	A	590	23.703	16.257	10.818	1.00	38.93	A	C
ATOM	756	CD2	LEU	A	590	23.344	15.693	13.217	1.00	41.47	A	C
ATOM	757	C	LEU	A	590	25.933	12.006	12.351	1.00	49.38	A	C
ATOM	758	O	LEU	A	590	26.514	11.935	11.270	1.00	53.92	A	O
ATOM	759	N	ASP	A	591	25.731	10.948	13.124	1.00	51.83	A	N
ATOM	760	CA	ASP	A	591	25.926	9.608	12.597	1.00	58.39	A	C
ATOM	761	CB	ASP	A	591	26.476	8.634	13.657	1.00	61.53	A	C
ATOM	762	CG	ASP	A	591	26.002	8.950	15.068	1.00	66.29	A	C
ATOM	763	OD1	ASP	A	591	24.841	9.389	15.249	1.00	69.83	A	O
ATOM	764	OD2	ASP	A	591	26.728	8.769	16.068	1.00	67.55	A	O
ATOM	765	C	ASP	A	591	24.608	9.112	12.009	1.00	61.73	A	C
ATOM	766	O	ASP	A	591	23.817	9.898	11.466	1.00	60.56	A	O
ATOM	767	N	ASP	A	592	24.385	7.806	12.120	1.00	65.41	A	N
ATOM	768	CA	ASP	A	592	23.149	7.182	11.686	1.00	66.25	A	C
ATOM	769	CB	ASP	A	592	23.412	5.723	11.323	1.00	70.88	A	C
ATOM	770	CG	ASP	A	592	24.441	5.578	10.196	1.00	76.70	A	C
ATOM	771	OD1	ASP	A	592	24.462	4.512	9.539	1.00	76.48	A	O
ATOM	772	OD2	ASP	A	592	25.270	6.475	9.893	1.00	79.23	A	O
ATOM	773	C	ASP	A	592	22.115	7.295	12.790	1.00	65.00	A	C
ATOM	774	O	ASP	A	592	20.915	7.302	12.529	1.00	69.47	A	O
ATOM	775	N	PHE	A	593	22.591	7.416	14.023	1.00	60.82	A	N
ATOM	776	CA	PHE	A	593	21.724	7.541	15.187	1.00	57.43	A	C
ATOM	777	CB	PHE	A	593	22.426	6.945	16.393	1.00	58.58	A	C
ATOM	778	CG	PHE	A	593	22.879	5.555	16.160	1.00	64.33	A	C
ATOM	779	CD1	PHE	A	593	24.232	5.255	16.095	1.00	67.61	A	C
ATOM	780	CE1	PHE	A	593	24.658	3.949	15.847	1.00	72.30	A	C
ATOM	781	CZ	PHE	A	593	23.706	2.924	15.645	1.00	73.94	A	C
ATOM	782	CE2	PHE	A	593	22.342	3.222	15.695	1.00	71.33	A	C
ATOM	783	CD2	PHE	A	593	21.941	4.539	15.943	1.00	68.72	A	C
ATOM	784	C	PHE	A	593	21.247	8.966	15.460	1.00	55.48	A	C
ATOM	785	O	PHE	A	593	20.196	9.182	16.089	1.00	58.42	A	O
ATOM	786	N	VAL	A	594	22.002	9.943	14.979	1.00	46.31	A	N
ATOM	787	CA	VAL	A	594	21.563	11.314	15.107	1.00	42.48	A	C
ATOM	788	CB	VAL	A	594	22.511	12.101	16.006	1.00	39.97	A	C
ATOM	789	CG1	VAL	A	594	22.170	13.566	15.996	1.00	41.29	A	C
ATOM	790	CG2	VAL	A	594	22.421	11.576	17.418	1.00	39.95	A	C
ATOM	791	C	VAL	A	594	21.365	11.966	13.739	1.00	45.57	A	C
ATOM	792	O	VAL	A	594	22.298	12.067	12.937	1.00	51.69	A	O
ATOM	793	N	SER	A	595	20.130	12.382	13.473	1.00	44.40	A	N
ATOM	794	CA	SER	A	595	19.777	13.041	12.214	1.00	46.13	A	C
ATOM	795	CB	SER	A	595	19.079	12.046	11.258	1.00	48.36	A	C
ATOM	796	OG	SER	A	595	17.667	11.921	11.450	1.00	42.75	A	O
ATOM	797	C	SER	A	595	18.901	14.258	12.486	1.00	46.72	A	C
ATOM	798	O	SER	A	595	18.242	14.322	13.521	1.00	53.75	A	O
ATOM	799	N	THR	A	596	18.892	15.227	11.581	1.00	40.90	A	N
ATOM	800	CA	THR	A	596	17.956	16.337	11.720	1.00	39.67	A	C
ATOM	801	CB	THR	A	596	18.517	17.621	11.097	1.00	44.54	A	C
ATOM	802	OG1	THR	A	596	18.456	17.514	9.664	1.00	46.83	A	O
ATOM	803	CG2	THR	A	596	20.006	17.800	11.412	1.00	44.46	A	C
ATOM	804	C	THR	A	596	16.683	15.984	10.990	1.00	35.98	A	C
ATOM	805	O	THR	A	596	16.735	15.238	10.024	1.00	39.34	A	O
ATOM	806	N	ILE	A	597	15.550	16.533	11.421	1.00	33.54	A	N
ATOM	807	CA	ILE	A	597	14.320	16.452	10.617	1.00	36.14	A	C
ATOM	808	CB	ILE	A	597	13.059	16.214	11.492	1.00	34.21	A	C
ATOM	809	CG1	ILE	A	597	11.823	16.072	10.603	1.00	37.04	A	C
ATOM	810	CD1	ILE	A	597	10.913	14.943	10.975	1.00	41.42	A	C
ATOM	811	CG2	ILE	A	597	12.842	17.358	12.464	1.00	32.87	A	C
ATOM	812	C	ILE	A	597	14.132	17.669	9.681	1.00	36.20	A	C
ATOM	813	O	ILE	A	597	14.605	18.768	9.974	1.00	39.83	A	O
ATOM	814	N	ASP	A	598	13.444	17.466	8.559	1.00	33.50	A	N
ATOM	815	CA	ASP	A	598	13.169	18.555	7.632	1.00	38.28	A	C
ATOM	816	CB	ASP	A	598	12.742	18.014	6.258	1.00	48.59	A	C
ATOM	817	CG	ASP	A	598	13.926	17.791	5.298	1.00	57.53	A	C
ATOM	818	OD1	ASP	A	598	15.099	17.784	5.742	1.00	62.59	A	O
ATOM	819	OD2	ASP	A	598	13.772	17.607	4.067	1.00	60.83	A	O
ATOM	820	C	ASP	A	598	12.094	19.456	8.227	1.00	35.55	A	C
ATOM	821	O	ASP	A	598	11.575	19.162	9.294	1.00	35.49	A	O
ATOM	822	N	LEU	A	599	11.774	20.550	7.538	1.00	34.01	A	N
ATOM	823	CA	LEU	A	599	10.771	21.514	7.981	1.00	30.60	A	C
ATOM	824	CB	LEU	A	599	11.468	22.770	8.469	1.00	30.58	A	C
ATOM	825	CG	LEU	A	599	11.894	23.007	9.904	1.00	31.49	A	C
ATOM	826	CD1	LEU	A	599	12.389	24.428	9.975	1.00	33.85	A	C
ATOM	827	CD2	LEU	A	599	10.752	22.828	10.850	1.00	34.76	A	C
ATOM	828	C	LEU	A	599	9.929	21.917	6.785	1.00	31.69	A	C
ATOM	829	O	LEU	A	599	10.417	21.832	5.664	1.00	36.90	A	O
ATOM	830	N	PRO	A	600	8.705	22.405	7.000	1.00	31.33	A	N
ATOM	831	CA	PRO	A	600	7.858	22.898	5.906	1.00	35.28	A	C
ATOM	832	CB	PRO	A	600	6.507	23.062	6.581	1.00	29.03	A	C
ATOM	833	CG	PRO	A	600	6.634	22.344	7.838	1.00	29.28	A	C
ATOM	834	CD	PRO	A	600	8.019	22.535	8.290	1.00	30.60	A	C
ATOM	835	C	PRO	A	600	8.289	24.265	5.340	1.00	44.44	A	C
ATOM	836	O	PRO	A	600	9.114	24.967	5.946	1.00	45.45	A	O
ATOM	837	N	ASN	A	601	7.740	24.626	4.176	1.00	48.63	A	N
ATOM	838	CA	ASN	A	601	7.846	25.994	3.658	1.00	49.79	A	C
ATOM	839	CB	ASN	A	601	7.684	26.017	2.141	1.00	54.84	A	C
ATOM	840	CG	ASN	A	601	9.009	26.081	1.424	1.00	60.02	A	C
ATOM	841	OD1	ASN	A	601	9.924	25.301	1.715	1.00	62.59	A	O
ATOM	842	ND2	ASN	A	601	9.132	27.017	0.485	1.00	61.65	A	N
ATOM	843	C	ASN	A	601	6.797	26.881	4.316	1.00	46.76	A	C
ATOM	844	O	ASN	A	601	5.729	26.396	4.691	1.00	48.29	A	O
ATOM	845	N	TYR	A	602	7.089	28.172	4.453	1.00	41.68	A	N
ATOM	846	CA	TYR	A	602	6.260	29.049	5.275	1.00	38.41	A	C
ATOM	847	CB	TYR	A	602	6.682	30.523	5.147	1.00	38.69	A	C
ATOM	848	CG	TYR	A	602	5.668	31.503	5.700	1.00	40.48	A	C
ATOM	849	CD1	TYR	A	602	5.116	31.332	6.968	1.00	45.45	A	C
ATOM	850	CE1	TYR	A	602	4.169	32.218	7.469	1.00	48.45	A	C
ATOM	851	CZ	TYR	A	602	3.774	33.291	6.698	1.00	48.94	A	C
ATOM	852	OH	TYR	A	602	2.842	34.166	7.192	1.00	56.21	A	O
ATOM	853	CE2	TYR	A	602	4.305	33.487	5.443	1.00	44.43	A	C
ATOM	854	CD2	TYR	A	602	5.246	32.591	4.950	1.00	42.93	A	C
ATOM	855	C	TYR	A	602	4.752	28.872	5.055	1.00	40.51	A	C
ATOM	856	O	TYR	A	602	4.026	28.531	5.988	1.00	43.26	A	O
ATOM	857	N	GLY	A	603	4.277	29.079	3.833	1.00	42.23	A	N
ATOM	858	CA	GLY	A	603	2.839	29.087	3.583	1.00	43.75	A	C
ATOM	859	C	GLY	A	603	2.105	27.749	3.576	1.00	42.17	A	C
ATOM	860	O	GLY	A	603	0.885	27.712	3.750	1.00	41.68	A	O
ATOM	861	N	SER	A	604	2.860	26.666	3.399	1.00	40.29	A	N
ATOM	862	CA	SER	A	604	2.350	25.319	3.121	1.00	39.35	A	C
ATOM	863	CB	SER	A	604	3.489	24.308	3.264	1.00	36.47	A	C
ATOM	864	OG	SER	A	604	4.073	24.379	4.548	1.00	32.06	A	O
ATOM	865	C	SER	A	604	1.132	24.815	3.900	1.00	43.44	A	C
ATOM	866	O	SER	A	604	0.886	25.206	5.043	1.00	44.15	A	O
ATOM	867	N	THR	A	605	0.376	23.933	3.249	1.00	49.57	A	N
ATOM	868	CA	THR	A	605	−0.707	23.190	3.891	1.00	54.12	A	C
ATOM	869	CB	THR	A	605	−2.016	23.296	3.074	1.00	53.99	A	C
ATOM	870	OG1	THR	A	605	−1.719	23.660	1.715	1.00	50.74	A	O
ATOM	871	CG2	THR	A	605	−2.905	24.422	3.618	1.00	53.92	A	C
ATOM	872	C	THR	A	605	−0.327	21.717	4.016	1.00	55.98	A	C
ATOM	873	O	THR	A	605	0.789	21.317	3.662	1.00	59.51	A	O
ATOM	874	N	ILE	A	606	−1.259	20.925	4.545	1.00	51.78	A	N
ATOM	875	CA	ILE	A	606	−1.223	19.465	4.436	1.00	46.91	A	C
ATOM	876	CB	ILE	A	606	−0.730	18.770	5.719	1.00	43.94	A	C
ATOM	877	CG1	ILE	A	606	−0.568	19.764	6.889	1.00	52.16	A	C
ATOM	878	CD1	ILE	A	606	−1.883	20.487	7.367	1.00	55.17	A	C
ATOM	879	CG2	ILE	A	606	0.531	17.972	5.410	1.00	35.80	A	C
ATOM	880	C	ILE	A	606	−2.621	18.970	4.105	1.00	46.21	A	C
ATOM	881	O	ILE	A	606	−3.602	19.485	4.653	1.00	49.11	A	O
ATOM	882	N	PRO	A	607	−2.721	17.976	3.224	1.00	40.22	A	N
ATOM	883	CA	PRO	A	607	−4.022	17.440	2.854	1.00	38.66	A	C
ATOM	884	CB	PRO	A	607	−3.695	16.531	1.678	1.00	40.37	A	C
ATOM	885	CG	PRO	A	607	−2.274	16.854	1.306	1.00	39.77	A	C
ATOM	886	CD	PRO	A	607	−1.623	17.263	2.547	1.00	38.08	A	C
ATOM	887	C	PRO	A	607	−4.561	16.628	4.020	1.00	42.73	A	C
ATOM	888	O	PRO	A	607	−3.782	16.103	4.830	1.00	39.65	A	O
ATOM	889	N	GLU	A	608	−5.884	16.539	4.114	1.00	48.15	A	N
ATOM	890	CA	GLU	A	608	−6.518	15.771	5.178	1.00	50.92	A	C
ATOM	891	CB	GLU	A	608	−8.026	15.990	5.172	1.00	57.50	A	C
ATOM	892	CG	GLU	A	608	−8.539	16.639	6.442	1.00	66.78	A	C
ATOM	893	CD	GLU	A	608	−9.840	17.392	6.234	1.00	75.65	A	C
ATOM	894	OE1	GLU	A	608	−10.170	17.712	5.066	1.00	77.06	A	O
ATOM	895	OE2	GLU	A	608	−10.537	17.664	7.243	1.00	80.92	A	O
ATOM	896	C	GLU	A	608	−6.194	14.288	5.060	1.00	46.92	A	C
ATOM	897	O	GLU	A	608	−5.885	13.787	3.981	1.00	45.35	A	O
ATOM	898	N	LYS	A	609	−6.256	13.594	6.187	1.00	45.44	A	N
ATOM	899	CA	LYS	A	609	−5.980	12.165	6.245	1.00	46.36	A	C
ATOM	900	CB	LYS	A	609	−7.001	11.366	5.423	1.00	49.56	A	C
ATOM	901	CG	LYS	A	609	−8.251	10.957	6.197	1.00	57.13	A	C
ATOM	902	CD	LYS	A	609	−9.444	11.878	5.894	1.00	63.83	A	C
ATOM	903	CE	LYS	A	609	−10.740	11.083	5.628	1.00	68.12	A	C
ATOM	904	NZ	LYS	A	609	−10.818	10.437	4.264	1.00	68.00	A	N
ATOM	905	C	LYS	A	609	−4.559	11.829	5.823	1.00	44.97	A	C
ATOM	906	O	LYS	A	609	−4.269	10.687	5.485	1.00	47.16	A	O
ATOM	907	N	THR	A	610	−3.676	12.822	5.837	1.00	45.02	A	N
ATOM	908	CA	THR	A	610	−2.257	12.558	5.646	1.00	45.55	A	C
ATOM	909	CB	THR	A	610	−1.477	13.849	5.416	1.00	44.23	A	C
ATOM	910	OG1	THR	A	610	−1.966	14.493	4.233	1.00	44.60	A	O
ATOM	911	CG2	THR	A	610	−0.043	13.519	5.053	1.00	45.14	A	C
ATOM	912	C	THR	A	610	−1.768	11.862	6.894	1.00	45.88	A	C
ATOM	913	O	THR	A	610	−2.047	12.321	8.000	1.00	50.74	A	O
ATOM	914	N	SER	A	611	−1.064	10.749	6.730	1.00	44.73	A	N
ATOM	915	CA	SER	A	611	−0.715	9.928	7.885	1.00	48.38	A	C
ATOM	916	CB	SER	A	611	−0.485	8.475	7.476	1.00	53.73	A	C
ATOM	917	OG	SER	A	611	0.802	8.291	6.929	1.00	59.49	A	O
ATOM	918	C	SER	A	611	0.487	10.489	8.618	1.00	46.61	A	C
ATOM	919	O	SER	A	611	1.387	11.030	7.990	1.00	48.47	A	O
ATOM	920	N	CYS	A	612	0.487	10.368	9.945	1.00	44.70	A	N
ATOM	921	CA	CYS	A	612	1.511	10.980	10.790	1.00	42.57	A	C
ATOM	922	CB	CYS	A	612	1.011	12.319	11.297	1.00	44.39	A	C
ATOM	923	SG	CYS	A	612	0.540	13.427	9.985	1.00	51.77	A	S
ATOM	924	C	CYS	A	612	1.878	10.150	12.004	1.00	41.16	A	C
ATOM	925	O	CYS	A	612	1.229	9.172	12.316	1.00	43.24	A	O
ATOM	926	N	SER	A	613	2.909	10.577	12.717	1.00	42.06	A	N
ATOM	927	CA	SER	A	613	3.273	9.956	13.985	1.00	40.39	A	C
ATOM	928	CB	SER	A	613	4.427	8.982	13.785	1.00	39.56	A	C
ATOM	929	OG	SER	A	613	4.162	8.149	12.669	1.00	43.63	A	O
ATOM	930	C	SER	A	613	3.654	10.986	15.028	1.00	38.90	A	C
ATOM	931	O	SER	A	613	4.210	12.038	14.685	1.00	40.20	A	O
ATOM	932	N	VAL	A	614	3.315	10.696	16.288	1.00	36.87	A	N
ATOM	933	CA	VAL	A	614	3.922	11.384	17.432	1.00	35.60	A	C
ATOM	934	CB	VAL	A	614	2.895	11.967	18.458	1.00	33.11	A	C
ATOM	935	CG1	VAL	A	614	2.072	13.070	17.828	1.00	35.92	A	C
ATOM	936	CG2	VAL	A	614	1.993	10.919	18.999	1.00	29.73	A	C
ATOM	937	C	VAL	A	614	4.904	10.424	18.092	1.00	36.63	A	C
ATOM	938	O	VAL	A	614	4.769	9.195	17.954	1.00	37.34	A	O
ATOM	939	N	TYR	A	615	5.907	10.981	18.770	1.00	33.21	A	N
ATOM	940	CA	TYR	A	615	6.951	10.172	19.389	1.00	34.27	A	C
ATOM	941	CB	TYR	A	615	8.215	10.242	18.564	1.00	33.61	A	C
ATOM	942	CG	TYR	A	615	8.110	9.650	17.205	1.00	33.31	A	C
ATOM	943	CD1	TYR	A	615	8.583	8.383	16.944	1.00	37.92	A	C
ATOM	944	CE1	TYR	A	615	8.514	7.853	15.677	1.00	40.92	A	C
ATOM	945	CZ	TYR	A	615	7.967	8.601	14.669	1.00	39.71	A	C
ATOM	946	OH	TYR	A	615	7.864	8.108	13.404	1.00	44.92	A	O
ATOM	947	CE2	TYR	A	615	7.503	9.850	14.911	1.00	37.86	A	C
ATOM	948	CD2	TYR	A	615	7.583	10.372	16.169	1.00	35.59	A	C
ATOM	949	C	TYR	A	615	7.298	10.644	20.787	1.00	35.76	A	C
ATOM	950	O	TYR	A	615	7.390	11.852	21.038	1.00	43.10	A	O
ATOM	951	N	GLY	A	616	7.547	9.721	21.703	1.00	34.06	A	N
ATOM	952	CA	GLY	A	616	7.847	10.190	23.040	1.00	45.60	A	C
ATOM	953	C	GLY	A	616	8.214	9.200	24.107	1.00	46.49	A	C
ATOM	954	O	GLY	A	616	7.930	8.010	23.969	1.00	55.54	A	O
ATOM	955	N	TRP	A	617	8.862	9.709	25.158	1.00	38.09	A	N
ATOM	956	CA	TRP	A	617	9.119	8.936	26.365	1.00	33.79	A	C
ATOM	957	CB	TRP	A	617	10.556	9.111	26.803	1.00	37.43	A	C
ATOM	958	CG	TRP	A	617	11.561	8.530	25.883	1.00	38.24	A	C
ATOM	959	CD1	TRP	A	617	11.946	7.242	25.830	1.00	38.92	A	C
ATOM	960	NE1	TRP	A	617	12.920	7.077	24.877	1.00	41.68	A	N
ATOM	961	CE2	TRP	A	617	13.179	8.283	24.288	1.00	36.78	A	C
ATOM	962	CD2	TRP	A	617	12.349	9.227	24.905	1.00	39.06	A	C
ATOM	963	CE3	TRP	A	617	12.431	10.559	24.480	1.00	41.65	A	C
ATOM	964	CZ3	TRP	A	617	13.336	10.889	23.459	1.00	37.19	A	C
ATOM	965	CH2	TRP	A	617	14.131	9.922	22.881	1.00	34.06	A	C
ATOM	966	CZ2	TRP	A	617	14.067	8.614	23.277	1.00	33.68	A	C
ATOM	967	C	TRP	A	617	8.194	9.320	27.523	1.00	30.56	A	C
ATOM	968	O	TRP	A	617	8.397	8.881	28.652	1.00	29.70	A	O
ATOM	969	N	GLY	A	618	7.188	10.147	27.242	1.00	29.36	A	N
ATOM	970	CA	GLY	A	618	6.196	10.533	28.231	1.00	27.68	A	C
ATOM	971	C	GLY	A	618	5.273	9.372	28.607	1.00	32.48	A	C
ATOM	972	O	GLY	A	618	5.533	8.204	28.256	1.00	40.20	A	O
ATOM	973	N	TYR	A	619	4.168	9.700	29.271	1.00	23.28	A	N
ATOM	974	CA	TYR	A	619	3.399	8.745	30.055	1.00	22.13	A	C
ATOM	975	CB	TYR	A	619	2.421	9.542	30.897	1.00	26.82	A	C
ATOM	976	CG	TYR	A	619	1.203	8.858	31.444	1.00	25.77	A	C
ATOM	977	CD1	TYR	A	619	0.003	8.928	30.787	1.00	32.29	A	C
ATOM	978	CE1	TYR	A	619	−1.132	8.335	31.302	1.00	34.56	A	C
ATOM	979	CZ	TYR	A	619	−1.090	7.702	32.501	1.00	30.93	A	C
ATOM	980	OH	TYR	A	619	−2.224	7.110	33.002	1.00	35.53	A	O
ATOM	981	CE2	TYR	A	619	0.079	7.645	33.189	1.00	32.42	A	C
ATOM	982	CD2	TYR	A	619	1.225	8.242	32.659	1.00	28.30	A	C
ATOM	983	C	TYR	A	619	2.697	7.786	29.164	1.00	27.28	A	C
ATOM	984	O	TYR	A	619	2.254	8.153	28.097	1.00	35.04	A	O
ATOM	985	N	THR	A	620	2.605	6.540	29.590	1.00	33.48	A	N
ATOM	986	CA	THR	A	620	1.992	5.508	28.751	1.00	34.79	A	C
ATOM	987	CB	THR	A	620	3.032	4.467	28.297	1.00	30.58	A	C
ATOM	988	OG1	THR	A	620	3.603	3.826	29.446	1.00	30.46	A	O
ATOM	989	CG2	THR	A	620	4.190	5.135	27.615	1.00	30.86	A	C
ATOM	990	C	THR	A	620	0.889	4.779	29.480	1.00	36.05	A	C
ATOM	991	O	THR	A	620	0.322	3.815	28.959	1.00	37.97	A	O
ATOM	992	N	GLY	A	621	0.623	5.217	30.700	1.00	35.69	A	N
ATOM	993	CA	GLY	A	621	−0.357	4.567	31.537	1.00	35.76	A	C
ATOM	994	C	GLY	A	621	−0.083	3.100	31.810	1.00	32.89	A	C
ATOM	995	O	GLY	A	621	−1.030	2.348	32.206	1.00	27.38	A	O
ATOM	996	N	LEU	A	622	1.179	2.698	31.597	1.00	27.99	A	N
ATOM	997	CA	LEU	A	622	1.584	1.314	31.819	1.00	28.48	A	C
ATOM	998	CB	LEU	A	622	2.693	0.921	30.869	1.00	24.30	A	C
ATOM	999	CG	LEU	A	622	2.470	0.789	29.384	1.00	26.16	A	C
ATOM	1000	CD1	LEU	A	622	3.849	0.846	28.758	1.00	31.43	A	C
ATOM	1001	CD2	LEU	A	622	1.847	−0.520	29.055	1.00	27.82	A	C
ATOM	1002	C	LEU	A	622	2.098	1.130	33.240	1.00	31.75	A	C
ATOM	1003	O	LEU	A	622	2.751	2.026	33.766	1.00	36.31	A	O
ATOM	1004	N	ILE	A	623	1.827	−0.027	33.845	1.00	30.28	A	N
ATOM	1005	CA	ILE	A	623	2.367	−0.360	35.164	1.00	29.88	A	C
ATOM	1006	CB	ILE	A	623	1.895	−1.743	35.609	1.00	22.88	A	C
ATOM	1007	CG1	ILE	A	623	0.388	−1.739	35.750	1.00	21.00	A	C
ATOM	1008	CD1	ILE	A	623	−0.217	−3.082	35.588	1.00	29.56	A	C
ATOM	1009	CG2	ILE	A	623	2.495	−2.136	36.935	1.00	12.88	A	C
ATOM	1010	C	ILE	A	623	3.892	−0.258	35.222	1.00	37.02	A	C
ATOM	1011	O	ILE	A	623	4.404	0.361	36.151	1.00	41.18	A	O
ATOM	1012	N	ASN	A	624	4.604	−0.848	34.253	1.00	37.31	A	N
ATOM	1013	CA	ASN	A	624	6.055	−0.609	34.129	1.00	41.70	A	C
ATOM	1014	CB	ASN	A	624	6.886	−1.744	34.730	1.00	47.75	A	C
ATOM	1015	CG	ASN	A	624	6.162	−2.469	35.808	1.00	57.21	A	C
ATOM	1016	OD1	ASN	A	624	6.429	−2.271	36.996	1.00	62.72	A	O
ATOM	1017	ND2	ASN	A	624	5.214	−3.313	35.413	1.00	62.41	A	N
ATOM	1018	C	ASN	A	624	6.583	−0.302	32.729	1.00	38.62	A	C
ATOM	1019	O	ASN	A	624	7.013	−1.197	31.992	1.00	39.41	A	O
ATOM	1020	N	TYR	A	625	6.584	0.978	32.390	1.00	31.87	A	N
ATOM	1021	CA	TYR	A	625	7.121	1.451	31.122	1.00	27.41	A	C
ATOM	1022	CB	TYR	A	625	7.014	2.968	31.110	1.00	21.78	A	C
ATOM	1023	CG	TYR	A	625	7.563	3.681	29.945	1.00	21.68	A	C
ATOM	1024	CD1	TYR	A	625	7.240	3.333	28.670	1.00	38.53	A	C
ATOM	1025	CE1	TYR	A	625	7.773	4.041	27.580	1.00	43.92	A	C
ATOM	1026	CZ	TYR	A	625	8.602	5.102	27.803	1.00	37.73	A	C
ATOM	1027	OH	TYR	A	625	9.137	5.816	26.773	1.00	46.04	A	O
ATOM	1028	CE2	TYR	A	625	8.921	5.444	29.052	1.00	32.64	A	C
ATOM	1029	CD2	TYR	A	625	8.393	4.736	30.117	1.00	29.30	A	C
ATOM	1030	C	TYR	A	625	8.562	1.032	31.031	1.00	32.45	A	C
ATOM	1031	O	TYR	A	625	9.352	1.365	31.901	1.00	37.87	A	O
ATOM	1032	N	ASP	A	626	8.911	0.284	29.993	1.00	37.23	A	N
ATOM	1033	CA	ASP	A	626	10.295	−0.174	29.824	1.00	40.95	A	C
ATOM	1034	CB	ASP	A	626	10.359	−1.346	28.850	1.00	47.19	A	C
ATOM	1035	CG	ASP	A	626	9.714	−1.028	27.515	1.00	53.70	A	C
ATOM	1036	OD1	ASP	A	626	10.455	−0.617	26.600	1.00	57.23	A	O
ATOM	1037	OD2	ASP	A	626	8.485	−1.159	27.286	1.00	55.98	A	O
ATOM	1038	C	ASP	A	626	11.271	0.932	29.386	1.00	38.07	A	C
ATOM	1039	O	ASP	A	626	12.470	0.712	29.359	1.00	36.48	A	O
ATOM	1040	N	GLY	A	627	10.754	2.102	29.017	1.00	36.16	A	N
ATOM	1041	CA	GLY	A	627	11.587	3.277	28.845	1.00	33.65	A	C
ATOM	1042	C	GLY	A	627	11.965	3.573	27.417	1.00	38.25	A	C
ATOM	1043	O	GLY	A	627	12.599	4.584	27.143	1.00	35.77	A	O
ATOM	1044	N	LEU	A	628	11.564	2.693	26.502	1.00	44.15	A	N
ATOM	1045	CA	LEU	A	628	11.857	2.851	25.075	1.00	39.54	A	C
ATOM	1046	CB	LEU	A	628	11.726	1.515	24.352	1.00	40.26	A	C
ATOM	1047	CG	LEU	A	628	12.855	0.497	24.547	1.00	39.29	A	C
ATOM	1048	CD1	LEU	A	628	12.568	−0.741	23.718	1.00	41.84	A	C
ATOM	1049	CD2	LEU	A	628	14.213	1.064	24.195	1.00	35.92	A	C
ATOM	1050	C	LEU	A	628	10.947	3.851	24.396	1.00	35.47	A	C
ATOM	1051	O	LEU	A	628	9.801	4.047	24.811	1.00	33.83	A	O
ATOM	1052	N	LEU	A	629	11.464	4.456	23.329	1.00	35.33	A	N
ATOM	1053	CA	LEU	A	629	10.720	5.450	22.569	1.00	36.46	A	C
ATOM	1054	CB	LEU	A	629	11.549	6.019	21.424	1.00	34.38	A	C
ATOM	1055	CG	LEU	A	629	10.883	7.241	20.773	1.00	38.04	A	C
ATOM	1056	CD1	LEU	A	629	11.042	8.480	21.644	1.00	37.39	A	C
ATOM	1057	CD2	LEU	A	629	11.357	7.509	19.315	1.00	38.24	A	C
ATOM	1058	C	LEU	A	629	9.455	4.830	22.025	1.00	39.26	A	C
ATOM	1059	O	LEU	A	629	9.445	3.662	21.595	1.00	45.57	A	O
ATOM	1060	N	ARG	A	630	8.379	5.602	22.067	1.00	34.06	A	N
ATOM	1061	CA	ARG	A	630	7.099	5.076	21.652	1.00	31.59	A	C
ATOM	1062	CB	ARG	A	630	6.155	5.029	22.833	1.00	29.16	A	C
ATOM	1063	CG	ARG	A	630	6.130	3.639	23.386	1.00	34.00	A	C
ATOM	1064	CD	ARG	A	630	5.512	3.490	24.722	1.00	34.33	A	C
ATOM	1065	NE	ARG	A	630	4.554	2.392	24.764	1.00	34.81	A	N
ATOM	1066	CZ	ARG	A	630	4.889	1.107	24.826	1.00	39.51	A	C
ATOM	1067	NH1	ARG	A	630	6.181	0.733	24.831	1.00	42.05	A	N
ATOM	1068	NH2	ARG	A	630	3.921	0.194	24.881	1.00	35.27	A	N
ATOM	1069	C	ARG	A	630	6.537	5.896	20.544	1.00	37.04	A	C
ATOM	1070	O	ARG	A	630	6.817	7.079	20.443	1.00	46.58	A	O
ATOM	1071	N	VAL	A	631	5.755	5.274	19.689	1.00	38.91	A	N
ATOM	1072	CA	VAL	A	631	5.213	6.000	18.555	1.00	38.59	A	C
ATOM	1073	CB	VAL	A	631	5.961	5.652	17.271	1.00	33.71	A	C
ATOM	1074	CG1	VAL	A	631	5.876	4.176	17.004	1.00	29.88	A	C
ATOM	1075	CG2	VAL	A	631	5.371	6.409	16.119	1.00	39.05	A	C
ATOM	1076	C	VAL	A	631	3.724	5.722	18.397	1.00	38.59	A	C
ATOM	1077	O	VAL	A	631	3.280	4.575	18.524	1.00	35.78	A	O
ATOM	1078	N	ALA	A	632	2.958	6.775	18.141	1.00	36.60	A	N
ATOM	1079	CA	ALA	A	632	1.541	6.603	17.909	1.00	41.30	A	C
ATOM	1080	CB	ALA	A	632	0.743	7.213	19.007	1.00	44.22	A	C
ATOM	1081	C	ALA	A	632	1.209	7.263	16.620	1.00	44.95	A	C
ATOM	1082	O	ALA	A	632	1.681	8.369	16.363	1.00	48.50	A	O
ATOM	1083	N	HIS	A	633	0.378	6.586	15.830	1.00	47.82	A	N
ATOM	1084	CA	HIS	A	633	−0.019	7.046	14.508	1.00	47.04	A	C
ATOM	1085	CB	HIS	A	633	−0.052	5.879	13.550	1.00	49.10	A	C
ATOM	1086	CG	HIS	A	633	1.256	5.168	13.466	1.00	58.13	A	C
ATOM	1087	ND1	HIS	A	633	2.312	5.644	12.719	1.00	62.57	A	N
ATOM	1088	CE1	HIS	A	633	3.342	4.823	12.843	1.00	66.84	A	C
ATOM	1089	NE2	HIS	A	633	2.995	3.837	13.654	1.00	68.11	A	N
ATOM	1090	CD2	HIS	A	633	1.697	4.036	14.065	1.00	64.36	A	C
ATOM	1091	C	HIS	A	633	−1.343	7.787	14.504	1.00	48.07	A	C
ATOM	1092	O	HIS	A	633	−2.313	7.364	15.134	1.00	52.00	A	O
ATOM	1093	N	LEU	A	634	−1.346	8.919	13.809	1.00	45.09	A	N
ATOM	1094	CA	LEU	A	634	−2.515	9.759	13.658	1.00	42.06	A	C
ATOM	1095	CB	LEU	A	634	−2.399	10.981	14.556	1.00	38.58	A	C
ATOM	1096	CG	LEU	A	634	−1.778	10.717	15.927	1.00	39.62	A	C
ATOM	1097	CD1	LEU	A	634	−1.089	11.951	16.502	1.00	36.37	A	C
ATOM	1098	CD2	LEU	A	634	−2.853	10.184	16.883	1.00	44.78	A	C
ATOM	1099	C	LEU	A	634	−2.618	10.199	12.209	1.00	47.99	A	C
ATOM	1100	O	LEU	A	634	−1.633	10.165	11.463	1.00	52.20	A	O
ATOM	1101	N	TYR	A	635	−3.818	10.598	11.811	1.00	48.00	A	N
ATOM	1102	CA	TYR	A	635	−4.050	11.161	10.494	1.00	46.87	A	C
ATOM	1103	CB	TYR	A	635	−5.218	10.448	9.828	1.00	51.37	A	C
ATOM	1104	CG	TYR	A	635	−4.913	8.995	9.562	1.00	58.24	A	C
ATOM	1105	CD1	TYR	A	635	−4.363	8.592	8.353	1.00	62.45	A	C
ATOM	1106	CE1	TYR	A	635	−4.065	7.255	8.106	1.00	69.61	A	C
ATOM	1107	CZ	TYR	A	635	−4.306	6.304	9.089	1.00	73.94	A	C
ATOM	1108	OH	TYR	A	635	−4.007	4.972	8.853	1.00	78.01	A	O
ATOM	1109	CE2	TYR	A	635	−4.851	6.687	10.309	1.00	71.12	A	C
ATOM	1110	CD2	TYR	A	635	−5.150	8.026	10.534	1.00	64.85	A	C
ATOM	1111	C	TYR	A	635	−4.349	12.622	10.727	1.00	45.01	A	C
ATOM	1112	O	TYR	A	635	−4.885	12.966	11.782	1.00	46.84	A	O
ATOM	1113	N	ILE	A	636	−3.969	13.489	9.788	1.00	40.98	A	N
ATOM	1114	CA	ILE	A	636	−4.273	14.915	9.938	1.00	38.58	A	C
ATOM	1115	CB	ILE	A	636	−3.433	15.808	9.011	1.00	34.96	A	C
ATOM	1116	CG1	ILE	A	636	−1.941	15.574	9.219	1.00	34.76	A	C
ATOM	1117	CD1	ILE	A	636	−1.376	16.211	10.465	1.00	35.79	A	C
ATOM	1118	CG2	ILE	A	636	−3.771	17.269	9.246	1.00	31.89	A	C
ATOM	1119	C	ILE	A	636	−5.747	15.162	9.675	1.00	39.87	A	C
ATOM	1120	O	ILE	A	636	−6.282	14.753	8.647	1.00	40.08	A	O
ATOM	1121	N	MET	A	637	−6.392	15.822	10.625	1.00	39.16	A	N
ATOM	1122	CA	MET	A	637	−7.769	16.225	10.488	1.00	42.04	A	C
ATOM	1123	CB	MET	A	637	−8.450	16.076	11.833	1.00	48.65	A	C
ATOM	1124	CG	MET	A	637	−9.945	15.830	11.791	1.00	55.71	A	C
ATOM	1125	SD	MET	A	637	−10.473	14.993	13.305	1.00	61.14	A	S
ATOM	1126	CE	MET	A	637	−9.368	13.410	13.241	1.00	56.87	A	C
ATOM	1127	C	MET	A	637	−7.742	17.681	10.131	1.00	42.51	A	C
ATOM	1128	O	MET	A	637	−6.807	18.382	10.504	1.00	48.86	A	O
ATOM	1129	N	GLY	A	638	−8.759	18.159	9.431	1.00	41.90	A	N
ATOM	1130	CA	GLY	A	638	−8.922	19.598	9.287	1.00	51.84	A	C
ATOM	1131	C	GLY	A	638	−9.275	20.283	10.607	1.00	56.75	A	C
ATOM	1132	O	GLY	A	638	−9.833	19.642	11.496	1.00	59.32	A	O
ATOM	1133	N	ASN	A	639	−8.952	21.571	10.741	1.00	59.25	A	N
ATOM	1134	CA	ASN	A	639	−9.334	22.343	11.933	1.00	62.23	A	C
ATOM	1135	CB	ASN	A	639	−8.637	23.707	11.948	1.00	62.68	A	C
ATOM	1136	CG	ASN	A	639	−7.130	23.593	11.858	1.00	66.94	A	C
ATOM	1137	OD1	ASN	A	639	−6.578	22.491	11.735	1.00	71.75	A	O
ATOM	1138	ND2	ASN	A	639	−6.451	24.732	11.909	1.00	66.88	A	N
ATOM	1139	C	ASN	A	639	−10.848	22.531	12.042	1.00	66.50	A	C
ATOM	1140	O	ASN	A	639	−11.425	22.500	13.140	1.00	58.81	A	O
ATOM	1141	N	GLU	A	640	−11.471	22.721	10.873	1.00	75.25	A	N
ATOM	1142	CA	GLU	A	640	−12.901	22.976	10.739	1.00	76.26	A	C
ATOM	1143	CB	GLU	A	640	−13.250	23.166	9.266	1.00	75.86	A	C
ATOM	1144	CG	GLU	A	640	−14.457	24.057	9.006	1.00	78.64	A	C
ATOM	1145	CD	GLU	A	640	−15.199	23.671	7.731	1.00	78.03	A	C
ATOM	1146	OE1	GLU	A	640	−16.091	22.796	7.805	1.00	78.97	A	O
ATOM	1147	OE2	GLU	A	640	−14.884	24.229	6.653	1.00	73.67	A	O
ATOM	1148	C	GLU	A	640	−13.726	21.853	11.371	1.00	78.47	A	C
ATOM	1149	O	GLU	A	640	−14.683	22.124	12.101	1.00	79.05	A	O
ATOM	1150	N	LYS	A	641	−13.336	20.603	11.104	1.00	80.15	A	N
ATOM	1151	CA	LYS	A	641	−13.935	19.431	11.758	1.00	81.49	A	C
ATOM	1152	CB	LYS	A	641	−13.718	18.161	10.922	1.00	82.67	A	C
ATOM	1153	CG	LYS	A	641	−14.652	18.018	9.716	1.00	86.07	A	C
ATOM	1154	CD	LYS	A	641	−16.120	18.376	10.035	1.00	86.82	A	C
ATOM	1155	CE	LYS	A	641	−16.680	19.437	9.071	1.00	85.12	A	C
ATOM	1156	NZ	LYS	A	641	−17.344	18.842	7.870	1.00	82.58	A	N
ATOM	1157	C	LYS	A	641	−13.381	19.233	13.172	1.00	78.08	A	C
ATOM	1158	O	LYS	A	641	−14.093	18.857	14.101	1.00	77.15	A	O
ATOM	1159	N	CYS	A	642	−12.098	19.505	13.322	1.00	75.38	A	N
ATOM	1160	CA	CYS	A	642	−11.435	19.365	14.598	1.00	74.30	A	C
ATOM	1161	CB	CYS	A	642	−9.968	19.720	14.440	1.00	67.83	A	C
ATOM	1162	SG	CYS	A	642	−8.958	19.389	15.873	1.00	58.78	A	S
ATOM	1163	C	CYS	A	642	−12.067	20.240	15.667	1.00	78.61	A	C
ATOM	1164	O	CYS	A	642	−12.059	19.879	16.843	1.00	79.99	A	O
ATOM	1165	N	SER	A	643	−12.601	21.391	15.254	1.00	83.11	A	N
ATOM	1166	CA	SER	A	643	−13.280	22.313	16.166	1.00	86.69	A	C
ATOM	1167	CB	SER	A	643	−13.636	23.615	15.440	1.00	86.56	A	C
ATOM	1168	OG	SER	A	643	−12.862	24.710	15.903	1.00	86.24	A	O
ATOM	1169	C	SER	A	643	−14.544	21.655	16.718	1.00	89.20	A	C
ATOM	1170	O	SER	A	643	−14.810	21.727	17.927	1.00	84.95	A	O
ATOM	1171	N	GLN	A	644	−15.273	20.992	15.804	1.00	93.43	A	N
ATOM	1172	CA	GLN	A	644	−16.581	20.351	16.022	1.00	94.78	A	C
ATOM	1173	CB	GLN	A	644	−17.270	20.097	14.678	1.00	98.01	A	C
ATOM	1174	CG	GLN	A	644	−17.847	21.315	13.972	1.00	102.80	A	C
ATOM	1175	CD	GLN	A	644	−18.544	20.945	12.658	1.00	106.90	A	C
ATOM	1176	OE1	GLN	A	644	−18.256	19.900	12.058	1.00	105.89	A	O
ATOM	1177	NE2	GLN	A	644	−19.464	21.798	12.216	1.00	109.02	A	N
ATOM	1178	C	GLN	A	644	−16.497	19.010	16.738	1.00	94.25	A	C
ATOM	1179	O	GLN	A	644	−17.523	18.429	17.092	1.00	94.53	A	O
ATOM	1180	N	HIS	A	645	−15.278	18.507	16.905	1.00	95.16	A	N
ATOM	1181	CA	HIS	A	645	−15.015	17.264	17.626	1.00	94.75	A	C
ATOM	1182	CB	HIS	A	645	−13.754	16.611	17.059	1.00	93.02	A	C
ATOM	1183	CG	HIS	A		645	−14.000	15.605	15.978	1.00	92.95	A	C
ATOM	1184	ND1	HIS	A		645	−13.933	14.246	16.199	1.00	93.64	A	N
ATOM	1185	CE1	HIS	A		645	−14.163	13.605	15.068	1.00	93.83	A	C
ATOM	1186	NE2	HIS	A		645	−14.362	14.499	14.116	1.00	94.05	A	N
ATOM	1187	CD2	HIS	A		645	−14.255	15.758	14.657	1.00	93.73	A	C
ATOM	1188	C	HIS	A		645	−14.773	17.552	19.115	1.00	95.54	A	C
ATOM	1189	O	HIS	A		645	−14.617	16.623	19.924	1.00	95.32	A	O
ATOM	1190	N	HIS	A	646	−14.758	18.833	19.478	1.00	94.63	A	N
ATOM	1191	CA	HIS	A	646	−14.042	19.245	20.677	1.00	96.37	A	C
ATOM	1192	CB	HIS	A	646	−12.865	20.142	20.278	1.00	91.79	A	C
ATOM	1193	CG	HIS	A	646	−11.540	19.451	20.363	1.00	87.26	A	C
ATOM	1194	ND1	HIS	A	646	−10.899	19.216	21.560	1.00	82.73	A	N
ATOM	1195	CE1	HIS	A	646	−9.768	18.574	21.333	1.00	82.76	A	C
ATOM	1196	NE2	HIS	A	646	−9.650	18.386	20.032	1.00	85.35	A	N
ATOM	1197	CD2	HIS	A	646	−10.747	18.921	19.402	1.00	87.17	A	C
ATOM	1198	C	HIS	A	646	−14.768	19.791	21.934	1.00	104.37	A	C
ATOM	1199	O	HIS	A	646	−14.130	19.909	22.978	1.00	107.00	A	O
ATOM	1200	N	ARG	A	647	−16.059	20.111	21.895	1.00	110.75	A	N
ATOM	1201	CA	ARG	A	647	−16.924	20.025	20.740	1.00	116.40	A	C
ATOM	1202	CB	ARG	A	647	−18.241	19.326	21.110	1.00	122.17	A	C
ATOM	1203	CG	ARG	A	647	−18.389	18.942	22.604	1.00	128.16	A	C
ATOM	1204	CD	ARG	A	647	−18.977	17.546	22.865	1.00	131.91	A	C
ATOM	1205	NE	ARG	A	647	−20.214	17.327	22.108	1.00	135.96	A	N
ATOM	1206	CZ	ARG	A	647	−21.245	16.587	22.514	1.00	137.12	A	C
ATOM	1207	NH1	ARG	A	647	−21.219	15.965	23.690	1.00	136.96	A	N
ATOM	1208	NH2	ARG	A	647	−22.313	16.470	21.733	1.00	137.41	A	N
ATOM	1209	C	ARG	A	647	−17.165	21.460	20.309	1.00	117.91	A	C
ATOM	1210	O	ARG	A	647	−17.190	21.766	19.120	1.00	121.75	A	O
ATOM	1211	N	GLY	A	648	−17.340	22.336	21.295	1.00	115.77	A	N
ATOM	1212	CA	GLY	A	648	−17.387	23.768	21.070	1.00	112.40	A	C
ATOM	1213	C	GLY	A	648	−16.419	24.419	22.030	1.00	110.02	A	C
ATOM	1214	O	GLY	A	648	−16.299	25.645	22.075	1.00	108.47	A	O
ATOM	1215	N	LYS	A	649	−15.727	23.576	22.795	1.00	109.50	A	N
ATOM	1216	CA	LYS	A	649	−14.805	24.016	23.842	1.00	109.43	A	C
ATOM	1217	CB	LYS	A	649	−14.286	22.820	24.659	1.00	110.52	A	C
ATOM	1218	CG	LYS	A	649	−15.241	22.300	25.762	1.00	109.90	A	C
ATOM	1219	CD	LYS	A	649	−14.528	21.939	27.084	1.00	105.80	A	C
ATOM	1220	CE	LYS	A	649	−13.234	21.146	26.869	1.00	104.48	A	C
ATOM	1221	NZ	LYS	A	649	−13.217	19.855	27.607	1.00	103.67	A	N
ATOM	1222	C	LYS	A	649	−13.624	24.821	23.301	1.00	108.12	A	C
ATOM	1223	O	LYS	A	649	−13.204	25.794	23.933	1.00	110.50	A	O
ATOM	1224	N	VAL	A	650	−13.092	24.416	22.144	1.00	104.25	A	N
ATOM	1225	CA	VAL	A	650	−11.940	25.091	21.528	1.00	99.47	A	C
ATOM	1226	CB	VAL	A	650	−10.672	24.186	21.496	1.00	100.20	A	C
ATOM	1227	CG1	VAL	A	650	−9.418	24.996	21.875	1.00	104.73	A	C
ATOM	1228	CG2	VAL	A	650	−10.829	22.947	22.386	1.00	97.30	A	C
ATOM	1229	C	VAL	A	650	−12.214	25.565	20.100	1.00	94.68	A	C
ATOM	1230	O	VAL	A	650	−12.916	24.882	19.346	1.00	94.84	A	O
ATOM	1231	N	THR	A	651	−11.676	26.734	19.743	1.00	91.93	A	N
ATOM	1232	CA	THR	A	651	−11.597	27.154	18.329	1.00	94.90	A	C
ATOM	1233	CB	THR	A	651	−12.592	28.315	17.966	1.00	97.15	A	C
ATOM	1234	OG1	THR	A	651	−13.946	27.856	18.100	1.00	98.56	A	O
ATOM	1235	CG2	THR	A	651	−12.509	28.667	16.464	1.00	94.87	A	C
ATOM	1236	C	THR	A	651	−10.148	27.469	17.910	1.00	90.43	A	C
ATOM	1237	O	THR	A	651	−9.474	28.306	18.522	1.00	92.16	A	O
ATOM	1238	N	LEU	A	652	−9.695	26.803	16.850	1.00	80.36	A	N
ATOM	1239	CA	LEU	A	652	−8.284	26.768	16.503	1.00	72.59	A	C
ATOM	1240	CB	LEU	A	652	−7.978	25.498	15.730	1.00	69.56	A	C
ATOM	1241	CG	LEU	A	652	−8.464	24.209	16.374	1.00	68.21	A	C
ATOM	1242	CD1	LEU	A	652	−8.414	23.106	15.368	1.00	69.16	A	C
ATOM	1243	CD2	LEU	A	652	−7.616	23.849	17.564	1.00	70.22	A	C
ATOM	1244	C	LEU	A	652	−7.817	27.950	15.693	1.00	72.26	A	C
ATOM	1245	O	LEU	A	652	−8.482	28.360	14.739	1.00	72.28	A	O
ATOM	1246	N	ASN	A	653	−6.654	28.479	16.065	1.00	73.54	A	N
ATOM	1247	CA	ASN	A	653	−6.003	29.522	15.278	1.00	78.63	A	C
ATOM	1248	CB	ASN	A	653	−4.964	30.257	16.123	1.00	83.81	A	C
ATOM	1249	CG	ASN	A	653	−5.508	31.544	16.722	1.00	88.62	A	C
ATOM	1250	OD1	ASN	A	653	−5.377	32.625	16.132	1.00	90.14	A	O
ATOM	1251	ND2	ASN	A	653	−6.131	31.433	17.898	1.00	89.12	A	N
ATOM	1252	C	ASN	A	653	−5.365	28.940	14.019	1.00	75.19	A	C
ATOM	1253	O	ASN	A	653	−5.153	27.734	13.938	1.00	76.29	A	O
ATOM	1254	N	GLU	A	654	−5.059	29.778	13.035	1.00	69.05	A	N
ATOM	1255	CA	GLU	A	654	−4.385	29.274	11.841	1.00	66.11	A	C
ATOM	1256	CB	GLU	A	654	−4.344	30.329	10.725	1.00	74.38	A	C
ATOM	1257	CG	GLU	A	654	−4.255	31.783	11.185	1.00	82.02	A	C
ATOM	1258	CD	GLU	A	654	−4.063	32.762	10.029	1.00	87.39	A	C
ATOM	1259	OE1	GLU	A	654	−3.090	32.611	9.244	1.00	89.55	A	O
ATOM	1260	OE2	GLU	A	654	−4.890	33.692	9.904	1.00	89.83	A	O
ATOM	1261	C	GLU	A	654	−2.981	28.749	12.169	1.00	58.30	A	C
ATOM	1262	O	GLU	A	654	−2.275	28.236	11.306	1.00	58.92	A	O
ATOM	1263	N	SER	A	655	−2.606	28.866	13.435	1.00	51.31	A	N
ATOM	1264	CA	SER	A	655	−1.296	28.475	13.927	1.00	49.53	A	C
ATOM	1265	CB	SER	A	655	−0.827	29.544	14.892	1.00	51.93	A	C
ATOM	1266	OG	SER	A	655	−1.674	29.564	16.028	1.00	56.85	A	O
ATOM	1267	C	SER	A	655	−1.305	27.128	14.671	1.00	50.76	A	C
ATOM	1268	O	SER	A	655	−0.262	26.645	15.119	1.00	51.56	A	O
ATOM	1269	N	GLU	A	656	−2.493	26.556	14.844	1.00	49.44	A	N
ATOM	1270	CA	GLU	A	656	−2.670	25.245	15.457	1.00	43.28	A	C
ATOM	1271	CB	GLU	A	656	−3.763	25.316	16.542	1.00	42.82	A	C
ATOM	1272	CG	GLU	A	656	−3.305	25.911	17.882	1.00	50.87	A	C
ATOM	1273	CD	GLU	A	656	−4.440	26.162	18.909	1.00	57.23	A	C
ATOM	1274	OE1	GLU	A	656	−5.401	26.908	18.588	1.00	63.80	A	O
ATOM	1275	OE2	GLU	A	656	−4.375	25.651	20.064	1.00	51.97	A	O
ATOM	1276	C	GLU	A	656	−3.022	24.243	14.333	1.00	41.77	A	C
ATOM	1277	O	GLU	A	656	−3.539	24.635	13.291	1.00	41.76	A	O
ATOM	1278	N	ILE	A	657	−2.728	22.960	14.533	1.00	44.22	A	N
ATOM	1279	CA	ILE	A	657	−2.986	21.902	13.530	1.00	43.95	A	C
ATOM	1280	CB	ILE	A	657	−1.712	21.687	12.649	1.00	36.22	A	C
ATOM	1281	CG1	ILE	A	657	−1.932	20.639	11.579	1.00	33.28	A	C
ATOM	1282	CD1	ILE	A	657	−0.616	20.125	10.975	1.00	29.39	A	C
ATOM	1283	CG2	ILE	A	657	−0.531	21.242	13.482	1.00	39.33	A	C
ATOM	1284	C	ILE	A	657	−3.462	20.598	14.230	1.00	48.04	A	C
ATOM	1285	O	ILE	A	657	−3.043	20.321	15.356	1.00	47.63	A	O
ATOM	1286	N	CYS	A	658	−4.340	19.819	13.590	1.00	50.39	A	N
ATOM	1287	CA	CYS	A	658	−4.901	18.611	14.236	1.00	49.95	A	C
ATOM	1288	CB	CYS	A	658	−6.414	18.638	14.204	1.00	51.51	A	C
ATOM	1289	SG	CYS	A	658	−7.064	19.848	15.306	1.00	57.34	A	S
ATOM	1290	C	CYS	A	658	−4.488	17.262	13.666	1.00	50.32	A	C
ATOM	1291	O	CYS	A	658	−4.323	17.090	12.445	1.00	51.27	A	O
ATOM	1292	N	ALA	A	659	−4.370	16.291	14.562	1.00	46.15	A	N
ATOM	1293	CA	ALA	A	659	−4.202	14.908	14.150	1.00	46.32	A	C
ATOM	1294	CB	ALA	A	659	−2.748	14.564	13.927	1.00	47.56	A	C
ATOM	1295	C	ALA	A	659	−4.800	14.004	15.188	1.00	46.76	A	C
ATOM	1296	O	ALA	A	659	−4.631	14.202	16.392	1.00	47.65	A	O
ATOM	1297	N	GLY	A	660	−5.514	13.007	14.701	1.00	47.44	A	N
ATOM	1298	CA	GLY	A	660	−6.117	12.014	15.555	1.00	51.02	A	C
ATOM	1299	C	GLY	A	660	−6.064	10.678	14.864	1.00	52.20	A	C
ATOM	1300	O	GLY	A	660	−5.707	10.590	13.693	1.00	55.62	A	O
ATOM	1301	N	ALA	A	661	−6.407	9.639	15.603	1.00	52.34	A	N
ATOM	1302	CA	ALA	A	661	−6.515	8.312	15.044	1.00	53.28	A	C
ATOM	1303	CB	ALA	A	661	−5.884	7.309	15.983	1.00	55.18	A	C
ATOM	1304	C	ALA	A	661	−7.995	8.062	14.894	1.00	54.47	A	C
ATOM	1305	O	ALA	A	661	−8.795	8.645	15.632	1.00	52.98	A	O
ATOM	1306	N	GLU	A	662	−8.371	7.217	13.940	1.00	58.57	A	N
ATOM	1307	CA	GLU	A	662	−9.792	6.985	13.686	1.00	63.20	A	C
ATOM	1308	CB	GLU	A	662	−10.015	6.298	12.329	1.00	70.71	A	C
ATOM	1309	CG	GLU	A	662	−11.191	6.843	11.514	1.00	77.87	A	C
ATOM	1310	CD	GLU	A	662	−12.170	5.754	11.069	1.00	85.04	A	C
ATOM	1311	OE1	GLU	A	662	−11.723	4.709	10.530	1.00	86.23	A	O
ATOM	1312	OE2	GLU	A	662	−13.399	5.937	11.256	1.00	87.81	A	O
ATOM	1313	C	GLU	A	662	−10.406	6.179	14.823	1.00	58.84	A	C
ATOM	1314	O	GLU	A	662	−9.953	5.071	15.110	1.00	58.51	A	O
ATOM	1315	N	LYS	A	663	−11.394	6.779	15.490	1.00	54.07	A	N
ATOM	1316	CA	LYS	A	663	−12.272	6.103	16.467	1.00	52.93	A	C
ATOM	1317	CB	LYS	A	663	−13.048	4.936	15.825	1.00	49.89	A	C
ATOM	1318	CG	LYS	A	663	−13.993	5.349	14.726	1.00	58.71	A	C
ATOM	1319	CD	LYS	A	663	−15.452	5.187	15.137	1.00	69.67	A	C
ATOM	1320	CE	LYS	A	663	−16.224	4.300	14.124	1.00	77.42	A	C
ATOM	1321	NZ	LYS	A	663	−17.728	4.464	14.149	1.00	79.62	A	N
ATOM	1322	C	LYS	A	663	−11.680	5.640	17.813	1.00	49.67	A	C
ATOM	1323	O	LYS	A	663	−12.417	5.121	18.649	1.00	55.81	A	O
ATOM	1324	N	ILE	A	664	−10.385	5.802	18.044	1.00	40.34	A	N
ATOM	1325	CA	ILE	A	664	−9.809	5.244	19.270	1.00	37.17	A	C
ATOM	1326	CB	ILE	A	664	−8.825	4.109	18.965	1.00	28.85	A	C
ATOM	1327	CG1	ILE	A	664	−7.553	4.627	18.315	1.00	15.23	A	C
ATOM	1328	CD1	ILE	A	664	−6.449	3.632	18.419	1.00	7.40	A	C
ATOM	1329	CG2	ILE	A	664	−9.462	3.044	18.106	1.00	36.00	A	C
ATOM	1330	C	ILE	A	664	−9.114	6.285	20.118	1.00	46.28	A	C
ATOM	1331	O	ILE	A	664	−8.991	7.436	19.699	1.00	59.36	A	O
ATOM	1332	N	GLY	A	665	−8.646	5.896	21.301	1.00	39.69	A	N
ATOM	1333	CA	GLY	A	665	−7.838	6.812	22.084	1.00	39.88	A	C
ATOM	1334	C	GLY	A	665	−6.358	6.507	21.961	1.00	41.10	A	C
ATOM	1335	O	GLY	A	665	−5.905	5.472	22.422	1.00	43.92	A	O
ATOM	1336	N	SER	A	666	−5.590	7.388	21.338	1.00	39.79	A	N
ATOM	1337	CA	SER	A	666	−4.134	7.258	21.370	1.00	38.94	A	C
ATOM	1338	CB	SER	A	666	−3.607	6.358	20.249	1.00	44.83	A	C
ATOM	1339	OG	SER	A	666	−3.617	6.986	18.973	1.00	54.44	A	O
ATOM	1340	C	SER	A	666	−3.617	8.650	21.253	1.00	36.61	A	C
ATOM	1341	O	SER	A	666	−4.401	9.530	20.919	1.00	39.14	A	O
ATOM	1342	N	GLY	A	667	−2.332	8.868	21.528	1.00	37.34	A	N
ATOM	1343	CA	GLY	A	667	−1.785	10.227	21.528	1.00	42.52	A	C
ATOM	1344	C	GLY	A	667	−0.778	10.644	22.605	1.00	41.01	A	C
ATOM	1345	O	GLY	A	667	−0.533	9.902	23.561	1.00	44.20	A	O
ATOM	1346	N	PRO	A	668	−0.158	11.813	22.434	1.00	37.69	A	N
ATOM	1347	CA	PRO	A	668	0.923	12.245	23.326	1.00	39.24	A	C
ATOM	1348	CB	PRO	A	668	1.570	13.414	22.571	1.00	38.32	A	C
ATOM	1349	CG	PRO	A	668	0.507	13.949	21.695	1.00	39.02	A	C
ATOM	1350	CD	PRO	A	668	−0.421	12.805	21.382	1.00	39.28	A	C
ATOM	1351	C	PRO	A	668	0.345	12.711	24.642	1.00	40.63	A	C
ATOM	1352	O	PRO	A	668	−0.888	12.776	24.742	1.00	45.06	A	O
ATOM	1353	N	CYS	A	669	1.206	13.029	25.608	1.00	35.75	A	N
ATOM	1354	CA	CYS	A	669	0.782	13.251	26.979	1.00	37.80	A	C
ATOM	1355	CB	CYS	A	669	0.477	11.911	27.611	1.00	45.73	A	C
ATOM	1356	SG	CYS	A	669	−0.549	12.119	29.045	1.00	59.82	A	S
ATOM	1357	C	CYS	A	669	1.854	13.936	27.821	1.00	41.35	A	C
ATOM	1358	O	CYS	A	669	2.850	14.446	27.287	1.00	41.11	A	O
ATOM	1359	N	GLU	A	670	1.673	13.931	29.143	1.00	40.48	A	N
ATOM	1360	CA	GLU	A	670	2.743	14.374	30.034	1.00	40.28	A	C
ATOM	1361	CB	GLU	A	670	2.453	14.003	31.486	1.00	41.30	A	C
ATOM	1362	CG	GLU	A	670	1.329	14.778	32.154	1.00	43.75	A	C
ATOM	1363	CD	GLU	A	670	1.706	16.206	32.497	1.00	46.62	A	C
ATOM	1364	OE1	GLU	A	670	2.927	16.504	32.570	1.00	46.28	A	O
ATOM	1365	OE2	GLU	A	670	0.767	17.032	32.682	1.00	46.89	A	O
ATOM	1366	C	GLU	A	670	4.070	13.744	29.599	1.00	42.40	A	C
ATOM	1367	O	GLU	A	670	4.123	12.556	29.239	1.00	38.92	A	O
ATOM	1368	N	GLY	A	671	5.132	14.549	29.607	1.00	45.96	A	N
ATOM	1369	CA	GLY	A	671	6.460	14.071	29.253	1.00	46.38	A	C
ATOM	1370	C	GLY	A	671	6.701	13.918	27.760	1.00	42.28	A	C
ATOM	1371	O	GLY	A	671	7.832	13.686	27.324	1.00	40.04	A	O
ATOM	1372	N	ASP	A	672	5.640	14.058	26.974	1.00	42.20	A	N
ATOM	1373	CA	ASP	A	672	5.751	13.988	25.523	1.00	43.79	A	C
ATOM	1374	CB	ASP	A	672	4.476	13.399	24.927	1.00	43.39	A	C
ATOM	1375	CG	ASP	A	672	4.373	11.896	25.095	1.00	44.59	A	C
ATOM	1376	OD1	ASP	A	672	5.414	11.178	25.082	1.00	40.12	A	O
ATOM	1377	OD2	ASP	A	672	3.248	11.348	25.209	1.00	46.78	A	O
ATOM	1378	C	ASP	A	672	5.998	15.346	24.853	1.00	44.68	A	C
ATOM	1379	O	ASP	A	672	6.479	15.369	23.706	1.00	47.64	A	O
ATOM	1380	N	TYR	A	673	5.660	16.446	25.556	1.00	38.29	A	N
ATOM	1381	CA	TYR	A	673	5.613	17.803	24.980	1.00	34.36	A	C
ATOM	1382	CB	TYR	A	673	5.162	18.849	26.016	1.00	31.83	A	C
ATOM	1383	CG	TYR	A	673	3.989	18.441	26.880	1.00	30.94	A	C
ATOM	1384	CD1	TYR	A	673	2.898	17.812	26.343	1.00	36.19	A	C
ATOM	1385	CE1	TYR	A	673	1.828	17.431	27.120	1.00	30.40	A	C
ATOM	1386	CZ	TYR	A	673	1.832	17.679	28.443	1.00	24.59	A	C
ATOM	1387	OH	TYR	A	673	0.744	17.259	29.186	1.00	23.65	A	O
ATOM	1388	CE2	TYR	A	673	2.890	18.328	29.006	1.00	26.17	A	C
ATOM	1389	CD2	TYR	A	673	3.964	18.701	28.226	1.00	28.74	A	C
ATOM	1390	C	TYR	A	673	6.945	18.243	24.395	1.00	38.55	A	C
ATOM	1391	O	TYR	A	673	8.004	17.903	24.924	1.00	43.33	A	O
ATOM	1392	N	GLY	A	674	6.889	19.017	23.316	1.00	35.97	A	N
ATOM	1393	CA	GLY	A	674	8.087	19.499	22.661	1.00	35.61	A	C
ATOM	1394	C	GLY	A	674	8.436	18.505	21.581	1.00	42.37	A	C
ATOM	1395	O	GLY	A	674	9.177	18.807	20.630	1.00	48.06	A	O
ATOM	1396	N	GLY	A	675	7.870	17.312	21.724	1.00	41.44	A	N
ATOM	1397	CA	GLY	A	675	8.025	16.261	20.738	1.00	42.59	A	C
ATOM	1398	C	GLY	A	675	7.423	16.623	19.389	1.00	38.22	A	C
ATOM	1399	O	GLY	A	675	6.514	17.451	19.320	1.00	36.26	A	O
ATOM	1400	N	PRO	A	676	7.927	16.000	18.323	1.00	36.98	A	N
ATOM	1401	CA	PRO	A	676	7.423	16.248	16.967	1.00	36.70	A	C
ATOM	1402	CB	PRO	A	676	8.538	15.694	16.080	1.00	35.67	A	C
ATOM	1403	CG	PRO	A	676	9.134	14.564	16.903	1.00	35.15	A	C
ATOM	1404	CD	PRO	A	676	9.012	14.996	18.335	1.00	34.98	A	C
ATOM	1405	C	PRO	A	676	6.135	15.490	16.668	1.00	35.69	A	C
ATOM	1406	O	PRO	A	676	5.947	14.343	17.103	1.00	34.29	A	O
ATOM	1407	N	LEU	A	677	5.241	16.142	15.942	1.00	34.70	A	N
ATOM	1408	CA	LEU	A	677	4.224	15.407	15.216	1.00	36.54	A	C
ATOM	1409	CB	LEU	A	677	2.928	16.198	15.123	1.00	33.41	A	C
ATOM	1410	CG	LEU	A	677	2.040	15.870	13.922	1.00	29.43	A	C
ATOM	1411	CD1	LEU	A	677	1.051	14.802	14.282	1.00	27.30	A	C
ATOM	1412	CD2	LEU	A	677	1.341	17.117	13.451	1.00	28.29	A	C
ATOM	1413	C	LEU	A	677	4.845	15.327	13.856	1.00	37.46	A	C
ATOM	1414	O	LEU	A	677	5.168	16.367	13.280	1.00	43.56	A	O
ATOM	1415	N	VAL	A	678	5.060	14.127	13.335	1.00	31.66	A	N
ATOM	1416	CA	VAL	A	678	5.706	14.085	12.035	1.00	34.44	A	C
ATOM	1417	CB	VAL	A	678	7.184	13.594	12.084	1.00	28.71	A	C
ATOM	1418	CG1	VAL	A	678	7.496	13.062	13.435	1.00	25.66	A	C
ATOM	1419	CG2	VAL	A	678	7.502	12.609	10.972	1.00	22.04	A	C
ATOM	1420	C	VAL	A	678	4.857	13.453	10.971	1.00	39.54	A	C
ATOM	1421	O	VAL	A	678	4.256	12.409	11.198	1.00	45.36	A	O
ATOM	1422	N	CYS	A	679	4.791	14.114	9.824	1.00	40.07	A	N
ATOM	1423	CA	CYS	A	679	4.026	13.622	8.708	1.00	47.18	A	C
ATOM	1424	CB	CYS	A	679	2.950	14.623	8.337	1.00	46.07	A	C
ATOM	1425	SG	CYS	A	679	1.845	14.971	9.701	1.00	49.44	A	S
ATOM	1426	C	CYS	A	679	4.970	13.460	7.561	1.00	56.16	A	C
ATOM	1427	O	CYS	A	679	6.137	13.818	7.680	1.00	56.93	A	O
ATOM	1428	N	GLU	A	680	4.469	12.892	6.467	1.00	67.82	A	N
ATOM	1429	CA	GLU	A	680	5.146	12.959	5.182	1.00	81.24	A	C
ATOM	1430	CB	GLU	A	680	6.175	11.843	5.022	1.00	90.07	A	C
ATOM	1431	CG	GLU	A	680	5.611	10.440	4.916	1.00	100.07	A	C
ATOM	1432	CD	GLU	A	680	6.680	9.394	5.158	1.00	107.31	A	C
ATOM	1433	OE1	GLU	A	680	7.501	9.156	4.235	1.00	108.70	A	O
ATOM	1434	OE2	GLU	A	680	6.705	8.826	6.279	1.00	110.84	A	O
ATOM	1435	C	GLU	A	680	4.144	12.929	4.050	1.00	86.73	A	C
ATOM	1436	O	GLU	A	680	3.079	12.308	4.173	1.00	86.70	A	O
ATOM	1437	N	GLN	A	681	4.495	13.615	2.961	1.00	94.18	A	N
ATOM	1438	CA	GLN	A	681	3.709	13.615	1.727	1.00	101.38	A	C
ATOM	1439	CB	GLN	A	681	2.642	14.742	1.706	1.00	102.61	A	C
ATOM	1440	CG	GLN	A	681	3.149	16.198	1.671	1.00	103.69	A	C
ATOM	1441	CD	GLN	A	681	3.823	16.644	2.971	1.00	105.16	A	C
ATOM	1442	OE1	GLN	A	681	3.147	16.978	3.949	1.00	104.94	A	O
ATOM	1443	NE2	GLN	A	681	5.154	16.653	2.977	1.00	104.44	A	N
ATOM	1444	C	GLN	A	681	4.616	13.626	0.489	1.00	105.72	A	C
ATOM	1445	O	GLN	A	681	4.715	12.613	−0.215	1.00	105.20	A	O
ATOM	1446	N	HIS	A	682	5.293	14.761	0.266	1.00	111.00	A	N
ATOM	1447	CA	HIS	A	682	6.099	15.028	−0.935	1.00	113.44	A	C
ATOM	1448	CB	HIS	A	682	6.976	16.292	−0.754	1.00	115.52	A	C
ATOM	1449	CG	HIS	A	682	6.211	17.583	−0.599	1.00	116.80	A	C
ATOM	1450	ND1	HIS	A	682	4.864	17.707	−0.873	1.00	117.06	A	N
ATOM	1451	CE1	HIS	A	682	4.480	18.952	−0.644	1.00	115.83	A	C
ATOM	1452	NE2	HIS	A	682	5.530	19.645	−0.240	1.00	114.65	A	N
ATOM	1453	CD2	HIS	A	682	6.625	18.814	−0.205	1.00	115.72	A	C
ATOM	1454	C	HIS	A	682	6.981	13.827	−1.296	1.00	112.92	A	C
ATOM	1455	O	HIS	A	682	6.840	13.250	−2.381	1.00	113.10	A	O
ATOM	1456	N	LYS	A	683	7.874	13.462	−0.371	1.00	110.95	A	N
ATOM	1457	CA	LYS	A	683	8.774	12.317	−0.510	1.00	108.18	A	C
ATOM	1458	CB	LYS	A	683	9.910	12.616	−1.504	1.00	113.61	A	C
ATOM	1459	CG	LYS	A	683	10.595	11.372	−2.099	1.00	117.52	A	C
ATOM	1460	CD	LYS	A	683	12.004	11.679	−2.634	1.00	118.90	A	C
ATOM	1461	CE	LYS	A	683	12.955	10.492	−2.456	1.00	119.08	A	C
ATOM	1462	NZ	LYS	A	683	13.416	10.330	−1.039	1.00	118.83	A	N
ATOM	1463	C	LYS	A	683	9.359	11.953	0.847	1.00	101.80	A	C
ATOM	1464	O	LYS	A	683	9.269	10.806	1.275	1.00	100.60	A	O
ATOM	1465	N	MET	A	684	9.945	12.947	1.515	1.00	96.97	A	N
ATOM	1466	CA	MET	A	684	10.666	12.755	2.779	1.00	93.07	A	C
ATOM	1467	CB	MET	A	684	12.014	13.500	2.750	1.00	97.15	A	C
ATOM	1468	CG	MET	A	684	11.974	14.904	2.121	1.00	101.00	A	C
ATOM	1469	SD	MET	A	684	12.278	14.933	0.323	1.00	103.09	A	S
ATOM	1470	CE	MET	A	684	14.014	15.513	0.260	1.00	102.46	A	C
ATOM	1471	C	MET	A	684	9.839	13.143	4.021	1.00	86.11	A	C
ATOM	1472	O	MET	A	684	8.650	13.447	3.904	1.00	85.56	A	O
ATOM	1473	N	ARG	A	685	10.478	13.126	5.195	1.00	77.84	A	N
ATOM	1474	CA	ARG	A	685	9.821	13.363	6.492	1.00	67.29	A	C
ATOM	1475	CB	ARG	A	685	10.397	12.420	7.562	1.00	67.86	A	C
ATOM	1476	CG	ARG	A	685	10.040	10.958	7.424	1.00	70.14	A	C
ATOM	1477	CD	ARG	A	685	11.245	10.039	7.195	1.00	77.65	A	C
ATOM	1478	NE	ARG	A	685	11.614	9.206	8.349	1.00	86.24	A	N
ATOM	1479	CZ	ARG	A	685	10.800	8.368	9.022	1.00	92.30	A	C
ATOM	1480	NH1	ARG	A	685	9.515	8.224	8.698	1.00	92.95	A	N
ATOM	1481	NH2	ARG	A	685	11.282	7.667	10.046	1.00	94.20	A	N
ATOM	1482	C	ARG	A	685	10.010	14.800	6.982	1.00	59.11	A	C
ATOM	1483	O	ARG	A	685	11.136	15.288	7.042	1.00	59.70	A	O
ATOM	1484	N	MET	A	686	8.918	15.457	7.363	1.00	52.07	A	N
ATOM	1485	CA	MET	A	686	8.979	16.806	7.932	1.00	52.77	A	C
ATOM	1486	CB	MET	A	686	8.240	17.775	7.013	1.00	56.34	A	C
ATOM	1487	CG	MET	A	686	8.911	18.076	5.693	1.00	63.29	A	C
ATOM	1488	SD	MET	A	686	7.870	19.177	4.709	1.00	72.90	A	S
ATOM	1489	CE	MET	A	686	9.003	19.605	3.294	1.00	73.19	A	C
ATOM	1490	C	MET	A	686	8.352	16.887	9.337	1.00	50.09	A	C
ATOM	1491	O	MET	A	686	7.330	16.255	9.579	1.00	57.19	A	O
ATOM	1492	N	VAL	A	687	8.930	17.658	10.261	1.00	40.20	A	N
ATOM	1493	CA	VAL	A	687	8.206	17.955	11.502	1.00	35.96	A	C
ATOM	1494	CB	VAL	A	687	9.105	18.371	12.717	1.00	37.17	A	C
ATOM	1495	CG1	VAL	A	687	10.031	19.518	12.404	1.00	31.99	A	C
ATOM	1496	CG2	VAL	A	687	8.223	18.743	13.901	1.00	40.76	A	C
ATOM	1497	C	VAL	A	687	7.132	19.000	11.232	1.00	32.99	A	C
ATOM	1498	O	VAL	A	687	7.426	20.085	10.762	1.00	35.40	A	O
ATOM	1499	N	LEU	A	688	5.886	18.670	11.531	1.00	31.53	A	N
ATOM	1500	CA	LEU	A	688	4.763	19.485	11.070	1.00	35.49	A	C
ATOM	1501	CB	LEU	A	688	3.836	18.631	10.224	1.00	33.52	A	C
ATOM	1502	CG	LEU	A	688	3.871	18.865	8.727	1.00	27.94	A	C
ATOM	1503	CD1	LEU	A	688	5.216	18.497	8.192	1.00	27.81	A	C
ATOM	1504	CD2	LEU	A	688	2.836	17.974	8.148	1.00	27.94	A	C
ATOM	1505	C	LEU	A	688	3.943	20.123	12.174	1.00	39.83	A	C
ATOM	1506	O	LEU	A	688	3.251	21.107	11.950	1.00	42.40	A	O
ATOM	1507	N	GLY	A	689	3.999	19.529	13.354	1.00	42.67	A	N
ATOM	1508	CA	GLY	A	689	3.380	20.095	14.528	1.00	41.64	A	C
ATOM	1509	C	GLY	A	689	4.332	19.860	15.665	1.00	39.90	A	C
ATOM	1510	O	GLY	A	689	5.215	18.992	15.557	1.00	37.02	A	O
ATOM	1511	N	VAL	A	690	4.159	20.632	16.739	1.00	38.49	A	N
ATOM	1512	CA	VAL	A	690	4.974	20.486	17.944	1.00	36.23	A	C
ATOM	1513	CB	VAL	A	690	5.742	21.770	18.293	1.00	33.80	A	C
ATOM	1514	CG1	VAL	A	690	6.504	21.581	19.575	1.00	40.76	A	C
ATOM	1515	CG2	VAL	A	690	6.694	22.148	17.198	1.00	30.12	A	C
ATOM	1516	C	VAL	A	690	4.049	20.142	19.085	1.00	36.97	A	C
ATOM	1517	O	VAL	A	690	3.064	20.828	19.302	1.00	41.25	A	O
ATOM	1518	N	ILE	A	691	4.349	19.068	19.803	1.00	38.52	A	N
ATOM	1519	CA	ILE	A	691	3.470	18.613	20.873	1.00	40.23	A	C
ATOM	1520	CB	ILE	A	691	3.932	17.256	21.416	1.00	39.21	A	C
ATOM	1521	CG1	ILE	A	691	3.816	16.178	20.341	1.00	35.12	A	C
ATOM	1522	CD1	ILE	A	691	4.715	15.000	20.598	1.00	31.55	A	C
ATOM	1523	CG2	ILE	A	691	3.120	16.870	22.634	1.00	40.22	A	C
ATOM	1524	C	ILE	A	691	3.458	19.642	21.993	1.00	41.66	A	C
ATOM	1525	O	ILE	A	691	4.503	20.033	22.497	1.00	40.52	A	O
ATOM	1526	N	VAL	A	692	2.264	20.094	22.348	1.00	43.82	A	N
ATOM	1527	CA	VAL	A	692	2.060	20.955	23.514	1.00	41.79	A	C
ATOM	1528	CB	VAL	A	692	1.644	22.399	23.113	1.00	37.14	A	C
ATOM	1529	CG1	VAL	A	692	2.645	22.999	22.114	1.00	28.48	A	C
ATOM	1530	CG2	VAL	A	692	0.216	22.428	22.568	1.00	38.18	A	C
ATOM	1531	C	VAL	A	692	0.986	20.293	24.378	1.00	44.75	A	C
ATOM	1532	O	VAL	A	692	0.299	19.388	23.903	1.00	54.64	A	O
ATOM	1533	N	PRO	A	693	0.828	20.709	25.628	1.00	41.31	A	N
ATOM	1534	CA	PRO	A	693	−0.174	20.081	26.490	1.00	40.59	A	C
ATOM	1535	CB	PRO	A	693	−0.069	20.890	27.786	1.00	43.86	A	C
ATOM	1536	CG	PRO	A	693	1.330	21.404	27.770	1.00	43.42	A	C
ATOM	1537	CD	PRO	A	693	1.570	21.770	26.333	1.00	41.50	A	C
ATOM	1538	C	PRO	A	693	−1.595	20.144	25.914	1.00	42.17	A	C
ATOM	1539	O	PRO	A	693	−2.014	21.132	25.259	1.00	42.65	A	O
ATOM	1540	N	GLY	A	694	−2.338	19.070	26.165	1.00	38.52	A	N
ATOM	1541	CA	GLY	A	694	−3.699	18.979	25.684	1.00	37.62	A	C
ATOM	1542	C	GLY	A	694	−4.779	19.248	26.705	1.00	38.72	A	C
ATOM	1543	O	GLY	A	694	−4.534	19.942	27.698	1.00	48.67	A	O
ATOM	1544	N	ARG	A	695	−5.970	18.692	26.447	1.00	37.38	A	N
ATOM	1545	CA	ARG	A	695	−7.097	18.746	27.365	1.00	34.19	A	C
ATOM	1546	CB	ARG	A	695	−8.237	19.459	26.716	1.00	34.82	A	C
ATOM	1547	CG	ARG	A	695	−7.918	20.935	26.594	1.00	44.94	A	C
ATOM	1548	CD	ARG	A	695	−8.646	21.660	25.475	1.00	47.02	A	C
ATOM	1549	NE	ARG	A	695	−9.682	22.488	26.059	1.00	46.61	A	N
ATOM	1550	CZ	ARG	A	695	−9.837	23.758	25.794	1.00	50.72	A	C
ATOM	1551	NH1	ARG	A	695	−9.022	24.349	24.925	1.00	49.70	A	N
ATOM	1552	NH2	ARG	A	695	−10.818	24.438	26.390	1.00	56.06	A	N
ATOM	1553	C	ARG	A	695	−7.483	17.358	27.847	1.00	39.34	A	C
ATOM	1554	O	ARG	A	695	−8.621	17.094	28.302	1.00	42.40	A	O
ATOM	1555	N	GLY	A	696	−6.482	16.485	27.793	1.00	38.78	A	N
ATOM	1556	CA	GLY	A	696	−6.610	15.106	28.215	1.00	43.16	A	C
ATOM	1557	C	GLY	A	696	−5.873	14.210	27.250	1.00	44.55	A	C
ATOM	1558	O	GLY	A	696	−5.834	14.500	26.068	1.00	50.18	A	O
ATOM	1559	N	CYS	A	697	−5.277	13.139	27.751	1.00	44.32	A	N
ATOM	1560	CA	CYS	A	697	−4.524	12.234	26.909	1.00	44.50	A	C
ATOM	1561	CB	CYS	A	697	−3.426	11.595	27.744	1.00	49.09	A	C
ATOM	1562	SG	CYS	A	697	−2.394	12.857	28.503	1.00	56.39	A	S
ATOM	1563	C	CYS	A	697	−5.429	11.178	26.286	1.00	47.38	A	C
ATOM	1564	O	CYS	A	697	−6.413	10.751	26.886	1.00	50.68	A	O
ATOM	1565	N	ALA	A	698	−5.101	10.766	25.068	1.00	52.54	A	N
ATOM	1566	CA	ALA	A	698	−5.835	9.702	24.363	1.00	53.20	A	C
ATOM	1567	CB	ALA	A	698	−5.124	8.372	24.560	1.00	50.25	A	C
ATOM	1568	C	ALA	A	698	−7.342	9.584	24.712	1.00	53.22	A	C
ATOM	1569	O	ALA	A	698	−7.823	8.498	25.079	1.00	55.37	A	O
ATOM	1570	N	ILE	A	699	−8.074	10.698	24.608	1.00	48.34	A	N
ATOM	1571	CA	ILE	A	699	−9.521	10.664	24.760	1.00	41.86	A	C
ATOM	1572	CB	ILE	A	699	−10.092	12.049	24.970	1.00	37.20	A	C
ATOM	1573	CG1	ILE	A	699	−10.057	12.394	26.447	1.00	44.24	A	C
ATOM	1574	CD1	ILE	A	699	−9.181	13.547	26.806	1.00	44.51	A	C
ATOM	1575	CG2	ILE	A	699	−11.536	12.045	24.615	1.00	34.30	A	C
ATOM	1576	C	ILE	A	699	−10.095	10.079	23.499	1.00	44.19	A	C
ATOM	1577	O	ILE	A	699	−9.861	10.609	22.417	1.00	52.15	A	O
ATOM	1578	N	PRO	A	700	−10.861	9.004	23.611	1.00	42.12	A	N
ATOM	1579	CA	PRO	A	700	−11.352	8.323	22.422	1.00	41.31	A	C
ATOM	1580	CB	PRO	A	700	−12.317	7.299	22.977	1.00	38.60	A	C
ATOM	1581	CG	PRO	A	700	−11.837	7.056	24.319	1.00	44.12	A	C
ATOM	1582	CD	PRO	A	700	−11.357	8.377	24.842	1.00	46.01	A	C
ATOM	1583	C	PRO	A	700	−12.077	9.330	21.566	1.00	45.33	A	C
ATOM	1584	O	PRO	A	700	−12.948	10.074	22.048	1.00	43.22	A	O
ATOM	1585	N	ASN	A	701	−11.635	9.385	20.315	1.00	48.30	A	N
ATOM	1586	CA	ASN	A	701	−12.299	10.115	19.251	1.00	52.07	A	C
ATOM	1587	CB	ASN	A	701	−13.693	9.544	19.019	1.00	55.65	A	C
ATOM	1588	CG	ASN	A	701	−14.174	9.804	17.641	1.00	58.03	A	C
ATOM	1589	OD1	ASN	A	701	−13.617	9.303	16.654	1.00	58.32	A	O
ATOM	1590	ND2	ASN	A	701	−15.196	10.627	17.544	1.00	61.70	A	N
ATOM	1591	C	ASN	A	701	−12.321	11.647	19.348	1.00	50.08	A	C
ATOM	1592	O	ASN	A	701	−13.204	12.310	18.770	1.00	45.34	A	O
ATOM	1593	N	ARG	A	702	−11.319	12.190	20.039	1.00	46.43	A	N
ATOM	1594	CA	ARG	A	702	−11.119	13.629	20.138	1.00	48.19	A	C
ATOM	1595	CB	ARG	A	702	−11.374	14.045	21.579	1.00	55.76	A	C
ATOM	1596	CG	ARG	A	702	−11.528	15.532	21.870	1.00	65.44	A	C
ATOM	1597	CD	ARG	A	702	−11.232	15.947	23.381	1.00	72.16	A	C
ATOM	1598	NE	ARG	A	702	−12.249	15.637	24.415	1.00	73.97	A	N
ATOM	1599	CZ	ARG	A	702	−13.488	15.134	24.213	1.00	78.19	A	C
ATOM	1600	NH1	ARG	A	702	−13.958	14.851	22.993	1.00	75.65	A	N
ATOM	1601	NH2	ARG	A	702	−14.274	14.909	25.262	1.00	80.63	A	N
ATOM	1602	C	ARG	A	702	−9.674	13.913	19.723	1.00	46.23	A	C
ATOM	1603	O	ARG	A	702	−8.760	13.640	20.481	1.00	50.59	A	O
ATOM	1604	N	PRO	A	703	−9.450	14.450	18.528	1.00	45.86	A	N
ATOM	1605	CA	PRO	A	703	−8.087	14.594	17.988	1.00	45.22	A	C
ATOM	1606	CB	PRO	A	703	−8.318	15.221	16.608	1.00	44.09	A	C
ATOM	1607	CG	PRO	A	703	−9.627	15.898	16.735	1.00	43.61	A	C
ATOM	1608	CD	PRO	A	703	−10.455	14.998	17.604	1.00	45.69	A	C
ATOM	1609	C	PRO	A	703	−7.197	15.520	18.806	1.00	43.55	A	C
ATOM	1610	O	PRO	A	703	−7.688	16.336	19.584	1.00	44.36	A	O
ATOM	1611	N	GLY	A	704	−5.890	15.384	18.619	1.00	44.43	A	N
ATOM	1612	CA	GLY	A	704	−4.928	16.256	19.268	1.00	43.96	A	C
ATOM	1613	C	GLY	A	704	−4.658	17.493	18.432	1.00	41.94	A	C
ATOM	1614	O	GLY	A	704	−4.565	17.418	17.199	1.00	47.94	A	O
ATOM	1615	N	ILE	A	705	−4.560	18.637	19.094	1.00	33.42	A	N
ATOM	1616	CA	ILE	A	705	−4.159	19.841	18.410	1.00	28.50	A	C
ATOM	1617	CB	ILE	A	705	−5.147	21.047	18.682	1.00	31.90	A	C
ATOM	1618	CG1	ILE	A	705	−4.460	22.418	18.561	1.00	36.99	A	C
ATOM	1619	CD1	ILE	A	705	−3.332	22.737	19.529	1.00	37.47	A	C
ATOM	1620	CG2	ILE	A	705	−5.965	20.889	19.949	1.00	32.67	A	C
ATOM	1621	C	ILE	A	705	−2.701	20.117	18.715	1.00	27.05	A	C
ATOM	1622	O	ILE	A	705	−2.281	20.125	19.865	1.00	35.29	A	O
ATOM	1623	N	PHE	A	706	−1.925	20.305	17.662	1.00	31.62	A	N
ATOM	1624	CA	PHE	A	706	−0.487	20.540	17.772	1.00	38.59	A	C
ATOM	1625	CB	PHE	A	706	0.282	19.522	16.932	1.00	34.95	A	C
ATOM	1626	CG	PHE	A	706	−0.072	18.096	17.223	1.00	32.87	A	C
ATOM	1627	CD1	PHE	A	706	0.855	17.248	17.783	1.00	37.19	A	C
ATOM	1628	CE1	PHE	A	706	0.542	15.911	18.024	1.00	38.47	A	C
ATOM	1629	CZ	PHE	A	706	−0.714	15.424	17.711	1.00	35.32	A	C
ATOM	1630	CE2	PHE	A	706	−1.645	16.268	17.163	1.00	32.01	A	C
ATOM	1631	CD2	PHE	A	706	−1.322	17.591	16.917	1.00	32.32	A	C
ATOM	1632	C	PHE	A	706	−0.203	21.944	17.258	1.00	39.92	A	C
ATOM	1633	O	PHE	A	706	−1.117	22.586	16.742	1.00	42.13	A	O
ATOM	1634	N	VAL	A	707	1.033	22.433	17.388	1.00	35.91	A	N
ATOM	1635	CA	VAL	A	707	1.341	23.750	16.833	1.00	34.53	A	C
ATOM	1636	CB	VAL	A	707	2.227	24.638	17.760	1.00	31.70	A	C
ATOM	1637	CG1	VAL	A	707	3.170	23.829	18.523	1.00	33.90	A	C
ATOM	1638	CG2	VAL	A	707	3.006	25.656	16.955	1.00	34.25	A	C
ATOM	1639	C	VAL	A	707	1.880	23.645	15.400	1.00	34.97	A	C
ATOM	1640	O	VAL	A	707	2.856	22.930	15.138	1.00	35.08	A	O
ATOM	1641	N	ARG	A	708	1.206	24.338	14.480	1.00	35.14	A	N
ATOM	1642	CA	ARG	A	708	1.601	24.377	13.075	1.00	39.69	A	C
ATOM	1643	CB	ARG	A	708	0.639	25.237	12.251	1.00	42.35	A	C
ATOM	1644	CG	ARG	A	708	0.392	24.734	10.859	1.00	46.08	A	C
ATOM	1645	CD	ARG	A	708	−1.037	24.982	10.339	1.00	52.26	A	C
ATOM	1646	NE	ARG	A	708	−1.026	26.025	9.318	1.00	60.83	A	N
ATOM	1647	CZ	ARG	A	708	−0.483	25.893	8.097	1.00	68.01	A	C
ATOM	1648	NH1	ARG	A	708	0.081	24.736	7.717	1.00	71.66	A	N
ATOM	1649	NH2	ARG	A	708	−0.511	26.917	7.244	1.00	65.48	A	N
ATOM	1650	C	ARG	A	708	2.984	24.972	13.008	1.00	39.97	A	C
ATOM	1651	O	ARG	A	708	3.186	26.120	13.373	1.00	43.82	A	O
ATOM	1652	N	VAL	A	709	3.948	24.175	12.584	1.00	37.94	A	N
ATOM	1653	CA	VAL	A	709	5.300	24.673	12.409	1.00	32.57	A	C
ATOM	1654	CB	VAL	A	709	6.281	23.524	12.228	1.00	28.96	A	C
ATOM	1655	CG1	VAL	A	709	7.631	24.029	11.747	1.00	21.41	A	C
ATOM	1656	CG2	VAL	A	709	6.378	22.707	13.519	1.00	28.08	A	C
ATOM	1657	C	VAL	A	709	5.315	25.563	11.178	1.00	35.08	A	C
ATOM	1658	O	VAL	A	709	5.949	26.606	11.168	1.00	31.30	A	O
ATOM	1659	N	ALA	A	710	4.585	25.162	10.144	1.00	41.73	A	N
ATOM	1660	CA	ALA	A	710	4.536	25.956	8.920	1.00	42.71	A	C
ATOM	1661	CB	ALA	A	710	3.512	25.382	7.952	1.00	44.89	A	C
ATOM	1662	C	ALA	A	710	4.245	27.434	9.215	1.00	40.16	A	C
ATOM	1663	O	ALA	A	710	4.770	28.317	8.549	1.00	39.48	A	O
ATOM	1664	N	TYR	A	711	3.433	27.694	10.235	1.00	40.18	A	N
ATOM	1665	CA	TYR	A	711	3.038	29.055	10.577	1.00	41.47	A	C
ATOM	1666	CB	TYR	A	711	1.959	29.040	11.643	1.00	39.79	A	C
ATOM	1667	CG	TYR	A	711	1.282	30.362	11.903	1.00	36.63	A	C
ATOM	1668	CD1	TYR	A	711	0.346	30.875	11.017	1.00	42.57	A	C
ATOM	1669	CE1	TYR	A	711	−0.301	32.087	11.266	1.00	46.47	A	C
ATOM	1670	CZ	TYR	A	711	−0.022	32.781	12.430	1.00	45.43	A	C
ATOM	1671	OH	TYR	A	711	−0.658	33.979	12.691	1.00	45.18	A	O
ATOM	1672	CE2	TYR	A	711	0.901	32.274	13.324	1.00	42.37	A	C
ATOM	1673	CD2	TYR	A	711	1.544	31.072	13.053	1.00	36.82	A	C
ATOM	1674	C	TYR	A	711	4.220	29.821	11.095	1.00	44.95	A	C
ATOM	1675	O	TYR	A	711	4.275	31.040	10.974	1.00	53.00	A	O
ATOM	1676	N	TYR	A	712	5.178	29.090	11.646	1.00	42.71	A	N
ATOM	1677	CA	TYR	A	712	6.345	29.695	12.266	1.00	42.49	A	C
ATOM	1678	CB	TYR	A	712	6.411	29.198	13.701	1.00	31.49	A	C
ATOM	1679	CG	TYR	A	712	5.262	29.691	14.537	1.00	26.75	A	C
ATOM	1680	CD1	TYR	A	712	5.061	31.049	14.711	1.00	28.18	A	C
ATOM	1681	CE1	TYR	A	712	4.027	31.532	15.503	1.00	30.60	A	C
ATOM	1682	CZ	TYR	A	712	3.161	30.659	16.121	1.00	29.77	A	C
ATOM	1683	OH	TYR	A	712	2.148	31.219	16.868	1.00	34.02	A	O
ATOM	1684	CE2	TYR	A	712	3.325	29.284	15.973	1.00	25.70	A	C
ATOM	1685	CD2	TYR	A	712	4.390	28.807	15.181	1.00	25.26	A	C
ATOM	1686	C	TYR	A	712	7.695	29.487	11.521	1.00	48.23	A	C
ATOM	1687	O	TYR	A	712	8.754	29.901	12.003	1.00	52.43	A	O
ATOM	1688	N	ALA	A	713	7.654	28.881	10.339	1.00	47.47	A	N
ATOM	1689	CA	ALA	A	713	8.875	28.421	9.692	1.00	48.61	A	C
ATOM	1690	CB	ALA	A	713	8.542	27.636	8.442	1.00	49.02	A	C
ATOM	1691	C	ALA	A	713	9.837	29.565	9.380	1.00	52.52	A	C
ATOM	1692	O	ALA	A	713	11.062	29.428	9.531	1.00	53.40	A	O
ATOM	1693	N	LYS	A	714	9.267	30.689	8.946	1.00	54.15	A	N
ATOM	1694	CA	LYS	A	714	10.025	31.899	8.639	1.00	50.72	A	C
ATOM	1695	CB	LYS	A	714	9.072	33.069	8.372	1.00	50.32	A	C
ATOM	1696	CG	LYS	A	714	9.550	34.058	7.354	1.00	49.64	A	C
ATOM	1697	CD	LYS	A	714	8.530	34.233	6.245	1.00	52.82	A	C
ATOM	1698	CE	LYS	A	714	9.107	33.779	4.892	1.00	56.98	A	C
ATOM	1699	NZ	LYS	A	714	9.283	34.895	3.904	1.00	55.47	A	N
ATOM	1700	C	LYS	A	714	10.865	32.199	9.858	1.00	46.97	A	C
ATOM	1701	O	LYS	A	714	12.103	32.125	9.813	1.00	43.57	A	O
ATOM	1702	N	TRP	A	715	10.170	32.477	10.963	1.00	42.31	A	N
ATOM	1703	CA	TRP	A	715	10.831	32.815	12.203	1.00	36.99	A	C
ATOM	1704	CB	TRP	A	715	9.844	32.968	13.342	1.00	33.70	A	C
ATOM	1705	CG	TRP	A	715	10.556	33.022	14.636	1.00	34.96	A	C
ATOM	1706	CD1	TRP	A	715	11.239	34.073	15.133	1.00	36.36	A	C
ATOM	1707	NE1	TRP	A	715	11.791	33.751	16.346	1.00	37.12	A	N
ATOM	1708	CE2	TRP	A	715	11.469	32.459	16.649	1.00	36.71	A	C
ATOM	1709	CD2	TRP	A	715	10.699	31.964	15.585	1.00	38.08	A	C
ATOM	1710	CE3	TRP	A	715	10.235	30.643	15.653	1.00	42.71	A	C
ATOM	1711	CZ3	TRP	A	715	10.557	29.880	16.758	1.00	43.82	A	C
ATOM	1712	CH2	TRP	A	715	11.335	30.409	17.800	1.00	42.73	A	C
ATOM	1713	CZ2	TRP	A	715	11.798	31.692	17.761	1.00	38.42	A	C
ATOM	1714	C	TRP	A	715	11.907	31.793	12.560	1.00	35.89	A	C
ATOM	1715	O	TRP	A	715	13.046	32.171	12.830	1.00	42.05	A	O
ATOM	1716	N	ILE	A	716	11.565	30.508	12.532	1.00	29.01	A	N
ATOM	1717	CA	ILE	A	716	12.551	29.472	12.818	1.00	25.70	A	C
ATOM	1718	CB	ILE	A	716	12.000	28.086	12.571	1.00	19.69	A	C
ATOM	1719	CG1	ILE	A	716	10.683	27.889	13.333	1.00	18.28	A	C
ATOM	1720	CD1	ILE	A	716	10.093	26.517	13.207	1.00	13.05	A	C
ATOM	1721	CG2	ILE	A	716	13.070	27.064	12.937	1.00	13.56	A	C
ATOM	1722	C	ILE	A	716	13.793	29.631	11.963	1.00	31.34	A	C
ATOM	1723	O	ILE	A	716	14.911	29.574	12.469	1.00	34.55	A	O
ATOM	1724	N	HIS	A	717	13.600	29.826	10.667	1.00	34.01	A	N
ATOM	1725	CA	HIS	A	717	14.737	29.888	9.776	1.00	40.72	A	C
ATOM	1726	CB	HIS	A	717	14.288	29.962	8.326	1.00	40.20	A	C
ATOM	1727	CG	HIS	A	717	13.989	28.628	7.732	1.00	38.10	A	C
ATOM	1728	ND1	HIS	A	717	12.706	28.210	7.458	1.00	37.66	A	N
ATOM	1729	CE1	HIS	A	717	12.743	26.991	6.947	1.00	39.42	A	C
ATOM	1730	NE2	HIS	A	717	14.004	26.602	6.889	1.00	39.68	A	N
ATOM	1731	CD2	HIS	A	717	14.804	27.608	7.374	1.00	38.80	A	C
ATOM	1732	C	HIS	A	717	15.646	31.053	10.134	1.00	47.42	A	C
ATOM	1733	O	HIS	A	717	16.868	30.892	10.177	1.00	50.86	A	O
ATOM	1734	N	LYS	A	718	15.048	32.211	10.421	1.00	49.56	A	N
ATOM	1735	CA	LYS	A	718	15.821	33.418	10.728	1.00	50.74	A	C
ATOM	1736	CB	LYS	A	718	14.932	34.674	10.689	1.00	53.23	A	C
ATOM	1737	CG	LYS	A	718	15.153	35.710	11.785	1.00	55.66	A	C
ATOM	1738	CD	LYS	A	718	13.871	35.914	12.598	1.00	60.99	A	C
ATOM	1739	CE	LYS	A	718	13.785	37.307	13.223	1.00	65.16	A	C
ATOM	1740	NZ	LYS	A	718	13.795	38.395	12.194	1.00	68.77	A	N
ATOM	1741	C	LYS	A	718	16.582	33.275	12.045	1.00	48.84	A	C
ATOM	1742	O	LYS	A	718	17.526	34.015	12.300	1.00	49.48	A	O
ATOM	1743	N	ILE	A	719	16.193	32.300	12.859	1.00	45.24	A	N
ATOM	1744	CA	ILE	A	719	16.927	32.002	14.080	1.00	43.16	A	C
ATOM	1745	CB	ILE	A	719	15.962	31.552	15.181	1.00	42.64	A	C
ATOM	1746	CG1	ILE	A	719	14.993	32.684	15.542	1.00	42.75	A	C
ATOM	1747	CD1	ILE	A	719	15.628	33.885	16.185	1.00	43.06	A	C
ATOM	1748	CG2	ILE	A	719	16.719	31.019	16.402	1.00	42.10	A	C
ATOM	1749	C	ILE	A	719	18.019	30.960	13.865	1.00	44.68	A	C
ATOM	1750	O	ILE	A	719	19.130	31.130	14.364	1.00	44.01	A	O
ATOM	1751	N	ILE	A	720	17.705	29.897	13.122	1.00	47.92	A	N
ATOM	1752	CA	ILE	A	720	18.604	28.739	12.998	1.00	53.56	A	C
ATOM	1753	CB	ILE	A	720	17.823	27.406	12.880	1.00	50.50	A	C
ATOM	1754	CG1	ILE	A	720	16.906	27.414	11.666	1.00	49.87	A	C
ATOM	1755	CD1	ILE	A	720	17.308	26.438	10.631	1.00	52.61	A	C
ATOM	1756	CG2	ILE	A	720	17.007	27.149	14.121	1.00	53.14	A	C
ATOM	1757	C	ILE	A	720	19.609	28.844	11.857	1.00	61.95	A	C
ATOM	1758	O	ILE	A	720	20.764	28.419	11.998	1.00	64.33	A	O
ATOM	1759	N	LEU	A	721	19.160	29.372	10.719	1.00	67.80	A	N
ATOM	1760	CA	LEU	A	721	20.049	29.574	9.586	1.00	70.56	A	C
ATOM	1761	CB	LEU	A	721	19.276	29.888	8.302	1.00	69.78	A	C
ATOM	1762	CG	LEU	A	721	19.365	28.816	7.207	1.00	69.35	A	C
ATOM	1763	CD1	LEU	A	721	18.168	27.844	7.255	1.00	63.65	A	C
ATOM	1764	CD2	LEU	A	721	19.535	29.464	5.812	1.00	69.06	A	C
ATOM	1765	C	LEU	A	721	20.980	30.700	9.969	1.00	73.23	A	C
ATOM	1766	O	LEU	A	721	20.544	31.726	10.494	1.00	70.65	A	O
ATOM	1767	N	THR	A	722	22.272	30.464	9.763	1.00	80.61	A	N
ATOM	1768	CA	THR	A	722	23.323	31.413	10.134	1.00	87.21	A	C
ATOM	1769	CB	THR	A	722	23.375	31.652	11.695	1.00	90.25	A	C
ATOM	1770	OG1	THR	A	722	24.652	32.191	12.076	1.00	93.38	A	O
ATOM	1771	CG2	THR	A	722	23.270	30.337	12.491	1.00	91.06	A	C
ATOM	1772	C	THR	A	722	24.686	30.991	9.567	1.00	86.57	A	C
ATOM	1773	O	THR	A	722	25.245	31.668	8.697	1.00	85.09	A	O
ATOM	1774	N	LYS	B	40	−40.439	42.342	56.132	1.00	88.31	B	N
ATOM	1775	CA	LYS	B	40	−40.314	40.869	55.911	1.00	89.08	B	C
ATOM	1776	CB	LYS	B	40	−41.319	40.112	56.792	1.00	91.05	B	C
ATOM	1777	CG	LYS	B	40	−41.370	38.601	56.568	1.00	91.08	B	C
ATOM	1778	CD	LYS	B	40	−42.788	38.072	56.744	1.00	90.84	B	C
ATOM	1779	CE	LYS	B	40	−43.407	37.692	55.409	1.00	90.34	B	C
ATOM	1780	NZ	LYS	B	40	−44.531	38.595	55.063	1.00	90.81	B	N
ATOM	1781	C	LYS	B	40	−40.506	40.510	54.433	1.00	87.17	B	C
ATOM	1782	O	LYS	B	40	−41.613	40.627	53.890	1.00	87.44	B	O
ATOM	1783	N	TYR	B	41	−39.423	40.070	53.793	1.00	82.82	B	N
ATOM	1784	CA	TYR	B	41	−39.455	39.735	52.369	1.00	77.74	B	C
ATOM	1785	CB	TYR	B	41	−38.214	40.264	51.652	1.00	74.81	B	C
ATOM	1786	CG	TYR	B	41	−38.096	41.772	51.602	1.00	73.26	B	C
ATOM	1787	CD1	TYR	B	41	−36.962	42.402	52.091	1.00	72.23	B	C
ATOM	1788	CE1	TYR	B	41	−36.824	43.787	52.050	1.00	71.49	B	C
ATOM	1789	CZ	TYR	B	41	−37.824	44.566	51.508	1.00	70.43	B	C
ATOM	1790	OH	TYR	B	41	−37.644	45.935	51.482	1.00	68.52	B	O
ATOM	1791	CE2	TYR	B	41	−38.976	43.969	51.004	1.00	72.04	B	C
ATOM	1792	CD2	TYR	B	41	−39.105	42.570	51.050	1.00	73.83	B	C
ATOM	1793	C	TYR	B	41	−39.609	38.240	52.108	1.00	74.94	B	C
ATOM	1794	O	TYR	B	41	−39.354	37.415	52.983	1.00	72.98	B	O
ATOM	1795	N	GLN	B	42	−40.028	37.917	50.887	1.00	73.46	B	N
ATOM	1796	CA	GLN	B	42	−40.326	36.552	50.471	1.00	72.07	B	C
ATOM	1797	CB	GLN	B	42	−41.851	36.391	50.273	1.00	74.52	B	C
ATOM	1798	CG	GLN	B	42	−42.323	35.498	49.116	1.00	76.03	B	C
ATOM	1799	CD	GLN	B	42	−42.263	34.010	49.439	1.00	74.54	B	C
ATOM	1800	OE1	GLN	B	42	−43.257	33.420	49.867	1.00	72.50	B	O
ATOM	1801	NE2	GLN	B	42	−41.100	33.402	49.222	1.00	74.77	B	N
ATOM	1802	C	GLN	B	42	−39.498	36.216	49.217	1.00	69.39	B	C
ATOM	1803	O	GLN	B	42	−39.776	36.699	48.116	1.00	70.35	B	O
ATOM	1804	N	LEU	B	43	−38.467	35.395	49.406	1.00	65.67	B	N
ATOM	1805	CA	LEU	B	43	−37.458	35.147	48.374	1.00	60.10	B	C
ATOM	1806	CB	LEU	B	43	−36.186	35.926	48.707	1.00	55.50	B	C
ATOM	1807	CG	LEU	B	43	−36.311	37.445	48.634	1.00	53.79	B	C
ATOM	1808	CD1	LEU	B	43	−35.264	38.123	49.493	1.00	51.21	B	C
ATOM	1809	CD2	LEU	B	43	−36.236	37.931	47.187	1.00	54.63	B	C
ATOM	1810	C	LEU	B	43	−37.129	33.658	48.226	1.00	58.51	B	C
ATOM	1811	O	LEU	B	43	−37.399	32.883	49.150	1.00	59.14	B	O
ATOM	1812	N	PRO	B	44	−36.578	33.255	47.070	1.00	54.41	B	N
ATOM	1813	CA	PRO	B	44	−36.135	31.871	46.864	1.00	52.74	B	C
ATOM	1814	CB	PRO	B	44	−35.464	31.930	45.497	1.00	50.09	B	C
ATOM	1815	CG	PRO	B	44	−36.199	33.016	44.788	1.00	48.95	B	C
ATOM	1816	CD	PRO	B	44	−36.385	34.064	45.850	1.00	52.02	B	C
ATOM	1817	C	PRO	B	44	−35.164	31.437	47.956	1.00	55.95	B	C
ATOM	1818	O	PRO	B	44	−34.059	31.975	48.057	1.00	57.32	B	O
ATOM	1819	N	ASN	B	45	−35.602	30.475	48.768	1.00	57.90	B	N
ATOM	1820	CA	ASN	B	45	−34.996	30.210	50.072	1.00	56.49	B	C
ATOM	1821	CB	ASN	B	45	−35.896	30.734	51.251	1.00	59.73	B	C
ATOM	1822	CG	ASN	B	45	−37.444	30.377	51.125	1.00	61.49	B	C
ATOM	1823	OD1	ASN	B	45	−38.318	31.134	51.606	1.00	56.31	B	O
ATOM	1824	ND2	ASN	B	45	−37.756	29.226	50.537	1.00	63.28	B	N
ATOM	1825	C	ASN	B	45	−34.559	28.770	50.323	1.00	55.39	B	C
ATOM	1826	O	ASN	B	45	−35.290	28.037	50.995	1.00	59.64	B	O
ATOM	1827	N	PHE	B	46	−33.381	28.356	49.826	1.00	50.73	B	N
ATOM	1828	CA	PHE	B	46	−32.858	27.004	50.170	1.00	45.86	B	C
ATOM	1829	CB	PHE	B	46	−32.065	26.320	49.053	1.00	45.33	B	C
ATOM	1830	CG	PHE	B	46	−31.521	24.969	49.467	1.00	44.34	B	C
ATOM	1831	CD1	PHE	B	46	−32.353	23.853	49.510	1.00	46.55	B	C
ATOM	1832	CE1	PHE	B	46	−31.859	22.600	49.920	1.00	43.16	B	C
ATOM	1833	CZ	PHE	B	46	−30.542	22.476	50.304	1.00	39.14	B	C
ATOM	1834	CE2	PHE	B	46	−29.712	23.588	50.285	1.00	38.80	B	C
ATOM	1835	CD2	PHE	B	46	−30.201	24.824	49.879	1.00	41.12	B	C
ATOM	1836	C	PHE	B	46	−32.060	26.841	51.473	1.00	41.12	B	C
ATOM	1837	O	PHE	B	46	−31.092	27.559	51.722	1.00	33.78	B	O
ATOM	1838	N	THR	B	47	−32.459	25.826	52.241	1.00	43.61	B	N
ATOM	1839	CA	THR	B	47	−31.914	25.507	53.555	1.00	47.93	B	C
ATOM	1840	CB	THR	B	47	−33.049	25.533	54.579	1.00	47.66	B	C
ATOM	1841	OG1	THR	B	47	−33.753	26.778	54.498	1.00	49.67	B	O
ATOM	1842	CG2	THR	B	47	−32.499	25.486	56.003	1.00	47.43	B	C
ATOM	1843	C	THR	B	47	−31.297	24.104	53.588	1.00	53.53	B	C
ATOM	1844	O	THR	B	47	−31.994	23.105	53.386	1.00	57.56	B	O
ATOM	1845	N	ALA	B	48	−30.006	24.023	53.886	1.00	54.57	B	N
ATOM	1846	CA	ALA	B	48	−29.338	22.731	54.009	1.00	57.41	B	C
ATOM	1847	CB	ALA	B	48	−27.942	22.816	53.453	1.00	61.70	B	C
ATOM	1848	C	ALA	B	48	−29.291	22.235	55.446	1.00	57.95	B	C
ATOM	1849	O	ALA	B	48	−29.491	23.005	56.387	1.00	58.63	B	O
ATOM	1850	N	GLU	B	49	−28.996	20.949	55.608	1.00	59.00	B	N
ATOM	1851	CA	GLU	B	49	−28.923	20.351	56.936	1.00	61.70	B	C
ATOM	1852	CB	GLU	B	49	−29.316	18.860	56.902	1.00	67.90	B	C
ATOM	1853	CG	GLU	B	49	−30.824	18.591	56.926	1.00	72.95	B	C
ATOM	1854	CD	GLU	B	49	−31.524	19.154	58.163	1.00	78.90	B	C
ATOM	1855	OE1	GLU	B	49	−31.300	18.617	59.277	1.00	81.87	B	O
ATOM	1856	OE2	GLU	B	49	−32.302	20.133	58.027	1.00	78.86	B	O
ATOM	1857	C	GLU	B	49	−27.568	20.562	57.620	1.00	57.45	B	C
ATOM	1858	O	GLU	B	49	−27.410	20.234	58.800	1.00	60.69	B	O
ATOM	1859	N	THR	B	50	−26.597	21.106	56.887	1.00	50.48	B	N
ATOM	1860	CA	THR	B	50	−25.287	21.443	57.459	1.00	46.07	B	C
ATOM	1861	CB	THR	B	50	−24.215	20.346	57.182	1.00	45.63	B	C
ATOM	1862	OG1	THR	B	50	−23.565	20.588	55.925	1.00	43.30	B	O
ATOM	1863	CG2	THR	B	50	−24.852	18.971	57.009	1.00	47.44	B	C
ATOM	1864	C	THR	B	50	−24.814	22.789	56.939	1.00	42.87	B	C
ATOM	1865	O	THR	B	50	−25.212	23.184	55.850	1.00	46.52	B	O
ATOM	1866	N	PRO	B	51	−23.969	23.486	57.704	1.00	39.97	B	N
ATOM	1867	CA	PRO	B	51	−23.454	24.813	57.318	1.00	41.14	B	C
ATOM	1868	CB	PRO	B	51	−22.417	25.100	58.402	1.00	39.83	B	C
ATOM	1869	CG	PRO	B	51	−22.894	24.330	59.568	1.00	39.25	B	C
ATOM	1870	CD	PRO	B	51	−23.441	23.060	59.012	1.00	39.48	B	C
ATOM	1871	C	PRO	B	51	−22.788	24.881	55.931	1.00	43.57	B	C
ATOM	1872	O	PRO	B	51	−22.138	23.917	55.502	1.00	46.80	B	O
ATOM	1873	N	ILE	B	52	−22.935	26.019	55.252	1.00	40.80	B	N
ATOM	1874	CA	ILE	B	52	−22.419	26.180	53.889	1.00	38.35	B	C
ATOM	1875	CB	ILE	B	52	−23.457	26.911	53.006	1.00	39.32	B	C
ATOM	1876	CG1	ILE	B	52	−24.813	26.203	53.092	1.00	37.65	B	C
ATOM	1877	CD1	ILE	B	52	−25.748	26.480	51.943	1.00	35.28	B	C
ATOM	1878	CG2	ILE	B	52	−22.924	27.055	51.565	1.00	41.75	B	C
ATOM	1879	C	ILE	B	52	−21.096	26.937	53.845	1.00	34.40	B	C
ATOM	1880	O	ILE	B	52	−21.038	28.113	54.165	1.00	35.36	B	O
ATOM	1881	N	GLN	B	53	−20.029	26.287	53.423	1.00	33.14	B	N
ATOM	1882	CA	GLN	B	53	−18.770	27.009	53.342	1.00	36.41	B	C
ATOM	1883	CB	GLN	B	53	−17.577	26.075	53.474	1.00	35.02	B	C
ATOM	1884	CG	GLN	B	53	−17.288	25.692	54.878	1.00	38.75	B	C
ATOM	1885	CD	GLN	B	53	−18.283	24.685	55.393	1.00	41.87	B	C
ATOM	1886	OE1	GLN	B	53	−19.091	25.007	56.271	1.00	45.15	B	O
ATOM	1887	NE2	GLN	B	53	−18.241	23.467	54.849	1.00	38.83	B	N
ATOM	1888	C	GLN	B	53	−18.627	27.820	52.068	1.00	38.87	B	C
ATOM	1889	O	GLN	B	53	−18.137	28.945	52.130	1.00	42.84	B	O
ATOM	1890	N	ASN	B	54	−19.044	27.247	50.934	1.00	34.88	B	N
ATOM	1891	CA	ASN	B	54	−18.616	27.716	49.617	1.00	39.39	B	C
ATOM	1892	CB	ASN	B	54	−17.328	27.018	49.209	1.00	42.49	B	C
ATOM	1893	CG	ASN	B	54	−16.126	27.575	49.912	1.00	46.56	B	C
ATOM	1894	OD1	ASN	B	54	−15.962	28.787	50.023	1.00	49.88	B	O
ATOM	1895	ND2	ASN	B	54	−15.271	26.692	50.397	1.00	50.16	B	N
ATOM	1896	C	ASN	B	54	−19.646	27.491	48.529	1.00	43.00	B	C
ATOM	1897	O	ASN	B	54	−20.502	26.607	48.660	1.00	46.24	B	O
ATOM	1898	N	VAL	B	55	−19.550	28.269	47.445	1.00	39.10	B	N
ATOM	1899	CA	VAL	B	55	−20.634	28.306	46.466	1.00	37.57	B	C
ATOM	1900	CB	VAL	B	55	−21.693	29.308	46.909	1.00	30.43	B	C
ATOM	1901	CG1	VAL	B	55	−22.337	29.978	45.755	1.00	23.21	B	C
ATOM	1902	CG2	VAL	B	55	−22.718	28.564	47.647	1.00	36.18	B	C
ATOM	1903	C	VAL	B	55	−20.206	28.583	45.037	1.00	44.19	B	C
ATOM	1904	O	VAL	B	55	−19.450	29.517	44.778	1.00	52.60	B	O
ATOM	1905	N	ILE	B	56	−20.698	27.778	44.104	1.00	44.46	B	N
ATOM	1906	CA	ILE	B	56	−20.324	27.934	42.704	1.00	45.81	B	C
ATOM	1907	CB	ILE	B	56	−19.295	26.842	42.287	1.00	46.87	B	C
ATOM	1908	CG1	ILE	B	56	−17.892	27.376	42.446	1.00	52.08	B	C
ATOM	1909	CD1	ILE	B	56	−17.318	27.148	43.792	1.00	56.76	B	C
ATOM	1910	CG2	ILE	B	56	−19.398	26.458	40.836	1.00	45.77	B	C
ATOM	1911	C	ILE	B	56	−21.570	27.873	41.858	1.00	47.28	B	C
ATOM	1912	O	ILE	B	56	−22.489	27.083	42.141	1.00	49.61	B	O
ATOM	1913	N	LEU	B	57	−21.611	28.720	40.832	1.00	43.17	B	N
ATOM	1914	CA	LEU	B	57	−22.684	28.649	39.859	1.00	43.94	B	C
ATOM	1915	CB	LEU	B	57	−23.326	30.017	39.659	1.00	44.30	B	C
ATOM	1916	CG	LEU	B	57	−24.339	30.154	38.525	1.00	41.92	B	C
ATOM	1917	CD1	LEU	B	57	−25.656	29.469	38.866	1.00	42.10	B	C
ATOM	1918	CD2	LEU	B	57	−24.549	31.616	38.288	1.00	39.61	B	C
ATOM	1919	C	LEU	B	57	−22.128	28.144	38.556	1.00	46.44	B	C
ATOM	1920	O	LEU	B	57	−21.215	28.748	38.011	1.00	49.16	B	O
ATOM	1921	N	HIS	B	58	−22.672	27.037	38.058	1.00	50.00	B	N
ATOM	1922	CA	HIS	B	58	−22.206	26.468	36.797	1.00	52.04	B	C
ATOM	1923	CB	HIS	B	58	−21.139	25.426	37.064	1.00	52.03	B	C
ATOM	1924	CG	HIS	B	58	−20.771	24.625	35.859	1.00	54.05	B	C
ATOM	1925	ND1	HIS	B	58	−20.016	25.142	34.828	1.00	51.30	B	N
ATOM	1926	CE1	HIS	B	58	−19.848	24.205	33.909	1.00	55.00	B	C
ATOM	1927	NE2	HIS	B	58	−20.479	23.109	34.299	1.00	54.05	B	N
ATOM	1928	CD2	HIS	B	58	−21.055	23.341	35.522	1.00	53.13	B	C
ATOM	1929	C	HIS	B	58	−23.331	25.874	35.954	1.00	53.48	B	C
ATOM	1930	O	HIS	B	58	−24.150	25.116	36.460	1.00	55.42	B	O
ATOM	1931	N	GLU	B	59	−23.359	26.224	34.670	1.00	55.38	B	N
ATOM	1932	CA	GLU	B	59	−24.352	25.707	33.736	1.00	58.47	B	C
ATOM	1933	CB	GLU	B	59	−23.874	24.385	33.133	1.00	63.90	B	C
ATOM	1934	CG	GLU	B	59	−24.051	24.281	31.628	1.00	72.24	B	C
ATOM	1935	CD	GLU	B	59	−22.992	25.055	30.864	1.00	81.17	B	C
ATOM	1936	OE1	GLU	B	59	−23.345	26.083	30.242	1.00	85.96	B	O
ATOM	1937	OE2	GLU	B	59	−21.805	24.643	30.885	1.00	84.29	B	O
ATOM	1938	C	GLU	B	59	−25.729	25.534	34.382	1.00	59.86	B	C
ATOM	1939	O	GLU	B	59	−26.275	24.427	34.430	1.00	61.83	B	O
ATOM	1940	N	HIS	B		60	−26.275	26.635	34.893	1.00	59.00	B	N
ATOM	1941	CA	HIS	B		60	−27.634	26.668	35.440	1.00	57.01	B	C
ATOM	1942	CB	HIS	B	60	−28.653	26.383	34.333	1.00	58.99	B	C
ATOM	1943	CG	HIS	B		60	−28.442	27.210	33.104	1.00	64.85	B	C
ATOM	1944	ND1	HIS	B		60	−28.149	28.556	33.155	1.00	67.98	B	N
ATOM	1945	CE1	HIS	B		60	−28.008	29.023	31.927	1.00	69.99	B	C
ATOM	1946	NE2	HIS	B		60	−28.192	28.025	31.080	1.00	71.81	B	N
ATOM	1947	CD2	HIS	B		60	−28.465	26.880	31.791	1.00	68.41	B	C
ATOM	1948	C	HIS	B		60	−27.854	25.774	36.671	1.00	54.57	B	C
ATOM	1949	O	HIS	B		60	−28.965	25.348	36.960	1.00	58.35	B	O
ATOM	1950	N	HIS	B	61	−26.789	25.502	37.404	1.00	50.20	B	N
ATOM	1951	CA	HIS	B	61	−26.920	24.835	38.682	1.00	48.51	B	C
ATOM	1952	CB	HIS	B	61	−26.548	23.373	38.552	1.00	53.72	B	C
ATOM	1953	CG	HIS	B	61	−27.395	22.614	37.579	1.00	60.35	B	C
ATOM	1954	ND1	HIS	B	61	−28.477	21.851	37.967	1.00	63.50	B	N
ATOM	1955	CE1	HIS	B	61	−29.019	21.284	36.904	1.00	63.17	B	C
ATOM	1956	NE2	HIS	B	61	−28.324	21.647	35.840	1.00	63.83	B	N
ATOM	1957	CD2	HIS	B	61	−27.301	22.476	36.235	1.00	62.28	B	C
ATOM	1958	C	HIS	B	61	−26.055	25.520	39.738	1.00	48.02	B	C
ATOM	1959	O	HIS	B	61	−25.152	26.297	39.424	1.00	49.98	B	O
ATOM	1960	N	ILE	B	62	−26.345	25.240	40.998	1.00	43.61	B	N
ATOM	1961	CA	ILE	B	62	−25.661	25.892	42.094	1.00	42.88	B	C
ATOM	1962	CB	ILE	B	62	−26.681	26.718	42.903	1.00	43.14	B	C
ATOM	1963	CG1	ILE	B	62	−27.102	27.963	42.128	1.00	36.21	B	C
ATOM	1964	CD1	ILE	B	62	−27.829	28.928	42.974	1.00	32.13	B	C
ATOM	1965	CG2	ILE	B	62	−26.133	27.093	44.292	1.00	47.65	B	C
ATOM	1966	C	ILE	B	62	−25.053	24.788	42.945	1.00	47.29	B	C
ATOM	1967	O	ILE	B	62	−25.740	23.833	43.313	1.00	53.80	B	O
ATOM	1968	N	PHE	B	63	−23.769	24.901	43.254	1.00	43.54	B	N
ATOM	1969	CA	PHE	B	63	−23.103	23.841	43.979	1.00	41.13	B	C
ATOM	1970	CB	PHE	B	63	−21.900	23.348	43.194	1.00	41.26	B	C
ATOM	1971	CG	PHE	B	63	−22.238	22.800	41.832	1.00	44.61	B	C
ATOM	1972	CD1	PHE	B	63	−22.270	23.640	40.714	1.00	45.84	B	C
ATOM	1973	CE1	PHE	B	63	−22.579	23.128	39.455	1.00	46.17	B	C
ATOM	1974	CZ	PHE	B	63	−22.852	21.745	39.310	1.00	46.42	B	C
ATOM	1975	CE2	PHE	B	63	−22.815	20.906	40.412	1.00	40.65	B	C
ATOM	1976	CD2	PHE	B	63	−22.510	21.434	41.660	1.00	43.43	B	C
ATOM	1977	C	PHE	B	63	−22.659	24.375	45.313	1.00	45.66	B	C
ATOM	1978	O	PHE	B	63	−21.739	25.196	45.389	1.00	52.04	B	O
ATOM	1979	N	LEU	B	64	−23.323	23.935	46.373	1.00	42.46	B	N
ATOM	1980	CA	LEU	B	64	−22.908	24.347	47.706	1.00	42.09	B	C
ATOM	1981	CB	LEU	B	64	−24.114	24.440	48.636	1.00	41.69	B	C
ATOM	1982	CG	LEU	B	64	−25.365	25.182	48.154	1.00	42.08	B	C
ATOM	1983	CD1	LEU	B	64	−26.591	24.571	48.787	1.00	44.25	B	C
ATOM	1984	CD2	LEU	B	64	−25.321	26.644	48.511	1.00	40.96	B	C
ATOM	1985	C	LEU	B	64	−21.855	23.387	48.267	1.00	40.28	B	C
ATOM	1986	O	LEU	B	64	−22.035	22.182	48.211	1.00	44.05	B	O
ATOM	1987	N	GLY	B	65	−20.755	23.920	48.791	1.00	37.34	B	N
ATOM	1988	CA	GLY	B	65	−19.732	23.101	49.422	1.00	37.17	B	C
ATOM	1989	C	GLY	B	65	−19.905	23.231	50.914	1.00	42.05	B	C
ATOM	1990	O	GLY	B	65	−19.662	24.296	51.471	1.00	47.10	B	O
ATOM	1991	N	ALA	B	66	−20.342	22.157	51.561	1.00	44.53	B	N
ATOM	1992	CA	ALA	B	66	−20.892	22.253	52.912	1.00	48.80	B	C
ATOM	1993	CB	ALA	B	66	−22.389	21.972	52.888	1.00	48.72	B	C
ATOM	1994	C	ALA	B	66	−20.203	21.287	53.836	1.00	53.33	B	C
ATOM	1995	O	ALA	B	66	−19.468	20.412	53.364	1.00	58.02	B	O
ATOM	1996	N	THR	B	67	−20.439	21.436	55.146	1.00	54.28	B	N
ATOM	1997	CA	THR	B	67	−19.855	20.522	56.139	1.00	51.15	B	C
ATOM	1998	CB	THR	B	67	−20.165	20.930	57.593	1.00	53.21	B	C
ATOM	1999	OG1	THR	B	67	−20.088	22.352	57.740	1.00	57.91	B	O
ATOM	2000	CG2	THR	B	67	−19.061	20.461	58.491	1.00	53.41	B	C
ATOM	2001	C	THR	B	67	−20.329	19.103	55.866	1.00	47.02	B	C
ATOM	2002	O	THR	B	67	−21.516	18.788	55.965	1.00	40.82	B	O
ATOM	2003	N	ASN	B	68	−19.383	18.272	55.451	1.00	50.36	B	N
ATOM	2004	CA	ASN	B	68	−19.649	16.877	55.108	1.00	52.51	B	C
ATOM	2005	CB	ASN	B	68	−20.235	16.140	56.331	1.00	52.59	B	C
ATOM	2006	CG	ASN	B	68	−19.210	15.965	57.461	1.00	51.03	B	C
ATOM	2007	OD1	ASN	B	68	−18.111	15.446	57.243	1.00	51.42	B	O
ATOM	2008	ND2	ASN	B	68	−19.563	16.406	58.662	1.00	45.80	B	N
ATOM	2009	C	ASN	B	68	−20.488	16.686	53.819	1.00	50.64	B	C
ATOM	2010	O	ASN	B	68	−20.866	15.565	53.458	1.00	44.48	B	O
ATOM	2011	N	TYR	B	69	−20.738	17.778	53.101	1.00	52.92	B	N
ATOM	2012	CA	TYR	B	69	−21.653	17.721	51.967	1.00	55.27	B	C
ATOM	2013	CB	TYR	B	69	−23.085	18.021	52.436	1.00	60.82	B	C
ATOM	2014	CG	TYR	B	69	−23.773	16.805	52.983	1.00	64.11	B	C
ATOM	2015	CD1	TYR	B	69	−23.769	16.542	54.351	1.00	66.02	B	C
ATOM	2016	CE1	TYR	B	69	−24.382	15.408	54.863	1.00	68.88	B	C
ATOM	2017	CZ	TYR	B	69	−25.006	14.521	53.997	1.00	71.22	B	C
ATOM	2018	OH	TYR	B	69	−25.616	13.398	54.506	1.00	75.18	B	O
ATOM	2019	CE2	TYR	B	69	−25.017	14.757	52.627	1.00	69.32	B	C
ATOM	2020	CD2	TYR	B	69	−24.397	15.895	52.130	1.00	66.33	B	C
ATOM	2021	C	TYR	B	69	−21.306	18.619	50.793	1.00	51.42	B	C
ATOM	2022	O	TYR	B	69	−20.702	19.677	50.962	1.00	51.14	B	O
ATOM	2023	N	ILE	B	70	−21.701	18.174	49.603	1.00	46.28	B	N
ATOM	2024	CA	ILE	B	70	−21.839	19.058	48.451	1.00	43.86	B	C
ATOM	2025	CB	ILE	B	70	−20.843	18.667	47.346	1.00	37.93	B	C
ATOM	2026	CG1	ILE	B	70	−19.444	19.128	47.717	1.00	32.94	B	C
ATOM	2027	CD1	ILE	B	70	−18.399	18.442	46.925	1.00	34.13	B	C
ATOM	2028	CG2	ILE	B	70	−21.259	19.241	45.989	1.00	35.59	B	C
ATOM	2029	C	ILE	B	70	−23.277	18.950	47.948	1.00	47.16	B	C
ATOM	2030	O	ILE	B	70	−23.763	17.838	47.730	1.00	53.11	B	O
ATOM	2031	N	TYR	B	71	−23.961	20.086	47.794	1.00	46.45	B	N
ATOM	2032	CA	TYR	B	71	−25.315	20.094	47.227	1.00	47.00	B	C
ATOM	2033	CB	TYR	B	71	−26.296	20.874	48.101	1.00	45.72	B	C
ATOM	2034	CG	TYR	B	71	−26.279	20.473	49.539	1.00	47.73	B	C
ATOM	2035	CD1	TYR	B	71	−26.054	21.415	50.527	1.00	50.65	B	C
ATOM	2036	CE1	TYR	B	71	−26.021	21.067	51.850	1.00	54.50	B	C
ATOM	2037	CZ	TYR	B	71	−26.222	19.753	52.207	1.00	60.11	B	C
ATOM	2038	OH	TYR	B	71	−26.193	19.402	53.541	1.00	67.11	B	O
ATOM	2039	CE2	TYR	B	71	−26.445	18.788	51.237	1.00	57.17	B	C
ATOM	2040	CD2	TYR	B	71	−26.476	19.157	49.912	1.00	50.73	B	C
ATOM	2041	C	TYR	B	71	−25.382	20.653	45.820	1.00	48.72	B	C
ATOM	2042	O	TYR	B	71	−24.512	21.401	45.377	1.00	53.16	B	O
ATOM	2043	N	VAL	B	72	−26.445	20.289	45.124	1.00	47.30	B	N
ATOM	2044	CA	VAL	B	72	−26.719	20.847	43.819	1.00	47.03	B	C
ATOM	2045	CB	VAL	B	72	−26.503	19.814	42.696	1.00	48.79	B	C
ATOM	2046	CG1	VAL	B	72	−26.205	20.515	41.378	1.00	48.07	B	C
ATOM	2047	CG2	VAL	B	72	−25.368	18.860	43.059	1.00	49.23	B	C
ATOM	2048	C	VAL	B	72	−28.145	21.372	43.824	1.00	44.93	B	C
ATOM	2049	O	VAL	B	72	−29.085	20.627	44.081	1.00	46.42	B	O
ATOM	2050	N	LEU	B	73	−28.288	22.667	43.571	1.00	42.05	B	N
ATOM	2051	CA	LEU	B	73	−29.594	23.294	43.462	1.00	40.82	B	C
ATOM	2052	CB	LEU	B	73	−29.690	24.478	44.406	1.00	39.41	B	C
ATOM	2053	CG	LEU	B	73	−28.964	24.390	45.744	1.00	38.24	B	C
ATOM	2054	CD1	LEU	B	73	−29.253	25.650	46.544	1.00	34.92	B	C
ATOM	2055	CD2	LEU	B	73	−29.368	23.121	46.520	1.00	36.03	B	C
ATOM	2056	C	LEU	B	73	−29.810	23.782	42.052	1.00	44.28	B	C
ATOM	2057	O	LEU	B	73	−28.848	24.014	41.318	1.00	46.00	B	O
ATOM	2058	N	ASN	B	74	−31.069	23.938	41.668	1.00	47.90	B	N
ATOM	2059	CA	ASN	B	74	−31.384	24.522	40.374	1.00	58.54	B	C
ATOM	2060	CB	ASN	B	74	−32.808	24.161	39.984	1.00	64.84	B	C
ATOM	2061	CG	ASN	B	74	−32.852	23.164	38.865	1.00	72.43	B	C
ATOM	2062	OD1	ASN	B	74	−32.112	23.291	37.881	1.00	76.53	B	O
ATOM	2063	ND2	ASN	B	74	−33.711	22.152	39.000	1.00	73.79	B	N
ATOM	2064	C	ASN	B	74	−31.226	26.037	40.393	1.00	62.21	B	C
ATOM	2065	O	ASN	B	74	−31.793	26.691	41.265	1.00	66.91	B	O
ATOM	2066	N	GLU	B	75	−30.472	26.603	39.448	1.00	61.46	B	N
ATOM	2067	CA	GLU	B	75	−30.289	28.065	39.404	1.00	61.67	B	C
ATOM	2068	CB	GLU	B	75	−29.537	28.526	38.146	1.00	60.79	B	C
ATOM	2069	CG	GLU	B	75	−29.614	30.042	37.927	1.00	62.00	B	C
ATOM	2070	CD	GLU	B	75	−29.076	30.516	36.586	1.00	64.68	B	C
ATOM	2071	OE1	GLU	B	75	−29.298	29.813	35.571	1.00	69.00	B	O
ATOM	2072	OE2	GLU	B	75	−28.441	31.601	36.542	1.00	60.03	B	O
ATOM	2073	C	GLU	B	75	−31.621	28.817	39.490	1.00	62.54	B	C
ATOM	2074	O	GLU	B	75	−31.722	29.860	40.144	1.00	58.12	B	O
ATOM	2075	N	GLU	B	76	−32.638	28.268	38.831	1.00	66.63	B	N
ATOM	2076	CA	GLU	B	76	−33.910	28.962	38.676	1.00	66.67	B	C
ATOM	2077	CB	GLU	B	76	−34.747	28.336	37.562	1.00	72.43	B	C
ATOM	2078	CG	GLU	B	76	−35.688	29.317	36.888	1.00	75.56	B	C
ATOM	2079	CD	GLU	B	76	−37.076	29.248	37.482	1.00	80.75	B	C
ATOM	2080	OE1	GLU	B	76	−37.390	28.214	38.116	1.00	82.06	B	O
ATOM	2081	OE2	GLU	B	76	−37.850	30.222	37.324	1.00	83.79	B	O
ATOM	2082	C	GLU	B	76	−34.711	29.097	39.965	1.00	60.03	B	C
ATOM	2083	O	GLU	B	76	−35.141	30.191	40.282	1.00	59.16	B	O
ATOM	2084	N	ASP	B	77	−34.892	28.018	40.718	1.00	55.97	B	N
ATOM	2085	CA	ASP	B	77	−35.711	28.109	41.925	1.00	56.24	B	C
ATOM	2086	CB	ASP	B	77	−37.060	27.418	41.706	1.00	61.87	B	C
ATOM	2087	CG	ASP	B	77	−36.977	25.912	41.842	1.00	67.33	B	C
ATOM	2088	OD1	ASP	B	77	−37.984	25.237	41.533	1.00	68.78	B	O
ATOM	2089	OD2	ASP	B	77	−35.953	25.316	42.248	1.00	69.35	B	O
ATOM	2090	C	ASP	B	77	−35.058	27.642	43.231	1.00	54.59	B	C
ATOM	2091	O	ASP	B	77	−35.696	27.645	44.279	1.00	54.85	B	O
ATOM	2092	N	LEU	B	78	−33.797	27.232	43.157	1.00	55.56	B	N
ATOM	2093	CA	LEU	B	78	−33.003	26.833	44.337	1.00	58.90	B	C
ATOM	2094	CB	LEU	B	78	−32.897	27.974	45.376	1.00	53.06	B	C
ATOM	2095	CG	LEU	B	78	−32.152	29.307	45.162	1.00	47.82	B	C
ATOM	2096	CD1	LEU	B	78	−31.018	29.485	46.171	1.00	44.03	B	C
ATOM	2097	CD2	LEU	B	78	−31.640	29.540	43.741	1.00	46.46	B	C
ATOM	2098	C	LEU	B	78	−33.450	25.516	45.012	1.00	65.07	B	C
ATOM	2099	O	LEU	B	78	−33.004	25.197	46.123	1.00	66.17	B	O
ATOM	2100	N	GLN	B	79	−34.319	24.760	44.339	1.00	67.54	B	N
ATOM	2101	CA	GLN	B	79	−34.654	23.397	44.756	1.00	69.76	B	C
ATOM	2102	CB	GLN	B	79	−35.741	22.814	43.850	1.00	76.35	B	C
ATOM	2103	CG	GLN	B	79	−36.637	21.762	44.505	1.00	80.54	B	C
ATOM	2104	CD	GLN	B	79	−38.004	22.319	44.866	1.00	82.06	B	C
ATOM	2105	OE1	GLN	B	79	−38.692	22.886	44.014	1.00	82.50	B	O
ATOM	2106	NE2	GLN	B	79	−38.394	22.170	46.128	1.00	82.37	B	N
ATOM	2107	C	GLN	B	79	−33.427	22.499	44.674	1.00	65.91	B	C
ATOM	2108	O	GLN	B	79	−32.692	22.539	43.679	1.00	65.87	B	O
ATOM	2109	N	LYS	B	80	−33.214	21.695	45.717	1.00	62.42	B	N
ATOM	2110	CA	LYS	B	80	−32.112	20.727	45.745	1.00	58.13	B	C
ATOM	2111	CB	LYS	B	80	−31.918	20.140	47.155	1.00	54.23	B	C
ATOM	2112	CG	LYS	B	80	−30.826	19.091	47.281	1.00	52.77	B	C
ATOM	2113	CD	LYS	B	80	−31.018	18.220	48.518	1.00	55.97	B	C
ATOM	2114	CE	LYS	B	80	−31.433	16.786	48.144	1.00	58.79	B	C
ATOM	2115	NZ	LYS	B	80	−32.514	16.211	49.026	1.00	58.94	B	N
ATOM	2116	C	LYS	B	80	−32.406	19.636	44.730	1.00	56.61	B	C
ATOM	2117	O	LYS	B	80	−33.469	19.024	44.760	1.00	58.06	B	O
ATOM	2118	N	VAL	B	81	−31.475	19.425	43.811	1.00	55.86	B	N
ATOM	2119	CA	VAL	B	81	−31.624	18.392	42.805	1.00	57.02	B	C
ATOM	2120	CB	VAL	B	81	−31.165	18.874	41.411	1.00	57.57	B	C
ATOM	2121	CG1	VAL	B	81	−31.286	17.752	40.378	1.00	59.42	B	C
ATOM	2122	CG2	VAL	B	81	−31.984	20.061	40.974	1.00	57.61	B	C
ATOM	2123	C	VAL	B	81	−30.836	17.164	43.232	1.00	58.29	B	C
ATOM	2124	O	VAL	B	81	−31.331	16.044	43.138	1.00	59.22	B	O
ATOM	2125	N	ALA	B	82	−29.616	17.380	43.714	1.00	59.89	B	N
ATOM	2126	CA	ALA	B	82	−28.717	16.274	44.032	1.00	62.94	B	C
ATOM	2127	CB	ALA	B	82	−27.822	15.975	42.837	1.00	63.74	B	C
ATOM	2128	C	ALA	B	82	−27.864	16.550	45.261	1.00	63.09	B	C
ATOM	2129	O	ALA	B	82	−27.544	17.704	45.552	1.00	64.92	B	O
ATOM	2130	N	GLU	B	83	−27.503	15.492	45.984	1.00	60.73	B	N
ATOM	2131	CA	GLU	B	83	−26.475	15.612	47.009	1.00	62.28	B	C
ATOM	2132	CB	GLU	B	83	−27.023	15.376	48.419	1.00	68.08	B	C
ATOM	2133	CG	GLU	B	83	−27.855	14.121	48.610	1.00	76.60	B	C
ATOM	2134	CD	GLU	B	83	−29.189	14.422	49.274	1.00	83.85	B	C
ATOM	2135	OE1	GLU	B	83	−29.224	15.283	50.188	1.00	84.72	B	O
ATOM	2136	OE2	GLU	B	83	−30.211	13.809	48.878	1.00	87.29	B	O
ATOM	2137	C	GLU	B	83	−25.299	14.691	46.742	1.00	62.10	B	C
ATOM	2138	O	GLU	B	83	−25.396	13.727	45.980	1.00	67.85	B	O
ATOM	2139	N	TYR	B	84	−24.171	15.015	47.349	1.00	56.36	B	N
ATOM	2140	CA	TYR	B	84	−23.093	14.063	47.448	1.00	54.60	B	C
ATOM	2141	CB	TYR	B	84	−22.068	14.297	46.377	1.00	50.63	B	C
ATOM	2142	CG	TYR	B	84	−20.818	13.464	46.515	1.00	49.86	B	C
ATOM	2143	CD1	TYR	B	84	−20.534	12.463	45.590	1.00	50.46	B	C
ATOM	2144	CE1	TYR	B	84	−19.367	11.713	45.684	1.00	53.44	B	C
ATOM	2145	CZ	TYR	B	84	−18.463	11.965	46.716	1.00	51.46	B	C
ATOM	2146	OH	TYR	B	84	−17.315	11.206	46.799	1.00	48.79	B	O
ATOM	2147	CE2	TYR	B	84	−18.723	12.965	47.649	1.00	48.70	B	C
ATOM	2148	CD2	TYR	B	84	−19.892	13.708	47.540	1.00	47.48	B	C
ATOM	2149	C	TYR	B	84	−22.479	14.221	48.808	1.00	58.89	B	C
ATOM	2150	O	TYR	B	84	−22.178	15.343	49.243	1.00	61.06	B	O
ATOM	2151	N	LYS	B	85	−22.298	13.081	49.465	1.00	57.68	B	N
ATOM	2152	CA	LYS	B	85	−21.894	13.027	50.851	1.00	60.94	B	C
ATOM	2153	CB	LYS	B	85	−22.559	11.835	51.556	1.00	73.10	B	C
ATOM	2154	CG	LYS	B	85	−23.450	10.931	50.661	1.00	84.97	B	C
ATOM	2155	CD	LYS	B	85	−22.697	10.288	49.455	1.00	90.64	B	C
ATOM	2156	CE	LYS	B	85	−23.613	9.395	48.601	1.00	93.15	B	C
ATOM	2157	NZ	LYS	B	85	−24.897	10.052	48.177	1.00	94.06	B	N
ATOM	2158	C	LYS	B	85	−20.391	12.897	50.924	1.00	59.56	B	C
ATOM	2159	O	LYS	B	85	−19.839	11.833	50.633	1.00	61.16	B	O
ATOM	2160	N	THR	B	86	−19.730	13.994	51.289	1.00	58.76	B	N
ATOM	2161	CA	THR	B	86	−18.303	13.977	51.629	1.00	54.81	B	C
ATOM	2162	CB	THR	B	86	−17.622	15.350	51.401	1.00	52.10	B	C
ATOM	2163	OG1	THR	B	86	−17.486	16.049	52.649	1.00	49.16	B	O
ATOM	2164	CG2	THR	B	86	−18.502	16.278	50.574	1.00	53.02	B	C
ATOM	2165	C	THR	B	86	−18.217	13.605	53.089	1.00	55.10	B	C
ATOM	2166	O	THR	B	86	−17.123	13.520	53.637	1.00	53.13	B	O
ATOM	2167	N	GLY	B	87	−19.405	13.451	53.690	1.00	57.63	B	N
ATOM	2168	CA	GLY	B	87	−19.688	12.920	55.024	1.00	58.47	B	C
ATOM	2169	C	GLY	B	87	−18.574	12.647	56.016	1.00	58.99	B	C
ATOM	2170	O	GLY	B	87	−17.429	12.406	55.627	1.00	66.01	B	O
ATOM	2171	N	PRO	B	88	−18.912	12.634	57.303	1.00	51.01	B	N
ATOM	2172	CA	PRO	B	88	−17.918	12.481	58.367	1.00	45.55	B	C
ATOM	2173	CB	PRO	B	88	−18.756	11.997	59.527	1.00	47.72	B	C
ATOM	2174	CG	PRO	B	88	−20.084	11.695	58.912	1.00	50.77	B	C
ATOM	2175	CD	PRO	B	88	−20.273	12.703	57.841	1.00	48.75	B	C
ATOM	2176	C	PRO	B	88	−16.898	11.426	57.981	1.00	44.01	B	C
ATOM	2177	O	PRO	B	88	−17.287	10.397	57.432	1.00	40.96	B	O
ATOM	2178	N	VAL	B	89	−15.622	11.696	58.249	1.00	47.96	B	N
ATOM	2179	CA	VAL	B	89	−14.507	10.857	57.790	1.00	54.42	B	C
ATOM	2180	CB	VAL	B	89	−13.786	11.555	56.641	1.00	51.16	B	C
ATOM	2181	CG1	VAL	B	89	−12.286	11.281	56.664	1.00	49.32	B	C
ATOM	2182	CG2	VAL	B	89	−14.409	11.150	55.323	1.00	53.87	B	C
ATOM	2183	C	VAL	B	89	−13.506	10.542	58.913	1.00	63.96	B	C
ATOM	2184	O	VAL	B	89	−13.316	11.368	59.808	1.00	69.59	B	O
ATOM	2185	N	LEU	B	90	−12.855	9.372	58.854	1.00	66.84	B	N
ATOM	2186	CA	LEU	B	90	−11.980	8.900	59.943	1.00	70.30	B	C
ATOM	2187	CB	LEU	B	90	−12.246	7.420	60.203	1.00	72.52	B	C
ATOM	2188	CG	LEU	B	90	−11.263	6.685	61.110	1.00	73.28	B	C
ATOM	2189	CD1	LEU	B	90	−11.986	6.110	62.309	1.00	72.75	B	C
ATOM	2190	CD2	LEU	B	90	−10.545	5.599	60.320	1.00	74.60	B	C
ATOM	2191	C	LEU	B	90	−10.459	9.144	59.791	1.00	73.50	B	C
ATOM	2192	O	LEU	B	90	−9.820	8.635	58.858	1.00	72.88	B	O
ATOM	2193	N	GLU	B	91	−9.892	9.905	60.734	1.00	77.68	B	N
ATOM	2194	CA	GLU	B	91	−8.464	10.260	60.730	1.00	83.04	B	C
ATOM	2195	CB	GLU	B	91	−8.196	11.607	61.431	1.00	83.67	B	C
ATOM	2196	CG	GLU	B	91	−9.029	12.788	60.952	1.00	87.14	B	C
ATOM	2197	CD	GLU	B	91	−8.398	13.569	59.802	1.00	90.79	B	C
ATOM	2198	OE1	GLU	B	91	−7.634	12.980	59.000	1.00	91.75	B	O
ATOM	2199	OE2	GLU	B	91	−8.683	14.786	59.690	1.00	91.43	B	O
ATOM	2200	C	GLU	B	91	−7.622	9.184	61.398	1.00	85.64	B	C
ATOM	2201	O	GLU	B	91	−8.017	8.612	62.414	1.00	83.23	B	O
ATOM	2202	N	HIS	B	92	−6.447	8.934	60.831	1.00	90.71	B	N
ATOM	2203	CA	HIS	B	92	−5.544	7.910	61.347	1.00	93.48	B	C
ATOM	2204	CB	HIS	B	92	−6.044	6.525	60.945	1.00	93.96	B	C
ATOM	2205	CG	HIS	B	92	−5.654	5.448	61.902	1.00	95.14	B	C
ATOM	2206	ND1	HIS	B	92	−4.667	4.530	61.624	1.00	95.64	B	N
ATOM	2207	CE1	HIS	B	92	−4.531	3.709	62.649	1.00	95.43	B	C
ATOM	2208	NE2	HIS	B	92	−5.392	4.066	63.584	1.00	96.05	B	N
ATOM	2209	CD2	HIS	B	92	−6.106	5.152	63.143	1.00	95.04	B	C
ATOM	2210	C	HIS	B	92	−4.102	8.100	60.865	1.00	94.62	B	C
ATOM	2211	O	HIS	B	92	−3.879	8.569	59.742	1.00	96.12	B	O
ATOM	2212	N	PRO	B	93	−3.125	7.753	61.710	1.00	93.29	B	N
ATOM	2213	CA	PRO	B	93	−1.720	7.761	61.287	1.00	92.34	B	C
ATOM	2214	CB	PRO	B	93	−0.966	7.348	62.558	1.00	91.96	B	C
ATOM	2215	CG	PRO	B	93	−1.913	7.623	63.683	1.00	91.22	B	C
ATOM	2216	CD	PRO	B	93	−3.270	7.355	63.125	1.00	91.62	B	C
ATOM	2217	C	PRO	B	93	−1.503	6.732	60.185	1.00	91.87	B	C
ATOM	2218	O	PRO	B	93	−0.830	7.029	59.194	1.00	89.55	B	O
ATOM	2219	N	ASP	B	94	−2.096	5.552	60.367	1.00	93.42	B	N
ATOM	2220	CA	ASP	B	94	−1.970	4.434	59.436	1.00	95.65	B	C
ATOM	2221	CB	ASP	B	94	−2.314	3.099	60.124	1.00	95.17	B	C
ATOM	2222	CG	ASP	B	94	−1.314	2.705	61.219	1.00	94.05	B	C
ATOM	2223	OD1	ASP	B	94	−0.971	3.553	62.073	1.00	93.69	B	O
ATOM	2224	OD2	ASP	B	94	−0.832	1.555	61.312	1.00	92.70	B	O
ATOM	2225	C	ASP	B	94	−2.840	4.620	58.190	1.00	97.92	B	C
ATOM	2226	O	ASP	B	94	−2.438	4.222	57.091	1.00	98.07	B	O
ATOM	2227	N	CYS	B	95	−4.021	5.217	58.353	1.00	100.21	B	N
ATOM	2228	CA	CYS	B	95	−4.911	5.449	57.210	1.00	103.84	B	C
ATOM	2229	CB	CYS	B	95	−6.373	5.586	57.641	1.00	104.67	B	C
ATOM	2230	SG	CYS	B	95	−7.538	5.098	56.347	1.00	106.67	B	S
ATOM	2231	C	CYS	B	95	−4.472	6.639	56.354	1.00	105.37	B	C
ATOM	2232	O	CYS	B	95	−4.582	7.798	56.769	1.00	104.25	B	O
ATOM	2233	N	PHE	B	96	−3.988	6.332	55.152	1.00	108.74	B	N
ATOM	2234	CA	PHE	B	96	−3.347	7.320	54.279	1.00	111.75	B	C
ATOM	2235	CB	PHE	B	96	−2.229	6.655	53.453	1.00	116.20	B	C
ATOM	2236	CG	PHE	B	96	−0.862	6.684	54.124	1.00	120.68	B	C
ATOM	2237	CD1	PHE	B	96	0.300	6.806	53.359	1.00	123.52	B	C
ATOM	2238	CE1	PHE	B	96	1.566	6.828	53.970	1.00	124.46	B	C
ATOM	2239	CZ	PHE	B	96	1.673	6.727	55.360	1.00	122.54	B	C
ATOM	2240	CE2	PHE	B	96	0.524	6.601	56.132	1.00	120.99	B	C
ATOM	2241	CD2	PHE	B	96	−0.734	6.577	55.514	1.00	120.92	B	C
ATOM	2242	C	PHE	B	96	−4.353	8.137	53.420	1.00	109.63	B	C
ATOM	2243	O	PHE	B	96	−5.543	7.804	53.372	1.00	110.42	B	O
ATOM	2244	N	PRO	B	97	−3.878	9.193	52.752	1.00	104.75	B	N
ATOM	2245	CA	PRO	B	97	−4.741	10.310	52.366	1.00	100.12	B	C
ATOM	2246	CB	PRO	B	97	−3.738	11.441	52.102	1.00	101.09	B	C
ATOM	2247	CG	PRO	B	97	−2.433	10.910	52.577	1.00	103.80	B	C
ATOM	2248	CD	PRO	B	97	−2.493	9.440	52.323	1.00	104.87	B	C
ATOM	2249	C	PRO	B	97	−5.700	10.152	51.179	1.00	96.19	B	C
ATOM	2250	O	PRO	B	97	−6.636	10.957	51.112	1.00	100.40	B	O
ATOM	2251	N	CYS	B	98	−5.520	9.208	50.266	1.00	87.61	B	N
ATOM	2252	CA	CYS	B	98	−6.560	9.081	49.241	1.00	84.10	B	C
ATOM	2253	CB	CYS	B	98	−6.045	9.392	47.830	1.00	80.73	B	C
ATOM	2254	SG	CYS	B	98	−6.621	10.975	47.108	1.00	71.77	B	S
ATOM	2255	C	CYS	B	98	−7.287	7.753	49.302	1.00	87.62	B	C
ATOM	2256	O	CYS	B	98	−8.265	7.540	48.576	1.00	85.32	B	O
ATOM	2257	N	GLN	B	99	−6.812	6.876	50.187	1.00	95.06	B	N
ATOM	2258	CA	GLN	B	99	−7.485	5.607	50.489	1.00	99.82	B	C
ATOM	2259	CB	GLN	B	99	−6.482	4.452	50.640	1.00	101.05	B	C
ATOM	2260	CG	GLN	B	99	−5.259	4.753	51.502	1.00	103.61	B	C
ATOM	2261	CD	GLN	B	99	−4.905	3.601	52.425	1.00	105.79	B	C
ATOM	2262	OE1	GLN	B	99	−5.161	3.659	53.631	1.00	104.51	B	O
ATOM	2263	NE2	GLN	B	99	−4.322	2.546	51.860	1.00	107.30	B	N
ATOM	2264	C	GLN	B	99	−8.364	5.743	51.730	1.00	101.30	B	C
ATOM	2265	O	GLN	B	99	−7.971	6.381	52.711	1.00	97.88	B	O
ATOM	2266	N	ASP	B	100	−9.560	5.158	51.669	1.00	107.39	B	N
ATOM	2267	CA	ASP	B	100	−10.548	5.309	52.745	1.00	114.11	B	C
ATOM	2268	CB	ASP	B	100	−11.900	5.864	52.210	1.00	121.61	B	C
ATOM	2269	CG	ASP	B	100	−12.948	4.773	51.925	1.00	126.01	B	C
ATOM	2270	OD1	ASP	B	100	−13.378	4.662	50.752	1.00	127.43	B	O
ATOM	2271	OD2	ASP	B	100	−13.428	4.013	52.803	1.00	126.52	B	O
ATOM	2272	C	ASP	B	100	−10.695	4.054	53.609	1.00	110.78	B	C
ATOM	2273	O	ASP	B	100	−10.300	2.963	53.201	1.00	110.09	B	O
ATOM	2274	N	CYS	B	101	−11.256	4.214	54.804	1.00	109.34	B	N
ATOM	2275	CA	CYS	B	101	−11.262	3.124	55.771	1.00	110.92	B	C
ATOM	2276	CB	CYS	B	101	−9.951	3.117	56.568	1.00	109.38	B	C
ATOM	2277	SG	CYS	B	101	−9.389	4.750	57.104	1.00	107.17	B	S
ATOM	2278	C	CYS	B	101	−12.452	3.054	56.735	1.00	113.41	B	C
ATOM	2279	O	CYS	B	101	−12.663	3.945	57.567	1.00	111.59	B	O
ATOM	2280	N	SER	B	102	−13.234	1.987	56.579	1.00	116.32	B	N
ATOM	2281	CA	SER	B	102	−13.985	1.389	57.683	1.00	116.98	B	C
ATOM	2282	CB	SER	B	102	−15.427	1.033	57.284	1.00	119.06	B	C
ATOM	2283	OG	SER	B	102	−15.554	0.767	55.894	1.00	121.46	B	O
ATOM	2284	C	SER	B	102	−13.181	0.145	58.076	1.00	114.30	B	C
ATOM	2285	O	SER	B	102	−13.592	−0.653	58.925	1.00	112.54	B	O
ATOM	2286	N	SER	B	103	−12.020	0.015	57.429	1.00	112.80	B	N
ATOM	2287	CA	SER	B	103	−11.023	−1.010	57.723	1.00	112.40	B	C
ATOM	2288	CB	SER	B	103	−10.246	−1.382	56.446	1.00	113.52	B	C
ATOM	2289	OG	SER	B	103	−8.915	−0.889	56.457	1.00	113.78	B	O
ATOM	2290	C	SER	B	103	−10.080	−0.556	58.847	1.00	110.28	B	C
ATOM	2291	O	SER	B	103	−8.990	−1.112	59.025	1.00	110.84	B	O
ATOM	2292	N	LYS	B	104	−10.510	0.469	59.583	1.00	107.08	B	N
ATOM	2293	CA	LYS	B	104	−9.869	0.886	60.832	1.00	104.77	B	C
ATOM	2294	CB	LYS	B	104	−8.674	1.814	60.569	1.00	102.55	B	C
ATOM	2295	CG	LYS	B	104	−7.350	1.277	61.118	1.00	102.04	B	C
ATOM	2296	CD	LYS	B	104	−7.255	1.436	62.647	1.00	102.16	B	C
ATOM	2297	CE	LYS	B	104	−7.226	0.095	63.414	1.00	97.37	B	C
ATOM	2298	NZ	LYS	B	104	−7.273	0.328	64.885	1.00	90.84	B	N
ATOM	2299	C	LYS	B	104	−10.873	1.536	61.796	1.00	103.99	B	C
ATOM	2300	O	LYS	B	104	−10.492	2.078	62.840	1.00	102.61	B	O
ATOM	2301	N	ALA	B	105	−12.157	1.443	61.446	1.00	104.09	B	N
ATOM	2302	CA	ALA	B	105	−13.239	2.100	62.181	1.00	104.10	B	C
ATOM	2303	CB	ALA	B	105	−14.590	1.774	61.543	1.00	101.87	B	C
ATOM	2304	C	ALA	B	105	−13.252	1.768	63.673	1.00	106.64	B	C
ATOM	2305	O	ALA	B	105	−13.732	2.566	64.484	1.00	105.54	B	O
ATOM	2306	N	ASN	B	106	−12.711	0.598	64.020	1.00	110.83	B	N
ATOM	2307	CA	ASN	B	106	−12.686	0.104	65.402	1.00	112.90	B	C
ATOM	2308	CB	ASN	B	106	−12.560	−1.419	65.419	1.00	112.61	B	C
ATOM	2309	CG	ASN	B	106	−13.662	−2.099	64.628	1.00	112.48	B	C
ATOM	2310	OD1	ASN	B	106	−14.782	−2.268	65.117	1.00	112.22	B	O
ATOM	2311	ND2	ASN	B	106	−13.353	−2.476	63.391	1.00	111.53	B	N
ATOM	2312	C	ASN	B	106	−11.624	0.767	66.287	1.00	114.33	B	C
ATOM	2313	O	ASN	B	106	−11.708	0.697	67.516	1.00	112.37	B	O
ATOM	2314	N	LEU	B	107	−10.638	1.397	65.638	1.00	116.71	B	N
ATOM	2315	CA	LEU	B	107	−9.740	2.421	66.219	1.00	117.65	B	C
ATOM	2316	CB	LEU	B	107	−10.501	3.735	66.558	1.00	118.18	B	C
ATOM	2317	CG	LEU	B	107	−11.825	3.803	67.349	1.00	117.62	B	C
ATOM	2318	CD1	LEU	B	107	−11.611	3.881	68.860	1.00	116.54	B	C
ATOM	2319	CD2	LEU	B	107	−12.698	4.964	66.876	1.00	116.79	B	C
ATOM	2320	C	LEU	B	107	−8.830	2.026	67.386	1.00	117.14	B	C
ATOM	2321	O	LEU	B	107	−9.295	1.490	68.392	1.00	118.13	B	O
ATOM	2322	N	SER	B	108	−7.532	2.304	67.243	1.00	116.38	B	N
ATOM	2323	CA	SER	B	108	−6.592	2.207	68.368	1.00	117.71	B	C
ATOM	2324	CB	SER	B	108	−5.433	1.245	68.066	1.00	118.45	B	C
ATOM	2325	OG	SER	B	108	−5.151	0.407	69.185	1.00	114.88	B	O
ATOM	2326	C	SER	B	108	−6.067	3.590	68.752	1.00	116.80	B	C
ATOM	2327	O	SER	B	108	−5.739	3.847	69.916	1.00	116.90	B	O
ATOM	2328	N	GLY	B	109	−5.991	4.470	67.757	1.00	115.23	B	N
ATOM	2329	CA	GLY	B	109	−5.668	5.870	67.965	1.00	114.60	B	C
ATOM	2330	C	GLY	B	109	−6.196	6.711	66.816	1.00	113.83	B	C
ATOM	2331	O	GLY	B	109	−5.471	7.544	66.262	1.00	115.22	B	O
ATOM	2332	N	GLY	B	110	−7.460	6.487	66.456	1.00	110.69	B	N
ATOM	2333	CA	GLY	B	110	−8.067	7.131	65.304	1.00	106.40	B	C
ATOM	2334	C	GLY	B	110	−9.356	7.848	65.640	1.00	103.85	B	C
ATOM	2335	O	GLY	B	110	−10.210	7.297	66.340	1.00	105.05	B	O
ATOM	2336	N	VAL	B		111	−9.495	9.074	65.135	1.00	99.89	B	N
ATOM	2337	CA	VAL	B	111	−10.651	9.922	65.442	1.00	97.25	B	C
ATOM	2338	CB	VAL	B	111	−10.219	11.257	66.141	1.00	97.47	B	C
ATOM	2339	CG1	VAL	B	111	−9.412	12.155	65.206	1.00	97.24	B	C
ATOM	2340	CG2	VAL	B	111	−11.424	12.001	66.734	1.00	97.90	B	C
ATOM	2341	C	VAL	B	111	−11.551	10.183	64.225	1.00	95.04	B	C
ATOM	2342	O	VAL	B	111	−11.072	10.317	63.102	1.00	96.37	B	O
ATOM	2343	N	TRP	B	112	−12.859	10.229	64.468	1.00	92.55	B	N
ATOM	2344	CA	TRP	B	112	−13.851	10.530	63.442	1.00	90.06	B	C
ATOM	2345	CB	TRP	B	112	−15.193	9.946	63.862	1.00	100.15	B	C
ATOM	2346	CG	TRP	B	112	−15.775	8.890	62.958	1.00	108.23	B	C
ATOM	2347	CD1	TRP	B	112	−15.115	8.104	62.042	1.00	107.69	B	C
ATOM	2348	NE1	TRP	B	112	−16.002	7.257	61.419	1.00	109.43	B	N
ATOM	2349	CE2	TRP	B	112	−17.260	7.476	61.926	1.00	114.91	B	C
ATOM	2350	CD2	TRP	B	112	−17.152	8.497	62.901	1.00	113.79	B	C
ATOM	2351	CE3	TRP	B	112	−18.319	8.912	63.578	1.00	114.66	B	C
ATOM	2352	CZ3	TRP	B	112	−19.538	8.306	63.268	1.00	115.28	B	C
ATOM	2353	CH2	TRP	B	112	−19.612	7.294	62.295	1.00	117.95	B	C
ATOM	2354	CZ2	TRP	B	112	−18.488	6.865	61.612	1.00	118.19	B	C
ATOM	2355	C	TRP	B	112	−13.964	12.047	63.285	1.00	80.41	B	C
ATOM	2356	O	TRP	B	112	−14.092	12.772	64.274	1.00	77.18	B	O
ATOM	2357	N	LYS	B	113	−13.921	12.525	62.044	1.00	72.68	B	N
ATOM	2358	CA	LYS	B	113	−13.757	13.959	61.785	1.00	65.54	B	C
ATOM	2359	CB	LYS	B	113	−12.296	14.273	61.423	1.00	64.56	B	C
ATOM	2360	CG	LYS	B	113	−11.738	15.565	62.025	1.00	66.31	B	C
ATOM	2361	CD	LYS	B	113	−11.284	15.412	63.479	1.00	70.15	B	C
ATOM	2362	CE	LYS	B	113	−11.922	16.489	64.389	1.00	73.85	B	C
ATOM	2363	NZ	LYS	B	113	−12.001	16.101	65.850	1.00	72.65	B	N
ATOM	2364	C	LYS	B	113	−14.731	14.574	60.761	1.00	59.44	B	C
ATOM	2365	O	LYS	B	113	−15.106	13.949	59.763	1.00	52.74	B	O
ATOM	2366	N	ASP	B	114	−15.139	15.807	61.055	1.00	56.80	B	N
ATOM	2367	CA	ASP	B	114	−16.058	16.573	60.230	1.00	52.56	B	C
ATOM	2368	CB	ASP	B	114	−16.678	17.707	61.046	1.00	55.24	B	C
ATOM	2369	CG	ASP	B	114	−18.062	17.386	61.523	1.00	55.57	B	C
ATOM	2370	OD1	ASP	B	114	−18.499	16.231	61.321	1.00	56.68	B	O
ATOM	2371	OD2	ASP	B	114	−18.779	18.228	62.111	1.00	54.42	B	O
ATOM	2372	C	ASP	B	114	−15.306	17.169	59.068	1.00	47.86	B	C
ATOM	2373	O	ASP	B	114	−14.254	17.788	59.250	1.00	46.73	B	O
ATOM	2374	N	ASN	B	115	−15.873	17.001	57.880	1.00	44.76	B	N
ATOM	2375	CA	ASN	B	115	−15.207	17.356	56.639	1.00	42.15	B	C
ATOM	2376	CB	ASN	B	115	−15.489	16.275	55.585	1.00	41.27	B	C
ATOM	2377	CG	ASN	B	115	−14.563	16.362	54.379	1.00	40.72	B	C
ATOM	2378	OD1	ASN	B	115	−13.708	17.245	54.284	1.00	41.54	B	O
ATOM	2379	ND2	ASN	B	115	−14.746	15.444	53.440	1.00	38.72	B	N
ATOM	2380	C	ASN	B	115	−15.596	18.735	56.118	1.00	40.63	B	C
ATOM	2381	O	ASN	B	115	−16.400	18.841	55.172	1.00	43.96	B	O
ATOM	2382	N	ILE	B	116	−15.020	19.784	56.711	1.00	36.29	B	N
ATOM	2383	CA	ILE	B	116	−15.301	21.157	56.255	1.00	42.57	B	C
ATOM	2384	CB	ILE	B	116	−14.724	22.206	57.236	1.00	41.18	B	C
ATOM	2385	CG1	ILE	B	116	−15.416	22.117	58.577	1.00	42.73	B	C
ATOM	2386	CD1	ILE	B	116	−14.515	21.560	59.639	1.00	52.68	B	C
ATOM	2387	CG2	ILE	B	116	−14.927	23.600	56.719	1.00	39.91	B	C
ATOM	2388	C	ILE	B	116	−14.817	21.430	54.810	1.00	41.86	B	C
ATOM	2389	O	ILE	B	116	−13.661	21.185	54.479	1.00	40.94	B	O
ATOM	2390	N	ASN	B	117	−15.711	21.918	53.955	1.00	41.50	B	N
ATOM	2391	CA	ASN	B	117	−15.304	22.323	52.622	1.00	44.19	B	C
ATOM	2392	CB	ASN	B	117	−16.480	22.617	51.715	1.00	46.40	B	C
ATOM	2393	CG	ASN	B	117	−16.035	22.856	50.298	1.00	50.38	B	C
ATOM	2394	OD1	ASN	B	117	−16.001	23.987	49.810	1.00	49.26	B	O
ATOM	2395	ND2	ASN	B	117	−15.632	21.778	49.635	1.00	57.83	B	N
ATOM	2396	C	ASN	B	117	−14.459	23.565	52.660	1.00	46.47	B	C
ATOM	2397	O	ASN	B	117	−14.845	24.573	53.239	1.00	54.75	B	O
ATOM	2398	N	MET	B	118	−13.315	23.510	52.006	1.00	43.70	B	N
ATOM	2399	CA	MET	B	118	−12.406	24.633	52.022	1.00	39.66	B	C
ATOM	2400	CB	MET	B	118	−11.039	24.186	52.479	1.00	31.69	B	C
ATOM	2401	CG	MET	B	118	−11.139	23.407	53.748	1.00	33.38	B	C
ATOM	2402	SD	MET	B	118	−10.931	24.407	55.204	1.00	31.79	B	S
ATOM	2403	CE	MET	B	118	−12.315	25.652	55.009	1.00	44.44	B	C
ATOM	2404	C	MET	B	118	−12.332	25.294	50.682	1.00	42.98	B	C
ATOM	2405	O	MET	B	118	−12.171	26.508	50.598	1.00	55.86	B	O
ATOM	2406	N	ALA	B	119	−12.468	24.509	49.629	1.00	35.90	B	N
ATOM	2407	CA	ALA	B	119	−12.353	25.057	48.304	1.00	37.59	B	C
ATOM	2408	CB	ALA	B	119	−10.947	24.869	47.801	1.00	37.93	B	C
ATOM	2409	C	ALA	B	119	−13.355	24.379	47.394	1.00	41.21	B	C
ATOM	2410	O	ALA	B	119	−13.808	23.271	47.675	1.00	44.45	B	O
ATOM	2411	N	LEU	B		120	−13.705	25.052	46.305	1.00	40.87	B	N
ATOM	2412	CA	LEU	B	120	−14.646	24.504	45.343	1.00	38.31	B	C
ATOM	2413	CB	LEU	B	120	−16.065	24.657	45.876	1.00	35.61	B	C
ATOM	2414	CG	LEU	B		120	−17.214	23.947	45.194	1.00	34.31	B	C
ATOM	2415	CD1	LEU	B	120	−16.986	22.455	45.139	1.00	36.68	B	C
ATOM	2416	CD2	LEU	B	120	−18.456	24.243	45.994	1.00	37.88	B	C
ATOM	2417	C	LEU	B	120	−14.456	25.243	44.041	1.00	39.32	B	C
ATOM	2418	O	LEU	B		120	−14.624	26.448	43.994	1.00	46.51	B	O
ATOM	2419	N	VAL	B	121	−14.057	24.512	43.005	1.00	40.71	B	N
ATOM	2420	CA	VAL	B	121	−13.658	25.055	41.703	1.00	38.95	B	C
ATOM	2421	CB	VAL	B	121	−12.125	24.890	41.486	1.00	38.21	B	C
ATOM	2422	CG1	VAL	B	121	−11.725	25.174	40.048	1.00	44.46	B	C
ATOM	2423	CG2	VAL	B	121	−11.353	25.784	42.382	1.00	37.18	B	C
ATOM	2424	C	VAL	B	121	−14.325	24.201	40.635	1.00	41.66	B	C
ATOM	2425	O	VAL	B	121	−14.182	22.971	40.636	1.00	43.10	B	O
ATOM	2426	N	VAL	B	122	−15.055	24.838	39.726	1.00	43.07	B	N
ATOM	2427	CA	VAL	B	122	−15.458	24.156	38.494	1.00	41.96	B	C
ATOM	2428	CB	VAL	B	122	−16.767	24.713	37.940	1.00	35.78	B	C
ATOM	2429	CG1	VAL	B	122	−16.605	25.113	36.525	1.00	34.77	B	C
ATOM	2430	CG2	VAL	B	122	−17.808	23.676	38.003	1.00	38.83	B	C
ATOM	2431	C	VAL	B	122	−14.333	24.362	37.489	1.00	43.26	B	C
ATOM	2432	O	VAL	B	122	−13.808	25.467	37.391	1.00	46.50	B	O
ATOM	2433	N	ASP	B	123	−13.928	23.308	36.785	1.00	44.35	B	N
ATOM	2434	CA	ASP	B	123	−12.900	23.451	35.752	1.00	51.92	B	C
ATOM	2435	CB	ASP	B	123	−11.695	22.544	35.963	1.00	61.96	B	C
ATOM	2436	CG	ASP	B	123	−11.083	22.086	34.628	1.00	64.45	B	C
ATOM	2437	OD1	ASP	B	123	−10.597	22.975	33.879	1.00	65.02	B	O
ATOM	2438	OD2	ASP	B	123	−11.090	20.887	34.242	1.00	61.38	B	O
ATOM	2439	C	ASP	B	123	−13.475	23.038	34.451	1.00	48.41	B	C
ATOM	2440	O	ASP	B	123	−14.202	22.060	34.379	1.00	53.22	B	O
ATOM	2441	N	THR	B	124	−13.080	23.730	33.400	1.00	47.40	B	N
ATOM	2442	CA	THR	B	124	−13.768	23.538	32.145	1.00	47.40	B	C
ATOM	2443	CB	THR	B	124	−14.883	24.554	32.038	1.00	43.24	B	C
ATOM	2444	OG1	THR	B	124	−16.097	23.823	31.851	1.00	47.08	B	O
ATOM	2445	CG2	THR	B	124	−14.727	25.442	30.816	1.00	37.20	B	C
ATOM	2446	C	THR	B	124	−12.882	23.507	30.928	1.00	49.31	B	C
ATOM	2447	O	THR	B	124	−13.375	23.395	29.813	1.00	52.93	B	O
ATOM	2448	N	TYR	B	125	−11.581	23.627	31.179	1.00	50.42	B	N
ATOM	2449	CA	TYR	B	125	−10.528	23.488	30.195	1.00	45.77	B	C
ATOM	2450	CB	TYR	B	125	−9.194	23.956	30.785	1.00	44.67	B	C
ATOM	2451	CG	TYR	B	125	−8.074	23.995	29.795	1.00	42.53	B	C
ATOM	2452	CD1	TYR	B	125	−8.168	24.795	28.667	1.00	44.26	B	C
ATOM	2453	CE1	TYR	B	125	−7.156	24.853	27.726	1.00	46.25	B	C
ATOM	2454	CZ	TYR	B	125	−6.021	24.100	27.902	1.00	50.62	B	C
ATOM	2455	OH	TYR	B	125	−5.040	24.192	26.926	1.00	57.46	B	O
ATOM	2456	CE2	TYR	B	125	−5.888	23.281	29.033	1.00	45.35	B	C
ATOM	2457	CD2	TYR	B	125	−6.925	23.234	29.972	1.00	41.33	B	C
ATOM	2458	C	TYR	B	125	−10.466	22.011	29.883	1.00	47.99	B	C
ATOM	2459	O	TYR	B	125	−10.520	21.620	28.719	1.00	55.63	B	O
ATOM	2460	N	TYR	B	126	−10.382	21.179	30.915	1.00	42.77	B	N
ATOM	2461	CA	TYR	B	126	−10.505	19.748	30.689	1.00	48.14	B	C
ATOM	2462	CB	TYR	B	126	−9.865	18.943	31.822	1.00	45.89	B	C
ATOM	2463	CG	TYR	B	126	−8.368	19.056	31.814	1.00	41.38	B	C
ATOM	2464	CD1	TYR	B	126	−7.611	18.680	32.893	1.00	34.20	B	C
ATOM	2465	CE1	TYR	B	126	−6.248	18.811	32.863	1.00	33.38	B	C
ATOM	2466	CZ	TYR	B	126	−5.642	19.304	31.750	1.00	37.54	B	C
ATOM	2467	OH	TYR	B	126	−4.290	19.467	31.673	1.00	48.33	B	O
ATOM	2468	CE2	TYR	B	126	−6.370	19.683	30.674	1.00	41.80	B	C
ATOM	2469	CD2	TYR	B	126	−7.714	19.567	30.707	1.00	44.40	B	C
ATOM	2470	C	TYR	B	126	−11.975	19.453	30.563	1.00	56.46	B	C
ATOM	2471	O	TYR	B	126	−12.779	20.380	30.560	1.00	64.10	B	O
ATOM	2472	N	ASP	B	127	−12.335	18.178	30.449	1.00	59.78	B	N
ATOM	2473	CA	ASP	B	127	−13.740	17.787	30.427	1.00	57.64	B	C
ATOM	2474	CB	ASP	B	127	−13.866	16.284	30.170	1.00	66.23	B	C
ATOM	2475	CG	ASP	B	127	−13.341	15.897	28.785	1.00	73.41	B	C
ATOM	2476	OD1	ASP	B	127	−14.141	15.903	27.817	1.00	72.62	B	O
ATOM	2477	OD2	ASP	B	127	−12.132	15.624	28.564	1.00	78.10	B	O
ATOM	2478	C	ASP	B	127	−14.364	18.224	31.739	1.00	50.09	B	C
ATOM	2479	O	ASP	B	127	−13.779	17.969	32.791	1.00	44.38	B	O
ATOM	2480	N	ASP	B	128	−15.511	18.920	31.639	1.00	50.03	B	N
ATOM	2481	CA	ASP	B	128	−16.159	19.689	32.725	1.00	46.93	B	C
ATOM	2482	CB	ASP	B	128	−17.615	20.032	32.395	1.00	57.55	B	C
ATOM	2483	CG	ASP	B	128	−17.778	20.854	31.128	1.00	66.78	B	C
ATOM	2484	OD1	ASP	B	128	−18.857	21.478	30.984	1.00	66.39	B	O
ATOM	2485	OD2	ASP	B	128	−16.917	20.927	30.218	1.00	75.20	B	O
ATOM	2486	C	ASP	B	128	−16.195	18.882	33.980	1.00	41.66	B	C
ATOM	2487	O	ASP	B	128	−16.663	17.741	33.967	1.00	47.23	B	O
ATOM	2488	N	GLN	B	129	−15.700	19.463	35.060	1.00	35.06	B	N
ATOM	2489	CA	GLN	B	129	−15.570	18.743	36.314	1.00	40.83	B	C
ATOM	2490	CB	GLN	B	129	−14.255	17.965	36.389	1.00	42.79	B	C
ATOM	2491	CG	GLN	B	129	−13.027	18.697	35.836	1.00	52.65	B	C
ATOM	2492	CD	GLN	B	129	−11.706	17.927	36.035	1.00	58.28	B	C
ATOM	2493	OE1	GLN	B	129	−10.651	18.548	36.212	1.00	56.96	B	O
ATOM	2494	NE2	GLN	B	129	−11.762	16.584	35.993	1.00	58.06	B	N
ATOM	2495	C	GLN	B	129	−15.664	19.675	37.495	1.00	45.17	B	C
ATOM	2496	O	GLN	B	129	−15.241	20.824	37.420	1.00	51.51	B	O
ATOM	2497	N	LEU	B	130	−16.241	19.183	38.581	1.00	43.79	B	N
ATOM	2498	CA	LEU	B	130	−16.167	19.872	39.845	1.00	43.88	B	C
ATOM	2499	CB	LEU	B	130	−17.454	19.661	40.627	1.00	42.37	B	C
ATOM	2500	CG	LEU	B		130	−17.573	20.644	41.785	1.00	43.44	B	C
ATOM	2501	CD1	LEU	B	130	−17.291	22.057	41.272	1.00	43.17	B	C
ATOM	2502	CD2	LEU	B	130	−18.938	20.554	42.438	1.00	40.31	B	C
ATOM	2503	C	LEU	B	130	−14.958	19.369	40.650	1.00	47.73	B	C
ATOM	2504	O	LEU	B	130	−14.846	18.181	40.939	1.00	54.37	B	O
ATOM	2505	N	ILE	B	131	−14.058	20.278	41.006	1.00	42.98	B	N
ATOM	2506	CA	ILE	B	131	−12.927	19.958	41.863	1.00	37.29	B	C
ATOM	2507	CB	ILE	B	131	−11.652	20.609	41.290	1.00	33.48	B	C
ATOM	2508	CG1	ILE	B	131	−11.204	19.859	40.043	1.00	36.20	B	C
ATOM	2509	CD1	ILE	B	131	−10.173	20.596	39.219	1.00	35.22	B	C
ATOM	2510	CG2	ILE	B	131	−10.527	20.572	42.282	1.00	31.94	B	C
ATOM	2511	C	ILE	B	131	−13.250	20.511	43.247	1.00	38.31	B	C
ATOM	2512	O	ILE	B	131	−13.578	21.683	43.371	1.00	42.71	B	O
ATOM	2513	N	SER	B	132	−13.178	19.687	44.285	1.00	35.31	B	N
ATOM	2514	CA	SER	B	132	−13.474	20.173	45.634	1.00	36.79	B	C
ATOM	2515	CB	SER	B	132	−14.862	19.710	46.084	1.00	36.06	B	C
ATOM	2516	OG	SER	B	132	−14.900	18.309	46.322	1.00	35.94	B	O
ATOM	2517	C	SER	B	132	−12.426	19.735	46.643	1.00	43.95	B	C
ATOM	2518	O	SER	B	132	−11.915	18.609	46.584	1.00	51.56	B	O
ATOM	2519	N	CYS	B	133	−12.122	20.604	47.595	1.00	42.29	B	N
ATOM	2520	CA	CYS	B	133	−11.007	20.333	48.478	1.00	43.14	B	C
ATOM	2521	CB	CYS	B	133	−9.878	21.294	48.169	1.00	46.61	B	C
ATOM	2522	SG	CYS	B	133	−9.498	21.339	46.411	1.00	49.26	B	S
ATOM	2523	C	CYS	B	133	−11.407	20.486	49.903	1.00	45.17	B	C
ATOM	2524	O	CYS	B	133	−11.608	21.596	50.371	1.00	48.43	B	O
ATOM	2525	N	GLY	B	134	−11.493	19.356	50.595	1.00	50.96	B	N
ATOM	2526	CA	GLY	B	134	−11.880	19.303	52.002	1.00	47.23	B	C
ATOM	2527	C	GLY	B	134	−10.753	19.528	52.986	1.00	39.00	B	C
ATOM	2528	O	GLY	B	134	−9.589	19.518	52.619	1.00	40.38	B	O
ATOM	2529	N	SER	B	135	−11.111	19.714	54.247	1.00	34.97	B	N
ATOM	2530	CA	SER	B	135	−10.146	20.011	55.299	1.00	40.38	B	C
ATOM	2531	CB	SER	B	135	−10.912	20.575	56.468	1.00	41.02	B	C
ATOM	2532	OG	SER	B	135	−11.915	19.643	56.838	1.00	43.62	B	O
ATOM	2533	C	SER	B	135	−9.425	18.783	55.840	1.00	48.34	B	C
ATOM	2534	O	SER	B	135	−8.572	18.894	56.711	1.00	55.69	B	O
ATOM	2535	N	VAL	B	136	−9.765	17.609	55.344	1.00	49.73	B	N
ATOM	2536	CA	VAL	B	136	−9.730	16.472	56.224	1.00	47.33	B	C
ATOM	2537	CB	VAL	B	136	−11.157	15.856	56.374	1.00	38.19	B	C
ATOM	2538	CG1	VAL	B	136	−11.435	14.768	55.351	1.00	32.38	B	C
ATOM	2539	CG2	VAL	B	136	−11.380	15.387	57.789	1.00	39.28	B	C
ATOM	2540	C	VAL	B	136	−8.586	15.485	55.993	1.00	58.89	B	C
ATOM	2541	O	VAL	B	136	−7.891	15.100	56.950	1.00	66.03	B	O
ATOM	2542	N	ASN	B	137	−8.351	15.083	54.752	1.00	63.66	B	N
ATOM	2543	CA	ASN	B	137	−7.286	14.102	54.531	1.00	66.38	B	C
ATOM	2544	CB	ASN	B	137	−7.739	12.971	53.616	1.00	70.31	B	C
ATOM	2545	CG	ASN	B	137	−8.170	11.750	54.398	1.00	74.06	B	C
ATOM	2546	OD1	ASN	B	137	−7.363	11.122	55.102	1.00	74.99	B	O
ATOM	2547	ND2	ASN	B	137	−9.450	11.411	54.295	1.00	75.95	B	N
ATOM	2548	C	ASN	B	137	−5.985	14.742	54.085	1.00	64.84	B	C
ATOM	2549	O	ASN	B	137	−5.452	14.451	53.019	1.00	62.52	B	O
ATOM	2550	N	ARG	B	138	−5.486	15.607	54.961	1.00	66.90	B	N
ATOM	2551	CA	ARG	B	138	−4.336	16.464	54.717	1.00	65.01	B	C
ATOM	2552	CB	ARG	B	138	−3.047	15.654	54.503	1.00	71.48	B	C
ATOM	2553	CG	ARG	B	138	−1.956	15.954	55.529	1.00	79.03	B	C
ATOM	2554	CD	ARG	B	138	−1.753	17.448	55.823	1.00	85.21	B	C
ATOM	2555	NE	ARG	B	138	−1.583	17.732	57.252	1.00	90.48	B	N
ATOM	2556	CZ	ARG	B	138	−2.579	17.968	58.109	1.00	92.99	B	C
ATOM	2557	NH1	ARG	B	138	−3.844	17.956	57.701	1.00	92.99	B	N
ATOM	2558	NH2	ARG	B	138	−2.306	18.218	59.387	1.00	94.36	B	N
ATOM	2559	C	ARG	B	138	−4.580	17.428	53.580	1.00	58.68	B	C
ATOM	2560	O	ARG	B	138	−3.652	17.754	52.855	1.00	57.43	B	O
ATOM	2561	N	GLY	B	139	−5.827	17.881	53.436	1.00	56.99	B	N
ATOM	2562	CA	GLY	B	139	−6.186	18.869	52.419	1.00	60.31	B	C
ATOM	2563	C	GLY	B	139	−6.125	18.413	50.959	1.00	56.23	B	C
ATOM	2564	O	GLY	B	139	−5.474	19.025	50.107	1.00	53.01	B	O
ATOM	2565	N	THR	B	140	−6.892	17.374	50.677	1.00	51.49	B	N
ATOM	2566	CA	THR	B	140	−6.708	16.542	49.523	1.00	44.96	B	C
ATOM	2567	CB	THR	B	140	−6.359	15.144	50.079	1.00	40.88	B	C
ATOM	2568	OG1	THR	B	140	−5.543	14.445	49.159	1.00	42.11	B	O
ATOM	2569	CG2	THR	B	140	−7.570	14.236	50.258	1.00	39.68	B	C
ATOM	2570	C	THR	B	140	−7.969	16.581	48.635	1.00	49.45	B	C
ATOM	2571	O	THR	B	140	−9.023	16.049	49.005	1.00	52.07	B	O
ATOM	2572	N	CYS	B	141	−7.860	17.234	47.475	1.00	51.13	B	N
ATOM	2573	CA	CYS	B	141	−9.010	17.478	46.577	1.00	50.29	B	C
ATOM	2574	CB	CYS	B	141	−8.664	18.515	45.512	1.00	47.76	B	C
ATOM	2575	SG	CYS	B	141	−7.972	20.064	46.098	1.00	47.46	B	S
ATOM	2576	C	CYS	B	141	−9.505	16.256	45.814	1.00	49.65	B	C
ATOM	2577	O	CYS	B	141	−8.722	15.377	45.478	1.00	54.28	B	O
ATOM	2578	N	GLN	B	142	−10.796	16.226	45.508	1.00	44.81	B	N
ATOM	2579	CA	GLN	B	142	−11.312	15.252	44.556	1.00	45.82	B	C
ATOM	2580	CB	GLN	B	142	−12.224	14.230	45.229	1.00	50.74	B	C
ATOM	2581	CG	GLN	B	142	−13.118	14.773	46.300	1.00	61.11	B	C
ATOM	2582	CD	GLN	B	142	−13.706	13.667	47.164	1.00	69.68	B	C
ATOM	2583	OE1	GLN	B	142	−14.920	13.650	47.414	1.00	73.98	B	O
ATOM	2584	NE2	GLN	B	142	−12.852	12.745	47.629	1.00	69.82	B	N
ATOM	2585	C	GLN	B	142	−12.032	15.898	43.371	1.00	45.42	B	C
ATOM	2586	O	GLN	B	142	−12.597	16.996	43.491	1.00	46.11	B	O
ATOM	2587	N	ARG	B	143	−12.007	15.216	42.227	1.00	40.44	B	N
ATOM	2588	CA	ARG	B	143	−12.773	15.673	41.079	1.00	42.36	B	C
ATOM	2589	CB	ARG	B	143	−11.916	15.712	39.821	1.00	43.64	B	C
ATOM	2590	CG	ARG	B	143	−10.693	14.855	39.870	1.00	46.96	B	C
ATOM	2591	CD	ARG	B	143	−9.746	15.107	38.695	1.00	52.05	B	C
ATOM	2592	NE	ARG	B	143	−10.263	14.581	37.430	1.00	53.03	B	N
ATOM	2593	CZ	ARG	B	143	−10.090	13.331	37.013	1.00	52.65	B	C
ATOM	2594	NH1	ARG	B	143	−9.405	12.456	37.758	1.00	50.91	B	N
ATOM	2595	NH2	ARG	B	143	−10.612	12.954	35.852	1.00	53.00	B	N
ATOM	2596	C	ARG	B	143	−14.063	14.872	40.836	1.00	42.84	B	C
ATOM	2597	O	ARG	B	143	−14.048	13.656	40.824	1.00	46.36	B	O
ATOM	2598	N	HIS	B	144	−15.175	15.575	40.664	1.00	37.53	B	N
ATOM	2599	CA	HIS	B	144	−16.422	14.988	40.232	1.00	35.23	B	C
ATOM	2600	CB	HIS	B	144	−17.549	15.616	41.028	1.00	37.05	B	C
ATOM	2601	CG	HIS	B	144	−17.291	15.651	42.499	1.00	43.08	B	C
ATOM	2602	ND1	HIS	B	144	−17.933	14.811	43.390	1.00	45.29	B	N
ATOM	2603	CE1	HIS	B	144	−17.513	15.068	44.617	1.00	44.50	B	C
ATOM	2604	NE2	HIS	B	144	−16.616	16.037	44.554	1.00	45.75	B	N
ATOM	2605	CD2	HIS	B	144	−16.460	16.421	43.240	1.00	43.81	B	C
ATOM	2606	C	HIS	B	144	−16.598	15.311	38.753	1.00	37.70	B	C
ATOM	2607	O	HIS	B	144	−16.655	16.476	38.387	1.00	43.32	B	O
ATOM	2608	N	VAL	B	145	−16.678	14.301	37.893	1.00	36.97	B	N
ATOM	2609	CA	VAL	B	145	−16.786	14.561	36.457	1.00	36.81	B	C
ATOM	2610	CB	VAL	B	145	−15.956	13.579	35.611	1.00	34.75	B	C
ATOM	2611	CG1	VAL	B	145	−15.910	14.054	34.189	1.00	35.76	B	C
ATOM	2612	CG2	VAL	B	145	−14.556	13.416	36.148	1.00	32.94	B	C
ATOM	2613	C	VAL	B	145	−18.223	14.441	35.995	1.00	43.42	B	C
ATOM	2614	O	VAL	B	145	−18.809	13.342	36.043	1.00	47.84	B	O
ATOM	2615	N	PHE	B	146	−18.785	15.564	35.543	1.00	43.72	B	N
ATOM	2616	CA	PHE	B	146	−20.146	15.592	35.018	1.00	44.43	B	C
ATOM	2617	CB	PHE	B	146	−20.522	16.990	34.570	1.00	45.43	B	C
ATOM	2618	CG	PHE	B	146	−20.341	18.050	35.610	1.00	49.30	B	C
ATOM	2619	CD1	PHE	B	146	−19.604	19.191	35.324	1.00	52.90	B	C
ATOM	2620	CE1	PHE	B	146	−19.451	20.197	36.271	1.00	54.03	B	C
ATOM	2621	CZ	PHE	B	146	−20.053	20.080	37.502	1.00	51.89	B	C
ATOM	2622	CE2	PHE	B	146	−20.808	18.963	37.786	1.00	50.76	B	C
ATOM	2623	CD2	PHE	B	146	−20.949	17.950	36.846	1.00	48.78	B	C
ATOM	2624	C	PHE	B	146	−20.233	14.726	33.787	1.00	49.11	B	C
ATOM	2625	O	PHE	B	146	−19.447	14.904	32.878	1.00	56.47	B	O
ATOM	2626	N	PRO	B	147	−21.176	13.793	33.751	1.00	52.30	B	N
ATOM	2627	CA	PRO	B	147	−21.520	13.069	32.523	1.00	55.83	B	C
ATOM	2628	CB	PRO	B	147	−22.685	12.195	32.959	1.00	54.10	B	C
ATOM	2629	CG	PRO	B	147	−22.490	12.025	34.405	1.00	55.02	B	C
ATOM	2630	CD	PRO	B	147	−21.968	13.337	34.901	1.00	53.64	B	C
ATOM	2631	C	PRO	B	147	−22.001	14.027	31.456	1.00	64.29	B	C
ATOM	2632	O	PRO	B	147	−22.433	15.127	31.786	1.00	64.18	B	O
ATOM	2633	N	HIS	B		148	−21.954	13.612	30.196	1.00	78.08	B	N
ATOM	2634	CA	HIS	B		148	−22.141	14.555	29.092	1.00	92.40	B	C
ATOM	2635	CB	HIS	B		148	−21.535	14.011	27.783	1.00	101.33	B	C
ATOM	2636	CG	HIS	B		148	−20.107	14.429	27.550	1.00	107.97	B	C
ATOM	2637	ND1	HIS	B		148	−19.759	15.689	27.106	1.00	111.16	B	N
ATOM	2638	CE1	HIS	B		148	−18.444	15.765	26.988	1.00	112.02	B	C
ATOM	2639	NE2	HIS	B		148	−17.926	14.601	27.338	1.00	110.28	B	N
ATOM	2640	CD2	HIS	B		148	−18.943	13.748	27.694	1.00	109.07	B	C
ATOM	2641	C	HIS	B		148	−23.572	15.096	28.892	1.00	94.82	B	C
ATOM	2642	O	HIS	B		148	−23.874	15.676	27.847	1.00	95.71	B	O
ATOM	2643	N	ASN	B	149	−24.438	14.908	29.888	1.00	97.59	B	N
ATOM	2644	CA	ASN	B	149	−25.715	15.626	29.928	1.00	101.83	B	C
ATOM	2645	CB	ASN	B	149	−26.774	14.995	29.018	1.00	108.36	B	C
ATOM	2646	CG	ASN	B	149	−27.356	16.003	28.019	1.00	114.29	B	C
ATOM	2647	OD1	ASN	B	149	−26.613	16.720	27.338	1.00	115.73	B	O
ATOM	2648	ND2	ASN	B	149	−28.689	16.066	27.937	1.00	116.16	B	N
ATOM	2649	C	ASN	B	149	−26.294	15.944	31.310	1.00	101.43	B	C
ATOM	2650	O	ASN	B	149	−26.712	17.082	31.546	1.00	103.14	B	O
ATOM	2651	N	HIS	B		150	−26.343	14.966	32.214	1.00	98.98	B	N
ATOM	2652	CA	HIS	B	150	−26.765	15.262	33.586	1.00	96.40	B	C
ATOM	2653	CB	HIS	B	150	−27.117	13.984	34.375	1.00	103.90	B	C
ATOM	2654	CG	HIS	B		150	−28.007	14.226	35.566	1.00	112.70	B	C
ATOM	2655	ND1	HIS	B		150	−28.322	13.236	36.477	1.00	115.18	B	N
ATOM	2656	CE1	HIS	B		150	−29.116	13.732	37.412	1.00	115.57	B	C
ATOM	2657	NE2	HIS	B		150	−29.329	15.008	37.143	1.00	116.22	B	N
ATOM	2658	CD2	HIS	B		150	−28.648	15.343	35.995	1.00	114.87	B	C
ATOM	2659	C	HIS	B		150	−25.678	16.092	34.283	1.00	86.18	B	C
ATOM	2660	O	HIS	B		150	−24.553	15.636	34.441	1.00	83.39	B	O
ATOM	2661	N	THR	B	151	−26.017	17.321	34.661	1.00	77.85	B	N
ATOM	2662	CA	THR	B	151	−25.064	18.239	35.284	1.00	71.05	B	C
ATOM	2663	CB	THR	B	151	−25.316	19.678	34.800	1.00	71.38	B	C
ATOM	2664	OG1	THR	B	151	−25.137	19.740	33.385	1.00	74.39	B	O
ATOM	2665	CG2	THR	B	151	−24.253	20.638	35.318	1.00	67.68	B	C
ATOM	2666	C	THR	B	151	−25.147	18.193	36.802	1.00	68.37	B	C
ATOM	2667	O	THR	B	151	−24.286	18.726	37.494	1.00	69.11	B	O
ATOM	2668	N	ALA	B	152	−26.188	17.569	37.328	1.00	65.26	B	N
ATOM	2669	CA	ALA	B	152	−26.322	17.475	38.766	1.00	66.60	B	C
ATOM	2670	CB	ALA	B	152	−27.775	17.454	39.151	1.00	70.48	B	C
ATOM	2671	C	ALA	B	152	−25.613	16.226	39.267	1.00	68.90	B	C
ATOM	2672	O	ALA	B	152	−25.715	15.868	40.450	1.00	73.24	B	O
ATOM	2673	N	ASP	B	153	−24.885	15.569	38.368	1.00	65.99	B	N
ATOM	2674	CA	ASP	B	153	−24.266	14.294	38.690	1.00	64.22	B	C
ATOM	2675	CB	ASP	B	153	−24.356	13.338	37.507	1.00	67.82	B	C
ATOM	2676	CG	ASP	B	153	−24.270	11.886	37.927	1.00	72.99	B	C
ATOM	2677	OD1	ASP	B	153	−23.834	11.619	39.070	1.00	77.73	B	O
ATOM	2678	OD2	ASP	B	153	−24.607	10.940	37.180	1.00	72.88	B	O
ATOM	2679	C	ASP	B	153	−22.836	14.427	39.205	1.00	61.94	B	C
ATOM	2680	O	ASP	B	153	−21.872	14.052	38.541	1.00	64.99	B	O
ATOM	2681	N	ILE	B	154	−22.743	14.962	40.415	1.00	59.23	B	N
ATOM	2682	CA	ILE	B	154	−21.538	15.035	41.245	1.00	57.56	B	C
ATOM	2683	CB	ILE	B	154	−21.912	15.942	42.471	1.00	55.70	B	C
ATOM	2684	CG1	ILE	B	154	−22.096	17.368	42.013	1.00	54.79	B	C
ATOM	2685	CD1	ILE	B	154	−21.086	17.754	40.980	1.00	57.56	B	C
ATOM	2686	CG2	ILE	B	154	−20.876	15.932	43.576	1.00	57.05	B	C
ATOM	2687	C	ILE	B	154	−21.074	13.635	41.729	1.00	58.25	B	C
ATOM	2688	O	ILE	B	154	−20.039	13.496	42.403	1.00	46.30	B	O
ATOM	2689	N	GLN	B	155	−21.846	12.612	41.359	1.00	63.86	B	N
ATOM	2690	CA	GLN	B	155	−21.941	11.372	42.127	1.00	67.23	B	C
ATOM	2691	CB	GLN	B	155	−23.412	11.112	42.485	1.00	75.19	B	C
ATOM	2692	CG	GLN	B	155	−23.688	9.775	43.154	1.00	82.02	B	C
ATOM	2693	CD	GLN	B	155	−23.728	9.870	44.673	1.00	86.58	B	C
ATOM	2694	OE1	GLN	B	155	−22.981	9.164	45.366	1.00	86.57	B	O
ATOM	2695	NE2	GLN	B	155	−24.603	10.737	45.194	1.00	87.11	B	N
ATOM	2696	C	GLN	B	155	−21.365	10.167	41.416	1.00	65.06	B	C
ATOM	2697	O	GLN	B	155	−20.639	9.377	42.023	1.00	66.82	B	O
ATOM	2698	N	SER	B	156	−21.684	10.025	40.135	1.00	61.98	B	N
ATOM	2699	CA	SER	B	156	−21.338	8.809	39.408	1.00	62.24	B	C
ATOM	2700	CB	SER	B	156	−22.242	8.638	38.183	1.00	62.44	B	C
ATOM	2701	OG	SER	B	156	−21.611	9.101	37.007	1.00	66.58	B	O
ATOM	2702	C	SER	B	156	−19.827	8.614	39.093	1.00	61.49	B	C
ATOM	2703	O	SER	B	156	−19.299	7.526	39.271	1.00	63.76	B	O
ATOM	2704	N	GLU	B	157	−19.126	9.654	38.658	1.00	63.78	B	N
ATOM	2705	CA	GLU	B	157	−17.672	9.542	38.424	1.00	60.36	B	C
ATOM	2706	CB	GLU	B	157	−17.346	9.605	36.933	1.00	61.77	B	C
ATOM	2707	CG	GLU	B	157	−15.858	9.657	36.659	1.00	62.96	B	C
ATOM	2708	CD	GLU	B	157	−15.568	9.856	35.201	1.00	69.04	B	C
ATOM	2709	OE1	GLU	B	157	−16.515	10.214	34.461	1.00	71.13	B	O
ATOM	2710	OE2	GLU	B	157	−14.399	9.656	34.799	1.00	72.81	B	O
ATOM	2711	C	GLU	B	157	−16.831	10.569	39.207	1.00	52.41	B	C
ATOM	2712	O	GLU	B	157	−16.754	11.743	38.834	1.00	50.81	B	O
ATOM	2713	N	VAL	B	158	−16.212	10.095	40.286	1.00	44.97	B	N
ATOM	2714	CA	VAL	B	158	−15.491	10.926	41.235	1.00	41.41	B	C
ATOM	2715	CB	VAL	B	158	−16.212	11.004	42.585	1.00	38.90	B	C
ATOM	2716	CG1	VAL	B	158	−15.343	11.713	43.606	1.00	41.55	B	C
ATOM	2717	CG2	VAL	B	158	−17.523	11.684	42.462	1.00	38.40	B	C
ATOM	2718	C	VAL	B	158	−14.181	10.246	41.544	1.00	44.87	B	C
ATOM	2719	O	VAL	B	158	−14.190	9.158	42.091	1.00	48.33	B	O
ATOM	2720	N	HIS	B	159	−13.066	10.897	41.222	1.00	48.81	B	N
ATOM	2721	CA	HIS	B	159	−11.728	10.413	41.558	1.00	49.97	B	C
ATOM	2722	CB	HIS	B	159	−10.822	10.456	40.334	1.00	55.24	B	C
ATOM	2723	CG	HIS	B	159	−11.455	9.934	39.092	1.00	57.18	B	C
ATOM	2724	ND1	HIS	B	159	−11.255	8.649	38.645	1.00	61.70	B	N
ATOM	2725	CE1	HIS	B	159	−11.921	8.472	37.518	1.00	66.34	B	C
ATOM	2726	NE2	HIS	B	159	−12.549	9.596	37.224	1.00	64.77	B	N
ATOM	2727	CD2	HIS	B	159	−12.266	10.528	38.190	1.00	59.87	B	C
ATOM	2728	C	HIS	B	159	−11.079	11.289	42.603	1.00	45.65	B	C
ATOM	2729	O	HIS	B	159	−11.085	12.512	42.465	1.00	46.99	B	O
ATOM	2730	N	CYS	B	160	−10.486	10.667	43.617	1.00	43.49	B	N
ATOM	2731	CA	CYS	B	160	−9.662	11.386	44.589	1.00	50.24	B	C
ATOM	2732	CB	CYS	B	160	−9.462	10.511	45.829	1.00	56.49	B	C
ATOM	2733	SG	CYS	B	160	−8.633	11.276	47.239	1.00	63.33	B	S
ATOM	2734	C	CYS	B	160	−8.319	11.773	43.936	1.00	50.29	B	C
ATOM	2735	O	CYS	B	160	−7.827	11.040	43.081	1.00	55.87	B	O
ATOM	2736	N	ILE	B	161	−7.741	12.924	44.286	1.00	47.03	B	N
ATOM	2737	CA	ILE	B	161	−6.490	13.348	43.632	1.00	46.63	B	C
ATOM	2738	CB	ILE	B	161	−6.543	14.777	43.026	1.00	38.65	B	C
ATOM	2739	CG1	ILE	B	161	−7.751	14.997	42.127	1.00	34.38	B	C
ATOM	2740	CD1	ILE	B	161	−7.701	16.338	41.444	1.00	34.32	B	C
ATOM	2741	CG2	ILE	B	161	−5.260	15.053	42.246	1.00	34.37	B	C
ATOM	2742	C	ILE	B	161	−5.317	13.324	44.583	1.00	56.92	B	C
ATOM	2743	O	ILE	B	161	−5.078	14.321	45.300	1.00	62.39	B	O
ATOM	2744	N	PHE	B	162	−4.580	12.209	44.556	1.00	60.69	B	N
ATOM	2745	CA	PHE	B	162	−3.338	12.051	45.300	1.00	61.03	B	C
ATOM	2746	CB	PHE	B	162	−3.620	11.632	46.745	1.00	59.23	B	C
ATOM	2747	CG	PHE	B	162	−2.393	11.330	47.547	1.00	66.31	B	C
ATOM	2748	CD1	PHE	B	162	−2.396	11.515	48.917	1.00	69.32	B	C
ATOM	2749	CE1	PHE	B	162	−1.268	11.236	49.679	1.00	71.72	B	C
ATOM	2750	CZ	PHE	B	162	−0.118	10.759	49.067	1.00	76.67	B	C
ATOM	2751	CE2	PHE	B	162	−0.102	10.560	47.681	1.00	75.24	B	C
ATOM	2752	CD2	PHE	B	162	−1.234	10.844	46.940	1.00	71.12	B	C
ATOM	2753	C	PHE	B	162	−2.451	11.023	44.616	1.00	64.46	B	C
ATOM	2754	O	PHE	B	162	−2.581	9.832	44.862	1.00	69.15	B	O
ATOM	2755	N	SER	B	163	−1.543	11.491	43.771	1.00	67.84	B	N
ATOM	2756	CA	SER	B	163	−0.518	10.642	43.167	1.00	72.18	B	C
ATOM	2757	CB	SER	B	163	−0.001	11.298	41.887	1.00	76.28	B	C
ATOM	2758	OG	SER	B	163	0.847	10.416	41.184	1.00	81.52	B	O
ATOM	2759	C	SER	B	163	0.645	10.423	44.137	1.00	72.44	B	C
ATOM	2760	O	SER	B	163	1.159	11.390	44.684	1.00	69.21	B	O
ATOM	2761	N	PRO	B	164	1.074	9.173	44.344	1.00	79.41	B	N
ATOM	2762	CA	PRO	B	164	2.144	8.879	45.318	1.00	83.15	B	C
ATOM	2763	CB	PRO	B	164	2.208	7.348	45.330	1.00	82.50	B	C
ATOM	2764	CG	PRO	B	164	1.633	6.927	44.023	1.00	81.14	B	C
ATOM	2765	CD	PRO	B	164	0.598	7.954	43.664	1.00	81.00	B	C
ATOM	2766	C	PRO	B	164	3.490	9.499	44.913	1.00	82.80	B	C
ATOM	2767	O	PRO	B	164	3.808	9.545	43.729	1.00	81.17	B	O
ATOM	2768	N	GLN	B	165	4.252	9.975	45.893	1.00	85.72	B	N
ATOM	2769	CA	GLN	B	165	5.390	10.850	45.629	1.00	91.50	B	C
ATOM	2770	CB	GLN	B	165	5.401	11.986	46.649	1.00	89.42	B	C
ATOM	2771	CG	GLN	B	165	5.925	13.312	46.096	1.00	87.88	B	C
ATOM	2772	CD	GLN	B	165	5.147	13.843	44.892	1.00	83.64	B	C
ATOM	2773	OE1	GLN	B	165	4.042	13.382	44.587	1.00	81.23	B	O
ATOM	2774	NE2	GLN	B	165	5.729	14.820	44.212	1.00	81.96	B	N
ATOM	2775	C	GLN	B	165	6.735	10.129	45.608	1.00	99.59	B	C
ATOM	2776	O	GLN	B	165	7.138	9.544	46.613	1.00	103.36	B	O
ATOM	2777	N	ILE	B	166	7.440	10.189	44.476	1.00	106.48	B	N
ATOM	2778	CA	ILE	B	166	8.581	9.286	44.246	1.00	113.53	B	C
ATOM	2779	CB	ILE	B	166	8.212	8.200	43.163	1.00	114.08	B	C
ATOM	2780	CG1	ILE	B	166	8.067	6.820	43.825	1.00	114.36	B	C
ATOM	2781	CD1	ILE	B	166	6.653	6.505	44.350	1.00	113.22	B	C
ATOM	2782	CG2	ILE	B	166	9.192	8.178	41.965	1.00	112.30	B	C
ATOM	2783	C	ILE	B	166	9.953	9.945	44.014	1.00	118.30	B	C
ATOM	2784	O	ILE	B	166	10.966	9.458	44.533	1.00	114.87	B	O
ATOM	2785	N	GLU	B	167	9.980	11.045	43.257	1.00	126.36	B	N
ATOM	2786	CA	GLU	B	167	11.223	11.788	43.003	1.00	131.46	B	C
ATOM	2787	CB	GLU	B	167	11.053	12.807	41.859	1.00	135.17	B	C
ATOM	2788	CG	GLU	B	167	10.514	12.245	40.540	1.00	138.96	B	C
ATOM	2789	CD	GLU	B	167	11.389	11.154	39.931	1.00	140.44	B	C
ATOM	2790	OE1	GLU	B	167	12.610	11.380	39.754	1.00	139.92	B	O
ATOM	2791	OE2	GLU	B	167	10.848	10.067	39.624	1.00	140.86	B	O
ATOM	2792	C	GLU	B	167	11.708	12.478	44.286	1.00	131.99	B	C
ATOM	2793	O	GLU	B	167	12.810	12.199	44.771	1.00	132.18	B	O
ATOM	2794	N	GLU	B	168	10.872	13.365	44.829	1.00	131.33	B	N
ATOM	2795	CA	GLU	B	168	11.119	13.991	46.126	1.00	128.96	B	C
ATOM	2796	CB	GLU	B	168	11.189	15.524	45.986	1.00	132.26	B	C
ATOM	2797	CG	GLU	B	168	12.602	16.105	45.894	1.00	136.32	B	C
ATOM	2798	CD	GLU	B	168	13.399	16.025	47.200	1.00	138.39	B	C
ATOM	2799	OE1	GLU	B	168	12.797	16.080	48.299	1.00	138.49	B	O
ATOM	2800	OE2	GLU	B	168	14.645	15.914	47.129	1.00	138.47	B	O
ATOM	2801	C	GLU	B	168	10.026	13.583	47.128	1.00	123.48	B	C
ATOM	2802	O	GLU	B	168	9.061	14.326	47.314	1.00	125.00	B	O
ATOM	2803	N	PRO	B	169	10.174	12.415	47.770	1.00	117.59	B	N
ATOM	2804	CA	PRO	B	169	9.169	11.894	48.718	1.00	112.28	B	C
ATOM	2805	CB	PRO	B	169	9.774	10.558	49.172	1.00	113.47	B	C
ATOM	2806	CG	PRO	B	169	10.708	10.189	48.084	1.00	115.63	B	C
ATOM	2807	CD	PRO	B	169	11.312	11.488	47.632	1.00	116.96	B	C
ATOM	2808	C	PRO	B	169	8.912	12.782	49.938	1.00	105.68	B	C
ATOM	2809	O	PRO	B	169	8.082	12.436	50.783	1.00	101.38	B	O
ATOM	2810	N	SER	B	170	9.621	13.905	50.011	1.00	102.05	B	N
ATOM	2811	CA	SER	B	170	9.467	14.878	51.087	1.00	97.82	B	C
ATOM	2812	CB	SER	B	170	10.746	15.715	51.247	1.00	99.30	B	C
ATOM	2813	OG	SER	B	170	11.837	15.150	50.530	1.00	100.06	B	O
ATOM	2814	C	SER	B	170	8.279	15.796	50.826	1.00	91.37	B	C
ATOM	2815	O	SER	B	170	7.655	16.293	51.766	1.00	91.05	B	O
ATOM	2816	N	GLN	B	171	7.976	16.008	49.547	1.00	83.23	B	N
ATOM	2817	CA	GLN	B	171	6.943	16.955	49.132	1.00	78.78	B	C
ATOM	2818	CB	GLN	B	171	7.286	17.565	47.768	1.00	82.89	B	C
ATOM	2819	CG	GLN	B	171	8.143	18.836	47.832	1.00	84.78	B	C
ATOM	2820	CD	GLN	B	171	7.735	19.785	48.947	1.00	85.40	B	C
ATOM	2821	OE1	GLN	B	171	8.498	19.992	49.901	1.00	87.87	B	O
ATOM	2822	NE2	GLN	B	171	6.535	20.362	48.837	1.00	82.96	B	N
ATOM	2823	C	GLN	B	171	5.544	16.347	49.096	1.00	72.27	B	C
ATOM	2824	O	GLN	B	171	5.398	15.122	49.101	1.00	73.45	B	O
ATOM	2825	N	CYS	B	172	4.525	17.211	49.084	1.00	62.06	B	N
ATOM	2826	CA	CYS	B	172	3.137	16.774	49.018	1.00	54.69	B	C
ATOM	2827	CB	CYS	B	172	2.534	16.578	50.395	1.00	52.71	B	C
ATOM	2828	SG	CYS	B	172	0.962	15.724	50.194	1.00	58.58	B	S
ATOM	2829	C	CYS	B	172	2.262	17.745	48.256	1.00	53.37	B	C
ATOM	2830	O	CYS	B	172	1.546	18.567	48.852	1.00	58.82	B	O
ATOM	2831	N	PRO	B	173	2.286	17.643	46.940	1.00	43.62	B	N
ATOM	2832	CA	PRO	B	173	1.628	18.638	46.099	1.00	40.98	B	C
ATOM	2833	CB	PRO	B	173	2.383	18.530	44.780	1.00	34.49	B	C
ATOM	2834	CG	PRO	B	173	3.372	17.483	45.011	1.00	38.66	B	C
ATOM	2835	CD	PRO	B	173	2.918	16.594	46.144	1.00	37.31	B	C
ATOM	2836	C	PRO	B	173	0.165	18.283	45.914	1.00	43.04	B	C
ATOM	2837	O	PRO	B	173	−0.543	18.973	45.190	1.00	48.61	B	O
ATOM	2838	N	ASP	B	174	−0.292	17.214	46.545	1.00	39.17	B	N
ATOM	2839	CA	ASP	B	174	−1.687	16.864	46.402	1.00	40.82	B	C
ATOM	2840	CB	ASP	B	174	−1.864	15.373	46.099	1.00	43.79	B	C
ATOM	2841	CG	ASP	B	174	−1.166	14.936	44.828	1.00	45.66	B	C
ATOM	2842	OD1	ASP	B	174	−1.259	15.623	43.779	1.00	46.41	B	O
ATOM	2843	OD2	ASP	B	174	−0.500	13.890	44.796	1.00	48.95	B	O
ATOM	2844	C	ASP	B	174	−2.379	17.257	47.692	1.00	42.23	B	C
ATOM	2845	O	ASP	B	174	−3.600	17.080	47.851	1.00	46.03	B	O
ATOM	2846	N	CYS	B	175	−1.574	17.773	48.614	1.00	38.28	B	N
ATOM	2847	CA	CYS	B	175	−2.068	18.295	49.860	1.00	42.16	B	C
ATOM	2848	CB	CYS	B	175	−1.022	18.087	50.935	1.00	47.27	B	C
ATOM	2849	SG	CYS	B	175	−0.658	16.364	51.258	1.00	53.13	B	S
ATOM	2850	C	CYS	B	175	−2.297	19.784	49.650	1.00	44.67	B	C
ATOM	2851	O	CYS	B	175	−1.408	20.606	49.901	1.00	54.11	B	O
ATOM	2852	N	VAL	B	176	−3.482	20.140	49.180	1.00	37.73	B	N
ATOM	2853	CA	VAL	B	176	−3.695	21.490	48.729	1.00	37.04	B	C
ATOM	2854	CB	VAL	B	176	−4.755	21.583	47.637	1.00	34.29	B	C
ATOM	2855	CG1	VAL	B	176	−4.717	22.976	47.038	1.00	36.64	B	C
ATOM	2856	CG2	VAL	B	176	−4.550	20.534	46.565	1.00	26.75	B	C
ATOM	2857	C	VAL	B	176	−4.146	22.382	49.855	1.00	45.28	B	C
ATOM	2858	O	VAL	B	176	−3.530	23.396	50.115	1.00	54.88	B	O
ATOM	2859	N	VAL	B	177	−5.224	22.006	50.523	1.00	44.67	B	N
ATOM	2860	CA	VAL	B	177	−5.956	22.942	51.359	1.00	41.51	B	C
ATOM	2861	CB	VAL	B	177	−7.431	22.706	51.098	1.00	39.22	B	C
ATOM	2862	CG1	VAL	B	177	−8.169	22.253	52.331	1.00	35.75	B	C
ATOM	2863	CG2	VAL	B	177	−8.037	23.920	50.460	1.00	42.41	B	C
ATOM	2864	C	VAL	B	177	−5.591	22.820	52.851	1.00	48.49	B	C
ATOM	2865	O	VAL	B	177	−5.154	21.755	53.307	1.00	55.50	B	O
ATOM	2866	N	SER	B	178	−5.731	23.902	53.617	1.00	45.01	B	N
ATOM	2867	CA	SER	B	178	−5.509	23.797	55.065	1.00	39.42	B	C
ATOM	2868	CB	SER	B	178	−4.477	24.797	55.579	1.00	36.20	B	C
ATOM	2869	OG	SER	B	178	−4.842	25.259	56.871	1.00	38.11	B	O
ATOM	2870	C	SER	B	178	−6.788	23.898	55.892	1.00	40.49	B	C
ATOM	2871	O	SER	B	178	−7.555	24.883	55.817	1.00	37.91	B	O
ATOM	2872	N	ALA	B	179	−6.974	22.855	56.695	1.00	39.49	B	N
ATOM	2873	CA	ALA	B	179	−8.061	22.723	57.648	1.00	31.63	B	C
ATOM	2874	CB	ALA	B	179	−7.722	21.632	58.655	1.00	37.29	B	C
ATOM	2875	C	ALA	B	179	−8.317	24.010	58.378	1.00	28.72	B	C
ATOM	2876	O	ALA	B	179	−9.466	24.300	58.740	1.00	30.40	B	O
ATOM	2877	N	LEU	B		180	−7.261	24.782	58.618	1.00	26.42	B	N
ATOM	2878	CA	LEU	B	180	−7.440	25.993	59.412	1.00	36.32	B	C
ATOM	2879	CB	LEU	B	180	−6.543	26.006	60.657	1.00	37.97	B	C
ATOM	2880	CG	LEU	B		180	−5.100	25.527	60.601	1.00	33.91	B	C
ATOM	2881	CD1	LEU	B	180	−4.212	26.631	60.098	1.00	34.16	B	C
ATOM	2882	CD2	LEU	B	180	−4.722	25.159	61.992	1.00	30.99	B	C
ATOM	2883	C	LEU	B	180	−7.329	27.285	58.632	1.00	40.07	B	C
ATOM	2884	O	LEU	B		180	−6.853	28.295	59.161	1.00	39.73	B	O
ATOM	2885	N	GLY	B	181	−7.786	27.238	57.379	1.00	45.44	B	N
ATOM	2886	CA	GLY	B	181	−7.998	28.425	56.567	1.00	44.24	B	C
ATOM	2887	C	GLY	B	181	−7.245	28.363	55.268	1.00	41.77	B	C
ATOM	2888	O	GLY	B	181	−6.011	28.299	55.287	1.00	40.12	B	O
ATOM	2889	N	ALA	B	182	−7.990	28.386	54.155	1.00	42.59	B	N
ATOM	2890	CA	ALA	B	182	−7.435	28.343	52.783	1.00	33.05	B	C
ATOM	2891	CB	ALA	B	182	−7.517	26.957	52.252	1.00	25.62	B	C
ATOM	2892	C	ALA	B	182	−8.184	29.261	51.846	1.00	34.56	B	C
ATOM	2893	O	ALA	B	182	−9.386	29.476	52.023	1.00	44.68	B	O
ATOM	2894	N	LYS	B	183	−7.490	29.813	50.859	1.00	33.14	B	N
ATOM	2895	CA	LYS	B	183	−8.171	30.373	49.678	1.00	36.30	B	C
ATOM	2896	CB	LYS	B	183	−8.171	31.896	49.646	1.00	39.28	B	C
ATOM	2897	CG	LYS	B	183	−9.279	32.532	50.470	1.00	49.30	B	C
ATOM	2898	CD	LYS	B	183	−10.623	32.584	49.732	1.00	58.73	B	C
ATOM	2899	CE	LYS	B	183	−11.785	32.976	50.668	1.00	61.53	B	C
ATOM	2900	NZ	LYS	B	183	−11.672	32.401	52.056	1.00	62.38	B	N
ATOM	2901	C	LYS	B	183	−7.520	29.845	48.426	1.00	35.29	B	C
ATOM	2902	O	LYS	B	183	−6.299	29.836	48.290	1.00	36.47	B	O
ATOM	2903	N	VAL	B	184	−8.348	29.379	47.514	1.00	33.14	B	N
ATOM	2904	CA	VAL	B	184	−7.855	28.698	46.337	1.00	27.03	B	C
ATOM	2905	CB	VAL	B	184	−8.357	27.264	46.296	1.00	24.13	B	C
ATOM	2906	CG1	VAL	B	184	−8.210	26.679	44.889	1.00	16.54	B	C
ATOM	2907	CG2	VAL	B	184	−7.609	26.438	47.354	1.00	23.45	B	C
ATOM	2908	C	VAL	B	184	−8.371	29.406	45.143	1.00	25.71	B	C
ATOM	2909	O	VAL	B	184	−9.561	29.648	45.032	1.00	31.46	B	O
ATOM	2910	N	LEU	B	185	−7.478	29.742	44.239	1.00	29.38	B	N
ATOM	2911	CA	LEU	B	185	−7.882	30.436	43.041	1.00	36.04	B	C
ATOM	2912	CB	LEU	B	185	−7.410	31.880	43.129	1.00	33.81	B	C
ATOM	2913	CG	LEU	B	185	−7.123	32.673	41.874	1.00	41.23	B	C
ATOM	2914	CD1	LEU	B	185	−8.215	32.469	40.836	1.00	52.79	B	C
ATOM	2915	CD2	LEU	B	185	−7.011	34.133	42.222	1.00	41.51	B	C
ATOM	2916	C	LEU	B	185	−7.276	29.681	41.879	1.00	40.80	B	C
ATOM	2917	O	LEU	B	185	−6.076	29.432	41.876	1.00	49.60	B	O
ATOM	2918	N	SER	B	186	−8.097	29.275	40.916	1.00	41.06	B	N
ATOM	2919	CA	SER	B	186	−7.589	28.435	39.828	1.00	48.57	B	C
ATOM	2920	CB	SER	B	186	−8.332	27.076	39.747	1.00	55.01	B	C
ATOM	2921	OG	SER	B	186	−8.931	26.835	38.468	1.00	54.97	B	O
ATOM	2922	C	SER	B	186	−7.712	29.173	38.536	1.00	46.06	B	C
ATOM	2923	O	SER	B	186	−8.736	29.782	38.294	1.00	55.39	B	O
ATOM	2924	N	SER	B	187	−6.687	29.108	37.703	1.00	42.07	B	N
ATOM	2925	CA	SER	B	187	−6.729	29.786	36.412	1.00	46.72	B	C
ATOM	2926	CB	SER	B	187	−6.203	31.218	36.557	1.00	49.29	B	C
ATOM	2927	OG	SER	B	187	−4.809	31.325	36.265	1.00	54.33	B	O
ATOM	2928	C	SER	B	187	−5.955	29.025	35.334	1.00	49.35	B	C
ATOM	2929	O	SER	B	187	−4.938	28.385	35.628	1.00	54.65	B	O
ATOM	2930	N	VAL	B	188	−6.424	29.089	34.090	1.00	44.80	B	N
ATOM	2931	CA	VAL	B	188	−5.719	28.408	33.005	1.00	45.35	B	C
ATOM	2932	CB	VAL	B	188	−6.627	28.078	31.861	1.00	44.43	B	C
ATOM	2933	CG1	VAL	B	188	−6.399	26.680	31.421	1.00	45.45	B	C
ATOM	2934	CG2	VAL	B	188	−8.064	28.268	32.285	1.00	53.50	B	C
ATOM	2935	C	VAL	B	188	−4.623	29.292	32.474	1.00	49.38	B	C
ATOM	2936	O	VAL	B	188	−4.833	30.475	32.252	1.00	52.76	B	O
ATOM	2937	N	LYS	B	189	−3.446	28.718	32.290	1.00	55.20	B	N
ATOM	2938	CA	LYS	B	189	−2.282	29.477	31.849	1.00	61.71	B	C
ATOM	2939	CB	LYS	B	189	−1.688	30.298	33.006	1.00	68.93	B	C
ATOM	2940	CG	LYS	B	189	−0.918	31.531	32.551	1.00	78.03	B	C
ATOM	2941	CD	LYS	B	189	−1.587	32.825	33.019	1.00	85.92	B	C
ATOM	2942	CE	LYS	B	189	−1.457	33.948	31.964	1.00	88.26	B	C
ATOM	2943	NZ	LYS	B	189	−0.885	35.223	32.509	1.00	87.34	B	N
ATOM	2944	C	LYS	B	189	−1.240	28.541	31.221	1.00	60.86	B	C
ATOM	2945	O	LYS	B	189	−0.802	27.544	31.834	1.00	61.91	B	O
ATOM	2946	N	ASP	B	190	−0.862	28.871	29.990	1.00	53.49	B	N
ATOM	2947	CA	ASP	B	190	0.075	28.068	29.222	1.00	48.50	B	C
ATOM	2948	CB	ASP	B	190	1.451	28.083	29.886	1.00	48.87	B	C
ATOM	2949	CG	ASP	B	190	2.270	29.280	29.461	1.00	54.63	B	C
ATOM	2950	OD1	ASP	B	190	1.731	30.121	28.695	1.00	53.84	B	O
ATOM	2951	OD2	ASP	B	190	3.456	29.469	29.832	1.00	59.09	B	O
ATOM	2952	C	ASP	B	190	−0.403	26.646	28.931	1.00	45.42	B	C
ATOM	2953	O	ASP	B	190	0.397	25.728	28.833	1.00	45.42	B	O
ATOM	2954	N	ARG	B	191	−1.709	26.484	28.754	1.00	43.30	B	N
ATOM	2955	CA	ARG	B	191	−2.339	25.176	28.510	1.00	38.92	B	C
ATOM	2956	CB	ARG	B	191	−1.695	24.424	27.338	1.00	34.43	B	C
ATOM	2957	CG	ARG	B	191	−1.910	25.039	26.008	1.00	35.89	B	C
ATOM	2958	CD	ARG	B	191	−0.698	24.935	25.096	1.00	43.60	B	C
ATOM	2959	NE	ARG	B	191	−0.925	25.495	23.757	1.00	45.85	B	N
ATOM	2960	CZ	ARG	B	191	−1.912	25.130	22.943	1.00	43.18	B	C
ATOM	2961	NH1	ARG	B	191	−2.774	24.186	23.326	1.00	46.90	B	N
ATOM	2962	NH2	ARG	B	191	−2.043	25.713	21.758	1.00	36.04	B	N
ATOM	2963	C	ARG	B	191	−2.367	24.276	29.731	1.00	40.27	B	C
ATOM	2964	O	ARG	B	191	−2.762	23.103	29.627	1.00	49.44	B	O
ATOM	2965	N	PHE	B	192	−1.928	24.799	30.876	1.00	37.02	B	N
ATOM	2966	CA	PHE	B		192	−2.050	24.071	32.144	1.00	36.02	B	C
ATOM	2967	CB	PHE	B	192	−0.697	24.004	32.864	1.00	38.65	B	C
ATOM	2968	CG	PHE	B	192	0.289	23.041	32.248	1.00	40.43	B	C
ATOM	2969	CD1	PHE	B	192	1.555	23.467	31.890	1.00	45.65	B	C
ATOM	2970	CE1	PHE	B	192	2.458	22.603	31.313	1.00	46.19	B	C
ATOM	2971	CZ	PHE	B	192	2.098	21.282	31.110	1.00	47.84	B	C
ATOM	2972	CE2	PHE	B	192	0.863	20.841	31.484	1.00	42.36	B	C
ATOM	2973	CD2	PHE	B	192	−0.036	21.719	32.051	1.00	42.76	B	C
ATOM	2974	C	PHE	B	192	−3.102	24.700	33.067	1.00	34.90	B	C
ATOM	2975	O	PHE	B	192	−3.181	25.926	33.177	1.00	38.45	B	O
ATOM	2976	N	ILE	B	193	−3.907	23.882	33.737	1.00	31.74	B	N
ATOM	2977	CA	ILE	B	193	−4.689	24.404	34.873	1.00	36.25	B	C
ATOM	2978	CB	ILE	B	193	−5.808	23.415	35.237	1.00	31.14	B	C
ATOM	2979	CG1	ILE	B	193	−6.790	23.305	34.079	1.00	34.97	B	C
ATOM	2980	CD1	ILE	B	193	−7.471	21.956	33.991	1.00	36.83	B	C
ATOM	2981	CG2	ILE	B	193	−6.500	23.822	36.511	1.00	20.62	B	C
ATOM	2982	C	ILE	B	193	−3.787	24.730	36.120	1.00	42.24	B	C
ATOM	2983	O	ILE	B	193	−3.135	23.840	36.702	1.00	40.91	B	O
ATOM	2984	N	ASN	B	194	−3.738	26.002	36.516	1.00	42.02	B	N
ATOM	2985	CA	ASN	B	194	−2.909	26.409	37.652	1.00	42.83	B	C
ATOM	2986	CB	ASN	B	194	−2.082	27.642	37.304	1.00	48.68	B	C
ATOM	2987	CG	ASN	B	194	−1.103	27.389	36.187	1.00	55.84	B	C
ATOM	2988	OD1	ASN	B	194	−0.970	26.269	35.705	1.00	57.27	B	O
ATOM	2989	ND2	ASN	B	194	−0.410	28.440	35.760	1.00	61.82	B	N
ATOM	2990	C	ASN	B	194	−3.715	26.709	38.903	1.00	42.86	B	C
ATOM	2991	O	ASN	B	194	−4.787	27.324	38.830	1.00	46.24	B	O
ATOM	2992	N	PHE	B	195	−3.187	26.291	40.049	1.00	35.15	B	N
ATOM	2993	CA	PHE	B	195	−3.822	26.562	41.315	1.00	32.96	B	C
ATOM	2994	CB	PHE	B	195	−4.081	25.255	42.030	1.00	35.85	B	C
ATOM	2995	CG	PHE	B	195	−5.338	24.580	41.616	1.00	43.13	B	C
ATOM	2996	CD1	PHE	B	195	−5.585	24.281	40.269	1.00	44.31	B	C
ATOM	2997	CE1	PHE	B	195	−6.752	23.637	39.882	1.00	40.86	B	C
ATOM	2998	CZ	PHE	B	195	−7.688	23.277	40.837	1.00	41.96	B	C
ATOM	2999	CE2	PHE	B	195	−7.455	23.559	42.189	1.00	44.66	B	C
ATOM	3000	CD2	PHE	B	195	−6.279	24.212	42.571	1.00	44.66	B	C
ATOM	3001	C	PHE	B	195	−2.944	27.435	42.182	1.00	36.69	B	C
ATOM	3002	O	PHE	B	195	−1.861	27.012	42.615	1.00	46.03	B	O
ATOM	3003	N	PHE	B	196	−3.411	28.646	42.453	1.00	35.16	B	N
ATOM	3004	CA	PHE	B	196	−2.778	29.532	43.434	1.00	34.28	B	C
ATOM	3005	CB	PHE	B	196	−2.859	30.958	42.956	1.00	32.45	B	C
ATOM	3006	CG	PHE	B	196	−2.313	31.131	41.592	1.00	38.26	B	C
ATOM	3007	CD1	PHE	B	196	−3.085	30.853	40.487	1.00	36.46	B	C
ATOM	3008	CE1	PHE	B	196	−2.575	30.991	39.225	1.00	35.74	B	C
ATOM	3009	CZ	PHE	B	196	−1.284	31.407	39.044	1.00	38.69	B	C
ATOM	3010	CE2	PHE	B	196	−0.493	31.692	40.128	1.00	41.38	B	C
ATOM	3011	CD2	PHE	B	196	−1.005	31.537	41.405	1.00	42.89	B	C
ATOM	3012	C	PHE	B	196	−3.505	29.387	44.741	1.00	34.55	B	C
ATOM	3013	O	PHE	B	196	−4.728	29.351	44.751	1.00	40.48	B	O
ATOM	3014	N	VAL	B	197	−2.768	29.294	45.841	1.00	32.43	B	N
ATOM	3015	CA	VAL	B	197	−3.370	28.869	47.102	1.00	34.63	B	C
ATOM	3016	CB	VAL	B	197	−3.238	27.343	47.287	1.00	35.94	B	C
ATOM	3017	CG1	VAL	B	197	−3.680	26.939	48.697	1.00	34.44	B	C
ATOM	3018	CG2	VAL	B	197	−3.983	26.585	46.213	1.00	32.05	B	C
ATOM	3019	C	VAL	B	197	−2.785	29.509	48.363	1.00	37.15	B	C
ATOM	3020	O	VAL	B	197	−1.611	29.267	48.738	1.00	41.19	B	O
ATOM	3021	N	GLY	B	198	−3.631	30.281	49.039	1.00	34.43	B	N
ATOM	3022	CA	GLY	B	198	−3.318	30.808	50.360	1.00	34.89	B	C
ATOM	3023	C	GLY	B	198	−3.738	29.863	51.478	1.00	31.71	B	C
ATOM	3024	O	GLY	B	198	−4.881	29.383	51.514	1.00	30.34	B	O
ATOM	3025	N	ASN	B	199	−2.824	29.609	52.406	1.00	28.72	B	N
ATOM	3026	CA	ASN	B	199	−3.102	28.668	53.473	1.00	33.64	B	C
ATOM	3027	CB	ASN	B	199	−2.558	27.282	53.117	1.00	32.78	B	C
ATOM	3028	CG	ASN	B	199	−3.633	26.337	52.613	1.00	29.87	B	C
ATOM	3029	OD1	ASN	B	199	−4.780	26.423	53.010	1.00	31.50	B	O
ATOM	3030	ND2	ASN	B	199	−3.254	25.417	51.756	1.00	26.99	B	N
ATOM	3031	C	ASN	B	199	−2.536	29.117	54.804	1.00	40.81	B	C
ATOM	3032	O	ASN	B	199	−1.316	29.309	54.934	1.00	45.86	B	O
ATOM	3033	N	THR	B	200	−3.430	29.295	55.781	1.00	41.96	B	N
ATOM	3034	CA	THR	B	200	−3.038	29.525	57.172	1.00	45.39	B	C
ATOM	3035	CB	THR	B	200	−4.233	29.913	58.008	1.00	47.52	B	C
ATOM	3036	OG1	THR	B	200	−5.152	30.661	57.188	1.00	58.61	B	O
ATOM	3037	CG2	THR	B	200	−3.811	30.890	59.076	1.00	39.80	B	C
ATOM	3038	C	THR	B	200	−2.456	28.243	57.701	1.00	47.44	B	C
ATOM	3039	O	THR	B	200	−2.978	27.164	57.436	1.00	50.95	B	O
ATOM	3040	N	ILE	B	201	−1.373	28.363	58.454	1.00	47.30	B	N
ATOM	3041	CA	ILE	B	201	−0.518	27.220	58.734	1.00	46.34	B	C
ATOM	3042	CB	ILE	B	201	0.588	27.217	57.680	1.00	39.76	B	C
ATOM	3043	CG1	ILE	B	201	0.408	26.018	56.782	1.00	39.93	B	C
ATOM	3044	CD1	ILE	B	201	1.659	25.680	56.053	1.00	45.00	B	C
ATOM	3045	CG2	ILE	B	201	1.989	27.282	58.274	1.00	39.70	B	C
ATOM	3046	C	ILE	B	201	−0.011	27.238	60.189	1.00	56.10	B	C
ATOM	3047	O	ILE	B	201	0.285	28.317	60.734	1.00	61.66	B	O
ATOM	3048	N	ASN	B	202	0.057	26.066	60.832	1.00	58.28	B	N
ATOM	3049	CA	ASN	B	202	0.121	26.055	62.299	1.00	60.14	B	C
ATOM	3050	CB	ASN	B	202	−1.312	26.021	62.917	1.00	59.83	B	C
ATOM	3051	CG	ASN	B	202	−1.615	24.758	63.742	1.00	58.90	B	C
ATOM	3052	OD1	ASN	B	202	−1.394	23.622	63.302	1.00	56.49	B	O
ATOM	3053	ND2	ASN	B	202	−2.175	24.968	64.938	1.00	58.00	B	N
ATOM	3054	C	ASN	B	202	1.150	25.162	62.990	1.00	63.14	B	C
ATOM	3055	O	ASN	B	202	1.034	24.872	64.185	1.00	67.58	B	O
ATOM	3056	N	SER	B	203	2.175	24.754	62.246	1.00	63.26	B	N
ATOM	3057	CA	SER	B	203	3.317	24.005	62.820	1.00	62.77	B	C
ATOM	3058	CB	SER	B	203	4.094	24.825	63.884	1.00	59.71	B	C
ATOM	3059	OG	SER	B	203	4.057	24.247	65.182	1.00	52.81	B	O
ATOM	3060	C	SER	B	203	3.024	22.603	63.340	1.00	60.77	B	C
ATOM	3061	O	SER	B	203	3.886	22.003	63.963	1.00	60.35	B	O
ATOM	3062	N	SER	B	204	1.828	22.082	63.095	1.00	64.29	B	N
ATOM	3063	CA	SER	B	204	1.629	20.645	63.172	1.00	72.70	B	C
ATOM	3064	CB	SER	B	204	0.170	20.260	62.914	1.00	70.92	B	C
ATOM	3065	OG	SER	B	204	−0.727	21.224	63.436	1.00	68.03	B	O
ATOM	3066	C	SER	B	204	2.581	20.019	62.136	1.00	84.48	B	C
ATOM	3067	O	SER	B	204	2.212	19.746	60.982	1.00	85.81	B	O
ATOM	3068	N	TYR	B	205	3.832	19.864	62.566	1.00	95.91	B	N
ATOM	3069	CA	TYR	B	205	4.895	19.220	61.807	1.00	106.72	B	C
ATOM	3070	CB	TYR	B	205	6.069	18.915	62.756	1.00	109.83	B	C
ATOM	3071	CG	TYR	B	205	7.343	18.333	62.153	1.00	112.86	B	C
ATOM	3072	CD1	TYR	B	205	8.575	18.553	62.772	1.00	114.06	B	C
ATOM	3073	CE1	TYR	B	205	9.751	18.026	62.250	1.00	116.83	B	C
ATOM	3074	CZ	TYR	B	205	9.705	17.260	61.091	1.00	118.54	B	C
ATOM	3075	OH	TYR	B	205	10.874	16.739	60.576	1.00	120.05	B	O
ATOM	3076	CE2	TYR	B	205	8.492	17.021	60.453	1.00	116.68	B	C
ATOM	3077	CD2	TYR	B	205	7.322	17.551	60.989	1.00	114.93	B	C
ATOM	3078	C	TYR	B	205	4.341	17.935	61.217	1.00	112.90	B	C
ATOM	3079	O	TYR	B	205	4.270	16.905	61.896	1.00	115.51	B	O
ATOM	3080	N	PHE	B	206	3.919	18.008	59.961	1.00	117.30	B	N
ATOM	3081	CA	PHE	B	206	3.410	16.828	59.285	1.00	121.57	B	C
ATOM	3082	CB	PHE	B	206	2.037	17.095	58.643	1.00	123.14	B	C
ATOM	3083	CG	PHE	B	206	1.039	15.987	58.866	1.00	125.12	B	C
ATOM	3084	CD1	PHE	B	206	−0.091	16.199	59.645	1.00	125.23	B	C
ATOM	3085	CE1	PHE	B	206	−1.021	15.174	59.859	1.00	125.71	B	C
ATOM	3086	CZ	PHE	B	206	−0.813	13.916	59.297	1.00	126.53	B	C
ATOM	3087	CE2	PHE	B	206	0.320	13.686	58.522	1.00	127.26	B	C
ATOM	3088	CD2	PHE	B	206	1.239	14.721	58.311	1.00	126.85	B	C
ATOM	3089	C	PHE	B	206	4.423	16.269	58.276	1.00	122.66	B	C
ATOM	3090	O	PHE	B	206	4.653	16.856	57.213	1.00	124.48	B	O
ATOM	3091	N	PRO	B	207	5.070	15.165	58.637	1.00	121.91	B	N
ATOM	3092	CA	PRO	B	207	5.781	14.346	57.654	1.00	121.85	B	C
ATOM	3093	CB	PRO	B	207	6.900	13.697	58.481	1.00	122.51	B	C
ATOM	3094	CG	PRO	B	207	6.437	13.761	59.928	1.00	122.28	B	C
ATOM	3095	CD	PRO	B	207	5.209	14.630	60.004	1.00	121.65	B	C
ATOM	3096	C	PRO	B	207	4.837	13.279	57.071	1.00	120.05	B	C
ATOM	3097	O	PRO	B	207	3.991	12.766	57.809	1.00	123.06	B	O
ATOM	3098	N	ASP	B	208	4.919	12.989	55.774	1.00	113.77	B	N
ATOM	3099	CA	ASP	B	208	5.694	13.766	54.818	1.00	107.36	B	C
ATOM	3100	CB	ASP	B	208	6.502	12.826	53.907	1.00	109.81	B	C
ATOM	3101	CG	ASP	B	208	7.957	12.657	54.354	1.00	109.55	B	C
ATOM	3102	OD1	ASP	B	208	8.743	13.626	54.253	1.00	109.43	B	O
ATOM	3103	OD2	ASP	B	208	8.413	11.579	54.792	1.00	109.72	B	O
ATOM	3104	C	ASP	B	208	4.712	14.613	53.996	1.00	99.67	B	C
ATOM	3105	O	ASP	B	208	4.823	14.687	52.766	1.00	95.43	B	O
ATOM	3106	N	HIS	B	209	3.752	15.236	54.693	1.00	93.92	B	N
ATOM	3107	CA	HIS	B	209	2.711	16.084	54.078	1.00	87.26	B	C
ATOM	3108	CB	HIS	B	209	1.319	15.433	54.174	1.00	90.82	B	C
ATOM	3109	CG	HIS	B	209	1.304	13.957	53.923	1.00	94.92	B	C
ATOM	3110	ND1	HIS	B	209	1.835	13.386	52.786	1.00	96.15	B	N
ATOM	3111	CE1	HIS	B	209	1.675	12.076	52.837	1.00	99.11	B	C
ATOM	3112	NE2	HIS	B	209	1.053	11.776	53.964	1.00	100.69	B	N
ATOM	3113	CD2	HIS	B	209	0.807	12.936	54.660	1.00	97.75	B	C
ATOM	3114	C	HIS	B	209	2.629	17.493	54.684	1.00	76.18	B	C
ATOM	3115	O	HIS	B	209	1.686	17.796	55.418	1.00	70.71	B	O
ATOM	3116	N	PRO	B	210	3.580	18.372	54.372	1.00	71.36	B	N
ATOM	3117	CA	PRO	B	210	3.530	19.709	54.951	1.00	68.49	B	C
ATOM	3118	CB	PRO	B	210	4.960	20.231	54.763	1.00	67.93	B	C
ATOM	3119	CG	PRO	B	210	5.432	19.566	53.498	1.00	68.51	B	C
ATOM	3120	CD	PRO	B	210	4.711	18.230	53.430	1.00	70.48	B	C
ATOM	3121	C	PRO	B	210	2.541	20.492	54.105	1.00	67.58	B	C
ATOM	3122	O	PRO	B	210	2.049	20.000	53.077	1.00	69.65	B	O
ATOM	3123	N	LEU	B	211	2.231	21.697	54.548	1.00	59.38	B	N
ATOM	3124	CA	LEU	B	211	1.387	22.567	53.776	1.00	45.84	B	C
ATOM	3125	CB	LEU	B	211	0.122	22.858	54.570	1.00	37.57	B	C
ATOM	3126	CG	LEU	B	211	−0.797	21.639	54.710	1.00	36.06	B	C
ATOM	3127	CD1	LEU	B	211	−2.121	22.022	55.306	1.00	41.90	B	C
ATOM	3128	CD2	LEU	B	211	−1.040	20.937	53.389	1.00	34.99	B	C
ATOM	3129	C	LEU	B	211	2.217	23.805	53.467	1.00	45.29	B	C
ATOM	3130	O	LEU	B	211	3.272	23.996	54.054	1.00	51.36	B	O
ATOM	3131	N	HIS	B	212	1.790	24.626	52.523	1.00	41.89	B	N
ATOM	3132	CA	HIS	B	212	2.529	25.838	52.252	1.00	40.20	B	C
ATOM	3133	CB	HIS	B	212	3.059	25.814	50.832	1.00	39.63	B	C
ATOM	3134	CG	HIS	B	212	3.964	24.671	50.553	1.00	37.59	B	C
ATOM	3135	ND1	HIS	B	212	5.163	24.504	51.203	1.00	38.64	B	N
ATOM	3136	CE1	HIS	B	212	5.752	23.408	50.758	1.00	41.59	B	C
ATOM	3137	NE2	HIS	B	212	4.975	22.860	49.842	1.00	42.57	B	N
ATOM	3138	CD2	HIS	B	212	3.847	23.631	49.698	1.00	40.72	B	C
ATOM	3139	C	HIS	B	212	1.644	27.056	52.444	1.00	45.66	B	C
ATOM	3140	O	HIS	B	212	0.419	26.959	52.320	1.00	50.32	B	O
ATOM	3141	N	SER	B	213	2.264	28.203	52.716	1.00	41.75	B	N
ATOM	3142	CA	SER	B	213	1.514	29.429	52.891	1.00	40.69	B	C
ATOM	3143	CB	SER	B	213	2.307	30.392	53.756	1.00	46.44	B	C
ATOM	3144	OG	SER	B	213	1.855	30.299	55.102	1.00	51.16	B	O
ATOM	3145	C	SER	B	213	0.983	30.071	51.585	1.00	39.99	B	C
ATOM	3146	O	SER	B	213	−0.173	30.478	51.532	1.00	41.81	B	O
ATOM	3147	N	ILE	B	214	1.816	30.180	50.553	1.00	38.33	B	N
ATOM	3148	CA	ILE	B	214	1.346	30.452	49.180	1.00	37.83	B	C
ATOM	3149	CB	ILE	B	214	1.530	31.936	48.676	1.00	34.62	B	C
ATOM	3150	CG1	ILE	B	214	2.868	32.534	49.139	1.00	42.04	B	C
ATOM	3151	CD1	ILE	B	214	2.996	32.857	50.671	1.00	49.36	B	C
ATOM	3152	CG2	ILE	B	214	0.270	32.808	48.863	1.00	25.30	B	C
ATOM	3153	C	ILE	B	214	2.169	29.595	48.260	1.00	40.06	B	C
ATOM	3154	O	ILE	B	214	3.331	29.282	48.547	1.00	39.53	B	O
ATOM	3155	N	SER	B	215	1.587	29.283	47.115	1.00	38.26	B	N
ATOM	3156	CA	SER	B	215	2.152	28.297	46.242	1.00	40.18	B	C
ATOM	3157	CB	SER	B	215	1.945	26.909	46.852	1.00	50.01	B	C
ATOM	3158	OG	SER	B	215	0.656	26.796	47.458	1.00	56.98	B	O
ATOM	3159	C	SER	B	215	1.434	28.339	44.923	1.00	40.51	B	C
ATOM	3160	O	SER	B	215	0.294	28.814	44.835	1.00	37.50	B	O
ATOM	3161	N	VAL	B	216	2.110	27.813	43.904	1.00	40.40	B	N
ATOM	3162	CA	VAL	B	216	1.500	27.562	42.607	1.00	37.18	B	C
ATOM	3163	CB	VAL	B	216	2.091	28.423	41.502	1.00	29.19	B	C
ATOM	3164	CG1	VAL	B	216	0.998	29.064	40.731	1.00	32.27	B	C
ATOM	3165	CG2	VAL	B	216	3.027	29.430	42.052	1.00	25.24	B	C
ATOM	3166	C	VAL	B	216	1.780	26.149	42.191	1.00	40.74	B	C
ATOM	3167	O	VAL	B	216	2.950	25.784	41.971	1.00	51.27	B	O
ATOM	3168	N	ARG	B	217	0.733	25.343	42.073	1.00	32.18	B	N
ATOM	3169	CA	ARG	B	217	0.923	24.045	41.450	1.00	29.02	B	C
ATOM	3170	CB	ARG	B	217	0.840	22.871	42.456	1.00	27.36	B	C
ATOM	3171	CG	ARG	B	217	−0.516	22.508	43.036	1.00	26.02	B	C
ATOM	3172	CD	ARG	B	217	−1.169	23.610	43.835	1.00	38.67	B	C
ATOM	3173	NE	ARG	B	217	−0.632	23.876	45.189	1.00	44.65	B	N
ATOM	3174	CZ	ARG	B	217	−0.536	22.985	46.183	1.00	36.92	B	C
ATOM	3175	NH1	ARG	B	217	−0.882	21.719	45.998	1.00	29.77	B	N
ATOM	3176	NH2	ARG	B	217	−0.068	23.368	47.360	1.00	33.63	B	N
ATOM	3177	C	ARG	B	217	−0.036	23.923	40.307	1.00	27.19	B	C
ATOM	3178	O	ARG	B	217	−1.095	24.556	40.329	1.00	30.77	B	O
ATOM	3179	N	ARG	B	218	0.347	23.140	39.300	1.00	24.74	B	N
ATOM	3180	CA	ARG	B	218	−0.562	22.817	38.205	1.00	29.88	B	C
ATOM	3181	CB	ARG	B	218	0.120	23.006	36.872	1.00	26.23	B	C
ATOM	3182	CG	ARG	B	218	1.227	22.044	36.596	1.00	28.59	B	C
ATOM	3183	CD	ARG	B	218	1.831	22.250	35.228	1.00	35.20	B	C
ATOM	3184	NE	ARG	B	218	2.799	21.210	34.902	1.00	43.71	B	N
ATOM	3185	CZ	ARG	B	218	2.482	20.043	34.355	1.00	43.88	B	C
ATOM	3186	NH1	ARG	B	218	1.219	19.765	34.058	1.00	47.77	B	N
ATOM	3187	NH2	ARG	B	218	3.427	19.160	34.090	1.00	37.51	B	N
ATOM	3188	C	ARG	B	218	−1.076	21.393	38.323	1.00	39.55	B	C
ATOM	3189	O	ARG	B	218	−0.468	20.584	39.017	1.00	46.37	B	O
ATOM	3190	N	LEU	B	219	−2.205	21.094	37.671	1.00	44.95	B	N
ATOM	3191	CA	LEU	B	219	−2.702	19.714	37.544	1.00	43.41	B	C
ATOM	3192	CB	LEU	B	219	−4.139	19.692	37.017	1.00	44.18	B	C
ATOM	3193	CG	LEU	B	219	−5.316	19.154	37.844	1.00	42.53	B	C
ATOM	3194	CD1	LEU	B	219	−6.467	18.699	36.936	1.00	37.24	B	C
ATOM	3195	CD2	LEU	B	219	−4.901	18.032	38.782	1.00	41.80	B	C
ATOM	3196	C	LEU	B	219	−1.821	18.982	36.552	1.00	42.76	B	C
ATOM	3197	O	LEU	B	219	−1.108	19.603	35.761	1.00	45.42	B	O
ATOM	3198	N	LYS	B	220	−1.846	17.663	36.593	1.00	41.24	B	N
ATOM	3199	CA	LYS	B	220	−1.169	16.914	35.556	1.00	42.17	B	C
ATOM	3200	CB	LYS	B	220	−0.670	15.590	36.110	1.00	40.03	B	C
ATOM	3201	CG	LYS	B	220	0.472	15.693	37.135	1.00	46.15	B	C
ATOM	3202	CD	LYS	B	220	1.435	14.475	37.057	1.00	53.99	B	C
ATOM	3203	CE	LYS	B	220	2.144	14.165	38.368	1.00	56.43	B	C
ATOM	3204	NZ	LYS	B	220	1.285	13.328	39.285	1.00	62.88	B	N
ATOM	3205	C	LYS	B	220	−2.245	16.717	34.480	1.00	46.84	B	C
ATOM	3206	O	LYS	B	220	−3.448	16.683	34.811	1.00	44.45	B	O
ATOM	3207	N	GLU	B	221	−1.848	16.639	33.204	1.00	43.21	B	N
ATOM	3208	CA	GLU	B	221	−2.829	16.369	32.153	1.00	37.91	B	C
ATOM	3209	CB	GLU	B	221	−2.249	16.485	30.733	1.00	42.50	B	C
ATOM	3210	CG	GLU	B	221	−3.320	16.757	29.669	1.00	51.31	B	C
ATOM	3211	CD	GLU	B	221	−2.817	16.628	28.238	1.00	58.55	B	C
ATOM	3212	OE1	GLU	B	221	−3.634	16.511	27.284	1.00	54.22	B	O
ATOM	3213	OE2	GLU	B	221	−1.588	16.651	28.058	1.00	68.04	B	O
ATOM	3214	C	GLU	B	221	−3.370	14.986	32.386	1.00	37.57	B	C
ATOM	3215	O	GLU	B	221	−4.433	14.627	31.867	1.00	46.72	B	O
ATOM	3216	N	THR	B	222	−2.652	14.194	33.176	1.00	31.96	B	N
ATOM	3217	CA	THR	B	222	−3.203	12.908	33.554	1.00	35.83	B	C
ATOM	3218	CB	THR	B	222	−2.117	11.873	33.864	1.00	40.54	B	C
ATOM	3219	OG1	THR	B	222	−1.116	12.463	34.688	1.00	46.68	B	O
ATOM	3220	CG2	THR	B	222	−1.331	11.529	32.615	1.00	42.02	B	C
ATOM	3221	C	THR	B	222	−4.240	13.027	34.663	1.00	36.10	B	C
ATOM	3222	O	THR	B	222	−4.816	12.036	35.064	1.00	41.48	B	O
ATOM	3223	N	LYS	B	223	−4.495	14.246	35.132	1.00	39.96	B	N
ATOM	3224	CA	LYS	B	223	−5.643	14.546	36.008	1.00	43.76	B	C
ATOM	3225	CB	LYS	B	223	−6.954	14.218	35.298	1.00	41.79	B	C
ATOM	3226	CG	LYS	B	223	−7.411	15.256	34.327	1.00	46.07	B	C
ATOM	3227	CD	LYS	B	223	−8.660	14.790	33.637	1.00	54.35	B	C
ATOM	3228	CE	LYS	B	223	−8.359	14.301	32.244	1.00	62.18	B	C
ATOM	3229	NZ	LYS	B	223	−9.324	14.941	31.302	1.00	74.28	B	N
ATOM	3230	C	LYS	B	223	−5.610	13.827	37.362	1.00	45.88	B	C
ATOM	3231	O	LYS	B	223	−6.627	13.747	38.078	1.00	46.67	B	O
ATOM	3232	N	ASP	B	224	−4.440	13.316	37.711	1.00	42.42	B	N
ATOM	3233	CA	ASP	B	224	−4.335	12.401	38.816	1.00	46.20	B	C
ATOM	3234	CB	ASP	B	224	−3.913	11.035	38.300	1.00	48.69	B	C
ATOM	3235	CG	ASP	B	224	−2.558	11.071	37.675	1.00	53.56	B	C
ATOM	3236	OD1	ASP	B	224	−1.751	10.146	37.880	1.00	57.92	B	O
ATOM	3237	OD2	ASP	B	224	−2.203	12.028	36.972	1.00	59.52	B	O
ATOM	3238	C	ASP	B	224	−3.293	12.916	39.773	1.00	49.82	B	C
ATOM	3239	O	ASP	B	224	−2.750	12.149	40.579	1.00	57.22	B	O
ATOM	3240	N	GLY	B	225	−2.995	14.207	39.682	1.00	45.94	B	N
ATOM	3241	CA	GLY	B	225	−2.039	14.799	40.595	1.00	44.41	B	C
ATOM	3242	C	GLY	B	225	−1.607	16.202	40.257	1.00	41.32	B	C
ATOM	3243	O	GLY	B	225	−1.470	16.567	39.093	1.00	37.54	B	O
ATOM	3244	N	PHE	B	226	−1.405	16.990	41.301	1.00	40.89	B	N
ATOM	3245	CA	PHE	B	226	−0.805	18.301	41.162	1.00	38.23	B	C
ATOM	3246	CB	PHE	B	226	−1.305	19.190	42.285	1.00	34.25	B	C
ATOM	3247	CG	PHE	B	226	−2.770	19.432	42.247	1.00	36.48	B	C
ATOM	3248	CD1	PHE	B	226	−3.645	18.568	42.875	1.00	34.58	B	C
ATOM	3249	CE1	PHE	B	226	−5.027	18.800	42.847	1.00	29.74	B	C
ATOM	3250	CZ	PHE	B	226	−5.532	19.891	42.187	1.00	29.66	B	C
ATOM	3251	CE2	PHE	B	226	−4.677	20.759	41.537	1.00	36.03	B	C
ATOM	3252	CD2	PHE	B	226	−3.292	20.529	41.571	1.00	40.84	B	C
ATOM	3253	C	PHE	B	226	0.724	18.201	41.225	1.00	38.49	B	C
ATOM	3254	O	PHE	B	226	1.272	17.294	41.883	1.00	43.61	B	O
ATOM	3255	N	MET	B	227	1.407	19.129	40.559	1.00	31.84	B	N
ATOM	3256	CA	MET	B	227	2.843	19.247	40.714	1.00	36.84	B	C
ATOM	3257	CB	MET	B	227	3.539	18.522	39.577	1.00	43.03	B	C
ATOM	3258	CG	MET	B	227	3.554	19.217	38.246	1.00	51.35	B	C
ATOM	3259	SD	MET	B	227	4.875	18.500	37.239	1.00	56.42	B	S
ATOM	3260	CE	MET	B	227	4.193	16.873	36.930	1.00	58.19	B	C
ATOM	3261	C	MET	B	227	3.372	20.680	40.906	1.00	40.56	B	C
ATOM	3262	O	MET	B	227	2.886	21.620	40.255	1.00	33.62	B	O
ATOM	3263	N	PHE	B	228	4.344	20.831	41.825	1.00	46.58	B	N
ATOM	3264	CA	PHE	B	228	5.021	22.119	42.060	1.00	47.51	B	C
ATOM	3265	CB	PHE	B	228	5.661	22.216	43.435	1.00	38.62	B	C
ATOM	3266	CG	PHE	B	228	4.692	22.332	44.543	1.00	37.82	B	C
ATOM	3267	CD1	PHE	B	228	4.846	21.567	45.683	1.00	36.64	B	C
ATOM	3268	CE1	PHE	B	228	3.963	21.652	46.709	1.00	41.22	B	C
ATOM	3269	CZ	PHE	B	228	2.888	22.515	46.617	1.00	46.15	B	C
ATOM	3270	CE2	PHE	B	228	2.720	23.294	45.490	1.00	45.56	B	C
ATOM	3271	CD2	PHE	B	228	3.624	23.197	44.456	1.00	42.25	B	C
ATOM	3272	C	PHE	B	228	6.137	22.183	41.075	1.00	56.71	B	C
ATOM	3273	O	PHE	B	228	6.926	21.243	40.998	1.00	58.54	B	O
ATOM	3274	N	LEU	B		229	6.223	23.287	40.337	1.00	62.47	B	N
ATOM	3275	CA	LEU	B	229	7.131	23.335	39.200	1.00	62.53	B	C
ATOM	3276	CB	LEU	B	229	6.693	24.393	38.200	1.00	69.25	B	C
ATOM	3277	CG	LEU	B		229	6.466	23.730	36.843	1.00	73.88	B	C
ATOM	3278	CD1	LEU	B	229	4.989	23.436	36.553	1.00	71.88	B	C
ATOM	3279	CD2	LEU	B	229	7.079	24.585	35.754	1.00	79.85	B	C
ATOM	3280	C	LEU	B	229	8.611	23.448	39.552	1.00	58.82	B	C
ATOM	3281	O	LEU	B		229	9.440	22.852	38.868	1.00	60.51	B	O
ATOM	3282	N	THR	B	230	8.928	24.226	40.590	1.00	54.11	B	N
ATOM	3283	CA	THR	B	230	10.273	24.310	41.166	1.00	56.90	B	C
ATOM	3284	CB	THR	B	230	11.124	25.377	40.502	1.00	56.66	B	C
ATOM	3285	OG1	THR	B	230	10.567	26.667	40.800	1.00	56.72	B	O
ATOM	3286	CG2	THR	B	230	11.095	25.267	38.981	1.00	57.50	B	C
ATOM	3287	C	THR	B	230	10.146	24.708	42.623	1.00	62.33	B	C
ATOM	3288	O	THR	B	230	9.046	25.052	43.066	1.00	64.63	B	O
ATOM	3289	N	ASP	B	231	11.272	24.705	43.352	1.00	62.30	B	N
ATOM	3290	CA	ASP	B	231	11.273	24.977	44.791	1.00	61.19	B	C
ATOM	3291	CB	ASP	B	231	12.584	24.512	45.455	1.00	68.70	B	C
ATOM	3292	CG	ASP	B	231	13.787	25.423	45.145	1.00	77.39	B	C
ATOM	3293	OD1	ASP	B	231	14.765	25.428	45.942	1.00	76.12	B	O
ATOM	3294	OD2	ASP	B	231	13.857	26.155	44.130	1.00	83.28	B	O
ATOM	3295	C	ASP	B	231	10.961	26.441	45.074	1.00	60.67	B	C
ATOM	3296	O	ASP	B	231	10.769	26.845	46.226	1.00	60.08	B	O
ATOM	3297	N	GLN	B	232	10.889	27.225	44.002	1.00	61.02	B	N
ATOM	3298	CA	GLN	B	232	10.543	28.635	44.084	1.00	63.06	B	C
ATOM	3299	CB	GLN	B	232	11.277	29.402	42.991	1.00	70.00	B	C
ATOM	3300	CG	GLN	B	232	12.295	30.405	43.507	1.00	80.47	B	C
ATOM	3301	CD	GLN	B	232	13.141	31.010	42.388	1.00	89.22	B	C
ATOM	3302	OE1	GLN	B	232	12.682	31.123	41.238	1.00	92.67	B	O
ATOM	3303	NE2	GLN	B	232	14.380	31.400	42.719	1.00	91.85	B	N
ATOM	3304	C	GLN	B	232	9.039	28.858	43.954	1.00	59.86	B	C
ATOM	3305	O	GLN	B	232	8.584	29.992	43.855	1.00	65.25	B	O
ATOM	3306	N	SER	B	233	8.271	27.774	43.958	1.00	54.46	B	N
ATOM	3307	CA	SER	B	233	6.841	27.840	43.706	1.00	46.84	B	C
ATOM	3308	CB	SER	B	233	6.379	26.632	42.892	1.00	50.64	B	C
ATOM	3309	OG	SER	B	233	7.127	26.481	41.699	1.00	53.85	B	O
ATOM	3310	C	SER	B	233	6.041	27.900	44.983	1.00	42.79	B	C
ATOM	3311	O	SER	B	233	4.824	27.930	44.933	1.00	46.51	B	O
ATOM	3312	N	TYR	B	234	6.702	27.884	46.131	1.00	40.06	B	N
ATOM	3313	CA	TYR	B	234	6.006	28.200	47.377	1.00	45.71	B	C
ATOM	3314	CB	TYR	B	234	5.705	26.967	48.225	1.00	48.88	B	C
ATOM	3315	CG	TYR	B	234	6.706	25.874	48.058	1.00	51.32	B	C
ATOM	3316	CD1	TYR	B	234	7.882	25.852	48.797	1.00	48.29	B	C
ATOM	3317	CE1	TYR	B	234	8.813	24.826	48.628	1.00	49.61	B	C
ATOM	3318	CZ	TYR	B	234	8.560	23.827	47.707	1.00	52.52	B	C
ATOM	3319	OH	TYR	B	234	9.439	22.802	47.494	1.00	53.66	B	O
ATOM	3320	CE2	TYR	B	234	7.397	23.837	46.964	1.00	57.47	B	C
ATOM	3321	CD2	TYR	B	234	6.479	24.854	47.142	1.00	55.92	B	C
ATOM	3322	C	TYR	B	234	6.832	29.142	48.196	1.00	46.38	B	C
ATOM	3323	O	TYR	B	234	8.058	29.132	48.098	1.00	49.19	B	O
ATOM	3324	N	ILE	B	235	6.145	29.957	48.990	1.00	43.14	B	N
ATOM	3325	CA	ILE	B	235	6.781	30.758	50.019	1.00	44.98	B	C
ATOM	3326	CB	ILE	B	235	6.577	32.254	49.738	1.00	42.96	B	C
ATOM	3327	CG1	ILE	B	235	7.321	32.660	48.458	1.00	41.25	B	C
ATOM	3328	CD1	ILE	B	235	6.708	33.807	47.709	1.00	39.31	B	C
ATOM	3329	CG2	ILE	B	235	6.989	33.094	50.953	1.00	39.46	B	C
ATOM	3330	C	ILE	B	235	6.146	30.368	51.337	1.00	49.83	B	C
ATOM	3331	O	ILE	B	235	4.916	30.407	51.474	1.00	54.64	B	O
ATOM	3332	N	ASP	B	236	6.971	29.990	52.306	1.00	49.31	B	N
ATOM	3333	CA	ASP	B	236	6.438	29.503	53.575	1.00	52.33	B	C
ATOM	3334	CB	ASP	B	236	6.869	28.058	53.785	1.00	57.78	B	C
ATOM	3335	CG	ASP	B	236	5.985	27.079	53.061	1.00	63.72	B	C
ATOM	3336	OD1	ASP	B	236	6.243	25.860	53.159	1.00	66.98	B	O
ATOM	3337	OD2	ASP	B	236	5.008	27.433	52.375	1.00	67.67	B	O
ATOM	3338	C	ASP	B	236	6.856	30.311	54.789	1.00	51.93	B	C
ATOM	3339	O	ASP	B	236	8.025	30.657	54.933	1.00	57.61	B	O
ATOM	3340	N	VAL	B	237	5.908	30.591	55.677	1.00	48.39	B	N
ATOM	3341	CA	VAL	B	237	6.255	31.044	57.029	1.00	45.95	B	C
ATOM	3342	CB	VAL	B	237	5.010	31.037	57.967	1.00	41.63	B	C
ATOM	3343	CG1	VAL	B	237	5.405	31.113	59.418	1.00	35.80	B	C
ATOM	3344	CG2	VAL	B	237	4.094	32.180	57.629	1.00	41.77	B	C
ATOM	3345	C	VAL	B	237	7.380	30.148	57.596	1.00	44.14	B	C
ATOM	3346	O	VAL	B	237	7.327	28.918	57.478	1.00	42.65	B	O
ATOM	3347	N	LEU	B	238	8.407	30.769	58.172	1.00	42.83	B	N
ATOM	3348	CA	LEU	B	238	9.515	30.015	58.751	1.00	43.08	B	C
ATOM	3349	CB	LEU	B	238	10.627	30.946	59.237	1.00	40.25	B	C
ATOM	3350	CG	LEU	B	238	11.641	31.454	58.215	1.00	41.13	B	C
ATOM	3351	CD1	LEU	B	238	12.642	32.352	58.880	1.00	40.12	B	C
ATOM	3352	CD2	LEU	B	238	12.369	30.309	57.517	1.00	45.90	B	C
ATOM	3353	C	LEU	B	238	9.026	29.143	59.902	1.00	46.38	B	C
ATOM	3354	O	LEU	B	238	8.185	29.575	60.692	1.00	51.15	B	O
ATOM	3355	N	PRO	B	239	9.538	27.917	59.988	1.00	46.41	B	N
ATOM	3356	CA	PRO	B	239	9.187	26.993	61.070	1.00	48.37	B	C
ATOM	3357	CB	PRO	B	239	10.328	25.986	61.028	1.00	47.70	B	C
ATOM	3358	CG	PRO	B	239	10.751	25.957	59.600	1.00	44.52	B	C
ATOM	3359	CD	PRO	B	239	10.486	27.307	59.039	1.00	45.44	B	C
ATOM	3360	C	PRO	B	239	9.108	27.648	62.457	1.00	51.15	B	C
ATOM	3361	O	PRO	B	239	8.221	27.305	63.234	1.00	51.28	B	O
ATOM	3362	N	GLU	B	240	10.006	28.586	62.741	1.00	54.22	B	N
ATOM	3363	CA	GLU	B	240	10.055	29.271	64.035	1.00	59.88	B	C
ATOM	3364	CB	GLU	B	240	11.323	30.137	64.140	1.00	67.63	B	C
ATOM	3365	CG	GLU	B	240	12.212	30.100	62.893	1.00	73.77	B	C
ATOM	3366	CD	GLU	B	240	13.507	30.897	63.023	1.00	76.92	B	C
ATOM	3367	OE1	GLU	B	240	13.725	31.559	64.076	1.00	78.28	B	O
ATOM	3368	OE2	GLU	B	240	14.308	30.854	62.054	1.00	75.94	B	O
ATOM	3369	C	GLU	B	240	8.813	30.117	64.334	1.00	57.36	B	C
ATOM	3370	O	GLU	B	240	8.355	30.166	65.481	1.00	57.03	B	O
ATOM	3371	N	PHE	B	241	8.276	30.773	63.306	1.00	53.58	B	N
ATOM	3372	CA	PHE	B	241	7.129	31.678	63.472	1.00	52.07	B	C
ATOM	3373	CB	PHE	B	241	7.345	32.976	62.693	1.00	52.16	B	C
ATOM	3374	CG	PHE	B	241	8.762	33.443	62.690	1.00	52.22	B	C
ATOM	3375	CD1	PHE	B	241	9.564	33.243	61.581	1.00	50.50	B	C
ATOM	3376	CE1	PHE	B	241	10.875	33.671	61.569	1.00	51.40	B	C
ATOM	3377	CZ	PHE	B	241	11.410	34.298	62.679	1.00	54.59	B	C
ATOM	3378	CE2	PHE	B	241	10.620	34.500	63.804	1.00	55.99	B	C
ATOM	3379	CD2	PHE	B	241	9.300	34.071	63.803	1.00	54.67	B	C
ATOM	3380	C	PHE	B	241	5.787	31.062	63.090	1.00	48.67	B	C
ATOM	3381	O	PHE	B	241	4.731	31.679	63.293	1.00	45.77	B	O
ATOM	3382	N	ARG	B	242	5.852	29.844	62.550	1.00	48.21	B	N
ATOM	3383	CA	ARG	B	242	4.694	29.048	62.135	1.00	50.12	B	C
ATOM	3384	CB	ARG	B	242	5.146	27.617	61.852	1.00	49.18	B	C
ATOM	3385	CG	ARG	B	242	4.870	27.113	60.463	1.00	48.17	B	C
ATOM	3386	CD	ARG	B	242	5.936	26.151	59.964	1.00	48.47	B	C
ATOM	3387	NE	ARG	B	242	6.231	26.331	58.546	1.00	47.70	B	N
ATOM	3388	CZ	ARG	B	242	7.220	25.726	57.902	1.00	49.41	B	C
ATOM	3389	NH1	ARG	B	242	8.036	24.893	58.542	1.00	48.09	B	N
ATOM	3390	NH2	ARG	B	242	7.397	25.956	56.608	1.00	51.25	B	N
ATOM	3391	C	ARG	B	242	3.557	29.021	63.158	1.00	52.31	B	C
ATOM	3392	O	ARG	B	242	2.426	28.663	62.831	1.00	55.05	B	O
ATOM	3393	N	ASP	B	243	3.876	29.382	64.394	1.00	53.59	B	N
ATOM	3394	CA	ASP	B	243	2.893	29.471	65.458	1.00	56.95	B	C
ATOM	3395	CB	ASP	B	243	3.286	28.560	66.632	1.00	56.30	B	C
ATOM	3396	CG	ASP	B	243	2.700	27.157	66.520	1.00	55.00	B	C
ATOM	3397	OD1	ASP	B	243	1.457	27.031	66.439	1.00	56.52	B	O
ATOM	3398	OD2	ASP	B	243	3.403	26.122	66.525	1.00	51.18	B	O
ATOM	3399	C	ASP	B	243	2.789	30.924	65.914	1.00	59.72	B	C
ATOM	3400	O	ASP	B	243	1.684	31.461	65.989	1.00	55.22	B	O
ATOM	3401	N	SER	B	244	3.951	31.541	66.185	1.00	66.19	B	N
ATOM	3402	CA	SER	B	244	4.089	32.898	66.761	1.00	68.87	B	C
ATOM	3403	CB	SER	B	244	5.300	33.633	66.167	1.00	70.26	B	C
ATOM	3404	OG	SER	B	244	6.500	32.916	66.410	1.00	70.08	B	O
ATOM	3405	C	SER	B	244	2.821	33.713	66.583	1.00	67.72	B	C
ATOM	3406	O	SER	B	244	2.127	34.020	67.556	1.00	72.14	B	O
ATOM	3407	N	TYR	B	245	2.545	34.082	65.340	1.00	62.87	B	N
ATOM	3408	CA	TYR	B	245	1.158	34.146	64.880	1.00	62.23	B	C
ATOM	3409	CB	TYR	B	245	0.174	34.918	65.820	1.00	64.16	B	C
ATOM	3410	CG	TYR	B	245	0.485	36.342	66.238	1.00	65.78	B	C
ATOM	3411	CD1	TYR	B	245	0.083	36.798	67.486	1.00	67.36	B	C
ATOM	3412	CE1	TYR	B	245	0.324	38.092	67.881	1.00	70.36	B	C
ATOM	3413	CZ	TYR	B	245	0.962	38.960	67.014	1.00	71.24	B	C
ATOM	3414	OH	TYR	B	245	1.202	40.246	67.422	1.00	75.50	B	O
ATOM	3415	CE2	TYR	B	245	1.356	38.549	65.758	1.00	67.14	B	C
ATOM	3416	CD2	TYR	B	245	1.112	37.247	65.376	1.00	67.51	B	C
ATOM	3417	C	TYR	B	245	0.912	34.247	63.344	1.00	54.35	B	C
ATOM	3418	O	TYR	B	245	1.823	34.500	62.555	1.00	51.13	B	O
ATOM	3419	N	PRO	B	246	−0.313	33.978	62.933	1.00	46.72	B	N
ATOM	3420	CA	PRO	B	246	−0.530	33.443	61.613	1.00	47.43	B	C
ATOM	3421	CB	PRO	B	246	−1.565	32.361	61.902	1.00	50.33	B	C
ATOM	3422	CG	PRO	B	246	−2.277	32.831	63.208	1.00	46.80	B	C
ATOM	3423	CD	PRO	B	246	−1.590	34.091	63.654	1.00	46.95	B	C
ATOM	3424	C	PRO	B	246	−1.074	34.470	60.626	1.00	46.80	B	C
ATOM	3425	O	PRO	B	246	−1.158	35.675	60.968	1.00	47.31	B	O
ATOM	3426	N	ILE	B	247	−1.436	33.959	59.436	1.00	38.47	B	N
ATOM	3427	CA	ILE	B	247	−1.840	34.741	58.278	1.00	36.07	B	C
ATOM	3428	CB	ILE	B	247	−0.774	34.623	57.179	1.00	35.40	B	C
ATOM	3429	CG1	ILE	B	247	0.612	34.986	57.710	1.00	34.70	B	C
ATOM	3430	CD1	ILE	B	247	1.738	34.674	56.747	1.00	36.11	B	C
ATOM	3431	CG2	ILE	B	247	−1.127	35.506	55.990	1.00	37.67	B	C
ATOM	3432	C	ILE	B	247	−3.187	34.279	57.717	1.00	39.08	B	C
ATOM	3433	O	ILE	B	247	−3.243	33.338	56.941	1.00	42.52	B	O
ATOM	3434	N	LYS	B	248	−4.269	34.949	58.097	1.00	41.51	B	N
ATOM	3435	CA	LYS	B	248	−5.576	34.640	57.539	1.00	47.33	B	C
ATOM	3436	CB	LYS	B	248	−6.707	35.325	58.344	1.00	54.93	B	C
ATOM	3437	CG	LYS	B	248	−7.774	34.372	58.969	1.00	62.42	B	C
ATOM	3438	CD	LYS	B	248	−7.130	33.130	59.696	1.00	65.56	B	C
ATOM	3439	CE	LYS	B	248	−7.609	32.961	61.161	1.00	67.44	B	C
ATOM	3440	NZ	LYS	B	248	−6.536	33.198	62.185	1.00	66.17	B	N
ATOM	3441	C	LYS	B	248	−5.594	35.099	56.086	1.00	47.12	B	C
ATOM	3442	O	LYS	B	248	−5.103	36.186	55.770	1.00	50.24	B	O
ATOM	3443	N	TYR	B	249	−6.146	34.271	55.204	1.00	44.18	B	N
ATOM	3444	CA	TYR	B	249	−6.320	34.666	53.807	1.00	41.12	B	C
ATOM	3445	CB	TYR	B	249	−5.694	33.610	52.873	1.00	39.51	B	C
ATOM	3446	CG	TYR	B	249	−4.179	33.494	53.061	1.00	39.99	B	C
ATOM	3447	CD1	TYR	B	249	−3.623	32.520	53.899	1.00	39.32	B	C
ATOM	3448	CE1	TYR	B	249	−2.252	32.420	54.084	1.00	37.22	B	C
ATOM	3449	CZ	TYR	B	249	−1.414	33.310	53.445	1.00	40.31	B	C
ATOM	3450	OH	TYR	B	249	−0.041	33.235	53.623	1.00	39.21	B	O
ATOM	3451	CE2	TYR	B	249	−1.944	34.294	52.624	1.00	40.32	B	C
ATOM	3452	CD2	TYR	B	249	−3.313	34.377	52.433	1.00	38.21	B	C
ATOM	3453	C	TYR	B	249	−7.797	34.965	53.497	1.00	41.07	B	C
ATOM	3454	O	TYR	B	249	−8.624	34.065	53.431	1.00	46.67	B	O
ATOM	3455	N	VAL	B	250	−8.132	36.237	53.330	1.00	40.04	B	N
ATOM	3456	CA	VAL	B	250	−9.531	36.646	53.156	1.00	41.00	B	C
ATOM	3457	CB	VAL	B	250	−9.740	38.102	53.563	1.00	39.09	B	C
ATOM	3458	CG1	VAL	B	250	−11.214	38.394	53.745	1.00	39.71	B	C
ATOM	3459	CG2	VAL	B	250	−9.000	38.388	54.839	1.00	44.78	B	C
ATOM	3460	C	VAL	B	250	−10.049	36.496	51.726	1.00	42.79	B	C
ATOM	3461	O	VAL	B	250	−11.206	36.126	51.501	1.00	44.52	B	O
ATOM	3462	N	HIS	B	251	−9.199	36.804	50.760	1.00	40.74	B	N
ATOM	3463	CA	HIS	B	251	−9.636	36.852	49.386	1.00	41.24	B	C
ATOM	3464	CB	HIS	B	251	−10.375	38.164	49.135	1.00	41.80	B	C
ATOM	3465	CG	HIS	B	251	−11.170	38.176	47.874	1.00	43.37	B	C
ATOM	3466	ND1	HIS	B	251	−11.037	39.164	46.925	1.00	46.38	B	N
ATOM	3467	CE1	HIS	B	251	−11.859	38.925	45.919	1.00	50.12	B	C
ATOM	3468	NE2	HIS	B	251	−12.518	37.812	46.183	1.00	52.95	B	N
ATOM	3469	CD2	HIS	B	251	−12.103	37.322	47.398	1.00	47.36	B	C
ATOM	3470	C	HIS	B	251	−8.459	36.747	48.444	1.00	42.18	B	C
ATOM	3471	O	HIS	B	251	−7.345	37.159	48.776	1.00	40.54	B	O
ATOM	3472	N	ALA	B	252	−8.713	36.184	47.268	1.00	42.50	B	N
ATOM	3473	CA	ALA	B	252	−7.744	36.220	46.184	1.00	39.62	B	C
ATOM	3474	CB	ALA	B	252	−6.959	34.920	46.122	1.00	34.04	B	C
ATOM	3475	C	ALA	B	252	−8.460	36.489	44.872	1.00	38.17	B	C
ATOM	3476	O	ALA	B	252	−9.628	36.158	44.727	1.00	40.85	B	O
ATOM	3477	N	PHE	B	253	−7.758	37.102	43.927	1.00	37.56	B	N
ATOM	3478	CA	PHE	B	253	−8.280	37.319	42.583	1.00	37.97	B	C
ATOM	3479	CB	PHE	B	253	−9.274	38.467	42.593	1.00	39.09	B	C
ATOM	3480	CG	PHE	B	253	−8.661	39.775	42.991	1.00	37.16	B	C
ATOM	3481	CD1	PHE	B	253	−8.132	40.634	42.024	1.00	35.82	B	C
ATOM	3482	CE1	PHE	B	253	−7.548	41.831	42.382	1.00	34.32	B	C
ATOM	3483	CZ	PHE	B	253	−7.481	42.184	43.711	1.00	35.35	B	C
ATOM	3484	CE2	PHE	B	253	−8.002	41.333	44.688	1.00	35.47	B	C
ATOM	3485	CD2	PHE	B	253	−8.585	40.137	44.325	1.00	35.03	B	C
ATOM	3486	C	PHE	B	253	−7.155	37.627	41.590	1.00	40.06	B	C
ATOM	3487	O	PHE	B	253	−6.099	38.144	41.954	1.00	38.73	B	O
ATOM	3488	N	GLU	B	254	−7.405	37.317	40.329	1.00	44.48	B	N
ATOM	3489	CA	GLU	B	254	−6.440	37.554	39.273	1.00	48.19	B	C
ATOM	3490	CB	GLU	B	254	−6.511	36.392	38.295	1.00	56.38	B	C
ATOM	3491	CG	GLU	B	254	−5.384	36.257	37.277	1.00	60.98	B	C
ATOM	3492	CD	GLU	B	254	−5.461	34.907	36.578	1.00	66.37	B	C
ATOM	3493	OE1	GLU	B	254	−6.409	34.140	36.883	1.00	68.84	B	O
ATOM	3494	OE2	GLU	B	254	−4.587	34.597	35.737	1.00	69.66	B	O
ATOM	3495	C	GLU	B	254	−6.909	38.781	38.573	1.00	44.37	B	C
ATOM	3496	O	GLU	B	254	−8.077	38.886	38.300	1.00	49.37	B	O
ATOM	3497	N	SER	B	255	−6.017	39.711	38.278	1.00	46.27	B	N
ATOM	3498	CA	SER	B	255	−6.357	40.842	37.418	1.00	53.56	B	C
ATOM	3499	CB	SER	B	255	−7.166	41.910	38.164	1.00	52.55	B	C
ATOM	3500	OG	SER	B	255	−6.783	43.221	37.762	1.00	47.80	B	O
ATOM	3501	C	SER	B	255	−5.106	41.472	36.856	1.00	62.94	B	C
ATOM	3502	O	SER	B	255	−4.139	41.714	37.592	1.00	64.63	B	O
ATOM	3503	N	ASN	B	256	−5.146	41.749	35.552	1.00	71.08	B	N
ATOM	3504	CA	ASN	B	256	−4.093	42.499	34.861	1.00	75.79	B	C
ATOM	3505	CB	ASN	B	256	−3.778	43.816	35.594	1.00	82.60	B	C
ATOM	3506	CG	ASN	B	256	−4.344	45.022	34.884	1.00	89.10	B	C
ATOM	3507	OD1	ASN	B	256	−4.107	45.224	33.691	1.00	92.54	B	O
ATOM	3508	ND2	ASN	B	256	−5.106	45.832	35.610	1.00	91.19	B	N
ATOM	3509	C	ASN	B	256	−2.816	41.706	34.685	1.00	70.33	B	C
ATOM	3510	O	ASN	B	256	−1.765	42.279	34.421	1.00	70.32	B	O
ATOM	3511	N	ASN	B	257	−2.916	40.393	34.846	1.00	66.90	B	N
ATOM	3512	CA	ASN	B	257	−1.759	39.509	34.750	1.00	72.76	B	C
ATOM	3513	CB	ASN	B	257	−0.871	39.894	33.564	1.00	82.20	B	C
ATOM	3514	CG	ASN	B	257	−1.003	38.933	32.403	1.00	89.28	B	C
ATOM	3515	OD1	ASN	B	257	−1.889	38.062	32.383	1.00	91.61	B	O
ATOM	3516	ND2	ASN	B	257	−0.113	39.079	31.424	1.00	91.54	B	N
ATOM	3517	C	ASN	B	257	−0.922	39.327	36.029	1.00	66.57	B	C
ATOM	3518	O	ASN	B	257	0.134	38.689	36.001	1.00	65.77	B	O
ATOM	3519	N	PHE	B	258	−1.406	39.874	37.140	1.00	59.48	B	N
ATOM	3520	CA	PHE	B	258	−0.951	39.446	38.457	1.00	53.56	B	C
ATOM	3521	CB	PHE	B	258	−0.515	40.635	39.283	1.00	56.13	B	C
ATOM	3522	CG	PHE	B	258	0.517	41.470	38.623	1.00	62.69	B	C
ATOM	3523	CD1	PHE	B	258	0.176	42.684	38.044	1.00	67.09	B	C
ATOM	3524	CE1	PHE	B	258	1.135	43.480	37.424	1.00	67.82	B	C
ATOM	3525	CZ	PHE	B	258	2.443	43.061	37.384	1.00	68.92	B	C
ATOM	3526	CE2	PHE	B	258	2.798	41.841	37.965	1.00	69.58	B	C
ATOM	3527	CD2	PHE	B	258	1.834	41.055	38.579	1.00	66.62	B	C
ATOM	3528	C	PHE	B	258	−2.018	38.648	39.221	1.00	48.68	B	C
ATOM	3529	O	PHE	B	258	−3.206	38.672	38.896	1.00	48.22	B	O
ATOM	3530	N	ILE	B	259	−1.573	37.912	40.224	1.00	40.91	B	N
ATOM	3531	CA	ILE	B	259	−2.485	37.301	41.153	1.00	39.53	B	C
ATOM	3532	CB	ILE	B	259	−2.055	35.890	41.478	1.00	40.17	B	C
ATOM	3533	CG1	ILE	B	259	−1.652	35.134	40.209	1.00	39.96	B	C
ATOM	3534	CD1	ILE	B	259	−2.786	34.790	39.319	1.00	45.11	B	C
ATOM	3535	CG2	ILE	B	259	−3.134	35.196	42.289	1.00	40.75	B	C
ATOM	3536	C	ILE	B	259	−2.386	38.128	42.408	1.00	44.07	B	C
ATOM	3537	O	ILE	B	259	−1.284	38.523	42.817	1.00	47.98	B	O
ATOM	3538	N	TYR	B	260	−3.533	38.385	43.026	1.00	42.44	B	N
ATOM	3539	CA	TYR	B	260	−3.574	39.155	44.257	1.00	39.09	B	C
ATOM	3540	CB	TYR	B	260	−4.389	40.432	44.059	1.00	38.57	B	C
ATOM	3541	CG	TYR	B	260	−3.826	41.372	43.025	1.00	37.97	B	C
ATOM	3542	CD1	TYR	B	260	−4.002	41.132	41.668	1.00	39.75	B	C
ATOM	3543	CE1	TYR	B	260	−3.479	41.993	40.708	1.00	38.56	B	C
ATOM	3544	CZ	TYR	B	260	−2.785	43.113	41.109	1.00	39.14	B	C
ATOM	3545	OH	TYR	B	260	−2.280	43.967	40.159	1.00	45.15	B	O
ATOM	3546	CE2	TYR	B	260	−2.603	43.378	42.448	1.00	36.98	B	C
ATOM	3547	CD2	TYR	B	260	−3.119	42.503	43.399	1.00	37.90	B	C
ATOM	3548	C	TYR	B	260	−4.162	38.337	45.398	1.00	36.34	B	C
ATOM	3549	O	TYR	B	260	−5.162	37.643	45.234	1.00	35.00	B	O
ATOM	3550	N	PHE	B	261	−3.536	38.421	46.559	1.00	33.91	B	N
ATOM	3551	CA	PHE	B	261	−4.176	37.919	47.754	1.00	34.52	B	C
ATOM	3552	CB	PHE	B	261	−3.360	36.804	48.363	1.00	32.25	B	C
ATOM	3553	CG	PHE	B	261	−3.601	35.472	47.728	1.00	32.31	B	C
ATOM	3554	CD1	PHE	B	261	−3.017	35.153	46.506	1.00	32.46	B	C
ATOM	3555	CE1	PHE	B	261	−3.226	33.916	45.917	1.00	28.63	B	C
ATOM	3556	CZ	PHE	B	261	−4.024	32.996	46.539	1.00	26.50	B	C
ATOM	3557	CE2	PHE	B	261	−4.615	33.299	47.759	1.00	29.46	B	C
ATOM	3558	CD2	PHE	B	261	−4.403	34.532	48.349	1.00	30.29	B	C
ATOM	3559	C	PHE	B	261	−4.442	39.011	48.771	1.00	38.12	B	C
ATOM	3560	O	PHE	B	261	−3.664	39.958	48.914	1.00	39.60	B	O
ATOM	3561	N	LEU	B	262	−5.571	38.883	49.457	1.00	39.87	B	N
ATOM	3562	CA	LEU	B	262	−5.890	39.764	50.566	1.00	40.14	B	C
ATOM	3563	CB	LEU	B	262	−7.258	40.378	50.377	1.00	42.28	B	C
ATOM	3564	CG	LEU	B	262	−7.193	41.526	49.367	1.00	44.27	B	C
ATOM	3565	CD1	LEU	B	262	−8.595	42.027	49.064	1.00	41.80	B	C
ATOM	3566	CD2	LEU	B	262	−6.289	42.667	49.862	1.00	44.80	B	C
ATOM	3567	C	LEU	B	262	−5.759	39.050	51.904	1.00	39.04	B	C
ATOM	3568	O	LEU	B	262	−6.107	37.879	52.049	1.00	37.11	B	O
ATOM	3569	N	THR	B	263	−5.226	39.760	52.883	1.00	40.23	B	N
ATOM	3570	CA	THR	B	263	−4.630	39.078	54.013	1.00	38.36	B	C
ATOM	3571	CB	THR	B	263	−3.201	38.746	53.650	1.00	36.92	B	C
ATOM	3572	OG1	THR	B	263	−2.786	37.650	54.448	1.00	46.37	B	O
ATOM	3573	CG2	THR	B	263	−2.249	39.871	54.055	1.00	32.81	B	C
ATOM	3574	C	THR	B	263	−4.693	39.833	55.338	1.00	38.68	B	C
ATOM	3575	O	THR	B	263	−4.705	41.067	55.356	1.00	42.54	B	O
ATOM	3576	N	VAL	B	264	−4.738	39.092	56.440	1.00	35.16	B	N
ATOM	3577	CA	VAL	B	264	−4.763	39.707	57.768	1.00	37.34	B	C
ATOM	3578	CB	VAL	B	264	−6.172	39.626	58.415	1.00	33.52	B	C
ATOM	3579	CG1	VAL	B	264	−6.117	39.809	59.939	1.00	23.23	B	C
ATOM	3580	CG2	VAL	B	264	−7.112	40.650	57.769	1.00	33.16	B	C
ATOM	3581	C	VAL	B	264	−3.695	39.080	58.654	1.00	41.03	B	C
ATOM	3582	O	VAL	B	264	−3.749	37.883	58.932	1.00	43.04	B	O
ATOM	3583	N	GLN	B	265	−2.724	39.892	59.083	1.00	43.99	B	N
ATOM	3584	CA	GLN	B	265	−1.511	39.378	59.723	1.00	46.02	B	C
ATOM	3585	CB	GLN	B	265	−0.705	38.512	58.739	1.00	45.87	B	C
ATOM	3586	CG	GLN	B	265	−0.727	38.986	57.265	1.00	46.68	B	C
ATOM	3587	CD	GLN	B	265	0.663	39.172	56.658	1.00	47.96	B	C
ATOM	3588	OE1	GLN	B	265	1.650	39.339	57.385	1.00	54.67	B	O
ATOM	3589	NE2	GLN	B	265	0.740	39.157	55.328	1.00	41.34	B	N
ATOM	3590	C	GLN	B	265	−0.573	40.442	60.261	1.00	49.72	B	C
ATOM	3591	O	GLN	B	265	−0.152	41.324	59.517	1.00	49.81	B	O
ATOM	3592	N	ARG	B	266	−0.283	40.345	61.565	1.00	56.89	B	N
ATOM	3593	CA	ARG	B	266	0.990	40.764	62.207	1.00	56.47	B	C
ATOM	3594	CB	ARG	B	266	1.979	39.575	62.168	1.00	58.34	B	C
ATOM	3595	CG	ARG	B	266	2.075	38.835	60.766	1.00	55.22	B	C
ATOM	3596	CD	ARG	B	266	3.450	38.296	60.372	1.00	49.40	B	C
ATOM	3597	NE	ARG	B	266	3.966	37.380	61.392	1.00	47.15	B	N
ATOM	3598	CZ	ARG	B	266	3.725	36.070	61.436	1.00	47.63	B	C
ATOM	3599	NH1	ARG	B	266	2.974	35.488	60.506	1.00	48.62	B	N
ATOM	3600	NH2	ARG	B	266	4.244	35.331	62.415	1.00	45.83	B	N
ATOM	3601	C	ARG	B	266	1.700	41.995	61.636	1.00	56.19	B	C
ATOM	3602	O	ARG	B	266	2.615	41.853	60.819	1.00	60.41	B	O
ATOM	3603	N	GLU	B	267	1.307	43.194	62.055	1.00	52.91	B	N
ATOM	3604	CA	GLU	B	267	1.960	44.403	61.549	1.00	52.98	B	C
ATOM	3605	CB	GLU	B	267	1.706	45.578	62.484	1.00	56.71	B	C
ATOM	3606	CG	GLU	B	267	1.691	46.934	61.805	1.00	58.19	B	C
ATOM	3607	CD	GLU	B	267	0.987	47.961	62.657	1.00	59.65	B	C
ATOM	3608	OE1	GLU	B	267	−0.256	48.072	62.543	1.00	58.53	B	O
ATOM	3609	OE2	GLU	B	267	1.675	48.636	63.456	1.00	61.07	B	O
ATOM	3610	C	GLU	B	267	3.460	44.152	61.410	1.00	51.15	B	C
ATOM	3611	O	GLU	B	267	4.090	44.565	60.435	1.00	46.09	B	O
ATOM	3612	N	THR	B	268	4.005	43.481	62.421	1.00	54.84	B	N
ATOM	3613	CA	THR	B	268	5.303	42.813	62.358	1.00	62.31	B	C
ATOM	3614	CB	THR	B	268	6.458	43.752	62.743	1.00	64.85	B	C
ATOM	3615	OG1	THR	B	268	5.939	44.927	63.383	1.00	65.50	B	O
ATOM	3616	CG2	THR	B	268	7.146	44.279	61.483	1.00	66.37	B	C
ATOM	3617	C	THR	B	268	5.263	41.587	63.275	1.00	64.01	B	C
ATOM	3618	O	THR	B	268	4.324	41.435	64.065	1.00	67.03	B	O
ATOM	3619	N	LEU	B	269	6.259	40.710	63.160	1.00	60.92	B	N
ATOM	3620	CA	LEU	B	269	6.266	39.470	63.929	1.00	60.85	B	C
ATOM	3621	CB	LEU	B	269	7.294	38.473	63.395	1.00	61.11	B	C
ATOM	3622	CG	LEU	B	269	8.696	38.888	62.946	1.00	62.75	B	C
ATOM	3623	CD1	LEU	B	269	9.146	37.935	61.854	1.00	61.57	B	C
ATOM	3624	CD2	LEU	B	269	8.792	40.346	62.475	1.00	63.50	B	C
ATOM	3625	C	LEU	B	269	6.490	39.772	65.397	1.00	63.03	B	C
ATOM	3626	O	LEU	B	269	7.050	40.821	65.733	1.00	65.56	B	O
ATOM	3627	N	ASP	B	270	6.046	38.851	66.256	1.00	64.16	B	N
ATOM	3628	CA	ASP	B	270	5.834	39.100	67.702	1.00	64.38	B	C
ATOM	3629	CB	ASP	B	270	6.965	38.532	68.616	1.00	63.72	B	C
ATOM	3630	CG	ASP	B	270	8.367	39.029	68.250	1.00	61.18	B	C
ATOM	3631	OD1	ASP	B	270	8.591	40.254	68.181	1.00	59.90	B	O
ATOM	3632	OD2	ASP	B	270	9.322	38.249	68.048	1.00	59.89	B	O
ATOM	3633	C	ASP	B	270	5.451	40.538	68.070	1.00	61.42	B	C
ATOM	3634	O	ASP	B	270	5.716	40.999	69.187	1.00	62.01	B	O
ATOM	3635	N	ALA	B	271	4.806	41.225	67.127	1.00	56.80	B	N
ATOM	3636	CA	ALA	B	271	4.461	42.626	67.293	1.00	55.54	B	C
ATOM	3637	CB	ALA	B	271	5.014	43.451	66.146	1.00	53.22	B	C
ATOM	3638	C	ALA	B	271	2.961	42.858	67.467	1.00	56.34	B	C
ATOM	3639	O	ALA	B	271	2.306	43.436	66.599	1.00	55.44	B	O
ATOM	3640	N	GLN	B	272	2.437	42.365	68.590	1.00	58.23	B	N
ATOM	3641	CA	GLN	B	272	1.131	42.749	69.154	1.00	60.29	B	C
ATOM	3642	CB	GLN	B	272	1.311	43.941	70.109	1.00	62.16	B	C
ATOM	3643	CG	GLN	B	272	2.416	43.749	71.142	1.00	66.34	B	C
ATOM	3644	CD	GLN	B	272	1.937	43.049	72.408	1.00	68.87	B	C
ATOM	3645	OE1	GLN	B	272	1.965	43.634	73.500	1.00	67.92	B	O
ATOM	3646	NE2	GLN	B	272	1.506	41.793	72.269	1.00	69.10	B	N
ATOM	3647	C	GLN	B	272	−0.061	43.009	68.206	1.00	58.84	B	C
ATOM	3648	O	GLN	B	272	−1.054	42.277	68.252	1.00	57.37	B	O
ATOM	3649	N	THR	B	273	0.049	44.044	67.368	1.00	57.66	B	N
ATOM	3650	CA	THR	B	273	−1.083	44.609	66.621	1.00	56.42	B	C
ATOM	3651	CB	THR	B	273	−1.024	46.172	66.636	1.00	57.29	B	C
ATOM	3652	OG1	THR	B	273	−1.629	46.695	65.447	1.00	61.32	B	O
ATOM	3653	CG2	THR	B	273	0.415	46.685	66.545	1.00	55.99	B	C
ATOM	3654	C	THR	B	273	−1.246	44.077	65.186	1.00	53.53	B	C
ATOM	3655	O	THR	B	273	−0.263	43.824	64.494	1.00	50.75	B	O
ATOM	3656	N	PHE	B	274	−2.503	43.944	64.751	1.00	52.92	B	N
ATOM	3657	CA	PHE	B	274	−2.839	43.377	63.438	1.00	51.47	B	C
ATOM	3658	CB	PHE	B	274	−3.888	42.275	63.569	1.00	46.97	B	C
ATOM	3659	CG	PHE	B	274	−3.333	40.979	64.073	1.00	42.64	B	C
ATOM	3660	CD1	PHE	B	274	−2.904	40.855	65.390	1.00	39.44	B	C
ATOM	3661	CE1	PHE	B	274	−2.388	39.657	65.869	1.00	37.37	B	C
ATOM	3662	CZ	PHE	B	274	−2.300	38.570	65.043	1.00	37.12	B	C
ATOM	3663	CE2	PHE	B	274	−2.732	38.671	63.717	1.00	42.55	B	C
ATOM	3664	CD2	PHE	B	274	−3.237	39.880	63.237	1.00	42.40	B	C
ATOM	3665	C	PHE	B	274	−3.232	44.419	62.374	1.00	53.87	B	C
ATOM	3666	O	PHE	B	274	−3.213	45.628	62.654	1.00	57.55	B	O
ATOM	3667	N	HIS	B	275	−3.637	43.940	61.189	1.00	49.35	B	N
ATOM	3668	CA	HIS	B	275	−3.129	44.498	59.942	1.00	44.95	B	C
ATOM	3669	CB	HIS	B	275	−1.634	44.213	60.011	1.00	49.77	B	C
ATOM	3670	CG	HIS	B	275	−0.802	44.995	59.060	1.00	54.02	B	C
ATOM	3671	ND1	HIS	B	275	−1.104	46.287	58.691	1.00	56.86	B	N
ATOM	3672	CE1	HIS	B	275	−0.177	46.724	57.857	1.00	59.62	B	C
ATOM	3673	NE2	HIS	B	275	0.712	45.762	57.676	1.00	58.82	B	N
ATOM	3674	CD2	HIS	B	275	0.349	44.673	58.425	1.00	54.88	B	C
ATOM	3675	C	HIS	B	275	−3.663	43.778	58.699	1.00	44.44	B	C
ATOM	3676	O	HIS	B	275	−3.753	42.552	58.678	1.00	44.99	B	O
ATOM	3677	N	THR	B	276	−3.975	44.528	57.644	1.00	42.61	B	N
ATOM	3678	CA	THR	B	276	−4.378	43.933	56.358	1.00	38.29	B	C
ATOM	3679	CB	THR	B	276	−5.746	44.500	55.911	1.00	35.81	B	C
ATOM	3680	OG1	THR	B	276	−6.786	43.962	56.728	1.00	39.39	B	O
ATOM	3681	CG2	THR	B	276	−6.127	44.011	54.527	1.00	34.00	B	C
ATOM	3682	C	THR	B	276	−3.352	44.264	55.286	1.00	39.94	B	C
ATOM	3683	O	THR	B	276	−2.967	45.424	55.157	1.00	45.44	B	O
ATOM	3684	N	ARG	B	277	−2.919	43.277	54.501	1.00	37.62	B	N
ATOM	3685	CA	ARG	B	277	−2.063	43.577	53.346	1.00	38.46	B	C
ATOM	3686	CB	ARG	B	277	−0.673	42.971	53.509	1.00	42.89	B	C
ATOM	3687	CG	ARG	B	277	0.089	43.397	54.743	1.00	48.14	B	C
ATOM	3688	CD	ARG	B	277	0.853	42.246	55.360	1.00	50.64	B	C
ATOM	3689	NE	ARG	B	277	1.732	42.636	56.460	1.00	51.88	B	N
ATOM	3690	CZ	ARG	B	277	2.995	42.246	56.562	1.00	51.75	B	C
ATOM	3691	NH1	ARG	B	277	3.517	41.462	55.618	1.00	50.20	B	N
ATOM	3692	NH2	ARG	B	277	3.735	42.636	57.598	1.00	49.27	B	N
ATOM	3693	C	ARG	B	277	−2.643	43.092	52.025	1.00	39.50	B	C
ATOM	3694	O	ARG	B	277	−3.572	42.278	52.010	1.00	38.59	B	O
ATOM	3695	N	ILE	B	278	−2.107	43.616	50.918	1.00	40.77	B	N
ATOM	3696	CA	ILE	B	278	−2.204	42.931	49.633	1.00	43.35	B	C
ATOM	3697	CB	ILE	B	278	−2.365	43.879	48.429	1.00	46.48	B	C
ATOM	3698	CG1	ILE	B	278	−3.534	44.833	48.611	1.00	53.74	B	C
ATOM	3699	CD1	ILE	B	278	−4.565	44.776	47.457	1.00	56.04	B	C
ATOM	3700	CG2	ILE	B	278	−2.626	43.059	47.159	1.00	45.36	B	C
ATOM	3701	C	ILE	B	278	−0.934	42.125	49.428	1.00	45.96	B	C
ATOM	3702	O	ILE	B	278	0.150	42.505	49.881	1.00	47.89	B	O
ATOM	3703	N	ILE	B	279	−1.086	41.003	48.740	1.00	45.37	B	N
ATOM	3704	CA	ILE	B	279	0.028	40.239	48.243	1.00	42.10	B	C
ATOM	3705	CB	ILE	B	279	−0.010	38.859	48.862	1.00	46.45	B	C
ATOM	3706	CG1	ILE	B	279	0.560	38.922	50.277	1.00	53.46	B	C
ATOM	3707	CD1	ILE	B	279	−0.234	38.137	51.300	1.00	58.89	B	C
ATOM	3708	CG2	ILE	B	279	0.786	37.873	48.043	1.00	48.44	B	C
ATOM	3709	C	ILE	B	279	−0.158	40.180	46.747	1.00	41.15	B	C
ATOM	3710	O	ILE	B	279	−1.258	39.945	46.256	1.00	43.82	B	O
ATOM	3711	N	ARG	B	280	0.910	40.421	46.012	1.00	41.34	B	N
ATOM	3712	CA	ARG	B	280	0.824	40.424	44.563	1.00	45.85	B	C
ATOM	3713	CB	ARG	B	280	0.811	41.869	44.068	1.00	51.26	B	C
ATOM	3714	CG	ARG	B	280	0.662	42.049	42.584	1.00	55.05	B	C
ATOM	3715	CD	ARG	B	280	1.913	42.550	41.938	1.00	60.03	B	C
ATOM	3716	NE	ARG	B	280	1.758	43.887	41.382	1.00	63.67	B	N
ATOM	3717	CZ	ARG	B	280	2.748	44.569	40.814	1.00	69.54	B	C
ATOM	3718	NH1	ARG	B	280	3.970	44.046	40.730	1.00	71.74	B	N
ATOM	3719	NH2	ARG	B	280	2.522	45.780	40.325	1.00	72.83	B	N
ATOM	3720	C	ARG	B	280	2.013	39.666	44.003	1.00	47.40	B	C
ATOM	3721	O	ARG	B	280	3.123	39.783	44.527	1.00	50.74	B	O
ATOM	3722	N	PHE	B	281	1.778	38.855	42.975	1.00	46.60	B	N
ATOM	3723	CA	PHE	B	281	2.872	38.195	42.258	1.00	45.38	B	C
ATOM	3724	CB	PHE	B	281	3.370	36.936	42.965	1.00	39.87	B	C
ATOM	3725	CG	PHE	B	281	2.282	36.035	43.438	1.00	37.45	B	C
ATOM	3726	CD1	PHE	B	281	1.625	35.184	42.549	1.00	39.49	B	C
ATOM	3727	CE1	PHE	B	281	0.595	34.323	42.983	1.00	37.51	B	C
ATOM	3728	CZ	PHE	B	281	0.229	34.318	44.309	1.00	37.59	B	C
ATOM	3729	CE2	PHE	B	281	0.905	35.157	45.220	1.00	40.03	B	C
ATOM	3730	CD2	PHE	B	281	1.925	36.010	44.776	1.00	36.13	B	C
ATOM	3731	C	PHE	B	281	2.474	37.862	40.845	1.00	49.53	B	C
ATOM	3732	O	PHE	B	281	1.286	37.795	40.527	1.00	47.11	B	O
ATOM	3733	N	CYS	B	282	3.490	37.663	40.011	1.00	56.23	B	N
ATOM	3734	CA	CYS	B	282	3.315	37.412	38.596	1.00	57.99	B	C
ATOM	3735	CB	CYS	B	282	4.663	37.392	37.899	1.00	65.24	B	C
ATOM	3736	SG	CYS	B	282	4.825	38.675	36.652	1.00	78.83	B	S
ATOM	3737	C	CYS	B	282	2.629	36.094	38.412	1.00	59.66	B	C
ATOM	3738	O	CYS	B	282	2.938	35.121	39.097	1.00	60.32	B	O
ATOM	3739	N	SER	B	283	1.681	36.086	37.484	1.00	67.93	B	N
ATOM	3740	CA	SER	B	283	0.865	34.913	37.149	1.00	72.78	B	C
ATOM	3741	CB	SER	B	283	−0.389	35.376	36.361	1.00	70.36	B	C
ATOM	3742	OG	SER	B	283	−1.117	34.287	35.803	1.00	72.53	B	O
ATOM	3743	C	SER	B	283	1.675	33.833	36.380	1.00	73.87	B	C
ATOM	3744	O	SER	B	283	1.633	33.762	35.146	1.00	77.97	B	O
ATOM	3745	N	ILE	B	284	2.430	33.007	37.094	1.00	70.60	B	N
ATOM	3746	CA	ILE	B	284	3.182	31.973	36.404	1.00	76.76	B	C
ATOM	3747	CB	ILE	B	284	4.622	32.445	35.992	1.00	76.61	B	C
ATOM	3748	CG1	ILE	B	284	4.722	33.963	35.880	1.00	75.68	B	C
ATOM	3749	CD1	ILE	B	284	5.398	34.456	34.599	1.00	78.40	B	C
ATOM	3750	CG2	ILE	B	284	5.028	31.806	34.660	1.00	80.65	B	C
ATOM	3751	C	ILE	B	284	3.239	30.618	37.122	1.00	83.89	B	C
ATOM	3752	O	ILE	B	284	3.513	30.530	38.330	1.00	83.74	B	O
ATOM	3753	N	ASN	B	285	2.964	29.574	36.333	1.00	86.69	B	N
ATOM	3754	CA	ASN	B	285	3.291	28.179	36.629	1.00	84.66	B	C
ATOM	3755	CB	ASN	B	285	3.435	27.449	35.306	1.00	87.10	B	C
ATOM	3756	CG	ASN	B	285	2.370	26.442	35.099	1.00	90.93	B	C
ATOM	3757	OD1	ASN	B	285	2.008	25.724	36.025	1.00	88.91	B	O
ATOM	3758	ND2	ASN	B	285	1.835	26.380	33.875	1.00	94.17	B	N
ATOM	3759	C	ASN	B	285	4.614	28.002	37.324	1.00	82.64	B	C
ATOM	3760	O	ASN	B	285	4.709	27.384	38.384	1.00	80.16	B	O
ATOM	3761	N	SER	B	286	5.629	28.566	36.673	1.00	84.00	B	N
ATOM	3762	CA	SER	B	286	7.039	28.312	36.927	1.00	85.66	B	C
ATOM	3763	CB	SER	B	286	7.896	29.115	35.934	1.00	88.63	B	C
ATOM	3764	OG	SER	B	286	7.581	30.505	35.951	1.00	88.36	B	O
ATOM	3765	C	SER	B	286	7.447	28.636	38.349	1.00	85.35	B	C
ATOM	3766	O	SER	B	286	8.517	28.211	38.807	1.00	88.05	B	O
ATOM	3767	N	GLY	B	287	6.595	29.390	39.038	1.00	79.54	B	N
ATOM	3768	CA	GLY	B	287	6.879	29.803	40.398	1.00	74.83	B	C
ATOM	3769	C	GLY	B	287	6.294	31.157	40.722	1.00	70.55	B	C
ATOM	3770	O	GLY	B	287	5.763	31.857	39.847	1.00	72.26	B	O
ATOM	3771	N	LEU	B	288	6.371	31.521	41.995	1.00	62.57	B	N
ATOM	3772	CA	LEU	B	288	5.925	32.830	42.422	1.00	56.34	B	C
ATOM	3773	CB	LEU	B	288	5.698	32.833	43.913	1.00	48.19	B	C
ATOM	3774	CG	LEU	B	288	4.757	31.729	44.318	1.00	44.46	B	C
ATOM	3775	CD1	LEU	B	288	5.230	31.232	45.641	1.00	50.30	B	C
ATOM	3776	CD2	LEU	B	288	3.331	32.254	44.391	1.00	41.40	B	C
ATOM	3777	C	LEU	B	288	7.022	33.798	42.087	1.00	58.68	B	C
ATOM	3778	O	LEU	B	288	8.149	33.631	42.564	1.00	55.28	B	O
ATOM	3779	N	HIS	B	289	6.713	34.806	41.273	1.00	62.56	B	N
ATOM	3780	CA	HIS	B	289	7.792	35.643	40.771	1.00	67.70	B	C
ATOM	3781	CB	HIS	B	289	7.951	35.543	39.242	1.00	69.53	B	C
ATOM	3782	CG	HIS	B	289	8.564	34.241	38.806	1.00	71.32	B	C
ATOM	3783	ND1	HIS	B	289	9.708	33.731	39.383	1.00	70.97	B	N
ATOM	3784	CE1	HIS	B	289	9.993	32.560	38.839	1.00	72.47	B	C
ATOM	3785	NE2	HIS	B	289	9.073	32.288	37.932	1.00	72.64	B	N
ATOM	3786	CD2	HIS	B	289	8.163	33.319	37.896	1.00	73.23	B	C
ATOM	3787	C	HIS	B	289	7.973	37.039	41.376	1.00	70.32	B	C
ATOM	3788	O	HIS	B	289	8.902	37.242	42.179	1.00	78.40	B	O
ATOM	3789	N	SER	B	290	7.142	38.010	41.053	1.00	63.75	B	N
ATOM	3790	CA	SER	B	290	7.478	39.304	41.628	1.00	62.91	B	C
ATOM	3791	CB	SER	B	290	7.361	40.425	40.605	1.00	68.79	B	C
ATOM	3792	OG	SER	B	290	8.626	40.636	40.007	1.00	70.89	B	O
ATOM	3793	C	SER	B	290	6.737	39.585	42.928	1.00	58.08	B	C
ATOM	3794	O	SER	B	290	5.916	40.503	43.015	1.00	63.24	B	O
ATOM	3795	N	TYR	B	291	7.069	38.791	43.941	1.00	47.39	B	N
ATOM	3796	CA	TYR	B	291	6.309	38.736	45.180	1.00	41.83	B	C
ATOM	3797	CB	TYR	B	291	6.660	37.456	45.927	1.00	37.48	B	C
ATOM	3798	CG	TYR	B	291	5.744	37.182	47.084	1.00	36.21	B	C
ATOM	3799	CD1	TYR	B	291	4.686	36.281	46.961	1.00	33.62	B	C
ATOM	3800	CE1	TYR	B	291	3.840	36.030	48.034	1.00	34.80	B	C
ATOM	3801	CZ	TYR	B	291	4.047	36.696	49.248	1.00	36.53	B	C
ATOM	3802	OH	TYR	B	291	3.213	36.478	50.320	1.00	36.69	B	O
ATOM	3803	CE2	TYR	B	291	5.089	37.600	49.387	1.00	36.23	B	C
ATOM	3804	CD2	TYR	B	291	5.927	37.836	48.309	1.00	35.98	B	C
ATOM	3805	C	TYR	B	291	6.536	39.944	46.085	1.00	45.26	B	C
ATOM	3806	O	TYR	B	291	7.676	40.338	46.333	1.00	49.90	B	O
ATOM	3807	N	MET	B	292	5.449	40.532	46.578	1.00	43.80	B	N
ATOM	3808	CA	MET	B	292	5.515	41.703	47.458	1.00	44.36	B	C
ATOM	3809	CB	MET	B	292	5.717	43.014	46.672	1.00	47.97	B	C
ATOM	3810	CG	MET	B	292	6.627	42.930	45.445	1.00	53.67	B	C
ATOM	3811	SD	MET	B	292	6.460	44.262	44.234	1.00	57.70	B	S
ATOM	3812	CE	MET	B	292	7.795	45.383	44.800	1.00	54.66	B	C
ATOM	3813	C	MET	B	292	4.227	41.812	48.250	1.00	44.44	B	C
ATOM	3814	O	MET	B	292	3.139	41.710	47.689	1.00	51.08	B	O
ATOM	3815	N	GLU	B	293	4.333	42.024	49.550	1.00	40.31	B	N
ATOM	3816	CA	GLU	B	293	3.143	42.289	50.339	1.00	38.64	B	C
ATOM	3817	CB	GLU	B	293	3.098	41.424	51.594	1.00	39.59	B	C
ATOM	3818	CG	GLU	B	293	3.923	40.150	51.552	1.00	38.35	B	C
ATOM	3819	CD	GLU	B	293	3.505	39.163	52.627	1.00	38.12	B	C
ATOM	3820	OE1	GLU	B	293	3.526	39.536	53.834	1.00	37.86	B	O
ATOM	3821	OE2	GLU	B	293	3.142	38.021	52.263	1.00	35.21	B	O
ATOM	3822	C	GLU	B	293	3.142	43.747	50.740	1.00	40.30	B	C
ATOM	3823	O	GLU	B	293	4.114	44.233	51.301	1.00	43.67	B	O
ATOM	3824	N	MET	B	294	2.060	44.454	50.460	1.00	39.60	B	N
ATOM	3825	CA	MET	B	294	1.975	45.843	50.866	1.00	41.04	B	C
ATOM	3826	CB	MET	B	294	2.044	46.749	49.639	1.00	44.09	B	C
ATOM	3827	CG	MET	B	294	1.049	47.881	49.546	1.00	48.48	B	C
ATOM	3828	SD	MET	B	294	0.858	48.261	47.786	1.00	56.51	B	S
ATOM	3829	CE	MET	B	294	−0.751	48.941	47.750	1.00	57.49	B	C
ATOM	3830	C	MET	B	294	0.733	46.079	51.708	1.00	43.27	B	C
ATOM	3831	O	MET	B	294	−0.370	45.731	51.289	1.00	48.54	B	O
ATOM	3832	N	PRO	B	295	0.933	46.610	52.917	1.00	42.18	B	N
ATOM	3833	CA	PRO	B	295	−0.154	46.989	53.833	1.00	39.90	B	C
ATOM	3834	CB	PRO	B	295	0.575	47.748	54.935	1.00	38.78	B	C
ATOM	3835	CG	PRO	B	295	1.934	48.002	54.398	1.00	41.92	B	C
ATOM	3836	CD	PRO	B	295	2.252	46.842	53.524	1.00	42.28	B	C
ATOM	3837	C	PRO	B	295	−1.218	47.899	53.233	1.00	40.13	B	C
ATOM	3838	O	PRO	B	295	−0.902	48.692	52.344	1.00	38.20	B	O
ATOM	3839	N	LEU	B	296	−2.451	47.757	53.731	1.00	41.86	B	N
ATOM	3840	CA	LEU	B	296	−3.620	48.548	53.334	1.00	41.65	B	C
ATOM	3841	CB	LEU	B	296	−4.625	47.670	52.598	1.00	36.91	B	C
ATOM	3842	CG	LEU	B	296	−4.347	47.267	51.149	1.00	38.16	B	C
ATOM	3843	CD1	LEU	B	296	−5.656	47.151	50.378	1.00	38.38	B	C
ATOM	3844	CD2	LEU	B	296	−3.432	48.251	50.447	1.00	39.97	B	C
ATOM	3845	C	LEU	B	296	−4.294	49.163	54.569	1.00	48.76	B	C
ATOM	3846	O	LEU	B	296	−4.422	48.509	55.610	1.00	51.59	B	O
ATOM	3847	N	GLU	B	297	−4.725	50.417	54.450	1.00	52.95	B	N
ATOM	3848	CA	GLU	B	297	−5.309	51.155	55.568	1.00	54.84	B	C
ATOM	3849	CB	GLU	B	297	−4.375	52.302	55.978	1.00	57.43	B	C
ATOM	3850	CG	GLU	B	297	−3.502	52.030	57.198	1.00	62.42	B	C
ATOM	3851	CD	GLU	B	297	−2.773	53.269	57.724	1.00	66.04	B	C
ATOM	3852	OE1	GLU	B	297	−3.095	54.411	57.309	1.00	67.50	B	O
ATOM	3853	OE2	GLU	B	297	−1.865	53.102	58.570	1.00	66.40	B	O
ATOM	3854	C	GLU	B	297	−6.669	51.730	55.184	1.00	56.60	B	C
ATOM	3855	O	GLU	B	297	−6.782	52.451	54.188	1.00	57.35	B	O
ATOM	3856	N	CYS	B	298	−7.701	51.403	55.957	1.00	56.57	B	N
ATOM	3857	CA	CYS	B	298	−8.980	52.111	55.851	1.00	55.08	B	C
ATOM	3858	CB	CYS	B	298	−10.152	51.153	55.764	1.00	52.43	B	C
ATOM	3859	SG	CYS	B	298	−11.578	51.921	54.988	1.00	53.14	B	S
ATOM	3860	C	CYS	B	298	−9.179	53.008	57.056	1.00	57.69	B	C
ATOM	3861	O	CYS	B	298	−8.995	52.570	58.186	1.00	59.46	B	O
ATOM	3862	N	ILE	B	299	−9.564	54.258	56.817	1.00	59.66	B	N
ATOM	3863	CA	ILE	B	299	−9.727	55.230	57.899	1.00	59.53	B	C
ATOM	3864	CB	ILE	B	299	−8.511	56.184	57.967	1.00	59.74	B	C
ATOM	3865	CG1	ILE	B	299	−8.095	56.653	56.565	1.00	61.08	B	C
ATOM	3866	CD1	ILE	B	299	−7.489	58.053	56.521	1.00	60.66	B	C
ATOM	3867	CG2	ILE	B	299	−7.354	55.506	58.679	1.00	59.40	B	C
ATOM	3868	C	ILE	B	299	−11.044	56.014	57.851	1.00	62.03	B	C
ATOM	3869	O	ILE	B	299	−11.657	56.170	56.785	1.00	58.16	B	O
ATOM	3870	N	LEU	B	300	−11.459	56.501	59.024	1.00	68.13	B	N
ATOM	3871	CA	LEU	B	300	−12.708	57.258	59.199	1.00	71.33	B	C
ATOM	3872	CB	LEU	B	300	−13.269	57.057	60.616	1.00	70.08	B	C
ATOM	3873	CG	LEU	B		300	−14.760	57.356	60.821	1.00	70.36	B	C
ATOM	3874	CD1	LEU	B	300	−15.630	56.190	60.371	1.00	69.76	B	C
ATOM	3875	CD2	LEU	B	300	−15.061	57.724	62.273	1.00	71.69	B	C
ATOM	3876	C	LEU	B	300	−12.603	58.760	58.883	1.00	73.92	B	C
ATOM	3877	O	LEU	B	300	−13.527	59.322	58.290	1.00	75.89	B	O
ATOM	3878	N	THR	B	301	−11.491	59.391	59.284	1.00	74.85	B	N
ATOM	3879	CA	THR	B	301	−11.243	60.839	59.111	1.00	73.74	B	C
ATOM	3880	CB	THR	B	301	−11.152	61.239	57.600	1.00	73.95	B	C
ATOM	3881	OG1	THR	B	301	−9.890	61.867	57.339	1.00	74.72	B	O
ATOM	3882	CG2	THR	B	301	−12.183	62.316	57.225	1.00	71.77	B	C
ATOM	3883	C	THR	B	301	−12.250	61.708	59.867	1.00	71.57	B	C
ATOM	3884	O	THR	B	301	−12.473	61.512	61.061	1.00	69.93	B	O
ATOM	3885	N	LYS	B	311	−5.981	59.549	63.217	1.00	75.59	B	N
ATOM	3886	CA	LYS	B	311	−6.434	58.536	62.267	1.00	76.17	B	C
ATOM	3887	CB	LYS	B	311	−5.240	57.941	61.505	1.00	78.74	B	C
ATOM	3888	CG	LYS	B	311	−4.699	58.809	60.371	1.00	81.19	B	C
ATOM	3889	CD	LYS	B	311	−3.521	58.136	59.662	1.00	81.72	B	C
ATOM	3890	CE	LYS	B	311	−2.818	59.103	58.711	1.00	81.77	B	C
ATOM	3891	NZ	LYS	B	311	−1.672	58.467	57.997	1.00	80.78	B	N
ATOM	3892	C	LYS	B	311	−7.197	57.416	62.973	1.00	73.12	B	C
ATOM	3893	O	LYS	B	311	−6.675	56.793	63.895	1.00	73.93	B	O
ATOM	3894	N	GLU	B	312	−8.431	57.172	62.546	1.00	70.40	B	N
ATOM	3895	CA	GLU	B	312	−9.203	56.030	63.036	1.00	70.15	B	C
ATOM	3896	CB	GLU	B	312	−10.627	56.461	63.418	1.00	71.10	B	C
ATOM	3897	CG	GLU	B	312	−11.398	55.423	64.225	1.00	72.95	B	C
ATOM	3898	CD	GLU	B	312	−11.576	55.806	65.684	1.00	73.81	B	C
ATOM	3899	OE1	GLU	B	312	−12.398	56.701	65.961	1.00	75.52	B	O
ATOM	3900	OE2	GLU	B	312	−10.907	55.209	66.559	1.00	73.04	B	O
ATOM	3901	C	GLU	B	312	−9.206	54.897	61.989	1.00	69.21	B	C
ATOM	3902	O	GLU	B	312	−9.962	54.938	61.011	1.00	68.31	B	O
ATOM	3903	N	VAL	B	313	−8.363	53.887	62.217	1.00	66.47	B	N
ATOM	3904	CA	VAL	B	313	−8.036	52.878	61.199	1.00	63.03	B	C
ATOM	3905	CB	VAL	B	313	−6.518	52.572	61.167	1.00	64.23	B	C
ATOM	3906	CG1	VAL	B	313	−6.090	52.118	59.787	1.00	65.00	B	C
ATOM	3907	CG2	VAL	B	313	−5.699	53.786	61.602	1.00	66.29	B	C
ATOM	3908	C	VAL	B	313	−8.790	51.558	61.344	1.00	60.30	B	C
ATOM	3909	O	VAL	B	313	−8.998	51.068	62.445	1.00	60.55	B	O
ATOM	3910	N	PHE	B	314	−9.178	50.985	60.211	1.00	60.20	B	N
ATOM	3911	CA	PHE	B	314	−9.881	49.708	60.177	1.00	63.28	B	C
ATOM	3912	CB	PHE	B	314	−11.215	49.846	59.443	1.00	68.40	B	C
ATOM	3913	CG	PHE	B	314	−12.164	50.797	60.111	1.00	72.13	B	C
ATOM	3914	CD1	PHE	B	314	−13.025	50.354	61.110	1.00	73.60	B	C
ATOM	3915	CE1	PHE	B	314	−13.900	51.235	61.743	1.00	73.55	B	C
ATOM	3916	CZ	PHE	B	314	−13.912	52.576	61.382	1.00	73.29	B	C
ATOM	3917	CE2	PHE	B	314	−13.048	53.034	60.393	1.00	73.17	B	C
ATOM	3918	CD2	PHE	B	314	−12.180	52.143	59.762	1.00	73.47	B	C
ATOM	3919	C	PHE	B	314	−8.980	48.623	59.585	1.00	62.17	B	C
ATOM	3920	O	PHE	B	314	−8.934	48.370	58.372	1.00	60.61	B	O
ATOM	3921	N	ASN	B	315	−8.262	47.985	60.492	1.00	60.37	B	N
ATOM	3922	CA	ASN	B	315	−7.112	47.181	60.146	1.00	59.51	B	C
ATOM	3923	CB	ASN	B	315	−6.130	47.235	61.306	1.00	59.70	B	C
ATOM	3924	CG	ASN	B	315	−6.766	46.820	62.609	1.00	59.13	B	C
ATOM	3925	OD1	ASN	B	315	−7.854	47.282	62.958	1.00	56.72	B	O
ATOM	3926	ND2	ASN	B	315	−6.102	45.925	63.328	1.00	61.68	B	N
ATOM	3927	C	ASN	B	315	−7.452	45.734	59.832	1.00	56.95	B	C
ATOM	3928	O	ASN	B	315	−6.575	44.968	59.423	1.00	57.41	B	O
ATOM	3929	N	ILE	B	316	−8.709	45.351	60.041	1.00	52.39	B	N
ATOM	3930	CA	ILE	B	316	−9.113	43.981	59.749	1.00	49.80	B	C
ATOM	3931	CB	ILE	B	316	−9.503	43.217	61.022	1.00	48.77	B	C
ATOM	3932	CG1	ILE	B	316	−8.296	43.127	61.947	1.00	49.54	B	C
ATOM	3933	CD1	ILE	B	316	−8.646	43.083	63.388	1.00	52.82	B	C
ATOM	3934	CG2	ILE	B	316	−9.924	41.790	60.676	1.00	51.23	B	C
ATOM	3935	C	ILE	B	316	−10.167	43.864	58.642	1.00	48.52	B	C
ATOM	3936	O	ILE	B	316	−11.376	44.011	58.879	1.00	50.06	B	O
ATOM	3937	N	LEU	B	317	−9.666	43.604	57.434	1.00	42.09	B	N
ATOM	3938	CA	LEU	B	317	−10.481	43.320	56.270	1.00	34.53	B	C
ATOM	3939	CB	LEU	B	317	−9.591	43.078	55.073	1.00	30.31	B	C
ATOM	3940	CG	LEU	B	317	−10.287	42.652	53.796	1.00	32.72	B	C
ATOM	3941	CD1	LEU	B	317	−10.778	43.860	53.020	1.00	33.80	B	C
ATOM	3942	CD2	LEU	B	317	−9.311	41.873	52.979	1.00	36.29	B	C
ATOM	3943	C	LEU	B	317	−11.340	42.102	56.533	1.00	36.99	B	C
ATOM	3944	O	LEU	B	317	−10.852	41.085	57.040	1.00	37.81	B	O
ATOM	3945	N	GLN	B	318	−12.622	42.232	56.190	1.00	39.38	B	N
ATOM	3946	CA	GLN	B	318	−13.667	41.275	56.559	1.00	38.34	B	C
ATOM	3947	CB	GLN	B	318	−14.842	42.008	57.198	1.00	35.95	B	C
ATOM	3948	CG	GLN	B	318	−14.550	42.550	58.560	1.00	34.95	B	C
ATOM	3949	CD	GLN	B	318	−14.256	41.448	59.549	1.00	34.71	B	C
ATOM	3950	OE1	GLN	B	318	−14.998	40.466	59.635	1.00	32.68	B	O
ATOM	3951	NE2	GLN	B	318	−13.169	41.598	60.290	1.00	35.89	B	N
ATOM	3952	C	GLN	B	318	−14.191	40.515	55.366	1.00	39.89	B	C
ATOM	3953	O	GLN	B	318	−14.563	39.350	55.482	1.00	43.86	B	O
ATOM	3954	N	ALA	B	319	−14.264	41.208	54.237	1.00	38.76	B	N
ATOM	3955	CA	ALA	B	319	−14.702	40.634	52.980	1.00	42.20	B	C
ATOM	3956	CB	ALA	B	319	−16.206	40.436	52.970	1.00	43.13	B	C
ATOM	3957	C	ALA	B	319	−14.296	41.631	51.919	1.00	45.19	B	C
ATOM	3958	O	ALA	B	319	−13.906	42.754	52.259	1.00	47.84	B	O
ATOM	3959	N	ALA	B	320	−14.397	41.224	50.648	1.00	43.30	B	N
ATOM	3960	CA	ALA	B	320	−14.019	42.068	49.516	1.00	38.82	B	C
ATOM	3961	CB	ALA	B	320	−12.515	42.188	49.442	1.00	39.16	B	C
ATOM	3962	C	ALA	B	320	−14.545	41.508	48.215	1.00	37.73	B	C
ATOM	3963	O	ALA	B	320	−14.533	40.290	48.028	1.00	42.20	B	O
ATOM	3964	N	ALA	B	321	−15.032	42.390	47.340	1.00	36.21	B	N
ATOM	3965	CA	ALA	B	321	−15.285	42.055	45.930	1.00	38.81	B	C
ATOM	3966	CB	ALA	B	321	−16.828	42.041	45.531	1.00	33.42	B	C
ATOM	3967	C	ALA	B	321	−14.496	42.994	45.032	1.00	41.25	B	C
ATOM	3968	O	ALA	B	321	−14.039	44.063	45.472	1.00	41.88	B	O
ATOM	3969	N	VAL	B	322	−14.346	42.573	43.775	1.00	42.72	B	N
ATOM	3970	CA	VAL	B	322	−13.604	43.306	42.759	1.00	43.41	B	C
ATOM	3971	CB	VAL	B	322	−12.337	42.565	42.360	1.00	45.20	B	C
ATOM	3972	CG1	VAL	B	322	−11.598	43.339	41.310	1.00	45.05	B	C
ATOM	3973	CG2	VAL	B	322	−11.448	42.329	43.572	1.00	49.72	B	C
ATOM	3974	C	VAL	B	322	−14.475	43.471	41.527	1.00	43.73	B	C
ATOM	3975	O	VAL	B	322	−14.951	42.514	40.965	1.00	47.79	B	O
ATOM	3976	N	SER	B	323	−14.695	44.699	41.105	1.00	47.05	B	N
ATOM	3977	CA	SER	B	323	−15.589	44.931	39.988	1.00	48.01	B	C
ATOM	3978	CB	SER	B	323	−17.061	44.989	40.444	1.00	47.16	B	C
ATOM	3979	OG	SER	B	323	−17.377	46.210	41.095	1.00	42.34	B	O
ATOM	3980	C	SER	B	323	−15.197	46.216	39.309	1.00	49.32	B	C
ATOM	3981	O	SER	B	323	−14.264	46.924	39.744	1.00	50.83	B	O
ATOM	3982	N	LYS	B	324	−15.914	46.509	38.234	1.00	42.95	B	N
ATOM	3983	CA	LYS	B	324	−15.702	47.733	37.528	1.00	39.54	B	C
ATOM	3984	CB	LYS	B	324	−16.078	47.489	36.082	1.00	45.40	B	C
ATOM	3985	CG	LYS	B	324	−14.884	47.335	35.169	1.00	47.01	B	C
ATOM	3986	CD	LYS	B	324	−14.282	45.960	35.203	1.00	47.97	B	C
ATOM	3987	CE	LYS	B	324	−12.862	46.016	34.666	1.00	52.58	B	C
ATOM	3988	NZ	LYS	B	324	−12.750	45.426	33.300	1.00	58.24	B	N
ATOM	3989	C	LYS	B	324	−16.589	48.768	38.212	1.00	37.81	B	C
ATOM	3990	O	LYS	B	324	−17.543	48.390	38.883	1.00	37.79	B	O
ATOM	3991	N	PRO	B	325	−16.269	50.054	38.103	1.00	39.23	B	N
ATOM	3992	CA	PRO	B	325	−17.136	51.106	38.648	1.00	42.38	B	C
ATOM	3993	CB	PRO	B	325	−16.155	52.250	38.890	1.00	39.95	B	C
ATOM	3994	CG	PRO	B	325	−15.199	52.131	37.747	1.00	40.77	B	C
ATOM	3995	CD	PRO	B	325	−15.064	50.629	37.479	1.00	41.47	B	C
ATOM	3996	C	PRO	B	325	−18.209	51.583	37.659	1.00	45.95	B	C
ATOM	3997	O	PRO	B	325	−18.120	51.312	36.448	1.00	49.67	B	O
ATOM	3998	N	GLY	B	326	−19.212	52.280	38.186	1.00	45.56	B	N
ATOM	3999	CA	GLY	B	326	−20.128	53.056	37.369	1.00	49.09	B	C
ATOM	4000	C	GLY	B	326	−19.605	54.476	37.241	1.00	48.35	B	C
ATOM	4001	O	GLY	B	326	−18.752	54.890	38.030	1.00	50.25	B	O
ATOM	4002	N	ALA	B	327	−20.119	55.227	36.272	1.00	43.52	B	N
ATOM	4003	CA	ALA	B	327	−19.586	56.559	35.995	1.00	45.27	B	C
ATOM	4004	CB	ALA	B	327	−20.368	57.232	34.898	1.00	49.23	B	C
ATOM	4005	C	ALA	B	327	−19.471	57.483	37.206	1.00	47.02	B	C
ATOM	4006	O	ALA	B	327	−18.439	58.129	37.373	1.00	49.70	B	O
ATOM	4007	N	GLN	B	328	−20.516	57.556	38.036	1.00	48.51	B	N
ATOM	4008	CA	GLN	B	328	−20.528	58.471	39.191	1.00	48.61	B	C
ATOM	4009	CB	GLN	B	328	−21.844	58.407	39.989	1.00	52.15	B	C
ATOM	4010	CG	GLN	B	328	−22.154	59.689	40.799	1.00	56.98	B	C
ATOM	4011	CD	GLN	B	328	−23.030	59.450	42.035	1.00	61.65	B	C
ATOM	4012	OE1	GLN	B	328	−22.527	59.373	43.161	1.00	63.61	B	O
ATOM	4013	NE2	GLN	B	328	−24.340	59.356	41.826	1.00	63.51	B	N
ATOM	4014	C	GLN	B	328	−19.351	58.186	40.100	1.00	47.42	B	C
ATOM	4015	O	GLN	B	328	−18.495	59.053	40.318	1.00	44.44	B	O
ATOM	4016	N	LEU	B	329	−19.294	56.958	40.608	1.00	48.25	B	N
ATOM	4017	CA	LEU	B	329	−18.167	56.568	41.431	1.00	47.42	B	C
ATOM	4018	CB	LEU	B	329	−18.294	55.129	41.906	1.00	46.47	B	C
ATOM	4019	CG	LEU	B	329	−17.867	54.835	43.349	1.00	43.93	B	C
ATOM	4020	CD1	LEU	B	329	−17.375	53.404	43.422	1.00	42.68	B	C
ATOM	4021	CD2	LEU	B	329	−16.826	55.809	43.905	1.00	39.29	B	C
ATOM	4022	C	LEU	B	329	−16.867	56.748	40.668	1.00	47.05	B	C
ATOM	4023	O	LEU	B	329	−15.892	57.231	41.236	1.00	49.30	B	O
ATOM	4024	N	ALA	B	330	−16.866	56.380	39.386	1.00	43.69	B	N
ATOM	4025	CA	ALA	B	330	−15.654	56.419	38.586	1.00	42.15	B	C
ATOM	4026	CB	ALA	B	330	−15.939	56.080	37.151	1.00	41.25	B	C
ATOM	4027	C	ALA	B	330	−15.034	57.788	38.713	1.00	46.79	B	C
ATOM	4028	O	ALA	B	330	−14.026	57.940	39.397	1.00	48.86	B	O
ATOM	4029	N	ARG	B	331	−15.656	58.783	38.080	1.00	52.99	B	N
ATOM	4030	CA	ARG	B	331	−15.266	60.185	38.196	1.00	54.31	B	C
ATOM	4031	CB	ARG	B	331	−16.508	61.047	38.047	1.00	57.66	B	C
ATOM	4032	CG	ARG	B	331	−16.285	62.389	37.401	1.00	66.59	B	C
ATOM	4033	CD	ARG	B	331	−17.572	63.218	37.248	1.00	74.27	B	C
ATOM	4034	NE	ARG	B	331	−18.753	62.389	36.960	1.00	78.56	B	N
ATOM	4035	CZ	ARG	B	331	−19.128	61.980	35.741	1.00	78.96	B	C
ATOM	4036	NH1	ARG	B	331	−18.423	62.316	34.663	1.00	78.56	B	N
ATOM	4037	NH2	ARG	B	331	−20.216	61.229	35.600	1.00	77.36	B	N
ATOM	4038	C	ARG	B	331	−14.587	60.491	39.537	1.00	54.34	B	C
ATOM	4039	O	ARG	B	331	−13.501	61.068	39.571	1.00	53.46	B	O
ATOM	4040	N	GLN	B	332	−15.219	60.057	40.627	1.00	54.05	B	N
ATOM	4041	CA	GLN	B	332	−14.801	60.401	41.987	1.00	56.11	B	C
ATOM	4042	CB	GLN	B	332	−15.908	60.051	42.978	1.00	56.59	B	C
ATOM	4043	CG	GLN	B	332	−17.171	60.858	42.840	1.00	57.97	B	C
ATOM	4044	CD	GLN	B	332	−18.350	60.192	43.518	1.00	60.52	B	C
ATOM	4045	OE1	GLN	B	332	−19.471	60.259	43.021	1.00	62.43	B	O
ATOM	4046	NE2	GLN	B	332	−18.102	59.547	44.654	1.00	60.21	B	N
ATOM	4047	C	GLN	B	332	−13.487	59.802	42.511	1.00	58.78	B	C
ATOM	4048	O	GLN	B	332	−12.777	60.464	43.264	1.00	61.01	B	O
ATOM	4049	N	ILE	B	333	−13.178	58.554	42.163	1.00	60.02	B	N
ATOM	4050	CA	ILE	B	333	−12.048	57.859	42.801	1.00	61.37	B	C
ATOM	4051	CB	ILE	B	333	−12.462	56.453	43.376	1.00	60.29	B	C
ATOM	4052	CG1	ILE	B	333	−13.532	55.790	42.520	1.00	57.86	B	C
ATOM	4053	CD1	ILE	B	333	−12.967	55.019	41.368	1.00	59.06	B	C
ATOM	4054	CG2	ILE	B	333	−12.884	56.542	44.846	1.00	62.90	B	C
ATOM	4055	C	ILE	B	333	−10.803	57.692	41.930	1.00	62.41	B	C
ATOM	4056	O	ILE	B	333	−9.843	57.034	42.344	1.00	65.96	B	O
ATOM	4057	N	GLY	B	334	−10.810	58.270	40.734	1.00	60.64	B	N
ATOM	4058	CA	GLY	B	334	−9.712	58.055	39.808	1.00	61.54	B	C
ATOM	4059	C	GLY	B	334	−10.127	57.351	38.531	1.00	63.72	B	C
ATOM	4060	O	GLY	B	334	−9.316	57.206	37.617	1.00	65.07	B	O
ATOM	4061	N	ALA	B	335	−11.375	56.876	38.504	1.00	64.54	B	N
ATOM	4062	CA	ALA	B	335	−12.128	56.609	37.270	1.00	63.84	B	C
ATOM	4063	CB	ALA	B	335	−12.319	57.925	36.447	1.00	68.98	B	C
ATOM	4064	C	ALA	B	335	−11.620	55.487	36.381	1.00	61.10	B	C
ATOM	4065	O	ALA	B	335	−10.965	54.560	36.853	1.00	60.42	B	O
ATOM	4066	N	SER	B	336	−11.920	55.627	35.087	1.00	62.19	B	N
ATOM	4067	CA	SER	B	336	−11.779	54.595	34.058	1.00	66.51	B	C
ATOM	4068	CB	SER	B	336	−10.412	53.901	34.109	1.00	74.49	B	C
ATOM	4069	OG	SER	B	336	−10.411	52.686	33.371	1.00	82.14	B	O
ATOM	4070	C	SER	B	336	−12.957	53.610	34.106	1.00	65.03	B	C
ATOM	4071	O	SER	B	336	−12.960	52.627	34.852	1.00	62.64	B	O
ATOM	4072	N	LEU	B	337	−13.962	53.911	33.291	1.00	66.13	B	N
ATOM	4073	CA	LEU	B	337	−15.194	53.136	33.176	1.00	66.47	B	C
ATOM	4074	CB	LEU	B	337	−15.887	53.528	31.861	1.00	69.76	B	C
ATOM	4075	CG	LEU	B	337	−17.392	53.824	31.789	1.00	73.26	B	C
ATOM	4076	CD1	LEU	B	337	−18.157	52.606	31.242	1.00	76.33	B	C
ATOM	4077	CD2	LEU	B	337	−17.982	54.285	33.126	1.00	73.40	B	C
ATOM	4078	C	LEU	B	337	−14.948	51.629	33.212	1.00	63.98	B	C
ATOM	4079	O	LEU	B	337	−15.752	50.857	33.748	1.00	57.87	B	O
ATOM	4080	N	ASN	B	338	−13.815	51.239	32.638	1.00	67.61	B	N
ATOM	4081	CA	ASN	B	338	−13.431	49.852	32.468	1.00	72.58	B	C
ATOM	4082	CB	ASN	B	338	−13.182	49.583	30.978	1.00	80.29	B	C
ATOM	4083	CG	ASN	B	338	−12.809	48.137	30.695	1.00	87.12	B	C
ATOM	4084	OD1	ASN	B	338	−13.556	47.205	31.028	1.00	88.04	B	O
ATOM	4085	ND2	ASN	B	338	−11.639	47.941	30.081	1.00	89.20	B	N
ATOM	4086	C	ASN	B	338	−12.205	49.500	33.324	1.00	70.16	B	C
ATOM	4087	O	ASN	B	338	−11.214	48.963	32.834	1.00	69.51	B	O
ATOM	4088	N	ASP	B	339	−12.286	49.806	34.615	1.00	69.79	B	N
ATOM	4089	CA	ASP	B	339	−11.199	49.517	35.542	1.00	67.80	B	C
ATOM	4090	CB	ASP	B	339	−10.582	50.807	36.054	1.00	70.33	B	C
ATOM	4091	CG	ASP	B	339	−9.113	50.877	35.767	1.00	77.20	B	C
ATOM	4092	OD1	ASP	B	339	−8.389	49.949	36.218	1.00	82.67	B	O
ATOM	4093	OD2	ASP	B	339	−8.594	51.796	35.090	1.00	76.34	B	O
ATOM	4094	C	ASP	B	339	−11.593	48.636	36.720	1.00	64.34	B	C
ATOM	4095	O	ASP	B	339	−12.700	48.730	37.238	1.00	64.14	B	O
ATOM	4096	N	ASP	B	340	−10.674	47.777	37.142	1.00	60.50	B	N
ATOM	4097	CA	ASP	B	340	−10.924	46.932	38.299	1.00	57.67	B	C
ATOM	4098	CB	ASP	B	340	−10.064	45.675	38.228	1.00	56.39	B	C
ATOM	4099	CG	ASP	B	340	−10.554	44.698	37.182	1.00	59.37	B	C
ATOM	4100	OD1	ASP	B	340	−11.784	44.529	37.020	1.00	58.17	B	O
ATOM	4101	OD2	ASP	B	340	−9.774	44.030	36.481	1.00	63.66	B	O
ATOM	4102	C	ASP	B	340	−10.699	47.676	39.622	1.00	57.34	B	C
ATOM	4103	O	ASP	B	340	−9.643	48.294	39.840	1.00	60.14	B	O
ATOM	4104	N	ILE	B	341	−11.708	47.635	40.491	1.00	50.94	B	N
ATOM	4105	CA	ILE	B	341	−11.584	48.209	41.822	1.00	46.54	B	C
ATOM	4106	CB	ILE	B	341	−12.555	49.357	42.014	1.00	44.72	B	C
ATOM	4107	CG1	ILE	B	341	−12.116	50.557	41.193	1.00	45.57	B	C
ATOM	4108	CD1	ILE	B	341	−12.832	50.677	39.908	1.00	44.81	B	C
ATOM	4109	CG2	ILE	B	341	−12.599	49.757	43.473	1.00	44.54	B	C
ATOM	4110	C	ILE	B	341	−11.845	47.164	42.884	1.00	49.43	B	C
ATOM	4111	O	ILE	B	341	−12.760	46.351	42.775	1.00	52.41	B	O
ATOM	4112	N	LEU	B	342	−11.030	47.201	43.922	1.00	48.88	B	N
ATOM	4113	CA	LEU	B	342	−11.190	46.319	45.055	1.00	46.16	B	C
ATOM	4114	CB	LEU	B	342	−9.812	45.918	45.596	1.00	42.06	B	C
ATOM	4115	CG	LEU	B	342	−9.746	45.306	46.989	1.00	40.05	B	C
ATOM	4116	CD1	LEU	B	342	−10.387	43.942	46.949	1.00	41.44	B	C
ATOM	4117	CD2	LEU	B	342	−8.314	45.213	47.477	1.00	39.40	B	C
ATOM	4118	C	LEU	B	342	−12.034	47.033	46.116	1.00	47.55	B	C
ATOM	4119	O	LEU	B	342	−11.562	47.949	46.811	1.00	50.43	B	O
ATOM	4120	N	PHE	B	343	−13.293	46.625	46.215	1.00	41.92	B	N
ATOM	4121	CA	PHE	B	343	−14.141	47.077	47.298	1.00	38.40	B	C
ATOM	4122	CB	PHE	B	343	−15.596	46.984	46.878	1.00	36.63	B	C
ATOM	4123	CG	PHE	B	343	−15.923	47.858	45.716	1.00	34.84	B	C
ATOM	4124	CD1	PHE	B	343	−16.015	47.326	44.440	1.00	34.47	B	C
ATOM	4125	CE1	PHE	B	343	−16.296	48.144	43.363	1.00	33.66	B	C
ATOM	4126	CZ	PHE	B	343	−16.470	49.511	43.565	1.00	30.55	B	C
ATOM	4127	CE2	PHE	B	343	−16.365	50.044	44.836	1.00	26.40	B	C
ATOM	4128	CD2	PHE	B	343	−16.100	49.225	45.893	1.00	29.75	B	C
ATOM	4129	C	PHE	B	343	−13.868	46.201	48.496	1.00	39.49	B	C
ATOM	4130	O	PHE	B	343	−14.008	44.987	48.422	1.00	43.25	B	O
ATOM	4131	N	GLY	B	344	−13.452	46.815	49.594	1.00	38.93	B	N
ATOM	4132	CA	GLY	B	344	−13.107	46.068	50.790	1.00	41.21	B	C
ATOM	4133	C	GLY	B	344	−13.843	46.525	52.032	1.00	44.97	B	C
ATOM	4134	O	GLY	B	344	−13.740	47.678	52.461	1.00	48.19	B	O
ATOM	4135	N	VAL	B	345	−14.597	45.616	52.624	1.00	45.74	B	N
ATOM	4136	CA	VAL	B	345	−15.332	45.943	53.832	1.00	48.71	B	C
ATOM	4137	CB	VAL	B	345	−16.716	45.237	53.825	1.00	50.32	B	C
ATOM	4138	CG1	VAL	B	345	−17.159	44.856	55.218	1.00	55.50	B	C
ATOM	4139	CG2	VAL	B	345	−17.767	46.121	53.156	1.00	45.23	B	C
ATOM	4140	C	VAL	B	345	−14.451	45.610	55.052	1.00	48.69	B	C
ATOM	4141	O	VAL	B	345	−14.153	44.437	55.309	1.00	47.46	B	O
ATOM	4142	N	PHE	B	346	−14.016	46.649	55.771	1.00	48.12	B	N
ATOM	4143	CA	PHE	B	346	−13.022	46.509	56.854	1.00	49.20	B	C
ATOM	4144	CB	PHE	B	346	−11.926	47.575	56.748	1.00	46.30	B	C
ATOM	4145	CG	PHE	B	346	−11.031	47.408	55.565	1.00	45.81	B	C
ATOM	4146	CD1	PHE	B	346	−11.440	47.830	54.302	1.00	44.17	B	C
ATOM	4147	CE1	PHE	B	346	−10.620	47.672	53.191	1.00	45.65	B	C
ATOM	4148	CZ	PHE	B	346	−9.370	47.097	53.336	1.00	47.76	B	C
ATOM	4149	CE2	PHE	B	346	−8.946	46.666	54.600	1.00	49.85	B	C
ATOM	4150	CD2	PHE	B	346	−9.779	46.829	55.707	1.00	48.05	B	C
ATOM	4151	C	PHE	B	346	−13.651	46.587	58.232	1.00	51.63	B	C
ATOM	4152	O	PHE	B	346	−14.873	46.585	58.350	1.00	59.52	B	O
ATOM	4153	N	ALA	B	347	−12.811	46.667	59.265	1.00	47.44	B	N
ATOM	4154	CA	ALA	B	347	−13.259	46.670	60.658	1.00	45.63	B	C
ATOM	4155	CB	ALA	B	347	−13.910	45.331	61.020	1.00	41.64	B	C
ATOM	4156	C	ALA	B	347	−12.119	46.991	61.633	1.00	48.68	B	C
ATOM	4157	O	ALA	B	347	−10.939	46.742	61.340	1.00	52.11	B	O
ATOM	4158	N	GLN	B	348	−12.485	47.528	62.797	1.00	46.37	B	N
ATOM	4159	CA	GLN	B	348	−11.523	47.935	63.812	1.00	46.50	B	C
ATOM	4160	CB	GLN	B	348	−12.030	49.163	64.566	1.00	51.95	B	C
ATOM	4161	CG	GLN	B	348	−11.016	49.802	65.518	1.00	56.38	B	C
ATOM	4162	CD	GLN	B	348	−11.488	51.143	66.055	1.00	59.58	B	C
ATOM	4163	OE1	GLN	B	348	−12.351	51.198	66.933	1.00	61.38	B	O
ATOM	4164	NE2	GLN	B	348	−10.925	52.227	65.528	1.00	60.96	B	N
ATOM	4165	C	GLN	B	348	−11.204	46.810	64.789	1.00	45.95	B	C
ATOM	4166	O	GLN	B	348	−12.095	46.089	65.248	1.00	45.26	B	O
ATOM	4167	N	SER	B	349	−9.916	46.688	65.099	1.00	45.22	B	N
ATOM	4168	CA	SER	B	349	−9.389	45.665	65.979	1.00	42.27	B	C
ATOM	4169	CB	SER	B	349	−7.881	45.644	65.851	1.00	41.04	B	C
ATOM	4170	OG	SER	B	349	−7.369	44.411	66.289	1.00	44.60	B	O
ATOM	4171	C	SER	B	349	−9.716	45.944	67.426	1.00	45.73	B	C
ATOM	4172	O	SER	B	349	−9.662	47.092	67.871	1.00	45.84	B	O
ATOM	4173	N	LYS	B	350	−10.060	44.886	68.157	1.00	49.08	B	N
ATOM	4174	CA	LYS	B	350	−10.035	44.916	69.614	1.00	51.24	B	C
ATOM	4175	CB	LYS	B	350	−10.611	43.627	70.201	1.00	54.70	B	C
ATOM	4176	CG	LYS	B	350	−12.127	43.567	70.242	1.00	59.23	B	C
ATOM	4177	CD	LYS	B	350	−12.620	42.165	70.587	1.00	63.81	B	C
ATOM	4178	CE	LYS	B	350	−14.036	42.200	71.153	1.00	68.32	B	C
ATOM	4179	NZ	LYS	B	350	−14.042	42.442	72.637	1.00	72.71	B	N
ATOM	4180	C	LYS	B	350	−8.562	45.042	69.985	1.00	51.58	B	C
ATOM	4181	O	LYS	B	350	−7.743	44.261	69.496	1.00	50.93	B	O
ATOM	4182	N	PRO	B	351	−8.211	46.015	70.826	1.00	52.22	B	N
ATOM	4183	CA	PRO	B	351	−6.802	46.361	71.048	1.00	52.90	B	C
ATOM	4184	CB	PRO	B	351	−6.872	47.347	72.200	1.00	50.68	B	C
ATOM	4185	CG	PRO	B	351	−8.197	47.984	72.011	1.00	50.11	B	C
ATOM	4186	CD	PRO	B	351	−9.110	46.859	71.633	1.00	50.04	B	C
ATOM	4187	C	PRO	B	351	−5.928	45.154	71.384	1.00	56.85	B	C
ATOM	4188	O	PRO	B	351	−6.322	44.304	72.189	1.00	55.91	B	O
ATOM	4189	N	ASP	B	352	−4.771	45.091	70.719	1.00	61.69	B	N
ATOM	4190	CA	ASP	B	352	−3.788	44.001	70.824	1.00	63.92	B	C
ATOM	4191	CB	ASP	B	352	−3.288	43.827	72.271	1.00	69.49	B	C
ATOM	4192	CG	ASP	B	352	−2.046	44.660	72.572	1.00	73.65	B	C
ATOM	4193	OD1	ASP	B	352	−2.038	45.865	72.230	1.00	75.00	B	O
ATOM	4194	OD2	ASP	B	352	−1.033	44.199	73.155	1.00	75.16	B	O
ATOM	4195	C	ASP	B	352	−4.265	42.667	70.249	1.00	60.93	B	C
ATOM	4196	O	ASP	B	352	−3.705	41.618	70.565	1.00	58.50	B	O
ATOM	4197	N	SER	B	353	−5.277	42.712	69.385	1.00	61.20	B	N
ATOM	4198	CA	SER	B	353	−5.843	41.487	68.817	1.00	61.71	B	C
ATOM	4199	CB	SER	B	353	−7.135	41.103	69.553	1.00	64.07	B	C
ATOM	4200	OG	SER	B	353	−8.282	41.293	68.734	1.00	64.99	B	O
ATOM	4201	C	SER	B	353	−6.077	41.526	67.301	1.00	58.70	B	C
ATOM	4202	O	SER	B	353	−5.708	42.488	66.620	1.00	56.25	B	O
ATOM	4203	N	ALA	B	354	−6.695	40.455	66.805	1.00	57.57	B	N
ATOM	4204	CA	ALA	B	354	−7.019	40.273	65.397	1.00	56.61	B	C
ATOM	4205	CB	ALA	B	354	−6.290	39.073	64.876	1.00	56.85	B	C
ATOM	4206	C	ALA	B	354	−8.524	40.089	65.214	1.00	56.79	B	C
ATOM	4207	O	ALA	B	354	−9.046	40.181	64.099	1.00	55.29	B	O
ATOM	4208	N	GLU	B	355	−9.200	39.810	66.323	1.00	59.16	B	N
ATOM	4209	CA	GLU	B	355	−10.652	39.736	66.385	1.00	62.50	B	C
ATOM	4210	CB	GLU	B	355	−11.094	39.174	67.741	1.00	70.39	B	C
ATOM	4211	CG	GLU	B	355	−10.388	37.885	68.155	1.00	78.56	B	C
ATOM	4212	CD	GLU	B	355	−9.384	38.086	69.291	1.00	84.21	B	C
ATOM	4213	OE1	GLU	B	355	−9.792	38.558	70.380	1.00	85.26	B	O
ATOM	4214	OE2	GLU	B	355	−8.183	37.763	69.103	1.00	86.79	B	O
ATOM	4215	C	GLU	B	355	−11.253	41.128	66.174	1.00	58.99	B	C
ATOM	4216	O	GLU	B	355	−10.697	42.127	66.640	1.00	58.55	B	O
ATOM	4217	N	PRO	B	356	−12.374	41.198	65.461	1.00	55.08	B	N
ATOM	4218	CA	PRO	B	356	−12.996	42.476	65.127	1.00	52.43	B	C
ATOM	4219	CB	PRO	B	356	−13.608	42.192	63.759	1.00	51.64	B	C
ATOM	4220	CG	PRO	B	356	−13.989	40.748	63.817	1.00	52.95	B	C
ATOM	4221	CD	PRO	B	356	−13.127	40.076	64.878	1.00	55.18	B	C
ATOM	4222	C	PRO	B	356	−14.100	42.892	66.088	1.00	52.14	B	C
ATOM	4223	O	PRO	B	356	−14.894	42.060	66.535	1.00	50.25	B	O
ATOM	4224	N	MET	B	357	−14.141	44.186	66.380	1.00	53.89	B	N
ATOM	4225	CA	MET	B	357	−15.249	44.794	67.102	1.00	57.79	B	C
ATOM	4226	CB	MET	B	357	−14.761	46.051	67.811	1.00	61.40	B	C
ATOM	4227	CG	MET	B	357	−14.551	45.873	69.292	1.00	64.49	B	C
ATOM	4228	SD	MET	B	357	−13.841	47.351	69.981	1.00	68.87	B	S
ATOM	4229	CE	MET	B	357	−15.363	48.302	70.459	1.00	67.95	B	C
ATOM	4230	C	MET	B	357	−16.375	45.139	66.126	1.00	57.94	B	C
ATOM	4231	O	MET	B	357	−16.177	45.089	64.920	1.00	61.91	B	O
ATOM	4232	N	ASP	B	358	−17.548	45.501	66.632	1.00	57.25	B	N
ATOM	4233	CA	ASP	B	358	−18.677	45.819	65.759	1.00	57.76	B	C
ATOM	4234	CB	ASP	B	358	−20.000	45.655	66.519	1.00	63.05	B	C
ATOM	4235	CG	ASP	B	358	−20.349	44.196	66.788	1.00	67.73	B	C
ATOM	4236	OD1	ASP	B	358	−21.292	43.955	67.575	1.00	69.44	B	O
ATOM	4237	OD2	ASP	B	358	−19.744	43.225	66.267	1.00	69.02	B	O
ATOM	4238	C	ASP	B	358	−18.578	47.214	65.124	1.00	56.07	B	C
ATOM	4239	O	ASP	B	358	−19.547	47.966	65.108	1.00	55.88	B	O
ATOM	4240	N	ARG	B	359	−17.403	47.550	64.599	1.00	55.50	B	N
ATOM	4241	CA	ARG	B	359	−17.165	48.841	63.956	1.00	57.49	B	C
ATOM	4242	CB	ARG	B	359	−16.070	49.611	64.702	1.00	58.09	B	C
ATOM	4243	CG	ARG	B	359	−16.531	50.420	65.893	1.00	59.68	B	C
ATOM	4244	CD	ARG	B	359	−15.554	51.509	66.290	1.00	62.07	B	C
ATOM	4245	NE	ARG	B	359	−16.131	52.845	66.143	1.00	66.02	B	N
ATOM	4246	CZ	ARG	B	359	−15.538	53.872	65.536	1.00	66.88	B	C
ATOM	4247	NH1	ARG	B	359	−14.331	53.736	64.998	1.00	66.41	B	N
ATOM	4248	NH2	ARG	B	359	−16.158	55.047	65.465	1.00	67.49	B	N
ATOM	4249	C	ARG	B	359	−16.728	48.625	62.507	1.00	58.84	B	C
ATOM	4250	O	ARG	B	359	−15.655	48.081	62.255	1.00	61.46	B	O
ATOM	4251	N	SER	B	360	−17.541	49.050	61.550	1.00	57.61	B	N
ATOM	4252	CA	SER	B	360	−17.193	48.821	60.158	1.00	57.19	B	C
ATOM	4253	CB	SER	B	360	−18.198	47.882	59.505	1.00	57.10	B	C
ATOM	4254	OG	SER	B	360	−18.169	46.613	60.119	1.00	56.60	B	O
ATOM	4255	C	SER	B	360	−17.070	50.085	59.332	1.00	60.28	B	C
ATOM	4256	O	SER	B	360	−17.589	51.143	59.696	1.00	61.65	B	O
ATOM	4257	N	ALA	B	361	−16.377	49.946	58.205	1.00	63.10	B	N
ATOM	4258	CA	ALA	B	361	−16.225	51.004	57.212	1.00	64.03	B	C
ATOM	4259	CB	ALA	B	361	−15.295	52.077	57.727	1.00	66.25	B	C
ATOM	4260	C	ALA	B	361	−15.648	50.377	55.960	1.00	61.46	B	C
ATOM	4261	O	ALA	B	361	−14.620	49.716	56.035	1.00	66.20	B	O
ATOM	4262	N	MET	B	362	−16.309	50.559	54.820	1.00	56.08	B	N
ATOM	4263	CA	MET	B	362	−15.803	50.023	53.559	1.00	51.84	B	C
ATOM	4264	CB	MET	B	362	−16.939	49.477	52.711	1.00	49.64	B	C
ATOM	4265	CG	MET	B	362	−16.540	49.118	51.303	1.00	47.97	B	C
ATOM	4266	SD	MET	B	362	−17.156	50.314	50.155	1.00	48.28	B	S
ATOM	4267	CE	MET	B	362	−15.969	50.265	48.955	1.00	50.81	B	C
ATOM	4268	C	MET	B	362	−15.074	51.106	52.794	1.00	49.81	B	C
ATOM	4269	O	MET	B	362	−15.430	52.274	52.905	1.00	52.45	B	O
ATOM	4270	N	CYS	B	363	−14.044	50.719	52.044	1.00	45.97	B	N
ATOM	4271	CA	CYS	B	363	−13.360	51.642	51.143	1.00	47.77	B	C
ATOM	4272	CB	CYS	B	363	−12.450	52.634	51.889	1.00	49.60	B	C
ATOM	4273	SG	CYS	B	363	−11.206	51.931	52.980	1.00	56.58	B	S
ATOM	4274	C	CYS	B	363	−12.653	50.921	49.997	1.00	48.50	B	C
ATOM	4275	O	CYS	B	363	−12.271	49.753	50.119	1.00	44.35	B	O
ATOM	4276	N	ALA	B	364	−12.503	51.636	48.879	1.00	50.42	B	N
ATOM	4277	CA	ALA	B	364	−12.252	51.017	47.577	1.00	49.03	B	C
ATOM	4278	CB	ALA	B	364	−13.368	51.371	46.627	1.00	49.45	B	C
ATOM	4279	C	ALA	B	364	−10.920	51.392	46.954	1.00	48.18	B	C
ATOM	4280	O	ALA	B	364	−10.594	52.572	46.847	1.00	51.58	B	O
ATOM	4281	N	PHE	B	365	−10.175	50.382	46.515	1.00	44.80	B	N
ATOM	4282	CA	PHE	B	365	−8.870	50.579	45.904	1.00	41.71	B	C
ATOM	4283	CB	PHE	B	365	−7.861	49.703	46.606	1.00	41.63	B	C
ATOM	4284	CG	PHE	B	365	−7.780	49.938	48.067	1.00	45.47	B	C
ATOM	4285	CD1	PHE	B	365	−8.780	49.470	48.913	1.00	48.02	B	C
ATOM	4286	CE1	PHE	B	365	−8.706	49.681	50.272	1.00	48.86	B	C
ATOM	4287	CZ	PHE	B	365	−7.619	50.366	50.797	1.00	49.81	B	C
ATOM	4288	CE2	PHE	B	365	−6.612	50.836	49.956	1.00	47.81	B	C
ATOM	4289	CD2	PHE	B	365	−6.697	50.618	48.605	1.00	45.32	B	C
ATOM	4290	C	PHE	B	365	−8.901	50.138	44.463	1.00	43.46	B	C
ATOM	4291	O	PHE	B	365	−9.124	48.964	44.205	1.00	51.12	B	O
ATOM	4292	N	PRO	B	366	−8.690	51.037	43.508	1.00	39.40	B	N
ATOM	4293	CA	PRO	B	366	−8.539	50.607	42.121	1.00	42.33	B	C
ATOM	4294	CB	PRO	B	366	−8.555	51.925	41.343	1.00	35.18	B	C
ATOM	4295	CG	PRO	B	366	−9.128	52.865	42.252	1.00	32.75	B	C
ATOM	4296	CD	PRO	B	366	−8.598	52.494	43.612	1.00	36.60	B	C
ATOM	4297	C	PRO	B	366	−7.199	49.893	41.996	1.00	46.12	B	C
ATOM	4298	O	PRO	B	366	−6.173	50.396	42.483	1.00	44.02	B	O
ATOM	4299	N	ILE	B	367	−7.211	48.714	41.382	1.00	48.74	B	N
ATOM	4300	CA	ILE	B	367	−5.995	47.916	41.347	1.00	50.89	B	C
ATOM	4301	CB	ILE	B	367	−6.237	46.423	40.917	1.00	49.40	B	C
ATOM	4302	CG1	ILE	B	367	−6.395	46.283	39.406	1.00	55.32	B	C
ATOM	4303	CD1	ILE	B	367	−5.207	45.601	38.745	1.00	59.97	B	C
ATOM	4304	CG2	ILE	B	367	−7.430	45.816	41.639	1.00	44.92	B	C
ATOM	4305	C	ILE	B	367	−4.934	48.625	40.515	1.00	51.72	B	C
ATOM	4306	O	ILE	B	367	−3.738	48.383	40.690	1.00	54.19	B	O
ATOM	4307	N	LYS	B	368	−5.376	49.526	39.637	1.00	50.99	B	N
ATOM	4308	CA	LYS	B	368	−4.440	50.293	38.828	1.00	51.13	B	C
ATOM	4309	CB	LYS	B	368	−5.170	51.118	37.760	1.00	50.48	B	C
ATOM	4310	CG	LYS	B	368	−4.782	52.580	37.653	1.00	53.35	B	C
ATOM	4311	CD	LYS	B	368	−6.001	53.489	37.860	1.00	58.19	B	C
ATOM	4312	CE	LYS	B	368	−6.688	53.898	36.542	1.00	60.10	B	C
ATOM	4313	NZ	LYS	B	368	−6.615	55.367	36.294	1.00	61.31	B	N
ATOM	4314	C	LYS	B	368	−3.515	51.116	39.726	1.00	50.15	B	C
ATOM	4315	O	LYS	B	368	−2.324	51.206	39.449	1.00	51.42	B	O
ATOM	4316	N	TYR	B	369	−4.051	51.660	40.821	1.00	49.60	B	N
ATOM	4317	CA	TYR	B	369	−3.243	52.431	41.775	1.00	49.84	B	C
ATOM	4318	CB	TYR	B	369	−4.095	53.424	42.574	1.00	54.03	B	C
ATOM	4319	CG	TYR	B	369	−4.700	54.486	41.694	1.00	58.71	B	C
ATOM	4320	CD1	TYR	B	369	−5.959	55.017	41.963	1.00	58.12	B	C
ATOM	4321	CE1	TYR	B	369	−6.513	55.977	41.129	1.00	59.82	B	C
ATOM	4322	CZ	TYR	B	369	−5.801	56.412	40.013	1.00	61.33	B	C
ATOM	4323	OH	TYR	B	369	−6.323	57.357	39.169	1.00	62.86	B	O
ATOM	4324	CE2	TYR	B	369	−4.554	55.905	39.731	1.00	62.39	B	C
ATOM	4325	CD2	TYR	B	369	−4.013	54.944	40.565	1.00	62.25	B	C
ATOM	4326	C	TYR	B	369	−2.438	51.545	42.700	1.00	48.25	B	C
ATOM	4327	O	TYR	B	369	−1.279	51.838	42.987	1.00	49.03	B	O
ATOM	4328	N	VAL	B	370	−3.051	50.460	43.160	1.00	46.31	B	N
ATOM	4329	CA	VAL	B	370	−2.331	49.415	43.882	1.00	44.83	B	C
ATOM	4330	CB	VAL	B	370	−3.176	48.117	44.009	1.00	44.32	B	C
ATOM	4331	CG1	VAL	B	370	−2.517	47.119	44.953	1.00	43.89	B	C
ATOM	4332	CG2	VAL	B	370	−4.592	48.429	44.475	1.00	43.16	B	C
ATOM	4333	C	VAL	B	370	−0.990	49.109	43.189	1.00	43.84	B	C
ATOM	4334	O	VAL	B	370	0.059	49.178	43.826	1.00	44.09	B	O
ATOM	4335	N	ASN	B	371	−1.033	48.799	41.891	1.00	41.71	B	N
ATOM	4336	CA	ASN	B	371	0.172	48.541	41.107	1.00	43.99	B	C
ATOM	4337	CB	ASN	B	371	−0.171	48.212	39.657	1.00	45.83	B	C
ATOM	4338	CG	ASN	B	371	−0.936	46.929	39.522	1.00	48.53	B	C
ATOM	4339	OD1	ASN	B	371	−0.773	46.014	40.321	1.00	50.49	B	O
ATOM	4340	ND2	ASN	B	371	−1.786	46.850	38.506	1.00	51.01	B	N
ATOM	4341	C	ASN	B	371	1.160	49.694	41.125	1.00	48.30	B	C
ATOM	4342	O	ASN	B	371	2.359	49.486	41.293	1.00	49.07	B	O
ATOM	4343	N	ASP	B	372	0.663	50.911	40.938	1.00	52.74	B	N
ATOM	4344	CA	ASP	B	372	1.534	52.076	40.962	1.00	58.36	B	C
ATOM	4345	CB	ASP	B	372	0.731	53.373	40.807	1.00	63.81	B	C
ATOM	4346	CG	ASP	B	372	0.061	53.483	39.447	1.00	67.32	B	C
ATOM	4347	OD1	ASP	B	372	0.402	52.669	38.553	1.00	67.14	B	O
ATOM	4348	OD2	ASP	B	372	−0.813	54.348	39.185	1.00	68.87	B	O
ATOM	4349	C	ASP	B	372	2.319	52.067	42.264	1.00	57.54	B	C
ATOM	4350	O	ASP	B	372	3.553	52.110	42.254	1.00	59.02	B	O
ATOM	4351	N	PHE	B	373	1.592	51.959	43.374	1.00	54.22	B	N
ATOM	4352	CA	PHE	B	373	2.191	51.901	44.695	1.00	54.15	B	C
ATOM	4353	CB	PHE	B	373	1.111	51.765	45.757	1.00	53.80	B	C
ATOM	4354	CG	PHE	B	373	1.442	52.457	47.035	1.00	53.26	B	C
ATOM	4355	CD1	PHE	B	373	1.209	53.824	47.176	1.00	54.06	B	C
ATOM	4356	CE1	PHE	B	373	1.520	54.477	48.359	1.00	55.19	B	C
ATOM	4357	CZ	PHE	B	373	2.072	53.754	49.416	1.00	56.46	B	C
ATOM	4358	CE2	PHE	B	373	2.312	52.380	49.281	1.00	53.58	B	C
ATOM	4359	CD2	PHE	B	373	1.997	51.747	48.096	1.00	51.74	B	C
ATOM	4360	C	PHE	B	373	3.197	50.765	44.829	1.00	57.41	B	C
ATOM	4361	O	PHE	B	373	4.187	50.899	45.545	1.00	60.76	B	O
ATOM	4362	N	PHE	B	374	2.942	49.656	44.138	1.00	58.65	B	N
ATOM	4363	CA	PHE	B	374	3.855	48.522	44.119	1.00	58.06	B	C
ATOM	4364	CB	PHE	B	374	3.154	47.283	43.576	1.00	54.16	B	C
ATOM	4365	CG	PHE	B	374	2.540	46.410	44.628	1.00	52.99	B	C
ATOM	4366	CD1	PHE	B	374	1.197	46.080	44.568	1.00	52.81	B	C
ATOM	4367	CE1	PHE	B	374	0.626	45.258	45.527	1.00	51.49	B	C
ATOM	4368	CZ	PHE	B	374	1.400	44.746	46.555	1.00	50.43	B	C
ATOM	4369	CE2	PHE	B	374	2.737	45.053	46.621	1.00	50.67	B	C
ATOM	4370	CD2	PHE	B	374	3.305	45.879	45.655	1.00	53.35	B	C
ATOM	4371	C	PHE	B	374	5.072	48.814	43.251	1.00	65.91	B	C
ATOM	4372	O	PHE	B	374	6.194	48.497	43.642	1.00	69.66	B	O
ATOM	4373	N	ASN	B	375	4.850	49.420	42.083	1.00	72.20	B	N
ATOM	4374	CA	ASN	B	375	5.911	49.628	41.089	1.00	79.93	B	C
ATOM	4375	CB	ASN	B	375	5.318	49.842	39.690	1.00	82.27	B	C
ATOM	4376	CG	ASN	B	375	4.508	48.657	39.204	1.00	85.14	B	C
ATOM	4377	OD1	ASN	B	375	4.745	47.514	39.600	1.00	85.93	B	O
ATOM	4378	ND2	ASN	B	375	3.538	48.927	38.335	1.00	86.47	B	N
ATOM	4379	C	ASN	B	375	6.882	50.771	41.388	1.00	85.35	B	C
ATOM	4380	O	ASN	B	375	8.100	50.578	41.353	1.00	88.87	B	O
ATOM	4381	N	LYS	B	376	6.338	51.951	41.679	1.00	86.99	B	N
ATOM	4382	CA	LYS	B	376	7.123	53.186	41.734	1.00	89.89	B	C
ATOM	4383	CB	LYS	B	376	6.193	54.394	41.939	1.00	93.49	B	C
ATOM	4384	CG	LYS	B	376	6.107	55.346	40.730	1.00	96.51	B	C
ATOM	4385	CD	LYS	B	376	5.448	54.695	39.504	1.00	98.20	B	C
ATOM	4386	CE	LYS	B	376	6.358	54.745	38.270	1.00	98.62	B	C
ATOM	4387	NZ	LYS	B	376	5.665	54.286	37.025	1.00	97.72	B	N
ATOM	4388	C	LYS	B	376	8.289	53.185	42.744	1.00	89.01	B	C
ATOM	4389	O	LYS	B	376	8.275	52.429	43.720	1.00	86.61	B	O
ATOM	4390	N	ALA	B	377	9.290	54.033	42.473	1.00	88.95	B	N
ATOM	4391	CA	ALA	B	377	10.514	54.155	43.277	1.00	86.04	B	C
ATOM	4392	CB	ALA	B	377	11.636	54.795	42.452	1.00	83.79	B	C
ATOM	4393	C	ALA	B	377	10.297	54.934	44.574	1.00	83.26	B	C
ATOM	4394	O	ALA	B	377	9.772	56.046	44.566	1.00	80.21	B	O
ATOM	4395	N	ASN	B	382	12.804	52.854	52.307	1.00	90.79	B	N
ATOM	4396	CA	ASN	B	382	11.818	52.620	51.256	1.00	93.43	B	C
ATOM	4397	CB	ASN	B	382	12.470	52.774	49.864	1.00	95.86	B	C
ATOM	4398	CG	ASN	B	382	11.509	52.453	48.697	1.00	96.25	B	C
ATOM	4399	OD1	ASN	B	382	11.915	51.847	47.699	1.00	94.77	B	O
ATOM	4400	ND2	ASN	B	382	10.249	52.878	48.812	1.00	95.05	B	N
ATOM	4401	C	ASN	B	382	11.112	51.263	51.392	1.00	91.79	B	C
ATOM	4402	O	ASN	B	382	9.929	51.201	51.741	1.00	90.56	B	O
ATOM	4403	N	VAL	B	383	11.853	50.188	51.127	1.00	90.36	B	N
ATOM	4404	CA	VAL	B	383	11.295	48.840	51.019	1.00	88.88	B	C
ATOM	4405	CB	VAL	B	383	11.441	48.311	49.569	1.00	87.27	B	C
ATOM	4406	CG1	VAL	B	383	11.215	46.818	49.500	1.00	85.52	B	C
ATOM	4407	CG2	VAL	B	383	10.485	49.030	48.636	1.00	88.67	B	C
ATOM	4408	C	VAL	B	383	11.986	47.870	51.980	1.00	89.70	B	C
ATOM	4409	O	VAL	B	383	13.212	47.750	51.970	1.00	92.76	B	O
ATOM	4410	N	ARG	B	384	11.202	47.177	52.802	1.00	87.96	B	N
ATOM	4411	CA	ARG	B	384	11.750	46.185	53.731	1.00	85.72	B	C
ATOM	4412	CB	ARG	B	384	10.849	46.045	54.964	1.00	83.28	B	C
ATOM	4413	CG	ARG	B	384	11.590	46.085	56.284	1.00	80.78	B	C
ATOM	4414	CD	ARG	B	384	10.782	45.579	57.471	1.00	80.11	B	C
ATOM	4415	NE	ARG	B	384	10.595	46.597	58.506	1.00	81.51	B	N
ATOM	4416	CZ	ARG	B	384	11.545	47.036	59.340	1.00	82.35	B	C
ATOM	4417	NH1	ARG	B	384	12.786	46.561	59.284	1.00	81.49	B	N
ATOM	4418	NH2	ARG	B	384	11.250	47.966	60.240	1.00	82.81	B	N
ATOM	4419	C	ARG	B	384	11.964	44.825	53.047	1.00	86.09	B	C
ATOM	4420	O	ARG	B	384	11.932	44.721	51.819	1.00	85.04	B	O
ATOM	4421	N	CYS	B	385	12.196	43.792	53.850	1.00	86.91	B	N
ATOM	4422	CA	CYS	B	385	12.377	42.437	53.342	1.00	86.40	B	C
ATOM	4423	CB	CYS	B	385	13.867	42.059	53.361	1.00	93.48	B	C
ATOM	4424	SG	CYS	B	385	14.337	40.488	54.130	1.00	101.78	B	S
ATOM	4425	C	CYS	B	385	11.491	41.475	54.140	1.00	80.84	B	C
ATOM	4426	O	CYS	B	385	11.177	41.727	55.311	1.00	79.23	B	O
ATOM	4427	N	LEU	B	386	11.090	40.382	53.494	1.00	75.98	B	N
ATOM	4428	CA	LEU	B	386	10.003	39.531	53.983	1.00	72.77	B	C
ATOM	4429	CB	LEU	B	386	9.596	38.520	52.914	1.00	72.03	B	C
ATOM	4430	CG	LEU	B	386	8.101	38.539	52.625	1.00	70.14	B	C
ATOM	4431	CD1	LEU	B	386	7.773	39.669	51.661	1.00	70.58	B	C
ATOM	4432	CD2	LEU	B	386	7.654	37.199	52.078	1.00	69.14	B	C
ATOM	4433	C	LEU	B	386	10.306	38.817	55.285	1.00	70.79	B	C
ATOM	4434	O	LEU	B	386	10.760	37.674	55.285	1.00	70.38	B	O
ATOM	4435	N	GLN	B	387	10.008	39.491	56.390	1.00	70.99	B	N
ATOM	4436	CA	GLN	B	387	10.450	39.070	57.719	1.00	71.21	B	C
ATOM	4437	CB	GLN	B	387	10.000	40.081	58.770	1.00	76.73	B	C
ATOM	4438	CG	GLN	B	387	11.090	40.472	59.747	1.00	83.54	B	C
ATOM	4439	CD	GLN	B	387	11.192	41.970	59.922	1.00	89.26	B	C
ATOM	4440	OE1	GLN	B	387	10.956	42.502	61.017	1.00	90.36	B	O
ATOM	4441	NE2	GLN	B	387	11.542	42.663	58.840	1.00	92.01	B	N
ATOM	4442	C	GLN	B	387	10.031	37.666	58.147	1.00	66.69	B	C
ATOM	4443	O	GLN	B	387	10.724	37.032	58.945	1.00	67.30	B	O
ATOM	4444	N	HIS	B	388	8.915	37.180	57.616	1.00	61.67	B	N
ATOM	4445	CA	HIS	B	388	8.366	35.889	58.029	1.00	60.32	B	C
ATOM	4446	CB	HIS	B	388	6.842	35.962	58.010	1.00	65.91	B	C
ATOM	4447	CG	HIS	B	388	6.284	36.234	56.652	1.00	75.18	B	C
ATOM	4448	ND1	HIS	B	388	5.974	37.506	56.219	1.00	77.75	B	N
ATOM	4449	CE1	HIS	B	388	5.524	37.441	54.977	1.00	80.74	B	C
ATOM	4450	NE2	HIS	B	388	5.545	36.177	54.584	1.00	78.94	B	N
ATOM	4451	CD2	HIS	B	388	6.024	35.403	55.612	1.00	77.60	B	C
ATOM	4452	C	HIS	B	388	8.850	34.697	57.178	1.00	55.01	B	C
ATOM	4453	O	HIS	B	388	8.593	33.542	57.521	1.00	50.27	B	O
ATOM	4454	N	PHE	B	389	9.544	34.986	56.080	1.00	53.61	B	N
ATOM	4455	CA	PHE	B	389	9.953	33.963	55.114	1.00	55.30	B	C
ATOM	4456	CB	PHE	B	389	9.411	34.301	53.714	1.00	57.26	B	C
ATOM	4457	CG	PHE	B	389	10.279	33.799	52.569	1.00	59.85	B	C
ATOM	4458	CD1	PHE	B	389	10.133	32.498	52.076	1.00	61.44	B	C
ATOM	4459	CE1	PHE	B	389	10.916	32.030	51.012	1.00	60.58	B	C
ATOM	4460	CZ	PHE	B	389	11.858	32.870	50.432	1.00	60.77	B	C
ATOM	4461	CE2	PHE	B	389	12.015	34.169	50.914	1.00	60.24	B	C
ATOM	4462	CD2	PHE	B	389	11.227	34.630	51.973	1.00	59.50	B	C
ATOM	4463	C	PHE	B	389	11.468	33.805	55.069	1.00	53.57	B	C
ATOM	4464	O	PHE	B	389	11.984	32.686	54.991	1.00	48.22	B	O
ATOM	4465	N	TYR	B	390	12.153	34.946	55.046	1.00	56.37	B	N
ATOM	4466	CA	TYR	B	390	13.584	35.028	55.271	1.00	60.65	B	C
ATOM	4467	CB	TYR	B	390	14.151	36.311	54.664	1.00	60.39	B	C
ATOM	4468	CG	TYR	B	390	14.215	36.368	53.159	1.00	62.98	B	C
ATOM	4469	CD1	TYR	B	390	13.526	37.355	52.456	1.00	65.15	B	C
ATOM	4470	CE1	TYR	B	390	13.591	37.427	51.067	1.00	67.84	B	C
ATOM	4471	CZ	TYR	B	390	14.363	36.508	50.366	1.00	68.16	B	C
ATOM	4472	OH	TYR	B	390	14.427	36.572	48.991	1.00	69.28	B	O
ATOM	4473	CE2	TYR	B	390	15.068	35.524	51.043	1.00	66.83	B	C
ATOM	4474	CD2	TYR	B	390	14.992	35.462	52.435	1.00	65.28	B	C
ATOM	4475	C	TYR	B	390	13.731	35.137	56.769	1.00	65.50	B	C
ATOM	4476	O	TYR	B	390	12.737	35.284	57.478	1.00	66.93	B	O
ATOM	4477	N	GLY	B	391	14.962	35.092	57.262	1.00	70.76	B	N
ATOM	4478	CA	GLY	B	391	15.203	35.522	58.625	1.00	79.44	B	C
ATOM	4479	C	GLY	B	391	14.958	37.024	58.689	1.00	85.18	B	C
ATOM	4480	O	GLY	B	391	14.863	37.674	57.641	1.00	83.68	B	O
ATOM	4481	N	PRO	B	392	14.818	37.584	59.891	1.00	89.97	B	N
ATOM	4482	CA	PRO	B	392	15.016	39.027	60.065	1.00	92.05	B	C
ATOM	4483	CB	PRO	B	392	14.600	39.273	61.519	1.00	91.69	B	C
ATOM	4484	CG	PRO	B	392	13.798	38.075	61.895	1.00	91.59	B	C
ATOM	4485	CD	PRO	B	392	14.429	36.928	61.153	1.00	91.23	B	C
ATOM	4486	C	PRO	B	392	16.499	39.320	59.860	1.00	94.53	B	C
ATOM	4487	O	PRO	B	392	16.865	40.438	59.504	1.00	94.28	B	O
ATOM	4488	N	ASN	B	393	17.330	38.299	60.064	1.00	97.98	B	N
ATOM	4489	CA	ASN	B	393	18.761	38.395	59.835	1.00	103.04	B	C
ATOM	4490	CB	ASN	B	393	19.524	38.000	61.103	1.00	104.26	B	C
ATOM	4491	CG	ASN	B	393	19.878	39.199	61.973	1.00	105.22	B	C
ATOM	4492	OD1	ASN	B	393	21.012	39.330	62.437	1.00	105.99	B	O
ATOM	4493	ND2	ASN	B	393	18.905	40.079	62.202	1.00	104.86	B	N
ATOM	4494	C	ASN	B	393	19.214	37.556	58.641	1.00	106.92	B	C
ATOM	4495	O	ASN	B	393	18.390	37.010	57.904	1.00	104.77	B	O
ATOM	4496	N	HIS	B	394	20.534	37.468	58.472	1.00	114.08	B	N
ATOM	4497	CA	HIS	B	394	21.197	36.791	57.343	1.00	120.13	B	C
ATOM	4498	CB	HIS	B	394	20.898	35.274	57.299	1.00	122.25	B	C
ATOM	4499	CG	HIS	B	394	22.118	34.407	57.441	1.00	123.57	B	C
ATOM	4500	ND1	HIS	B	394	22.990	34.510	58.507	1.00	123.45	B	N
ATOM	4501	CE1	HIS	B	394	23.963	33.626	58.367	1.00	123.00	B	C
ATOM	4502	NE2	HIS	B	394	23.755	32.951	57.251	1.00	123.36	B	N
ATOM	4503	CD2	HIS	B	394	22.608	33.419	56.653	1.00	123.77	B	C
ATOM	4504	C	HIS	B	394	20.967	37.477	55.982	1.00	121.03	B	C
ATOM	4505	O	HIS	B	394	20.172	38.420	55.871	1.00	120.31	B	O
ATOM	4506	N	GLU	B	395	21.685	36.987	54.967	1.00	122.26	B	N
ATOM	4507	CA	GLU	B	395	21.757	37.598	53.636	1.00	124.02	B	C
ATOM	4508	CB	GLU	B	395	22.643	36.767	52.686	1.00	124.48	B	C
ATOM	4509	CG	GLU	B	395	23.282	35.525	53.293	1.00	125.18	B	C
ATOM	4510	CD	GLU	B	395	24.693	35.779	53.798	1.00	125.91	B	C
ATOM	4511	OE1	GLU	B	395	25.650	35.595	53.017	1.00	126.50	B	O
ATOM	4512	OE2	GLU	B	395	24.848	36.160	54.978	1.00	125.56	B	O
ATOM	4513	C	GLU	B	395	20.390	37.865	52.995	1.00	125.92	B	C
ATOM	4514	O	GLU	B	395	19.347	37.484	53.544	1.00	127.28	B	O
ATOM	4515	N	HIS	B	396	20.416	38.503	51.822	1.00	125.20	B	N
ATOM	4516	CA	HIS	B	396	19.221	38.992	51.121	1.00	121.60	B	C
ATOM	4517	CB	HIS	B	396	18.197	37.877	50.851	1.00	121.80	B	C
ATOM	4518	CG	HIS	B	396	18.812	36.558	50.496	1.00	123.47	B	C
ATOM	4519	ND1	HIS	B	396	19.370	36.304	49.262	1.00	124.95	B	N
ATOM	4520	CE1	HIS	B	396	19.831	35.066	49.235	1.00	125.85	B	C
ATOM	4521	NE2	HIS	B	396	19.596	34.509	50.410	1.00	126.04	B	N
ATOM	4522	CD2	HIS	B	396	18.958	35.419	51.216	1.00	124.24	B	C
ATOM	4523	C	HIS	B	396	18.583	40.158	51.880	1.00	118.72	B	C
ATOM	4524	O	HIS	B	396	18.293	41.199	51.291	1.00	119.52	B	O
ATOM	4525	N	CYS	B	397	18.391	39.980	53.186	1.00	114.19	B	N
ATOM	4526	CA	CYS	B	397	17.796	40.999	54.042	1.00	110.17	B	C
ATOM	4527	CB	CYS	B	397	17.284	40.371	55.338	1.00	106.64	B	C
ATOM	4528	SG	CYS	B	397	15.560	40.767	55.731	1.00	102.28	B	S
ATOM	4529	C	CYS	B	397	18.761	42.148	54.341	1.00	110.73	B	C
ATOM	4530	O	CYS	B	397	18.333	43.281	54.567	1.00	110.81	B	O
ATOM	4531	N	PHE	B	398	20.057	41.852	54.346	1.00	111.68	B	N
ATOM	4532	CA	PHE	B	398	21.086	42.879	54.497	1.00	112.35	B	C
ATOM	4533	CB	PHE	B	398	22.096	42.466	55.579	1.00	110.38	B	C
ATOM	4534	CG	PHE	B	398	22.058	43.322	56.824	1.00	110.12	B	C
ATOM	4535	CD1	PHE	B	398	20.857	43.849	57.302	1.00	109.64	B	C
ATOM	4536	CE1	PHE	B	398	20.828	44.640	58.459	1.00	109.56	B	C
ATOM	4537	CZ	PHE	B	398	22.013	44.904	59.152	1.00	110.46	B	C
ATOM	4538	CE2	PHE	B	398	23.220	44.380	58.687	1.00	110.54	B	C
ATOM	4539	CD2	PHE	B	398	23.235	43.592	57.528	1.00	111.21	B	C
ATOM	4540	C	PHE	B	398	21.776	43.112	53.146	1.00	114.23	B	C
ATOM	4541	O	PHE	B	398	23.008	43.110	53.055	1.00	114.14	B	O
ATOM	4542	N	ASN	B	399	20.969	43.318	52.101	1.00	116.16	B	N
ATOM	4543	CA	ASN	B	399	21.465	43.388	50.719	1.00	116.83	B	C
ATOM	4544	CB	ASN	B	399	21.302	42.022	50.027	1.00	114.97	B	C
ATOM	4545	CG	ASN	B	399	22.618	41.273	49.877	1.00	112.37	B	C
ATOM	4546	OD1	ASN	B	399	23.371	41.500	48.928	1.00	111.41	B	O
ATOM	4547	ND2	ASN	B	399	22.890	40.365	50.808	1.00	110.93	B	N
ATOM	4548	C	ASN	B	399	20.875	44.521	49.840	1.00	117.60	B	C
ATOM	4549	O	ASN	B	399	21.156	45.702	50.067	1.00	116.73	B	O
ATOM	4550	N	ARG	B	400	20.057	44.136	48.853	1.00	118.44	B	N
ATOM	4551	CA	ARG	B	400	19.609	45.005	47.751	1.00	117.82	B	C
ATOM	4552	CB	ARG	B	400	18.609	46.074	48.216	1.00	115.30	B	C
ATOM	4553	CG	ARG	B	400	17.187	45.876	47.688	1.00	113.12	B	C
ATOM	4554	CD	ARG	B	400	17.015	46.104	46.189	1.00	111.57	B	C
ATOM	4555	NE	ARG	B	400	15.717	45.618	45.717	1.00	110.25	B	N
ATOM	4556	CZ	ARG	B	400	15.384	45.448	44.438	1.00	108.16	B	C
ATOM	4557	NH1	ARG	B	400	16.249	45.723	43.469	1.00	108.42	B	N
ATOM	4558	NH2	ARG	B	400	14.177	45.001	44.124	1.00	105.39	B	N
ATOM	4559	C	ARG	B	400	20.775	45.638	46.987	1.00	118.38	B	C
ATOM	4560	O	ARG	B	400	21.136	45.190	45.896	1.00	118.43	B	O
ATOM	4561	N	ASP	B	414	11.162	37.092	40.828	1.00	118.53	B	N
ATOM	4562	CA	ASP	B	414	12.040	35.945	40.646	1.00	121.11	B	C
ATOM	4563	CB	ASP	B	414	13.014	36.193	39.474	1.00	123.45	B	C
ATOM	4564	CG	ASP	B	414	13.127	34.999	38.521	1.00	124.03	B	C
ATOM	4565	OD1	ASP	B	414	14.022	34.149	38.731	1.00	122.65	B	O
ATOM	4566	OD2	ASP	B	414	12.384	34.840	37.523	1.00	124.38	B	O
ATOM	4567	C	ASP	B	414	12.803	35.641	41.943	1.00	121.30	B	C
ATOM	4568	O	ASP	B	414	12.532	34.639	42.607	1.00	120.92	B	O
ATOM	4569	N	GLU	B	415	13.726	36.531	42.314	1.00	121.17	B	N
ATOM	4570	CA	GLU	B	415	14.741	36.237	43.332	1.00	117.56	B	C
ATOM	4571	CB	GLU	B	415	16.122	36.716	42.865	1.00	118.51	B	C
ATOM	4572	CG	GLU	B	415	16.578	36.105	41.546	1.00	120.09	B	C
ATOM	4573	CD	GLU	B	415	17.038	34.664	41.688	1.00	120.61	B	C
ATOM	4574	OE1	GLU	B	415	18.161	34.461	42.198	1.00	121.28	B	O
ATOM	4575	OE2	GLU	B	415	16.286	33.739	41.289	1.00	119.11	B	O
ATOM	4576	C	GLU	B	415	14.441	36.780	44.730	1.00	113.94	B	C
ATOM	4577	O	GLU	B	415	14.597	36.062	45.716	1.00	112.85	B	O
ATOM	4578	N	TYR	B	416	14.019	38.040	44.809	1.00	111.10	B	N
ATOM	4579	CA	TYR	B	416	13.765	38.699	46.097	1.00	108.01	B	C
ATOM	4580	CB	TYR	B	416	14.486	40.060	46.204	1.00	116.70	B	C
ATOM	4581	CG	TYR	B	416	15.349	40.472	45.015	1.00	125.64	B	C
ATOM	4582	CD1	TYR	B	416	14.876	40.373	43.691	1.00	128.98	B	C
ATOM	4583	CE1	TYR	B	416	15.670	40.760	42.603	1.00	130.95	B	C
ATOM	4584	CZ	TYR	B	416	16.946	41.268	42.835	1.00	131.58	B	C
ATOM	4585	OH	TYR	B	416	17.732	41.657	41.774	1.00	131.74	B	O
ATOM	4586	CE2	TYR	B	416	17.434	41.386	44.135	1.00	130.79	B	C
ATOM	4587	CD2	TYR	B	416	16.634	40.992	45.217	1.00	128.48	B	C
ATOM	4588	C	TYR	B	416	12.270	38.849	46.436	1.00	98.37	B	C
ATOM	4589	O	TYR	B	416	11.403	38.858	45.550	1.00	97.84	B	O
ATOM	4590	N	ARG	B	417	11.996	38.971	47.732	1.00	86.10	B	N
ATOM	4591	CA	ARG	B	417	10.646	38.935	48.269	1.00	76.02	B	C
ATOM	4592	CB	ARG	B	417	10.423	37.608	48.995	1.00	72.99	B	C
ATOM	4593	CG	ARG	B	417	9.785	36.517	48.128	1.00	70.00	B	C
ATOM	4594	CD	ARG	B	417	10.764	35.574	47.442	1.00	65.42	B	C
ATOM	4595	NE	ARG	B	417	10.280	35.179	46.122	1.00	63.02	B	N
ATOM	4596	CZ	ARG	B	417	10.061	33.922	45.754	1.00	63.41	B	C
ATOM	4597	NH1	ARG	B	417	10.286	32.924	46.600	1.00	64.27	B	N
ATOM	4598	NH2	ARG	B	417	9.615	33.657	44.535	1.00	61.59	B	N
ATOM	4599	C	ARG	B	417	10.437	40.107	49.216	1.00	73.44	B	C
ATOM	4600	O	ARG	B	417	10.948	40.110	50.333	1.00	74.00	B	O
ATOM	4601	N	THR	B	418	9.654	41.086	48.768	1.00	72.29	B	N
ATOM	4602	CA	THR	B	418	9.659	42.430	49.350	1.00	71.34	B	C
ATOM	4603	CB	THR	B	418	9.921	43.475	48.234	1.00	74.11	B	C
ATOM	4604	OG1	THR	B	418	9.420	42.981	46.983	1.00	77.18	B	O
ATOM	4605	CG2	THR	B	418	11.413	43.622	47.967	1.00	74.10	B	C
ATOM	4606	C	THR	B	418	8.418	42.837	50.152	1.00	68.83	B	C
ATOM	4607	O	THR	B	418	7.307	42.872	49.640	1.00	69.50	B	O
ATOM	4608	N	GLU	B	419	8.637	43.152	51.420	1.00	68.82	B	N
ATOM	4609	CA	GLU	B	419	7.639	43.798	52.263	1.00	69.08	B	C
ATOM	4610	CB	GLU	B	419	7.934	43.489	53.731	1.00	71.63	B	C
ATOM	4611	CG	GLU	B	419	6.716	43.402	54.635	1.00	75.07	B	C
ATOM	4612	CD	GLU	B	419	7.003	42.674	55.942	1.00	78.09	B	C
ATOM	4613	OE1	GLU	B	419	7.584	41.558	55.909	1.00	79.05	B	O
ATOM	4614	OE2	GLU	B	419	6.639	43.218	57.008	1.00	79.41	B	O
ATOM	4615	C	GLU	B	419	7.699	45.313	52.040	1.00	68.22	B	C
ATOM	4616	O	GLU	B	419	8.740	45.850	51.659	1.00	69.26	B	O
ATOM	4617	N	PHE	B	420	6.584	45.996	52.275	1.00	66.82	B	N
ATOM	4618	CA	PHE	B	420	6.533	47.450	52.187	1.00	65.27	B	C
ATOM	4619	CB	PHE	B	420	5.407	47.905	51.254	1.00	65.84	B	C
ATOM	4620	CG	PHE	B	420	5.821	48.053	49.802	1.00	65.70	B	C
ATOM	4621	CD1	PHE	B	420	6.559	47.058	49.154	1.00	67.04	B	C
ATOM	4622	CE1	PHE	B	420	6.933	47.196	47.811	1.00	66.15	B	C
ATOM	4623	CZ	PHE	B	420	6.562	48.337	47.105	1.00	64.22	B	C
ATOM	4624	CE2	PHE	B	420	5.818	49.325	47.737	1.00	63.92	B	C
ATOM	4625	CD2	PHE	B	420	5.448	49.179	49.075	1.00	64.43	B	C
ATOM	4626	C	PHE	B	420	6.304	47.983	53.585	1.00	66.39	B	C
ATOM	4627	O	PHE	B	420	5.642	47.335	54.402	1.00	64.77	B	O
ATOM	4628	N	THR	B	421	6.856	49.162	53.855	1.00	68.67	B	N
ATOM	4629	CA	THR	B	421	6.843	49.736	55.198	1.00	68.95	B	C
ATOM	4630	CB	THR	B	421	8.187	50.410	55.504	1.00	70.44	B	C
ATOM	4631	OG1	THR	B	421	8.945	50.546	54.295	1.00	71.76	B	O
ATOM	4632	CG2	THR	B	421	9.049	49.497	56.363	1.00	71.22	B	C
ATOM	4633	C	THR	B	421	5.693	50.709	55.436	1.00	69.61	B	C
ATOM	4634	O	THR	B	421	5.372	51.011	56.583	1.00	70.63	B	O
ATOM	4635	N	THR	B	422	5.080	51.198	54.356	1.00	71.01	B	N
ATOM	4636	CA	THR	B	422	3.919	52.096	54.452	1.00	70.55	B	C
ATOM	4637	CB	THR	B	422	4.256	53.523	53.958	1.00	73.13	B	C
ATOM	4638	OG1	THR	B	422	4.820	53.458	52.640	1.00	74.02	B	O
ATOM	4639	CG2	THR	B	422	5.350	54.168	54.819	1.00	74.37	B	C
ATOM	4640	C	THR	B	422	2.705	51.584	53.681	1.00	66.95	B	C
ATOM	4641	O	THR	B	422	2.830	51.012	52.590	1.00	65.46	B	O
ATOM	4642	N	ALA	B	423	1.530	51.826	54.254	1.00	63.45	B	N
ATOM	4643	CA	ALA	B	423	0.263	51.413	53.655	1.00	59.07	B	C
ATOM	4644	CB	ALA	B	423	−0.817	51.297	54.727	1.00	58.52	B	C
ATOM	4645	C	ALA	B	423	−0.205	52.347	52.549	1.00	55.58	B	C
ATOM	4646	O	ALA	B	423	0.216	53.489	52.456	1.00	57.64	B	O
ATOM	4647	N	LEU	B	424	−1.071	51.828	51.696	1.00	55.39	B	N
ATOM	4648	CA	LEU	B	424	−1.829	52.637	50.771	1.00	54.07	B	C
ATOM	4649	CB	LEU	B	424	−2.076	51.854	49.481	1.00	53.16	B	C
ATOM	4650	CG	LEU	B	424	−2.428	52.537	48.159	1.00	53.34	B	C
ATOM	4651	CD1	LEU	B	424	−2.975	51.496	47.196	1.00	52.78	B	C
ATOM	4652	CD2	LEU	B	424	−3.431	53.671	48.323	1.00	54.86	B	C
ATOM	4653	C	LEU	B	424	−3.138	52.889	51.500	1.00	54.78	B	C
ATOM	4654	O	LEU	B	424	−3.909	51.956	51.758	1.00	55.38	B	O
ATOM	4655	N	GLN	B	425	−3.382	54.143	51.857	1.00	53.26	B	N
ATOM	4656	CA	GLN	B	425	−4.586	54.469	52.605	1.00	50.56	B	C
ATOM	4657	CB	GLN	B	425	−4.265	55.326	53.833	1.00	57.95	B	C
ATOM	4658	CG	GLN	B	425	−4.052	56.810	53.566	1.00	64.03	B	C
ATOM	4659	CD	GLN	B	425	−3.515	57.523	54.783	1.00	67.46	B	C
ATOM	4660	OE1	GLN	B	425	−4.202	57.623	55.803	1.00	67.84	B	O
ATOM	4661	NE2	GLN	B	425	−2.278	58.004	54.692	1.00	70.00	B	N
ATOM	4662	C	GLN	B	425	−5.661	55.115	51.751	1.00	43.53	B	C
ATOM	4663	O	GLN	B	425	−5.378	55.805	50.770	1.00	40.15	B	O
ATOM	4664	N	ARG	B	426	−6.899	54.844	52.139	1.00	40.50	B	N
ATOM	4665	CA	ARG	B	426	−8.084	55.424	51.534	1.00	39.82	B	C
ATOM	4666	CB	ARG	B	426	−8.641	54.524	50.435	1.00	40.11	B	C
ATOM	4667	CG	ARG	B	426	−7.739	54.326	49.235	1.00	41.18	B	C
ATOM	4668	CD	ARG	B	426	−7.735	55.478	48.261	1.00	42.28	B	C
ATOM	4669	NE	ARG	B	426	−6.378	55.792	47.829	1.00	45.34	B	N
ATOM	4670	CZ	ARG	B	426	−5.993	55.870	46.559	1.00	47.98	B	C
ATOM	4671	NH1	ARG	B	426	−6.871	55.663	45.570	1.00	46.25	B	N
ATOM	4672	NH2	ARG	B	426	−4.724	56.168	46.277	1.00	49.60	B	N
ATOM	4673	C	ARG	B	426	−9.122	55.581	52.631	1.00	42.57	B	C
ATOM	4674	O	ARG	B	426	−9.062	54.907	53.663	1.00	40.06	B	O
ATOM	4675	N	VAL	B	427	−10.081	56.468	52.393	1.00	48.48	B	N
ATOM	4676	CA	VAL	B	427	−11.068	56.844	53.401	1.00	52.05	B	C
ATOM	4677	CB	VAL	B	427	−11.393	58.346	53.327	1.00	51.13	B	C
ATOM	4678	CG1	VAL	B	427	−10.956	59.031	54.603	1.00	52.45	B	C
ATOM	4679	CG2	VAL	B	427	−10.741	58.996	52.093	1.00	50.22	B	C
ATOM	4680	C	VAL	B	427	−12.363	56.063	53.243	1.00	54.73	B	C
ATOM	4681	O	VAL	B	427	−12.691	55.626	52.136	1.00	58.88	B	O
ATOM	4682	N	ASP	B	428	−13.090	55.894	54.350	1.00	52.40	B	N
ATOM	4683	CA	ASP	B	428	−14.414	55.274	54.327	1.00	48.88	B	C
ATOM	4684	CB	ASP	B	428	−15.051	55.293	55.727	1.00	52.09	B	C
ATOM	4685	CG	ASP	B	428	−16.360	54.500	55.802	1.00	53.53	B	C
ATOM	4686	OD1	ASP	B	428	−16.851	54.049	54.748	1.00	56.25	B	O
ATOM	4687	OD2	ASP	B	428	−16.970	54.276	56.876	1.00	50.49	B	O
ATOM	4688	C	ASP	B	428	−15.304	55.986	53.305	1.00	43.23	B	C
ATOM	4689	O	ASP	B	428	−15.346	57.213	53.233	1.00	38.01	B	O
ATOM	4690	N	LEU	B	429	−15.984	55.193	52.494	1.00	41.94	B	N
ATOM	4691	CA	LEU	B	429	−16.854	55.713	51.463	1.00	44.73	B	C
ATOM	4692	CB	LEU	B	429	−16.849	54.772	50.266	1.00	42.69	B	C
ATOM	4693	CG	LEU	B	429	−15.909	55.232	49.159	1.00	45.03	B	C
ATOM	4694	CD1	LEU	B	429	−14.963	54.120	48.741	1.00	47.96	B	C
ATOM	4695	CD2	LEU	B	429	−16.711	55.735	47.974	1.00	45.51	B	C
ATOM	4696	C	LEU	B	429	−18.263	55.885	52.016	1.00	48.78	B	C
ATOM	4697	O	LEU	B	429	−19.132	56.509	51.383	1.00	49.46	B	O
ATOM	4698	N	PHE	B	430	−18.473	55.331	53.206	1.00	48.13	B	N
ATOM	4699	CA	PHE	B	430	−19.757	55.397	53.874	1.00	51.15	B	C
ATOM	4700	CB	PHE	B	430	−20.098	54.034	54.463	1.00	47.94	B	C
ATOM	4701	CG	PHE	B	430	−20.464	52.998	53.427	1.00	47.14	B	C
ATOM	4702	CD1	PHE	B	430	−19.868	51.746	53.430	1.00	46.71	B	C
ATOM	4703	CE1	PHE	B		430	−20.219	50.777	52.479	1.00	44.76	B	C
ATOM	4704	CZ	PHE	B	430	−21.160	51.056	51.520	1.00	43.07	B	C
ATOM	4705	CE2	PHE	B	430	−21.760	52.297	51.501	1.00	46.29	B	C
ATOM	4706	CD2	PHE	B	430	−21.413	53.267	52.451	1.00	47.40	B	C
ATOM	4707	C	PHE	B	430	−19.749	56.486	54.939	1.00	57.21	B	C
ATOM	4708	O	PHE	B	430	−20.801	56.883	55.451	1.00	58.51	B	O
ATOM	4709	N	MET	B	431	−18.549	56.979	55.242	1.00	62.60	B	N
ATOM	4710	CA	MET	B	431	−18.330	58.080	56.189	1.00	66.92	B	C
ATOM	4711	CB	MET	B	431	−18.965	59.387	55.685	1.00	71.06	B	C
ATOM	4712	CG	MET	B	431	−18.235	60.033	54.527	1.00	78.05	B	C
ATOM	4713	SD	MET	B	431	−19.019	59.627	52.944	1.00	86.26	B	S
ATOM	4714	CE	MET	B	431	−19.859	61.190	52.582	1.00	86.91	B	C
ATOM	4715	C	MET	B	431	−18.804	57.769	57.611	1.00	66.59	B	C
ATOM	4716	O	MET	B	431	−19.202	58.664	58.348	1.00	69.83	B	O
ATOM	4717	N	GLY	B	432	−18.749	56.500	57.997	1.00	65.32	B	N
ATOM	4718	CA	GLY	B	432	−19.175	56.097	59.324	1.00	63.07	B	C
ATOM	4719	C	GLY	B	432	−20.603	55.595	59.364	1.00	61.89	B	C
ATOM	4720	O	GLY	B	432	−21.057	55.116	60.403	1.00	61.93	B	O
ATOM	4721	N	GLN	B	433	−21.307	55.699	58.237	1.00	60.80	B	N
ATOM	4722	CA	GLN	B	433	−22.661	55.167	58.095	1.00	60.89	B	C
ATOM	4723	CB	GLN	B	433	−23.011	55.019	56.611	1.00	64.40	B	C
ATOM	4724	CG	GLN	B	433	−24.331	55.642	56.186	1.00	69.58	B	C
ATOM	4725	CD	GLN	B	433	−25.420	55.499	57.239	1.00	74.21	B	C
ATOM	4726	OE1	GLN	B	433	−26.012	54.429	57.383	1.00	75.27	B	O
ATOM	4727	NE2	GLN	B	433	−25.682	56.578	57.979	1.00	76.91	B	N
ATOM	4728	C	GLN	B	433	−22.815	53.812	58.783	1.00	59.31	B	C
ATOM	4729	O	GLN	B	433	−23.914	53.425	59.184	1.00	57.45	B	O
ATOM	4730	N	PHE	B	434	−21.697	53.106	58.924	1.00	58.44	B	N
ATOM	4731	CA	PHE	B	434	−21.698	51.738	59.410	1.00	57.23	B	C
ATOM	4732	CB	PHE	B	434	−21.399	50.804	58.243	1.00	51.73	B	C
ATOM	4733	CG	PHE	B	434	−22.448	50.818	57.187	1.00	45.56	B	C
ATOM	4734	CD1	PHE	B	434	−22.164	51.316	55.926	1.00	44.36	B	C
ATOM	4735	CE1	PHE	B	434	−23.132	51.333	54.930	1.00	43.99	B	C
ATOM	4736	CZ	PHE	B	434	−24.409	50.862	55.207	1.00	46.41	B	C
ATOM	4737	CE2	PHE	B	434	−24.706	50.368	56.480	1.00	46.50	B	C
ATOM	4738	CD2	PHE	B	434	−23.727	50.350	57.457	1.00	43.77	B	C
ATOM	4739	C	PHE	B	434	−20.710	51.495	60.546	1.00	59.69	B	C
ATOM	4740	O	PHE	B	434	−20.254	50.362	60.763	1.00	58.41	B	O
ATOM	4741	N	SER	B	435	−20.405	52.553	61.288	1.00	61.94	B	N
ATOM	4742	CA	SER	B	435	−19.361	52.490	62.304	1.00	64.51	B	C
ATOM	4743	CB	SER	B	435	−18.734	53.869	62.507	1.00	64.60	B	C
ATOM	4744	OG	SER	B	435	−19.723	54.880	62.488	1.00	65.36	B	O
ATOM	4745	C	SER	B	435	−19.841	51.900	63.631	1.00	66.67	B	C
ATOM	4746	O	SER	B	435	−19.125	51.947	64.635	1.00	67.92	B	O
ATOM	4747	N	GLU	B	436	−21.045	51.332	63.632	1.00	68.21	B	N
ATOM	4748	CA	GLU	B	436	−21.578	50.691	64.833	1.00	68.82	B	C
ATOM	4749	CB	GLU	B	436	−22.713	51.525	65.412	1.00	69.36	B	C
ATOM	4750	CG	GLU	B	436	−22.218	52.768	66.124	1.00	71.12	B	C
ATOM	4751	CD	GLU	B	436	−23.180	53.228	67.190	1.00	73.99	B	C
ATOM	4752	OE1	GLU	B	436	−24.040	54.080	66.878	1.00	75.03	B	O
ATOM	4753	OE2	GLU	B	436	−23.079	52.731	68.333	1.00	75.48	B	O
ATOM	4754	C	GLU	B	436	−22.003	49.230	64.633	1.00	68.01	B	C
ATOM	4755	O	GLU	B	436	−22.383	48.555	65.602	1.00	67.22	B	O
ATOM	4756	N	VAL	B	437	−21.904	48.750	63.386	1.00	65.67	B	N
ATOM	4757	CA	VAL	B	437	−22.197	47.354	63.009	1.00	60.81	B	C
ATOM	4758	CB	VAL	B	437	−23.421	47.248	62.059	1.00	60.54	B	C
ATOM	4759	CG1	VAL	B	437	−24.699	47.669	62.761	1.00	62.37	B	C
ATOM	4760	CG2	VAL	B	437	−23.206	48.075	60.798	1.00	60.85	B	C
ATOM	4761	C	VAL	B	437	−20.995	46.679	62.331	1.00	57.32	B	C
ATOM	4762	O	VAL	B	437	−20.110	47.370	61.812	1.00	55.78	B	O
ATOM	4763	N	LEU	B	438	−20.980	45.339	62.334	1.00	52.98	B	N
ATOM	4764	CA	LEU	B	438	−19.895	44.548	61.727	1.00	49.77	B	C
ATOM	4765	CB	LEU	B	438	−19.444	43.414	62.667	1.00	49.82	B	C
ATOM	4766	CG	LEU	B	438	−18.042	42.764	62.637	1.00	49.14	B	C
ATOM	4767	CD1	LEU	B	438	−18.127	41.240	62.819	1.00	47.45	B	C
ATOM	4768	CD2	LEU	B	438	−17.194	43.113	61.406	1.00	47.89	B	C
ATOM	4769	C	LEU	B	438	−20.257	43.975	60.347	1.00	48.76	B	C
ATOM	4770	O	LEU	B	438	−20.828	42.878	60.248	1.00	47.95	B	O
ATOM	4771	N	LEU	B	439	−19.913	44.727	59.296	1.00	45.69	B	N
ATOM	4772	CA	LEU	B	439	−20.106	44.305	57.910	1.00	40.13	B	C
ATOM	4773	CB	LEU	B	439	−19.723	45.427	56.962	1.00	36.46	B	C
ATOM	4774	CG	LEU	B	439	−20.577	46.684	57.053	1.00	39.82	B	C
ATOM	4775	CD1	LEU	B	439	−19.976	47.807	56.216	1.00	38.71	B	C
ATOM	4776	CD2	LEU	B	439	−22.007	46.400	56.625	1.00	43.44	B	C
ATOM	4777	C	LEU	B	439	−19.258	43.080	57.631	1.00	40.26	B	C
ATOM	4778	O	LEU	B	439	−18.054	43.083	57.883	1.00	42.45	B	O
ATOM	4779	N	THR	B	440	−19.889	42.023	57.135	1.00	37.08	B	N
ATOM	4780	CA	THR	B	440	−19.215	40.739	57.017	1.00	34.37	B	C
ATOM	4781	CB	THR	B	440	−19.895	39.677	57.883	1.00	34.54	B	C
ATOM	4782	OG1	THR	B	440	−21.305	39.699	57.643	1.00	34.99	B	O
ATOM	4783	CG2	THR	B	440	−19.766	40.012	59.361	1.00	38.15	B	C
ATOM	4784	C	THR	B	440	−19.232	40.257	55.602	1.00	35.73	B	C
ATOM	4785	O	THR	B	440	−18.657	39.208	55.301	1.00	38.80	B	O
ATOM	4786	N	SER	B	441	−19.900	41.006	54.732	1.00	33.65	B	N
ATOM	4787	CA	SER	B	441	−19.974	40.613	53.337	1.00	36.43	B	C
ATOM	4788	CB	SER	B	441	−20.985	39.476	53.181	1.00	35.52	B	C
ATOM	4789	OG	SER	B	441	−21.583	39.526	51.900	1.00	44.41	B	O
ATOM	4790	C	SER	B	441	−20.279	41.780	52.384	1.00	38.69	B	C
ATOM	4791	O	SER	B	441	−21.182	42.570	52.629	1.00	44.18	B	O
ATOM	4792	N	ILE	B	442	−19.520	41.883	51.298	1.00	39.13	B	N
ATOM	4793	CA	ILE	B	442	−19.767	42.918	50.287	1.00	37.48	B	C
ATOM	4794	CB	ILE	B	442	−18.750	44.080	50.391	1.00	37.49	B	C
ATOM	4795	CG1	ILE	B	442	−18.952	45.067	49.241	1.00	36.31	B	C
ATOM	4796	CD1	ILE	B	442	−18.239	46.385	49.411	1.00	37.95	B	C
ATOM	4797	CG2	ILE	B	442	−17.308	43.552	50.369	1.00	40.87	B	C
ATOM	4798	C	ILE	B	442	−19.741	42.353	48.875	1.00	35.99	B	C
ATOM	4799	O	ILE	B	442	−19.038	41.371	48.589	1.00	41.60	B	O
ATOM	4800	N	SER	B	443	−20.496	43.011	48.007	1.00	24.89	B	N
ATOM	4801	CA	SER	B	443	−20.629	42.656	46.618	1.00	24.75	B	C
ATOM	4802	CB	SER	B	443	−21.674	41.540	46.490	1.00	26.63	B	C
ATOM	4803	OG	SER	B	443	−22.647	41.816	45.507	1.00	31.94	B	O
ATOM	4804	C	SER	B	443	−21.032	43.969	45.924	1.00	28.80	B	C
ATOM	4805	O	SER	B	443	−21.431	44.926	46.603	1.00	33.49	B	O
ATOM	4806	N	THR	B	444	−20.930	44.045	44.597	1.00	26.26	B	N
ATOM	4807	CA	THR	B	444	−21.014	45.339	43.927	1.00	29.84	B	C
ATOM	4808	CB	THR	B	444	−19.618	46.001	43.918	1.00	31.03	B	C
ATOM	4809	OG1	THR	B	444	−19.448	46.780	45.114	1.00	32.86	B	O
ATOM	4810	CG2	THR	B	444	−19.518	47.038	42.810	1.00	34.52	B	C
ATOM	4811	C	THR	B	444	−21.592	45.304	42.512	1.00	35.65	B	C
ATOM	4812	O	THR	B	444	−21.283	44.406	41.723	1.00	37.14	B	O
ATOM	4813	N	PHE	B	445	−22.419	46.294	42.176	1.00	39.23	B	N
ATOM	4814	CA	PHE	B	445	−22.930	46.380	40.807	1.00	43.15	B	C
ATOM	4815	CB	PHE	B	445	−24.112	45.419	40.562	1.00	41.98	B	C
ATOM	4816	CG	PHE	B	445	−25.347	45.754	41.329	1.00	44.70	B	C
ATOM	4817	CD1	PHE	B	445	−26.443	46.316	40.687	1.00	47.35	B	C
ATOM	4818	CE1	PHE	B	445	−27.611	46.622	41.386	1.00	46.24	B	C
ATOM	4819	CZ	PHE	B	445	−27.688	46.358	42.746	1.00	47.03	B	C
ATOM	4820	CE2	PHE	B	445	−26.603	45.793	43.401	1.00	49.40	B	C
ATOM	4821	CD2	PHE	B	445	−25.435	45.491	42.689	1.00	48.57	B	C
ATOM	4822	C	PHE	B	445	−23.256	47.778	40.320	1.00	45.35	B	C
ATOM	4823	O	PHE	B	445	−23.404	48.720	41.113	1.00	43.42	B	O
ATOM	4824	N	ILE	B	446	−23.350	47.887	38.994	1.00	46.73	B	N
ATOM	4825	CA	ILE	B	446	−23.651	49.144	38.320	1.00	43.12	B	C
ATOM	4826	CB	ILE	B	446	−22.786	49.303	37.034	1.00	38.88	B	C
ATOM	4827	CG1	ILE	B	446	−21.293	49.483	37.358	1.00	34.98	B	C
ATOM	4828	CD1	ILE	B	446	−20.344	49.107	36.186	1.00	30.34	B	C
ATOM	4829	CG2	ILE	B	446	−23.278	50.468	36.201	1.00	39.10	B	C
ATOM	4830	C	ILE	B	446	−25.120	49.151	37.944	1.00	43.23	B	C
ATOM	4831	O	ILE	B	446	−25.637	48.157	37.447	1.00	45.02	B	O
ATOM	4832	N	LYS	B	447	−25.794	50.265	38.206	1.00	47.38	B	N
ATOM	4833	CA	LYS	B	447	−27.074	50.566	37.558	1.00	50.70	B	C
ATOM	4834	CB	LYS	B	447	−28.255	50.536	38.543	1.00	55.97	B	C
ATOM	4835	CG	LYS	B	447	−29.283	49.425	38.266	1.00	60.13	B	C
ATOM	4836	CD	LYS	B	447	−30.344	49.858	37.234	1.00	63.00	B	C
ATOM	4837	CE	LYS	B	447	−30.918	48.661	36.457	1.00	61.30	B	C
ATOM	4838	NZ	LYS	B	447	−30.831	48.836	34.979	1.00	58.41	B	N
ATOM	4839	C	LYS	B	447	−26.934	51.932	36.906	1.00	45.71	B	C
ATOM	4840	O	LYS	B	447	−26.796	52.942	37.591	1.00	42.70	B	O
ATOM	4841	N	GLY	B	448	−26.926	51.941	35.579	1.00	43.97	B	N
ATOM	4842	CA	GLY	B	448	−26.660	53.147	34.820	1.00	47.86	B	C
ATOM	4843	C	GLY	B	448	−25.401	53.871	35.255	1.00	48.53	B	C
ATOM	4844	O	GLY	B	448	−24.299	53.495	34.882	1.00	50.36	B	O
ATOM	4845	N	ASP	B	449	−25.569	54.917	36.049	1.00	51.47	B	N
ATOM	4846	CA	ASP	B	449	−24.435	55.695	36.521	1.00	56.72	B	C
ATOM	4847	CB	ASP	B	449	−24.756	57.187	36.451	1.00	63.14	B	C
ATOM	4848	CG	ASP	B	449	−24.788	57.712	35.022	1.00	69.19	B	C
ATOM	4849	OD1	ASP	B	449	−24.985	56.905	34.079	1.00	72.01	B	O
ATOM	4850	OD2	ASP	B	449	−24.627	58.923	34.747	1.00	70.41	B	O
ATOM	4851	C	ASP	B	449	−24.086	55.302	37.940	1.00	56.41	B	C
ATOM	4852	O	ASP	B	449	−23.024	55.644	38.458	1.00	59.77	B	O
ATOM	4853	N	LEU	B	450	−24.982	54.559	38.563	1.00	54.31	B	N
ATOM	4854	CA	LEU	B	450	−24.849	54.265	39.970	1.00	54.00	B	C
ATOM	4855	CB	LEU	B	450	−26.228	54.064	40.579	1.00	49.47	B	C
ATOM	4856	CG	LEU	B		450	−27.011	55.358	40.763	1.00	45.84	B	C
ATOM	4857	CD1	LEU	B	450	−28.188	55.102	41.673	1.00	45.47	B	C
ATOM	4858	CD2	LEU	B		450	−26.113	56.458	41.319	1.00	43.49	B	C
ATOM	4859	C	LEU	B	450	−23.992	53.047	40.214	1.00	58.29	B	C
ATOM	4860	O	LEU	B	450	−24.019	52.093	39.428	1.00	60.64	B	O
ATOM	4861	N	THR	B	451	−23.228	53.093	41.306	1.00	59.31	B	N
ATOM	4862	CA	THR	B	451	−22.509	51.918	41.813	1.00	55.51	B	C
ATOM	4863	CB	THR	B	451	−21.010	52.252	42.009	1.00	53.64	B	C
ATOM	4864	OG1	THR	B	451	−20.370	52.312	40.728	1.00	55.62	B	O
ATOM	4865	CG2	THR	B	451	−20.280	51.137	42.722	1.00	46.00	B	C
ATOM	4866	C	THR	B	451	−23.164	51.458	43.117	1.00	51.77	B	C
ATOM	4867	O	THR	B	451	−23.294	52.240	44.065	1.00	49.91	B	O
ATOM	4868	N	ILE	B	452	−23.590	50.198	43.155	1.00	49.75	B	N
ATOM	4869	CA	ILE	B	452	−24.301	49.679	44.329	1.00	45.76	B	C
ATOM	4870	CB	ILE	B	452	−25.751	49.322	43.975	1.00	40.39	B	C
ATOM	4871	CG1	ILE	B	452	−26.520	50.598	43.645	1.00	36.18	B	C
ATOM	4872	CD1	ILE	B	452	−27.881	50.350	43.055	1.00	37.39	B	C
ATOM	4873	CG2	ILE	B	452	−26.415	48.592	45.137	1.00	39.83	B	C
ATOM	4874	C	ILE	B	452	−23.622	48.535	45.095	1.00	44.89	B	C
ATOM	4875	O	ILE	B	452	−23.334	47.467	44.541	1.00	43.92	B	O
ATOM	4876	N	ALA	B	453	−23.387	48.786	46.379	1.00	43.54	B	N
ATOM	4877	CA	ALA	B	453	−22.919	47.770	47.308	1.00	44.19	B	C
ATOM	4878	CB	ALA	B	453	−22.318	48.427	48.516	1.00	44.73	B	C
ATOM	4879	C	ALA	B	453	−24.065	46.872	47.749	1.00	44.71	B	C
ATOM	4880	O	ALA	B	453	−25.180	47.348	47.990	1.00	45.36	B	O
ATOM	4881	N	ASN	B	454	−23.781	45.576	47.842	1.00	40.95	B	N
ATOM	4882	CA	ASN	B	454	−24.655	44.623	48.514	1.00	41.90	B	C
ATOM	4883	CB	ASN	B	454	−24.845	43.368	47.655	1.00	42.70	B	C
ATOM	4884	CG	ASN	B	454	−25.754	43.598	46.475	1.00	42.78	B	C
ATOM	4885	OD1	ASN	B	454	−26.895	44.022	46.644	1.00	48.51	B	O
ATOM	4886	ND2	ASN	B	454	−25.264	43.308	45.269	1.00	36.52	B	N
ATOM	4887	C	ASN	B	454	−24.012	44.251	49.852	1.00	44.33	B	C
ATOM	4888	O	ASN	B	454	−22.978	43.565	49.890	1.00	52.12	B	O
ATOM	4889	N	LEU	B	455	−24.604	44.687	50.952	1.00	39.41	B	N
ATOM	4890	CA	LEU	B	455	−23.942	44.508	52.234	1.00	41.76	B	C
ATOM	4891	CB	LEU	B	455	−23.848	45.837	52.963	1.00	44.00	B	C
ATOM	4892	CG	LEU	B	455	−22.929	46.833	52.269	1.00	46.17	B	C
ATOM	4893	CD1	LEU	B	455	−22.703	48.020	53.179	1.00	49.05	B	C
ATOM	4894	CD2	LEU	B	455	−21.610	46.176	51.897	1.00	47.33	B	C
ATOM	4895	C	LEU	B	455	−24.575	43.459	53.125	1.00	44.02	B	C
ATOM	4896	O	LEU	B	455	−25.768	43.190	53.021	1.00	50.25	B	O
ATOM	4897	N	GLY	B	456	−23.759	42.879	54.002	1.00	41.74	B	N
ATOM	4898	CA	GLY	B	456	−24.182	41.846	54.933	1.00	43.52	B	C
ATOM	4899	C	GLY	B	456	−23.527	42.039	56.291	1.00	48.25	B	C
ATOM	4900	O	GLY	B	456	−22.424	42.592	56.390	1.00	50.51	B	O
ATOM	4901	N	THR	B	457	−24.195	41.556	57.335	1.00	49.52	B	N
ATOM	4902	CA	THR	B	457	−23.906	41.955	58.711	1.00	51.08	B	C
ATOM	4903	CB	THR	B	457	−24.976	42.970	59.152	1.00	52.55	B	C
ATOM	4904	OG1	THR	B	457	−24.848	44.155	58.360	1.00	51.16	B	O
ATOM	4905	CG2	THR	B	457	−24.737	43.468	60.578	1.00	56.96	B	C
ATOM	4906	C	THR	B	457	−23.911	40.759	59.654	1.00	50.98	B	C
ATOM	4907	O	THR	B	457	−24.577	39.765	59.388	1.00	54.42	B	O
ATOM	4908	N	SER	B	458	−23.182	40.865	60.761	1.00	48.51	B	N
ATOM	4909	CA	SER	B	458	−23.175	39.810	61.764	1.00	52.73	B	C
ATOM	4910	CB	SER	B	458	−22.139	40.088	62.852	1.00	55.88	B	C
ATOM	4911	OG	SER	B	458	−21.805	41.459	62.901	1.00	60.09	B	O
ATOM	4912	C	SER	B	458	−24.549	39.588	62.398	1.00	56.80	B	C
ATOM	4913	O	SER	B	458	−24.846	38.479	62.858	1.00	57.21	B	O
ATOM	4914	N	GLU	B	459	−25.378	40.634	62.423	1.00	60.11	B	N
ATOM	4915	CA	GLU	B	459	−26.721	40.546	63.008	1.00	62.67	B	C
ATOM	4916	CB	GLU	B	459	−27.235	41.929	63.451	1.00	69.19	B	C
ATOM	4917	CG	GLU	B	459	−28.035	41.934	64.760	1.00	77.41	B	C
ATOM	4918	CD	GLU	B	459	−28.984	43.142	64.927	1.00	83.69	B	C
ATOM	4919	OE1	GLU	B	459	−29.075	44.007	64.014	1.00	85.31	B	O
ATOM	4920	OE2	GLU	B	459	−29.656	43.235	65.991	1.00	84.05	B	O
ATOM	4921	C	GLU	B	459	−27.701	39.850	62.049	1.00	58.99	B	C
ATOM	4922	O	GLU	B	459	−28.800	39.458	62.449	1.00	61.26	B	O
ATOM	4923	N	GLY	B	460	−27.290	39.678	60.796	1.00	52.54	B	N
ATOM	4924	CA	GLY	B	460	−28.113	39.003	59.812	1.00	51.41	B	C
ATOM	4925	C	GLY	B	460	−28.703	39.949	58.779	1.00	54.46	B	C
ATOM	4926	O	GLY	B	460	−29.418	39.523	57.868	1.00	56.75	B	O
ATOM	4927	N	ARG	B	461	−28.403	41.236	58.904	1.00	53.63	B	N
ATOM	4928	CA	ARG	B	461	−29.029	42.225	58.039	1.00	54.19	B	C
ATOM	4929	CB	ARG	B	461	−29.048	43.598	58.711	1.00	59.04	B	C
ATOM	4930	CG	ARG	B	461	−29.954	43.657	59.934	1.00	64.20	B	C
ATOM	4931	CD	ARG	B	461	−31.192	44.545	59.792	1.00	67.13	B	C
ATOM	4932	NE	ARG	B	461	−31.338	45.373	60.979	1.00	70.07	B	N
ATOM	4933	CZ	ARG	B	461	−30.687	46.515	61.172	1.00	74.01	B	C
ATOM	4934	NH1	ARG	B	461	−29.858	46.972	60.238	1.00	73.29	B	N
ATOM	4935	NH2	ARG	B	461	−30.864	47.207	62.296	1.00	76.45	B	N
ATOM	4936	C	ARG	B	461	−28.367	42.289	56.668	1.00	52.80	B	C
ATOM	4937	O	ARG	B	461	−27.141	42.358	56.566	1.00	52.65	B	O
ATOM	4938	N	PHE	B	462	−29.193	42.247	55.623	1.00	49.71	B	N
ATOM	4939	CA	PHE	B	462	−28.739	42.429	54.247	1.00	46.62	B	C
ATOM	4940	CB	PHE	B	462	−29.313	41.345	53.356	1.00	45.04	B	C
ATOM	4941	CG	PHE	B	462	−29.078	41.585	51.903	1.00	45.52	B	C
ATOM	4942	CD1	PHE	B	462	−27.916	41.136	51.294	1.00	46.69	B	C
ATOM	4943	CE1	PHE	B	462	−27.679	41.357	49.946	1.00	47.63	B	C
ATOM	4944	CZ	PHE	B	462	−28.613	42.032	49.191	1.00	52.02	B	C
ATOM	4945	CE2	PHE	B	462	−29.790	42.486	49.791	1.00	52.61	B	C
ATOM	4946	CD2	PHE	B	462	−30.012	42.260	51.141	1.00	48.34	B	C
ATOM	4947	C	PHE	B	462	−29.218	43.758	53.719	1.00	48.50	B	C
ATOM	4948	O	PHE	B	462	−30.392	44.086	53.874	1.00	53.90	B	O
ATOM	4949	N	MET	B	463	−28.346	44.519	53.066	1.00	48.12	B	N
ATOM	4950	CA	MET	B	463	−28.769	45.841	52.590	1.00	51.33	B	C
ATOM	4951	CB	MET	B	463	−28.715	46.868	53.723	1.00	51.90	B	C
ATOM	4952	CG	MET	B	463	−27.387	46.980	54.406	1.00	52.83	B	C
ATOM	4953	SD	MET	B	463	−27.615	47.955	55.864	1.00	54.23	B	S
ATOM	4954	CE	MET	B	463	−27.473	46.667	57.089	1.00	54.31	B	C
ATOM	4955	C	MET	B	463	−28.048	46.386	51.363	1.00	50.31	B	C
ATOM	4956	O	MET	B	463	−26.827	46.286	51.264	1.00	56.78	B	O
ATOM	4957	N	GLN	B	464	−28.820	46.978	50.453	1.00	42.79	B	N
ATOM	4958	CA	GLN	B	464	−28.297	47.571	49.230	1.00	40.97	B	C
ATOM	4959	CB	GLN	B	464	−29.272	47.344	48.067	1.00	42.04	B	C
ATOM	4960	CG	GLN	B	464	−29.567	45.888	47.717	1.00	42.69	B	C
ATOM	4961	CD	GLN	B	464	−30.184	45.723	46.318	1.00	44.59	B	C
ATOM	4962	OE1	GLN	B	464	−31.267	46.250	46.036	1.00	43.02	B	O
ATOM	4963	NE2	GLN	B	464	−29.492	44.985	45.446	1.00	45.35	B	N
ATOM	4964	C	GLN	B	464	−28.064	49.079	49.404	1.00	41.44	B	C
ATOM	4965	O	GLN	B	464	−29.013	49.830	49.649	1.00	41.15	B	O
ATOM	4966	N	VAL	B	465	−26.808	49.517	49.262	1.00	41.53	B	N
ATOM	4967	CA	VAL	B	465	−26.453	50.947	49.310	1.00	38.42	B	C
ATOM	4968	CB	VAL	B	465	−25.397	51.267	50.379	1.00	33.77	B	C
ATOM	4969	CG1	VAL	B	465	−25.309	52.770	50.585	1.00	27.24	B	C
ATOM	4970	CG2	VAL	B	465	−25.690	50.549	51.685	1.00	35.35	B	C
ATOM	4971	C	VAL	B	465	−25.857	51.451	48.003	1.00	41.08	B	C
ATOM	4972	O	VAL	B	465	−25.300	50.672	47.225	1.00	43.64	B	O
ATOM	4973	N	VAL	B	466	−25.961	52.765	47.792	1.00	40.30	B	N
ATOM	4974	CA	VAL	B	466	−25.289	53.456	46.694	1.00	37.42	B	C
ATOM	4975	CB	VAL	B	466	−26.139	54.619	46.132	1.00	29.50	B	C
ATOM	4976	CG1	VAL	B	466	−25.475	55.239	44.927	1.00	25.98	B	C
ATOM	4977	CG2	VAL	B	466	−27.513	54.130	45.750	1.00	28.27	B	C
ATOM	4978	C	VAL	B	466	−23.938	53.983	47.168	1.00	41.60	B	C
ATOM	4979	O	VAL	B	466	−23.828	54.595	48.230	1.00	44.30	B	O
ATOM	4980	N	VAL	B	467	−22.914	53.737	46.365	1.00	44.45	B	N
ATOM	4981	CA	VAL	B	467	−21.554	54.133	46.691	1.00	49.08	B	C
ATOM	4982	CB	VAL	B	467	−20.561	53.127	46.097	1.00	50.63	B	C
ATOM	4983	CG1	VAL	B	467	−19.166	53.354	46.650	1.00	52.55	B	C
ATOM	4984	CG2	VAL	B	467	−21.031	51.707	46.389	1.00	51.28	B	C
ATOM	4985	C	VAL	B	467	−21.252	55.533	46.169	1.00	51.76	B	C
ATOM	4986	O	VAL	B	467	−21.438	55.806	44.975	1.00	52.74	B	O
ATOM	4987	N	SER	B	468	−20.799	56.416	47.061	1.00	54.51	B	N
ATOM	4988	CA	SER	B	468	−20.439	57.787	46.673	1.00	58.45	B	C
ATOM	4989	CB	SER	B	468	−21.689	58.621	46.372	1.00	58.52	B	C
ATOM	4990	OG	SER	B	468	−21.343	59.852	45.764	1.00	57.13	B	O
ATOM	4991	C	SER	B	468	−19.589	58.522	47.702	1.00	60.39	B	C
ATOM	4992	O	SER	B	468	−19.705	58.283	48.905	1.00	63.74	B	O
ATOM	4993	N	ARG	B	469	−18.736	59.414	47.207	1.00	60.12	B	N
ATOM	4994	CA	ARG	B	469	−18.012	60.350	48.048	1.00	64.67	B	C
ATOM	4995	CB	ARG	B	469	−16.757	60.861	47.334	1.00	62.58	B	C
ATOM	4996	CG	ARG	B	469	−15.639	59.844	47.145	1.00	61.40	B	C
ATOM	4997	CD	ARG	B	469	−14.329	60.189	47.865	1.00	62.15	B	C
ATOM	4998	NE	ARG	B	469	−14.371	59.832	49.286	1.00	64.27	B	N
ATOM	4999	CZ	ARG	B	469	−13.932	58.678	49.802	1.00	68.65	B	C
ATOM	5000	NH1	ARG	B	469	−13.393	57.732	49.024	1.00	71.37	B	N
ATOM	5001	NH2	ARG	B	469	−14.034	58.463	51.109	1.00	67.94	B	N
ATOM	5002	C	ARG	B	469	−18.964	61.508	48.311	1.00	71.94	B	C
ATOM	5003	O	ARG	B	469	−19.378	61.747	49.446	1.00	72.50	B	O
ATOM	5004	N	SER	B	470	−19.317	62.209	47.234	1.00	79.52	B	N
ATOM	5005	CA	SER	B	470	−20.306	63.278	47.255	1.00	84.96	B	C
ATOM	5006	CB	SER	B	470	−20.197	64.117	45.977	1.00	87.60	B	C
ATOM	5007	OG	SER	B	470	−20.151	65.505	46.271	1.00	90.87	B	O
ATOM	5008	C	SER	B	470	−21.702	62.676	47.376	1.00	87.59	B	C
ATOM	5009	O	SER	B	470	−22.277	62.207	46.391	1.00	87.54	B	O
ATOM	5010	N	GLY	B	471	−22.240	62.695	48.591	1.00	91.10	B	N
ATOM	5011	CA	GLY	B	471	−23.490	62.023	48.893	1.00	96.12	B	C
ATOM	5012	C	GLY	B	471	−23.223	60.953	49.935	1.00	100.89	B	C
ATOM	5013	O	GLY	B	471	−22.493	59.993	49.663	1.00	102.51	B	O
ATOM	5014	N	PRO	B	472	−23.789	61.123	51.132	1.00	102.46	B	N
ATOM	5015	CA	PRO	B	472	−23.551	60.202	52.252	1.00	101.06	B	C
ATOM	5016	CB	PRO	B	472	−23.580	61.143	53.460	1.00	102.61	B	C
ATOM	5017	CG	PRO	B	472	−24.489	62.320	53.020	1.00	102.73	B	C
ATOM	5018	CD	PRO	B	472	−24.699	62.219	51.518	1.00	102.43	B	C
ATOM	5019	C	PRO	B	472	−24.675	59.172	52.358	1.00	98.22	B	C
ATOM	5020	O	PRO	B	472	−25.289	59.035	53.417	1.00	100.80	B	O
ATOM	5021	N	SER	B	473	−24.915	58.446	51.270	1.00	92.28	B	N
ATOM	5022	CA	SER	B	473	−26.193	57.768	51.055	1.00	85.23	B	C
ATOM	5023	CB	SER	B	473	−26.281	57.209	49.630	1.00	87.85	B	C
ATOM	5024	OG	SER	B	473	−26.618	58.236	48.708	1.00	89.36	B	O
ATOM	5025	C	SER	B	473	−26.603	56.715	52.088	1.00	76.93	B	C
ATOM	5026	O	SER	B	473	−25.769	56.014	52.685	1.00	71.07	B	O
ATOM	5027	N	THR	B	474	−27.916	56.651	52.286	1.00	71.17	B	N
ATOM	5028	CA	THR	B	474	−28.548	55.708	53.189	1.00	67.45	B	C
ATOM	5029	CB	THR	B	474	−29.644	56.393	54.018	1.00	68.82	B	C
ATOM	5030	OG1	THR	B	474	−30.325	57.345	53.199	1.00	69.66	B	O
ATOM	5031	CG2	THR	B	474	−29.040	57.239	55.145	1.00	69.65	B	C
ATOM	5032	C	THR	B	474	−29.170	54.608	52.351	1.00	63.31	B	C
ATOM	5033	O	THR	B	474	−29.694	54.870	51.267	1.00	60.40	B	O
ATOM	5034	N	PRO	B	475	−29.137	53.386	52.874	1.00	61.03	B	N
ATOM	5035	CA	PRO	B	475	−29.483	52.201	52.091	1.00	57.57	B	C
ATOM	5036	CB	PRO	B	475	−29.198	51.048	53.062	1.00	61.28	B	C
ATOM	5037	CG	PRO	B	475	−28.340	51.636	54.142	1.00	61.97	B	C
ATOM	5038	CD	PRO	B	475	−28.806	53.042	54.269	1.00	62.40	B	C
ATOM	5039	C	PRO	B	475	−30.947	52.204	51.716	1.00	52.11	B	C
ATOM	5040	O	PRO	B	475	−31.784	52.514	52.556	1.00	50.78	B	O
ATOM	5041	N	HIS	B	476	−31.243	51.868	50.470	1.00	49.87	B	N
ATOM	5042	CA	HIS	B	476	−32.625	51.779	50.025	1.00	52.15	B	C
ATOM	5043	CB	HIS	B	476	−32.746	52.159	48.557	1.00	56.56	B	C
ATOM	5044	CG	HIS	B	476	−31.676	51.576	47.702	1.00	58.73	B	C
ATOM	5045	ND1	HIS	B	476	−31.865	50.434	46.955	1.00	61.50	B	N
ATOM	5046	CE1	HIS	B	476	−30.752	50.148	46.306	1.00	63.67	B	C
ATOM	5047	NE2	HIS	B	476	−29.848	51.064	46.610	1.00	64.44	B	N
ATOM	5048	CD2	HIS	B	476	−30.400	51.966	47.485	1.00	59.29	B	C
ATOM	5049	C	HIS	B	476	−33.226	50.399	50.259	1.00	50.23	B	C
ATOM	5050	O	HIS	B	476	−34.445	50.229	50.180	1.00	53.09	B	O
ATOM	5051	N	VAL	B	477	−32.373	49.419	50.530	1.00	46.49	B	N
ATOM	5052	CA	VAL	B	477	−32.832	48.111	50.996	1.00	47.76	B	C
ATOM	5053	CB	VAL	B	477	−32.606	47.006	49.934	1.00	46.95	B	C
ATOM	5054	CG1	VAL	B	477	−32.646	45.618	50.565	1.00	47.09	B	C
ATOM	5055	CG2	VAL	B	477	−33.639	47.103	48.841	1.00	45.62	B	C
ATOM	5056	C	VAL	B	477	−32.144	47.758	52.326	1.00	49.84	B	C
ATOM	5057	O	VAL	B	477	−30.931	47.921	52.471	1.00	50.41	B	O
ATOM	5058	N	ASN	B	478	−32.930	47.291	53.292	1.00	49.08	B	N
ATOM	5059	CA	ASN	B	478	−32.428	46.989	54.625	1.00	47.03	B	C
ATOM	5060	CB	ASN	B	478	−32.276	48.274	55.430	1.00	42.47	B	C
ATOM	5061	CG	ASN	B	478	−31.610	48.049	56.764	1.00	42.92	B	C
ATOM	5062	OD1	ASN	B	478	−31.747	46.985	57.390	1.00	43.55	B	O
ATOM	5063	ND2	ASN	B	478	−30.882	49.057	57.219	1.00	43.21	B	N
ATOM	5064	C	ASN	B	478	−33.384	46.057	55.346	1.00	50.05	B	C
ATOM	5065	O	ASN	B	478	−34.540	46.422	55.584	1.00	53.51	B	O
ATOM	5066	N	PHE	B	479	−32.900	44.869	55.711	1.00	49.23	B	N
ATOM	5067	CA	PHE	B	479	−33.753	43.845	56.312	1.00	48.17	B	C
ATOM	5068	CB	PHE	B	479	−34.837	43.412	55.314	1.00	46.07	B	C
ATOM	5069	CG	PHE	B	479	−34.348	42.487	54.247	1.00	42.47	B	C
ATOM	5070	CD1	PHE	B	479	−34.525	41.111	54.371	1.00	44.25	B	C
ATOM	5071	CE1	PHE	B	479	−34.072	40.238	53.387	1.00	45.91	B	C
ATOM	5072	CZ	PHE	B	479	−33.447	40.747	52.254	1.00	45.90	B	C
ATOM	5073	CE2	PHE	B	479	−33.276	42.125	52.117	1.00	45.61	B	C
ATOM	5074	CD2	PHE	B	479	−33.722	42.984	53.116	1.00	42.76	B	C
ATOM	5075	C	PHE	B	479	−33.015	42.608	56.846	1.00	49.08	B	C
ATOM	5076	O	PHE	B	479	−31.814	42.428	56.618	1.00	50.71	B	O
ATOM	5077	N	LEU	B	480	−33.772	41.749	57.530	1.00	46.27	B	N
ATOM	5078	CA	LEU	B	480	−33.249	40.559	58.177	1.00	44.17	B	C
ATOM	5079	CB	LEU	B	480	−34.053	40.279	59.445	1.00	41.95	B	C
ATOM	5080	CG	LEU	B	480	−33.432	40.258	60.850	1.00	41.22	B	C
ATOM	5081	CD1	LEU	B	480	−33.112	38.820	61.275	1.00	41.81	B	C
ATOM	5082	CD2	LEU	B	480	−32.216	41.165	61.000	1.00	38.89	B	C
ATOM	5083	C	LEU	B		480	−33.282	39.324	57.277	1.00	49.14	B	C
ATOM	5084	O	LEU	B	480	−34.350	38.875	56.853	1.00	50.31	B	O
ATOM	5085	N	LEU	B	481	−32.097	38.800	56.974	1.00	51.40	B	N
ATOM	5086	CA	LEU	B	481	−31.942	37.423	56.533	1.00	52.20	B	C
ATOM	5087	CB	LEU	B	481	−30.746	37.309	55.607	1.00	51.29	B	C
ATOM	5088	CG	LEU	B	481	−30.934	37.705	54.147	1.00	51.97	B	C
ATOM	5089	CD1	LEU	B	481	−29.604	37.552	53.419	1.00	49.65	B	C
ATOM	5090	CD2	LEU	B	481	−32.024	36.870	53.474	1.00	52.97	B	C
ATOM	5091	C	LEU	B	481	−31.714	36.573	57.782	1.00	57.76	B	C
ATOM	5092	O	LEU	B	481	−31.457	37.115	58.867	1.00	58.80	B	O
ATOM	5093	N	ASP	B	482	−31.784	35.251	57.638	1.00	64.02	B	N
ATOM	5094	CA	ASP	B	482	−31.758	34.344	58.799	1.00	72.45	B	C
ATOM	5095	CB	ASP	B	482	−31.563	32.892	58.370	1.00	76.40	B	C
ATOM	5096	CG	ASP	B	482	−32.823	32.303	57.791	1.00	82.98	B	C
ATOM	5097	OD1	ASP	B	482	−32.919	32.251	56.542	1.00	85.28	B	O
ATOM	5098	OD2	ASP	B	482	−33.778	31.897	58.502	1.00	84.14	B	O
ATOM	5099	C	ASP	B	482	−30.771	34.709	59.896	1.00	72.93	B	C
ATOM	5100	O	ASP	B	482	−29.630	35.038	59.623	1.00	74.57	B	O
ATOM	5101	N	SER	B	483	−31.244	34.649	61.135	1.00	73.97	B	N
ATOM	5102	CA	SER	B	483	−30.507	35.101	62.318	1.00	74.74	B	C
ATOM	5103	CB	SER	B	483	−31.111	34.477	63.577	1.00	77.91	B	C
ATOM	5104	OG	SER	B	483	−32.362	33.876	63.292	1.00	81.95	B	O
ATOM	5105	C	SER	B	483	−28.996	34.859	62.309	1.00	73.44	B	C
ATOM	5106	O	SER	B	483	−28.259	35.552	63.009	1.00	74.47	B	O
ATOM	5107	N	HIS	B	484	−28.539	33.880	61.531	1.00	69.37	B	N
ATOM	5108	CA	HIS	B	484	−27.114	33.600	61.427	1.00	67.50	B	C
ATOM	5109	CB	HIS	B	484	−26.894	32.195	60.857	1.00	78.88	B	C
ATOM	5110	CG	HIS	B	484	−27.277	31.090	61.801	1.00	89.66	B	C
ATOM	5111	ND1	HIS	B	484	−27.930	31.316	62.999	1.00	93.08	B	N
ATOM	5112	CE1	HIS	B	484	−28.131	30.165	63.616	1.00	94.13	B	C
ATOM	5113	NE2	HIS	B	484	−27.633	29.198	62.863	1.00	95.47	B	N
ATOM	5114	CD2	HIS	B	484	−27.093	29.749	61.723	1.00	92.90	B	C
ATOM	5115	C	HIS	B	484	−26.426	34.673	60.578	1.00	58.79	B	C
ATOM	5116	O	HIS	B	484	−27.027	35.178	59.638	1.00	56.11	B	O
ATOM	5117	N	PRO	B	485	−25.175	35.022	60.893	1.00	53.92	B	N
ATOM	5118	CA	PRO	B	485	−24.482	36.124	60.207	1.00	49.97	B	C
ATOM	5119	CB	PRO	B	485	−23.048	36.028	60.746	1.00	47.43	B	C
ATOM	5120	CG	PRO	B	485	−23.162	35.349	62.017	1.00	49.05	B	C
ATOM	5121	CD	PRO	B	485	−24.305	34.378	61.893	1.00	53.07	B	C
ATOM	5122	C	PRO	B	485	−24.464	35.955	58.692	1.00	49.45	B	C
ATOM	5123	O	PRO	B	485	−24.781	34.876	58.193	1.00	52.13	B	O
ATOM	5124	N	VAL	B	486	−24.091	37.006	57.969	1.00	49.91	B	N
ATOM	5125	CA	VAL	B	486	−23.974	36.925	56.510	1.00	51.43	B	C
ATOM	5126	CB	VAL	B	486	−24.359	38.252	55.823	1.00	51.96	B	C
ATOM	5127	CG1	VAL	B	486	−24.307	38.106	54.321	1.00	51.08	B	C
ATOM	5128	CG2	VAL	B	486	−25.749	38.696	56.258	1.00	53.12	B	C
ATOM	5129	C	VAL	B	486	−22.562	36.498	56.106	1.00	50.68	B	C
ATOM	5130	O	VAL	B	486	−21.572	36.985	56.656	1.00	53.67	B	O
ATOM	5131	N	SER	B	487	−22.478	35.583	55.147	1.00	47.61	B	N
ATOM	5132	CA	SER	B	487	−21.204	34.984	54.780	1.00	42.82	B	C
ATOM	5133	CB	SER	B	487	−21.408	33.541	54.319	1.00	43.71	B	C
ATOM	5134	OG	SER	B	487	−20.368	33.132	53.457	1.00	44.64	B	O
ATOM	5135	C	SER	B	487	−20.519	35.801	53.701	1.00	39.94	B	C
ATOM	5136	O	SER	B	487	−21.190	36.324	52.792	1.00	37.15	B	O
ATOM	5137	N	PRO	B	488	−19.187	35.889	53.795	1.00	38.13	B	N
ATOM	5138	CA	PRO	B	488	−18.388	36.671	52.843	1.00	40.98	B	C
ATOM	5139	CB	PRO	B	488	−16.990	36.684	53.481	1.00	35.56	B	C
ATOM	5140	CG	PRO	B	488	−16.944	35.471	54.289	1.00	32.78	B	C
ATOM	5141	CD	PRO	B	488	−18.335	35.240	54.805	1.00	32.47	B	C
ATOM	5142	C	PRO	B	488	−18.359	36.006	51.467	1.00	44.47	B	C
ATOM	5143	O	PRO	B	488	−18.133	36.692	50.465	1.00	46.31	B	O
ATOM	5144	N	GLU	B	489	−18.597	34.694	51.428	1.00	45.82	B	N
ATOM	5145	CA	GLU	B	489	−18.694	33.967	50.171	1.00	47.70	B	C
ATOM	5146	CB	GLU	B	489	−18.602	32.461	50.409	1.00	50.47	B	C
ATOM	5147	CG	GLU	B	489	−17.273	31.990	50.995	1.00	62.01	B	C
ATOM	5148	CD	GLU	B	489	−16.042	32.659	50.383	1.00	71.18	B	C
ATOM	5149	OE1	GLU	B	489	−15.157	33.106	51.163	1.00	72.92	B	O
ATOM	5150	OE2	GLU	B	489	−15.946	32.727	49.129	1.00	75.99	B	O
ATOM	5151	C	GLU	B	489	−19.991	34.336	49.467	1.00	47.82	B	C
ATOM	5152	O	GLU	B	489	−21.071	34.064	49.984	1.00	52.07	B	O
ATOM	5153	N	VAL	B	490	−19.885	34.984	48.305	1.00	44.97	B	N
ATOM	5154	CA	VAL	B	490	−21.065	35.520	47.619	1.00	41.07	B	C
ATOM	5155	CB	VAL	B	490	−21.256	37.023	47.926	1.00	41.20	B	C
ATOM	5156	CG1	VAL	B	490	−21.323	37.267	49.440	1.00	45.24	B	C
ATOM	5157	CG2	VAL	B	490	−20.156	37.855	47.311	1.00	36.78	B	C
ATOM	5158	C	VAL	B	490	−20.991	35.353	46.117	1.00	42.15	B	C
ATOM	5159	O	VAL	B	490	−19.899	35.341	45.552	1.00	48.59	B	O
ATOM	5160	N	ILE	B	491	−22.150	35.242	45.470	1.00	40.75	B	N
ATOM	5161	CA	ILE	B	491	−22.215	35.204	44.001	1.00	41.60	B	C
ATOM	5162	CB	ILE	B	491	−22.684	33.818	43.526	1.00	36.63	B	C
ATOM	5163	CG1	ILE	B	491	−21.562	32.824	43.740	1.00	43.17	B	C
ATOM	5164	CD1	ILE	B	491	−21.483	31.715	42.697	1.00	53.37	B	C
ATOM	5165	CG2	ILE	B	491	−23.050	33.833	42.066	1.00	35.14	B	C
ATOM	5166	C	ILE	B	491	−23.084	36.329	43.393	1.00	44.75	B	C
ATOM	5167	O	ILE	B	491	−24.221	36.577	43.841	1.00	43.94	B	O
ATOM	5168	N	VAL	B	492	−22.544	37.007	42.380	1.00	41.70	B	N
ATOM	5169	CA	VAL	B	492	−23.348	37.943	41.595	1.00	43.44	B	C
ATOM	5170	CB	VAL	B	492	−22.767	39.368	41.599	1.00	40.20	B	C
ATOM	5171	CG1	VAL	B	492	−23.561	40.274	40.664	1.00	38.26	B	C
ATOM	5172	CG2	VAL	B	492	−22.761	39.937	42.984	1.00	37.76	B	C
ATOM	5173	C	VAL	B	492	−23.439	37.456	40.158	1.00	47.34	B	C
ATOM	5174	O	VAL	B	492	−22.437	37.132	39.557	1.00	52.98	B	O
ATOM	5175	N	GLU	B	493	−24.633	37.390	39.599	1.00	53.09	B	N
ATOM	5176	CA	GLU	B	493	−24.717	37.032	38.200	1.00	62.17	B	C
ATOM	5177	CB	GLU	B	493	−25.062	35.575	38.000	1.00	64.03	B	C
ATOM	5178	CG	GLU	B	493	−24.305	35.007	36.815	1.00	66.27	B	C
ATOM	5179	CD	GLU	B	493	−25.195	34.219	35.890	1.00	66.33	B	C
ATOM	5180	OE1	GLU	B	493	−26.290	33.805	36.332	1.00	66.86	B	O
ATOM	5181	OE2	GLU	B	493	−24.785	33.998	34.731	1.00	68.08	B	O
ATOM	5182	C	GLU	B	493	−25.683	37.881	37.444	1.00	68.85	B	C
ATOM	5183	O	GLU	B	493	−26.852	37.964	37.794	1.00	71.46	B	O
ATOM	5184	N	HIS	B	494	−25.176	38.484	36.380	1.00	74.96	B	N
ATOM	5185	CA	HIS	B	494	−25.947	39.409	35.583	1.00	78.80	B	C
ATOM	5186	CB	HIS	B	494	−25.019	40.425	34.932	1.00	78.18	B	C
ATOM	5187	CG	HIS	B	494	−24.054	41.053	35.883	1.00	74.88	B	C
ATOM	5188	ND1	HIS	B	494	−24.363	42.176	36.618	1.00	72.93	B	N
ATOM	5189	CE1	HIS	B	494	−23.325	42.502	37.367	1.00	75.94	B	C
ATOM	5190	NE2	HIS	B	494	−22.356	41.632	37.144	1.00	76.91	B	N
ATOM	5191	CD2	HIS	B	494	−22.787	40.715	36.218	1.00	76.17	B	C
ATOM	5192	C	HIS	B	494	−26.747	38.689	34.520	1.00	84.27	B	C
ATOM	5193	O	HIS	B	494	−26.450	37.560	34.149	1.00	85.88	B	O
ATOM	5194	N	THR	B	495	−27.778	39.363	34.045	1.00	93.42	B	N
ATOM	5195	CA	THR	B	495	−28.557	38.892	32.922	1.00	103.57	B	C
ATOM	5196	CB	THR	B	495	−29.865	38.219	33.407	1.00	106.89	B	C
ATOM	5197	OG1	THR	B	495	−30.187	38.672	34.730	1.00	108.84	B	O
ATOM	5198	CG2	THR	B	495	−29.647	36.719	33.613	1.00	107.44	B	C
ATOM	5199	C	THR	B	495	−28.816	40.107	32.045	1.00	108.32	B	C
ATOM	5200	O	THR	B	495	−28.671	41.251	32.503	1.00	107.90	B	O
ATOM	5201	N	LEU	B	496	−29.174	39.860	30.786	1.00	113.43	B	N
ATOM	5202	CA	LEU	B	496	−29.323	40.925	29.792	1.00	116.98	B	C
ATOM	5203	CB	LEU	B	496	−29.878	40.365	28.478	1.00	118.11	B	C
ATOM	5204	CG	LEU	B	496	−29.179	40.837	27.198	1.00	119.60	B	C
ATOM	5205	CD1	LEU	B	496	−27.997	39.932	26.825	1.00	118.19	B	C
ATOM	5206	CD2	LEU	B	496	−30.188	40.949	26.047	1.00	121.39	B	C
ATOM	5207	C	LEU	B	496	−30.182	42.088	30.289	1.00	117.02	B	C
ATOM	5208	O	LEU	B	496	−31.197	41.868	30.957	1.00	117.36	B	O
ATOM	5209	N	ASN	B	497	−29.740	43.310	29.968	1.00	116.73	B	N
ATOM	5210	CA	ASN	B	497	−30.419	44.577	30.308	1.00	116.78	B	C
ATOM	5211	CB	ASN	B	497	−31.935	44.522	30.017	1.00	119.09	B	C
ATOM	5212	CG	ASN	B	497	−32.275	44.789	28.551	1.00	120.22	B	C
ATOM	5213	OD1	ASN	B	497	−31.749	44.140	27.643	1.00	121.41	B	O
ATOM	5214	ND2	ASN	B	497	−33.179	45.734	28.321	1.00	120.02	B	N
ATOM	5215	C	ASN	B	497	−30.144	45.112	31.728	1.00	114.89	B	C
ATOM	5216	O	ASN	B	497	−30.892	45.947	32.244	1.00	115.25	B	O
ATOM	5217	N	GLN	B	498	−29.073	44.617	32.349	1.00	112.39	B	N
ATOM	5218	CA	GLN	B	498	−28.541	45.155	33.614	1.00	109.04	B	C
ATOM	5219	CB	GLN	B	498	−28.317	46.680	33.522	1.00	108.39	B	C
ATOM	5220	CG	GLN	B	498	−27.048	47.177	34.216	1.00	108.33	B	C
ATOM	5221	CD	GLN	B	498	−26.557	48.511	33.672	1.00	108.37	B	C
ATOM	5222	OE1	GLN	B	498	−26.860	49.569	34.230	1.00	108.10	B	O
ATOM	5223	NE2	GLN	B	498	−25.794	48.464	32.586	1.00	108.25	B	N
ATOM	5224	C	GLN	B	498	−29.275	44.793	34.922	1.00	105.07	B	C
ATOM	5225	O	GLN	B	498	−29.174	45.532	35.909	1.00	104.96	B	O
ATOM	5226	N	ASN	B	499	−29.996	43.668	34.941	1.00	99.22	B	N
ATOM	5227	CA	ASN	B	499	−30.388	43.060	36.225	1.00	93.30	B	C
ATOM	5228	CB	ASN	B	499	−31.920	42.898	36.427	1.00	93.03	B	C
ATOM	5229	CG	ASN	B	499	−32.640	42.347	35.210	1.00	92.94	B	C
ATOM	5230	OD1	ASN	B	499	−33.119	43.106	34.368	1.00	93.01	B	O
ATOM	5231	ND2	ASN	B	499	−32.760	41.023	35.136	1.00	91.88	B	N
ATOM	5232	C	ASN	B	499	−29.579	41.797	36.559	1.00	86.53	B	C
ATOM	5233	O	ASN	B	499	−28.408	41.707	36.186	1.00	86.38	B	O
ATOM	5234	N	GLY	B	500	−30.195	40.843	37.260	1.00	78.18	B	N
ATOM	5235	CA	GLY	B	500	−29.510	39.665	37.771	1.00	67.60	B	C
ATOM	5236	C	GLY	B	500	−29.802	39.461	39.247	1.00	61.51	B	C
ATOM	5237	O	GLY	B	500	−30.786	39.989	39.748	1.00	68.61	B	O
ATOM	5238	N	TYR	B	501	−28.955	38.718	39.953	1.00	50.28	B	N
ATOM	5239	CA	TYR	B	501	−29.215	38.388	41.347	1.00	44.13	B	C
ATOM	5240	CB	TYR	B	501	−30.105	37.149	41.420	1.00	43.20	B	C
ATOM	5241	CG	TYR	B	501	−29.497	35.910	40.788	1.00	46.13	B	C
ATOM	5242	CD1	TYR	B	501	−28.689	35.035	41.535	1.00	50.06	B	C
ATOM	5243	CE1	TYR	B	501	−28.121	33.889	40.960	1.00	47.10	B	C
ATOM	5244	CZ	TYR	B	501	−28.360	33.610	39.628	1.00	46.87	B	C
ATOM	5245	OH	TYR	B	501	−27.809	32.486	39.048	1.00	43.18	B	O
ATOM	5246	CE2	TYR	B	501	−29.163	34.459	38.871	1.00	47.16	B	C
ATOM	5247	CD2	TYR	B	501	−29.725	35.603	39.453	1.00	44.69	B	C
ATOM	5248	C	TYR	B	501	−27.929	38.123	42.116	1.00	46.69	B	C
ATOM	5249	O	TYR	B	501	−26.900	37.838	41.518	1.00	52.06	B	O
ATOM	5250	N	THR	B	502	−27.992	38.208	43.443	1.00	44.56	B	N
ATOM	5251	CA	THR	B	502	−26.901	37.766	44.295	1.00	42.16	B	C
ATOM	5252	CB	THR	B	502	−26.597	38.772	45.369	1.00	43.95	B	C
ATOM	5253	OG1	THR	B	502	−26.543	40.071	44.795	1.00	51.23	B	O
ATOM	5254	CG2	THR	B	502	−25.186	38.570	45.902	1.00	45.26	B	C
ATOM	5255	C	THR	B	502	−27.386	36.550	45.003	1.00	46.82	B	C
ATOM	5256	O	THR	B	502	−28.552	36.500	45.423	1.00	47.28	B	O
ATOM	5257	N	LEU	B	503	−26.494	35.573	45.145	1.00	46.91	B	N
ATOM	5258	CA	LEU	B	503	−26.745	34.443	46.020	1.00	41.81	B	C
ATOM	5259	CB	LEU	B	503	−26.258	33.153	45.401	1.00	39.18	B	C
ATOM	5260	CG	LEU	B	503	−26.990	32.801	44.116	1.00	43.11	B	C
ATOM	5261	CD1	LEU	B	503	−26.080	31.952	43.246	1.00	49.37	B	C
ATOM	5262	CD2	LEU	B	503	−28.293	32.085	44.407	1.00	42.13	B	C
ATOM	5263	C	LEU	B	503	−26.031	34.721	47.317	1.00	43.62	B	C
ATOM	5264	O	LEU	B	503	−24.846	35.060	47.323	1.00	45.71	B	O
ATOM	5265	N	VAL	B	504	−26.766	34.589	48.416	1.00	43.24	B	N
ATOM	5266	CA	VAL	B	504	−26.293	35.037	49.714	1.00	38.51	B	C
ATOM	5267	CB	VAL	B	504	−26.956	36.339	50.069	1.00	30.99	B	C
ATOM	5268	CG1	VAL	B	504	−26.314	36.928	51.274	1.00	32.01	B	C
ATOM	5269	CG2	VAL	B	504	−26.845	37.291	48.900	1.00	28.27	B	C
ATOM	5270	C	VAL	B	504	−26.514	34.012	50.823	1.00	44.16	B	C
ATOM	5271	O	VAL	B	504	−27.659	33.706	51.195	1.00	40.91	B	O
ATOM	5272	N	ILE	B	505	−25.387	33.506	51.338	1.00	51.60	B	N
ATOM	5273	CA	ILE	B	505	−25.326	32.444	52.357	1.00	52.85	B	C
ATOM	5274	CB	ILE	B	505	−24.007	31.652	52.218	1.00	55.32	B	C
ATOM	5275	CG1	ILE	B	505	−23.946	30.935	50.872	1.00	55.99	B	C
ATOM	5276	CD1	ILE	B	505	−22.711	31.244	50.082	1.00	58.09	B	C
ATOM	5277	CG2	ILE	B	505	−23.855	30.648	53.350	1.00	58.75	B	C
ATOM	5278	C	ILE	B	505	−25.432	32.974	53.789	1.00	51.35	B	C
ATOM	5279	O	ILE	B	505	−24.711	33.897	54.181	1.00	52.97	B	O
ATOM	5280	N	THR	B	506	−26.315	32.358	54.565	1.00	48.09	B	N
ATOM	5281	CA	THR	B	506	−26.593	32.779	55.924	1.00	47.09	B	C
ATOM	5282	CB	THR	B	506	−27.931	33.526	55.950	1.00	48.13	B	C
ATOM	5283	OG1	THR	B	506	−27.697	34.939	55.863	1.00	48.97	B	O
ATOM	5284	CG2	THR	B	506	−28.595	33.374	57.292	1.00	50.75	B	C
ATOM	5285	C	THR	B	506	−26.671	31.519	56.766	1.00	48.75	B	C
ATOM	5286	O	THR	B	506	−27.584	30.719	56.585	1.00	52.12	B	O
ATOM	5287	N	GLY	B	507	−25.721	31.330	57.679	1.00	50.28	B	N
ATOM	5288	CA	GLY	B	507	−25.621	30.075	58.412	1.00	51.01	B	C
ATOM	5289	C	GLY	B	507	−25.590	28.880	57.461	1.00	51.67	B	C
ATOM	5290	O	GLY	B	507	−24.529	28.536	56.899	1.00	51.19	B	O
ATOM	5291	N	LYS	B	508	−26.758	28.261	57.271	1.00	50.11	B	N
ATOM	5292	CA	LYS	B	508	−26.916	27.171	56.304	1.00	51.34	B	C
ATOM	5293	CB	LYS	B	508	−27.022	25.812	57.008	1.00	50.25	B	C
ATOM	5294	CG	LYS	B	508	−27.934	25.776	58.225	1.00	49.54	B	C
ATOM	5295	CD	LYS	B	508	−27.205	25.229	59.434	1.00	50.14	B	C
ATOM	5296	CE	LYS	B	508	−27.202	23.706	59.431	1.00	51.54	B	C
ATOM	5297	NZ	LYS	B	508	−28.176	23.135	60.400	1.00	54.37	B	N
ATOM	5298	C	LYS	B	508	−28.094	27.380	55.345	1.00	53.15	B	C
ATOM	5299	O	LYS	B	508	−28.794	26.431	54.990	1.00	54.71	B	O
ATOM	5300	N	LYS	B	509	−28.302	28.621	54.919	1.00	55.68	B	N
ATOM	5301	CA	LYS	B	509	−29.359	28.947	53.960	1.00	61.78	B	C
ATOM	5302	CB	LYS	B	509	−30.583	29.558	54.669	1.00	68.02	B	C
ATOM	5303	CG	LYS	B	509	−31.209	28.645	55.754	1.00	75.10	B	C
ATOM	5304	CD	LYS	B	509	−31.956	29.428	56.867	1.00	76.79	B	C
ATOM	5305	CE	LYS	B	509	−32.161	28.625	58.170	1.00	73.41	B	C
ATOM	5306	NZ	LYS	B	509	−31.388	29.179	59.327	1.00	70.29	B	N
ATOM	5307	C	LYS	B	509	−28.845	29.884	52.861	1.00	61.33	B	C
ATOM	5308	O	LYS	B	509	−28.210	30.909	53.142	1.00	66.26	B	O
ATOM	5309	N	ILE	B	510	−29.112	29.529	51.610	1.00	53.31	B	N
ATOM	5310	CA	ILE	B	510	−28.732	30.387	50.500	1.00	47.96	B	C
ATOM	5311	CB	ILE	B	510	−27.847	29.621	49.486	1.00	47.05	B	C
ATOM	5312	CG1	ILE	B	510	−27.390	30.539	48.349	1.00	47.77	B	C
ATOM	5313	CD1	ILE	B	510	−25.914	30.482	48.051	1.00	43.29	B	C
ATOM	5314	CG2	ILE	B	510	−28.569	28.418	46.943	1.00	48.55	B	C
ATOM	5315	C	ILE	B	510	−29.970	31.038	49.868	1.00	44.99	B	C
ATOM	5316	O	ILE	B	510	−30.965	30.375	49.584	1.00	46.16	B	O
ATOM	5317	N	THR	B	511	−29.889	32.345	49.669	1.00	40.67	B	N
ATOM	5318	CA	THR	B	511	−31.032	33.160	49.292	1.00	41.47	B	C
ATOM	5319	CB	THR	B	511	−31.242	34.217	50.363	1.00	45.32	B	C
ATOM	5320	OG1	THR	B	511	−30.734	33.722	51.618	1.00	50.07	B	O
ATOM	5321	CG2	THR	B	511	−32.716	34.453	50.602	1.00	44.33	B	C
ATOM	5322	C	THR	B	511	−30.723	33.859	47.992	1.00	40.90	B	C
ATOM	5323	O	THR	B	511	−29.586	34.276	47.782	1.00	46.23	B	O
ATOM	5324	N	LYS	B	512	−31.722	34.009	47.126	1.00	35.30	B	N
ATOM	5325	CA	LYS	B	512	−31.491	34.566	45.793	1.00	29.91	B	C
ATOM	5326	CB	LYS	B	512	−32.092	33.665	44.723	1.00	22.89	B	C
ATOM	5327	CG	LYS	B	512	−31.582	33.925	43.325	1.00	23.69	B	C
ATOM	5328	CD	LYS	B	512	−32.402	33.133	42.302	1.00	28.13	B	C
ATOM	5329	CE	LYS	B	512	−31.796	33.207	40.901	1.00	31.45	B	C
ATOM	5330	NZ	LYS	B	512	−32.717	32.728	39.823	1.00	34.26	B	N
ATOM	5331	C	LYS	B	512	−32.048	35.975	45.682	1.00	36.32	B	C
ATOM	5332	O	LYS	B	512	−33.093	36.207	45.059	1.00	42.57	B	O
ATOM	5333	N	ILE	B	513	−31.340	36.920	46.287	1.00	35.43	B	N
ATOM	5334	CA	ILE	B	513	−31.769	38.312	46.289	1.00	31.31	B	C
ATOM	5335	CB	ILE	B	513	−31.049	39.064	47.397	1.00	27.61	B	C
ATOM	5336	CG1	ILE	B	513	−31.137	38.249	48.691	1.00	25.50	B	C
ATOM	5337	CD1	ILE	B	513	−30.231	38.744	49.771	1.00	27.33	B	C
ATOM	5338	CG2	ILE	B	513	−31.611	40.493	47.533	1.00	25.53	B	C
ATOM	5339	C	ILE	B	513	−31.524	38.979	44.937	1.00	33.99	B	C
ATOM	5340	O	ILE	B	513	−30.373	39.099	44.510	1.00	36.24	B	O
ATOM	5341	N	PRO	B	514	−32.606	39.381	44.265	1.00	34.33	B	N
ATOM	5342	CA	PRO	B	514	−32.527	40.131	43.007	1.00	36.56	B	C
ATOM	5343	CB	PRO	B	514	−33.982	40.490	42.738	1.00	35.33	B	C
ATOM	5344	CG	PRO	B	514	−34.626	40.356	44.067	1.00	35.03	B	C
ATOM	5345	CD	PRO	B	514	−34.003	39.138	44.647	1.00	34.41	B	C
ATOM	5346	C	PRO	B	514	−31.769	41.412	43.199	1.00	40.43	B	C
ATOM	5347	O	PRO	B	514	−31.944	42.037	44.240	1.00	46.11	B	O
ATOM	5348	N	LEU	B	515	−30.968	41.807	42.217	1.00	42.57	B	N
ATOM	5349	CA	LEU	B	515	−30.198	43.044	42.312	1.00	45.31	B	C
ATOM	5350	CB	LEU	B	515	−29.175	43.131	41.178	1.00	44.56	B	C
ATOM	5351	CG	LEU	B	515	−28.031	42.114	41.142	1.00	43.12	B	C
ATOM	5352	CD1	LEU	B	515	−27.300	42.208	39.819	1.00	41.22	B	C
ATOM	5353	CD2	LEU	B	515	−27.071	42.344	42.296	1.00	42.46	B	C
ATOM	5354	C	LEU	B	515	−31.052	44.311	42.310	1.00	48.69	B	C
ATOM	5355	O	LEU	B	515	−30.612	45.335	42.818	1.00	50.19	B	O
ATOM	5356	N	ASN	B	516	−32.272	44.239	41.774	1.00	51.39	B	N
ATOM	5357	CA	ASN	B	516	−32.944	45.458	41.344	1.00	53.55	B	C
ATOM	5358	CB	ASN	B	516	−32.905	45.545	39.822	1.00	52.30	B	C
ATOM	5359	CG	ASN	B	516	−31.683	46.288	39.322	1.00	53.51	B	C
ATOM	5360	OD1	ASN	B	516	−31.298	47.325	39.867	1.00	52.78	B	O
ATOM	5361	ND2	ASN	B	516	−31.062	45.758	38.284	1.00	57.11	B	N
ATOM	5362	C	ASN	B	516	−34.336	45.839	41.876	1.00	58.86	B	C
ATOM	5363	O	ASN	B	516	−34.521	46.936	42.433	1.00	62.39	B	O
ATOM	5364	N	GLY	B	517	−35.322	44.973	41.685	1.00	59.47	B	N
ATOM	5365	CA	GLY	B	517	−36.691	45.350	42.011	1.00	59.33	B	C
ATOM	5366	C	GLY	B	517	−36.963	45.689	43.470	1.00	55.99	B	C
ATOM	5367	O	GLY	B	517	−37.901	46.422	43.778	1.00	56.60	B	O
ATOM	5368	N	LEU	B	518	−36.109	45.178	44.353	1.00	52.22	B	N
ATOM	5369	CA	LEU	B	518	−36.430	45.004	45.763	1.00	46.10	B	C
ATOM	5370	CB	LEU	B	518	−35.300	44.246	46.464	1.00	44.34	B	C
ATOM	5371	CG	LEU	B	518	−35.765	43.451	47.683	1.00	44.94	B	C
ATOM	5372	CD1	LEU	B	518	−36.183	42.040	47.310	1.00	47.31	B	C
ATOM	5373	CD2	LEU	B	518	−34.681	43.414	48.726	1.00	44.90	B	C
ATOM	5374	C	LEU	B	518	−36.784	46.268	46.532	1.00	42.67	B	C
ATOM	5375	O	LEU	B	518	−37.728	46.271	47.322	1.00	41.36	B	O
ATOM	5376	N	GLY	B	519	−36.039	47.342	46.303	1.00	40.30	B	N
ATOM	5377	CA	GLY	B	519	−36.232	48.563	47.065	1.00	42.21	B	C
ATOM	5378	C	GLY	B	519	−37.584	49.234	46.869	1.00	42.24	B	C
ATOM	5379	O	GLY	B	519	−37.761	50.411	47.203	1.00	41.48	B	O
ATOM	5380	N	CYS	B	520	−38.532	48.482	46.326	1.00	39.31	B	N
ATOM	5381	CA	CYS	B	520	−39.857	48.996	46.045	1.00	38.82	B	C
ATOM	5382	CB	CYS	B	520	−40.146	48.886	44.554	1.00	37.59	B	C
ATOM	5383	SG	CYS	B	520	−39.027	49.892	43.568	1.00	35.58	B	S
ATOM	5384	C	CYS	B	520	−40.884	48.208	46.809	1.00	40.00	B	C
ATOM	5385	O	CYS	B	520	−41.929	48.736	47.170	1.00	39.24	B	O
ATOM	5386	N	ARG	B	521	−40.562	46.944	47.065	1.00	44.69	B	N
ATOM	5387	CA	ARG	B	521	−41.533	45.968	47.537	1.00	49.98	B	C
ATOM	5388	CB	ARG	B	521	−40.938	44.564	47.523	1.00	55.09	B	C
ATOM	5389	CG	ARG	B	521	−40.870	43.953	46.124	1.00	63.59	B	C
ATOM	5390	CD	ARG	B	521	−40.265	42.554	46.079	1.00	71.10	B	C
ATOM	5391	NE	ARG	B	521	−40.860	41.682	47.095	1.00	75.72	B	N
ATOM	5392	CZ	ARG	B	521	−40.277	40.602	47.605	1.00	76.13	B	C
ATOM	5393	NH1	ARG	B	521	−39.067	40.230	47.193	1.00	73.32	B	N
ATOM	5394	NH2	ARG	B	521	−40.914	39.891	48.529	1.00	76.82	B	N
ATOM	5395	C	ARG	B	521	−42.097	46.301	48.905	1.00	51.00	B	C
ATOM	5396	O	ARG	B	521	−43.202	45.869	49.243	1.00	53.86	B	O
ATOM	5397	N	HIS	B	522	−41.366	47.099	49.676	1.00	50.09	B	N
ATOM	5398	CA	HIS	B	522	−41.825	47.444	51.021	1.00	51.92	B	C
ATOM	5399	CB	HIS	B	522	−40.640	47.602	51.975	1.00	53.81	B	C
ATOM	5400	CG	HIS	B	522	−39.993	48.944	51.903	1.00	54.81	B	C
ATOM	5401	ND1	HIS	B	522	−38.950	49.215	51.039	1.00	56.49	B	N
ATOM	5402	CE1	HIS	B	522	−38.588	50.479	51.188	1.00	58.86	B	C
ATOM	5403	NE2	HIS	B	522	−39.367	51.039	52.107	1.00	57.45	B	N
ATOM	5404	CD2	HIS	B	522	−40.254	50.100	52.572	1.00	54.77	B	C
ATOM	5405	C	HIS	B	522	−42.758	48.664	51.124	1.00	50.26	B	C
ATOM	5406	O	HIS	B	522	−43.078	49.084	52.240	1.00	53.55	B	O
ATOM	5407	N	PHE	B	523	−43.181	49.240	49.992	1.00	43.87	B	N
ATOM	5408	CA	PHE	B	523	−44.156	50.344	50.016	1.00	34.84	B	C
ATOM	5409	CB	PHE	B	523	−43.887	51.377	48.926	1.00	30.23	B	C
ATOM	5410	CG	PHE	B	523	−42.620	52.145	49.132	1.00	29.35	B	C
ATOM	5411	CD1	PHE	B	523	−41.454	51.792	48.407	1.00	29.06	B	C
ATOM	5412	CE1	PHE	B	523	−40.263	52.498	48.594	1.00	25.47	B	C
ATOM	5413	CZ	PHE	B	523	−40.225	53.557	49.514	1.00	24.47	B	C
ATOM	5414	CE2	PHE	B	523	−41.381	53.918	50.245	1.00	30.23	B	C
ATOM	5415	CD2	PHE	B	523	−42.574	53.211	50.050	1.00	30.94	B	C
ATOM	5416	C	PHE	B	523	−45.581	49.814	49.935	1.00	34.18	B	C
ATOM	5417	O	PHE	B	523	−45.994	49.215	48.929	1.00	34.09	B	O
ATOM	5418	N	GLN	B	524	−46.318	50.033	51.023	1.00	33.26	B	N
ATOM	5419	CA	GLN	B	524	−47.561	49.326	51.259	1.00	35.86	B	C
ATOM	5420	CB	GLN	B	524	−47.719	49.086	52.773	1.00	39.90	B	C
ATOM	5421	CG	GLN	B	524	−48.046	47.645	53.194	1.00	45.25	B	C
ATOM	5422	CD	GLN	B	524	−47.197	46.574	52.485	1.00	50.10	B	C
ATOM	5423	OE1	GLN	B	524	−47.730	45.571	51.998	1.00	51.86	B	O
ATOM	5424	NE2	GLN	B	524	−45.883	46.782	52.436	1.00	52.55	B	N
ATOM	5425	C	GLN	B	524	−48.758	50.081	50.682	1.00	35.92	B	C
ATOM	5426	O	GLN	B	524	−49.915	49.692	50.899	1.00	36.74	B	O
ATOM	5427	N	SER	B	525	−48.473	51.156	49.941	1.00	33.82	B	N
ATOM	5428	CA	SER	B	525	−49.514	52.071	49.473	1.00	30.97	B	C
ATOM	5429	CB	SER	B	525	−50.004	52.943	50.632	1.00	33.70	B	C
ATOM	5430	OG	SER	B	525	−49.155	54.099	50.818	1.00	39.19	B	O
ATOM	5431	C	SER	B	525	−49.061	52.962	48.318	1.00	27.28	B	C
ATOM	5432	O	SER	B	525	−47.912	53.482	48.309	1.00	27.58	B	O
ATOM	5433	N	CYS	B	526	−49.998	53.163	47.365	1.00	24.58	B	N
ATOM	5434	CA	CYS	B	526	−49.681	53.950	46.157	1.00	19.24	B	C
ATOM	5435	CB	CYS	B	526	−50.960	54.320	45.354	1.00	18.73	B	C
ATOM	5436	SG	CYS	B	526	−50.512	55.211	43.829	1.00	15.67	B	S
ATOM	5437	C	CYS	B	526	−48.893	55.216	46.465	1.00	16.28	B	C
ATOM	5438	O	CYS	B	526	−47.652	55.318	46.047	1.00	15.73	B	O
ATOM	5439	N	SER	B	527	−49.622	56.172	47.193	1.00	15.92	B	N
ATOM	5440	CA	SER	B	527	−48.928	57.403	47.589	1.00	15.45	B	C
ATOM	5441	CB	SER	B	527	−49.640	58.093	48.735	1.00	16.48	B	C
ATOM	5442	OG	SER	B	527	−48.651	58.912	49.479	1.00	20.53	B	O
ATOM	5443	C	SER	B	527	−47.482	57.178	48.031	1.00	18.59	B	C
ATOM	5444	O	SER	B	527	−46.569	57.788	47.481	1.00	19.04	B	O
ATOM	5445	N	GLN	B	528	−47.284	56.316	49.030	1.00	22.16	B	N
ATOM	5446	CA	GLN	B	528	−45.958	56.092	49.604	1.00	23.92	B	C
ATOM	5447	CB	GLN	B	528	−46.029	55.001	50.669	1.00	26.41	B	C
ATOM	5448	CG	GLN	B	528	−45.788	55.518	52.080	1.00	29.27	B	C
ATOM	5449	CD	GLN	B	528	−46.734	54.916	53.111	1.00	27.95	B	C
ATOM	5450	OE1	GLN	B	528	−46.683	53.709	53.387	1.00	27.67	B	O
ATOM	5451	NE2	GLN	B	528	−47.589	55.756	53.691	1.00	22.48	B	N
ATOM	5452	C	GLN	B	528	−44.976	55.718	48.507	1.00	25.49	B	C
ATOM	5453	O	GLN	B	528	−43.832	56.202	48.477	1.00	28.91	B	O
ATOM	5454	N	CYS	B	529	−45.460	54.875	47.597	1.00	24.45	B	N
ATOM	5455	CA	CYS	B	529	−44.686	54.336	46.476	1.00	21.14	B	C
ATOM	5456	CB	CYS	B	529	−45.522	53.278	45.752	1.00	22.04	B	C
ATOM	5457	SG	CYS	B	529	−44.724	52.460	44.370	1.00	22.10	B	S
ATOM	5458	C	CYS	B	529	−44.276	55.432	45.503	1.00	19.89	B	C
ATOM	5459	O	CYS	B	529	−43.151	55.464	45.033	1.00	21.64	B	O
ATOM	5460	N	LEU	B	530	−45.175	56.349	45.204	1.00	19.23	B	N
ATOM	5461	CA	LEU	B	530	−44.791	57.455	44.343	1.00	23.13	B	C
ATOM	5462	CB	LEU	B	530	−46.019	58.272	43.898	1.00	22.39	B	C
ATOM	5463	CG	LEU	B	530	−47.106	57.578	43.083	1.00	20.21	B	C
ATOM	5464	CD1	LEU	B	530	−48.027	58.574	42.460	1.00	16.44	B	C
ATOM	5465	CD2	LEU	B	530	−46.469	56.700	42.020	1.00	22.29	B	C
ATOM	5466	C	LEU	B	530	−43.775	58.374	45.020	1.00	25.56	B	C
ATOM	5467	O	LEU	B	530	−43.232	59.287	44.380	1.00	29.36	B	O
ATOM	5468	N	SER	B	531	−43.528	58.148	46.309	1.00	24.02	B	N
ATOM	5469	CA	SER	B	531	−42.709	59.078	47.074	1.00	29.39	B	C
ATOM	5470	CB	SER	B	531	−43.379	59.424	48.410	1.00	32.04	B	C
ATOM	5471	OG	SER	B	531	−43.995	60.717	48.379	1.00	32.10	B	O
ATOM	5472	C	SER	B	531	−41.279	58.578	47.265	1.00	33.38	B	C
ATOM	5473	O	SER	B	531	−40.428	59.284	47.811	1.00	35.32	B	O
ATOM	5474	N	ALA	B	532	−41.021	57.369	46.773	1.00	35.38	B	N
ATOM	5475	CA	ALA	B	532	−39.723	56.707	46.889	1.00	33.85	B	C
ATOM	5476	CB	ALA	B	532	−39.824	55.287	46.347	1.00	31.65	B	C
ATOM	5477	C	ALA	B	532	−38.604	57.464	46.171	1.00	35.34	B	C
ATOM	5478	O	ALA	B	532	−38.870	58.236	45.242	1.00	35.60	B	O
ATOM	5479	N	PRO	B	533	−37.359	57.234	46.597	1.00	36.25	B	N
ATOM	5480	CA	PRO	B	533	−36.180	57.792	45.924	1.00	35.80	B	C
ATOM	5481	CB	PRO	B	533	−35.017	57.082	46.619	1.00	37.77	B	C
ATOM	5482	CG	PRO	B	533	−35.640	55.914	47.337	1.00	36.66	B	C
ATOM	5483	CD	PRO	B	533	−36.978	56.414	47.761	1.00	36.96	B	C
ATOM	5484	C	PRO	B	533	−36.177	57.452	44.437	1.00	37.92	B	C
ATOM	5485	O	PRO	B	533	−36.250	56.268	44.067	1.00	35.73	B	O
ATOM	5486	N	PRO	B	534	−36.082	58.484	43.602	1.00	40.65	B	N
ATOM	5487	CA	PRO	B	534	−36.281	58.348	42.154	1.00	43.08	B	C
ATOM	5488	CB	PRO	B	534	−35.967	59.749	41.622	1.00	43.53	B	C
ATOM	5489	CG	PRO	B	534	−35.176	60.391	42.706	1.00	44.34	B	C
ATOM	5490	CD	PRO	B	534	−35.753	59.868	43.982	1.00	42.50	B	C
ATOM	5491	C	PRO	B	534	−35.375	57.305	41.501	1.00	43.92	B	C
ATOM	5492	O	PRO	B	534	−35.866	56.544	40.667	1.00	46.13	B	O
ATOM	5493	N	PHE	B	535	−34.098	57.255	41.874	1.00	43.31	B	N
ATOM	5494	CA	PHE	B	535	−33.171	56.293	41.260	1.00	43.87	B	C
ATOM	5495	CB	PHE	B	535	−31.750	56.409	41.839	1.00	43.86	B	C
ATOM	5496	CG	PHE	B	535	−31.571	55.740	43.177	1.00	40.68	B	C
ATOM	5497	CD1	PHE	B	535	−31.264	54.386	43.261	1.00	42.53	B	C
ATOM	5498	CE1	PHE	B	535	−31.099	53.777	44.497	1.00	44.40	B	C
ATOM	5499	CZ	PHE	B	535	−31.237	54.537	45.664	1.00	43.40	B	C
ATOM	5500	CE2	PHE	B	535	−31.539	55.884	45.585	1.00	36.71	B	C
ATOM	5501	CD2	PHE	B	535	−31.700	56.473	44.351	1.00	38.28	B	C
ATOM	5502	C	PHE	B	535	−33.658	54.841	41.302	1.00	41.68	B	C
ATOM	5503	O	PHE	B	535	−33.407	54.085	40.369	1.00	43.66	B	O
ATOM	5504	N	VAL	B	536	−34.350	54.464	42.378	1.00	37.37	B	N
ATOM	5505	CA	VAL	B	536	−34.867	53.103	42.538	1.00	32.40	B	C
ATOM	5506	CB	VAL	B	536	−35.492	52.886	43.936	1.00	28.07	B	C
ATOM	5507	CG1	VAL	B	536	−36.062	51.491	44.074	1.00	19.57	B	C
ATOM	5508	CG2	VAL	B	536	−34.471	53.121	45.017	1.00	28.40	B	C
ATOM	5509	C	VAL	B	536	−35.905	52.789	41.461	1.00	34.29	B	C
ATOM	5510	O	VAL	B	536	−36.122	51.628	41.138	1.00	37.01	B	O
ATOM	5511	N	GLN	B	537	−36.536	53.831	40.921	1.00	34.19	B	N
ATOM	5512	CA	GLN	B	537	−37.489	53.717	39.813	1.00	37.25	B	C
ATOM	5513	CB	GLN	B	537	−36.781	53.359	38.491	1.00	43.61	B	C
ATOM	5514	CG	GLN	B	537	−35.602	54.262	38.115	1.00	50.57	B	C
ATOM	5515	CD	GLN	B	537	−34.857	53.780	36.869	1.00	54.96	B	C
ATOM	5516	OE1	GLN	B	537	−35.090	54.295	35.767	1.00	55.50	B	O
ATOM	5517	NE2	GLN	B	537	−33.961	52.793	37.040	1.00	55.50	B	N
ATOM	5518	C	GLN	B	537	−38.661	52.763	40.079	1.00	35.11	B	C
ATOM	5519	O	GLN	B	537	−38.912	51.849	39.295	1.00	33.64	B	O
ATOM	5520	N	CYS	B	538	−39.378	52.994	41.178	1.00	33.99	B	N
ATOM	5521	CA	CYS	B	538	−40.621	52.275	41.474	1.00	30.58	B	C
ATOM	5522	CB	CYS	B	538	−40.895	52.284	42.968	1.00	31.61	B	C
ATOM	5523	SG	CYS	B	538	−39.461	51.843	43.916	1.00	40.00	B	S
ATOM	5524	C	CYS	B	538	−41.816	52.913	40.807	1.00	26.54	B	C
ATOM	5525	O	CYS	B	538	−41.788	54.102	40.475	1.00	21.86	B	O
ATOM	5526	N	GLY	B	539	−42.874	52.120	40.648	1.00	25.92	B	N
ATOM	5527	CA	GLY	B	539	−44.177	52.639	40.256	1.00	29.71	B	C
ATOM	5528	C	GLY	B	539	−45.343	51.874	40.855	1.00	27.62	B	C
ATOM	5529	O	GLY	B	539	−45.148	50.834	41.491	1.00	28.31	B	O
ATOM	5530	N	TRP	B	540	−46.559	52.370	40.654	1.00	22.58	B	N
ATOM	5531	CA	TRP	B	540	−47.701	51.678	41.235	1.00	23.87	B	C
ATOM	5532	CB	TRP	B	540	−48.631	52.656	41.935	1.00	20.61	B	C
ATOM	5533	CG	TRP	B	540	−49.674	51.979	42.757	1.00	18.60	B	C
ATOM	5534	CD1	TRP	B	540	−51.011	51.861	42.458	1.00	22.67	B	C
ATOM	5535	NE1	TRP	B	540	−51.668	51.190	43.462	1.00	21.67	B	N
ATOM	5536	CE2	TRP	B	540	−50.745	50.858	44.436	1.00	16.29	B	C
ATOM	5537	CD2	TRP	B	540	−49.478	51.343	44.024	1.00	16.67	B	C
ATOM	5538	CE3	TRP	B	540	−48.359	51.133	44.861	1.00	18.20	B	C
ATOM	5539	CZ3	TRP	B	540	−48.541	50.457	46.055	1.00	16.38	B	C
ATOM	5540	CH2	TRP	B	540	−49.813	49.997	46.434	1.00	13.70	B	C
ATOM	5541	CZ2	TRP	B	540	−50.924	50.189	45.640	1.00	14.20	B	C
ATOM	5542	C	TRP	B	540	−48.475	50.813	40.255	1.00	27.32	B	C
ATOM	5543	O	TRP	B	540	−49.143	51.309	39.348	1.00	31.37	B	O
ATOM	5544	N	CYS	B	541	−48.392	49.507	40.472	1.00	29.65	B	N
ATOM	5545	CA	CYS	B	541	−49.100	48.540	39.645	1.00	34.46	B	C
ATOM	5546	CB	CYS	B	541	−48.187	47.360	39.313	1.00	37.32	B	C
ATOM	5547	SG	CYS	B	541	−48.608	46.580	37.747	1.00	41.09	B	S
ATOM	5548	C	CYS	B	541	−50.404	48.050	40.285	1.00	34.49	B	C
ATOM	5549	O	CYS	B	541	−50.475	46.923	40.795	1.00	34.58	B	O
ATOM	5550	N	HIS	B	542	−51.423	48.910	40.249	1.00	33.21	B	N
ATOM	5551	CA	HIS	B	542	−52.771	48.591	40.736	1.00	35.58	B	C
ATOM	5552	CB	HIS	B	542	−53.396	47.435	39.939	1.00	39.34	B	C
ATOM	5553	CG	HIS	B	542	−54.803	47.117	40.343	1.00	42.34	B	C
ATOM	5554	ND1	HIS	B	542	−55.132	45.989	41.065	1.00	42.44	B	N
ATOM	5555	CE1	HIS	B	542	−56.436	45.973	41.279	1.00	43.94	B	C
ATOM	5556	NE2	HIS	B	542	−56.964	47.050	40.722	1.00	44.40	B	N
ATOM	5557	CD2	HIS	B	542	−55.963	47.784	40.133	1.00	42.97	B	C
ATOM	5558	C	HIS	B	542	−52.887	48.322	42.243	1.00	34.45	B	C
ATOM	5559	O	HIS	B	542	−53.626	49.028	42.943	1.00	35.13	B	O
ATOM	5560	N	ASP	B	543	−52.194	47.289	42.725	1.00	30.98	B	N
ATOM	5561	CA	ASP	B	543	−52.203	46.954	44.147	1.00	28.77	B	C
ATOM	5562	CB	ASP	B	543	−52.993	45.675	44.428	1.00	30.73	B	C
ATOM	5563	CG	ASP	B	543	−52.640	44.538	43.483	1.00	34.62	B	C
ATOM	5564	OD1	ASP	B	543	−53.579	44.032	42.828	1.00	35.81	B	O
ATOM	5565	OD2	ASP	B	543	−51.480	44.071	43.335	1.00	35.65	B	O
ATOM	5566	C	ASP	B	543	−50.823	46.836	44.763	1.00	29.02	B	C
ATOM	5567	O	ASP	B	543	−50.698	46.896	45.978	1.00	33.51	B	O
ATOM	5568	N	LYS	B	544	−49.792	46.672	43.940	1.00	26.83	B	N
ATOM	5569	CA	LYS	B	544	−48.438	46.489	44.449	1.00	25.39	B	C
ATOM	5570	CB	LYS	B	544	−47.897	45.134	43.989	1.00	30.32	B	C
ATOM	5571	CG	LYS	B	544	−47.894	44.934	42.472	1.00	36.12	B	C
ATOM	5572	CD	LYS	B	544	−48.387	43.546	42.073	1.00	41.41	B	C
ATOM	5573	CE	LYS	B	544	−47.218	42.597	41.759	1.00	43.22	B	C
ATOM	5574	NZ	LYS	B	544	−47.668	41.282	41.192	1.00	43.58	B	N
ATOM	5575	C	LYS	B	544	−47.504	47.621	44.016	1.00	24.84	B	C
ATOM	5576	O	LYS	B	544	−47.849	48.419	43.159	1.00	25.15	B	O
ATOM	5577	N	CYS	B	545	−46.316	47.683	44.605	1.00	27.68	B	N
ATOM	5578	CA	CYS	B	545	−45.302	48.665	44.212	1.00	31.24	B	C
ATOM	5579	CB	CYS	B	545	−44.950	49.560	45.406	1.00	27.50	B	C
ATOM	5580	SG	CYS	B	545	−43.724	50.847	45.041	1.00	26.28	B	S
ATOM	5581	C	CYS	B	545	−44.032	47.994	43.625	1.00	37.80	B	C
ATOM	5582	O	CYS	B	545	−43.457	47.089	44.236	1.00	39.35	B	O
ATOM	5583	N	VAL	B	546	−43.600	48.457	42.447	1.00	42.68	B	N
ATOM	5584	CA	VAL	B	546	−42.500	47.838	41.694	1.00	43.63	B	C
ATOM	5585	CB	VAL	B	546	−42.872	46.404	41.284	1.00	42.90	B	C
ATOM	5586	CG1	VAL	B	546	−44.193	46.366	40.499	1.00	39.68	B	C
ATOM	5587	CG2	VAL	B	546	−41.744	45.783	40.509	1.00	46.05	B	C
ATOM	5588	C	VAL	B	546	−42.075	48.626	40.432	1.00	47.24	B	C
ATOM	5589	O	VAL	B	546	−42.790	49.548	39.997	1.00	45.55	B	O
ATOM	5590	N	ARG	B	547	−40.925	48.254	39.848	1.00	48.48	B	N
ATOM	5591	CA	ARG	B	547	−40.461	48.861	38.588	1.00	52.40	B	C
ATOM	5592	CB	ARG	B	547	−38.930	48.907	38.498	1.00	55.38	B	C
ATOM	5593	CG	ARG	B	547	−38.274	47.742	37.824	1.00	58.48	B	C
ATOM	5594	CD	ARG	B	547	−37.139	47.148	38.619	1.00	58.66	B	C
ATOM	5595	NE	ARG	B	547	−37.308	45.704	38.751	1.00	59.52	B	N
ATOM	5596	CZ	ARG	B	547	−36.682	44.802	38.005	1.00	59.56	B	C
ATOM	5597	NH1	ARG	B	547	−35.830	45.185	37.057	1.00	59.35	B	N
ATOM	5598	NH2	ARG	B	547	−36.904	43.510	38.211	1.00	59.12	B	N
ATOM	5599	C	ARG	B	547	−41.114	48.248	37.341	1.00	50.72	B	C
ATOM	5600	O	ARG	B	547	−41.588	47.115	37.389	1.00	48.52	B	O
ATOM	5601	N	SER	B	548	−41.138	48.999	36.237	1.00	51.45	B	N
ATOM	5602	CA	SER	B	548	−42.079	48.719	35.141	1.00	53.15	B	C
ATOM	5603	CB	SER	B	548	−42.016	49.770	34.017	1.00	53.59	B	C
ATOM	5604	OG	SER	B	548	−40.685	50.128	33.704	1.00	56.77	B	O
ATOM	5605	C	SER	B	548	−42.002	47.297	34.589	1.00	53.91	B	C
ATOM	5606	O	SER	B	548	−43.027	46.611	34.509	1.00	53.72	B	O
ATOM	5607	N	GLU	B	549	−40.793	46.858	34.234	1.00	55.87	B	N
ATOM	5608	CA	GLU	B	549	−40.573	45.504	33.700	1.00	57.44	B	C
ATOM	5609	CB	GLU	B	549	−39.081	45.187	33.539	1.00	53.42	B	C
ATOM	5610	CG	GLU	B	549	−38.205	45.646	34.684	1.00	50.56	B	C
ATOM	5611	CD	GLU	B	549	−37.353	46.841	34.307	1.00	52.88	B	C
ATOM	5612	OE1	GLU	B	549	−37.894	47.851	33.796	1.00	53.25	B	O
ATOM	5613	OE2	GLU	B	549	−36.129	46.769	34.525	1.00	55.17	B	O
ATOM	5614	C	GLU	B	549	−41.233	44.415	34.543	1.00	59.78	B	C
ATOM	5615	O	GLU	B	549	−41.718	43.419	34.008	1.00	65.11	B	O
ATOM	5616	N	GLU	B	550	−41.261	44.630	35.854	1.00	56.62	B	N
ATOM	5617	CA	GLU	B	550	−41.779	43.666	36.814	1.00	52.20	B	C
ATOM	5618	CB	GLU	B	550	−40.971	43.811	38.095	1.00	53.08	B	C
ATOM	5619	CG	GLU	B	550	−40.746	42.572	38.938	1.00	55.13	B	C
ATOM	5620	CD	GLU	B	550	−40.158	42.947	40.291	1.00	59.40	B	C
ATOM	5621	OE1	GLU	B	550	−40.795	42.651	41.326	1.00	61.85	B	O
ATOM	5622	OE2	GLU	B	550	−39.075	43.581	40.323	1.00	60.17	B	O
ATOM	5623	C	GLU	B	550	−43.269	43.887	37.096	1.00	49.10	B	C
ATOM	5624	O	GLU	B	550	−43.796	43.359	38.073	1.00	49.30	B	O
ATOM	5625	N	CYS	B	551	−43.946	44.653	36.241	1.00	47.59	B	N
ATOM	5626	CA	CYS	B	551	−45.365	44.959	36.447	1.00	49.58	B	C
ATOM	5627	CB	CYS	B	551	−45.576	46.471	36.598	1.00	47.57	B	C
ATOM	5628	SG	CYS	B	551	−47.260	47.072	36.293	1.00	46.78	B	S
ATOM	5629	C	CYS	B	551	−46.298	44.370	35.380	1.00	53.53	B	C
ATOM	5630	O	CYS	B	551	−46.203	44.705	34.190	1.00	51.95	B	O
ATOM	5631	N	LEU	B	552	−47.209	43.513	35.852	1.00	58.99	B	N
ATOM	5632	CA	LEU	B	552	−48.178	42.748	35.043	1.00	64.62	B	C
ATOM	5633	CB	LEU	B	552	−49.131	41.961	35.976	1.00	70.91	B	C
ATOM	5634	CG	LEU	B	552	−48.920	40.480	36.370	1.00	75.43	B	C
ATOM	5635	CD1	LEU	B	552	−47.505	40.152	36.915	1.00	74.61	B	C
ATOM	5636	CD2	LEU	B	552	−50.005	40.032	37.369	1.00	75.38	B	C
ATOM	5637	C	LEU	B	552	−48.995	43.553	34.009	1.00	62.25	B	C
ATOM	5638	O	LEU	B	552	−48.683	43.524	32.816	1.00	60.24	B	O
ATOM	5639	N	SER	B	553	−50.026	44.263	34.480	1.00	62.45	B	N
ATOM	5640	CA	SER	B	553	−51.006	44.956	33.622	1.00	62.32	B	C
ATOM	5641	CB	SER	B	553	−52.275	45.291	34.423	1.00	61.74	B	C
ATOM	5642	OG	SER	B	553	−51.974	46.123	35.528	1.00	60.96	B	O
ATOM	5643	C	SER	B	553	−50.506	46.210	32.879	1.00	61.08	B	C
ATOM	5644	O	SER	B	553	−49.335	46.583	32.956	1.00	61.29	B	O
ATOM	5645	N	GLY	B	554	−51.416	46.855	32.156	1.00	59.99	B	N
ATOM	5646	CA	GLY	B	554	−51.073	47.999	31.329	1.00	59.38	B	C
ATOM	5647	C	GLY	B	554	−50.898	49.309	32.076	1.00	56.97	B	C
ATOM	5648	O	GLY	B	554	−50.475	50.309	31.490	1.00	58.37	B	O
ATOM	5649	N	THR	B	555	−51.237	49.317	33.361	1.00	51.98	B	N
ATOM	5650	CA	THR	B	555	−51.065	50.511	34.175	1.00	46.15	B	C
ATOM	5651	CB	THR	B	555	−52.207	50.669	35.184	1.00	46.99	B	C
ATOM	5652	OG1	THR	B	555	−51.844	51.675	36.136	1.00	48.11	B	O
ATOM	5653	CG2	THR	B	555	−52.355	49.418	36.049	1.00	47.37	B	C
ATOM	5654	C	THR	B	555	−49.733	50.477	34.907	1.00	42.63	B	C
ATOM	5655	O	THR	B	555	−49.145	49.408	35.096	1.00	44.37	B	O
ATOM	5656	N	TRP	B	556	−49.280	51.658	35.318	1.00	34.63	B	N
ATOM	5657	CA	TRP	B	556	−48.032	51.846	36.056	1.00	26.61	B	C
ATOM	5658	CB	TRP	B	556	−46.874	51.122	35.395	1.00	13.10	B	C
ATOM	5659	CG	TRP	B	556	−45.634	51.046	36.208	1.00	10.94	B	C
ATOM	5660	CD1	TRP	B	556	−45.329	50.103	37.159	1.00	15.04	B	C
ATOM	5661	NE1	TRP	B	556	−44.068	50.317	37.676	1.00	10.32	B	N
ATOM	5662	CE2	TRP	B	556	−43.517	51.408	37.056	1.00	8.38	B	C
ATOM	5663	CD2	TRP	B	556	−44.477	51.896	36.120	1.00	10.63	B	C
ATOM	5664	CE3	TRP	B	556	−44.147	53.026	35.354	1.00	9.06	B	C
ATOM	5665	CZ3	TRP	B	556	−42.890	53.628	35.549	1.00	4.82	B	C
ATOM	5666	CH2	TRP	B	556	−41.974	53.118	36.488	1.00	2.00	B	C
ATOM	5667	CZ2	TRP	B	556	−42.268	52.017	37.248	1.00	2.48	B	C
ATOM	5668	C	TRP	B	556	−47.768	53.327	35.985	1.00	28.65	B	C
ATOM	5669	O	TRP	B	556	−47.689	53.885	34.887	1.00	32.89	B	O
ATOM	5670	N	THR	B	557	−47.657	53.969	37.144	1.00	25.23	B	N
ATOM	5671	CA	THR	B	557	−47.338	55.388	37.180	1.00	19.31	B	C
ATOM	5672	CB	THR	B	557	−48.562	56.227	37.597	1.00	14.69	B	C
ATOM	5673	OG1	THR	B	557	−49.483	55.370	38.312	1.00	13.85	B	O
ATOM	5674	CG2	THR	B	557	−49.329	56.705	36.332	1.00	14.28	B	C
ATOM	5675	C	THR	B	557	−46.192	55.674	38.127	1.00	19.82	B	C
ATOM	5676	O	THR	B	557	−45.692	54.781	38.849	1.00	13.19	B	O
ATOM	5677	N	GLN	B	558	−45.774	56.939	38.069	1.00	21.06	B	N
ATOM	5678	CA	GLN	B	558	−44.924	57.558	39.065	1.00	19.59	B	C
ATOM	5679	CB	GLN	B	558	−43.510	57.741	38.513	1.00	23.72	B	C
ATOM	5680	CG	GLN	B	558	−42.499	56.735	39.040	1.00	28.82	B	C
ATOM	5681	CD	GLN	B	558	−41.472	56.320	37.996	1.00	31.49	B	C
ATOM	5682	OE1	GLN	B	558	−41.767	56.314	36.797	1.00	30.94	B	O
ATOM	5683	NE2	GLN	B	558	−40.263	55.968	38.451	1.00	32.36	B	N
ATOM	5684	C	GLN	B	558	−45.580	58.904	39.360	1.00	16.29	B	C
ATOM	5685	O	GLN	B	558	−44.915	59.864	39.743	1.00	19.47	B	O
ATOM	5686	N	GLN	B	559	−46.897	58.972	39.188	1.00	10.08	B	N
ATOM	5687	CA	GLN	B	559	−47.560	60.262	39.273	1.00	9.23	B	C
ATOM	5688	CB	GLN	B	559	−47.447	60.967	37.925	1.00	16.38	B	C
ATOM	5689	CG	GLN	B	559	−46.092	61.588	37.637	1.00	20.31	B	C
ATOM	5690	CD	GLN	B	559	−45.789	61.587	36.157	1.00	23.58	B	C
ATOM	5691	OE1	GLN	B	559	−46.430	62.328	35.359	1.00	18.19	B	O
ATOM	5692	NE2	GLN	B	559	−44.823	60.740	35.765	1.00	23.75	B	N
ATOM	5693	C	GLN	B	559	−49.044	60.305	39.727	1.00	8.01	B	C
ATOM	5694	O	GLN	B	559	−49.539	61.359	40.270	1.00	9.84	B	O
ATOM	5695	N	ILE	B	560	−49.764	59.197	39.491	1.00	6.13	B	N
ATOM	5696	CA	ILE	B	560	−51.221	59.261	39.713	1.00	2.72	B	C
ATOM	5697	CB	ILE	B	560	−51.936	59.155	38.222	1.00	3.13	B	C
ATOM	5698	CG1	ILE	B	560	−52.238	60.671	37.707	1.00	8.67	B	C
ATOM	5699	CD1	ILE	B	560	−50.799	61.181	37.073	1.00	12.88	B	C
ATOM	5700	CG2	ILE	B	560	−53.258	58.451	38.338	1.00	4.97	B	C
ATOM	5701	C	ILE	B	560	−51.760	58.170	40.639	1.00	6.20	B	C
ATOM	5702	O	ILE	B	560	−51.463	56.931	40.449	1.00	8.34	B	O
ATOM	5703	N	CYS	B	561	−52.555	58.623	41.633	1.00	6.24	B	N
ATOM	5704	CA	CYS	B	561	−53.104	57.519	42.583	1.00	7.85	B	C
ATOM	5705	CB	CYS	B	561	−52.670	57.845	44.061	1.00	10.20	B	C
ATOM	5706	SG	CYS	B	561	−50.816	57.253	44.183	1.00	12.15	B	S
ATOM	5707	C	CYS	B	561	−54.639	57.583	42.382	1.00	9.24	B	C
ATOM	5708	O	CYS	B	561	−55.224	58.700	42.507	1.00	14.16	B	O
ATOM	5709	N	LEU	B	562	−55.296	56.422	42.058	1.00	9.86	B	N
ATOM	5710	CA	LEU	B	562	−56.756	56.495	41.763	1.00	14.76	B	C
ATOM	5711	CB	LEU	B	562	−57.163	55.407	40.696	1.00	14.45	B	C
ATOM	5712	CG	LEU	B	562	−56.351	55.710	39.345	1.00	10.42	B	C
ATOM	5713	CD1	LEU	B	562	−56.207	54.397	38.579	1.00	13.65	B	C
ATOM	5714	CD2	LEU	B	562	−56.994	56.855	38.446	1.00	8.39	B	C
ATOM	5715	C	LEU	B	562	−57.518	56.375	43.094	1.00	17.35	B	C
ATOM	5716	O	LEU	B	562	−56.964	55.809	44.055	1.00	21.25	B	O
ATOM	5717	N	PRO	B	563	−58.770	56.913	43.154	1.00	16.54	B	N
ATOM	5718	CA	PRO	B	563	−59.567	56.864	44.396	1.00	18.87	B	C
ATOM	5719	CB	PRO	B	563	−60.938	57.426	43.962	1.00	22.52	B	C
ATOM	5720	CG	PRO	B	563	−60.666	58.234	42.720	1.00	21.69	B	C
ATOM	5721	CD	PRO	B	563	−59.525	57.553	42.038	1.00	18.04	B	C
ATOM	5722	C	PRO	B	563	−59.727	55.409	44.856	1.00	21.04	B	C
ATOM	5723	O	PRO	B	563	−60.628	54.714	44.364	1.00	24.65	B	O
ATOM	5724	N	ALA	B	564	−58.855	54.941	45.745	1.00	21.91	B	N
ATOM	5725	CA	ALA	B	564	−59.038	53.611	46.336	1.00	21.94	B	C
ATOM	5726	CB	ALA	B	564	−57.714	52.858	46.441	1.00	16.58	B	C
ATOM	5727	C	ALA	B	564	−59.718	53.740	47.709	1.00	24.09	B	C
ATOM	5728	O	ALA	B	564	−60.674	54.518	47.881	1.00	20.73	B	O
END

TABLE 3


BURIED RESIDUES IN INTERFACE ON HGF
(numbers refer to the amount of buried surface in A2)

	TYR A 513	24.00
	LYS A 516	34.00
	ARG A 533	36.00
	GLN A 534	48.00
	PHE A 536	6.00
	PRO A 537	67.00
	SER A 538	1.00
	ARG A 539	10.00
	ASP A 578	29.00
	TYR A 619	30.00
	ARG A 647	39.00
	LYS A 649	71.00
	GLU A 656	24.00
	PRO A 668	2.00
	CYS A 669	6.00
	GLU A 670	97.00
	TYR A 673	20.00
	VAL A 692	11.00
	PRO A 693	49.00
	GLY A 694	36.00
	ARG A 695	92.00
	GLY A 696	28.00
	CYS A 697	24.00
	ILE A 699	10.00
	ARG A 702	38.00
	ILE A 705	8.00
	VAL A 707	3.00

BURIED RESIDUES IN INTERFACE ON MET

(numbers refer to the amount of buried surface in A2)

	THR B 124	17.00
	TYR B 125	77.00
	TYR B 126	21.00
	ASP B 127	61.00
	ASP B 128	11.00
	HIS B 148	50.00
	GLU B 167	38.00
	ASP B 190	69.00
	ARG B 191	144.00
	PHE B 192	59.00
	ARG B 218	15.00
	LYS B 220	9.00
	GLU B 221	138.00
	THR B 222	72.00
	LYS B 223	18.00
	ASP B 224	6.00
	MET B 227	5.00
	LEU B 229	43.00
	THR B 230	38.00
	ILE B 284	1.00
	SER B 286	23.00
	ASP B 414	11.00

TABLE 4


An Amino Acid Sequence of HGF-β

	495 501 511 521 531
	VVNGIP TRTNIGWMVS LRYRNKHICG GSLIKESWVL TARQCFPSRD	540	(SEQ ID NO:1)

541	LKDYEAWLGI HDVHGRGDEK CKQVLNVSQL VYGPEGSDLV LMKLARPAVL	590

591	DDFVSTIDLP NYGSTIPEKT SCSVYGWGYT GLINYDGLLR VAHLYIMGNE	640

641	KCSQHHRGKV TLNESEICAG AEKIGSGPCE GDYGGPLVCE QHKMRMVLGV	690

691	IVPGRGCAIP NRPGIFVRVA YYAKWIHKII LTYKVPQS

TABLE 5


An Amino Acid Sequence of the Met Receptor

	1 11 21 31 41
1	MKAPAVLAPG ILVLLFTLVQ RSNGECKEAL AKSEMNVNMK YQLPNFTAET	50	(SEQ ID NO: 2)

51	PIQNVILHEH HIFLGATNYI YVLNEEDLQK VAEYKTGPVL EHPDCFPCQD	100

101	CSSKANLSGG VWKDNINMAL VVDTYYDDQL ISCGSVNRGT CQRHVFPHNH	150

151	TADIQSEVHC IFSPQIEEPS QCPDCVVSAL GAKVLSSVKD RFINFFVGNT	200

201	INSSYFPDHP LHSISVRRLK ETKDGFMFLT DQSYIDVLPE FRDSYPIKYV	250

251	HAFESNNFIY FLTVQRETLD AQTFHTRIIR FCSINSGLHS YMEMPLECIL	300

301	TEKRKKRSTK KEVFNILQAA YVSKPGAQLA RQIGASLNDD ILFGVFAQSK	350

351	PDSAEPMDRS AMCAFPIKYV NDFFNKIVNK NNVRCLQHFY GPNHEHCFNR	400

401	TLLRNSSGCE ARRDEYRTEF TTALQRVDLF MGQFSEVLLT SISTFIKGDL	450

451	TIANLGTSEG RFMQVVVSRS GPSTPHVNFL LDSHPVSPEV IVEHTLNQNG	500

501	YTLVITGKKI TKIPLNGLGC RHFQSCSQCL SAPPFVQCGW CHDKCVRSEE	550

551	CLSGTWTQQI CLPAIYKVFP NSAPLEGGTR LTICGWDFGF RRNNKFDLKK	600

601	TRVLLGNESC TLTLSESTMN TLKCTVGPAM NKHFNMSIII SNGHGTTQYS	650

651	TFSYVDPVIT SISPKYGPMA GGTLLTLTGN YLNSGNSRHI SIGGKTCTLK	700

701	SVSNSILECY TPAQTISTEF AVKLKIDLAN RETSIFSYRE DPIVYEIHPT	750

751	KSFISGGSTI TGVGKNLNSV SVPRMVINVH EAGRNFTVAC QHRSNSEIIC	800

801	CTTPSLQQLN LQLPLKTKAF FMLDGILSKY FDLIYVHNPV FKPFEKPVMI	850

851	SMGNENVLEI KGNDIDPEAV KGEVLKVGNK SCENIHLHSE AVLCTVPNDL	900

901	LKLNSELNIE WKQAISSTVL GKVIVQPDQN FTGLIAGVVS ISTALLLLLG	950

951	FFLWLKKRKQ IKDLGSELVR YDARVHTPHL DRLVSARSVS PTTEMVSNES	1000

1001	VDYRATFPED QFPNSSQNGS CRQVQYPLTD MSPILTSGDS DISSPLLQNT	1050

1051	VHIDLSALNP ELVQAVQHVV IGPSSLIVHF NEVIGRGHFG CVYHGTLLDN	1100

1101	DGKKIHCAVK SLNRITDIGE VSQFLTEFII MKDFSHPNVL SLLGICLRSE	1150

1151	GSPLVVLPYM KHGDLRNFIR NETHNPTVKD LIGFGLQVAK GMKYLASKKF	1200

1201	VHRDLAARNC MLDEKFTVKV ADFGLARDMY DKEYYSVHNK TGAKLPVKWM	1250

1251	ALESLQTQKF TTKSDVWSFG VVLWELMTRG APPYPDVNTF DITVYLLQGR	1300

1301	RLLQPEYCPD PLYEVMLKCW HPKAEMRPSF SELVSRISAI FSTFIGEHYV	1350

1351	HVNATYVNVK CVAPYPSLLS SEDNADDEVD TRPASFWETS

TABLE 6


An Amino Acid Sequence of Human Sema Domain 4d
and the Psi Domain of Met Receptor.

	25 31 41 51
	ECKEAL AKSEMNVMNK YQLPNFTAET PIQNVILHEH HIFLGATNYI	70	(SEQ ID NO: 3)

71	YVLNEEDLQK VAEYKTGPVL EHPDCFPCQD CSSKANLSGG VWKDNINMAL	120

121	VVDTYYDDQL ISCGSVNRGT CQRNVFPHNH TADIQSEVHC IFSPQIEEPS	170

171	QCPDCVVSAL GAKVLSSVKD RFINFFVGNT INSSYFPDHP LHSISVRRLK	220

221	ETKDGFMFLT DQSYIDVLPE FRDSYPIKYV HAFESNNFIY FLTVQRETLD	270

271	AQTFHTRIIR FCSINSFLHS YMEMPLECIL TELVPRGSTK KEVFNILQAA	320

321	YVSKPGAQLA RQIGASLNDD ILFGVFAQSK PDSAEPMDRS AMCAFPIKYV	370

371	NDFFNKIVNK NNVRCLQHFY GPNHEHCFNR TLLRNSSGCE AARDEYRTEF	420

421	TTALQRVLDF MGQFSEVLLT SISTFIKGDL TIANLGTSEG RFMQVVVSRS	470

471	GPSTPHVNFL LDSHPVSPEV IVENTLNQNG YTLVITGKKI TKIPLNGLGC	520

521	RHFQSCSQCL SAPPFVQCGW CHDKCVRSEE CLSGTWTQQI CLPAIYK

TABLE 8


An Amino Acid Sequence of Wild-Type HGF β

VVNGIPTRTNIGWMVSLRYSNKHICGGSLIKESWV	(SEQ ID NO:14)

LTARQCFPSRDLKDYEAWLGIHDVHGRGDEKCKQV

LNVSQLVYGPEGSDLVLMKLARPAVLDDFVSTIDL

PNYGCTIPEKTSCSVYGWGYTGLINYDGLLRVAHL

YIMGNEKCSQHHRGKVTLNESEICAGAEKIGSGPC

EGDYGGPLVCEQHKMRMVLGVIVPGRGCAIPNRPG

IFVRVAYYAKWIHKIILTYKVPQS

TABLE 7


Atomic Coordinates of Hepatocyte Growth Factor Beta Chain with Met
Receptor Secondary Structural Features

		Amino
Structural	Feature	Acid	Amino Acid
Feature	Number	Types	Numbers

HELIX 1	1	ARG A 533	CYS A 535 5
HELIX 2	2	LEU A 541	ASP A 543 5
HELIX 3	3	ASN A 639	GLN A 644 1
HELIX 4	4	ALA A 710	ILE A 720 5
HELIX 5	5	ASP B 231	SER B 233 5
HELIX 6	6	ALA B 327	ILE B 333 1
HELIX 7	7	ILE B 367	ASN B 375 1
HELIX 8	8	GLY B 517	CYS B 520 5
HELIX 9	9	CYS B 526	SER B 531 1
HELIX 10	10	PRO B 534	VAL B 536 5
HELIX 11	11	SER B 548	GLU B 550 5
SHEET 1	A7	GLN A 563	LEU A 565 0
SHEET 2	A7	TYR A 544	LEU A 548-1 N LEU A 548 O GLN A 563
SHEET 3	A7	MET A 508	TYR A 513-1 N ARG A 512 O GLU A 545
SHEET 4	A7	LYS A 516	LYS A 525-1 N GLY A 521 O VAL A 509
SHEET 5	A7	TRP A 528	ALA A 532-1 N LEU A 530 O SER A 522
SHEET 6	A7	LEU A 579	LEU A 584-1 N MET A 582 O VAL A 529
SHEET 7	A7V	AL A 567	TYR A 572-1 N VAL A 571 O LEU A 581
SHEET 1	B6	ARG A 685	VAL A 690 0
SHEET 2	B6	PRO A 676	GLU A 680-1 N CYS A 679 O MET A 686
SHEET 3	B6	SER A 611	GLY A 616-1 N SER A 613 O VAL A 678
SHEET 4	B6	ARG A 630	MET A 637-1 N LEU A 634 O CYS A 612
SHEET 5	B6	GLU A 656	GLY A 660-1 N GLY A 660 O TYR A 63S
SHEET 6	B6	GLY A 704	VAL A 707-1 N PHE A 706 O ILE A 6S7
SHEET
1	C4	ASN B 45	THR B 47 0
SHEET 2	C4	LYS B 509	PRO B 514-1 N ILE B 510 O PHE B 46
SHEET 3	C4	ASN B	499	THR B 506-1 N THR B 506 O LYS B 509
SHEET 4	C4	VAL B	490	THR B 495-1 N THR B 495 O ASN B 499
SHEET 1	D4	ILE B 52	HIS B 58 0
SHEET 2	D4	HIS B 61	ALA B 66-1 N GLY B 65 O GLN B 53
SHEET 3	D4	TYR B 69	ASN B 74-1 N LEU B 73 O ILE B 62
SHEET 4	D4	LYS B	80	LYS B 85-1 N TYR B 84 O ILE B 70
SHEET 1	E2	VAL B 89	GLU B 91 0
SHEET 2	E2	VAL B	111	LYS B 113-1 N LYS B 113 O VAL B 89
SHEET 1	F4	VAL B 158	GYS B 160 0
SHEET 2	F4	CYS B 141	VAL B 145-1 N ARG B 143 O HIS B 159
SHEET 3	F4	GLN B 129	GLY B 134-1 N SER B 132 O GLN B 142
SHEET 4	F4	ASN B 117	ASP B 123-1 N ASP B 123 O GLN B 129
SHEET 1	G4	ALA B 182	LYS B 189 0
SHEET 2	G4	PHE B	192	ASN B 199-1 N GLY B 198 O LYS B 183
SHEET 3	G4	VAL B 216	LEU B 219-1 N ARG B 217 O PHE B 195
SHEET 4	G4	PHE B 226	PHE B 228-1 N MET B 227 O ARG B 218
SHEET 1	H5	LEU B 424	VAL B 427 0
SHEET 2	H5	MET B 292	ILE B 299 1 N GLU B 297 O LEU B 424
SHEET 3	H5	THR B 276	CYS B 282-1 N ARG B 280 O MET B 292
SHEET 4	H5	PHE B 258	VAL B 264-1 N THR B 263 O ARG B 277
SHEET 5	H5	LYS B 248	SER B 255-1 N SER B 255 O PHE B 258
SHEET 1	I3	ALA B 319	LYS B 324 0
SHEET 2	I3	ASP B 340	ALA B 347-1 N VAL B 345 O ALA B 319
SHEET 3	I3	SER B 360	PRO B 366-1 N PHE B 36S O LEU B 342
SHEET 1	J4	VAL B 477	LEU B 480 0
SHEET 2	J4	ARG B 461	VAL B 466-1 N GLN B 464 O VAL B 477
SHEET 3	J4	LEU B	450	THR B 457-1 N LEU B 455 O MET B 463
SHEET 4	J4	LEU B 439	LYS B 447-1 N LYS B 447 O LEU B 450
SHEET 1	K2	GLY B 539	CYS B 541 0
SHEET 2	K2	LYS B 544	VAL B 546-1 N VAL B 546 O GLY B 539
SSBOND 1		CYS A 519	CYS A 535
SSBOND 2		CYS A 612	CYS A 679
SSBOND 3		CYS A 642	CYS A 658
SSBOND 4		CYS A 669	CYS A 697
SSBOND 5		CYS B 95	CYS B 101
SSBOND 6		CYS B 98	CYS B 160
SSBOND 7		CYS B 133	CYS B 141
SSBOND 8		CYS B 172	CYS B 175
SSBOND 9		CYS B 298	CYS B 363
SSBOND 10		CYS B 385	CYS B 397
SSBOND 11		CYS B 520	CYS B 538
SSBOND 12		CYS B 526	CYS B 561
SSBOND 13		CYS B 529	CYS B 545
SSBOND 14		CYS B 541	CYS B 551

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Claims

1. A crystal of HGF β complexed with Met comprising a human hepatocyte growth factor beta chain comprising an amino acid sequence of SEQ ID NO:1 or conservative substitutions thereof complexed with an extracellular fragment of a Met Receptor comprising an amino acid sequence of SEQ ID NO:3 or conservative substitutions thereof.

2. Crystalline form of a complex of HGF β-chain with an extracellular fragment of the Met Receptor.

3. A crystal of a 1:1 complex of the HGF β-chain with an extracellular fragment of the Met Receptor having a space group symmetry of P2₁2₁2 and comprising a unit cell having the dimensions of a, b, and c, where a is about 137.1 Å, b is about 186.4 Å, and c is about 66.7 Å.

4. The cocrystal of claim 3, wherein the HGF β-chain with an extracellular fragment of the Met Receptor has the three-dimensional coordinates of Table 2.

5. The crystal of claim 1, wherein the crystal diffracts X-rays for the determination of atomic coordinates to a resolution of 5 Å or better.

6. A composition comprising a crystal of claim 1, and a carrier.

7. A molecule or molecular complex comprising at least a portion of the Met binding site for HGF β of a polypeptide comprising an amino acid sequence of SEQ ID NO:3 or conservative substitution thereof, wherein the binding site comprises at least one amino acid residue corresponding to residues 124 to 128, 148, 167, 190 to 192, 218, 220 to 224, 229, 230, 286, 414 or mixtures thereof, the binding site defined by a set of points having a root mean square deviation of less than about 0.70 Å from points representing the backbone atoms of the amino acids as represented by the structure coordinates listed in Table 2.

8. (canceled)

9. (canceled)

10. A three-dimensional configuration of points, wherein at least a portion of the points are derived from structure coordinates representing locations of at least the backbone atoms of amino acids defining the Met binding site for HGF β.

11. (canceled)

12. The three-dimensional configuration of points of claim 10 displayed as a holographic image, a stereodiagram, a model, or a computer-displayed image.

13. A machine-readable data storage medium comprising a data storage material encoded with machine-readable data, wherein a machine programmed with instructions for using such data displays a graphical three-dimensional representation of at least one molecule or molecular complex comprising at least a portion of a Met binding site for HGF β, the binding site defined by a set of points having a root mean square deviation of less than about 0.05 Å from points representing the atoms of the amino acids as represented by the structure coordinates listed in Table 2.

14. (canceled)

15. A method for obtaining structural information about a molecule or molecular complex comprising applying of at least a portion of the HGF β:Met structure coordinates of a crystal of claim 5 to an X-ray diffraction pattern of the molecule or molecular complex's crystal structure to generate a three-dimensional electron density map of at least a portion of the molecule or molecular complex.

16-22. (canceled)

23. A method of identifying a molecule that binds Met and blocks binding of HGF β to Met comprising:

(a) searching a molecular structure database with the structural coordinates of a crystal of claim 5; and

(b) selecting a molecule from the database that mimics the structural coordinates of bound HGF in HGF β:Met.

24. A method of assessing agents that are antagonists or agonists of HGF and/or Met comprising:

applying at least a portion of the crystallography coordinates of a crystal of claim 5 to a computer algorithm that generates a 3 dimensional model of HGF β:Met or of the Met binding site for HGF βsuitable for designing molecules that are antagonists or agonists; and

searching a molecular structure database to identify potential antagonists or agonists of Met or HGF β:Met.

25. The method of claim 24, further comprising:

(a) synthesizing or obtaining the antagonist or agonist;

(b) contacting the antagonist or agonist with Met and selecting the antagonist or agonist that binds to Met.

26. The method of any of claim 24, further comprising selecting an agonist or antagonist that can associate with at least one or more or all amino acid residues on the Met receptor that comprise amino acids corresponding to residues Y125, Y126, D127, H148, E168, R191, F192, R218, E221, K223, D224 or mixtures thereof of a polypeptide comprising an amino acid sequence of SEQ ID NO:3.

27. The method of claim 24, further comprising selecting an agonist or antagonist that can associate with at least one or more or all amino acid residues on HGF β that comprise amino acids corresponding to residues Y513, K516, R533, D578, Y619, R647, K649, E656, E670, Y673, R695, R702 or mixtures thereof of a polypeptide comprising an amino acid sequence of SEQ ID NO:1.

28. (canceled)

29. A molecule or molecular complex comprising at least a portion of the HGF β binding site for Met of a polypeptide comprising an amino acid sequence of SEQ ID NO: 1 or conservative substitution thereof, wherein the binding site comprises at least one amino acid residue corresponding to amino acid residues 513, 516, 533, 534, 537, 578, 619, 647, 649, 656, 669, 670, 673, 692, 693, 694, 695, 696, 697, 699, 702 or mixtures thereof, the binding site defined by a set of points having a root mean square deviation of less than about 0.70 Å from points representing the backbone atoms of the amino acids as represented by the structure coordinates listed in Table 2.

30. The three-dimensional configuration of points of claim 29, wherein at least a portion of the points are derived from structure coordinates representing locations of at least the backbone atoms of amino acids defining the Met binding site for HGF β.

31. The three-dimensional configuration of points of claim 29 displayed as a holographic image, a stereodiagram, a model, or a computer-displayed image.

32. A machine-readable data storage medium comprising a data storage material encoded with machine-readable data, wherein a machine programmed with instructions for using such data displays a graphical three-dimensional representation of at least one molecule or molecular complex comprising at least a portion of a Met binding site on HGF β, the binding site defined by a set of points having a root mean square deviation of less than about 0.05 Å from points representing the atoms of the amino acids as represented by the structure coordinates listed in Table 2.

33. (canceled)