WO2003068932A2 - Method for crystallizing human gsk3 and novel crystal structure thereof - Google Patents

Abstract

The invention provides the three-dimensional structure of a construct of human glycogen synthase kinase 3 (GSK3); crystals of a construct of human glycogen synthase kinase 3-β (GSK3-β) containing the protein's catalytic kinase domain; a method for crystallizing the protein construct to provide a GSK3 crystal sufficient for structure determination; and a method for using the GSK3 construct's three-dimensional structure for the identification of possible therapeutic compounds in the treatment of various disease conditions mediated by GSK3 activity.

Description

METHOD FOR CRYSTALLIZING HUMAN GSK3 AND NOVEL CRYSTAL STRUCTURE THEREOF

FIELD OF THE INVENTION This invention relates to the three-dimensional structure of human glycogen synthase kinase 3 (GSK3); to crystals of a ternary complex of a GSK3 construct, adenosine diphosphate, and a phosphorylated peptide; to methods for forming crystals of the GSK3 ternary complex; to methods for determining the crystal structure of the GSK3 ternary complex; and to methods for using the three-dimensional structure of the GSK3 ternary complex to identify possible therapeutic compounds for the treatment of various disease conditions mediated by GSK3 activity.

BACKGROUND OF THE INVENTION Glycogen synthase kinase 3 (GSK3) is a serine/threonine kinase for which two isoforms, α and β, have been identified. Woodgett, Trends Biochem. Sci., 16:177-81 (1991). Both GSK3 isoforms are constitutively active in resting cells. GSK3 was originally identified as a kinase that inhibits glycogen synthase by direct phosphorylation. Upon insulin activation, GSK3 is inactivated, thereby allowing the activation of glycogen synthase and possibly other insulin-dependent events, such as glucose transport. Subsequently, it has been shown that GSK3 activity is also inactivated by other growth factors that, like insulin, signal through receptor tyrosine kinases (RTKs). Examples of such signaling molecules include IGF-1 and EGF Saito et al., Biochem. J. 303:27-31, 1994; Welsh et al., Biochem. J. 294:625-29, 1993; and Cross et al., Biochem. J. 303:21-26, 1994.

Agents that inhibit GSK3 activity are useful in the treatment of disorders that are mediated by GSK3 activity. In addition, inhibition of GSK3 mimics the activation of growth factor signaling pathways and consequently GSK3 inhibitors are useful in the treatment of diseases in which such pathways are insufficiently active. Examples of diseases that can be treated with GSK3 inhibitors include diabetes, Alzheimer's disease, CNS disorders such as bipolar disorder, and immune potentiation-related conditions, among others.

Because inhibitors of GSK3 are useful in the treatment of many diseases, the identification of new inhibitors of GSK3 would be highly desirable. The present invention provides a method for identifying possible therapeutic compounds for the treatment of various disease conditions mediated by GSK3 activity. The method of the present invention utilizes the three-dimensional structure of a GSK3 ternary complex that contains the protein's catalytic domain to identify possible therapeutic compounds and to optimize the structure of lead therapeutic compounds. SUMMARY OF THE INVENTION

In accordance with the present invention, the three-dimensional structure of ternary complex of a construct of human glycogen synthase kinase 3 (GSK3), adenosine diphosphate, and a phosphorylated peptide is provided.

In one aspect, the invention provides crystals of a ternary GSK3 complex including a construct of human glycogen synthase kinase 3-β (GSK3-β) containing the protein's catalytic kinase domain, adenosine diphosphate, and a phosphorylated peptide. In one embodiment, the crystal includes a GSK3 construct and a phosphorylated peptide. The GSK3 construct can have the amino acid sequence set forth in SEQ ID NO: 1 or an active mutant or variant thereof. The phosphorylated peptide can be a diphosphorylated polypeptide. The crystal can have the atomic coordinates set forth in Table 2.

In another aspect of the invention, a method for crystallizing the GSK3 ternary complex to provide a GSK3 crystal sufficient for structure determination is provided. In one embodiment, the method includes crystallizing a purified GSK3 protein to provide a crystallized GSK3 protein having biological activity, wherein the crystallized GSK3 protein comprises a GSK3 construct and a phosphorylated polypeptide and wherein the crystallized GSK3 protein is resolvable using x-ray crystallography to obtain x-ray patterns suitable for three-dimensional structure determination of the crystallized GSK3 protein. In one embodiment, crystallizing the GSK3 protein includes crystallizing by a hanging drop vapor diffusion method. The GSK3 construct can have the amino acid sequence set forth in SEQ ID NO: 1 or an active mutant or variant thereof. The phosphorylated peptide can be a diphosphorylated polypeptide. The crystal can have the atomic coordinates set forth in Table 2. A crystallized GSK3 protein provided by the method is also provided.

In a further aspect, a method for making a GSK3 protein complex is provided. In one embodiment, the method includes combining a polypeptide that is capable of being phosphorylated, adenosine triphosphate, a magnesium salt, and a GSK3 protein to provide a GSK3 protein complex comprising a phosphorylated polypeptide, adenosine diphosphate, and the GSK3 protein. In this embodiment, the polypeptide capable of being phosphorylated can be a monophosphorylated polypeptide. In another embodiment, the method includes combining a phosphorylated polypeptide, adenosine diphosphate, and a GSK3 protein to provide a GSK3 protein complex comprising a phosphorylated polypeptide, adenosine diphosphate, and the GSK3 protein. In this embodiment, the phosphorylated polypeptide can be a diphosphorylated polypeptide.

Crystals can be made from these GSK3 protein complexes by adding a precipitant to solutions containing these complexes. Suitable precipitants include polyethylene glycol and 2-methyl-2,4-pentanediol. The GSK3 protein can have the amino acid sequence set forth in SEQ ID NO: 1 or an active mutant or variant thereof. The crystal can have the atomic coordinates set forth in Table 2.

In yet another aspect of the invention, a method for making a GSK3 protein crystal that includes a potential GSK3 mediator is provided. In one embodiment, the method includes contacting a crystallized GSK3 protein with a potential GSK3 mediator. The crystallized GSK3 protein can include a GSK3 construct and a phosphorylated polypeptide. A crystal produced by the method is also provided.

In another aspect, the invention provides a method for providing an atomic model of a GSK3 protein. In one embodiment, the method includes the steps: (a) providing a computer readable medium having stored thereon atomic coordinate/x-ray diffraction data of a GSK3 protein in crystalline form, the data sufficient to model the three-dimensional structure of the GSK3 protein, and the GSK3 protein in crystalline form includes a GSK3 construct and a phosphorylated polypeptide; (b) analyzing the atomic coordinate/x-ray diffraction data from step (a) to provide data output defining an atomic model of the GSK3 protein; and (c) obtaining atomic model output data defining the three-dimensional structure of the GSK3 protein. A computer readable medium having stored thereon atomic model data of the

GSK3 protein produced by the method and a GSK3-β ligand corresponding to the physical model of the atomic model of the ligand model produced by the method are also provided.

In yet another aspect, a method is provided for using the GSK3 ternary complex's three-dimensional structure for the identification of possible therapeutic compounds in the treatment of various disease conditions mediated by GSK3 activity. In one embodiment, the invention provides a method for designing ligands that bind to a GSK3 protein, comprising using some or all of the atomic coordinates of the GSK3 complex. In one embodiment, the method includes the steps: (a) crystallizing a purified GSK3 protein to provide a crystallized GSK3 protein having biological activity, wherein the crystallized GSK3 protein comprises a GSK3 construct and a phosphorylated polypeptide;

(b) resolving the structure of the crystallized GSK3 protein using x-ray crystallography to obtain data suitable for three-dimensional structure determination of the GSK3 protein;

(c) applying the data generated from resolving the structure of the crystallized GSK3 protein to a computer algorithm to generate a model of the GSK3 protein suitable for use in designing ligands that will bind to the GSK3 protein active site; and (d) applying an iterative process whereby molecular structures are applied to the computer generated model to identify GSK3 binding ligands. The crystallized GSK3 protein can include the atomic coordinates set forth in Table 2. The GSK3 protein can include the amino acid sequence set forth in SEQ ID NO: 1 or an active mutant or variant thereof. A GSK binding ligand designed by the method is also provided.

In another aspect, the invention provides a method for identifying a GSK3 mediator by determining the binding interactions between a potential mediator and a GSK3 binding site, the binding site being defined by at least some of a GSK3 crystal's atomic coordinates. In one embodiment, the method includes the steps: (a) generating a binding cavity defined by the binding site on a computer screen; (b) generating compounds with their spatial structure; and (c) determining whether the compounds bind at the GSK3 binding she. The invention also provides a method for identifying a compound that mediates GSK3 activity. In one embodiment, the method includes the steps: (a) designing a potential mediator for GSK3 that will form non-covalent bonds with amino acids in the GSK3 binding site based on at least some of the GSK3 crystal's atomic coordinates; (b) obtaining the potential mediator; and (c) determining whether the potential mediator mediates the activity of GSK3. In another embodiment, the method includes the steps: (a) using a three-dimensional structure of GSK3 as defined by the GSK3 crystal's atomic coordinates to design or select the potential mediator; (b) obtaining the potential mediator; and (c) contacting the potential mediator with GSK3 to determine whether the potential mediator mediates the activity of GSK3. In a further aspect, the invention provides a computer for producing a three- dimensional representation of a molecule or molecular complex, the molecule or molecular complex including a binding pocket defined by at least some of a GSK3 crystal's atomic coordinates, or a three-dimensional representation of a homologue of the molecule or molecular complex. In one embodiment, the computer includes (a) a machine-readable data storage medium comprising a data storage material encoded with machine-readable data, the data including the GSK3 crystal's atomic coordinates; (b) a working memory for storing instructions for processing the machine-readable data; (c) a central-processing unit coupled to the working memory and to the machine-readable data storage medium for processing the machine readable data into the three-dimensional representation; and (d) a display coupled to the central-processing unit for displaying the three-dimensional representation.

The invention also provides a computer for determining at least a portion of the atomic coordinates corresponding to an X-ray diffraction pattern of a molecule or molecular complex. In one embodiment, the computer includes (a) a machine-readable data storage medium comprising a data storage material encoded with machine-readable data, wherein the data includes at least a portion of a GSK3 crystal's atomic coordinates;

(b) a machine-readable data storage medium comprising a data storage material encoded with machine-readable data, wherein the data includes an X-ray diffraction pattern of the molecule or molecular complex; (c) a working memory for storing instructions for processing the machine-readable data of (a) and (b); (d) a central-processing unit coupled to the working memory and to the machine-readable data storage medium of (a) and (b) for performing a Fourier transform of the machine readable data of (a) and for processing the machine readable data of (b) into structure coordinates; and (e) a display coupled to the central-processing unit for displaying the structure coordinates of the molecule or molecular complex.

BRIEF DESCRIPTION OF THE DRAWINGS The foregoing aspects and many of the attendant advantages of this invention will become more readily appreciated as the same become better understood by reference to the following detailed description, when taken in conjunction with the accompanying drawings, wherein:

FIGURE 1 is an illustration of the structure of the GSK3-β ternary complex; FIGURES 2A and 2B are surface representations of the GSK3-β ternary complex active site with bound peptide;

FIGURES 3A-3C are illustrations of a representation of a compound soaked into the active site of GSK3-β; FIGURE 4 is a flow diagram of a representative method of the invention using the three-dimensional structure of the GSK3-β ternary complex for identifying possible therapeutic compounds for mediating GSK3-β activity; and

FIGURE 5 is a flow diagram of a representative method of the invention using the three-dimensional structure of the GSK3-β ternary complex for identifying possible therapeutic compounds for mediating GSK3-β activity.

DETAILED DESCRIPTION OF THE PREFERRED EMBODIMENT In accordance with the present invention, crystals of a ternary complex that includes a protein construct of human glycogen synthase kinase 3-β (GSK3-β) containing the protein's catalytic kinase domain, adenosine diphosphate, and a phosphorylated peptide are provided. Methods for crystallizing the ternary complex, the three- dimensional structure of the ternary complex, and methods for using the three- dimensional structure of the ternary complex for the identification of possible therapeutic compounds in the treatment of various disease conditions mediated by GSK3-β activity are provided.

The Ternary Complex: GSK-3β Construct, Adenosine Diphosphate. and Phosphorylated Peptide The ternary complex of the invention includes a GSK3-β construct, adenosine diphosphate, and a phosphorylated peptide. The complex can be formed by combining a GSK3 construct with adenosine triphosphate (ATP) and a peptide that is capable of phosphorylation by the GSK-3 construct. Peptide phosphorylation provides the complex including a phosphorylated peptide and adenosine diphosphate (ADP). The complex can also be formed by combining a phosphorylated peptide and adenosine diphosphate with the GSK3-β construct. As described below, the crystal structure of the ternary complex structure shows that the phosphorylated peptide (e.g., a diphosphorylated peptide) spans the area between two symmetry related proteins in the crystal and is positioned to accept another serine residue. Without being bound by the theory, it is believed that the phosphorylated peptide may catalyze crystal formation of the ternary complex. Compared to other GSK3 crystals, the ternary complex crystals of the invention offer the advantages of stability, ease of soaking in candidate GSK mediators, and high resolution. For example, crystals grown by the method described in Characterization of the GSK-3β Protein and Methods of Use Thereof, U.S. Patent Application No. 60/233,538, filed September 19, 2000, and PCT/USO 1/29549, filed September 19, 2001, each expressly incorporated herein by reference in its entirety, provide crystals that have limitations with regard to resolution (2.2 Angstroms maximum), time of data collection (typically 36 hours), and the size of ligand which can soaked into the ATP- binding site (approximately less than about 400 daltons). The ternary complex crystals are superior in all aspects: the maximum resolution achieved is 2.0 Angstroms (with 1.8 Angstroms possible); the time of data collection is drastically reduced (typically 24 hours); and there is no identified limitation to the mass of ligand which can be soaked into the ATP-binding site. Various candidate GSK3 mediators (i.e., lead compounds) can be soaked into crystals of the ternary complex and their crystal structures determined. In the resulting crystals, the lead compounds are soaked in and ADP and phosphorylated peptide soak out. Because of the nature of the ternary complex crystals, relatively large lead compounds can be accommodated by the crystal. This appears to be a result of the phosphorylated peptide on the crystal structure. The binding site of the enzyme in the ternary complex crystal appears not to be occluded by crystal packing. This is in contrast to other GSK3 crystals studied, which suffer from a limitation of the size and shape of lead compound that can be accommodated by the crystal. The crystals of the ternary complex afford relatively unobstructed access to the enzyme's binding site. As noted above, crystals prepared as described in PCT/USO 1/29549 cannot easily soak compounds of greater than about 400 daltons, while crystals of the present invention can easily soak compounds having molecular weights in excess of 450 daltons.

Crystals of the ternary complex crystals can be highly resolved (e.g., 1.8 Angstrom). Similarly, co-crystals including the enzyme and candidate mediator can also be highly resolved (e.g., 2.6 Angstrom or better).

As noted above, the ternary complex includes a phosphorylated peptide that can be produced by the action of ATP, magnesium, and the GSK3 construct. The phosphorylated peptide can be derived from a peptide that is capable of phosphorylation by the GSK3 construct. Suitable peptides that are capable of phosphorylation include amino acid residues that can be phosphorylated. Suitable amino acid residues that can be phosphorylated include serine and threonine, among others. The phosphorylated peptide can also be derived from a phosphorylated peptide that includes an amino acid residue that can be phosphorylated (e.g., a monophosphorylated peptide can be phosphorylated to provide a diphosphorylated peptide). Other suitable peptides include, for example, diphosphorylated peptides that can be combined with the GSK3 construct to provide the complex. Suitable phosphorylated polypeptides include those that span the area between two symmetry related proteins in the crystal to provide relatively unobstructed access to the enzyme's binding site. Suitable peptides can include from about 6 to about 8 amino acid residues. In one embodiment, the phosphorylated peptide useful in combining with ATP and the GSK3 construct to provide the complex includes seven (7) amino acid residues including a phosphoserine residue. In another embodiment, the phosphorylated peptide useful in combining with ATP and the GSK3 construct to provide the complex includes six (6) amino acid residues including a phosphoserine residue. A representative phosphorylated peptide that can be combined with ATP and the GSK3 construct to provide the ternary complex has the sequence: LSRRPS*Y (SEQ ID NO: 2), where S* represents a phosphoserine. It will be appreciated that other phosphorylated peptides, such as diphosphorylated peptides, and other peptides, such a peptides that can be phosphorylated, can be used to provide the ternary complex of the invention.

FIGURE 1 is an illustration of the structure of a GSK 3-β ternary complex showing a polypeptide bridging the enzyme. FIGURES 2A and 2B are surface representations of a GSK 3-β ternary complex active site with bound polypeptide. FIGURES 3 A-C is an illustration of a representative compound soaked into the active site of a GSK 3-β ternary complex. The compound:

is shown interacting with the enzyme's active site: the compound's amino-pyridine group forms two hydrogen bonds to the linker region, the compound's imidazole forms no hydrogen bonds to the β-strand region, and the compound's dichlorophenyl group fits into the hydrophobic pocket near the catalytic region of the kinase. The three-dimensional structure of the GSK3-β construct with the above compound soaked in provided as a tabulations of atomic coordinates is given in Table 3.

The GSK3-β Protein Construct: Expression. Purification, and Crystallization

In one aspect, the invention provides a composition that is a ternary complex that includes a GSK3-β construct, adenosine diphosphate, and a phosphorylated peptide. The GSK3-β construct contains the protein's catalytic kinase domain. The construct includes at least residues 37-384 of human GSK3-β and lacks the 36 amino acids at the protein's C-terminus. The composition is a crystalline form sufficient for structure determination by diffraction studies by X-ray.

It will be appreciated that GSK3 protein constructs other than the construct described herein, for example, active mutants or variants thereof, can provide three- dimensional structural information useful in identifying possible therapeutic compounds in the treatment of various disease conditions mediated by GSK3 activity.

Construct Sequence. The construct sequence, SEQ ID NO: 1, is provided below.

The asterisk indicates the first residue that is seen in the crystal structure. The following construct and additional useful constructs and their preparation are described in co-pending U.S. Patent Application Serial No. 60/221,242, filed July 27, 2000, the disclosure of which is incorporated herein by reference in its entirety and for all purposes.

N-terminus: MEYMPMEGGGGSK

*VTTVVATPGQGPDRPQEVSYTDTKVIGNGSFGVVYQAKLCDSGELVAIK KVLQDKRFKNRELQIMRKLDHCNIVRLRYFFYSSGEKKDEVYLNLVLDYVPETV YRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTA VLKLCDFGSAKQLVRGEPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAE LLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREMNPNYTEFKFPQIKAHPWTKVF RPRTPPEAIALCSRLLEYTPTARLTPLEACAHSFFDELRDPNVKLPNGRDTPALFN FTTQELSSNPPLATILIPPHARI: C-terminus (SEQ ID NO: 1)

Construct Purification. The GSK3-β protein construct was extracted from SF-9 cells infected with a baculovirus carrying GSK3-β 580 cDNA construct. The GSK3-β protein construct was purified to apparent homogeneity using S-Fractogel, Phenyl-650 M, and Glu-tag affinity chromatographies. The purified protein was then concentrated for crystallization. Purification of the construct is described in Example 1.

Construct Crystallization. Protein crystals can be formed from solutions of the GSK3 construct by, for example, the hanging drop technique. A representative method for forming suitable crystals of the GSK3 construct suitable for structure determination is described in Example 2.

It will be appreciated that various crystallization methods including, for example, microcrystallization methods can be utilized to obtain three-dimensional structural information useful in identifying possible therapeutic compounds in the treatment of various disease conditions mediated by GSK3 activity.

The GSK3-B Protein Construct Structure

In another aspect of the invention, the three-dimensional structure of the GSK3 ternary complex is provided. Amino acid sequence data and atomic coordinates derived from X-ray diffraction data were used to determine the construct's three-dimensional structure. The construct's atomic coordinates were calculated from an electron density map produced from the combination of X-ray diffraction and phase data.

With the GSK3 ternary complex available in crystalline form suitable for structural determination, the crystal structure can be obtained by a variety of techniques. In a representative method, diffraction patterns were obtained using an X-ray image plate device. Phase data was then obtained by molecular replacement. Electron density maps were then constructed and the structure solved and molecule built. The resulting structure was refined and the structure validated. The ultimate result was an atomic model of the GSK3 construct. A representative method for obtaining the GSK3 crystal structure is described in Example 3. It will be appreciated that the GSK3 structure can be solved by a variety of methods. The statistics for collecting the crystallographic data are summarized in Table 1. Table 1. Data and Model Statistics for Structure Solution.

Native 2.0A

Space Group P2(l)

Highest Resolution (A) 2.0

^Rmerge (°^/o) 7.6

I/sigmaσ(total) 17.8

Final Shell 2.06-2.0

I/sigmaσ(Final Shell) 2.8

R-factor (%) 25.1

Free-R factor (%) 30.2

The three-dimensional structure of the GSK3-β ternary complex provided as a tabulation of atomic coordinates is given in Table 2. In the table, "OH2" refers to structural water molecules, and "TER" refers to the terminus of a peptide chain.

The three-dimensional structure of the GSK3-β ternary complex based on the derived crystal structure is schematically illustrated in FIGURE 1. The ternary complex includes N-terminal and C-terminal domains with the active site formed between the two domains. The N-terminal domain includes a β-barrel. The active site region includes the ATP binding site, the magnesium binding/catalytic base site, and substrate binding site.

The three-dimensional structure of the GSK3-β ternary complex's active site (including the catalytic site and substrate binding site) based on the derived crystal structure is schematically illustrated in FIGURES 2 A and 2B. The active site includes Pro 136 and Phe67 among other amino acid residues.

The area of interaction of the phosphorylated peptide lies in the substrate binding region of the enzyme, not in the ATP binding site (the site of action of most of the lead drug compounds). It is believed that the interactions formed between the peptide and the enzyme, as well as the between the peptide and symmetry mates of the enzyme in the crystal matrix, are what allow a superior form of crystal to be formed. The interactions of the peptide with the enzyme are varied. The first set of key interactions are that the N- terminal phosphoserine of the phosphorylated peptide interacts with Arg-96 (an electrostatic interaction) and the main chain amide of Val-214 through a hydrogen bond. The second set of key interactions is that the second arginine of the peptide (proceeding towards the C-terminus) forms key electrostatic interactions with the adjacent symmetry mate of the enzyme by interacting with the main chain carbonyl of Pro-258' and the side chain Asp-260' (prime denotes symmetry mate). The peptide makes several other minor hydrophobic interactions with both the enzyme and adjacent symmetry mates.

Structural information of the apoprotein active site can provide a basis for the rational design of ligands leading to therapeutic compounds effective in the treatment of various disease conditions mediated by GSK3-β activity. Thus, the structural information obtained from the crystallographic data can be used to develop a ligand profile and for the rational design of drugs for mediating GSK3-β activity as described below.

GSK3 Structural Representation. As noted above, in one aspect, the invention provides a method for identifying possible therapeutic compounds in the treatment of various disease conditions mediated by GSK3-β activity. The method involves the use of a three-dimensional structural representation of the GSK ternary complex. The three- dimensional structural representation may be a representation that includes (a) the complete GSK construct, (b) a fragment of GSK3 that includes the GSK construct, or (c) a fragment of the GSK construct that includes the amino acids that interact with ligands that can mediate GSK3 activity.

The structural representation is preferably based on or derived from the atomic coordinates as set out in Table 2, which represents the structure of the complete GSK construct. Suitable structural representations include three-dimensional models and molecular surfaces derived from these atomic coordinates. The coordinates in Table 2 include structural water molecules. These will vary, and may even be absent, in other models derived structurally (they are resolution and space group dependent). These solvent molecules will vary from crystal to crystal.

Variants of the atomic coordinates noted in Table 2 can also be used for the invention, such as variants in which the RMS deviation of the x, y, and z coordinates for all heavy (i.e., not hydrogen) atoms are less than about 2.5A, for example, less than about 2A, preferably less than about lA, more preferably less than about 0.5 A, or most preferably less than about 0.1 A) compared with the atomic coordinates noted in Table 2. Coordinate transformations that retain the three-dimensional spatial relationships of atoms can also be used to give suitable variants. The atomic coordinates provided herein can also be used as the basis of models of further protein structures. For example, a homology model could be based on the GSK construct structure. The coordinates can also be used in the solution or refinement of further crystal structures of GSK3, such as co-crystal structures with new ligands. GSK3 Structural Representation Storage Medium. The atomic coordinates of the

GSK ternary complex can be stored on a medium for subsequent use with a computational device, such as a computer (e.g., supercomputer, mainframe, minicomputer, or microprocessor). Typically, the coordinates are stored on a medium useful to hold large amounts of data, such as magnetic or optical media (e.g., floppy disks, hard disks, compact disks, magneto-optical media ("floptical" disks, or magnetic tape) or electronic media (e.g., random-access memory (RAM), or read-only memory (ROM). The storage medium can be local to the computer, or can be remote (e.g., a networked storage medium, including the Internet). The choice of computer, storage medium, networking, and other devices or techniques will be familiar to those of skill in the structural/computational chemistry arts.

The invention also provides a computer-readable medium for a computer, which contains atomic coordinates and/or a three-dimensional structural representation of the GSK ternary complex. The atomic coordinates are preferably those noted in Table 2 or variants thereof. Any suitable computer can be used in the present invention. GSK3-β Ligand Profile Development. As noted above, the structural information obtained from the crystallographic data can be used to develop a ligand profile useful for the rational design of compounds for mediating GSK3-β activity. A ligand profile can be developed by taking into account the structural information obtained as described above for the apoprotein. The ligand profile can be further developed and refined with the determination of additional structures of protein with bound ligands. The ultimately developed ligand profile identifies possible therapeutic compounds for mediating GSK3-β activity.

The ligand profile can be primarily based on a shape interaction between the ligand and the protein ligand binding site. The evaluation of the shape interaction can include consideration of the ligand's conformational properties, ranking ligands based on their ability to achieve low energy conformations compatible with the ligand binding site. The shape interaction can also seek to maximize enthalpic interactions between the ligand and the binding site. The process of developing a ligand profile can vary widely. For example, the profile can be developed by visual inspection of active site structures by experts. Such an inspection can include the consideration of the binding site and ligand structures and compound database searching. The development of the profile can also consider biological data and structure activity relationships (SAR) as well the consideration of known ligand binding interaction with other similar proteins.

In any event, the ligand profile is developed by considering ligand binding interactions including primary and secondary interactions and results in defining the pharmacophore. The term "pharmacophore" refers to a collection of chemical features and three-dimensional constraints that represent specific characteristics responsible for a ligand's activity. The pharmacophore includes surface-accessible features, hydrogen bond donors and acceptors, charged/ionizable groups, and/or hydrophobic patches, among other features.

In addition to the process for ligand profile development noted above, other structure-based drug design techniques can be applied to the structural representation of the GSK3 construct in order to identify compounds that interact with GSK3 to mediate

GSK3 activity. A variety of suitable techniques are available to one of ordinary skill in the art.

Software packages for implementing molecular modeling techniques for use in structure-based drug design include SYBYL (available from Tripos Inc., http://www/tripos.com); AMBER (available from Oxford Molecular, http://www/oxmol.co.uk/); CERIUS^ (available from Molecular Simulations Inc., http ://www/msn. com/) INSIGHT II (available from Molecular Simulations Inc., http://www/msn.com/) CATALYST (available from Molecular Simulations Inc., http://www/msn.com/) QUANTA (available from Molecular Simulations Inc., http ://www/msn. com/) HYPERCHEM (available from Hypercube Inc., http://www/hyper.com/); FIRST DISCOVERY (available from Schrodinger Inc., http://www/schrodinger.com), MOE (available from Chemical Computing Group, http://www/chemcomp.com), and CHEMSITE (available from Pyramid Learning, http://www/chemsite.org/), among others.

The modeling software can be used to determine GSK3 binding surfaces and to reveal features such as van der Waals contacts, electrostatic interactions, and/or hydrogen bonding opportunities. These binding surfaces can be used to model docking of ligands with GSK3, to arrive at pharmacophore hypotheses, and to design possible therapeutic compounds de novo.

GSK3-β Ligand Virtual Screening

The three-dimensional structure of the apoprotein, and the structure of the protein's active site in particular, allows for the determination of the fit of compounds into the active site. Utilizing a fast docking program, individual compounds from, for example, a compound database, can be evaluated for active site binding. The fit of a particular compound can be evaluated and scored. Setting a score threshold can then provides a family of compounds as a solution to the virtual screen. At the first level, the virtual screen takes into account the three-dimensional structure of the apoprotein's active site. At the second level, the virtual screen considers the ligand profile and can utilize information obtained from the determination of the structure of protein with bound ligand. A virtual screen is possible even if there is no structural information on a bound ligand. Information gained from the virtual screen can be considered to further develop the ligand profile. Alternatively, where the results of the virtual screen indicate a promising compound, the compound can be obtained and screened for the relevant biological activity.

Docking. Docking refers to a process in which two or more molecules are aligned based on energy considerations. Docking aligns the three-dimensional structures of two or more molecules to predict the conformation of a complex formed from the molecules (see, e.g., Blaney & Dixon, Perspectives in Drug Discovery and Design 7:301, 1993). In the practice of the present invention, molecules are docked with the GSK3 construct structure to assess their ability to interact with GSK3. Docking can be accomplished by either geometric matching of the ligand and its receptor or by minimizing the energy of interaction. Geometric matching algorithms are preferred because of their relative speed.

Suitable docking algorithms include DOCK (Kuntz et al., J. Mol. Biol. 161:269- 288, 1982, available from UCSF), the prototypical program for structure-based drug design; AUTODOCK (Goodsell & Olson, Proteins: Structure, Function and Genetics 8:195-202, 1990 and available from Oxford Molecular, http://www/oxmol.co.uk/), which docks ligands in a flexible manner to receptors using grid-based Monte Carlo simulated annealing. The flexible nature of the AUTODOCK procedure helps to avoid bias (e.g., in orientation and conformation of the ligand in the active site) introduced by the user searcher (Meyer et al., Persp. Drug Disc. 5:168-95, 1995) because, while the starting conformation in a rigid docking is normally biased towards a minimum energy conformation of the ligand, the binding conformation may be of relatively high conformational energy (Nicklaus et al., Bioorganic & Medicinal Chemistry 3 :4\ \, 1995).

Other suitable docking algorithms include MOE — DOCK (available from Chemical Computing Group Inc., http://www/chemcomp.com), in which a simulated annealing search algorithm is used to flexibly dock ligands and a grid-based energy evaluation is used to score docked conformations; FLExX (available from Tripos Inc., http://www/tripos.com), which docks conformationally flexible ligands into a binding site using an incremental construction algorithm that builds the ligand in the site, and scores docked conformations based on the strength of ligand-receptor interactions; GOLD (Jones et al., J. Mol. Biol. 2(57:727-748, 1997), a genetic algorithm for flexible ligand docking, with full ligand and partial protein flexibility, and in which energy functions are partly based on conformation and non-bonded contact information; AFFINITY (available from Molecular Simulations Inc., http://www/msn.com/), which uses a two step process to dock ligands: first, initial placements of the ligand within the receptor are made using a Monte Carlo-type procedure to search both conformational and Cartesian space; and second, a simulated annealing phase optimizes the location of each ligand placement, during this phase, AFFINITY holds the "bulk" of the receptor (atoms not in the binding site) rigid, while the binding site atoms and ligand atoms are movable; C^ LigandFit (available from Molecular Simulations Inc., http://www/msn.com/), which uses the energy of the ligand-receptor complex to automatically find best binding modes and stochastic conformation search techniques, with the best results from the conformational sampling retained. A grid method is used to evaluate non-bonded interactions between the rigid receptor and the flexible ligand atoms. DOCKIT (available from Metaphorics LLC) uses distance geometry for fast flexible ligand docking. GLIDE (available from Schrodinger Inc.) uses a pre-computed energy grid and an efficiently pruned systematic search for flexible docking.

Preferably, the docking algorithm is used in a high-throughput mode, in which members of large structural libraries of potential ligands are screened against the receptor structure (Martin, J Med. Chem. 55:2145-54, 1992). Suitable structural libraries include the ACD (Available Chemical Directory, form MDL Inc.), AsInEx, Bionet, ComGenex, the Derwent World Drug Index (WDI), the Contact Service Company database, LaboTest, ChemBridge Express Pick, ChemStar, BioByteMasterFile, Orion, SALOR, TRIAD, ILIAD, the National Cancer Institute database (NCI), and the Aldrich, Fluka, Sigma, and Maybridge catalogs. These are commercially available (e.g., the HTS Chemicals collection from Oxford Molecular, or the LeadQuest™ files from Tripos).

Defining the Pharmacophore. As noted above, a pharmacophore can be defined for the GSK3 ternary complex that includes surface-accessible features, hydrogen bond donors and acceptors, charged/ionizable groups, and/or hydrophobic patches, among other features. These features can be weighted depending on their relative importance in conferring activity (see, e.g., Computer-Assisted Lead Finding and Optimization, Testra & Folkers, 1997).

Pharmacophores can be determined using software such as CATALYST (including HypoGen or HipHop, available from Molecular Simulations Inc., http ://www/msn. com ), CERIUS2, or constructed by hand from a known conformation of a lead compound. The pharmacophore can be used to screen structural libraries, using a program such as CATALYST. The CLIX program (Davic & Lawrence, Proteins 12:3 - 41, 1992) can also be used, which searches for orientations of candidate molecules in structural databases that yield maximum spatial coincidence with chemical groups which interact with the receptor. The DISCO program (available from Tripos) uses a method of clique detection to identify common pharmacophoric features in each structure, produce optimally aligned structures, and extract the key features of the pharmacophore. The GASP program (available from Tripos) uses a genetic algorithm to automatically find pharmacophores with conformational flexibility. de novo Compound Design. The binding surface or pharmacophore of the GSK3 ternary complex can be used to map favorable interaction positions for functional groups (e.g., protons, hydroxyl groups, amine groups, acidic groups, hydrophobic groups and/or divalent cations) or small molecule fragments. Compounds can then be designed de novo in which the relevant functional groups are located in the correct spatial relationship to interact with GSK3.

Once functional groups or small molecule fragments which can interact with specific sites in the binding surface of GSK3 have been identified, they can be linked in a single compound using either bridging fragments with the correct size and geometry or frameworks which can support the functional groups at favorable orientations, thereby providing a compound according to the invention. While linking of functional groups in this way can be done manually, perhaps with the help of software such as QUANTA or SYBYL, automated or semi-automated de novo design approaches can also be used.

Suitable de novo design software includes MCDLNG (Gehlhaar et al., J. Med. Chem. 38:466-72, 1995), which fills a receptor binding site with a close-packed array of generic atoms and uses a Monte Carlo procedure to randomly vary atom types, positions, bonding arrangements and other properties; MCSS HOOK (Caflish et al., J. Med. Chem. 55:2142-67, 1993; Eisen et al., Proteins: Str. Funct. Genet. 19: 199-221, 1994; available from Molecular Simulations Inc., http://www/msn.com), which links multiple functional groups with molecular templates taken from a database; LUDI (Bohm, J. Comp. Aided Molec. Design (5:61-78, 1992, available from Molecular Simulations Inc., http://www/msn.com), which computes the points of interaction that would ideally be fulfilled by a ligand, places fragments in the binding site based on their ability to interact with the receptor, and then connects them to produce a ligand; GROW (Moon and Howe, Proteins: Str. Funct. Genet. 77:314-328, 1991), which starts with an initial "seed" fragment (placed manually or automatically) and grows the ligand outwards; SPROUT (available from http://chem.leeds.ac.uk/ICAMS/SPROUT.html), which includes molecules to identify favorable hydrogen bonding and hydrophobic regions within a binding pocket (HIPPO module), selects functional groups and positions them at target sites to form starting fragments for structure generation (EleFanT), generates skeletons that satisfy the steric constraints of the binding pocket by growing spacer fragments onto the start fragments and then connecting the resulting part skeletons (SPIDeR), substitutes hetero atoms into the skeletons to generate molecules with the electrostatic properties that are complementary to those of the receptor site (MARABOU), and the solutions can be clustered and scored using the ALLigaTOR module; LEAPFROG (available from Tripos Inc., http://www/tripos.com), which evaluates ligands by making small stepwise structural changes and rapidly evaluating the binding energy of the new compound, keeps or discards changes based on the altered binding energy, and evolves structures to increase the interaction energy with the receptor; GROUPBUILD (Rorstein et al., J. Med. Chem. 36: 1700, 1993), which uses a library of common organic templates and a complete empirical force field description of the non-bonding interactions between a ligand and receptor to construct ligands that have chemically reasonable structure and have steric and electrostatic properties complimentary to the receptor binding site; CAVEAT (Lauri and Bartlett, Comp. Aided Mol. Design 5:51-66, 1994), which designs linking units to constrain acyclic molecules; and RASSE (Lai, J. Chem. Inf. Comput. Sci. 36:1187-1194, 1996).

GSK3-B Ligands

Most lead compounds that initiate structure-based design cycles are identified by high-throughput screening. As a result of high throughput screening and the ligand profile and virtual screening described above, ligands are identified having the requisite conformational energies to assume a suitable shape and bind with the protein's active site. In addition to having Tow conformational energy and spatial compatibility with the apoprotein active site, the identified ligands are preferably synthetically accessible. The identified ligands can then be obtained (e.g., commercially obtained or synthesized) and screened for biological activity. The identified ligands can also be co-crystallized with the protein construct and the three-dimensional structure determined for the protein with bound ligand. The information obtained from structure of the protein with bound ligand can then be used to further develop the ligand profile as described above.

Suitable GSK3-β biological screening methods for evaluating ligand biological activity are known and include, for example, those noted in U.S. patent application Serial No. 60/193,043, filed March 29, 2000, and expressly incorporated herein be reference in its entirety.

Method for Rational Drug Discovery Using GSK3 Crystal Structures In another aspect, the invention provides a method for using a GSK3 crystal structure, specifically the three-dimensional structure of the GSK3 construct's active site, to design ligands for binding to and mediating the activity of GSK3-β.

In one embodiment, the method is an iterative structure-based method for therapeutic compound design. A representative method is depicted by the flow diagram shown in FIGURE 4. Referring to FIGURE 4, the crystal structures of the apoprotein and the protein with bound ligand are determined in steps 102 and 104, respectively. From the structural information obtained from steps 102 and 104, a ligand profile is developed in step 106. A ligand profile can also be developed directly from the crystal structure of the apoprotein. Using the resulting profile, new ligands can be designed and/or obtained, screened for biological activity, and/or co-crystallized with the protein in step 108, or alternatively, the ligand profile can be used in a virtual screen in step 110. If the ligand obtained from the developed profile is co-crystallized, the structure of the co-crystal is determined in step 104 and the resulting structural information is used to further develop the ligand profile in step 106. If the ligand profile is used in a virtual screen in step 110, the virtual screen is either successful and identifies one or more ligands that can be obtained, screened, and/or co-crystallized in step 108. If the virtual screen is unsuccessful in identifying a suitable ligand, the ligand profile is further developed in step 106.

Lead compounds can be identified from biological screening of ligands developed by the ligand profile. A representative method for identifying a lead compound is depicted by the flow diagram shown FIGURE 5. Referring to FIGURE 5, the crystal structures of the apoprotein and the protein with bound ligand are determined in steps 202 and 204, respectively. From the structural information obtained from steps 202 and 204, a ligand profile is developed in step 206. A ligand profile can also be developed directly from the crystal structure of the apoprotein. From the resulting profile, a new ligand can be designed and/or obtained in step 208, and either screened for biological activity in step 210 and/or co-crystallized with the protein in step 212. If the biological screen is successful, a lead compound is identified in step 214. In a subsequent iteration, the lead compound can be co-crystallized in step 212 and iterations continued until a new drug candidate is identified. If the biological screen is not successful, that information can be used to further develop the ligand profile in step 206. If the ligand is co-crystallized, the co-crystal structure can be determined in step 204 and the structural information used in further developing the ligand profile in step 206.

Alternatively, the results of the ligand profile can be used in a virtual screen in step 216. If the virtual screen is successful and identifies one or more ligands, the ligand can be obtained in step 208 and screened in step 210 to determine its biological activity and whether or not a lead compound has been identified. The ligand obtained in step 208 can also be co-crystallized in step 212 and its structure determined and the resulting information used to further develop the ligand profile. If the virtual screen is unsuccessful in identifying a suitable ligand, the ligand profile is further developed in step 206. GSK3 Ligands and Their Uses

The method of the invention identifies ligands that can interact with GSK3. These compounds can be designed de novo, can be known compounds, or can be based on known compounds. The compounds can be useful pharmaceuticals themselves, or can be prototypes that can be used for further pharmaceutical refinement (i.e., lead compounds) in order to improve binding affinity or other pharmacologically important features (e.g., bio-availability, toxicology, metabolism, pharmacokinetics).

Accordingly, in another aspect, the invention provides (1) a compound identified using the method of the invention; (2) a compound identified using the method of the invention for use as a pharmaceutical; (3) the use of a compound identified using the method of the invention in the manufacture of a medicament for mediating GSK3 activity; and (4) a method of treating a patient afflicted with a condition mediated by GSK3 activity that includes administering an amount of a compound identified using the method of the invention that is effective to mediate GSK3 activity. These compounds preferably interact with GSK3 with a binding constraint in the micromolar or, more preferably, nanomolar range or stronger.

As well as being useful compounds individually, ligands identified by the structure-based design techniques can also be used to suggest libraries of compounds for traditional in vitro or in vivo screening methods. Important pharmaceutical motifs in the ligands can be identified and mimicked in compound libraries (e.g., combinatorial libraries) for screening for GSK3 -binding activity.

The foregoing and other aspects of the invention may be better understood in connection with the following representative examples.

EXAMPLES Example 1

GSK3-B Construct Purification In this example, the purification of the GSK3-β protein construct is described. The construct was extracted from SF-9 cells infected with a baculovirus carrying GSK3-β 580 cDNA construct and purified to apparent homogeneity using S-Fractogel, Phenyl-650 M, and Glu-tag affinity chromatographies as described below.

Extraction. Cell paste from 20L fermentation of infected SF-9 cells was washed 100 mL PBS (10 mM NaPi, pH 7.5, 150 mM NaCl) and then resuspended with 300 mL of Buffer H (20 mM Tris, pH 7.5, 1 mM tungstate, 1 mM arsenate, 50 mM DTT, 10 μg/mL leupeptin, 1 μg/mL pepstatin A, 10% glycerol, 0.35% octyl glycoside, 1 mM Mg2+). Cells were homogenized in a 100-mL Douncer (20 strokes with pestel B). The combined homogenate was centrifuged in a Ti45 rotor at 40,000 rpm for 35 minutes to remove cell debris and nuclei. The supernatant from the centrifugation were carefully decanted and filtered through 0.45 μ filter.

S-Fractogel Chromatography. 175 mL S-fractogel (EM Science, Cat #18882) was packed into 5 cm x 8.9 cm column and equilibrated with 5 column volumes of Buffer A (20 mM Tris, Ph 7.5, 10% glycerol). Prior to loading the filtered supernatant, one column volume of Buffer A containing 50 mM DTT was passed over the equilibrated column. The filtrate from the previous step was then loaded at 20 mL/min onto the column. The column was washed with 3 column volumes of Buffer A containing 50 mM DTT and 2 column volumes of Buffer A and then eluted with a linear gradient from 0 to 1 M NaCl in Buffer A over 20 column volumes. The eluant was fractionated into 20 mL fractions. Fractions containing GSK3 were detected by Western Blot using anti-GSK antibody (Santa Cruz Biotech, Cat # SC-7291). The Western-Blot positive fractions were pooled and mixed with equal volume of Buffer M (20 mM Tris, pH 7.5, 10% glycerol, 3.1 M NaCl) and filtered through a 0.45 μ filter. The filtrate was used for Phenyl-650 M chromatography.

Phenyl-650 M Chromatography. 37.5 mL Phenyl-650 M (Tosohass, Cat #014943) was packed into a 2.2 x 10 cm column and equilibrated with 5 column volumes of Buffer C (20 mM Tris, pH 7.5, 10% glycerol, 1.6 M NaCl). Filtrate from S-fractogel step was loaded onto the column at 7.5 mL/min. After the loading was completed, the column was washed with 5 column volumes of Buffer C and eluted with linear gradient from 0% to 100% Buffer A (20 mM Tris, pH 7.5, 10% glycerol) over 20 column volumes. Fractions were collected at 15 mL each and GSK containing fractions were detected by Western Blot using anti-GSK antibody. The Western positive fractions were pooled and loaded onto a Glu-tag antibody affinity column.

Glu-tag Affinity Chromatography. 50 mg of Glu-tag antibody was immobilized onto 28 mL of Affi-Gel 10 (BioRAD, Cat #153-6046) and the packed into 2.2 x 6.5 cm column. The column was equilibrated with 5 column volumes of Buffer D (20 mM Tris, pH 7.5, 20% glycerol, 0.3 M NaCl, 0.2% octylglucoside) and the fraction pool from Phenyl-650 M step was loaded at 2.8 mL/min. After the loaded was completed, the column was wash with 5 column volumes of Buffer D and then eluted with 100 mL Glu-tag peptide (100 μg/mL) in Buffer D and fractionated into 4 mL fractions. GSK containing fractions were detected with SDS-PAGE and Coomassie Blue staining. These fractions were pooled, concentrated, and diafiltered into Buffer D to approximately 4.8 mg/mL in an Amicon concentrator using a 10 k MWCO YM10 membrane. The concentrated material was then submitted for crystallization.

Example 2 GSK3-B Construct Crystallization In this example, the crystallization of the GSK3-β ternary complex is described. A solution containing 100 mM of a seven residue peptide (N-LSRRPS*Y-C, purchased from Research Genetics), 20 mM ATP, 100 mM MgCl₂, and 100 mM Tris- HC1, pH 7.5 was mixed in a 1:10 ratio (v:v) with GSK-β protein solution in standard storage buffer. The GSK3-β protein solution used contained GSK3-β protein at 4.8 mg/ml in a storage buffer of 1 X TBS, 300mM NaCl, 20% glycerol, 0.2% (v:v) octylglucopyranoside, and 5mM DTT. The resulting solution was incubated in an ice bucket at 4° C for two hours. Following this incubation period, crystal drops were set up using the hanging drop method. A two-dimensional grid of a precipitant solution containing 7-12 % (w:v) PEG 6000 and 5-8% MPD (v:v) with 100 mM HEPES, pH 7.5, as the buffer, was established in the reservoirs of a linbro culture plate. The protein solution (2 uL) was mixed with 2 uL of the precipitant solution from the reservoir on a glass cover slip. The cover slip was then placed over the reservoir of the well. Ternary crystals grew overnight and reached maximum size in four days. The crystals were cryopreserved in the standard GSK3-β cryosolution. The resulting crystals grow in the P21 space group with a monomer in the asymmetric unit and have the following approximate unit cell: a=57.0 A, b=64.8 A, c=57.2 A , α=τ=90°, β=100.9°. These crystals diffract to better than 2.2 A on an in-house X-ray source and to better than 2.0 A on a synchrotron beamline. It should be noted that the peptide that actually appears to form the ternary complex is the diphosphorylated peptide, which must be formed in the enzymatic reaction during the incubation period.

Soaking of compounds for drug discovery is easily done by transplanting a crystal to a drop consisting of 5 uL of well solution (see above) and ImM (or other appropriate concentration) of lead compound for 12-24 hours. During this time, the ADP and peptide 'soak' out of the crystal while the lead compound 'soaks' in. This lowers the resolution that the crystal is capable of diffracting to somewhat (to around 2.5 Angstroms), but allows rapid determination of the structure of the complex. These crystals seem impervious to changes caused by the compounds soaked in.

The crystals can be cryoprotected for data collection in a cryosolution consisting of 12% PEG 6000, 11% MPD, 0.1 M HEPES pH 7.5, 20% glycerol. The cryosolution can include from about 10 to about 14 percent by weight polyethylene glycol (PEG 6000), from about 9 to about 13 percent by weight 2-methyl-2,4-pentanediol (MPD), and from about 18 to about 22 percent by weight glycerol. The cryosolution can have a pH of from about 7.3 to about 7.7.

Example 3 GSK3-β Ternary Complex Crystal Structure Resolution

In this example, a representative method for resolving the crystal structure of the GSK3-β ternary complex is described.

The crystal structure of the GSK3-β ternary complex crystal structure was obtained using the C222(l) crystal structure (see PCT/USO 1/29549) and the program EPMR (Kissinger, et al., "Rapid Automated Molecular Replacement By Evolutionary Search, Ada Crystallogr D Biol Crystallogr. 55 (Pt 2):AU-9\, February 1999). The solution was then processed through several rounds of a refinement macrocycle. A typical refinement macrocycle consists of 100-200 rounds of conjugate gradient minimization, simulated annealing with either torsion or Cartesian dynamics, and grouped or individual temperature factor calculation. All refinement procedures were executed using the program CNX (Molecular Simulation, Inc.) This was followed by calculation of new electron density maps and manual rebuilding of the model based on features within these maps using the program O (DATAONO AB). All data from 50A-2.0A in the data set was used. It should be note that the majority of the structure is very similar to the crystal form of GSK3-β described in PCT USO 1/29549. ADP and peptide were built into the electron density maps after the first round of refinement. The structure went through several rounds of refinement, including the addition of 235 structural waters, before the process converged at an R-factor of 25.1 and an R-free of 31.9 for all data from 50.0 -2.0 Angstroms. More traditional methods such as single/multiple isomorphous replacement or

MAD phasing by themselves or in conjunction with molecular replacement could have been used equally as well. A description of these methods and other crystallographic principles can be found in Shoichet, B.K. and D.E. Bussiere, "The Role of Macromolecular Crystallography and Structure For Drug Discovery: Advances and Caveats, Current Opinion in Drug Discovery & Development 3(A): 408-422, 2000.

The atomic coordinates for the GSK3-β ternary complex and the GSK3-β construct with representative compound soaked in are set forth in Tables 2 and 3, respectively. It will be appreciated that water positions will change from crystal to crystal.

Table 2

REMARK refinement resolution: 50.0 - 2.0 A

REMARK starting r= 0.2516 free_r= 0.3216

REMARK final ι= 0.2511 free_r= 0.3191

REMARK B rmsd for bonded mainchain atoms= 1.738 target= 1.5

REMARK B rmsd for bonded sidechain atoms= 2.030 target= 2.0

REMARK B rmsd for angle mainchain atoms= 2.997 target= 2.0

REMARK B rmsd for angle sidechain atoms= 3.170 target= 2.5

REMARK wa= 275140

REMARK rweight=7.340273E-02

REMARK target= residual steps= 50

REMARK sg= P2(l) a= 57.011 b= 64.769 c= 57.212 alpha= 90 beta= 100.931 gamma= 90

REMARK parameter file 1 : MSI_CNX_TOPPAR:protein.param

REMARK parameter file 2 : ptr.par

REMARK parameter file 3 : ../pgatp_10mM/model/sep.par

REMARK parameter file 4 : MSI_CNX_TOPPAR:water_rep.param REMARK parameter file 5 : ../pgatp_10mM/adp.par

REMARK molecular structure file: water_pick2_hrl .psf

REMARK input coordinates: water_pick2_hrl .pdb

REMARK reflection file= pgatp_complex_amalgam_hires.fob.cv

REMARK ncs= none

REMARK B-correction resolution: 6.0 - 2.0

REMARK initial B-factor correction applied to fobs :

REMARK Bl l= 9.519 B22= 9.818 B33= -19.337

REMARK B12= 0.000 B13= 2.929 B23= 0.000

REMARK B-factor correction applied to coordinate array B : 1.058

REMARK bulk solvent: (Mask) density level= 0.288754 e/A^Λ3, B-factor= 35.9759 A^Λ2

REMARK reflections with |Fobs|/sigma_F < 0.0 rejected

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

REMARK theoretical total number of refl. in resol. range: 27787 ( 100.0 % )

REMARK number of unobserved reflections (no entry or |F|=0): 674 ( 2.4 % )

REMARK number of reflections rejected: 0 ( 0.0 % )

REMARK total number of reflections used: 27113 ( 97.6 % )

REMARK number of reflections in working set: 25794 ( 92.8 % )

REMARK number of reflections in test set: 1319 ( 4.7 % )

REMARK Written by CNX VERSION:2000

ATOM 1 CB VAL A 37 52.964 39.855 11.567 1.00 62.47 A C ATOM 2 CGI VAL A 37 52.434 40.879 10.550^" 1.00 62.00 A C

ATOM 3 CG2 VAL A 37 53.806 38.778 10.891 1.00 63.77 A C

ATOM 4 C VAL A 37 53.071 41.785 13.164 1.00 63.31 A C

ATOM 5 O VAL A 37 52.166 41.687 14.001 1.00 62.97 A O

ATOM 6 N VAL A 37 54.231 39.594 13.697 1.00 62.28 A N

ATOM 7 CA VAL A 37 53.808 40.551 12.630 1.00 63.03 A C

ATOM 8 N THR A 38 53.417 42.936 12.594 1.00 64.28 A N

ATOM 9 CA THR A 38 52.886 44.227 13.022 1.00 65.25 A C

ATOM 10 CB THR A 38 54.050 45.289 13.025 1.00 66.02 A C

ATOM 11 OG1 THR A 38 53.589 46.538 13.553 1.00 66.31 A O

ATOM 12 CG2 THR A 38 54.626 45.492 11.609 1.00 67.12 A C

ATOM 13 C THR A 38 51.616 44.775 12.337 1.00 65.20 A C

ATOM 14 O THR A 38 51.400 44.587 11.134 1.00 64.53 A O

ATOM 15 N THR A 39 50.753 45.392 13.152 1.00 66.00 A N

ATOM 16 CA THR A 39 49.497 46.004 12.707 1.00 68.03 A C

ATOM 17 CB THR A 39 48.231 45.113 12.996 1.00 68.50 A C

ATOM 18 OG1 THR A 39 47.630 45.508 14.236 1.00 66.42 A O

ATOM 19 CG2 THR A 39 48.576 43.635 13.046 1.00 68.42 A C

ATOM 20 C THR A 39 49.318 47.348 13.438 1.00 69.40 A C

ATOM 21 O THR A 39 49.676 47.467 14.611 1.00 68.70 A O

ATOM 22 N VAL A 40 48.723 48.331 12.752 1.00 71.80 A N ATOM 23 CA VAL A 40 48.500 49.684 13.293 1.00 72.99 A C

ATOM 24 CB VAL A 40 49.391 50.740 12.526 1.00 73.77 A C

ATOM 25 CGI VAL A 40 50.875 50.368 12.606 1.00 72.91 A C

ATOM 26 CG2 VAL A 40 48.964 50.846 11.060 1.00 74.75 A C

ATOM 27 C VAL A 40 47.019 50.144 13.245 1.00 72.92 A C

ATOM 28 0 VAL A 40 46.300 49.852 12.273 1.00 73.69 A O

ATOM 29 N VAL A 41 46.583 50.870 14.286 1.00 72.36 A N

ATOM 30 CA VAL A 41 45.203 51.402 14.388 1.00 71.35 A C

ATOM 31 CB VAL A 41 44.275 50.464 15.202 1.00 71.28 A C

ATOM 32 CGI VAL A 41 43.862 49.270 14.371 1.00 70.39 A C

ATOM 33 CG2 VAL A 41 44.970 50.010 16.476 1.00 70.96 A C

ATOM 34 C VAL A 41 45.099 52.808 15.017 1.00 70.96 A C

ATOM 35 O VAL A 41 46.100 53.500 15.194 1.00 71.36 A O

ATOM 36 N ALA A 42 43.873 53.236 15.314 1.00 70.30 A N

ATOM 37 CA ALA A 42 43.627 54.540 15.932 1.00 70.21 A C

ATOM 38 CB ALA A 42 43.279 55.593 14.876 1.00 69.83 A C

ATOM 39 C ALA A 42 42.473 54.364 16.911 1.00 70.35 A C

ATOM 40 O ALA A 42 41.398 53.894 16.528 1.00 69.05 A O

ATOM 41 N THR A 43 42.709 54.742 18.171 1.00 70.96 A N

ATOM 42 CA THR A 43 41.711 54.605 19.248 1.00 71.53 A C

ATOM 43 CB THR A 43 41.821 53.234 19.884 1.00 72.10 A C ATOM 44 OG1 THR A 43 41.161 53.253 21.157 1.00 74.61 A O

ATOM 45 CG2 THR A 43 43.297 52.873 20.061 1.00 72.38 A C

ATOM 46 C THR A 43 41.874 55.627 20.382 1.00 70.59 A C

ATOM 47 0 THR A 43 42.986 56.095 20.618 1.00 71.06 A O

ATOM 48 N PRO A 44 40.772 55.939 21.121 1.00 69.22 A N

ATOM 49 CD PRO A 44 39.430 55.601 20.625 1.00 68.67 A C

ATOM 50 CA PRO A 44 40.650 56.884 22.253 1.00 68.74 A C

ATOM 51 CB PRO A 44 39.142 57.190 22.279 1.00 68.39 A C

ATOM 52 CG PRO A 44 38.682 56.874 20.900 1.00 68.54 A C

ATOM 53 C PRO A 44 41.144 56.510 23.669 1.00 68.26 A C

ATOM 54 0 PRO A 44 42.110 57.082 24.176 1.00 66.74 A O

ATOM 55 N GLY A 45 40.389 55.657 24.349 1.00 69.08 A N

ATOM 56 CA GLY A 45 40.756 55.258 25.693 1.00 70.50 A C

ATOM 57 C GLY A 45 39.875 55.865 26.769 1.00 72.53 A C

ATOM 58 O GLY A 45 38.911 56.571 26.465 1.00 72.84 A O

ATOM 59 N GLN A 46 40.204 55.588 28.030 1.00 75.01 A N

ATOM 60 CA GLN A 46 39.440 56.107 29.168 1.00 77.46 A C

ATOM 61 CB GLN A 46 39.478 55.106 30.327 1.00 77.83 A C

ATOM 62 CG GLN A 46 38.473 55.393 31.434 1.00 76.50 A C

ATOM 63 CD GLN A 46 38.925 54.871 32.799 1.00 75.55 A C

ATOM 64 OE1 GLN A 46 38.426 55.312 33.842 1.00 71.80 A O ATOM 65 NE2GLNA 46 39.87953.93732.796 1.0075.03 A N

ATOM 66 C GLNA 46 39.90657.49929.651 1.0079.37 A C

ATOM 670 GLNA 46 39.24758.12630.481 1.0078.65 A O

ATOM 68 N GLY A 47 41.061 57.95529.166 1.0081.96 A N

ATOM 69 CA GLY A 47 41.56259.27329.536 1.0085.04 A C

ATOM 70 C GLY A 47 40.89760.35628.687 1.0087.64 A C

ATOM 71 O GLY A 47 39.68660.28428.448 1.0088.30 A O

ATOM 72 N PROA 48 41.64961.37628.216 1.0089.17 A N

ATOM 73 CD PROA 48 43.02761.67428.664 1.0088.86 A C

ATOM 74 CA PROA 48 41.11662.47627.383 1.0089.64 A C

ATOM 75 CB PROA 48 42.09963.61527.670 1.0089.70 A C

ATOM 76 CG PROA 48 43.40962.88427.803 1.0089.22 A C

ATOM 77 C PROA 48 41.03262.16825.865 1.0089.93 A C

ATOM 78 O PROA 48 42.04762.21825.159 1.0090.23 A O

ATOM 79 N ASP A 49 39.81761.91125.368 1.0089.62 A N

ATOM 80 CA ASP A 49 39.571 61.57923.950 1.0089.54 A C

ATOM 81 CB ASP A 49 38.18862.08223.495 1.0088.53 A C

ATOM 82 CG ASP A 49 37.04961.19223.957 1.0086.66 A C

ATOM 83 OD1ASPA 49 37.31660.12724.552 1.0086.34 A O

ATOM 84 OD2ASPA 49 35.881 61.561 23.716 1.0084.70 A O

ATOM 85 C ASP A 49 40.61862.08822.958 1.0089.67 A C ATOM 86 0 ASP A 49 40.411 63.109 22.302 1.00 90.28 A O

ATOM 87 N ARG A 50 41.693 61.327 22.783 1.00 89.65 A N

ATOM 88 CA ARG A 50 42.761 61.724 21.867 1.00 89.99 A C

ATOM 89 CB ARG A 50 43.890 62.413 22.645 1.00 93.04 A C

ATOM 90 CG ARG A 50 44.407 63.702 21.999 1.00 98.81 A C

ATOM 91 CD ARG A 50 45.314 63.438 20.789 1.00103.62 A C

ATOM 92 NE ARG A 50 45.605 64.658 20.031 1.00107.53 A N

ATOM 93 CZ ARG A 50 45.282 64.845 18.750 1.00109.68 A C

ATOM 94 NH1 ARG A 50 44.657 63.894 18.060 1.00110.84 A N

ATOM 95 NH2 ARG A 50 45.556 66.001 18.163 1.00110.65 A N

ATOM 96 C ARG A 50 43.308 60.521 21.097 1.00 87.41 A C

ATOM 97 O ARG A 50 44.296 59.905 21.500 1.00 85.65 A O

ATOM 98 N PRO A 51 42.658 60.177 19.974 1.00 85.57 A N

ATOM 99 CD PRO A 51 41.431 60.869 19.548 1.00 84.89 A C

ATOM 100 CA PRO A 51 42.975 59.071 19.060 1.00 84.99 A C

ATOM 101 CB PRO A 51 41.997 59.312 17.913 1.00 85.36 A C

ATOM 102 CG PRO A 51 40.799 59.854 18.631 1.00 85.38 A C

ATOM 103 C PRO A 51 44.434 59.010 18.569 1.00 84.41 A C

ATOM 104 O PRO A 51 44.867 59.870 17.792 1.00 84.99 A O

ATOM 105 N GLN A 52 45.148 57.945 18.958 1.00 83.27 A N

ATOM 106 CA GLN A 52 46.566 57.753 18.603 1.00 82.53 A C ATOM 107 CB GLN A 52 47.435 57.781 19.864 1.00 84.07 A C

ATOM 108 CG GLN A 52 47.229 56.603 20.789 1.00 86.46 A C

ATOM 109 CD GLN A 52 47.519 56.949 22.247 1.00 88.48 A C

ATOM 110 OE1 GLN A 52 48.464 56.425 22.849 1.00 89.88 A O

ATOM 111 NE2 GLN A 52 46.694 57.825 22.827 1.00 88.28 A N

ATOM 112 C GLN A 52 46.924 56.501 17.803 1.00 80.58 A C

ATOM 113 O GLN A 52 46.188 55.525 17.782 1.00 80.54 A O

ATOM 114 N GLU A 53 48.095 56.538 17.176 1.00 79.33 A N

ATOM 115 CA GLU A 53 48.587 55.433 16.364 1.00 78.55 A C

ATOM 116 CB GLU A 53 49.458 55.962 15.205 1.00 80.14 A C

ATOM 117 CG GLU A 53 50.483 57.036 15.611 1.00 83.84 A C

ATOM 118 CD GLU A 53 51.551 57.317 14.539 1.00 85.69 A C

ATOM 119 OE1 GLU A 53 52.102 58.446 14.531 1.00 85.65 A O

ATOM 120 OE2 GLU A 53 51.858 56.406 13.731 1.00 86.49 A O

ATOM 121 C GLU A 53 49.351 54.389 17.186 1.00 76.89 A C

ATOM 122 O GLU A 53 50.568 54.478 17.354 1.00 75.34 A O

ATOM 123 N VAL A 54 48.615 53.406 17.703 1.00 76.02 A N

ATOM 124 CA VAL A 54 49.192 52.319 18.494 1.00 73.93 A C

ATOM 125 CB VAL A 54 48.286 51.922 19.667 1.00 73.59 A C

ATOM 126 CGI VAL A 54 48.242 53.046 20.689 1.00 74.90 A C

ATOM 127 CG2 VAL A 54 46.894 51.582 19.161 1.00 72.04 A C ATOM 128 C VAL A 54 49.413 51.089 17.627 1.00 72.92 A C

ATOM 129 O VAL A 54 48.489 50.606 16.963 1.00 72.97 A O

ATOM 130 N SER A 55 50.646 50.587 17.654 1.00 71.85 A N

ATOM 131 CA SER A 55 51.057 49.417 16.875 1.00 70.15 A C

ATOM 132 CB SER A 55 52.245 49.770 15.959 1.00 71.94 A C

ATOM 133 OG SER A 55 51.966 50.872 15.101 1.00 73.30 A O

ATOM 134 C SER A 55 51.444 48.245 17.786 1.00 67.67 A C

ATOM 135 O SER A 55 52.337 48.361 18.634 1.00 66.29 A O

ATOM 136 N TYR A 56 50.778 47.112 17.575 1.00 65.56 A N

ATOM 137 CA TYR A 56 51.013 45.904 18.355 1.00 63.50 A C

ATOM 138 CB TYR A 56 49.740 45.525 19.113 1.00 62.76 A C

ATOM 139 CG TYR A 56 48.515 45.253 18.250 1.00 63.19 A C

ATOM 140 CD1 TYR A 56 47.449 46.151 18.211 1.00 62.39 A C

ATOM 141 CE1 TYR A 56 46.267 45.854 17.503 1.00 63.83 A C

ATOM 142 CD2 TYR A 56 48.382 44.051 17.548 1.00 63.71 A C

ATOM 143 CE2 TYR A 56 47.209 43.745 16.838 1.00 65.04 A C

ATOM 144 CZ TYR A 56 46.150 44.646 16.820 1.00 64.23 A C

ATOM 145 OH TYR A 56 44.979 44.316 16.148 1.00 63.09 A O

ATOM 146 C TYR A 56 51.513 44.735 17.499 1.00 62.16 A C

ATOM 147 O TYR A 56 51.437 44.769 16.276 1.00 62.63 A O

ATOM 148 N THR A 57 52.048 43.708 18.144 1.00 60.34 A N ATOM 149 CA THR A 57 52.564 42.554 17.419 1.00 59.63 A C

ATOM 150 CB THR A 57 54.026 42.829 16.928 1.00 57.54 A C

ATOM 151 OG1 THR A 57 54.448 41.808 16.015 1.00 54.97 A O

ATOM 152 CG2 THR A 57 54.995 42.901 18.105 1.00 56.04 A C

ATOM 153 C THR A 57 52.467 41.298 18.312 1.00 60.85 A C

ATOM 154 O THR A 57 51.829 41.334 19.368 1.00 61.73 A O

ATOM 155 N ASP A 58 53.055 40.183 17.880 1.00 61.67 A N

ATOM 156 CA ASP A 58 53.003 38.937 18.655 1.00 60.38 A C

ATOM 157 CB ASP A 58 53.855 39.050 19.915 1.00 61.29 A C

ATOM 158 CG ASP A 58 55.311 39.313 19.604 1.00 60.65 A C

ATOM 159 OD1 ASP A 58 55.918 38.504 18.869 1.00 59.43 A O

ATOM 160 OD2 ASP A 58 55.841 40.333 20.097 1.00 62.10 A O

ATOM 161 C ASP A 58 51.570 38.627 19.037 1.00 59.00 A C

ATOM 162 0 ASP A 58 51.215 38.634 20.218 1.00 59.66 A O

ATOM 163 N THR A 59 50.763 38.362 18.013 1.00 57.34 A N

ATOM 164 CA THR A 59 49.346 38.063 18.153 1.00 54.67 A C

ATOM 165 CB THR A 59 48.551 38.626 16.943 1.00 55.34 A C

ATOM 166 OG1 THR A 59 48.116 39.960 17.231 1.00 55.66 A O

ATOM 167 CG2 THR A 59 47.357 37.760 16.614 1.00 55.50 A C

ATOM 168 C THR A 59 49.042 36.580 18.298 1.00 52.46 A C

ATOM 169 O THR A 59 49.484 35.756 17.497 1.00 52.93 A O ATOM 170 N LYS A 60 48.309 36.248 19.353 1.00 50.20 A N

ATOM 171 CA LYS A 60 47.900 34.880 19.598 1.00 48.19 A C

ATOM 172 CB LYS A 60 48.973 34.095 20.370 1.00 48.28 A C

ATOM 173 CG LYS A 60 49.209 34.524 21.815 1.00 52.03 A C

ATOM 174 CD LYS A 60 50.218 33.576 22.519 1.00 55.27 A C

ATOM 175 CE LYS A 60 50.339 33.828 24.037 1.00 55.03 A C

ATOM 176 NZ LYS A 60 51.305 32.887 24.711 1.00 56.36 A N

ATOM 177 C LYS A 60 46.580 34.929 20.357 1.00 46.35 A C

ATOM 178 O LYS A 60 46.276 35.915 21.026 1.00 45.31 A O

ATOM 179 N VAL A 61 45.751 33.911 20.149 1.00 44.84 A N

ATOM 180 CA VAL A 61 44.463 33.811 20.820 1.00 42.01 A C

ATOM 181 CB VAL A 61 43.514 32.868 20.027 1.00 41.45 A C

ATOM 182 CGI VAL A 61 42.091 32.955 20.561 1.00 42.35 A C

ATOM 183 CG2 VAL A 61 43.547 33.210 18.557 1.00 40.20 A C

ATOM 184 C VAL A 61 44.715 33.251 22.229 1.00 40.40 A C

ATOM 185 O VAL A 61 45.370 32.218 22.386 1.00 37.34 A O

ATOM 186 N ILE A 62 44.274 33.971 23.256 1.00 40.99 A N

ATOM 187 CA ILE A 62 44.475 33.488 24.614 1.00 43.02 A C

ATOM 188 CB ILE A 62 45.227 34.492 25.536 1.00 40.23 A C

ATOM 189 CG2 ILE A 62 46.631 34.733 25.024 1.00 40.71 A C

ATOM 190 CGI ILE A 62 44.445 35.787 25.711 1.00 38.13 A C ATOM 191 CD1 ILE A 62 45.190 36.849 26.504 1.00 36.04 A C

ATOM 192 C ILE A 62 43.191 33.091 25.301 1.00 46.67 A C

ATOM 193 O ILE A 62 43.228 32.418 26.331 1.00 48.93 A O

ATOM 194 N GLY A 63 42.056 33.474 24.724 1.00 49.61 A N

ATOM 195 CA GLY A 63 40.785 33.151 25.349 1.00 53.04 A C

ATOM 196 C GLY A 63 39.552 33.066 24.462 1.00 55.86 A C

ATOM 197 0 GLY A 63 39.626 33.023 23.227 1.00 56.41 A O

ATOM 198 N ASN A 64 38.403 32.994 25.126 1.00 57.93 A N

ATOM 199 CA ASN A 64 37.108 32.889 24.465 1.00 60.54 A C

ATOM 200 CB ASN A 64 37.099 31.688 23.509 1.00 59.42 A C

ATOM 201 CG ASN A 64 36.157 31.875 22.347 1.00 58.37 A C

ATOM 202 OD1 ASN A 64 35.362 32.814 22.313 1.00 57.86 A O

ATOM 203 ND2 ASN A 64 36.251 30.985 21.373 1.00 59.04 A N

ATOM 204 C ASN A 64 36.054 32.699 25.561 1.00 62.61 A C

ATOM 205 O ASN A 64 36.387 32.424 26.723 1.00 63.00 A O

ATOM 206 N GLY A 65 34.789 32.879 25.201 1.00 64.05 A N

ATOM 207 CA GLY A 65 33.727 32.714 26.175 1.00 64.83 A C

ATOM 208 C GLY A 65 32.388 33.242 25.698 1.00 65.71 A C

ATOM 209 O GLY A 65 32.155 33.393 24.491 1.00 63.50 A O

ATOM 210 N SER A 66 31.506 33.500 26.664 1.00 67.34 A N

ATOM 211 CA SER A 66 30.161 34.025 26.415 1.00 68.47 A C ATOM 212 CB SER A 66 29.757 34.984 27.562 1.00 71.11 A C

ATOM 213 OG SER A 66 30.761 35.958 27.857 1.00 72.83 A O

ATOM 214 C SER A 66 30.071 34.713 25.043 1.00 67.30 A C

ATOM 215 O SER A 66 29.298 34.309 24.171 1.00 67.14 A O

ATOM 216 N PHE A 67 30.858 35.771 24.885 1.00 66.38 A N

ATOM 217 CA PHE A 67 30.953 36.527 23.638 1.00 63.66 A C

ATOM 218 CB PHE A 67 29.934 37.675 23.558 1.00 63.82 A C

ATOM 219 CG PHE A 67 29.067 37.817 24.775 1.00 64.38 A C

ATOM 220 CD1 PHE A 67 27.735 37.407 24.745 1.00 64.61 A C

ATOM 221 CD2 PHE A 67 29.584 38.345 25.955 1.00 64.60 A C

ATOM 222 CE1 PHE A 67 26.928 37.523 25.870 1.00 65.17 A C

ATOM 223 CE2 PHE A 67 28.789 38.466 27.088 1.00 66.15 A C

ATOM 224 CZ PHE A 67 27.454 38.050 27.047 1.00 64.78 A C

ATOM 225 C PHE A 67 32.371 37.086 23.610 1.00 62.03 A C

ATOM 226 O PHE A 67 33.018 37.237 24.665 1.00 63.08 A O

ATOM 227 N GLY A 68 32.887 37.285 22.403 1.00 59.06 A N

ATOM 228 CA GLY A 68 34.224 37.825 22.249 1.00 54.57 A C

ATOM 229 C GLY A 68 35.429 36.936 22.524 1.00 50.88 A C

ATOM 230 O GLY A 68 35.589 36.381 23.620 1.00 50.54 A O

ATOM 231 N VAL A 69 36.245 36.758 21.486 1.00 46.18 A N

ATOM 232 CA VAL A 69 37.480 36.001 21.591 1.00 41.79 A C ATOM 233 CB VAL A 69 37.929 35.416 20.230 1.00 39.57 A C

ATOM 234 CGI VAL A 69 37.536 36.328 19.118 1.00 40.48 A C

ATOM 235 CG2 VAL A 69 39.423 35.223 20.219 1.00 37.24 A C

ATOM 236 C VAL A 69 38.491 37.023 22.107 1.00 39.35 A C

ATOM 237 O VAL A 69 38.333 38.217 21.894 1.00 41.42 A O

ATOM 238 N VAL A 70 39.504 36.566 22.822 1.00 37.57 A N

ATOM 239 CA VAL A 70 40.496 37.464 23.390 1.00 34.90 A C

ATOM 240 CB VAL A 70 40.453 37.400 24.928 1.00 32.97 A C

ATOM 241 CGI VAL A 70 41.390 38.415 25.514 1.00 31.00 A C

ATOM 242 CG2 VAL A 70 39.027 37.610 25.423 1.00 29.51 A C

ATOM 243 C VAL A 70 41.881 37.082 22.878 1.00 36.21 A C

ATOM 244 O VAL A 70 42.205 35.905 22.750 1.00 35.35 A O

ATOM 245 N TYR A 71 42.680 38.080 22.534 1.00 37.09 A N

ATOM 246 CA TYR A 71 44.006 37.817 22.018 1.00 38.38 A C

ATOM 247 CB TYR A 71 44.167 38.434 20.632 1.00 39.29 A C

ATOM 248 CG TYR A 71 43.178 37.971 19.600 1.00 40.04 A C

ATOM 249 CD1 TYR A 71 43.529 37.005 18.669 1.00 40.03 A C

ATOM 250 CE1 TYR A 71 42.648 36.620 17.676 1.00 43.33 A C

ATOM 251 CD2 TYR A 71 41.912 38.542 19.519 1.00 40.56 A C

ATOM 252 CE2 TYR A 71 41.017 38.169 18.535 1.00 41.56 A C

ATOM 253 CZ TYR A 71 41.384 37.204 17.608 1.00 45.04 A C ATOM 254 OH TYR A 71 40.494 36.818 16.612 1.00 46.56 A O

ATOM 255 C TYR A 71 45.056 38.423 22.917 1.00 38.85 A C

ATOM 256 O TYR A 71 44.751 39.218 23.797 1.00 37.35 A O

ATOM 257 N GLN A 72 46.298 38.005 22.716 1.00 41.61 A N

ATOM 258 CA GLN A 72 47.404 38.567 23.476 1.00 45.29 A C

ATOM 259 CB GLN A 72 48.297 37.481 24.072 1.00 45.63 A C

ATOM 260 CG GLN A 72 49.349 38.062 24.978 1.00 47.29 A C

ATOM 261 CD GLN A 72 50.519 37.143 25.165 1.00 50.13 A C

ATOM 262 OE1 GLN A 72 50.915 36.844 26.294 1.00 53.20 A O

ATOM 263 NE2 GLN A 72 51.099 36.698 24.058 1.00 51.52 A N

ATOM 264 C GLN A 72 48.209 39.399 22.475 1.00 46.18 A C

ATOM 265 O GLN A 72 48.392 38.987 21.322 1.00 46.65 A O

ATOM 266 N ALA A 73 48.686 40.563 22.904 1.00 46.77 A N

ATOM 267 CA ALA A 73 49.451 41.419 22.001 1.00 45.68 A C

ATOM 268 CB ALA A 73 48.501 42.334 21.200 1.00 44.21 A C

ATOM 269 C ALA A 73 50.544 42.246 22.667 1.00 44.64 A C

ATOM 270 O ALA A 73 50.344 42.873 23.719 1.00 44.26 A O

ATOM 271 N LYS A 74 51.713 42.211 22.042 1.00 42.69 A N

ATOM 272 CA LYS A 74 52.856 42.970 22.503 1.00 43.50 A C

ATOM 273 CB LYS A 74 54.161 42.221 22.149 1.00 42.65 A C

ATOM 274 CG LYS A 74 55.470 42.919 22.605 1.00 45.76 A C ATOM 275 CD LYS A 74 56.709 42.000 22.490 1.00 45.94 A C

ATOM 276 CE LYS A 74 58.037 42.739 22.731 1.00 45.49 A C

ATOM 277 NZ LYS A 74 58.362 43.716 21.649 1.00 42.82 A N

ATOM 278 C LYS A 74 52.791 44.355 21.829 1.00 44.66 A C

ATOM 279 0 LYS A 74 52.877 44.463 20.603 1.00 44.66 A O

ATOM 280 N LEU A 75 52.484 45.391 22.608 1.00 45.67 A N

ATOM 281 CA LEU A 75 52.446 46.745 22.069 1.00 45.49 A C

ATOM 282 CB LEU A 75 52.062 47.758 23.146 1.00 44.22 A C

ATOM 283 CG LEU A 75 50.722 47.698 23.867 1.00 42.65 A C

ATOM 284 CD1 LEU A 75 50.577 48.906 24.764 1.00 42.75 A C

ATOM 285 CD2 LEU A 75 49.626 47.699 22.860 1.00 45.10 A C

ATOM 286 C LEU A 75 53.881 47.023 21.618 1.00 47.69 A C

ATOM 287 0 LEU A 75 54.837 46.602 22.278 1.00 47.15 A O

ATOM 288 N CYS A 76 54.040 47.735 20.505 1.00 49.43 A N

ATOM 289 CA CYS A 76 55.371 48.022 19.987 1.00 50.01 A C

ATOM 290 CB CYS A 76 55.291 48.362 18.501 1.00 50.31 A C

ATOM 291 SG CYS A 76 54.816 46.959 17.466 1.00 49.00 A S

ATOM 292 C CYS A 76 56.116 49.113 20.753 1.00 50.60 A C

ATOM 293 O CYS A 76 57.321 48.992 21.003 1.00 50.79 A O

ATOM 294 N ASP A 77 55.403 50.164 21.144 1.00 50.83 A N

ATOM 295 CA ASP A 77 56.035 51.256 21.882 1.00 52.89 A C ATOM 296 CB ASP A 77 55.085 52.448 21.998 1.00 54.92 A C

ATOM 297 CG ASP A 77 55.500 53.613 21.099 1.00 56.94 A C

ATOM 298 OD1 ASP A 77 54.620 54.136 20.369 1.00 58.09 A O

ATOM 299 OD2 ASP A 77 56.701 53.994 21.124 1.00 56.18 A O

ATOM 300 C ASP A 77 56.543 50.852 23.263 1.00 52.60 A C

ATOM 301 O ASP A 77 57.755 50.701 23.469 1.00 51.51 A O

ATOM 302 N SER A 78 55.604 50.659 24.194 1.00 53.59 A N

ATOM 303 CA SER A 78 55.907 50.267 25.578 1.00 52.82 A C

ATOM 304 CB SER A 78 54.659 50.421 26.460 1.00 51.56 A C

ATOM 305 OG SER A 78 53.572 49.657 25.971 1.00 50.80 A O

ATOM 306 C SER A 78 56.548 48.878 25.784 1.00 52.05 A C

ATOM 307 O SER A 78 57.326 48.696 26.726 1.00 54.38 A O

ATOM 308 N GLY A 79 56.247 47.921 24.902 1.00 51.13 A N

ATOM 309 CA GLY A 79 56.808 46.575 25.008 1.00 49.18 A C

ATOM 310 C GLY A 79 55.941 45.680 25.880 1.00 48.85 A C

ATOM 311 O GLY A 79 56.233 44.496 26.109 1.00 47.80 A O

ATOM 312 N GLU A 80 54.858 46.284 26.361 1.00 47.52 A N

ATOM 313 CA GLU A 80 53.880 45.649 27.226 1.00 45.90 A C

ATOM 314 CB GLU A 80 52.988 46.724 27.865 1.00 46.60 A C

ATOM 315 CG GLU A 80 53.651 47.618 28.904 1.00 49.65 A C

ATOM 316 CD GLU A 80 52.732 48.760 29.352 1.00 52.98 A C ATOM 317 OE1 GLU A 80 52.078 49.368 28.468 1.00 56.66 A O

ATOM 318 OE2 GLU A 80 52.660 49.058 30.572 1.00 53.37 A O

ATOM 319 C GLU A 80 52.965 44.677 26.496 1.00 44.23 A C

ATOM 320 O GLU A 80 52.466 44.972 25.420 1.00 45.57 A O

ATOM 321 N LEU A 81 52.752 43.504 27.069 1.00 42.25 A N

ATOM 322 CA LEU A 81 51.810 42.588 26.460 1.00 40.35 A C

ATOM 323 CB LEU A 81 51.934 41.180 27.037 1.00 40.73 A C

ATOM 324 CG LEU A 81 53.247 40.421 26.953 1.00 41.22 A C

ATOM 325 CD1 LEU A 81 54.411 41.271 27.470 1.00 43.81 A C

ATOM 326 CD2 LEU A 81 53.094 39.157 27.780 1.00 41.64 A C

ATOM 327 C LEU A 81 50.481 43.177 26.929 1.00 38.72 A C

ATOM 328 O LEU A 81 50.419 43.845 27.970 1.00 38.10 A O

ATOM 329 N VAL A 82 49.428 42.933 26.158 1.00 38.70 A N

ATOM 330 CA VAL A 82 48.077 43.406 26.475 1.00 36.80 A C

ATOM 331 CB VAL A 82 47.751 44.757 25.793 1.00 37.25 A C

ATOM 332 CGI VAL A 82 48.460 45.894 26.488 1.00 36.40 A C

ATOM 333 CG2 VAL A 82 48.144 44.697 24.308 1.00 35.48 A C

ATOM 334 C VAL A 82 47.109 42.386 25.904 1.00 34.77 A C

ATOM 335 0 VAL A 82 47.482 41.606 25.038 1.00 36.41 A O

ATOM 336 N ALA A 83 45.874 42.395 26.393 1.00 33.95 A N

ATOM 337 CA ALA A 83 44.840 41.486 25.906 1.00 34.92 A C ATOM 338 CB ALA A 83 44.134 40.816 27.058 1.00 32.65 A C

ATOM 339 C ALA A 83 43.846 42.307 25.092 1.00 35.73 A C

ATOM 340 O ALA A 83 43.449 43.389 25.506 1.00 36.73 A O

ATOM 341 N ILE A 84 43.517 41.829 23.897 1.00 37.22 A N

ATOM 342 CA ILE A 84 42.562 42.507 23.025 1.00 37.12 A C

ATOM 343 CB ILE A 84 43.184 42.757 21.632 1.00 38.05 A C

ATOM 344 CG2 ILE A 84 42.123 43.281 20.656 1.00 38.96 A C

ATOM 345 CGI ILE A 84 44.369 43.715 21.773 1.00 37.32 A C

ATOM 346 CD1 ILE A 84 45.111 43.974 20.496 1.00 38.63 A C

ATOM 347 C ILE A 84 41.281 41.670 22.894 1.00 36.12 A C

ATOM 348 O ILE A 84 41.281 40.614 22.250 1.00 36.23 A O

ATOM 349 N LYS A 85 40.204 42.142 23.526 1.00 37.57 A N

ATOM 350 CA LYS A 85 38.910 41.460 23.509 1.00 38.77 A C

ATOM 351 CB LYS A 85 38.201 41.619 24.857 1.00 36.36 A C

ATOM 352 CG LYS A 85 37.027 40.685 24.999 1.00 37.09 A C

ATOM 353 CD LYS A 85 36.080 41.081 26.130 1.00 37.90 A C

ATOM 354 CE LYS A 85 34.814 40.214 26.079 1.00 39.15 A C

ATOM 355 NZ LYS A 85 33.746 40.539 27.072 1.00 40.17 A N

ATOM 356 C LYS A 85 38.003 41.946 22.368 1.00 41.60 A C

ATOM 357 0 LYS A 85 37.274 42.945 22.508 1.00 41.50 A O

ATOM 358 N LYS A 86 38.064 41.222 21.249 1.00 42.66 A N ATOM 359 CA LYS A 86 37.282 41.514 20.048 1.00 46.44 A C

ATOM 360 CB LYS A 86 38.046 41.014 18.819 1.00 44.97 A C

ATOM 361 CG LYS A 86 37.554 41.514 17.465 1.00 43.06 A C

ATOM 362 CD LYS A 86 38.397 40.881 16.364 1.00 39.98 A C

ATOM 363 CE LYS A 86 38.332 41.635 15.047 1.00 40.29 A C

ATOM 364 NZ LYS A 86 39.138 40.926 13.996 1.00 38.08 A N

ATOM 365 C LYS A 86 35.888 40.870 20.090 1.00 48.90 A C

ATOM 366 O LYS A 86 35.738 39.686 19.794 1.00 47.95 A O

ATOM 367 N VAL A 87 34.873 41.674 20.418 1.00 53.67 A N

ATOM 368 CA VAL A 87 33.481 41.210 20.519 1.00 56.92 A C

ATOM 369 CB VAL A 87 32.922 41.417 21.979 1.00 57.46 A C

ATOM 370 CGI VAL A 87 33.301 42.811 22.537 1.00 58.89 A C

ATOM 371 CG2 VAL A 87 31.418 41.200 22.011 1.00 57.01 A C

ATOM 372 C VAL A 87 32.520 41.790 19.461 1.00 58.81 A C

ATOM 373 O VAL A 87 31.768 42.720 19.725 1.00 58.46 A O

ATOM 374 N LEU A 88 32.560 41.202 18.268 1.00 62.36 A N

ATOM 375 CA LEU A 88 31.738 41.586 17.115 1.00 66.69 A C

ATOM 376 CB LEU A 88 31.654 40.391 16.143 1.00 66.45 A C

ATOM 377 CG LEU A 88 30.610 40.283 15.010 1.00 65.72 A C

ATOM 378 CD1 LEU A 88 29.232 39.883 15.532 1.00 64.69 A C

ATOM 379 CD2 LEU A 88 30.520 41.581 14.235 1.00 66.21 A C ATOM 380 C LEU A 88 30.325 42.122 17.396 1.00 70.04 A C

ATOM 381 O LEU A 88 29.951 43.202 16.919 1.00 69.57 A O

ATOM 382 N GLN A 89 29.540 41.322 18.117 1.00 74.14 A N

ATOM 383 CA GLN A 89 28.145 41.612 18.486 1.00 78.26 A C

ATOM 384 CB GLN A 89 27.981 41.624 20.014 1.00 80.37 A C

ATOM 385 CG GLN A 89 28.592 40.416 20.720 1.00 84.39 A C

ATOM 386 CD GLN A 89 28.167 39.084 20.115 1.00 86.80 A C

ATOM 387 OE1 GLN A 89 27.061 38.955 19.580 1.00 88.73 A O

ATOM 388 NE2 GLN A 89 29.051 38.085 20.193 1.00 87.39 A N

ATOM 389 C GLN A 89 27.408 42.818 17.876 1.00 79.47 A C

ATOM 390 O GLN A 89 26.964 43.719 18.607 1.00 79.93 A O

ATOM 391 N ASP A 90 27.260 42.829 16.548 1.00 80.34 A N

ATOM 392 CA ASP A 90 26.521 43.901 15.875 1.00 80.46 A C

ATOM 393 CB ASP A 90 26.918 44.043 14.393 1.00 77.64 A C

ATOM 394 CG ASP A 90 28.337 44.609 14.188 1.00 76.14 A C

ATOM 395 OD1 ASP A 90 28.678 44.928 13.020 1.00 72.76 A O

ATOM 396 OD2 ASP A 90 29.113 44.720 15.171 1.00 73.73 A O

ATOM 397 C ASP A 90 25.061 43.460 15.982 1.00 81.90 A C

ATOM 398 O ASP A 90 24.257 43.680 15.073 1.00 82.46 A O

ATOM 399 N LYS A 91 24.773 42.735 17.066 1.00 83.55 A N

ATOM 400 CA LYS A 91 23.435 42.230 17.368 1.00 84.72 A C ATOM 401 CB LYS A 91 23.503 40.879 18.086 1.00 85.25 A C

ATOM 402 CG LYS A 91 22.135 40.280 18.370 1.00 85.50 A C

ATOM 403 CD LYS A 91 22.192 39.109 19.358 1.00 87.22 A C

ATOM 404 CE LYS A 91 22.881 37.856 18.796 1.00 87.91 A C

ATOM 405 NZ LYS A 91 24.342 37.800 19.073 1.00 87.56 A N

ATOM 406 C LYS A 91 22.762 43.237 18.280 1.00 84.57 A C

ATOM 407 O LYS A 91 23.237 43.500 19.388 1.00 82.89 A O

ATOM 408 N ARG A 92 21.656 43.800 17.813 1.00 85.67 A N

ATOM 409 CA ARG A 92 20.965 44.788 18.607 1.00 86.46 A C

ATOM 410 CB ARG A 92 20.255 45.818 17.732 1.00 87.35 A C

ATOM 411 CG ARG A 92 21.282 46.786 17.134 1.00 87.74 A C

ATOM 412 CD ARG A 92 22.292 47.185 18.237 1.00 87.41 A C

ATOM 413 NE ARG A 92 23.515 47.818 17.741 1.00 86.69 A N

ATOM 414 CZ ARG A 92 23.815 49.109 17.885 1.00 86.44 A C

ATOM 415 NH1 ARG A 92 22.979 49.927 18.508 1.00 85.91 A N

ATOM 416 NH2 ARG A 92 24.972 49.584 17.434 1.00 87.03 A N

ATOM 417 C ARG A 92 20.135 44.269 19.760 1.00 86.49 A C

ATOM 418 O ARG A 92 18.965 43.884 19.632 1.00 85.79 A O

ATOM 419 N PHE A 93 20.869 44.174 20.866 1.00 86.66 A N

ATOM 420 CA PHE A 93 20.427 43.741 22.182 1.00 85.60 A C

ATOM 421 CB PHE A 93 21.058 42.388 22.520 1.00 87.23 A C ATOM 422 CG PHE A 93 20.083 41.256 22.574 1.00 88.81 A C

ATOM 423 CD1 PHE A 93 19.395 40.978 23.752 1.00 89.73 A C

ATOM 424 CD2 PHE A 93 19.870 40.450 21.458 1.00 89.70 A C

ATOM 425 CE1 PHE A 93 18.505 39.908 23.823 1.00 90.90 A C

ATOM 426 CE2 PHE A 93 18.985 39.376 21.514 1.00 90.88 A C

ATOM 427 CZ PHE A 93 18.298 39.104 22.704 1.00 91.21 A C

ATOM 428 C PHE A 93 21.068 44.814 23.064 1.00 83.88 A C

ATOM 429 0 PHE A 93 21.148 45.983 22.671 1.00 84.09 A O

ATOM 430 N LYS A 94 21.591 44.414 24.216 1.00 80.64 A N

ATOM 431 CA LYS A 94 22.238 45.372 25.092 1.00 77.91 A C

ATOM 432 CB LYS A 94 21.358 45.641 26.315 1.00 75.52 A C

ATOM 433 CG LYS A 94 19.923 46.039 25.981 1.00 71.68 A C

ATOM 434 CD LYS A 94 19.822 47.363 25.214 1.00 69.76 A C

ATOM 435 CE LYS A 94 20.000 48.592 26.112 1.00 69.19 A C

ATOM 436 NZ LYS A 94 19.587 49.853 25.417 1.00 66.98 A N

ATOM 437 C LYS A 94 23.622 44.873 25.515 1.00 77.27 A C

ATOM 438 O LYS A 94 23.736 43.942 26.309 1.00 77.15 A O

ATOM 439 N ASN A 95 24.671 45.444 24.927 1.00 76.47 A N

ATOM 440 CA ASN A 95 26.033 45.062 25.292 1.00 75.53 A C

ATOM 441 CB ASN A 95 27.030 45.413 24.194 1.00 77.06 A C

ATOM 442 CG ASN A 95 28.461 45.144 24.620 1.00 78.69 A C ATOM 443 OD1 ASN A 95 28.787 44.029 25.048 1.00 78.05 A O

ATOM 444 ND2 ASN A 95 29.314 46.171 24.551 1.00 78.69 A N

ATOM 445 C ASN A 95 26.433 45.806 26.563 1.00 73.89 A C

ATOM 446 0 ASN A 95 26.598 45.204 27.625 1.00 75.23 A O

ATOM 447 N ARG A 96 26.621 47.118 26.434 1.00 70.94 A N

ATOM 448 CA ARG A 96 26.988 47.967 27.565 1.00 67.78 A C

ATOM 449 CB ARG A 96 26.060 47.697 28.756 1.00 67.41 A C

ATOM 450 CG ARG A 96 24.592 47.925 28.472 1.00 67.84 A C

ATOM 451 CD ARG A 96 23.743 47.571 29.688 1.00 68.02 A C

ATOM 452 NE ARG A 96 22.334 47.904 29.473 1.00 69.43 A N

ATOM 453 CZ ARG A 96 21.318 47.071 29.685 1.00 69.75 A C

ATOM 454 NHl ARG A 96 21.546 45.840 30.125 1.00 68.74 A N

ATOM 455 NH2 ARG A 96 20.072 47.469 29.446 1.00 70.71 A N

ATOM 456 C ARG A 96 28.430 47.790 28.030 1.00 65.38 A C

ATOM 457 O ARG A 96 28.931 48.586 28.824 1.00 64.64 A O

ATOM 458 N GLU A 97 29.115 46.765 27.544 1.00 62.10 A N

ATOM 459 CA GLU A 97 30.463 46.568 28.033 1.00 58.33 A C

ATOM 460 CB GLU A 97 31.103 45.310 27.464 1.00 54.66 A C

ATOM 461 CG GLU A 97 32.313 44.919 28.252 1.00 51.20 A C

ATOM 462 CD GLU A 97 33.045 43.731 27.687 1.00 51.15 A C

ATOM 463 OEI GLU A 97 33.697 43.042 28.489 1.00 50.55 A O ATOM 464 OE2 GLU A 97 32.996 43.493 26.460 1.00 50.87 A O

ATOM 465 C GLU A 97 31.346 47.769 27.774 1.00 58.86 A C

ATOM 466 O GLU A 97 32.033 48.240 28.676 1.00 59.91 A O

ATOM 467 N LEU A 98 31.306 48.284 26.550 1.00 58.36 A N

ATOM 468 CA LEU A 98 32.133 49.426 26.170 1.00 56.36 A C

ATOM 469 CB LEU A 98 31.915 49.760 24.691 1.00 58.43 A C

ATOM 470 CG LEU A 98 32.615 50.940 23.991 1.00 59.61 A C

ATOM 471 CD1 LEU A 98 31.924 52.275 24.316 1.00 59.81 A C

ATOM 472 CD2 LEU A 98 34.097 50.969 24.324 1.00 59.74 A C

ATOM 473 C LEU A 98 31.923 50.662 27.028 1.00 55.35 A C

ATOM 474 0 LEU A 98 32.892 51.292 27.439 1.00 54.06 A O

ATOM 475 N GLN A 99 30.664 51.002 27.308 1.00 55.73 A N

ATOM 476 CA GLN A 99 30.365 52.190 28.108 1.00 55.38 A C

ATOM 477 CB GLN A 99 28.969 52.750 27.770 1.00 55.93 A C

ATOM 478 CG GLN A 99 27.797 51.842 28.051 1.00 55.63 A C

ATOM 479 CD GLN A 99 26.992 52.295 29.265 1.00 58.08 A C

ATOM 480 OE1 GLN A 99 25.770 52.121 29.318 1.00 58.26 A O

ATOM 481 NE2 GLN A 99 27.674 52.882 30.245 1.00 59.21 A N

ATOM 482 C GLN A 99 30.565 52.074 29.624 1.00 54.26 A C

ATOM 483 O GLN A 99 30.742 53.086 30.299 1.00 55.13 A O

ATOM 484 N ILE A 100 30.555 50.853 30.155 1.00 53.11 A N ATOM 485 CA ILE A 100 30.746 50.638 31.597 1.00 51.69 A C

ATOM 486 CB ILE A 100 29.982 49.376 32.116 1.00 51.11 A C

ATOM 487 CG2 ILE A 100 30.351 49.059 33.558 1.00 48.57 A C

ATOM 488 CGI ILE A 100 28.477 49.583 32.056 1.00 51.95 A C

ATOM 489 CD1 ILE A 100 27.701 48.525 32.846 1.00 54.98 A C

ATOM 490 C ILE A 100 32.228 50.486 31.965 1.00 51.22 A C

ATOM 491 O ILE A 100 32.637 50.821 33.066 1.00 50.62 A O

ATOM 492 N MET A 101 33.038 49.976 31.053 1.00 51.32 A N

ATOM 493 CA MET A 101 34.447 49.805 31.359 1.00 53.62 A C

ATOM 494 CB MET A 101 35.075 48.730 30.460 1.00 53.39 A C

ATOM 495 CG MET A 101 34.861 47.295 30.970 1.00 50.53 A C

ATOM 496 SD MET A 101 36.349 46.274 30.786 1.00 51.20 A S

ATOM 497 CE MET A 101 35.988 45.468 29.259 1.00 46.01 A C

ATOM 498 C MET A 101 35.261 51.110 31.358 1.00 56.00 A C

ATOM 499 0 MET A 101 36.223 51.248 32.118 1.00 56.87 A O

ATOM 500 N ARG A 102 34.895 52.061 30.500 1.00 58.14 A N

ATOM 501 CA ARG A 102 35.592 53.346 30.466 1.00 59.40 A C

ATOM 502 CB ARG A 102 35.658 53.908 29.039 1.00 60.86 A C

ATOM 503 CG ARG A 102 34.333 53.917 28.295 1.00 62.76 A C

ATOM 504 CD ARG A 102 34.556 54.210 26.816 1.00 63.43 A C

ATOM 505 NE ARG A 102 35.345 55.421 26.613 1.00 64.58 A N ATOM 506 CZ ARG A 102 34.985 56.431 25.825 1.00 66.38 A C

ATOM 507 NHl ARG A 102 33.837 56.381 25.150 1.00 66.63 A N

ATOM 508 NH2 ARG A 102 35.770 57.502 25.728 1.00 67.99 A N

ATOM 509 C ARG A 102 34.808 54.258 31.405 1.00 58.97 A C

ATOM 510 O ARG A 102 34.267 55.288 31.002 1.00 61.35 A O

ATOM 511 N LYS A 103 34.739 53.820 32.663 1.00 57.41 A N

ATOM 512 CA LYS A 103 34.029 54.487 33.759 1.00 54.91 A C

ATOM 513 CB LYS A 103 32.517 54.234 33.605 1.00 56.05 A C

ATOM 514 CG LYS A 103 31.627 54.647 34.781 1.00 58.18 A C

ATOM 515 CD LYS A 103 30.193 54.114 34.600 1.00 59.37 A C

ATOM 516 CE LYS A 103 29.227 54.645 35.665 1.00 59.73 A C

ATOM 517 NZ LYS A 103 27.813 54.217 35.410 1.00 60.49 A N

ATOM 518 C LYS A 103 34.546 53.816 35.045 1.00 52.85 A C

ATOM 519 0 LYS A 103 34.203 54.200 36.171 1.00 52.32 A O

ATOM 520 N LEU A 104 35.406 52.820 34.858 1.00 49.69 A N

ATOM 521 CA LEU A 104 35.954 52.071 35.984 1.00 47.86 A C

ATOM 522 CB LEU A 104 35.576 50.579 35.880 1.00 46.36 A C

ATOM 523 CG LEU A 104 34.101 50.161 35.883 1.00 42.83 A C

ATOM 524 CD1 LEU A 104 34.011 48.661 35.581 1.00 41.91 A C

ATOM 525 CD2 LEU A 104 33.424 50.515 37.215 1.00 40.25 A C

ATOM 526 C LEU A 104 37.462 52.206 36.212 1.00 45.38 A C ATOM 527 0 LEU A 104 38.277 52.140 35.285 1.00 44.77 A O

ATOM 528 N ASP A 105 37.804 52.352 37.487 1.00 44.69 A N

ATOM 529 CA ASP A 105 39.181 52.492 37.939 1.00 43.77 A C

ATOM 530 CB ASP A 105 39.541 53.977 38.068 1.00 45.37 A C

ATOM 531 CG ASP A 105 41.024 54.207 38.292 1.00 46.12 A C

ATOM 532 OD1 ASP A 105 41.354 55.140 39.041 1.00 48.52 A O

ATOM 533 OD2 ASP A 105 41.859 53.476 37.720 1.00 46.94 A O

ATOM 534 C ASP A 105 39.319 51.812 39.310 1.00 41.80 A C

ATOM 535 O ASP A 105 39.042 52.437 40.347 1.00 42.18 A O

ATOM 536 N HIS A 106 39.675 50.520 39.298 1.00 37.59 A N

ATOM 537 CA HIS A 106 39.886 49.739 40.522 1.00 33.12 A C

ATOM 538 CB HIS A 106 38.625 48.963 40.939 1.00 31.57 A C

ATOM 539 CG HIS A 106 38.578 48.580 42.395 1.00 27.81 A C

ATOM 540 CD2 HIS A 106 38.058 49.224 43.470 1.00 28.07 A C

ATOM 541 ND1 HIS A 106 39.047 47.372 42.871 1.00 27.43 A N

ATOM 542 CE1 HIS A 106 38.816 47.289 44.172 1.00 27.42 A C

ATOM 543 NE2 HIS A 106 38.218 48.400 44.560 1.00 26.05 A N

ATOM 544 C HIS A 106 41.026 48.776 40.226 1.00 33.24 A C

ATOM 545 0 HIS A 106 41.189 48.294 39.089 1.00 31.87 A O

ATOM 546 N CYS A 107 41.865 48.585 41.241 1.00 33.77 A N

ATOM 547 CA CYS A 107 43.020 47.701 41.159 1.00 32.36 A C ATOM 548 CB CYS A 107 43.930 47.914 42.380 1.00 34.33 A C

ATOM 549 SG CYS A 107 43.112 47.762 44.014 1.00 37.57 A S

ATOM 550 C CYS A 107 42.571 46.244 41.074 1.00 31.13 A C

ATOM 551 0 CYS A 107 43.382 45.357 40.789 1.00 33.04 A O

ATOM 552 N ASN A 108 41.285 46.004 41.339 1.00 26.92 A N

ATOM 553 CA ASN A 108 40.739 44.665 41.279 1.00 23.95 A C

ATOM 554 CB ASN A 108 40.096 44.303 42.613 1.00 23.35 A C

ATOM 555 CG ASN A 108 41.134 44.085 43.697 1.00 22.75 A C

ATOM 556 OD1 ASN A 108 40.935 44.430 44.866 1.00 23.77 A O

ATOM 557 ND2 ASN A 108 42.267 43.504 43.306 1.00 21.50 A N

ATOM 558 C ASN A 108 39.805 44.466 40.084 1.00 24.27 A C

ATOM 559 0 ASN A 108 39.003 43.533 40.043 1.00 22.46 A O

ATOM 560 N ILE A 109 39.992 45.310 39.070 1.00 23.70 A N

ATOM 561 CA ILE A 109 39.224 45.256 37.833 1.00 23.34 A C

ATOM 562 CB ILE A 109 38.015 46.273 37.873 1.00 23.41 A C

ATOM 563 CG2 ILE A 109 37.277 46.312 36.535 1.00 25.40 A C

ATOM 564 CGI ILE A 109 37.005 45.860 38.940 1.00 23.61 A C

ATOM 565 CD1 ILE A 109 35.928 46.851 39.186 1.00 23.75 A C

ATOM 566 C ILE A 109 40.203 45.559 36.678 1.00 23.85 A C

ATOM 567 0 ILE A 109 40.974 46.510 36.763 1.00 24.61 A O

ATOM 568 N VAL A 110 40.222 44.718 35.638 1.00 25.42 A N ATOM 569 CA VAL A 110 41.13444.92934.500 1.0030.37 A C

ATOM 570 CB VAL A 110 40.90343.94233.297 1.0031.05 A C

ATOM 571 CGI VALA 110 42.22443.33932.825 1.0029.62 A C

ATOM 572 CG2VALA110 39.891 42.883 33.637 1.0034.59 A C

ATOM 573 C VALA 110 40.92846.33233.945 1.0032.52 A C

ATOM 574 O VALA 110 39.79746.80933.834 1.0031.60 A O

ATOM 575 N ARG A 111 42.03046.991 33.607 1.0036.56 A N

ATOM 576 CA ARGA 111 41.96448.33933.058 1.0038.83 A C

ATOM 577 CB ARGA 111 43.181 49.17933.466 1.0039.00 A C

ATOM 578 CG ARGA 111 43.13450.595 32.904 1.0039.84 A C

ATOM 579 CD ARGA 111 44.45451.313 33.058 1.0041.02 A C

ATOM 580 NE ARGA 111 45.52250.59032.389 1.0043.02 A N

ATOM 581 CZ ARGA 111 46.81750.835 32.542 1.0045.60 A C

ATOM 582 NHl ARGA 111 47.23451.803 33.355 1.0045.36 A N

ATOM 583 NH2ARGA111 47.695 50.10731.864 1.0047.87 A N

ATOM 584 C ARGA 111 41.87348.32831.545 1.0038.29 A C

ATOM 585 O ARGA 111 42.58647.57830.864 1.0037.13 A O

ATOM 586 N LEU A 112 40.94649.13831.043 1.0040.88 A N

ATOM 587 CA LEU A 112 40.741 49.30429.618 1.0042.64 A C

ATOM 588 CB LEUA112 39.26649.58429.317 1.0042.13 A C

ATOM 589 CG LEUA112 38.941 50.02827.885 1.0041.67 A C ATOM 590 CD1 LEU A 112 39.294 48.951 26.863 1.00 39.98 A C

ATOM 591 CD2 LEU A 112 37.472 50.402 27.811 1.00 42.47 A C

ATOM 592 C LEU A 112 41.605 50.483 29.174 1.00 44.33 A C

ATOM 593 O LEU A 112 41.341 51.643 29.515 1.00 44.94 A O

ATOM 594 N ARG A 113 42.683 50.170 28.474 1.00 46.58 A N

ATOM 595 CA ARG A 113 43.562 51.201 27.977 1.00 49.96 A C

ATOM 596 CB ARG A 113 44.880 50.596 27.536 1.00 49.33 A C

ATOM 597 CG ARG A 113 45.533 49.731 28.574 1.00 52.35 A C

ATOM 598 CD ARG A 113 46.918 49.337 28.119 1.00 54.97 A C

ATOM 599 NE ARG A 113 47.440 48.197 28.856 1.00 56.47 A N

ATOM 600 CZ ARG A 113 48.623 48.180 29.449 1.00 57.97 A C

ATOM 601 NHl ARG A 113 49.397 49.259 29.390 1.00 57.41 A N

ATOM 602 NH2 ARG A 113 49.040 47.072 30.063 1.00 60.91 A N

ATOM 603 C ARG A 113 42.895 51.899 26.790 1.00 53.46 A C

ATOM 604 O ARG A 113 42.491 53.059 26.903 1.00 55.67 A O

ATOM 605 N TYR A 114 42.724 51.164 25.684 1.00 55.99 A N

ATOM 606 CA TYR A 114 42.129 51.693 24.447 1.00 58.32 A C

ATOM 607 CB TYR A 114 43.200 51.786 23.347 1.00 57.35 A C

ATOM 608 CG TYR A 114 44.544 52.332 23.792 1.00 57.73 A C

ATOM 609 CD1 TYR A 114 45.668 51.518 23.809 1.00 57.85 A C

ATOM 610 CE1 TYR A 114 46.894 52.003 24.214 1.00 60.01 A C ATOM 611 CD2 TYR A 114 44.688 53.656 24.195 1.00 59.32 A C

ATOM 612 CE2 TYR A 114 45.910 54.154 24.604 1.00 59.56 A C

ATOM 613 CZ TYR A 114 47.013 53.325 24.610 1.00 60.94 A C

ATOM 614 OH TYR A 114 48.248 53.819 24.996 1.00 64.22 A O

ATOM 615 C TYR A 114 40.984 50.824 23.933 1.00 60.21 A C

ATOM 616 0 TYR A 114 40.771 49.734 24.437 1.00 60.68 A O

ATOM 617 N PHE A 115 40.282 51.304 22.905 1.00 64.05 A N

ATOM 618 CA PHE A 115 39.155 50.583 22.279 1.00 68.07 A C

ATOM 619 CB PHE A 115 37.855 50.790 23.077 1.00 69.09 A C

ATOM 620 CG PHE A 115 37.194 52.124 22.831 1.00 70.84 A C

ATOM 621 CD1 PHE A 115 36.181 52.250 21.882 1.00 71.34 A C

ATOM 622 CD2 PHE A 115 37.597 53.254 23.537 1.00 71.16 A C

ATOM 623 CE1 PHE A 115 35.586 53.479 21.639 1.00 71.98 A C

ATOM 624 CE2 PHE A 115 37.006 54.489 23.300 1.00 71.38 A C

ATOM 625 CZ PHE A 115 36.000 54.604 22.351 1.00 71.48 A C

ATOM 626 C PHE A 115 38.918 51.055 20.832 1.00 70.42 A C

ATOM 627 0 PHE A 115 38.644 52.237 20.607 1.00 71.61 A O

ATOM 628 N PHE A 116 39.018 50.145 19.859 1.00 72.32 A N

ATOM 629 CA PHE A 116 38.791 50.508 18.450 1.00 73.84 A C

ATOM 630 CB PHE A 116 40.107 50.552 17.668 1.00 74.62 A C

ATOM 631 CG PHE A 116 40.862 49.247 17.642 1.00 76.56 A C ATOM 632 CDl PHE A 116 40.73048.374 16.563 1.0077.09 A C

ATOM 633 CD2PHEA116 41.76848.930 18.655 1.0076.69 A C

ATOM 634 CE1PHEA116 41.491 47.212 16.489 1.0077.07 A C

ATOM 635 CE2 PHE A 116 42.53547.772 18.592 1.0075.51 A C

ATOM 636 CZ PHE A 116 42.39946.912 17.507 1.0076.47 A C

ATOM 637 C PHE A 116 37.75649.649 17.709 1.0074.55 A C

ATOM 638 O PHEA116 36.99048.915 18.339 1.0075.46 A O

ATOM 639 N TYRA117 37.671 49.836 16.388 1.0074.71 A N

ATOM 640 CA TYRA117 36.741 49.093 15.5141.0074.55 A C

ATOM 641 CB TYR A 117 35.53949.968 15.112 1.0067.13 A C

ATOM 642 CG TYR A 117 34.583 50.33416.234 1.0059.10 A C

ATOM 643 CDl TYR A 117 33.42949.606 16.451 1.0055.00 A C

ATOM 644 CE1 TYR A 117 32.53349.962 17.445 1.0054.09 A C

ATOM 645 CD2TYRA117 34.821 51.432 17.046 1.0057.38 A C

ATOM 646 CE2TYRA117 33.931 51.799 18.049 1.0054.84 A C

ATOM 647 CZ TYR A 117 32.785 51.060 18.250 1.0053.40 A C

ATOM 648 OH TYR A 117 31.90851.397 19.271 1.0048.17 A O

ATOM 649 C TYR A 117 37.51448.640 14.263 1.0078.31 A C

ATOM 650 O TYR A 117 38.43349.337 13.817 1.0078.31 A O

ATOM 651 N SERA 118 37.17347.478 13.704 1.0082.98 A N

ATOM 652 CA SERA 118 37.89847.000 12.521 1.0088.44 A C ATOM 653 CB SER A 118 39.377 46.765 12.871 1.00 87.26 A C

ATOM 654 OG SER A 118 39.555 45.560 13.607 1.00 85.26 A O

ATOM 655 C SER A 118 37.347 45.726 11.877 1.00 92.60 A C

ATOM 656 O SER A 118 36.213 45.326 12.129 1.00 93.26 A O

ATOM 657 N SER A 119 38.182 45.114 11.035 1.00 97.53 A N

ATOM 658 CA SER A 119 37.896 43.862 10.322 1.00102.53 A C

ATOM 659 CB SER A 119 37.729 42.696 11.306 1.00102.11 A C

ATOM 660 OG SER A 119 38.932 42.454 12.013 1.00103.47 A O

ATOM 661 C SER A 119 36.770 43.846 9.284 1.00105.96 A C

ATOM 662 0 SER A 119 36.047 44.838 9.107 1.00106.64 A O

ATOM 663 N GLY A 120 36.638 42.697 8.612 1.00109.33 A N

ATOM 664 CA GLY A 120 35.637 42.511 7.565 1.00113.28 A C

ATOM 665 C GLY A 120 36.097 43.092 6.229 1.00115.71 A C

ATOM 666 0 GLY A 120 35.968 44.303 6.012 1.00116.49 A O

ATOM 667 N GLU A 121 36.587 42.241 5.317 1.00117.12 A N

ATOM 668 CA GLU A 121 37.094 42.706 4.011 1.00118.33 A C

ATOM 669 CB GLU A 121 38.562 42.255 3.818 1.00119.45 A C

ATOM 670 CG GLU A 121 39.588 43.009 4.709 1.00120.23 A C

ATOM 671 CD GLU A 121 40.994 42.385 4.724 1.00120.94 A C

ATOM 672 OEI GLU A 121 41.656 42.355 3.660 1.00121.17 A O

ATOM 673 OE2 GLU A 121 41.443 41.948 5.812 1.00120.33 A O ATOM 674 C GLU A 121 36.268 42.473 2.711 1.00118.24 A C

ATOM 675 0 GLU A 121 36.817 42.058 1.681 1.00118.10 A O

ATOM 676 N LYS A 122 34.964 42.779 2.769 1.00117.74 A N

ATOM 677 CA LYS A 122 34.025 42.681 1.626 1.00116.06 A C

ATOM 678 CB LYS A 122 33.818 41.240 1.145 1.00114.80 A C

ATOM 679 CG LYS A 122 32.895 41.127 -0.084 1.00112.84 A C

ATOM 680 CD LYS A 122 33.557 41.699 -1.360 1.00111.74 A C

ATOM 681 CE LYS A 122 33.412 43.225 -1.538 1.00110.22 A C

ATOM 682 NZ LYS A 122 32.064 43.663 -1.976 1.00109.02 A N

ATOM 683 C LYS A 122 32.655 43.315 1.927 1.00115.39 A C

ATOM 684 0 LYS A 122 32.201 44.207 1.200 1.00115.16 A O

ATOM 685 N LYS A 123 31.984 42.825 2.972 1.00114.01 A N

ATOM 686 CA LYS A 123 30.684 43.364 3.370 1.00112.21 A C

ATOM 687 CB LYS A 123 29.582 42.295 3.279 1.00112.84 A C

ATOM 688 CG LYS A 123 29.035 42.074 1.864 1.00113.44 A C

ATOM 689 CD LYS A 123 27.628 41.481 1.897 1.00113.87 A C

ATOM 690 CE LYS A 123 26.938 41.543 0.529 1.00114.47 A C

ATOM 691 NZ LYS A 123 27.535 40.621 -0.478 1.00114.00 A N

ATOM 692 C LYS A 123 30.685 44.036 4.755 1.00110.67 A C

ATOM 693 O LYS A 123 31.713 44.533 5.222 1.00110.40 A O

ATOM 694 N ASP A 124 29.522 44.049 5.400 1.00109.19 A N ATOM 695 CA ASP A 124 29.345 44.685 6.711 1.00106.97 A C

ATOM 696 CB ASP A 124 27.846 44.737 7.069 1.00106.42 A C

ATOM 697 CG ASP A 124 27.142 43.400 6.871 1.00105.35 A C

ATOM 698 OD1 ASP A 124 27.356 42.462 7.677 1.00104.12 A O

ATOM 699 OD2 ASP A 124 26.361 43.297 5.902 1.00105.49 A O

ATOM 700 C ASP A 124 30.156 44.190 7.929 1.00105.28 A C

ATOM 701 O ASP A 124 31.391 44.071 7.871 1.00104.96 A O

ATOM 702 N GLU A 125 29.427 43.973 9.035 1.00102.47 A N

ATOM 703 CA GLU A 125 29.943 43.528 10.340 1.00 97.57 A C

ATOM 704 CB GLU A 125 29.870 41.995 10.483 1.00 96.91 A C

ATOM 705 CG GLU A 125 30.510 41.197 9.350 1.00 97.60 A C

ATOM 706 CD GLU A 125 30.624 39.710 9.666 1.00 97.50 A C

ATOM 707 OE1 GLU A 125 29.748 39.190 10.389 1.00 97.21 A O

ATOM 708 OE2 GLU A 125 31.595 39.067 9.199 1.00 97.16 A O

ATOM 709 C GLU A 125 31.322 44.081 10.757 1.00 94.98 A C

ATOM 710 O GLU A 125 32.366 43.542 10.373 1.00 93.99 A O

ATOM 711 N VAL A 126 31.300 45.198 11.496 1.00 91.91 A N

ATOM 712 CA VAL A 126 32.510 45.863 12.018 1.00 88.16 A C

ATOM 713 CB VAL A 126 32.541 47.415 11.711 1.00 88.34 A C

ATOM 714 CGI VAL A 126 32.865 47.667 10.234 1.00 88.24 A C

ATOM 715 CG2 VAL A 126 31.215 48.082 12.075 1.00 88.10 A C ATOM 716 C VAL A 126 32.599 45.614 13.537 1.00 85.14 A C

ATOM 717 O VAL A 126 31.857 46.204 14.325 1.00 85.94 A O

ATOM 718 N TYR A 127 33.505 44.721 13.929 1.00 81.03 A N

ATOM 719 CA TYR A 127 33.685 44.320 15.327 1.00 76.14 A C

ATOM 720 CB TYR A 127 34.626 43.095 15.406 1.00 77.59 A C

ATOM 721 CG TYR A 127 34.600 42.131 14.214 1.00 79.50 A C

ATOM 722 CDl TYR A 127 34.716 42.592 12.900 1.00 80.76 A C

ATOM 723 CE1 TYR A 127 34.739 41.701 11.807 1.00 82.49 A C

ATOM 724 CD2 TYR A 127 34.506 40.753 14.410 1.00 80.31 A C

ATOM 725 CE2 TYR A 127 34.530 39.854 13.329 1.00 82.30 A C

ATOM 726 CZ TYR A 127 34.647 40.333 12.022 1.00 82.76 A C

ATOM 727 OH TYR A 127 34.671 39.465 10.931 1.00 83.20 A O

ATOM 728 C TYR A 127 34.211 45.418 16.264 1.00 71.69 A C

ATOM 729 O TYR A 127 34.801 46.408 15.817 1.00 70.97 A O

ATOM 730 N LEU A 128 33.957 45.241 17.560 1.00 66.32 A N

ATOM 731 CA LEU A 128 34.445 46.158 18.600 1.00 61.86 A C

ATOM 732 CB LEU A 128 33.369 46.421 19.670 1.00 60.15 A C

ATOM 733 CG LEU A 128 33.840 46.909 21.058 1.00 58.82 A C

ATOM 734 CDl LEU A 128 34.623 48.192 20.938 1.00 58.66 A C

ATOM 735 CD2 LEU A 128 32.655 47.088 22.026 1.00 58.42 A C

ATOM 736 C LEU A 128 35.659 45.505 19.276 1.00 58.96 A C ATOM 737 0 LEU A 128 35.648 44.310 19.552 1.00 59.74 A O

ATOM 738 N- ASN A 129 36.714 46.271 19.520 1.00 54.46 A N

ATOM 739 CA ASN A 129 37.882 45.717 20.184 1.00 51.02 A C

ATOM 740 CB ASN A 129 39.118 45.808 19.295 1.00 52.71 A C

ATOM 741 CG ASN A 129 38.895 45.221 17.934 1.00 53.98 A C

ATOM 742 OD1 ASN A 129 37.965 45.612 17.246 1.00 56.47 A O

ATOM 743 ND2 ASN A 129 39.757 44.290 17.523 1.00 54.27 A N

ATOM 744 C ASN A 129 38.162 46.463 21.475 1.00 48.35 A C

ATOM 745 0 ASN A 129 37.960 47.666 21.572 1.00 47.89 A O

ATOM 746 N LEU A 130 38.610 45.735 22.483 1.00 45.63 A N

ATOM 747 CA LEU A 130 38.952 46.347 23.754 1.00 42.61 A C

ATOM 748 CB LEU A 130 38.062 45.800 24.863 1.00 41.40 A C

ATOM 749 CG LEU A 130 36.568 46.041 24.688 1.00 42.53 A C

ATOM 750 CD1 LEU A 130 35.778 45.528 25.907 1.00 41.18 A C

ATOM 751 CD2 LEU A 130 36.351 47.519 24.504 1.00 43.02 A C

ATOM 752 C LEU A 130 40.396 45.988 24.041 1.00 41.25 A C

ATOM 753 O LEU A 130 40.766 44.833 23.884 1.00 43.06 A O

ATOM 754 N VAL A 131 41.244 46.975 24.321 1.00 40.44 A N

ATOM 755 CA VAL A 131 42.641 46.686 24.662 1.00 40.17 A C

ATOM 756 CB VAL A 131 43.628 47.665 24.007 1.00 40.61 A C

ATOM 757 CGI VAL A 131 45.061 47.270 24.367 1.00 38.55 A C ATOM 758 CG2 VAL A 131 43.436 47.685 22.502 1.00 37.67 A C

ATOM 759 C VAL A 131 42.758 46.783 26.198 1.00 41.44 A C

ATOM 760 O VAL A 131 42.668 47.873 26.772 1.00 42.39 A O

ATOM 761 N LEU A 132 42.957 45.635 26.853 1.00 40.54 A N

ATOM 762 CA LEU A 132 43.024 45.552 28.316 1.00 38.63 A C

ATOM 763 CB LEU A 132 42.024 44.496 28.785 1.00 36.48 A C

ATOM 764 CG LEU A 132 40.590 44.617 28.268 1.00 32.94 A C

ATOM 765 CDl LEU A 132 39.871 43.287 28.435 1.00 34.26 A C

ATOM 766 CD2 LEU A 132 39.864 45.734 28.979 1.00 31.75 A C

ATOM 767 C LEU A 132 44.396 45.180 28.851 1.00 37.78 A C

ATOM 768 0 LEU A 132 45.309 44.884 28.086 1.00 38.30 A O

ATOM 769 N ASP A 133 44.541 45.231 30.175 1.00 37.79 A N

ATOM 770 CA ASP A 133 45.792 44.848 30.829 1.00 36.20 A C

ATOM 771 CB ASP A 133 45.711 45.104 32.333 1.00 39.92 A C

ATOM 772 CG ASP A 133 45.820 46.564 32.695 1.00 42.64 A C

ATOM 773 OD1 ASP A 133 46.491 47.319 31.952 1.00 40.59 A O

ATOM 774 OD2 ASP A 133 45.253 46.933 33.755 1.00 46.04 A O

ATOM 775 C ASP A 133 45.910 43.343 30.643 1.00 35.09 A C

ATOM 776 0 ASP A 133 44.899 42.632 30.749 1.00 36.43 A O

ATOM 777 N TYR A 134 47.111 42.837 30.374 1.00 30.51 A N

ATOM 778 CA TYR A 134 47.229 41.401 30.212 1.00 31.24 A C ATOM 779 CB TYR A 134 48.452 40.995 29.408 1.00 30.01 A C

ATOM 780 CG TYR A 134 48.587 39.495 29.329 1.00 30.92 A C

ATOM 781 CDl TYR A 134 47.674 38.742 28.607 1.00 31.11 A C

ATOM 782 CE1 TYR A 134 47.760 37.346 28.559 1.00 31.93 A C

ATOM 783 CD2 TYR A 134 49.601 38.821 30.009 1.00 30.38 A C

ATOM 784 CE2 TYR A 134 49.700 37.420 29.971 1.00 29.91 A C

ATOM 785 CZ TYR A 134 48.772 36.684 29.244 1.00 31.78 A C

ATOM 786 OH TYR A 134 48.822 35.292 29.205 1.00 33.71 A O

ATOM 787 C TYR A 134 47.341 40.762 31.568 1.00 30.92 A C

ATOM 788 0 TYR A 134 48.216 41.144 32.327 1.00 31.99 A O

ATOM 789 N VAL A 135 46.422 39.834 31.869 1.00 31.34 A N

ATOM 790 CA VAL A 135 46.398 39.059 33.124 1.00 30.12 A C

ATOM 791 CB VAL A 135 45.112 39.323 33.925 1.00 30.41 A C

ATOM 792 CGI VAL A 135 45.351 39.049 35.420 1.00 28.09 A C

ATOM 793 CG2 VAL A 135 44.669 40.751 33.721 1.00 31.27 A C

ATOM 794 C VAL A 135 46.492 37.574 32.693 1.00 30.65 A C

ATOM 795 O VAL A 135 45.562 37.027 32.082 1.00 31.35 A O

ATOM 796 N PRO A 136 47.600 36.897 33.069 1.00 28.98 A N

ATOM 797 CD PRO A 136 48.526 37.489 34.052 1.00 27.15 A C

ATOM 798 CA PRO A 136 47.975 35.504 32.784 1.00 29.38 A C

ATOM 799 CB PRO A 136 49.385 35.410 33.369 1.00 28.43 A C ATOM 800 CG PRO A 136 49.336 36.301 34.517 1.00 27.21 A C

ATOM 801 C PRO A 136 47.095 34.285 33.154 1.00 30.94 A C

ATOM 802 O PRO A 136 47.037 33.303 32.384 1.00 32.42 A O

ATOM 803 N GLU A 137 46.396 34.352 34.290 1.00 28.86 A N

ATOM 804 CA GLU A 137 45.546 33.246 34.733 1.00 26.99 A C

ATOM 805 CB GLU A 137 46.230 32.476 35.884 1.00 24.62 A C

ATOM 806 CG GLU A 137 47.481 31.679 35.488 1.00 25.11 A C

ATOM 807 CD GLU A 137 47.174 30.425 34.642 1.00 28.61 A C

ATOM 808 OE1 GLU A 137 45.979 30.104 34.459 1.00 27.71 A O

ATOM 809 OE2 GLU A 137 48.131 29.754 34.161 1.00 32.05 A O

ATOM 810 C GLU A 137 44.140 33.691 35.146 1.00 23.84 A C

ATOM 811 0 GLU A 137 43.799 34.858 35.041 1.00 26.68 A O

ATOM 812 N THR A 138 43.302 32.724 35.506 1.00 23.98 A N

ATOM 813 CA THR A 138 41.938 32.957 35.978 1.00 23.44 A C

ATOM 814 CB THR A 138 40.875 32.629 34.896 1.00 24.38 A C

ATOM 815 OG1 THR A 138 40.950 31.252 34.516 1.00 23.40 A O

ATOM 816 CG2 THR A 138 41.099 33.462 33.675 1.00 26.18 A C

ATOM 817 C THR A 138 41.718 32.021 37.178 1.00 25.19 A C

ATOM 818 0 THR A 138 42.396 31.008 37.315 1.00 25.00 A O

ATOM 819 N VAL A 139 40.833 32.402 38.090 1.00 26.96 A N

ATOM 820 CA VAL A 139 40.518 31.561 39.246 1.00 24.71 A C ATOM 821 CB VAL A 139 39.422 32.245 40.146 1.00 21.67 A C

ATOM 822 CGI VAL A 139 38.919 31.305 41.214 1.00 20.54 A C

ATOM 823 CG2 VAL A 139 40.030 33.498 40.829 1.00 19.99 A C

ATOM 824 C VAL A 139 40.098 30.183 38.684 1.00 25.77 A C

ATOM 825 O VAL A 139 40.489 29.144 39.190 1.00 26.29 A O

ATOM 826 N TYR A 140 39.427 30.175 37.543 1.00 27.74 A N

ATOM 827 CA TYR A 140 39.028 28.909 36.957 1.00 28.83 A C

ATOM 828 CB TYR A 140 38.306 29.128 35.631 1.00 31.23 A C

ATOM 829 CG TYR A 140 37.899 27.823 35.031 1.00 31.38 A C

ATOM 830 CDl TYR A 140 36.954 27.024 35.663 1.00 32.48 A C

ATOM 831 CE1 TYR A 140 36.668 25.776 35.204 1.00 35.51 A C

ATOM 832 CD2 TYR A 140 38.537 27.331 33.914 1.00 31.73 A C

ATOM 833 CE2 TYR A 140 38.261 26.086 33.443 1.00 34.86 A C

ATOM 834 CZ TYR A 140 37.328 25.299 34.095 1.00 37.26 A C

ATOM 835 OH TYR A 140 37.093 24.006 33.669 1.00 43.07 A O

ATOM 836 C TYR A 140 40.228 27.973 36.706 1.00 28.58 A C

ATOM 837 0 TYR A 140 40.276 26.861 37.220 1.00 27.27 A O

ATOM 838 N ARG A 141 41.175 28.425 35.884 1.00 29.70 A N

ATOM 839 CA ARG A 141 42.367 27.648 35.540 1.00 27.80 A C

ATOM 840 CB ARG A 141 43.222 28.402 34.526 1.00 29.79 A C

ATOM 841 CG ARG A 141 42.673 28.338 33.116 1.00 30.98 A C ATOM 842 CD ARG A 141 43.345 29.337 32.236 1.00 33.78 A C

ATOM 843 NE ARG A 141 44.790 29.177 32.242 1.00 37.91 A N

ATOM 844 CZ ARG A 141 45.495 28.771 31.191 1.00 42.94 A C

ATOM 845 NHl ARG A 141 44.881 28.476 30.052 1.00 45.84 A N

ATOM 846 NH2 ARG A 141 46.817 28.702 31.256 1.00 46.11 A N

ATOM 847 C ARG A 141 43.205 27.235 36.739 1.00 27.98 A C

ATOM 848 O ARG A 141 43.615 26.073 36.822 1.00 27.80 A O

ATOM 849 N VAL A 142 43.455 28.176 37.658 1.00 27.34 A N

ATOM 850 CA VAL A 142 44.233 27.900 38.883 1.00 28.31 A C

ATOM 851 CB VAL A 142 44.595 29.205 39.698 1.00 26.72 A C

ATOM 852 CGI VAL A 142 45.162 28.827 41.055 1.00 26.02 A C

ATOM 853 CG2 VAL A 142 45.638 30.038 38.951 1.00 22.80 A C

ATOM 854 C VAL A 142 43.493 26.897 39.788 1.00 27.97 A C

ATOM 855 O VAL A 142 44.088 25.962 40.302 1.00 29.73 A O

ATOM 856 N ALA A 143 42.184 27.065 39.919 1.00 28.69 A N

ATOM 857 CA ALA A 143 41.370 26.174 40.731 1.00 27.52 A C

ATOM 858 CB ALA A 143 39.959 26.713 40.859 1.00 27.01 A C

ATOM 859 C ALA A 143 41.357 24.772 40.134 1.00 29.06 A C

ATOM 860 O ALA A 143 41.314 23.795 40.884 1.00 28.56 A O

ATOM 861 N ARG A 144 41.396 24.689 38.798 1.00 27.51 A N

ATOM 862 CA ARG A 144 41.408 23.417 38.057 1.00 29.74 A C ATOM 863 CB ARG A 144 40.978 23.653 36.604 1.00 33.05 A C

ATOM 864 CG ARG A 144 41.024 22.468 35.654 1.00 35.25 A C

ATOM 865 CD ARG A 144 41.357 22.999 34.238 1.00 40.10 A C

ATOM 866 NE ARG A 144 40.302 22.802 33.234 1.00 44.51 A N

ATOM 867 CZ ARG A 144 40.257 23.422 32.046 1.00 46.13 A C

ATOM 868 NHl ARG A 144 41.208 24.299 31.706 1.00 44.86 A N

ATOM 869 NH2 ARG A 144 39.297 23.121 31.168 1.00 45.68 A N

ATOM 870 C ARG A 144 42.802 22.731 38.126 1.00 29.30 A C

ATOM 871 O ARG A 144 42.895 21.501 38.091 1.00 29.07 A O

ATOM 872 N HIS A 145 43.871 23.522 38.236 1.00 27.70 A N

ATOM 873 CA HIS A 145 45.218 22.971 38.376 1.00 28.20 A C

ATOM 874 CB HIS A 145 46.261 24.098 38.418 1.00 32.67 A C

ATOM 875 CG HIS A 145 47.614 23.658 38.894 1.00 37.97 A C

ATOM 876 CD2 HIS A 145 ' 48.718 23.254 38.209 1.00 38.19 A C

ATOM 877 ND1 HIS A 145 47.938 23.543 40.231 1.00 41.76 A N

ATOM 878 CE1 HIS A 145 49.172 23.082 40.354 1.00 40.83 A C

ATOM 879 NE2 HIS A 145 49.662 22.900 39.137 1.00 41.20 A N

ATOM 880 C HIS A 145 45.298 22.153 39.683 1.00 28.12 A C

ATOM 881 0 HIS A 145 45.862 21.069 39.731 1.00 29.84 A O

ATOM 882 N TYR A 146 44.752 22.706 40.750 1.00 24.78 A N

ATOM 883 CA TYR A 146 44.743 22.044 42.037 1.00 25.16 A C ATOM 884 CB TYR A 146 44.311 23.041 43.116 1.00 21.12 A C

ATOM 885 CG TYR A 146 45.452 23.906 43.527 1.00 20.16 A C

ATOM 886 CDl TYR A 146 45.651 25.156 42.954 1.00 18.74 A C

ATOM 887 CE1 TYR A 146 46.788 25.909 43.242 1.00 20.28 A C

ATOM 888 CD2 TYR A 146 46.410 23.430 44.409 1.00 22.97 A C

ATOM 889 CE2 TYR A 146 47.549 24.166 44.708 1.00 23.73 A C

ATOM 890 CZ TYR A 146 47.739 25.408 44.121 1.00 21.19 A C

ATOM 891 OH TYR A 146 48.889 26.129 44.408 1.00 25.87 A O

ATOM 892 C TYR A 146 43.819 20.850 41.998 1.00 27.00 A C

ATOM 893 O TYR A 146 44.177 19.779 42.449 1.00 29.00 A O

ATOM 894 N SER A 147 42.633 21.043 41.435 1.00 31.32 A N

ATOM 895 CA SER A 147 41.610 20.006 41.303 1.00 34.47 A C

ATOM 896 CB SER A 147 40.407 20.594 40.558 1.00 34.35 A C

ATOM 897 OG SER A 147 39.272 19.759 40.645 1.00 40.28 A O

ATOM 898 C SER A 147 42.134 18.754 40.561 1.00 36.70 A C

ATOM 899 0 SER A 147 41.869 17.618 40.973 1.00 36.08 A O

ATOM 900 N ARG A 148 42.867 18.961 39.468 1.00 37.11 A N

ATOM 901 CA ARG A 148 43.406 17.844 38.712 1.00 39.33 A C

ATOM 902 CB ARG A 148 43.914 18.314 37.350 1.00 41.05 A C

ATOM 903 CG ARG A 148 42.824 18.454 36.295 1.00 44.82 A C

ATOM 904 CD ARG A 148 43.416 18.854 34.952 1.00 47.26 A C ATOM 905 NE ARG A 148 42.377 19.097 33.957 1.00 51.12 A N

ATOM 906 CZ ARG A 148 42.412 20.078 33.055 1.00 53.10 A C

ATOM 907 NHl ARG A 148 43.444 20.918 33.019 1.00 53.33 A N

ATOM 908 NH2 ARG A 148 41.408 20.223 32.194 1.00 52.55 A N

ATOM 909 C ARG A 148 44.519 17.103 39.458 1.00 40.50 A C

ATOM 910 O ARG A 148 44.702 15.891 39.275 1.00 39.30 A O

ATOM 911 N ALA A 149 45.276 17.844 40.269 1.00 41.08 A N

ATOM 912 CA ALA A 149 46.379 17.280 41.046 1.00 39.72 A C

ATOM 913 CB ALA A 149 47.435 18.338 41.303 1.00 38.73 A C

ATOM 914 C ALA A 149 45.877 16.707 42.363 1.00 40.87 A C

ATOM 915 O ALA A 149 46.656 16.519 43.305 1.00 42.44 A O

ATOM 916 N LYS A 150 44.564 16.468 42.417 1.00 41.69 A N

ATOM 917 CA LYS A 150 43.867 15.919 43.582 1.00 41.88 A C

ATOM 918 CB LYS A 150 44.342 14.493 43.857 1.00 43.33 A C

ATOM 919 CG LYS A 150 44.012 13.514 42.721 1.00 45.60 A C

ATOM 920 CD LYS A 150 42.543 13.661 42.270 1.00 49.16 A C

ATOM 921 CE LYS A 150 41.523 13.401 43.398 1.00 48.64 A C

ATOM 922 NZ LYS A 150 40.187 14.027 43.117 1.00 47.59 A N

ATOM 923 C LYS A 150 43.874 16.752 44.866 1.00 42.31 A C

ATOM 924 0 LYS A 150 43.549 16.244 45.940 1.0042.11 A O

ATOM 925 N GLN A 151 44.201 18.038 44.740 1.00 41.75 A N ATOM 926 CA GLNA 151 44.244 18.95945.876 1.0040.32 A C

ATOM 927 CB GLNA 151 45.615 19.625 45.985 1.0041.69 A C

ATOM 928 CG GLNA 151 46.766 18.67645.761 1.0045.57 A C

ATOM 929 CD GLNA 151 48.064 19.39745.444 1.0047.43 A C

ATOM 930 OE1 GLNA 151 48.818 18.98944.551 1.0048.65 A O

ATOM 931 NE2 GLNA 151 48.333 20.47546.178 1.0047.43 A N

ATOM 932 C GLNA 151 43.17720.04845.756 1.0038.97 A C

ATOM 933 O GLNA 151 42.48620.19344.737 1.0037.05 A O

ATOM 934 N THR A 152 43.07820.833 46.817 1.0036.12 A N

ATOM 935 CA THRA152 42.12021.911 46.887 1.0030.43 A C

ATOM 936 CB THR A 152 41.16021.62748.098 1.0032.05 A C

ATOM 937 OG1 THR A 152 40.08422.56748.118 1.0034.33 A O

ATOM 938 CG2THRA152 41.93021.59649.441 1.0025.51 A C

ATOM 939 C THR A 152 42.99823.17347.031 1.0029.40 A C

ATOM 940 O THR A 152 44.15023.08247.451 1.0029.65 A O

ATOM 941 N LEU A 153 42.52224.31346.545 1.0026.53 A N

ATOM 942 CA LEU A 153 43.28325.55246.649 1.0024.95 A C

ATOM 943 CB LEU A 153 42.50726.68845.954 1.0026.82 A C

ATOM 944 CG LEU A 153 43.12028.061 45.618 1.0025.65 A C

ATOM 945 CDl LEU A 153 44.23627.921 44.557 1.0025.60 A C

ATOM 946 CD2LEUA153 42.01729.00645.115 1.0024.41 A C ATOM 947 C LEU A 153 43.510 25.890 48.130 1.00 24.38 A C

ATOM 948 0 LEU A 153 42.570 25.885 48.921 1.00 23.56 A O

ATOM 949 N PRO A 154 44.774 26.158 48.527 1.00 26.09 A N

ATOM 950 CD PRO A 154 46.020 26.126 47.731 1.00 24.06 A C

ATOM 951 CA PRO A 154 45.063 26.493 49.929 1.00 24.19 A C

ATOM 952 CB PRO A 154 46.526 26.914 49.894 1.00 24.86 A C

ATOM 953 CG PRO A 154 47.081 26.048 48.822 1.00 25.37 A C

ATOM 954 C PRO A 154 44.176 27.629 50.385 1.00 27.34 A C

ATOM 955 0 PRO A 154 43.904 28.554 49.615 1.00 30.70 A O

ATOM 956 N VAL A 155 43.729 27.551 51.636 1.00 26.02 A N

ATOM 957 CA VAL A 155 42.847 28.544 52.200 1.00 26.41 A C

ATOM 958 CB VAL A 155 42.546 28.252 53.648 1.00 26.31 A C

ATOM 959 CGI VAL A 155 41.260 28.980 54.060 1.00 27.04 A C

ATOM 960 CG2 VAL A 155 42.423 26.771 53.829 1.00 28.43 A C

ATOM 961 C VAL A 155 43.344 29.969 52.065 1.00 26.71 A C

ATOM 962 0 VAL A 155 42.533 30.879 51.874 1.00 29.38 A O

ATOM 963 N ILE A 156 44.660 30.170 52.136 1.00 25.06 A N

ATOM 964 CA ILE A 156 45.215 31.515 52.001 1.00 23.58 A C

ATOM 965 CB ILE A 156 46.733 31.532 52.236 1.00 22.58 A C

ATOM 966 CG2 ILE A 156 47.440 30.804 51.121 1.00 22.74 A C

ATOM 967 CGI ILE A 156 47.222 32.971 52.397 1.00 23.47 A C ATOM 968 CDl ILE A 156 46.427 33.793 53.445 1.00 24.69 A C

ATOM 969 C ILE A 156 44.856 32.150 50.642 1.00 22.60 A C

ATOM 970 O ILE A 156 44.598 33.344 50.569 1.00 21.23 A O

ATOM 971 N TYR A 157 44.779 31.341 49.587 1.00 21.96 A N

ATOM 972 CA TYR A 157 44.421 31.854 48.266 1.00 21.89 A C

ATOM 973 CB TYR A 157 44.919 30.929 47.142 1.00 24.47 A C

ATOM 974 CG TYR A 157 46.425 30.911 46.981 1.00 29.69 A C

ATOM 975 CDl TYR A 157 47.139 29.723 47.061 1.00 31.71 A C

ATOM 976 CE1 TYR A 157 48.527 29.704 46.968 1.00 32.61 A C

ATOM 977 CD2 TYR A 157 47.137 32.088 46.792 1.00 30.79 A C

ATOM 978 CE2 TYR A 157 48.525 32.085 46.697 1.00 33.89 A C

ATOM 979 CZ TYR A 157 49.221 30.887 46.790 1.00 34.85 A C

ATOM 980 OH TYR A 157 50.608 30.887 46.750 1.00 36.72 A O

ATOM 981 C TYR A 157 42.914 32.043 48.174 1.00 21.57 A C

ATOM 982 0 TYR A 157 42.426 32.935 47.481 1.00 20.67 A O

ATOM 983 N VAL A 158 42.166 31.182 48.849 1.00 22.66 A N

ATOM 984 CA VAL A 158 40.708 31.313 48.826 1.00 21.35 A C

ATOM 985 CB VAL A 158 39.970 30.100 49.543 1.00 17.78 A C

ATOM 986 CGI VAL A 158 38.514 30.422 49.774 1.00 14.58 A C

ATOM 987 CG2 VAL A 158 40.067 28.818 48.712 1.00 14.89 A C

ATOM 988 C VAL A 158 40.375 32.648 49.495 1.00 22.61 A C ATOM 989 O VAL A 158 39.525 33.393 49.009 1.00 27.34 A O

ATOM 990 N LYS A 159 41.057 32.961 50.599 1.00 20.08 A N

ATOM 991 CA LYS A 159 40.823 34.228 51.291 1.00 18.19 A C

ATOM 992 CB LYS A 159 41.669 34.295 52.575 1.00 18.97 A C

ATOM 993 CG LYS A 159 41.241 33.346 53.655 1.00 17.13 A C

ATOM 994 CD LYS A 159 42.174 33.347 54.851 1.00 17.71 A C

ATOM 995 CE LYS A 159 41.796 32.245 55.871 1.00 15.78 A C

ATOM 996 NZ LYS A 159 42.733 32.136 57.037 1.00 17.90 A N

ATOM 997 C LYS A 159 41.186 35.395 50.351 1.00 18.53 A C

ATOM 998 0 LYS A 159 40.364 36.256 50.041 1.00 19.01 A O

ATOM 999 N LEU A 160 42.413 35.367 49.852 1.00 20.41 A N

ATOM 1000 CA LEU A 160 42.911 36.392 48.953 1.00 22.14 A C

ATOM 1001 CB LEU A 160 44.369 36.101 48.590 1.00 24.48 A C

ATOM 1002 CG LEU A 160 45.432 36.386 49.659 1.00 25.34 A C

ATOM 1003 CDl LEU A 160 46.664 35.516 49.430 1.00 27.51 A C

ATOM 1004 CD2 LEU A 160 45.773 37.893 49.668 1.00 26.79 A C

ATOM 1005 C LEU A 160 42.093 36.623 47.684 1.00 21.83 A C

ATOM 1006 O LEU A 160 41.830 37.768 47.338 1.00 24.16 A O

ATOM 1007 N TYR A 161 41.703 35.555 46.978 1.00 21.65 A N

ATOM 1008 CA TYR A 161 40.911 35.689 45.740 1.00 18.41 A C

ATOM 1009 CB TYR A 161 40.875 34.353 44.965 1.00 20.20 A C ATOM 1010 CG TYR A 161 42.259 33.836 44.550 1.00 24.61 A C

ATOM 1011 CDl TYR A 161 43.403 34.613 44.726 1.00 23.78 A C

ATOM 1012 CE1 TYR A 161 44.665 34.159 44.321 1.00 26.70 A C

ATOM 1013 CD2 TYR A 161 42.416 32.572 43.952 1.00 25.92 A C

ATOM 1014 CE2 TYR A 161 43.671 32.109 43.541 1.00 27.86 A C

ATOM 1015 CZ TYR A 161 44.801 32.910 43.727 1.00 29.25 A C

ATOM 1016 OH TYR A 161 46.070 32.470 43.314 1.00 34.56 A O

ATOM 1017 C TYR A 161 39.499 36.171 46.061 1.00 16.19 A C

ATOM 1018 O TYR A 161 38.999 37.121 45.477 1.00 11.97 A O

ATOM 1019 N MET A 162 38.883 35.552 47.055 1.00 16.43 A N

ATOM 1020 CA MET A 162 37.543 35.938 47.444 1.00 19.11 A C

ATOM 1021 CB MET A 162 36.992 34.972 48.506 1.00 20.40 A C

ATOM 1022 CG MET A 162 36.446 33.660 47.954 1.00 21.64 A C

ATOM 1023 SD MET A 162 35.135 33.905 46.727 1.00 25.37 A S

ATOM 1024 CE MET A 162 36.064 33.640 45.329 1.00 23.88 A C

ATOM 1025 C MET A 162 37.484 37.363 47.973 1.00 22.02 A C

ATOM 1026 O MET A 162 36.556 38.108 47.666 1.00 24.37 A O

ATOM 1027 N TYR A 163 38.455 37.737 48.801 1.00 23.77 A N

ATOM 1028 CA TYR A 163 38.479 39.088 49.367 1.00 22.41 A C

ATOM 1029 CB TYR A 163 39.664 39.242 50.306 1.00 22.27 A C

ATOM 1030 CG TYR A 163 39.826 40.634 50.856 1.00 22.47 A C ATOM 1031 CDl TYR A 163 39.240 40.997 52.058 1.00 21.90 A C

ATOM 1032 CE1 TYR A 163 39.398 42.269 52.564 1.00 23.96 A C

ATOM 1033 CD2 TYR A 163 40.572 41.581 50.174 1.00 22.00 A C

ATOM 1034 CE2 TYR A 163 40.736 42.851 50.664 1.00 23.66 A C

ATOM 1035 CZ TYR A 163 40.154 43.197 51.862 1.00 23.14 A C

ATOM 1036 OH TYR A 163 40.384 44.450 52.395 1.00 27.41 A O

ATOM 1037 C TYR A 163 38.519 40.180 48.279 1.00 21.87 A C

ATOM 1038 O TYR A 163 37.752 41.138 48.319 1.00 20.75 A O

ATOM 1039 N GLN A 164 39.413 40.006 47.310 1.00 20.19 A N

ATOM 1040 CA GLN A 164 39.570 40.929 46.213 1.00 18.36 A C

ATOM 1041 CB GLN A 164 40.806 40.555 45.416 1.00 17.98 A C

ATOM 1042 CG GLN A 164 42.077 40.776 46.177 1.00 19.68 A C

ATOM 1043 CD GLN A 164 43.305 40.305 45.441 1.00 24.12 A C

ATOM 1044 OE1 GLN A 164 43.826 41.002 44.568 1.00 26.81 A O

ATOM 1045 NE2 GLN A 164 43.797 39.131 45.805 1.00 24.95 A N

ATOM 1046 C GLN A 164 38.359 40.898 45.306 1.00 21.03 A C

ATOM 1047 O GLN A 164 38.088 41.864 44.594 1.00 22.49 A O

ATOM 1048 N LEU A 165 37.662 39.763 45.270 1.00 25.43 A N

ATOM 1049 CA LEU A 165 36.458 39.626 44.433 1.00 24.56 A C

ATOM 1050 CB LEU A 165 35.952 38.181 44.448 1.00 26.41 A C

ATOM 1051 CG LEU A 165 34.899 37.750 43.422 1.00 27.21 A C ATOM 1052 CDl LEU A 165 33.808 36.930 44.087 1.00 26.04 A C

ATOM 1053 CD2 LEU A 165 34.337 38.949 42.683 1.00 26.49 A C

ATOM 1054 C LEU A 165 35.397 40.545 45.018 1.00 25.10 A C

ATOM 1055 O LEU A 165 34.775 41.331 44.300 1.00 24.18 A O

ATOM 1056 N PHE A 166 35.210 40.456 46.333 1.00 25.76 A N

ATOM 1057 CA PHE A 166 34.240 41.308 47.016 1.00 27.18 A C

ATOM 1058 CB PHE A 166 34.065 40.879 48.460 1.00 25.41 A C

ATOM 1059 CG PHE A 166 33.331 39.584 48.610 1.00 25.89 A C

ATOM 1060 CDl PHE A 166 33.975 38.456 49.095 1.00 25.44 A C

ATOM 1061 CD2 PHE A 166 31.990 39.497 48.264 1.00 23.82 A C

ATOM 1062 CE1 PHE A 166 33.290 37.257 49.233 1.00 27.27 A C

ATOM 1063 CE2 PHE A 166 31.292 38.305 48.395 1.00 23.99 A C

ATOM 1064 CZ PHE A 166 31.939 37.180 48.881 1.00 24.37 A C

ATOM 1065 C PHE A 166 34.577 42.795 46.924 1.00 28.83 A C

ATOM 1066 O PHE A 166 33.674 43.600 46.712 1.00 32.98 A O

ATOM 1067 N ARG A 167 35.860 43.157 47.028 1.00 29.02 A N

ATOM 1068 CA ARG A 167 36.280 44.561 46.926 1.00 29.11 A C

ATOM 1069 CB ARG A 167 37.803 44.717 46.987 1.00 29.85 A C

ATOM 1070 CG ARG A 167 38.357 45.047 48.345 1.00 33.71 A C

ATOM 1071 CD ARG A 167 39.821 45.452 48.240 1.00 35.16 A C

ATOM 1072 NE ARG A 167 40.000 46.716 47.523 1.00 36.03 A N ATOM 1073 CZ ARG A 167 41.112 47.438 47.577 1.00 32.13 A C

ATOM 1074 NHl ARG A 167 42.121 47.012 48.315 1.00 33.00 A N

ATOM 1075 NH2 ARG A 167 41.219 48.565 46.891 1.00 32.45 A N

ATOM 1076 C ARG A 167 35.836 45.119 45.602 1.00 27.36 A C

ATOM 1077 O ARG A 167 35.350 46.249 45.512 1.00 28.57 A O

ATOM 1078 N SER A 168 36.047 44.325 44.564 1.00 25.95 A N

ATOM 1079 CA SER A 168 35.688 44.746 43.227 1.00 25.72 A C

ATOM 1080 CB SER A 168 36.237 43.771 42.162 1.00 24.35 A C

ATOM 1081 OG SER A 168 35.622 42.502 42.228 1.00 24.26 A O

ATOM 1082 C SER A 168 34.178 44.879 43.151 1.00 24.47 A C

ATOM 1083 O SER A 168 33.682 45.802 42.532 1.00 24.30 A O

ATOM 1084 N LEU A 169 33.456 43.990 43.824 1.00 23.95 A N

ATOM 1085 CA LEU A 169 32.000 44.049 43.801 1.00 24.98 A C

ATOM 1086 CB LEU A 169 31.359 42.796 44.415 1.00 24.67 A C

ATOM 1087 CG LEU A 169 31.312 41.496 43.604 1.00 22.03 A C

ATOM 1088 CDl LEU A 169 30.369 40.533 44.259 1.00 21.18 A C

ATOM 1089 CD2 LEU A 169 30.866 41.789 42.177 1.00 23.84 A C

ATOM 1090 C LEU A 169 31.517 45.281 44.544 1.00 27.72 A C

ATOM 1091 O LEU A 169 30.616 45.970 44.079 1.00 29.52 A O

ATOM 1092 N ALA A 170 32.101 45.538 45.709 1.00 28.15 A N

ATOM 1093 CA ALA A 170 31.728 46.680 46.526 1.00 27.37 A C ATOM 1094 CB ALA A 170 32.653 46.773 47.722 1.00 24.60 A C

ATOM 1095 C ALA A 170 31.836 47.945 45.701 1.00 29.32 A C

ATOM 1096 O ALA A 170 30.975 48.813 45.751 1.00 31.35 A O

ATOM 1097 N TYR A 171 32.878 48.012 44.892 1.00 31.67 A N

ATOM 1098 CA TYR A 171 33.153 49.182 44.071 1.00 34.20 A C

ATOM 1099 CB TYR A 171 34.594 49.125 43.519 1.00 35.01 A C

ATOM 1100 CG TYR A 171 34.932 50.153 42.440 1.00 36.05 A C

ATOM 1101 CDl TYR A 171 35.165 51.491 42.757 1.00 36.55 A C

ATOM 1102 CE1 TYR A 171 35.485 52.426 41.759 1.00 34.98 A C

ATOM 1103 CD2 TYR A 171 35.032 49.775 41.102 1.00 35.50 A C

ATOM 1104 CE2 TYR A 171 35.349 50.693 40.109 1.00 35.45 A C

ATOM 1105 CZ TYR A 171 35.575 52.019 40.437 1.00 35.83 A C

ATOM 1106 OH TYR A 171 35.878 52.931 39.436 1.00 33.90 A O

ATOM 1107 C TYR A 171 32.157 49.413 42.955 1.00 34.90 A C

ATOM 1108 O TYR A 171 31.845 50.556 42.637 1.00 36.36 A O

ATOM 1109 N ILE A 172 31.685 48.350 42.316 1.00 35.15 A N

ATOM 1110 CA ILE A 172 30.728 48.535 41.241 1.00 32.43 A C

ATOM 1111 CB ILE A 172 30.716 47.354 40.208 1.00 32.82 A C

ATOM 1112 CG2 ILE A 172 32.008 47.363 39.367 1.00 30.44 A C

ATOM 1113 CGI ILE A 172 30.473 46.003 40.889 1.00 30.73 A C

ATOM 1114 CDl ILE A 172 30.186 44.906 39.907 1.00 28.01 A C ATOM 1115 C ILE A 172 29.355 48.756 41.850 1.00 33.06 A C

ATOM 1116 0 ILE A 172 28.649 49.665 41.462 1.00 33.78 A O

ATOM 1117 N HIS A 173 28.994 47.956 42.838 1.00 33.57 A N

ATOM 1118 CA HIS A 173 27.705 48.119 43.482 1.00 38.13 A C

ATOM 1119 CB HIS A 173 27.489 47.057 44.561 1.00 38.21 A C

ATOM 1120 CG HIS A 173 27.453 45.662 44.034 1.00 37.10 A C

ATOM 1121 CD2 HIS A 173 27.645 45.174 42.787 1.00 36.51 A C

ATOM 1122 ND1 HIS A 173 27.175 44.579 44.841 1.00 35.25 A N

ATOM 1123 CE1 HIS A 173 27.197 43.480 44.107 1.00 37.48 A C

ATOM 1124 NE2 HIS A 173 27.479 43.809 42.858 1.00 35.95 A N

ATOM 1125 C HIS A 173 27.550 49.497 44.133 1.00 42.62 A C

ATOM 1126 0 HIS A 173 26.461 49.832 44.618 1.00 46.29 A O

ATOM 1127 N SER A 174 28.636 50.267 44.223 1.00 44.10 A N

ATOM 1128 CA SER A 174 28.550 51.606 44.818 1.00 45.16 A C

ATOM 1129 CB SER A 174 29.861 52.006 45.516 1.00 42.98 A C

ATOM 1130 OG SER A 174 30.862 52.381 44.585 1.00 40.08 A O

ATOM 1131 C SER A 174 28.161 52.621 43.721 1.00 46.86 A C

ATOM 1132 O SER A 174 27.863 53.784 44.006 1.00 49.12 A O

ATOM 1133 N PHE A 175 28.185 52.162 42.469 1.00 47.61 A N

ATOM 1134 CA PHE A 175 27.799 52.958 41.302 1.00 49.07 A C

ATOM 1135 CB PHE A 175 28.778 52.766 40.152 1.00 51.72 A C ATOM 1136 CG PHE A 175 29.980 53.625 40.233 1.00 56.04 A C

ATOM 1137 CDl PHE A 175 31.088 53.345 39.440 1.00 57.99 A C

ATOM 1138 CD2 PHE A 175 30.007 54.728 41.088 1.00 57.69 A C

ATOM 1139 CE1 PHE A 175 32.214 54.157 39.488 1.00 60.19 A C

ATOM 1140 CE2 PHE A 175 31.124 55.555 41.153 1.00 58.16 A C

ATOM 1141 CZ PHE A 175 32.233 55.271 40.354 1.00 60.56 A C

ATOM 1142 C PHE A 175 26.452 52.421 40.838 1.00 49.69 A C

ATOM 1143 O PHE A 175 25.915 52.867 39.816 1.00 50.31 A O

ATOM 1144 N GLY A 176 25.931 51.445 41.590 1.00 49.12 A N

ATOM 1145 CA GLY A 176 24.669 50.806 41.259 1.00 46.45 A C

ATOM 1146 C GLY A 176 24.842 49.799 40.128 1.00 44.90 A C

ATOM 1147 O GLY A 176 23.853 49.326 39.566 1.00 45.37 A O

ATOM 1148 N ILE A 177 26.098 49.489 39.780 1.00 41.77 A N

ATOM 1149 CA ILE A 177 26.406 48.534 38.707 1.00 39.39 A C

ATOM 1150 CB ILE A 177 27.753 48.873 37.983 1.00 36.54 A C

ATOM 1151 CG2 ILE A 177 27.969 47.936 36.789 1.00 38.95 A C

ATOM 1152 CGI ILE A 177 27.713 50.309 37.448 1.00 36.23 A C

ATOM 1153 CDl ILE A 177 28.870 50.689 36.531 1.00 34.19 A C

ATOM 1154 C ILE A 177 26.387 47.055 39.153 1.00 37.59 A C

ATOM 1155 O ILE A 177 26.849 46.708 40.234 1.00 36.47 A O

ATOM 1156 N CYS A 178 25.774 46.209 38.333 1.00 36.06 A N ATOM 1157 CA CYS A 178 25.668 44.787 38.623 1.00 35.83 A C

ATOM 1158 CB CYS A 178 24.207 44.366 38.636 1.00 36.65 A C

ATOM 1159 SG CYS A 178 23.933 42.728 39.283 1.00 41.98 A S

ATOM 1160 C CYS A 178 26.404 44.054 37.514 1.00 36.68 A C

ATOM 1161 O CYS A 178 26.168 44.312 36.318 1.00 36.59 A O

ATOM 1162 N HIS A 179 27.314 43.163 37.908 1.00 35.03 A N

ATOM 1163 CA HIS A 179 28.114 42.423 36.942 1.00 33.21 A C

ATOM 1164 CB HIS A 179 29.282 41.716 37.644 1.00 32.61 A C

ATOM 1165 CG HIS A 179 30.272 41.119 36.700 1.00 30.80 A C

ATOM 1166 CD2 HIS A 179 31.376 41.643 36.113 1.00 31.78 A C

ATOM 1167 ND1 HIS A 179 30.160 39.835 36.218 1.00 30.90 A N

ATOM 1168 CE1 HIS A 179 31.148 39.593 35.374 1.00 30.00 A C

ATOM 1169 NE2 HIS A 179 31.900 40.675 35.296 1.00 29.07 A N

ATOM 1170 C HIS A 179 27.256 41.429 36.180 1.00 33.40 A C

ATOM 1171 0 HIS A 179 27.333 41.347 34.952 1.00 32.87 A O

ATOM 1172 N ARG A 180 26.455 40.673 36.933 1.00 34.70 A N

ATOM 1173 CA ARG A 180 25.519 39.664 36.405 1.00 34.36 A C

ATOM 1174 CB ARG A 180 24.431 40.330 35.537 1.00 32.84 A C

ATOM 1175 CG ARG A 180 23.661 41.435 36.265 1.00 33.19 A C

ATOM 1176 CD ARG A 180 22.369 41.788 35.554 1.00 35.01 A C

ATOM 1177 NE ARG A 180 22.531 42.077 34.120 1.00 37.70 A N ATOM 1178 CZ ARG A 180 21.535 42.466 33.312 1.00 36.42 A C

ATOM 1179 NHl ARG A 180 20.308 42.633 33.793 1.00 31.94 A N

ATOM 1180 NH2 ARG A 180 21.745 42.601 32.005 1.00 34.86 A N

ATOM 1181 C ARG A 180 26.093 38.440 35.691 1.00 33.32 A C

ATOM 1182 O ARG A 180 25.373 37.759 34.970 1.00 35.45 A O

ATOM 1183 N ASP A 181 27.373 38.145 35.913 1.00 31.42 A N

ATOM 1184 CA ASP A 181 28.029 36.993 35.286 1.00 28.48 A C

ATOM 1185 CB ASP A 181 28.402 37.318 33.837 1.00 29.60 A C

ATOM 1186 CG ASP A 181 28.786 36.086 33.050 1.00 31.80 A C

ATOM 1187 OD1 ASP A 181 28.451 34.977 33.518 1.00 30.23 A O

ATOM 1188 OD2 ASP A 181 29.419 36.230 31.973 1.00 34.83 A O

ATOM 1189 C ASP A 181 29.272 36.603 36.091 1.00 27.54 A C

ATOM 1190 O ASP A 181 30.349 36.324 35.551 1.00 24.95 A O

ATOM 1191 N ILE A 182 29.118 36.639 37.404 1.00 24.85 A N

ATOM 1192 CA ILE A 182 30.206 36.299 38.289 1.0026.96 A C

ATOM 1193 CB ILE A 182 29.945 36.849 39.728 1.00 25.13 A C

ATOM 1194 CG2 ILE A 182 30.890 36.205 40.718 1.00 23.49 A C

ATOM 1195 CGI ILE A 182 30.038 38.392 39.737 1.00 25.25 A C

ATOM 1196 CDl ILE A 182 31.359 38.950 39.271 1.00 26.54 A C

ATOM 1197 C ILE A 182 30.472 34.788 38.306 1.00 26.98 A C

ATOM 1198 0 ILE A 182 29.604 33.999 38.681 1.00 27.37 A O ATOM 1199 N LYS A 183 31.657 34.411 37.825 1.00 26.70 A N

ATOM 1200 CA LYS A 183 32.112 33.021 37.768 1.00 26.63 A C

ATOM 1201 CB LYS A 183 31.493 32.265 36.568 1.00 24.83 A C

ATOM 1202 CG LYS A 183 31.887 32.781 35.199 1.00 24.93 A C

ATOM 1203 CD LYS A 183 31.170 32.010 34.116 1.00 28.93 A C

ATOM 1204 CE LYS A 183 31.310 32.670 32.752 1.00 33.05 A C

ATOM 1205 NZ LYS A 183 30.929 31.747 31.630 1.00 36.58 A N

ATOM 1206 C LYS A 183 33.647 33.027 37.692 1.00 26.01 A C

ATOM 1207 O LYS A 183 34.261 34.044 37.378 1.00 26.68 A O

ATOM 1208 N PRO A 184 34.286 31.890 38.014 1.00 25.65 A N

ATOM 1209 CD PRO A 184 33.653 30.627 38.426 1.00 25.23 A C

ATOM 1210 CA PRO A 184 35.744 31.746 37.995 1.00 22.74 A C

ATOM 1211 CB PRO A 184 35.937 30.257 38.256 1.00 23.88 A C

ATOM 1212 CG PRO A 184 34.800 29.930 39.141 1.00 23.86 A C

ATOM 1213 C PRO A 184 36.406 32.163 36.687 1.00 21.53 A C

ATOM 1214 O PRO A 184 37.461 32.764 36.698 1.00 21.96 A O

ATOM 1215 N GLN A 185 35.795 31.827 35.565 1.00 22.84 A N

ATOM 1216 CA GLN A 185 36.357 32.169 34.254 1.00 23.03 A C

ATOM 1217 CB GLN A 185 35.533 31.525 33.146 1.00 24.06 A C

ATOM 1218 CG GLN A 185 35.478 30.000 33.203 1.00 28.72 A C

ATOM 1219 CD GLN A 185 34.367 29.454 34.106 1.00 32.32 A C ATOM 1220 OE1 GLN A 185 33.912 30.120 35.042 1.00 36.77 A O

ATOM 1221 NE2 GLN A 185 33.926 28.233 33.819 1.00 34.64 A N

ATOM 1222 C GLN A 185 36.437 33.666 34.024 1.00 22.17 A C

ATOM 1223 O GLN A 185 37.173 34.132 33.163 1.00 22.19 A O

ATOM 1224 N ASN A 186 35.629 34.417 34.760 1.00 23.70 A N

ATOM 1225 CA ASN A 186 35.619 35.876 34.650 1.00 24.35 A C

ATOM 1226 CB ASN A 186 34.214 36.432 34.774 1.00 24.49 A C

ATOM 1227 CG ASN A 186 33.387 36.159 33.570 1.00 27.41 A C

ATOM 1228 OD1 ASN A 186 33.912 36.066 32.439 1.00 27.69 A O

ATOM 1229 ND2 ASN A 186 32.079 36.000 33.785 1.00 24.24 A N

ATOM 1230 C ASN A 186 36.464 36.573 35.699 1.00 26.47 A C

ATOM 1231 O ASN A 186 36.426 37.802 35.795 1.00 28.78 A O

ATOM 1232 N LEU A 187 37.170 35.794 36.520 1.00 25.93 A N

ATOM 1233 CA LEU A 187 38.037 36.335 37.563 1.00 24.39 A C

ATOM 1234 CB LEU A 187 37.769 35.647 38.903 1.00 21.68 A C

ATOM 1235 CG LEU A 187 36.292 35.588 39.348 1.00 21.52 A C

ATOM 1236 CDl LEU A 187 36.179 34.855 40.652 1.00 16.97 A C

ATOM 1237 CD2 LEU A 187 35.731 36.965 39.539 1.00 18.81 A C

ATOM 1238 C LEU A 187 39.477 36.116 37.115 1.00 25.35 A C

ATOM 1239 O LEU A 187 39.991 35.005 37.147 1.00 25.06 A O

ATOM 1240 N LEU A 188 40.082 37.177 36.592 1.00 26.51 A N ATOM 1241 CA LEU A 188 41.450 37.119 36.114 1.00 23.80 A C

ATOM 1242 CB LEU A 188 41.766 38.324 35.222 1.00 24.03 A C

ATOM 1243 CG LEU A 188 40.899 38.449 33.971 1.00 18.91 A C

ATOM 1244 CDl LEU A 188 41.491 39.559 33.136 1.00 20.30 A C

ATOM 1245 CD2 LEU A 188 40.853 37.132 33.180 1.00 19.91 A C

ATOM 1246 C LEU A 188 42.382 37.041 37.306 1.00 24.18 A C

ATOM 1247 O LEU A 188 42.041 37.493 38.390 1.00 21.55 A O

ATOM 1248 N LEU A 189 43.604 36.589 37.070 1.00 26.20 A N

ATOM 1249 CA LEU A 189 44.519 36.393 38.157 1.00 27.92 A C

ATOM 1250 CB LEU A 189 44.140 35.039 38.740 1.00 29.84 A C

ATOM 1251 CG LEU A 189 44.250 34.680 40.198 1.00 32.69 A C

ATOM 1252 CDl LEU A 189 43.640 33.305 40.374 1.00 33.69 A C

ATOM 1253 CD2 LEU A 189 45.706 34.684 40.610 1.00 37.86 A C

ATOM 1254 C LEU A 189 46.004 36.379 37.756 1.00 28.63 A C

ATOM 1255 0 LEU A 189 46.377 35.849 36.717 1.00 27.82 A O

ATOM 1256 N ASP A 190 46.836 36.987 38.597 1.00 30.40 A N

ATOM 1257 CA ASP A 190 48.285 36.992 38.420 1.00 32.67 A C

ATOM 1258 CB ASP A 190 48.843 38.419 38.519 1.00 33.70 A C

ATOM 1259 CG ASP A 190 50.371 38.482 38.373 1.00 34.20 A C

ATOM 1260 OD1 ASP A 190 50.927 39.565 38.599 1.00 36.02 A O

ATOM 1261 OD2 ASP A 190 51.021 37.472 38.045 1.00 35.65 A O ATOM 1262 C ASP A 190 48.757 36.117 39.594 1.00 31.59 A C

ATOM 1263 0 ASP A 190 48.814 36.562 40.727 1.00 33.25 A O

ATOM 1264 N PRO A 191 49.092 34.850 39.326 1.00 32.88 A N

ATOM 1265 CD PRO A 191 49.230 34.236 37.993 1.0Q 31.26 A C

ATOM 1266 CA PRO A 191 49.537 33.928 40.374 1.00 33.35 A C

ATOM 1267 CB PRO A 191 49.774 32.636 39.601 1.00 32.59 A C

ATOM 1268 CG PRO A 191 50.214 33.140 38.252 1.00 32.61 A C

ATOM 1269 C PRO A 191 50.736 34.317 41.250 1.00 35.09 A C

ATOM 1270 O PRO A 191 50.793 33.909 42.420 1.00 36.26 A O

ATOM 1271 N ASP A 192 51.681 35.079 40.692 1.00 35.22 A N

ATOM 1272 CA ASP A 192 52.884 35.510 41.414 1.00 37.07 A C

ATOM 1273 CB ASP A 192 53.900 36.153 40.470 1.00 40.26 A C

ATOM 1274 CG ASP A 192 54.673 35.151 39.641 1.00 40.42 A C

ATOM 1275 OD1 ASP A 192 54.441 33.930 39.776 1.00 37.69 A O

ATOM 1276 OD2 ASP A 192 55.527 35.614 38.851 1.00 41.42 A O

ATOM 1277 C ASP A 192 52.576 36.545 42.478 1.00 38.30 A C

ATOM 1278 0 ASP A 192 53.160 36.515 43.566 1.00 41.04 A O

ATOM 1279 N THR A 193 51.721 37.508 42.129 1.00 37.07 A N

ATOM 1280 CA THR A 193 51.348 38.574 43.055 1.00 34.71 A C

ATOM 1281 CB THR A 193 51.306 39.942 42.337 1.00 32.86 A C

ATOM 1282 OG1 THR A 193 50.274 39.945 41.353 1.00 30.96 A O ATOM 1283 CG2 THR A 193 52.620 40.173 41.630 1.00 31.06 A C

ATOM 1284 C THR A 193 50.035 38.296 43.776 1.00 33.51 A C

ATOM 1285 O THR A 193 49.732 38.922 44.792 1.00 33.85 A O

ATOM 1286 N ALA A 194 49.332 37.271 43.295 1.00 32.21 A N

ATOM 1287 CA ALA A 194 48.024 36.848 43.803 1.00 30.97 A C

ATOM 1288 CB ALA A 194 48.101 36.400 45.251 1.00 30.54 A C

ATOM 1289 C ALA A 194 47.003 37.961 43.623 1.00 30.28 A C

ATOM 1290 O ALA A 194 46.062 38.108 44.392 1.00 32.52 A O

ATOM 1291 N VAL A 195 47.204 38.736 42.573 1.00 29.44 A N

ATOM 1292 CA VAL A 195 46.330 39.836 42.228 1.00 29.45 A C

ATOM 1293 CB VAL A 195 47.101 40.962 41.499 1.00 31.02 A C

ATOM 1294 CGI VAL A 195 46.125 41.922 40.780 1.00 30.06 A C

ATOM 1295 CG2 VAL A 195 47.974 41.719 42.511 1.00 31.20 A C

ATOM 1296 C VAL A 195 45.222 39.351 41.330 1.00 28.12 A C

ATOM 1297 0 VAL A 195 45.468 38.741 40.301 1.00 28.23 A O

ATOM 1298 N LEU A 196 44.002 39.661 41.735 1.00 26.08 A N

ATOM 1299 CA LEU A 196 42.817 39.295 41.004 1.00 24.78 A C

ATOM 1300 CB LEU A 196 41.809 38.700 41.982 1.00 24.48 A C

ATOM 1301 CG LEU A 196 40.434 38.320 41.448 1.00 23.75 A C

ATOM 1302 CDl LEU A 196 39.876 37.168 42.282 1.00 27.10 A C

ATOM 1303 CD2 LEU A 196 39.535 39.534 41.499 1.00 23.28 A C ATOM 1304 C LEU A 196 42.231 40.524 40.330 1.00 25.58 A C

ATOM 1305 O LEU A 196 42.178 41.589 40.931 1.00 30.48 A O

ATOM 1306 N LYS A 197 41.776 40.354 39.090 1.00 26.26 A N

ATOM 1307 CA LYS A 197 41.146 41.413 38.275 1.00 24.81 A C

ATOM 1308 CB LYS A 197 42.035 41.818 37.089 1.00 21.80 A C

ATOM 1309 CG LYS A 197 43.402 42.425 37.444 1.00 26.31 A C

ATOM 1310 CD LYS A 197 43.294 43.704 38.276 1.00 29.08 A C .

ATOM 1311 CE LYS A 197 44.634 44.418 38.417 1.00 30.93 A C

ATOM 1312 NZ LYS A 197 45.217 44.567 37.062 1.00 37.10 A N

ATOM 1313 C LYS A 197 39.814 40.903 37.712 1.00 25.33 A C

ATOM 1314 0 LYS A 197 39.776 39.921 36.977 1.00 25.96 A O

ATOM 1315 N LEU A 198 38.726 41.576 38.063 1.00 26.02 A N

ATOM 1316 CA LEU A 198 37.409 41.215 37.582 1.00 24.94 A C

ATOM 1317 CB LEU A 198 36.355 42.041 38.313 1.00 27.25 A C

ATOM 1318 CG LEU A 198 34.992 41.470 38.710 1.00 28.56 A C

ATOM 1319 CDl LEU A 198 34.010 42.625 38.860 1.00 26.58 A C

ATOM 1320 CD2 LEU A 198 34.488 40.491 37.678 1.00 29.04 A C

ATOM 1321 C LEU A 198 37.358 41.589 36.109 1.00 25.54 A C

ATOM 1322 O LEU A 198 37.905 42.611 35.712 1.00 23.47 A O

ATOM 1323 N CYS A 199 36.701 40.761 35.303 1.00 27.06 A N

ATOM 1324 CA CYS A 199 36.546 41.053 33.890 1.00 26.95 A C ATOM 1325 CB CYS A 199 37.664 40.435 33.047 1.00 27.29 A C

ATOM 1326 SG CYS A 199 37.600 38.675 32.727 1.00 27.04 A S

ATOM 1327 C CYS A 199 35.168 40.688 33.353 1.00 28.18 A C

ATOM 1328 0 CYS A 199 34.245 40.407 34.135 1.00 24.57 A O

ATOM 1329 N ASP A 200 35.057 40.739 32.017 1.00 30.94 A N

ATOM 1330 CA ASP A 200 33.845 40.486 31.230 1.00 30.60 A C

ATOM 1331 CB ASP A 200 33.474 39.003 31.109 1.00 31.99 A C

ATOM 1332 CG ASP A 200 32.232 38.777 30.209 1.00 35.20 A C

ATOM 1333 OD1 ASP A 200 31.350 37.964 30.567 1.00 36.52 A O

ATOM 1334 OD2 ASP A 200 32.117 39.421 29.134 1.00 39.61 A O

ATOM 1335 C ASP A 200 32.672 41.251 31.775 1.00 32.71 A C

ATOM 1336 O ASP A 200 32.003 40.798 32.702 1.00 33.36 A O

ATOM 1337 N PHE A 201 32.432 42.430 31.216 1.00 34.02 A N

ATOM 1338 CA PHE A 201 31.296 43.242 31.642 1.00 37.31 A C

ATOM 1339 CB PHE A 201 31.774 44.655 31.991 1.00 36.67 A C

ATOM 1340 CG PHE A 201 32.506 44.726 33.302 1.00 34.55 A C

ATOM 1341 CDl PHE A 201 33.862 44.434 33.376 1.00 34.34 A C

ATOM 1342 CD2 PHE A 201 31.829 45.073 34.471 1.00 35.02 A C

ATOM 1343 CE1 PHE A 201 34.534 44.480 34.594 1.00 31.36 A C

ATOM 1344 CE2 PHE A 201 32.489 45.123 35.691 1.00 34.05 A C

ATOM 1345 CZ PHE A 201 33.851 44.826 35.751 1.00 31.93 A C ATOM 1346 C PHE A 201 30.177 43.236 30.584 1.00 38.92 A C

ATOM 1347 O PHE A 201 29.297 44.103 30.562 1.00 38.59 A O

ATOM 1348 N GLY A 202 30.203 42.200 29.750 1.00 41.08 A N

ATOM 1349 CA GLY A 202 29.232 42.057 28.686 1.00 45.08 A C

ATOM 1350 C GLY A 202 27.800 41.828 29.139 1.00 47.51 A C

ATOM 1351 O GLY A 202 26.863 41.996 28.351 1.00 50.35 A O

ATOM 1352 N SER A 203 27.622 41.432 30.397 1.00 48.34 A N

ATOM 1353 CA SER A 203 26.288 41.181 30.934 1.00 47.92 A C

ATOM 1354 CB SER A 203 26.186 39.744 31.488 1.00 49.53 A C

ATOM 1355 OG SER A 203 26.524 38.768 30.509 1.00 50.50 A O

ATOM 1356 C SER A 203 26.032 42.192 32.048 1.00 48.85 A C

ATOM 1357 O SER A 203 25.037 42.102 32.781 1.00 48.61 A O

ATOM 1358 N ALA A 204 26.957 43.143 32.182 1.00 48.52 A N

ATOM 1359 CA ALA A 204 26.856 44.186 33.199 1.00 47.92 A C

ATOM 1360 CB ALA A 204 28.208 44.890 33.369 1.00 48.73 A C

ATOM 1361 C ALA A 204 25.776 45.202 32.856 1.00 46.94 A C

ATOM 1362 O ALA A 204 25.525 45.498 31.680 1.00 46.50 A O

ATOM 1363 N LYS A 205 25.159 45.752 33.893 1.00 46.53 A N

ATOM 1364 CA LYS A 205 24.121 46.737 33.702 1.00 48.03 A C

ATOM 1365 CB LYS A 205 22.838 46.052 33.221 1.0049.84 A C

ATOM 1366 CG LYS A 205 21.665 46.999 33.043 1.00 52.67 A C ATOM 1367 CD LYS A 205 20.336 46.267 33.015 1.00 54.12 A C

ATOM 1368 CE LYS A 205 19.281 46.991 33.873 1.00 55.97 A C

ATOM 1369 NZ LYS A 205 17.891 46.432 33.715 1.00 51.58 A N

ATOM 1370 C LYS A 205 23.843 47.508 34.986 1.00 48.17 A C

ATOM 1371 O LYS A 205 23.662 46.913 36.052 1.00 45.43 A O

ATOM 1372 N GLN A 206 23.835 48.838 34.890 1.00 50.42 A N

ATOM 1373 CA GLN A 206 23.537 49.656 36.060 1.00 51.09 A C

ATOM 1374 CB GLN A 206 23.802 51.138 35.812 1.00 51.00 A C

ATOM 1375 CG GLN A 206 23.638 51.964 37.074 1.00 55.43 A C

ATOM 1376 CD GLN A 206 23.668 53.464 36.832 1.00 58.62 A C

ATOM 1377 OE1 GLN A 206 23.219 54.238 37.682 1.00 60.73 A O

ATOM 1378 NE2 GLN A 206 24.196 53.886 35.677 1.00 58.59 A N

ATOM 1379 C GLN A 206 22.064 49.437 36.309 1.00 51.56 A C

ATOM 1380 O GLN A 206 21.234 49.629 35.416 1.00 52.14 A O

ATOM 1381 N LEU A 207 21.750 48.963 37.503 1.00 53.49 A N

ATOM 1382 CA LEU A 207 20.372 48.694 37.861 1.00 55.48 A C

ATOM 1383 CB LEU A 207 20.300 47.547 38.874 1.00 52.46 A C

ATOM 1384 CG LEU A 207 20.966 46.208 38.531 1.00 50.81 A C

ATOM 1385 CDl LEU A 207 20.413 45.156 39.482 1.00 50.23 A C

ATOM 1386 CD2 LEU A 207 20.738 45.798 37.071 1.00 48.02 A C

ATOM 1387 C LEU A 207 19.718 49.942 38.446 1.00 59.23 A C ATOM 1388 O LEU A 207 20.384 50.743 39.123 1.00 58.87 A O

ATOM 1389 N VAL A 208 18.418 50.095 38.163 1.00 62.57 A N

ATOM 1390 CA VAL A 208 17.590 51.215 38.642 1.00 64.00 A C

ATOM 1391 CB VAL A 208 17.519 52.363 37.605 1.00 62.01 A C

ATOM 1392 CGI VAL A 208 17.474 51.802 36.198 1.00 61.19 A C

ATOM 1393 CG2 VAL A 208 16.299 53.212 37.864 1.00 61.93 A C

ATOM 1394 C VAL A 208 16.182 50.693 38.901 1.00 65.50 A C

ATOM 1395 0 VAL A 208 15.686 49.880 38.122 1.00 66.73 A O

ATOM 1396 N ARG A 209 15.551 51.131 39.994 1.00 67.63 A N

ATOM 1397 CA ARG A 209 14.198 50.670 40.319 1.00 69.71 A C

ATOM 1398 CB ARG A 209 13.755 51.108 41.721 1.00 72.23 A C

ATOM 1399 CG ARG A 209 13.539 52.608 41.907 1.00 75.01 A C

ATOM 1400 CD ARG A 209 14.846 53.370 41.838 1.00 77.95 A C

ATOM 1401 NE ARG A 209 14.712 54.747 42.310 1.00 80.82 A N

ATOM 1402 CZ ARG A 209 15.377 55.779 41.798 1.00 81.99 A C

ATOM 1403 NHl ARG A 209 16.220 55.592 40.787 1.00 81.89 A N

ATOM 1404 NH2 ARG A 209 15.225 56.993 42.318 1.00 83.70 A N

ATOM 1405 C ARG A 209 13.224 51.189 39.285 1.00 69.54 A C

ATOM 1406 O ARG A 209 13.281 52.360 38.898 1.00 69.25 A O

ATOM 1407 N GLY A 210 12.344 50.306 38.826 1.00 69.42 A N

ATOM 1408 CA GLY A 210 11.383 50.694 37.815 1.00 69.06 A C ATOM 1409 C GLY A 210 11.756 50.171 36.440 1.00 68.46 A C

ATOM 1410 O GLY A 210 10.878 49.792 35.673 1.00 69.37 A O

ATOM 1411 N GLU A 211 13.041 50.193 36.096 1.00 66.88 A N

ATOM 1412 CA GLU A 211 13.481 49.677 34.799 1.00 66.19 A C

ATOM 1413 CB GLU A 211 14.687 50.480 34.287 1.00 67.27 A C

ATOM 1414 CG GLU A 211 14.414 52.001 34.244 1.00 67.78 A C

ATOM 1415 CD GLU A 211 15.365 52.786 33.327 1.00 68.52 A C

ATOM 1416 OEI GLU A 211 16.595 52.645 33.487 1.00 67.46 A O

ATOM 1417 OE2 GLU A 211 14.885 53.554 32.450 1.00 69.67 A O

ATOM 1418 C GLU A 211 13.788 48.180 35.004 1.00 65.00 A C

ATOM 1419 O GLU A 211 14.675 47.815 35.776 1.00 65.37 A O

ATOM 1420 N PRO A 212 13.011 47.299 34.348 1.00 63.55 A N

ATOM 1421 CD PRO A 212 11.977 47.679 33.369 1.00 64.19 A C

ATOM 1422 CA PRO A 212 13.118 45.840 34.420 1.00 61.55 A C

ATOM 1423 CB PRO A 212 11.750 45.390 33.938 1.00 61.93 A C

ATOM 1424 CG PRO A 212 11.555 46.315 32.778 1.00 63.79 A C

ATOM 1425 C PRO A 212 14.218 45.200 33.594 1.00 59.49 A C

ATOM 1426 O PRO A 212 14.383 45.475 32.405 1.00 59.70 A O

ATOM 1427 N ASN A 213 14.856 44.221 34.224 1.00 57.24 A N

ATOM 1428 CA ASN A 213 15.965 43.476 33.652 1.00 52.53 A C

ATOM 1429 CB ASN A 213 17.184 43.635 34.569 1.00 50.18 A C ATOM 1430 CG ASN A 213 16.966 44.683 35.665 1.00 48.59 A C

ATOM 1431 OD1 ASN A 213 17.436 45.821 35.566 1.00 48.28 A O

ATOM 1432 ND2 ASN A 213 16.218 44.308 36.699 1.00 46.52 A N

ATOM 1433 C ASN A 213 15.590 41.997 33.534 1.00 50.89 A C

ATOM 1434 0 ASN A 213 14.796 41.493 34.336 1.00 50.48 A O

ATOM 1435 N VAL A 214 16.167 41.309 32.543 1.00 48.62 A N

ATOM 1436 CA VAL A 214 15.905 39.880 32.309 1.00 45.70 A C

ATOM 1437 CB VAL A 214 16.723 39.312 31.143 1.00 44.23 A C

ATOM 1438 CGI VAL A 214 15.949 39.402 29.867 1.00 45.41 A C

ATOM 1439 CG2 VAL A 214 18.039 40.027 31.045 1.00 40.36 A C

ATOM 1440 C VAL A 214 16.21 1 38.975 33.488 1.00 44.58 A C

ATOM 1441 O VAL A 214 17.195 39.179 34.204 1.00 44.08 A O

ATOM 1442 N SER A 215 15.379 37.948 33.646 1.00 43.51 A N

ATOM 1443 CA SER A 215 15.541 36.965 34.702 1.00 41.53 A C

ATOM 1444 CB SER A 215 14.224 36.262 34.960 1.00 40.28 A C

ATOM 1445 OG SER A 215 13.244 37.187 35.349 1.00 44.40 A O

ATOM 1446 C SER A 215 16.564 35.937 34.234 1.00 40.92 A C

ATOM 1447 O SER A 215 17.394 35.482 35.015 1.00 41.15 A O

ATOM 1448 N PTR A 216 16.474 35.551 32.963 1.00 40.14 A N

ATOM 1449 CA PTR A 216 17.401 34.578 32.409 1.00 40.46 A C

ATOM 1450 CB PTR A 216 16.848 33.925 31.141 1.00 40.63 A C ATOM 1451 CG PTR A 216 17.534 32.603 30.821 1.00 40.78 A C

ATOM 1452 CDl PTR A 216 17.136 31.432 31.450 1.00 41.37 A C

ATOM 1453 CE1 PTR A 216 17.759 30.216 31.187 1.00 41.30 A C

ATOM 1454 CD2 PTR A 216 18.584 32.524 29.918 1.00 38.09 A C

ATOM 1455 CE2 PTR A 216 19.219 31.304 29.650 1.00 38.06 A C

ATOM 1456 CZ PTR A 216 18.799 30.150 30.288 1.00 39.44 A C

ATOM 1457 OH PTR A 216 19.360 28.905 29.996 1.00 41.40 A O

ATOM 1458 C PTR A 216 18.719 35.248 32.092 1.00 41.06 A C

ATOM 1459 O PTR A 216 18.988 35.604 30.943 1.00 41.01 A O

ATOM 1460 P PTR A 216 20.633 28.391 30.790 1.00 38.82 A P

ATOM 1461 O1P PTR A 216 21.164 27.232 29.920 1.00 38.25 A O

ATOM 1462 O2P PTR A 216 20.052 27.820 32.128 1.00 35.47 A O

ATOM 1463 O3P PTR A 216 21.677 29.458 31.002 1.00 35.59 A O

ATOM 1464 N ILE A 217 19.532 35.420 33.128 1.00 41.67 A N

ATOM 1465 CA ILE A 217 20.840 36.061 33.014 1.00 41.37 A C

ATOM 1466 CB ILE A 217 20.728 37.589 33.302 1.00 38.71 A C

ATOM 1467 CG2 ILE A 217 20.540 37.837 34.788 1.00 35.11 A C

ATOM 1468 CGI ILE A 217 21.989 38.316 32.827 1.00 39.70 A C

ATOM 1469 CDl ILE A 217 22.306 38.150 31.349 1.00 36.80 A C

ATOM 1470 C ILE A 217 21.782 35.407 34.042 1.0043.45 A C

ATOM 1471 O ILE A 217 21.310 34.814 35.028 1.00 43.91 A O ATOM 1472 N CYS A 218 23.096 35.490 33.797 1.00 43.60 A N

ATOM 1473 CA CYS A 218 24.108 34.920 34.705 1.00 42.50 A C

ATOM 1474 CB CYS A 218 23.701 35.166 36.173 1.00 40.92 A C

ATOM 1475 SG CYS A 218 24.917 34.666 37.397 1.00 47.75 A S

ATOM 1476 C CYS A 218 24.327 33.425 34.453 1.00 40.80 A C

ATOM 1477 O CYS A 218 23.365 32.690 34.236 1.00 42.78 A O

ATOM 1478 N SER A 219 25.588 32.986 34.451 1.00 38.62 A N

ATOM 1479 CA SER A 219 25.913 31.577 34.219 1.00 34.41 A C

ATOM 1480 CB SER A 219 27.413 31.330 34.330 1.00 34.07 A C

ATOM 1481 OG SER A 219 28.047 31.609 33.098 1.00 37.97 A O

ATOM 1482 C SER A 219 25.156 30.656 35.153 1.00 31.88 A C

ATOM 1483 O SER A 219 25.235 30.792 36.379 1.00 31.16 A O

ATOM 1484 N ARG A 220 24.497 29.664 34.557 1.00 29.33 A N

ATOM 1485 CA ARG A 220 23.654 28.710 35.285 1.00 27.16 A C

ATOM 1486 CB ARG A 220 23.324 27.478 34.435 1.00 28.01 A C

ATOM 1487 CG ARG A 220 22.183 26.644 35.022 1.00 29.01 A C

ATOM 1488 CD ARG A 220 22.117 25.265 34.364 1.00 33.09 A C

ATOM 1489 NE ARG A 220 21.904 25.346 32.919 1.00 34.89 A N

ATOM 1490 CZ ARG A 220 22.335 24.463 32.020 1.00 33.04 A C

ATOM 1491 NHl ARG A 220 23.023 23.391 32.384 1.00 34.49 A N

ATOM 1492 NH2 ARG A 220 22.080 24.673 30.740 1.00 33.47 A N ATOM 1493 C ARG A 220 24.055 28.250 36.675 1.00 24.73 A C

ATOM 1494 O ARG A 220 23.247 28.325 37.577 1.00 24.64 A O

ATOM 1495 N TYR A 221 25.262 27.722 36.830 1.00 22.54 A N

ATOM 1496 CA TYR A 221 25.712 27.231 38.121 1.00 23.80 A C

ATOM 1497 CB TYR A 221 27.070 26.539 37.974 1.00 23.89 A C

ATOM 1498 CG TYR A 221 27.124 25.341 37.044 1.00 28.24 A C

ATOM 1499 CDl TYR A 221 28.340 24.765 36.744 1.00 30.22 A C

ATOM 1500 CE1 TYR A 221 28.443 23.649 35.955 1.00 31.53 A C

ATOM 1501 CD2 TYR A 221 25.981 24.759 36.508 1.00 28.46 A C

ATOM 1502 CE2 TYR A 221 26.070 23.628 35.699 1.00 29.73 A C

ATOM 1503 CZ TYR A 221 27.326 23.071 35.433 1.00 31.40 A C

ATOM 1504 OH TYR A 221 27.513 21.911 34.687 1.00 34.11 A O

ATOM 1505 C TYR A 221 25.833 28.336 39.181 1.00 23.02 A C

ATOM 1506 O TYR A 221 25.752 28.072 40.369 1.00 20.91 A O

ATOM 1507 N TYR A 222 26.054 29.568 38.743 1.00 24.21 A N

ATOM 1508 CA TYR A 222 26.246 30.688 39.658 1.00 24.73 A C

ATOM 1509 CB TYR A 222 27.522 31.463 39.241 1.00 22.79 A C

ATOM 1510 CG TYR A 222 28.724 30.554 38.965 1.00 22.45 A C

ATOM 1511 CD1 TYR A 222 29.609 30.193 39.985 1.00 21.00 A C

ATOM 1512 CE1 TYR A 222 30.632 29.245 39.769 1.00 20.63 A C

ATOM 1513 CD2 TYR A 222 28.903 29.960 37.713 1.00 19.14 A C ATOM 1514 CE2 TYR A 222 29.913 29.017 37.499 1.00 18.85 A C

ATOM 1515 CZ TYR A 222 30.770 28.649 38.519 1.00 19.59 A C

ATOM 1516 OH TYR A 222 31.691 27.631 38.318 1.00 16.40 A O

ATOM 1517 C TYR A 222 25.022 31.610 39.722 1.00 24.44 A C

ATOM 1518 O TYR A 222 25.037 32.640 40.397 1.00 26.04 A O

ATOM 1519 N ARG A 223 23.942 31.191 39.070 1.00 24.33 A N

ATOM 1520 CA ARG A 223 22.706 31.958 39.021 1.00 23.24 A C

ATOM 1521 CB ARG A 223 21.818 31.395 37.933 1.00 25.82 A C

ATOM 1522 CG ARG A 223 20.589 32.224 37.663 1.00 28.19 A C

ATOM 1523 CD ARG A 223 19.841 31.661 36.469 1.00 29.16 A C

ATOM 1524 NE ARG A 223 20.627 31.758 35.238 1.00 30.38 A N

ATOM 1525 CZ ARG A 223 20.579 30.874 34.253 1.00 28.67 A C

ATOM 1526 NHl ARG A 223 19.782 29.803 34.356 1.00 30.82 A N

ATOM 1527 NH2 ARG A 223 21.296 31.089 33.150 1.00 29.60 A N

ATOM 1528 C ARG A 223 21.944 31.942 40.343 1.00 25.78 A C

ATOM 1529 O ARG A 223 21.648 30.865 40.875 1.00 28.11 A O

ATOM 1530 N ALA A 224 21.582 33.125 40.836 1.00 25.24 A N

ATOM 1531 CA ALA A 224 20.844 33.251 42.098 1.00 27.32 A C

ATOM 1532 CB ALA A 224 20.769 34.710 42.522 1.00 26.42 A C

ATOM 1533 C ALA A 224 19.448 32.688 41.957 1.00 28.09 A C

ATOM 1534 O ALA A 224 18.864 32.775 40.883 1.00 29.27 A O ATOM 1535 N PRO A 225 18.860 32.181 43.057 1.00 29.46 A N

ATOM 1536 CD PRO A 225 19.357 32.195 44.441 1.00 31.14 A C

ATOM 1537 CA PRO A 225 17.506 31.615 43.005 1.00 31.01 A C

ATOM 1538 CB PRO A 225 17.301 31.093 44.430 1.00 31.05 A C

ATOM 1539 CG PRO A 225 18.074 32.059 45.243 1.00 30.52 A C

ATOM 1540 C PRO A 225 16.421 32.612 42.527 1.00 33.71 A C

ATOM 1541 O PRO A 225 15.570 32.240 41.720 1.00 33.75 A O

ATOM 1542 N GLU A 226 16.481 33.877 42.960 1.00 36.24 A N

ATOM 1543 CA GLU A 226 15.510 34.875 42.486 1.00 37.76 A C

ATOM 1544 CB GLU A 226 15.963 36.325 42.744 1.00 39.65 A C

ATOM 1545 CG GLU A 226 16.445 36.679 44.109 1.00 40.28 A C

ATOM 1546 CD GLU A 226 17.937 36.487 44.247 1.00 39.21 A C

ATOM 1547 OEI GLU A 226 18.710 37.361 43.771 1.00 40.55 A O

ATOM 1548 OE2 GLU A 226 18.321 35.455 44.837 1.00 35.91 A O

ATOM 1549 C GLU A 226 15.362 34.769 40.966 1.00 37.11 A C

ATOM 1550 O GLU A 226 14.263 34.806 40.441 1.00 37.86 A O

ATOM 1551 N LEU A 227 16.488 34.755 40.264 1.00 38.01 A N

ATOM 1552 CA LEU A 227 16.494 34.675 38.812 1.00 39.83 A C

ATOM 1553 CB LEU A 227 17.935 34.682 38.305 1.00 39.84 A C

ATOM 1554 CG LEU A 227 18.763 35.952 38.408 1.0040.58 A C

ATOM 1555 CDl LEU A 227 18.050 37.070 37.664 1.00 42.21 A C ATOM 1556 CD2 LEU A 227 18.984 36.297 39.858 1.00 41.30 A C

ATOM 1557 C LEU A 227 15.790 33.422 38.275 1.00 41.64 A C

ATOM 1558 O LEU A 227 15.231 33.427 37.163 1.00 40.70 A O

ATOM 1559 N ILE A 228 15.883 32.338 39.045 1.00 42.13 A N

ATOM 1560 CA ILE A 228 15.288 31.053 38.677 1.00 41.98 A C

ATOM 1561 CB ILE A 228 15.943 29.911 39.504 1.00 41.07 A C

ATOM 1562 CG2 ILE A 228 15.548 28.550 38.948 1.00 40.33 A C

ATOM 1563 CGI ILE A 228 17.471 30.051 39.429 1.00 38.76 A C

ATOM 1564 CDl ILE A 228 18.226 29.081 40.281 1.00 37.40 A C

ATOM 1565 C ILE A 228 13.750 31.101 38.821 1.00 41.98 A C

ATOM 1566 O ILE A 228 13.021 30.462 38.048 1.00 43.60 A O

ATOM 1567 N PHE A 229 13.283 31.919 39.768 1.00 39.71 A N

ATOM 1568 CA PHE A 229 11.859 32.148 40.038 1.00 38.89 A C

ATOM 1569 CB PHE A 229 11.614 32.418 41.515 1.00 35.12 A C

ATOM 1570 CG PHE A 229 11.615 31.187 42.353 1.00 37.40 A C

ATOM 1571 CDl PHE A 229 12.760 30.785 43.017 1.00 35.70 A C

ATOM 1572 CD2 PHE A 229 10.449 30.454 42.527 1.00 39.78 A C

ATOM 1573 CE1 PHE A 229 12.749 29.683 43.848 1.00 38.38 A C

ATOM 1574 CE2 PHE A 229 10.422 29.339 43.363 1.00 41.77 A C

ATOM 1575 CZ PHE A 229 11.574 28.954 44.028 1.00 40.44 A C

ATOM 1576 C PHE A 229 11.298 33.312 39.224 1.00 40.12 A C ATOM 1577 O PHE A 229 10.226 33.837 39.531 1.00 41.20 A O

ATOM 1578 N GLY A 230 12.073 33.765 38.245 1.00 41.63 A N

ATOM 1579 CA GLY A 230 11.636 34.834 37.359 1.00 43.05 A C

ATOM 1580 C GLY A 230 11.640 36.302 37.761 1.00 43.47 A C

ATOM 1581 O GLY A 230 11.105 37.128 37.006 1.00 43.20 A O

ATOM 1582 N ALA A 231 12.220 36.640 38.914 1.00 43.29 A N

ATOM 1583 CA ALA A 231 12.260 38.028 39.360 1.00 42.22 A C

ATOM 1584 CB ALA A 231 13.033 38.140 40.668 1.00 41.84 A C

ATOM 1585 C ALA A 231 12.902 38.894 38.276 1.00 44.04 A C

ATOM 1586 O ALA A 231 13.803 38.439 37.544 1.00 45.16 A O

ATOM 1587 N THR A 232 12.392 40.118 38.130 1.00 44.50 A N

ATOM 1588 CA THR A 232 12.908 41.072 37.139 1.00 43.69 A C

ATOM 1589 CB THR A 232 11.877 41.338 35.998 1.00 43.60 A C

ATOM 1590 OG1 THR A 232 10.547 41.302 36.534 1.00 43.96 A O

ATOM 1591 CG2 THR A 232 12.002 40.308 34.878 1.00 42.69 A C

ATOM 1592 C THR A 232 13.215 42.374 37.881 1.00 43.92 A C

ATOM 1593 0 THR A 232 13.717 43.340 37.293 1.00 43.42 A O

ATOM 1594 N ASP A 233 12.912 42.353 39.184 1.00 45.51 A N

ATOM 1595 CA ASP A 233 13.105 43.471 40.121 1.00 48.09 A C

ATOM 1596 CB ASP A 233 11.804 43.747 40.899 1.00 52.12 A C

ATOM 1597 CG ASP A 233 11.326 42.528 41.735 1.00 56.77 A C ATOM 1598 OD1 ASP A 233 11.244 41.406 41.170 1.00 57.99 A O

ATOM 1599 OD2 ASP A 233 11.012 42.697 42.951 1.00 58.75 A O

ATOM 1600 C ASP A 233 14.190 43.103 41.127 1.00 47.45 A C

ATOM 1601 O ASP A 233 14.120 43.475 42.301 1.00 47.30 A O

ATOM 1602 N TYR A 234 15.188 42.360 40.659 1.00 47.32 A N

ATOM 1603 CA TYR A 234 16.284 41.895 41.503 1.00 45.77 A C

ATOM 1604 CB TYR A 234 16.889 40.616 40.905 1.00 41.41 A C

ATOM 1605 CG TYR A 234 17.382 40.751 39.479 1.00 36.80 A C

ATOM 1606 CD1 TYR A 234 18.671 41.195 39.205 1.00 35.39 A C

ATOM 1607 CE1 TYR A 234 19.135 41.292 37.910 1.00 31.99 A C

ATOM 1608 CD2 TYR A 234 16.573 40.409 38.411 1.00 35.34 A C

ATOM 1609 CE2 TYR A 234 17.026 40.505 37.109 1.00 33.26 A C

ATOM 1610 CZ TYR A 234 18.312 40.947 36.856 1.00 32.63 A C

ATOM 1611 OH TYR A 234 18.776 41.051 35.541 1.00 32.50 A O

ATOM 1612 C TYR A 234 17.379 42.929 41.795 1.00 46.81 A C

ATOM 1613 O TYR A 234 17.541 43.924 41.072 1.00 47.03 A O

ATOM 1614 N THR A 235 18.120 42.690 42.871 1.00 47.19 A N

ATOM 1615 CA THR A 235 19.188 43.596 43.253 1.00 46.66 A C

ATOM 1616 CB THR A 235 19.195 43.780 44.778 1.00 48.48 A C

ATOM 1617 OG1 THR A 235 18.980 42.519 45.430 1.00 51.51 A O

ATOM 1618 CG2 THR A 235 18.076 44.704 45.168 1.00 50.02 A C ATOM 1619 C THR A 235 20.584 43.222 42.720 1.00 46.29 A C

ATOM 1620 O THR A 235 20.718 42.506 41.714 1.00 45.29 A O

ATOM 1621 N SER A 236 21.617 43.791 43.343 1.00 44.53 A N

ATOM 1622 CA SER A 236 23.008 43.521 42.967 1.00 41.78 A C

ATOM 1623 CB SER A 236 23.884 44.760 43.161 1.00 39.95 A C

ATOM 1624 OG SER A 236 23.836 45.198 44.508 1.00 45.19 A O

ATOM 1625 C SER A 236 23.511 42.366 43.831 1.00 38.89 A C

ATOM 1626 O SER A 236 24.616 41.862 43.633 1.00 38.04 A O

ATOM 1627 N SER A 237 22.677 41.964 44.789 1.00 35.99 A N

ATOM 1628 CA SER A 237 22.976 40.850 45.668 1.00 34.52 A C

ATOM 1629 CB SER A 237 21.988 40.800 46.833 1.00 33.62 A C

ATOM 1630 OG SER A 237 20.663 40.726 46.357 1.00 35.66 A O

ATOM 1631 C SER A 237 22.951 39.519 44.894 1.00 32.95 A C

ATOM 1632 O SER A 237 23.123 38.457 45.487 1.00 33.79 A O

ATOM 1633 N ILE A 238 22.684 39.570 43.587 1.00 31.53 A N

ATOM 1634 CA ILE A 238 22.702 38.355 42.763 1.00 30.22 A C

ATOM 1635 CB ILE A 238 22.012 38.536 41.356 1.00 26.21 A C

ATOM 1636 CG2 ILE A 238 20.537 38.803 41.518 1.00 29.08 A C

ATOM 1637 CGI ILE A 238 22.656 39.659 40.555 1.00 26.02 A C

ATOM 1638 CDl ILE A 238 22.093 39.796 39.182 1.00 26.47 A C

ATOM 1639 C ILE A 238 24.191 37.985 42.604 1.00 30.52 A C ATOM 1640 O ILE A 238 24.548 36.802 42.508 1.00 31.51 A O

ATOM 1641 N ASP A 239 25.040 39.022 42.620 1.00 30.54 A N

ATOM 1642 CA ASP A 239 26.490 38.887 42.522 1.00 26.94 A C

ATOM 1643 CB ASP A 239 27.169 40.244 42.288 1.00 27.41 A C

ATOM 1644 CG ASP A 239 26.994 40.752 40.875 1.00 27.90 A C

ATOM 1645 OD1 ASP A 239 26.559 39.972 40.005 1.00 29.28 A O

ATOM 1646 OD2 ASP A 239 27.307 41.936 40.620 1.00 30.96 A O

ATOM 1647 C ASP A 239 26.991 38.290 43.823 1.00 25.46 A C

ATOM 1648 O ASP A 239 27.938 37.524 43.826 1.00 25.21 A O

ATOM 1649 N VAL A 240 26.374 38.646 44.940 1.00 24.64 A N

ATOM 1650 CA VAL A 240 26.833 38.079 46.200 1.00 25.12 A C

ATOM 1651 CB VAL A 240 26.262 38.822 47.413 1.00 23.29 A C

ATOM 1652 CGI VAL A 240 26.488 38.015 48.667 1.00 23.70 A C

ATOM 1653 CG2 VAL A 240 26.949 40.154 47.545 1.00 21.83 A C

ATOM 1654 C VAL A 240 26.522 36.584 46.237 1.00 24.34 A C

ATOM 1655 O VAL A 240 27.321 35.782 46.725 1.00 27.47 A O

ATOM 1656 N TRP A 241 25.383 36.198 45.679 1.00 24.52 A N

ATOM 1657 CA TRP A 241 25.034 34.785 45.609 1.00 23.05 A C

ATOM 1658 CB TRP A 241 23.648 34.607 44.986 1.00 24.31 A C

ATOM 1659 CG TRP A 241 23.330 33.166 44.670 1.00 23.07 A C

ATOM 1660 CD2 TRP A 241 22.601 32.246 45.488 1.00 22.44 A C ATOM 1661 CE2 TRP A 241 22.621 30.997 44.837 1.00 23.53 A C

ATOM 1662 CE3 TRP A 241 21.938 32.353 46.704 1.00 22.25 A C

ATOM 1663 CDl TRP A 241 23.740 32.458 43.576 1.00 24.37 A C

ATOM 1664 NE1 TRP A 241 23.323 31.152 43.671 1.00 23.84 A N

ATOM 1665 CZ2 TRP A 241 22.005 29.867 45.376 1.00 22.52 A C

ATOM 1666 CZ3 TRP A 241 21.331 31.234 47.230 1.00 22.17 A C

ATOM 1667 CH2 TRP A 241 21.366 30.013 46.572 1.00 23.92 A C

ATOM 1668 C TRP A 241 26.080 34.098 44.717 1.00 22.93 A C

ATOM 1669 O TRP A 241 26.643 33.066 45.083 1.00 23.57 A O

ATOM 1670 N SER A 242 26.337 34.689 43.549 1.00 21.92 A N

ATOM 1671 CA SER A 242 27.321 34.160 42.605 1.00 23.80 A C

ATOM 1672 CB SER A 242 27.444 35.081 41.404 1.00 22.23 A C

ATOM 1673 OG SER A 242 26.222 35.126 40.708 1.00 24.61 A O

ATOM 1674 C SER A 242 28.697 33.997 43.239 1.00 24.81 A C

ATOM 1675 O SER A 242 29.378 33.007 42.998 1.00 24.82 A O

ATOM 1676 N ALA A 243 29.105 34.997 44.024 1.00 26.07 A N

ATOM 1677 CA ALA A 243 30.390 34.988 44.711 1.00 24.84 A C

ATOM 1678 CB ALA A 243 30.642 36.325 45.391 1.00 25.84 A C

ATOM 1679 C ALA A 243 30.386 33.862 45.726 1.00 24.61 A C

ATOM 1680 O ALA A 243 31.406 33.224 45.926 1.00 26.65 A O

ATOM 1681 N GLY A 244 29.246 33.633 46.379 1.00 25.37 A N ATOM 1682 CA GLY A 244 29.148 32.546 47.349 1.00 24.68 A C

ATOM 1683 C GLY A 244 29.335 31.182 46.668 1.00 24.83 A C

ATOM 1684 O GLY A 244 29.874 30.254 47.257 1.00 25.31 A O

ATOM 1685 N CYS A 245 28.893 31.059 45.415 1.00 23.66 A N

ATOM 1686 CA CYS A 245 29.035 29.812 44.668 1.00 22.85 A C

ATOM 1687 CB CYS A 245 28.193 29.851 43.394 1.00 23.45 A C

ATOM 1688 SG CYS A 245 26.404 29.904 43.670 1.00 27.08 A S

ATOM 1689 C CYS A 245 30.505 29.580 44.320 1.00 23.15 A C

ATOM 1690 O CYS A 245 30.986 28.446 44.329 1.00 24.13 A O

ATOM 1691 N VAL A 246 31.212 30.663 43.993 1.00 23.76 A N

ATOM 1692 CA VAL A 246 32.632 30.589 43.665 1.00 19.75 A C

ATOM 1693 CB VAL A 246 33.177 31.950 43.234 1.00 18.39 A C

ATOM 1694 CGI VAL A 246 34.668 31.848 43.030 1.00 17.77 A C

ATOM 1695 CG2 VAL A 246 32.488 32.421 41.957 1.00 17.97 A C

ATOM 1696 C VAL A 246 33.415 30.119 44.886 1.00 21.03 A C

ATOM 1697 0 VAL A 246 34.285 29.250 44.797 1.00 19.93 A O

ATOM 1698 N LEU A 247 33.093 30.720 46.030 1.00 20.14 A N

ATOM 1699 CA LEU A 247 33.716 30.388 47.312 1.00 18.91 A C

ATOM 1700 CB LEU A 247 33.084 31.246 48.415 1.00 19.92 A C

ATOM 1701 CG LEU A 247 33.429 30.747 49.810 1.00 22.16 A C

ATOM 1702 CDl LEU A 247 34.924 30.909 50.050 1.00 22.30 A C ATOM 1703 CD2 LEU A 247 32.604 31.482 50.839 1.00 24.26 A C

ATOM 1704 C LEU A 247 33.512 28.898 47.635 1.00 18.38 A C

ATOM 1705 O LEU A 247 34.468 28.168 47.884 1.00 19.50 A O

ATOM 1706 N ALA A 248 32.254 28.454 47.609 1.00 19.50 A N

ATOM 1707 CA ALA A 248 31.907 27.069 47.903 1.00 19.25 A C

ATOM 1708 CB ALA A 248 30.421 26.861 47.754 1.00 20.42 A C

ATOM 1709 C ALA A 248 32.661 26.139 46.968 1.00 20.69 A C

ATOM 1710 O ALA A 248 33.125 25.088 47.385 1.00 22.26 A O

ATOM 1711 N GLU A 249 32.781 26.549 45.706 1.00 20.13 A N

ATOM 1712 CA GLU A 249 33.480 25.782 44.665 1.00 20.03 A C

ATOM 1713 CB GLU A 249 33.270 26.471 43.318 1.00 18.13 A C

ATOM 1714 CG GLU A 249 34.094 25.902 42.190 1.00 16.32 A C

ATOM 1715 CD GLU A 249 33.549 26.339 40.833 1.00 22.40 A C

ATOM 1716 OEI GLU A 249 32.363 26.786 40.773 1.00 21.31 A O

ATOM 1717 OE2 GLU A 249 34.304 26.225 39.829 1.00 26.86 A O

ATOM 1718 C GLU A 249 34.987 25.668 44.926 1.00 22.17 A C

ATOM 1719 O GLU A 249 35.603 24.631 44.653 1.00 22.61 A O

ATOM 1720 N LEU A 250 35.579 26.764 45.415 1.00 24.09 A N

ATOM 1721 CA LEU A 250 37.010 26.816 45.722 1.00 22.80 A C

ATOM 1722 CB LEU A 250 37.439 28.257 46.020 1.00 23.36 A C

ATOM 1723 CG LEU A 250 37.397 29.299 44.895 1.00 22.14 A C ATOM 1724 CDl LEU A 250 37.795 30.638 45.458 1.00 21.99 A C

ATOM 1725 CD2 LEU A 250 38.363 28.897 43.756 1.00 23.96 A C

ATOM 1726 C LEU A 250 37.306 25.915 46.909 1.00 23.35 A C

ATOM 1727 O LEU A 250 38.418 25.390 47.047 1.00 22.51 A O

ATOM 1728 N LEU A 251 36.297 25.757 47.768 1.00 25.45 A N

ATOM 1729 CA LEU A 251 36.374 24.902 48.955 1.00 26.07 A C

ATOM 1730 CB LEU A 251 35.331 25.338 49.984 1.00 22.67 A C

ATOM 1731 CG LEU A 251 35.513 26.709 50.651 1.00 20.92 A C

ATOM 1732 CDl LEU A 251 34.414 26.949 51.674 1.00 18.65 A C

ATOM 1733 CD2 LEU A 251 36.876 26.800 51.314 1.00 19.51 A C

ATOM 1734 C LEU A 251 36.145 23.421 48.608 1.00 28.24 A C

ATOM 1735 O LEU A 251 36.866 22.544 49.092 1.00 31.53 A O

ATOM 1736 N LEU A 252 35.154 23.152 47.761 1.00 28.65 A N

ATOM 1737 CA LEU A 252 34.807 21.783 47.367 1.00 28.70 A C

ATOM 1738 CB LEU A 252 33.374 21.703 46.819 1.00 29.15 A C

ATOM 1739 CG LEU A 252 32.184 21.983 47.734 1.00 32.55 A C

ATOM 1740 CDl LEU A 252 30.921 22.157 46.891 1.00 31.58 A C

ATOM 1741 CD2 LEU A 252 32.018 20.853 48.731 1.00 32.33 A C .

ATOM 1742 C LEU A 252 35.716 21.224 46.306 1.00 28.03 A C

ATOM 1743 O LEU A 252 35.969 20.017 46.278 1.00 28.89 A O

ATOM 1744 N GLY A 253 36.163 22.093 45.406 1.00 27.05 A N ATOM 1745 CA GLY A 253 37.001 21.644 44.311 1.00 26.54 A C

ATOM 1746 C GLY A 253 36.158 21.287 43.082 1.00 26.63 A C

ATOM 1747 O GLY A 253 36.624 20.624 42.159 1.00 28.26 A O

ATOM 1748 N GLN A 254 34.902 21.719 43.086 1.00 26.69 A N

ATOM 1749 CA GLN A 254 33.948 21.483 41.998 1.00 28.53 A C

ATOM 1750 CB GLN A 254 33.485 20.024 41.980 1.00 31.61 A C

ATOM 1751 CG GLN A 254 32.590 19.627 43.135 1.00 34.67 A C

ATOM 1752 CD GLN A 254 32.630 18.139 43.398 1.00 38.01 A C

ATOM 1753 OE1 GLN A 254 31.888 17.378 42.788 1.00 42.67 A O

ATOM 1754 NE2 GLN A 254 33.505 17.714 44.311 1.00 38.91 A N

ATOM 1755 C GLN A 254 32.760 22.415 42.273 1.00 27.95 A C

ATOM 1756 0 GLN A 254 32.516 22.802 43.422 1.00 31.13 A O

ATOM 1757 N PRO A 255 32.037 22.830 41.230 1.00 25.57 A N

ATOM 1758 CD PRO A 255 32.218 22.606 39.790 1.00 24.89 A C

ATOM 1759 CA PRO A 255 30.909 23.730 41.500 1.00 25.85 A C

ATOM 1760 CB PRO A 255 30.299 23.964 40.110 1.00 24.39 A C

ATOM 1761 CG PRO A 255 30.817 22.807 39.279 1.00 26.35 A C

ATOM 1762 C PRO A 255 29.933 23.125 42.482 1.00 25.58 A C

ATOM 1763 O PRO A 255 29.694 21.928 42.441 1.00 27.24 A O

ATOM 1764 N ILE A 256 29.385 23.945 43.374 1.00 24.44 A N

ATOM 1765 CA ILE A 256 28.442 23.425 44.360 1.00 22.49 A C ATOM 1766 CB ILE A 256 28.355 24.338 45.647 1.00 23.25 A C

ATOM 1767 CG2 ILE A 256 27.993 25.772 45.307 1.00 21.43 A C

ATOM 1768 CGI ILE A 256 27.369 23.740 46.669 1.00 23.68 A C

ATOM 1769 CDl ILE A 256 27.268 24.535 47.989 1.00 22.45 A C

ATOM 1770 C ILE A 256 27.060 23.105 43.786 1.00 22.05 A C

ATOM 1771 O ILE A 256 26.447 22.117 44.167 1.00 20.94 A O

ATOM 1772 N PHE A 257 26.590 23.914 42.841 1.00 21.81 A N

ATOM 1773 CA PHE A 257 25.282 23.697 42.220 1.00 22.95 A C

ATOM 1774 CB PHE A 257 24.378 24.907 42.464 1.00 20.86 A C

ATOM 1775 CG PHE A 257 24.210 25.276 43.924 1.00 21.19 A C

ATOM 1776 CDl PHE A 257 23.809 24.326 44.862 1.00 23.12 A C

ATOM 1777 CD2 PHE A 257 24.375 26.593 44.332 1.00 20.95 A C

ATOM 1778 CE1 PHE A 257 23.567 24.690 46.178 1.00 23.71 A C

ATOM 1779 CE2 PHE A 257 24.142 26.970 45.630 1.00 22.20 A C

ATOM 1780 CZ PHE A 257 23.735 26.018 46.559 1.00 24.57 A C

ATOM 1781 C PHE A 257 25.350 23.422 40.686 1.00 23.79 A C

ATOM 1782 0 PHE A 257 25.110 24.307 39.868 1.00 24.10 A O

ATOM 1783 N PRO A 258 25.659 22.189 40.287 1.00 23.31 A N

ATOM 1784 CD PRO A 258 26.239 21.067 41.047 1.00 22.47 A C

ATOM 1785 CA PRO A 258 25.724 21.936 38.859 1.00 24.12 A C

ATOM 1786 CB PRO A 258 26.736 20.797 38.786 1.00 22.05 A C ATOM 1787 CG PRO A 258 26.394 20.001 39.992 1.00 22.01 A C

ATOM 1788 C PRO A 258 24.382 21.575 38.200 1.00 27.03 A C

ATOM 1789 O PRO A 258 24.158 20.434 37.809 1.00 31.26 A O

ATOM 1790 N GLY A 259 23.515 22.556 38.006 1.00 28.00 A N

ATOM 1791 CA GLY A 259 22.243 22.272 37.369 1.00 28.12 A C

ATOM 1792 C GLY A 259 22.403 21.903 35.904 1.00 30.21 A C

ATOM 1793 O GLY A 259 23.404 22.251 35.262 1.00 28.55 A O

ATOM 1794 N ASP A 260 21.417 21.182 35.381 1.00 33.14 A N

ATOM 1795 CA ASP A 260 21.411 20.746 33.979 1.00 36.83 A C

ATOM 1796 CB ASP A 260 20.973 19.295 33.879 1.00 39.67 A C

ATOM 1797 CG ASP A 260 22.046 18.338 34.321 1.00 43.41 A C

ATOM 1798 OD1 ASP A 260 21.697 17.184 34.641 1.00 49.07 A O

ATOM 1799 OD2 ASP A 260 23.236 18.724 34.338 1.00 45.58 A O

ATOM 1800 C ASP A 260 20.471 21.592 33.127 1.00 36.78 A C

ATOM 1801 O ASP A 260 20.449 21.480 31.897 1.00 37.91 A O

ATOM 1802 N SER A 261 19.702 22.437 33.802 1.00 34.36 A N

ATOM 1803 CA SER A 261 18.747 23.313 33.157 1.00 34.33 A C

ATOM 1804 CB SER A 261 17.524 22.510 32.747 1.00 35.79 A C

ATOM 1805 OG SER A 261 16.936 21.933 33.908 1.00 36.67 A O

ATOM 1806 C SER A 261 18.360 24.323 34.230 1.00 35.39 A C

ATOM 1807 O SER A 261 18.766 24.184 35.385 1.00 37.88 A O ATOM 1808 N GLY A 262 17.566 25.322 33.859 1.00 34.13 A N

ATOM 1809 CA GLY A 262 17.155 26.331 34.814 1.00 32.25 A C

ATOM 1810 C GLY A 262 16.491 25.729 36.037 1.00 31.53 A C

ATOM 1811 O GLY A 262 16.791 26.120 37.163 1.00 31.96 A O

ATOM 1812 N VAL A 263 15.603 24.762 35.812 1.00 31.41 A N

ATOM 1813 CA VAL A 263 14.893 24.095 36.906 1.00 31.51 A C

ATOM 1814 CB VAL A 263 13.661 23.270 36.394 1.00 31.95 A C

ATOM 1815 CGI VAL A 263 12.830 22.774 37.579 1.00 29.08 A C

ATOM 1816 CG2 VAL A 263 12.815 24.094 35.428 1.00 31.08 A C

ATOM 1817 C VAL A 263 15.798 23.165 37.734 1.00 30.50 A C

ATOM 1818 O VAL A 263 15.784 23.211 38.967 1.00 29.12 A O

ATOM 1819 N ASP A 264 16.567 22.309 37.067 1.00 29.87 A N

ATOM 1820 CA ASP A 264 17.433 21.400 37.805 1.00 32.22 A C

ATOM 1821 CB ASP A 264 18.203 20.454 36.879 1.00 32.96 A C

ATOM 1822 CG ASP A 264 19.056 19.454 37.659 1.00 35.53 A C

ATOM 1823 OD1 ASP A 264 18.565 18.852 38.648 1.00 38.23 A O

ATOM 1824 OD2 ASP A 264 20.237 19.293 37.306 1.00 36.58 A O

ATOM 1825 C ASP A 264 18.405 22.184 38.669 1.00 32.04 A C

ATOM 1826 O ASP A 264 18.973 21.654 39.638 1.00 30.30 A O

ATOM 1827 N GLN A 265 18.615 23.442 38.288 1.00 32.04 A N

ATOM 1828 CA GLN A 265 19.511 24.327 39.032 1.00 32.07 A C ATOM 1829 CB GLN A 265 19.708 25.656 38.274 1.00 29.80 A C

ATOM 1830 CG GLN A 265 20.699 26.629 38.932 1.00 27.71 A C

ATOM 1831 CD GLN A 265 22.093 26.057 39.066 1.00 26.15 A C

ATOM 1832 OE1 GLN A 265 22.783 26.309 40.055 1.00 28.18 A O

ATOM 1833 NE2 GLN A 265 22.520 25.291 38.068 1.00 26.11 A N

ATOM 1834 C GLN A 265 18.941 24.562 40.443 1.00 30.56 A C

ATOM 1835 O GLN A 265 19.658 24.440 41.434 1.00 28.26 A O

ATOM 1836 N LEU A 266 17.632 24.829 40.508 1.00 31.85 A N

ATOM 1837 CA LEU A 266 16.921 25.065 41.771 1.00 33.17 A C

ATOM 1838 CB LEU A 266 15.491 25.576 41.479 1.00 34.38 A C

ATOM 1839 CG LEU A 266 14.570 25.869 42.685 1.00 37.81 A C

ATOM 1840 CDl LEU A 266 15.223 26.855 43.646 1.00 37.84 A C

ATOM 1841 CD2 LEU A 266 13.206 26.390 42.217 1.00 36.24 A C

ATOM 1842 C LEU A 266 16.879 23.782 42.620 1.00 31.08 A C

ATOM 1843 0 LEU A 266 16.986 23.825 43.840 1.00 31.37 A O

ATOM 1844 N VAL A 267 16.726 22.648 41.937 1.00 31.74 A N

ATOM 1845 CA VAL A 267 16.673 21.320 42.545 1.00 29.73 A C

ATOM 1846 CB VAL A 267 16.413 20.206 41.462 1.00 29.26 A C

ATOM 1847 CGI VAL A 267 16.626 18.801 42.068 1.00 29.23 A C

ATOM 1848 CG2 VAL A 267 14.995 20.331 40.889 1.00 24.78 A C

ATOM 1849 C VAL A 267 18.000 21.029 43.213 1.00 29.61 A C ATOM 1850 O VAL A 267 18.045 20.448 44.294 1.00 32.14 A O

ATOM 1851 N GLU A 268 19.067 21.430 42.524 1.00 27.95 A N

ATOM 1852 CA GLU A 268 20.456 21.267 42.937 1.00 28.15 A C

ATOM 1853 CB GLU A 268 21.344 21.686 41.776 1.00 28.98 A C

ATOM 1854 CG GLU A 268 22.701 21.108 41.825 1.00 35.29 A C

ATOM 1855 CD GLU A 268 22.684 19.614 41.688 1.00 37.88 A C

ATOM 1856 OEI GLU A 268 21.809 19.105 40.954 1.00 43.08 A O

ATOM 1857 OE2 GLU A 268 23.547 18.954 42.305 1.00 39.33 A O

ATOM 1858 C GLU A 268 20.770 22.120 44.171 1.00 28.18 A C

ATOM 1859 O GLU A 268 21.594 21.752 45.027 1.00 28.17 A O

ATOM 1860 N ILE A 269 20.134 23.290 44.208 1.00 30.49 A N

ATOM 1861 CA ILE A 269 20.232 24.260 45.309 1.00 30.41 A C

ATOM 1862 CB ILE A 269 19.659 25.642 44.881 1.00 29.62 A C

ATOM 1863 CG2 ILE A 269 19.606 26.579 46.058 1.00 32.02 A C

ATOM 1864 CGI ILE A 269 20.531 26.265 43.793 1.00 26.27 A C

ATOM 1865 CDl ILE A 269 19.945 27.497 43.173 1.00 25.57 A C

ATOM 1866 C ILE A 269 19.400 23.745 46.492 1.00 30.30 A C

ATOM 1867 0 ILE A 269 19.774 23.920 47.649 1.00 32.10 A O

ATOM 1868 N ILE A 270 18.244 23.167 46.179 1.00 29.33 A N

ATOM 1869 CA ILE A 270 17.365 22.596 47.184 1.00 31.81 A C

ATOM 1870 CB ILE A 270 15.995 22.145 46.542 1.00 30.88 A C ATOM 1871 CG2 ILE A 270 15.236 21.203 47.491 1.00 27.47 A C

ATOM 1872 CGI ILE A 270 15.161 23.397 46.187 1.00 28.47 A C

ATOM 1873 CDl ILE A 270 13.913 23.170 45.394 1.00 26.46 A C

ATOM 1874 C ILE A 270 18.070 21.453 47.934 1.00 32.83 A C

ATOM 1875 O ILE A 270 17.938 21.325 49.151 1.00 33.58 A O

ATOM 1876 N LYS A 271 18.905 20.698 47.222 1.00 33.61 A N

ATOM 1877 CA LYS A 271 19.647 19.578 47.801 1.00 34.70 A C

ATOM 1878 CB LYS A 271 20.400 18.820 46.697 1.00 36.76 A C

ATOM 1879 CG LYS A 271 19.505 18.100 45.683 1.00 38.77 A C

ATOM 1880 CD LYS A 271 20.300 17.075 44.863 1.00 41.89 A C

ATOM 1881 CE LYS A 271 19.394 16.243 43.942 1.00 46.13 A C

ATOM 1882 NZ LYS A 271 18.949 16.931 42.676 1.00 48.67 A N

ATOM 1883 C LYS A 271 20.634 19.981 48.908 1.00 36.40 A C

ATOM 1884 O LYS A 271 21.272 19.132 49.545 1.00 36.44 A O

ATOM 1885 N VAL A 272 20.781 21.280 49.123 1.00 36.74 A N

ATOM 1886 CA VAL A 272 21.700 21.764 50.140 1.00 36.41 A C

ATOM 1887 CB VAL A 272 23.044 22.282 49.496 1.00 35.51 A C

ATOM 1888 CGI VAL A 272 23.790 23.204 50.449 1.00 36.23 A C

ATOM 1889 CG2 VAL A 272 23.946 21.098 49.133 1.00 35.03 A C

ATOM 1890 C VAL A 272 20.996 22.824 50.985 1.00 36.49 A C

ATOM 1891 O VAL A 272 21.031 22.783 52.211 1.00 36.63 A O ATOM 1892 N LEU A 273 20.283 23.729 50.335 1.00 36.62 A N

ATOM 1893 CA LEU A 273 19.572 24.769 51.069 1.00 37.50 A C

ATOM 1894 CB LEU A 273 19.462 26.018 50.200 1.00 36.90 A C

ATOM 1895 CG LEU A 273 20.617 26.976 50.397 1.00 37.23 A C

ATOM 1896 CDl LEU A 273 20.421 28.228 49.549 1.00 38.59 A C

ATOM 1897 CD2 LEU A 273 20.629 27.330 51.891 1.00 40.42 A C

ATOM 1898 C LEU A 273 18.178 24.339 51.545 1.00 39.19 A C

ATOM 1899 O LEU A 273 17.552 25.000 52.376 1.00 39.97 A O

ATOM 1900 N GLY A 274 17.686 23.228 51.010 1.00 39.40 A N

ATOM 1901 CA GLY A 274 16.362 22.778 51.380 1.00 37.58 A C

ATOM 1902 C GLY A 274 15.333 23.604 50.653 1.00 37.25 A C

ATOM 1903 O GLY A 274 15.651 24.645 50.097 1.00 37.82 A O

ATOM 1904 N THR A 275 14.090 23.140 50.657 1.00 39.11 A N

ATOM 1905 CA THR A 275 13.010 23.847 49.987 1.00 38.46 A C

ATOM 1906 CB THR A 275 11.737 23.033 50.071 1.00 39.29 A C

ATOM 1907 OG1 THR A 275 12.048 21.682 49.718 1.00 41.41 A O

ATOM 1908 CG2 THR A 275 10.689 23.559 49.091 1.00 43.20 A C

ATOM 1909 C THR A 275 12.793 25.208 50.605 1.00 37.05 A C

ATOM 1910 O THR A 275 12.752 25.343 51.815 1.00 37.12 A O

ATOM 1911 N PRO A 276 12.722 26.249 49.776 1.00 39.10 A N

ATOM 1912 CD PRO A 276 12.734 26.238 48.305 1.00 38.36 A C ATOM 1913 CA PRO A 276 12.512 27.606 50.288 1.00 43.26 A C

ATOM 1914 CB PRO A 276 12.592 28.460 49.020 1.00 41.50 A C

ATOM 1915 CG PRO A 276 12.037 27.542 47.967 1.00 38.04 A C

ATOM 1916 C PRO A 276 11.123 27.695 50.906 1.00 47.74 A C

ATOM 1917 O PRO A 276 10.223 26.959 50.494 1.00 49.89 A O

ATOM 1918 N THR A 277 10.948 28.552 51.912 1.00 50.49 A N

ATOM 1919 CA THR A 277 9.631 28.702 52.521 1.00 52.46 A C

ATOM 1920 CB THR A 277 9.679 29.333 53.930 1.00 50.91 A C

ATOM 1921 OG1 THR A 277 10.105 30.696 53.837 1.00 49.30 A O

ATOM 1922 CG2 THR A 277 10.599 28.557 54.844 1.00 48.81 A C

ATOM 1923 C THR A 277 8.783 29.593 51.613 1.00 55.88 A C

ATOM 1924 0 THR A 277 9.286 30.160 50.633 1.00 56.73 A O

ATOM 1925 N ARG A 278 7.493 29.688 51.926 1.00 58.65 A N

ATOM 1926 CA ARG A 278 6.573 30.504 51.144 1.00 60.44 A C

ATOM 1927 CB ARG A 278 5.120 30.273 51.598 1.00 64.53 A C

ATOM 1928 CG ARG A 278 4.900 30.160 53.119 1.00 68.29 A C

ATOM 1929 CD ARG A 278 3.423 29.840 53.454 1.00 70.77 A C

ATOM 1930 NE ARG A 278 2.494 30.939 53.152 1.00 71.15 A N

ATOM 1931 CZ ARG A 278 1.837 31.094 52.002 1.00 71.31 A C

ATOM 1932 NHl ARG A 278 1.994 30.222 51.012 1.00 71.08 A N

ATOM 1933 NH2 ARG A 278 1.014 32.126 51.846 1.00 71.56 A N ATOM 1934 C ARG A 278 6.953 31.978 51.226 1.00 59.87 A C

ATOM 1935 O ARG A 278 6.760 32.726 50.270 1.00 58.41 A O

ATOM 1936 N GLU A 279 7.475 32.392 52.380 1.00 60.02 A N

ATOM 1937 CA GLU A 279 7.908 33.771 52.555 1.00 60.57 A C

ATOM 1938 CB GLU A 279 8.051 34.129 54.045 1.00 62.28 A C

ATOM 1939 CG GLU A 279 8.494 35.584 54.293 1.00 65.13 A C

ATOM 1940 CD GLU A 279 7.628 36.622 53.548 1.00 67.00 A C

ATOM 1941 OE1 GLU A 279 8.186 37.605 53.001 1.00 65.40 A O

ATOM 1942 OE2 GLU A 279 6.386 36.455 53.508 1.00 68.90 A O

ATOM 1943 C GLU A 279 9.243 33.971 51.819 1.00 59.65 A C

ATOM 1944 O GLU A 279 9.531 35.076 51.347 1.00 59.83 A O

ATOM 1945 N GLN A 280 10.053 32.906 51.731 1.00 57.19 A N

ATOM 1946 CA GLN A 280 11.344 32.962 51.031 1.00 52.60 A C

ATOM 1947 CB GLN A 280 12.228 31.745 51.353 1.00 50.20 A C

ATOM 1948 CG GLN A 280 13.209 31.992 52.500 1.00 44.34 A C

ATOM 1949 CD GLN A 280 13.961 30.749 52.950 1.00 43.42 A C

ATOM 1950 OE1 GLN A 280 13.525 29.614 52.726 1.00 41.23 A O

ATOM 1951 NE2 GLN A 280 15.097 30.962 53.616 1.00 43.42 A N

ATOM 1952 C GLN A 280 11.149 33.116 49.526 1.00 52.70 A C

ATOM 1953 O GLN A 280 11.942 33.783 48.870 1.00 53.18 A O

ATOM 1954 N ILE A 281 10.090 32.512 48.988 1.00 52.81 A N ATOM 1955 CA ILE A 281 9.769 32.626 47.564 1.00 52.86 A C

ATOM 1956 CB ILE A 281 8.693 31.593 47.124 1.00 51.64 A C

ATOM 1957 CG2 ILE A 281 8.363 31.769 45.637 1.00 49.72 A C

ATOM 1958 CGI ILE A 281 9.180 30.164 47.418 1.00 51.24 A C

ATOM 1959 CDl ILE A 281 8.203 29.066 47.052 1.00 47.72 A C

ATOM 1960 C ILE A 281 9.217 34.028 47.340 1.00 54.71 A C

ATOM 1961 O ILE A 281 9.445 34.641 46.299 1.00 54.52 A O

ATOM 1962 N ARG A 282 8.503 34.523 48.348 1.00 57.89 A N

ATOM 1963 CA ARG A 282 7.907 35.858 48.339 1.00 61.57 A C

ATOM 1964 CB ARG A 282 7.115 36.065 49.649 1.00 65.77 A C

ATOM 1965 CG ARG A 282 6.304 37.382 49.785 1.00 70.81 A C

ATOM 1966 CD ARG A 282 4.780 37.122 49.924 1.00 74.24 A C

ATOM 1967 NE ARG A 282 4.174 36.704 48.654 1.00 77.26 A N

ATOM 1968 CZ ARG A 282 3.795 35.461 48.363 1.00 78.31 A C

ATOM 1969 NHl ARG A 282 3.942 34.490 49.261 1.00 77.99 A N

ATOM 1970 NH2 ARG A 282 3.327 35.182 47.147 1.00 79.39 A N

ATOM 1971 C ARG A 282 9.030 36.898 48.223 1.00 62.70 A C

ATOM 1972 0 ARG A 282 8.943 37.837 47.415 1.00 61.98 A O

ATOM 1973 N GLU A 283 10.077 36.707 49.035 1.00 63.46 A N

ATOM 1974 CA GLU A 283 11.253 37.586 49.079 1.00 63.98 A C

ATOM 1975 CB GLU A 283 12.276 37.027 50.069 1.00 65.14 A C ATOM 1976 CG GLU A 283 11.714 36.699 51.434 1.00 69.02 A C

ATOM 1977 CD GLU A 283 11.867 37.845 52.414 1.00 72.19 A C

ATOM 1978 OEI GLU A 283 11.893 37.576 53.641 1.00 72.91 A O

ATOM 1979 OE2 GLU A 283 11.976 39.010 51.955 1.00 73.68 A O

ATOM 1980 C GLU A 283 11.908 37.678 47.699 1.00 64.28 A C

ATOM 1981 0 GLU A 283 12.278 38.764 47.238 1.00 64.39 A O

ATOM 1982 N MET A 284 12.076 36.517 47.067 1.00 64.56 A N

ATOM 1983 CA MET A 284 12.685 36.408 45.744 1.00 64.45 A C

ATOM 1984 CB MET A 284 13.048 34.960 45.446 1.00 63.90 A C

ATOM 1985 CG MET A 284 14.116 34.406 46.337 1.00 62.32 A C

ATOM 1986 SD MET A 284 14.526 32.763 45.814 1.00 61.63 A S

ATOM 1987 CE MET A 284 13.713 31.797 47.077 1.00 62.42 A C

ATOM 1988 C MET A 284 11.764 36.917 44.654 1.00 65.86 A C

ATOM 1989 0 MET A 284 12.198 37.634 43.754 1.00 67.29 A O

ATOM 1990 N ASN A 285 10.509 36.482 44.687 1.00 66.58 A N

ATOM 1991 CA ASN A 285 9.545 36.941 43.701 1.00 67.61 A C

ATOM 1992 CB ASN A 285 9.253 35.866 42.658 1.00 69.13 A C

ATOM 1993 CG ASN A 285 8.518 36.423 41.447 1.00 69.68 A C

ATOM 1994 OD1 ASN A 285 8.879 36.150 40.296 1.00 68.82 A O

ATOM 1995 ND2 ASN A 285 7.491 37.228 41.704 1.00 71.06 A N

ATOM . 1996 C ASN A 285 8.264 37.357 44.397 1.00 68.27 A C ATOM 1997 0 ASN A 285 7.546 36.528 44.962 1.00 67.84 A O

ATOM 1998 N PRO A 286 7.969 38.664 44.372 1.00 69.70 A N

ATOM 1999 CD PRO A 286 8.764 39.688 43.669 1.00 70.02 A C

ATOM 2000 CA PRO A 286 6.778 39.255 44.989 1.00 71.26 A C

ATOM 2001 CB PRO A 286 6.908 40.740 44.617 1.00 71.42 A C

ATOM 2002 CG PRO A 286 7.723 40.722 43.334 1.00 70.10 A C

ATOM 2003 C PRO A 286 5.446 38.648 44.513 1.00 71.88 A C

ATOM 2004 O PRO A 286 4.474 38.564 45.269 1.00 71.95 A O

ATOM 2005 N ASN A 287 5.414 38.185 43.273 1.00 71.98 A N

ATOM 2006 CA ASN A 287 4.194 37.608 42.756 1.00 73.66 A C

ATOM 2007 CB ASN A 287 3.628 38.509 41.670 1.00 74.28 A C

ATOM 2008 CG ASN A 287 4.680 38.947 40.688 1.00 75.29 A C

ATOM 2009 OD1 ASN A 287 5.302 39.998 40.860 1.00 75.80 A O

ATOM 2010 ND2 ASN A 287 4.910 38.131 39.663 1.00 75.24 A N

ATOM 2011 C ASN A 287 4.366 36.194 42.226 1.00 74.95 A C

ATOM 2012 O ASN A 287 4.551 35.995 41.025 1.00 73.70 A O

ATOM 2013 N TYR A 288 4.321 35.214 43.131 1.00 77.12 A N

ATOM 2014 CA TYR A 288 4.437 33.817 42.728 1.00 78.50 A C

ATOM 2015 CB TYR A 288 5.728 33.176 43.243 1.00 76.75 A C

ATOM 2016 CG TYR A 288 6.290 32.211 42.229 1.00 75.51 A C

ATOM 2017 CDl TYR A 288 6.578 32.638 40.931 1.00 75.77 A C ATOM 2018 CE1 TYR A 288 7.010 31.746 39.955 1.00 73.80 A C

ATOM 2019 CD2 TYR A 288 6.459 30.865 42.529 1.00 74.29 A C

ATOM 2020 CE2 TYR A 288 6.891 29.965 41.561 1.00 72.41 A C

ATOM 2021 CZ TYR A 288 7.163 30.411 40.278 1.00 72.58 A C

ATOM 2022 OH TYR A 288 7.581 29.525 39.312 1.00 72.10 A O

ATOM 2023 C TYR A 288 3.219 32.977 43.120 1.00 80.65 A C

ATOM 2024 O TYR A 288 2.452 33.325 44.027 1.00 81.49 A O

ATOM 2025 N THR A 289 3.033 31.875 42.408 1.00 82.25 A N

ATOM 2026 CA THR A 289 1.900 31.006 42.663 1.00 84.05 A C

ATOM 2027 CB THR A 289 0.654 31.542 41.945 1.00 85.30 A C

ATOM 2028 OG1 THR A 289 1.064 32.369 40.844 1.00 84.50 A O

ATOM 2029 CG2 THR A 289 -0.207 32.355 42.913 1.00 85.63 A C

ATOM 2030 C THR A 289 2.163 29.550 42.274 1.00 85.09 A C

ATOM 2031 O THR A 289 1.606 29.024 41.298 1.00 84.94 A O

ATOM 2032 N GLU A 290 3.021 28.916 43.065 1.00 86.20 A N

ATOM 2033 CA GLU A 290 3.403 27.521 42.889 1.00 87.69 A C

ATOM 2034 CB GLU A 290 4.891 27.417 42.546 1.00 87.88 A C

ATOM 2035 CG GLU A 290 5.544 26.100 42.971 1.00 87.42 A C

ATOM 2036 CD GLU A 290 6.685 26.306 43.954 1.00 87.10 A C

ATOM 2037 OEI GLU A 290 7.330 27.374 43.911 1.00 87.45 A O

ATOM 2038 OE2 GLU A 290 6.942 25.399 44.772 1.00 86.98 A O ATOM 2039 C GLU A 290 3.164 26.860 44.230 1.00 89.30 A C

ATOM 2040 O GLU A 290 2.168 26.171 44.432 1.00 90.44 A O

ATOM 2041 N PHE A 291 4.101 27.084 45.144 1.00 90.96 A N

ATOM 2042 CA PHE A 291 4.033 26.557 46.502 1.00 92.39 A C

ATOM 2043 CB PHE A 291 2.932 27.304 47.278 1.00 93.84 A C

ATOM 2044 CG PHE A 291 3.105 28.816 47.263 1.00 95.33 A C

ATOM 2045 CDl PHE A 291 2.664 29.573 46.174 1.00 95.95 A C

ATOM 2046 CD2 PHE A 291 3.756 29.471 48.309 1.00 95.47 A C

ATOM 2047 CE1 PHE A 291 2.874 30.952 46.120 1.00 96.04 A C

ATOM 2048 CE2 PHE A 291 3.971 30.854 48.266 1.00 95.86 A C

ATOM 2049 CZ PHE A 291 3.529 31.594 47.167 1.00 95.84 A C

ATOM 2050 C PHE A 291 3.923 25.025 46.651 1.00 92.34 A C

ATOM 2051 O PHE A 291 3.186 24.523 47.500 1.00 91.41 A O

ATOM 2052 N LYS A 292 4.678 24.292 45.829 1.00 93.11 A N

ATOM 2053 CA LYS A 292 4.697 22.827 45.895 1.00 94.07 A C

ATOM 2054 CB LYS A 292 4.043 22.183 44.667 1.00 93.74 A C

ATOM 2055 CG LYS A 292 2.512 22.195 44.708 1.00 94.62 A C

ATOM 2056 CD LYS A 292 1.931 21.395 45.890 1.00 93.86 A C

ATOM 2057 CE LYS A 292 1.963 19.885 45.638 1.00 93.49 A C

ATOM 2058 NZ LYS A 292 1.251 19.097 46.695 1.00 92.59 A N

ATOM 2059 C LYS A 292 6.095 22.247 46.138 1.00 94.39 A C ATOM 2060 O LYS A 292 6.958 22.918 46.715 1.00 95.11 A O

ATOM 2061 N PHE A 293 6.325 21.019 45.670 1.00 93.89 A N

ATOM 2062 CA PHE A 293 7.600 20.315 45.886 1.00 93.12 A C

ATOM 2063 CB PHE A 293 8.808 21.208 45.536 1.00 91.37 A C

ATOM 2064 CG PHE A 293 10.052 20.441 45.114 1.00 88.10 A C

ATOM 2065 CDl PHE A 293 10.728 20.789 43.947 1.00 85.71 A C

ATOM 2066 CD2 PHE A 293 10.569 19.411 45.900 1.00 87.28 A C

ATOM 2067 CE1 PHE A 293 11.886 20.124 43.566 1.00 84.42 A C

ATOM 2068 CE2 PHE A 293 11.733 18.738 45.524 1.00 85.93 A C

ATOM 2069 CZ PHE A 293 12.393 19.102 44.360 1.00 84.27 A C

ATOM 2070 C PHE A 293 7.590 19.964 47.380 1.00 93.58 A C

ATOM 2071 O PHE A 293 7.380 20.832 48.232 1.00 93.31 A O

ATOM 2072 N PRO A 294 7.772 18.677 47.715 1.00 94.65 A N

ATOM 2073 CD PRO A 294 8.138 17.567 46.813 1.00 94.70 A C

ATOM 2074 CA PRO A 294 7.766 18.250 49.124 1.00 95.40 A C

ATOM 2075 CB PRO A 294 8.122 16.757 49.032 1.00 95.87 A C

ATOM 2076 CG PRO A 294 8.915 16.656 47.725 1.00 95.35 A C

ATOM 2077 C PRO A 294 8.738 19.038 50.013 1.00 95.26 A C

ATOM 2078 O PRO A 294 9.561 19.799 49.507 1.00 96.69 A O

ATOM 2079 N GLN A 295 8.636 18.872 51.331 1.00 93.87 A N

ATOM 2080 CA GLN A 295 9.536 19.578 52.245 1.00 91.58 A C ATOM 2081 CB GLN A 295 8.860 19.835 53.597 1.00 93.08 A C

ATOM 2082 CG GLN A 295 9.744 20.558 54.618 1.00 94.67 A C

ATOM 2083 CD GLN A 295 10.176 21.942 54.152 1.00 96.42 A C

ATOM 2084 OE1 GLN A 295 9.344 22.780 53.789 1.00 97.73 A O

ATOM 2085 NE2 GLN A 295 11.484 22.192 54.169 1.00 97.29 A N

ATOM 2086 C GLN A 295 10.875 18.855 52.463 1.00 89.73 A C

ATOM 2087 O GLN A 295 11.025 18.064 53.412 1.00 90.32 A O

ATOM 2088 N ILE A 296 11.825 19.111 51.558 1.00 86.50 A N

ATOM 2089 CA ILE A 296 13.173 18.548 51.629 1.00 82.27 A C

ATOM 2090 CB ILE A 296 13.877 18.594 50.250 1.00 80.67 A C

ATOM 2091 CG2 ILE A 296 15.247 17.945 50.332 1.00 79.90 A C

ATOM 2092 CGI ILE A 296 13.026 17.877 49.202 1.00 80.01 A C

ATOM 2093 CDl ILE A 296 12.703 16.432 49.541 1.00 80.62 A C

ATOM 2094 C ILE A 296 13.910 19.452 52.617 1.00 80.55 A C

ATOM 2095 O ILE A 296 13.809 20.680 52.538 1.00 78.56 A O

ATOM 2096 N LYS A 297 14.618 18.859 53.572 1.00 79.61 A N

ATOM 2097 CA LYS A 297 15.308 19.671 54.569 1.00 78.21 A C

ATOM 2098 CB LYS A 297 15.248 19.018 55.957 1.00 79.28 A C

ATOM 2099 CG LYS A 297 15.248 20.036 57.100 1.00 80.65 A C

ATOM 2100 CD LYS A 297 14.145 21.064 56.881 1.00 81.45 A C

ATOM 2101 CE LYS A 297 14.092 22.115 57.980 1.00 81.91 A C ATOM 2102 NZ LYS A 297 13.001 23.103 57.710 1.00 80.82 A N

ATOM 2103 C LYS A 297 16.742 20.034 54.205 1.00 76.12 A C

ATOM 2104 O LYS A 297 17.401 19.342 53.416 1.00 75.82 A O

ATOM 2105 N ALA A 298 17.205 21.144 54.776 1.00 73.08 A N

ATOM 2106 CA ALA A 298 18.549 21.639 54.532 1.00 69.06 A C

ATOM 2107 CB ALA A 298 18.721 23.008 55.147 1.00 68.63 A C

ATOM 2108 C ALA A 298 19.606 20.703 55.068 1.00 66.97 A C

ATOM 2109 O ALA A 298 19.516 20.214 56.194 1.00 65.72 A O

ATOM 2110 N HIS A 299 20.594 20.421 54.236 1.00 65.83 A N

ATOM 2111 CA HIS A 299 21.687 19.571 54.661 1.00 65.16 A C

ATOM 2112 CB HIS A 299 22.358 18.917 53.442 1.00 66.44 A C

ATOM 2113 CG HIS A 299 22.755 17.489 53.672 1.00 68.36 A C

ATOM 2114 CD2 HIS A 299 22.445 16.356 52.998 1.00 68.94 A C

ATOM 2115 ND1 HIS A 299 23.530 17.097 54.745 1.00 68.97 A N

ATOM 2116 CE1 HIS A 299 23.675 15.784 54.723 1.00 69.68 A C

ATOM 2117 NE2 HIS A 299 23.027 15.309 53.674 1.00 69.24 A N

ATOM 2118 C HIS A 299 22.671 20.486 55.417 1.00 62.98 A C

ATOM 2119 O HIS A 299 23.095 21.519 54.887 1.00 63.93 A O

ATOM 2120 N PRO A 300 23.003 20.147 56.679 1.00 59.13 A N

ATOM 2121 CD PRO A 300 22.665 18.881 57.338 1.00 57.19 A C

ATOM 2122 CA PRO A 300 23.928 20.930 57.514 1.00 56.39 A C ATOM 2123 CB PRO A 300 24.339 19.936 58.609 1.00 56.10 A C

ATOM 2124 CG PRO A 300 23.948 18.578 58.043 1.00 56.40 A C

ATOM 2125 C PRO A 300 25.136 21.465 56.749 1.00 53.76 A C

ATOM 2126 O PRO A 300 25.824 20.717 56.057 1.00 51.52 A O

ATOM 2127 N TRP A 301 25.387 22.766 56.877 1.00 53.44 A N

ATOM 2128 CA TRP A 301 26.498 23.399 56.167 1.00 53.15 A C

ATOM 2129 CB TRP A 301 26.569 24.892 56.488 1.00 54.73 A C

ATOM 2130 CG TRP A 301 25.691 25.757 55.617 1.00 57.29 A C

ATOM 2131 CD2 TRP A 301 25.791 25.931 54.194 1.00 57.65 A C

ATOM 2132 CE2 TRP A 301 24.757 26.809 53.804 1.00 58.15 A C

ATOM 2133 CE3 TRP A 301 26.647 25.425 53.212 1.00 58.15 A C

ATOM 2134 CDl TRP A 301 24.632 26.520 56.020 1.00 59.38 A C

ATOM 2135 NE1 TRP A 301 24.063 27.155 54.935 1.00 59.83 A N

ATOM 2136 CZ2 TRP A 301 24.560 27.188 52.472 1.00 58.11 A C

ATOM 2137 CZ3 TRP A 301 26.447 25.802 51.886 1.00 59.05 A C

ATOM 2138 CH2 TRP A 301 25.413 26.674 51.531 1.00 59.26 A C

ATOM 2139 C TRP A 301 27.848 22.752 56.431 1.00 52.73 A C

ATOM 2140 O TRP A 301 28.720 22.735 55.567 1.00 52.39 A O

ATOM 2141 N THR A 302 28.019 22.225 57.635 1.00 53.22 A N

ATOM 2142 CA THR A 302 29.267 21.586 58.022 1.00 53.06 A C

ATOM 2143 CB THR A 302 29.344 21.422 59.553 1.00 52.33 A C ATOM 2144 OG1 THR A 302 28.278 20.566 59.989 1.00 53.54 A O

ATOM 2145 CG2 THR A 302 29.199 22.784 60.241 1.00 51.05 A C

ATOM 2146 C THR A 302 29.422 20.220 57.360 1.00 54.26 A C

ATOM 2147 O THR A 302 30.537 19.712 57.262 1.00 55.39 A O

ATOM 2148 N LYS A 303 28.303 19.648 56.896 1.00 54.83 A N

ATOM 2149 CA LYS A 303 28.264 18.326 56.232 1.00 53.18 A C

ATOM 2150 CB LYS A 303 26.937 17.598 56.526 1.00 55.86 A C

ATOM 2151 CG LYS A 303 26.845 16.951 57.900 1.00 58.61 A C

ATOM 2152 CD LYS A 303 27.815 15.791 58.006 1.00 63.03 A C

ATOM 2153 CE LYS A 303 27.575 14.971 59.264 1.00 64.64 A C

ATOM 2154 NZ LYS A 303 28.453 13.764 59.289 1.00 65.98 A N

ATOM 2155 C LYS A 303 28.469 18.402 54.715 1.00 50.85 A C

ATOM 2156 O LYS A 303 28.839 17.405 54.080 1.00 49.92 A O

ATOM 2157 N VAL A 304 28.173 19.565 54.134 1.00 47.30 A N

ATOM 2158 CA VAL A 304 28.351 19.763 52.702 1.00 45.63 A C

ATOM 2159 CB VAL A 304 27.613 21.017 52.211 1.00 44.60 A C

ATOM 2160 CGI VAL A 304 27.938 22.179 53.085 1.00 46.51 A C

ATOM 2161 CG2 VAL A 304 27.978 21.314 50.775 1.00 43.54 A C

ATOM 2162 C VAL A 304 29.837 19.846 52.350 1.00 44.52 A C

ATOM 2163 O VAL A 304 30.284 19.281 51.356 1.00 44.39 A O

ATOM 2164 N PHE A 305 30.610 20.517 53.192 1.00 44.21 A N ATOM 2165 CA PHE A 305 32.042 20.645 52.956 1.00 44.80 A C

ATOM 2166 CB PHE A 305 32.530 22.006 53.438 1.00 42.07 A C

ATOM 2167 CG PHE A 305 31.864 23.156 52.744 1.00 39.78 A C

ATOM 2168 CDl PHE A 305 32.069 23.372 51.375 1.00 37.45 A C

ATOM 2169 CD2 PHE A 305 31.012 24.013 53.446 1.00 36.45 A C

ATOM 2170 CE1 PHE A 305 31.441 24.414 50.721 1.00 33.84 A C

ATOM 2171 CE2 PHE A 305 30.380 25.059 52.796 1.00 34.18 A C

ATOM 2172 CZ PHE A 305 30.597 25.256 51.429 1.00 34.04 A C

ATOM 2173 C PHE A 305 32.872 19.536 53.599 1.00 47.33 A C

ATOM 2174 O PHE A 305 32.428 18.866 54.536 1.00 48.48 A O

ATOM 2175 N ARG A 306 34.080 19.339 53.081 1.00 48.81 A N

ATOM 2176 CA ARG A 306 34.970 18.322 53.609 1.00 48.89 A C

ATOM 2177 CB ARG A 306 36.164 18.142 52.673 1.00 49.99 A C

ATOM 2178 CG ARG A 306 37.164 19.292 52.666 1.00 51.90 A C

ATOM 2179 CD ARG A 306 38.370 18.936 51.770 1.00 55.36 A C

ATOM 2180 NE ARG A 306 39.381 19.995 51.659 1.00 55.23 A N

ATOM 2181 CZ ARG A 306 40.363 20.198 52.533 1.00 54.45 A C

ATOM 2182 NHl ARG A 306 40.467 19.423 53.601 1.00 54.45 A N

ATOM 2183 NH2 ARG A 306 41.274 21.139 52.309 1.00 54.15 A N

ATOM 2184 C ARG A 306 35.475 18.714 54.992 1.00 49.49 A C

ATOM 2185 O ARG A 306 35.517 19.888 55.328 1.00 48.86 A O ATOM 2186 N PRO A 307 35.776 17.728 55.850 1.00 51.03 A N

ATOM 2187 CD PRO A 307 35.660 16.264 55.730 1.00 51.81 A C

ATOM 2188 CA PRO A 307 36.279 18.113 57.174 1.00 52.33 A C

ATOM 2189 CB PRO A 307 36.281 16.786 57.940 1.00 52.40 A C

ATOM 2190 CG PRO A 307 36.581 15.784 56.851 1.00 53.45 A C

ATOM 2191 C PRO A 307 37.698 18.629 56.932 1.00 53.22 A C

ATOM 2192 O PRO A 307 38.417 18.109 56.064 1.00 54.90 A O

ATOM 2193 N ARG A 308 38.084 19.656 57.682 1.00 53.43 A N

ATOM 2194 CA ARG A 308 39.395 20.296 57.556 1.00 53.93 A C

ATOM 2195 CB ARG A 308 40.343 19.516 56.628 1.00 56.89 A C

ATOM 2196 CG ARG A 308 41.721 19.150 57.240 1.00 62.21 A C

ATOM 2197 CD ARG A 308 41.670 17.934 58.189 1.00 66.15 A C

ATOM 2198 NE ARG A 308 41.220 18.277 59.545 1.00 69.51 A N

ATOM 2199 CZ ARG A 308 40.164 17.742 60.165 1.00 70.12 A C

ATOM 2200 NHl ARG A 308 39.410 16.821 59.568 1.00 70.90 A N

ATOM 2201 NH2 ARG A 308 39.874 18.109 61.404 1.00 70.42 A N

ATOM 2202 C ARG A 308 39.110 21.667 56.971 1.00 51.42 A C

ATOM 2203 O ARG A 308 40.017 22.479 56.808 1.00 53.93 A O

ATOM 2204 N THR A 309 37.835 21.886 56.636 1.00 48.02 A N

ATOM 2205 CA THR A 309 37.319 23.147 56.084 1.0043.15 A C

ATOM 2206 CB THR A 309 35.958 22.905 55.335 1.00 42.42 A C ATOM 2207 OG1 THR A 309 36.166 22.012 54.235 1.00 41.09 A O

ATOM 2208 CG2 THR A 309 35.368 24.206 54.800 1.00 40.07 A C

ATOM 2209 C THR A 309 37.123 24.167 57.235 1.00 41.47 A C

ATOM 2210 O THR A 309 36.339 23.944 58.168 1.00 41.71 A O

ATOM 2211 N PRO A 310 37.851 25.295 57.193 1.00 40.09 A N

ATOM 2212 CD PRO A 310 38.818 25.687 56.149 1.00 39.28 A C

ATOM 2213 CA PRO A 310 37.750 26.330 58.233 1.00 40.15 A C

ATOM 2214 CB PRO A 310 38.492 27.507 57.599 1.00 38.80 A C

ATOM 2215 CG PRO A 310 39.576 26.823 56.810 1.00 38.52 A C

ATOM 2216 C PRO A 310 36.314 26.710 58.631 1.00 40.82 A C

ATOM 2217 O PRO A 310 35.477 26.982 57.767 1.00 41.57 A O

ATOM 2218 N PRO A 311 36.003 26.704 59.945 1.00 41.00 A N

ATOM 2219 CD PRO A 311 36.837 26.264 61.081 1.00 41.74 A C

ATOM 2220 CA PRO A 311 34.653 27.060 60.394 1.00 38.86 A C

ATOM 2221 CB PRO A 311 34.800 27.084 61.920 1.00 38.92 A C

ATOM 2222 CG PRO A 311 35.801 26.002 62.168 1.00 40.08 A C

ATOM 2223 C PRO A 311 34.202 28.421 59.846 1.00 38.07 A C

ATOM 2224 O PRO A 311 33.036 28.593 59.499 1.00 38.17 A O

ATOM 2225 N GLU A 312 35.127 29.376 59.736 1.00 37.33 A N

ATOM 2226 CA GLU A 312 34.780 30.710 59.250 1.00 37.51 A C

ATOM 2227 CB GLU A 312 35.856 31.753 59.604 1.00 41.12 A C ATOM 2228 CG GLU A 312 36.591 31.536 60.940 1.00 44.01 A C

ATOM 2229 CD GLU A 312 37.738 30.521 60.817 1.00 46.77 A C

ATOM 2230 OE1 GLU A 312 38.555 30.645 59.864 1.00 46.40 A O

ATOM 2231 OE2 GLU A 312 37.821 29.602 61.667 1.00 48.12 A O

ATOM 2232 C GLU A 312 34.470 30.746 57.753 1.00 36.53 A C

ATOM 2233 O GLU A 312 33.817 31.683 57.284 1.00 38.60 A O

ATOM 2234 N ALA A 313 34.943 29.743 57.007 1.00 32.61 A N

ATOM 2235 CA ALA A 313 34.672 29.643 55.568 1.00 30.50 A C

ATOM 2236 CB ALA A 313 35.640 28.678 54.919 1.00 26.90 A C

ATOM 2237 C ALA A 313 33.232 29.138 55.389 1.00 32.00 A C

ATOM 2238 O ALA A 313 32.497 29.592 54.512 1.00 31.09 A O

ATOM 2239 N ILE A 314 32.852 28.168 56.219 1.00 30.90 A N

ATOM 2240 CA ILE A 314 31.514 27.595 56.195 1.00 31.31 A C

ATOM 2241 CB ILE A 314 31.473 26.325 57.069 1.00 29.56 A C

ATOM 2242 CG2 ILE A 314 30.089 25.798 57.224 1.00 28.99 A C

ATOM 2243 CGI ILE A 314 32.397 25.270 56.499 1.00 29.23 A C

ATOM 2244 CDl ILE A 314 32.618 24.139 57.469 1.00 33.00 A C

ATOM 2245 C ILE A 314 30.519 28.652 56.713 1.00 32.69 A C

ATOM 2246 O ILE A 314 29.422 28.808 56.164 1.00 34.20 A O

ATOM 2247 N ALA A 315 30.914 29.401 57.746 1.00 31.67 A N

ATOM 2248 CA ALA A 315 30.046 30.444 58.301 1.00 29.37 A C ATOM 2249 CB ALA A 315 30.600 30.959 59.604 1.00 31.47 A C

ATOM 2250 C ALA A 315 29.864 31.589 57.316 1.00 28.53 A C

ATOM 2251 O ALA A 315 28.759 32.104 57.160 1.00 27.48 A O

ATOM 2252 N LEU A 316 30.945 31.994 56.648 1.00 27.86 A N

ATOM 2253 CA LEU A 316 30.840 33.060 55.658 1.00 26.99 A C

ATOM 2254 CB LEU A 316 32.218 33.445 55.093 1.00 22.62 A C

ATOM 2255 CG LEU A 316 32.146 34.208 53.746 1.00 21.40 A C

ATOM 2256 CDl LEU A 316 31.342 35.491 53.840 1.00 20.39 A C

ATOM 2257 CD2 LEU A 316 33.535 34.512 53.239 1.00 22.56 A C

ATOM 2258 C LEU A 316 29.932 32.591 54.515 1.00 27.58 A C

ATOM 2259 O LEU A 316 29.112 33.330 53.993 1.00 27.33 A O

ATOM 2260 N CYS A 317 30.086 31.342 54.130 1.00 30.89 A N

ATOM 2261 CA CYS A 317 29.314 30.819 53.036 1.00 32.18 A C

ATOM 2262 CB CYS A 317 29.785 29.420 52.698 1.00 35.80 A C

ATOM 2263 SG CYS A 317 29.183 28.888 51.123 1.00 40.78 A S

ATOM 2264 C CYS A 317 27.829 30.819 53.329 1.00 33.09 A C

ATOM 2265 O CYS A 317 27.041 31.117 52.442 1.00 33.68 A O

ATOM 2266 N SER A 318 27.441 30.495 54.564 1.00 32.85 A N

ATOM 2267 CA SER A 318 26.021 30.475 54.912 1.00 32.51 A C

ATOM 2268 CB SER A 318 25.803 29.909 56.323 1.00 30.97 A C

ATOM 2269 OG SER A 318 26.537 30.621 57.292 1.00 31.88 A O ATOM 2270 C SER A 318 25.389 31.862 54.776 1.00 33.51 A C

ATOM 2271 O SER A 318 24.193 31.996 54.507 1.00 36.08 A O

ATOM 2272 N ARG A 319 26.216 32.891 54.893 1.00 32.72 A N

ATOM 2273 CA ARG A 319 25.760 34.266 54.802 1.00 32.06 A C

ATOM 2274 CB ARG A 319 26.649 35.164 55.679 1.00 35.37 A C

ATOM 2275 CG ARG A 319 26.606 34.855 57.186 1.00 41.25 A C

ATOM 2276 CD ARG A 319 25.471 35.594 57.895 1.00 46.70 A C

ATOM 2277 NE ARG A 319 24.191 35.283 57.259 1.00 54.82 A N

ATOM 2278 CZ ARG A 319 23.402 36.176 56.661 1.00 57.65 A C

ATOM 2279 NHl ARG A 319 23.758 37.459 56.635 1.00 59.93 A N

ATOM 2280 NH2 ARG A 319 22.300 35.771 56.018 1.00 57.91 A N

ATOM 2281 C ARG A 319 25.719 34.794 53.361 1.00 30.32 A C

ATOM 2282 O ARG A 319 25.369 35.952 53.130 1.00 28.75 A O

ATOM 2283 N LEU A 320 26.067 33.946 52.390 1.00 30.34 A N

ATOM 2284 CA LEU A 320 26.063 34.334 50.965 1.00 27.78 A C

ATOM 2285 CB LEU A 320 27.434 34.123 50.344 1.00 28.29 A C

ATOM 2286 CG LEU A 320 28.616 34.851 50.978 1.00 29.36 A C

ATOM 2287 CDl LEU A 320 29.913 34.343 50.341 1.00 29.51 A C

ATOM 2288 CD2 LEU A 320 28.467 36.357 50.801 1.00 29.87 A C

ATOM 2289 C LEU A 320 25.048 33.528 50.155 1.0028.32 A C

ATOM 2290 O LEU A 320 24.387 34.053 49.262 1.00 26.82 A O ATOM 2291 N LEU A 321 24.958 32.237 50.458 1.00 28.84 A N

ATOM 2292 CA LEU A 321 24.031 31.336 49.782 1.00 29.38 A C

ATOM 2293 CB LEU A 321 24.672 29.951 49.610 1.00 27.04 A C

ATOM 2294 CG LEU A 321 25.955 30.000 48.764 1.00 25.10 A C

ATOM 2295 CDl LEU A 321 26.509 28.596 48.566 1.00 22.83 A C

ATOM 2296 CD2 LEU A 321 25.656 30.665 47.421 1.00 23.61 A C

ATOM 2297 C LEU A 321 22.743 31.248 50.592 1.00 30.12 A C

ATOM 2298 O LEU A 321 22.475 30.260 51.269 1.00 30.60 A O

ATOM 2299 N GLU A 322 21.984 32.331 50.563 1.00 32.99 A N

ATOM 2300 CA GLU A 322 20.723 32.411 51.283 1.00 35.35 A C

ATOM 2301 CB GLU A 322 20.845 33.432 52.440 1.00 39.44 A C

ATOM 2302 CG GLU A 322 20.031 33.075 53.699 1.00 45.14 A C

ATOM 2303 CD GLU A 322 18.561 32.709 53.390 1.00 49.02 A C

ATOM 2304 OEI GLU A 322 18.278 31.537 52.998 1.00 48.76 A O

ATOM 2305 OE2 GLU A 322 17.690 33.603 53.528 1.00 50.22 A O

ATOM 2306 C GLU A 322 19.679 32.868 50.246 1.00 35.18 A C

ATOM 2307 O GLU A 322 19.994 33.675 49.368 1.00 32.98 A O

ATOM 2308 N TYR A 323 18.460 32.322 50.318 1.00 36.47 A N

ATOM 2309 CA TYR A 323 17.376 32.680 49.386 1.00 35.07 A C

ATOM 2310 CB TYR A 323 16.122 31.833 49.632 1.00 35.73 A C

ATOM 2311 CG TYR A 323 16.268 30.370 49.288 1.00 36.48 A C ATOM 2312 CDl TYR A 323 16.316 29.950 47.968 1.00 36.94 A C

ATOM 2313 CE1 TYR A 323 16.403 28.612 47.649 1.00 35.30 A C

ATOM 2314 CD2 TYR A 323 16.314 29.407 50.281 1.00 35.92 A C

ATOM 2315 CE2 TYR A 323 16.395 28.073 49.972 1.00 35.74 A C

ATOM 2316 CZ TYR A 323 16.437 27.675 48.654 1.00 35.11 A C

ATOM 2317 OH TYR A 323 16.480 26.332 48.343 1.00 35.85 A O

ATOM 2318 C TYR A 323 16.980 34.148 49.408 1.00 35.43 A C

ATOM 2319 O TYR A 323 16.855 34.765 48.360 1.00 35.68 A O

ATOM 2320 N THR A 324 16.730 34.695 50.595 1.00 36.52 A N

ATOM 2321 CA THR A 324 16.343 36.098 50.713 1.00 35.98 A C

ATOM 2322 CB THR A 324 15.968 36.447 52.183 1.00 37.86 A C

ATOM 2323 OG1 THR A 324 15.183 35.388 52.755 1.00 35.45 A O

ATOM 2324 CG2 THR A 324 15.171 37.761 52.233 1.00 37.80 A C

ATOM 2325 C THR A 324 17.529 36.949 50.262 1.00 35.55 A C

ATOM 2326 O THR A 324 18.558 36.976 50.912 1.00 37.14 A O

ATOM 2327 N PRO A 325 17.414 37.631 49.121 1.00 36.35 A N

ATOM 2328 CD PRO A 325 16.339 37.558 48.118 1.00 35.78 A C

ATOM 2329 CA PRO A 325 18.544 38.454 48.658 1.00 38.73 A C

ATOM 2330 CB PRO A 325 18.072 38.966 47.284 1.00 40.10 A C

ATOM 2331 CG PRO A 325 16.559 38.822 47.318 1.00 39.73 A C

ATOM 2332 C PRO A 325 19.039 39.588 49.583 1.00 40.75 A C ATOM 2333 O PRO A 325 20.194 40.058 49.464 1.00 39.35 A O

ATOM 2334 N THR A 326 18.169 40.010 50.502 1.00 41.77 A N

ATOM 2335 CA THR A 326 18.484 41.078 51.446 1.00 42.08 A C

ATOM 2336 CB THR A 326 17.240 41.936 51.812 1.00 43.80 A C

ATOM 2337 OG1 THR A 326 16.280 41.127 52.507 1.00 44.31 A O

ATOM 2338 CG2 THR A 326 16.593 42.546 50.554 1.00 43.61 A C

ATOM 2339 C THR A 326 19.049 40.507 52.730 1.00 43.10 A C

ATOM 2340 O THR A 326 19.348 41.262 53.657 1.00 45.68 A O

ATOM 2341 N ALA A 327 19.112 39.175 52.819 1.00 41.67 A N

ATOM 2342 CA ALA A 327 19.685 38.492 53.991 1.00 41.21 A C

ATOM 2343 CB ALA A 327 18.935 37.210 54.290 1.00 42.03 A C

ATOM 2344 C ALA A 327 21.161 38.175 53.716 1.00 40.39 A C

ATOM 2345 O ALA A 327 21.91 1 37.789 54.613 1.00 38.69 A O

ATOM 2346 N ARG A 328 21.551 38.300 52.449 1.00 39.41 A N

ATOM 2347 CA ARG A 328 22.925 38.050 52.036 1.00 37.97 A C

ATOM 2348 CB ARG A 328 23.011 37.737 50.537 1.00 34.85 A C

ATOM 2349 CG ARG A 328 22.158 36.607 50.067 1.00 31.64 A C

ATOM 2350 CD ARG A 328 22.138 36.598 48.566 1.00 31.39 A C

ATOM 2351 NE ARG A 328 21.061 35.748 48.087 1.00 32.71 A N

ATOM 2352 CZ ARG A 328 20.474 35.862 46.902 1.00 30.91 A C

ATOM 2353 NHl ARG A 328 20.869 36.798 46.050 1.00 28.07 A N ATOM 2354 NH2 ARG A 328 19.456 35.057 46.598 1.00 30.25 A N

ATOM 2355 C ARG A 328 23.743 39.309 52.306 1.00 38.90 A C

ATOM 2356 O ARG A 328 23.264 40.443 52.101 1.00 39.08 A O

ATOM 2357 N LEU A 329 25.002 39.085 52.682 1.00 38.98 A N

ATOM 2358 CA LEU A 329 25.938 40.159 52.963 1.00 36.91 A C

ATOM 2359 CB LEU A 329 27.291 39.611 53.404 1.00 34.76 A C

ATOM 2360 CG LEU A 329 27.285 38.696 54.607 1.00 34.37 A C

ATOM 2361 CDl LEU A 329 28.643 38.028 54.736 1.00 36.96 A C

ATOM 2362 CD2 LEU A 329 26.941 39.499 55.844 1.00 36.75 A C

ATOM 2363 C LEU A 329 26.166 41.044 51.753 1.00 37.04 A C

ATOM 2364 O LEU A 329 25.768 40.747 50.607 1.00 35.16 A O

ATOM 2365 N THR A 330 26.771 42.178 52.049 1.00 36.05 A N

ATOM 2366 CA THR A 330 27.093 43.129 51.020 1.00 35.84 A C

ATOM 2367 CB THR A 330 26.866 44.576 51.510 1.00 36.88 A C

ATOM 2368 OG1 THR A 330 27.687 44.825 52.664 1.00 38.57 A O

ATOM 2369 CG2 THR A 330 25.385 44.780 51.877 1.00 34.49 A C

ATOM 2370 C THR A 330 28.565 42.861 50.723 1.00 33.23 A C

ATOM 2371 O THR A 330 29.264 42.217 51.512 1.00 29.88 A O

ATOM 2372 N PRO A 331 29.020 43.253 49.531 1.00 32.89 A N

ATOM 2373 CD PRO A 331 28.314 43.865 48.393 1.00 31.30 A C

ATOM 2374 CA PRO A 331 30.417 43.016 49.215 1.00 31.44 A C ATOM 2375 CB PRO A 331 30.590 43.835 47.938 1.00 32.91 A C

ATOM 2376 CG PRO A 331 29.259 43.582 47.243 1.00 30.03 A C

ATOM 2377 C PRO A 331 31.316 43.452 50.379 1.00 32.42 A C

ATOM 2378 O PRO A 331 32.119 42.655 50.887 1.00 33.23 A O

ATOM 2379 N LEU A 332 31.135 44.686 50.846 1.00 33.33 A N

ATOM 2380 CA LEU A 332 31.923 45.221 51.962 1.00 32.18 A C

ATOM 2381 CB LEU A 332 31.587 46.692 52.196 1.00 35.97 A C

ATOM 2382 CG LEU A 332 32.405 47.843 51.612 1.00 39.70 A C

ATOM 2383 CDl LEU A 332 32.090 49.080 52.436 1.00 40.02 A C

ATOM 2384 CD2 LEU A 332 33.900 47.558 51.679 1.00 40.52 A C

ATOM 2385 C LEU A 332 31.764 44.490 53.291 1.00 29.85 A C

ATOM 2386 O LEU A 332 32.645 44.555 54.132 1.00 32.12 A O

ATOM 2387 N GLU A 333 30.610 43.884 53.533 1.00 32.44 A N

ATOM 2388 CA GLU A 333 30.382 43.172 54.796 1.00 33.33 A C

ATOM 2389 CB GLU A 333 28.876 42.979 55.049 1.00 36.12 A C

ATOM 2390 CG GLU A 333 28.176 44.253 55.506 1.00 38.27 A C

ATOM 2391 CD GLU A 333 26.654 44.229 55.368 1.00 41.80 A C

ATOM 2392 OE1 GLU A 333 26.007 45.113 55.992 1.00 42.66 A O

ATOM 2393 OE2 GLU A 333 26.111 43.367 54.626 1.00 40.17 A O

ATOM 2394 C GLU A 333 31.103 41.836 54.781 1.00 33.17 A C

ATOM 2395 O GLU A 333 31.571 41.340 55.817 1.00 33.94 A O ATOM 2396 N ALA A 334 31.157 41.257 53.582 1.00 33.77 A N

ATOM 2397 CA ALA A 334 31.819 39.983 53.348 1.00 32.19 A C

ATOM 2398 CB ALA A 334 31.653 39.574 51.908 1.00 33.03 A C

ATOM 2399 C ALA A 334 33.295 40.178 53.693 1.00 31.70 A C

ATOM 2400 O ALA A 334 33.811 39.507 54.592 1.00 32.27 A O

ATOM 2401 N CYS A 335 33.948 41.130 53.015 1.00 29.04 A N

ATOM 2402 CA CYS A 335 35.354 41.463 53.280 1.00 28.08 A C

ATOM 2403 CB CYS A 335 35.684 42.820 52.700 1.00 25.06 A C

ATOM 2404 SG CYS A 335 35.664 42.913 50.983 1.00 31.08 A S

ATOM 2405 C CYS A 335 35.632 41.588 54.780 1.00 29.42 A C

ATOM 2406 O CYS A 335 36.694 41.200 55.271 1.00 30.83 A O

ATOM 2407 N ALA A 336 34.694 42.228 55.470 1.00 30.07 A N

ATOM 2408 CA ALA A 336 34.775 42.469 56.899 1.00 32.45 A C

ATOM 2409 CB ALA A 336 33.708 43.477 57.306 1.00 33.21 A C

ATOM 2410 C ALA A 336 34.620 41.184 57.698 1.00 33.44 A C

ATOM 2411 O ALA A 336 34.901 41.162 58.905 1.00 32.85 A O

ATOM 2412 N HIS A 337 34.175 40.124 57.021 1.00 32.02 A N

ATOM 2413 CA HIS A 337 33.986 38.832 57.658 1.00 30.44 A C

ATOM 2414 CB HIS A 337 33.390 37.807 56.673 1.00 29.63 A C

ATOM 2415 CG HIS A 337 32.956 36.526 57.323 1.00 27.00 A C

ATOM 2416 CD2 HIS A 337 31.733 36.110 57.736 1.00 29.14 A C ATOM 2417 ND1 HIS A 337 33.837 35.523 57.674 1.00 28.86 A N

ATOM 2418 CE1 HIS A 337 33.177 34.549 58.280 1.00 28.43 A C

ATOM 2419 NE2 HIS A 337 31.898 34.881 58.330 1.00 29.35 A N

ATOM 2420 C HIS A 337 35.306 38.326 58.229 1.00 30.54 A C

ATOM 2421 O HIS A 337 36.385 38.615 57.704 1.00 29.81 A O

ATOM 2422 N SER A 338 35.209 37.565 59.310 1.00 30.75 A N

ATOM 2423 CA SER A 338 36.394 37.048 59.969 1.00 33.89 A C

ATOM 2424 CB SER A 338 36.088 36.545 61.384 1.00 32.18 A C

ATOM 2425 OG SER A 338 35.068 35.569 61.378 1.00 36.74 A O

ATOM 2426 C SER A 338 37.100 35.982 59.167 1.00 35.32 A C

ATOM 2427 0 SER A 338 38.199 35.564 59.532 1.00 38.56 A O

ATOM 2428 N PHE A 339 36.469 35.494 58.106 1.00 33.93 A N

ATOM 2429 CA PHE A 339 37.154 34.509 57.289 1.00 32.49 A C

ATOM 2430 CB PHE A 339 36.266 34.071 56.130 1.00 29.12 A C

ATOM 2431 CG PHE A 339 36.958 33.172 55.162 1.00 28.40 A C

ATOM 2432 CDl PHE A 339 36.917 33.438 53.798 1.00 25.87 A C

ATOM 2433 CD2 PHE A 339 37.649 32.045 55.617 1.00 28.57 A C

ATOM 2434 CE1 PHE A 339 37.549 32.589 52.894 1.00 27.62 A C

ATOM 2435 CE2 PHE A 339 38.290 31.181 54.721 1.00 28.61 A C

ATOM 2436 CZ PHE A 339 38.236 31.457 53.357 1.00 27.87 A C

ATOM 2437 C PHE A 339 38.459 35.177 56.785 1.00 31.43 A C ATOM 2438 O PHE A 339 39.529 34.575 56.799 1.00 32.88 A O

ATOM 2439 N PHE A 340 38.369 36.467 56.478 1.00 31.90 A N

ATOM 2440 CA PHE A 340 39.497 37.248 55.994 1.00 32.43 A C

ATOM 2441 CB PHE A 340 38.979 38.337 55.075 1.00 32.03 A C

ATOM 2442 CG PHE A 340 38.095 37.817 53.993 1.00 35.36 A C

ATOM 2443 CDl PHE A 340 38.598 36.938 53.040 1.00 35.28 A C

ATOM 2444 CD2 PHE A 340 36.758 38.188 53.924 1.00 34.74 A C

ATOM 2445 CE1 PHE A 340 37.775 36.437 52.027 1.00 35.62 A C

ATOM 2446 CE2 PHE A 340 35.925 37.691 52.914 1.00 35.63 A C

ATOM 2447 CZ PHE A 340 36.432 36.816 51.967 1.00 33.48 A C

ATOM 2448 C PHE A 340 40.406 37.877 57.055 1.00 34.61 A C

ATOM 2449 O PHE A 340 41.306 38.641 56.700 1.00 35.72 A O

ATOM 2450 N ASP A 341 40.207 37.567 58.339 1.00 35.33 A N

ATOM 2451 CA ASP A 341 41.059 38.152 59.391 1.00 35.61 A C

ATOM 2452 CB ASP A 341 40.687 37.632 60.784 1.00 36.67 A C

ATOM 2453 CG ASP A 341 39.411 38.245 61.315 1.00 38.76 A C

ATOM 2454 OD1 ASP A 341 39.001 39.318 60.814 1.00 40.77 A O

ATOM 2455 OD2 ASP A 341 38.816 37.644 62.237 1.00 39.86 A O

ATOM 2456 C ASP A 341 42.543 37.907 59.168 1.00 34.98 A C

ATOM 2457 O ASP A 341 43.364 38.794 59.417 1.00 36.99 A O

ATOM 2458 N GLU A 342 42.895 36.699 58.730 1.00 34.36 A N ATOM 2459 CA GLU A 342 44.300 36.389 58.502 1.00 34.14 A C

ATOM 2460 CB GLU A 342 44.510 34.944 58.026 1.00 36.25 A C

ATOM 2461 CG GLU A 342 45.980 34.645 57.716 1.00 35.88 A C

ATOM 2462 CD GLU A 342 46.222 33.239 57.219 1.00 38.38 A C

ATOM 2463 OE1 GLU A 342 45.333 32.678 56.542 1.00 38.14 A O

ATOM 2464 OE2 GLU A 342 47.314 32.698 57.503 1.00 39.48 A O

ATOM 2465 C GLU A 342 44.985 37.354 57.540 1.00 32.97 A C

ATOM 2466 O GLU A 342 46.184 37.585 57.677 1.00 32.96 A O

ATOM 2467 N LEU A 343 44.236 37.922 56.587 1.00 31.99 A N

ATOM 2468 CA LEU A 343 44.806 38.866 55.607 1.00 31.42 A C

ATOM 2469 CB LEU A 343 43.844 39.131 54.449 1.00 30.92 A C

ATOM 2470 CG LEU A 343 43.539 38.079 53.383 1.00 27.15 A C

ATOM 2471 CDl LEU A 343 43.101 36.803 54.039 1.00 28.27 A C

ATOM 2472 CD2 LEU A 343 42.451 38.595 52.468 1.00 21.59 A C

ATOM 2473 C LEU A 343 45.150 40.197 56.243 1.00 31.51 A C

ATOM 2474 O LEU A 343 45.965 40.949 55.715 1.00 31.66 A O

ATOM 2475 N ARG A 344 44.480 40.497 57.350 1.00 33.95 A N

ATOM 2476 CA ARG A 344 44.709 41.733 58.085 1.00 35.66 A C

ATOM 2477 CB ARG A 344 43.390 42.241 58.649 1.00 30.95 A C

ATOM 2478 CG ARG A 344 42.498 42.793 57.581 1.00 26.72 A C

ATOM 2479 CD ARG A 344 41.166 43.229 58.144 1.00 27.97 A C ATOM 2480 NE ARG A 344 40.322 42.105 58.534 1.00 25.79 A N

ATOM 2481 CZ ARG A 344 39.321 41.653 57.787 1.00 27.16 A C

ATOM 2482 NHl ARG A 344 39.049 42.242 56.625 1.00 25.96 A N

ATOM 2483 NH2 ARG A 344 38.647 40.575 58.164 1.00 29.04 A N

ATOM 2484 C ARG A 344 45.784 41.596 59.179 1.00 39.42 A C

ATOM 2485 O ARG A 344 46.086 42.555 59.892 1.00 40.56 A O

ATOM 2486 N ASP A 345 46.320 40.384 59.322 1.00 42.31 A N

ATOM 2487 CA ASP A 345 47.389 40.087 60.279 1.00 43.57 A C

ATOM 2488 CB ASP A 345 47.656 38.573 60.320 1.00 46.53 A C

ATOM 2489 CG ASP A 345 48.526 38.144 61.508 1.00 48.58 A C

ATOM 2490 OD1 ASP A 345 49.669 38.642 61.642 1.00 50.52 A O

ATOM 2491 OD2 ASP A 345 48.063 37.282 62.293 1.00 48.36 A O

ATOM 2492 C ASP A 345 48.603 40.814 59.700 1.00 43.04 A C

ATOM 2493 O ASP A 345 48.872 40.718 58.508 1.00 39.51 A O

ATOM 2494 N PRO A 346 49.373 41.521 60.546 1.00 43.85 A N

ATOM 2495 CD PRO A 346 49.255 41.606 62.013 1.00 42.53 A C

ATOM 2496 CA PRO A 346 50.550 42.264 60.064 1.00 43.73 A C

ATOM 2497 CB PRO A 346 51.048 42.989 61.323 1.00 43.51 A C

ATOM 2498 CG PRO A 346 49.854 42.956 62.270 1.00 44.13 A C

ATOM 2499 C PRO A 346 51.676 41.441 59.423 1.00 44.71 A C

ATOM 2500 O PRO A 346 52.479 41.979 58.653 1.00 42.18 A O ATOM 2501 N ASN A 347 51.734 40.150 59.748 1.00 45.80 A N

ATOM 2502 CA ASN A 347 52.780 39.274 59.226 1.00 48.40 A C

ATOM 2503 CB ASN A 347 53.489 38.548 60.392 1.00 50.52 A C

ATOM 2504 CG ASN A 347 53.829 39.481 61.575 1.00 51.68 A _, C

ATOM 2505 OD1 ASN A 347 53.106 39.510 62.583 1.00 52.97 A O

ATOM 2506 ND2 ASN A 347 54.943 40.219 61.465 1.00 50.64 A N

ATOM 2507 C ASN A 347 52.212 38.227 58.269 1.00 49.43 A C

ATOM 2508 O ASN A 347 52.649 37.078 58.294 1.00 51.30 A O

ATOM 2509 N VAL A 348 51.284 38.626 57.397 1.0049.86 A N

ATOM 2510 CA VAL A 348 50.646 37.687 56.465 1.00 49.86 A C

ATOM 2511 CB VAL A 348 49.626 38.381 55.516 1.00 50.32 A C

ATOM 2512 CGI VAL A 348 48.619 37.356 54.995 1.00 50.90 A C

ATOM 2513 CG2 VAL A 348 48.926 39.542 56.193 1.00 51.72 A C

ATOM 2514 C VAL A 348 51.601 36.891 55.573 1.00 50.39 A C

ATOM 2515 O VAL A 348 51.924 35.726 55.850 1.00 52.96 A O

ATOM 2516 N LYS A 349 51.988 37.508 54.462 1.00 48.93 A N

ATOM 2517 CA LYS A 349 52.882 36.888 53.496 1.00 48.04 A C

ATOM 2518 CB LYS A 349 54.174 36.458 54.174 1.00 48.29 A C

ATOM 2519 CG LYS A 349 55.054 37.623 54.626 1.00 51.32 A C

ATOM 2520 CD LYS A 349 55.759 38.308 53.455 1.00 51.87 A C

ATOM 2521 CE LYS A 349 56.898 39.207 53.940 1.00 52.70 A C ATOM 2522 NZ LYS A 349 57.699 39.755 52.802 1.00 55.92 A N

ATOM 2523 C LYS A 349 52.310 35.726 52.683 1.00 47.81 A C

ATOM 2524 O LYS A 349 51.711 34.792 53.217 1.00 48.27 A O

ATOM 2525 N LEU A 350 52.498 35.806 51.372 1.00 47.80 A N

ATOM 2526 CA LEU A 350 52.045 34.764 50.470 1.00 47.07 A C

ATOM 2527 CB LEU A 350 52.152 35.227 49.019 1.00 45.84 A C

ATOM 2528 CG LEU A 350 51.388 36.459 48.554 1.00 42.81 A C

ATOM 2529 CDl LEU A 350 51.513 36.571 47.034 1.00 45.47 A C

ATOM 2530 CD2 LEU A 350 49.943 36.350 48.977 1.00 40.23 A C

ATOM 2531 C LEU A 350 52.939 33.537 50.636 1.00 48.97 A C

ATOM 2532 O LEU A 350 54.081 33.632 51.096 1.00 47.91 A O

ATOM 2533 N PRO A 351 52.423 32.362 50.261 1.00 49.92 A N

ATOM 2534 CD PRO A 351 51.025 32.123 49.856 1.00 49.34 A C

ATOM 2535 CA PRO A 351 53.167 31.103 50.358 1.00 50.91 A C

ATOM 2536 CB PRO A 351 52.199 30.105 49.729 1.00 51.84 A C

ATOM 2537 CG PRO A 351 50.854 30.656 50.147 1.00 49.35 A C

ATOM 2538 C PRO A 351 54.510 31.137 49.621 1.00 51.08 A C

ATOM 2539 O PRO A 351 55.435 30.391 49.956 1.00 51.03 A O

ATOM 2540 N ASN A 352 54.605 32.019 48.627 1.00 51.91 A N

ATOM 2541 CA ASN A 352 55.819 32.165 47.830 1.00 51.60 A C

ATOM 2542 CB ASN A 352 55.488 32.575 46.388 1.00 53.18 A C ATOM 2543 CG ASN A 352 54.492 33.720 46.313 1.00 54.15 A C

ATOM 2544 OD1 ASN A 352 54.857 34.882 46.523 1.00 54.22 A O

ATOM 2545 ND2 ASN A 352 53.221 33.397 46.007 1.00 53.45 A N

ATOM 2546 C ASN A 352 56.783 33.149 48.439 1.00 51.29 A C

ATOM 2547 O ASN A 352 57.821 33.432 47.866 1.00 51.94 A O

ATOM 2548 N GLY A 353 56.425 33.694 49.591 1.00 52.10 A N

ATOM 2549 CA GLY A 353 57.301 34.637 50.254 1.00 51.67 A C

ATOM 2550 C GLY A 353 57.033 36.093 49.924 1.00 52.59 A C

ATOM 2551 O GLY A 353 57.364 36.976 50.721 1.00 52.88 A O

ATOM 2552 N ARG A 354 56.434 36.354 48.764 1.00 52.20 A N

ATOM 2553 CA ARG A 354 56.131 37.723 48.355 1.00 52.91 A C

ATOM 2554 CB ARG A 354 55.795 37.733 46.867 1.00 54.87 A C

ATOM 2555 CG ARG A 354 56.859 37.012 46.055 1.00 58.36 A C

ATOM 2556 CD ARG A 354 56.491 36.885 44.598 1.00 60.35 A C

ATOM 2557 NE ARG A 354 56.715 38.114 43.846 1.00 62.57 A N

ATOM 2558 CZ ARG A 354 57.119 38.141 42.578 1.00 62.68 A C

ATOM 2559 NHl ARG A 354 57.345 37.004 41.930 1.00 63.15 A N

ATOM 2560 NH2 ARG A 354 57.283 39.300 41.951 1.00 63.20 A N

ATOM 2561 C ARG A 354 55.012 38.369 49.189 1.00 52.68 A C

ATOM 2562 0 ARG A 354 54.091 37.690 49.645 1.00 52.84 A O

ATOM 2563 N ASP A 355 55.114 39.675 49.423 1.00 52.60 A N ATOM 2564 CA ASP A 355 54.104 40.391 50.209 1.00 51.13 A C

ATOM 2565 CB ASP A 355 54.472 41.868 50.315 1.00 52.98 A C

ATOM 2566 CG ASP A 355 55.022 42.228 51.662 1.00 55.75 A C

ATOM 2567 OD1 ASP A 355 56.168 41.827 51.964 1.00 56.98 A O

ATOM 2568 OD2 ASP A 355 54.303 42.912 52.420 1.00 58.14 A O

ATOM 2569 C ASP A 355 52.709 40.304 49.609 1.00 48.33 A C

ATOM 2570 O ASP A 355 52.558 40.122 48.402 1.00 47.92 A O

ATOM 2571 N THR A 356 51.695 40.471 50.453 1.00 45.12 A N

ATOM 2572 CA THR A 356 50.318 40.453 49.985 1.00 41.61 A C

ATOM 2573 CB THR A 356 49.315 40.509 51.136 1.00 41.89 A C

ATOM 2574 OG1 THR A 356 49.610 41.641 51.967 1.00 43.46 A O

ATOM 2575 CG2 THR A 356 49.350 39.222 51.938 1.00 40.77 A C

ATOM 2576 C THR A 356 50.053 41.682 49.135 1.00 39.93 A C

ATOM 2577 O THR A 356 50.681 42.726 49.302 1.00 38.71 A O

ATOM 2578 N PRO A 357 49.106 41.568 48.202 1.00 38.90 A N

ATOM 2579 CD PRO A 357 48.306 40.379 47.877 1.00 38.06 A C

ATOM 2580 CA PRO A 357 48.754 42.683 47.327 1.00 37.44 A C

ATOM 2581 CB PRO A 357 47.750 42.052 46.357 1.00 37.15 A C

ATOM 2582 CG PRO A 357 48.028 40.598 46.426 1.00 37.65 A C

ATOM 2583 C PRO A 357 48.072 43.787 48.145 1.00 36.52 A C

ATOM 2584 0 PRO A 357 47.899 43.670 49.371 1.00 35.18 A O ATOM 2585 N ALA A 358 47.696 44.855 47.445 1.00 36.31 A N

ATOM 2586 CA ALA A 358 47.013 45.992 48.045 1.00 36.89 A C

ATOM 2587 CB ALA A 358 46.871 47.116 47.022 1.00 39.29 A C

ATOM 2588 C ALA A 358 45.642 45.503 48.460 1.00 36.54 A C

ATOM 2589 O ALA A 358 44.804 45.203 47.617 1.00 40.51 A O

ATOM 2590 N LEU A 359 45.418 45.376 49.753 1.00 33.58 A N

ATOM 2591 CA LEU A 359 44.135 44.911 50.197 1.00 31.97 A C

ATOM 2592 CB LEU A 359 44.319 43.680 51.079 1.00 31.56 A C

ATOM 2593 CG LEU A 359 44.939 42.380 50.578 1.00 30.94 A C

ATOM 2594 CDl LEU A 359 45.021 41.419 51.745 1.00 27.42 A C

ATOM 2595 CD2 LEU A 359 44.102 41.782 49.456 1.00 27.95 A C

ATOM 2596 C LEU A 359 43.430 45.978 51.009 1.00 34.57 A C

ATOM 2597 O LEU A 359 42.273 45.807 51.388 1.00 35.39 A O

ATOM 2598 N PHE A 360 44.110 47.079 51.295 1.00 35.45 A N

ATOM 2599 CA PHE A 360 43.479 48.083 52.128 1.00 36.39 A C

ATOM 2600 CB PHE A 360 44.128 48.080 53.507 1.00 37.60 A C

ATOM 2601 CG PHE A 360 44.351 46.699 54.062 1.00 39.23 A C

ATOM 2602 CDl PHE A 360 45.633 46.197 54.217 1.00 36.41 A C

ATOM 2603 CD2 PHE A 360 43.270 45.902 54.427 1.00 41.40 A C

ATOM 2604 CE1 PHE A 360 45.841 44.935 54.723 1.00 37.04 A C

ATOM 2605 CE2 PHE A 360 43.470 44.628 54.939 1.00 42.88 A C ATOM 2606 CZ PHE A 360 44.766 44.146 55.086 1.00 40.52 A C

ATOM 2607 C PHE A 360 43.432 49.492 51.591 1.00 37.54 A C

ATOM 2608 O PHE A 360 42.997 50.388 52.298 1.00 38.49 A O

ATOM 2609 N ASN A 361 43.824 49.691 50.338 1.00 37.15 A N

ATOM 2610 CA ASN A 361 43.813 51.028 49.758 1.00 38.30 A C

ATOM 2611 CB ASN A 361 44.779 51.087 48.573 1.00 40.99 A C

ATOM 2612 CG ASN A 361 44.603 49.920 47.631 1.00 42.98 A C

ATOM 2613 OD1 ASN A 361 43.681 49.127 47.807 1.00 46.33 A O

ATOM 2614 ND2 ASN A 361 45.492 49.791 46.637 1.00 42.76 A N

ATOM 2615 C ASN A 361 42.430 51.478 49.314 1.00 40.07 A C

ATOM 2616 O ASN A 361 42.260 51.910 48.178 1.00 41.25 A O

ATOM 2617 N PHE A 362 41.449 51.415 50.211 1.00 41.81 A N

ATOM 2618 CA PHE A 362 40.067 51.815 49.887 1.00 43.99 A C

ATOM 2619 CB PHE A 362 39.110 51.544 51.064 1.00 41.50 A C

ATOM 2620 CG PHE A 362 38.961 50.077 51.454 1.00 41.10 A C

ATOM 2621 CDl PHE A 362 39.584 49.579 52.609 1.00 40.14 A C

ATOM 2622 CD2 PHE A 362 38.122 49.224 50.731 1.00 38.57 A C

ATOM 2623 CE1 PHE A 362 39.366 48.266 53.040 1.00 39.44 A C

ATOM 2624 CE2 PHE A 362 37.897 47.909 51.152 1.00 37.72 A C

ATOM 2625 CZ PHE A 362 38.518 47.431 52.307 1.00 38.85 A C

ATOM 2626 C PHE A 362 39.949 53.303 49.548 1.00 46.68 A C ATOM 2627 O PHE A 362 40.839 54.098 49.844 1.00 48.75 A O

ATOM 2628 N THR A 363 38.837 53.671 48.927 1.00 50.09 A N

ATOM 2629 CA THR A 363 38.571 55.057 48.587 1.00 53.08 A C

ATOM 2630 CB THR A 363 38.021 55.207 47.160 1.00 54.70 A C

ATOM 2631 OG1 THR A 363 38.520 54.160 46.324 1.00 58.50 A O

ATOM 2632 CG2 THR A 363 38.445 56.547 46.576 1.00 57.95 A C

ATOM 2633 C THR A 363 37.445 55.444 49.535 1.00 54.64 A C

ATOM 2634 O THR A 363 37.296 54.861 50.606 1.00 56.75 A O

ATOM 2635 N THR A 364 36.662 56.439 49.137 1.00 56.19 A N

ATOM 2636 CA THR A 364 35.505 56.907 49.898 1.00 54.68 A C

ATOM 2637 CB THR A 364 35.438 58.435 49.858 1.00 56.11 A C

ATOM 2638 OG1 THR A 364 35.506 58.875 48.491 1.00 54.01 A O

ATOM 2639 CG2 THR A 364 36.611 59.033 50.649 1.00 56.34 A C

ATOM 2640 C THR A 364 34.336 56.325 49.110 1.00 53.24 A C

ATOM 2641 O THR A 364 33.298 55.977 49.658 1.00 51.97 A O

ATOM 2642 N GLN A 365 34.573 56.187 47.808 1.00 52.95 A N

ATOM 2643 CA GLN A 365 33.627 55.627 46.859 1.00 52.88 A C

ATOM 2644 CB GLN A 365 34.192 55.742 45.439 1.00 54.99 A C

ATOM 2645 CG GLN A 365 33.253 55.259 44.346 1.00 58.42 A C

ATOM 2646 CD GLN A 365 31.930 56.000 44.343 1.00 60.34 A C

ATOM 2647 OE1 GLN A 365 31.857 57.164 44.740 1.00 62.13 A O ATOM 2648 NE2 GLN A 365 30.871 55.323 43.902 1.00 61.74 A N

ATOM 2649 C GLN A 365 33.372 54.162 47.201 1.00 51.51 A C

ATOM 2650 O GLN A 365 32.220 53.732 47.261 1.00 52.21 A O

ATOM 2651 N GLU A 366 34.446 53.403 47.431 1.00 49.50 A N

ATOM 2652 CA GLU A 366 34.346 51.970 47.787 1.00 46.94 A C

ATOM 2653 CB GLU A 366 35.732 51.313 47.880 1.00 45.51 A C

ATOM 2654 CG GLU A 366 36.589 51.362 46.633 1.00 46.49 A C

ATOM 2655 CD GLU A 366 37.812 50.471 46.750 1.00 46.59 A C

ATOM 2656 OEI GLU A 366 38.905 50.882 46.300 1.00 48.74 A O

ATOM 2657 OE2 GLU A 366 37.677 49.350 47.278 1.00 43.88 A O

ATOM 2658 C GLU A 366 33.661 51.745 49.133 1.00 45.13 A C

ATOM 2659 O GLU A 366 33.024 50.715 49.361 1.00 43.49 A O

ATOM 2660 N LEU A 367 33.853 52.702 50.035 1.00 45.48 A N

ATOM 2661 CA LEU A 367 33.302 52.650 51.383 1.00 45.45 A C

ATOM 2662 CB LEU A 367 34.321 53.245 52.353 1.00 44.94 A C

ATOM 2663 CG LEU A 367 35.590 52.406 52.524 1.00 43.11 A C

ATOM 2664 CDl LEU A 367 36.764 53.303 52.872 1.00 40.53 A C

ATOM 2665 CD2 LEU A 367 35.360 51.340 53.606 1.00 41.73 A C

ATOM 2666 C LEU A 367 31.953 53.362 51.515 1.00 47.21 A C

ATOM 2667 O LEU A 367 31.287 53.268 52.556 1.00 44.98 A O

ATOM 2668 N SER A 368 31.551 54.066 50.455 1.00 50.33 A N ATOM 2669 CA SER A 368 30.269 54.777 50.452 1.00 53.30 A C

ATOM 2670 CB SER A 368 29.900 55.252 49.026 1.00 51.90 A C

ATOM 2671 OG SER A 368 29.543 54.189 48.160 1.00 51.58 A O

ATOM 2672 C SER A 368 29.198 53.831 51.041 1.00 55.02 A C

ATOM 2673 O SER A 368 28.481 54.180 51.979 1.00 56.62 A O

ATOM 2674 N SER A 369 29.154 52.608 50.525 1.00 56.53 A N

ATOM 2675 CA SER A 369 28.229 51.586 50.995 1.00 55.52 A C

ATOM 2676 CB SER A 369 28.736 50.210 50.521 1.00 56.85 A C

ATOM 2677 OG SER A 369 28.273 49.153 51.347 1.00 60.02 A O

ATOM 2678 C SER A 369 28.108 51.600 52.526 1.00 53.64 A C

ATOM 2679 O SER A 369 27.033 51.402 53.066 1.00 52.74 A O

ATOM 2680 N ASN A 370 29.196 51.885 53.227 1.00 53.25 A N

ATOM 2681 CA ASN A 370 29.155 51.861 54.690 1.00 54.72 A C

ATOM 2682 CB ASN A 370 28.781 50.436 55.133 1.00 53.59 A C

ATOM 2683 CG ASN A 370 28.581 50.309 56.624 1.00 52.90 A C

ATOM 2684 OD1 ASN A 370 29.072 51.130 57.406 1.00 52.40 A O

ATOM 2685 ND2 ASN A 370 27.869 49.257 57.034 1.00 53.35 A N

ATOM 2686 C ASN A 370 30.524 52.287 55.269 1.00 56.11 A C

ATOM 2687 O ASN A 370 31.404 51.457 55.527 1.00 55.51 A O

ATOM 2688 N PRO A 371 30.723 53.601 55.454 1.00 56.66 A N

ATOM 2689 CD PRO A 371 29.897 54.707 54.940 1.00 56.97 A C ATOM 2690 CA PRO A 371 31.982 54.113 55.989 1.00 56.41 A C

ATOM 2691 CB PRO A 371 31.762 55.622 55.955 1.00 55.85 A C

ATOM 2692 CG PRO A 371 30.925 55.796 54.732 1.00 55.46 A C

ATOM 2693 C PRO A 371 32.430 53.603 57.366 1.00 57.02 A C

ATOM 2694 O PRO A 371 33.626 53.487 57.619 1.00 59.45 A O

ATOM 2695 N PRO A 372 31.497 53.308 58.281 1.00 55.69 A N

ATOM 2696 CD PRO A 372 30.057 53.594 58.279 1.00 55.67 A C

ATOM 2697 CA PRO A 372 31.946 52.820 59.600 1.00 54.92 A C

ATOM 2698 CB PRO A 372 30.668 52.851 60.439 1.00 55.56 A C

ATOM 2699 CG PRO A 372 29.816 53.893 59.749 1.00 56.25 A C

ATOM 2700 C PRO A 372 32.569 51.417 59.631 1.00 55.36 A C

ATOM 2701 O PRO A 372 32.874 50.895 60.711 1.00 56.43 A O

ATOM 2702 N LEU A 373 32.689 50.784 58.462 1.00 55.09 A N

ATOM 2703 CA LEU A 373 33.281 49.438 58.349 1.00 53.58 A C

ATOM 2704 CB LEU A 373 32.701 48.662 57.151 1.00 50.84 A C

ATOM 2705 CG LEU A 373 31.470 47.783 57.401 1.00 49.68 A C

ATOM 2706 CDl LEU A 373 31.241 46.918 56.175 1.00 49.06 A C

ATOM 2707 CD2 LEU A 373 31.667 46.909 58.633 1.00 46.66 A C

ATOM 2708 C LEU A 373 34.793 49.550 58.193 1.00 52.36 A C

ATOM 2709 O LEU A 373 35.546 48.612 58.470 1.00 50.89 A O

ATOM 2710 N ALA A 374 35.221 50.715 57.732 1.00 50.53 A N ATOM 2711 CA ALA A 374 36.621 50.969 57.547 1.00 48.79 A C

ATOM 2712 CB ALA A 374 36.830 52.392 57.095 1.00 49.05 A C

ATOM 2713 C ALA A 374 37.352 50.689 58.857 1.00 48.09 A C

ATOM 2714 O ALA A 374 38.554 50.436 58.850 1.00 50.11 A O

ATOM 2715 N THR A 375 36.631 50.691 59.976 1.00 46.43 A N

ATOM 2716 CA THR A 375 37.265 50.414 61.269 1.00 44.93 A C

ATOM 2717 CB THR A 375 36.285 50.632 62.456 1.00 44.95 A C

ATOM 2718 OG1 THR A 375 35.844 51.993 62.476 1.00 42.25 A O

ATOM 2719 CG2 THR A 375 36.971 50.303 63.794 1.00 45.26 A C

ATOM 2720 C THR A 375 37.797 48.972 61.321 1.00 45.05 A C

ATOM 2721 O THR A 375 38.819 48.700 61.959 1.00 44.91 A O

ATOM 2722 N ILE A 376 37.082 48.058 60.659 1.00 46.07 A N

ATOM 2723 CA ILE A 376 37.436 46.631 60.602 1.00 46.25 A C

ATOM 2724 CB ILE A 376 36.168 45.719 60.423 1.00 47.47 A C

ATOM 2725 CG2 ILE A 376 36.587 44.258 60.410 1.00 49.84 A C

ATOM 2726 CGI ILE A 376 35.117 45.950 61.518 1.00 47.90 A C

ATOM 2727 CDl ILE A 376 35.379 45.210 62.832 1.00 48.70 A C

ATOM 2728 C ILE A 376 38.328 46.358 59.377 1.00 45.31 A C

ATOM 2729 O ILE A 376 39.412 45.771 59.485 1.00 46.01 A O

ATOM 2730 N LEU A 377 37.832 46.788 58.219 1.00 42.65 A N

ATOM 2731 CA LEU A 377 38.484 46.605 56.929 1.00 40.14 A C ATOM 2732 CB LEU A 377 37.644 47.251 55.842 1.00 37.52 A C

ATOM 2733 CG LEU A 377 36.236 46.720 55.598 1.00 34.72 A C

ATOM 2734 CDl LEU A 377 35.498 47.655 54.649 1.00 32.35 A C

ATOM 2735 CD2 LEU A 377 36.300 45.311 55.046 1.00 32.96 A C

ATOM 2736 C LEU A 377 39.894 47.136 56.812 1.00 41.30 A C

ATOM 2737 O LEU A 377 40.637 46.751 55.914 1.00 42.07 A O

ATOM 2738 N ILE A 378 40.245 48.061 57.687 1.00 42.94 A N

ATOM 2739 CA ILE A 378 41.572 48.663 57.674 1.00 43.58 A C

ATOM 2740 CB ILE A 378 41.464 50.174 57.318 1.00 41.23 A C

ATOM 2741 CG2 ILE A 378 42.838 50.784 57.156 1.00 40.66 A C

ATOM 2742 CGI ILE A 378 40.657 50.333 56.021 1.00 41.34 A C

ATOM 2743 CDl ILE A 378 40.715 51.714 55.390 1.00 38.27 A C

ATOM 2744 C ILE A 378 42.267 48.421 59,038 1.00 44.75 A C

ATOM 2745 O ILE A 378 41.972 49.088 60.044 1.00 44.69 A O

ATOM 2746 N PRO A 379 43.144 47.394 59.104 1.00 44.54 A N

ATOM 2747 CD PRO A 379 43.472 46.393 58.066 1.00 43.70 A C

ATOM 2748 CA PRO A 379 43.840 47.105 60.368 1.00 44.21 A C

ATOM 2749 CB PRO A 379 44.467 45.717 60.111 1.00 44.60 A C

ATOM 2750 CG PRO A 379 44.729 45.731 58.623 1.00 43.70 A C

ATOM 2751 C PRO A 379 44.869 48.184 60.793 1.00 42.55 A C

ATOM 2752 O PRO A 379 45.392 48.933 59.965 1.00 40.25 A O ATOM 2753 N PRO A 380 45.126 48.298 62.108 1.00 41.77 A N

ATOM 2754 CD PRO A 380 44.477 47.465 63.139 1.00 41.86 A C

ATOM 2755 CA PRO A 380 46.054 49.251 62.727 1.00 42.53 A C

ATOM 2756 CB PRO A 380 46.365 48.585 64.068 1.00 40.69 A C

ATOM 2757 CG PRO A 380 45.022 48.050 64.465 1.00 41.83 A C

ATOM 2758 C PRO A 380 47.316 49.608 61.944 1.00 42.81 A C

ATOM 2759 O PRO A 380 47.639 50.792 61.810 1.00 45.00 A O

ATOM 2760 N HIS A 381 48.005 48.588 61.420 1.00 43.34 A N

ATOM 2761 CA HIS A 381 49.259 48.744 60.659 1.00 41.55 A C

ATOM 2762 CB HIS A 381 50.013 47.398 60.562 1.00 40.10 A C

ATOM 2763 CG HIS A 381 49.301 46.357 59.750 1.00 38.99 A C

ATOM 2764 CD2 HIS A 381 48.395 45.412 60.105 1.00 37.41 A C

ATOM 2765 ND1 HIS A 381 49.456 46.243 58.385 1.00 36.11 A N

ATOM 2766 CE1 HIS A 381 48.674 45.280 57.932 1.00 35.67 A C

ATOM 2767 NE2 HIS A 381 48.020 44.759 58.956 1.00 35.32 A N

ATOM 2768 C HIS A 381 49.147 49.352 59.260 1.00 41.65 A C

ATOM 2769 O HIS A 381 50.117 49.899 58.757 1.00 41.61 A O

ATOM 2770 N ALA A 382 47.999 49.188 58.604 1.00 44.05 A N

ATOM 2771 CA ALA A 382 47.781 49.737 57.259 1.00 44.82 A C

ATOM 2772 CB ALA A 382 46.907 48.805 56.429 1.00 44.94 A C

ATOM 2773 C ALA A 382 47.132 51.113 57.380 1.00 45.71 A C ATOM 2774 O ALA A 382 47.020 51.849 56.385 1.00 42.45 A O

ATOM 2775 N ARG A 383 46.696 51.428 58.611 1.00 48.21 A N

ATOM 2776 CA ARG A 383 46.081 52.717 58.962 1.00 49.82 A C

ATOM 2777 CB ARG A 383 45.505 52.694 60.391 1.00 49.34 A C

ATOM 2778 CG ARG A 383 44.415 51.685 60.670 1.00 51.27 A C

ATOM 2779 CD ARG A 383 43.684 52.026 61.979 1.00 51.98 A C

ATOM 2780 NE ARG A 383 43.172 50.844 62.682 1.00 53.22 A N

ATOM 2781 CZ ARG A 383 41.970 50.756 63.251 1.00 54.13 A C

ATOM 2782 NHl ARG A 383 41.135 51.781 63.190 1.00 56.67 A N

ATOM 2783 NH2 ARG A 383 41.622 49.666 63.933 1.00 53.27 A N

ATOM 2784 C ARG A 383 47.155 53.810 58.927 1.00 50.51 A C

ATOM 2785 O ARG A 383 48.083 53.788 59.744 1.00 51.82 A O

ATOM 2786 N ILE A 384 47.052 54.751 57.990 1.00 50.19 A N

ATOM 2787 CA ILE A 384 48.032 55.825 57.943 1.00 50.40 A C

ATOM 2788 CB ILE A 384 48.234 56.409 56.512 1.00 51.59 A C

ATOM 2789 CG2 ILE A 384 49.205 55.530 55.719 1.00 49.98 A C

ATOM 2790 CGI ILE A 384 46.894 56.596 55.790 1.00 53.19 A C

ATOM 2791 CDl ILE A 384 47.036 57.098 54.346 1.00 54.20 A C

ATOM 2792 C ILE A 384 47.717 56.925 58.975 1.00 51.15 A C

ATOM 2793 OT1 ILE A 384 46.656 57.601 58.901 1.00 50.81 A O

ATOM 2794 OXT ILE A 384 48.541 57.045 59.909 1.00 51.15 A O TER 2795 ILE A 384 A

ATOM 2796 CB VAL B 1 22.328 39.735 28.119 1.00 81.87 B C

ATOM 2797 CGI VAL B 1 23.701 39.102 27.940 1.00 82.12 B C

ATOM 2798 CG2 VAL B 1 22.307 41.115 27.469 1.00 80.67 B C

ATOM 2799 C VAL B 1 19.830 39.324 27.895 1.00 82.10 B C

ATOM 2800 O VAL B 1 19.035 38.597 28.497 1.00 82.19 B O

ATOM 2801 N VAL B 1 21.358 38.643 26.048 1.00 82.72 B N

ATOM 2802 CA VAL B 1 21.217 38.800 27.521 1.00 81.98 B C

ATOM 2803 N SEP B 2 19.515 40.545 27.461 1.00 81.49 B N

ATOM 2804 CA SEP B 2 18.236 41.185 27.778 1.00 80.59 B C

ATOM 2805 CB SEP B 2 18.484 42.644 28.142 1.00 75.26 B C

ATOM 2806 OG SEP B 2 17.792 43.018 29.313 1.00 67.40 B O

ATOM 2807 C SEP B 2 17.208 41.184 26.646 1.00 83.73 B C

ATOM 2808 O SEP B 2 16.557 40.176 26.361 1.00 83.80 B O

ATOM 2809 P SEP B 2 18.543 43.859 30.470 1.00 61.96 B P

ATOM 2810 O1P SEP B 2 18.083 45.275 30.375 1.00 63.44 B O

ATOM 2811 O2P SEP B 2 18.130 43.447 31.826 1.00 59.37 B O

ATOM 2812 O3P SEP B 2 19.970 43.523 30.331 1.00 64.76 B O

ATOM 2813 N ARG B 3 17.019 42.375 26.088 1.00 87.21 B N

ATOM 2814 CA ARG B 3 16.080 42.643 25.011 1.00 91.65 B C

ATOM 2815 CB ARG B 3 14.679 42.120 25.373 1.00 92.13 B C ATOM 2816 CG ARG B 3 13.569 42.466 24.373 1.00 92.21 B C

ATOM 2817 CD ARG B 3 13.913 42.042 22.941 1.00 92.25 B C

ATOM 2818 NE ARG B 3 14.104 40.599 22.801 1.00 93.15 B N

ATOM 2819 CZ ARG B 3 14.938 40.033 21.930 1.00 93.75 B C

ATOM 2820 NHl ARG B 3 15.665 40.789 21.113 1.00 93.91 B N

ATOM 2821 NH2 ARG B 3 15.053 38.711 21.879 1.00 93.24 B N

ATOM 2822 C ARG B 3 16.068 44.164 24.911 1.00 94.89 B C

ATOM 2823 O ARG B 3 15.757 44.856 25.891 1.00 94.58 B O

ATOM 2824 N ARG B 4 16.439 44.677 23.740 1.00 98.73 B N

ATOM 2825 CA ARG B 4 16.497 46.119 23.509 1.00103.02 B C

ATOM 2826 CB ARG B 4 17.252 46.404 22.203 1.00101.19 B C

ATOM 2827 CG ARG B 4 17.736 47.837 22.086 1.00100.25 B C

ATOM 2828 CD ARG B 4 18.906 47.974 21.123 1.00 99.56 B C

ATOM 2829 NE ARG B 4 19.576 49.262 21.303 1.00 98.46 B N

ATOM 2830 CZ ARG B 4 19.829 50.129 20.326 1.00 97.17 B C

ATOM 2831 NHl ARG B 4 19.475 49.856 19.078 1.00 96.96 B N

ATOM 2832 NH2 ARG B 4 20.432 51.278 20.603 1.00 95.91 B N

ATOM 2833 C ARG B 4 15.121 46.814 23.504 1.00107.14 B C

ATOM 2834 O ARG B 4 14.153 46.286 22.957 1.00107.35 B O

ATOM 2835 N PRO B 5 15.016 48.000 24.143 1.00111.23 B N

ATOM 2836 CD PRO B 5 16.051 48.646 24.972 1.00112.66 B C ATOM 2837 CA PRO B 5 13.753 48.756 24.202 1.00113.91 B C

ATOM 2838 CB PRO B 5 14.097 49.945 25.119 1.00113.87 B C

ATOM 2839 CG PRO B 5 15.595 50.092 24.979 1.00113.39 B C

ATOM 2840 C PRO B 5 13.200 49.210 22.837 1.00116.16 B C

ATOM 2841 O PRO B 5 13.957 49.492 21.904 1.00116.49 B O

ATOM 2842 N SEP B 6 11.870 49.284 22.749 1.00118.72 B N

ATOM 2843 CA SEP B 6 11.152 49.668 21.528 1.00120.60 B C

ATOM 2844 CB SEP B 6 10.079 48.609 21.211 1.00122.57 B C

ATOM 2845 OG SEP B 6 10.659 47.324 20.975 1.00125.89 B O

ATOM 2846 P SEP B 6 10.404 46.005 21.940 1.00127.40 B P

ATOM 2847 O1P SEP B 6 11.195 44.861 21.359 1.00127.04 B O

ATOM 2848 O2P SEP B 6 10.994 46.165 23.300 1.00128.18 B O

ATOM 2849 O3P SEP B 6 8.936 45.899 22.124 1.00127.08 B O

ATOM 2850 C SEP B 6 10.488 51.053 21.670 1.00120.63 B C

ATOM 2851 OT1 SEP B 6 11.224 52.065 21.637 1.00120.40 B O

ATOM 2852 OXT SEP B 6 9.241 51.115 21.795 1.00120.72 B O

TER 2853 SEP B 6 B

ATOM 2854 PB ADP C 96 33.471 35.320 29.692 1.00 47.42 ADP P

ATOM 2855 O1B ADP C 96 34.093 34.088 30.298 1.00 44.20 ADP O

ATOM 2856 O2B ADP C 96 33.166 35.260 28.037 1.00 42.68 ADP O

ATOM 2857 O3B ADP C 96 32.183 35.599 30.395 1.00 49.46 ADP O ATOM 2858 PA ADP C 96 35.306 37.208 28.500 1.00 38.40 ADP P

ATOM 2859 O1A ADP C 96 35.895 38.477 28.913 1.00 33.24 ADP O

ATOM 2860 O2A ADP C 96 34.315 37.309 27.357 1.00 35.71 ADP O

ATOM 2861 O3A ADP C 96 34.554 36.496 29.734 1.00 42.89 ADP O

ATOM 2862 O19 ADP C 96 36.409 36.135 28.135 1.00 40.70 ADP O

ATOM 2863 C18 ADP C 96 37.739 36.445 27.762 1.00 39.43 ADP C

ATOM 2864 C17 ADP C 96 38.549 35.237 28.242 1.00 37.73 ADP C

ATOM 2865 O16 ADP C 96 39.926 35.405 27.909 1.00 39.45 ADP O

ATOM 2866 C15 ADP C 96 38.492 35.023 29.765 1.00 38.02 ADP C

ATOM 2867 O14 ADP C 96 37.745 33.880 30.173 1.00 37.38 ADP O

ATOM 2868 C13 ADP C 96 39.902 34.896 30.270 1.00 38.92 ADP C

ATOM 2869 O12 ADP C 96 40.146 33.587 30.794 1.00 39.07 ADP O

ATOM 2870 C11 ADP C 96 40.774 35.244 29.080 1.00 41.85 ADP C

ATOM 2871 N10 ADP C 96 41.712 36.455 29.364 1.00 41.53 ADP N

ATOM 2872 C9 ADP C 96 43.062 36.353 29.559 1.00 39.70 ADP C

ATOM 2873 N8 ADP C 96 43.587 37.564 29.772 1.00 36.28 ADP N

ATOM 2874 C7 ADP C 96 42.619 38.435 29.740 1.00 39.29 ADP C

ATOM 2875 C6 ADP C 96 42.542 39.796 29.859 1.00 39.23 ADP C

ATOM 2876 N5 ADP C 96 43.633 40.519 30.114 1.00 37.34 ADP N

ATOM 2877 N4 ADP C 96 41.339 40.405 29.755 1.00 44.99 ADP N

ATOM 2878 C3 ADP C 96 40.202 39.702 29.497 1.00 42.78 ADP C ATOM 2879 N2 ADP C 96 40.262 38.385 29.362 1.00 38.79 ADP N

ATOM 2880 CI ADP C 96 41.408 37.721 29.450 1.00 38.91 ADP C

TER 2881 ADP C 96 ADP

ATOM 2882 OH2 TIP 1 37.614 24.548 42.639 1.00 30.08 S O

ATOM 2883 OH2 TIP 2 32.674 26.543 36.071 1.00 29.91 S O

ATOM 2884 OH2 TIP 3 28.976 48.935 47.768 1.00 28.66 S O

ATOM 2885 OH2 TIP 4 37.738 22.847 51.778 1.00 33.12 S O

ATOM 2886 OH2 TIP 5 43.802 47.292 37.017 1.00 28.37 S O

ATOM 2887 OH2 TIP 6 49.392 29.259 42.658 1.00 32.65 S O

ATOM 2888 OH2 TIP 7 38.998 50.786 32.685 1.00 25.50 S O

ATOM 2889 OH2 TIP 8 36.790 23.947 39.558 1.00 33.61 S O

ATOM 2890 OH2 TIP 9 39.779 30.462 32.033 1.00 25.94 S O

ATOM 2891 OH2 TIP 10 23.267 28.801 41.609 1.00 27.49 S O

ATOM 2892 OH2 TIP 11 26.713 37.609 38.682 1.00 24.60 S O

ATOM 2893 OH2 TIP 12 27.633 26.163 41.315 1.00 21.83 S O

ATOM 2894 OH2 TIP 13 43.665 33.333 30.694 1.00 35.98 S O

ATOM 2895 OH2 TIP 14 40.153 27.668 30.495 1.00 32.97 S O

ATOM 2896 OH2 TIP 15 43.621 41.169 16.055 1.00 41.82 S O

ATOM 2897 OH2 TIP 16 44.310 24.341 34.334 1.00 34.18 S O

ATOM 2898 OH2 TIP 17 51.648 27.387 48.125 1.00 53.31 S O

ATOM 2899 OH2 TIP 18 29.611 34.850 60.678 1.00 47.87 S O ATOM 2900 OH2 TIP 19 23.146 35.582 40.243 1.00 28.50 S O

ATOM 2901 OH2 TIP 20 37.034 42.300 30.493 1.00 33.58 S O

ATOM 2902 OH2 TIP 21 47.884 47.445 36.937 1.00 32.44 S O

ATOM 2903 OH2 TIP 22 32.467 37.655 60.695 1.00 37.71 S O

ATOM 2904 OH2 TIP 23 41.786 51.156 43.578 1.00 44.25 S O

ATOM 2905 OH2 TIP 24 30.713 26.255 60.849 1.00 34.45 S O

ATOM 2906 OH2 TIP 25 43.060 53.870 32.088 1.00 44.99 S O

ATOM 2907 OH2 TIP 26 52.130 53.156 24.222 1.00 44.73 S O

ATOM 2908 OH2 TIP 27 24.267 29.221 31.552 1.00 38.95 S O

ATOM 2909 OH2 TIP 28 49.120 45.157 44.532 1.00 42.88 S O

ATOM 2910 OH2 TIP 29 43.249 52.213 41.174 1.00 33.64 S O

ATOM 2911 OH2 TIP 30 9.208 48.177 40.018 1.00 42.03 S O

ATOM 2912 OH2 TIP 31 16.850 50.229 18.553 1.00 58.28 S O

ATOM 2913 OH2 TIP 32 50.662 43.082 54.636 1.00 36.48 S O

ATOM 2914 OH2 TIP 33 13.439 37.991 31.209 1.00 33.60 S O

ATOM 2915 OH2 TIP 34 25.684 17.185 52.610 1.00 43.92 S O

ATOM 2916 OH2 TIP 35 28.975 19.204 43.354 1.00 42.57 S O

ATOM 2917 OH2 TIP 36 33.283 22.454 62.532 1.00 51.22 S O

ATOM 2918 OH2 TIP 37 22.186 29.863 54.142 1.00 46.37 S O

ATOM 2919 OH2 TIP 38 27.789 32.961 61.168 1.00 51.05 S O

ATOM 2920 OH2 TIP 39 24.049 53.393 43.944 1.00 37.40 S O ATOM 2921 OH2 TIP 40 49.154 31.325 55.519 1.00 30.82 S O

ATOM 2922 OH2 TIP 41 54.775 41.195 45.154 1.00 43.68 S O

ATOM 2923 OH2 TIP 42 47.369 47.566 9.871 1.00 41.01 S O

ATOM 2924 OH2 TIP 43 54.622 36.086 29.775 1.00 37.49 S O

ATOM 2925 OH2 TIP 44 40.435 46.225 9.607 1.00 41.30 S O

ATOM 2926 OH2 TIP 45 22.035 27.764 57.363 1.00 45.26 S O

ATOM 2927 OH2 TIP 46 33.267 31.533 29.843 1.00 40.42 S O

ATOM 2928 OH2 TIP 47 21.762 47.364 45.382 1.00 38.82 S O

ATOM 2929 OH2 TIP 48 58.121 44.019 53.336 1.0048.52 S O

ATOM 2930 OH2 TIP 49 36.765 56.356 41.574 1.00 54.37 S O

ATOM 2931 OH2 TIP 50 24.534 43.501 29.287 1.0041.69 S O

ATOM 2932 OH2 TIP 51 35.058 20.889 50.922 1.00 48.01 S O

ATOM 2933 OH2 TIP 52 13.886 39.904 42.973 1.00 56.12 S O

ATOM 2934 OH2 TIP 53 16.328 35.883 23.460 1.00 48.03 S O

ATOM 2935 OH2 TIP 54 19.016 58.276 40.961 1.00 56.32 S O

ATOM 2936 OH2 TIP 55 41.544 40.262 2.500 1.00 46.18 S O

ATOM 2937 OH2 TIP 56 44.279 55.225 57.112 1.00 42.91 S O

ATOM 2938 OH2 TIP 57 14.621 26.661 53.689 1.00 40.46 S O

ATOM 2939 OH2 TIP 58 22.480 50.514 26.918 1.00 48.08 S O

ATOM 2940 OH2 TIP 59 40.544 58.184 45.516 1.00 36.43 S O

ATOM 2941 OH2 TIP 60 28.046 57.913 39.878 1.00 51.50 S O ATOM 2942 OH2 TIP 61 39.964 53.691 60.049 1.00 45.68 S O

ATOM 2943 OH2 TIP 62 41.938 63.496 30.969 1.00 54.21 S O

ATOM 2944 OH2 TIP 63 35.807 21.046 38.176 1.00 43.54 S O

ATOM 2945 OH2 TIP 64 22.071 38.798 14.766 1.00 47.50 S O

ATOM 2946 OH2 TIP 65 52.246 34.086 16.948 1.00 56.85 S O

ATOM 2947 OH2 TIP 66 12.969 46.862 37.866 1.00 48.26 S O

ATOM 2948 OH2 TIP 67 32.618 34.031 20.366 1.00 47.96 S O

ATOM 2949 OH2 TIP 68 42.491 44.502 14.078 1.00 43.80 S O

ATOM 2950 OH2 TIP 69 28.879 18.119 48.981 1.00 47.32 S O

ATOM 2951 OH2 TIP 70 47.866 26.718 35.776 1.00 43.68 S O

ATOM 2952 OH2 TIP 71 51.653 29.326 53.522 1.00 50.51 S O

ATOM 2953 OH2 TIP 72 27.530 27.567 34.559 1.00 36.31 S O

ATOM 2954 OH2 TIP 73 43.448 35.329 61.731 1.00 46.58 S O

ATOM 2955 OH2 TIP 74 13.760 44.396 53.266 1.00 43.30 S O

ATOM 2956 OH2 TIP 75 49.912 51.983 34.635 1.00 39.49 S O

ATOM 2957 OH2 TIP 76 47.211 48.560 50.927 1.00 29.73 S O

ATOM 2958 OH2 TIP 77 20.660 23.190 58.655 1.00 58.96 S O

ATOM 2959 OH2 TIP 78 25.392 41.268 12.909 1.00 50.54 S O

ATOM 2960 OH2 TIP 79 18.414 53.555 42.040 1.00 33.95 S O

ATOM 2961 OH2 TIP 80 38.389 48.986 34.941 1.00 37.30 S O

ATOM 2962 OH2 TIP 81 30.056 44.675 22.094 1.00 49.21 S O ATOM 2963 OH2 TIP 82 33.883 32.890 62.125 1.00 47.01 S O

ATOM 2964 OH2 TIP 83 14.141 46.463 20.036 1.00 49.20 S O

ATOM 2965 OH2 TIP 84 32.345 16.403 51.561 1.00 59.53 S O

ATOM 2966 OH2 TIP 85 16.280 42.332 47.016 1.00 54.91 S O

ATOM 2967 OH2 TIP 86 56.299 43.978 62.800 1.00 53.85 S O

ATOM 2968 OH2 TIP 87 39.623 52.317 13.650 1.00 53.90 S O

ATOM 2969 OH2 TIP 88 3.822 34.078 53.161 1.00 45.64 S O

ATOM 2970 OH2 TIP 89 46.952 21.914 48.519 1.00 36.91 S O

ATOM 2971 OH2 TIP 90 44.388 13.268 47.302 1.00 55.98 S O

ATOM 2972 OH2 TIP 91 25.913 23.929 60.193 1.00 69.29 S O

ATOM 2973 OH2 TIP 92 15.259 25.158 31.304 1.00 49.66 S O

ATOM 2974 OH2 TIP 93 40.649 56.382 53.093 1.00 49.07 S O

ATOM 2975 OH2 TIP 94 17.371 27.378 53.774 1.00 43.50 S O

ATOM 2976 OH2 TIP 95 36.389 21.782 35.209 1.00 44.35 S O

ATOM 2977 OH2 TIP 96 44.744 39.555 6.616 1.00 46.67 S O

ATOM 2978 OH2 TIP 97 9.970 44.788 37.824 1.00 44.81 S O

ATOM 2979 OH2 TIP 98 24.129 43.481 48.119 1.00 42.31 S O

ATOM 2980 OH2 TIP 99 38.604 65.156 21.999 1.00 39.47 S O

ATOM 2981 OH2 TIP 100 60.337 48.176 25.733 1.00 48.72 S O

ATOM 2982 OH2 TIP 101 22.010 24.865 54.650 1.00 38.82 S O

ATOM 2983 OH2 TIP 102 30.955 41.414 25.553 1.00 53.24 S O ATOM 2984 OH2 TIP 103 49.651 26.977 31.613 1.00 48.95 S O

ATOM 2985 OH2 TIP 104 56.482 49.787 30.885 1.00 65.25 S O

ATOM 2986 OH2 TIP 105 46.340 45.344 43.520 1.00 45.31 S O

ATOM 2987 OH2 TIP 106 14.977 28.933 32.619 1.00 38.78 S O

ATOM 2988 OH2 TIP 107 56.104 37.575 58.211 1.00 47.83 S O

ATOM 2989 OH2 TIP 108 41.940 44.597 62.550 1.00 57.32 S O

ATOM 2990 OH2 TIP 109 45.687 50.954 43.171 1.00 42.89 S O

ATOM 2991 OH2 TIP 110 2.086 39.603 38.590 1.00 66.59 S O

ATOM 2992 OH2 TIP 111 40.351 24.401 60.082 1.00 75.01 S O

ATOM 2993 OH2 TIP 112 19.111 38.206 18.146 1.00 41.19 S O

ATOM 2994 OH2 TIP 113 43.454 37.606 63.990 1.00 62.50 S O

ATOM 2995 OH2 TIP 114 42.139 20.942 29.257 1.00 40.32 S O

ATOM 2996 OH2 TIP 115 41.880 51.132 36.408 1.00 39.00 S O

ATOM 2997 OH2 TIP 116 31.511 29.105 62.997 1.00 41.99 S O

ATOM 2998 OH2 TIP 117 51.119 40.450 33.476 1.00 38.15 S O

ATOM 2999 OH2 TIP 118 49.058 46.834 53.066 1.00 55.54 S O

ATOM 3000 OH2 TIP 119 27.461 24.253 31.296 1.00 49.05 S O

ATOM 3001 OH2 TIP 120 26.884 19.778 47.851 1.00 42.39 S O

ATOM 3002 OH2 TIP 121 57.142 42.263 48.872 1.00 42.97 S O

ATOM 3003 OH2 TIP 122 59.011 41.470 44.710 1.0046.77 S O

ATOM 3004 OH2 TIP 123 9.437 42.980 32.259 1.00 39.15 S O ATOM 3005 OH2 TIP 124 43.418 56.347 41.714 1.00 39.04 S O

ATOM 3006 OH2 TIP 125 47.258 19.642 37.741 1.00 29.93 S O

ATOM 3007 OH2 TIP 126 38.114 44.410 64.709 1.00 49.06 S O

ATOM 3008 OH2 TIP 127 55.332 29.406 45.454 1.00 62.34 S O

ATOM 3009 OH2 TIP 128 49.121 55.958 11.620 1.00 47.32 S O

ATOM 3010 OH2 TIP 129 51.937 41.204 45.436 1.00 41.64 S O

ATOM 3011 OH2 TIP 130 38.419 61.242 32.284 1.00 52.63 S O

ATOM 3012 OH2 TIP 131 26.891 31.505 25.814 1.00 48.64 S O

ATOM 3013 OH2 TIP 132 21.947 15.755 57.484 1.00 51.94 S O

ATOM 3014 OH2 TIP 133 19.192 16.280 54.429 1.00 57.94 S O

ATOM 3015 OH2 TIP 134 49.652 24.281 50.748 1.00 54.31 S O

ATOM 3016 OH2 TIP 135 45.871 54.230 27.371 1.00 46.12 S O

ATOM 3017 OH2 TIP 136 34.044 58.747 38.213 1.00 53.08 S O

ATOM 3018 OH2 TIP 137 20.834 14.951 47.923 1.00 79.72 S O

ATOM 3019 OH2 TIP 138 11.234 46.371 26.007 1.00 41.81 S O

ATOM 3020 OH2 TIP 139 21.863 36.871 23.804 1.00 54.35 S O

ATOM 3021 OH2 TIP 140 40.464 33.664 60.063 1.00 49.84 S O

ATOM 3022 OH2 TIP 141 8.216 47.553 26.261 1.00 60.31 S O

ATOM 3023 OH2 TIP 142 51.926 45.284 47.051 1.00 51.74 S O

ATOM 3024 OH2 TIP 143 17.335 48.464 28.268 1.00109.91 S O

ATOM 3025 OH2 TIP 144 28.841 43.961 -1.494 1.00 53.54 S O ATOM 3026 OH2 TIP 145 30.365 27.938 33.491 1.00 70.00 S O

ATOM 3027 OH2 TIP 146 20.509 44.273 49.023 1.00 49.63 S O

ATOM 3028 OH2 TIP 147 33.412 14.069 41.724 1.00 67.32 S O

ATOM 3029 OH2 TIP 148 55.179 32.407 53.701 1.00 48.38 S O

ATOM 3030 OH2 TIP 149 29.898 47.226 2.890 1.00 48.69 S O

ATOM 3031 OH2 TIP 150 18.125 28.926 26.869 1.00 44.15 S O

ATOM 3032 OH2 TIP 151 49.583 59.244 21.010 1.00 58.07 S O

ATOM 3033 OH2 TIP 152 52.174 34.230 28.143 1.00 48.65 S O

ATOM 3034 OH2 TIP 153 28.121 57.015 52.739 1.00 38.58 S O

ATOM 3035 OH2 TIP 154 44.194 28.871 57.719 1.00 57.76 S O

ATOM 3036 OH2 TIP 155 25.750 35.717 31.227 1.00 41.59 S O

ATOM 3037 OH2 TIP 156 53.171 47.082 59.301 1.00 44.51 S O

ATOM 3038 OH2 TIP 157 40.024 16.950 43.163 1.00 47.16 S O

ATOM 3039 OH2 TIP 1 30.135 26.823 42.209 1.00 38.18 S2 O

ATOM 3040 OH2 TIP 2 26.740 27.035 61.214 1.00 54.62 S2 O

ATOM 3041 OH2 TIP 3 37.111 63.675 28.567 1.00 53.33 S2 O

ATOM 3042 OH2 TIP 4 45.585 60.276 59.473 1.00 45.06 S2 O

ATOM 3043 OH2 TIP 5 44.287 33.287 65.508 1.00 54.07 S2 O

ATOM 3044 OH2 TIP 6 18.122 14.745 47.303 1.00 59.76 S2 O

ATOM 3045 OH2 TIP 7 31.081 41.110 6.258 1.00 55.31 S2 O

ATOM 3046 OH2 TIP 8 32.117 35.049 62.410 1.00 55.71 S2 O ATOM 3047 OH2 TIP 9 23.264 34.646 25.434 1.00 48.22 S2 O

ATOM 3048 OH2 TIP 10 11.942 47.740 28.204 1.00 52.81 S2 O

ATOM 3049 OH2 TIP 11 51.500 30.621 35.783 1.00 43.93 S2 O

ATOM 3050 OH2 TIP 12 44.436 57.094 39.270 1.00 46.42 S2 O

ATOM 3051 OH2 TIP 13 50.631 25.488 46.243 1.00 58.86 S2 O

ATOM 3052 OH2 TIP 14 48.345 31.234 30.399 1.00 50.48 S2 O

ATOM 3053 OH2 TIP 15 12.196 43.594 45.699 1.00 62.40 S2 O

ATOM 3054 OH2 TIP 16 52.735 30.385 40.337 1.00 59.49 S2 O

ATOM 3055 OH2 TIP 17 -0.876 28.719 40.420 1.00 65.29 S2 O

ATOM 3056 OH2 TIP 18 9.956 38.515 28.872 1.00 61.25 S2 O

ATOM 3057 OH2 TIP 19 33.912 9.937 41.712 1.00 54.20 S2 O

ATOM 3058 OH2 TIP 20 40.701 23.793 28.102 1.00 53.91 S2 O

ATOM 3059 OH2 TIP 21 22.786 59.706 41.265 1.00 60.58 S2 O

ATOM 3060 OH2 TIP 22 47.763 53.128 36.131 1.00 72.78 S2 O

ATOM 3061 OH2 TIP 23 36.918 62.026 45.954 1.00 60.21 S2 O

ATOM 3062 OH2 TIP 24 18.732 38.110 58.060 1.00 50.61 S2 O

ATOM 3063 OH2 TIP 25 29.752 20.272 35.535 1.00 52.93 S2 O

ATOM 3064 OH2 TIP 26 32.263 26.225 66.071 1.00 65.79 S2 O

ATOM 3065 OH2 TIP 27 46.076 49.812 40.653 1.00 44.93 S2 O

ATOM 3066 OH2 TIP 28 52.282 26.343 31.282 1.00 50.78 S2 O

ATOM 3067 OH2 TIP 29 30.710 60.585 38.033 1.00 62.34 S2 O ATOM 3068 OH2 TIP 30 29.436 28.269 66.530 1.00 72.80 S2 O

ATOM 3069 OH2 TIP 31 12.312 41.678 31.485 1.00 62.00 S2 O

ATOM 3070 OH2 TIP 32 48.531 49.645 45.658 1.00 56.81 S2 O

ATOM 3071 OH2 TIP 33 17.275 48.625 44.781 1.00 49.79 S2 O

ATOM 3072 OH2 TIP 34 34.720 24.509 32.066 1.00 54.66 S2 O

ATOM 3073 OH2 TIP 35 35.003 36.100 11.946 1.00 60.45 S2 O

ATOM 3074 OH2 TIP 36 24.570 31.918 59.493 1.00 65.83 S2 O

ATOM 3075 OH2 TIP 37 26.346 47.555 48.204 1.00 59.47 S2 O

ATOM 3076 OH2 TIP 38 17.855 47.113 48.430 1.00 59.77 S2 O

ATOM 3077 OH2 TIP 39 8.868 27.656 37.861 1.00 58.94 S2 O

ATOM 3078 OH2 TIP 40 52.463 45.676 64.501 1.00 53.60 S2 O

ATOM 3079 OH2 TIP 41 34.986 57.302 53.223 1.00 68.37 S2 O

ATOM 3080 OH2 TIP 42 27.614 56.546 45.392 1.00 60.22 S2 O

ATOM 3081 OH2 TIP 43 54.387 35.092 59.734 1.00 63.06 S2 O

ATOM 3082 OH2 TIP 44 34.307 22.272 59.708 1.00 58.20 S2 O

ATOM 3083 OH2 TIP 45 31.482 17.307 59.598 1.00 66.86 S2 O

ATOM 3084 OH2 TIP 46 38.629 28.849 26.984 1.00 67.10 S2 O

ATOM 3085 OH2 TIP 47 17.339 49.418 30.900 1.00 60.39 S2 O

ATOM 3086 OH2 TIP 48 7.548 16.489 51.658 1.00 69.42 S2 O

ATOM 3087 OH2 TIP 49 43.887 67.501 23.936 1.00 50.86 S2 O

ATOM 3088 OH2 TIP 50 49.064 46.587 40.492 1.00 59.08 S2 O ATOM 3089 OH2 TIP 51 45.936 53.901 51.981 1.00 55.31 S2 O

ATOM 3090 OH2 TIP 52 16.008 46.876 17.581 1.00 50.50 S2 O

ATOM 3091 OH2 TIP 53 16.553 46.946 42.091 1.00 55.64 S2 O

ATOM 3092 OH2 TIP 54 18.327 16.162 35.532 1.00 55.08 S2 O

ATOM 3093 OH2 TIP 55 29.189 28.138 30.559 1.00 50.26 S2 O

ATOM 3094 OH2 TIP 56 22.622 31.452 28.529 1.00 54.49 S2 O

ATOM 3095 OH2 TIP 57 56.809 35.090 18.492 1.00 80.17 S2 O

ATOM 3096 OH2 TIP 58 36.986 40.916 61.883 1.00 62.46 S2 O

ATOM 3097 OH2 TIP 59 38.678 53.126 43.052 1.00 51.60 S2 O

ATOM 3098 OH2 TIP 60 33.936 60.318 21.616 1.00 68.61 S2 O

ATOM 3099 OH2 TIP 61 21.246 57.192 42.724 1.00 54.85 S2 O

ATOM 3100 OH2 TIP 62 52.196 28.620 28.356 1.00 66.46 S2 O

ATOM 3101 OH2 TIP 63 51.548 52.552 29.029 1.00 57.51 S2 O

ATOM 3102 OH2 TIP 64 28.623 46.815 50.133 1.00 95.47 S2 O

ATOM 3103 OH2 TIP 65 0.980 38.378 36.256 1.00 58.96 S2 O

ATOM 3104 OH2 TIP 66 39.816 24.300 45.030 1.00 46.36 S2 O

ATOM 3105 OH2 TIP 67 17.241 34.153 21.709 1.00 69.76 S2 O

ATOM 3106 OH2 TIP 68 60.457 39.363 54.183 1.00 54.30 S2 O

ATOM 3107 OH2 TIP 69 29.664 10.401 58.320 1.00 51.22 S2 O

ATOM 3108 OH2 TIP 70 51.986 46.814 50.070 1.00 63.48 S2 O

ATOM 3109 OH2 TIP 71 49.739 45.640 32.649 1.00 68.23 S2 O ATOM 3110 OH2 TIP 72 12.027 54.886 36.495 1.00 55.37 S2 O

ATOM 3111 OH2 TIP 73 44.385 54.827 45.868 1.00 58.74 S2 O

ATOM 3112 OH2 TIP 74 51.888 27.430 56.253 1.00 52.15 S2 O

ATOM 3113 OH2 TIP 75 45.620 32.466 61.384 1.00 66.18 S2 O

ATOM 3114 OH2 TIP 76 40.285 46.837 64.089 1.00 63.00 S2 O

ATOM 3115 OH2 TIP 77 52.804 46.032 44.106 1.00 77.31 S2 O

ATOM 3116 OH2 TIP 78 40.983 40.978 61.850 1.00 51.00 S2 O

END

Table 3

REMARK refinement resolution: 50.0 - 2.6 A

REMARK starting r= 0.2425 free_r= 0.3110

REMARK final r= 0.2388 free_r= 0.3157

REMARK rmsd bonds= 0.014399 rmsd angles= 1.97234

REMARK wa= 5.28293

REMARK target= mlf cycles= 1 steps= 150

REMARK sg= P2(l) a= 56.855 b= 65.194 c= 57.372 alpha= 90 beta= 100.504 ganima= 90

REMARK parameter file 1 : MSI_CNX_TOPPAR:protein.param

REMARK parameter file 2 : ../pgatp_10mM/ptr.par

REMARK parameter file 3 : MSI_CNX_TOPPAR:ion.param

REMARK parameter file 4 : MSI_CNX_TOPPAR:water_rep.param

REMARK parameter file 5 : 911.par REMARK molecular structure file: water_pick.psf

REMARK input coordinates: bind_wp.pdb

REMARK reflection file= gsk3_7391 l_amalgam.fob.cv

REMARK ncs= none

REMARK B-correction resolution: 6.0 - 2.6

REMARK initial B-factor correction applied to fobs :

REMARK Bl l= -15.378 B22= 6.692 B33= 8.686

REMARK B12= 0.000 B13= 2.330 B23= 0.000

REMARK B-factor correction applied to coordinate array B: 0.538

REMARK bulk solvent: (Mask) density level= 0.267943 e/A^Λ3, B-factor= 14.8853 A^Λ2

REMARK reflections with |Fobs|/sigma_F < 0.0 rejected

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

REMARK theoretical total number of refl. in resol. range: 12818 ( 100.0 % )

REMARK number of unobserved reflections (no entry or |F|=0): 271 ( 2.1 % )

REMARK number of reflections rejected: 0 ( 0.0 % )

REMARK total number of reflections used: 12547 ( 97.9 % )

REMARK number of reflections in working set: 11903 ( 92.9 % )

REMARK number of reflections in test set: 644 ( 5.0 % )

REMARK Written by CNX VERSION:2000

ATOM 1 CB VAL A 37 -20.449 37.645 27.079 1.00 63.97 A C

ATOM 2 CGI VAL A 37 -21.351 38.789 27.514 1.00 64.03 A C ATOM 3 CG2VALA 37 -19.103 37.76827.790 1.0063.72 A C

ATOM 4 C VALA 37 -20.40735.08926.711 1.0064.64 A C

ATOM 5 O VALA 37 -19.58835.26825.797 1.0065.48 A O

ATOM 6 N VALA 37 -21.261 36.05628.866 1.0061.85 A N

ATOM 7 CA VALA 37 -21.133 36.26927.393 1.0063.68 A C

ATOM 8 N THRA 38 -20.815 33.881 27.097 1.0065.62 A N

ATOM 9 CA THRA 38 -20.235 32.62426.607 1.0065.68 A C

ATOM 10 CB THRA 38 -20.23031.54827.746 1.0065.84 A C

ATOM 11 OG1THRA 38 -19.75930.28927.241 1.0063.83 A O

ATOM 12 CG2THRA 38 -21.62731.38828.376 1.0066.38 A C

ATOM 13 C THRA 38 -20.773 32.00025.313 1.0066.01 A C

ATOM 14 O THRA 38 -21.97432.02725.048 1.0066.82 A O

ATOM 15 N THRA 39 -19.84931.44024.524 1.0066.48 A N

ATOM 16 CA THRA 39 -20.14630.75023.260 1.0066.51 A C

ATOM 17 CB THRA 39 -19.50431.44522.0301.0066.18 A C

ATOM 18 OG1THRA 39 -18.10031.57922.244 1.0066.67 A O

ATOM 19 CG2THRA 39 -20.11732.823 21.770 1.0065.27 A C

ATOM 20 C THRA 39 -19.56729.33323.374 1.0067.41 A C

ATOM 21 O THRA 39 -18.631 29.11324.148 1.0067.02 A O

ATOM 22 N VALA 40 -20.10428.39722.584 1.0068.28 A N

ATOM 23 CA VALA 40 -19.67726.98822.594 1.0068.51 A C ATOM 24 CB VALA 40 -20.66726.11823.479 1.0068.79 A C

ATOM 25 CGI VAL A 40 -22.11826.231 22.990 1.0069.33 A C

ATOM 26 CG2VALA 40 -20.221 24.66323.556 1.0068.92 A C

ATOM 27 C VALA 40 -19.47826.393 21.179 1.0068.20 A C

ATOM 280 VALA 40 -20.371 26.473 20.327 1.0069.61 A O

ATOM 29 N VALA 41 -18.29025.82520.940 1.0067.45 A N

ATOM 30 CA VALA 41 -17.91825.211 19.645 1.0067.05 A C

ATOM 31 CB VALA 41 -17.101 26.200 18.747 1.0067.26 A C

ATOM 32 CGI VAL A 41 -18.021 27.220 18.080 1.0067.96 A C

ATOM 33 CG2VALA 41 -16.01026.902 19.558 1.0067.07 A C

ATOM 34 C VALA 41 -17.10723.903 19.782 1.0066.87 A C

ATOM 350 VALA 41 -16.79523.48420.900 1.0066.42 A O

ATOM 36 N ALA A 42 -16.79423.263 18.645 1.0066.67 A N

ATOM 37 CA ALA A 42 -16.001 22.018 18.601 1.0066.46 A C

ATOM 38 CB ALA A 42 -16.86720.815 18.232 1.0066.57 A C

ATOM 39 C ALA A 42 -14.83622.162 17.621 1.0066.09 A C

ATOM 40 O ALA A 42 -15.01222.703 16.523 1.0064.72 A O

ATOM 41 N THRA 43 -13.67221.611 17.998 1.0066.01 A N

ATOM 42 CA THRA 43 -12.43421.733 17.202 1.0066.68 A C

ATOM 43 CB THRA 43 -11.81323.12017.490 1.0066.24 A C

ATOM 44 OG1THRA 43 -10.51423.207 16.894 1.0066.38 A O ATOM 45 CG2THRA 43 -11.73023.369 18.985 1.0066.90 A C

ATOM 46 C THRA 43 -11.32420.669 17.440 1.0066.97 A C

ATOM 47 O THRA 43 -11.27620.085 18.525 1.0068.13 A O

ATOM 48 N PROA 44 -10.42820.408 16.432 1.0066.74 A N

ATOM 49 CD PROA 44 -10.691 20.633 14.992 1.0066.39 A C

ATOM 50 CA PROA 44 -9.327 19.424 16.563 1.0067.07 A C

ATOM 51 CB PROA 44 -8.960 19.126 15.105 1.0066.81 A C

ATOM 52 CG PROA 44 -10.225 19.359 14.377 1.0067.07 A C

ATOM 53 C PROA 44 -8.064 19.811 17.381 1.0067.23 A C

ATOM 54 O PROA 44 -7.847 19.283 18.477 1.0065.63 A O

ATOM 55 N GLYA 45 -7.20520.656 16.804 1.0067.43 A N

ATOM 56 CA GLYA 45 -5.98621.082 17.473 1.0068.55 A C

ATOM 57 C GLYA 45 -4.69620.544 16.879 1.0070.54 A C

ATOM 58 O GLYA 45 -4.734 19.644 16.036 1.0070.42 A O

ATOM 59 N GLNA 46 -3.56221.093 17.340 1.0072.31 A N

ATOM 60 CA GLNA 46 -2.19620.716 16.912 1.0073.38 A C

ATOM 61 CB GLNA 46 -1.16721.740 17.463 1.0074.35 A C

ATOM 62 CG GLNA 46 0.28421.243 17.805 1.0075.04 A C

ATOM 63 CD GLNA 46 1.26921.245 16.638 1.0076.02 A C

ATOM 64 OEl GLNA 46 2.30621.916 16.687 1.0074.90 A O

ATOM 65 NE2GLNA 46 0.97720.453 15.611 1.0076.72 A N ATOM 66 C GLNA 46 -1.784 19.277 17.272 1.0073.69 A C

ATOM 67 O GLNA 46 -1.204 18.576 16.438 1.0073.44 A O

ATOM 68 N GLYA 47 -2.076 18.858 18.506 1.0074.61 A N

ATOM 69 CA GLYA 47 -1.729 17.518 18.967 1.0076.25 A C

ATOM 70 C GLYA 47 -2.553 16.398 18.337 1.0077.59 A C

ATOM 71 O GLYA 47 -2.708 16.388 17.104 1.0077.93 A O

ATOM 72 N PROA 48 -3.063 15.420 19.128 1.0078.09 A N

ATOM 73 CD PROA 48 -2.811 15.193 20.566 1.0078.23 A C

ATOM 74 CA PROA 48 -3.869 14.321 18.566 1.0078.51 A C

ATOM 75 CB PROA 48 -4.083 13.392 19.772 1.0078.25 A C

ATOM 76 CG PROA 48 -3.962 14.30820.961 1.0077.68 A C

ATOM 77 C PROA 48 -5.189 14.810 17.952 1.0078.48 A C

ATOM 780 PRO A 48 -5.930 15.573 18.587 1.0078.17 A O

ATOM 79 N ASP A 49 -5.421 14.421 16.693 1.0078.11 A N

ATOM 80 CA ASP A 49 -6.618 14.799 15.925 1.0077.95 A C

ATOM 81 CB ASP A 49 -6.440 14.398 14.449 1.0078.50 A C

ATOM 82 CG ASPA 49 -7.387 15.145 13.511 1.0078.95 A C

ATOM 83 OD1ASPA 49 -6.886 15.921 12.668 1.0078.90 A O

ATOM 84 OD2ASPA 49 -8.622 14.953 13.604 1.0078.68 A O

ATOM 85 C ASP A 49 -7.888 14.172 16.521 1.0077.47 A C

ATOM 860 ASP A 49 -8.339 13.098 16.100 1.0078.29 A O ATOM 87 N ARGA 50 -8.452 14.882 17.496 1.0076.39 A N

ATOM 88 CA ARGA 50 -9.645 14.458 18.219 1.0074.91 A C

ATOM 89 CB ARGA 50 -9.225 13.719 19.504 1.0077.01 A C

ATOM 90 CG ARGA 50 -10.371 13.18620.348 1.0078.74 A C

ATOM 91 CD ARGA 50 -10.070 11.79720.900 1.0079.88 A C

ATOM 92 NE ARGA 50 -11.260 11.15421.461 1.0080.00 A N

ATOM 93 CZ ARGA 50 -12.308 10.73320.752 1.0080.68 A C

ATOM 94 NHl ARGA 50 -12.349 10.873 19.428 1.0080.61 A N

ATOM 95 NH2ARGA 50 -13.333 10.17921.374 1.0081.57 A N

ATOM 96 C ARGA 50 -10.534 15.678 18.536 1.0072.67 A C

ATOM 970 ARGA 50 -10.265 16.420 19.491 1.0071.57 A O

ATOM 98 N PROA 51 -11.597 15.905 17.726 1.0070.55 A N

ATOM 99 CD PROA 51 -11.883 15.203 16.459 1.0070.53 A C

ATOM 100 CA PROA 51 -12.537 17.023 17.896 1.0068.80 A C

ATOM 101 CB PROA 51 -13.516 16.816 16.743 1.0069.04 A C

ATOM 102 CG PROA 51 -12.638 16.249 15.689 1.0069.83 A C

ATOM 103 C PROA 51 -13.239 17.081 19.252 1.0067.26 A C

ATOM 104 O PROA 51 -13.990 16.167 19.616 1.0068.56 A O

ATOM 105 N GLNA 52 -12.967 18.156 19.993 1.0064.23 A N

ATOM 106 CA GLNA 52 -13.532 18.35221.327 1.0062.31 A C

ATOM 107 CB GLNA 52 -12.443 18.18822.395 1.0060.62 A C ATOM 108 CG GLN A 52 -11.198 19.044 22.206 1.00 58.43 A C

ATOM 109 CD GLN A 52 -9.974 18.424 22.855 1.00 56.66 A C

ATOM 110 OEl GLN A 52 -9.515 18.882 23.898 1.00 57.67 A O

ATOM 111 NE2 GLN A 52 -9.443 17.370 22.239 1.00 53.32 A N

ATOM 112 C GLN A 52 -14.315 19.643 21.557 1.00 61.88 A C

ATOM 113 0 GLN A 52 -14.100 20.652 20.882 1.00 61.74 A O

ATOM 114 N _. GLU A 53 -15.203 19.591 22.550 1.00 61.18 A N

ATOM 115 CA GLU A 53 -16.063 20.708 22.930 1.00 60.09 A C

ATOM 116 CB GLU A 53 -17.328 20.168 23.628 1.00 61.08 A C

ATOM 117 CG GLU A 53 -18.446 21.192 23.806 1.00 63.17 A C

ATOM 118 CD GLU A 53 -19.666 20.636 24.515 1.00 64.14 A C

ATOM 119 OEI GLU A 53 -20.564 20.108 23.819 1.00 65.25 A O

ATOM 120 OE2 GLU A 53 -19.732 20.749 25.761 1.00 62.56 A O

ATOM 121 C GLU A 53 -15.350 21.750 23.809 1.00 58.28 A C

ATOM 122 O GLU A 53 -15.037 21.492 24.976 1.00 56.98 A O

ATOM 123 N VAL A 54 -15.057 22.906 23.210 1.00 57.67 A N

ATOM 124 CA VAL A 54 -14.405 24.026 23.899 1.00 57.21 A C

ATOM 125 CB VAL A 54 -13.072 24.470 23.207 1.00 58.22 A C

ATOM 126 CGI VAL A 54 -12.070 23.332 23.224 1.00 58.63 A C

ATOM 127 CG2 VAL A 54 -13.313 24.950 21.771 1.00 57.09 A C

ATOM 128 C VAL A 54 -15.359 25.218 24.004 1.00 56.95 A C ATOM 129 O VALA 54 -16.11825.511 23.069 1.0058.14 A O

ATOM 130 N SERA 55 -15.32025.89925.144 1.0055.99 A N

ATOM 131 CA SERA 55 -16.18727.04625.374 1.0055.55 A C

ATOM 132 CB SERA 55 -17.33626.67526.320 1.0056.90 A C

ATOM 133 OG SERA 55 -18.09225.58325.820 1.0057.74 A O

ATOM 134 C SERA 55 -15.41528.22625.936 1.0055.32 A C

ATOM 135 O SERA 55 -14.671 28.09026.916 1.0053.79 A O

ATOM 136 N TYRA 56 -15.60629.38225.300 1.0055.27 A N

ATOM 137 CA TYRA 56 -14.95030.61725.704 1.0054.08 A C

ATOM 138 CB TYRA 56 -13.90831.04824.656 1.0054.14 A C

ATOM 139 CG TYRA 56 -14.421 31.30423.247 1.0054.07 A C

ATOM 140 CDl TYRA 56 -14.31630.31322.249 1.0054.75 A C

ATOM 141 CE1TYRA 56 -14.73830.57320.907 1.0055.53 A C

ATOM 142 CD2TYRA 56 -14.961 32.561 22.887 1.0053.38 A C

ATOM 143 CE2TYRA 56 -15.38632.83221.562 1.0055.52 A C

ATOM 144 CZ TYRA 56 -15.271 31.83820.579 1.0055.95 A C

ATOM 145 OH TYRA 56 -15.67732.127 19.295 1.0058.36 A O

ATOM 146 C TYRA 56 -15.91831.75626.024 1.0053.58 A C

ATOM 1470 TYRA 56 -17.06631.74825.575 1.0053.02 A O

ATOM 148 N THRA 57 -15.413 32.75226.751 1.0053.31 A N

ATOM 149 C A THRA 57 -16.18033.93227.155 1.0052.73 A C ATOM 150 CB THR A 57 -16.763 33.749 28.603 1.00 51.39 A C

ATOM 151 OG1 THR A 57 -17.672 34.818 28.892 1.00 50.63 A O

ATOM 152 CG2 THR A 57 -15.654 33.694 29.671 1.00 48.86 A C

ATOM 153 C THR A 57 -15.306 35.203 27.059 1.00 53.61 A C

ATOM 154 O THR A 57 -14.207 35.159 26.500 1.00 52.98 A O

ATOM 155 N ASP A 58 -15.817 36.319 27.597 1.00 55.26 A N

ATOM 156 CA ASP A 58 -15.147 37.632 27.630 1.00 56.97 A C

ATOM 157 CB ASP A 58 -14.107 37.675 28.772 1.00 58.09 A C

ATOM 158 CG ASP A 58 -14.736 37.567 30.166 1.00 58.68 A C

ATOM 159 OD1 ASP A 58 -13.976 37.645 31.157 1.00 59.45 A O

ATOM 160 OD2 ASP A 58 -15.974 37.406 30.283 1.00 59.50 A O

ATOM 161 C ASP A 58 -14.536 38.073 26.287 1.00 57.52 A C

ATOM 162 0 ASP A 58 -13.385 38.526 26.221 1.00 58.39 A O

ATOM 163 N THR A 59 -15.328 37.928 25.223 1.00 57.12 A N

ATOM 164 CA THR A 59 -14.904 38.270 23.870 1.00 55.77 A C

ATOM 165 CB THR A 59 -15.766 37.544 22.809 1.00 55.17 A C

ATOM 166 OG1 THR A 59 -15.826 36.152 23.133 1.00 52.98 A O

ATOM 167 CG2 THR A 59 -15.144 37.663 21.422 1.00 54.68 A C

ATOM 168 C THR A 59 -14.841 39.778 23.626 1.00 56.17 A C

ATOM 169 O THR A 59 -15.842 40.496 23.731 1.00 56.02 A O

ATOM 170 N LYS A 60 -13.620 40.228 23.347 L00 56.47 A N ATOM 171 CA LYS A 60 -13.301 41.627 23.089 1.00 56.73 A C

ATOM 172 CB LYS A 60 -12.439 42.165 24.241 1.00 58.12 A C

ATOM 173 CG LYS A 60 -12.392 43.688 24.369 1.00 63.26 A C

ATOM 174 CD LYS A 60 -11.485 44.158 25.528 1.00 65.77 A C

ATOM 175 CE LYS A 60 -9.990 44.020 25.214 1.00 66.52 A C

ATOM 176 NZ LYS A 60 -9.112 44.513 26.320 1.00 68.79 A N

ATOM 177 C LYS A 60 -12.525 41.669 21.770 1.00 55.70 A C

ATOM 178 O LYS A 60 -11.749 40.762 21.481 1.00 55.63 A O

ATOM 179 N VAL A 61 -12.763 42.704 20.966 1.00 54.52 A N

ATOM 180 CA VAL A 61 -12.092 42.881 19.672 1.00 53.33 A C

ATOM 181 CB VAL A 61 -12.954 43.743 18.691 1.00 53.45 A C

ATOM 182 CGI VAL A 61 -12.413 43.654 17.260 1.00 51.55 A C

ATOM 183 CG2 VAL A 61 -14.416 43.337 18.744 1.00 52.75 A C

ATOM 184 C VAL A 61 -10.775 43.623 19.887 1.00 53.48 A C

ATOM 185 O VAL A 61 -10.783 44.741 20.414 1.00 53.86 A O

ATOM 186 N ILE A 62 -9.652 43.018 19.497 1.00 54.12 A N

ATOM 187 CA ILE A 62 -8.371 43.705 19.657 1.00 54.63 A C

ATOM 188 CB ILE A 62 -7.289 42.878 20.437 1.00 54.25 A C

ATOM 189 CG2 ILE A 62 -7.633 42.893 21.944 1.00 55.56 A C

ATOM 190 CGI ILE A 62 -7.138 41.461 19.886 1.00 51.93 A C

ATOM 191 CDl ILE A 62 -6.152 40.565 20.637 1.00 50.17 A C ATOM 192 C ILE A 62 -7.840 44.426 18.414 1.00 55.43 A C

ATOM 193 O ILE A 62 -6.781 45.061 18.458 1.00 58.47 A O

ATOM 194 N GLY A 63 -8.614 44.367 17.327 1.00 55.99 A N

ATOM 195 CA GLY A 63 -8.262 45.082 16.110 1.00 55.34 A C

ATOM 196 C GLY A 63 -8.092 44.406 14.767 1.00 55.89 A C

ATOM 197 0 GLY A 63 -8.640 43.336 14.484 1.00 55.20 A O

ATOM 198 N ASN A 64 -7.389 45.159 13.918 1.00 56.64 A N

ATOM 199 CA ASN A 64 -6.980 44.867 12.533 1.00 58.30 A C

ATOM 200 CB ASN A 64 -5.703 43.955 12.471 1.00 55.34 A C

ATOM 201 CG ASN A 64 -5.992 42.452 12.314 1.00 53.59 A C

ATOM 202 OD1 ASN A 64 -6.890 41.905 12.951 1.00 52.22 A O

ATOM 203 ND2 ASN A 64 -5.165 41.773 11.505 1.00 53.43 A N

ATOM 204 C ASN A 64 -7.982 44.544 11.436 1.00 60.09 A C

ATOM 205 O ASN A 64 -9.180 44.421 11.674 1.00 60.19 A O

ATOM 206 N GLY A 65 -7.444 44.459 10.225 1.00 61.52 A N

ATOM 207 CA GLY A 65 -8.215 44.147 9.045 1.00 63.20 A C

ATOM 208 C GLY A 65 -7.293 43.869 7.879 1.00 64.73 A C

ATOM 209 O GLY A 65 -7.779 43.735 6.744 1.00 66.51 A O

ATOM 210 N SER A 66 -5.979 43.765 8.162 1.00 63.40 A N

ATOM 211 CA SERA 66 -4.926 43.483 7.165 1.00 60.59 A C

ATOM 212 CB SER A 66 -3.598 43.174 7.857 1.00 61.32 A C ATOM 213 OG SER A 66 -2.579 42.933 6.898 1.00 58.93 A O

ATOM 214 C SER A 66 -5.419 42.274 6.401 1.00 59.23 A C

ATOM 215 0 SER A 66 -5.505 42.275 5.176 1.00 59.67 A O

ATOM 216 N PHE A 67 -5.751 41.262 7.192 1.00 57.91 A N

ATOM 217 CA PHE A 67 -6.383 40.012 6.802 1.00 57.58 A C

ATOM 218 CB PHE A 67 -5.677 39.120 5.745 1.00 59.96 A C

ATOM 219 CG PHE A 67 -4.197 38.992 5.887 1.00 63.34 A C

ATOM 220 CDl PHE A 67 -3.342 39.800 5.109 1.00 65.19 A C

ATOM 221 CD2 PHE A 67 -3.639 38.012 6.722 1.00 64.67 A C

ATOM 222 CE1 PHE A 67 -1.942 39.634 5.158 1.00 66.64 A C

ATOM 223 CE2 PHE A 67 -2.244 37.835 6.781 1.00 65.66 A C

ATOM 224 CZ PHE A 67 -1.395 38.648 5.996 1.00 66.74 A C

ATOM 225 C PHE A 67 -6.767 39.295 8.079 1.00 54.40 A C

ATOM 226 0 PHE A 67 -5.928 38.982 8.936 1.00 51.54 A O

ATOM 227 N GLY A 68 -8.082 39.249 8.261 1.00 51.86 A N

ATOM 228 CA GLY A 68 -8.679 38.643 9.424 1.00 48.19 A C

ATOM 229 C GLY A 68 -8.901 39.681 10.497 1.00 45.00 A C

ATOM 230 O GLY A 68 -8.550 40.851 10.348 1.00 44.50 A O

ATOM 231 N VAL A 69 -9.506 39.233 11.582 1.00 43.46 A N

ATOM 232 CA VAL A 69 -9.780 40.070 12.730 1.00 42.57 A C

ATOM 233 CB VAL A 69 -11.272 40.572 12.742 1.00 40.97 A C ATOM 234 CGI VAL A 69 -12.257 39.419 12.607 1.00 39.98 A C

ATOM 235 CG2 VAL A 69 -11.558 41.394 13.994 1.00 41.42 A C

ATOM 236 C VAL A 69 -9.409 39.229 13.951 1.00 41.72 A C

ATOM 237 O VAL A 69 -9.641 38.016 13.959 1.00 43.43 A O

ATOM 238 N VAL A 70 -8.732 39.841 14.924 1.00 39.49 A N

ATOM 239 CA VAL A 70 -8.343 39.112 16.129 1.00 36.66 A C

ATOM 240 CB VAL A 70 -6.818 39.148 16.373 1.00 34.76 A C

ATOM 241 CGI VAL A 70 -6.427 38.248 17.532 1.00 34.59 A C

ATOM 242 CG2 VAL A 70 -6.095 38.668 15.153 1.00 35.75 A C

ATOM 243 C VAL A 70 -9.114 39.537 17.376 1.00 36.48 A C

ATOM 244 O VAL A 70 -9.228 40.724 17.689 1.00 36.60 A O

ATOM 245 N TYR A 71 -9.635 38.536 18.081 1.00 35.72 A N

ATOM 246 CA TYR A 71 -10.393 38.744 19.304 1.00 34.83 A C

ATOM 247 CB TYR A 71 -11.723 37.979 19.252 1.00 33.13 A C

ATOM 248 CG TYR A 71 -12.676 38.416 18.160 1.00 33.84 A C

ATOM 249 CDl TYR A 71 -13.610 39.451 18.387 1.00 30.31 A C

ATOM 250 CE1 TYR A 71 -14.502 39.866 17.371 1.00 31.89 A C

ATOM 251 CD2 TYR A 71 -12.656 37.797 16.884 1.00 31.57 A C

ATOM 252 CE2 TYR A 71 -13.544 38.206 15.860 1.00 31.46 A C

ATOM 253 CZ TYRA 71 -14.462 39.244 16.110 1.00 32.48 A C

ATOM 254 OH TYR A 71 -15.294 39.695 15.105 1.00 34.90 A O ATOM 255 C TYR A 71 -9.610 38.248 20.506 1.00 35.20 A C

ATOM 256 O TYR A 71 -8.708 37.423 20.368 1.00 35.34 A O

ATOM 257 N GLN A 72 -9.934 38.791 21.674 1.00 35.83 A N

ATOM 258 CA GLN A 72 -9.331 38.362 22.928 1.00 38.84 A C

ATOM 259 CB GLN A 72 -8.910 39.558 23.782 1.00 39.22 A C

ATOM 260 CG GLN A 72 -8.210 39.178 25.095 1.00 42.43 A C

ATOM 261 CD GLN A 72 -8.169 40.317 26.107 1.00 45.69 A C

ATOM 262 OEl GLN A 72 -7.740 41.442 25.800 1.00 47.58 A O

ATOM 263 NE2 GLN A 72 -8.611 40.029 27.324 1.00 45.18 A N

ATOM 264 C GLN A 72 -10.464 37.623 23.639 1.00 40.58 A C

ATOM 265 O GLN A 72 -11.573 38.150 23.745 1.00 40.96 A O

ATOM 266 N ALA A 73 -10.197 36.406 24.103 1.00 41.34 A N

ATOM 267 CA ALA A 73 -11.209 35.628 24.814 1.00 42.89 A C

ATOM 268 CB ALA A 73 -11.998 34.754 23.840 1.00 45.03 A C

ATOM 269 C ALA A 73 -10.597 34.774 25.912 1.00 42.74 A C

ATOM 270 O ALA A 73 -9.411 34.463 25.872 1.00 43.66 A O

ATOM 271 N LYS A 74 -11.423 34.399 26.885 1.00 42.37 A N

ATOM 272 CA LYS A 74 -10.995 33.573 28.006 1.00 41.79 A C

ATOM 273 CB LYS A 74 -11.407 34.242 29.325 1.00 40.42 A C

ATOM 274 CG LYS A 74 -11.217 33.402 30.594 1.00 39.17 A C

ATOM 275 CD LYS A 74 -11.912 34.062 31.763 1.00 39.48 A C ATOM 276 CE LYS A 74 -12.145 33.091 32.893 1.00 39.54 A C

ATOM 277 NZ LYS A 74 -12.844 33.762 34.026 1.00 40.89 A N

ATOM 278 C LYS A 74 -11.597 32.172 27.918 1.00 43.34 A C

ATOM 279 O LYS A 74 -12.821 32.029 27.852 1.00 45.48 A O

ATOM 280 N LEU A 75 -10.741 31.147 27.918 1.00 43.14 A N

ATOM 281 CA LEU A 75 -11.194 29.752 27.902 1.00 43.75 A C

ATOM 282 CB LEU A 75 -10.034 28.786 27.670 1.00 42.46 A C

ATOM 283 CG LEU A 75 -9.250 28.779 26.366 1.00 42.04 A C

ATOM 284 CDl LEU A 75 -8.165 27.728 26.474 1.00 42.68 A C

ATOM 285 CD2 LEU A 75 -10.143 28.488 25.166 1.00 43.53 A C

ATOM 286 C LEU A 75 -11.780 29.476 29.288 1.00 45.42 A C

ATOM 287 O LEU A 75 -11.098 29.664 30.307 1.00 44.91 A O

ATOM 288 N CYS A 76 -13.051 29.073 29.308 1.00 47.32 A N

ATOM 289 CA CYS A 76 -13.805 28.782 30.535 1.00 47.32 A C

ATOM 290 CB CYS A 76 -15.250 28.429 30.182 1.00 46.97 A C

ATOM 291 SG CYS A 76 -16.185 29.686 29.273 1.00 46.90 A S

ATOM 292 C CYS A 76 -13.221 27.653 31.383 1.00 48.08 A C

ATOM 293 O CYS A 76 -13.314 27.688 32.613 1.00 48.28 A O

ATOM 294 N ASP A 77 -12.577 26.696 30.713 1.00 48.14 A N

ATOM 295 CA ASP A 77 -11.970 25.525 31.348 1.00 49.94 A C

ATOM 296 CB ASP A 77 -11.576 24.488 30.290 1.00 54.40 A C ATOM 297 CG ASP A 77 -12.50624.48729.092 1.0059.69 A C

ATOM 298 OD1ASPA 77 -12.33925.37528.219 1.0061.78 A O

ATOM 299 OD2ASPA 77 -13.401 23.611 29.032 1.0061.90 A O

ATOM 300 C ASP A 77 -10.74725.84232.204 1.0049.54 A C

ATOM 301 O ASP A 77 -10.79525.71633.428 1.0048.70 A O

ATOM 302 N SERA 78 -9.67526.29431.550 1.0050.53 A N

ATOM 303 CA SERA 78 -8.40226.61732.203 1.0050.36 A C

ATOM 304 CB SERA 78 -7.24926.32231.244 1.0049.94 A C

ATOM 305 OG SERA 78 -7.39927.03630.027 1.0051.20 A O

ATOM 306 C SERA 78 -8.25028.02732.793 1.0049.87 A C

ATOM 307 O SERA 78 -7.35428.263 33.620 1.0050.40 A O

ATOM 308 N GLYA 79 -9.11628.951 32.367 1.0048.73 A N

ATOM 309 CA GLYA 79 -9.06830.32832.852 1.0048.45 A C

ATOM 310 C GLYA 79 -7.931 31.11632.226 1.0047.57 A C

ATOM 311 0 GLYA 79 -7.39532.04932.827 1.0047.86 A O

ATOM 312 N GLUA 80 -7.55730.70431.017 1.0046.60 A N

ATOM 313 CA GLUA 80 -6.471 31.30730.261 1.0046.20 A C

ATOM 314 CB GLUA 80 -5.65030.21629.577 1.0047.50 A C

ATOM 315 CG GLUA 80 -4.81529.35930.510 1.0050.27 A C

ATOM 316 CD GLUA 80 -4.02728.301 29.760 1.0051.79 A C

ATOM 317 OEIGLUA 80 -4.58427.21629.502 1.0053.92 A O ATOM 318 OE2 GLU A 80 -2.854 28.556 29.416 1.00 52.56 A O

ATOM 319 C GLU A 80 -6.996 32.248 29.201 1.00 44.99 A C

ATOM 320 O GLU A 80 -8.135 32.119 28.764 1.00 46.86 A O

ATOM 321 N LEU A 81 -6.163 33.200 28.799 1.00 41.73 A N

ATOM 322 CA LEU A 81 -6.533 34.143 27.755 1.00 39.45 A C

ATOM 323 CB LEU A 81 -5.961 35.534 28.015 1.00 39.84 A C

ATOM 324 CG LEU A 81 -6.462 36.330 29.215 1.00 42.15 A C

ATOM 325 CDl LEU A 81 -5.616 35.986 30.443 1.00 46.21 A C

ATOM 326 CD2 LEU A 81 -6.348 37.815 28.920 1.00 43.31 A C

ATOM 327 C LEU A 81 -5.988 33.604 26.446 1.00 37.86 A C

ATOM 328 0 LEU A 81 -4.876 33.056 26.403 1.00 38.05 A O

ATOM 329 N VAL A 82 -6.792 33.718 25.393 1.00 34.14 A N

ATOM 330 CA VAL A 82 -6.416 33.249 24.063 1.00 32.45 A C

ATOM 331 CB VAL A 82 -7.149 31.940 23.645 1.00 34.24 A C

ATOM 332 CGI VAL A 82 -6.535 30.741 24.347 1.00 30.19 A C

ATOM 333 CG2 VAL A 82 -8.677 32.051 23.877 1.00 33.28 A C

ATOM 334 C VAL A 82 -6.715 34.295 23.019 1.00 30.95 A C

ATOM 335 O VAL A 82 -7.424 35.265 23.292 1.00 33.09 A O

ATOM 336 N ALA A 83 -6.150 34.097 21.832 1.00 29.50 A N

ATOM 337 CA ALA A 83 -6.367 34.986 20.702 1.00 28.28 A C

ATOM 338 CB ALA A 83 -5.091 35.561 20.228 1.00 27.06 A C ATOM 339 C ALA A 83 -7.019 34.180 19.599 1.00 29.27 A C

ATOM 340 O ALA A 83 -6.652 33.029 19.356 1.00 28.10 A O

ATOM 341 N ILE A 84 -8.023 34.781 18.964 1.00 31.89 A N

ATOM 342 CA ILE A 84 -8.778 34.139 17.889 1.00 33.15 A C

ATOM 343 CB ILE A 84 -10.306 34.028 18.257 1.00 32.07 A C

ATOM 344 CG2 ILE A 84 -11.111 33.397 17.097 1.00 31.51 A C

ATOM 345 CGI ILE A 84 -10.486 33.192 19.535 1.00 32.39 A C

ATOM 346 CDl ILE A 84 -11.863 33.275 20.162 1.00 33.33 A C

ATOM 347 C ILE A 84 -8.617 34.907 16.579 1.00 34.75 A C

ATOM 348 O ILE A 84 -9.122 36.024 16.447 1.00 34.78 A O

ATOM 349 N LYS A 85 -7.916 34.309 15.618 1.00 36.38 A N

ATOM 350 CA LYS A 85 -7.745 34.947 14.322 1.00 39.35 A C

ATOM 351 CB LYS A 85 -6.335 34.738 13.773 1.00 36.93 A C

ATOM 352 CG LYS A 85 -5.972 35.802 12.757 1.00 37.08 A C

ATOM 353 CD LYS A 85 -4.486 35.972 12.601 1.00 36.30 A C

ATOM 354 CE LYS A 85 -3.942 34.988 11.601 1.00 39.48 A C

ATOM 355 NZ LYS A 85 -4.487 35.151 10.216 1.00 37.35 A N

ATOM 356 C LYS A 85 -8.817 34.410 13.370 1.00 43.60 A C

ATOM 357 O LYS A 85 -8.708 33.293 12.850 1.00 43.72 A O

ATOM 358 N LYS A 86 -9.883 35.204 13.226 1.00 47.54 A N

ATOM 359 CA LYS A 86 -11.041 34.896 12.382 1.00 50.00 A C ATOM 360 CB LYS A 86 -12.318 35.495 12.994 1.00 51.56 A C

ATOM 361 CG LYS A 86 -13.643 35.056 12.367 1.00 53.09 A C

ATOM 362 CD LYS A 86 -14.824 35.658 13.136 1.00 55.36 A C

ATOM 363 CE LYS A 86 -16.161 35.050 12.738 1.00 55.87 A C

ATOM 364 NZ LYS A 86 -17.289 35.650 13.503 1.00 57.01 A N

ATOM 365 C LYS A 86 -10.793 35.447 10.992 1.00 50.80 A C

ATOM 366 O LYS A 86 -10.755 36.657 10.785 1.00 50.18 A O

ATOM 367 N VAL A 87 -10.600 34.532 10.051 1.00 53.53 A N

ATOM 368 CA VAL A 87 -10.322 34.867 8.662 1.00 54.79 A C

ATOM 369 CB VAL A 87 -8.840 34.463 8.292 1.00 53.70 A C

ATOM 370 CGI VAL A 87 -8.437 33.165 8.984 1.00 54.22 A C

ATOM 371 CG2 VAL A 87 -8.627 34.340 6.796 1.00 51.64 A C

ATOM 372 C VAL A 87 -11.367 34.274 7.715 1.00 57.22 A C

ATOM 373 O VAL A 87 -11.795 33.125 7.872 1.00 57.46 A O

ATOM 374 N LEU A 88 -11.816 35.105 6.777 1.00 59.24 A N

ATOM 375 CA LEU A 88 -12.784 34.705 5.762 1.00 61.71 A C

ATOM 376 CB LEU A 88 -13.593 35.934 5.287 1.00 61.62 A C

ATOM 377 CG LEU A 88 -14.676 35.989 4.182 1.00 61.11 A C

ATOM 378 CDl LEU A 88 -14.097 36.489 2.868 1.00 60.62 A C

ATOM 379 CD2 LEU A 88 -15.420 34.671 3.998 1.00 61.26 A C

ATOM 380 C LEU A 88 -11.983 34.103 4.615 1.00 63.45 A C ATOM 381 O LEU A 88 -11.949 32.882 4.453 1.00 62.58 A O

ATOM 382 N GLN A 89 -11.295 35.002 3.902 1.00 66.52 A N

ATOM 383 CA GLN A 89 -10.450 34.777 2.721 1.00 69.88 A C

ATOM 384 CB GLN A 89 -9.000 35.239 2.981 1.00 72.16 A C

ATOM 385 CG GLN A 89 -8.800 36.541 3.823 1.00 75.25 A C

ATOM 386 CD GLN A 89 -9.787 37.678 3.538 1.00 76.60 A C

ATOM 387 OEl GLN A 89 -9.835 38.227 2.435 1.00 77.91 A O

ATOM 388 NE2 GLN A 89 -10.565 38.044 4.556 1.00 76.81 A N

ATOM 389 C GLN A 89 -10.503 33.431 1.981 1.00 71.07 A C

ATOM 390 O GLN A 89 -9.579 32.608 2.048 1.00 70.30 A O

ATOM 391 N ASP A 90 -11.647 33.213 1.331 1.00 73.00 A N

ATOM 392 CA ASP A 90 -11.919 32.017 0.536 1.00 75.16 A C

ATOM 393 CB ASP A 90 -13.362 31.515 0.785 1.00 75.05 A C

ATOM 394 CG ASP A 90 -13.676 31.255 2.276 1.00 75.86 A C

ATOM 395 OD1 ASP A 90 -14.830 31.516 2.687 1.00 76.25 A O

ATOM 396 OD2 ASP A 90 -12.798 30.780 3.035 1.00 74.74 A O

ATOM 397 C ASP A 90 -11.748 32.527 -0.901 1.00 76.66 A C

ATOM 398 O ASP A 90 -12.723 32.715 -1.643 1.00 77.06 A O

ATOM 399 N LYS A 91 -10.492 32.805 -1.255 1.00 77.91 A N

ATOM 400 CA LYS A 91 -10.147 33.354 -2.564 1.00 79.52 A C

ATOM 401 CB LYS A 91 -9.440 34.706 -2.364 1.00 79.06 A C ATOM 402 CG LYS A 91 -9.886 35.805 -3.329 1.00 78.84 A C

ATOM 403 CD LYS A 91 -9.999 37.169 -2.644 1.00 78.71 A C

ATOM 404 CE LYS A 91 -11.320 37.318 -1.877 1.00 78.79 A C

ATOM 405 NZ LYS A 91 -11.477 38.650 -1.222 1.00 77.30 A N

ATOM 406 C LYS A 91 -9.319 32.420 -3.453 1.00 80.43 A C

ATOM 407 O LYS A 91 -9.050 31.272 -3.083 1.00 79.35 A O

ATOM 408 N ARG A 92 -8.965 32.919 -4.644 1.00 82.11 A N

ATOM 409 CA ARG A 92 -8.172 32.193 -5.642 1.00 84.06 A C

ATOM 410 CB ARG A 92 -8.375 32.799 -7.036 1.00 85.93 A C

ATOM 411 CG ARG A 92 -9.577 32.250 -7.814 1.00 88.55 A C

ATOM 412 CD ARG A 92 -9.386 30.795 -8.281 1.00 90.11 A C

ATOM 413 NE ARG A 92 -8.232 30.623 -9.171 1.00 91.97 A N

ATOM 414 CZ ARG A 92 -8.026 29.569 -9.965 1.00 93.33 A C

ATOM 415 NHl ARG A 92 -8.897 28.564 -10.009 1.00 93.76 A N

ATOM 416 NH2 ARG A 92 -6.927 29.506 -10.705 1.00 92.97 A N

ATOM 417 C ARG A 92 -6.681 32.133 -5.314 1.00 84.45 A C

ATOM 418 O ARG A 92 -5.932 31.359 -5.926 1.00 85.44 A O

ATOM 419 N PHE A 93 -6.258 32.980 -4.375 1.00 84.02 A N

ATOM 420 CA PHE A 93 -4.875 33.021 -3.905 1.00 83.00 A C

ATOM 421 CB PHE A 93 -4.533 34.400 -3.329 1.00 84.31 A C

ATOM 422 CG PHE A 93 -4.084 35.398 -4.357 1.00 86.67 A C ATOM 423 CDl PHE A 93 -2.759 35.374 -4.850 1.00 87.56 A C

ATOM 424 CD2 PHE A 93 -4.975 36.378 -4.838 1.00 87.66 A C

ATOM 425 CE1 PHE A 93 -2.317 36.322 -5.821 1.00 88.57 A C

ATOM 426 CE2 PHE A 93 -4.557 37.338 -5.810 1.00 88.84 A C

ATOM 427 CZ PHE A 93 -3.221 37.308 -6.303 1.00 89.04 A C

ATOM 428 C PHE A 93 -4.710 31.970 -2.812 1.00 81.99 A C

ATOM 429 O PHE A 93 -5.694 31.546 -2.187 1.00 82.59 A O

ATOM 430 N LYS A 94 -3.467 31.551 -2.588 1.00 79.57 A N

ATOM 431 CA LYS A 94 -3.152 30.559 -1.560 1.00 76.73 A C

ATOM 432 CB LYS A 94 -1.801 29.904 -1.860 1.00 76.69 A C

ATOM 433 CG LYS A 94 -1.675 29.263 -3.244 1.00 77.93 A C

ATOM 434 CD LYS A 94 -2.442 27.946 -3.343 1.00 80.11 A C

ATOM 435 CE LYS A 94 -2.302 27.316 -4.724 1.00 80.68 A C

ATOM 436 NZ LYS A 94 -3.130 26.083 -4.867 1.00 80.96 A N

ATOM 437 C LYS A 94 -3.103 31.233 -0.184 1.00 74.12 A C

ATOM 438 O LYS A 94 -2.766 32.414 -0.085 1.00 73.53 A O

ATOM 439 N ASN A 95 -3.515 30.506 0.853 1.00 71.17 A N

ATOM 440 CA ASN A 95 -3.478 31.021 2.224 1.00 67.52 A C

ATOM 441 CB ASN A 95 -4.800 30.757 2.951 1.00 67.06 A C

ATOM 442 CG ASN A 95 -4.759 31.171 4.421 1.00 67.16 A C

ATOM 443 OD1 ASN A 95 -4.492 32.330 4.753 1.00 65.03 A O ATOM 444 ND2 ASN A 95 -4.984 30.207 5.306 1.00 67.41 A N

ATOM 445 C ASN A 95 -2.316 30.347 2.957 1.00 64.89 A C

ATOM 446 O ASN A 95 -1.489 31.029 3.574 1.00 65.50 A O

ATOM 447 N ARG A 96 -2.307 29.009 2.908 1.00 60.67 A N

ATOM 448 CA ARG A 96 -1.290 28.122 3.505 1.00 57.24 A C

ATOM 449 CB ARG A 96 0.072 28.309 2.817 1.00 59.08 A C

ATOM 450 CG ARG A 96 0.128 27.932 1.349 1.00 60.20 A C

ATOM 451 CD ARG A 96 1.485 28.300 0.788 1.00 60.74 A C

ATOM 452 NE ARG A 96 1.642 27.932 -0.618 1.00 62.80 A N

ATOM 453 CZ ARG A 96 1.777 28.798 -1.620 1.00 62.08 A C

ATOM 454 NHl ARG A 96 1.776 30.110 -1.393 1.00 59.80 A N

ATOM 455 NH2 ARG A 96 1.950 28.349 -2.858 1.00 62.64 A N

ATOM 456 C ARG A 96 -1.076 28.137 5.022 1.00 53.84 A C

ATOM 457 O ARG A 96 -0.542 27.175 5.582 1.00 52.27 A O

ATOM 458 N GLU A 97 -1.512 29.211 5.675 1.00 50.79 A N

ATOM 459 CA GLU A 97 -1.351 29.410 7.115 1.00 48.93 A C

ATOM 460 CB GLU A 97 -2.110 30.663 7.559 1.00 47.48 A C

ATOM 461 CG GLU A 97 -1.973 30.971 9.038 1.00 48.39 A C

ATOM 462 CD GLU A 97 -2.501 32.318 9.430 1.00 50.87 A C

ATOM 463 OEI GLU A 97 -1.866 32.945 10.301 1.00 53.13 A O

ATOM 464 OE2 GLU A 97 -3.541 32.756 8.897 1.00 50.53 A O ATOM 465 C GLU A 97 -1.694 28.236 8.030 1.00 47.73 A C

ATOM 466 O GLU A 97 -0.858 27.815 8.829 1.00 48.73 A O

ATOM 467 N LEU A 98 -2.914 27.721 7.887 1.00 46.72 A N

ATOM 468 CA LEU A 98 -3.452 26.606 8.672 1.00 43.78 A C

ATOM 469 CB LEU A 98 -4.792 26.164 8.053 1.00 42.50 A C

ATOM 470 CG LEU A 98 -5.744 25.073 8.577 1.00 42.22 A C

ATOM 471 CDl LEU A 98 -5.392 23.663 8.035 1.00 41.98 A C

ATOM 472 CD2 LEU A 98 -5.836 25.116 10.091 1.00 40.51 A C

ATOM 473 C LEU A 98 -2.512 25.411 8.822 1.00 43.82 A C

ATOM 474 O LEU A 98 -2.161 25.039 9.941 1.00 42.54 A O

ATOM 475 N GLN A 99 -2.104 24.839 7.688 1.00 43.66 A N

ATOM 476 CA GLN A 99 -1.232 23.673 7.671 1.00 43.80 A C

ATOM 477 CB GLN A 99 -1.271 22.996 6.288 1.00 44.98 A C

ATOM 478 CG GLN A 99 -0.849 23.853 5.083 1.00 47.67 A C

ATOM 479 CD GLN A 99 0.506 23.437 4.494 1.00 49.93 A C

ATOM 480 OEl GLN A 99 1.125 24.191 3.736 1.00 50.40 A O

ATOM 481 NE2 GLN A 99 0.966 22.233 4.839 1.00 49.29 A N

ATOM 482 C GLN A 99 0.195 23.938 8.158 1.00 43.06 A C

ATOM 483 0 GLN A 99 0.888 23.021 8.614 1.00 44.55 A O

ATOM 484 N ILE A 100 0.601 25.204 8.105 1.00 41.89 A N

ATOM 485 CA ILE A 100 1.929 25.627 8.551 1.00 40.86 A C ATOM 486 CB ILE A 100 2.361 26.936 7.832 1.00 40.41 A C

ATOM 487 CG2 ILE A 100 3.397 27.737 8.645 1.00 41.53 A C

ATOM 488 CGI ILE A 100 2.874 26.573 6.435 1.00 39.91 A C

ATOM 489 CDl ILE A 100 3.162 27.750 5.527 1.00 40.69 A C

ATOM 490 C ILE A 100 1.973 25.736 10.077 1.00 39.97 A C

ATOM 491 O ILE A 100 2.921 25.267 10.691 1.00 39.96 A O

ATOM 492 N MET A 101 0.904 26.261 10.676 1.00 39.76 A N

ATOM 493 CA MET A 101 0.804 26.415 12.132 1.00 40.67 A C

ATOM 494 CB MET A 101 -0.372 27.322 12.489 1.00 39.39 A C

ATOM 495 CG MET A 101 -0.195 28.758 12.023 1.00 38.88 A C

ATOM 496 SD MET A 101 0.499 29.851 13.282 1.00 42.14 A S

ATOM 497 CE MET A 101 -0.668 31.237 13.182 1.00 37.39 A C

ATOM 498 C MET A 101 0.698 25.083 12.873 1.00 41.77 A C

ATOM 499 0 MET A 101 1.064 24.993 14.054 1.00 42.55 A O

ATOM 500 N ARG A 102 0.253 24.049 12.148 1.00 43.40 A N

ATOM 501 CA ARG A 102 0.100 22.682 12.675 1.00 44.45 A C

ATOM 502 CB ARG A 102 -1.021 21.933 11.938 1.00 45.97 A C

ATOM 503 CG ARG A 102 -2.422 22.480 12.168 1.00 48.87 A C

ATOM 504 CD ARG A 102 -3.483 21.662 11.434 1.00 51.77 A C

ATOM 505 NE ARG A 102 -3.672 20.337 12.029 1.00 55.60 A N

ATOM 506 CZ ARG A 102 -4.463 19.383 11.540 1.00 57.08 A C ATOM 507 NHl ARG A 102 -5.164 19.582 10.427 1.00 57.90 A N

ATOM 508 NH2 ARG A 102 -4.580 18.231 12.190 1.00 58.58 A N

ATOM 509 C ARG A 102 1.404 21.886 12.551 1.00 42.69 A C

ATOM 510 O ARG A 102 1.463 20.715 12.916 1.00 44.06 A O

ATOM 511 N LYS A 103 2.431 22.538 12.016 1.00 41.77 A N

ATOM 512 CA LYS A 103 3.752 21.942 11.813 1.00 40.65 A C

ATOM 513 CB LYS A 103 4.193 22.171 10.350 1.00 42.26 A C

ATOM 514 CG LYS A 103 5.438 21.397 9.860 1.00 44.81 A C

ATOM 515 CD LYS A 103 5.959 21.932 8.506 1.00 47.46 A C

ATOM 516 CE LYS A 103 5.016 21.613 7.324 1.00 50.80 A C

ATOM 517 NZ LYS A 103 5.299 22.401 6.073 1.00 50.60 A N

ATOM 518 C LYS A 103 4.755 22.595 12.770 1.00 37.52 A C

ATOM 519 0 LYS A 103 5.806 22.020 13.062 1.00 37.53 A O

ATOM 520 N LEU A 104 4.414 23.784 13.267 1.00 32.67 A N

ATOM 521 CA LEU A 104 5.303 24.521 14.154 1.00 30.44 A C

ATOM 522 CB LEU A 104 5.313 26.010 13.809 1.00 27.57 A C

ATOM 523 CG LEU A 104 5.501 26.420 12.349 1.00 25.33 A C

ATOM 524 CDl LEU A 104 5.358 27.916 12.251 1.00 21.03 A C

ATOM 525 CD2 LEU A 104 6.824 25.916 11.743 1.00 21.93 A C

ATOM 526 C LEU A 104 5.130 24.357 15.651 1.00 30.04 A C

ATOM 527 0 LEU A 104 4.025 24.381 16.189 1.00 28.26 A O ATOM 528 N ASP A 105 6.276 24.210 16.304 1.00 32.22 A N

ATOM 529 CA ASP A 105 6.379 24.066 17.742 1.00 33.54 A C

ATOM 530 CB ASP A 105 6.308 22.586 18.145 1.00 33.42 A C

ATOM 531 CG ASP A 105 6.280 22.384 19.648 1.00 32.07 A C

ATOM 532 OD1 ASP A 105 6.348 21.212 20.070 1.00 33.96 A O

ATOM 533 OD2 ASP A 105 6.199 23.381 20.405 1.00 31.71 A O

ATOM 534 C ASP A 105 7.725 24.685 18.143 1.00 34.25 A C

ATOM 535 0 ASP A 105 8.789 24.081 17.941 1.00 33.37 A O

ATOM 536 N HIS A 106 7.648 25.899 18.697 1.00 32.99 A N

ATOM 537 CA HIS A 106 8.811 26.662 19.150 1.00 29.56 A C

ATOM 538 CB HIS A 106 9.458 27.365 17.962 1.00 29.95 A C

ATOM 539 CG HIS A 106 10.858 27.830 18.203 1.00 29.98 A C

ATOM 540 CD2 HIS A 106 12.048 27.212 18.002 1.00 28.61 A C

ATOM 541 ND1 HIS A 106 11.154 29.110 18.623 1.00 28.32 A N

ATOM 542 CE1 HIS A 106 12.467 29.262 18.661 1.00 27.31 A C

ATOM 543 NE2 HIS A 106 13.032 28.127 18.289 1.00 27.49 A N

ATOM 544 C HIS A 106 8.338 27.697 20.164 1.00 28.43 A C

ATOM 545 0 HIS A 106 7.236 28.242 20.052 1.00 24.05 A O

ATOM 546 N CYS A 107 9.199 27.970 21.140 1.00 29.61 A N

ATOM 547 CA CYS A 107 8.939 28.933 22.208 1.00 30.22 A C

ATOM 548 CB CYS A 107 9.987 28.769 23.308 1.00 32.19 A C ATOM 549 SG CYS A 107 11.693 28.878 22.719 1.00 40.81 A S

ATOM 550 C CYS A 107 8.899 30.395 21.735 1.00 29.43 A C

ATOM 551 0 CYS A 107 8.377 31.268 22.442 1.00 30.02 A O

ATOM 552 N ASN A 108 9.445 30.656 20.547 1.00 27.53 A N

ATOM 553 CA ASN A 108 9.451 32.013 20.002 1.00 26.72 A C

ATOM 554 CB ASN A 108 10.872 32.457 19.647 1.00 24.38 A C

ATOM 555 CG ASN A 108 11.780 32.521 20.862 1.00 24.81 A C

ATOM 556 OD1 ASN A 108 12.949 32.106 20.815 1.00 24.17 A O

ATOM 557 ND2 ASN A 108 11.253 33.060 21.958 1.00 21.53 A N

ATOM 558 C ASN A 108 8.482 32.236 18.844 1.00 24.85 A C

ATOM 559 0 ASN A 108 8.624 33.190 18.069 1.00 22.84 A O

ATOM 560 N ILE A 109 7.491 31.342 18.754 1.00 22.79 A N

ATOM 561 CA ILE A 109 6.427 31.353 17.737 1.00 20.07 A C

ATOM 562 CB ILE A 109 6.676 30.280 16.625 1.00 19.83 A C

ATOM 563 CG2 ILE A 109 5.471 30.210 15.647 1.00 19.73 A C

ATOM 564 CGI ILE A 109 7.978 30.577 15.862 1.00 16.39 A C

ATOM 565 CDl ILE A 109 8.446 29.497 14.918 1.00 10.51 A C

ATOM 566 C ILE A 109 5.142 30.990 18.485 1.00 18.63 A C

ATOM 567 0 ILE A 109 5.157 30.050 19.279 1.00 18.91 A O

ATOM 568 N VAL A 110 4.049 31.726 18.246 1.00 17.94 A N

ATOM 569 CA VAL A 110 2.766 31.440 18.910 1.00 21.24 A C ATOM 570 CB VAL A 110 1.61732.425 18.576 1.0021.98 A C

ATOM 571 CGI VALA 110 1.57533.540 19.555 1.0021.89 A C

ATOM 572 CG2VALA110 1.701 32.918 17.154 1.0024.93 A C

ATOM 573 C VALA 110 2.231 30.064 18.601 1.0021.98 A C

ATOM 5740 VALA 110 2.221 29.628 17.440 1.0021.41 A O

ATOM 575 N ARG A 111 1.81729.384 19.663 1.0024.70 A N

ATOM 576 CA ARGA 111 1.27028.039 19.567 1.0028.73 A C

ATOM 577 CB ARG A 111 1.39227.32020.919 1.0029.40 A C

ATOM 578 CG ARGA 111 0.84925.88520.967 1.0035.17 A C

ATOM 579 CD ARG A 111 0.74625.343 22.403 1.0036.48 A C

ATOM 580 NE ARG A 111 0.02026.25423.289 1.0036.86 A N

ATOM 581 CZ ARG A 111 -0.25426.02024.571 1.0038.52 A C

ATOM 582 NHl ARGA 111 0.11524.881 25.156 1.0039.27 A N

ATOM 583 NH2 ARG A 111 -0.82326.973 25.301 1.0035.94 A N

ATOM 584 C ARGA 111 -0.19028.100 19.132 1.0029.34 A C

ATOM 585 O ARGA 111 -0.94828.971 19.582 1.0028.48 A O

ATOM 586 N LEUA112 -0.52827.247 18.165 1.0029.85 A N

ATOM 587 CA LEU A 112 -1.89527.118 17.692 1.0029.70 A C

ATOM 588 CB LEUA112 -1.951 26.646 16.233 1.0031.70 A C

ATOM 589 CG LEUA112 -3.35226.312 15.678 1.0032.75 A C

ATOM 590 CDl LEU A 112 -4.161 27.570 15.464 1.0033.07 A C ATOM 591 CD2 LEU A 112 -3.244 25.526 14.394 1.00 34.44 A C

ATOM 592 C LEU A 112 -2.512 26.067 18.606 1.00 29.49 A C

ATOM 593 O LEU A 112 -2.065 24.909 18.639 1.00 27.49 A O

ATOM 594 N ARG A 113 -3.470 26.511 19.412 1.00 30.42 A N

ATOM 595 CA ARG A 113 -4.182 25.638 20.335 1.00 32.08 A C

ATOM 596 CB ARG A 113 -4.991 26.466 21.330 1.00 30.08 A C

ATOM 597 CG ARG A 113 -4.465 26.536 22.718 1.00 29.02 A C

ATOM 598 CD ARG A 113 -3.459 27.650 22.895 1.00 29.80 A C

ATOM 599 NE ARG A 113 -3.721 28.525 24.047 1.00 28.97 A N

ATOM 600 CZ ARG A 113 -3.775 28.150 25.329 1.00 30.80 A C

ATOM 601 NHl ARG A 113 -3.597 26.880 25.688 1.00 34.69 A N

ATOM 602 NH2 ARG A 113 -3.959 29.069 26.270 1.00 31.31 A N

ATOM 603 C ARG A 113 -5.146 24.795 19.518 1.00 34.91 A C

ATOM 604 O ARG A 113 -4.955 23.590 19.365 1.00 35.85 A O

ATOM 605 N TYR A 114 -6.144 25.464 18.936 1.00 38.25 A N

ATOM 606 CA TYR A 114 -7.191 24.808 18.150 1.00 40.77 A C

ATOM 607 CB TYR A 114 -8.459 24.680 19.004 1.00 40.31 A C

ATOM 608 CG TYR A 114 -8.336 24.151 20.432 1.00 40.66 A C

ATOM 609 CDl TYR A 114 -8.644 24.984 21.530 1.00 40.37 A C

ATOM 610 CE1 TYR A 114 -8.600 24.496 22.861 1.00 40.52 A C

ATOM 611 CD2 TYR A 114 -7.972 22.808 20.697 1.00 41.14 A C ATOM 612 CE2 TYR A 114 -7.92622.30422.035 1.0039.28 A C

ATOM 613 CZ TYRA 114 -8.24723.15723.101 1.0040.33 A C

ATOM 614 OH TYRA 114 -8.26922.681 24.390 1.0042.49 A O

ATOM 615 C TYRA 114 -7.54725.607 16.892 1.0041.56 A C

ATOM 6160 TYRA 114 -6.96626.656 16.644 1.0044.00 A O

ATOM 617 N PHEA115 -8.50925.098 16.113 1.0044.34 A N

ATOM 618 CA PHE A 115 -9.021 25.742 14.883 1.0046.13 A C

ATOM 619 CB PHEA115 -8.05725.555 13.684 1.0045.12 A C

ATOM 620 CG PHEA115 -7.85224.116 13.253 1.0046.81 A C

ATOM 621 CDl PHE A 115 -8.47323.626 12.085 1.0049.33 A C

ATOM 622 CD2PHEA115 -7.01823.252 13.989 1.0048.46 A C

ATOM 623 CE1 PHE A 115 -8.26522.285 11.645 1.0051.04 A C

ATOM 624 CE2 PHE A 115 -6.79621.907 13.565 1.0050.07^" A C

ATOM 625 CZ PHE A 115 -7.42421.425 12.389 1.0049.96 A C

ATOM 626 C PHE A 115 -10.45225.270 14.518 1.0047.83 A C

ATOM 6270 PHE A 115 -10.66624.079 14.268 1.0048.32 A O

ATOM 628 N PHE A 116 -11.43026.180 14.536 1.0048.38 A N

ATOM 629 CA PHE A 116 -12.81425.824 14.192 1.0048.69 A C

ATOM 630 CB PHEA116 -13.72725.801 15.437 1.0049.59 A C

ATOM 631 CG PHEA116 -13.92627.148 16.103 1.0050.11 A C

ATOM 632 CDl PHE A 116 -15.07027.929 15.818 1.0049.65 A C ATOM 633 CD2 PHE A 116 -12.97727.648 17.007 1.0048.22 A C

ATOM 634 CE1PHEA116 -15.26229.191 16.426 1.0049.16 A C

ATOM 635 CE2PHEA116 -13.15828.911 17.625 1.0047.45 A C

ATOM 636 CZ PHE A 116 -14.301 29.683 17.333 1.0047.95 A C

ATOM 637 C PHE A 116 -13.42426.713 13.120 1.0050.20 A C

ATOM 6380 PHE A 116 -13.14927.913 13.074 1.0050.64 A O

ATOM 639 N TYRA117 -14.30626.131 12.309 1.0051.52 A N

ATOM 640 CA TYR A 117 -14.98926.873 11.249 1.0051.88 A C

ATOM 641 CB TYR A 117 -15.12726.029 9.977 1.0046.80 A C

ATOM 642 CG TYRA 117 -13.83225.773 9.226 1.0043.88 A C

ATOM 643 CDl TYRA 117 -13.50826.516 8.071 1.0040.86 A C

ATOM 644 CE1 TYRA 117 -12.30226.265 7.339 1.0040.26 A C

ATOM 645 CD2 TYRA 117 -12.92824.764 9.644 1.0043.30 A C

ATOM 646 CE2TYRA117 -11.71424.498 8.913 1.0040.72 A C

ATOM 647 CZ TYR A 117 -11.41525.254 7.766 1.0039.84 A C

ATOM 648 OH TYRA 117 -10.25325.008 7.057 1.0038.55 A O

ATOM 649 C TYRA 117 -16.36027.351 11.735 1.0054.74 A C

ATOM 650 O TYRA 117 -17.08726.616 12.415 1.0054.00 A O

ATOM 651 N SERA118 -16.66928.610 11.438 1.0058.47 A N

ATOM 652 CA SERA 118 -17.93929.217 11.828 1.0062.82 A C

ATOM 653 CB SERA 118 -17.791 29.994 13.155 1.0063.02 A C ATOM 654 OG SER A 118 -17.119 31.237 12.984 1.00 63.23 A O

ATOM 655 C SER A 118 -18.424 30.138 10.708 1.00 66.42 A C

ATOM 656 0 SER A 118 -17.979 30.019 9.564 1.00 65.62 A O

ATOM 657 N SER A 119 -19.345 31.038 11.059 1.00 70.65 A N

ATOM 658 CA SER A 119 -19.942 32.019 10.151 1.00 74.60 A C

ATOM 659 CB SER A 119 -21.015 31.365 9.262 1.00 74.93 A C

ATOM 660 OG SER A 119 -21.936 30.596 10.022 1.00 74.84 A O

ATOM 661 C SER A 119 -20.567 33.132 10.987 1.00 77.54 A C

ATOM 662 0 SER A 119 -20.497 34.318 10.629 1.00 77.18 A O

ATOM 663 N GLY A 120 -21.142 32.722 12.120 1.00 80.95 A N

ATOM 664 CA GLY A 120 -21.806 33.631 13.037 1.00 84.13 A C

ATOM 665 C GLY A 120^' -23.299 33.645 12.766 1.00 86.64 A C

ATOM 666 O GLY A 120 -24.085 33.094 13.547 1.00 86.23 A O

ATOM 667 N GLU A 121 -23.682 34.306 11.667 1.00 89.00 A N

ATOM 668 CA GLU A 121 -25.084 34.417 11.247 1.00 91.11 A C

ATOM 669 CB GLU A 121 -25.785 35.642 11.900 1.00 92.07 A C

ATOM 670 CG GLU A 121 -24.926 36.910 12.161 1.00 92.86 A C

ATOM 671 CD GLU A 121 -24.330 36.983 13.579 1.00 93.33 A C

ATOM 672 OEl GLU A 121 -24.759 36.217 14.474 1.00 93.37 A O

ATOM 673 OE2 GLU A 121 -23.425 37.819 13.798 1.00 93.27 A O

ATOM 674 C GLU A 121 -25.381 34.325 9.726 1.00 91.77 A C ATOM 675 0 GLU A 121 -25.375 33.222 9.167 1.00 91.66 A O

ATOM 676 N LYS A 122 -25.596 35.471 9.067 1.00 92.61 A N

ATOM 677 CA LYS A 122 -25.949 35.554 7.632 1.00 92.88 A C

ATOM 678 CB LYS A 122 -26.536 36.957 7.325 1.00 93.33 A C

ATOM 679 CG LYS A 122 -27.247 37.150 5.957 1.00 92.18 A C

ATOM 680 CD LYS A 122 -28.544 36.342 5.810 1.00 91.50 A C

ATOM 681 CE LYS A 122 -28.621 35.577 4.493 1.00 90.99 A C

ATOM 682 NZ LYS A 122 -28.303 36.419 3.309 1.00 90.55 A N

ATOM 683 C LYS A 122 -24.907 35.152 6.564 1.00 92.49 A C

ATOM 684 0 LYS A 122 -23.691 35.208 6.788 1.00 93.08 A O

ATOM 685 N LYS A 123 -25.449 34.736 5.411 1.00 91.41 A N

ATOM 686 CA LYS A 123 -24.756 34.289 4.194 1.00 90.02 A C

ATOM 687 CB LYS A 123 -24.005 35.443 3.498 1.00 90.40 A C

ATOM 688 CG LYS A 123 -24.902 36.538 2.900 1.00 91.10 A C

ATOM 689 CD LYS A 123 -24.792 36.668 1.368 1.00 91.44 A C

ATOM 690 CE LYS A 123 -25.672 35.669 0.595 1.00 90.62 A C

ATOM 691 NZ LYS A 123 -27.131 35.835 0.860 1.00 89.82 A N

ATOM 692 C LYS A 123 -23.896 33.028 4.271 1.00 89.07 A C

ATOM 693 O LYS A 123 -23.618 32.504 5.357 1.00 88.53 A O

ATOM 694 N ASP A 124 -23.509 32.539 3.091 1.00 88.23 A N

ATOM 695 CA ASP A 124 -22.692 31.333 2.933 1.00 86.86 A C ATOM 696 CB ASP A 124 -22.607 30.927 1.448 1.00 86.94 A C

ATOM 697 CG ASP A 124 -21.833 31.931 0.596 1.00 87.24 A C

ATOM 698 OD1 ASP A 124 -20.759 31.557 0.079 1.00 87.84 A O

ATOM 699 OD2 ASP A 124 -22.287 33.089 0.459 1.00 87.92 A O

ATOM 700 C ASP A 124 -21.285 31.443 3.522 1.00 85.10 A C

ATOM 701 O ASP A 124 -20.703 30.425 3.911 1.00 86.04 A O

ATOM 702 N GLU A 125 -20.779 32.682 3.606 1.00 82.22 A N

ATOM 703 CA GLU A 125 -19.438 33.004 4.120 1.00 78.05 A C

ATOM 704 CB GLU A 125 -19.229 34.536 4.209 1.00 77.65 A C

ATOM 705 CG GLU A 125 -20.398 35.366 4.773 1.00 78.10 A C

ATOM 706 CD GLU A 125 -20.204 36.887 4.671 1.00 77.56 A C

ATOM 707 OEl GLU A 125 -19.356 37.358 3.875 1.00 74.79 A O

ATOM 708 OE2 GLU A 125 -20.923 37.618 5.392 1.00 76.86 A O

ATOM 709 C GLU A 125 -19.011 32.281 5.406 1.00 75.44 A C

ATOM 710 O GLU A 125 -19.420 32.631 6.518 1.00 74.62 A O

ATOM 711 N VAL A 126 -18.283 31.183 5.193 1.00 72.75 A N

ATOM 712 CA VAL A 126 -17.757 30.328 6.257 1.00 69.40 A C

ATOM 713 CB VAL A 126 -17.751 28.805 5.821 1.00 70.96 A C

ATOM 714 CGI VAL A 126 -17.055 28.606 4.474 1.00 71.90 A C

ATOM 715 CG2 VAL A 126 -17.129 27.910 6.902 1.00 72.54 A C

ATOM 716 C VAL A 126 -16.384 30.851 6.705 1.00 65.08 A C ATOM 717 0 VAL A 126 -15.436 30.929 5.914 1.00 64.86 A O

ATOM 718 N TYR A 127 -16.320 31.259 7.969 1.00 60.73 A N

ATOM 719 CA TYR A 127 -15.104 31.825 8.557 1.00 56.58 A C

ATOM 720 CB TYR A 127 -15.482 32.953 9.535 1.00 56.20 A C

ATOM 721 CG TYR A 127 -16.057 34.225 8.900 1.00 56.66 A C

ATOM 722 CDl TYR A 127 -17.387 34.272 8.425 1.00 55.45 A C

ATOM 723 CE1 TYR A 127 -17.931 35.457 7.842 1.00 55.12 A C

ATOM 724 CD2 TYR A 127 -15.274 35.394 8.782 1.00 56.70 A C

ATOM 725 CE2 TYR A 127 -15.804 36.588 8.198 1.00 58.25 A C

ATOM 726 CZ TYR A 127 -17.133 36.607 7.730 1.00 57.71 A C

ATOM 727 OH TYR A 127 -17.639 37.754 7.146 1.00 56.53 A O

ATOM 728 C TYR A 127 -14.202 30.802 9.256 1.00 52.61 A C

ATOM 729 0 TYR A 127 -14.685 29.931 9.982 1.00 51.15 A O

ATOM 730 N LEU A 128 -12.901 30.880 8.967 1.00 48.55 A N

ATOM 731 CA LEU A 128 -11.879 30.017 9.578 1.00 43.88 A C

ATOM 732 CB LEU A 128 -10.715 29.778 8.590 1.00 42.20 A C

ATOM 733 CG LEU A 128 -9.326 29.263 9.034 1.00 41.94 A C

ATOM 734 CDl LEU A 128 -9.379 27.864 9.661 1.00 43.16 A C

ATOM 735 CD2 LEU A 128 -8.384 29.271 7.839 1.00 42.29 A C

ATOM 736 C LEU A 128 -11.378 30.747 10.835 1.00 40.19 A C

ATOM 737 0 LEU A 128 -10.876 31.865 10.744 1.00 40.68 A O ATOM 738 N ASNA129 -11.561 30.133 11.999 1.0036.45 A N

ATOM 739 CA ASNA129 -11.12830.737 13.264 1.0033.88 A C

ATOM 740 CB ASN A 129 -12.28430.800 14.279 1.0034.37 A C

ATOM 741 CG ASN A 129 -13.54031.462 13.730 1.0033.33 A C

ATOM 742 OD1 ASNA129 -14.113 31.008 12.743 1.0036.35 A O

ATOM 743 ND2ASNA129 -13.99732.513 14.401 1.0031.97 A N

ATOM 744 C ASN A 129 -9.98829.933 13.886 1.0032.07 A C

ATOM 745 O ASN A 129 -10.19228.784 14.262 1.0031.07 A O

ATOM 746 N LEU A 130 -8.80730.550 14.003 1.0030.70 A N

ATOM 747 CA LEU A 130 -7.61229.919 14.591 1.0028.47 A C

ATOM 748 CB LEU A 130 -6.35730.359 13.832 1.0026.34 A C

ATOM 749 CG LEU A 130 -6.22230.069 12.336 1.0028.51 A C

ATOM 750 CD1LEUA130 -5.31031.097 11.683 1.0026.00 A C

ATOM 751 CD2LEUA130 -5.701 28.652 12.102 1.0026.67 A C

ATOM 752 C LEU A 130 -7.45630.327 16.060 1.0027.86 A C

ATOM 753 O LEUA130 -7.23831.506 16.340 1.0027.53 A O

ATOM 754 N VAL A 131 -7.59829.377 16.994 1.0026.68 A N

ATOM 755 CA VALA 131 -7.44229.676 18.429 1.0028.08 A C

ATOM 756 CB VAL A 131 -8.32228.767 19.332 1.0030.39 A C

ATOM 757 CGI VALA 131 -8.05329.03520.820 1.0030.65 A C

ATOM 758 CG2 VALA 131 -9.77929.016 19.046 1.0028.27 A C ATOM 759 C VAL A 131 -5.964 29.544 18.789 1.00 27.17 A C

ATOM 760 O VAL A 131 -5.391 28.458 18.695 1.00 25.59 A O

ATOM 761 N LEU A 132 -5.361 30.688 19.135 1.00 27.45 A N

ATOM 762 CA LEU A 132 -3.933 30.813 19.467 1.00 26.12 A C

ATOM 763 CB LEU A 132 -3.270 31.732 18.442 1.00 26.03 A C

ATOM 764 CG LEU A 132 -3.165 31.271 16.986 1.00 28.47 A C

ATOM 765 CDl LEU A 132 -3.688 32.363 16.046 1.00 27.02 A C

ATOM 766 CD2 LEU A 132 -1.714 30.905 16.673 1.00 26.94 A C

ATOM 767 C LEU A 132 -3.607 31.346 20.870 1.00 25.75 A C

ATOM 768 O LEU A 132 -4.465 31.889 21.572 1.00 22.73 A O

ATOM 769 N ASP A 133 -2.338 31.218 21.252 1.00 26.31 A N

ATOM 770 CA ASP A 133 -1.858 31.699 22.543 1.00 27.99 A C

ATOM 771 CB ASP A 133 -0.458 31.171 22.806 1.00 31.88 A C

ATOM 772 CG ASP A 133 -0.461 29.915 23.626 1.00 33.68 A C

ATOM 773 OD1 ASP A 133 -1.154 29.866 24.664 1.00 36.12 A O

ATOM 774 OD2 ASP A 133 0.249 28.978 23.242 1.00 38.19 A O

ATOM 775 C ASP A 133 -1.832 33.222 22.606 1.00 29.00 A C

ATOM 776 0 ASP A 133 -1.386 33.870 21.648 1.00 29.34 A O

ATOM 777 N TYR A 134 -2.373 33.785 23.692 1.00 26.69 A N

ATOM 778 CA TYR A 134 -2.388 35.234 23.864 1.00 25.43 A C

ATOM 779 CB TYR A 134 -3.553 35.690 24.738 1.00 22.57 A C ATOM 780 CG TYR A 134 -3.639 37.185 25.015 1.00 21.80 A C

ATOM 781 CDl TYR A 134 -4.096 38.088 24.024 1.00 18.90 A C

ATOM 782 CE1 TYR A 134 -4.171 39.504 24.292 1.00 18.04 A C

ATOM 783 CD2 TYR A 134 -3.256 37.710 26.284 1.00 18.73 A C

ATOM 784 CE2 TYR A 134 -3.325 39.108 26.561 1.00 15.99 A C

ATOM 785 CZ TYR A 134 -3.782 40.001 25.564 1.00 18.68 A C

ATOM 786 OH TYR A 134 -3.849 41.366 25.842 1.00 18.13 A O

ATOM 787 C TYR A 134 -1.071 35.691 24.466 1.00 26.26 A C

ATOM 788 O TYR A 134 -0.468 35.001 25.303 1.00 26.61 A O

ATOM 789 N VAL A 135 -0.613 36.834 23.958 1.00 24.85 A N

ATOM 790 CA VAL A 135 0.627 37.480 24.379 1.00 25.09 A C

ATOM 791 CB VAL A 135 1.742 37.334 23.308 1.00 22.94 A C

ATOM 792 CGI VAL A 135 3.063 37.620 23.923 1.00 23.51 A C

ATOM 793 CG2 VAL A 135 1.790 35.923 22.733 1.00 17.58 A C

ATOM 794 C VAL A 135 0.168 38.934 24.544 1.00 25.50 A C

ATOM 795 O VAL A 135 -0.421 39.496 23.630 1.00 26.56 A O

ATOM 796 N PRO A 136 0.429 39.560 25.706 1.00 23.87 A N

ATOM 797 CD PRO A 136 0.978 38.981 26.948 1.00 24.88 A C

ATOM 798 CA PRO A 136 -0.018 40.948 25.924 1.00 24.35 A C

ATOM 799 CB PRO A 136 0.213 41.166 27.428 1.00 24.03 A C

ATOM 800 CG PRO A 136 1.283 40.191 27.766 1.00 25.67 A C ATOM 801 C PRO A 136 0.388 42.156 25.085 1.00 24.04 A C

ATOM 802 O PRO A 136 -0.406 43.093 24.958 1.00 26.03 A O

ATOM 803 N GLU A 137 1.591 42.149 24.509 1.00 22.49 A N

ATOM 804 CA GLU A 137 2.067 43.289 23.718 1.00 19.62 A C

ATOM 805 CB GLU A 137 3.058 44.122 24.558 1.00 18.33 A C

ATOM 806 CG GLU A 137 2.425 45.059 25.602 1.00 15.10 A C

ATOM 807 CD GLU A 137 1.498 46.124 25.005 1.00 18.86 A C

ATOM 808 OEl GLU A 137 1.565 46.408 23.784 1.00 17.56 A O

ATOM 809 OE2 GLU A 137 0.682 46.683 25.767 1.00 24.07 A O

ATOM 810 C GLU A 137 2.710 42.929 22.385 1.00 17.50 A C

ATOM 811 O GLU A 137 2.721 41.775 22.008 1.00 17.40 A O

ATOM 812 N THR A 138 3.129 43.942 21.628 1.00 16.15 A N

ATOM 813 CA THR A 138 3.833 43.749 20.357 1.00 17.07 A C

ATOM 814 CB THR A 138 3.008 44.179 19.091 1.00 15.32 A C

ATOM 815 OG1 THR A 138 2.722 45.579 19.132 1.00 11.52 A O

ATOM 816 CG2 THR A 138 1.720 43.401 18.957 1.00 14.61 A C

ATOM 817 C THR A 138 5.089 44.624 20.425 1.00 18.97 A C

ATOM 818 O THR A 138 5.144 45.562 21.237 1.00 20.86 A O

ATOM 819 N VAL A 139 6.085 44.339 19.577 1.00 18.95 A N

ATOM 820 CA VAL A 139 7.323 45.137 19.537 1.00 19.72 A C

ATOM 821 CB VAL A 139 8.433 44.487 18.626 1.00 17.86 A C ATOM 822 CGI VAL A 139 9.514 45.459 18.256 1.00 16.24 A C

ATOM 823 CG2 VAL A 139 9.102 43.356 19.347 1.00 17.17 A C

ATOM 824 C VAL A 139 6.979 46.559 19.100 1.00 20.98 A C

ATOM 825 O VAL A 139 7.462 47.501 19.702 1.00 21.50 A O

ATOM 826 N TYR A 140 6.076 46.693 18.123 1.00 22.72 A N

ATOM 827 CA TYR A 140 5.643 47.993 17.621 1.00 25.95 A C

ATOM 828 CB TYR A 140 4.598 47.829 16.509 1.00 31.87 A C

ATOM 829 CG TYR A 140 4.061 49.135 15.945 1.00 33.87 A C

ATOM 830 CDl TYR A 140 4.865 49.953 15.122 1.00 35.27 A C

ATOM 831 CE1 TYR A 140 4.387 51.193 14.633 1.00 39.03 A C

ATOM 832 CD2 TYR A 140 2.759 49.579 16.267 1.00 34.43 A C

ATOM 833 CE2 TYR A 140 2.267 50.819 15.786 1.00 38.29 A C

ATOM 834 CZ TYR A 140 3.089 51.620 14.970 1.00 40.12 A C

ATOM 835 OH TYR A 140 2.624 52.835 14.507 1.00 44.26 A O

ATOM 836 C TYR A 140 5.067 48.830 18.758 1.00 27.09 A C

ATOM 837 0 TYR A 140 5.524 49.942 18.983 1.00 26.72 A O

ATOM 838 N ARG A 141 4.096 48.273 19.483 1.00 27.22 A N

ATOM 839 CA ARG A 141 3.476 48.969 20.608 1.00 26.45 A C

ATOM 840 CB ARG A 141 2.332 48.150 21.202 1.00 26.63 A C

ATOM 841 CG ARG A 141 1.052 48.172 20.351 1.00 29.13 A C

ATOM 842 CD ARG A 141 -0.143 47.607 21.102 1.00 27.11 A C ATOM 843 NE ARG A 141 -0.324 48.279 22.384 1.00 30.83 A N

ATOM 844 CZ ARG A 141 -1.207 47.932 23.317 1.00 34.02 A C

ATOM 845 NHl ARG A 141 -2.047 46.912 23.121 1.00 38.45 A N

ATOM 846 NH2 ARG A 141 -1.134 48.498 24.516 1.00 32.23 A N

ATOM 847 C ARG A 141 4.481 49.365 21.691 1.00 25.66 A C

ATOM 848 O ARG A 141 4.444 50.505 22.174 1.00 26.13 A O

ATOM 849 N VAL A 142 5.435 48.472 21.983 1.00 24.01 A N

ATOM 850 CA VAL A 142 6.464 48.749 22.993 1.00 23.59 A C

ATOM 851 CB VAL A 142 7.088 47.443 23.572 1.00 22.50 A C

ATOM 852 CGI VAL A 142 8.353 47.729 24.375 1.00 19.27 A C

ATOM 853 CG2 VAL A 142 6.070 46.751 24.510 1.00 20.12 A C

ATOM 854 C VAL A 142 7.518 49.729 22.471 1.00 24.65 A C

ATOM 855 0 VAL A 142 7.950 50.620 23.203 1.00 26.20 A O

ATOM 856 N ALA A 143 7.852 49.618 21.187 1.00 25.08 A N

ATOM 857 CA ALA A 143 8.821 50.507 20.555 1.00 25.54 A C

ATOM 858 CB ALA A 143 9.251 49.950 19.207 1.00 23.86 A C

ATOM 859 C ALA A 143 8.222 51.907 20.392 1.00 26.54 A C

ATOM 860 O ALA A 143 8.943 52.895 20.474 1.00 28.74 A O

ATOM 861 N ARG A 144 6.895 51.967 20.251 1.00 27.36 A N

ATOM 862 CA ARG A 144 6.131 53.214 20.087 1.00 29.98 A C

ATOM 863 CB ARG A 144 4.740 52.898 19.527 1.00 32.69 A C ATOM 864 CG ARG A 144 3.905 54.063 19.032 1.00 34.14 A C

ATOM 865 CD ARG A 144 2.459 53.721 19.281 1.00 37.19 A C

ATOM 866 NE ARG A 144 1.596 54.000 18.139 1.00 40.63 A N

ATOM 867 CZ ARG A 144 0.365 53.506 17.999 1.00 41.79 A C

ATOM 868 NHl ARG A 144 -0.152 52.702 18.929 1.00 40.02 A N

ATOM 869 NH2 ARG A 144 -0.356 53.826 16.931 1.00 42.14 A N

ATOM 870 C ARG A 144 5.984 53.946 21.416 1.00 29.28 A C

ATOM 871 O ARG A 144 5.937 55.169 21.440 1.00 29.55 A O

ATOM 872 N HIS A 145 5.914 53.186 22.509 1.00 29.56 A N

ATOM 873 CA HIS A 145 5.798 53.740 23.860 1.00 29.77 A C

ATOM 874 CB HIS A 145 5.558 52.610 24.876 1.00 31.77 A C

ATOM 875 CG HIS A 145 5.591 53.053 26.309 1.00 36.22 A C

ATOM 876 CD2 HIS A 145 4.673 53.699 27.066 1.00 37.45 A C

ATOM 877 ND1 HIS A 145 6.679 52.833 27.130 1.00 38.32 A N

ATOM 878 CE1 HIS A 145 6.427 53.321 28.331 1.00 37.02 A C

ATOM 879 NE2 HIS A 145 5.218 53.853 28.319 1.00 38.72 A N

ATOM 880 C HIS A 145 7.055 54.556 24.214 1.00 28.01 A C

ATOM 881 0 HIS A 145 6.944 55.712 24.647 1.00 26.93 A O

ATOM 882 N TYR A 146 8.228 53.953 23.993 1.00 26.45 A N

ATOM 883 CA TYR A 146 9.519 54.606 24.249 1.00 26.53 A C

ATOM 884 CB TYR A 146 10.692 53.618 24.124 1.00 23.97 A C ATOM 885 CG TYR A 146 10.885 52.742 25.347 1.00 20.61 A C

ATOM 886 CDl TYR A 146 10.296 51.462 25.416 1.00 18.00 A C

ATOM 887 CE1 TYR A 146 10.433 50.642 26.579 1.00 17.99 A C

ATOM 888 CD2 TYR A 146 11.626 53.200 26.464 1.00 19.40 A C

ATOM 889 CE2 TYR A 146 11.774 52.390 27.643 1.00 18.16 A C

ATOM 890 CZ TYR A 146 11.174 51.111 27.683 1.00 19.24 A C

ATOM 891 OH TYR A 146 11.336 50.285 28.779 1.00 19.81 A O

ATOM 892 C TYR A 146 9.742 55.806 23.326 1.00 26.54 A C

ATOM 893 0 TYR A 146 10.155 56.859 23.801 1.00 26.81 A O

ATOM 894 N SER A 147 9.379 55.665 22.046 1.00 25.86 A N

ATOM 895 CA SER A 147 9.524 56.721 21.037 1.00 27.77 A C

ATOM 896 CB SER A 147 9.154 56.186 19.649 1.00 28.75 A C

ATOM 897 OG SER A 147 9.378 57.153 18.624 1.00 29.72 A O

ATOM 898 C SER A 147 8.706 57.987 21.343 1.00 30.68 A C

ATOM 899 0 SER A 147 9.248 59.100 21.308 1.00 29.28 A O

ATOM 900 N ARG A 148 7.425 57.800 21.685 1.00 32.90 A N

ATOM 901 CA ARG A 148 6.514 58.899 22.022 1.00 34.64 A C

ATOM 902 CB ARG A 148 5.070 58.390 22.170 1.00 37.64 A C

ATOM 903 CG ARG A 148 4.430 57.992 20.843 1.00 41.36 A C

ATOM 904 CD ARG A 148 2.907 57.986 20.870 1.00 44.26 A C

ATOM 905 NE ARG A 148 2.363 58.283 19.536 1.00 48.03 A N ATOM 906 CZ ARG A 148 1.348 57.643 18.946 1.00 49.42 A C

ATOM 907 NHl ARG A 148 0.718 56.642 19.558 1.00 47.68 A N

ATOM 908 NH2 ARG A 148 0.982 57.987 17.712 1.00 48.98 A N

ATOM 909 C ARG A 148 6.963 59.648 23.287 1.00 35.38 A C

ATOM 910 O ARG A 148 6.604 60.818 23.493 1.00 33.18 A O

ATOM 911 N ALA A 149 7.811 58.980 24.076 1.00 35.64 A N

ATOM 912 CA ALA A 149 8.374 59.524 25.313 1.00 36.33 A C

ATOM 913 CB ALA A 149 8.280 58.492 26.429 1.00 35.66 A C

ATOM 914 C ALA A 149 9.825 59.966 25.100 1.00 37.03 A C

ATOM 915 O ALA A 149 10.628 60.005 26.046 1.00 37.12 A O

ATOM 916 N LYS A 150 10.142 60.293 23.840 1.00 37.06 A N

ATOM 917 CA LYS A 150 11.466 60.746 23.389 1.00 37.94 A C

ATOM 918 CB LYS A 150 11.648 62.251 23.649 1.00 39.56 A C

ATOM 919 CG LYS A 150 10.960 63.145 22.617 1.00 43.00 A C

ATOM 920 CD LYS A 150 11.681 63.111 21.260 1.00 44.89 A C

ATOM 921 CE LYS A 150 11.089 64.114 20.276 1.00 46.47 A C

ATOM 922 NZ LYS A 150 11.909 64.230 19.033 1.00 47.00 A N

ATOM 923 C LYS A 150 12.655 59.930 23.898 1.00 36.49 A C

ATOM 924 O LYS A 150 13.723 60.465 24.200 1.00 36.82 A O

ATOM 925 N GLN A 151 12.439 58.620 23.969 1.00 34.84 A N

ATOM 926 CA GLN A 151 13.445 57.677 24.428 1.00 33.37 A C ATOM 927 CB GLN A 151 13.080 57.127 25.812 1.00 34.05 A C

ATOM 928 CG GLN A 151 14.226 56.379 26.501 1.00 38.78 A C

ATOM 929 CD GLN A 151 13.912 55.938 27.920 1.00 41.78 A C

ATOM 930 OEl GLN A 151 12.977 56.451 28.562 1.00 39.31 A O

ATOM 931 NE2 GLN A 151 14.717 54.989 28.432 1.00 41.05 A N

ATOM 932 C GLN A 151 13.587 56.548 23.426 1.00 30.24 A C

ATOM 933 0 GLN A 151 12.746 56.363 22.552 1.00 29.98 A O

ATOM 934 N THR A 152 14.712 55.852 23.521 1.00 28.74 A N

ATOM 935 CA THR A 152 15.015 54.724 22.662 1.00 24.49 A C

ATOM 936 CB THR A 152 16.443 54.914 22.018 1.00 24.37 A C

ATOM 937 OG1 THR A 152 16.336 54.858 20.588 1.00 23.47 A O

ATOM 938 CG2 THR A 152 17.470 53.891 22.498 1.00 26.16 A C

ATOM 939 C THR A 152 14.880 53.494 23.552 1.00 21.94 A C

ATOM 940 O THR A 152 15.094 53.579 24.766 1.00 23.32 A O

ATOM 941 N LEU A 153 14.452 52.382 22.964 1.00 19.61 A N

ATOM 942 CA LEU A 153 14.298 51.112 23.676 1.00 18.67 A C

ATOM 943 CB LEU A 153 13.728 50.067 22.713 1.00 18.78 A C

ATOM 944 CG LEU A 153 13.448 48.636 23.183 1.00 20.73 A C

ATOM 945 CDl LEU A 153 12.109 48.558 23.919 1.00 17.83 A C

ATOM 946 CD2 LEU A 153 13.457 47.684 21.996 1.00 16.10 A C

ATOM 947 C LEU A 153 15.701 50.698 24.136 1.00 18.65 A C ATOM 948 0 LEU A 153 16.615 50.697 23.323 1.00 20.94 A O

ATOM 949 N PRO A 154 15.907 50.435 25.451 1.00 19.11 A N

ATOM 950 CD PRO A 154 14.962 50.594 26.575 1.00 20.76 A C

ATOM 951 CA PRO A 154 17.225 50.035 25.967 1.00 19.35 A C

ATOM 952 CB PRO A 154 16.938 49.692 27.427 1.00 18.17 A C

ATOM 953 CG PRO A 154 15.897 50.685 27.778 1.00 19.29 A C

ATOM 954 C PRO A 154 17.803 48.858 25.217 1.00 19.91 A C

ATOM 955 O PRO A 154 17.102 47.882 24.964 1.00 21.15 A O

ATOM 956 N VAL A 155 19.066 49.006 24.820 1.00 19.62 A N

ATOM 957 CA VAL A 155 19.825 48.016 24.054 1.00 20.67 A C

ATOM 958 CB VAL A 155 21.327 48.406 23.976 1.00 21.91 A C

ATOM 959 CGI VAL A 155 22.064 47.530 23.001 1.00 23.46 A C

ATOM 960 CG2 VAL A 155 21.456 49.832 23.491 1.00 25.92 A C

ATOM 961 C VAL A 155 19.662 46.548 24.470 1.00 18.71 A C

ATOM 962 0 VAL A 155 19.642 45.664 23.604 1.00 20.28 A O

ATOM 963 N ILE A 156 19.453 46.303 25.764 1.00 15.16 A N

ATOM 964 CA ILE A 156 19.269 44.941 26.271 1.00 13.81 A C

ATOM 965 CB ILE A 156 19.382 44.893 27.827 1.00 11.15 A C

ATOM 966 CG2 ILE A 156 18.336 45.789 28.479 1.00 10.21 A C

ATOM 967 CGI ILE A 156 19.280 43.455 28.367 1.00 13.17 A C

ATOM 968 CDl ILE A 156 20.459 42.576 28.076 1.00 9.54 A C ATOM 969 C ILE A 156 17.957 44.301 25.747 1.00 15.23 A C

ATOM 970 O ILE A 156 17.911 43.097 25.530 1.00 16.61 A O

ATOM 971 N TYR A 157 16.933 45.117 25.489 1.00 13.61 A N

ATOM 972 CA TYR A 157 15.666 44.614 24.960 1.00 12.61 A C

ATOM 973 CB TYR A 157 14.494 45.556 25.266 1.00 11.76 A C

ATOM 974 CG TYR A 157 14.086 45.630 26.730 1.00 12.85 A C

ATOM 975 CDl TYR A 157 14.149 46.854 27.434 1.00 15.71 A C

ATOM 976 CE1 TYR A 157 13.763 46.954 28.803 1.00 12.18 A C

ATOM 977 CD2 TYR A 157 13.631 44.491 27.422 1.00 13.30 A C

ATOM 978 CE2 TYR A 157 13.247 44.567 28.791 1.00 16.53 A C

ATOM 979 CZ TYR A 157 13.316 45.808 29.470 1.00 16.06 A C

ATOM 980 OH TYR A 157 12.941 45.896 30.792 1.00 14.94 A O

ATOM 981 C TYR A 157 15.811 44.409 23.464 1.00 13.12 A C

ATOM 982 0 TYR A 157 15.285 43.443 22.920 1.00 13.91 A O

ATOM 983 N VAL A 158 16.591 45.277 22.816 1.00 15.26 A N

ATOM 984 CA VAL A 158 16.862 45.178 21.372 1.00 15.53 A C

ATOM 985 CB VAL A 158 17.785 46.344 20.846 1.00 15.48 A C

ATOM 986 CGI VAL A 158 18.104 46.172 19.378 1.00 15.22 A C

ATOM 987 CG2 VAL A 158 17.134 47.675 21.053 1.00 12.99 A C

ATOM 988 C VAL A 158 17.575 43.850 21.159 1.00 14.83 A C

ATOM 989 0 VAL A 158 17.206 43.111 20.267 1.00 20.37 A O ATOM 990 N LYS A 159 18.537 43.535 22.032 1.00 14.37 A N

ATOM 991 CA LYS A 159 19.300 42.287 21.975 1.00 14.73 A C

ATOM 992 CB LYS A 159 20.398 42.264 23.052 1.00 17.05 A C

ATOM 993 CG LYS A 159 21.623 43.117 22.768 1.00 17.71 A C

ATOM 994 CD LYS A 159 22.621 43.103 23.921 1.00 17.41 A C

ATOM 995 CE LYS A 159 23.670 44.169 23.734 1.00 13.09 A C

ATOM 996 NZ LYS A 159 24.918 43.895 24.487 1.00 16.53 A N

ATOM 997 C LYS A 159 18.392 41.074 22.172 1.00 14.07 A C

ATOM 998 0 LYS A 159 18.422 40.143 21.395 1.00 14.83 A O

ATOM 999 N LEU A 160 17.564 41.122 23.206 1.00 13.93 A N

ATOM 1000 CA LEU A 160 16.639 40.056 23.532 1.00 16.72 A C

ATOM 1001 CB LEU A 160 15.909 40.397 24.816 1.00 15.82 A C

ATOM 1002 CG LEU A 160 16.687 40.134 26.087 1.00 17.14 A C

ATOM 1003 CDl LEU A 160 16.029 40.935 27.164 1.00 16.63 A C

ATOM 1004 CD2 LEU A 160 16.740 38.631 26.421 1.00 19.20 A C

ATOM 1005 C LEU A 160 15.603 39.749 22.467 1.00 18.54 A C

ATOM 1006 O LEU A 160 15.426 38.589 22.075 1.00 18.28 A O

ATOM 1007 N TYR A 161 14.960 40.810 21.979 1.00 19.35 A N

ATOM 1008 CA TYR A 161 13.897 40.709 20.982 1.00 18.69 A C

ATOM 1009 CB TYR A 161 13.194 42.066 20.828 1.00 19.53 A C

ATOM 1010 CG TYR A 161 12.579 42.636 22.107 1.00 20.40 A C ATOM 1011 CDl TYR A 161 12.482 41.859 23.297 1.00 19.87 A C

ATOM 1012 CE1 TYR A 161 11.893 42.378 24.473 1.00 21.10 A C

ATOM 1013 CD2 TYR A 161 12.071 43.957 22.132 1.00 19.09 A C

ATOM 1014 CE2 TYR A 161 11.469 44.494 23.308 1.00 18.79 A C

ATOM 1015 CZ TYR A 161 11.381 43.692 24.470 1.00 22.26 A C

ATOM 1016 OH TYR A 161 10.744 44.166 25.601 1.00 25.56 A O

ATOM 1017 C TYR A 161 14.401 40.212 19.646 1.00 18.80 A C

ATOM 1018 O TYR A 161 13.825 39.287 19.065 1.00 19.39 A O

ATOM 1019 N MET A 162 15.546 40.753 19.237 1.00 18.46 A N

ATOM 1020 CA MET A 162 16.193 40.407 17.980 1.00 20.35 A C

ATOM 1021 CB MET A 162 17.262 41.455 17.670 1.00 24.61 A C

ATOM 1022 CG MET A 162 17.379 41.846 16.200 1.00 29.46 A C

ATOM 1023 SD MET A 162 15.867 42.505 15.463 1.00 27.23 A S

ATOM 1024 CE MET A 162 15.445 43.669 16.614 1.00 26.70 A C

ATOM 1025 C MET A 162 16.788 38.998 17.941 1.00 19.88 A C

ATOM 1026 O MET A 162 16.828 38.371 16.879 1.00 20.15 A O

ATOM 1027 N TYR A 163 17.220 38.503 19.101 1.00 17.08 A N

ATOM 1028 CA TYR A 163 17.778 37.159 19.231 1.00 18.01 A C

ATOM 1029 CB TYR A 163 18.469 37.033 20.592 1.00 15.14 A C

ATOM 1030 CG TYR A 163 19.065 35.686 20.899 1.00 15.15 A C

ATOM 1031 CDl TYR A 163 20.331 35.320 20.412 1.00 14.59 A C ATOM 1032 CE1 TYR A 163 20.871 34.038 20.697 1.00 14.78 A C

ATOM 1033 CD2 TYR A 163 18.354 34.755 21.674 1.00 14.93 A C

ATOM 1034 CE2 TYR A 163 18.875 33.494 21.953 1.00 16.91 A C

ATOM 1035 CZ TYR A 163 20.128 33.135 21.468 1.00 16.54 A C

ATOM 1036 OH TYR A 163 20.609 31.875 21.767 1.00 22.13 A O

ATOM 1037 C TYR A 163 16.668 36.092 19.083 1.00 19.83 A C

ATOM 1038 O TYR A 163 16.870 35.054 18.439 1.00 19.39 A O

ATOM 1039 N GLN A 164 15.523 36.349 19.713 1.00 18.29 A N

ATOM 1040 CA GLN A 164 14.388 35.439 19.671 1.00 18.68 A C

ATOM 1041 CB GLN A 164 13.383 35.803 20.754 1.00 17.81 A C

ATOM 1042 CG GLN A 164 13.928 35.581 22.144 1.00 16.73 A C

ATOM 1043 CD GLN A 164 13.025 36.114 23.218 1.00 18.60 A C

ATOM 1044 OEl GLN A 164 12.420 35.346 23.955 1.00 20.73 A O

ATOM 1045 NE2 GLN A 164 12.953 37.441 23.343 1.00 19.75 A N

ATOM 1046 C GLN A 164 13.736 35.427 18.296 1.00 22.63 A C

ATOM 1047 O GLN A 164 13.118 34.425 17.898 1.00 23.42 A O

ATOM 1048 N LEU A 165 13.915 36.527 17.557 1.00 22.82 A N

ATOM 1049 CA LEU A 165 13.390 36.643 16.199 1.00 22.39 A C

ATOM 1050 CB LEU A 165 13.472 38.080 15.692 1.00 22.76 A C

ATOM 1051 CG LEU A 165 12.505 38.662 14.659 1.00 20.98 A C

ATOM 1052 CDl LEU A 165 13.272 39.678 13.891 1.00 21.25 A C ATOM 1053 CD2 LEU A 165 11.873 37.654 13.696 1.00 26.60 A C

ATOM 1054 C LEU A 165 14.258 35.765 15.309 1.00 20.30 A C

ATOM 1055 O LEU A 165 13.741 34.973 14.539 1.00 21.43 A O

ATOM 1056 N PHE A 166 15.574 35.887 15.459 1.00 20.09 A N

ATOM 1057 CA PHE A 166 16.526 35.098 14.676 1.00 19.88 A C

ATOM 1058 CB PHE A 166 17.942 35.644 14.818 1.00 16.41 A C

ATOM 1059 CG PHE A 166 18.185 36.904 14.043 1.00 17.58 A C

ATOM 1060 CDl PHE A 166 18.813 38.001 14.653 1.00 18.19 A C

ATOM 1061 CD2 PHE A 166 17.804 37.001 12.687 1.00 19.26 A C

ATOM 1062 CE1 PHE A 166 19.063 39.186 13.932 1.00 18.03 A C

ATOM 1063 CE2 PHE A 166 18.044 38.175 11.947 1.00 17.78 A C

ATOM 1064 CZ PHE A 166 18.675 39.274 12.569 1.00 19.13 A C

ATOM 1065 C PHE A 166 16.492 33.625 15.025 1.00 19.72 A C

ATOM 1066 O PHE A 166 16.838 32.787 14.195 1.00 23.09 A O

ATOM 1067 N ARG A 167 16.053 33.317 16.244 1.00 19.37 A N

ATOM 1068 CA ARG A 167 15.921 31.935 16.707 1.00 20.74 A C

ATOM 1069 CB ARG A 167 15.828 31.896 18.238 1.00 19.95 A C

ATOM 1070 CG ARG A 167 16.119 30.563 18.869 1.00 21.19 A C

ATOM 1071 CD ARG A 167 16.701 30.719 20.274 1.00 23.38 A C

ATOM 1072 NE ARG A 167 15.908 30.076 21.329 1.00 27.21 A N

ATOM 1073 CZ ARG A 167 15.771 28.761 21.500 1.00 27.17 A C ATOM 1074 NHl ARG A 167 16.369 27.893 20.695 1.00 24.83 A N

ATOM 1075 NH2 ARG A 167 15.003 28.310 22.471 1.00 29.82 A N

ATOM 1076 C ARG A 167 14.658 31.358 16.038 1.00 21.01 A C

ATOM 1077 O ARG A 167 14.716 30.282 15.438 1.00 21.84 A O

ATOM 1078 N SER A 168 13.579 32.155 16.023 1.00 21.52 A N

ATOM 1079 CA SER A 168 12.294 31.780 15.408 1.00 22.69 A C

ATOM 1080 CB SER A 168 11.204 32.812 15.730 1.00 24.69 A C

ATOM 1081 OG SER A 168 11.412 34.045 15.053 1.00 24.23 A O

ATOM 1082 C SER A 168 12.432 31.655 13.892 1.00 21.63 A C

ATOM 1083 O SER A 168 11.736 30.852 13.257 1.00 20.43 A O

ATOM 1084 N LEU A 169 13.329 32.455 13.322 1.00 19.92 A N

ATOM 1085 CA LEU A 169 13.562 32.401 11.889 1.00 22.34 A C

ATOM 1086 CB LEU A 169 14.154 33.708 11.353 1.00 19.42 A C

ATOM 1087 CG LEU A 169 13.297 34.983 11.235 1.00 17.78 A C

ATOM 1088 CDl LEU A 169 14.139 36.091 10.586 1.00 17.05 A C

ATOM 1089 CD2 LEU A 169 12.016 34.746 10.444 1.00 14.48 A C

ATOM 1090 C LEU A 169 14.418 31.188 11.501 1.00 24.54 A C

ATOM 1091 O LEU A 169 14.162 30.562 10.472 L00 22.76 A O

ATOM 1092 N ALA A 170 15.337 30.793 12.391 1.00 24.89 A N

ATOM 1093 CA ALA A 170 16.229 29.646 12.176 1.00 23.84 A C

ATOM 1094 CB ALA A 170 17.245 29.564 13.306 1.00 21.64 A C ATOM 1095 C ALA A 170 15.44328.355 12.093 1.0025.42 A C

ATOM 1096 O ALA A 170 15.70727.502 11.243 1.0026.20 A O

ATOM 1097 N TYRA 171 14.43028.273 12.949 1.0027.33 A N

ATOM 1098 CA TYRA 171 13.54327.127 13.048 1.0027.49 A C

ATOM 1099 CB TYRA 171 12.64627.279 14.290 1.0025.45 A C

ATOM 1100 CG TYRA171 11.59026.196 14.487 1.0025.00 A C

ATOM 1101 CDl TYRA 171 11.941 24.901 14.918 1.0022.50 A C

ATOM 1102 CE1 TYRA 171 10.94823.900 15.106 1.0024.34 A C

ATOM 1103 CD2 TYRA 171 10.23226.471 14.249 1.0024.77 A C

ATOM 1104 CE2 TYRA 171 9.23425.486 14.433 1.0025.75 A C

ATOM 1105 CZ TYRA 171 9.59424.208 14.861 1.0025.96 A C

ATOM 1106 OH TYRA 171 8.60623.263 15.053 1.0027.53 A O

ATOM 1107 C TYRA 171 12.70826.923 11.787 1.0027.67 A C

ATOM 1108 O TYRA 171 12.67625.815 11.254 1.0029.21 A O

ATOM 1109 N ILEA 172 12.02027.976 11.337 1.0028.82 A N

ATOM 1110 CA ILEA172 11.17727.879 10.145 1.0028.16 A C

ATOM 1111 CB ILEA 172 10.13729.048 10.005 1.0027.47 A C

ATOM 1112 CG2 ILE A 172 9.10828.982 11.128 1.0025.75 A C

ATOM 1113 CGI ILE A 172 10.81530.415 9.930 1.0024.37 A C

ATOM 1114 CDl ILEA 172 9.90631.537 9.480 1.0022.33 A C

ATOM 1115 C ILEA 172 11.98827.709 8.863 1.0029.06 A C ATOM 1116 0 ILE A 172 11.593 26.945 7.985 1.00 29.17 A O

ATOM 1117 N HIS A 173 13.157 28.350 8.801 1.00 29.31 A N

ATOM 1118 CA HIS A 173 14.028 28.246 7.635 1.00 29.89 A C

ATOM 1119 CB HIS A 173 15.149 29.285 7.674 1.00 26.91 A C

ATOM 1120 CG HIS A 173 14.687 30.689 7.440 1.00 27.24 A C

ATOM 1121 CD2 HIS A 173 13.444 31.219 7.326 1.00 25.67 A C

ATOM 1122 ND1 HIS A 173 15.565 31.748 7.348 1.00 26.72 A N

ATOM 1123 CE1 HIS A 173 14.882 32.870 7.198 1.00 26.23 A C

ATOM 1124 NE2 HIS A 173 13.593 32.577 7.181 1.00 27.18 A N

ATOM 1125 C HIS A 173 14.616 26.845 7.499 1.00 32.53 A C

ATOM 1126 0 HIS A 173 14.881 26.405 6.379 1.00 37.00 A O

ATOM 1127 N SER A 174 14.755 26.133 8.625 1.00 32.07 A N

ATOM 1128 CA SER A 174 15.288 24.765 8.632 1.00 33.69 A C

ATOM 1129 CB SER A 174 15.741 24.355 10.036 1.00 32.18 A C

ATOM 1130 OG SER A 174 14.653 24.093 10.907 1.00 28.45 A O

ATOM 1131 C SER A 174 14.242 23.784 8.096 1.00 35.80 A C

ATOM 1132 0 SER A 174 14.562 22.651 7.718 1.00 37.14 A O

ATOM 1133 N PHE A 175 12.990 24.241 8.110 1.00 37.64 A N

ATOM 1134 CA PHE A 175 11.841 23.499 7.598 1.00 40.20 A C

ATOM 1135 CB PHE A 175 10.613 23,782 8.464 1.00 44.61 A C

ATOM 1136 CG PHE A 175 10.319 22.726 9.489 1.00 47.63 A C ATOM 1137 CDl PHE A 175 10.362 23.038 10.861 1.00 48.58 A C

ATOM 1138 CD2 PHE A 175 9.923 21.429 9.092 1.00 47.83 A C

ATOM 1139 CE1 PHE A 175 10.005 22.068 11.843 1.00 51.84 A C

ATOM 1140 CE2 PHE A 175 9.563 20.444 10.051 1.00 50.25 A C

ATOM 1141 CZ PHE A 175 9.601 20.762 11.434 1.00 51.82 A C

ATOM 1142 C PHE A 175 11.569 23.978 6.160 1.00 40.39 A C

ATOM 1143 0 PHE A 175 10.633 23.501 5.497 1.00 39.81 A O

ATOM 1144 N GLY A 176 12.381 24.949 5.716 1.00 39.69 A N

ATOM 1145 CA GLY A 176 12.278 25.529 4.383 1.00 36.62 A C

ATOM 1146 C GLY A 176 11.225 26.613 4.231 1.00 34.33 A C

ATOM 1147 0 GLY A 176 11.041 27.132 3.127 1.00 33.92 A O

ATOM 1148 N ILE A 177 10.580 26.978 5.343 1.00 31.96 A N

ATOM 1149 CA ILE A 177 9.505 27.984 5.382 1.00 31.27 A C

ATOM 1150 CB ILE A 177 8.463 27.656 6.513 1.00 30.38 A C

ATOM 1151 CG2 ILE A 177 7.300 28.673 6.504 1.00 31.04 A C

ATOM 1152 CGI ILE A 177 7.929 26.223 6.340 1.00 30.32 A C

ATOM 1153 CDl ILE A 177 6.897 25.766 7.374 1.00 28.01 A C

ATOM 1154 C ILE A 177 9.968 29.447 5.528 1.00 30.13 A C

ATOM 1155 O ILE A 177 10.794 29.776 6.380 1.00 28.36 A O

ATOM 1156 N CYS A 178 9.358 30.313 4.721 1.00 28.94 A N

ATOM 1157 CA CYS A 178 9.644 31.738 4.716 1.00 29.00 A C ATOM 1158 CB CYS A 178 10.069 32.167 3.326 1.00 28.54 A C

ATOM 1159 SG CYS A 178 10.722 33.811 3.220 1.00 31.05 A S

ATOM 1160 C CYS A 178 8.390 32.497 5.142 1.00 29.43 A C

ATOM 1161 0 CYS A 178 7.344 32.411 4.482 1.00 28.90 A O

ATOM 1162 N HIS A 179 8.518 33.257 6.232 1.00 26.83 A N

ATOM 1163 CA HIS A 179 7.418 34.032 6.805 1.00 25.43 A C

ATOM 1164 CB HIS A 179 7.888 34.674 8.116 1.00 24.10 A C

ATOM 1165 CG HIS A 179 6.798 35.333 8.894 1.00 21.36 A C

ATOM 1166 CD2 HIS A 179 5.978 34.854 9.858 1.00 20.67 A C

ATOM 1167 ND1 HIS A 179 6.451 36.655 8.712 1.00 21.07 A N

ATOM 1168 CE1 HIS A 179 5.461 36.959 9.537 1.00 22.86 A C

ATOM 1169 NE2 HIS A 179 5.156 35.885 10.242 1.00 19.76 A N

ATOM 1170 C HIS A 179 6.830 35.082 5.841 1.00 24.76 A C

ATOM 1171 O HIS A 179 5.602 35.225 5.746 1.00 23.83 A O

ATOM 1172 N ARG A 180 7.719 35.787 5.137 1.00 21.70 A N

ATOM 1173 CA ARG A 180 7.378 36.810 4.138 1.00 25.08 A C

ATOM 1174 CB ARG A 180 6.667 36.193 2.901 1.00 24.27 A C

ATOM 1175 CG ARG A 180 7.432 35.074 2.187 1.00 26.19 A C

ATOM 1176 CD ARG A 180 6.831 34.712 0.844 1.00 27.56 A C

ATOM 1177 NE ARG A 180 5.398 34.423 0.929 1.00 30.48 A N

ATOM 1178 CZ ARG A 180 4.607 34.166 -0.115 1.00 31.58 A C ATOM 1179 NHl ARG A 180 5.092 34.151 -1.354 1.00 27.82 A N

ATOM 1180 NH2 ARG A 180 3.320 33.897 0.090 1.00 31.74 A N

ATOM 1181 C ARG A 180 6.628 38.074 4.588 1.00 25.17 A C

ATOM 1182 0 ARG A 180 6.015 38.738 3.758 1.00 27.79 A O

ATOM 1183 N ASP A 181 6.627 38.366 5.890 1.00 25.38 A N

ATOM 1184 CA ASP A 181 5.991 39.572 6.444 1.00 21.79 A C

ATOM 1185 CB ASP A 181 4.458 39.458 6.480 1.00 21.64 A C

ATOM 1186 CG ASP A 181 3.770 40.826 6.567 1.00 20.59 A C

ATOM 1187 OD1 ASP A 181 4.442 41.856 6.364 1.00 21.96 A O

ATOM 1188 OD2 ASP A 181 2.562 40.878 6.850 1.00 24.24 A O

ATOM 1189 C ASP A 181 6.544 39.929 7.838 1.00 21.31 A C

ATOM 1190 O ASP A 181 _. 5.797 40.262 8.764 1.00 22.46 A O

ATOM 1191 N ILE A 182 7.863 39.879 7.970 1.00 19.49 A N

ATOM 1192 CA ILE A 182 8.526 40.204 9.222 1.00 20.02 A C

ATOM 1193 CB ILE A 182 9.977 39.632 9.246 1.00 19.38 A C

ATOM 1194 CG2 ILE A 182 10.810 40.226 10.395 1.00 18.82 A C

ATOM 1195 CGI ILE A 182 9.948 38.096 9.232 1.00 16.75 A C

ATOM 1196 CDl ILE A 182 9.299 37.457 10.437 1.00 13.80 A C

ATOM 1197 C ILE A 182 8.505 41.716 9.399 1.00 20.65 A C

ATOM 1198 0 ILE A 182 8.992 42.464 8.554 1.00 20.96 A O

ATOM 1199 N LYS A 183 7.821 42.131 10.461 1.00 21.97 A N ATOM 1200 CA LYS A 183 7.650 43.527 10.845 1.00 21.58 A C

ATOM 1201 CB LYS A 183 6.480 44.151 10.056 1.00 22.46 A C

ATOM 1202 CG LYS A 183 5.149 43.433 10.113 1.00 27.57 A C

ATOM 1203 CD LYS A 183 4.075 44.307 9.496 1.00 31.15 A C

ATOM 1204 CE LYS A 183 2.746 43.586 9.330 1.00 30.47 A C

ATOM 1205 NZ LYS A 183 1.770 44.446 8.604 1.00 31.06 A N

ATOM 1206 C LYS A 183 7.355 43.530 12.355 1.00 20.88 A C

ATOM 1207 O LYS A 183 6.914 42.514 12.875 1.00 21.10 A O

ATOM 1208 N PRO A 184 7.603 44.655 13.078 1.00 20.98 A N

ATOM 1209 CD PRO A 184 8.340 45.863 12.662 1.00 19.71 A C

ATOM 1210 CA PRO A 184 7.341 44.730 14.522 1.00 20.53 A C

ATOM 1211 CB PRO A 184 7.777 46.141 14.862 1.00 20.46 A C

ATOM 1212 CG PRO A 184 8.898 46.362 13.945 1.00 19.75 A C

ATOM 1213 C PRO A 184 5.904 44.459 14.981 1.00 22.58 A C

ATOM 1214 0 PRO A 184 5.680 44.101 16.146 1.00 25.06 A O

ATOM 1215 N GLN A 185 4.947 44.593 14.063 1.00 21.33 A N

ATOM 1216 CA GLN A 185 3.530 44.361 14.355 1.00 22.67 A C

ATOM 1217 CB GLN A 185 2.646 44.962 13.252 1.00 23.73 A C

ATOM 1218 CG GLN A 185 2.597 46.518 13.186 1.00 26.60 A C

ATOM 1219 CD GLN A 185 3.798 47.196 12.484 1.00 28.80 A C

ATOM 1220 OEl GLN A 185 4.778 46.551 12.079 1.00 27.47 A O ATOM 1221 NE2 GLN A 185 3.702 48.518 12.330 1.00 30.26 A N

ATOM 1222 C GLN A 185 3.245 42.865 14.517 1.00 22.34 A C

ATOM 1223 O GLN A 185 2.318 42.461 15.221 1.00 22.90 A O

ATOM 1224 N ASN A 186 4.102 42.055 13.906 1.00 22.13 A N

ATOM 1225 CA ASN A 186 3.993 40.605 13.963 1.00 20.93 A C

ATOM 1226 CB ASN A 186 4.219 40.017 12.575 1.00 19.79 A C

ATOM 1227 CG ASN A 186 3.119 40.374 11.610 1.00 21.23 A C

ATOM 1228 OD1 ASN A 186 2.051 40.866 12.007 1.00 21.92 A O

ATOM 1229 ND2 ASN A 186 3.369 40.134 10.322 1.00 21.11 A N

ATOM 1230 C ASN A 186 4.932 39.959 14.982 1.00 20.81 A C

ATOM 1231 O ASN A 186 5.052 38.726 15.035 1.00 22.28 A O

ATOM 1232 N LEU A 187 5.616 40.789 15.769 1.00 18.81 A N

ATOM 1233 CA LEU A 187 6.524 40.299 16.813 1.00 19.18 A C

ATOM 1234 CB LEU A 187 7.908 40.948 16.701 1.00 16.59 A C

ATOM 1235 CG LEU A 187 8.615 41.088 15.367 1.00 16.91 A C

ATOM 1236 CDl LEU A 187 9.949 41.762 15.593 1.00 13.39 A C

ATOM 1237 CD2 LEU A 187 8.770 39.755 14.672 1.00 19.53 A C

ATOM 1238 C LEU A 187 5.909 40.597 18.181 1.00 17.56 A C

ATOM 1239 O LEU A 187 6.103 41.672 18.745 1.00 17.89 A O

ATOM 1240 N LEU A 188 5.143 39.638 18.685 1.00 19.82 A N

ATOM 1241 CA LEU A 188 4.447 39.733 19.971 1.00 20.71 A C ATOM 1242 CB LEU A 188 3.428 38.617 20.073 1.00 20.11 A C

ATOM 1243 CG LEU A 188 2.426 38.443 18.940 1.00 20.95 A C

ATOM 1244 CDl LEU A 188 1.693 37.143 19.168 1.00 22.75 A C

ATOM 1245 CD2 LEU A 188 1.449 39.598 18.855 1.00 17.53 A C

ATOM 1246 C LEU A 188 5.378 39.663 21.173 1.00 22.99 A C

ATOM 1247 0 LEU A 188 6.374 38.946 21.139 1.00 23.79 A O

ATOM 1248 N LEU A 189 5.036 40.396 22.231 1.00 24.53 A N

ATOM 1249 CA LEU A 189 5.842 40.473 23.452 1.00 28.04 A C

ATOM 1250 CB LEU A 189 6.522 41.824 23.558 1.00 32.40 A C

ATOM 1251 CG LEU A 189 7.599 42.320 22.638 1.00 37.51 A C

ATOM 1252 CDl LEU A 189 7.960 43.673 23.166 1.00 39.70 A C

ATOM 1253 CD2 LEU A 189 8.805 41.393 22.614 1.00 41.58 A C

ATOM 1254 C LEU A 189 5.130 40.342 24.784 1.00 28.18 A C

ATOM 1255 O LEU A 189 4.013 40.829 24.962 1.00 27.14 A O

ATOM 1256 N ASP A 190 5.847 39.756 25.739 1.00 28.19 A N

ATOM 1257 CA ASP A 190 5.382 39.627 27.108 1.00 28.55 A C

ATOM 1258 CB ASP A 190 5.500 38.178 27.592 1.00 28.74 A C

ATOM 1259 CG ASP A 190 4.860 37.961 28.957 1.00 28.01 A C

ATOM 1260 OD1 ASP A 190 5.303 38.605 29.926 1.00 26.72 A O

ATOM 1261 OD2 ASP A 190 3.913 37.150 29.061 1.00 30.00 A O

ATOM 1262 C ASP A 190 6.371 40.569 27.837 1.00 27.97 A C ATOM 1263 O ASP A 190 7.548 40.245 27.955 1.00 27.40 A O

ATOM 1264 N PRO A 191 5.910 41.766 28.279 1.00 29.41 A N

ATOM 1265 CD PRO A 191 4.504 42.212 28.204 1.00 29.28 A C

ATOM 1266 CA PRO A 191 6.705 42.788 28.980 1.00 30.33 A C

ATOM 1267 CB PRO A 191 5.653 43.813 29.403 1.00 31.04 A C

ATOM 1268 CG PRO A 191 4.637 43.694 28.370 1.00 30.48 A C

ATOM 1269 C PRO A 191 7.485 42.341 30.205 1.00 31.91 A C

ATOM 1270 O PRO A 191 8.620 42.784 30.413 1.00 34.32 A O

ATOM 1271 N ASP A 192 6.878 41.463 31.001 1.00 31.32 A N

ATOM 1272 CA ASP A 192 7.498 40.979 32.224 1.00 33.48 A C

ATOM 1273 CB ASP A 192 6.457 40.322 33.140 1.00 37.68 A C

ATOM 1274 CG ASP A 192 5.354 41.286 33.587 1.00 41.32 A C

ATOM 1275 OD1 ASP A 192 5.573 42.525 33.582 1.00 41.23 A O

ATOM 1276 OD2 ASP A 192 4.257 40.790 33.943 1.00 41.76 A O

ATOM 1277 C ASP A 192 8.649 40.017 31.997 1.00 33.36 A C

ATOM 1278 O ASP A 192 9.733 40.220 32.546 1.00 33.73 A O

ATOM 1279 N THR A 193 8.427 39.021 31.138 1.00 31.42 A N

ATOM 1280 CA THR A 193 9.424 37.990 30.853 1.00 30.79 A C

ATOM 1281 CB THR A 193 8.765 36.628 30.655 1.00 29.36 A C

ATOM 1282 OGl THR A 193 7.864 36.703 29.549 1.00 33.26 A O

ATOM 1283 CG2 THR A 193 8.010 36.200 31.899 1.00 29.96 A C ATOM 1284 C THR A 193 10.368 38.210 29.672 1.00 30.22 A C

ATOM 1285 O THR A 193 11.349 37.471 29.528 1.00 30.58 A O

ATOM 1286 N ALA A 194 10.074 39.211 28.838 1.00 26.81 A N

ATOM 1287 CA ALA A 194 10.863 39.533 27.639 1.00 25.60 A C

ATOM 1288 CB ALA A 194 12.331 39.863 27.999 1.00 26.36 A C

ATOM 1289 C ALA A 194 10.786 38.463 26.530 1.00 24.26 A C

ATOM 1290 O ALA A 194 11.630 38.414 25.626 1.00 22.45 A O

ATOM 1291 N VAL A 195 9.750 37.626 26.604 1.00 22.33 A N

ATOM 1292 CA VAL A 195 9.500 36.577 25.622 1.00 22.37 A C

ATOM 1293 CB VAL A 195 8.528 35.485 26.190 1.00 24.64 A C

ATOM 1294 CGI VAL A 195 8.078 34.508 25.095 1.00 21.02 A C

ATOM 1295 CG2 VAL A 195 9.211 34.693 27.308 1.00 25.69 A C

ATOM 1296 C VAL A 195 8.891 37.176 24.348 1.00 22.61 A C

ATOM 1297 0 VAL A 195 7.910 37.946 24.411 1.00 21.55 A O

ATOM 1298 N LEU A 196 9.505 36.847 23.210 1.00 20.27 A N

ATOM 1299 CA LEU A 196 9.016 37.297 21.911 1.00 20.16 A C

ATOM 1300 CB LEU A 196 10.126 37.925 21.050 1.00 20.66 A C

ATOM 1301 CG LEU A 196 9.721 38.503 19.669 1.00 22.78 A C

ATOM 1302 CDl LEU A 196 10.422 39.815 19.404 1.00 19.39 A C

ATOM 1303 CD2 LEU A 196 10.005 37.517 18.528 1.00 23.32 A C

ATOM 1304 C LEU A 196 8.412 36.097 21.205 1.00 18.39 A C ATOM 1305 O LEU A 196 8.975 35.008 21.246 1.00 19.06 A O

ATOM 1306 N LYS A 197 7.245 36.300 20.598 1.00 18.23 A N

ATOM 1307 CA LYS A 197 6.543 35.249 19.853 1.00 17.32 A C

ATOM 1308 CB LYS A 197 5.261 34.812 20.568 1.00 18.32 A C

ATOM 1309 CG LYS A 197 5.463 34.234 21.960 1.00 18.93 A C

ATOM 1310 CD LYS A 197 5.298 32.745 22.007 1.00 23.31 A C

ATOM 1311 CE LYS A 197 5.333 32.225 23.444 1.00 24.38 A C

ATOM 1312 NZ LYS A 197 4.270 32.858 24.285 1.00 24.87 A N

ATOM 1313 C LYS A 197 6.222 35.774 18.454 1.00 17.16 A C

ATOM 1314 0 LYS A 197 5.679 36.872 18.304 1.00 16.49 A O

ATOM 1315 N LEU A 198 6.627 35.025 17.432 1.00 16.38 A N

ATOM 1316 CA LEU A 198 6.383 35.409 16.039 1.00 17.74 A C

ATOM 1317 CB LEU A 198 7.323 34.650 15.093 1.00 19.56 A C

ATOM 1318 CG LEU A 198 8.010 35.358 13.912 1.00 21.82 A C

ATOM 1319 CDl LEU A 198 8.542 34.287 12.960 1.00 18.92 A C

ATOM 1320 CD2 LEU A 198 7.093 36.334 13.157 1.00 20.47 A C

ATOM 1321 C LEU A 198 4.952 35.033 15.687 1.00 16.43 A C

ATOM 1322 O LEU A 198 4.493 33.962 16.061 1.00 17.30 A O

ATOM 1323 N CYS A 199 4.251 35.916 14.984 1.00 15.15 A N

ATOM 1324 CA CYS A 199 2.886 35.618 14.590 1.00 16.52 A C

ATOM 1325 CB CYS A 199 1.900 36.237 15.569 1.00 14.37 A C ATOM 1326 SG CYS A 199 1.711 37.992 15.453 1.0014.21 A S

ATOM 1327 C CYS A 199 2.55436.010 13.157 1.0017.24 A C

ATOM 1328 O CYS A 199 3.41836.509 12.443 1.0017.85 A O

ATOM 1329 N ASP A 200 1.29835.761 12.764 1.0018.31 A N

ATOM 1330 CA ASPA200 0.723 36.052 11.440 1.0020.20 A C

ATOM 1331 CB ASP A 200 0.61637.563 11.174 1.0021.20 A C

ATOM 1332 CG ASP A 200 -0.371 37.911 10.039 1.0026.31 A C

ATOM 1333 OD1 ASP A 200 -0.66539.116 9.871 1.0028.42 A O

ATOM 1334 OD2ASPA200 -0.85837.002 9.323 1.0023.86 A O

ATOM 1335 C ASP A 200 1.441 35.356 10.295 1.0022.53 A C

ATOM 1336 O ASP A 200 2.30035.940 9.629 1.0023.49 A O

ATOM 1337 N PHEA201 1.02634.124 10.035 1.0023.42 A N

ATOM 1338 CA PHE A 201 1.62033.336 8.977 1.0025.50 A C

ATOM 1339 CB PHE A 201 1.911 31.919 9.481 1.0024.98 A C

ATOM 1340 CG PHEA201 3.043 31.850 10.454 1.0022.19 A C

ATOM 1341 CDl PHE A 201 2.84232.168 11.808 1.0023.18 A C

ATOM 1342 CD2PHEA201 4.32931.500 10.021 1.0022.96 A C

ATOM 1343 CE1PHEA201 3.91032.145 12.723 1.0021.08 A C

ATOM 1344 CE2PHEA201 5.41631.469 10.923 1.0022.15 A C

ATOM 1345 CZ PHE A 201 5.20731.795 12.279 1.0021.37 A C

ATOM 1346 C PHE A 201 0.763 33.317 7.711 1.0026.58 A C ATOM 1347 O PHE A 201 1.016 32.523 6.786 1.00 28.36 A O

ATOM 1348 N GLY A 202 -0.204 34.234 7.645 1.00 24.70 A N

ATOM 1349 CA GLY A 202 -1.096 34.331 6.495 1.00 25.81 A C

ATOM 1350 C GLY A 202 -0.432 34.616 5.155 1.00 27.13 A C

ATOM 1351 O GLY A 202 -1.096 34.562 4.114 1.00 28.89 A O

ATOM 1352 N SER A 203 0.872 34.908 5.194 1.00 27.63 A N

ATOM 1353 CA SER A 203 1.681 35.191 4.010 1.00 28.84 A C

ATOM 1354 CB SER A 203 2.285 36.611 4.085 1.00 31.91 A C

ATOM 1355 OG SER A 203 1.340 37.600 4.458 1.00 35.26 A O

ATOM 1356 C SER A 203 2.827 34.171 3.904 1.00 29.78 A C

ATOM 1357 O SER A 203 3.680 34.280 3.011 1.00 30.08 A O

ATOM 1358 N ALA A 204 2.860 33.195 4.816 1.00 30.20 A N

ATOM 1359 CA ALA A 204 3.916 32.170 4.823 1.00 30.42 A C

ATOM 1360 CB ALA A 204 3.978 31.473 6.156 1.00 27.81 A C

ATOM 1361 C ALA A 204 3.793 31.152 3.703 1.00 32.11 A C

ATOM 1362 O ALA A 204 2.690 30.718 3.356 1.00 34.10 A O

ATOM 1363 N LYS A 205 4.941 30.789 3.145 1.00 34.28 A N

ATOM 1364 CA LYS A 205 5.026 29.840 2.045 1.00 36.42 A C

ATOM 1365 CB LYS A 205 5.113 30.598 0.713 1.00 38.04 A C

ATOM 1366 CG LYS A 205 5.085 29.738 -0.544 1.00 40.33 A C

ATOM 1367 CD LYS A 205 5.628 30.491 -1.735 1.00 41.67 A C ATOM 1368 CE LYS A 205 4.786 30.303 -3.000 1.00 44.03 A C

ATOM 1369 NZ LYS A 205 4.628 28.902 -3.454 1.00 45.07 A N

ATOM 1370 C LYS A 205 6.269 28.986 2.203 1.00 37.24 A C

ATOM 1371 O LYS A 205 7.310 29.472 2.653 1.00 36.33 A O

ATOM 1372 N GLN A 206 6.158 27.724 1.788 1.00 39.70 A N

ATOM 1373 CA GLN A 206 7.272 26.781 1.839 1.00 42.41 A C

ATOM 1374 CB GLN A 206 6.749 25.344 1.969 1.00 42.64 A C

ATOM 1375 CG GLN A 206 7.628 24.408 2.796 1.00 47.15 A C

ATOM 1376 CD GLN A 206 8.627 23.604 1.971 1.00 49.24 A C

ATOM 1377 OEl GLN A 206 9.714 24.087 1.648 1.00 50.26 A O

ATOM 1378 NE2 GLN A 206 8.270 22.357 1.655 1.00 48.19 A N

ATOM 1379 C GLN A 206 7.999 26.986 0.516 1.00 42.01 A C

ATOM 1380 O GLN A 206 7.461 26.663 -0.543 1.00 45.02 A O

ATOM 1381 N LEU A 207 9.153 27.645 0.571 1.00 40.97 A N

ATOM 1382 CA LEU A 207 9.940 27.904 -0.628 1.00 41.31 A C

ATOM 1383 CB LEU A 207 10.917 29.054 -0.433 1.00 40.06 A C

ATOM 1384 CG LEU A 207 10.445 30.442 -0.016 1.00 40.01 A C

ATOM 1385 CDl LEU A 207 11.651 31.358 -0.067 1.00 41.28 A C

ATOM 1386 CD2 LEU A 207 9.347 30.990 -0.883 1.00 36.64 A C

ATOM 1387 C LEU A 207 10.716 26.686 -1.082 1.00 43.20 A C

ATOM 1388 O LEU A 207 11.447 26.057 -0.306 1.00 42.97 A O ATOM 1389 N VAL A 208 10.506 26.344 -2.345 1.00 45.35 A N

ATOM 1390 CA VAL A 208 11.167 25.218 -2.981 1.00 48.65 A C

ATOM 1391 CB VAL A 208 10.177 24.002 -3.192 1.00 48.43 A C

ATOM 1392 CGI VAL A 208 8.771 24.484 -3.540 1.00 47.91 A C

ATOM 1393 CG2 VAL A 208 10.718 22.997 -4.226 1.00 47.77 A C

ATOM 1394 C VAL A 208 11.782 25.767 -4.261 1.00 49.99 A C

ATOM 1395 O VAL A 208 11.149 26.553 -4.968 1.00 50.65 A O

ATOM 1396 N ARG A 209 13.035 25.385 -4.510 1.00 53.00 A N

ATOM 1397 CA ARG A 209 13.792 25.840 -5.676 1.00 56.27 A C

ATOM 1398 CB ARG A 209 15.256 25.338 -5.611 1.00 59.41 A C

ATOM 1399 CG ARG A 209 15.535 23.905 -6.108 1.00 63.33 A C

ATOM 1400 CD ARG A 209 15.206 22.796 -5.109 1.00 67.47 A C

ATOM 1401 NE ARG A 209 15.000 21.486 -5.751 1.00 70.85 A N

ATOM 1402 CZ ARG A 209 15.943 20.743 -6.340 1.00 71.66 A C

ATOM 1403 NHl ARG A 209 17.210 21.151 -6.399 1.00 71.51 A N

ATOM 1404 NH2 ARG A 209 15.613 19.571 -6.874 1.00 70.99 A N

ATOM 1405 C ARG A 209 13.130 25.503 -7.019 1.00 55.85 A C

ATOM 1406 O ARG A 209 12.474 24.461 -7.153 1.00 56.16 A O

ATOM 1407 N GLY A 210 13.232 26.443 -7.959 1.00 55.61 A N

ATOM 1408 CA GLY A 210 12.657 26.272 -9.283 1.00 54.50 A C

ATOM 1409 C GLY A 210 11.200 26.676 -9.437 1.00 53.43 A C ATOM 1410 O GLY A 210 10.759 26.932 -10.562 1.00 53.60 A O

ATOM 1411 N GLU A 211 10.458 26.727 -8.326 1.00 52.91 A N

ATOM 1412 CA GLU A 211 9.033 27.098 -8.324 1.00 53.50 A C

ATOM 1413 CB GLU A 211 8.260 26.209 -7.338 1.00 56.66 A C

ATOM 1414 CG GLU A 211 8.097 24.768 -7.833 1.00 63.39 A C

ATOM 1415 CD GLU A 211 7.567 23.802 -6.778 1.00 66.35 A C

ATOM 1416 OEl GLU A 211 8.287 22.830 -6.455 1.00 68.23 A O

ATOM 1417 OE2 GLU A 211 6.439 24.000 -6.273 1.00 68.02 A O

ATOM 1418 C GLU A 211 8.839 28.585 -7.994 1.00 50.77 A C

ATOM 1419 O GLU A 211 9.065 28.990 -6.857 1.00 53.00 A O

ATOM 1420 N PRO A 212 8.401 29.412 -8.978 1.00 48.23 A N

ATOM 1421 CD PRO A 212 8.073 29.052 -10.372 1.00 47.12 A C

ATOM 1422 CA PRO A 212 8.192 30.855 -8.774 1.00 45.39 A C

ATOM 1423 CB PRO A 212 7.833 31.355 -10.177 1.00 43.61 A C

ATOM 1424 CG PRO A 212 7.180 30.189 -10.798 1.00 45.59 A C

ATOM 1425 C PRO A 212 7.180 31.312 -7.718 1.00 43.14 A C

ATOM 1426 O PRO A 212 6.031 30.856 -7.676 1.00 43.13 A O

ATOM 1427 N ASN A 213 7.650 32.215 -6.860 1.00 39.61 A N

ATOM 1428 CA ASN A 213 6.855 32.788 -5.775 1.00 36.37 A C

ATOM 1429 CB ASN A 213 7.588 32.624 -4.439 1.00 35.62 A C

ATOM 1430 CG ASN A 213 8.398 31.328 -4.356 1.00 35.34 A C ATOM 1431 OD1 ASN A 213 . 7.841 30.233 -4.220 1.00 32.84 A O

ATOM 1432 ND2 ASN A 213 9.724 31.454 -4.454 1.00 33.41 A N

ATOM 1433 C ASN A 213 6.679 34.273 -6.097 1.00 34.54 A C

ATOM 1434 O ASN A 213 7.559 34.860 -6.739 1.00 30.67 A O

ATOM 1435 N VAL A 214 5.563 34.862 -5.637 1.00 32.85 A N

ATOM 1436 CA VAL A 214 5.198 36.282 -5.867 1.00 33.27 A C

ATOM 1437 CB VAL A 214 3.783 36.633 -5.275 1.00 34.50 A C

ATOM 1438 CGI VAL A 214 2.682 36.064 -6.143 1.00 34.62 A C

ATOM 1439 CG2 VAL A 214 3.633 36.109 -3.833 1.00 31.85 A C

ATOM 1440 C VAL A 214 6.176 37.360 -5.372 1.00 34.39 A C

ATOM 1441 O VAL A 214 6.724 37.258 -4.267 1.00 34.49 A O

ATOM 1442 N SER A 215 6.356 38.405 -6.186 1.00 33.74 A N

ATOM 1443 CA SER A 215 7.249 39.531 -5.867 1.00 32.25 A C

ATOM 1444 CB SER A 215 7.706 40.237 -7.133 1.00 30.98 A C

ATOM 1445 OG SER A 215 8.626 39.422 -7.815 1.00 34.87 A O

ATOM 1446 C SER A 215 6.638 40.562 -4.934 1.00 30.58 A C

ATOM 1447 O SER A 215 7.310 41.050 -4.030 1.00 31.79 A O

ATOM 1448 N PTR A 216 5.381 40.917 -5.178 1.00 28.49 A N

ATOM 1449 CA PTR A 216 4.690 41.890 -4.347 1.00 27.79 A C

ATOM 1450 CB PTR A 216 3.558 42.573 -5.132 1.00 27.56 A C

ATOM 1451 CG PTR A 216 3.198 43.941 -4.605 1.00 26.28 A C ATOM 1452 CDl PTR A 216 4.14644.992 -4.616 1.0026.29 A C

ATOM 1453 CE1PTRA216 3.83346.272 -4.102 1.0025.08 A C

ATOM 1454 CD2PTRA216 1.91944.198 -4.069 1.0027.05 A C

ATOM 1455 CE2PTRA216 1.58745.486 -3.542 1.0026.39 A C

ATOM 1456 CZ PTR A 216 2.55346.507 -3.567 1.0027.76 A C

ATOM 1457 OH PTR A 216 2.24647.746 -3.064 1.0029.85 A O

ATOM 1458 C PTR A 216 4.18341.173 -3.091 1.0028.51 A C

ATOM 1459 O PTR A 216 3.07340.617 -3.049 1.0028.32 A O

ATOM 1460 P PTR A 216 2.74348.116 -1.618 1.0030.02 A P

ATOM 1461 O1PPTRA216 1.76549.242 -1.160 1.0029.39 A O

ATOM 1462 O2PPTRA216 4.171 48.722 -1.822 1.0028.79 A O

ATOM 1463 O3PPTRA216 2.74346.943 -0.686 1.0028.98 A O

ATOM 1464 N ILE A 217 5.06641.154 -2.092 1.0029.04 A N

ATOM 1465 CA ILE A 217 4.83640.512 -0.805 1.0027.27 A C

ATOM 1466 CB ILE A 217 5.18938.975 -0.929 1.0027.34 A C

ATOM 1467 CG2ILEA217 6.703 38.740 -1.007 1.0024.93 A C

ATOM 1468 CGI ILE A 217 4.46738.150 0.140 1.0029.00 A C

ATOM 1469 CDl ILE A 217 2.94338.019 -0.058 1.0027.14 A C

ATOM 1470 C ILE A 217 5.66641.288 0.256 1.0027.97 A C

ATOM 1471 O ILE A 217 6.63441.965 -0.099 1.0024.98 A O

ATOM 1472 N CYSA218 5.27241.177 1.537 1.0029.57 A N ATOM 1473 CA CYS A 218 5.862 41.861 2.722 1.00 28.63 A C

ATOM 1474 CB CYS A 218 7.398 41.890 2.751 1.00 30.93 A C

ATOM 1475 SG CYS A 218 8.206 40.392 2.332 1.00 38.61 A S

ATOM 1476 C CYS A 218 5.420 43.303 2.845 1.00 27.95 A C

ATOM 1477 O CYS A 218 5.154 43.972 1.834 1.00 29.09 A O

ATOM 1478 N SER A 219 5.392 43.802 4.084 1.00 26.02 A N

ATOM 1479 CA SER A 219 5.035 45.195 4.331 1.00 23.32 A C

ATOM 1480 CB SER A 219 4.883 45.460 5.811 1.00 22.90 A C

ATOM 1481 OG SER A 219 3.863 44.645 6.338 1.00 25.98 A O

ATOM 1482 C SER A 219 6.174 46.014 3.749 1.00 22.69 A C

ATOM 1483 O SER A 219 7.353 45.691 3.937 1.00 21.63 A O

ATOM 1484 N ARG A 220 5.780 46.967 2.913 1.00 22.94 A N

ATOM 1485 CA ARG A 220 6.665 47.858 2.180 1.00 22.75 A C

ATOM 1486 CB ARG A 220 5.899 49.112 1.745 1.00 24.79 A C

ATOM 1487 CG ARG A 220 6.578 49.889 0.605 1.00 28.86 A C

ATOM 1488 CD ARG A 220 5.952 51.233 0.388 1.00 29.90 A C

ATOM 1489 NE ARG A 220 4.591 51.110 -0.123 1.00 34.40 A N

ATOM 1490 CZ ARG A 220 3.579 51.908 0.211 1.00 35.77 A C

ATOM 1491 NHl ARG A 220 3.755 52.911 1.069 1.00 33.84 A N

ATOM 1492 NH2 ARG A 220 2.383 51.706 -0.330 1.00 38.27 A N

ATOM 1493 C ARG A 220 7.986 48.255 2.823 1.00 21.80 A C ATOM 1494 0 ARG A 220 9.035 47.959 2.272 1.00 19.45 A O

ATOM 1495 N TYR A 221 7.924 48.799 4.039 1.00 22.04 A N

ATOM 1496 CA TYR A 221 9.113 49.277 4.747 1.00 21.20 A C

ATOM 1497 CB TYR A 221 8.706 49.992 6.047 1.00 20.06 A C

ATOM 1498 CG TYR A 221 7.763 51.192 5.922 1.00 23.24 A C

ATOM 1499 CDl TYR A 221 7.231 51.804 7.082 1.00 23.96 A C

ATOM 1500 CE1 TYR A 221 6.349 52.922 6.995 1.00 22.05 A C

ATOM 1501 CD2 TYR A 221 7.386 51.727 4.665 1.00 22.76 A C

ATOM 1502 CE2 TYR A 221 6.504 52.835 4.571 1.00 22.62 A C

ATOM 1503 CZ TYR A 221 6.001 53.425 5.739 1.00 23.22 A C

ATOM 1504 OH TYR A 221 5.192 54.528 5.646 1.00 26.64 A O

ATOM 1505 C TYR A 221 10.156 48.203 5.055 1.00 21.73 A C

ATOM 1506 O TYR A 221 11.336 48.502 5.278 1.00 21.18 A O

ATOM 1507 N TYR A 222 9.715 46.950 4.978 1.00 22.51 A N

ATOM 1508 CA TYR A 222 10.540 45.782 5.304 1.00 22.04 A C

ATOM 1509 CB TYR A 222 9.821 44.952 6.389 1.00 20.59 A C

ATOM 1510 CG TYR A 222 9.331 45.808 7.543 1.00 21.83 A C

ATOM 1511 CDl TYR A 222 10.195 46.148 8.606 1.00 22.50 A C

ATOM 1512 CE1 TYR A 222 9.802 47.078 9.609 1.00 21.27 A C

ATOM 1513 CD2 TYR A 222 8.047 46.401 7.513 1.00 17.37 A C

ATOM 1514 CE2 TYR A 222 7.639 47.327 8.510 1.00 16.78 A C ATOM 1515 CZ TYR A 222 8.527 47.662 9.548 1.00 20.10 A C

ATOM 1516 OH TYR A 222 8.167 48.582 10.502 1.00 21.58 A O

ATOM 1517 C TYR A 222 10.877 44.911 4.106 1.00 20.47 A C

ATOM 1518 O TYR A 222 11.677 43.987 4.220 1.00 22.09 A O

ATOM 1519 N ARG A 223 10.305 45.247 2.953 1.00 19.61 A N

ATOM 1520 CA ARG A 223 10.501 44.506 1.710 1.00 19.52 A C

ATOM 1521 CB ARG A 223 9.487 45.008 0.689 1.00 20.62 A C

ATOM 1522 CG ARG A 223 9.364 44.214 -0.591 1.00 22.09 A C

ATOM 1523 CD ARG A 223 8.304 44.815 -1.504 1.00 19.75 A C

ATOM 1524 NE ARG A 223 6.965 44.700 -0.933 1.00 17.36 A N

ATOM 1525 CZ ARG A 223 6.023 45.636 -0.989 1.00 18.98 A C

ATOM 1526 NHl ARG A 223 6.251 46.800 -1.598 1.00 18.60 A N

ATOM 1527 NH2 ARG A 223 4.843 45.404 -0.421. 1.00 19.71 A N

ATOM 1528 C ARG A 223 11.930 44.568 1.154 1.00 22.14 A C

ATOM 1529 O ARG A 223 12.491 45.648 0.935 1.00 21.59 A O

ATOM 1530 N ALA A 224 12.507 43.385 0.947 1.00 25.00 A N

ATOM 1531 CA ALA A 224 13.865 43.228 0.422 1.00 28.52 A C

ATOM 1532 CB ALA A 224 14.297 41.765 0.524 1.00 28.25 A C

ATOM 1533 C ALA A 224 14.011 43.749 -1.006 1.00 29.59 A C

ATOM 1534 O ALA A 224 13.070 43.645 -1.792 1.00 30.88 A O

ATOM 1535 N PRO A 225 15.190 44.315 -1.360 1.00 30.76 A N ATOM 1536 CD PRO A 225 16.382 44.545 -0.526 1.00 29.59 A C

ATOM 1537 CA PRO A 225 15.420 44.849 -2.705 1.00 31.34 A C

ATOM 1538 CB PRO A 225 16.798 45.499 -2.592 1.00 31.48 A C

ATOM 1539 CG PRO A 225 17.471 44.689 -1.529 1.00 32.57 A C

ATOM 1540 C PRO A 225 15.273 43.895 -3.891 1.00 31.12 A C

ATOM 1541 O PRO A 225 15.088 44.353 -5.001 1.00 32.29 A O

ATOM 1542 N GLU A 226 15.254 42.585 -3.640 1.00 32.81 A N

ATOM 1543 CA GLU A 226 15.065 41.582 -4.706 1.00 33.56 A C

ATOM 1544 CB GLU A 226 15.218 40.144 -4.194 1.00 34.04 A C

ATOM 1545 CG GLU A 226 16.510 39.804 -3.531 1.00 34.67 A C

ATOM 1546 CD GLU A 226 16.536 40.202 -2.078 1.00 36.49 A C

ATOM 1547 OEl GLU A 226 16.222 39.353 -1.218 1.00 37.14 A O

ATOM 1548 OE2 GLU A 226 16.882 41.368 -1.796 1.00 34.66 A O

ATOM 1549 C GLU A 226 13.643 41.709 -5.219 1.00 34.54 A C

ATOM 1550 O GLU A 226 13.410 41.667 -6.428 1.00 35.78 A O

ATOM 1551 N LEU A 227 12.709 41.906 -4.283 1.00 34.91 A N

ATOM 1552 CA LEU A 227 11.291 42.042 -4.601 1.00 36.36 A C

ATOM 1553 CB LEU A 227 10.423 41.853 -3.359 1.00 40.67 A C

ATOM 1554 CG LEU A 227 10.400 40.586 -2.500 1.00 43.41 A C

ATOM 1555 CDl LEU A 227 10.793 39.370 -3.290 1.00 43.06 A C

ATOM 1556 CD2 LEU A 227 11.305 40.766 -1.331 1.00 43.69 A C ATOM 1557 C LEU A 227 10.92943.358 -5.267 1.0034.40 A C

ATOM 1558 O LEUA227 9.93343.423 -6.001 1.0035.29 A O

ATOM 1559 N ILEA228 11.71344.405 -4.989 1.0032.56 A N

ATOM 1560 CA ILE A 228 11.48745.720 -5.608 1.0032.16 A C

ATOM 1561 CB ILE A 228 12.35846.862 -4.988 1.0032.60 A C

ATOM 1562 CG2ILEA228 11.88048.216 -5.523 1.0028.97 A C

ATOM 1563 CGI ILE A 228 12.36246.827 -3.443 1.0031.25 A C

ATOM 1564 CDl ILE A 228 11.09547.221 -2.742 1.0035.65 A C

ATOM 1565 C ILE A 228 11.87645.552 -7.090 1.0030.83 A C

ATOM 1566 O ILE A 228 11.16746.024 -7.986 1.0028.70 A O

ATOM 1567 N PHEA229 12.96044.802 -7.314 1.0029.19 A N

ATOM 1568 CA PHE A 229 13.46444.485 -8.651 1.0030.76 A C

ATOM 1569 CB PHE A 229 14.95544.130 -8.607 1.0027.42 A C

ATOM 1570 CG PHE A 229 15.87045.324 -8.493 1.0026.49 A C

ATOM 1571 CDl PHE A 229 16.42045.695 -7.254 1.0025.53 A C

ATOM 1572 CD2PHEA229 16.201 46.078 -9.627 1.0026.43 A C

ATOM 1573 CE1PHEA229 17.29746.811 -7.133 1.0026.62 A C

ATOM 1574 CE2PHEA229 17.07947.204 -9.540 1.0029.28 A C

ATOM 1575 CZ PHE A 229 17.63047.572 -8.280 1.0029.17 A C

ATOM 1576 C PHE A 229 12.65043.343 -9.287 1.0032.87 A C

ATOM 15770 PHE A 229 12.96542.873-10.388 1.0033.65 A O ATOM 1578 N GLY A 230 11.623 42.890 -8.564 1.00 33.72 A N

ATOM 1579 CA GLY A 230 10.731 41.851 -9.054 1.00 35.89 A C

ATOM 1580 C GLY A 230 11.176 40.400 -9.164 1.00 37.51 A C

ATOM 1581 O GLY A 230 10.628 39.667 -10.002 1.00 36.98 A O

ATOM 1582 N ALA A 231 12.084 39.957 -8.288 1.00 37.64 A N

ATOM 1583 CA ALA A 231 12.574 38.575 -8.302 1.00 38.32 A C

ATOM 1584 CB ALA A 231 13.759 38.424 -7.391 1.00 37.75 A C

ATOM 1585 C ALA A 231 11.485 37.590 -7.898 1.00 40.02 A C

ATOM 1586 O ALA A 231 10.649 37.893 -7.040 1.00 40.82 A O

ATOM 1587 N THR A 232 11.463 36.443 -8.574 1.00 39.60 A N

ATOM 1588 CA THR A 232 10.483 35.401 -8.299 1.00 39.65 A C

ATOM 1589 CB THR A 232 9.559 35.132 -9.533 1.00 41.94 A C

ATOM 1590 OGl THR A 232 10.346 35.024 -10.730 1.00 42.76 A O

ATOM 1591 CG2 THR A 232 8.512 36.249 -9.696 1.00 40.72 A C

ATOM 1592 C THR A 232 11.133 34.105 -7.803 1.00 39.31 A C

ATOM 1593 O THR A 232 10.434 33.172 -7.400 1.00 40.10 A O

ATOM 1594 N ASP A 233 12.468 34.077 -7.795 1.00 40.13 A N

ATOM 1595 CA ASP A 233 13.250 32.916 -7.348 1.00 41.25 A C

ATOM 1596 CB ASP A 233 14.129 32.374 -8.506 1.00 43.94 A C

ATOM 1597 CG ASP A 233 15.313 33.306 -8.884 1.00 47.37 A C

ATOM 1598 OD1 ASP A 233 16.351 32.771 -9.350 1.00 46.27 A O ATOM 1599 OD2ASPA233 15.21934.546 -8.700 1.0048.50 A O

ATOM 1600 C ASP A 233 14.101 33.250 -6.110 1.0041.12 A C

ATOM 1601 O ASPA233 15.211 32.729 -5.940 1.0041.52 A O

ATOM 1602 N TYRA234 13.56934.126 -5.257 1.0039.65 A N

ATOM 1603 CA TYR A 234 14.25034.579 -4.038 1.0039.13 A C

ATOM 1604 CB TYR A 234 13.61735.892 -3.531 1.0036.13 A C

ATOM 1605 CG TYR A 234 12.11835.822 -3.293 1.0034.48 A C

ATOM 1606 CDl TYR A 234 11.59535.516 -2.014 1.0033.16 A C

ATOM 1607 CE1 TYR A 234 10.20435.407 -1.798 1.0033.47 A C

ATOM 1608 CD2TYRA234 11.21336.025 -4.351 1.0034.12 A C

ATOM 1609 CE2 TYR A 234 9.81035.923 -4.149 1.0036.01 A C

ATOM 1610 CZ TYR A 234 9.31935.611 -2.868 1.0035.41 A C

ATOM 1611 OH TYRA234 7.961 35.483 -2.668 1.0035.00 A O

ATOM 1612 C TYR A 234 14.28433.536 -2.911 1.0040.34 A C

ATOM 1613 O TYR A 234 13.33632.748 -2.753 1.0040.52 A O

ATOM 1614 N THRA235 15.35533.582 -2.113 1.0040.13 A N

ATOM 1615 CA THRA235 15.551 32.672 -0.978 1.0039.29 A C

ATOM 1616 CB THR A 235 17.06432.367 -0.746 1.0040.43 A C

ATOM 1617 OGl THR A 235 17.80833.592 -0.636 1.0045.53 A O

ATOM 1618 CG2THRA235 17.62631.550 -1.899 1.0039.97 A C

ATOM 1619 C THR A 235 14.90333.229 0.295 1.0036.84 A C ATOM 1620 O THR A 235 14.415 34.360 0.297 1.00 36.88 A O

ATOM 1621 N SER A 236 14.906 32.441 1.376 1.00 35.70 A N

ATOM 1622 CA SER A 236 14.308 32.842 2.664 1.00 33.11 A C

ATOM 1623 CB SER A 236 14.196 31.645 3.614 1.00 32.13 A C

ATOM 1624 OG SER A 236 15.465 31.228 4.076 1.00 36.13 A O

ATOM 1625 C SER A 236 15.044 34.005 3.327 1.00 30.51 A C

ATOM 1626 O SER A 236 14.610 34.549 4.345 1.00 29.27 A O

ATOM 1627 N SER A 237 16.109 34.426 2.648 1.00 27.13 A N

ATOM 1628 CA SER A 237 16.983 35.535 2.997 1.00 22.41 A C

ATOM 1629 CB SER A 237 18.086 35.598 1.939 1.00 20.91 A C

ATOM 1630 OG SER A 237 18.953 36.686 2.118 1.00 24.91 A O

ATOM 1631 C SER A 237 16.226 36.876 3.067 1.00 21.98 A C

ATOM 1632 O SER A 237 16.749 37.852 3.610 1.00 23.14 A O

ATOM 1633 N ILE A 238 15.003 36.923 2.521 1.00 20.97 A N

ATOM 1634 CA ILE A 238 14.172 38.137 2.547 1.00 19.72 A C

ATOM 1635 CB ILE A 238 12.949 38.060 1.604 1.00 18.06 A C

ATOM 1636 CG2 ILE A 238 13.404 38.049 0.153 1.00 19.86 A C

ATOM 1637 CGI ILE A 238 12.091 36.833 1.902 1.00 18.85 A C

ATOM 1638 CDl ILE A 238 10.645 37.047 1.563 1.00 15.98 A C

ATOM 1639 C ILE A 238 13.710 38.482 3.965 1.00 20.89 A C

ATOM 1640 O ILE A 238 13.580 39.663 4.309 1.00 20.87 A O ATOM 1641 N ASP A 239 13.520 37.438 4.783 1.00 22.24 A N

ATOM 1642 CA ASP A 239 13.1 19 37.559 6.189 1.00 21.94 A C

ATOM 1643 CB ASP A 239 12.774 36.188 6.807 1.00 23.31 A C

ATOM 1644 CG ASP A 239 11.451 35.604 6.305 1.00 25.59 A C

ATOM 1645 OD1 ASP A 239 10.643 36.323 5.675 1.00 24.86 A O

ATOM 1646 OD2 ASP A 239 11.216 34.398 6.556 1.00 26.08 A O

ATOM 1647 C ASP A 239 14.286 38.153 6.962 1.00 20.53 A C

ATOM 1648 O ASP A 239 14.079 38.904 7.918 1.00 22.47 A O

ATOM 1649 N VAL A 240 15.505 37.855 6.505 1.00 17.51 A N

ATOM 1650 CA VAL A 240 16.721 38.366 7.138 1.00 17.98 A C

ATOM 1651 CB VAL A 240 17.994 37.592 6.679 1.00 16.44 A C

ATOM 1652 CGI VAL A 240 19.247 38.139 7.350 1.00 13.47 A C

ATOM 1653 CG2 VAL A 240 17.849 36.105 7.022 1.00 13.28 A C

ATOM 1654 C VAL A 240 16.864 39.867 6.913 1.00 17.18 A C

ATOM 1655 O VAL A 240 17.247 40.588 7.825 1.00 20.03 A O

ATOM 1656 N TRP A 241 16.520 40.332 5.713 1.00 19.12 A N

ATOM 1657 CA TRP A 241 16.568 41.761 5.384 1.00 17.41 A C

ATOM 1658 CB TRP A 241 16.226 41.995 3.904 1.00 17.34 A C

ATOM 1659 CG TRP A 241 15.955 43.466 3.563 1.00 18.47 A C

ATOM 1660 CD2 TRP A 241 16.898 44.415 3.078 1.00 19.08 A C

ATOM 1661 CE2 TRP A 241 16.217 45.664 2.964 1.00 18.40 A C ATOM 1662 CE3 TRP A 241 18.259 44.343 2.714 1.00 18.24 A C

ATOM 1663 CDl TRP A 241 14.764 44.157 3.712 1.00 18.48 A C

ATOM 1664 NE1 TRP A 241 14.921 45.469 3.360 1.00 19.49 A N

ATOM 1665 CZ2 TRP A 241 16.852 46.824 2.507 1.00 16.68 A C

ATOM 1666 CZ3 TRP A 241 18.892 45.515 2.250 1.00 18.40 A C

ATOM 1667 CH2 TRP A 241 18.182 46.733 2.155 1.00 16.97 A C

ATOM 1668 C TRP A 241 15.532 42.477 6.259 1.00 15.48 A C

ATOM 1669 O . TRP A 241 15.805 43.542 6.822 1.00 14.74 A O

ATOM 1670 N SER A 242 14.318 41.932 6.237 1.00 12.59 A N

ATOM 1671 CA SER A 242 13.195 42.443 7.005 1.00 13.83 A C

ATOM 1672 CB SER A 242 11.996 41.532 6.844 1.00 11.05 A C

ATOM 1673 OG SER A 242 11.493 41.552 5.526 1.00 16.25 A O

ATOM 1674 C SER A 242 13.542 42.560 8.474 1.00 15.02 A C

ATOM 1675 0 SER A 242 13.247 43.578 9.092 1.00 16.74 A O

ATOM 1676 N ALA A 243 14.266 41.552 8.978 1.00 16.60 A N

ATOM 1677 CA ALA A 243 14.721 41.479 10.368 1.00 14.09 A C

ATOM 1678 CB ALA A 243 15.329 40.144 10.641 1.00 11.12 A C

ATOM 1679 C ALA A 243 15.714 42.590 10.650 1.00 15.69 A C

ATOM 1680 O ALA A 243 15.698 43.189 11.728 1.00 16.31 A O

ATOM 1681 N GLY A 244 16.527 42.901 9.641 1.00 16.63 A N

ATOM 1682 CA GLY A 244 17.504 43.975 9.741 1.00 19.58 A C ATOM 1683 C GLY A 244 16.845 45.346 9.777 1.00 20.75 A C

ATOM 1684 O GLY A 244 17.396 46.275 10.367 1.00 22.25 A O

ATOM 1685 N CYS A 245 15.676 45.464 9.132 1.00 20.19 A N

ATOM 1686 CA CYS A 245 14.895 46.697 9.097 1.00 18.63 A C

ATOM 1687 CB CYS A 245 13.796 46.620 8.037 1.00 19.55 A C

ATOM 1688 SG CYS A 245 14.354 46.652 6.290 1.00 22.46 A S

ATOM 1689 C CYS A 245 14.291 46.923 10.481 1.00 17.40 A C

ATOM 1690 O CYS A 245 14.195 48.057 10.939 1.00 19.09 A O

ATOM 1691 N VAL A 246 13.965 45.825 11.168 1.00 16.69 A N

ATOM 1692 C A VAL A 246 13.413 45.861 12.534 1.00 17.03 A C

ATOM 1693 CB VAL A 246 12.923 44.462 13.011 1.00 17.12 A C

ATOM 1694 CGI VAL A 246 12.365 44.543 14.444 1.00 14.75 A C

ATOM 1695 CG2 VAL A 246 11.907 43.882 12.038 1.00 13.18 A C

ATOM 1696 C VAL A 246 14.521 46.320 13.494 1.00 16.65 A C

ATOM 1697 0 VAL A 246 14.304 47.203 14.320 1.00 19.70 A O

ATOM 1698 N LEU A 247 15.704 45.728 13.352 1.00 15.00 A N

ATOM 1699 CA LEU A 247 16.861 46.068 14.170 1.00 17.14 A C

ATOM 1700 CB LEU A 247 18.072 45.219 13.764 1.00 18.29 A C

ATOM 1701 CG LEU A 247 19.389 45.551 14.467 1.00 18.64 A C

ATOM 1702 CDl LEU A 247 19.332 45.227 15.953 1.00 19.89 A C

ATOM 1703 CD2 LEU A 247 20.497 44.819 13.806 1.00 20.99 A C ATOM 1704 C LEU A 247 17.198 47.548 14.059 1.00 16.69 A C

ATOM 1705 O LEU A 247 17.345 48.245 15.070 1.00 17.59 A O

ATOM 1706 N ALA A 248 17.206 48.030 12.824 1.00 16.14 A N

ATOM 1707 CA ALA A 248 17.501 49.414 12.546 1.00 15.97 A C

ATOM 1708 CB ALA A 248 17.626 49.605 11.071 1.00 17.23 A C

ATOM 1709 C ALA A 248 16.446 50.340 13.143 1.00 16.83 A C

ATOM 1710 O ALA A 248 16.795 51.332 13.780 1.00 19.30 A O

ATOM 1711 N GLU A 249 15.175 49.927 13.061 1.00 18.04 A N

ATOM 1712 CA GLU A 249 14.036 50.695 13.591 1.00 18.02 A C

ATOM 1713 CB GLU A 249 12.714 50.021 13.181 1.00 17.49 A C

ATOM 1714 CG GLU A 249 11.427 50.757 13.588 1.00 18.63 A C

ATOM 1715 CD GLU A 249 10.192 50.296 12.816 1.00 24.35 A C

ATOM 1716 OEl GLU A 249 10.320 49.876 11.643 1.00 23.91 A O

ATOM 1717 OE2 GLU A 249 9.074 50.384 13.372 1.00 28.62 A O

ATOM 1718 C GLU A 249 14.119 50.818 15.120 1.00 19.52 A C

ATOM 1719 O GLU A 249 13.918 51.906 15.690 1.00 15.73 A O

ATOM 1720 N LEU A 250 14.515 49.716 15.756 1.00 19.28 A N

ATOM 1721 CA LEU A 250 14.625 49.656 17.208 1.00 20.52 A C

ATOM 1722 CB LEU A 250 14.779 48.199 17.682 1.00 21.30 A C

ATOM 1723 CG LEU A 250 13.574 47.239 17.537 1.00 18.87 A C

ATOM 1724 CDl LEU A 250 13.786 46.050 18.423 1.00 16.34 A C ATOM 1725 CD2 LEU A 250 12.262 47.916 17.942^' 1.00 17.21 A C

ATOM 1726 C LEU A 250 15.716 50.545 17.778 1.00 20.14 A C

ATOM 1727 O LEU A 250 15.600 51.023 18.912 1.00 22.30 A O

ATOM 1728 N LEU A 251 16.713 50.843 16.946 1.00 18.89 A N

ATOM 1729 CA LEU A 251 17.840 51.697 17.336 1.00 18.41 A C

ATOM 1730 CB LEU A 251 19.127 51.214 16.660 1.00 12.63 A C

ATOM 1731 CG LEU A 251 19.555 49.767 16.953 1.00 10.51 A C

ATOM 1732 CDl LEU A 251 20.565 49.278 15.919 1.00 5.57 A C

ATOM 1733 CD2 LEU A 251 20.090 49.633 18.370 1.00 9.38 A C

ATOM 1734 C LEU A 251 17.597 53.155 16.971 1.00 19.33 A C

ATOM 1735 O LEU A 251 18.084 54.066 17.651 1.00 21.92 A O

ATOM 1736 N LEU A 252 16.844 53.367 15.896 1.00 17.42 A N

ATOM 1737 CA LEU A 252 16.557 54.702 15.409 1.00 18.59 A C

ATOM 1738 CB LEU A 252 16.387 54.677 13.899 1.00 21.67 A C

ATOM 1739 CG LEU A 252 17.688 54.802 13.124 1.00 22.29 A C

ATOM 1740 CDl LEU A 252 17.494 54.355 11.697 1.00 27.61 A C

ATOM 1741 CD2 LEU A 252 18.164 56.241 13.184 1.00 27.99 A C

ATOM 1742 C LEU A 252 15.364 55.373 16.030 1.00 20.79 A C

ATOM 1743 O LEU A 252 15.317 56.611 16.109 1.00 21.21 A O

ATOM 1744 N GLY A 253 14.387 54.553 16.420 1.00 22.24 A N

ATOM 1745 CA GLY A 253 13.160 55.051 17.022 1.00 24.26 A C ATOM 1746 C GLY A 253 12.086 55.367 15.993 1.00 26.26 A C

ATOM 1747 O GLY A 253 11.047 55.940 16.319 1.00 27.52 A O

ATOM 1748 N GLN A 254 12.382 55.056 14.735 1.00 26.36 A N

ATOM 1749 CA GLN A 254 11.477 55.270 13.605 1.00 28.51 A C

ATOM 1750 CB GLN A 254 11.479 56.755 13.172 1.00 30.13 A C

ATOM 1751 CG GLN A 254 12.843 57.346 12.871 1.00 33.35 A C

ATOM 1752 CD GLN A 254 12.760 58.511 11.930 1.00 36.40 A C

ATOM 1753 OEl GLN A 254 13.138 58.409 10.759 1.00 38.80 A O

ATOM 1754 NE2 GLN A 254 12.251 59.629 12.423 1.00 39.90 A N

ATOM 1755 C GLN A 254 11.955 54.350 12.463 1.00 27.98 A C

ATOM 1756 O GLN A 254 13.128 53.954 12.446 1.00 31.61 A O

ATOM 1757 N PRO A 255 11.057 53.945 11.532 1.00 25.97 A N

ATOM 1758 CD PRO A 255 9.587 54.063 11.504 1.00 26.58 A C

ATOM 1759 CA PRO A 255 11.507 53.067 10.438 1.00 24.03 A C

ATOM 1760 CB PRO A 255 10.212 52.774 9.669 1.00 23.65 A C

ATOM 1761 CG PRO A 255 9.300 53.870 10.052 1.00 25.92 A C

ATOM 1762 C PRO A 255 12.620 53.635 9.571 1.00 21.35 A C

ATOM 1763 O PRO A 255 12.608 54.825 9.242 1.00 21.96 A O

ATOM 1764 N ILE A 256 13.614 52.790 9.287 1.00 19.07 A N

ATOM 1765 CA ILE A 256 14.773 53.188 8.496 1.00 17.54 A C

ATOM 1766 CB ILE A 256 15.973 52.179 8.629 1.00 17.39 A C ATOM 1767 CG2 ILE A 256 15.591 50.769 8.162 1.00 13.59 A C

ATOM 1768 CGI ILE A 256 17.237 52.746 7.939 1.00 16.44 A C

ATOM 1769 CDl ILE A 256 18.494 51.913 8.077 1.00 14.86 A C

ATOM 1770 C ILE A 256 14.435 53.466 7.049 1.00 20.68 A C

ATOM 1771 O ILE A 256 14.965 54.408 6.448 1.00 21.57 A O

ATOM 1772 N PHE A 257 13.533 52.666 6.484 1.00 22.77 A N

ATOM 1773 CA PHE A 257 13.143 52.861 5.087 1.00 22.10 A C

ATOM 1774 CB PHE A 257 13.566 51.668 4.223 1.00 19.66 A C

ATOM 1775 CG PHE A 257 15.002 51.308 4.341 1.00 16.70 A C

ATOM 1776 CDl PHE A 257 16.007 52.286 4.181 1.00 16.19 A C

ATOM 1777 CD2 PHE A 257 15.370 49.980 4.597 1.00 16.77 A C

ATOM 1778 CE1 PHE A 257 17.353 51.948 4.272 1.00 13.12 A C

ATOM 1779 CE2 PHE A 257 16.728 49.615 4.693 1.00 16.25 A C

ATOM 1780 CZ PHE A 257 17.723 50.599 4.529 1.00 16.81 A C

ATOM 1781 C PHE A 257 11.652 53.146 4.882 1.00 22.20 A C

ATOM 1782 O PHE A 257 10.916 52.269 4.434 1.00 24.07 A O

ATOM 1783 N PRO A 258 1 1.202 54.392 5.143 1.00 23.42 A N

ATOM 1784 CD PRO A 258 11.883 55.506 5.845 1.00 22.97 A C

ATOM 1785 CA PRO A 258 9.776 54.695 4.964 1.00 25.60 A C

ATOM 1786 CB PRO A 258 9.542 55.782 6.009 1.00 25.06 A C

ATOM 1787 CG PRO A 258 10.825 56.580 5.924 1.00 23.84 A C ATOM 1788 C PRO A 258 9.320 55.130 3.561 1.00 27.86 A C

ATOM 1789 0 PRO A 258 8.834 56.252 3.378 1.00 31.43 A O

ATOM 1790 N GLY A 259 9.388 54.216 2.597 1.00 28.74 A N

ATOM 1791 CA GLY A 259 8.993 54.542 1.232 1.00 31.74 A C

ATOM 1792 C GLY A 259 7.507 54.768 0.989 1.00 33.82 A C

ATOM 1793 O GLY A 259 6.659 54.242 1.726 1.00 33.71 A O

ATOM 1794 N ASP A 260 7.195 55.572 -0.030 1.00 34.60 A N

ATOM 1795 CA ASP A 260 5.803 55.871 -0.393 1.00 35.75 A C

ATOM 1796 CB ASP A 260 5.675 57.284 -0.949 1.00 37.17 A C

ATOM 1797 CG ASP A 260 5.595 58.325 0.143 1.00 42.70 A C

ATOM 1798 OD1 ASP A 260 6.291 59.362 0.022 1.00 43.50 A O

ATOM 1799 OD2 ASP A 260 4.831 58.104 1.122 1.00 42.33 A O

ATOM 1800 C ASP A 260 5.212 54.878 -1.378 1.00 34.19 A C

ATOM 1801 O ASP A 260 4.006 54.649 -1.386 1.00 35.08 A O

ATOM 1802 N SER A 261 6.082 54.269 -2.175 1.00 32.74 A N

ATOM 1803 CA SER A 261 5.687 53.292 -3.183 1.00 32.28 A C

ATOM 1804 CB SER A 261 5.565 53.973 -4.560 1.00 33.32 A C

ATOM 1805 OG SER A 261 6.808 54.524 -4.983 1.00 32.63 A O

ATOM 1806 C SER A 261 6.757 52.217 -3.246 1.00 30.14 A C

ATOM 1807 O SER A 261 7.752 52.282 -2.521 1.00 30.74 A O

ATOM 1808 N GLY A 262 6.550 51.248 -4.134 1.00 28.27 A N ATOM 1809 CA GLY A 262 7.510 50.181 -4.345 1.00 28.00 A C

ATOM 1810 C GLY A 262 8.793 50.742 -4.929 1.00 28.04 A C

ATOM 1811 O GLY A 262 9.879 50.317 -4.550 1.00 29.79 A O

ATOM 1812 N VAL A 263 8.666 51.776 -5.759 1.00 29.12 A N

ATOM 1813 CA VAL A 263 9.824 52.413 -6.382 1.00 30.23 A C

ATOM 1814 CB VAL A 263 9.472 53.147 -7.729 1.00 31.30 A C

ATOM 1815 CGI VAL A 263 10.749 53.439 -8.515 1.00 30.29 A C

ATOM 1816 CG2 VAL A 263 8.539 52.292 -8.597 1.00 31.94 A C

ATOM 1817 C VAL A 263 10.497 53.371 -5.398 1.00 29.25 A C

ATOM 1818 O VAL A 263 11.724 53.418 -5.328 1.00 29.30 A O

ATOM 1819 N ASP A 264 9.700 54.082 -4.599 1.00 29.24 A N

ATOM 1820 CA ASP A 264 10.256 55.010 -3.607 1.00 28.75 A C

ATOM 1821 CB ASP A 264 9.199 55.978 -3.047 1.00 30.46 A C

ATOM 1822 CG ASP A 264 9.812 57.046 -2.144 1.00 33.03 A C

ATOM 1823 OD1 ASP A 264 10.871 57.603 -2.512 1.00 34.94 A O

ATOM 1824 OD2 ASP A 264 9.280 57.278 -1.040 1.00 37.33 A O

ATOM 1825 C ASP A 264 10.971 54.270 -2.469 1.00 26.56 A C

ATOM 1826 O ASP A 264 11.865 54.831 -1.829 1.00 26.01 A O

ATOM 1827 N GLN A 265 10.572 53.018 -2.234 1.00 23.87 A N

ATOM 1828 CA GLN A 265 11.198 52.175 -1.219 1.00 23.64 A C

ATOM 1829 CB GLN A 265 10.468 50.836 -1.079 1.00 22.07 A C ATOM 1830 CG GLN A 265 10.926 49.971 0.110 1.00 19.47 A C

ATOM 1831 CD GLN A 265 10.674 50.606 1.468 1.00 21.09 A C

ATOM 1832 OEl GLN A 265 11.471 50.457 2.389 1.00 23.45 A O

ATOM 1833 NE2 GLN A 265 9.535 51.265 1.618 1.00 22,26 A N

ATOM 1834 C GLN A 265 12.659 51.931 -1.609 1.00 24.35 A C

ATOM 1835 O GLN A 265 13.541 51.905 -0.740 1.00 19.95 A O

ATOM 1836 N LEU A 266 12.903 51.815 -2.920 1.00 24.99 A N

ATOM 1837 CA LEU A 266 14.252 51.604 -3.440 1.00 26.98 A C

ATOM 1838 CB LEU A 266 14.209 51.120 -4.887 1.00 30.33 A C

ATOM 1839 CG LEU A 266 15.506 50.603 -5.530 1.00 33.62 A C

ATOM 1840 CDl LEU A 266 16.128 49.484 -4.695 1.00 34.02 A C

ATOM 1841 CD2 LEU A 266 15.218 50.126 -6.937 1.00 33.72 A C

ATOM 1842 C LEU A 266 15.102 52.879 -3.320 1.00 25.91 A C

ATOM 1843 O LEU A 266 16.282 52.799 -3.029 1.00 25.13 A O

ATOM 1844 N VAL A 267 14.471 54.044 -3.450 1.00 25.29 A N

ATOM 1845 CA VAL A 267 15.169 55.330 -3.342 1.00 26.05 A C

ATOM 1846 CB VAL A 267 14.271 56.515 -3.778 1.00 25.47 A C

ATOM 1847 CGI VAL A 267 15.064 57.829 -3.762 1.00 23.88 A C

ATOM 1848 CG2 VAL A 267 13.712 56.248 -5.167 1.00 23.02 A C

ATOM 1849 C VAL A 267 15.601 55.532 -1.905 1.00 25.54 A C

ATOM 1850 O VAL A 267 16.706 56.001 -1.621 1.00 29.62 A O ATOM 1851 N GLU A 268 14.752 55.043 -1.022 1.00 23.24 A N

ATOM 1852 CA GLU A 268 14.944 55.121 0.399 1.00 22.64 A C

ATOM 1853 CB GLU A 268 13.602 54.827 1.043 1.00 21.78 A C

ATOM 1854 CG GLU A 268 13.440 55.269 2.433 1.00 24.50 A C

ATOM 1855 CD GLU A 268 13.797 56.692 2.692 1.00 26.24 A C

ATOM 1856 OEl GLU A 268 13.065 57.580 2.209 1.00 28.07 A O

ATOM 1857 OE2 GLU A 268 14.812 56.903 3.396 1.00 27.50 A O

ATOM 1858 C GLU A 268 16.046 54.177 0.885 1.00 22.74 A C

ATOM 1859 O GLU A 268 16.728 54.475 1.864 1.00 24.12 A O

ATOM 1860 N ILE A 269 16.236 53.075 0.155 1.00 23.95 A N

ATOM 1861 CA ILE A 269 17.265 52.064 0.432 1.00 23.66 A C

ATOM 1862 CB ILE A 269 16.875 50.668 -0.173 1.00 23.47 A C

ATOM 1863 CG2 ILE A 269 18.058 49.681 -0.147 1.00 22.43 A C

ATOM 1864 CGI ILE A 269 15.710 50.067 0.631 1.00 22.30 A C

ATOM 1865 CDl ILE A 269 15.007 48.883 -0.035 1.00 20.05 A C

ATOM 1866 C ILE A 269 18.596 52.568 -0.133 1.00 25.13 A C

ATOM 1867 O ILE A 269 19.641 52.465 0.530 1.00 26.08 A O

ATOM 1868 N ILE A 270 18.523 53.166 -1.327 1.00 25.14 A N

ATOM 1869 CA ILE A 270 19.675 53.738 -2.023 1.00 23.85 A C

ATOM 1870 CB ILE A 270 19.301 54.163 -3.502 1.00 24.45 A C

ATOM 1871 CG2 ILE A 270 20.390 55.067 -4.140 1.00 22.63 A C ATOM 1872 CGI ILE A 270 19.123 52.909 -4.372 1.00 22.79 A C

ATOM 1873 CDl ILE A 270 18.624 53.160 -5.777 1.00 20.24 A C

ATOM 1874 C ILE A 270 20.243 54.914 -1.218 1.00 24.63 A C

ATOM 1875 O ILE A 270 21.468 55.071 -1.142 1.00 23.03 A O

ATOM 1876 N LYS A 271 19.362 55.669 -0.547 1.00 23.96 A N

ATOM 1877 CA LYS A 271 19.771 56.820 0.275 1.00 24.69 A C

ATOM 1878 CB LYS A 271 18.550 57.542 0.841 1.00 26.54 A C

ATOM 1879 CG LYS A 271 17.940 58.618 -0.041 1.00 27.03 A C

ATOM 1880 CD LYS A 271 16.692 59.194 0.635 1.00 28.96 A C

ATOM 1881 CE LYS A 271 16.323 60.601 0.125 1.00 34.13 A C

ATOM 1882 NZ LYS A 271 15.887 60.697 -1.316 1.00 34.78 A N

ATOM 1883 C LYS A 271 20.714 56.458 1.433 1.00 25.82 A C

ATOM 1884 O LYS A 271 21.286 57.343 2.065 1.00 29.20 A O

ATOM 1885 N VAL A 272 20.849 55.160 1.720 1.00 26.09 A N

ATOM 1886 CA VAL A 272 21.726 54.664 2.781 1.00 24.70 A C

ATOM 1887 CB VAL A 272 20.912 53.923 3.927 1.00 24.12 A C

ATOM 1888 CGI VAL A 272 21.850 53.291 4.961 1.00 24.21 A C

ATOM 1889 CG2 VAL A 272 20.009 54.902 4.659 1.00 22.10 A C

ATOM 1890 C VAL A 272 22.807 53.742 2.199 1.00 24.35 A C

ATOM 1891 O VAL A 272 23.996 54.007 2.365 1.00 25.45 A O

ATOM 1892 N LEU A 273 22.392 52.682 1.503 1.00 22.66 A N ATOM 1893 CA LEU A 273 23.320 51.703 0.928 1.00 23.33 A C

ATOM 1894 CB LEU A 273 22.584 50.400 0.611 1.00 21.78 A C

ATOM 1895 CG LEU A 273 21.801 49.616 1.669 1.00 24.90 A C

ATOM 1896 CDl LEU A 273 21.578 48.189 1.191 1.00 21.65 A C

ATOM 1897 CD2 LEU A 273 22.547 49.594 2.993 1.00 24.53 A C

ATOM 1898 C LEU A 273 24.052 52.158 -0.333 1.00 26.01 A C

ATOM 1899 O LEU A 273 25.062 51.562 -0.735 1.00 26.55 A O

ATOM 1900 N GLY A 274 23.506 53.189 -0.974 1.00 26.36 A N

ATOM 1901 CA GLY A 274 24.075 53.699 -2.200 1.00 26.43 A C

ATOM 1902 C GLY A 274 23.530 52.920 -3.376 1.00 27.76 A C

ATOM 1903 O GLY A 274 22.844 51.906 -3.198 1.00 26.91 A O

ATOM 1904 N THR A 275 23.854 53.389 -4.578 1.00 29.66 A N

ATOM 1905 CA THR A 275 23.430 52.760 -5.827 1.00 33.25 A C

ATOM 1906 CB THR A 275 23.924 53.576 -7.028 1.00 33.53 A C

ATOM 1907 OGl THR A 275 23.697 54.965 -6.765 1.00 36.65 A O

ATOM 1908 CG2 THR A 275 23.178 53.176 -8.305 1.00 35.68 A C

ATOM 1909 C THR A 275 24.003 51.338 -5.919 1.00 34.88 A C

ATOM 1910 O THR A 275 25.205 51.139 -5.698 1.00 32.97 A O

ATOM 1911 N PRO A 276 23.129 50.327 -6.131 1.00 36.10 A N

ATOM 1912 CD PRO A 276 21.654 50.365 -6.141 1.00 34.88 A C

ATOM 1913 CA PRO A 276 23.611 48.945 -6.237 1.00 38.86 A C ATOM 1914 CB PROA276 22.31848.129 -6.326 1.0036.70 A C

ATOM 1915 CG PRO A 276 21.30649.106 -6.846 1.0035.97 A C

ATOM 1916 C PRO A 276 24.48748.759 -7.464 1.0042.29 A C

ATOM 19170 PRO A 276 24.17949.290 -8.538 1.0044.40 A O

ATOM 1918 N THR A 277 25.60248.051 -7.289 1.0045.73 A N

ATOM 1919 CA THR A 277 26.531 47.799 -8.390 1.0049.94 A C

ATOM 1920 CB THR A 277 27.86847.162 -7.914 1.0049.78 A C

ATOM 1921 OG1THRA277 27.64445.806 -7.504 1.0052.18 A O

ATOM 1922 CG2THRA277 28.47347.955 -6.766 1.0050.32 A C

ATOM 1923 C THRA277 25.89546.879 -9.431 1.0052.29 A C

ATOM 19240 THRA277 24.831 46.294 -9.188 1.005229 A O

ATOM 1925 N ARG A 278 26.57346.757-10.573 1.0055.65 A N

ATOM 1926 CA ARGA278 26.15845.931-11.713 1.0057.29 A C

ATOM 1927 CB ARG A 278 27.28545.929-12.759 1.0062.83 A C

ATOM 1928 CG ARG A 278 27.77447.329-13.194 1.0069.46 A C

ATOM 1929 CD ARG A 278 29.09647.274-13.987 1.0074.01 A C

ATOM 1930 NE ARG A 278 28.99846.485-15.219 1.0079.03 A N

ATOM 1931 CZ ARG A 278 28.92346.989-16.452 1.0081.31 A C

ATOM 1932 NHl ARG A 278 28.93848.305-16.657 1.0082.60 A N

ATOM 1933 NH2 ARG A 278 28.79246.167-17.488 1.0082.13 A N

ATOM 1934 C ARG A 278 25.85444.490-11.277 1.0055.48 A C ATOM 1935 O ARG A 278 24.764 43.965 -11.539 1.00 53.52 A O

ATOM 1936 N GLU A 279 26.792 43.925 -10.511 1.00 52.84 A N

ATOM 1937 CA GLU A 279 26.717 42.565 -9.990 1.00 50.16 A C

ATOM 1938 CB GLU A 279 28.122 42.122 -9.518 1.00 51.58 A C

ATOM 1939 CG GLU A 279 28.277 40.659 -9.023 1.00 53.57 A C

ATOM 1940 CD GLU A 279 27.807 39.603 -10.028 1.00 56.33 A C

ATOM 1941 OEl GLU A 279 27.084 38.670 -9.610 1.00 55.45 A O

ATOM 1942 OE2 GLU A 279 28.151 39.704 -11230 1.00 58.95 A O

ATOM 1943 C GLU A 279 25.667 42.411 -8.877 1.00 48.03 A C

ATOM 1944 O GLU A 279 25.032 41.351 -8.766 1.00 46.34 A O

ATOM 1945 N GLN A 280 25.467 43.473 -8.085 1.00 44.34 A N

ATOM 1946 CA GLN A 280 24.478 43.461 -7.003 1.00 40.87 A C

ATOM 1947 CB GLN A 280 24.609 44.702 -6.108 1.00 39.68 A C

ATOM 1948 CG GLN A 280 25.721 44.589 -5.063 1.00 36.03 A C

ATOM 1949 CD GLN A 280 25.948 45.871 -4.265 1.00 35.25 A C

ATOM 1950 OEl GLN A 280 25.967 46.967 -4.819 1.00 35.32 A O

ATOM 1951 NE2 GLN A 280 26.160 45.729 -2.959 1.00 33.42 A N

ATOM 1952 C GLN A 280 23.050 43.300 -7.533 1.00 39.21 A C

ATOM 1953 O GLN A 280 22.218 42.692 -6.872 1.00 36.70 A O

ATOM 1954 N ILE A 281 22.805 43.770 -8.758 1.00 40.26 A N

ATOM 1955 CA ILE A 281 21.494 43.643 -9.414 1.00 42.46 A C ATOM 1956 CB ILE A 281 21.379 44.494 -10.726 1.00 43.27 A C

ATOM 1957 CG2 ILE A 281 19.943 44.415 -11.305 1.00 43.18 A C

ATOM 1958 CGI ILE A 281 21.829 45.946 -10.505 1.00 43.86 A C

ATOM 1959 CDl ILE A 281 20.881 46.812 -9.721 1.00 44.42 A C

ATOM 1960 C ILE A 281 21.291 42.188 -9.834 1.00 43.67 A C

ATOM 1961 O ILE A 281 20.235 41.610 -9.576 1.00 44.15 A O

ATOM 1962 N ARG A 282 22.319 41.617 -10.472 1.00 46.57 A N

ATOM 1963 CA ARG A 282 22.309 40238 -10.980 1.00 49.33 A C

ATOM 1964 CB ARG A 282 23.665 39.896 -11.622 1.00 53.32 A C

ATOM 1965 CG ARG A 282 23.620 38.777 -12.688 1.00 57.88 A C

ATOM 1966 CD ARG A 282 23.646 39.317 -14.132 1.00 61.04 A C

ATOM 1967 NE ARG A 282 22.512 40.191 -14.452 1.00 63.02 A N

ATOM 1968 CZ ARG A 282 22.617 41.416 -14.969 1.00 65.07 A C

ATOM 1969 NHl ARG A 282 23.812 41.936 -15.239 1.00 65.14 A N

ATOM 1970 NH2 ARG A 282 21.522 42.141 -15.184 1.00 64.85 A N

ATOM 1971 C ARG A 282 21.957 39.206 -9.908 1.00 49.41 A C

ATOM 1972 0 ARG A 282 21.114 38.328 -10.139 1.00 49.71 A O

ATOM 1973 N GLU A 283 22.546 39.370 -8.721 1.00 48.54 A N

ATOM 1974 CA GLU A 283 22.307 38.477 -7.590 1.00 47.57 A C

ATOM 1975 CB GLU A 283 23.435 38.609 -6.575 1.00 49.61 A C

ATOM 1976 CG GLU A 283 24.750 38.066 -7.118 1.00 51.95 A C ATOM 1977 CD GLU A 283 25.903 38.221 -6.158 1.00 53.45 A C

ATOM 1978 OEl GLU A 283 26.431 37.185 -5.706 1.00 54.54 A O

ATOM 1979 OE2 GLU A 283 26.290 39.372 -5.855 1.00 55.06 A O

ATOM 1980 C GLU A 283 20.931 38.667 -6.944 1.00 46.54 A C

ATOM 1981 O GLU A 283 20.426 37.769 -6.267 1.00 44.63 A O

ATOM 1982 N MET A 284 20.306 39.811 -7.222 1.00 47.59 A N

ATOM 1983 CA MET A 284 18.972 40.120 -6.713 1.00 49.71 A C

ATOM 1984 CB MET A 284 18.807 41.626 -6.472 1.00 48.77 A C

ATOM 1985 CG MET A 284 19.514 42.119 -5.214 1.00 49.31 A C

ATOM 1986 SD MET A 284 19.046 43.777 -4.689 1.00 49.93 A S

ATOM 1987 CE MET A 284 19.994 44.785 -5.823 1.00 50.67 A C

ATOM 1988 C MET A 284 17.905 39.600 -7.677 1.00 51.96 A C

ATOM 1989 O MET A 284 16.990 38.879 -7.266 1.00 52.27 A O

ATOM 1990 N ASN A 285 18.056 39.948 -8.957 1.00 53.90 A N

ATOM 1991 CA ASN A 285 17.146 39.528 -10.028 1.00 55.70 A C

ATOM 1992 CB ASN A 285 16.023 40.561 -10.234 1.00 56.50 A C

ATOM 1993 CG ASN A 285 14.913 40.069 -11.168 1.00 57.30 A C

ATOM 1994 OD1 ASN A 285 14.139 40.871 -11.684 1.00 57.07 A O

ATOM 1995 ND2 ASN A 285 14.824 38.754 -11.371 1.00 57.03 A N

ATOM 1996 C ASN A 285 17.981 39.353 -11.310 1.00 56.48 A C

ATOM 1997 0 ASN A 285 18.445 40.340 -11.892 1.00 55.42 A O ATOM 1998 N PROA286 18.19738.089-11.748 1.0057.65 A N

ATOM 1999 CD PROA286 17.81636.855-11.022 1.0057.96 A C

ATOM 2000 CA PRO A 286 18.97937.756-12.950 1.0058.42 A C

ATOM 2001 CB PRO A 286 19.145 36.236-12.835 1.0059.11 A C

ATOM 2002 CG PRO A 286 17.913 35.801-12.083 1.0057.92 A C

ATOM 2003 C PRO A 286 18.431 38.176-14.326 1.0059.68 A C

ATOM 2004 O PRO A 286 19.21038.507-15.231 1.0059.11 A O

ATOM 2005 N ASN A 287 17.10638.182-14.474 1.0060.25 A N

ATOM 2006 CA ASN A 287 16.47838.551-15.744 1.0061.07 A C

ATOM 2007 CB ASN A 287 15.24037.674-16.017 1.0060.87 A C

ATOM 2008 CG ASN A 287 14.23937.681-14.871 1.0060.13 A C

ATOM 2009 OD1 ASN A 287 14.17936.735-14.080 1.0060.26 A O

ATOM 2010 ND2 ASN A 287 13.44238.744-14.784 1.0058.34 A N

ATOM 2011 C ASNA287 16.15540.041-15.898 1.0062.03 A C

ATOM 2012 O ASNA287 15.48540.438-16.860 1.0062.85 A O

ATOM 2013 N TYR A 288 16.65840.853-14.966 1.0062.57 A N

ATOM 2014 CA TYRA 288 16.44742.306-14.972 1.0064.13 A C

ATOM 2015 CB TYR A 288 16.32642.826-13.528 1.0061.79 A C

ATOM 2016 CG TYR A 288 15.78844.243-13.382 1.0060.32 A C

ATOM 2017 CDl TYRA 288 14.39444.490-13.332 1.0059.79 A C

ATOM 2018 CE1 TYR A 288 13.88745.817-13.192 1.0059.11 A C ATOM 2019 CD2 TYR A 288 16.66845.348-13290 1.0057.69 A C

ATOM 2020 CE2 TYR A 288 16.17746.669-13.154 1.0056.95 A C

ATOM 2021 CZ TYR A 288 14.79246.896-13.105 1.0058.96 A C

ATOM 2022 OH TYR A 288 14.32548.184-12.959 1.0059.81 A O

ATOM 2023 C TYRA288 17.59643.023-15.692 1.0065.78 A C

ATOM 2024 O TYR A 288 18.75342.601-15.601 1.0067.08 A O

ATOM 2025 N THRA289 17.261 44.122-16.371 1.0066.83 A N

ATOM 2026 CA THR A 289 18.22644.941-17.105 1.0069.81 A C

ATOM 2027 CB THR A 289 18.47644.395-18.562 1.0070.61 A C

ATOM 2028 OGl THR A 289 19.251 43.187-18.499 1.0070.37 A O

ATOM 2029 CG2 THR A 289 19.20945.423-19.451 1.0070.60 A C

ATOM 2030 C THRA289 17.73246.383-17.172 1.0071.26 A C

ATOM 2031 O THRA289 16.59046.645-17.569 1.0073.06 A O

ATOM 2032 N GLU A 290 18.62047.302-16.794 1.0071.55 A N

ATOM 2033 CA GLU A 290 18.36948.742-16.808 1.0072.31 A C

ATOM 2034 CB GLU A 290 17.51049.170-15.582 1.0070.96 A C

ATOM 2035 CG GLU A 290 18.00450.302-14.639 1.0071.20 A C

ATOM 2036 CD GLU A 290 18.64349.794-13.337 1.0070.18 A C

ATOM 2037 OEl GLU A 290 19.38048.786-13.366 1.0070.87 A O

ATOM 2038 OE2GLUA290 18.42050.416-12.278 1.0068.63 A O

ATOM 2039 C GLU A 290 19.72949.440-16.884 1.0074.42 A C ATOM 2040 O GLU A 290 19.98250.202-17.822 1.0075.10 A O

ATOM 2041 N PHE A 291 20.61249.105-15.933 1.0075.92 A N

ATOM 2042 CA PHE A 291 21.97749.649-15.797 1.0076.83 A C

ATOM 2043 CB PHE A 291 22.92748.997-16.825 1.0078.67 A C

ATOM 2044 CG PHE A 291 23.49547.661-16.385 1.0080.61 A C

ATOM 2045 CDl PHE A 291 24.82647.320-16.707 1.0081.40 A C

ATOM 2046 CD2 PHE A 291 22.71946.738-15.642 1.0081.26 A C

ATOM 2047 CE1 PHE A 291 25.38746.075-16.297 1.0081.96 A C

ATOM 2048 CE2PHEA291 23.261 45.489-15.222 1.0082.68 A C

ATOM 2049 CZ PHE A 291 24.60245.158-15.552 1.0082.53 A C

ATOM 2050 C PHE A 291 22.10851.184-15.781 1.0076.37 A C

ATOM 2051 O PHE A 291 23.13651.744-16.177 1.0076.51 A O

ATOM 2052 N LYS A 292 21.06751.849-15.278 1.0075.05 A N

ATOM 2053 CA LYSA292 21.041 53.305-15.195 1.0073.58 A C

ATOM 2054 CB LYS A 292 19.755 53.853-15.832 1.0074.80 A C

ATOM 2055 CG LYS A 292 19.92555.150-16.654 1.0075.02 A C

ATOM 2056 CD LYS A 292 19.561 56.439-15.895 1.0076.51 A C

ATOM 2057 CE LYS A 292 18.09856.468-15.435 1.0076.47 A C

ATOM 2058 NZ LYS A 292 17.77657.705-14.679 1.0075.94 A N

ATOM 2059 C LYS A 292 21.21653.777-13.748 1.0071.73 A C

ATOM 2060 O LYS A 292 22.133 53.309-13.060 1.0071.43 A O ATOM 2061 N PHE A 293 20.338 54.694 -13.305 1.00 69.00 A N

ATOM 2062 CA PHE A 293 20.325 55.346 -11.977 1.00 65.75 A C

ATOM 2063 CB PHE A 293 19.973 54.363 -10.837 1.00 66.67 A C

ATOM 2064 CG PHE A 293 19.050 54.948 -9.784 1.00 67.00 A C

ATOM 2065 CDl PHE A 293 17.655 54.814 -9.906 1.00 67.27 A C

ATOM 2066 CD2 PHE A 293 19.567 55.681 -8.694 1.00 67.07 A C

ATOM 2067 CE1 PHE A 293 16.775 55.409 -8.955 1.00 67.07 A C

ATOM 2068 CE2 PHE A 293 18.705 56.287 -7.736 1.00 66.86 A C

ATOM 2069 CZ PHE A 293 17.306 56.150 -7.868 1.00 66.82 A C

ATOM 2070 C PHE A 293 21.653 56.084 -11.711 1.00 62.49 A C

ATOM 2071 O PHE A 293 22.728 55.570 -12.056 1.00 62.02 A O

ATOM 2072 N PRO A 294 21.602 57.324 -11.163 1.00 59.76 A N

ATOM 2073 CD PRO A 294 20.457 58.244 -10.999 1.00 58.61 A C

ATOM 2074 CA PRO A 294 22.857 58.045 -10.899 1.00 57.77 A C

ATOM 2075 CB PRO A 294 22.364 59.394 -10.336 1.00 58.98 A C

ATOM 2076 CG PRO A 294 20.930 59.128 -9.897 1.00 57.12 A C

ATOM 2077 C PRO A 294 23.872 57.348 -9.970 1.00 55.35 A C

ATOM 2078 O PRO A 294 24.007 56.115 -9.965 1.00 53.70 A O

ATOM 2079 N GLN A 295 24.675 58.146 -9.286 1.00 53.74 A N

ATOM 2080 CA GLN A 295 25.640 57.594 -8.364 1.00 52.43 A C

ATOM 2081 CB GLN A 295 27.060 57.685 -8.892 1.00 54.44 A C ATOM 2082 CG GLN A 295 27.602 56.356 -9.358 1.00 55.11 A C

ATOM 2083 CD GLN A 295 28.004 55.451 -8.226 1.00 57.23 A C

ATOM 2084 OEl GLN A 295 27.348 54.443 -7.963 1.00 59.23 A O

ATOM 2085 NE2 GLN A 295 29.097 55.797 -7.552 1.00 58.58 A N

ATOM 2086 C GLN A 295 25.520 58.276 -7.048 1.00 50.54 A C

ATOM 2087 O GLN A 295 25.817 59.466 -6.904 1.00 50.04 A O

ATOM 2088 N ILE A 296 24.900 57.533 -6.143 1.00 49.44 A N

ATOM 2089 CA ILE A 296 24.686 57.958 -4.777 1.00 48.83 A C

ATOM 2090 CB ILE A 296 23.218 57.731 -4.329 1.00 45.74 A C

ATOM 2091 CG2 ILE A 296 22.995 58.279 -2.918 1.00 47.20 A C

ATOM 2092 CGI ILE A 296 22.225 58.346 -5.342 1.00 45.93 A C

ATOM 2093 CDl ILE A 296 22.358 59.862 -5.624 1.00 41.55 A C

ATOM 2094 C ILE A 296 25.632 57.060 -3.998 1.00 49.22 A C

ATOM 2095 O ILE A 296 25.631 55.830 -4.170 1.00 47.11 A O

ATOM 2096 N LYS A 297 26.522 57.695 -3243 1.00 50.72 A N

ATOM 2097 CA LYS A 297 27.481 56.957 -2.441 1.00 51.94 A C

ATOM 2098 CB LYS A 297 28.798 57.736 -2.310 1.00 53.90 A C

ATOM 2099 CG LYS A 297 30.031 56.871 -1.962 1.00 58.32 A C

ATOM 2100 CD LYS A 297 30274 55.681 -2.924 1.00 59.47 A C

ATOM 2101 CE LYS A 297 30.927 56.090 -4.251 1.00 61.75 A C

ATOM 2102 NZ LYS A 297 31.287 54.898 -5.086 1.00 60.74 A N ATOM 2103 C LYS A 297 26.874 56.610 -1.087 1.00 50.71 A C

ATOM 2104 O LYS A 297 25.990 57.315 -0.587 1.00 50.69 A O

ATOM 2105 N ALA A 298 27.304 55.471 -0.551 1.00 50.58 A N

ATOM 2106 CA ALA A 298 26.836 54.956 0.733 1.00 49.92 A C

ATOM 2107 CB ALA A 298 27.491 53.612 1.025 1.00 50.71 A C

ATOM 2108 C ALA A 298 27.092 55.913 1.882 1.00 49.11 A C

ATOM 2109 O ALA A 298 28.221 56.367 2.078 1.00 49.94 A O

ATOM 2110 N HIS A 299 26.015 56.281 2.571 1.00 48.23 A N

ATOM 2111 CA HIS A 299 26.075 57.167 3.731 1.00 48.83 A C

ATOM 2112 CB HIS A 299 24.661 57.662 4.062 1.00 49.57 A C

ATOM 2113 CG HIS A 299 24.605 58.751 5.092 1.00 52.29 A C

ATOM 2114 CD2 HIS A 299 25.170 59.981 5.127 1.00 52.86 A C

ATOM 2115 ND1 HIS A 299 23.822 58.659 6.224 1.00 53.30 A N

ATOM 2116 CE1 HIS A 299 23.901 59.786 6.907 1.00 52.43 A C

ATOM 2117 NE2 HIS A 299 24.714 60.604 6.264 1.00 54.26 A N

ATOM 2118 C HIS A 299 26.634 56.261 4.846 1.00 49.16 A C

ATOM 2119 O HIS A 299 26.001 55.249 5.181 1.00 49.39 A O

ATOM 2120 N PRO A 300 27.853 56.570 5.378 1.00 48.45 A N

ATOM 2121 CD PRO A 300 28.644 57.781 5.091 1.00 46.91 A C

ATOM 2122 CA PRO A 300 28.513 55.787 6.442 1.00 47.09 A C

ATOM 2123 CB PRO A 300 29.591 56.739 6.975 1.00 47.32 A C ATOM 2124 CG PRO A 300 29.201 58.098 6.429 1.00 48.24 A C

ATOM 2125 C PRO A 300 27.617 55.228 7.552 1.00 45.52 A C

ATOM 2126 O PRO A 300 26.694 55.897 8.043 1.00 43.48 A O

ATOM 2127 N TRP A 301 27.884 53.970 7.887 1.00 44.25 A N

ATOM 2128 CA TRP A 301 27.125 53.227 8.882 1.00 43.78 A C

ATOM 2129 CB TRP A 301 27.601 51.771 8.931 1.00 44.00 A C

ATOM 2130 CG TRP A 301 26.986 50.869 7.857 1.00 45.30 A C

ATOM 2131 CD2 TRP A 301 25.597 50.501 7.704 1.00 43.30 A C

ATOM 2132 CE2 TRP A 301 25.516 49.631 6.581 1.00 43.83 A C

ATOM 2133 CE3 TRP A 301 24.411 50.821 8.400 1.00 43.13 A C

ATOM 2134 CDl TRP A 301 27.660 50.226 6.848 1.00 46.40 A C

ATOM 2135 NE1 TRP A 301 26.785 49.482 6.083 1.00 45.93 A N

ATOM 2136 CZ2 TRP A 301 24.294 49.073 6.137 1.00 42.32 A C

ATOM 2137 CZ3 TRP A 301 23.182 50.263 7.954 1.00 42.11 A C

ATOM 2138 CH2 TRP A 301 23.143 49.400 6.831 1.00 40.59 A C

ATOM 2139 C TRP A 301 26.983 53.807 10.282 1.00 42.35 A C

ATOM 2140 O TRP A 301 26.010 53.512 10.982 1.00 40.29 A O

ATOM 2141 N THR A 302 27.915 54.681 10.652 1.00 41.74 A N

ATOM 2142 CA THR A 302 27.898 55.329 11.958 1.00 41.49 A C

ATOM 2143 CB THR A 302 29.319 55.526 12.493 1.00 41.53 A C

ATOM 2144 OG1 THR A 302 30.159 56.028 11.446 1.00 43.97 A O ATOM 2145 CG2 THR A 302 29.868 54.216 13.003 1.00 42.58 A C

ATOM 2146 C THR A 302 27.164 56.670 11.956 1.00 41.40 A C

ATOM 2147 O THR A 302 26.928 57.243 13.019 1.00 42.82 A O

ATOM 2148 N LYS A 303 26.805 57.161 10.769 1.00 41.27 A N

ATOM 2149 CA LYS A 303 26.099 58.434 10.633 1.00 42.22 A C

ATOM 2150 CB LYS A 303 26.660 59.253 9.465 1.00 45.05 A C

ATOM 2151 CG LYS A 303 28.076 59.800 9.668 1.00 48.74 A C

ATOM 2152 CD LYS A 303 28.142 60.875 10.747 1.00 52.10 A C

ATOM 2153 CE LYS A 303 29.509 61.539 10.793 1.00 53.01 A C

ATOM 2154 NZ LYS A 303 29.757 62.388 9.592 1.00 55.47 A N

ATOM 2155 C LYS A 303 24.583 58.283 10.500 1.00 42.12 A C

ATOM 2156 O LYS A 303 23.847 59.267 10.643 1.00 42.03 A O

ATOM 2157 N VAL A 304 24.124 57.063 10.211 1.00 40.30 A N

ATOM 2158 CA VAL A 304 22.688 56.777 10.094 1.00 40.53 A C

ATOM 2159 CB VAL A 304 22.386 55.544 9.151 1.00 40.77 A C

ATOM 2160 CGI VAL A 304 23.278 54.379 9.456 1.00 40.85 A C

ATOM 2161 CG2 VAL A 304 20.924 55.113 9.227 1.00 41.70 A C

ATOM 2162 C VAL A 304 22.113 56.602 11.503 1.00 40.90 A C

ATOM 2163 O VAL A 304 20.996 57.042 11.789 1.00 42.47 A O

ATOM 2164 N PHE A 305 22.909 56.005 12.385 1.00 39.77 A N

ATOM 2165 CA PHE A 305 22.510 55.797 13.769 1.00 38.03 A C ATOM 2166 CB PHE A 305 22.950 54.418 14260 1.00 35.95 A C

ATOM 2167 CG PHE A 305 22.404 53.279 13.449 1.00 32.65 A C

ATOM 2168 CDl PHE A 305 21.036 52.959 13.491 1.00 3320 A C

ATOM 2169 CD2 PHE A 305 23.251 52.528 12.618 1.00 32.70 A C

ATOM 2170 CE1 PHE A 305 20.507 51.903 12.710 1.00 30.62 A C

ATOM 2171 CE2 PHE A 305 22.744 51.464 11.826 1.00 31.75 A C

ATOM 2172 CZ PHE A 305 21.363 51.154 11.874 1.00 32.22 A C

ATOM 2173 C PHE A 305 23.139 56.884 14.625 1.00 39.55 A C

ATOM 2174 0 PHE A 305 24.211 57.397 14.299 1.00 39.69 A O

ATOM 2175 N ARG A 306 22.468 57.219 15.727 1.00 41.25 A N

ATOM 2176 CA ARG A 306 22.910 58.248 16.671 1.00 43.59 A C

ATOM 2177 CB ARG A 306 21.818 58.430 17.745 1.00 43.64 A C

ATOM 2178 CG ARG A 306 21.524 57.196 18.597 1.00 44.87 A C

ATOM 2179 CD ARG A 306 20.314 57.378 19.515 1.00 47.95 A C

ATOM 2180 NE ARG A 306 20.130 56.224 20.405 1.00 48.19 A N

ATOM 2181 CZ ARG A 306 20.553 56.166 21.670 1.00 48.40 A C

ATOM 2182 NHl ARG A 306 21.188 57.195 22.215 1.00 48.42 A N

ATOM 2183 NH2 ARG A 306 20.364 55.068 22.388 1.00 45.82 A N

ATOM 2184 C ARG A 306 24.267 57.880 17.316 1.00 45.34 A C

ATOM 2185 O ARG A 306 24.664 56.714 17.271 1.00 44.67 A O

ATOM 2186 N PRO A 307 25.041 58.869 17.834 1.00 47.15 A N ATOM 2187 CD PRO A 307 24.982 60.343 17.754 1.00 47.97 A C

ATOM 2188 CA PRO A 307 26.311 58.446 18.446 1.00 48.12 A C

ATOM 2189 CB PRO A 307 27.026 59.775 18.731 1.00 48.01 A C

ATOM 2190 CG PRO A 307 25.908 60.757 18.876 1.00 48.71 A C

ATOM 2191 C PRO A 307 26.040 57.645 19.721 1.00 48.30 A C

ATOM 2192 O PRO A 307 24.901 57.596 20.203 1.00 50.01 A O

ATOM 2193 N ARG A 308 27.072 56.978 20.229 1.00 48.83 A N

ATOM 2194 CA ARG A 308 26.985 56.139 21.433 1.00 49.80 A C

ATOM 2195 CB ARG A 308 26.571 56.953 22.687 1.00 52.05 A C

ATOM 2196 CG ARG A 308 27.509 58.147 23.019 1.00 54.22 A C

ATOM 2197 CD ARG A 308 28.764 57.762 23.806 1.00 57.43 A C

ATOM 2198 NE ARG A 308 28.612 57.968 25.252 1.00 59.09 A N

ATOM 2199 CZ ARG A 308 29.448 58.678 26.015 1.00 60.62 A C

ATOM 2200 NHl ARG A 308 30.516 59.266 25.484 1.00 61.71 A N

ATOM 2201 NH2 ARG A 308 29.215 58.809 27.319 1.00 60.15 A N

ATOM 2202 C ARG A 308 26.140 54.855 21.234 1.00 48.81 A C

ATOM 2203 O ARG A 308 25.914 54.095 22.177 1.00 48.97 A O

ATOM 2204 N THR A 309 25.715 54.615 19.984 1.00 46.95 A N

ATOM 2205 CA THR A 309 24.971 53.406 19.579 1.00 43.38 A C

ATOM 2206 CB THR A 309 24.320 53.564 18.141 1.00 42.89 A C

ATOM 2207 OGl THR A 309 23.233 54.491 18.199 1.00 41.63 A O ATOM 2208 CG2 THR A 309 23.785 52.231 17.587 1.00 41.95 A C

ATOM 2209 C THR A 309 26.071 52.333 19.515 1.00 40.81 A C

ATOM 2210 O THR A 309 27.112 52.572 18.896 1.00 41.04 A O

ATOM 2211 N PRO A 310 25.878 51.167 20.181 1.00 39.14 A N

ATOM 2212 CD PRO A 310 24.769 50.805 21.087 1.00 38.13 A C

ATOM 2213 CA PRO A 310 26.881 50.090 20.175 1.00 37.91 A C

ATOM 2214 CB PRO A 310 26.142 48.939 20.851 1.00 35.79 A C

ATOM 2215 CG PRO A 310 25.349 49.636 21.859 1.00 37.87 A C

ATOM 2216 C PRO A 310 27.436 49.690 18.799 1.00 37.77 A C

ATOM 2217 0 PRO A 310 26.664 49.418 17.868 1.00 35.62 A O

ATOM 2218 N PRO A 311 28.786 49.730 18.637 1.00 37.56 A N

ATOM 2219 CD PRO A 311 29.756 50.273 19.614 1.00 36.69 A C

ATOM 2220 CA PRO A 311 29.482 49.376 17.389 1.00 35.84 A C

ATOM 2221 CB PRO A 311 30.951 49.447 17.799 1.00 35.19 A C

ATOM 2222 CG PRO A 311 30.960 50.577 18.749 1.00 36.48 A C

ATOM 2223 C PRO A 311 29.115 47.986 16.851 1.00 34.34 A C

ATOM 2224 O PRO A 311 29.062 47.764 15.636 1.00 34.96 A O

ATOM 2225 N GLU A 312 28.795 47.081 17.768 1.00 33.05 A N

ATOM 2226 CA GLU A 312 28.411 45.716 17.425 1.00 32.11 A C

ATOM 2227 CB GLU A 312 28.514 44.811 18.654 1.00 34.52 A C

ATOM 2228 CG GLU A 312 29.641 45.161 19.630 1.00 37.63 A C ATOM 2229 CD GLU A 312 29.151 45.985 20.827 1.00 42.08 A C

ATOM 2230 OEl GLU A 312 28.191 45.537 21.505 1.00 43.26 A O

ATOM 2231 OE2 GLU A 312 29.732 47.067 21.098 1.00 40.84 A O

ATOM 2232 C GLU A 312 26.989 45.670 16.844 1.00 29.46 A C

ATOM 2233 O GLU A 312 26.666 44.778 16.073 1.00 28.20 A O

ATOM 2234 N ALA A 313 26.164 46.664 17.186 1.00 29.26 A N

ATOM 2235 CA ALA A 313 24.776 46.761 16.692 1.00 28.36 A C

ATOM 2236 CB ALA A 313 23.986 47.756 17.538 1.00 26.03 A C

ATOM 2237 C ALA A 313 24.761 47.186 15.225 1.00 27.13 A C

ATOM 2238 O ALA A 313 24.043 46.613 14.395 1.00 27.48 A O

ATOM 2239 N ILE A 314 25.616 48.161 14.930 1.00 24.41 A N

ATOM 2240 CA ILE A 314 25.802 48.717 13.606 1.00 2322 A C

ATOM 2241 CB ILE A 314 26.745 49.947 13.665 1.00 22.88 A C

ATOM 2242 CG2 ILE A 314 26.912 50.547 12.295 1.00 20.78 A C

ATOM 2243 CGI ILE A 314 26.178 50.998 14.621 1.00 20.70 A C

ATOM 2244 CDl ILE A 314 27.172 52.058 15.035 1.00 25.96 A C

ATOM 2245 C ILE A 314 26.397 47.639 12.703 1.00 22.09 A C

ATOM 2246 O ILE A 314 25.922 47.440 11.582 1.00 22.62 A O

ATOM 2247 N ALA A 315 27.388 46.914 13.228 1.00 22.17 A N

ATOM 2248 CA ALA A 315 28.069 45.837 12.496 1.00 21.80 A C

ATOM 2249 CB ALA A 315 29.246 45.294 13.303 1.00 23.07 A C ATOM 2250 C ALA A 315 27.097 44.716 12.142 1.00 21.81 A C

ATOM 2251 O ALA A 315 27.113 44.205 11.015 1.00 21.35 A O

ATOM 2252 N LEU A 316 26.202 44.381 13.079 1.00 23.17 A N

ATOM 2253 CA LEU A 316 25.196 43.355 12.807 1.00 23.10 A C

ATOM 2254 CB LEU A 316 24.378 42.999 14.046 1.00 20.49 A C

ATOM 2255 CG LEU A 316 23.225 41.994 13.839 1.00 18.83 A C

ATOM 2256 CD1 LEU A 316 23.696 40.642 13.326 1.00 20.59 A C

ATOM 2257 CD2 LEU A 316 22.457 41.835 15.104 1.00 17.79 A C

ATOM 2258 C LEU A 316 24.280 43.851 11.697 1.00 24.38 A C

ATOM 2259 O LEU A 316 24.041 43.130 10.735 1.00 25.32 A O

ATOM 2260 N CYS A 317 23.892 45.122 11.775 1.00 25.36 A N

ATOM 2261 CA CYS A 317 23.016 45.705 10.778 1.00 28.75 A C

ATOM 2262 CB CYS A 317 22.626 47.116 11.179 1.00 31.11 A C

ATOM 2263 SG CYS A 317 21.332 47.759 10.160 1.00 33.71 A S

ATOM 2264 C CYS A 317 23.623 45.692 9.379 1.00 29.89 A C

ATOM 2265 O CYS A 317 22.940 45.339 8.412 1.00 29.61 A O

ATOM 2266 N SER A 318 24.927 45.966 9.295 1.00 30.12 A N

ATOM 2267 CA SER A 318 25.633 45.972 8.014 1.00 31.04 A C

ATOM 2268 CB SER A 318 27.062 46.515 8.171 1.00 32.40 A C

ATOM 2269 OG SER A 318 27.894 45.646 8.916 1.00 37.10 A O

ATOM 2270 C SER A 318 25.640 44.598 7.338 1.00 30.58 A C ATOM 2271 O SER A 318 25.556 44.502 6.113 1.00 32.71 A O

ATOM 2272 N ARG A 319 25.682 43.544 8.146 1.00 29.61 A N

ATOM 2273 CA ARG A 319 25.668 42.187 7.628 1.00 30.36 A C

ATOM 2274 CB ARG A 319 26.593 41.292 8.451 1.00 34.56 A C

ATOM 2275 CG ARG A 319 28.096 41.484 8.179 1.00 40.63 A C

ATOM 2276 CD ARG A 319 28.568 40.843 6.858 1.00 47.97 A C

ATOM 2277 NE ARG A 319 28.184 41.600 5.661 1.00 53.18 A N

ATOM 2278 CZ ARG A 319 28.445 41.240 4.402 1.00 57.45 A C

ATOM 2279 NHl ARG A 319 29.106 40.117 4.129 1.00 59.71 A N

ATOM 2280 NH2 ARG A 319 28.033 42.010 3.402 1.00 59.71 A N

ATOM 2281 C ARG A 319 24.260 41.590 7.478 1.00 29.92 A C

ATOM 2282 O ARG A 319 24.098 40.384 7.263 1.00 28.71 A O

ATOM 2283 N LEU A 320 23.246 42.456 7.566 1.00 30.59 A N

ATOM 2284 CA LEU A 320 21.838 42.071 7.407 1.00 28.72 A C

ATOM 2285 CB LEU A 320 21.028 42.381 8.660 1.00 29.26 A C

ATOM 2286 CG LEU A 320 21.327 41.635 9.957 1.00 31.05 A C

ATOM 2287 CD1 LEU A 320 20.504 42.219 11.072 1.00 32.16 A C

ATOM 2288 CD2 LEU A 320 21.092 40.149 9.815 1.00 31.46 A C

ATOM 2289 C LEU A 320 21.258 42.870 6.270 1.00 28.07 A C

ATOM 2290 O LEU A 320 20.582 42.329 5.388 1.00 28.47 A O

ATOM 2291 N LEU A 321 21.529 44.173 6.309 1.00 27.98 A N ATOM 2292 CA LEU A 321 21.046 45.098 5.299 1.00 26.38 A C

ATOM 2293 CB LEU A 321 20.654 46.459 5.914 1.00 21.14 A C

ATOM 2294 CG LEU A 321 19.485 46.516 6.917 1.00 17.19 A C

ATOM 2295 CDl LEU A 321 19.185 47.942 7.328 1.00 10.82 A C

ATOM 2296 CD2 LEU A 321 18.235 45.906 6.324 1.00 18.88 A C

ATOM 2297 C LEU A 321 21.989 45.254 4.111 1.00 27.46 A C

ATOM 2298 O LEU A 321 22.505 46.338 3.834 1.00 28.05 A O

ATOM 2299 N GLU A 322 22.205 44.143 3.418 1.00 28.61 A N

ATOM 2300 CA GLU A 322 23.034 44.127 2225 1.00 31.24 A C

ATOM 2301 CB GLU A 322 24.266 43.216 2.389 1.00 34.15 A C

ATOM 2302 CG GLU A 322 25.607 43.843 1.922 1.00 39.62 A C

ATOM 2303 CD GLU A 322 25.616 44.289 0.445 1.00 44.43 A C

ATOM 2304 OEl GLU A 322 25.363 45.492 0.162 1.00 43.55 A O

ATOM 2305 OE2 GLU A 322 25.854 43.425 -0.431 1.00 46.30 A O

ATOM 2306 C GLU A 322 - 22.186 43.657 1.043 1.00 31.28 A C

ATOM 2307 O GLU A 322 21.335 42.763 1.181 1.00 31.25 A O

ATOM 2308 N TYR A 323 22.462 44.253 -0.120 1.00 30.59 A N

ATOM 2309 CA TYR A 323 21.788 43.957 -1.383 1.00 27.98 A C

ATOM 2310 CB TYR A 323 22.389 44.796 -2.503 1.00 26.77 A C

ATOM 2311 CG TYR A 323 21.913 46.227 -2.543 1.00 26.75 A C

ATOM 2312 CDl TYR A 323 20.546 46.526 -2.710 1.00 2723 A C ATOM 2313 CE1 TYR A 323 20.087 47.864 -2.786 1.00 26.14 A C

ATOM 2314 CD2 TYR A 323 22.824 47.299 -2.450 1.00 25.50 A C

ATOM 2315 CE2 TYR A 323 22.376 48.641 -2.526 1.00 27.00 A C

ATOM 2316 CZ TYR A 323 21.001 48.908 -2.692 1.00 24.56 A C

ATOM 2317 OH TYR A 323 20.540 50.197 -2.756 1.00 24.65 A O

ATOM 2318 C TYR A 323 21.863 42.499 -1.771 1.00 28.42 A C

ATOM 2319 O TYR A 323 20.830 41.878 -1.990 1.00 29.46 A O

ATOM 2320 N THR A 324 23.091 41.965 -1.809 1.00 28.83 A N

ATOM 2321 CA THR A 324 23.395 40.568 -2.154 1.00 29.36 A C

ATOM 2322 CB THR A 324 24.955 40.361 -2202 1.00 31.12 A C

ATOM 2323 OG1 THR A 324 25.536 41.304 -3.110 1.00 3426 A O

ATOM 2324 CG2 THR A 324 25.342 38.942 -2.638 1.00 29.15 A C

ATOM 2325 C THR A 324 22.744 39.649 -1.103 1.00 27.97 A C

ATOM 2326 O THR A 324 23.127 39.686 0.059 1.00 30.82 A O

ATOM 2327 N PRO A 325 21.735 38.843 -1.497 1.00 27.81 A N

ATOM 2328 CD PRO A 325 21.209 38.737 -2.871 1.00 28.41 A C

ATOM 2329 CA PRO A 325 21.006 37.919 -0.604 1.00 27.26 A C

ATOM 2330 CB PRO A 325 20.017 37.230 -1.547 1.00 27.65 A C

ATOM 2331 CG PRO A 325 19.822 38212 -2.634 1.00 28.72 A C

ATOM 2332 C PRO A 325 21.847 36.886 0.145 1.00 27.99 A C

ATOM 2333 O PRO A 325 21.712 36.735 1.369 1.00 25.28 A O ATOM 2334 N THR A 326 22.738 36.218 -0.594 1.00 2822 A N

ATOM 2335 CA THR A 326 23.638 35.194 -0.046 1.00 28.20 A C

ATOM 2336 CB THR A 326 24.268 34.315 -1.173 1.00 29.04 A C

ATOM 2337 OG1 THR A 326 25.096 35.127 -2.017 1.00 28.94 A O

ATOM 2338 CG2 THR A 326 23.175 33.633 -2.026 1.00 26.65 A C

ATOM 2339 C THR A 326 24.757 35.772 0.845 1.00 27.68 A C

ATOM 2340 O THR A 326 25.501 35.009 1.489 1.00 26.85 A O

ATOM 2341 N ALA A 327 24.874 37.106 0.872 1.00 25.97 A N

ATOM 2342 CA ALA A 327 25.875 37.789 1.708 1.00 26.96 A C

ATOM 2343 CB ALA A 327 26.389 39.067 1.051 1.00 25.07 A C

ATOM 2344 C ALA A 327 25.312 38.107 3.089 1.00 27.09 A C

ATOM 2345 O ALA A 327 26.065 38.417 4.020 1.00 24.79 A O

ATOM 2346 N ARG A 328 23.980 38.060 3.201 1.00 28.34 A N

ATOM 2347 CA ARG A 328 23.292 38.318 4.465 1.00 26.61 A C

ATOM 2348 CB ARG A 328 21.799 38.547 4256 1.00 25.56 A C

ATOM 2349 CG ARG A 328 21.450 39.765 3.444 1.00 25.90 A C

ATOM 2350 CD ARG A 328 19.961 39.810 3.199 1.00 22.23 A C

ATOM 2351 NE ARG A 328 19.673 40.511 1.957 1.00 22.11 A N

ATOM 2352 CZ ARG A 328 18.578 40.353 1.227 1.00 22.06 A C

ATOM 2353 NHl ARG A 328 17.620 39.518 1.596 1.00 24.48 A N

ATOM 2354 NH2 ARG A 328 18.477 40.987 0.077 1.00 23.49 A N ATOM 2355 C ARG A 328 23.470 37.102 5.337 1.00 25.96 A C

ATOM 2356 O ARG A 328 23.532 35.979 4.839 1.00 27.07 A O

ATOM 2357 N LEU A 329 23.553 37.342 6.639 1.00 27.31 A N

ATOM 2358 CA LEU A 329 23.718 36.291 7.631 1.00 25.55 A C

ATOM 2359 CB LEU A 329 23.948 36.904 9.012 1.00 25.84 A C

ATOM 2360 CG LEU A 329 25.215 37.715 9.232 1.00 26.07 A C

ATOM 2361 CD1 LEU A 329 25.229 38269 10.639 1.00 25.95 A C

ATOM 2362 CD2 LEU A 329 26.437 36.861 8.998 1.00 26.33 A C

ATOM 2363 C LEU A 329 22.472 35.449 7.705 1.00 2521 A C

ATOM 2364 O LEU A 329 21.376 35.937 7.454 1.00 25.29 A O

ATOM 2365 N THR A 330 22.648 34.172 8.030 1.00 26.30 A N

ATOM 2366 CA THR A 330 21.518 33.267 8.190 1.00 23.67 A C

ATOM 2367 CB THR A 330 21.945 31.767 8.133 1.00 24.57 A C

ATOM 2368 OGl THR A 330 22.516 31.375 9.394 1.00 2526 A O

ATOM 2369 CG2 THR A 330 22.907 31.509 6.977 1.00 23.23 A C

ATOM 2370 C THR A 330 21.052 33.599 9.609 1.00 23.65 A C

ATOM 2371 O THR A 330 21.816 34201 10.382 1.00 23.44 A O

ATOM 2372 N PRO A 331 19.791 33.268 9.959 1.00 24.00 A N

ATOM 2373 CD PRO A 331 18.669 32.781 9.123 1.00 21.51 A C

ATOM 2374 CA PRO A 331 19.312 33.561 11.313 1.00 23.30 A C

ATOM 2375 CB PRO A 331 17.970 32.867 11.329 1.00 23.67 A C ATOM 2376 CG PRO A 331 17.494 33.048 9.969 1.00 22.76 A C

ATOM 2377 C PRO A 331 20.218 33.054 12.437 1.00 23.42 A C

ATOM 2378 O PRO A 331 20.474 33.785 13.393 1.00 2523 A O

ATOM 2379 N LEU A 332 20.768 31.847 12.265 1.00 25.53 A N

ATOM 2380 CA LEU A 332 21.672 31.228 13.247 1.00 25.04 A C

ATOM 2381 CB LEU A 332 21.950 29.759 12.915 1.00 25.54 A C

ATOM 2382 CG LEU A 332 21.263 28.576 13.616 1.00 27.38 A C

ATOM 2383 CDl LEU A 332 22.299 27.453 13.749 1.00 24.16 A C

ATOM 2384 CD2 LEU A 332 20.722 28.921 15.003 1.00 25.32 A C

ATOM 2385 C LEU A 332 22.999 31.955 13.355 1.00 24.53 A C

ATOM 2386 0 LEU A 332 23.546 32.100 14.442 1.00 25.49 A O

ATOM 2387 N GLU A 333 23.498 32.429 12.224 1.00 26.96 A N

ATOM 2388 CA GLU A 333 24.761 33.164 12.182 1.00 32.56 A C

ATOM 2389 CB GLU A 333 25.208 33.374 10.729 1.00 33.46 A C

ATOM 2390 CG GLU A 333 25.584 32.083 10.017 1.00 35.64 A C

ATOM 2391 CD GLU A 333 26.067 32.299 8.596 1.00 39.68 A C

ATOM 2392 OEl GLU A 333 27.008 31.585 8.183 1.00 40.69 A O

ATOM 2393 OE2 GLU A 333 25.503 33.163 7.885 1.00 40.82 A O

ATOM 2394 C GLU A 333 24.561 34.497 12.887 1.00 33.10 A C

ATOM 2395 O GLU A 333 25.413 34.948 13.663 1.00 33.77 A O

ATOM 2396 N ALA A 334 23.366 35.053 12.679 1.00 34.71 A N ATOM 2397 CA ALA A 334 22.945 36.318 13.272 1.00 32.79 A C

ATOM 2398 CB ALA A 334 21.638 36.737 12.686 1.00 33.12 A C

ATOM 2399 C ALA A 334 22.846 36.167 14.785 1.00 31.49 A C

ATOM 2400 O ALA A 334 23.345 37.008 15.512 1.00 31.13 A O

ATOM 2401 N CYS A 335 22.289 35.043 15.240 1.00 30.01 A N

ATOM 2402 CA CYS A 335 22.170 34.724 16.668 1.00 28.69 A C

ATOM 2403 CB CYS A 335 21.452 33.393 16.843 1.00 28.08 A C

ATOM 2404 SG CYS A 335 19.687 33.454 17.012 1.00 3120 A S

ATOM 2405 C CYS A 335 23.558 34.598 17.311 1.00 28.97 A C

ATOM 2406 O CYS A 335 23.758 34.976 18.467 1.00 27.56 A O

ATOM 2407 N ALA A 336 24.515 34.120 16.512 1.00 28.87 A N

ATOM 2408 CA ALA A 336 25.891 33.904 16.947 1.00 28.10 A C

ATOM 2409 CB ALA A 336 26.514 32.780 16.138 1.00 2821 A C

ATOM 2410 C ALA A 336 26.778 35.140 16.907 1.00 28.39 A C

ATOM 2411 O ALA A 336 27.938 35.079 17.321 1.00 29.86 A O

ATOM 2412 N HIS A 337 26.220 36.258 16.437 1.00 27.79 A N

ATOM 2413 CA HIS A 337 26.929 37.538 16.340 1.00 25.93 A C

ATOM 2414 CB HIS A 337 26.058 38.559 15.585 1.00 26.12 A C

ATOM 2415 CG HIS A 337 26.749 39.855 15.280 1.00 27.57 A C

ATOM 2416 CD2 HIS A 337 27.314 40.314 14.138 1.00 24.19 A C

ATOM 2417 ND1 HIS A 337 26.974 40.823 16.237 1.00 25.30 A N ATOM 2418 CE1 HIS A 337 27.656 41.818 15.701 1.00 23.12 A C

ATOM 2419 NE2 HIS A 337 27.872 41.535 14.428 1.00 26.35 A N

ATOM 2420 C HIS A 337 27.303 38.071 17.731 1.00 27.28 A C

ATOM 2421 O HIS A 337 26.595 37.822 18.719 1.00 26.23 A O

ATOM 2422 N SER A 338 28.391 38.847 17.773 1.00 27.62 A N

ATOM 2423 CA SER A 338 28.917 39.429 19.007 1.00 27.81 A C

ATOM 2424 CB SER A 338 30.314 40.014 18.782 1.00 27.03 A C

ATOM 2425 OG SER A 338 30.265 41.231 18.059 1.00 32.03 A O

ATOM 2426 C SER A 338 28.020 40.456 19.694 1.00 27.51 A C

ATOM 2427 O SER A 338 28.282 40.841 20.844 1.00 29.60 A O

ATOM 2428 N PHE A 339 26.973 40.900 18.997 1.00 23.94 A N

ATOM 2429 CA PHE A 339 26.024 41.860 19.562 1.00 23.11 A C

ATOM 2430 CB PHE A 339 25.100 42.416 18.467 1.00 22.52 A C

ATOM 2431 CG PHE A 339 24.016 43.347 18.970 1.00 19.21 A C

ATOM 2432 CDl PHE A 339 22.666 43.075 18.675 1.00 17.00 A C

ATOM 2433 CD2 PHE A 339 24.343 44.524 19.696 1.00 17.34 A C

ATOM 2434 CE1 PHE A 339 21.635 43.966 19.082 1.00 16.11 A C

ATOM 2435 CE2 PHE A 339 23.341 45.427 20.117 1.00 13.86 A C

ATOM 2436 CZ PHE A 339 21.977 45.155 19.806 1.00 18.48 A C

ATOM 2437 C PHE A 339 25.196 41.186 20.656 1.00 22.18 A C

ATOM 2438 O PHE A 339 24.739 41.844 21.570 1.00 22.78 A O ATOM 2439 N PHE A 340 25.048 39.872 20.567 1.00 22.67 A N

ATOM 2440 CA PHE A 340 24.276 39.123 21.546 1.00 23.49 A C

ATOM 2441 CB PHE A 340 23.452 38.051 20.838 1.00 21.00 A C

ATOM 2442 CG PHE A 340 22.544 38.597 19.787 1.00 22.12 A C

ATOM 2443 CDl PHE A 340 21.371 39.297 20.141 1.00 19.33 A C

ATOM 2444 CD2 PHE A 340 22.856 38.438 18.423 1.00 22.58 A C

ATOM 2445 CE1 PHE A 340 20.513 39.835 19.146 1.00 13.87 A C

ATOM 2446 CE2 PHE A 340 21.998 38.974 17.416 1.00 19.37 A C

ATOM 2447 CZ PHE A 340 20.826 39.672 17.788 1.00 17.95 A C

ATOM 2448 C PHE A 340 25.107 38.502 22.665 1.00 24.37 A C

ATOM 2449 O PHE A 340 24.596 37.659 23.407 1.00 23.70 A O

ATOM 2450 N ASP A 341 26.362 38.950 22.819 1.00 25.46 A N

ATOM 2451 CA ASP A 341 27.266 38.410 23.855 1.00 25.43 A C

ATOM 2452 CB ASP A 341 28.716 38.883 23.661 1.00 24.12 A C

ATOM 2453 CG ASP A 341 29.452 38.104 22.573 1.00 21.89 A C

ATOM 2454 OD1 ASP A 341 29.045 36.972 22.243 1.00 19.83 A O

ATOM 2455 OD2 ASP A 341 30.439 38.636 22.027 1.00 21.39 A O

ATOM 2456 C ASP A 341 26.824 38.626 25.293 1.00 26.72 A C

ATOM 2457 O ASP A 341 27.002 37.737 26.125 1.00 27.88 A O

ATOM 2458 N GLU A 342 26.165 39.761 25.553 1.00 28.64 A N

ATOM 2459 CA GLU A 342 25.638 40.103 26.883 1.00 29.30 A C ATOM 2460 CB GLU A 342 24.992 41.496 26.863 1.00 30.64 A C

ATOM 2461 CG GLU A 342 24.751 42.102 28.252 1.00 31.79 A C

ATOM 2462 CD GLU A 342 24.045 43.456 28.247 1.00 33.12 A C

ATOM 2463 OEl GLU A 342 23.962 44.133 27.189 1.00 32.04 A O

ATOM 2464 OE2 GLU A 342 23.568 43.846 29.337 1.00 35.06 A O

ATOM 2465 C GLU A 342 24.596 39.056 27.322 1.00 29.07 A C

ATOM 2466 O GLU A 342 24.503 38.713 28.503 1.00 29.80 A O

ATOM 2467 N LEU A 343 23.880 38.505 26.342 1.00 28.35 A N

ATOM 2468 CA LEU A 343 22.853 37.488 26.577 1.00 28.37 A C

ATOM 2469 CB LEU A 343 21.985 37.338 25.333 1.00 26.38 A C

ATOM 2470 CG LEU A 343 20.724 38.175 25.137 1.00 24.83 A C

ATOM 2471 CDl LEU A 343 20.800 39.562 25.751 1.00 23.95 A C

ATOM 2472 CD2 LEU A 343 20.438 38.221 23.658 1.00 23.33 A C

ATOM 2473 C LEU A 343 23.417 36.129 26.969 1.00 28.43 A C

ATOM 2474 O LEU A 343 22.717 35.314 27.560 1.00 28.03 A O

ATOM 2475 N ARG A 344 24.690 35.912 26.652 1.00 30.54 A N

ATOM 2476 CA ARG A 344 25.384 34.660 26.956 1.00 33.48 A C

ATOM 2477 CB ARG A 344 26.256 34.252 25.768 1.00 31.55 A C

ATOM 2478 CG ARG A 344 25.459 33.677 24.613 1.00 29.17 A C

ATOM 2479 CD ARG A 344 26.330 33.406 23.412 1.00 28.28 A C

ATOM 2480 NE ARG A 344 26.735 34.634 22.729 1.00 28.30 A N ATOM 2481 CZ ARG A 344 26.197 35.069 21.590 1.00 28.60 A C

ATOM 2482 NHl ARG A 344 25.230 34.377 20.996 1.00 26.79 A N

ATOM 2483 NH2 ARG A 344 26.604 36.213 21.055 1.00 27.56 A N

ATOM 2484 C ARG A 344 26.203 34.717 28.257 1.00 35.95 A C

ATOM 2485 O ARG A 344 26.701 33.690 28.739 1.00 36.48 A O

ATOM 2486 N ASP A 345 26.288 35.918 28.835 1.00 38.09 A N

ATOM 2487 CA ASP A 345 27.001 36.183 30.090 1.00 40.69 A C

ATOM 2488 CB ASP A 345 27.062 37.708 30.298 1.00 43.13 A C

ATOM 2489 CG ASP A 345 27.959 38.128 31.455 1.00 45.65 A C

ATOM 2490 OD1 ASP A 345 27.655 37.778 32.615 1.00 48.79 A O

ATOM 2491 OD2 ASP A 345 28.950 38.849 31.207 1.00 48.78 A O

ATOM _. 2492 C ASP A 345 26.207 35.504 31.231 1.00 40.75 A C

ATOM 2493 O ASP A 345 24.985 35.602 31261 1.00 41.05 A O

ATOM 2494 N PRO A 346 26.888 34.801 32.169 1.00 40.50 A N

ATOM 2495 CD PRO A 346 28.337 34.519 32.240 1.00 40.27 A C

ATOM 2496 CA PRO A 346 26.184 34.132 33.277 1.00 39.85 A C

ATOM 2497 CB PRO A 346 27.320 33.479 34.061 1.00 39.63 A C

ATOM 2498 CG PRO A 346 28.379 33.268 33.054 1.00 40.55 A C

ATOM 2499 C PRO A 346 25.392 35.069 34.197 1.00 40.57 A C

ATOM 2500 O PRO A 346 24.360 34.675 34.755 1.00 39.40 A O

ATOM 2501 N ASN A 347 25.858 36.315 34.302 1.00 41.45 A N ATOM 2502 CA ASN A 347 25.246 37.328 35.169 1.00 43.97 A C

ATOM 2503 CB ASN A 347 26.359 38.102 35.907 1.00 45.59 A C

ATOM 2504 CG ASN A 347 27.424 37.181 36.507 1.00 47.23 A C

ATOM 2505 OD1 ASN A 347 28.618 37.338 36.235 1.00 47.48 A O

ATOM 2506 ND2 ASN A 347 26.989 36.193 37.291 1.00 46.71 A N

ATOM 2507 C ASN A 347 24.313 38.289 34.408 1.00 44.21 A C

ATOM 2508 O ASN A 347 24.292 39.500 34.670 1.00 44.66 A O

ATOM 2509 N VAL A 348 23.522 37.711 33.499 1.00 43.66 A N

ATOM 2510 CA VAL A 348 22.560 38.402 32.628 1.00 42.37 A C

ATOM 2511 CB VAL A 348 21.701 37.382 31.835 1.00 44.63 A C

ATOM 2512 CGI VAL A 348 22.387 36.978 30.564 1.00 44.29 A C

ATOM 2513 CG2 VAL A 348 21.326 36.157 32.704 1.00 45.37 A C

ATOM 2514 C VAL A 348 21.606 39.450 33.230 1.00 41.89 A C

ATOM 2515 O VAL A 348 21.909 40.647 33.224 1.00 43.60 A O

ATOM 2516 N LYS A 349 20.455 38.980 33.723 1.00 40.05 A N

ATOM 2517 CA LYS A 349 19.376 39.769 34.340 1.00 39.12 A C

ATOM 2518 CB LYS A 349 19.777 40.327 35.716 1.00 39.09 A C

ATOM 2519 CG LYS A 349 20.201 39.288 36.747 1.00 42.20 A C

ATOM 2520 CD LYS A 349 19.148 38.221 36.998 1.00 43.56 A C

ATOM 2521 CE LYS A 349 19.675 37.187 37.976 1.00 45.21 A C

ATOM 2522 NZ LYS A 349 18.720 36.067 38.160 1.00 48.86 A N ATOM 2523 C LYS A 349 18.682 40.863 33.533 1.00 38.10 A C

ATOM 2524 O LYS A 349 19.314 41.738 32.927 1.00 37.45 A O

ATOM 2525 N LEU A 350 17.353 40.809 33.569 1.00 36.56 A N

ATOM 2526 CA LEU A 350 16.510 41.798 32.910 1.00 34.72 A C

ATOM 2527 CB LEU A 350 15.088 41.244 32.741 1.00 31.52 A C

ATOM 2528 CG LEU A 350 14.845 39.963 31.938 1.00 29.74 A C

ATOM 2529 CDl LEU A 350 13.349 39.704 31.841 1.00 29.61 A C

ATOM 2530 CD2 LEU A 350 15.457 40.050 30.568 1.00 24.93 A C

ATOM 2531 C LEU A 350 16.489 43.014 33.849 1.00 34.43 A C

ATOM 2532 0 LEU A 350 16.720 42.849 35.053 1.00 34.97 A O

ATOM 2533 N PRO A 351 16.268 44.246 33.322 1.00 33.99 A N

ATOM 2534 CD PRO A 351 16.296 44.614 31.890 1.00 33.98 A C

ATOM 2535 CA PRO A 351 16.225 45.466 34.146 1.00 34.03 A C

ATOM 2536 CB PRO A 351 15.798 46.522 33.146 1.00 35.34 A C

ATOM 2537 CG PRO A 351 16.557 46.102 31.938 1.00 36.02 A C

ATOM 2538 C PRO A 351 15.295 45.446 35.363 1.00 36.05 A C

ATOM 2539 0 PRO A 351 15.386 46.326 36.227 1.00 36.69 A O

ATOM 2540 N ASN A 352 14.439 44.421 35.432 1.00 35.67 A N

ATOM 2541 CA ASN A 352 13.496 44.229 36.527 1.00 34.99 A C

ATOM 2542 CB ASN A 352 12.070 44.049 35.974 1.00 34.88 A C

ATOM 2543 CG ASN A 352 11.869 42.745 35.183 1.00 34.90 A C ATOM 2544 OD1 ASN A 352 12.812 42.011 34.894 1.00 33.67 A O

ATOM 2545 ND2 ASN A 352 10.614 42.456 34.853 1.00 35.20 A N

ATOM 2546 C ASN A 352 13.898 43.082 37.476 1.00 36.87 A C

ATOM 2547 0 ASN A 352 13.059 42.520 38.185 1.00 37.32 A O

ATOM 2548 N GLY A 353 15.176 42.706 37.432 1.00 38.73 A N

ATOM 2549 CA GLY A 353 15.701 41.655 38.294 1.00 39.34 A C

ATOM 2550 C GLY A 353 15.462 40.212 37.889 1.00 41.09 A C

ATOM 2551 O GLY A 353 16.219 39.321 38.305 1.00 40.79 A O

ATOM 2552 N ARG A 354 14.409 39.979 37.100 1.00 42.00 A N

ATOM 2553 CA ARG A 354 14.037 38.644 36.611 1.00 4220 A C

ATOM 2554 CB ARG A 354 12.721 38.713 35.834 1.00 44.15 A C

ATOM 2555 CG ARG A 354 11.489 38.961 36.667 1.00 47.59 A C

ATOM 2556 CD ARG A 354 10.268 39.072 35.777 1.00 4826 A C

ATOM 2557 NE ARG A 354 9.183 38.207 36.232 1.00 52.92 A N

ATOM 2558 CZ ARG A 354 7.958 38.622 36.554 1.00 53.77 A C

ATOM 2559 NHl ARG A 354 7.634 39.912 36.478 1.00 54.10 A N

ATOM 2560 NH2 ARG A 354 7.051 37.736 36.947 1.00 52.64 A N

ATOM 2561 C ARG A 354 15.076 37.995 35.695 1.00 4226 A C

ATOM 2562 O ARG A 354 15.971 38.669 35.155 1.00 43.19 A O

ATOM 2563 N ASP A 355 14.929 36.684 35.504 1.0041.33 A N

ATOM 2564 CA ASP A 355 15.810 35.917 34.626 1.00 39.84 A C ATOM 2565 CB ASP A 355 15.654 34.412 34.873 1.00 39.06 A C

ATOM 2566 CG ASP A 355 16.682 33.861 35.837 1.00 40.57 A C

ATOM 2567 OD1 ASP A 355 17.569 34.621 36290 1.00 40.69 A O

ATOM 2568 OD2 ASP A 355 16.611 32.647 36.131 1.00 4022 A O

ATOM 2569 C ASP A 355 15.454 36201 33.178 1.00 37.90 A C

ATOM 2570 O ASP A 355 14.374 36.708 32.879 1.00 36.61 A O

ATOM 2571 N THR A 356 16.384 35.902 32.283 1.00 35.96 A N

ATOM 2572 CA THR A 356 16.154 36.079 30.859 1.00 34.24 A C

ATOM 2573 CB THR A 356 17.461 36.012 3D.080 1.00 33.41 A C

ATOM 2574 OGl THR A 356 18.172 34.817 30.439 1.00 35.40 A O

ATOM 2575 CG2 THR A 356 18276 37.225 30.354 1.00 34.32 A C

ATOM 2576 C THR A 356 15.334 34.879 30.444 1.00 3323 A C

ATOM 2577 O THR A 356 15.353 33.858 31.146 1.00 34.34 A O

ATOM 2578 N PRO A 357 14.564 34.981 29.339 1.00 31.33 A N

ATOM 2579 CD PRO A 357 14.121 36.135 28.532 1.00 30.35 A C

ATOM 2580 CA PRO A 357 13.805 33.785 28.970 1.00 30.39 A C

ATOM 2581 CB PRO A 357 12.898 34:293 27.851 1.00 29.53 A C

ATOM 2582 CG PRO A 357 13.620 35.474 27.297 1.00 29.44 A C

ATOM 2583 C PRO A 357 14.748 32.672 28.490 1.00 29.76 A C

ATOM 2584 0 PRO A 357 15.980 32.814 28.564 1.00 28.76 A O

ATOM 2585 N ALA A 358 14.162 31.545 28.096 1.00 29.88 A N ATOM 2586 CA ALA A 358 14.906 30.403 27.574 1.00 31.14 A C

ATOM 2587 CB ALA A 358 13.951 29.251 27.306 1.00 33.79 A C

ATOM 2588 C ALA A 358 15.507 30.905 26269 1.00 31.85 A C

ATOM 2589 O ALA A 358 14.794 31.470 25.431 1.00 35.64 A O

ATOM 2590 N LEU A 359 16.826 30.851 26.171 1.00 28.86 A N

ATOM 2591 CA LEU A 359 17.509 31.342 24.985 1.00 29.84 A C

ATOM 2592 CB LEU A 359 18.344 32.580 25.336 1.00 29.99 A C

ATOM 2593 CG LEU A 359 17.733 33.872 25.904 1.00 32.52 A C

ATOM 2594 CDl LEU A 359 18.840 34.878 26.155 1.00 30.47 A C

ATOM 2595 CD2 LEU A 359 16.661 34.448 24.993 1.00 28.48 A C

ATOM 2596 C LEU A 359 18.447 30.313 24.408 1.00 31.82 A C

ATOM 2597 0 LEU A 359 18.994 30.490 23.302 1.00 32.46 A O

ATOM 2598 N PHE A 360 18.667 29.247 25.173 1.00 31.89 A N

ATOM 2599 CA PHE A 360 19.628 28233 24.780 1.00 31.61 A C

ATOM 2600 CB PHE A 360 20.800 28.257 25.767 1.00 31.56 A C

ATOM 2601 CG PHE A 360 21.321 29.645 26.056 1.00 30.67 A C

ATOM 2602 CDl PHE A 360 21.253 30.172 27.354 1.00 30.88 A C

ATOM 2603 CD2 PHE A 360 21.845 30.448 25.022 1.00 31.67 A C

ATOM 2604 CEl PHE A 360 21.705 31.493 27.633 1.00 31.64 A C

ATOM 2605 CE2 PHE A 360 22.295 31.767 25.278 1.00 32.88 A C

ATOM 2606 CZ PHE A 360 22.224 32.290 26.594 1.00 31.45 A C ATOM 2607 C PHE A 360 19.146 26.819 24.531 1.00 31.34 A C

ATOM 2608 O PHE A 360 19.917 25.991 24.039 1.00 33.51 A O

ATOM 2609 N ASN A 361 17.863 26.566 24.774 1.00 30.04 A N

ATOM 2610 CA ASN A 361 17.257 25.248 24.562 1.00 30.01 A C

ATOM 2611 CB ASN A 361 15.922 25.158 25.326 1.00 30.57 A C

ATOM 2612 CG ASN A 361 15.021 26.386 25.120 1.00 33.81 A C

ATOM 2613 OD1 ASN A 361 15.501 27.509 24.962 1.00 33.89 A O

ATOM 2614 ND2 ASN A 361 13.706 26.169 25.148 1.00 33.68 A N

ATOM 2615 C ASN A 361 17.097 24.850 23.069 1.00 31.99 A C

ATOM 2616 O ASN A 361 15.989 24.585 22.596 1.00 34.16 A O

ATOM 2617 N PHE A 362 18.221 24.800 22.348 1.00 31.99 A N

ATOM 2618 CA PHE A 362 18.266 24.452 20.919 1.00 33.58 A C

ATOM 2619 CB PHE A 362 19.620 24.847 20.292 1.00 31.94 A C

ATOM 2620 CG PHE A 362 19.789 26.329 20.035 1.00 31.80 A C

ATOM 2621 CDl PHE A 362 20.505 27.140 20.945 1.00 33.02 A C

ATOM 2622 CD2 PHE A 362 19.264 26.921 18.868 1.00 30.18 A C

ATOM 2623 CEl PHE A 362 20.701 28.533 20.699 1.00 31.76 A C

ATOM 2624 CE2 PHE A 362 19.445 28.313 18.599 1.00 29.91 A C

ATOM 2625 CZ PHE A 362 20.168 29.123 19.520 1.00 31.28 A C

ATOM 2626 C PHE A 362 18.021 22.974 20.604 1.00 35.07 A C

ATOM 2627 O PHE A 362 18.567 22.082 21.247 1.00 36.71 A O ATOM 2628 N THR A 363 17.211 22.742 19.581 1.00 37.25 A N

ATOM 2629 CA THR A 363 16.885 21.407 19.092 1.00 39.86 A C

ATOM 2630 CB THR A 363 15.392 21.369 18.610 1.00 39.85 A C

ATOM 2631 OGl THR A 363 14.536 21.648 19.723 1.00 40.62 A O

ATOM 2632 CG2 THR A 363 14.989 19.999 18.050 1.00 43.82 A C

ATOM 2633 C THR A 363 17.862 21.164 17.930 1.00 41.16 A C

ATOM 2634 O THR A 363 18.531 22.103 17.478 1.00 43.39 A O

ATOM 2635 N THR A 364 17.985 19.909 17.491 1.00 41.31 A N

ATOM 2636 CA THR A 364 18.857 19.539 16.374 1.00 41.08 A C

ATOM 2637 CB THR A 364 19.061 18.010 16.298 1.00 43.82 A C

ATOM 2638 OGl THR A 364 17.805 17.341 16.481 1.00 47.82 A O

ATOM 2639 CG2 THR A 364 20.038 17.553 17.380 1.00 44.21 A C

ATOM 2640 C THR A 364 18.297 20.079 15.057 1.00 39.64 A C

ATOM 2641 O THR A 364 19.052 20.392 14.137 1.00 39.67 A O

ATOM 2642 N GLN A 365 16.976 20.263 15.020 1.00 40.75 A N

ATOM 2643 CA GLN A 365 16.255 20.820 13.864 1.00 41.65 A C

ATOM 2644 CB GLN A 365 14.736 20.677 14.072 1.00 40.80 A C

ATOM 2645 CG GLN A 365 13.822 21.264 12.975 1.00 41.31 A C

ATOM 2646 CD GLN A 365 13.736 20.433 11.694 1.00 40.91 A C

ATOM 2647 OEl GLN A 365 14.283 19.331 11.593 1.00 43.99 A O

ATOM 2648 NE2 GLN A 365 13.029 20.964 10.713 1.00 39.51 A N ATOM 2649 C GLN A 365 16.637 22.299 13.703 1.00 42.27 A C

ATOM 2650 O GLN A 365 16.798 22.773 12.588 1.00 43.60 A O

ATOM 2651 N GLU A 366 16.821 22.996 14.828 1.00 4228 A N

ATOM 2652 CA GLU A 366 17216 24.410 14.844 1.00 43.46 A C

ATOM 2653 CB GLU A 366 - 17.073 24.996 16.242 1.00 44.68 A C

ATOM 2654 CG GLU A 366 15.678 25.305 16.684 1.00 46.61 A C

ATOM 2655 CD GLU A 366 15.674 26.085 17.977 1.00 46.39 A C

ATOM 2656 OEl GLU A 366 15.980 27.299 17.941 1.00 4522 A O

ATOM 2657 OE2 GLU A 366 15.365 25.485 19.026 1.00 48.69 A O

ATOM 2658 C GLU A 366 18.676 24.575 14.447 1.00 43.55 A C

ATOM 2659 O GLU A 366 19.085 25.619 13.932 1.00 44.87 A O

ATOM 2660 N LEU A 367 19.454 23.541 14.738 1.00 42.42 A N

ATOM 2661 CA LEU A 367 20.872 23.515 14.449 1.00 42.72 A C

ATOM 2662 CB LEU A 367 21.593 22.734 15.547 1.00 44.58 A C

ATOM 2663 CG LEU A 367 22.495 23.442 16.567 1.00 44.63 A C

ATOM 2664 CDl LEU A 367 21.984 24.813 17.016 1.00 43.17 A C

ATOM 2665 CD2 LEU A 367 22.633 22.510 17.752 1.00 46.66 A C

ATOM 2666 C LEU A 367 21.198 22.931 13.086 1.00 42.45 A C

ATOM 2667 O LEU A 367 22.330 23.056 12.630 1.00 40.12 A O

ATOM 2668 N SER A 368 20.186 22.381 12.401 1.00 43.40 A N

ATOM 2669 CA SER A 368 20.356 21.762 11.072 1.00 42.65 A C ATOM 2670 CB SER A 368 19.095 20.981 10.662 1.00 4328 A C

ATOM 2671 OG SER A 368 17.978 21.828 10.473 1.00 43.81 A O

ATOM 2672 C SER A 368 20.795 22.720 9.958 1.00 42.18 A C

ATOM 2673 O SER A 368 20.852 22.349 8.783 1.00 43.92 A O

ATOM 2674 N SER A 369 21.107 23.951 10.354 1.00 40.82 A N

ATOM 2675 CA SER A 369 21.589 24.997 9.460 1.00 38.06 A C

ATOM 2676 CB SER A 369 21.049 26.360 9.902 1.00 36.55 A C

ATOM 2677 OG SER A 369 21.750 27.415 9.265 1.00 36.86 A O

ATOM 2678 C SER A 369 23.109 25.004 9.566 1.00 3624 A C

ATOM 2679 O SER A 369 23.810 25.232 8.584 1.00 33.99 A O

ATOM 2680 N ASN A 370 23.595 24.760 10.782 1.00 37.20 A N

ATOM 2681 CA ASN A 370 25.022 24.760 11.085 1.00 37.99 A C

ATOM 2682 CB ASN A 370 25.523 26.215 11.049 1.00 39.63 A C

ATOM 2683 CG ASN A 370 27.017 26.327 10.950 1.00 40.91 A C

ATOM 2684 OD1 ASN A 370 27.761 25.661 11.669 1.00 42.76 A O

ATOM 2685 ND2 ASN A 370 27.475 27.219 10.085 1.00 43.93 A N

ATOM 2686 C ASN A 370 25.226 24.168 12.491 1.00 37.29 A C

ATOM 2687 O ASN A 370 25.091 24.886 13.483 1.00 36.34 A O

ATOM 2688 N PRO A 371 25.474 22.837 12.603 1.00 37.92 A N

ATOM 2689 CD PRO A 371 25.151 21.738 11.668 1.00 37.00 A C

ATOM 2690 CA PRO A 371 25.677 22.295 13.957 1.00 38.12 A C ATOM 2691 CB PRO A 371 25.607 20.779 13.743 1.00 36.53 A C

ATOM 2692 CG PRO A 371 24.640 20.667 12.619 1.00 35.64 A C

ATOM 2693 C PRO A 371 26.921 22.789 14.755 1.00 40.21 A C

ATOM 2694 O PRO A 371 26.825 22.899 15.985 1.00 42.81 A O

ATOM 2695 N PRO A 372 28.085 23.092 14.095 1.00 40.62 A N

ATOM 2696 CD PRO A 372 28.562 22.603 12.783 1.00 40.82 A C

ATOM 2697 CA PRO A 372 29.255 23.581 14.852 1.00 40.90 A C

ATOM 2698 CB PRO A 372 30.360 23.578 13.798 1.00 40.63 A C

ATOM 2699 CG PRO A 372 30.031 22.396 13.014 1.00 4129 A C

ATOM 2700 C PRO A 372 29.113 24.981 15.483 1.00 41.12 A C

ATOM 2701 O PRO A 372 30.025 25.455 16.176 1.00 40.90 A O

ATOM 2702 N LEU A 373 27.993 25.653 15.206 1.00 41.11 A N

ATOM 2703 CA LEU A 373 27.731 26.977 15.782 1.00 40.39 A C

ATOM 2704 CB LEU A 373 26.765 27.801 14.923 1.00 38.71 A C

ATOM 2705 CG LEU A 373 27.343 28.693 13.819 1.00 38.73 A C

ATOM 2706 CDl LEU A 373 26.201 29.491 13.231 1.00 39.93 A C

ATOM 2707 CD2 LEU A 373 28.450 29.634 14.297 1.00 37.22 A C

ATOM 2708 C LEU A 373 27200 26.877 17.209 1.00 38.50 A C

ATOM 2709 O LEU A 373 27.171 27.876 17.932 1.00 36.70 A O

ATOM 2710 N ALA A 374 26.864 25.648 17.617 1.00 37.57 A N

ATOM 2711 CA ALA A 374 26.342 25.338 18.948 1.00 36.57 A C ATOM 2712 CB ALA A 374 25.970 23.864 19.045 1.00 35.33 A C

ATOM 2713 C ALA A 374 27.325 25.705 20.051 1.00 36.53 A C

ATOM 2714 O ALA A 374 26.909 26.095 21.142 1.00 36.38 A O

ATOM 2715 N THR A 375 28.621 25.645 19.738 1.00 36.46 A N

ATOM 2716 CA THR A 375 29.670 25.981 20.700 1.00 39.15 A C

ATOM 2717 CB THR A 375 31.066 25.481 20.240 1.00 39.99 A C

ATOM 2718 OG1 THR A 375 31.249 25.756 18.847 1.00 42.40 A O

ATOM 2719 CG2 THR A 375 31.204 23.978 20.485 1.00 39.43 A C

ATOM 2720 C THR A 375 29.706 27.472 21.059 1.00 39.85 A C

ATOM 2721 O THR A 375 30.147 27.841 22.151 1.00 41.78 A O

ATOM 2722 N ILE A 376 29.201 28.316 20.157 1.00 40.30 A N

ATOM 2723 CA ILE A 376 29.142 29.759 20.399 1.00 40.61 A C

ATOM 2724 CB ILE A 376 29.401 30.613 19.114 1.00 43.21 A C

ATOM 2725 CG2 ILE A 376 29.454 32.110 19.477 1.00 43.37 A C

ATOM 2726 CGI ILE A 376 30.726 30.208 18.451 1.00 44.28 A C

ATOM 2727 CDl ILE A 376 31.011 30.896 17.113 1.00 4726 A C

ATOM 2728 C ILE A 376 27.752 30.077 20.923 1.00 39.70 A C

ATOM 2729 O ILE A 376 27.609 30.877 21.849 1.00 41.57 A O

ATOM 2730 N LEU A 377 26.748 29.411 20.349 1.00 36.93 A N

ATOM 2731 CA LEU A 377 25.345 29.596 20.704 1.00 35.17 A C

ATOM 2732 CB LEU A 377 24.457 28.861 19.714 1.00 35.83 A C ATOM 2733 CG LEU A 377 24.286 29.461 18.322 1.00 35.42 A C

ATOM 2734 CDl LEU A 377 23.478 28.504 17.491 1.00 32.72 A C

ATOM 2735 CD2 LEU A 377 23.610 30.807 18.399 1.00 35.31 A C

ATOM 2736 C LEU A 377 24.943 29.183 22.108 1.00 35.42 A C

ATOM 2737 0 LEU A 377 24.166 29.880 22.763 1.00 35.78 A O

ATOM 2738 N ILE A 378 25.414 28.010 22.527 1.00 35.05 A N

ATOM 2739 CA ILE A 378 25.139 27.467 23.857 1.00 33.16 A C

ATOM 2740 CB ILE A 378 24.758 25.946 23.790 1.00 32.63 A C

ATOM 2741 CG2 ILE A 378 24.365 25.418 25.187 1.00 33.68 A C

ATOM 2742 CGI ILE A 378 23.581 25.736 22.826 1.00 32.69 A C

ATOM 2743 CDl ILE A 378 23.462 24.332 22.234 1.00 28.71 A C

ATOM 2744 C ILE A 378 26.406 27.683 24.704 1.00 32.26 A C

ATOM 2745 O ILE A 378 27.372 26.929 24.583 1.00 34.21 A O

ATOM 2746 N PRO A 379 26.426 28.738 25.548 1.00 32.35 A N

ATOM 2747 CD PRO A 379 25.319 29.692 25.762 1.00 31.13 A C

ATOM 2748 CA PRO A 379 27.556 29.083 26.422 1.00 32.80 A C

ATOM 2749 CB PRO A 379 27.141 30.467 26.950 1.00 31.77 A C

ATOM 2750 CG PRO A 379 25.672 30.342 27.053 1.00 30.94 A C

ATOM 2751 C PRO A 379 27.768 28.041 27.558 1.00 33.22 A C

ATOM 2752 O PRO A 379 26.833 27.306 27.902 1.00 30.92 A O

ATOM 2753 N PRO A 380 28.987 27.974 28.150 1.00 34.30 A N ATOM 2754 CD PRO A 380 30.180 28.786 27.852 1.00 35.46 A C

ATOM 2755 CA PRO A 380 29.313 27.027 29.232 1.00 35.89 A C

ATOM 2756 CB PRO A 380 30.618 27.594 29.805 1.00 36.70 A C

ATOM 2757 CG PRO A 380 30.725 28.998 29.224 1.00 38.77 A C

ATOM 2758 C PRO A 380 28.292 26.723 30.338 1.00 36.41 A C

ATOM 2759 O PRO A 380 28.005 25.550 30.609 1.00 35.01 A O

ATOM 2760 N HIS A 381 27.705 27.770 30.917 1.00 35.63 A N

ATOM 2761 CA HIS A 381 26.727 27.632 31.996 1.00 35.85 A C

ATOM 2762 CB HIS A 381 26.475 28.994 32.654 1.00 36.20 A C

ATOM 2763 CG HIS A 381 25.954 30.036 31.713 1.00 37.76 A C

ATOM 2764 CD2 HIS A 381 26.591 30.826 30.817 1.00 37.18 A C

ATOM 2765 ND1 HIS A 381 24.613 30.350 31.619 1.00 37.12 A N

ATOM 2766 CEl HIS A 381 24.448 31.290 30.706 1.00 39.74 A C

ATOM 2767 NE2 HIS A 381 25.633 31.596 30.205 1.00 40.39 A N

ATOM 2768 C HIS A 381 25.394 26.990 31.593 1.00 36.29 A C

ATOM 2769 O HIS A 381 24.667 26.488 32.450 1.00 36.09 A O

ATOM 2770 N ALA A 382 25.080 27.030 30.297 1.00 37.15 A N

ATOM 2771 CA ALA A 382 23.834 26.466 29.754 1.00 37.39 A C

ATOM 2772 CB ALA A 382 23.301 27.359 28.648 1.00 35.23 A C

ATOM 2773 C ALA A 382 24.044 25.046 29.228 1.00 37.85 A C

ATOM 2774 O ALA A 382 23.087 24.311 28.973 1.00 37.21 A O ATOM 2775 N ARG A 383 25.318 24.685 29.087 1.00 39.37 A N

ATOM 2776 CA ARG A 383 25.768 23.381 28.609 1.00 40.62 A C

ATOM 2777 CB ARG A 383 27.270 23.460 28.314 1.00 40.00 A C

ATOM 2778 CG ARG A 383 27.793 22.612 27.183 1.00 39.15 A C

ATOM 2779 CD ARG A 383 28.239 23.474 26.007 1.00 40.27 A C

ATOM 2780 NE ARG A 383 29.193 24.534 26.360 1.00 42.31 A N

ATOM 2781 CZ ARG A 383 30.096 25.051 25.521 1.00 44.20 A C

ATOM 2782 NHl ARG A 383 30.199 24.605 24.273 1.00 45.71 A N

ATOM 2783 NH2 ARG A 383 30.853 26.072 25.902 1.00 43.13 A N

ATOM 2784 C ARG A 383 25.528 22.351 29.711 1.00 41.86 A C

ATOM 2785 O ARG A 383 25.967 22.547 30.848 1.00 4128 A O

ATOM 2786 N ILE A 384 24.747 21.320 29.398 1.00 42.60 A N

ATOM 2787 CA ILE A 384 24.466 20.250 30.354 1.00 44.95 A C

ATOM 2788 CB ILE A 384 23.082 20.414 31.102 1.00 47.12 A C

ATOM 2789 CG2 ILE A 384 23.246 21.301 32.352 1.00 45.31 A C

ATOM 2790 CGI ILE A 384 21.974 20.899 30.150 1.00 50.65 A C

ATOM 2791 CDl ILE A 384 20.565 20.958 30.769 1.00 52.17 A C

ATOM 2792 C ILE A 384 24.573 18.861 29.717 1.00 46.94 A C

ATOM 2793 OXT ILE A 384 23.875 18.610 28.706 1.00 49.13 A O

TER 2794 ILE A 384 A

ATOM 2795 CI 911 1 -2.099 39.361 19.377 1.00 17.41 C ATOM 2796 C2 911 -1.979 39.019 20.788 1.00 20.21

ATOM 2797 N3 911 -1.929 40.019 21.737 1.00 21.52 N

ATOM 2798 C4 911 -1.978 41.354 21249 1.00 19.29

ATOM 2799 C5 911 -1.911 42.725 21.889 1.00 24.54

ATOM 2800 N6 911 -2.070 43.075 20.531 1.00 22.53 N

ATOM 2801 C7 911 -2.243 43.935 19.596 1.00 23.36

ATOM 2802 N8 911 -1.899 37.700 21.143 1.00 22.23 N

ATOM 2803 C9 911 -1.917 36.693 20.195 1.00 18.35

ATOM 2804 CIO 911 -2.028 37.007 18.799 1.00 19.23

ATOM 2805 Cl l 911 -2.037 35.981 17.807 1.00 23.00

ATOM 2806 N12 911 -2.025 35.075 16.923 1.00 25.04 N

ATOM 2807 C13 911 -2.125 38.354 18.401 1.00 16.13

ATOM 2808 N14 911 -2.259 43201 18.496 1.00 22.90 N

ATOM 2809 C15 911 -2.448 43.663 17.308 1.00 24.02

ATOM 2810 C16 911 -2.414 42.601 16.345 1.00 20.01

ATOM 2811 C17 911 -2.679 45.103 17.166 1.00 25.88

ATOM 2812 C18 911 -2.981 45.761 15.949 1.00 31.01

ATOM 2813 C19 911 -2.634 45.884 18.413 1.00 23.65 C

ATOM 2814 N20 911 -2.410 45.265 19.642 1.00 22.85 N

ATOM 2815 N21 911 -3.237 47.094 15.837 1.00 37.37 N

ATOM 2816 C22 911 -3.469 47.300 14.486 1.00 39.18 C ATOM 2817 C23 911 1 -3.804 48.625 13.840 1.00 42.96 C

ATOM 2818 C24 911 1 -3.339 46.119 13.860 1.00 37.75 C

ATOM 2819 N25 911 1 -3.050 45.200 14.719 1.00 33.10 N

ATOM 2820 C26 911 1 -1.126 42.051 15.987 1.00 20.71 C

ATOM 2821 C27 911 1 -1.022 40.974 15.056 1.00 17.60 C

ATOM 2822 C28 911 1 -2.205 40.428 14.461 1.00 18.33 C

ATOM 2823 CL29 911 1 -2.081 39.096 13.330 1.00 5.54 CL

ATOM 2824 C30 911 1 -3.492 40.965 14.806 1.00 15.33 C

ATOM 2825 C31 911 1 -3.614 42.044 15.740 1.00 16.68 C

ATOM 2826 CL32 911 1 -5.228 42.619 16.119 1.00 7.38 CL

ATOM 2827 OH2 TIP 1 3.519 32.951 -3.643 1.00 16.57 S O

ATOM 2828 OH2 TIP 2 -18.111 34.312 1.385 1.00 34.33 S O

ATOM 2829 OH2 TIP 3 -1.193 48.777 16.143 1.00 38.40 S O

ATOM 2830 OH2 TIP 4 13.184 47.448 2.829 1.00 29.56 S O

ATOM 2831 OH2 TIP 5 29.406 40.325 27.491 1.00 44.55 S O

ATOM 2832 OH2 TIP 6 8229 53.016 15.458 1.00 26.00 S O

ATOM 2833 OH2 TIP 7 0.809 46.462 17.029 1.00 31.42 S O

ATOM 2834 OH2 TIP 8 4.554 27.748 17.918 1.00 40.42 S O

ATOM 2835 OH2 TIP 9 15.156 19.575 8.017 1.00 32.18 S O

ATOM 2836 OH2 TIP 10 12.974 58.863 -0.966 1.00 45.47 S O

ATOM 2837 OH2 TIP 11 25259 42.433 31.980 1.00 35.93 S O ATOM 2838 OH2 TIP 12 2.502 47.199 2.432 1.00 24.60 S O

ATOM 2839 OH2 TIP 13 9.794 59.038 1.375 1.00 34.46 S O

ATOM 2840 OH2 TIP 14 30.784 50.185 13.673 1.00 21.33 S O

ATOM 2841 OH2 TIP 15 17.922 26.780 7.702 1.00 50.73 S O

ATOM 2842 OH2 TIP 16 12.447 49.743 9.377 1.00 27.99 S O

ATOM 2843 OH2 TIP 17 19.653 29.633 9.895 1.00 39.28 S O

ATOM 2844 OH2 TIP 18 5.263 48.916 5.860 1.00 37.92 S O

ATOM 2845 OH2 TIP 19 27.306 50.429 3.066 1.00 27.70 S O

ATOM 2846 OH2 TIP 20 28.550 60.003 -5.780 1.00 27.04 S O

ATOM 2847 OH2 TIP 21 3.716 29.276 26.107 1.00 29.15 S O

ATOM 2848 OH2 TIP 22 -4.637 22.872 22.808 1.00 34.86 S O

ATOM 2849 OH2 TIP 23 -22.724 28.516 20.421 1.00 58.97 S O

ATOM 2850 OH2 TIP 24 11.898 32.240 25.009 1.00 42.27 S O

ATOM 2851 OH2 TIP 25 9.885 46.950 28.465 1.00 47.15 S O

ATOM 2852 OH2 TIP 26 14.656 21.994 3.898 1.00 34.95 S O

ATOM 2853 OH2 TIP 27 16.119 29.366 1.375 1.00 18.85 S O

ATOM 2854 OH2 TIP 28 -1.175 43.756 12.788 1.00 20.87 S O

ATOM 2855 OH2 TIP 29 2.705 49.548 25.939 1.00 39.70 S O

ATOM 2856 OH2 TIP 30 11.096 52.150 17.509 1.00 33.83 S O

ATOM 2857 OH2 TIP 31 5.232 29.294 21.937 1.00 18.19 S O

ATOM 2858 OH2 TIP 32 4.210 33.455 -8.903 1.00 30.20 S O ATOM 2859 OH2 TIP 33 -14.937 35.158 -0.996 1.00 43.25 S O

ATOM 2860 OH2 TIP 34 -20.626 37.458 8.527 1.00 39.12 S O

ATOM 2861 OH2 TIP 35 0.060 22.680 20.356 1.00 45.34 S O

ATOM 2862 OH2 TIP 36 -0.585 41.816 10.715 1.00 57.14 S O

ATOM 2863 OH2 TIP 37 1.539 42.459 3.563 1.00 53.49 S O

ATOM 2864 OH2 TIP 38 22.817 53.174 -18209 1.00 35.74 S O

ATOM 2865 OH2 TIP 39 26.969 32.150 0.631 1.00 41.90 S O

ATOM 2866 OH2 TIP 40 30.263 38.603 15.589 1.00 29.00 S O

ATOM 2867 OH2 TIP 41 -3.722 29.682 -7.880 1.00 59.47 S O

ATOM 2868 OH2 TIP 42 -10.540 29.580 5.124 1.00 32.15 S O

ATOM 2869 OH2 TIP 43 6.128 50.604 11.404 1.00 40.65 S O

ATOM 2870 OH2 TIP 44 16.996 24.052 -8.701 1.00 35.66 S O

ATOM 2871 OH2 TIP 45 -5.648 24.571 24.933 1.00 51.50 S O

ATOM 2872 OH2 TIP 46 21.102 19.443 21.075 1.00 42.64 S O

ATOM 2873 OH2 TIP 47 16.818 15.091 18.344 1.00 33.39 S O

ATOM 2874 OH2 TIP 48 33.965 41.827 17.984 1.00 43.11 S O

ATOM 2875 OH2 TIP 49 -2.829 32.638 30.155 1.00 47.14 S O

ATOM 2876 OH2 TIP 50 26.053 15.853 28.335 1.00 38.68 S O

ATOM 2877 OH2 TIP 51 -2.836 21.590 20.631 1.00 41.84 S O

ATOM 2878 OH2 TIP 52 -5.951 29.665 0.033 1.00 51.25 S O

ATOM 2879 OH2 TIP 53 11.107 40.852 -13.765 1.00 41.02 S O ATOM 2880 OH2 TIP 54 8.201 30.682 26.083 1.00 60.19 S O

ATOM 2881 OH2 TIP 55 1.449 42.290 -0.483 1.00 62.54 S O

ATOM 2882 OH2 TIP 56 26.221 60.218 14.193 1.00 42.92 S O

ATOM 2883 OH2 TIP 57 21.366 56.675 -19.108 1.00 49.21 S O

ATOM 2884 OH2 TIP 58 8.709 44.602 -9.430 1.00 34.08 S O

ATOM 2885 OH2 TIP 59 -4.612 46.703 21.968 1.00 37.46 S O

ATOM 2886 OH2 TIP 60 31.785 41.035 14.348 1.00 32.88 S O

ATOM 2887 OH2 TIP 61 11.831 49.560 -9.633 1.00 40.70 S O

ATOM 2888 OH2 TIP 62 17.518 35.393 -3.198 1.00 31.18 S O

ATOM 2889 OH2 TIP 63 20.516 53.304 19.364 1.00 45.42 S O

ATOM 2890 OH2 TIP 64 -22.615 35.186 24.758 1.00 5222 S O

ATOM 2891 OH2 TIP 65 0.408 61.513 20.076 1.00 48.52 S O

ATOM 2892 OH2 TIP 66 20.504 44.688 31.823 1.00 40.03 S O

ATOM 2893 OH2 TIP 67 5.080 38.325 -8.727 1.00 34.83 S O

ATOM 2894 OH2 TIP 68 -21.340 29.171 17.542 1.00 61.07 S O

ATOM 2895 OH2 TIP 69 30.060 42.039 12.713 1.00 33.64 S O

ATOM 2896 OH2 TIP 70 17.771 51.244 20.977 1.00 39.82 S O

ATOM 2897 OH2 TIP 71 31.991 61.399 8.053 1.00 35.67 S O

ATOM 2898 OH2 TIP 72 31.347 64.436 10.848 1.00 4321 S O

ATOM 2899 OH2 TIP 73 12.674 24.093 19.580 1.00 48.39 S O

ATOM 2900 OH2 TIP 74 27.536 44279 28.770 1.00 43.90 S O ATOM 2901 OH2 TIP 75 4.035 56.178 16.097 1.00 44.11 S O

ATOM 2902 OH2 TIP 76 27.362 53.320 -4.698 1.00 39.13 S O

ATOM 2903 OH2 TIP 77 0.491 45.431 -0.343 1.00 49.14 S O

ATOM 2904 OH2 TIP 78 -11.443 45.826 11.620 1.00 34.98 S O

ATOM 2905 OH2 TIP 79 -19.009 42.127 24.662 1.00 52.17 S O

ATOM 2906 OH2 TIP 80 22.891 56.639 -15.103 1.00 40.03 S O

ATOM 2907 OH2 TIP 81 9.151 24.039 22.182 1.00 43.64 S O

ATOM 2908 OH2 TIP 82 -1.776 52.715 13.965 1.00 50.14 S O

ATOM 2909 OH2 TIP 83 -7.798 30.645 3.978 1.00 37.72 S O

ATOM 2910 OH2 TIP 84 27.677 42.444 23.407 1.00 39.63 S O

ATOM 2911 OH2 TIP 85 11.367 31.300 -10.613 1.00 52.86 S O

ATOM 2912 OH2 TIP 86 18.405 31.450 6.151 1.00 32.72 S O

ATOM 2913 OH2 TIP 87 9.812 39.158 5.604 1.00 42.35 S O

ATOM 2914 OH2 TIP 88 -6.643 26256 -5.266 1.00 56.86 S O

ATOM 2915 OH2 TIP 89 14.190 33.188 -12.189 1.00 60.28 S O

ATOM 2916 OH2 TIP 90 18.734 57.743 16.298 1.00 65.11 S O

ATOM 2917 OH2 TIP 91 17.145 57.024 7.052 1.00 42.35 S O

ATOM 2918 OH2 TIP 92 2.583 35.112 27.158 1.00 47.01 S O

ATOM 2919 OH2 TIP 93 15.189 63.271 23.577 1.00 33.86 S O

ATOM 2920 OH2 TIP 94 29.354 54.037 21.318 1.00 53.67 S O

ATOM 2921 OH2 TIP 95 13.884 29.677 -3.710 1.00 58.47 S O ATOM 2922 OH2 TIP 96 25.590 46.649 3.859 1.00 50.68 S O

ATOM 2923 OH2 TIP 97 26.641 55.372 15.719 1.00 66.43 S O

ATOM 2924 OH2 TIP 98 1.793 39.753 -6.157 1.00 52.77 S O

ATOM 2925 OH2 TIP 99 6.173 34.524 29.142 1.00 46.48 S O

ATOM 2926 OH2 TIP 100 2.019 55.519 22.653 1.00 44.21 S O

ATOM 2927 OH2 TIP 101 9.034 20.561 18.446 1.00 24.12 S O

ATOM 2928 OH2 TIP 102 -12.287 38.499 8.791 1.00 38.64 S O

ATOM 2929 OH2 TIP 103 -6.409 33.685 0.777 1.00 52.36 S O

ATOM 2930 OH2 TIP 104 -15.886 35262 17.514 1.00 38.58 S O

ATOM 2931 OH2 TIP 105 14.952 17.778 20.539 1.00 30.44 S O

ATOM 2932 OH2 TIP 106 13.389 49.661 31.461 1.00 34.32 S O

ATOM 2933 OH2 TIP 107 32.372 53.573 9.559 1.00 36.19 S O

ATOM 2934 OH2 TIP 108 4.214 25.589 20.488 1.00 49.34 S O

ATOM 2935 OH2 TIP 109 -0.552 40.396 2.427 1.00 59.78 S O

ATOM 2936 OH2 TIP 110 -15.298 40.078 6.709 1.00 45.34 S O

ATOM 2937 OH2 TIP 111 18225 34.787 -8.197 1.00 27.76 S O

ATOM 2938 OH2 TIP 112 -0.146 35.717 28.427 1.00 42.11 S O

ATOM 2939 OH2 TIP 113 7.679 39.515 -10.847 1.00 31.78 S O

ATOM 2940 OH2 TIP 114 16.984 16.913 12.972 1.00 67.85 S O

ATOM 2941 OH2 TIP 115 8.712 19.014 2.872 1.00 42.52 S O

ATOM 2942 OH2 TIP 116 8.198 44.158 34.086 1.00 37.02 S O ATOM 2943 OH2 TIP 117 -2.910 15.830 11.287 1.00 34.31 S O

ATOM 2944 OH2 TIP 118 -1.997 32.068 26.939 1.00 48.52 S O

ATOM 2945 OH2 TIP 119 9.831 57.462 9.164 1.00 28.90 S O

ATOM 2946 OH2 TIP 120 -25.333 29.208 1.643 1.00 58.81 S O

ATOM 2947 OH2 TIP 121 8.099 20.459 5.865 1.00 41.51 S O

ATOM 2948 OH2 TIP 122 8.436 19.165 22.385 1.00 59.09 S O

ATOM 2949 OH2 TIP 123 -11.153 43.854 9.021 1.00 45.74 S O

ATOM 2950 OH2 TIP 124 -16.926 40.898 20.693 1.00 40.45 S O

ATOM 2951 OH2 TIP 125 0.330 50.583 -4.589 1.00 42.01 S O

ATOM 2952 OH2 TIP 126 23.399 32.516 22.014 1.00 31.76 S O

ATOM 2953 OH2 TIP 127 -3.095 27.693 33.779 1.00 68.72 S O

ATOM 2954 OH2 TIP 128 25.582 59.602 24.776 1.00 50.29 S O

ATOM 2955 OH2 TIP 129 30.932 45.342 -18.901 1.00 49.88 S O

ATOM 2956 OH2 TIP 130 2.858 52.418 4.564 1.00 41.54 S O

ATOM 2957 OH2 TIP 131 -10.955 41.110 1.222 1.00 38.13 S O

ATOM 2958 OH2 TIP 132 5.205 25.733 -1.653 1.00 39.47 S O

ATOM 2959 OH2 TIP 133 12.520 47.868 35.531 1.00 46.04 S O

ATOM 2960 OH2 TIP 134 18.467 58.591 9.998 1.00 66.38 S O

ATOM 2961 OH2 TIP 135 -1.657 34.133 1.341 1.00 32.64 S O

ATOM 2962 OH2 TIP 136 -5.273 48.189 18.164 1.00 75.53 S O

ATOM 2963 OH2 TIP 137 -15.495 10.770 19.235 1.00 67.03 S O ATOM 2964 OH2 TIP 138 -6.986 49.629 10.903 1.00 31.16 S O

ATOM 2965 OH2 TIP 139 10.825 22.412 -9.270 1.00 52.63 S O

ATOM 2966 OH2 TIP 140 14.242 23.401 -2.089 1.00 47.93 S O

ATOM 2967 OH2 TIP 141 4.219 36.375 37.389 1.00 37.71 S O

ATOM 2968 OH2 TIP 142 16.169 20.549 23.367 1.00 38.34 S O

ATOM 2969 OH2 TIP 143 -19.832 29.214 -1.120 1.00 63.68 S O

ATOM 2970 OH2 TIP 144 16.587 63.221 1.845 1.00 48.55 S O

ATOM 2971 OH2 TIP 145 2.573 17.750 14.486 1.00 47.73 S O

ATOM 2972 OH2 TIP 146 28.599 46.148 0.702 1.00 48.87 S O

ATOM 2973 OH2 TIP 147 22.071 23.744 5.544 1.00 41.02 S O

ATOM 2974 OH2 TIP 148 4.430 26.644 -5.150 1.00 53.95 S O

ATOM 2975 OH2 TIP 149 31.991 42.944 16.456 1.00 36.38 S O

ATOM 2976 OH2 TIP 150 13.706 30.393 35.566 1.00 34.43 S O

ATOM 2977 OH2 TIP 151 -8.927 24.840 28.174 1.00 49.19 S O

ATOM 2978 OH2 TIP 152 20.798 59.707 13.645 1.00 38.69 S O

ATOM 2979 OH2 TIP 153 1.401 45.680 29.309 1.00 37.43 S O

ATOM 2980 OH2 TIP 154 32.678 59.607 -5.112 1.00 43.71 S O

ATOM 2981 OH2 TIP 155 -6.700 39.184 2.850 1.00 68.13 S O

ATOM 2982 OH2 TIP 156 1.764 46.906 9.974 1.00 42.32 S O

ATOM 2983 OH2 TIP 157 20.949 51.475 -11.033 1.00 64.79 S O

ATOM 2984 OH2 TIP 158 9.913 43.769 -12.840 1.00 53.16 S O ATOM 2985 OH2 TIP 159 1.107 32.251 1.523 1.00 35.80 S O

ATOM 2986 OH2 TIP 160 24.448 50.273 -12.912 1.00 43.68 S O

ATOM 2987 OH2 TIP 161 -2.328 43.677 27.605 1.00 40.52 S O

ATOM 2988 OH2 TIP 162 -12.391 33.882 -5.094 1.00 59.21 S O

ATOM 2989 OH2 TIP 163 1.018 38.340 7.126 1.00 51.66 S O

ATOM 2990 OH2 TIP 164 28.227 19.148 15.962 1.00 51.92 S O

ATOM 2991 OH2 TIP 165 -22.990 31.334 -3.602 1.00 65.49 S O

ATOM 2992 OH2 TIP 166 32.281 29.119 23.671 1.00 43.47 S O

ATOM 2993 OH2 TIP 167 -18.410 39.176 30.344 1.00 83.33 S O

ATOM 2994 OH2 TIP 168 -28.321 37.642 -1.802 1.00 50.58 S O

ATOM 2995 OH2 TIP 169 9.841 20.892 15.864 1.00 22.54 S O

ATOM 2996 OH2 TIP 170 -11.075 13.785 23.440 1.00 57.17 S O

ATOM 2997 OH2 TIP 171 -15.649 38.583 34.354 1.00 38.70 S O

ATOM 2998 OH2 TIP 172 23.891 37.353 38.826 1.00 40.19 S O

ATOM 2999 OH2 TIP 173 -4.402 46.850 25.098 1.00 26.76 S O

ATOM 3000 OH2 TIP 174 -7.879 41.469 30.407 1.00 44.51 S O

ATOM 3001 OH2 TIP 175 24.672 40.796 38.201 1.00 42.87 S O

ATOM 3002 OH2 TIP 176 0.323 49.278 10.809 1.00 44.27 S O

ATOM 3003 OH2 TIP 177 -1.563 49.710 27.029 1.00 42.25 S O

ATOM 3004 OH2 TIP 178 30.467 28.497 9.731 1.00 70.19 S O

ATOM 3005 OH2 TIP 179 21.062 20.055 26.928 1.00 38.07 S O ATOM 3006 OH2 TIP 180 -10.108 41.945 6.596 1.00 63.83 S O

ATOM 3007 OH2 TIP 181 18.002 31.621 39.753 1.00 44.14 S O

ATOM 3008 OH2 TIP 182 -5.867 26.073 35.363 1.00 56.58 S O

ATOM 3009 OH2 TIP 183 -12.725 17.108 25.355 1.00 79.37 S O

ATOM 3010 OH2 TIP 184 26.533 51.508 -9.941 1.00 56.56 S O

ATOM 3011 OH2 TIP 185 1.968 52.801 23.026 1.00102.86 S O

ATOM 3012 OH2 TIP 186 3.970 23.738 -7.068 1.00 50.94 S O

ATOM 3013 OH2 TIP 187 -20.685 36.643 13.221 1.00 34.27 S O

ATOM 3014 OH2 TIP 188 10.415 26.628 25.767 1.00 37.17 S O

ATOM 3015 OH2 TIP 189 32.397 37.704 37.161 1.00 53.37 S O

END

While the preferred embodiment of the invention has been illustrated and described, it will be appreciated that various changes can be made therein without departing from the spirit and scope of the invention.

Claims

The embodiments of the invention in which an exclusive property or privilege is claimed are defined as follows:

1. A crystallized GSK3-β complex, comprising:

(a) a GSK3 construct; and

(b) a phosphorylated polypeptide.

2. The complex of Claim 1, wherein the construct has the amino acid sequence set forth in SEQ ID NO: 1 or an active mutant or variant thereof.

3. The complex of Claim 1, wherein the phosphorylated polypeptide comprises a diphosphorylated polypeptide.

4. A crystallized GSK3-β complex, comprising:

(a) a GSK3-β construct having the atomic coordinates set forth in Table 2; and

(b) a phosphorylated polypeptide.

5. The complex of Claim 4, wherein the phosphorylated polypeptide comprises a diphosphorylated polypeptide.

6. A polypeptide in a crystallized form, comprising the active form of GSK3 and the inhibitor binding site thereof, wherein the polypeptide comprises the atomic coordinates set forth in Table 2.

7. The polypeptide of Claim 6 further comprising a bound ligand.

8. A method for providing an atomic model of a GSK3 protein, comprising:

(a) providing a computer readable medium having stored thereon atomic coordinate/x-ray diffraction data of a GSK3 protein in crystalline form, the data sufficient to model the three-dimensional structure of the GSK3 protein, wherein the GSK3 protein in crystalline form comprises a GSK3 construct and a phosphorylated polypeptide;

(b) analyzing the atomic coordinate/x-ray diffraction data from (a) to provide data output defining an atomic model of the GSK3 protein; and (c) obtaining atomic model output data defining the three-dimensional structure of the GSK3 protein.

9. A computer readable medium having stored thereon atomic model data of the GSK3 protein produced by the method of Claim 8.

10. A GSK3-β ligand corresponding to the physical model of the atomic model of the ligand model produced by the method of Claim 8.

11. A method for designing ligands that bind to a GSK3 protein, comprising using some or all of the atomic coordinates of the GSK3 complex presented in Table 2.

12. A method for designing ligands that bind to a GSK3 protein, comprising:

(a) crystallizing a purified GSK3 protein to provide a crystallized GSK3 protein having biological activity, wherein the crystallized GSK3 protein comprises a GSK3 construct and a phosphorylated polypeptide;

(b) resolving the structure of the crystallized GSK3 protein using x-ray crystallography to obtain data suitable for three-dimensional structure determination of the GSK3 protein;

(c) applying the data generated from resolving the structure of the crystallized GSK3 protein to a computer algorithm to generate a model of the GSK3 protein suitable for use in designing ligands that will bind to the GSK3 protein active site; and

(d) applying an iterative process whereby molecular structures are applied to the computer generated model to identify GSK3 binding ligands.

13. The method of Claim 12, wherein the crystallized GSK3 protein comprises the atomic coordinates set forth in Table 2.

14. The method of Claim 12, wherein the GSK3 protein comprises the amino acid sequence set forth in SEQ ID NO: 1 or an active mutant or variant thereof.

15. A GSK binding ligand designed by the method of any one of Claims 11-14.

16. A method for identifying a GSK3 mediator by determining the binding interactions between a potential mediator and a GSK3 binding site, the binding site being defined by at least some of the atomic coordinates set forth in Table 2, the method comprising:

(a) generating a binding cavity defined by the binding site on a computer screen;

(b) generating compounds with their spatial structure; and

(c) determining whether the compounds bind at the GSK3 binding site.

17. A method for identifying a compound that mediates GSK3 activity, comprising:

(a) designing a potential mediator for GSK3 that will form non- covalent bonds with amino acids in the GSK3 binding site based on at least some of the atomic structure coordinates set forth in Table 2;

(b) obtaining the potential mediator; and

(c) determining whether the potential mediator mediates the activity of GSK3.

18. A method for identifying a compound that mediates GSK3 activity, comprising:

(a) using a three-dimensional structure of GSK3 as defined by the atomic coordinates set forth in Table 2 to design or select the potential mediator;

(b) obtaining the potential mediator; and

(c) contacting the potential mediator with GSK3 to determine whether the potential mediator mediates the activity of GSK3.

19. A computer for producing a three-dimensional representation of a molecule or molecular complex, wherein the molecule or molecular complex comprises a binding pocket defined by at least some of the atomic coordinates of GSK3 provided in Table 2, or a three-dimensional representation of a homologue of the molecule or molecular complex, wherein the computer comprises:

(a) a machine-readable data storage medium comprising a data storage material encoded with machine-readable data, wherein the data comprises the atomic coordinates set forth in Table 2; (b) a working memory for storing instructions for processing the machine-readable data;

(c) a central-processing unit coupled to the working memory and to the machine-readable data storage medium for processing the machine readable data into the three-dimensional representation; and

(d) a display coupled to the central-processing unit for displaying the three-dimensional representation.

20. A computer for determining at least a portion of the atomic coordinates corresponding to an X-ray diffraction pattern of a molecule or molecular complex, wherein the computer comprises:

(a) a machine-readable data storage medium comprising a data storage material encoded with machine-readable data, wherein the data comprises at least a portion of the atomic coordinates set forth in Table 2;

(b) a machine-readable data storage medium comprising a data storage material encoded with machine-readable data, wherein the data comprises an X-ray diffraction pattern of the molecule or molecular complex;

(c) a working memory for storing instructions for processing the machine-readable data of (a) and (b);

(d) a central-processing unit coupled to the working memory and to the machine-readable data storage medium of (a) and (b) for performing a Fourier transform of the machine readable data of (a) and for processing the machine readable data of (b) into structure coordinates; and

(e) a display coupled to the central-processing unit for displaying the structure coordinates of the molecule or molecular complex.

21. A method for crystallizing a human glycogen synthase kinase 3 (GSK3) protein, comprising: crystallizing a purified GSK3 protein to provide a crystallized GSK3 protein having biological activity, wherein the crystallized GSK3 protein comprises a GSK3 construct and a phosphorylated polypeptide, and wherein the crystallized GSK3 protein is resolvable using x-ray crystallography to obtain x-ray patterns suitable for three- dimensional structure determination of the crystallized GSK3 protein.

22. The method of Claim 21, wherein crystallizing the GSK3 protein comprises crystallizing by a hanging drop vapor diffusion method.

23. The method of Claim 21 , wherein the crystallized GSK3 protein comprises the atomic coordinates set forth in Table 2.

24. The method of Claim 21, wherein the GSK3 protein comprises the amino acid sequence set forth in SEQ ID NO: 1 or an active mutant or variant thereof.

25. The method of Claim 21, wherein the phosphorylated polypeptide comprises a diphosphorylated polypeptide.

26. A crystallized GSK3 protein provided by the method of Claim 21.

27. A method for making a human glycogen synthase kinase 3 (GSK3) protein complex, comprising: combining a polypeptide that is capable of being phosphorylated, adenosine triphosphate, a magnesium salt, and a GSK3 protein to provide a GSK3 protein complex comprising a phosphorylated polypeptide, adenosine diphosphate, and the GSK3 protein.

28. The method of Claim 27, wherein the protein comprises the amino acid sequence set forth in SEQ ID NO: 1 or an active mutant or variant thereof.

29. The method of Claim 27, wherein the polypeptide capable of being phosphorylated comprises a monophosphorylated polypeptide.

30. A method for making a human glycogen synthase kinase 3 (GSK3) protein complex, comprising: combining a phosphorylated polypeptide, and a GSK3 protein to provide a GSK3 protein complex.

31. The method of Claim 30, wherein the protein comprises the amino acid sequence set forth in SEQ ID NO: 1 or an active mutant or variant thereof.

32. The method of Claim 30, wherein the phosphorylated polypeptide comprises a diphosphorylated polypeptide.

33. A method for making a human glycogen synthase kinase 3 (GSK3) protein crystal, comprising: adding a precipitant to a solution comprising a polypeptide that is capable of being phosphorylated, adenosine triphosphate, a magnesium salt, and a GSK3 protein.

34. The method of Claim 33, wherein the precipitant comprises polyethylene glycol.

35. The method of Claim 33, wherein the precipitant comprises 2-methyl-2,4-pentanediol.

36. The method of Claim 33, wherein the protein crystal comprises the atomic coordinates set forth in Table 2.

37. The method of Claim 33, wherein the protein comprises the amino acid sequence set forth in SEQ ID NO: 1 or an active mutant or variant thereof.

38. The method of Claim 33, wherein the phosphorylated polypeptide comprises a monophosphorylated polypeptide.

39. A crystallized GSK3 protein provided by the method of Claim 33.

40. A method for making a human glycogen synthase kinase 3 (GSK3) protein crystal, comprising: adding a precipitant to a solution comprising a phosphorylated polypeptide and a GSK3 protein.

41. The method of Claim 40, wherein the precipitant comprises polyethylene glycol.

42. The method of Claim 40, wherein the precipitant comprises 2-methyl-2 ,4-pentanediol .

43. The method of Claim 40, wherein the protein comprises the amino acid sequence set forth in SEQ ID NO: 1 or an active mutant or variant thereof.

44. The method of Claim 40, wherein the phosphorylated polypeptide comprises a diphosphorylated polypeptide.

45. A method for making a human glycogen synthase kinase 3 (GSK3) protein crystal, comprising: contacting a crystallized GSK3 protein with a potential GSK3 mediator, wherein the crystallized GSK3 protein comprises a GSK3 construct and a phosphorylated polypeptide.

46. The method of Claim 45, wherein the GSK3 protein comprises the amino acid sequence set forth in SEQ ID NO: 1 or an active mutant or variant thereof.

47. The method of Claim 45, wherein the phosphorylated polypeptide comprises a diphosphorylated polypeptide.

48. A crystallized GSK3 protein provided by the method of Claim 45.