Crystalline phosphatase and method for use thereof

Abstract

This disclosure is directed to a crystalline form of a human protein tyrosine phosphatase designated cdc14A and more particularly to a crystal of human cdc14A, a method of crystallization thereof, and its structure, obtained by x-ray diffraction. In addition, the disclosure relates to methods of identifying new PTP binding agents and more particularly cdc14 (A or B) substrates and inhibitors.

Description

TECHNICAL FIELD

This disclosure is directed to a crystalline form of a human protein tyrosine phosphatase designated cdc14A and more particularly to a crystal of human cdc14A, a method of crystallization thereof, and its structure, obtained by x-ray diffraction. In addition, the disclosure relates to methods of identifying new PTP binding agents and more particularly cdc14 (A or B) substrates and inhibitors.

BACKGROUND

It is estimated that 1,334,100 new cancer cases will be diagnosed and 556,500 cancer deaths will occur in 2003-2004. The direct and indirect costs of cancer in the US are expected to reach $171.6 billion. Despite progress in treatment of many forms of cancer, the five-year survival rates for lung, pancreatic, and esophageal cancers between 1992 and 1998 were still below 20% (Cancer Facts and Figures, 2003. Atlanta, Ga.: American Cancer Society (2003)).

Chemotherapeutic drugs are a mainstay of cancer treatment. Most of these agents target key steps in DNA replication or cell division. Although chemotherapy targets rapidly growing tumor cells, it can also damage healthy proliferating tissues such as epithelium and bone marrow. Side effects can include hair loss, nausea and vomiting, diarrhea, anemia, and potentially fatal infections caused by neutropenia (Devita V T., In Cancer: principles and practice of oncology 4^th ed.; Devita V T; Hellman S; Rosenberg S A, Eds; J. B. Lippincott Co.: Philadelphia, Pa., 1993; pp. 276-292). Chemotherapy drugs are rarely associated with complete remission or cure of most cancers. For example, chemotherapy in lung cancers is primarily palliative (Rigas Semin. Oncol. 25 (suppl. 8): 5-9 (1998)). In addition to low therapeutic index, chemotherapeutic failure may be due to drug resistance, where cancers that are initially sensitive to chemotherapy progress to more aggressive forms with poor treatment response (Pratt et al. Chapter 4: Resistance to anticancer drugs. In: The anticancer drugs 2^nd ed. Oxford University Press, Inc.: New York, N.Y., (1994); pp. 50-66). Newer agents that target different mechanisms of cell survival or proliferation, and that exhibit an improved therapeutic index are desperately needed.

Reversible protein tyrosine phosphorylation, coordinated by the action of protein tyrosine kinases (PTKs) that phosphorylate certain tyrosine residues in polypeptides, and protein tyrosine phosphatases (“PTPs” ) that dephosphorylate certain phosphotyrosine residues, is a key mechanism in regulating many cellular activities. It is becoming apparent that the diversity and complexity of the PTPs and PTKs are comparable, and that PTPs are equally important in delivering both positive and negative signals for proper function of cellular machinery. Regulated tyrosine phosphorylation contributes to specific pathways for biological signal transduction, including those associated with cell division, proliferation and differentiation. Defects and/or malfunctions in these pathways may underlie certain disease conditions for which effective means for intervention remain elusive including, for example, malignancy, autoimmune disorders, diabetes, obesity, inflammation and infection.

The PTP family of enzymes consists of approximately 100 structurally diverse proteins that have in common a highly conserved amino acid PTP catalytic domain, but which display considerable variation in their non-catalytic segments. This structural diversity presumably reflects the diversity of physiological roles of individual PTP family members, which in certain cases have been demonstrated to have specific functions in growth, development and differentiation (Desai et al., Cell 84:599-609, 1996; Kishihara et al., Cell 74:143-156, 1993; Perkins et al., Cell 70:225-236, 1992; Pingel and Thomas, Cell 58:1055-1065, 1989; Schultz et al., Cell 73:1445-1454, 1993). PTPs participate in a variety of physiologic functions, providing a number of opportunities for therapeutic intervention in physiologic processes through alteration or modulation (e.g., up-regulation or down-regulation) of PTP activity. For example, therapeutic inhibition of PTPs such as PTP1B in the insulin-signaling pathway may serve to augment insulin action, thereby ameliorating the state of insulin resistance common in Type II diabetes patients.

Although recent studies have also generated considerable information regarding the structure, expression and regulation of PTPs, the identity of some of the tyrosine phosphorylated substrates through which the PTPs exert their effects remains to be determined. Studies with a limited number of synthetic phosphopeptide substrates have demonstrated some differences in the substrate selectivity of different PTPs (Cho et al., Protein Sci. 2:977-984, 1993; Dechert et al., Eur. J. Biochem. 231:673-681, 1995). Analyses of PTP-mediated dephosphorylation of PTP substrates suggest that catalytic activity may be favored by the presence of certain amino acid residues at specific positions in the substrate polypeptide relative to the phosphorylated tyrosine residue (Ruzzene et al., Eur. J. Biochem. 211:289-295, 1993; Zhang et al., Biochemistry. 33:2285-2290, 1994). Thus, although the physiological relevance of the substrates used in these studies is unclear, PTPs display a certain level of substrate selectivity in vitro. The family of PTPs can be subdivided into two categories: the classical PTPs, pTyr-specific enzymes typified by PTP1B and CD45, and the dual specificity phosphatases (“DSPs”), which dephosphorylate Ser, Thr as well as Tyr residues. The DSPs largely maintain the same catalytic mechanism as the classical PTPs but display differences in architecture of the active site and have been implicated in fundamentally important signaling events from control of MAP kinases in cell proliferation to the regulation of cyclin dependent kinases in the cell cycle.

Mitogen-activated protein kinases (MAP-kinases) are components of conserved cellular signal transduction pathways that have a variety of conserved members and that are integral to the cell's response to stimuli such as growth factors, hormones, cytokines, and environmental stresses. MAP-kinases are activated by phosphorylation by MAP-kinase kinases at a dual phosphorylation motif that has the sequence Thr-X-Tyr, in which phosphorylation at the tyrosine and threonine residues is required for activity. Activated MAP-kinases phosphorylate several transduction targets, including effector protein kinases and transcription factors. Inactivation of MAP-kinases is mediated by dephosphorylation at the Thr-X-Tyr site by dual-specificity phosphatases referred to as MAP-kinase phosphatases. In higher eukaryotes, the physiological role of MAP-kinase signaling has been correlated with cellular events such as proliferation, oncogenesis, development, and differentiation. Accordingly, the ability to regulate signal transduction via these pathways can lead to the development of treatments and preventive therapies for human diseases associated with MAP-kinase signaling, such as cancer.

As stated above, dual-specificity protein tyrosine phosphatases dephosphorylate both phosphotyrosine and phosphor-threonine/serine residues (Walton et al., Ann. Rev. Biochem. 62:101-120, 1993). More than 50 dual-specificity phosphatases that dephosphorylate and inactivate a MAP-kinase have been identified (Shen et al., Proc. Natl. Acad. Sci. USA 98:13613-18, 2001), including MKP-1 (WO 97/00315; Keyse and Emslie, Nature 59:644-647 (1992)); MKP-2 (WO97/00315); MKP-4, MKP-5, MKP-7, Hb5 (WO 97/06245); PAC1 (Ward et al., Nature 367:651-654, 1994); HVH2 (Guan and Butch, J. Biol. Chem. 270:7197-7203, 1995); and PYST1 (Groom et al., EMBO J. 15:3621-3632, 1996). These dual-specificity phosphatases differ in expression, tissue and subcellular distribution, and specificity for MAP-kinase family members. Expression of certain dual-specific phosphatases are induced by stress or mitogens, but others appear to be expressed constitutively in specific cell types. The regulation of dual-specific phosphatase expression and activity is critical for control of MAP-kinase mediated cellular functions, including cell proliferation, cell differentiation and cell survival. For example, dual-specific phosphatases may function as negative regulators of cell proliferation. It is likely that there are many such dual-specific phosphatases, with varying specificity with regard to cell type or activation.

cdc14p in Saccharomyces cerevisiae is an important cell cycle protein phosphatase that regulates exit from mitosis. cdc14p promotes mitosis by inducing degradation of Clb2p mitotic cyclin (equivalent to human cyclin-B), through two mechanisms. The first is by upregulation of the mitotic cyclin dependent kinase inhibitor Sic1p, and the second is by targeting Clb2p for degradation by the 26S proteasome via ubiquitination. cdc14p dephosphorylates the Anaphase Promoting Complex (APC) regulatory subunit Cdh1p, making Clb2p cyclin a better substrate for APC mediated ubiquitination. During most of the cell cycle cdc14p is sequestered in the nucleolus by Net1p, however during early anaphase it is released by activation of a pathway referred to as the Mitotic Exit Network (MEN). This shift in localization explains how cdc14p functions at the proper time to instigate mitotic exit (Gray et al., EMBO J 22:3524-3535, 2003).

In humans there are two homologs of yeast cdc14p referred to as cdc14A and cdc14B (Li et al., J Biol Chem; 272:29403-29406, 1997). cdc14A shares 64% identity with yeast cdc14. Furthermore, cdc14A is 85% identical to cdc14B, with the greatest alignment in the catalytic domain. The two cdc14 homologs vary in sequence predominantly at the N- and C-termini, and cdc14A has a functional nuclear export sequence while cdc14B does not. As a result cdc14B localizes to the nucleolus throughout the cell cycle while cdc14A is found at the centrosomes (Mailand et al., Nature Cell Biology; 4:317-322, 2002; Kaiser et al., Mol Biol Cell; 13:2289-2300, 2002). To date, a biological function for cdc14B has not been determined, although both cdc14A and cdc14B reportedly bind p53 and dephosphorylate pSer-315 in vitro (Li et al., J Biol Chem 275:2410-2414, 2002). A recent study demonstrated that cdc14A dephosphorylates the APC regulatory protein Cdh1 in vitro and that dephosphorylated APCCdh1 has activated ubiquitination of cyclin-B1 (Bembenek and Yu, J Biol Chem, 276:48237-48242, 2001). However, dephosphorylation of Cdh1 by cdc14A and regulation of the APC has not been reported in vivo. Overexpression of catalytically active cdc14A results in premature centrosomal splitting and supernumerary mitotic spindles (Mailand et al., Nature Cell Biology, 4:317-322, 2002; Kaiser et al., Mol Biol Cell, 13:2289-2300, 2002). Both overexpression and down regulation of cdc14A caused aberrant chromosome partitioning into daughter cells, premature centrosome splitting and the formation of supernumerary mitotic spindles (Mailand et al., supra). Down regulation of endogenous cdc14A by short inhibitory RNA duplexes induced mitotic defects, including impaired centrosome separation and failure to undergo cytokinesis (Mailand et al., supra; Gruneberg et al., J Cell Biol; 158:901-914, 2002). These studies implicate cdc14A as a positive regulator of the centrosome duplication cycle. Therefore, inhibition of cdc14A would be expected to block cell proliferation. Finally, very recent data indicate that yeast cdc14p is a master regulator of the inner centromere protein (INCENP)-Aurora kinase complex (Sli15-Ipl1), a complex conserved from yeast through mammalian cells (Pereira and Schiebel, Science, 302:2120-2124, 2003). As part of this complex, yeast cdc14p regulates mitotic exit by modulating spindle behavior through Sli15-Ipl1. It is not known whether mammalian Ccd14A regulates this complex. Notably, in mammalian cells, survivin, a caspase inhibitor implicated in mitosis and potentially cell survival is part of the INCENP complex. This could couple cell mitotic control to decisions for cell survival and apoptosis.

Inhibition of mitosis through the use of agents that perturb microtubule dynamics and disrupt the function of the mitotic spindle have proven useful as strategies for treating diseases involving excessive cell proliferation, most notable human cancers. New targets in this space include inhibitors of aurora-2 kinase and kinesin spindle protein, which are both undergoing evaluation for safety and efficacy in clinical trials involving select malignancies. From all available evidence, mammalian cdc14 homologs appear to regulate a master network of proteins and enzymes that modulate microtubule dynamics involved in chromosome segregation and mitotic exit. cdc14A is a fundamentally important target for cell cycle progression and cell survival. Modulating cdc14A with a selective inhibitor would be anticipated to evoke a conflict signal in the growth fraction of human tumors. Thus, a cdc14A inhibitor might be a novel anti-cancer agent expanding the arsenal of drugs available to better manage cancer, having potential synergies with other anti-mitotics, both classical (e.g. taxanes) and new (e.g. proteasome inhibitors). The design of such an inhibitor would be assisted by more detailed information on the cdc14A polypeptide, such as crystallographic information.

SUMMARY

The disclosure provides a crystalline cdc14A polypeptide.

The disclosure further provides the three-dimensional coordinates of a crystalline cdc14A polypeptide.

The disclosure also provides a crystal formed by cdc14A that diffracts x-ray radiation to produce a diffraction pattern representing the three-dimensional structure of the cdc14A. Further provided by the disclosure is a crystalline polypeptide comprising the approximate cell constants of a=74 angstroms, b=81 angstroms, and c=69 angstroms.

The disclosure further provides a method of crystallizing cdc14A comprising (a) mixing an aqueous solution comprising cdc14A with a reservoir solution comprising a precipitant to form a mixed volume; and (b) crystallizing the mixed volume.

Also provided is a method for determining a three-dimensional structure of cdc14A comprising: (a) obtaining crystalline cdc14A; (b) irradiating the crystalline cdc14A to obtain a diffraction pattern characteristic of the crystalline cdc14A; and (c) transforming the diffraction pattern into a three-dimensional structure of the cdc14A.

The disclosure further provides a machine-readable data storage medium comprising a data storage material encoded with machine-readable data that, when read by an appropriate machine, displays a three-dimensional representation of a crystal of a molecule comprising cdc14A or fragment or variant thereof. Further included in the present disclosure is a computer means for producing a three-dimensional representation of a cdc14A crystal, or a cdc14A crystal: binding agent complex, or co-crystal.

The disclosure provides a method for evaluating the potential of a candidate binding agent to associate with a cdc14A polypeptide or a fragment thereof. The method includes (a) modeling (or producing a three-dimensional representation of) one or more domains of a cdc14A polypeptide, defined by a plurality of atomic coordinates of the cdc14A polypeptide; and (b) modeling (or producing a three-dimensional representation of) the association of a candidate binding agent with said modeled cdc14A polypeptide.

The disclosure further provides a computer program on a computer readable medium comprising instructions to cause a computer to: (a) define a cdc14A polypeptide or fragment thereof based on a plurality of atomic coordinates of the cdc14A polypeptide; and (b) model (or producing a three-dimensional representation of) a potential binding agent that interacts with the cdc14A polypeptide. Further disclosed is a computer with display means for displaying the atomic coordinates.

In yet a further aspect, the disclosure provides a method of designing a compound that mimics the 3-dimensional surface shape of cdc14A polypeptide comprising the steps of: (a) determining the 3-dimensional structure of a cdc14A polypeptide; and (b) designing a compound that complements the 3-dimensional surface configuration of the cdc14A polypeptide.

The disclosure provides a method for determining at least a portion of a three-dimensional structure of a molecular complex, said complex comprising cdc14A and said method comprising the steps of: (a) determining the structural coordinates of a crystal of a cdc14A polypeptide; (b) calculating phases from the structural coordinates; (c) calculating an electron density map from the phases obtained in step (b); and (d) determining the structure of at least a portion of the complex based on said electron density map.

The disclosure also provides a method for evaluating the ability of a chemical entity to associate with cdc14A or a complex thereof. The method includes (a) employing computational or experimental means to perform a fitting operation between the chemical entity and the cdc14A or complex thereof, thereby obtaining data related to the association; and (b) analyzing the data obtained in step (a) to determine the characteristics of the association between the chemical entity and the cdc14A or complex thereof.

The disclosure provides a heavy-atom derivative of a crystallized form of cdc14A.

In yet another aspect, the disclosure provides a method of computationally or experimentally evaluating a chemical entity, or binding agent to obtain information about its association with a domain of cdc14A using a crystal of cdc14A having the structural coordinates described in Table 2.

The disclosure provides a crystalline complex comprising a cdc14A polypeptide and a candidate binding agent.

The disclosure further provides a method for determining the binding of a candidate binding agent to cdc14A, comprising (a) introducing the candidate binding agent and a crystalline cdc14A in an environment such that the agent and crystalline cdc14A can interact; and (b) analyzing the crystalline cdc14A to determine whether the candidate binding agent binds thereto.

The disclosure provides a method of identifying a candidate binding agent for binding to cdc14A. The method includes (a) constructing a three-dimensional structure of cdc14A polypeptide using atomic coordinates shown in Table 2, (b) performing structure-based design of said candidate binding agent using said atomic coordinates of (a); and (c) identifying a candidate binding agent predicted by said structure based design to bind to cdc14A polypeptide.

The details of one or more embodiments of the disclosure are set forth in the accompanying drawings and the description below. Other features, objects, and advantages of the disclosure will be apparent from the description and drawings, and from the claims.

DESCRIPTION OF DRAWINGS

FIG. 1A shows pile-ups of cdc14Aiso1 (SEQ ID NO:2), cdc14Aiso2 (SEQ ID NO:4), and cdc14Aiso3 (SEQ ID NO:6) amino acid sequences in comparison to a consensus amino acid sequence (SEQ ID NO:13).

FIG. 1B shows pile-ups of cdc14Biso1 (SEQ ID NO:8), cdc14Biso2 (SEQ ID NO:10), and cdc14Biso3 (SEQ ID NO:12) amino acid sequences in comparison to a consensus amino acid sequence (SEQ ID NO:14).

FIG. 2A shows a catalytic domain and representative amino acid residues of cdc14 with a C-alpha backbone trace of the active site region.

FIG. 2B shows a catalytic domain and representative amino acid residues of cdc14 with an all-atom representation of the active site region in the same orientation as FIG. 2A.

FIG. 2C shows a catalytic domain and representative amino acid residues of cdc14 with an all-atom representation of the active site region rotated 90° with respect to FIG. 2B.

FIG. 3 shows a computer system useful with the methods of the disclosure.

FIG. 4A shows the nucleic acid sequence of the CDC14Aiso1 coding sequence (SEQ ID NO:1).

FIG. 4B shows the nucleic acid sequence of the CDC14Aiso2 coding sequence (SEQ ID NO:3).

FIG. 4C shows the nucleic acid sequence of the CDC14Aiso3 coding sequence (SEQ ID NO:5).

FIG. 4D shows the nucleic acid sequence of the CDC14Biso1 coding sequence (SEQ ID NO:7).

FIG. 4E shows the nucleic acid sequence of the CDC14Biso2 coding sequence (SEQ ID NO:9).

FIG. 4F shows the nucleic acid sequence of the CDC14Biso3 coding sequence (SEQ ID NO:11).

DETAILED DESCRIPTION

As used in this disclosure, the phrase “modulating phosphorylation” and correlatives thereof such as “modulate” or “modulating” phosphorylation means increasing or decreasing a molecule's state of phosphorylation relative to a control or normal state. It will be appreciated that the degree of modulation provided by a PTP binding agent (e.g., an inhibitor or an activator) will vary and will depend upon the assay conditions. An inhibitor of cdc14 includes any agent that decreases dephosphorylation of a molecule relative to an untreated control. An activator of cdc14 includes any agent that increases dephosphorylation of a molecule compared to a control lacking such an agent.

The terms “cdc14A polypeptide” or “cdc14A” each refer to a polypeptide comprising an amino acid sequence as set forth in SEQ ID NO: 2, or to mutants, fragments, variants (e.g., SEQ ID Nos:4 or 6) and conservative substitutions thereof comprising L- or D-amino acids and includes modified forms thereof, such as glycoproteins.

A “cdc14B polypeptide” or “cdc14B” is intended to encompass a polypeptide comprising an amino acid sequence as set forth in SEQ ID NO:8, or to mutants, fragments, variants (e.g., SEQ ID Nos:10 or 12) and conservative substitutions thereof comprising L- or D-amino acids and include modified forms thereof, such as glycoproteins.

The terms “cdc14 polypeptide” and “cdc14” are each intended to encompass either or both a cdc14A and/or a cdc14B polypeptide, as the context requires.

The term “binding agent” means any compound that is capable of binding to or interacting with a cdc14 polypeptide's binding domain (e.g., active site or catalytic site) or other domain (e.g., an allosteric or exosite domain). For example, a binding agent can bind to or interact with a domain on the cdc14 polypeptide causing a change in the conformation of the polypeptide thereby rendering the cdc14 inactive. Such compounds can include polypeptides, peptidomimetics, antibodies, antibody fragments, small chemical molecules, and the like. The binding agent may inhibit activity of cdc14 polypeptide by acting as a competitive binding agent to a naturally occurring substrate of a cdc14 polypeptide. A binding agent may also be a natural or modified substrate for cdc14 polypeptide, such as, for example, p53 (J Biol Chem. 275(4):2410-4, 2000); hCdh1 (J Biol Chem. 276(51):48237-42, 2001); p27Kip1 (Mol Biol Cell. 13(7):2289-300, 2002); histone H1 (Mol Biol Cell. 13(7):2289-300, 2002); cdc15 (Curr Biol. 10(10):615-8, 2000); and Sic1 (Mol Cell. 2(6):709-18, 1998). Alternatively, a binding agent can be a fragment of a naturally occurring polypeptide or a synthetic polypeptide that is designed (based on the disclosure herein) to interact with a binding cavity of a cdc14 polypeptide.

The term “polypeptide” refers to a chain of amino acid residues, regardless of length or posttranslational modification (e.g., glycosylation or phosphorylation). A polypeptide refers to a polymer in which the monomers are amino acid residues that are joined together through amide bonds. When the amino acids are alpha-amino acids, either the L-optical isomer or the D-optical isomer can be used, the L-isomers being typical.

As used herein, a “substantially pure” polypeptide is a polypeptide that has been separated from components that naturally accompany it. Typically, a polypeptide is substantially pure when it is at least 60%, by weight, free from the proteins and naturally-occurring molecules with which it is naturally associated. Typically, the preparation is at least 75%, 90%, typically 95%, and most typically at least 99%, by weight, free from the proteins and naturally-occurring molecules with which it is naturally associated. A substantially pure polypeptide may be obtained, for example, by extraction from a natural source; by expression of a recombinant nucleic acid encoding a desired polypeptide; or by chemically synthesizing the polypeptide. Purity can be measured by any appropriate method (e.g., column chromatography, polyacrylamide gel electrophoresis, by HPLC analysis, and the like).

Accordingly, the polypeptides of the disclosure are intended to cover naturally occurring proteins, as well as those that are recombinantly or synthetically synthesized. Polypeptide fragments are also encompassed by the disclosure. Fragments have fewer amino acid residues than the polypeptides of SEQ ID NO:2 or SEQ ID NO:8, and therein can have the same or substantially the same amino acid sequence as the naturally occurring polypeptide over the corresponding region. A polypeptide or peptide having substantially the same sequence means that an amino acid sequence is largely, but not entirely, the same, and, for purposes of certain aspects of this invention, retains the three-dimensional structure conformation of the sequence to which it is related. Indeed, if a certain domain or region of a cdc14 is targeted for potential binding, the full-length protein may not need to be crystallized in order to provide the benefit of a three-dimensional representation of the conformation of such domain or region. A fragment containing the cdc14 region or domain of interest can be used and crystallized or even co-crystallized with a candidate binding agent. The representation of the fragment or domain or region can provide valuable information in the design of candidate binding agents, and in particular in rational drug design. In general, polypeptides of the disclosure include peptides, or full length polypeptides or fragments, that contain substitutions, deletions, or insertions into the protein backbone that would still have approximately 70%, 80%, 90%, 95% or 99% homology to the original polypeptide over the corresponding portion of the molecule. A yet greater degree of departure from homology is allowed if like-amino acids, i.e., conservative amino acid substitutions, are not considered a change in the sequence.

A polypeptide that is substantially related to a naturally occurring protein, but for a conservative variation, is also contemplated to be within the methods of the disclosure. For example, a binding agent can be modeled to interact with a variant cdc14 polypeptide based upon the structural coordinates described herein. In another aspect, a polypeptide binding agent can be modified to generate variants that interact with a cdc14 polypeptide. A conservative variation denotes the replacement of an amino acid residue by another, biologically similar residue. Examples of conservative variations include the substitution of one hydrophobic residue such as isoleucine, valine, leucine or methionine, for another hydrophobic residue, or the substitution of one polar residue for another, such as the substitution of arginine for lysine, glutamic acid for aspartic acids, or glutamine for asparagine, and the like. Other illustrative, non-limiting, examples of conservative substitutions include the changes of: alanine to serine; arginine to lysine; asparagine to glutamine or histidine; aspartate to glutamate; cysteine to serine; glutamine to asparagine; glutamate to aspartate; glycine to proline; histidine to asparagine or glutamine; isoleucine to leucine or valine; leucine to valine or isoleucine; lysine to arginine, glutamine, or glutamate; methionine to leucine or isoleucine; phenylalanine to tyrosine, leucine or methionine; serine to threonine; threonine to serine; tryptophan to tyrosine or phenylalanine; tryptophan to phenylalanine; tyrosine to tryptophan or phenylalanine; and valine to isoleucine or leucine.

Modifications and substitutions are not limited to replacement of amino acids. For a variety of purposes, such as increased stability, solubility, or configuration concerns, one skilled in the art will recognize the potential value of introducing, (by deletion, replacement, or addition) other modifications. Examples of such other modifications include incorporation of rare amino acids, D-amino acids, glycosylation sites, cytosine for specific disulfide bridge formation, and the like. The use of modified polypeptide binding agents that incorporate non-naturally occurring amino acids for increased stability can be developed for therapeutic administration. The modified polypeptide binding agents can be modeled to interact with the binding domain/catalytic domain of a cdc14A polypeptide based upon the structural coordinates described herein. The modified peptides can be chemically synthesized, or the isolated gene can be site-directed mutagenized, or a synthetic gene can be synthesized and expressed in bacteria, yeast, baculovirus, tissue culture, and the like, to obtain the modified polypeptide.

Variations to a cdc14A polypeptide wherein the polypeptide still retains its biological activity, can be made by any number of means known in the art. For example, variations can be obtained by such methods as error-prone PCR, shuffling, oligonucleotide-directed mutagenesis, assembly PCR, sexual PCR mutagenesis, and the like, as well as any combination of two or more thereof. The resulting varigated polypeptide can then be screened by high throughput screening techniques that measure the ability of the varigated polypeptide to function as a PTP or to function as a PTP substrate. With reference to FIG. 1A and 1B, one of skill in the art can easily identify the conserved amino acid residues and those amino acid residues that are not conserved and thus can be modified without destroying the activity of a cdc14 polypeptide.

The term “substantially identical” means a polypeptide or nucleic acid exhibiting at least 50%, 85%, 90%, but typically at least 95% identity to a reference amino acid or nucleic acid sequence.

Identity is often measured using sequence analysis software (e.g., Sequence Analysis Software Package of the Genetics Computer Group, University of Wisconsin Biotechnology Center, 1710 University Avenue, Madison, Wis. 53705). Such software matches sequences by assigning degrees of homology to various deletions, substitutions and other modifications. The terms “homology” and “identity” in the context of two or more nucleic acids or polypeptide sequences, refer to two or more sequences or subsequences that are the same or have a specified percentage of amino acid residues or nucleotides that are the same when compared and aligned for maximum correspondence over a comparison window or designated region as measured using any number of sequence comparison algorithms or by manual alignment and visual inspection.

For sequence comparison, one sequence acts as a reference sequence, to which test sequences are compared. When using a sequence comparison algorithm, test and reference sequences are entered into a computer, subsequence coordinates are designated, if necessary, and sequence algorithm program parameters are designated. Default program parameters can be used, or alternative parameters can be designated. The sequence comparison algorithm then calculates the percent sequence identities for the test sequences relative to the reference sequence, based on the program parameters.

A comparison window includes reference to a segment of any one of the number of contiguous positions falling in the range of about 20 to about 600, usually from about 50 to about 200, more usually from about 100 to about 150 in which a sequence may be compared to a reference sequence of the same number of contiguous positions after the two sequences are optimally aligned. Methods of alignment of sequences for comparison are well-known in the art. Optimal alignment of sequences for comparison can be conducted, e.g., by the local homology algorithm of Smith &Waterman, Adv Appl Math 2:482, 1981, by the homology alignment algorithm of Needleman and Wunsch, J Mol Biol 48:443, 1970, by the search for similarity method of person & Lipman, Proc. Nat'l. Acad. Sci. USA 85:2444,1988, by computerized implementations of these algorithms (GAP, BESTFIT, FASTA, and TFASTA in the Wisconsin Genetics Software Package, Genetics Computer Group, 575 Science Dr., Madison, Wis.), by manual alignment and visual inspection, and the like. Other algorithms for determining homology or identity include, for example, BLAST (Basic Local Alignment Search Tool), ALIGN, AMAS (Analysis of Multiply Aligned Sequences), AMPS (Protein Multiple Sequence Alignment), ASSET (Aligned Segment Statistical Evaluation Tool), BANDS, BESTSCOR, BIOSCAN (Biological Sequence Comparative Analysis Node), BLIMPS (BLocks IMProved Searcher), FASTA, Intervals &Points, BMB, CLUSTAL V, CLUSTAL W, CONSENSUS, LCONSENSUS, WCONSENSUS, Smith-Waterman algorithm, DARWIN, Las Vegas algorithm, FNAT (Forced Nucleotide Alignment Tool), Framealign, Framesearch, DYNAMIC, FILTER, FSAP (Fristensky Sequence Analysis Package), GAP (Global Alignment Program), GENAL, GIBBS, GenQuest, ISSC (Sensitive Sequence Comparison), LALIGN (Local Sequence Alignment), LCP (Local Content Program), MACAW (Multiple Alignment Construction & Analysis Workbench), MAP (Multiple Alignment Program), MBLKP, MBLKN, PIMA (Pattern-Induced Multi-sequence Alignment), SAGA (Sequence Alignment by Genetic Algorithms) and WHAT-IF. Such alignment programs can also be used to screen genome databases to identify polynucleotide sequences having substantially identical sequences. A number of genome databases are available.

Software for performing BLAST analyses is publicly available through the National Center for Biotechnology Information (http://www.ncbi.nlm.nih. gov). This algorithm involves first identifying high scoring sequence pairs (HSPs) by identifying short words of length W in the query sequence, which either match or satisfy some positive-valued threshold score T when aligned with a word of the same length in a database sequence. T is referred to as the neighborhood word score threshold (Altschul et al., supra). These initial neighborhood word hits act as seeds for initiating searches to find longer HSPs containing them. The word hits are extended in both directions along each sequence for as far as the cumulative alignment score can be increased. Cumulative scores are calculated using, for nucleotide sequences, the parameters M (reward score for a pair of matching residues; always >0). For amino acid sequences, a scoring matrix is used to calculate the cumulative score. Extension of the word hits in each direction are halted when: the cumulative alignment score falls off by the quantity X from its maximum achieved value; the cumulative score goes to zero or below, due to the accumulation of one or more negative-scoring residue alignments; or the end of either sequence is reached. The BLAST algorithm parameters W, T, and X determine the sensitivity and speed of the alignment. The BLASTN program (for nucleotide sequences) uses as defaults a wordlength (W) of 11, an expectation (E) of 10, M=5, N=−4 and a comparison of both strands. For amino acid sequences, the BLASTP program uses as defaults a wordlength of 3, and expectations (E) of 10, and the BLOSUM62 scoring matrix (see Henikoff &Henikoff, Proc. Natl. Acad. Sci. USA 89:10915,1989) alignments (B) of 50, expectation (E) of 10, M=5, N=−4, and a comparison of both strands.

The disclosure provides a functional model based upon the crystal structure coordinates of cdc14A. Accordingly, the structure coordinates of cdc14A, or portions thereof, as provided by this disclosure are particularly useful to assist in solving the structure of a cdc14 (A or B) mutant. As discussed above, cdc14A shares a great deal of homology and identity with cdc14B. A sequence alignment of the cdc14A and B polypeptide sequences demonstrates the conserved nature of the two molecules (See FIGS. 1A-1B). Because cdc14A and B share conservation within their putative catalytic binding domains, a binding agent of a cdc14A catalytic binding domain identified by the crystal structure coordinates provided herein, may interact with a catalytic binding domain of cdc14B. For example, referring to FIG. 1A and FIG. 1B it will be apparent that the active sites of both cdc14A and B comprise, (from N- to C-) HCKAGLGRT (e.g., SEQ ID NO:2 from amino acid 277-285 (atom 2205 through atom 2268 as shown in Table 2); SEQ ID NO:8 from 313-321, respectively) in a central loop (FIGS. 2A-2C) comprising a catalytic cysteine residue. Other loop sections surround this central loop of cdc14A and B as set forth in Table 1 below:

	TABLE 1
	SEQ ID NO:	amino acids	sequence
	2, 4, 6	46-49	ENFY
	2, 4, 6	131-135	DASFG
	2, 4, 6	173-181	ERVENGDFN
	2, 4, 6	191-195	FSGPH
	2, 4, 6	204-206	YPL
	2, 4, 6	227-229	LNK
	2, 4, 6	249-253	FIDGS
	2, 4, 6	312-320	RPGSIIGPQ
	8, 10, 12	83-86	ENFY
	8, 10, 12	167-172	DAAYGS
	8, 10, 12	209-217	EKAENGDLN
	8, 10, 12	227-231	FCGPH
	8, 10, 12	240-242	YHQ
	8, 10, 12	263-265	LNK
	8, 10, 12	285-289	FADGS
	8, 10, 12	348-356	RPGSVIGPQ

For the first time, the disclosure permits the use of molecular design techniques to design, select and synthesize chemical entities and compounds, including inhibitory compounds, substrates, and the like, capable of binding to a cdc14A polypeptide alone, or both to a cdc14A polypeptide and a cdc14B polypeptide, in whole or in part.

One aspect of the disclosure resides in obtaining crystals of the cdc14A polypeptide of sufficient quality to determine the three dimensional (tertiary) structure of the protein by X-ray diffraction methods. The knowledge obtained concerning the three-dimensional structure of cdc14A can be used to assist in the determination of the three-dimensional structure of other PTP proteins. Candidate binding agents can also be designed by various computer models as described herein. Based on the structural coordinates of the cdc14A polypeptide (i.e., the three dimensional protein structure), as described herein, small molecules or polypeptides that mimic the shape or configuration or are capable of interacting with, a catalytic domain of a cdc14 can be designed and synthesized to modulate cdc14 biological functions (e.g., modulate dephosphorylation). Further, the structural coordinates of cdc14 may be used to design candidate binding agents that bind to non-catalytic regions of cdc14. Such agents are sometimes called “allosteric” or “exosite” binding agents. Such allosteric binding agents are useful if they are able to cause a change in the conformation of the polypeptide thus modulating the biological activity of cdc14, even though no binding to the catalytic domain occurs. Accordingly, in one embodiment, the disclosure provides a method of “rational” drug design. Another approach to rational drug design is based on a lead compound that is discovered using high-throughput screens; the lead compound can be further modified based on a crystal structure of the binding domains of cdc14A. Such lead compounds and related variants are resynthesized and can be co-crystallized with cdc14A. Accordingly, another aspect of the disclosure is to provide material, which is a starting material in the rational design of drugs, which modulate the action of cdc14A.

The term “crystal structure coordinates” refers to mathematical coordinates derived from mathematical equations related to the patterns obtained from diffraction of a monochromatic beam of X-rays by the atoms (scattering centers) of a polypeptide in crystal form (e.g., a cdc14A polypeptide). The diffraction data are used to calculate an electron density map of the repeating unit of the crystal. The electron density maps are used to establish the positions of the individual atoms within the unit cell of the crystal. The crystal structure coordinates of a cdc14A polypeptide crystal having space group P₂₁₂₁₂ (have the unique unit cell dimensions of a=74 Å, b=81 Å, c=69 Å, and contain one protein molecule per asymmetric unit) are set forth in Table 2. The coordinates of the cdc14A polypeptide can also be obtained by means of computational analysis.

Various methods for crystallization are known in the art. Selenomethionine substitution refers to a method of producing a chemically modified form of a crystal of cdc14A. For example, and not by way of limitation, the cdc14A polypeptide can be expressed by bacteria in media that is depleted in methionine and supplemented with selenomethionine. Selenium can be thereby incorporated into the crystal in place of the sulfur of methionine. The location(s) of selenium are then determined by X-ray diffraction analysis of the crystal. This information is used to generate the phase information used to construct a three-dimensional structure of the protein.

Heavy atom derivatization refers to a method of producing a chemically modified form of a crystal of cdc14A. For example, a crystal is soaked in a solution containing heavy metal atom salts or organometallic compounds, which can diffuse through the crystal and bind to the surface of a polypeptide. The location(s) of the bound heavy metal atom(s) are determined by X-ray diffraction analysis of the soaked crystal. This information is used to generate the phase information used to construct a three-dimensional structure of the polypeptide.

The term “unit cell” refers to the simplest volume element that by repeated translation describes the crystal. The term “asymmetric unit” refers to the smallest non-repeating element of the unit cell.

The term “space group” refers to the combination of symmetry operators that when applied to the asymmetric unit describes the contents of the unit cell.

The methods of the disclosure allow the modeling and identification of binding agents that can interact with the catalytic domains of both cdc14A and cdc14B, or one catalytic domain (e.g., a cdc14A catalytic domain) but not a catalytic domain of the other polypeptide (e.g., a cdc14B). Furthermore, binding agents for binding domains of related PTPs that share at least 80%, 90%, 95%, 98% or 99% identity to a cdc14A polypeptide or its binding domain can be identified by the methods and systems of the disclosure. For example, the catalytic domain of a cdc14A polypeptide includes residues 277-285 of SEQ ID NO:2, and can involve the interaction of additional amino acids such as those identified in Table 1. The coordinates of the atoms associated with the crystal structure of the cdc14A polypeptide are provided in Table 2. More specifically, the atoms associated with the catalytic domain of cdc14A extend from atom 2205 through atom 2268 (i.e., amino acid 277 285 of SEQ ID NO:2). As used herein a “binding domain” includes a site (such as an atom, a functional group of an amino acid residue or a plurality of such atoms and/or groups) in a cdc14A binding cavity. In one aspect, the binding domain is a catalytic domain, which may interact with a binding agent (e.g., a substrate, an inhibitor or an activator). In another embodiment, a binding domain may be allosteric. Depending on the particular molecule in the cavity, sites may exhibit attractive or repulsive binding interactions, brought about by charge, steric considerations and the like.

One approach enabled by the disclosure is to use the structure coordinates as set forth in Table 2 to design binding agents that bind to a cdc14A polypeptide. The physical properties of the binding agent can be modified in different ways (e.g., to alter solubility). For example, the disclosure enables the design of binding agents that act as inhibitors or substrates of a PTP polypeptide by binding to the cdc14A molecule.

In another approach a cdc14A polypeptide crystal is contacted with a variety of different binding entities to determine optimal sites for interaction between candidate binding agents (e.g., inhibitors or substrates) and a cdc14A binding domain.

In another embodiment, an approach made possible and enabled by the disclosure, is to screen computationally small molecule databases for putative binding entities that can bind in whole, or in part, to a cdc14A polypeptide or fragment thereof. In such screening, the quality of fit of such a binding entity to the binding domain may be judged in a variety of ways, e.g., by shape complementarity or by estimated interaction energy (Meng et al., J Comp Chem, 13:505-524, 1992). Candidate binding agents can then be synthesized using conventional methods and tested for cdc14 binding using conventional methods or using those methods described herein.

In addition, a cdc14A polypeptide mutant may be crystallized in association or complex with known binding agents, substrates, or inhibitors. The crystal structures of a series of such complexes may then be solved by molecular replacement and compared with that of a wild-type cdc14 molecule. Potential sites for modification within the cdc14 molecule may thus be identified. This information provides an additional tool for determining the most efficient binding interactions, for example, increased hydrophobic interactions, between a cdc14 polypeptide and a candidate binding agent or compound.

All of the complexes referred to above may be studied using known X-ray diffraction techniques and may be refined versus 2-3 Å resolution X-ray data to an R value of about 0.20 or less using computer software, such as X-PLOR (Yale University, 1992, distributed by Molecular Simulations, Inc.; see also, Methods in Enzymology, vol. 114 and 115, H. W. Wyckoff et al., eds., Academic Press (1985)). This information may thus be used to design, synthesize and optimize cdc14 binding agents (e.g., inhibitors or substrates).

The design of binding agents that bind to or inhibit a cdc14A polypeptide according to the disclosure generally involves consideration of two factors. First, the binding agent should be capable of physically and structurally associating with a cdc14A polypeptide. Non-covalent molecular interactions, important in the association of a PTP with a substrate, include hydrogen bonding, van der Waals and electrostatic interactions, and the like. Second, the binding agent should be able to assume a conformation that allows it to associate with a cdc14A polypeptide. Although certain portions of the binding agent will not directly participate in the association, those portions may still influence the overall conformation of the polypeptide. This, in turn, may have a significant impact on potency, and/or pharmacokinetic properties. Such conformational requirements include the overall three-dimensional structure and orientation of the binding agent in relation to all or a portion of the binding domain, e.g., active site or accessory binding site of a cdc14A polypeptide, or the spacing between functional groups of a compound comprising several chemical entities that directly interact with cdc14A.

The potential inhibitory or binding effect of a binding agent on cdc14A may be analyzed prior to its actual synthesis and testing by the use of computer modeling techniques as described herein or those known in the art using information provided herein. If the theoretical structure of the candidate or test binding agent has insufficient interaction and association between the binding agent and cdc14A, synthesis and testing of the binding agent may be obviated. However, if computer modeling indicates a potentially strong interaction, the binding agent may then be synthesized and tested for its ability to bind to cdc14A. Whether or not the binding agent possesses cdc14A or cdc14B inhibitory or modulating characteristics can be determined through routine assays. Methods of assaying for cdc14 activity are known in the art (as identified and discussed herein).

A candidate or test binding agent of cdc14A or cdc14B polypeptide may be computationally evaluated and designed by means of a series of steps in which putative binding agents are screened and selected for their ability to associate with the catalytic domain or other areas of cdc14.

One skilled in the art may use one of several methods to screen candidate binding agents for their ability to associate with a cdc14 polypeptide. This process may begin by visual inspection of, for example, the catalytic domain on a computer screen based on the cdc14A coordinates provided in Table 2 using methods and equipment described above and elsewhere herein; or used routinely in the art. A computer model of a selected binding agent may then be positioned in a variety of orientations, or docked, within an individual binding pocket. Docking may be accomplished using software such as, and without limitation, QUANTA and SYBYL, followed by energy minimization and molecular dynamics with standard molecular mechanics force fields, such as, and without limitation, CHARM and AMBER.

Specialized computer programs may also assist in the process of selecting candidate binding agents. These include but are not limited to:

• 1. GRID (Goodford, P. J., “A Computational Procedure for Determining Energetically Favorable Binding Sites on Biologically Important Macromolecules”, Med. Chem., 28, pp. 849-857 (1985)). GRID is available from Oxford University, Oxford, UK.
• 2. MCSS (Miranker, A. and M. Karplus, “Functionality Maps of Binding Sites: A Multiple Copy Simultaneous Search Method.” Proteins: Structure. Function and Genetics, 11, pp. 29-34 (1991)). MCSS is available from Molecular Simulations, Burlington, Mass.
• 3. AUTODOCK (Goodsell, D. S. and A. J. Olsen, “Automated Docking of Substrates to Proteins by Simulated Annealling, Proteins: Structure. Function, and Genetics, 8, pp. 195-202 (1990)). AUTODOCK is available from Scripps Research Institute, La Jolla, Calif.
• 4. DOCK (Kuntz, I. D. et al., “A Geometric Approach to Macromolecule-Ligand Interactions”, J. Mol. Biol., 161, pp. 269-288 (1982)). DOCK is available from The University of California, San Francisco, Calif.

Where fragments of candidate binding agents are modeled, those fragments can be altered using computer programs. Useful programs to aid one of skill in the art in connecting the individual fragments include:

• 1. CAVEAT (Bartlett, P. A. et al, “CAVEAT: A Program to Facilitate the Structure-Derived Design of Biologically Active Molecules”. In “Molecular Recognition in Chemical and Biological Problems”, Special Pub., Royal Chem. Soc., 78, pp. 182-196 (1989)). CAVEAT is available from the University of California, Berkeley, Calif.
• 2. Database systems such as MACCS-31) (MDL Information Systems, San Leandro, Calif.). This area is reviewed in Martin, Y. C., “31) Database Searching in Drug Design. Med. Chem., 35, pp. 2145-2154 (1992)).
• 3. HOOK (available from Molecular Simulations, Burlington, Mass.).

In addition to the method of building or identifying a binding agent in a step-wise fashion one fragment (or moiety) or chemical entity at a time as described above, or as otherwise known in the art, candidate binding agents may be designed as a whole or “de novo” using either an empty active site or optionally including some portion(s) of a known binding site, using methods, such as and without limitation:

• 1. LUDI (Bohm, et al., “The Computer Program LUDI: A New Method for the De Novo Design of Enzyme Inhibitors”, J. Comp. Aid. Molec. Design, 6, pp. 61-78 (1992)). LUDI is available from Biosym Technologies, San Diego, Calif.
• 2. LEGEND (Nishibata, Y. and A. Itai, Tetrahedron, 47, p. 8985 (1991)). LEGEND is available from Molecular Simulations, Burlington, Mass.
• 3. LeapFrog (available from Tripos Associates, St. Louis, Mo.).

Other molecular modeling techniques may also be employed in accordance with this disclosure. See, e.g., Cohen, N. C. et al., “Molecular Modeling Software and Methods for Medicinal Chemistry”, J. Med. Chem., 33, pp. 883-894 (1990). See also, Navia, M. A. and M. A. Murcko, “The Use of Structural Information in Drug Design, Current Opinions in Structural Biology,” 2, pp. 202-210 (1992).

Once a compound or binding agent has been designed or selected by the above methods, the potency with which that binding agent may bind to cdc14 may be tested and optimized by computational evaluation.

A candidate or test binding agent or compound designed or selected as cdc14A candidate binding agent may be further computationally optimized so that in its bound state it would lack repulsive electrostatic interaction with the target binding site. Such non-complementary (e.g., electrostatic) interactions include repulsive charge-charge, dipole-dipole and charge-dipole interactions. Specifically, the sum of all electrostatic interactions between the binding agent and cdc14A when the binding agent is bound to cdc14A, should have a neutral or favorable contribution to the enthalpy of binding.

Specific computer software is available in the art to evaluate compound deformation energy and electrostatic interaction. Examples of programs designed for such uses by way of non-limiting example include: Gaussian 92, revision C (M. J. Frisch, Gaussian, Inc., Pittsburgh, Pa., 1992); AMBER, version 4.0 (P. A. Kollman, University of California at San Francisco, 1994); QUANTA/CHARMM (Molecular Simulations, Inc., Burlington, Mass. 1994); and Insight H/Discover (Biosysm Technologies Inc., San Diego, Calif., 1994). These programs may be implemented, for example, using a Silicon Graphics workstation, IRIS 4D/35 or IBM RISC/6000 workstation model 550. Other hardware systems and software packages will be known to those skilled in the art of which the speed and capacity are frequently modified.

Once a candidate binding agent has been selected or designed, as described above, substitutions may then be made in some of its atoms or side groups in order to improve or modify the binding properties. Generally, initial substitutions are conservative, e.g., the replacement group will have approximately the same size, shape, hydrophobicity and charge as the original group. Such substituted binding agents may then be analyzed for efficiency of fit to a cdc14A binding domain by the same computer methods described, above. Other changes may not be conservative and can be used to test groups of differing sizes, charges, and the like.

Using the invention disclosed herein, those of skill in the art may identify binding agents or modulatory agents as inhibitors or activators by computer fitting kinetic data using standard equations according to Segel, I. H., Enzyme Kinetics, J. Wiley &Sons, (1975).

In one aspect, once a test binding agent has been modeled and synthesized, it can be soaked and then co-crystallized with a cdc14A polypeptide. The co-crystallization data comprising atomic coordinates can then be analyzed via computer to generate a 3D image of the test agent interacting or associating with the cdc14A polypeptide. Analysis of the interaction data can lead to the design of a more productive structure-activity-relationship analysis (commonly referred to in the art as “SAR”), or medicinal chemistry. An iterative process of co-crystallization, analysis, further SAR, can greatly enhance the rate at which rational drug design is performed. Described herein are methods of performing “soaks” to obtain co-crystallization data. Further provided are co-crystals of a complex comprising a cdc14A polypeptide and a binding agent.

The crystal structure data provided herein can be used in the design of new or improved binding agents. For example, the cdc14A polypeptide coordinates can be directly compared to the coordinates of similar enzymes that have inhibitors or substrate bound thereto to give an approximation of the way these and related inhibitors might bind to cdc14A. For example, the crystal structure of cdc14A (disclosed) can be overlaid with the crystal structure of cdc14B (see, e.g., EMBO J. 22(14):3524-35, 2003).

Alternatively, computer programs employed in the practice of rational drug design can be used to identify binding agents that reproduce interaction characteristics similar to those found between a cdc14A polypeptide and a co-crystallized binding agent (e.g., a substrate or inhibitor). Furthermore, detailed knowledge of the nature of binding site interactions allows for the modification of binding agents to alter or improve solubility, pharmacokinetics, and the like, without affecting binding activity. Such modifications can be made using known techniques.

Computer programs are widely available that are capable of carrying out the activities necessary to design binding agents using the crystal structure information provided herein. Examples include, but are not limited to, the computer programs listed below:

• • Catalyst Database^STM—an information retrieval program accessing chemical databases such as BioByte Master File, Derwent WDI and ACD;
  • Catalyst/HYPO™—generates models of compounds and hypotheses to explain variations of activity with the structure of binding candidates;
  • Ludi™—fits molecules into the active site of a protein by identifying and matching complementary polar and hydrophobic groups;
  • Leapfrog™—“grows” new ligands using a genetic algorithm with parameters under the control of the user.

In addition, various general purpose machines may be used with programs written in accordance with the teachings herein, or it may be more convenient to construct more specialized apparatus to perform the operations. However, the embodiment will typically be implemented in one or more computer programs executing on programmable systems each comprising at least one processor, at least one data storage system (including volatile and non-volatile memory and/or storage elements), at least one input device, and at least one output device. The program is executed on the processor to perform the functions described herein.

Each such program may be implemented in any desired computer language (including machine, assembly, high level procedural, or object oriented programming languages) to communicate with a computer system. In any case, the language may be a compiled or interpreted language. The computer program will typically be stored on a storage media or device (e.g., ROM, CD-ROM, or magnetic or optical media) readable by a general or special purpose programmable computer, for configuring and operating the computer when the storage media or device is read by the computer to perform the procedures described herein. The system may also be considered to be implemented as a computer-readable storage medium, configured with a computer program, where the storage medium so configured causes a computer to operate in a specific and predefined manner to perform the functions described herein.

Embodiments of the disclosure include systems (e.g., internet based systems), particularly computer systems which store, display and manipulate the coordinate and sequence information described herein. One example of a computer system 100 is illustrated in block diagram form in FIG. 3. As used herein, “a computer system” refers to the hardware components, software components, and data storage components used to analyze the coordinates (see, e.g., Table 2) and sequences such as those set forth in SEQ ID Nos: 2, 4, 6, 8, 10, 12, and Table 2. The computer system 100 typically includes a processor for processing, e.g., data and instructions, accessing and manipulating the sequence data and structural coordinates. The processor 105 can be any well-known type of central processing unit, such as, for example, the Pentium IV from Intel Corporation, or a similar processor from other suppliers such as Sun, Motorola, Compaq, AMD or International Business Machines.

Typically the computer system 100 is a general purpose system that comprises the processor 105 and one or more internal data storage components 110 for storing data, and one or more data retrieving devices for retrieving the data stored on the data storage components. A skilled artisan can readily appreciate that any one of the currently available computer systems are suitable.

In one particular embodiment, the computer system 100 includes a processor 105 connected to a bus which is connected to a main memory 115 (typically implemented as RAM) and one or more internal data storage devices 110, such as a hard drive and/or other computer readable media having data recorded thereon. In some embodiments, the computer system 100 further includes one or more data retrieving means 118 for reading the data stored on the internal data storage means 110. The data retrieving means 118 may represent, for example, a floppy disk drive, a compact disk drive, a magnetic tape drive, or means for connecting to external data-retrieving means, such as ethernet, a modem capable of connection to a remote data storage system (e.g., via the internet), and the like. In some embodiments, the internal data storage means 110 is a removable computer readable medium such as a floppy disk, a compact disk, a magnetic tape, and the like, containing control logic and/or data recorded thereon. The computer system 100 may advantageously include or be programmed by appropriate software for reading the control logic and/or the data from the data storage component once inserted in the data retrieving means or device.

The computer system 100 includes a display means 120 which is used to display output, such as for example a three-dimensional model of a crystalline cdc14A polypeptide, or a complex comprising the crystalline cdc14A polypeptide with a candidate binding agent, to a computer user. It should also be noted that the computer system 100 can be linked to other computer systems 125a-c in a network or wide area network to provide centralized access to the computer system 100.

Software for accessing and processing the coordinates of Table 2 and sequences of SEQ ID Nos:2, 4, 6, 8, 10, 12 and Table 1 (such as search tools, compare tools, modeling tools and the like) may reside in main memory 115 during execution.

According to the disclosure, substrates of cdc14A may include full length tyrosine phosphorylated proteins and polypeptides as well as fragments (e.g., portions), derivatives or analogs thereof that can be phosphorylated at a tyrosine residue and that may, in certain embodiments, also be able to undergo phosphorylation at a serine or a threonine residue. Such fragments, derivatives and analogs include any naturally occurring or artificially engineered cdc14A substrate polypeptide that retains at least the biological function of interacting with a cdc14A as provided herein, for example by forming a complex with a cdc14A polypeptide.

cdc14A polypeptides may be tested for cdc14A activity using any suitable assay, e.g., for p53 and/or APC activity. For example, cdc14A binds p53 and dephosphorylate pSer-315 in vitro (Li et al., J Biol Chem 275:2410-2414, 2002). A recent study demonstrated that cdc14A dephosphorylates the APC regulatory protein Cdh1 in vitro and that dephosphorylated APCCdh1 has activated ubiquitination of cyclin-B1 (Bembenek and Yu, J Biol Chem, 276:48237-48242, 2001). Such assays may be performed in vitro or within a cell-based assay. For example, ³²P-radiolabeled substrate (e.g., p53 or APC) may be used for the kinase reaction, resulting in radiolabeled, activated protein. A cdc14A polypeptide may then be tested (in the presence and absence of an inhibitor) for the ability to dephosphorylate a p53 or APC by contacting the cdc14A polypeptide with the p53 or APC under conditions sufficient to promote dephosporylation of p53 or APC. Dephosphorylation of the APC, for example, may be detected by measuring ubiquitination of cyclin-B1 or measuring the loss of radioactive phosphate groups by (1) gel electrophoresis, followed by autoradiography; (2) the shift in electrophoretic mobility following dephosphorylation; (3) the loss of reactivity with an antibody specific for phosphotyrosine or phosphothreonine; or (4) a phosphoamino acid analysis of the p53 or APC protein. Modulation of a cdc14A activity can be determined by measuring the dephosphorylation activity in the presence and absence of binding agents identified by the methods of the disclosure. For example, a difference in cdc14A polypeptide dephosphorylation of a p53 or APC or a phosphorylated substrate (such as a tyrosine-, serine-, and/or threonine phosphorylated peptide) in the presence of a binding agent that is greater or less than the amount of dephosphorylation observed in the presence of a comparable amount of native human cdc14A is indicative of a binding agent that modulates cdc14A activity. It will be apparent that other substrates (i.e., binding agents) identified by the methods of the disclosure can be assayed in a similar manner as described herein for p53 or APC, or by using methods known in the art.

Candidate binding agents for use in a method of screening for a modulator of cdc14A according to the disclosure may be provided as “libraries” or collections of compounds, compositions or molecules. Such molecules typically include compounds known in the art as “small molecules” and having molecular weights less than 10⁴, less than 10³ and preferably less than 10². For example, candidate binding agents will typically have a molecular weight of 300-1000, typical for small molecule agents. For example, members of a library of test compounds can be administered to a plurality of samples, each containing at least one cdc14A polypeptide as provided herein, and then assayed for their ability to enhance or inhibit cdc14A-mediated dephosphorylation of, or binding to, a substrate. Compounds so identified as capable of modulating cdc14A function (e.g., phosphotyrosine and/or phosphoserine/threonine dephosphorylation) are valuable for potential therapeutic and/or diagnostic purposes, since they may permit treatment and/or detection of diseases associated with cdc14A activity. Such compounds are also valuable in research directed to molecular signaling mechanisms that involve cdc14A, and to refinements in the discovery and development of future cdc14A compounds exhibiting greater specificity.

Candidate binding agents further may be provided as members of a combinatorial library, which includes synthetic agents prepared according to a plurality of predetermined chemical reactions performed in a plurality of reaction vessels. For example, various starting compounds may be prepared employing one or more of solid-phase synthesis, recorded random mix methodologies and recorded reaction split techniques that permit a given constituent to traceably undergo a plurality of permutations and/or combinations of reaction conditions. The resulting products comprise a library that can be screened followed by iterative selection and synthesis procedures, such as a synthetic combinatorial library of peptides or other compositions that may include small molecules as provided herein (see e.g., PCT/US94/08542, EP 0774464, U.S. Pat. No. 5,798,035, U.S. Pat. No. 5,789,172, U.S. Pat. No. 5,751,629, which are hereby incorporated by reference in their entireties). Those having ordinary skill in the art will appreciate that a diverse assortment of such libraries may be prepared according to established procedures, and tested using cdc14A according to the present disclosure, by first modeling similar compounds and then testing likely candidates in vitro.

In certain embodiments, binding agents may be identified by combining a candidate binding agent with a cdc14A polypeptide in vitro or in vivo, and evaluating the effect of the candidate binding agent on the cdc14A phosphatase activity using, for example, a representative assay described herein. An increase or decrease in phosphatase activity can be measured by performing a representative assay provided herein in the presence and absence of a candidate binding agent. Briefly, a candidate binding agent is modeled using the structural coordinates of a catalytic domain of cdc14A. Likely candidate binding agents that interact in silico may be included in a mixture of active cdc14A polypeptide and substrate (e.g., a phosphorylated p53 or APC), with or without pre-incubation with one or more components of the mixture. The effect of the agent on cdc14A activity may then be evaluated by quantifying the loss of phosphate from the substrate, and comparing the loss with that achieved using cdc14A without the addition of a candidate binding agent.

Cdc14A activity may also be measured in whole cells transfected with a reporter gene whose expression is dependent upon the activation of an appropriate substrate. For example, appropriate cells (i.e., cells that express cdc14A) may be transfected with a substrate-dependent promoter linked to a reporter gene. In such a system, expression of the reporter gene (which may be readily detected using methods well known to those of ordinary skill in the art) depends upon activation of substrate. Dephosphorylation of substrate may be detected based on a decrease in reporter activity. Candidate modulating agents may be added to such a system, as described above, to evaluate their effect on cdc14A activity.

In another aspect, once an agent has been identified as a suitable binding agent using the in silico methods described herein, standard binding assays such as yeast two-hybrid screens, phage display and affinity techniques can be used to determine in vitro the ability of the binding agent to interact with cdc14A in vitro. Such techniques may be performed using routine protocols, which are well known to those having ordinary skill in the art (see, e.g., Bartel et al., In Cellular Interactions in Development: A Practical Approach, D. A. Harley, ed., Oxford University Press (Oxford, UK), pp. 153-179, 1993).

The invention will now be described by reference to the following non-limiting examples.

EXAMPLES

Methods of Crystallization. Crystals were grown by the hanging-drop vapor-diffusion method. Purified cdc14A (10-339aa of SEQ ID NO:2) protein was concentrated to ˜10 mg/ml (0.33 mM) in a buffer containing 700 mM NaCl, 20 mM Tris (7.2), 1 mM EDTA, and 2 mM DTT, and stored at −80° C. Drops consisting of 2 μl of protein solution were mixed with 2 μl of reservoir solution (200-250 mM MgCl₂, 50 mM Tris (8.0), 16-18% PEG 8000, 5 mM DTT) on a coverslip. The coverslip was inverted and allowed to equilibrate over a 0.5 ml reservoir at 23° C. A greased seal isolated the hanging drop and the reservoir solution from the exterior environment. Over the course of several days the hanging drop equilibrated to the same osmotic strength as the reservoir and small protein crystals appeared (80×80×400 mm³) After crystals were identified and selected for exposure to X-rays, they were transferred first to a cryo-solution and then flash-cooled. The cryo-solution is identical to the reservoir solution except that the PEG 8000 is increased ˜5% and 10% 2-methyl-2,4-pentanediol (MPD) is included to impede ice formation.

The crystals belong to the space group P₂₁₂₁₂, have unit cell dimensions of a=74 Å, b=81 Å, c=69 Å, and contain one protein molecule per asymmetric unit.

The active site is comprised of a central loop, amino acid residues 277 to 285 (atom 2205 through atom 2268 as shown in Table 2), which contains the catalytic cysteine 278, as well as several additional loop sections that surround the central loop and provide residues for making specific contacts to substrates and inhibitors. The additional loop sections are comprised of residues 46 to 49, 131 to 135, 173 to 181, 191 to 195, 204 to 206, 227 to 229, 249 to 253, and 312 to 320 (see, e.g., FIG. 2A-2C).

Methods for soaking candidate binding agents into the active site: Crystals were stabilized in a solution comprising approximately 50 mM Tris (8.0), 25 mM MgCl₂, 50 mM NaCl, 5 mM DTT, 10% MPD, and 20% PEG8000 overnight. These crystals were then transferred to an identical solution that contains about 4-10 mM of candidate binding agent. After equilibrating for several hours in the candidate binding agent-containing solution, crystals were flash-cooled by plunging into liquid nitrogen. X-ray diffraction data was collected on a Raxis IV using 1.54 Å wavelength CuKα X-rays generated from a rotating anode. Crystals were mounted in cryoloops and maintained at about 150 K (−120° C.) throughout the data collections in a cryo stream. After the diffraction data were collected, the images were processed and reduced to a scaled and indexed set of unique intensities. The protein structural content of the unit cell was then determined by molecular replacement technique. For cdc14A, the initial search model is the homologous protein cdc14B (Pdb accession number:1OHC). After the correct rotation and translation has been applied to the search model, subsequent rounds of conventional refinement and manual model building are performed.

COMPND	- - -
REMARK	3
REMARK	3	REFINEMENT.
REMARK	3	PROGRAM   : REFMAC 5.1.24
REMARK	3
REMARK	3	REFINEMENT TARGET: MAXIMUM LIKELIHOOD
REMARK	3
REMARK	3	DATA USED IN REFINEMENT.
REMARK	3	RESOLUTION RANGE HIGH	(ANGSTROMS)	:   2.40
REMARK	3	RESOLUTION RANGE LOW	(ANGSTROMS)	:  30.00
REMARK	3	DATA CUTOFF	(SIGMA(F))	: NONE
REMARK	3	COMPLETENESS FOR RANGE	(%)	:   90.90
REMARK	3	NUMBER OF REFLECTIONS		:   14069
REMARK	3
REMARK	3	FIT TO DATA USED IN REFINEMENT.
REMARK	3	CROSS-VALIDATION METHOD	: THROUGHOUT
REMARK	3	FREE R VALUE TEST SET SELECTION	: RANDOM
REMARK	3	R VALUE	(WORKING + TEST SET)	: 0.19653
REMARK	3	R VALUE	(WORKING SET)	:  0.19159
REMARK	3	FREE R VALUE	:  0.29120
REMARK	3	FREE R VALUE TEST SET SIZE	(%)	:  5.0
REMARK	3	FREE R VALUE TEST SET COUNT		:  747
REMARK	3
REMARK	3	FIT IN THE HIGHEST RESOLUTION BIN.
REMARK	3	TOTAL NUMBER OF BINS USED	:    20
REMARK	3	BIN RESOLUTION RANGE HIGH	:  2.400
REMARK	3	BIN RESOLUTION RANGE LOW	:  2.462
REMARK	3	REFLECTION IN BIN	(WORKING SET)	:    602
REMARK	3	BIN R VALUE	(WORKING SET)	:  0.207
REMARK	3	BIN FREE R VALUE SET COUNT	:    27
REMARK	3	BIN FREE R VALUE	:  0.290
REMARK	3
REMARK	3	NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK	3	ALL ATOMS	:   2796
REMARK	3
REMARK	3	B VALUES.
REMARK	3	FROM WILSON PLOT	(A**2)	: NULL
REMARK	3	MEAN B VALUE	(OVERALL, A**2)	:  32.190
REMARK	3	OVERALL ANISOTROPIC B VALUE.
REMARK	3	B11 (A**2):    2.14
REMARK	3	B22 (A**2):  −1.73
REMARK	3	B33 (A**2):  −0.41
REMARK	3	B12 (A**2):    0.00
REMARK	3	B13 (A**2):    0.00
REMARK	3	B23 (A**2):    0.00
REMARK	3
REMARK	3	ESTIMATED OVERALL COORDINATE ERROR.
REMARK	3	ESU BASED ON R VALUE	(A):	0.475
REMARK	3	ESU BASED ON FREE R VALUE	(A):	0.327
REMARK	3	ESU BASED ON MAXIMUM LIKELIHOOD	(A):	0.209
REMARK	3	ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD	(A**2):	9.079
REMARK	3
REMARK	3	CORRELATION COEFFICIENTS.
REMARK	3	CORRELATION COEFFICIENT FO-FC	:  0.934
REMARK	3	CORRELATION COEFFICIENT FO-FC FREE	:  0.834
REMARK	3
REMARK	3	RMS DEVIATIONS FROM IDEAL VALUES	COUNT	RMS	WEIGHT
REMARK	3	BOND LENGTHS REFINED ATOMS	(A):	2783 ;	0.023 ;	0.021
REMARK	3	BOND ANGLES REFINED ATOMS	(DEGREES):	3763 ;	1.929 ;	1.935
REMARK	3	TORSION ANGLES, PERIOD 1	(DEGREES):	329 ;	8.319 ;	5.000
REMARK	3	CHIRAL-CENTER RESTRAINTS	(A**3):	387 ;	0.145 ;	0.200
REMARK	3	GENERAL PLANES REFINED ATOMS	(A):	2167 ;	0.008 ;	0.020
REMARK	3	NON-BONDED CONTACTS REFINED ATOMS	(A):	1307 ;	0.228 ;	0.200
REMARK	3	H-BOND (X...Y) REFINED ATOMS	(A):	136 ;	0.162 ;	0.200
REMARK	3	SYMMETRY VDW REFINED ATOMS	(A):	45 ;	0.238 ;	0.200
REMARK	3	SYMMETRY H-BOND REFINED ATOMS	(A):	7 ;	0.095 ;	0.200
REMARK	3
REMARK	3	ISOTROPIC THERMAL FACTOR RESTRAINTS.		COUNT	RMS	WEIGHT
REMARK	3	MAIN-CHAIN BOND REFINED ATOMS	(A**2):	1643 ;	0.993 ;	1.500
REMARK	3	MAIN-CHAIN ANGLE REFINED ATOMS	(A**2):	2645 ;	1.878 ;	2.000
REMARK	3	SIDE-CHAIN BOND REFINED ATOMS	(A**2):	1140 ;	2.923 ;	3.000
REMARK	3	SIDE-CHAIN ANGLE REFINED ATOMS	(A**2):	1118 ;	4.595 ;	4.500
REMARK	3
REMARK	3	NCS RESTRAINTS STATISTICS
REMARK	3	NUMBER OF NCS GROUPS: NULL
REMARK	3
REMARK	3
REMARK	3	TLS DETAILS
REMARK	3	NUMBER OF TLS GROUPS: NULL
REMARK	3
REMARK	3
REMARK	3	BULK SOLVENT MODELLING.
REMARK	3	METHOD USED: BABINET MODEL WITH MASK
REMARK	3	PARAMETERS FOR MASK CALCULATION
REMARK	3	VDW PROBE RADIUS	:  1.40
REMARK	3	ION PROBE RADIUS	:  0.80
REMARK	3	SHRINKAGE RADIUS	:  0.80
REMARK	3
REMARK	3	OTHER REFINEMENT REMARKS: NULL
REMARK	3
CISPEP	1	GLY A	53  PRO A   54     0.00
CISPEP	2	ASN A	123  PRO A  124     0.00
CRYST1	72.011  81.064  68.759  90.00  90.00 90.00 P 21 21 2
SCALE1	0.013887  0.000000  0.000000   0.00000
SCALE2	0.000000  0.012336  0.000000   0.00000
SCALE3	0.000000  0.000000  0.014544   0.00000
ATOM	1	N	SER	A	9	19.662	57.726	8.709	1.00	62.15	N
ATOM	2	CA	SER	A	9	18.895	58.913	9.205	1.00	61.84	C
ATOM	3	CB	SER	A	9	18.424	59.804	8.019	1.00	62.25	C
ATOM	4	OG	SER	A	9	17.775	59.048	6.990	1.00	61.94	O
ATOM	5	C	SER	A	9	17.716	58.464	10.113	1.00	61.37	C
ATOM	6	O	SER	A	9	16.630	58.071	9.604	1.00	61.58	O
ATOM	7	N	GLY	A	10	17.954	58.521	11.438	1.00	60.06	N
ATOM	8	CA	GLY	A	10	17.016	58.110	12.492	1.00	57.88	C
ATOM	9	C	GLY	A	10	17.699	57.490	13.741	1.00	56.74	C
ATOM	10	O	GLY	A	10	18.309	58.266	14.525	1.00	56.92	O
ATOM	11	N	ALA	A	11	17.638	56.120	13.862	1.00	54.20	N
ATOM	12	CA	ALA	A	11	17.996	55.246	15.021	1.00	50.29	C
ATOM	13	CB	ALA	A	11	16.715	54.774	15.653	1.00	49.91	C
ATOM	14	C	ALA	A	11	18.877	53.990	14.658	1.00	48.23	C
ATOM	15	O	ALA	A	11	18.785	53.545	13.517	1.00	48.84	O
ATOM	16	N	CYS	A	12	19.749	53.503	15.591	1.00	44.24	N
ATOM	17	CA	CYS	A	12	20.292	52.067	15.817	1.00	39.99	C
ATOM	18	CB	CYS	A	12	19.195	50.993	16.014	1.00	39.88	C
ATOM	19	SG	CYS	A	12	18.219	50.858	17.556	1.00	31.25	S
ATOM	20	C	CYS	A	12	21.502	51.373	15.079	1.00	38.96	C
ATOM	21	O	CYS	A	12	21.337	50.493	14.232	1.00	38.11	O
ATOM	22	N	GLU	A	13	22.714	51.673	15.506	1.00	37.26	N
ATOM	23	CA	GLU	A	13	23.906	51.314	14.742	1.00	37.01	C
ATOM	24	CB	GLU	A	13	24.893	52.482	14.724	1.00	36.96	C
ATOM	25	CG	GLU	A	13	26.295	52.184	14.214	1.00	39.82	C
ATOM	26	CD	GLU	A	13	27.190	53.437	14.288	1.00	45.97	C
ATOM	27	OE1	GLU	A	13	26.863	54.478	13.653	1.00	46.25	O
ATOM	28	OE2	GLU	A	13	28.212	53.410	14.991	1.00	46.97	O
ATOM	29	C	GLU	A	13	24.576	50.038	15.232	1.00	36.01	C
ATOM	30	O	GLU	A	13	24.823	49.874	16.433	1.00	34.64	O
ATOM	31	N	PHE	A	14	24.857	49.148	14.270	1.00	35.10	N
ATOM	32	CA	PHE	A	14	25.503	47.889	14.547	1.00	34.48	C
ATOM	33	CB	PHE	A	14	24.615	46.724	14.111	1.00	33.19	C
ATOM	34	CG	PHE	A	14	23.643	46.357	15.141	1.00	29.91	C
ATOM	35	CD1	PHE	A	14	22.472	47.077	15.295	1.00	27.77	C
ATOM	36	CE1	PHE	A	14	21.578	46.766	16.309	1.00	24.54	C
ATOM	37	CZ	PHE	A	14	21.873	45.736	17.185	1.00	22.84	C
ATOM	38	CE2	PHE	A	14	23.035	45.021	17.043	1.00	24.99	C
ATOM	39	CD2	PHE	A	14	23.923	45.331	16.039	1.00	27.65	C
ATOM	40	C	PHE	A	14	26.884	47.846	13.915	1.00	35.81	C
ATOM	41	O	PHE	A	14	27.818	47.369	14.531	1.00	35.24	O
ATOM	42	N	MET	A	15	27.008	48.337	12.683	1.00	37.23	N
ATOM	43	CA	MET	A	15	28.341	48.638	12.131	1.00	39.18	C
ATOM	44	CB	MET	A	15	28.736	47.670	11.043	1.00	38.92	C
ATOM	45	CG	MET	A	15	28.616	46.269	11.485	1.00	40.64	C
ATOM	46	SD	MET	A	15	28.426	45.291	10.021	1.00	49.13	S
ATOM	47	CE	MET	A	15	30.200	45.157	9.457	1.00	45.40	C
ATOM	48	C	MET	A	15	28.389	50.066	11.630	1.00	39.77	C
ATOM	49	O	MET	A	15	27.523	50.473	10.860	1.00	39.63	O
ATOM	50	N	LYS	A	16	29.372	50.825	12.114	1.00	41.22	N
ATOM	51	CA	LYS	A	16	29.562	52.237	11.746	1.00	42.40	C
ATOM	52	CB	LYS	A	16	30.999	52.657	12.134	1.00	43.34	C
ATOM	53	CG	LYS	A	16	31.249	54.158	12.245	1.00	46.60	C
ATOM	54	CD	LYS	A	16	32.355	54.448	13.275	1.00	54.40	C
ATOM	55	CE	LYS	A	16	31.864	54.266	14.760	1.00	58.20	C
ATOM	56	NZ	LYS	A	16	31.580	55.586	15.396	1.00	60.01	N
ATOM	57	C	LYS	A	16	29.352	52.436	10.236	1.00	41.31	C
ATOM	58	O	LYS	A	16	30.056	51.787	9.423	1.00	41.42	O
ATOM	59	N	ASP	A	17	28.360	53.265	9.877	1.00	39.88	N
ATOM	60	CA	ASP	A	17	28.080	53.652	8.468	1.00	39.08	C
ATOM	61	CB	ASP	A	17	29.237	54.491	7.868	1.00	38.82	C
ATOM	62	CG	ASP	A	17	29.575	55.764	8.724	1.00	42.67	C
ATOM	63	OD1	ASP	A	17	28.665	56.597	9.012	1.00	42.03	O
ATOM	64	OD2	ASP	A	17	30.733	55.990	9.170	1.00	43.25	O
ATOM	65	C	ASP	A	17	27.685	52.499	7.498	1.00	37.98	C
ATOM	66	O	ASP	A	17	27.609	52.697	6.276	1.00	38.24	O
ATOM	67	N	ARG	A	18	27.444	51.307	8.034	1.00	35.23	N
ATOM	68	CA	ARG	A	18	27.212	50.166	7.195	1.00	33.76	C
ATOM	69	CB	ARG	A	18	28.509	49.330	7.056	1.00	33.09	C
ATOM	70	CG	ARG	A	18	28.327	47.842	6.773	1.00	33.66	C
ATOM	71	CD	ARG	A	18	28.970	47.295	5.486	1.00	31.95	C
ATOM	72	NE	ARG	A	18	28.129	47.608	4.365	1.00	28.78	N
ATOM	73	CZ	ARG	A	18	27.983	46.890	3.261	1.00	28.49	C
ATOM	74	NH1	ARG	A	18	28.643	45.725	3.062	1.00	21.52	N
ATOM	75	NH2	ARG	A	18	27.123	47.376	2.346	1.00	25.02	N
ATOM	76	C	ARG	A	18	25.953	49.360	7.611	1.00	32.55	C
ATOM	77	O	ARG	A	18	25.181	48.993	6.756	1.00	31.32	O
ATOM	78	N	LEU	A	19	25.764	49.101	8.913	1.00	31.85	N
ATOM	79	CA	LEU	A	19	24.659	48.290	9.398	1.00	30.15	C
ATOM	80	CB	LEU	A	19	25.105	46.841	9.648	1.00	30.29	C
ATOM	81	CG	LEU	A	19	24.038	45.809	10.157	1.00	29.73	C
ATOM	82	CD1	LEU	A	19	22.992	45.378	9.117	1.00	22.51	C
ATOM	83	CD2	LEU	A	19	24.693	44.575	10.850	1.00	25.72	C
ATOM	84	C	LEU	A	19	23.798	48.872	10.549	1.00	29.89	C
ATOM	85	O	LEU	A	19	24.252	49.223	11.655	1.00	29.50	O
ATOM	86	N	TYR	A	20	22.515	48.953	10.261	1.00	29.58	N
ATOM	87	CA	TYR	A	20	21.587	49.655	11.106	1.00	28.97	C
ATOM	88	CB	TYR	A	20	21.235	50.989	10.486	1.00	29.76	C
ATOM	89	CG	TYR	A	20	22.383	51.951	10.535	1.00	34.15	C
ATOM	90	CD1	TYR	A	20	23.289	52.025	9.481	1.00	34.82	C
ATOM	91	CE1	TYR	A	20	24.356	52.865	9.536	1.00	36.86	C
ATOM	92	CZ	TYR	A	20	24.558	53.665	10.644	1.00	37.89	C
ATOM	93	OH	TYR	A	20	25.644	54.493	10.650	1.00	43.53	O
ATOM	94	CE2	TYR	A	20	23.697	53.637	11.707	1.00	37.99	C
ATOM	95	CD2	TYR	A	20	22.594	52.762	11.654	1.00	37.46	C
ATOM	96	C	TYR	A	20	20.347	48.841	11.214	1.00	27.82	C
ATOM	97	O	TYR	A	20	19.998	48.082	10.283	1.00	27.77	O
ATOM	98	N	PHE	A	21	19.701	49.001	12.364	1.00	26.31	N
ATOM	99	CA	PHE	A	21	18.402	48.437	12.644	1.00	25.46	C
ATOM	100	CB	PHE	A	21	18.436	47.516	13.891	1.00	24.90	C
ATOM	101	CG	PHE	A	21	17.058	47.019	14.320	1.00	25.37	C
ATOM	102	CD1	PHE	A	21	16.287	46.179	13.455	1.00	25.42	C
ATOM	103	CE1	PHE	A	21	14.998	45.749	13.806	1.00	25.23	C
ATOM	104	CZ	PHE	A	21	14.460	46.141	15.061	1.00	24.11	C
ATOM	105	CE2	PHE	A	21	15.231	46.987	15.944	1.00	23.38	C
ATOM	106	CD2	PHE	A	21	16.509	47.413	15.560	1.00	24.10	C
ATOM	107	C	PHE	A	21	17.425	49.581	12.851	1.00	24.92	C
ATOM	108	O	PHE	A	21	17.685	50.451	13.662	1.00	24.89	O
ATOM	109	N	ALA	A	22	16.303	49.606	12.149	1.00	24.43	N
ATOM	110	CA	ALA	A	22	15.365	50.669	12.451	1.00	26.30	C
ATOM	111	CB	ALA	A	22	15.567	51.901	11.493	1.00	25.37	C
ATOM	112	C	ALA	A	22	13.877	50.254	12.553	1.00	27.20	C
ATOM	113	O	ALA	A	22	13.445	49.274	11.955	1.00	28.31	O
ATOM	114	N	THR	A	23	13.109	51.013	13.328	1.00	28.54	N
ATOM	115	CA	THR	A	23	11.656	50.837	13.407	1.00	29.96	C
ATOM	116	CB	THR	A	23	11.177	50.774	14.932	1.00	29.64	C
ATOM	117	OG1	THR	A	23	11.735	49.620	15.571	1.00	31.21	O
ATOM	118	CG2	THR	A	23	9.688	50.559	15.049	1.00	27.42	C
ATOM	119	C	THR	A	23	11.019	52.004	12.656	1.00	30.17	C
ATOM	120	O	THR	A	23	11.219	53.168	13.005	1.00	30.14	O
ATOM	121	N	LEU	A	24	10.255	51.689	11.627	1.00	32.58	N
ATOM	122	CA	LEU	A	24	9.689	52.705	10.725	1.00	34.66	C
ATOM	123	CB	LEU	A	24	10.284	52.578	9.295	1.00	34.15	C
ATOM	124	CG	LEU	A	24	11.815	52.805	9.266	1.00	33.44	C
ATOM	125	CD1	LEU	A	24	12.509	52.514	7.910	1.00	35.21	C
ATOM	126	CD2	LEU	A	24	12.229	54.149	9.819	1.00	28.56	C
ATOM	127	C	LEU	A	24	8.197	52.563	10.682	1.00	37.23	C
ATOM	128	O	LEU	A	24	7.668	51.437	10.576	1.00	36.39	O
ATOM	129	N	ARG	A	25	7.535	53.717	10.828	1.00	40.96	N
ATOM	130	CA	ARG	A	25	6.091	53.888	10.613	1.00	43.72	C
ATOM	131	CB	ARG	A	25	5.652	55.304	10.977	1.00	44.00	C
ATOM	132	CG	ARG	A	25	6.337	55.881	12.265	1.00	49.11	C
ATOM	133	CD	ARG	A	25	5.399	56.505	13.374	1.00	55.41	C
ATOM	134	NE	ARG	A	25	4.743	55.546	14.298	1.00	59.34	N
ATOM	135	CZ	ARG	A	25	3.751	54.675	13.984	1.00	61.86	C
ATOM	136	NH1	ARG	A	25	3.260	54.555	12.738	1.00	62.51	N
ATOM	137	NH2	ARG	A	25	3.251	53.900	14.938	1.00	61.08	N
ATOM	138	C	ARG	A	25	5.735	53.570	9.175	1.00	45.25	C
ATOM	139	O	ARG	A	25	4.654	53.093	8.894	1.00	46.11	O
ATOM	140	N	ASN	A	26	6.640	53.778	8.233	1.00	47.16	N
ATOM	141	CA	ASN	A	26	6.303	53.318	6.876	1.00	49.13	C
ATOM	142	CB	ASN	A	26	5.822	54.499	5.997	1.00	50.22	C
ATOM	143	CG	ASN	A	26	4.648	55.255	6.632	1.00	53.43	C
ATOM	144	OD1	ASN	A	26	3.581	54.657	6.904	1.00	56.04	O
ATOM	145	ND2	ASN	A	26	4.847	56.551	6.901	1.00	51.11	N
ATOM	146	C	ASN	A	26	7.401	52.538	6.181	1.00	48.82	C
ATOM	147	O	ASN	A	26	8.566	52.629	6.548	1.00	49.78	O
ATOM	148	N	ARG	A	27	7.006	51.790	5.169	1.00	48.67	N
ATOM	149	CA	ARG	A	27	7.919	51.136	4.261	1.00	49.18	C
ATOM	150	CB	ARG	A	27	7.101	50.408	3.191	1.00	50.10	C
ATOM	151	CG	ARG	A	27	7.383	48.919	3.034	1.00	54.74	C
ATOM	152	CD	ARG	A	27	7.980	48.564	1.650	1.00	61.77	C
ATOM	153	NE	ARG	A	27	7.001	48.770	0.578	1.00	67.79	N
ATOM	154	CZ	ARG	A	27	6.927	49.840	−0.236	1.00	69.53	C
ATOM	155	NH1	ARG	A	27	7.793	50.867	−0.157	1.00	66.65	N
ATOM	156	NH2	ARG	A	27	5.961	49.863	−1.155	1.00	70.95	N
ATOM	157	C	ARG	A	27	8.842	52.189	3.620	1.00	48.14	C
ATOM	158	O	ARG	A	27	8.368	53.159	3.015	1.00	48.52	O
ATOM	159	N	PRO	A	28	10.156	52.031	3.795	1.00	47.23	N
ATOM	160	CA	PRO	A	28	11.137	52.841	3.061	1.00	45.88	C
ATOM	161	CB	PRO	A	28	12.369	52.766	3.974	1.00	46.00	C
ATOM	162	CG	PRO	A	28	12.257	51.416	4.642	1.00	44.87	C
ATOM	163	CD	PRO	A	28	10.817	51.091	4.733	1.00	46.57	C
ATOM	164	C	PRO	A	28	11.453	52.235	1.678	1.00	45.12	C
ATOM	165	O	PRO	A	28	11.368	51.021	1.496	1.00	44.72	O
ATOM	166	N	LYS	A	29	11.805	53.068	0.712	1.00	44.59	N
ATOM	167	CA	LYS	A	29	12.299	52.550	−0.566	1.00	44.92	C
ATOM	168	CB	LYS	A	29	11.773	53.369	−1.774	1.00	46.13	C
ATOM	169	CG	LYS	A	29	10.343	54.003	−1.581	1.00	52.89	C
ATOM	170	CD	LYS	A	29	10.174	55.427	−2.237	1.00	60.91	C
ATOM	171	CE	LYS	A	29	9.219	56.355	−1.404	1.00	64.61	C
ATOM	172	NZ	LYS	A	29	9.908	57.432	−0.555	1.00	64.43	N
ATOM	173	C	LYS	A	29	13.837	52.575	−0.512	1.00	42.59	C
ATOM	174	O	LYS	A	29	14.430	53.579	−0.064	1.00	42.14	O
ATOM	175	N	SER	A	30	14.447	51.457	−0.921	1.00	40.10	N
ATOM	176	CA	SER	A	30	15.899	51.322	−1.078	1.00	38.26	C
ATOM	177	CB	SER	A	30	16.263	49.963	−1.670	1.00	37.56	C
ATOM	178	OG	SER	A	30	16.339	48.939	−0.698	1.00	37.00	O
ATOM	179	C	SER	A	30	16.368	52.426	−2.036	1.00	37.84	C
ATOM	180	O	SER	A	30	15.693	52.716	−3.026	1.00	36.80	O
ATOM	181	N	THR	A	31	17.485	53.068	−1.719	1.00	36.75	N
ATOM	182	CA	THR	A	31	18.079	53.982	−2.669	1.00	35.89	C
ATOM	183	CB	THR	A	31	18.330	55.358	−2.076	1.00	36.18	C
ATOM	184	OG1	THR	A	31	19.340	55.241	−1.066	1.00	37.03	O
ATOM	185	CG2	THR	A	31	17.064	55.984	−1.421	1.00	34.55	C
ATOM	186	C	THR	A	31	19.413	53.518	−3.181	1.00	35.24	C
ATOM	187	O	THR	A	31	19.951	52.482	−2.803	1.00	35.24	O
ATOM	188	N	VAL	A	32	19.920	54.341	−4.084	1.00	35.00	N
ATOM	189	CA	VAL	A	32	21.309	54.400	−4.513	1.00	33.98	C
ATOM	190	CB	VAL	A	32	21.386	55.671	−5.435	1.00	35.04	C
ATOM	191	CG1	VAL	A	32	22.387	56.741	−4.959	1.00	36.43	C
ATOM	192	CG2	VAL	A	32	21.447	55.307	−6.917	1.00	33.99	C
ATOM	193	C	VAL	A	32	22.300	54.370	−3.298	1.00	32.70	C
ATOM	194	O	VAL	A	32	23.304	53.721	−3.338	1.00	32.40	O
ATOM	195	N	ASN	A	33	21.969	54.995	−2.183	1.00	31.77	N
ATOM	196	CA	ASN	A	33	22.841	54.937	−1.007	1.00	31.55	C
ATOM	197	CB	ASN	A	33	22.961	56.344	−0.418	1.00	31.36	C
ATOM	198	CG	ASN	A	33	23.644	57.297	−1.395	1.00	34.53	C
ATOM	199	OD1	ASN	A	33	24.854	57.135	−1.701	1.00	35.37	O
ATOM	200	ND2	ASN	A	33	22.870	58.231	−1.954	1.00	34.78	N
ATOM	201	C	ASN	A	33	22.511	53.918	0.110	1.00	31.31	C
ATOM	202	O	ASN	A	33	23.401	53.577	0.928	1.00	31.11	O
ATOM	203	N	THR	A	34	21.253	53.444	0.141	1.00	30.05	N
ATOM	204	CA	THR	A	34	20.762	52.618	1.229	1.00	29.45	C
ATOM	205	CB	THR	A	34	19.990	53.464	2.250	1.00	28.90	C
ATOM	206	OG1	THR	A	34	20.795	54.563	2.654	1.00	30.20	O
ATOM	207	CG2	THR	A	34	19.828	52.723	3.551	1.00	29.93	C
ATOM	208	C	THR	A	34	19.865	51.517	0.737	1.00	28.85	C
ATOM	209	O	THR	A	34	18.903	51.782	0.019	1.00	30.03	O
ATOM	210	N	HIS	A	35	20.199	50.296	1.149	1.00	27.91	N
ATOM	211	CA	HIS	A	35	19.373	49.098	1.070	1.00	27.08	C
ATOM	212	CB	HIS	A	35	20.285	47.883	0.853	1.00	27.24	C
ATOM	213	CG	HIS	A	35	19.546	46.598	0.638	1.00	27.50	C
ATOM	214	ND1	HIS	A	35	18.851	46.324	−0.519	1.00	29.10	N
ATOM	215	CE1	HIS	A	35	18.294	45.127	−0.431	1.00	27.39	C
ATOM	216	NE2	HIS	A	35	18.618	44.608	0.740	1.00	27.15	N
ATOM	217	CD2	HIS	A	35	19.381	45.516	1.438	1.00	27.12	C
ATOM	218	C	HIS	A	35	18.577	48.869	2.375	1.00	27.25	C
ATOM	219	O	HIS	A	35	19.155	48.627	3.463	1.00	27.25	O
ATOM	220	N	TYR	A	36	17.257	48.917	2.265	1.00	26.68	N
ATOM	221	CA	TYR	A	36	16.356	48.562	3.368	1.00	26.09	C
ATOM	222	CB	TYR	A	36	15.184	49.481	3.394	1.00	24.96	C
ATOM	223	CG	TYR	A	36	15.542	50.915	3.670	1.00	25.94	C
ATOM	224	CD1	TYR	A	36	15.705	51.840	2.617	1.00	24.06	C
ATOM	225	CE1	TYR	A	36	16.037	53.140	2.881	1.00	21.69	C
ATOM	226	CZ	TYR	A	36	16.180	53.564	4.191	1.00	24.35	C
ATOM	227	OH	TYR	A	36	16.479	54.880	4.463	1.00	23.26	O
ATOM	228	CE2	TYR	A	36	16.004	52.686	5.254	1.00	23.47	C
ATOM	229	CD2	TYR	A	36	15.708	51.367	4.980	1.00	23.94	C
ATOM	230	C	TYR	A	36	15.797	47.164	3.136	1.00	26.98	C
ATOM	231	O	TYR	A	36	15.430	46.828	1.985	1.00	26.24	O
ATOM	232	N	PHE	A	37	15.770	46.327	4.193	1.00	26.52	N
ATOM	233	CA	PHE	A	37	15.034	45.055	4.088	1.00	26.46	C
ATOM	234	CB	PHE	A	37	15.945	43.897	3.671	1.00	25.81	C
ATOM	235	CG	PHE	A	37	16.855	43.383	4.799	1.00	29.24	C
ATOM	236	CD1	PHE	A	37	16.544	42.179	5.484	1.00	29.15	C
ATOM	237	CE1	PHE	A	37	17.374	41.719	6.526	1.00	30.92	C
ATOM	238	CZ	PHE	A	37	18.537	42.487	6.909	1.00	28.21	C
ATOM	239	CE2	PHE	A	37	18.831	43.676	6.233	1.00	26.00	C
ATOM	240	CD2	PHE	A	37	18.002	44.118	5.194	1.00	26.66	C
ATOM	241	C	PHE	A	37	14.300	44.768	5.390	1.00	26.04	C
ATOM	242	O	PHE	A	37	14.781	45.116	6.466	1.00	27.71	O
ATOM	243	N	SER	A	38	13.147	44.123	5.283	1.00	25.44	N
ATOM	244	CA	SER	A	38	12.383	43.673	6.432	1.00	23.69	C
ATOM	245	CB	SER	A	38	11.005	44.314	6.419	1.00	23.14	C
ATOM	246	OG	SER	A	38	10.202	43.780	7.443	1.00	19.48	O
ATOM	247	C	SER	A	38	12.227	42.161	6.353	1.00	24.13	C
ATOM	248	O	SER	A	38	12.267	41.604	5.273	1.00	23.27	O
ATOM	249	N	ILE	A	39	12.035	41.488	7.491	1.00	23.83	N
ATOM	250	CA	ILE	A	39	11.744	40.056	7.442	1.00	22.52	C
ATOM	251	CB	ILE	A	39	12.930	39.219	8.074	1.00	23.28	C
ATOM	252	CG1	ILE	A	39	13.304	39.723	9.472	1.00	20.65	C
ATOM	253	CD1	ILE	A	39	12.187	39.574	10.548	1.00	17.20	C
ATOM	254	CG2	ILE	A	39	14.174	39.251	7.193	1.00	21.36	C
ATOM	255	C	ILE	A	39	10.440	39.766	8.160	1.00	22.79	C
ATOM	256	O	ILE	A	39	10.094	38.601	8.389	1.00	23.13	O
ATOM	257	N	ASP	A	40	9.731	40.829	8.530	1.00	23.09	N
ATOM	258	CA	ASP	A	40	8.484	40.748	9.305	1.00	24.11	C
ATOM	259	CB	ASP	A	40	7.845	42.154	9.486	1.00	22.64	C
ATOM	260	CG	ASP	A	40	8.597	43.036	10.534	1.00	24.02	C
ATOM	261	OD1	ASP	A	40	9.618	42.611	11.201	1.00	20.71	O
ATOM	262	OD2	ASP	A	40	8.217	44.200	10.760	1.00	26.51	O
ATOM	263	C	ASP	A	40	7.477	39.778	8.664	1.00	25.87	C
ATOM	264	O	ASP	A	40	6.740	39.053	9.392	1.00	26.77	O
ATOM	265	N	GLU	A	41	7.447	39.756	7.325	1.00	26.73	N
ATOM	266	CA	GLU	A	41	6.481	38.952	6.567	1.00	27.93	C
ATOM	267	CB	GLU	A	41	5.890	39.750	5.414	1.00	28.29	C
ATOM	268	CG	GLU	A	41	4.935	40.839	5.907	1.00	35.78	C
ATOM	269	CD	GLU	A	41	3.728	40.239	6.627	1.00	43.85	C
ATOM	270	OE1	GLU	A	41	3.533	40.486	7.848	1.00	46.69	O
ATOM	271	OE2	GLU	A	41	2.974	39.495	5.958	1.00	49.53	O
ATOM	272	C	GLU	A	41	7.159	37.740	6.044	1.00	27.13	C
ATOM	273	O	GLU	A	41	6.571	36.912	5.360	1.00	27.88	O
ATOM	274	N	GLU	A	42	8.423	37.599	6.382	1.00	26.98	N
ATOM	275	CA	GLU	A	42	9.158	36.471	5.844	1.00	26.62	C
ATOM	276	CB	GLU	A	42	10.410	36.941	5.136	1.00	25.66	C
ATOM	277	CG	GLU	A	42	11.262	35.771	4.674	1.00	29.23	C
ATOM	278	CD	GLU	A	42	12.585	36.257	4.169	1.00	33.29	C
ATOM	279	OE1	GLU	A	42	12.662	37.495	4.009	1.00	39.18	O
ATOM	280	OE2	GLU	A	42	13.509	35.446	3.942	1.00	32.02	O
ATOM	281	C	GLU	A	42	9.493	35.423	6.907	1.00	25.64	C
ATOM	282	O	GLU	A	42	9.402	34.194	6.660	1.00	25.35	O
ATOM	283	N	LEU	A	43	9.924	35.890	8.073	1.00	24.48	N
ATOM	284	CA	LEU	A	43	10.237	34.943	9.136	1.00	22.53	C
ATOM	285	CB	LEU	A	43	11.588	35.235	9.679	1.00	21.18	C
ATOM	286	CG	LEU	A	43	12.709	35.170	8.639	1.00	20.88	C
ATOM	287	CD1	LEU	A	43	13.897	35.767	9.251	1.00	18.58	C
ATOM	288	CD2	LEU	A	43	13.008	33.723	8.182	1.00	12.93	C
ATOM	289	C	LEU	A	43	9.132	35.094	10.176	1.00	23.87	C
ATOM	290	O	LEU	A	43	9.104	36.061	10.998	1.00	23.60	O
ATOM	291	N	VAL	A	44	8.203	34.152	10.127	1.00	22.85	N
ATOM	292	CA	VAL	A	44	6.982	34.352	10.840	1.00	23.80	C
ATOM	293	CB	VAL	A	44	5.759	34.393	9.821	1.00	25.82	C
ATOM	294	CG1	VAL	A	44	4.391	34.323	10.566	1.00	22.76	C
ATOM	295	CG2	VAL	A	44	5.885	35.639	8.770	1.00	22.93	C
ATOM	296	C	VAL	A	44	6.796	33.318	11.959	1.00	24.29	C
ATOM	297	O	VAL	A	44	6.654	32.112	11.710	1.00	25.56	O
ATOM	298	N	TYR	A	45	6.791	33.810	13.184	1.00	24.25	N
ATOM	299	CA	TYR	A	45	6.507	33.009	14.354	1.00	24.54	C
ATOM	300	CB	TYR	A	45	6.426	33.912	15.574	1.00	23.10	C
ATOM	301	CG	TYR	A	45	6.290	33.138	16.872	1.00	20.21	C
ATOM	302	CD1	TYR	A	45	7.398	32.522	17.434	1.00	19.20	C
ATOM	303	CE1	TYR	A	45	7.312	31.818	18.577	1.00	18.09	C
ATOM	304	CZ	TYR	A	45	6.114	31.703	19.244	1.00	18.00	C
ATOM	305	OH	TYR	A	45	6.113	30.982	20.458	1.00	13.97	O
ATOM	306	CE2	TYR	A	45	4.982	32.320	18.714	1.00	16.93	C
ATOM	307	CD2	TYR	A	45	5.084	33.021	17.524	1.00	15.67	C
ATOM	308	C	TYR	A	45	5.158	32.312	14.257	1.00	25.34	C
ATOM	309	O	TYR	A	45	4.148	32.983	13.973	1.00	25.82	O
ATOM	310	N	GLU	A	46	5.152	31.003	14.498	1.00	25.80	N
ATOM	311	CA	GLU	A	46	3.914	30.240	14.669	1.00	28.29	C
ATOM	312	CB	GLU	A	46	4.067	28.847	14.091	1.00	29.39	C
ATOM	313	CG	GLU	A	46	3.685	28.752	12.605	1.00	35.45	C
ATOM	314	CD	GLU	A	46	3.939	27.333	12.057	1.00	44.77	C
ATOM	315	OE1	GLU	A	46	4.758	27.221	11.108	1.00	47.72	O
ATOM	316	OE2	GLU	A	46	3.358	26.319	12.578	1.00	45.80	O
ATOM	317	C	GLU	A	46	3.457	30.149	16.147	1.00	27.92	C
ATOM	318	O	GLU	A	46	4.033	29.403	16.957	1.00	28.79	O
ATOM	319	N	ASN	A	47	2.447	30.933	16.497	1.00	26.95	N
ATOM	320	CA	ASN	A	47	1.996	31.010	17.878	1.00	26.35	C
ATOM	321	CB	ASN	A	47	1.134	32.267	18.076	1.00	25.57	C
ATOM	322	CG	ASN	A	47	−0.105	32.275	17.168	1.00	26.38	C
ATOM	323	OD1	ASN	A	47	−0.006	32.506	15.950	1.00	24.60	O
ATOM	324	ND2	ASN	A	47	−1.268	32.020	17.755	1.00	23.51	N
ATOM	325	C	ASN	A	47	1.194	29.750	18.311	1.00	25.74	C
ATOM	326	O	ASN	A	47	0.391	29.253	17.545	1.00	24.46	O
ATOM	327	N	PHE	A	48	1.406	29.288	19.547	1.00	24.99	N
ATOM	328	CA	PHE	A	48	0.487	28.350	20.163	1.00	25.50	C
ATOM	329	CB	PHE	A	48	1.143	27.560	21.292	1.00	26.09	C
ATOM	330	CG	PHE	A	48	2.135	26.591	20.787	1.00	25.50	C
ATOM	331	CD1	PHE	A	48	3.482	27.011	20.536	1.00	23.50	C
ATOM	332	CE1	PHE	A	48	4.404	26.162	20.020	1.00	21.12	C
ATOM	333	CZ	PHE	A	48	4.022	24.819	19.724	1.00	21.91	C
ATOM	334	CE2	PHE	A	48	2.689	24.380	19.925	1.00	23.87	C
ATOM	335	CD2	PHE	A	48	1.736	25.296	20.457	1.00	24.44	C
ATOM	336	C	PHE	A	48	−0.749	29.058	20.665	1.00	25.24	C
ATOM	337	O	PHE	A	48	−1.847	28.651	20.351	1.00	24.76	O
ATOM	338	N	TYR	A	49	−0.578	30.120	21.439	1.00	25.71	N
ATOM	339	CA	TYR	A	49	−1.727	30.931	21.778	1.00	24.86	C
ATOM	340	CB	TYR	A	49	−2.292	30.527	23.128	1.00	24.98	C
ATOM	341	CG	TYR	A	49	−3.550	31.267	23.517	1.00	25.94	C
ATOM	342	CD1	TYR	A	49	−4.766	30.967	22.935	1.00	24.71	C
ATOM	343	CE1	TYR	A	49	−5.907	31.658	23.298	1.00	24.67	C
ATOM	344	CZ	TYR	A	49	−5.842	32.661	24.256	1.00	24.24	C
ATOM	345	OH	TYR	A	49	−6.993	33.383	24.628	1.00	20.90	O
ATOM	346	CE2	TYR	A	49	−4.624	32.981	24.819	1.00	22.17	C
ATOM	347	CD2	TYR	A	49	−3.510	32.282	24.483	1.00	23.72	C
ATOM	348	C	TYR	A	49	−1.462	32.423	21.601	1.00	25.42	C
ATOM	349	O	TYR	A	49	−1.594	32.907	20.458	1.00	26.08	O
ATOM	350	N	ALA	A	50	−1.055	33.129	22.682	1.00	23.94	N
ATOM	351	CA	ALA	A	50	−0.698	34.550	22.651	1.00	22.19	C
ATOM	352	CB	ALA	A	50	−1.349	35.319	23.865	1.00	22.45	C
ATOM	353	C	ALA	A	50	0.825	34.829	22.623	1.00	21.88	C
ATOM	354	O	ALA	A	50	1.252	35.993	22.510	1.00	21.42	O
ATOM	355	N	ASP	A	51	1.646	33.794	22.753	1.00	21.12	N
ATOM	356	CA	ASP	A	51	3.076	33.935	22.495	1.00	20.63	C
ATOM	357	CB	ASP	A	51	3.794	32.602	22.706	1.00	19.89	C
ATOM	358	CG	ASP	A	51	3.098	31.458	22.038	1.00	22.43	C
ATOM	359	OD1	ASP	A	51	1.935	31.139	22.430	1.00	19.30	O
ATOM	360	OD2	ASP	A	51	3.653	30.785	21.103	1.00	27.20	O
ATOM	361	C	ASP	A	51	3.318	34.404	21.075	1.00	20.82	C
ATOM	362	O	ASP	A	51	2.546	34.057	20.163	1.00	20.23	O
ATOM	363	N	PHE	A	52	4.417	35.148	20.868	1.00	20.82	N
ATOM	364	CA	PHE	A	52	4.672	35.824	19.581	1.00	20.22	C
ATOM	365	CB	PHE	A	52	4.170	37.288	19.629	1.00	19.43	C
ATOM	366	CG	PHE	A	52	4.884	38.167	20.671	1.00	20.55	C
ATOM	367	CD1	PHE	A	52	6.071	38.818	20.361	1.00	19.91	C
ATOM	368	CE1	PHE	A	52	6.728	39.625	21.278	1.00	21.17	C
ATOM	369	CZ	PHE	A	52	6.214	39.782	22.534	1.00	22.23	C
ATOM	370	CE2	PHE	A	52	4.994	39.131	22.881	1.00	21.22	C
ATOM	371	CD2	PHE	A	52	4.360	38.327	21.950	1.00	20.06	C
ATOM	372	C	PHE	A	52	6.170	35.755	19.244	1.00	21.05	C
ATOM	373	O	PHE	A	52	6.635	36.298	18.207	1.00	20.41	O
ATOM	374	N	GLY	A	53	6.916	35.053	20.101	1.00	20.85	N
ATOM	375	CA	GLY	A	53	8.370	34.980	19.992	1.00	21.80	C
ATOM	376	C	GLY	A	53	9.002	34.419	21.261	1.00	22.23	C
ATOM	377	O	GLY	A	53	8.280	34.175	22.265	1.00	23.39	O
ATOM	378	N	PRO	A	54	10.317	34.220	21.278	1.00	21.95	N
ATOM	379	CA	PRO	A	54	11.240	34.656	20.229	1.00	22.68	C
ATOM	380	CB	PRO	A	54	12.613	34.563	20.939	1.00	21.95	C
ATOM	381	CG	PRO	A	54	12.463	33.382	21.864	1.00	20.71	C
ATOM	382	CD	PRO	A	54	11.016	33.461	22.350	1.00	21.92	C
ATOM	383	C	PRO	A	54	11.237	33.691	19.016	1.00	22.87	C
ATOM	384	O	PRO	A	54	10.827	32.528	19.195	1.00	23.94	O
ATOM	385	N	LEU	A	55	11.701	34.165	17.857	1.00	22.30	N
ATOM	386	CA	LEU	A	55	11.786	33.389	16.614	1.00	22.94	C
ATOM	387	CB	LEU	A	55	12.319	34.276	15.474	1.00	21.89	C
ATOM	388	CG	LEU	A	55	11.311	34.808	14.466	1.00	24.12	C
ATOM	389	CD1	LEU	A	55	9.879	35.062	15.038	1.00	23.36	C
ATOM	390	CD2	LEU	A	55	11.868	36.019	13.817	1.00	24.86	C
ATOM	391	C	LEU	A	55	12.700	32.172	16.795	1.00	23.23	C
ATOM	392	O	LEU	A	55	13.663	32.222	17.572	1.00	25.04	O
ATOM	393	N	ASN	A	56	12.432	31.089	16.091	1.00	22.62	N
ATOM	394	CA	ASN	A	56	13.149	29.881	16.370	1.00	21.13	C
ATOM	395	CB	ASN	A	56	12.293	28.665	16.078	1.00	20.76	C
ATOM	396	CG	ASN	A	56	12.085	28.386	14.594	1.00	20.89	C
ATOM	397	OD1	ASN	A	56	13.009	28.462	13.772	1.00	22.96	O
ATOM	398	ND2	ASN	A	56	10.871	27.931	14.263	1.00	20.12	N
ATOM	399	C	ASN	A	56	14.537	29.815	15.774	1.00	21.85	C
ATOM	400	O	ASN	A	56	14.912	30.678	14.990	1.00	21.40	O
ATOM	401	N	LEU	A	57	15.317	28.811	16.190	1.00	22.52	N
ATOM	402	CA	LEU	A	57	16.697	28.630	15.743	1.00	23.07	C
ATOM	403	CB	LEU	A	57	17.252	27.286	16.209	1.00	23.07	C
ATOM	404	CG	LEU	A	57	18.636	27.073	16.843	1.00	23.92	C
ATOM	405	CD1	LEU	A	57	19.200	25.790	16.354	1.00	23.47	C
ATOM	406	CD2	LEU	A	57	19.678	28.214	16.868	1.00	20.08	C
ATOM	407	C	LEU	A	57	16.810	28.674	14.226	1.00	23.71	C
ATOM	408	O	LEU	A	57	17.789	29.297	13.689	1.00	23.89	O
ATOM	409	N	ALA	A	58	15.836	28.026	13.550	1.00	22.25	N
ATOM	410	CA	ALA	A	58	15.819	27.952	12.075	1.00	22.65	C
ATOM	411	CB	ALA	A	58	14.630	27.009	11.490	1.00	22.39	C
ATOM	412	C	ALA	A	58	15.713	29.310	11.467	1.00	22.63	C
ATOM	413	O	ALA	A	58	16.371	29.611	10.452	1.00	22.40	O
ATOM	414	N	MET	A	59	14.832	30.129	12.045	1.00	22.67	N
ATOM	415	CA	MET	A	59	14.602	31.440	11.443	1.00	21.64	C
ATOM	416	CB	MET	A	59	13.253	31.945	11.817	1.00	21.65	C
ATOM	417	CG	MET	A	59	12.117	31.201	11.133	1.00	19.69	C
ATOM	418	SD	MET	A	59	10.562	31.918	11.777	1.00	25.76	S
ATOM	419	CE	MET	A	59	9.315	30.394	11.394	1.00	20.19	C
ATOM	420	C	MET	A	59	15.723	32.402	11.788	1.00	22.08	C
ATOM	421	O	MET	A	59	16.043	33.261	10.967	1.00	22.17	O
ATOM	422	N	VAL	A	60	16.359	32.203	12.962	1.00	21.46	N
ATOM	423	CA	VAL	A	60	17.592	32.904	13.334	1.00	21.58	C
ATOM	424	CB	VAL	A	60	18.031	32.557	14.799	1.00	22.34	C
ATOM	425	CG1	VAL	A	60	19.413	33.118	15.121	1.00	20.93	C
ATOM	426	CG2	VAL	A	60	16.993	33.042	15.818	1.00	20.43	C
ATOM	427	C	VAL	A	60	18.728	32.596	12.322	1.00	21.49	C
ATOM	428	O	VAL	A	60	19.454	33.503	11.870	1.00	20.76	O
ATOM	429	N	TYR	A	61	18.814	31.313	11.952	1.00	21.71	N
ATOM	430	CA	TYR	A	61	19.691	30.811	10.914	1.00	21.55	C
ATOM	431	CB	TYR	A	61	19.471	29.304	10.690	1.00	22.05	C
ATOM	432	CG	TYR	A	61	20.391	28.707	9.625	1.00	21.88	C
ATOM	433	CD1	TYR	A	61	21.800	28.602	9.845	1.00	21.28	C
ATOM	434	CE1	TYR	A	61	22.648	28.066	8.854	1.00	21.35	C
ATOM	435	CZ	TYR	A	61	22.086	27.604	7.606	1.00	23.78	C
ATOM	436	OH	TYR	A	61	22.909	27.032	6.603	1.00	26.98	O
ATOM	437	CE2	TYR	A	61	20.710	27.677	7.393	1.00	19.42	C
ATOM	438	CD2	TYR	A	61	19.874	28.251	8.411	1.00	20.84	C
ATOM	439	C	TYR	A	61	19.445	31.529	9.601	1.00	22.63	C
ATOM	440	O	TYR	A	61	20.391	32.193	9.068	1.00	22.99	O
ATOM	441	N	ARG	A	62	18.203	31.383	9.072	1.00	21.76	N
ATOM	442	CA	ARG	A	62	17.827	31.970	7.790	1.00	20.95	C
ATOM	443	CB	ARG	A	62	16.378	31.728	7.427	1.00	21.34	C
ATOM	444	CG	ARG	A	62	16.067	30.253	7.106	1.00	19.00	C
ATOM	445	CD	ARG	A	62	14.616	29.968	6.753	1.00	20.97	C
ATOM	446	NE	ARG	A	62	14.507	28.557	6.328	1.00	20.81	N
ATOM	447	CZ	ARG	A	62	14.993	28.091	5.188	1.00	24.90	C
ATOM	448	NH1	ARG	A	62	15.567	28.909	4.317	1.00	19.33	N
ATOM	449	NH2	ARG	A	62	14.899	26.800	4.894	1.00	29.25	N
ATOM	450	C	ARG	A	62	18.110	33.431	7.834	1.00	22.54	C
ATOM	451	O	ARG	A	62	18.647	33.970	6.894	1.00	24.20	O
ATOM	452	N	TYR	A	63	17.811	34.091	8.938	1.00	23.54	N
ATOM	453	CA	TYR	A	63	18.170	35.503	9.050	1.00	24.24	C
ATOM	454	CB	TYR	A	63	17.679	36.142	10.358	1.00	24.14	C
ATOM	455	CG	TYR	A	63	18.152	37.591	10.521	1.00	23.55	C
ATOM	456	CD1	TYR	A	63	17.395	38.645	10.004	1.00	23.90	C
ATOM	457	CE1	TYR	A	63	17.800	39.954	10.119	1.00	17.65	C
ATOM	458	CZ	TYR	A	63	18.948	40.273	10.797	1.00	20.07	C
ATOM	459	OH	TYR	A	63	19.242	41.626	10.964	1.00	19.48	O
ATOM	460	CE2	TYR	A	63	19.745	39.255	11.358	1.00	22.70	C
ATOM	461	CD2	TYR	A	63	19.333	37.908	11.206	1.00	24.54	C
ATOM	462	C	TYR	A	63	19.669	35.758	8.929	1.00	24.26	C
ATOM	463	O	TYR	A	63	20.055	36.695	8.227	1.00	25.67	O
ATOM	464	N	CYS	A	64	20.497	34.974	9.626	1.00	23.62	N
ATOM	465	CA	CYS	A	64	21.945	35.204	9.601	1.00	23.77	C
ATOM	466	CB	CYS	A	64	22.687	34.417	10.699	1.00	22.29	C
ATOM	467	SG	CYS	A	64	22.363	35.034	12.405	1.00	21.22	S
ATOM	468	C	CYS	A	64	22.513	34.970	8.194	1.00	24.86	C
ATOM	469	O	CYS	A	64	23.282	35.784	7.716	1.00	25.98	O
ATOM	470	N	CYS	A	65	22.105	33.894	7.529	1.00	26.06	N
ATOM	471	CA	CYS	A	65	22.454	33.651	6.123	1.00	28.12	C
ATOM	472	CB	CYS	A	65	21.778	32.384	5.620	1.00	27.83	C
ATOM	473	SG	CYS	A	65	22.378	30.987	6.591	1.00	34.44	S
ATOM	474	C	CYS	A	65	22.111	34.813	5.190	1.00	28.85	C
ATOM	475	O	CYS	A	65	22.936	35.215	4.328	1.00	30.99	O
ATOM	476	N	LYS	A	66	20.918	35.358	5.369	1.00	27.69	N
ATOM	477	CA	LYS	A	66	20.442	36.454	4.582	1.00	27.67	C
ATOM	478	CB	LYS	A	66	19.052	36.824	5.031	1.00	27.95	C
ATOM	479	CG	LYS	A	66	18.415	37.837	4.160	1.00	29.16	C
ATOM	480	CD	LYS	A	66	17.038	38.212	4.746	1.00	33.61	C
ATOM	481	CE	LYS	A	66	15.922	38.040	3.658	1.00	39.39	C
ATOM	482	NZ	LYS	A	66	15.608	39.407	3.061	1.00	40.02	N
ATOM	483	C	LYS	A	66	21.364	37.657	4.717	1.00	27.46	C
ATOM	484	O	LYS	A	66	21.906	38.160	3.715	1.00	27.88	O
ATOM	485	N	LEU	A	67	21.559	38.085	5.956	1.00	26.41	N
ATOM	486	CA	LEU	A	67	22.294	39.321	6.244	1.00	25.71	C
ATOM	487	CB	LEU	A	67	22.208	39.632	7.735	1.00	23.89	C
ATOM	488	CG	LEU	A	67	22.864	40.911	8.238	1.00	23.02	C
ATOM	489	CD1	LEU	A	67	22.649	42.134	7.303	1.00	18.87	C
ATOM	490	CD2	LEU	A	67	22.374	41.173	9.686	1.00	19.52	C
ATOM	491	C	LEU	A	67	23.733	39.153	5.798	1.00	26.43	C
ATOM	492	O	LEU	A	67	24.325	40.036	5.148	1.00	26.22	O
ATOM	493	N	ASN	A	68	24.288	38.008	6.156	1.00	27.02	N
ATOM	494	CA	ASN	A	68	25.593	37.631	5.695	1.00	29.37	C
ATOM	495	CB	ASN	A	68	25.889	36.230	6.188	1.00	29.90	C
ATOM	496	CG	ASN	A	68	27.116	36.204	6.977	1.00	34.36	C
ATOM	497	OD1	ASN	A	68	28.193	36.439	6.417	1.00	42.15	O
ATOM	498	ND2	ASN	A	68	27.002	35.996	8.300	1.00	36.36	N
ATOM	499	C	ASN	A	68	25.807	37.760	4.173	1.00	29.87	C
ATOM	500	O	ASN	A	68	26.765	38.380	3.741	1.00	29.85	O
ATOM	501	N	LYS	A	69	24.901	37.175	3.376	1.00	31.06	N
ATOM	502	CA	LYS	A	69	24.909	37.317	1.923	1.00	31.81	C
ATOM	503	CB	LYS	A	69	23.756	36.517	1.321	1.00	33.34	C
ATOM	504	CG	LYS	A	69	23.684	36.438	−0.226	1.00	38.02	C
ATOM	505	CD	LYS	A	69	24.968	35.799	−0.831	1.00	47.34	C
ATOM	506	CE	LYS	A	69	24.670	34.944	−2.072	1.00	50.82	C
ATOM	507	NZ	LYS	A	69	25.384	33.614	−1.934	1.00	51.61	N
ATOM	508	C	LYS	A	69	24.851	38.810	1.511	1.00	31.76	C
ATOM	509	O	LYS	A	69	25.646	39.236	0.670	1.00	32.11	O
ATOM	510	N	LYS	A	70	23.985	39.609	2.139	1.00	30.29	N
ATOM	511	CA	LYS	A	70	23.910	41.048	1.835	1.00	30.53	C
ATOM	512	CB	LYS	A	70	22.772	41.786	2.612	1.00	29.69	C
ATOM	513	CG	LYS	A	70	21.384	41.403	2.141	1.00	27.01	C
ATOM	514	CD	LYS	A	70	20.329	41.910	3.053	1.00	27.77	C
ATOM	515	CE	LYS	A	70	18.936	41.387	2.650	1.00	26.05	C
ATOM	516	NZ	LYS	A	70	18.434	42.096	1.406	1.00	28.59	N
ATOM	517	C	LYS	A	70	25.194	41.775	2.092	1.00	31.47	C
ATOM	518	O	LYS	A	70	25.555	42.676	1.348	1.00	32.01	O
ATOM	519	N	LEU	A	71	25.879	41.395	3.169	1.00	33.76	N
ATOM	520	CA	LEU	A	71	27.009	42.169	3.688	1.00	34.29	C
ATOM	521	CB	LEU	A	71	27.280	41.814	5.133	1.00	32.98	C
ATOM	522	CG	LEU	A	71	26.467	42.537	6.195	1.00	33.76	C
ATOM	523	CD1	LEU	A	71	26.712	41.912	7.622	1.00	30.41	C
ATOM	524	CD2	LEU	A	71	26.665	44.086	6.201	1.00	28.86	C
ATOM	525	C	LEU	A	71	28.240	41.899	2.822	1.00	35.52	C
ATOM	526	O	LEU	A	71	29.212	42.702	2.810	1.00	35.14	O
ATOM	527	N	LYS	A	72	28.140	40.805	2.064	1.00	36.68	N
ATOM	528	CA	LYS	A	72	29.218	40.315	1.192	1.00	38.91	C
ATOM	529	CB	LYS	A	72	29.399	38.807	1.350	1.00	38.84	C
ATOM	530	CG	LYS	A	72	30.101	38.385	2.659	1.00	43.37	C
ATOM	531	CD	LYS	A	72	30.072	36.855	2.787	1.00	49.95	C
ATOM	532	CE	LYS	A	72	30.207	36.395	4.242	1.00	55.10	C
ATOM	533	NZ	LYS	A	72	31.624	36.353	4.772	1.00	58.22	N
ATOM	534	C	LYS	A	72	29.014	40.643	−0.280	1.00	38.89	C
ATOM	535	O	LYS	A	72	29.963	40.602	−1.060	1.00	40.38	O
ATOM	536	N	SER	A	73	27.793	40.956	−0.676	1.00	38.82	N
ATOM	537	CA	SER	A	73	27.532	41.184	−2.087	1.00	38.78	C
ATOM	538	CB	SER	A	73	26.021	41.194	−2.431	1.00	39.36	C
ATOM	539	OG	SER	A	73	25.392	42.379	−1.977	1.00	38.87	O
ATOM	540	C	SER	A	73	28.219	42.441	−2.588	1.00	38.82	C
ATOM	541	O	SER	A	73	28.231	43.532	−1.948	1.00	38.16	O
ATOM	542	N	TYR	A	74	28.798	42.260	−3.759	1.00	39.10	N
ATOM	543	CA	TYR	A	74	29.420	43.348	−4.425	1.00	39.12	C
ATOM	544	CB	TYR	A	74	30.060	42.862	−5.736	1.00	39.94	C
ATOM	545	CG	TYR	A	74	30.649	44.055	−6.446	1.00	44.84	C
ATOM	546	CD1	TYR	A	74	31.636	44.812	−5.815	1.00	44.93	C
ATOM	547	CE1	TYR	A	74	32.141	45.950	−6.391	1.00	51.13	C
ATOM	548	CZ	TYR	A	74	31.659	46.377	−7.628	1.00	52.41	C
ATOM	549	OH	TYR	A	74	32.223	47.512	−8.146	1.00	54.97	O
ATOM	550	CE2	TYR	A	74	30.657	45.661	−8.300	1.00	52.47	C
ATOM	551	CD2	TYR	A	74	30.140	44.497	−7.693	1.00	48.92	C
ATOM	552	C	TYR	A	74	28.402	44.528	−4.624	1.00	38.24	C
ATOM	553	O	TYR	A	74	28.726	45.692	−4.303	1.00	37.75	O
ATOM	554	N	SER	A	75	27.180	44.230	−5.082	1.00	36.39	N
ATOM	555	CA	SER	A	75	26.225	45.281	−5.475	1.00	36.24	C
ATOM	556	CB	SER	A	75	25.085	44.685	−6.321	1.00	35.91	C
ATOM	557	OG	SER	A	75	24.349	43.785	−5.504	1.00	34.20	O
ATOM	558	C	SER	A	75	25.624	46.124	−4.293	1.00	36.24	C
ATOM	559	O	SER	A	75	25.088	47.227	−4.512	1.00	35.40	O
ATOM	560	N	LEU	A	76	25.687	45.585	−3.070	1.00	35.22	N
ATOM	561	CA	LEU	A	76	25.246	46.314	−1.883	1.00	34.96	C
ATOM	562	CB	LEU	A	76	24.444	45.435	−0.926	1.00	33.68	C
ATOM	563	CG	LEU	A	76	23.221	44.853	−1.625	1.00	32.74	C
ATOM	564	CD1	LEU	A	76	22.453	43.981	−0.664	1.00	32.03	C
ATOM	565	CD2	LEU	A	76	22.347	45.957	−2.156	1.00	30.02	C
ATOM	566	C	LEU	A	76	26.451	46.881	−1.187	1.00	35.19	C
ATOM	567	O	LEU	A	76	26.319	47.615	−0.208	1.00	35.57	O
ATOM	568	N	LEU	A	77	27.611	46.527	−1.727	1.00	35.60	N
ATOM	569	CA	LEU	A	77	28.944	46.966	−1.276	1.00	37.06	C
ATOM	570	CB	LEU	A	77	29.933	46.800	−2.454	1.00	37.26	C
ATOM	571	CG	LEU	A	77	31.370	46.643	−2.034	1.00	41.74	C
ATOM	572	CD1	LEU	A	77	32.278	47.884	−2.316	1.00	45.22	C
ATOM	573	CD2	LEU	A	77	31.394	46.208	−0.538	1.00	45.32	C
ATOM	574	C	LEU	A	77	29.088	48.406	−0.736	1.00	36.23	C
ATOM	575	O	LEU	A	77	29.725	48.634	0.307	1.00	35.94	O
ATOM	576	N	ARG	A	78	28.550	49.361	−1.492	1.00	35.16	N
ATOM	577	CA	ARG	A	78	28.822	50.744	−1.264	1.00	35.98	C
ATOM	578	CB	ARG	A	78	29.283	51.384	−2.582	1.00	36.55	C
ATOM	579	CG	ARG	A	78	30.678	50.918	−3.103	1.00	39.84	C
ATOM	580	CD	ARG	A	78	30.948	51.248	−4.592	1.00	45.88	C
ATOM	581	NE	ARG	A	78	30.779	52.690	−4.811	1.00	49.47	N
ATOM	582	CZ	ARG	A	78	29.965	53.255	−5.713	1.00	48.60	C
ATOM	583	NH1	ARG	A	78	29.250	52.490	−6.561	1.00	44.22	N
ATOM	584	NH2	ARG	A	78	29.920	54.601	−5.776	1.00	45.83	N
ATOM	585	C	ARG	A	78	27.567	51.411	−0.741	1.00	36.22	C
ATOM	586	O	ARG	A	78	27.325	52.627	−0.965	1.00	36.77	O
ATOM	587	N	LYS	A	79	26.753	50.603	−0.053	1.00	35.92	N
ATOM	588	CA	LYS	A	79	25.482	51.032	0.534	1.00	34.46	C
ATOM	589	CB	LYS	A	79	24.365	50.250	−0.122	1.00	33.75	C
ATOM	590	CG	LYS	A	79	24.315	50.445	−1.610	1.00	32.90	C
ATOM	591	CD	LYS	A	79	22.905	50.267	−2.122	1.00	33.09	C
ATOM	592	CE	LYS	A	79	22.795	50.379	−3.657	1.00	34.16	C
ATOM	593	NZ	LYS	A	79	21.336	50.206	−4.000	1.00	34.67	N
ATOM	594	C	LYS	A	79	25.472	50.800	2.048	1.00	34.30	C
ATOM	595	O	LYS	A	79	26.110	49.849	2.546	1.00	34.80	O
ATOM	596	N	LYS	A	80	24.765	51.676	2.769	1.00	33.17	N
ATOM	597	CA	LYS	A	80	24.309	51.388	4.119	1.00	32.58	C
ATOM	598	CB	LYS	A	80	23.643	52.608	4.757	1.00	33.33	C
ATOM	599	CG	LYS	A	80	24.533	53.687	5.287	1.00	35.93	C
ATOM	600	CD	LYS	A	80	23.684	54.930	5.708	1.00	43.43	C
ATOM	601	CE	LYS	A	80	22.634	54.620	6.813	1.00	46.31	C
ATOM	602	NZ	LYS	A	80	21.533	55.655	6.950	1.00	47.16	N
ATOM	603	C	LYS	A	80	23.238	50.290	4.025	1.00	31.30	C
ATOM	604	O	LYS	A	80	22.360	50.361	3.142	1.00	31.89	O
ATOM	605	N	ILE	A	81	23.326	49.283	4.894	1.00	28.79	N
ATOM	606	CA	ILE	A	81	22.279	48.305	5.062	1.00	27.54	C
ATOM	607	CB	ILE	A	81	22.823	46.852	4.953	1.00	28.44	C
ATOM	608	CG1	ILE	A	81	23.258	46.542	3.506	1.00	26.56	C
ATOM	609	CD1	ILE	A	81	24.341	45.457	3.461	1.00	25.49	C
ATOM	610	CG2	ILE	A	81	21.718	45.814	5.246	1.00	27.21	C
ATOM	611	C	ILE	A	81	21.369	48.576	6.324	1.00	26.98	C
ATOM	612	O	ILE	A	81	21.826	48.834	7.453	1.00	25.28	O
ATOM	613	N	VAL	A	82	20.067	48.619	6.065	1.00	25.86	N
ATOM	614	CA	VAL	A	82	19.097	48.883	7.106	1.00	24.81	C
ATOM	615	CB	VAL	A	82	18.463	50.272	6.959	1.00	25.08	C
ATOM	616	CG1	VAL	A	82	17.372	50.516	8.037	1.00	24.27	C
ATOM	617	CG2	VAL	A	82	19.545	51.347	7.056	1.00	23.95	C
ATOM	618	C	VAL	A	82	18.062	47.765	7.141	1.00	24.34	C
ATOM	619	O	VAL	A	82	17.267	47.577	6.186	1.00	23.31	O
ATOM	620	N	HIS	A	83	18.168	46.977	8.218	1.00	23.68	N
ATOM	621	CA	HIS	A	83	17.140	46.036	8.638	1.00	23.40	C
ATOM	622	CB	HIS	A	83	17.710	44.994	9.618	1.00	23.75	C
ATOM	623	CG	HIS	A	83	16.667	44.047	10.157	1.00	25.25	C
ATOM	624	ND1	HIS	A	83	16.947	43.089	11.108	1.00	25.43	N
ATOM	625	CE1	HIS	A	83	15.841	42.416	11.392	1.00	24.89	C
ATOM	626	NE2	HIS	A	83	14.862	42.886	10.641	1.00	25.43	N
ATOM	627	CD2	HIS	A	83	15.354	43.897	9.848	1.00	23.41	C
ATOM	628	C	HIS	A	83	16.085	46.853	9.359	1.00	23.08	C
ATOM	629	O	HIS	A	83	16.356	47.386	10.399	1.00	22.98	O
ATOM	630	N	TYR	A	84	14.897	46.994	8.795	1.00	23.46	N
ATOM	631	CA	TYR	A	84	13.840	47.788	9.439	1.00	23.16	C
ATOM	632	CB	TYR	A	84	13.281	48.888	8.538	1.00	23.32	C
ATOM	633	CG	TYR	A	84	12.452	48.430	7.333	1.00	23.65	C
ATOM	634	CD1	TYR	A	84	11.031	48.372	7.394	1.00	22.45	C
ATOM	635	CE1	TYR	A	84	10.268	47.967	6.282	1.00	23.08	C
ATOM	636	CZ	TYR	A	84	10.946	47.620	5.086	1.00	25.73	C
ATOM	637	OH	TYR	A	84	10.256	47.211	3.975	1.00	27.67	O
ATOM	638	CE2	TYR	A	84	12.344	47.691	4.994	1.00	22.09	C
ATOM	639	CD2	TYR	A	84	13.085	48.106	6.116	1.00	23.02	C
ATOM	640	C	TYR	A	84	12.740	46.857	9.807	1.00	23.35	C
ATOM	641	O	TYR	A	84	12.655	45.738	9.255	1.00	22.88	O
ATOM	642	N	THR	A	85	11.938	47.289	10.771	1.00	22.98	N
ATOM	643	CA	THR	A	85	10.723	46.578	11.131	1.00	23.17	C
ATOM	644	CB	THR	A	85	10.950	45.731	12.436	1.00	23.24	C
ATOM	645	OG1	THR	A	85	9.788	44.945	12.717	1.00	21.72	O
ATOM	646	CG2	THR	A	85	11.125	46.621	13.685	1.00	21.59	C
ATOM	647	C	THR	A	85	9.631	47.671	11.234	1.00	24.47	C
ATOM	648	O	THR	A	85	9.892	48.831	10.806	1.00	25.06	O
ATOM	649	N	CYS	A	86	8.424	47.338	11.714	1.00	24.52	N
ATOM	650	CA	CYS	A	86	7.377	48.363	11.905	1.00	25.71	C
ATOM	651	CB	CYS	A	86	6.097	47.988	11.171	1.00	24.91	C
ATOM	652	SG	CYS	A	86	5.577	46.286	11.518	1.00	28.14	S
ATOM	653	C	CYS	A	86	7.049	48.561	13.365	1.00	26.56	C
ATOM	654	O	CYS	A	86	7.746	48.062	14.259	1.00	28.49	O
ATOM	655	N	PHE	A	87	5.947	49.236	13.609	1.00	27.49	N
ATOM	656	CA	PHE	A	87	5.474	49.520	14.957	1.00	28.28	C
ATOM	657	CB	PHE	A	87	4.905	50.944	15.004	1.00	30.20	C
ATOM	658	CG	PHE	A	87	5.978	52.011	15.157	1.00	32.60	C
ATOM	659	CD1	PHE	A	87	6.670	52.483	14.039	1.00	33.30	C
ATOM	660	CE1	PHE	A	87	7.667	53.427	14.163	1.00	36.55	C
ATOM	661	CZ	PHE	A	87	8.023	53.929	15.434	1.00	41.13	C
ATOM	662	CE2	PHE	A	87	7.350	53.477	16.579	1.00	42.24	C
ATOM	663	CD2	PHE	A	87	6.319	52.493	16.424	1.00	38.55	C
ATOM	664	C	PHE	A	87	4.486	48.509	15.550	1.00	27.81	C
ATOM	665	O	PHE	A	87	3.905	48.733	16.622	1.00	28.40	O
ATOM	666	N	ASP	A	88	4.281	47.406	14.839	1.00	26.53	N
ATOM	667	CA	ASP	A	88	3.817	46.180	15.438	1.00	25.44	C
ATOM	668	CB	ASP	A	88	3.559	45.168	14.277	1.00	25.07	C
ATOM	669	CG	ASP	A	88	2.998	43.816	14.751	1.00	27.95	C
ATOM	670	OD1	ASP	A	88	3.205	43.384	15.903	1.00	29.33	O
ATOM	671	OD2	ASP	A	88	2.325	43.076	13.998	1.00	33.99	O
ATOM	672	C	ASP	A	88	4.938	45.742	16.453	1.00	24.06	C
ATOM	673	O	ASP	A	88	5.998	45.271	16.087	1.00	24.52	O
ATOM	674	N	GLN	A	89	4.713	45.961	17.727	1.00	23.68	N
ATOM	675	CA	GLN	A	89	5.670	45.589	18.795	1.00	22.99	C
ATOM	676	CB	GLN	A	89	5.116	46.041	20.148	1.00	21.66	C
ATOM	677	CG	GLN	A	89	4.974	47.548	20.200	1.00	22.43	C
ATOM	678	CD	GLN	A	89	6.336	48.274	20.041	1.00	23.15	C
ATOM	679	OE1	GLN	A	89	7.445	47.677	20.237	1.00	21.37	O
ATOM	680	NE2	GLN	A	89	6.263	49.538	19.676	1.00	19.76	N
ATOM	681	C	GLN	A	89	6.118	44.106	18.888	1.00	23.50	C
ATOM	682	O	GLN	A	89	7.236	43.794	19.367	1.00	21.81	O
ATOM	683	N	ARG	A	90	5.234	43.197	18.456	1.00	22.98	N
ATOM	684	CA	ARG	A	90	5.568	41.789	18.475	1.00	22.87	C
ATOM	685	CB	ARG	A	90	4.290	40.930	18.521	1.00	23.02	C
ATOM	686	CG	ARG	A	90	3.435	41.371	19.725	1.00	22.17	C
ATOM	687	CD	ARG	A	90	2.147	40.597	20.019	1.00	23.75	C
ATOM	688	NE	ARG	A	90	1.522	41.136	21.230	1.00	25.10	N
ATOM	689	CZ	ARG	A	90	0.733	42.212	21.237	1.00	24.20	C
ATOM	690	NH1	ARG	A	90	0.445	42.816	20.072	1.00	18.03	N
ATOM	691	NH2	ARG	A	90	0.222	42.654	22.401	1.00	19.50	N
ATOM	692	C	ARG	A	90	6.508	41.412	17.341	1.00	22.91	C
ATOM	693	O	ARG	A	90	7.418	40.620	17.563	1.00	23.65	O
ATOM	694	N	LYS	A	91	6.261	41.945	16.135	1.00	22.85	N
ATOM	695	CA	LYS	A	91	7.202	41.868	15.026	1.00	22.49	C
ATOM	696	CB	LYS	A	91	6.621	42.553	13.778	1.00	24.25	C
ATOM	697	CG	LYS	A	91	5.408	41.838	13.161	1.00	25.33	C
ATOM	698	CD	LYS	A	91	5.816	40.790	12.183	1.00	29.92	C
ATOM	699	CE	LYS	A	91	4.742	39.696	12.059	1.00	28.71	C
ATOM	700	NZ	LYS	A	91	5.398	38.484	11.557	1.00	31.36	N
ATOM	701	C	LYS	A	91	8.515	42.556	15.362	1.00	21.22	C
ATOM	702	O	LYS	A	91	9.618	42.007	15.125	1.00	20.54	O
ATOM	703	N	ARG	A	92	8.392	43.764	15.905	1.00	19.60	N
ATOM	704	CA	ARG	A	92	9.544	44.577	16.258	1.00	18.86	C
ATOM	705	CB	ARG	A	92	9.068	45.884	16.833	1.00	18.24	C
ATOM	706	CG	ARG	A	92	10.211	46.787	17.242	1.00	17.54	C
ATOM	707	CD	ARG	A	92	9.732	47.982	18.039	1.00	19.99	C
ATOM	708	NE	ARG	A	92	10.732	48.998	18.357	1.00	22.45	N
ATOM	709	CZ	ARG	A	92	10.806	49.609	19.539	1.00	26.21	C
ATOM	710	NH1	ARG	A	92	9.919	49.317	20.516	1.00	25.57	N
ATOM	711	NH2	ARG	A	92	11.729	50.550	19.733	1.00	27.48	N
ATOM	712	C	ARG	A	92	10.527	43.910	17.255	1.00	19.97	C
ATOM	713	O	ARG	A	92	11.723	44.067	17.087	1.00	20.04	O
ATOM	714	N	ALA	A	93	10.022	43.156	18.256	1.00	19.68	N
ATOM	715	CA	ALA	A	93	10.868	42.520	19.263	1.00	20.02	C
ATOM	716	CB	ALA	A	93	10.051	42.008	20.408	1.00	17.43	C
ATOM	717	C	ALA	A	93	11.643	41.379	18.600	1.00	21.04	C
ATOM	718	O	ALA	A	93	12.830	41.187	18.832	1.00	20.73	O
ATOM	719	N	ASN	A	94	10.947	40.641	17.741	1.00	21.86	N
ATOM	720	CA	ASN	A	94	11.553	39.568	17.014	1.00	22.80	C
ATOM	721	CB	ASN	A	94	10.491	38.771	16.272	1.00	22.93	C
ATOM	722	CG	ASN	A	94	9.896	37.709	17.113	1.00	24.46	C
ATOM	723	OD1	ASN	A	94	10.609	36.824	17.660	1.00	23.67	O
ATOM	724	ND2	ASN	A	94	8.567	37.764	17.246	1.00	23.49	N
ATOM	725	C	ASN	A	94	12.591	40.079	16.017	1.00	23.68	C
ATOM	726	O	ASN	A	94	13.616	39.427	15.823	1.00	24.67	O
ATOM	727	N	ALA	A	95	12.330	41.223	15.365	1.00	23.75	N
ATOM	728	CA	ALA	A	95	13.303	41.780	14.423	1.00	23.02	C
ATOM	729	CB	ALA	A	95	12.706	42.938	13.686	1.00	22.91	C
ATOM	730	C	ALA	A	95	14.534	42.231	15.207	1.00	22.92	C
ATOM	731	O	ALA	A	95	15.674	41.975	14.798	1.00	23.39	O
ATOM	732	N	ALA	A	96	14.291	42.905	16.327	1.00	22.79	N
ATOM	733	CA	ALA	A	96	15.361	43.340	17.264	1.00	22.63	C
ATOM	734	CB	ALA	A	96	14.776	44.099	18.458	1.00	20.68	C
ATOM	735	C	ALA	A	96	16.195	42.141	17.721	1.00	23.09	C
ATOM	736	O	ALA	A	96	17.425	42.158	17.578	1.00	24.19	O
ATOM	737	N	PHE	A	97	15.518	41.080	18.185	1.00	22.58	N
ATOM	738	CA	PHE	A	97	16.157	39.844	18.588	1.00	21.23	C
ATOM	739	CB	PHE	A	97	15.082	38.826	19.021	1.00	21.64	C
ATOM	740	CG	PHE	A	97	15.573	37.360	19.027	1.00	22.22	C
ATOM	741	CD1	PHE	A	97	16.621	36.956	19.860	1.00	18.26	C
ATOM	742	CE1	PHE	A	97	17.068	35.634	19.859	1.00	20.21	C
ATOM	743	CZ	PHE	A	97	16.457	34.672	19.035	1.00	17.63	C
ATOM	744	CE2	PHE	A	97	15.399	35.045	18.200	1.00	21.17	C
ATOM	745	CD2	PHE	A	97	14.963	36.396	18.188	1.00	23.02	C
ATOM	746	C	PHE	A	97	17.069	39.240	17.504	1.00	20.49	C
ATOM	747	O	PHE	A	97	18.188	38.770	17.810	1.00	20.28	O
ATOM	748	N	LEU	A	98	16.578	39.250	16.260	1.00	19.14	N
ATOM	749	CA	LEU	A	98	17.280	38.669	15.123	1.00	18.12	C
ATOM	750	CB	LEU	A	98	16.436	38.729	13.852	1.00	17.22	C
ATOM	751	CG	LEU	A	98	15.285	37.705	13.808	1.00	12.82	C
ATOM	752	CD1	LEU	A	98	14.570	37.771	12.495	1.00	13.88	C
ATOM	753	CD2	LEU	A	98	15.795	36.325	14.010	1.00	10.79	C
ATOM	754	C	LEU	A	98	18.620	39.355	14.921	1.00	19.17	C
ATOM	755	O	LEU	A	98	19.677	38.698	14.931	1.00	18.82	O
ATOM	756	N	ILE	A	99	18.591	40.677	14.788	1.00	20.17	N
ATOM	757	CA	ILE	A	99	19.818	41.407	14.510	1.00	21.46	C
ATOM	758	CB	ILE	A	99	19.550	42.849	13.968	1.00	22.67	C
ATOM	759	CG1	ILE	A	99	20.824	43.358	13.253	1.00	25.07	C
ATOM	760	CD1	ILE	A	99	20.749	44.792	12.789	1.00	26.95	C
ATOM	761	CG2	ILE	A	99	19.003	43.828	15.076	1.00	19.79	C
ATOM	762	C	ILE	A	99	20.780	41.383	15.707	1.00	22.23	C
ATOM	763	O	ILE	A	99	21.976	41.217	15.510	1.00	22.73	O
ATOM	764	N	GLY	A	100	20.275	41.522	16.940	1.00	22.57	N
ATOM	765	CA	GLY	A	100	21.081	41.242	18.131	1.00	22.63	C
ATOM	766	C	GLY	A	100	21.748	39.866	18.112	1.00	23.87	C
ATOM	767	O	GLY	A	100	22.891	39.710	18.531	1.00	23.91	O
ATOM	768	N	ALA	A	101	21.034	38.841	17.652	1.00	24.80	N
ATOM	769	CA	ALA	A	101	21.618	37.495	17.637	1.00	25.52	C
ATOM	770	CB	ALA	A	101	20.556	36.428	17.383	1.00	24.83	C
ATOM	771	C	ALA	A	101	22.724	37.432	16.570	1.00	26.10	C
ATOM	772	O	ALA	A	101	23.759	36.789	16.783	1.00	25.75	O
ATOM	773	N	TYR	A	102	22.489	38.091	15.430	1.00	25.89	N
ATOM	774	CA	TYR	A	102	23.548	38.231	14.434	1.00	27.00	C
ATOM	775	CB	TYR	A	102	23.061	38.997	13.198	1.00	26.28	C
ATOM	776	CG	TYR	A	102	24.157	39.098	12.133	1.00	28.41	C
ATOM	777	CD1	TYR	A	102	24.246	38.149	11.106	1.00	26.73	C
ATOM	778	CE1	TYR	A	102	25.238	38.220	10.130	1.00	25.58	C
ATOM	779	CZ	TYR	A	102	26.189	39.231	10.178	1.00	26.70	C
ATOM	780	OH	TYR	A	102	27.184	39.274	9.210	1.00	27.65	O
ATOM	781	CE2	TYR	A	102	26.148	40.194	11.193	1.00	27.35	C
ATOM	782	CD2	TYR	A	102	25.133	40.125	12.176	1.00	27.22	C
ATOM	783	C	TYR	A	102	24.852	38.906	15.024	1.00	27.41	C
ATOM	784	O	TYR	A	102	25.975	38.423	14.826	1.00	28.19	O
ATOM	785	N	ALA	A	103	24.669	40.022	15.717	1.00	26.71	N
ATOM	786	CA	ALA	A	103	25.722	40.767	16.347	1.00	26.63	C
ATOM	787	CB	ALA	A	103	25.116	41.945	17.093	1.00	26.52	C
ATOM	788	C	ALA	A	103	26.514	39.844	17.283	1.00	26.86	C
ATOM	789	O	ALA	A	103	27.743	39.774	17.205	1.00	27.99	O
ATOM	790	N	VAL	A	104	25.820	39.101	18.131	1.00	26.43	N
ATOM	791	CA	VAL	A	104	26.484	38.119	19.006	1.00	25.44	C
ATOM	792	CB	VAL	A	104	25.501	37.467	20.010	1.00	25.13	C
ATOM	793	CG1	VAL	A	104	26.212	36.382	20.852	1.00	21.00	C
ATOM	794	CG2	VAL	A	104	24.812	38.513	20.861	1.00	21.99	C
ATOM	795	C	VAL	A	104	27.201	36.993	18.254	1.00	25.58	C
ATOM	796	O	VAL	A	104	28.311	36.604	18.651	1.00	25.47	O
ATOM	797	N	ILE	A	105	26.591	36.468	17.189	1.00	25.87	N
ATOM	798	CA	ILE	A	105	27.198	35.313	16.503	1.00	26.40	C
ATOM	799	CB	ILE	A	105	26.181	34.410	15.758	1.00	26.12	C
ATOM	800	CG1	ILE	A	105	25.234	33.724	16.740	1.00	24.84	C
ATOM	801	CD1	ILE	A	105	23.832	33.527	16.179	1.00	22.42	C
ATOM	802	CG2	ILE	A	105	26.897	33.349	14.957	1.00	23.46	C
ATOM	803	C	ILE	A	105	28.298	35.766	15.552	1.00	27.57	C
ATOM	804	O	ILE	A	105	29.393	35.197	15.552	1.00	26.48	O
ATOM	805	N	TYR	A	106	28.014	36.811	14.770	1.00	28.26	N
ATOM	806	CA	TYR	A	106	28.912	37.173	13.672	1.00	29.03	C
ATOM	807	CB	TYR	A	106	28.139	37.221	12.356	1.00	28.77	C
ATOM	808	CG	TYR	A	106	27.629	35.874	12.051	1.00	26.91	C
ATOM	809	CD1	TYR	A	106	28.513	34.862	11.640	1.00	28.72	C
ATOM	810	CE1	TYR	A	106	28.052	33.532	11.389	1.00	26.22	C
ATOM	811	CZ	TYR	A	106	26.724	33.260	11.554	1.00	23.02	C
ATOM	812	OH	TYR	A	106	26.296	31.968	11.353	1.00	27.51	O
ATOM	813	CE2	TYR	A	106	25.832	34.273	11.952	1.00	24.11	C
ATOM	814	CD2	TYR	A	106	26.292	35.562	12.218	1.00	23.29	C
ATOM	815	C	TYR	A	106	29.742	38.432	13.866	1.00	30.17	C
ATOM	816	O	TYR	A	106	30.730	38.614	13.149	1.00	30.38	O
ATOM	817	N	LEU	A	107	29.368	39.270	14.836	1.00	30.49	N
ATOM	818	CA	LEU	A	107	30.060	40.542	15.040	1.00	32.24	C
ATOM	819	CB	LEU	A	107	29.071	41.712	14.891	1.00	31.33	C
ATOM	820	CG	LEU	A	107	28.348	42.044	13.566	1.00	30.42	C
ATOM	821	CD1	LEU	A	107	27.535	43.321	13.801	1.00	27.56	C
ATOM	822	CD2	LEU	A	107	29.202	42.247	12.309	1.00	24.25	C
ATOM	823	C	LEU	A	107	30.843	40.639	16.375	1.00	32.88	C
ATOM	824	O	LEU	A	107	31.315	41.700	16.757	1.00	32.31	O
ATOM	825	N	LYS	A	108	30.921	39.514	17.078	1.00	34.97	N
ATOM	826	CA	LYS	A	108	31.642	39.355	18.367	1.00	36.91	C
ATOM	827	CB	LYS	A	108	33.161	39.369	18.172	1.00	38.04	C
ATOM	828	CG	LYS	A	108	33.752	37.921	18.065	1.00	45.38	C
ATOM	829	CD	LYS	A	108	34.774	37.750	16.877	1.00	53.27	C
ATOM	830	CE	LYS	A	108	36.255	38.020	17.301	1.00	55.83	C
ATOM	831	NZ	LYS	A	108	37.025	38.576	16.130	1.00	56.41	N
ATOM	832	C	LYS	A	108	31.238	40.325	19.437	1.00	36.01	C
ATOM	833	O	LYS	A	108	32.065	40.757	20.250	1.00	36.78	O
ATOM	834	N	LYS	A	109	29.960	40.687	19.432	1.00	34.53	N
ATOM	835	CA	LYS	A	109	29.434	41.571	20.449	1.00	32.34	C
ATOM	836	CB	LYS	A	109	28.324	42.439	19.877	1.00	32.47	C
ATOM	837	CG	LYS	A	109	28.849	43.578	19.041	1.00	34.25	C
ATOM	838	CD	LYS	A	109	27.887	43.944	17.966	1.00	40.41	C
ATOM	839	CE	LYS	A	109	27.819	45.454	17.781	1.00	44.11	C
ATOM	840	NZ	LYS	A	109	26.755	45.987	18.721	1.00	44.88	N
ATOM	841	C	LYS	A	109	28.946	40.724	21.592	1.00	30.94	C
ATOM	842	O	LYS	A	109	28.547	39.574	21.419	1.00	31.39	O
ATOM	843	N	THR	A	110	28.999	41.282	22.774	1.00	29.11	N
ATOM	844	CA	THR	A	110	28.409	40.623	23.901	1.00	27.95	C
ATOM	845	CB	THR	A	110	29.034	41.096	25.276	1.00	28.33	C
ATOM	846	OG1	THR	A	110	28.761	42.493	25.475	1.00	26.85	O
ATOM	847	CG2	THR	A	110	30.628	40.915	25.309	1.00	22.67	C
ATOM	848	C	THR	A	110	26.913	40.902	23.815	1.00	27.94	C
ATOM	849	O	THR	A	110	26.476	41.843	23.105	1.00	27.73	O
ATOM	850	N	PRO	A	111	26.116	40.083	24.497	1.00	27.19	N
ATOM	851	CA	PRO	A	111	24.674	40.355	24.573	1.00	27.89	C
ATOM	852	CB	PRO	A	111	24.175	39.302	25.548	1.00	27.39	C
ATOM	853	CG	PRO	A	111	25.169	38.113	25.259	1.00	27.23	C
ATOM	854	CD	PRO	A	111	26.493	38.823	25.154	1.00	26.12	C
ATOM	855	C	PRO	A	111	24.413	41.784	25.031	1.00	29.19	C
ATOM	856	O	PRO	A	111	23.555	42.416	24.417	1.00	29.81	O
ATOM	857	N	GLU	A	112	25.195	42.283	26.020	1.00	30.20	N
ATOM	858	CA	GLU	A	112	25.040	43.607	26.631	1.00	29.83	C
ATOM	859	CB	GLU	A	112	25.946	43.730	27.881	1.00	30.47	C
ATOM	860	CG	GLU	A	112	26.042	45.123	28.523	1.00	29.09	C
ATOM	861	CD	GLU	A	112	24.754	45.592	29.214	1.00	29.95	C
ATOM	862	OE1	GLU	A	112	24.635	46.821	29.476	1.00	27.45	O
ATOM	863	OE2	GLU	A	112	23.839	44.745	29.482	1.00	30.96	O
ATOM	864	C	GLU	A	112	25.311	44.713	25.626	1.00	29.55	C
ATOM	865	O	GLU	A	112	24.530	45.647	25.516	1.00	29.49	O
ATOM	866	N	GLU	A	113	26.426	44.608	24.917	1.00	29.44	N
ATOM	867	CA	GLU	A	113	26.733	45.497	23.808	1.00	29.90	C
ATOM	868	CB	GLU	A	113	28.004	45.023	23.116	1.00	29.87	C
ATOM	869	CG	GLU	A	113	29.331	45.490	23.641	1.00	34.06	C
ATOM	870	CD	GLU	A	113	30.451	44.724	22.934	1.00	39.46	C
ATOM	871	OE1	GLU	A	113	31.229	45.296	22.150	1.00	46.18	O
ATOM	872	OE2	GLU	A	113	30.553	43.514	23.090	1.00	41.26	O
ATOM	873	C	GLU	A	113	25.590	45.481	22.737	1.00	29.46	C
ATOM	874	O	GLU	A	113	25.137	46.539	22.275	1.00	29.52	O
ATOM	875	N	ALA	A	114	25.160	44.294	22.306	1.00	29.15	N
ATOM	876	CA	ALA	A	114	24.099	44.204	21.264	1.00	29.08	C
ATOM	877	CB	ALA	A	114	23.825	42.783	20.914	1.00	28.02	C
ATOM	878	C	ALA	A	114	22.823	44.870	21.776	1.00	29.47	C
ATOM	879	O	ALA	A	114	22.127	45.587	21.035	1.00	29.76	O
ATOM	880	N	TYR	A	115	22.555	44.657	23.064	1.00	28.65	N
ATOM	881	CA	TYR	A	115	21.335	45.111	23.650	1.00	28.89	C
ATOM	882	CB	TYR	A	115	21.092	44.422	24.999	1.00	29.03	C
ATOM	883	CG	TYR	A	115	19.793	44.838	25.669	1.00	30.80	C
ATOM	884	CD1	TYR	A	115	18.558	44.612	25.060	1.00	35.00	C
ATOM	885	CE1	TYR	A	115	17.358	44.964	25.694	1.00	35.83	C
ATOM	886	CZ	TYR	A	115	17.403	45.574	26.929	1.00	34.86	C
ATOM	887	OH	TYR	A	115	16.242	45.954	27.534	1.00	38.54	O
ATOM	888	CE2	TYR	A	115	18.605	45.824	27.543	1.00	34.31	C
ATOM	889	CD2	TYR	A	115	19.795	45.446	26.917	1.00	34.66	C
ATOM	890	C	TYR	A	115	21.428	46.606	23.793	1.00	28.40	C
ATOM	891	O	TYR	A	115	20.436	47.307	23.608	1.00	27.89	O
ATOM	892	N	ARG	A	116	22.635	47.073	24.138	1.00	27.90	N
ATOM	893	CA	ARG	A	116	22.903	48.498	24.305	1.00	27.17	C
ATOM	894	CB	ARG	A	116	24.359	48.723	24.764	1.00	27.73	C
ATOM	895	CG	ARG	A	116	24.531	49.360	26.147	1.00	27.66	C
ATOM	896	CD	ARG	A	116	25.268	48.564	27.200	1.00	27.14	C
ATOM	897	NE	ARG	A	116	26.480	49.287	27.444	1.00	31.22	N
ATOM	898	CZ	ARG	A	116	27.319	49.178	28.489	1.00	30.27	C
ATOM	899	NH1	ARG	A	116	27.121	48.359	29.514	1.00	22.78	N
ATOM	900	NH2	ARG	A	116	28.399	49.948	28.468	1.00	30.55	N
ATOM	901	C	ARG	A	116	22.640	49.162	22.955	1.00	26.79	C
ATOM	902	O	ARG	A	116	21.921	50.131	22.901	1.00	25.84	O
ATOM	903	N	ALA	A	117	23.174	48.589	21.859	1.00	25.50	N
ATOM	904	CA	ALA	A	117	22.916	49.087	20.526	1.00	24.83	C
ATOM	905	CB	ALA	A	117	23.617	48.252	19.503	1.00	24.55	C
ATOM	906	C	ALA	A	117	21.423	49.177	20.221	1.00	26.27	C
ATOM	907	O	ALA	A	117	20.991	50.170	19.666	1.00	25.96	O
ATOM	908	N	LEU	A	118	20.633	48.176	20.630	1.00	28.06	N
ATOM	909	CA	LEU	A	118	19.175	48.156	20.403	1.00	30.15	C
ATOM	910	CB	LEU	A	118	18.535	46.816	20.834	1.00	28.28	C
ATOM	911	CG	LEU	A	118	18.890	45.592	19.978	1.00	26.73	C
ATOM	912	CD1	LEU	A	118	18.323	44.316	20.625	1.00	23.60	C
ATOM	913	CD2	LEU	A	118	18.551	45.747	18.445	1.00	19.36	C
ATOM	914	C	LEU	A	118	18.425	49.243	21.141	1.00	33.49	C
ATOM	915	O	LEU	A	118	17.328	49.597	20.738	1.00	34.26	O
ATOM	916	N	LEU	A	119	18.958	49.730	22.262	1.00	37.01	N
ATOM	917	CA	LEU	A	119	18.163	50.641	23.067	1.00	40.25	C
ATOM	918	CB	LEU	A	119	18.245	50.368	24.573	1.00	40.28	C
ATOM	919	CG	LEU	A	119	19.496	49.992	25.366	1.00	42.24	C
ATOM	920	CD1	LEU	A	119	20.677	51.138	25.505	1.00	44.50	C
ATOM	921	CD2	LEU	A	119	19.020	49.531	26.725	1.00	39.51	C
ATOM	922	C	LEU	A	119	18.496	52.058	22.704	1.00	42.83	C
ATOM	923	O	LEU	A	119	18.006	53.005	23.346	1.00	43.04	O
ATOM	924	N	SER	A	120	19.277	52.186	21.622	1.00	45.43	N
ATOM	925	CA	SER	A	120	19.840	53.470	21.222	1.00	47.93	C
ATOM	926	CB	SER	A	120	21.365	53.378	20.889	1.00	47.58	C
ATOM	927	OG	SER	A	120	21.653	52.891	19.583	1.00	45.53	O
ATOM	928	C	SER	A	120	19.054	54.194	20.131	1.00	49.80	C
ATOM	929	O	SER	A	120	19.501	54.286	19.008	1.00	50.21	O
ATOM	930	N	GLY	A	121	17.889	54.729	20.474	1.00	52.03	N
ATOM	931	CA	GLY	A	121	17.262	55.732	19.619	1.00	54.16	C
ATOM	932	C	GLY	A	121	15.765	55.583	19.729	1.00	55.85	C
ATOM	933	O	GLY	A	121	15.029	56.449	20.308	1.00	56.66	O
ATOM	934	N	SER	A	122	15.305	54.456	19.182	1.00	55.84	N
ATOM	935	CA	SER	A	122	13.944	54.046	19.458	1.00	55.43	C
ATOM	936	CB	SER	A	122	13.323	53.255	18.307	1.00	55.58	C
ATOM	937	OG	SER	A	122	12.847	54.149	17.312	1.00	55.39	O
ATOM	938	C	SER	A	122	13.860	53.341	20.823	1.00	54.71	C
ATOM	939	O	SER	A	122	14.392	52.213	21.026	1.00	54.73	O
ATOM	940	N	ASN	A	123	13.381	54.157	21.781	1.00	52.84	N
ATOM	941	CA	ASN	A	123	12.287	53.813	22.683	1.00	49.95	C
ATOM	942	CB	ASN	A	123	12.409	54.527	24.053	1.00	51.19	C
ATOM	943	CG	ASN	A	123	12.687	53.523	25.243	1.00	54.07	C
ATOM	944	OD1	ASN	A	123	12.220	53.729	26.393	1.00	51.68	O
ATOM	945	ND2	ASN	A	123	13.447	52.425	24.944	1.00	56.52	N
ATOM	946	C	ASN	A	123	11.153	54.377	21.815	1.00	46.56	C
ATOM	947	O	ASN	A	123	11.401	55.361	21.111	1.00	47.75	O
ATOM	948	N	PRO	A	124	9.937	53.823	21.821	1.00	42.45	N
ATOM	949	CA	PRO	A	124	9.383	52.996	22.908	1.00	38.79	C
ATOM	950	CB	PRO	A	124	7.994	52.612	22.371	1.00	38.26	C
ATOM	951	CG	PRO	A	124	8.137	52.699	20.904	1.00	40.81	C
ATOM	952	CD	PRO	A	124	8.995	53.945	20.691	1.00	42.10	C
ATOM	953	C	PRO	A	124	10.207	51.745	23.273	1.00	35.01	C
ATOM	954	O	PRO	A	124	11.069	51.303	22.516	1.00	34.14	O
ATOM	955	N	PRO	A	125	9.945	51.194	24.442	1.00	32.31	N
ATOM	956	CA	PRO	A	125	10.600	49.946	24.831	1.00	31.12	C
ATOM	957	CB	PRO	A	125	10.197	49.755	26.301	1.00	30.53	C
ATOM	958	CG	PRO	A	125	9.512	50.992	26.699	1.00	32.36	C
ATOM	959	CD	PRO	A	125	9.016	51.702	25.474	1.00	31.76	C
ATOM	960	C	PRO	A	125	10.094	48.785	23.988	1.00	30.23	C
ATOM	961	O	PRO	A	125	9.026	48.865	23.368	1.00	30.66	O
ATOM	962	N	TYR	A	126	10.888	47.728	23.926	1.00	28.51	N
ATOM	963	CA	TYR	A	126	10.447	46.472	23.353	1.00	26.99	C
ATOM	964	CB	TYR	A	126	11.670	45.608	23.083	1.00	26.64	C
ATOM	965	CG	TYR	A	126	12.631	46.286	22.143	1.00	22.34	C
ATOM	966	CD1	TYR	A	126	13.761	46.943	22.636	1.00	21.11	C
ATOM	967	CE1	TYR	A	126	14.645	47.586	21.793	1.00	19.27	C
ATOM	968	CZ	TYR	A	126	14.412	47.584	20.393	1.00	20.18	C
ATOM	969	OH	TYR	A	126	15.300	48.263	19.587	1.00	19.55	O
ATOM	970	CE2	TYR	A	126	13.278	46.989	19.857	1.00	18.19	C
ATOM	971	CD2	TYR	A	126	12.378	46.333	20.745	1.00	22.38	C
ATOM	972	C	TYR	A	126	9.506	45.792	24.324	1.00	26.51	C
ATOM	973	O	TYR	A	126	9.736	45.951	25.539	1.00	25.01	O
ATOM	974	N	LEU	A	127	8.422	45.140	23.831	1.00	26.39	N
ATOM	975	CA	LEU	A	127	7.678	44.234	24.720	1.00	27.32	C
ATOM	976	CB	LEU	A	127	6.111	43.982	24.567	1.00	28.19	C
ATOM	977	CG	LEU	A	127	5.285	44.099	23.325	1.00	31.03	C
ATOM	978	CD1	LEU	A	127	6.370	44.305	22.311	1.00	33.21	C
ATOM	979	CD2	LEU	A	127	4.359	42.887	23.003	1.00	24.43	C
ATOM	980	C	LEU	A	127	8.399	42.956	24.888	1.00	26.39	C
ATOM	981	O	LEU	A	127	8.897	42.389	23.924	1.00	26.55	O
ATOM	982	N	PRO	A	128	8.442	42.529	26.151	1.00	25.75	N
ATOM	983	CA	PRO	A	128	9.022	41.236	26.543	1.00	24.92	C
ATOM	984	CB	PRO	A	128	8.809	41.211	28.043	1.00	23.92	C
ATOM	985	CG	PRO	A	128	8.688	42.697	28.423	1.00	27.53	C
ATOM	986	CD	PRO	A	128	7.904	43.297	27.301	1.00	24.75	C
ATOM	987	C	PRO	A	128	8.297	40.046	25.928	1.00	24.31	C
ATOM	988	O	PRO	A	128	7.101	40.102	25.689	1.00	23.14	O
ATOM	989	N	PHE	A	129	9.033	38.971	25.685	1.00	24.18	N
ATOM	990	CA	PHE	A	129	8.374	37.760	25.287	1.00	24.67	C
ATOM	991	CB	PHE	A	129	9.350	36.757	24.651	1.00	23.51	C
ATOM	992	CG	PHE	A	129	10.036	37.301	23.432	1.00	21.95	C
ATOM	993	CD1	PHE	A	129	11.439	37.538	23.426	1.00	22.34	C
ATOM	994	CE1	PHE	A	129	12.075	38.067	22.268	1.00	21.31	C
ATOM	995	CZ	PHE	A	129	11.296	38.390	21.150	1.00	18.80	C
ATOM	996	CE2	PHE	A	129	9.914	38.172	21.155	1.00	15.81	C
ATOM	997	CD2	PHE	A	129	9.294	37.649	22.297	1.00	20.43	C
ATOM	998	C	PHE	A	129	7.526	37.189	26.434	1.00	25.75	C
ATOM	999	O	PHE	A	129	7.782	37.398	27.634	1.00	25.54	O
ATOM	1000	N	ARG	A	130	6.532	36.428	26.015	1.00	25.77	N
ATOM	1001	CA	ARG	A	130	5.448	35.987	26.867	1.00	26.47	C
ATOM	1002	CB	ARG	A	130	4.262	36.752	26.330	1.00	26.57	C
ATOM	1003	CG	ARG	A	130	3.027	36.625	26.987	1.00	28.73	C
ATOM	1004	CD	ARG	A	130	1.874	36.157	26.079	1.00	25.43	C
ATOM	1005	NE	ARG	A	130	1.360	35.038	26.884	1.00	27.32	N
ATOM	1006	CZ	ARG	A	130	0.278	35.046	27.615	1.00	18.67	C
ATOM	1007	NH1	ARG	A	130	−0.558	36.083	27.607	1.00	17.78	N
ATOM	1008	NH2	ARG	A	130	0.005	33.970	28.300	1.00	21.18	N
ATOM	1009	C	ARG	A	130	5.293	34.468	26.605	1.00	26.27	C
ATOM	1010	O	ARG	A	130	5.758	33.965	25.579	1.00	25.79	O
ATOM	1011	N	ASP	A	131	4.631	33.748	27.503	1.00	25.84	N
ATOM	1012	CA	ASP	A	131	4.573	32.290	27.422	1.00	24.74	C
ATOM	1013	CB	ASP	A	131	4.650	31.694	28.824	1.00	24.29	C
ATOM	1014	CG	ASP	A	131	3.282	31.656	29.548	1.00	26.41	C
ATOM	1015	OD1	ASP	A	131	2.262	32.247	29.099	1.00	23.77	O
ATOM	1016	OD2	ASP	A	131	3.127	31.019	30.606	1.00	28.99	O
ATOM	1017	C	ASP	A	131	3.347	31.828	26.629	1.00	24.73	C
ATOM	1018	O	ASP	A	131	2.663	32.647	26.042	1.00	23.44	O
ATOM	1019	N	ALA	A	132	3.062	30.524	26.600	1.00	25.90	N
ATOM	1020	CA	ALA	A	132	1.988	30.004	25.730	1.00	26.46	C
ATOM	1021	CB	ALA	A	132	2.461	28.828	24.910	1.00	26.22	C
ATOM	1022	C	ALA	A	132	0.748	29.622	26.503	1.00	27.31	C
ATOM	1023	O	ALA	A	132	−0.067	28.834	26.021	1.00	28.17	O
ATOM	1024	N	SER	A	133	0.569	30.191	27.689	1.00	27.45	N
ATOM	1025	CA	SER	A	133	−0.614	29.881	28.474	1.00	27.16	C
ATOM	1026	CB	SER	A	133	−0.332	30.032	29.997	1.00	27.00	C
ATOM	1027	OG	SER	A	133	−0.354	31.385	30.504	1.00	29.17	O
ATOM	1028	C	SER	A	133	−1.754	30.758	27.970	1.00	28.05	C
ATOM	1029	O	SER	A	133	−1.494	31.793	27.322	1.00	28.39	O
ATOM	1030	N	PHE	A	134	−3.006	30.313	28.184	1.00	28.59	N
ATOM	1031	CA	PHE	A	134	−4.192	31.162	28.147	1.00	29.09	C
ATOM	1032	CB	PHE	A	134	−5.430	30.313	28.419	1.00	29.62	C
ATOM	1033	CG	PHE	A	134	−5.650	29.134	27.465	1.00	29.14	C
ATOM	1034	CD1	PHE	A	134	−6.493	28.050	27.867	1.00	29.61	C
ATOM	1035	CE1	PHE	A	134	−6.782	26.948	27.014	1.00	28.32	C
ATOM	1036	CZ	PHE	A	134	−6.210	26.921	25.709	1.00	31.09	C
ATOM	1037	CE2	PHE	A	134	−5.360	28.000	25.289	1.00	30.12	C
ATOM	1038	CD2	PHE	A	134	−5.118	29.117	26.177	1.00	29.55	C
ATOM	1039	C	PHE	A	134	−3.991	32.134	29.315	1.00	30.40	C
ATOM	1040	O	PHE	A	134	−3.250	31.860	30.252	1.00	31.30	O
ATOM	1041	N	GLY	A	135	−4.565	33.302	29.345	1.00	31.88	N
ATOM	1042	CA	GLY	A	135	−4.231	34.062	30.570	1.00	32.41	C
ATOM	1043	C	GLY	A	135	−2.912	34.862	30.618	1.00	33.07	C
ATOM	1044	O	GLY	A	135	−2.093	34.846	29.680	1.00	32.39	O
ATOM	1045	N	ASN	A	136	−2.724	35.560	31.739	1.00	33.50	N
ATOM	1046	CA	ASN	A	136	−1.743	36.645	31.893	1.00	34.47	C
ATOM	1047	CB	ASN	A	136	−2.160	37.621	33.016	1.00	34.16	C
ATOM	1048	CG	ASN	A	136	−1.378	38.954	32.978	1.00	40.33	C
ATOM	1049	OD1	ASN	A	136	−1.309	39.644	31.922	1.00	46.32	O
ATOM	1050	ND2	ASN	A	136	−0.784	39.336	34.132	1.00	40.72	N
ATOM	1051	C	ASN	A	136	−0.409	36.026	32.232	1.00	34.00	C
ATOM	1052	O	ASN	A	136	−0.349	35.067	33.025	1.00	35.04	O
ATOM	1053	N	CYS	A	137	0.643	36.569	31.638	1.00	31.87	N
ATOM	1054	CA	CYS	A	137	1.979	36.077	31.852	1.00	30.52	C
ATOM	1055	CB	CYS	A	137	2.661	35.634	30.539	1.00	30.04	C
ATOM	1056	SG	CYS	A	137	4.459	35.252	30.701	1.00	29.14	S
ATOM	1057	C	CYS	A	137	2.766	37.199	32.503	1.00	30.36	C
ATOM	1058	O	CYS	A	137	2.712	38.370	32.090	1.00	30.44	O
ATOM	1059	N	THR	A	138	3.539	36.810	33.495	1.00	29.99	N
ATOM	1060	CA	THR	A	138	4.212	37.750	34.364	1.00	31.65	C
ATOM	1061	CB	THR	A	138	3.767	37.396	35.803	1.00	32.14	C
ATOM	1062	OG1	THR	A	138	2.537	38.090	36.064	1.00	34.20	O
ATOM	1063	CG2	THR	A	138	4.765	37.873	36.838	1.00	33.17	C
ATOM	1064	C	THR	A	138	5.743	37.692	34.205	1.00	30.66	C
ATOM	1065	O	THR	A	138	6.458	38.638	34.608	1.00	30.21	O
ATOM	1066	N	TYR	A	139	6.204	36.546	33.669	1.00	29.09	N
ATOM	1067	CA	TYR	A	139	7.611	36.268	33.426	1.00	27.63	C
ATOM	1068	CB	TYR	A	139	7.889	34.743	33.415	1.00	27.44	C
ATOM	1069	CG	TYR	A	139	9.360	34.431	33.299	1.00	27.17	C
ATOM	1070	CD1	TYR	A	139	10.019	34.464	32.038	1.00	24.30	C
ATOM	1071	CE1	TYR	A	139	11.423	34.265	31.957	1.00	24.67	C
ATOM	1072	CZ	TYR	A	139	12.160	34.010	33.107	1.00	21.51	C
ATOM	1073	OH	TYR	A	139	13.496	33.755	32.996	1.00	22.68	O
ATOM	1074	CE2	TYR	A	139	11.541	33.948	34.343	1.00	22.48	C
ATOM	1075	CD2	TYR	A	139	10.135	34.180	34.444	1.00	24.80	C
ATOM	1076	C	TYR	A	139	7.883	36.909	32.069	1.00	27.07	C
ATOM	1077	O	TYR	A	139	7.316	36.501	31.055	1.00	26.68	O
ATOM	1078	N	ASN	A	140	8.693	37.959	32.075	1.00	26.50	N
ATOM	1079	CA	ASN	A	140	8.924	38.774	30.879	1.00	26.51	C
ATOM	1080	CB	ASN	A	140	9.042	40.254	31.238	1.00	25.51	C
ATOM	1081	CG	ASN	A	140	7.713	40.892	31.645	1.00	28.62	C
ATOM	1082	OD1	ASN	A	140	6.625	40.507	31.217	1.00	30.72	O
ATOM	1083	ND2	ASN	A	140	7.811	41.877	32.489	1.00	30.10	N
ATOM	1084	C	ASN	A	140	10.258	38.315	30.371	1.00	26.60	C
ATOM	1085	O	ASN	A	140	11.303	38.590	31.000	1.00	28.63	O
ATOM	1086	N	LEU	A	141	10.255	37.561	29.288	1.00	25.69	N
ATOM	1087	CA	LEU	A	141	11.520	37.099	28.716	1.00	24.92	C
ATOM	1088	CB	LEU	A	141	11.351	35.715	28.036	1.00	23.68	C
ATOM	1089	CG	LEU	A	141	12.586	35.119	27.357	1.00	21.71	C
ATOM	1090	CD1	LEU	A	141	13.550	34.422	28.422	1.00	17.75	C
ATOM	1091	CD2	LEU	A	141	12.111	34.113	26.273	1.00	16.16	C
ATOM	1092	C	LEU	A	141	11.996	38.168	27.719	1.00	24.66	C
ATOM	1093	O	LEU	A	141	11.392	38.299	26.680	1.00	25.07	O
ATOM	1094	N	THR	A	142	13.023	38.948	28.055	1.00	24.46	N
ATOM	1095	CA	THR	A	142	13.458	40.061	27.190	1.00	24.86	C
ATOM	1096	CB	THR	A	142	14.148	41.215	28.029	1.00	25.61	C
ATOM	1097	OG1	THR	A	142	15.495	40.819	28.312	1.00	24.93	O
ATOM	1098	CG2	THR	A	142	13.502	41.401	29.447	1.00	22.18	C
ATOM	1099	C	THR	A	142	14.432	39.645	26.083	1.00	25.39	C
ATOM	1100	O	THR	A	142	15.089	38.562	26.117	1.00	25.52	O
ATOM	1101	N	ILE	A	143	14.585	40.553	25.125	1.00	25.46	N
ATOM	1102	CA	ILE	A	143	15.592	40.368	24.075	1.00	25.21	C
ATOM	1103	CB	ILE	A	143	15.621	41.589	23.130	1.00	25.23	C
ATOM	1104	CG1	ILE	A	143	14.283	41.725	22.363	1.00	24.13	C
ATOM	1105	CD1	ILE	A	143	13.974	43.153	21.870	1.00	19.79	C
ATOM	1106	CG2	ILE	A	143	16.798	41.475	22.179	1.00	23.27	C
ATOM	1107	C	ILE	A	143	16.997	40.099	24.646	1.00	25.28	C
ATOM	1108	O	ILE	A	143	17.801	39.365	24.020	1.00	26.31	O
ATOM	1109	N	LEU	A	144	17.326	40.708	25.787	1.00	23.71	N
ATOM	1110	CA	LEU	A	144	18.646	40.457	26.404	1.00	23.32	C
ATOM	1111	CB	LEU	A	144	18.959	41.474	27.479	1.00	23.06	C
ATOM	1112	CG	LEU	A	144	20.236	41.277	28.259	1.00	23.66	C
ATOM	1113	CD1	LEU	A	144	21.489	41.498	27.371	1.00	21.51	C
ATOM	1114	CD2	LEU	A	144	20.222	42.231	29.537	1.00	23.81	C
ATOM	1115	C	LEU	A	144	18.792	39.032	26.965	1.00	23.36	C
ATOM	1116	O	LEU	A	144	19.888	38.414	26.784	1.00	23.64	O
ATOM	1117	N	ASP	A	145	17.726	38.526	27.640	1.00	21.96	N
ATOM	1118	CA	ASP	A	145	17.644	37.119	27.994	1.00	21.81	C
ATOM	1119	CB	ASP	A	145	16.282	36.709	28.628	1.00	21.69	C
ATOM	1120	CG	ASP	A	145	15.913	37.562	29.833	1.00	24.03	C
ATOM	1121	OD1	ASP	A	145	16.833	38.066	30.507	1.00	24.77	O
ATOM	1122	OD2	ASP	A	145	14.728	37.803	30.185	1.00	26.80	O
ATOM	1123	C	ASP	A	145	17.894	36.281	26.746	1.00	21.79	C
ATOM	1124	O	ASP	A	145	18.666	35.281	26.799	1.00	21.14	O
ATOM	1125	N	CYS	A	146	17.245	36.650	25.629	1.00	20.55	N
ATOM	1126	CA	CYS	A	146	17.371	35.792	24.453	1.00	20.45	C
ATOM	1127	CB	CYS	A	146	16.357	36.156	23.374	1.00	19.54	C
ATOM	1128	SG	CYS	A	146	14.598	35.956	23.930	1.00	20.53	S
ATOM	1129	C	CYS	A	146	18.832	35.779	23.953	1.00	21.59	C
ATOM	1130	O	CYS	A	146	19.417	34.704	23.680	1.00	22.81	O
ATOM	1131	N	LEU	A	147	19.438	36.960	23.892	1.00	22.04	N
ATOM	1132	CA	LEU	A	147	20.798	37.126	23.435	1.00	23.01	C
ATOM	1133	CB	LEU	A	147	21.103	38.631	23.344	1.00	24.08	C
ATOM	1134	CG	LEU	A	147	20.277	39.337	22.260	1.00	24.35	C
ATOM	1135	CD1	LEU	A	147	20.757	40.790	21.963	1.00	24.20	C
ATOM	1136	CD2	LEU	A	147	20.369	38.494	21.013	1.00	22.13	C
ATOM	1137	C	LEU	A	147	21.767	36.400	24.355	1.00	22.97	C
ATOM	1138	O	LEU	A	147	22.663	35.712	23.873	1.00	23.50	O
ATOM	1139	N	GLN	A	148	21.568	36.504	25.670	1.00	23.59	N
ATOM	1140	CA	GLN	A	148	22.360	35.718	26.643	1.00	24.35	C
ATOM	1141	CB	GLN	A	148	22.014	36.089	28.084	1.00	24.65	C
ATOM	1142	CG	GLN	A	148	22.367	37.533	28.439	1.00	26.89	C
ATOM	1143	CD	GLN	A	148	22.030	37.903	29.858	1.00	28.07	C
ATOM	1144	OE1	GLN	A	148	21.033	37.428	30.439	1.00	32.47	O
ATOM	1145	NE2	GLN	A	148	22.830	38.776	30.414	1.00	29.22	N
ATOM	1146	C	GLN	A	148	22.167	34.220	26.490	1.00	25.26	C
ATOM	1147	O	GLN	A	148	23.146	33.439	26.625	1.00	26.88	O
ATOM	1148	N	GLY	A	149	20.928	33.806	26.224	1.00	23.85	N
ATOM	1149	CA	GLY	A	149	20.653	32.409	25.910	1.00	23.60	C
ATOM	1150	C	GLY	A	149	21.367	31.960	24.664	1.00	23.74	C
ATOM	1151	O	GLY	A	149	21.987	30.866	24.663	1.00	23.01	O
ATOM	1152	N	ILE	A	150	21.310	32.799	23.615	1.00	23.39	N
ATOM	1153	CA	ILE	A	150	22.057	32.526	22.397	1.00	24.08	C
ATOM	1154	CB	ILE	A	150	21.807	33.600	21.312	1.00	24.63	C
ATOM	1155	CG1	ILE	A	150	20.376	33.453	20.716	1.00	23.89	C
ATOM	1156	CD1	ILE	A	150	20.238	32.293	19.678	1.00	23.89	C
ATOM	1157	CG2	ILE	A	150	22.933	33.499	20.225	1.00	22.80	C
ATOM	1158	C	ILE	A	150	23.569	32.390	22.662	1.00	25.15	C
ATOM	1159	O	ILE	A	150	24.210	31.461	22.188	1.00	23.67	O
ATOM	1160	N	ARG	A	151	24.119	33.326	23.438	1.00	26.84	N
ATOM	1161	CA	ARG	A	151	25.540	33.324	23.740	1.00	29.01	C
ATOM	1162	CB	ARG	A	151	25.946	34.568	24.530	1.00	29.88	C
ATOM	1163	CG	ARG	A	151	27.466	34.733	24.539	1.00	36.14	C
ATOM	1164	CD	ARG	A	151	27.998	35.469	25.726	1.00	45.97	C
ATOM	1165	NE	ARG	A	151	28.346	34.540	26.803	1.00	54.94	N
ATOM	1166	CZ	ARG	A	151	27.700	34.482	27.970	1.00	57.24	C
ATOM	1167	NH1	ARG	A	151	26.651	35.293	28.225	1.00	55.92	N
ATOM	1168	NH2	ARG	A	151	28.113	33.610	28.874	1.00	57.54	N
ATOM	1169	C	ARG	A	151	26.001	32.068	24.495	1.00	28.39	C
ATOM	1170	O	ARG	A	151	27.092	31.522	24.218	1.00	27.88	O
ATOM	1171	N	LYS	A	152	25.173	31.651	25.454	1.00	28.26	N
ATOM	1172	CA	LYS	A	152	25.469	30.517	26.328	1.00	28.39	C
ATOM	1173	CB	LYS	A	152	24.655	30.648	27.637	1.00	28.19	C
ATOM	1174	CG	LYS	A	152	25.286	30.028	28.948	1.00	31.16	C
ATOM	1175	CD	LYS	A	152	26.406	30.824	29.609	1.00	32.05	C
ATOM	1176	CE	LYS	A	152	26.001	31.318	31.007	1.00	37.78	C
ATOM	1177	NZ	LYS	A	152	26.976	32.373	31.591	1.00	40.05	N
ATOM	1178	C	LYS	A	152	25.299	29.153	25.563	1.00	28.23	C
ATOM	1179	O	LYS	A	152	26.095	28.224	25.789	1.00	28.57	O
ATOM	1180	N	GLY	A	153	24.335	29.074	24.625	1.00	26.69	N
ATOM	1181	CA	GLY	A	153	24.224	27.954	23.692	1.00	26.81	C
ATOM	1182	C	GLY	A	153	25.430	27.808	22.784	1.00	27.48	C
ATOM	1183	O	GLY	A	153	25.924	26.720	22.536	1.00	26.19	O
ATOM	1184	N	LEU	A	154	25.921	28.940	22.303	1.00	29.26	N
ATOM	1185	CA	LEU	A	154	27.121	28.986	21.492	1.00	31.32	C
ATOM	1186	CB	LEU	A	154	27.382	30.426	21.008	1.00	31.37	C
ATOM	1187	CG	LEU	A	154	28.211	30.534	19.720	1.00	29.91	C
ATOM	1188	CD1	LEU	A	154	27.762	29.539	18.710	1.00	28.79	C
ATOM	1189	CD2	LEU	A	154	28.029	31.923	19.179	1.00	31.99	C
ATOM	1190	C	LEU	A	154	28.323	28.486	22.268	1.00	33.26	C
ATOM	1191	O	LEU	A	154	29.074	27.594	21.780	1.00	34.36	O
ATOM	1192	N	GLN	A	155	28.485	29.063	23.470	1.00	34.05	N
ATOM	1193	CA	GLN	A	155	29.617	28.841	24.382	1.00	35.31	C
ATOM	1194	CB	GLN	A	155	29.368	29.645	25.684	1.00	36.22	C
ATOM	1195	CG	GLN	A	155	30.582	30.047	26.563	1.00	42.94	C
ATOM	1196	CD	GLN	A	155	30.943	31.570	26.415	1.00	52.44	C
ATOM	1197	OE1	GLN	A	155	30.097	32.463	26.705	1.00	54.15	O
ATOM	1198	NE2	GLN	A	155	32.194	31.863	25.946	1.00	53.26	N
ATOM	1199	C	GLN	A	155	29.768	27.315	24.642	1.00	34.24	C
ATOM	1200	O	GLN	A	155	30.861	26.759	24.569	1.00	33.35	O
ATOM	1201	N	HIS	A	156	28.645	26.638	24.882	1.00	33.47	N
ATOM	1202	CA	HIS	A	156	28.678	25.187	25.085	1.00	32.43	C
ATOM	1203	CB	HIS	A	156	27.774	24.829	26.240	1.00	31.60	C
ATOM	1204	CG	HIS	A	156	28.247	25.407	27.528	1.00	31.75	C
ATOM	1205	ND1	HIS	A	156	27.744	26.591	28.043	1.00	30.94	N
ATOM	1206	CE1	HIS	A	156	28.373	26.869	29.175	1.00	33.28	C
ATOM	1207	NE2	HIS	A	156	29.278	25.923	29.399	1.00	33.82	N
ATOM	1208	CD2	HIS	A	156	29.234	25.006	28.371	1.00	31.29	C
ATOM	1209	C	HIS	A	156	28.466	24.268	23.870	1.00	31.74	C
ATOM	1210	O	HIS	A	156	28.266	23.099	24.054	1.00	30.84	O
ATOM	1211	N	GLY	A	157	28.560	24.805	22.641	1.00	31.76	N
ATOM	1212	CA	GLY	A	157	28.396	24.016	21.414	1.00	30.84	C
ATOM	1213	C	GLY	A	157	26.980	23.446	21.211	1.00	30.55	C
ATOM	1214	O	GLY	A	157	26.836	22.365	20.626	1.00	30.95	O
ATOM	1215	N	PHE	A	158	25.947	24.152	21.687	1.00	28.74	N
ATOM	1216	CA	PHE	A	158	24.571	23.655	21.609	1.00	28.97	C
ATOM	1217	CB	PHE	A	158	23.627	24.341	22.629	1.00	29.04	C
ATOM	1218	CG	PHE	A	158	23.797	23.865	24.078	1.00	27.97	C
ATOM	1219	CD1	PHE	A	158	22.916	24.288	25.058	1.00	28.65	C
ATOM	1220	CE1	PHE	A	158	23.064	23.862	26.393	1.00	29.02	C
ATOM	1221	CZ	PHE	A	158	24.089	23.000	26.736	1.00	26.60	C
ATOM	1222	CE2	PHE	A	158	24.975	22.585	25.779	1.00	28.52	C
ATOM	1223	CD2	PHE	A	158	24.826	23.013	24.447	1.00	27.88	C
ATOM	1224	C	PHE	A	158	24.040	23.907	20.206	1.00	29.45	C
ATOM	1225	O	PHE	A	158	23.023	23.357	19.819	1.00	29.58	O
ATOM	1226	N	PHE	A	159	24.731	24.770	19.464	1.00	29.35	N
ATOM	1227	CA	PHE	A	159	24.491	24.941	18.039	1.00	28.99	C
ATOM	1228	CB	PHE	A	159	23.280	25.863	17.764	1.00	28.70	C
ATOM	1229	CG	PHE	A	159	23.546	27.320	17.960	1.00	26.56	C
ATOM	1230	CD1	PHE	A	159	23.736	28.165	16.859	1.00	28.40	C
ATOM	1231	CE1	PHE	A	159	23.957	29.564	17.017	1.00	24.25	C
ATOM	1232	CZ	PHE	A	159	23.953	30.078	18.270	1.00	21.56	C
ATOM	1233	CE2	PHE	A	159	23.771	29.220	19.377	1.00	22.57	C
ATOM	1234	CD2	PHE	A	159	23.557	27.865	19.210	1.00	22.83	C
ATOM	1235	C	PHE	A	159	25.720	25.463	17.321	1.00	29.25	C
ATOM	1236	O	PHE	A	159	26.619	26.033	17.908	1.00	29.22	O
ATOM	1237	N	ASP	A	160	25.723	25.282	16.022	1.00	30.21	N
ATOM	1238	CA	ASP	A	160	26.841	25.679	15.194	1.00	31.35	C
ATOM	1239	CB	ASP	A	160	27.866	24.520	15.071	1.00	31.26	C
ATOM	1240	CG	ASP	A	160	29.181	24.968	14.450	1.00	33.00	C
ATOM	1241	OD1	ASP	A	160	29.287	26.150	14.017	1.00	34.51	O
ATOM	1242	OD2	ASP	A	160	30.164	24.191	14.350	1.00	36.44	O
ATOM	1243	C	ASP	A	160	26.253	25.933	13.847	1.00	30.90	C
ATOM	1244	O	ASP	A	160	25.877	24.979	13.127	1.00	30.50	O
ATOM	1245	N	PHE	A	161	26.184	27.205	13.488	1.00	31.02	N
ATOM	1246	CA	PHE	A	161	25.593	27.561	12.196	1.00	31.11	C
ATOM	1247	CB	PHE	A	161	25.251	29.039	12.138	1.00	30.24	C
ATOM	1248	CG	PHE	A	161	23.980	29.390	12.815	1.00	28.13	C
ATOM	1249	CD1	PHE	A	161	23.651	30.746	13.042	1.00	27.47	C
ATOM	1250	CE1	PHE	A	161	22.445	31.105	13.675	1.00	24.39	C
ATOM	1251	CZ	PHE	A	161	21.538	30.085	14.073	1.00	24.13	C
ATOM	1252	CE2	PHE	A	161	21.867	28.745	13.838	1.00	24.09	C
ATOM	1253	CD2	PHE	A	161	23.079	28.407	13.193	1.00	26.67	C
ATOM	1254	C	PHE	A	161	26.486	27.115	11.003	1.00	32.30	C
ATOM	1255	O	PHE	A	161	26.053	27.161	9.825	1.00	32.47	O
ATOM	1256	N	GLU	A	162	27.707	26.663	11.287	1.00	33.13	N
ATOM	1257	CA	GLU	A	162	28.495	26.052	10.212	1.00	34.78	C
ATOM	1258	CB	GLU	A	162	29.982	26.100	10.500	1.00	35.08	C
ATOM	1259	CG	GLU	A	162	30.638	27.343	9.910	1.00	42.53	C
ATOM	1260	CD	GLU	A	162	32.009	27.616	10.528	1.00	52.76	C
ATOM	1261	OE1	GLU	A	162	32.602	26.674	11.133	1.00	55.95	O
ATOM	1262	OE2	GLU	A	162	32.500	28.774	10.427	1.00	55.62	O
ATOM	1263	C	GLU	A	162	28.039	24.649	9.824	1.00	34.02	C
ATOM	1264	O	GLU	A	162	28.167	24.286	8.685	1.00	34.49	O
ATOM	1265	N	THR	A	163	27.484	23.861	10.744	1.00	33.62	N
ATOM	1266	CA	THR	A	163	27.070	22.481	10.420	1.00	32.12	C
ATOM	1267	CB	THR	A	163	27.629	21.439	11.460	1.00	33.09	C
ATOM	1268	OG1	THR	A	163	27.349	21.875	12.801	1.00	31.88	O
ATOM	1269	CG2	THR	A	163	29.173	21.336	11.422	1.00	34.37	C
ATOM	1270	C	THR	A	163	25.568	22.334	10.423	1.00	31.00	C
ATOM	1271	O	THR	A	163	25.070	21.327	9.914	1.00	31.20	O
ATOM	1272	N	PHE	A	164	24.853	23.284	11.064	1.00	29.22	N
ATOM	1273	CA	PHE	A	164	23.395	23.234	11.248	1.00	26.33	C
ATOM	1274	CB	PHE	A	164	22.895	24.592	11.639	1.00	26.85	C
ATOM	1275	CG	PHE	A	164	21.399	24.681	11.887	1.00	24.78	C
ATOM	1276	CD1	PHE	A	164	20.788	23.940	12.905	1.00	23.14	C
ATOM	1277	CE1	PHE	A	164	19.458	24.077	13.173	1.00	24.88	C
ATOM	1278	CZ	PHE	A	164	18.674	25.000	12.472	1.00	23.98	C
ATOM	1279	CE2	PHE	A	164	19.246	25.754	11.465	1.00	26.35	C
ATOM	1280	CD2	PHE	A	164	20.622	25.591	11.171	1.00	26.63	C
ATOM	1281	C	PHE	A	164	22.685	22.941	9.982	1.00	26.50	C
ATOM	1282	O	PHE	A	164	22.978	23.538	8.937	1.00	26.06	O
ATOM	1283	N	ASP	A	165	21.689	22.085	10.085	1.00	26.20	N
ATOM	1284	CA	ASP	A	165	20.954	21.636	8.929	1.00	27.29	C
ATOM	1285	CB	ASP	A	165	21.047	20.088	8.821	1.00	27.81	C
ATOM	1286	CG	ASP	A	165	20.579	19.559	7.455	1.00	33.34	C
ATOM	1287	OD1	ASP	A	165	19.854	20.277	6.676	1.00	36.53	O
ATOM	1288	OD2	ASP	A	165	20.911	18.407	7.074	1.00	40.25	O
ATOM	1289	C	ASP	A	165	19.506	22.133	9.042	1.00	26.26	C
ATOM	1290	O	ASP	A	165	18.699	21.566	9.754	1.00	26.93	O
ATOM	1291	N	VAL	A	166	19.179	23.197	8.332	1.00	26.16	N
ATOM	1292	CA	VAL	A	166	17.932	23.883	8.564	1.00	25.89	C
ATOM	1293	CB	VAL	A	166	17.990	25.309	7.916	1.00	27.36	C
ATOM	1294	CG1	VAL	A	166	18.128	25.264	6.280	1.00	24.30	C
ATOM	1295	CG2	VAL	A	166	16.847	26.249	8.477	1.00	21.96	C
ATOM	1296	C	VAL	A	166	16.761	23.080	7.990	1.00	27.26	C
ATOM	1297	O	VAL	A	166	15.599	23.243	8.398	1.00	27.08	O
ATOM	1298	N	ASP	A	167	17.065	22.227	7.018	1.00	27.61	N
ATOM	1299	CA	ASP	A	167	16.059	21.384	6.416	1.00	28.47	C
ATOM	1300	CB	ASP	A	167	16.529	20.823	5.050	1.00	29.05	C
ATOM	1301	CG	ASP	A	167	16.753	21.926	4.013	1.00	30.75	C
ATOM	1302	OD1	ASP	A	167	15.913	22.841	3.892	1.00	31.04	O
ATOM	1303	OD2	ASP	A	167	17.750	21.974	3.275	1.00	32.55	O
ATOM	1304	C	ASP	A	167	15.624	20.278	7.384	1.00	28.44	C
ATOM	1305	O	ASP	A	167	14.444	19.895	7.397	1.00	28.39	O
ATOM	1306	N	GLU	A	168	16.563	19.769	8.182	1.00	28.88	N
ATOM	1307	CA	GLU	A	168	16.245	18.673	9.101	1.00	29.52	C
ATOM	1308	CB	GLU	A	168	17.498	17.917	9.619	1.00	30.17	C
ATOM	1309	CG	GLU	A	168	18.237	17.086	8.561	1.00	32.86	C
ATOM	1310	CD	GLU	A	168	18.509	15.619	8.929	1.00	37.43	C
ATOM	1311	OE1	GLU	A	168	18.933	14.856	8.015	1.00	38.97	O
ATOM	1312	OE2	GLU	A	168	18.329	15.188	10.108	1.00	39.49	O
ATOM	1313	C	GLU	A	168	15.447	19.260	10.245	1.00	29.28	C
ATOM	1314	O	GLU	A	168	14.441	18.642	10.710	1.00	29.71	O
ATOM	1315	N	TYR	A	169	15.863	20.463	10.660	1.00	27.40	N
ATOM	1316	CA	TYR	A	169	15.185	21.174	11.706	1.00	26.54	C
ATOM	1317	CB	TYR	A	169	15.857	22.518	11.962	1.00	27.66	C
ATOM	1318	CG	TYR	A	169	15.220	23.246	13.121	1.00	26.69	C
ATOM	1319	CD1	TYR	A	169	15.692	23.106	14.422	1.00	23.65	C
ATOM	1320	CE1	TYR	A	169	15.008	23.817	15.533	1.00	20.94	C
ATOM	1321	CZ	TYR	A	169	13.914	24.609	15.271	1.00	18.98	C
ATOM	1322	OH	TYR	A	169	13.236	25.297	16.261	1.00	20.44	O
ATOM	1323	CE2	TYR	A	169	13.439	24.732	13.975	1.00	22.43	C
ATOM	1324	CD2	TYR	A	169	14.101	24.078	12.911	1.00	26.21	C
ATOM	1325	C	TYR	A	169	13.735	21.402	11.365	1.00	26.33	C
ATOM	1326	O	TYR	A	169	12.838	21.064	12.165	1.00	27.10	O
ATOM	1327	N	GLU	A	170	13.507	21.977	10.186	1.00	25.59	N
ATOM	1328	CA	GLU	A	170	12.166	22.344	9.695	1.00	25.25	C
ATOM	1329	CB	GLU	A	170	12.237	23.348	8.508	1.00	25.52	C
ATOM	1330	CG	GLU	A	170	12.859	24.687	8.934	1.00	25.86	C
ATOM	1331	CD	GLU	A	170	13.088	25.676	7.794	1.00	28.33	C
ATOM	1332	OE1	GLU	A	170	12.960	25.276	6.587	1.00	33.24	O
ATOM	1333	OE2	GLU	A	170	13.384	26.868	8.105	1.00	20.68	O
ATOM	1334	C	GLU	A	170	11.296	21.160	9.317	1.00	24.78	C
ATOM	1335	O	GLU	A	170	10.071	21.290	9.317	1.00	24.84	O
ATOM	1336	N	HIS	A	171	11.909	20.010	9.022	1.00	24.26	N
ATOM	1337	CA	HIS	A	171	11.171	18.785	8.674	1.00	23.40	C
ATOM	1338	CB	HIS	A	171	12.158	17.789	8.001	1.00	22.83	C
ATOM	1339	CG	HIS	A	171	11.549	16.468	7.616	1.00	25.54	C
ATOM	1340	ND1	HIS	A	171	10.689	16.316	6.532	1.00	24.70	N
ATOM	1341	CE1	HIS	A	171	10.332	15.042	6.434	1.00	24.97	C
ATOM	1342	NE2	HIS	A	171	10.917	14.360	7.419	1.00	27.27	N
ATOM	1343	CD2	HIS	A	171	11.677	15.228	8.178	1.00	24.54	C
ATOM	1344	C	HIS	A	171	10.585	18.203	9.944	1.00	22.99	C
ATOM	1345	O	HIS	A	171	9.367	17.971	10.099	1.00	22.63	O
ATOM	1346	N	TYR	A	172	11.487	18.008	10.887	1.00	23.01	N
ATOM	1347	CA	TYR	A	172	11.188	17.274	12.100	1.00	23.19	C
ATOM	1348	CB	TYR	A	172	12.490	16.705	12.712	1.00	22.67	C
ATOM	1349	CG	TYR	A	172	13.052	15.554	11.930	1.00	25.00	C
ATOM	1350	CD1	TYR	A	172	14.381	15.597	11.454	1.00	28.66	C
ATOM	1351	CE1	TYR	A	172	14.908	14.542	10.728	1.00	28.38	C
ATOM	1352	CZ	TYR	A	172	14.103	13.428	10.478	1.00	29.24	C
ATOM	1353	OH	TYR	A	172	14.634	12.425	9.741	1.00	29.26	O
ATOM	1354	CE2	TYR	A	172	12.777	13.352	10.920	1.00	26.08	C
ATOM	1355	CD2	TYR	A	172	12.263	14.417	11.632	1.00	25.04	C
ATOM	1356	C	TYR	A	172	10.385	18.106	13.110	1.00	23.00	C
ATOM	1357	O	TYR	A	172	9.796	17.529	14.011	1.00	23.59	O
ATOM	1358	N	GLU	A	173	10.317	19.434	12.957	1.00	22.98	N
ATOM	1359	CA	GLU	A	173	9.571	20.234	13.955	1.00	23.51	C
ATOM	1360	CB	GLU	A	173	10.005	21.715	13.926	1.00	22.17	C
ATOM	1361	CG	GLU	A	173	9.439	22.479	12.734	1.00	23.15	C
ATOM	1362	CD	GLU	A	173	9.706	23.962	12.771	1.00	22.09	C
ATOM	1363	OE1	GLU	A	173	10.296	24.486	11.812	1.00	22.18	O
ATOM	1364	OE2	GLU	A	173	9.257	24.613	13.741	1.00	24.64	O
ATOM	1365	C	GLU	A	173	8.078	20.110	13.706	1.00	24.37	C
ATOM	1366	O	GLU	A	173	7.236	20.387	14.577	1.00	24.83	O
ATOM	1367	N	ARG	A	174	7.772	19.745	12.470	1.00	26.23	N
ATOM	1368	CA	ARG	A	174	6.421	19.576	11.999	1.00	27.17	C
ATOM	1369	CB	ARG	A	174	6.427	19.503	10.477	1.00	28.20	C
ATOM	1370	CG	ARG	A	174	6.812	20.772	9.730	1.00	29.82	C
ATOM	1371	CD	ARG	A	174	6.618	20.624	8.189	1.00	38.21	C
ATOM	1372	NE	ARG	A	174	7.817	21.063	7.471	1.00	43.10	N
ATOM	1373	CZ	ARG	A	174	8.432	20.373	6.500	1.00	45.83	C
ATOM	1374	NH1	ARG	A	174	7.947	19.188	6.100	1.00	46.06	N
ATOM	1375	NH2	ARG	A	174	9.548	20.867	5.938	1.00	42.94	N
ATOM	1376	C	ARG	A	174	5.787	18.308	12.569	1.00	27.32	C
ATOM	1377	O	ARG	A	174	6.425	17.239	12.705	1.00	26.29	O
ATOM	1378	N	VAL	A	175	4.504	18.433	12.884	1.00	28.58	N
ATOM	1379	CA	VAL	A	175	3.726	17.305	13.401	1.00	29.08	C
ATOM	1380	CB	VAL	A	175	2.289	17.711	13.713	1.00	29.27	C
ATOM	1381	CG1	VAL	A	175	1.567	16.539	14.471	1.00	28.96	C
ATOM	1382	CG2	VAL	A	175	2.313	18.973	14.570	1.00	30.24	C
ATOM	1383	C	VAL	A	175	3.776	16.080	12.474	1.00	28.66	C
ATOM	1384	O	VAL	A	175	4.038	14.982	12.958	1.00	29.34	O
ATOM	1385	N	GLU	A	176	3.592	16.265	11.169	1.00	28.55	N
ATOM	1386	CA	GLU	A	176	3.741	15.142	10.186	1.00	30.23	C
ATOM	1387	CB	GLU	A	176	3.545	15.522	8.658	1.00	30.04	C
ATOM	1388	CG	GLU	A	176	2.701	16.734	8.343	1.00	35.06	C
ATOM	1389	CD	GLU	A	176	3.477	18.025	8.467	1.00	42.21	C
ATOM	1390	OE1	GLU	A	176	3.304	18.697	9.503	1.00	41.78	O
ATOM	1391	OE2	GLU	A	176	4.270	18.360	7.530	1.00	46.19	O
ATOM	1392	C	GLU	A	176	5.074	14.395	10.270	1.00	29.66	C
ATOM	1393	O	GLU	A	176	5.116	13.284	9.774	1.00	30.67	O
ATOM	1394	N	ASN	A	177	6.157	14.997	10.798	1.00	28.71	N
ATOM	1395	CA	ASN	A	177	7.405	14.248	11.021	1.00	28.29	C
ATOM	1396	CB	ASN	A	177	8.531	14.799	10.160	1.00	28.16	C
ATOM	1397	CG	ASN	A	177	8.067	15.089	8.748	1.00	30.59	C
ATOM	1398	OD1	ASN	A	177	7.576	14.187	8.056	1.00	35.73	O
ATOM	1399	ND2	ASN	A	177	8.184	16.331	8.318	1.00	26.97	N
ATOM	1400	C	ASN	A	177	7.813	13.977	12.491	1.00	28.69	C
ATOM	1401	O	ASN	A	177	8.944	13.656	12.797	1.00	29.52	O
ATOM	1402	N	GLY	A	178	6.861	14.050	13.401	1.00	28.56	N
ATOM	1403	CA	GLY	A	178	7.077	13.515	14.725	1.00	28.29	C
ATOM	1404	C	GLY	A	178	7.180	14.565	15.820	1.00	28.73	C
ATOM	1405	O	GLY	A	178	7.510	14.230	16.967	1.00	28.00	O
ATOM	1406	N	ASP	A	179	6.897	15.818	15.454	1.00	28.21	N
ATOM	1407	CA	ASP	A	179	7.051	16.968	16.334	1.00	28.09	C
ATOM	1408	CB	ASP	A	179	5.736	17.217	17.068	1.00	28.08	C
ATOM	1409	CG	ASP	A	179	5.769	18.508	17.837	1.00	30.36	C
ATOM	1410	OD1	ASP	A	179	6.702	19.310	17.550	1.00	32.17	O
ATOM	1411	OD2	ASP	A	179	4.947	18.803	18.730	1.00	30.94	O
ATOM	1412	C	ASP	A	179	8.253	16.975	17.337	1.00	26.72	C
ATOM	1413	O	ASP	A	179	8.099	16.744	18.544	1.00	26.87	O
ATOM	1414	N	PHE	A	180	9.446	17.225	16.842	1.00	25.72	N
ATOM	1415	CA	PHE	A	180	10.617	17.216	17.725	1.00	24.58	C
ATOM	1416	CB	PHE	A	180	11.164	15.785	17.965	1.00	24.35	C
ATOM	1417	CG	PHE	A	180	11.967	15.175	16.803	1.00	23.08	C
ATOM	1418	CD1	PHE	A	180	13.280	15.568	16.542	1.00	25.09	C
ATOM	1419	CE1	PHE	A	180	14.011	14.999	15.507	1.00	25.23	C
ATOM	1420	CZ	PHE	A	180	13.432	13.969	14.742	1.00	25.63	C
ATOM	1421	CE2	PHE	A	180	12.137	13.574	14.988	1.00	23.36	C
ATOM	1422	CD2	PHE	A	180	11.413	14.169	16.014	1.00	22.24	C
ATOM	1423	C	PHE	A	180	11.695	18.229	17.331	1.00	24.09	C
ATOM	1424	O	PHE	A	180	11.741	18.677	16.174	1.00	23.50	O
ATOM	1425	N	ASN	A	181	12.486	18.605	18.338	1.00	22.86	N
ATOM	1426	CA	ASN	A	181	13.673	19.463	18.250	1.00	23.07	C
ATOM	1427	CB	ASN	A	181	13.321	20.877	18.712	1.00	21.79	C
ATOM	1428	CG	ASN	A	181	12.132	21.446	17.973	1.00	24.49	C
ATOM	1429	OD1	ASN	A	181	10.966	21.374	18.457	1.00	22.41	O
ATOM	1430	ND2	ASN	A	181	12.399	22.000	16.765	1.00	20.86	N
ATOM	1431	C	ASN	A	181	14.781	18.974	19.200	1.00	23.38	C
ATOM	1432	O	ASN	A	181	14.503	18.584	20.355	1.00	22.70	O
ATOM	1433	N	TRP	A	182	16.018	19.001	18.736	1.00	23.27	N
ATOM	1434	CA	TRP	A	182	17.149	18.904	19.666	1.00	25.06	C
ATOM	1435	CB	TRP	A	182	18.475	18.697	18.910	1.00	25.23	C
ATOM	1436	CG	TRP	A	182	18.528	17.268	18.364	1.00	27.65	C
ATOM	1437	CD1	TRP	A	182	18.152	16.856	17.110	1.00	29.08	C
ATOM	1438	NE1	TRP	A	182	18.297	15.492	16.996	1.00	31.04	N
ATOM	1439	CE2	TRP	A	182	18.789	14.990	18.173	1.00	31.05	C
ATOM	1440	CD2	TRP	A	182	18.926	16.083	19.073	1.00	28.54	C
ATOM	1441	CE3	TRP	A	182	19.393	15.828	20.378	1.00	24.47	C
ATOM	1442	CZ3	TRP	A	182	19.695	14.547	20.743	1.00	26.36	C
ATOM	1443	CH2	TRP	A	182	19.548	13.451	19.821	1.00	28.93	C
ATOM	1444	CZ2	TRP	A	182	19.082	13.661	18.544	1.00	30.64	C
ATOM	1445	C	TRP	A	182	17.225	20.157	20.547	1.00	24.67	C
ATOM	1446	O	TRP	A	182	17.130	21.253	20.056	1.00	24.96	O
ATOM	1447	N	ILE	A	183	17.366	19.977	21.851	1.00	25.06	N
ATOM	1448	CA	ILE	A	183	17.682	21.088	22.750	1.00	24.58	C
ATOM	1449	CB	ILE	A	183	16.909	20.949	24.058	1.00	24.64	C
ATOM	1450	CG1	ILE	A	183	15.423	20.559	23.783	1.00	22.81	C
ATOM	1451	CD1	ILE	A	183	14.529	21.630	23.056	1.00	16.30	C
ATOM	1452	CG2	ILE	A	183	17.139	22.205	24.933	1.00	21.67	C
ATOM	1453	C	ILE	A	183	19.143	21.128	23.094	1.00	26.01	C
ATOM	1454	O	ILE	A	183	19.702	22.221	23.241	1.00	27.10	O
ATOM	1455	N	VAL	A	184	19.732	19.937	23.312	1.00	26.51	N
ATOM	1456	CA	VAL	A	184	21.146	19.762	23.484	1.00	25.87	C
ATOM	1457	CB	VAL	A	184	21.564	19.495	24.947	1.00	26.64	C
ATOM	1458	CG1	VAL	A	184	23.080	19.294	25.053	1.00	24.48	C
ATOM	1459	CG2	VAL	A	184	21.097	20.641	25.935	1.00	23.34	C
ATOM	1460	C	VAL	A	184	21.564	18.607	22.601	1.00	27.80	C
ATOM	1461	O	VAL	A	184	21.165	17.418	22.832	1.00	27.84	O
ATOM	1462	N	PRO	A	185	22.379	18.946	21.587	1.00	28.75	N
ATOM	1463	CA	PRO	A	185	22.902	17.945	20.633	1.00	29.60	C
ATOM	1464	CB	PRO	A	185	23.962	18.742	19.841	1.00	29.75	C
ATOM	1465	CG	PRO	A	185	23.386	20.164	19.879	1.00	29.45	C
ATOM	1466	CD	PRO	A	185	22.872	20.305	21.285	1.00	28.09	C
ATOM	1467	C	PRO	A	185	23.568	16.766	21.378	1.00	29.43	C
ATOM	1468	O	PRO	A	185	24.381	17.020	22.297	1.00	29.15	O
ATOM	1469	N	GLY	A	186	23.220	15.529	20.988	1.00	28.64	N
ATOM	1470	CA	GLY	A	186	23.797	14.330	21.570	1.00	28.38	C
ATOM	1471	C	GLY	A	186	23.289	14.020	22.977	1.00	28.74	C
ATOM	1472	O	GLY	A	186	23.836	13.153	23.642	1.00	29.89	O
ATOM	1473	N	LYS	A	187	22.230	14.702	23.429	1.00	28.05	N
ATOM	1474	CA	LYS	A	187	21.941	14.747	24.839	1.00	26.20	C
ATOM	1475	CB	LYS	A	187	22.707	15.908	25.535	1.00	26.76	C
ATOM	1476	CG	LYS	A	187	22.700	15.774	27.113	1.00	30.34	C
ATOM	1477	CD	LYS	A	187	23.083	14.333	27.589	1.00	32.58	C
ATOM	1478	CE	LYS	A	187	23.409	14.251	29.083	1.00	37.04	C
ATOM	1479	NZ	LYS	A	187	23.782	12.872	29.420	1.00	39.18	N
ATOM	1480	C	LYS	A	187	20.480	14.832	25.113	1.00	24.99	C
ATOM	1481	O	LYS	A	187	19.945	13.999	25.840	1.00	25.34	O
ATOM	1482	N	PHE	A	188	19.815	15.837	24.542	1.00	23.98	N
ATOM	1483	CA	PHE	A	188	18.399	16.007	24.784	1.00	22.58	C
ATOM	1484	CB	PHE	A	188	18.136	17.136	25.757	1.00	22.50	C
ATOM	1485	CG	PHE	A	188	18.363	16.793	27.172	1.00	23.86	C
ATOM	1486	CD1	PHE	A	188	19.392	17.431	27.895	1.00	25.27	C
ATOM	1487	CE1	PHE	A	188	19.620	17.150	29.247	1.00	24.43	C
ATOM	1488	CZ	PHE	A	188	18.820	16.215	29.902	1.00	25.35	C
ATOM	1489	CE2	PHE	A	188	17.770	15.556	29.195	1.00	29.14	C
ATOM	1490	CD2	PHE	A	188	17.546	15.860	27.824	1.00	27.02	C
ATOM	1491	C	PHE	A	188	17.646	16.290	23.499	1.00	23.01	C
ATOM	1492	O	PHE	A	188	17.946	17.250	22.735	1.00	22.53	O
ATOM	1493	N	LEU	A	189	16.661	15.440	23.288	1.00	22.98	N
ATOM	1494	CA	LEU	A	189	15.670	15.597	22.250	1.00	24.38	C
ATOM	1495	CB	LEU	A	189	15.625	14.328	21.351	1.00	24.36	C
ATOM	1496	CG	LEU	A	189	14.620	14.323	20.172	1.00	23.50	C
ATOM	1497	CD1	LEU	A	189	15.134	13.571	18.945	1.00	21.90	C
ATOM	1498	CD2	LEU	A	189	13.281	13.789	20.635	1.00	19.56	C
ATOM	1499	C	LEU	A	189	14.308	15.760	22.959	1.00	24.64	C
ATOM	1500	O	LEU	A	189	13.990	14.978	23.882	1.00	25.03	O
ATOM	1501	N	ALA	A	190	13.529	16.762	22.545	1.00	23.75	N
ATOM	1502	CA	ALA	A	190	12.188	16.963	23.095	1.00	24.54	C
ATOM	1503	CB	ALA	A	190	12.042	18.370	23.703	1.00	23.54	C
ATOM	1504	C	ALA	A	190	11.147	16.720	22.000	1.00	24.22	C
ATOM	1505	O	ALA	A	190	11.309	17.189	20.862	1.00	25.33	O
ATOM	1506	N	PHE	A	191	10.111	15.956	22.311	1.00	23.92	N
ATOM	1507	CA	PHE	A	191	9.020	15.708	21.351	1.00	23.85	C
ATOM	1508	CB	PHE	A	191	9.325	14.512	20.461	1.00	22.29	C
ATOM	1509	CG	PHE	A	191	9.366	13.172	21.186	1.00	24.53	C
ATOM	1510	CD1	PHE	A	191	8.678	12.070	20.656	1.00	21.17	C
ATOM	1511	CE1	PHE	A	191	8.714	10.806	21.297	1.00	25.15	C
ATOM	1512	CZ	PHE	A	191	9.469	10.621	22.482	1.00	27.06	C
ATOM	1513	CE2	PHE	A	191	10.171	11.741	23.051	1.00	27.19	C
ATOM	1514	CD2	PHE	A	191	10.117	13.001	22.389	1.00	25.19	C
ATOM	1515	C	PHE	A	191	7.632	15.567	21.963	1.00	24.92	C
ATOM	1516	O	PHE	A	191	7.442	15.511	23.192	1.00	25.19	O
ATOM	1517	N	SER	A	192	6.664	15.516	21.068	1.00	26.49	N
ATOM	1518	CA	SER	A	192	5.312	15.058	21.358	1.00	27.84	C
ATOM	1519	CB	SER	A	192	4.455	15.334	20.134	1.00	27.26	C
ATOM	1520	OG	SER	A	192	3.892	16.585	20.385	1.00	27.76	O
ATOM	1521	C	SER	A	192	5.186	13.568	21.737	1.00	28.10	C
ATOM	1522	O	SER	A	192	5.811	12.718	21.130	1.00	27.68	O
ATOM	1523	N	GLY	A	193	4.377	13.267	22.743	1.00	29.67	N
ATOM	1524	CA	GLY	A	193	4.243	11.903	23.216	1.00	32.97	C
ATOM	1525	C	GLY	A	193	3.618	11.055	22.124	1.00	35.23	C
ATOM	1526	O	GLY	A	193	2.563	11.435	21.621	1.00	35.83	O
ATOM	1527	N	PRO	A	194	4.272	9.953	21.724	1.00	36.70	N
ATOM	1528	CA	PRO	A	194	3.687	8.984	20.783	1.00	37.38	C
ATOM	1529	CB	PRO	A	194	4.672	7.811	20.821	1.00	37.27	C
ATOM	1530	CG	PRO	A	194	5.959	8.353	21.346	1.00	37.18	C
ATOM	1531	CD	PRO	A	194	5.627	9.558	22.146	1.00	37.05	C
ATOM	1532	C	PRO	A	194	2.288	8.477	21.216	1.00	38.18	C
ATOM	1533	O	PRO	A	194	1.845	8.646	22.362	1.00	35.98	O
ATOM	1534	N	HIS	A	195	1.614	7.860	20.247	1.00	39.82	N
ATOM	1535	CA	HIS	A	195	0.207	7.464	20.370	1.00	41.17	C
ATOM	1536	CB	HIS	A	195	−0.712	8.249	19.373	1.00	40.62	C
ATOM	1537	CG	HIS	A	195	−1.198	9.555	19.944	1.00	41.35	C
ATOM	1538	ND1	HIS	A	195	−0.460	10.723	19.866	1.00	40.13	N
ATOM	1539	CE1	HIS	A	195	−1.079	11.678	20.548	1.00	41.11	C
ATOM	1540	NE2	HIS	A	195	−2.190	11.175	21.067	1.00	41.61	N
ATOM	1541	CD2	HIS	A	195	−2.288	9.849	20.709	1.00	40.35	C
ATOM	1542	C	HIS	A	195	0.190	5.946	20.208	1.00	42.44	C
ATOM	1543	O	HIS	A	195	1.131	5.367	19.601	1.00	42.18	O
ATOM	1544	N	PRO	A	196	−0.829	5.312	20.810	1.00	43.69	N
ATOM	1545	CA	PRO	A	196	−0.978	3.834	20.810	1.00	44.56	C
ATOM	1546	CB	PRO	A	196	−2.323	3.606	21.513	1.00	44.52	C
ATOM	1547	CG	PRO	A	196	−3.008	5.007	21.558	1.00	44.93	C
ATOM	1548	CD	PRO	A	196	−1.904	6.008	21.548	1.00	42.99	C
ATOM	1549	C	PRO	A	196	−0.978	3.230	19.399	1.00	46.29	C
ATOM	1550	O	PRO	A	196	−0.345	2.187	19.203	1.00	46.94	O
ATOM	1551	N	LYS	A	197	−1.678	3.841	18.435	1.00	47.65	N
ATOM	1552	CA	LYS	A	197	−1.292	3.643	17.029	1.00	49.00	C
ATOM	1553	CB	LYS	A	197	−1.936	2.388	16.387	1.00	49.53	C
ATOM	1554	CG	LYS	A	197	−3.191	2.589	15.527	1.00	50.00	C
ATOM	1555	CD	LYS	A	197	−3.068	1.756	14.266	1.00	54.69	C
ATOM	1556	CE	LYS	A	197	−4.108	2.116	13.220	1.00	55.60	C
ATOM	1557	NZ	LYS	A	197	−5.001	0.946	13.078	1.00	58.34	N
ATOM	1558	C	LYS	A	197	−1.370	4.883	16.124	1.00	49.84	C
ATOM	1559	O	LYS	A	197	−2.100	5.843	16.407	1.00	48.18	O
ATOM	1560	N	SER	A	198	−0.566	4.783	15.055	1.00	52.12	N
ATOM	1561	CA	SER	A	198	−0.359	5.726	13.951	1.00	54.78	C
ATOM	1562	CB	SER	A	198	0.719	5.159	13.023	1.00	54.45	C
ATOM	1563	OG	SER	A	198	2.004	5.217	13.625	1.00	57.82	O
ATOM	1564	C	SER	A	198	−1.582	6.033	13.081	1.00	56.53	C
ATOM	1565	O	SER	A	198	−1.560	5.769	11.875	1.00	57.00	O
ATOM	1566	N	LYS	A	199	−2.627	6.603	13.680	1.00	58.23	N
ATOM	1567	CA	LYS	A	199	−3.815	7.002	12.943	1.00	59.63	C
ATOM	1568	CB	LYS	A	199	−5.062	6.726	13.802	1.00	59.35	C
ATOM	1569	CG	LYS	A	199	−5.425	7.837	14.820	1.00	59.90	C
ATOM	1570	CD	LYS	A	199	−6.238	7.329	16.017	1.00	59.89	C
ATOM	1571	CE	LYS	A	199	−7.732	7.251	15.715	1.00	61.84	C
ATOM	1572	NZ	LYS	A	199	−8.480	6.824	16.936	1.00	61.00	N
ATOM	1573	C	LYS	A	199	−3.701	8.481	12.469	1.00	60.97	C
ATOM	1574	O	LYS	A	199	−2.652	9.109	12.617	1.00	60.83	O
ATOM	1575	N	ILE	A	200	−4.761	9.007	11.853	1.00	62.78	N
ATOM	1576	CA	ILE	A	200	−4.901	10.447	11.615	1.00	64.28	C
ATOM	1577	CB	ILE	A	200	−4.878	10.813	10.072	1.00	64.26	C
ATOM	1578	CG1	ILE	A	200	−3.464	10.604	9.495	1.00	64.64	C
ATOM	1579	CD1	ILE	A	200	−3.381	10.271	7.991	1.00	66.22	C
ATOM	1580	CG2	ILE	A	200	−5.405	12.265	9.823	1.00	64.05	C
ATOM	1581	C	ILE	A	200	−6.176	10.902	12.332	1.00	65.19	C
ATOM	1582	O	ILE	A	200	−7.265	10.411	12.053	1.00	65.26	O
ATOM	1583	N	GLU	A	201	−6.032	11.799	13.296	1.00	66.49	N
ATOM	1584	CA	GLU	A	201	−7.176	12.197	14.090	1.00	68.20	C
ATOM	1585	CB	GLU	A	201	−6.991	11.903	15.585	1.00	68.23	C
ATOM	1586	CG	GLU	A	201	−8.315	11.584	16.276	1.00	70.09	C
ATOM	1587	CD	GLU	A	201	−8.242	11.565	17.807	1.00	72.03	C
ATOM	1588	OE1	GLU	A	201	−7.333	12.218	18.392	1.00	71.86	O
ATOM	1589	OE2	GLU	A	201	−9.111	10.896	18.430	1.00	71.14	O
ATOM	1590	C	GLU	A	201	−7.535	13.656	13.841	1.00	69.14	C
ATOM	1591	O	GLU	A	201	−6.976	14.574	14.471	1.00	68.93	O
ATOM	1592	N	ASN	A	202	−8.465	13.837	12.890	1.00	70.17	N
ATOM	1593	CA	ASN	A	202	−9.124	15.120	12.626	1.00	70.58	C
ATOM	1594	CB	ASN	A	202	−9.978	15.550	13.844	1.00	70.91	C
ATOM	1595	CG	ASN	A	202	−10.864	14.397	14.391	1.00	72.18	C
ATOM	1596	OD1	ASN	A	202	−10.817	13.241	13.906	1.00	71.09	O
ATOM	1597	ND2	ASN	A	202	−11.674	14.716	15.405	1.00	73.05	N
ATOM	1598	C	ASN	A	202	−8.102	16.172	12.151	1.00	70.44	C
ATOM	1599	O	ASN	A	202	−7.740	17.132	12.877	1.00	69.89	O
ATOM	1600	N	GLY	A	203	−7.629	15.933	10.921	1.00	70.23	N
ATOM	1601	CA	GLY	A	203	−6.522	16.668	10.325	1.00	69.97	C
ATOM	1602	C	GLY	A	203	−5.160	16.130	10.750	1.00	69.43	C
ATOM	1603	O	GLY	A	203	−4.269	15.930	9.918	1.00	68.50	O
ATOM	1604	N	TYR	A	204	−5.050	15.850	12.053	1.00	69.24	N
ATOM	1605	CA	TYR	A	204	−3.787	15.628	12.778	1.00	68.98	C
ATOM	1606	CB	TYR	A	204	−4.026	15.928	14.275	1.00	70.26	C
ATOM	1607	CG	TYR	A	204	−3.086	16.955	14.871	1.00	73.85	C
ATOM	1608	CD1	TYR	A	204	−3.023	18.258	14.352	1.00	76.57	C
ATOM	1609	CE1	TYR	A	204	−2.146	19.210	14.895	1.00	78.69	C
ATOM	1610	CZ	TYR	A	204	−1.332	18.858	15.971	1.00	79.10	C
ATOM	1611	OH	TYR	A	204	−0.475	19.797	16.504	1.00	79.76	O
ATOM	1612	CE2	TYR	A	204	−1.382	17.566	16.509	1.00	78.94	C
ATOM	1613	CD2	TYR	A	204	−2.256	16.625	15.959	1.00	76.89	C
ATOM	1614	C	TYR	A	204	−3.110	14.244	12.611	1.00	66.93	C
ATOM	1615	O	TYR	A	204	−3.746	13.217	12.827	1.00	67.00	O
ATOM	1616	N	PRO	A	205	−1.824	14.225	12.244	1.00	65.07	N
ATOM	1617	CA	PRO	A	205	−1.029	12.987	12.241	1.00	63.61	C
ATOM	1618	CB	PRO	A	205	0.189	13.345	11.391	1.00	63.43	C
ATOM	1619	CG	PRO	A	205	−0.086	14.711	10.866	1.00	64.39	C
ATOM	1620	CD	PRO	A	205	−1.035	15.377	11.787	1.00	64.74	C
ATOM	1621	C	PRO	A	205	−0.569	12.555	13.647	1.00	61.93	C
ATOM	1622	O	PRO	A	205	−0.036	13.371	14.410	1.00	61.56	O
ATOM	1623	N	LEU	A	206	−0.792	11.274	13.958	1.00	60.19	N
ATOM	1624	CA	LEU	A	206	−0.420	10.652	15.245	1.00	58.09	C
ATOM	1625	CB	LEU	A	206	−1.615	10.005	15.960	1.00	57.94	C
ATOM	1626	CG	LEU	A	206	−2.737	10.948	16.434	1.00	57.99	C
ATOM	1627	CD1	LEU	A	206	−3.806	10.194	17.194	1.00	58.59	C
ATOM	1628	CD2	LEU	A	206	−2.219	12.129	17.291	1.00	57.80	C
ATOM	1629	C	LEU	A	206	0.628	9.621	14.962	1.00	56.60	C
ATOM	1630	O	LEU	A	206	0.523	8.904	13.974	1.00	56.64	O
ATOM	1631	N	HIS	A	207	1.664	9.592	15.803	1.00	54.99	N
ATOM	1632	CA	HIS	A	207	2.818	8.718	15.595	1.00	52.67	C
ATOM	1633	CB	HIS	A	207	4.102	9.541	15.442	1.00	53.00	C
ATOM	1634	CG	HIS	A	207	4.076	10.479	14.268	1.00	53.89	C
ATOM	1635	ND1	HIS	A	207	4.580	10.137	13.027	1.00	54.73	N
ATOM	1636	CE1	HIS	A	207	4.397	11.140	12.186	1.00	56.05	C
ATOM	1637	NE2	HIS	A	207	3.788	12.119	12.834	1.00	56.79	N
ATOM	1638	CD2	HIS	A	207	3.569	11.728	14.137	1.00	54.65	C
ATOM	1639	C	HIS	A	207	2.919	7.671	16.713	1.00	51.17	C
ATOM	1640	O	HIS	A	207	2.801	7.990	17.916	1.00	50.68	O
ATOM	1641	N	ALA	A	208	3.072	6.412	16.309	1.00	48.68	N
ATOM	1642	CA	ALA	A	208	3.257	5.348	17.283	1.00	46.56	C
ATOM	1643	CB	ALA	A	208	2.638	4.058	16.787	1.00	46.66	C
ATOM	1644	C	ALA	A	208	4.771	5.180	17.562	1.00	44.74	C
ATOM	1645	O	ALA	A	208	5.603	5.486	16.674	1.00	44.01	O
ATOM	1646	N	PRO	A	209	5.128	4.686	18.764	1.00	42.41	N
ATOM	1647	CA	PRO	A	209	6.533	4.678	19.187	1.00	40.46	C
ATOM	1648	CB	PRO	A	209	6.535	3.722	20.389	1.00	40.29	C
ATOM	1649	CG	PRO	A	209	5.168	3.776	20.956	1.00	39.85	C
ATOM	1650	CD	PRO	A	209	4.238	4.101	19.797	1.00	41.61	C
ATOM	1651	C	PRO	A	209	7.478	4.205	18.082	1.00	39.38	C
ATOM	1652	O	PRO	A	209	8.527	4.796	17.912	1.00	39.18	O
ATOM	1653	N	GLU	A	210	7.090	3.201	17.310	1.00	38.71	N
ATOM	1654	CA	GLU	A	210	7.973	2.569	16.318	1.00	38.62	C
ATOM	1655	CB	GLU	A	210	7.329	1.283	15.762	1.00	38.71	C
ATOM	1656	CG	GLU	A	210	7.116	0.150	16.778	1.00	39.01	C
ATOM	1657	CD	GLU	A	210	5.852	0.298	17.636	1.00	39.09	C
ATOM	1658	OE1	GLU	A	210	5.586	−0.553	18.514	1.00	38.08	O
ATOM	1659	OE2	GLU	A	210	5.097	1.261	17.444	1.00	42.37	O
ATOM	1660	C	GLU	A	210	8.473	3.500	15.187	1.00	38.55	C
ATOM	1661	O	GLU	A	210	9.549	3.262	14.606	1.00	39.94	O
ATOM	1662	N	ALA	A	211	7.738	4.574	14.898	1.00	38.25	N
ATOM	1663	CA	ALA	A	211	8.186	5.601	13.918	1.00	38.00	C
ATOM	1664	CB	ALA	A	211	7.113	6.629	13.713	1.00	37.25	C
ATOM	1665	C	ALA	A	211	9.509	6.276	14.318	1.00	37.70	C
ATOM	1666	O	ALA	A	211	10.278	6.734	13.485	1.00	37.84	O
ATOM	1667	N	TYR	A	212	9.810	6.293	15.600	1.00	37.71	N
ATOM	1668	CA	TYR	A	212	10.995	7.031	16.058	1.00	37.21	C
ATOM	1669	CB	TYR	A	212	10.705	7.628	17.418	1.00	35.73	C
ATOM	1670	CG	TYR	A	212	9.681	8.703	17.363	1.00	31.92	C
ATOM	1671	CD1	TYR	A	212	10.040	10.016	17.064	1.00	33.63	C
ATOM	1672	CE1	TYR	A	212	9.095	11.035	17.009	1.00	29.78	C
ATOM	1673	CZ	TYR	A	212	7.791	10.732	17.248	1.00	29.81	C
ATOM	1674	OH	TYR	A	212	6.847	11.733	17.219	1.00	27.16	O
ATOM	1675	CE2	TYR	A	212	7.417	9.424	17.546	1.00	31.56	C
ATOM	1676	CD2	TYR	A	212	8.369	8.427	17.599	1.00	30.00	C
ATOM	1677	C	TYR	A	212	12.252	6.193	16.163	1.00	37.65	C
ATOM	1678	O	TYR	A	212	13.341	6.723	16.299	1.00	38.01	O
ATOM	1679	N	PHE	A	213	12.068	4.879	16.100	1.00	38.12	N
ATOM	1680	CA	PHE	A	213	13.108	3.911	16.379	1.00	37.80	C
ATOM	1681	CB	PHE	A	213	12.547	2.504	16.184	1.00	38.29	C
ATOM	1682	CG	PHE	A	213	11.567	2.064	17.268	1.00	37.57	C
ATOM	1683	CD1	PHE	A	213	11.055	2.969	18.185	1.00	34.48	C
ATOM	1684	CE1	PHE	A	213	10.162	2.553	19.187	1.00	34.46	C
ATOM	1685	CZ	PHE	A	213	9.804	1.223	19.265	1.00	35.33	C
ATOM	1686	CE2	PHE	A	213	10.313	0.286	18.352	1.00	32.71	C
ATOM	1687	CD2	PHE	A	213	11.190	0.700	17.376	1.00	37.42	C
ATOM	1688	C	PHE	A	213	14.313	4.126	15.489	1.00	37.94	C
ATOM	1689	O	PHE	A	213	15.431	4.214	16.015	1.00	37.70	O
ATOM	1690	N	PRO	A	214	14.120	4.195	14.153	1.00	37.43	N
ATOM	1691	CA	PRO	A	214	15.270	4.351	13.245	1.00	36.90	C
ATOM	1692	CB	PRO	A	214	14.646	4.308	11.817	1.00	37.01	C
ATOM	1693	CG	PRO	A	214	13.287	3.731	11.955	1.00	35.10	C
ATOM	1694	CD	PRO	A	214	12.853	4.032	13.405	1.00	37.24	C
ATOM	1695	C	PRO	A	214	16.018	5.648	13.505	1.00	37.03	C
ATOM	1696	O	PRO	A	214	17.259	5.652	13.556	1.00	36.87	O
ATOM	1697	N	TYR	A	215	15.280	6.751	13.699	1.00	36.89	N
ATOM	1698	CA	TYR	A	215	15.952	8.042	13.993	1.00	35.30	C
ATOM	1699	CB	TYR	A	215	15.001	9.227	13.729	1.00	34.41	C
ATOM	1700	CG	TYR	A	215	15.642	10.600	13.935	1.00	33.51	C
ATOM	1701	CD1	TYR	A	215	16.036	11.380	12.841	1.00	30.80	C
ATOM	1702	CE1	TYR	A	215	16.604	12.621	13.019	1.00	31.79	C
ATOM	1703	CZ	TYR	A	215	16.802	13.123	14.323	1.00	35.40	C
ATOM	1704	OH	TYR	A	215	17.358	14.372	14.518	1.00	31.69	O
ATOM	1705	CE2	TYR	A	215	16.418	12.360	15.442	1.00	34.03	C
ATOM	1706	CD2	TYR	A	215	15.822	11.124	15.239	1.00	30.82	C
ATOM	1707	C	TYR	A	215	16.638	8.084	15.413	1.00	34.15	C
ATOM	1708	O	TYR	A	215	17.771	8.545	15.544	1.00	32.85	O
ATOM	1709	N	PHE	A	216	15.909	7.650	16.442	1.00	34.08	N
ATOM	1710	CA	PHE	A	216	16.426	7.474	17.804	1.00	35.04	C
ATOM	1711	CB	PHE	A	216	15.382	6.812	18.696	1.00	34.04	C
ATOM	1712	CG	PHE	A	216	14.287	7.736	19.171	1.00	32.22	C
ATOM	1713	CD1	PHE	A	216	14.095	9.012	18.614	1.00	29.44	C
ATOM	1714	CE1	PHE	A	216	13.097	9.879	19.085	1.00	25.12	C
ATOM	1715	CZ	PHE	A	216	12.255	9.471	20.096	1.00	27.88	C
ATOM	1716	CE2	PHE	A	216	12.426	8.201	20.676	1.00	29.00	C
ATOM	1717	CD2	PHE	A	216	13.463	7.348	20.217	1.00	31.23	C
ATOM	1718	C	PHE	A	216	17.712	6.622	17.811	1.00	36.90	C
ATOM	1719	O	PHE	A	216	18.758	7.060	18.318	1.00	37.19	O
ATOM	1720	N	LYS	A	217	17.655	5.447	17.177	1.00	38.00	N
ATOM	1721	CA	LYS	A	217	18.794	4.535	17.190	1.00	39.43	C
ATOM	1722	CB	LYS	A	217	18.392	3.096	16.772	1.00	39.74	C
ATOM	1723	CG	LYS	A	217	19.025	2.005	17.691	1.00	44.88	C
ATOM	1724	CD	LYS	A	217	18.215	1.632	18.979	1.00	48.78	C
ATOM	1725	CE	LYS	A	217	17.539	0.195	18.897	1.00	52.10	C
ATOM	1726	NZ	LYS	A	217	16.470	−0.007	17.788	1.00	51.63	N
ATOM	1727	C	LYS	A	217	20.014	5.116	16.460	1.00	39.25	C
ATOM	1728	O	LYS	A	217	21.153	4.971	16.928	1.00	39.72	O
ATOM	1729	N	LYS	A	218	19.775	5.858	15.381	1.00	39.38	N
ATOM	1730	CA	LYS	A	218	20.835	6.565	14.656	1.00	39.17	C
ATOM	1731	CB	LYS	A	218	20.392	6.821	13.206	1.00	39.37	C
ATOM	1732	CG	LYS	A	218	20.204	8.243	12.763	1.00	40.46	C
ATOM	1733	CD	LYS	A	218	20.826	8.491	11.379	1.00	46.84	C
ATOM	1734	CE	LYS	A	218	19.901	9.273	10.409	1.00	49.08	C
ATOM	1735	NZ	LYS	A	218	19.650	10.751	10.763	1.00	52.18	N
ATOM	1736	C	LYS	A	218	21.403	7.843	15.326	1.00	39.76	C
ATOM	1737	O	LYS	A	218	22.464	8.355	14.904	1.00	40.14	O
ATOM	1738	N	HIS	A	219	20.710	8.379	16.338	1.00	39.66	N
ATOM	1739	CA	HIS	A	219	21.235	9.509	17.110	1.00	39.01	C
ATOM	1740	CB	HIS	A	219	20.321	10.696	17.014	1.00	39.15	C
ATOM	1741	CG	HIS	A	219	20.427	11.402	15.696	1.00	40.67	C
ATOM	1742	ND1	HIS	A	219	19.545	11.175	14.659	1.00	39.13	N
ATOM	1743	CE1	HIS	A	219	19.900	11.908	13.620	1.00	38.12	C
ATOM	1744	NE2	HIS	A	219	20.982	12.596	13.945	1.00	40.67	N
ATOM	1745	CD2	HIS	A	219	21.342	12.291	15.234	1.00	39.39	C
ATOM	1746	C	HIS	A	219	21.493	9.153	18.546	1.00	39.34	C
ATOM	1747	O	HIS	A	219	21.627	10.033	19.417	1.00	41.02	O
ATOM	1748	N	ASN	A	220	21.564	7.849	18.784	1.00	38.15	N
ATOM	1749	CA	ASN	A	220	22.151	7.286	19.978	1.00	37.53	C
ATOM	1750	CB	ASN	A	220	23.620	7.736	20.102	1.00	36.97	C
ATOM	1751	CG	ASN	A	220	24.344	7.114	21.298	1.00	39.01	C
ATOM	1752	OD1	ASN	A	220	24.059	5.981	21.689	1.00	38.31	O
ATOM	1753	ND2	ASN	A	220	25.304	7.863	21.880	1.00	38.93	N
ATOM	1754	C	ASN	A	220	21.302	7.681	21.179	1.00	37.06	C
ATOM	1755	O	ASN	A	220	21.846	8.038	22.246	1.00	36.97	O
ATOM	1756	N	VAL	A	221	19.984	7.609	20.977	1.00	35.09	N
ATOM	1757	CA	VAL	A	221	19.015	7.763	22.028	1.00	34.42	C
ATOM	1758	CB	VAL	A	221	17.557	8.020	21.490	1.00	34.52	C
ATOM	1759	CG1	VAL	A	221	16.508	8.010	22.652	1.00	33.88	C
ATOM	1760	CG2	VAL	A	221	17.428	9.309	20.691	1.00	33.03	C
ATOM	1761	C	VAL	A	221	18.990	6.436	22.783	1.00	35.49	C
ATOM	1762	O	VAL	A	221	18.655	5.374	22.208	1.00	36.40	O
ATOM	1763	N	THR	A	222	19.318	6.487	24.072	1.00	34.76	N
ATOM	1764	CA	THR	A	222	19.301	5.318	24.919	1.00	33.92	C
ATOM	1765	CB	THR	A	222	20.700	5.114	25.572	1.00	34.73	C
ATOM	1766	OG1	THR	A	222	21.049	6.271	26.364	1.00	35.15	O
ATOM	1767	CG2	THR	A	222	21.831	4.981	24.497	1.00	32.40	C
ATOM	1768	C	THR	A	222	18.219	5.410	25.997	1.00	34.65	C
ATOM	1769	O	THR	A	222	17.935	4.420	26.698	1.00	36.12	O
ATOM	1770	N	ALA	A	223	17.615	6.588	26.188	1.00	32.78	N
ATOM	1771	CA	ALA	A	223	16.509	6.666	27.118	1.00	29.51	C
ATOM	1772	CB	ALA	A	223	16.965	7.257	28.449	1.00	28.07	C
ATOM	1773	C	ALA	A	223	15.331	7.468	26.527	1.00	28.41	C
ATOM	1774	O	ALA	A	223	15.510	8.447	25.811	1.00	27.82	O
ATOM	1775	N	VAL	A	224	14.137	7.012	26.855	1.00	27.08	N
ATOM	1776	CA	VAL	A	224	12.939	7.753	26.688	1.00	27.15	C
ATOM	1777	CB	VAL	A	224	11.957	7.003	25.747	1.00	27.55	C
ATOM	1778	CG1	VAL	A	224	10.618	7.748	25.636	1.00	26.78	C
ATOM	1779	CG2	VAL	A	224	12.600	6.839	24.359	1.00	26.91	C
ATOM	1780	C	VAL	A	224	12.347	7.983	28.070	1.00	27.03	C
ATOM	1781	O	VAL	A	224	12.255	7.054	28.862	1.00	27.48	O
ATOM	1782	N	VAL	A	225	11.968	9.232	28.352	1.00	26.97	N
ATOM	1783	CA	VAL	A	225	11.332	9.614	29.619	1.00	27.02	C
ATOM	1784	CB	VAL	A	225	12.158	10.695	30.334	1.00	26.85	C
ATOM	1785	CG1	VAL	A	225	11.409	11.234	31.536	1.00	26.21	C
ATOM	1786	CG2	VAL	A	225	13.537	10.173	30.709	1.00	25.31	C
ATOM	1787	C	VAL	A	225	9.931	10.189	29.349	1.00	27.86	C
ATOM	1788	O	VAL	A	225	9.789	11.153	28.571	1.00	27.89	O
ATOM	1789	N	ARG	A	226	8.901	9.583	29.955	1.00	28.09	N
ATOM	1790	CA	ARG	A	226	7.554	10.083	29.785	1.00	27.85	C
ATOM	1791	CB	ARG	A	226	6.600	8.951	29.450	1.00	28.36	C
ATOM	1792	CG	ARG	A	226	5.081	9.309	29.616	1.00	30.26	C
ATOM	1793	CD	ARG	A	226	4.102	8.251	29.082	1.00	36.13	C
ATOM	1794	NE	ARG	A	226	4.480	6.944	29.586	1.00	38.35	N
ATOM	1795	CZ	ARG	A	226	4.057	5.775	29.132	1.00	38.86	C
ATOM	1796	NH1	ARG	A	226	3.189	5.724	28.137	1.00	36.80	N
ATOM	1797	NH2	ARG	A	226	4.532	4.644	29.687	1.00	36.90	N
ATOM	1798	C	ARG	A	226	7.098	10.822	31.047	1.00	27.86	C
ATOM	1799	O	ARG	A	226	7.215	10.295	32.150	1.00	26.60	O
ATOM	1800	N	LEU	A	227	6.576	12.038	30.863	1.00	27.48	N
ATOM	1801	CA	LEU	A	227	6.106	12.876	31.974	1.00	28.27	C
ATOM	1802	CB	LEU	A	227	6.712	14.292	31.869	1.00	27.87	C
ATOM	1803	CG	LEU	A	227	8.223	14.332	31.568	1.00	28.82	C
ATOM	1804	CD1	LEU	A	227	8.624	15.782	31.352	1.00	27.85	C
ATOM	1805	CD2	LEU	A	227	9.060	13.663	32.709	1.00	25.02	C
ATOM	1806	C	LEU	A	227	4.583	12.970	32.014	1.00	28.25	C
ATOM	1807	O	LEU	A	227	3.978	13.472	32.972	1.00	27.00	O
ATOM	1808	N	ASN	A	228	3.960	12.473	30.969	1.00	28.67	N
ATOM	1809	CA	ASN	A	228	2.521	12.556	30.935	1.00	31.25	C
ATOM	1810	CB	ASN	A	228	2.088	13.217	29.631	1.00	29.75	C
ATOM	1811	CG	ASN	A	228	2.354	12.364	28.433	1.00	28.21	C
ATOM	1812	OD1	ASN	A	228	3.428	11.794	28.280	1.00	28.19	O
ATOM	1813	ND2	ASN	A	228	1.388	12.294	27.552	1.00	30.94	N
ATOM	1814	C	ASN	A	228	1.836	11.190	31.181	1.00	32.96	C
ATOM	1815	O	ASN	A	228	2.508	10.151	31.199	1.00	33.48	O
ATOM	1816	N	LYS	A	229	0.516	11.183	31.347	1.00	35.64	N
ATOM	1817	CA	LYS	A	229	−0.187	9.917	31.639	1.00	38.66	C
ATOM	1818	CB	LYS	A	229	−1.637	10.140	32.112	1.00	38.02	C
ATOM	1819	CG	LYS	A	229	−2.648	10.172	31.032	1.00	41.80	C
ATOM	1820	CD	LYS	A	229	−3.801	11.224	31.265	1.00	46.00	C
ATOM	1821	CE	LYS	A	229	−4.225	11.939	29.896	1.00	44.34	C
ATOM	1822	NZ	LYS	A	229	−4.417	10.990	28.726	1.00	42.38	N
ATOM	1823	C	LYS	A	229	−0.037	8.961	30.468	1.00	39.82	C
ATOM	1824	O	LYS	A	229	0.134	9.439	29.334	1.00	41.23	O
ATOM	1825	N	LYS	A	230	−0.038	7.636	30.742	1.00	41.15	N
ATOM	1826	CA	LYS	A	230	0.320	6.589	29.737	1.00	41.74	C
ATOM	1827	CB	LYS	A	230	0.890	5.294	30.366	1.00	41.79	C
ATOM	1828	CG	LYS	A	230	1.080	5.287	31.896	1.00	43.14	C
ATOM	1829	CD	LYS	A	230	2.348	4.512	32.297	1.00	44.36	C
ATOM	1830	CE	LYS	A	230	2.057	3.231	33.103	1.00	44.40	C
ATOM	1831	NZ	LYS	A	230	1.194	3.402	34.291	1.00	43.43	N
ATOM	1832	C	LYS	A	230	−0.777	6.256	28.721	1.00	42.04	C
ATOM	1833	O	LYS	A	230	−1.963	6.178	29.044	1.00	42.75	O
ATOM	1834	N	ILE	A	231	−3.356	6.030	27.489	1.00	42.06	N
ATOM	1835	CA	ILE	A	231	−1.254	6.065	26.362	1.00	42.57	C
ATOM	1836	CB	ILE	A	231	−1.206	7.503	25.740	1.00	43.10	C
ATOM	1837	CG1	ILE	A	231	−2.563	8.184	25.826	1.00	43.77	C
ATOM	1838	CD1	ILE	A	231	−2.657	9.379	24.863	1.00	48.89	C
ATOM	1839	CG2	ILE	A	231	−0.700	7.540	24.296	1.00	41.89	C
ATOM	1840	C	ILE	A	231	−0.753	5.032	25.400	1.00	42.99	C
ATOM	1841	O	ILE	A	231	−1.432	4.677	24.421	1.00	43.33	O
ATOM	1842	N	TYR	A	232	0.467	4.598	25.666	1.00	42.56	N
ATOM	1843	CA	TYR	A	232	1.133	3.558	24.924	1.00	43.70	C
ATOM	1844	CB	TYR	A	232	2.142	4.154	23.891	1.00	43.71	C
ATOM	1845	CG	TYR	A	232	3.366	4.920	24.483	1.00	44.23	C
ATOM	1846	CD1	TYR	A	232	4.570	4.279	24.736	1.00	43.18	C
ATOM	1847	CE1	TYR	A	232	5.664	4.987	25.245	1.00	43.34	C
ATOM	1848	CZ	TYR	A	232	5.546	6.329	25.532	1.00	40.78	C
ATOM	1849	OH	TYR	A	232	6.605	7.047	26.088	1.00	36.91	O
ATOM	1850	CE2	TYR	A	232	4.360	6.968	25.287	1.00	42.31	C
ATOM	1851	CD2	TYR	A	232	3.294	6.283	24.780	1.00	43.88	C
ATOM	1852	C	TYR	A	232	1.836	2.676	25.985	1.00	44.08	C
ATOM	1853	O	TYR	A	232	2.106	3.145	27.121	1.00	43.69	O
ATOM	1854	N	GLU	A	233	2.173	1.448	25.593	1.00	43.70	N
ATOM	1855	CA	GLU	A	233	2.794	0.473	26.472	1.00	44.26	C
ATOM	1856	CB	GLU	A	233	2.388	−0.938	25.982	1.00	45.45	C
ATOM	1857	CG	GLU	A	233	2.847	−2.167	26.787	1.00	49.43	C
ATOM	1858	CD	GLU	A	233	2.883	−1.973	28.312	1.00	54.59	C
ATOM	1859	OE1	GLU	A	233	4.013	−1.759	28.836	1.00	55.60	O
ATOM	1860	OE2	GLU	A	233	1.803	−2.061	28.979	1.00	55.74	O
ATOM	1861	C	GLU	A	233	4.306	0.702	26.404	1.00	43.66	C
ATOM	1862	O	GLU	A	233	4.902	0.492	25.344	1.00	44.27	O
ATOM	1863	N	ALA	A	234	4.946	1.130	27.504	1.00	43.05	N
ATOM	1864	CA	ALA	A	234	6.411	1.376	27.472	1.00	42.22	C
ATOM	1865	CB	ALA	A	234	6.977	1.670	28.887	1.00	42.17	C
ATOM	1866	C	ALA	A	234	7.244	0.285	26.779	1.00	41.83	C
ATOM	1867	O	ALA	A	234	8.293	0.600	26.197	1.00	42.45	O
ATOM	1868	N	LYS	A	235	6.780	−0.973	26.829	1.00	41.10	N
ATOM	1869	CA	LYS	A	235	7.510	−2.144	26.306	1.00	40.88	C
ATOM	1870	CB	LYS	A	235	6.712	−3.430	26.534	1.00	41.57	C
ATOM	1871	CG	LYS	A	235	7.051	−4.180	27.828	1.00	44.74	C
ATOM	1872	CD	LYS	A	235	7.748	−5.577	27.558	1.00	47.48	C
ATOM	1873	CE	LYS	A	235	8.112	−6.246	28.948	1.00	50.15	C
ATOM	1874	NZ	LYS	A	235	9.530	−6.020	29.495	1.00	45.13	N
ATOM	1875	C	LYS	A	235	7.911	−2.084	24.830	1.00	40.48	C
ATOM	1876	O	LYS	A	235	8.893	−2.719	24.400	1.00	39.16	O
ATOM	1877	N	ARG	A	236	7.135	−1.330	24.049	1.00	40.16	N
ATOM	1878	CA	ARG	A	236	7.424	−1.145	22.641	1.00	39.07	C
ATOM	1879	CB	ARG	A	236	6.269	−0.405	21.964	1.00	39.40	C
ATOM	1880	CG	ARG	A	236	4.890	−0.956	22.362	1.00	37.54	C
ATOM	1881	CD	ARG	A	236	3.691	−0.133	21.934	1.00	34.61	C
ATOM	1882	NE	ARG	A	236	3.717	0.138	20.498	1.00	34.15	N
ATOM	1883	CZ	ARG	A	236	2.677	0.631	19.807	1.00	35.58	C
ATOM	1884	NH1	ARG	A	236	1.554	0.941	20.456	1.00	28.19	N
ATOM	1885	NH2	ARG	A	236	2.784	0.884	18.475	1.00	33.74	N
ATOM	1886	C	ARG	A	236	8.745	−0.417	22.480	1.00	38.83	C
ATOM	1887	O	ARG	A	236	9.488	−0.681	21.531	1.00	39.65	O
ATOM	1888	N	PHE	A	237	9.046	0.487	23.414	1.00	38.24	N
ATOM	1889	CA	PHE	A	237	10.392	1.073	23.531	1.00	37.24	C
ATOM	1890	CB	PHE	A	237	10.374	2.429	24.300	1.00	36.68	C
ATOM	1891	CG	PHE	A	237	10.024	3.622	23.432	1.00	30.94	C
ATOM	1892	CD1	PHE	A	237	10.849	4.004	22.410	1.00	27.15	C
ATOM	1893	CE1	PHE	A	237	10.535	5.057	21.605	1.00	27.94	C
ATOM	1894	CZ	PHE	A	237	9.365	5.745	21.822	1.00	27.16	C
ATOM	1895	CE2	PHE	A	237	8.539	5.406	22.824	1.00	25.28	C
ATOM	1896	CD2	PHE	A	237	8.862	4.323	23.631	1.00	31.30	C
ATOM	1897	C	PHE	A	237	11.361	0.069	24.156	1.00	37.27	C
ATOM	1898	O	PHE	A	237	12.431	−0.150	23.622	1.00	36.59	O
ATOM	1899	N	THR	A	238	10.963	−0.574	25.251	1.00	38.47	N
ATOM	1900	CA	THR	A	238	11.898	−1.466	25.938	1.00	41.11	C
ATOM	1901	CB	THR	A	238	11.518	−1.701	27.425	1.00	41.38	C
ATOM	1902	OG1	THR	A	238	10.103	−1.921	27.577	1.00	43.82	O
ATOM	1903	CG2	THR	A	238	11.704	−0.400	28.235	1.00	42.85	C
ATOM	1904	C	THR	A	238	12.282	−2.759	25.156	1.00	42.23	C
ATOM	1905	O	THR	A	238	13.435	−3.225	25.283	1.00	42.40	O
ATOM	1906	N	ASP	A	239	11.384	−3.290	24.300	1.00	42.91	N
ATOM	1907	CA	ASP	A	239	11.780	−4.416	23.415	1.00	43.62	C
ATOM	1908	CB	ASP	A	239	10.656	−5.016	22.535	1.00	43.54	C
ATOM	1909	CG	ASP	A	239	9.446	−5.549	23.333	1.00	45.80	C
ATOM	1910	OD1	ASP	A	239	9.538	−5.917	24.544	1.00	42.75	O
ATOM	1911	OD2	ASP	A	239	8.313	−5.623	22.774	1.00	51.39	O
ATOM	1912	C	ASP	A	239	12.884	−3.938	22.518	1.00	42.96	C
ATOM	1913	O	ASP	A	239	13.880	−4.628	22.367	1.00	43.19	O
ATOM	1914	N	ALA	A	240	12.745	−2.724	21.984	1.00	43.01	N
ATOM	1915	CA	ALA	A	240	13.660	−2.238	20.918	1.00	42.90	C
ATOM	1916	CB	ALA	A	240	13.020	−1.148	20.104	1.00	43.06	C
ATOM	1917	C	ALA	A	240	15.039	−1.805	21.370	1.00	42.95	C
ATOM	1918	O	ALA	A	240	15.879	−1.408	20.531	1.00	43.55	O
ATOM	1919	N	GLY	A	241	15.298	−1.911	22.673	1.00	43.13	N
ATOM	1920	CA	GLY	A	241	16.606	−1.581	23.222	1.00	42.68	C
ATOM	1921	C	GLY	A	241	16.574	−0.378	24.165	1.00	42.42	C
ATOM	1922	O	GLY	A	241	17.365	−0.318	25.119	1.00	43.37	O
ATOM	1923	N	PHE	A	242	15.664	0.571	23.921	1.00	40.27	N
ATOM	1924	CA	PHE	A	242	15.675	1.822	24.667	1.00	38.64	C
ATOM	1925	CB	PHE	A	242	14.784	2.888	24.005	1.00	38.33	C
ATOM	1926	CG	PHE	A	242	14.895	2.975	22.483	1.00	37.73	C
ATOM	1927	CD1	PHE	A	242	15.896	3.741	21.881	1.00	34.04	C
ATOM	1928	CE1	PHE	A	242	15.982	3.864	20.506	1.00	32.34	C
ATOM	1929	CZ	PHE	A	242	15.028	3.240	19.707	1.00	35.96	C
ATOM	1930	CE2	PHE	A	242	13.993	2.487	20.291	1.00	35.46	C
ATOM	1931	CD2	PHE	A	242	13.929	2.361	21.662	1.00	37.05	C
ATOM	1932	C	PHE	A	242	15.259	1.613	26.158	1.00	38.09	C
ATOM	1933	O	PHE	A	242	14.373	0.767	26.477	1.00	37.60	O
ATOM	1934	N	GLU	A	243	15.905	2.363	27.057	1.00	35.83	N
ATOM	1935	CA	GLU	A	243	15.437	2.415	28.432	1.00	35.24	C
ATOM	1936	CB	GLU	A	243	16.464	3.028	29.428	1.00	34.84	C
ATOM	1937	CG	GLU	A	243	17.805	2.305	29.542	1.00	39.39	C
ATOM	1938	CD	GLU	A	243	18.971	3.294	29.717	1.00	45.45	C
ATOM	1939	OE1	GLU	A	243	19.980	3.133	28.962	1.00	44.87	O
ATOM	1940	OE2	GLU	A	243	18.869	4.240	30.594	1.00	42.25	O
ATOM	1941	C	GLU	A	243	14.227	3.324	28.364	1.00	33.37	C
ATOM	1942	O	GLU	A	243	14.213	4.277	27.577	1.00	32.60	O
ATOM	1943	N	HIS	A	244	13.250	3.053	29.224	1.00	31.08	N
ATOM	1944	CA	HIS	A	244	12.089	3.887	29.368	1.00	29.13	C
ATOM	1945	CB	HIS	A	244	10.915	3.273	28.617	1.00	27.66	C
ATOM	1946	CG	HIS	A	244	9.698	4.144	28.563	1.00	21.87	C
ATOM	1947	ND1	HIS	A	244	8.867	4.318	29.646	1.00	17.46	N
ATOM	1948	CE1	HIS	A	244	7.874	5.120	29.321	1.00	20.24	C
ATOM	1949	NE2	HIS	A	244	8.008	5.436	28.045	1.00	21.82	N
ATOM	1950	CD2	HIS	A	244	9.140	4.837	27.546	1.00	18.54	C
ATOM	1951	C	HIS	A	244	11.762	4.136	30.847	1.00	30.55	C
ATOM	1952	O	HIS	A	244	11.902	3.239	31.714	1.00	31.45	O
ATOM	1953	N	TYR	A	245	11.323	5.365	31.124	1.00	30.58	N
ATOM	1954	CA	TYR	A	245	11.086	5.822	32.470	1.00	30.95	C
ATOM	1955	CB	TYR	A	245	12.250	6.722	32.960	1.00	30.16	C
ATOM	1956	CG	TYR	A	245	13.653	6.091	32.852	1.00	28.65	C
ATOM	1957	CD1	TYR	A	245	14.395	6.215	31.693	1.00	27.94	C
ATOM	1958	CE1	TYR	A	245	15.681	5.644	31.591	1.00	27.22	C
ATOM	1959	CZ	TYR	A	245	16.260	4.943	32.668	1.00	28.94	C
ATOM	1960	OH	TYR	A	245	17.550	4.424	32.493	1.00	27.52	O
ATOM	1961	CE2	TYR	A	245	15.558	4.790	33.835	1.00	22.12	C
ATOM	1962	CD2	TYR	A	245	14.229	5.378	33.922	1.00	26.55	C
ATOM	1963	C	TYR	A	245	9.801	6.585	32.505	1.00	32.22	C
ATOM	1964	O	TYR	A	245	9.461	7.309	31.565	1.00	32.35	O
ATOM	1965	N	ASP	A	246	9.072	6.416	33.594	1.00	33.96	N
ATOM	1966	CA	ASP	A	246	7.837	7.141	33.785	1.00	35.29	C
ATOM	1967	CB	ASP	A	246	6.652	6.196	34.033	1.00	36.07	C
ATOM	1968	CG	ASP	A	246	5.931	5.853	32.758	1.00	38.43	C
ATOM	1969	OD1	ASP	A	246	6.038	4.680	32.352	1.00	39.32	O
ATOM	1970	OD2	ASP	A	246	5.295	6.705	32.075	1.00	40.60	O
ATOM	1971	C	ASP	A	246	8.036	8.045	34.945	1.00	35.45	C
ATOM	1972	O	ASP	A	246	8.350	7.598	36.082	1.00	37.00	O
ATOM	1973	N	LEU	A	247	7.849	9.320	34.668	1.00	34.92	N
ATOM	1974	CA	LEU	A	247	8.195	10.342	35.620	1.00	34.71	C
ATOM	1975	CB	LEU	A	247	9.540	10.973	35.234	1.00	34.09	C
ATOM	1976	CG	LEU	A	247	10.744	10.960	36.170	1.00	32.78	C
ATOM	1977	CD1	LEU	A	247	11.424	12.273	36.047	1.00	31.61	C
ATOM	1978	CD2	LEU	A	247	10.388	10.756	37.609	1.00	35.22	C
ATOM	1979	C	LEU	A	247	7.042	11.278	35.542	1.00	34.29	C
ATOM	1980	O	LEU	A	247	7.139	12.376	35.044	1.00	35.70	O
ATOM	1981	N	PHE	A	248	5.913	10.784	35.988	1.00	34.49	N
ATOM	1982	CA	PHE	A	248	4.682	11.532	35.921	1.00	35.03	C
ATOM	1983	CB	PHE	A	248	3.450	10.624	36.149	1.00	35.31	C
ATOM	1984	CG	PHE	A	248	2.149	11.372	36.116	1.00	34.16	C
ATOM	1985	CD1	PHE	A	248	1.581	11.762	34.888	1.00	34.27	C
ATOM	1986	CE1	PHE	A	248	0.367	12.476	34.818	1.00	31.97	C
ATOM	1987	CZ	PHE	A	248	−0.276	12.811	35.979	1.00	34.83	C
ATOM	1988	CE2	PHE	A	248	0.292	12.419	37.249	1.00	34.87	C
ATOM	1989	CD2	PHE	A	248	1.504	11.706	37.290	1.00	33.55	C
ATOM	1990	C	PHE	A	248	4.649	12.688	36.928	1.00	35.60	C
ATOM	1991	O	PHE	A	248	4.901	12.498	38.121	1.00	35.37	O
ATOM	1992	N	PHE	A	249	4.354	13.884	36.415	1.00	35.44	N
ATOM	1993	CA	PHE	A	249	3.748	14.904	37.221	1.00	35.94	C
ATOM	1994	CB	PHE	A	249	4.734	15.895	37.845	1.00	34.76	C
ATOM	1995	CG	PHE	A	249	5.564	16.650	36.870	1.00	34.05	C
ATOM	1996	CD1	PHE	A	249	5.467	18.051	36.816	1.00	30.40	C
ATOM	1997	CE1	PHE	A	249	6.276	18.780	35.970	1.00	30.04	C
ATOM	1998	CZ	PHE	A	249	7.206	18.106	35.118	1.00	27.36	C
ATOM	1999	CE2	PHE	A	249	7.279	16.686	35.129	1.00	29.07	C
ATOM	2000	CD2	PHE	A	249	6.486	15.973	36.017	1.00	31.77	C
ATOM	2001	C	PHE	A	249	2.649	15.581	36.457	1.00	37.24	C
ATOM	2002	O	PHE	A	249	2.590	15.536	35.205	1.00	37.41	O
ATOM	2003	N	ILE	A	250	1.755	16.178	37.232	1.00	38.35	N
ATOM	2004	CA	ILE	A	250	0.501	16.703	36.691	1.00	40.18	C
ATOM	2005	CB	ILE	A	250	−0.450	17.080	37.919	1.00	40.19	C
ATOM	2006	CG1	ILE	A	250	−1.390	15.901	38.299	1.00	42.73	C
ATOM	2007	CD1	ILE	A	250	−2.597	15.568	37.259	1.00	49.36	C
ATOM	2008	CG2	ILE	A	250	−1.173	18.393	37.754	1.00	40.85	C
ATOM	2009	C	ILE	A	250	0.790	17.840	35.643	1.00	39.62	C
ATOM	2010	O	ILE	A	250	1.670	18.685	35.865	1.00	39.16	O
ATOM	2011	N	ASP	A	251	0.093	17.790	34.509	1.00	38.79	N
ATOM	2012	CA	ASP	A	251	0.067	18.872	33.528	1.00	38.62	C
ATOM	2013	CB	ASP	A	251	−0.961	18.584	32.412	1.00	39.07	C
ATOM	2014	CG	ASP	A	251	−0.787	19.513	31.185	1.00	39.25	C
ATOM	2015	OD1	ASP	A	251	0.202	20.273	31.145	1.00	41.44	O
ATOM	2016	OD2	ASP	A	251	−1.568	19.561	30.221	1.00	37.02	O
ATOM	2017	C	ASP	A	251	−0.203	20.255	34.118	1.00	38.15	C
ATOM	2018	O	ASP	A	251	−1.098	20.427	34.935	1.00	38.39	O
ATOM	2019	N	GLY	A	252	0.593	21.237	33.698	1.00	38.07	N
ATOM	2020	CA	GLY	A	252	0.483	22.606	34.197	1.00	37.90	C
ATOM	2021	C	GLY	A	252	1.097	22.904	35.561	1.00	37.77	C
ATOM	2022	O	GLY	A	252	0.871	23.975	36.156	1.00	38.18	O
ATOM	2023	N	SER	A	253	1.882	21.962	36.069	1.00	37.46	N
ATOM	2024	CA	SER	A	253	2.410	22.064	37.432	1.00	36.50	C
ATOM	2025	CB	SER	A	253	1.830	20.963	38.331	1.00	36.53	C
ATOM	2026	OG	SER	A	253	2.736	19.869	38.455	1.00	36.46	O
ATOM	2027	C	SER	A	253	3.938	22.000	37.418	1.00	35.52	C
ATOM	2028	O	SER	A	253	4.552	21.611	36.411	1.00	33.73	O
ATOM	2029	N	THR	A	254	4.544	22.374	38.548	1.00	34.92	N
ATOM	2030	CA	THR	A	254	5.991	22.227	38.660	1.00	34.27	C
ATOM	2031	CB	THR	A	254	6.569	23.400	39.419	1.00	34.14	C
ATOM	2032	OG1	THR	A	254	6.024	23.361	40.715	1.00	34.47	O
ATOM	2033	CG2	THR	A	254	6.051	24.737	38.835	1.00	33.34	C
ATOM	2034	C	THR	A	254	6.399	20.864	39.268	1.00	33.63	C
ATOM	2035	O	THR	A	254	5.666	20.310	40.117	1.00	32.44	O
ATOM	2036	N	PRO	A	255	7.562	20.341	38.838	1.00	33.32	N
ATOM	2037	CA	PRO	A	255	8.063	19.027	39.298	1.00	33.83	C
ATOM	2038	CB	PRO	A	255	9.251	18.749	38.339	1.00	32.84	C
ATOM	2039	CG	PRO	A	255	9.749	20.086	37.939	1.00	31.39	C
ATOM	2040	CD	PRO	A	255	8.543	20.988	37.949	1.00	32.83	C
ATOM	2041	C	PRO	A	255	8.561	19.091	40.769	1.00	33.79	C
ATOM	2042	O	PRO	A	255	9.333	20.014	41.093	1.00	33.22	O
ATOM	2043	N	SER	A	256	8.086	18.176	41.628	1.00	34.22	N
ATOM	2044	CA	SER	A	256	8.593	18.060	43.015	1.00	34.71	C
ATOM	2045	CB	SER	A	256	7.912	16.934	43.813	1.00	33.96	C
ATOM	2046	OG	SER	A	256	8.289	15.651	43.323	1.00	33.61	O
ATOM	2047	C	SER	A	256	10.058	17.791	42.979	1.00	34.97	C
ATOM	2048	O	SER	A	256	10.644	17.488	41.933	1.00	35.81	O
ATOM	2049	N	ASP	A	257	10.655	17.904	44.143	1.00	36.74	N
ATOM	2050	CA	ASP	A	257	12.075	17.634	44.315	1.00	37.33	C
ATOM	2051	CB	ASP	A	257	12.530	18.132	45.691	1.00	38.23	C
ATOM	2052	CG	ASP	A	257	12.611	19.682	45.728	1.00	41.57	C
ATOM	2053	OD1	ASP	A	257	11.975	20.302	44.853	1.00	43.82	O
ATOM	2054	OD2	ASP	A	257	13.287	20.376	46.531	1.00	47.11	O
ATOM	2055	C	ASP	A	257	12.494	16.214	43.939	1.00	36.53	C
ATOM	2056	O	ASP	A	257	13.515	16.030	43.256	1.00	36.07	O
ATOM	2057	N	ASN	A	258	11.662	15.245	44.292	1.00	36.12	N
ATOM	2058	CA	ASN	A	258	11.899	13.838	43.947	1.00	37.33	C
ATOM	2059	CB	ASN	A	258	10.797	12.925	44.572	1.00	38.74	C
ATOM	2060	CG	ASN	A	258	11.218	12.323	45.902	1.00	44.26	C
ATOM	2061	OD1	ASN	A	258	12.281	12.701	46.478	1.00	47.97	O
ATOM	2062	ND2	ASN	A	258	10.383	11.402	46.431	1.00	47.79	N
ATOM	2063	C	ASN	A	258	11.917	13.606	42.439	1.00	36.01	C
ATOM	2064	O	ASN	A	258	12.784	12.883	41.915	1.00	36.05	O
ATOM	2065	N	ILE	A	259	10.921	14.188	41.756	1.00	34.53	N
ATOM	2066	CA	ILE	A	259	10.875	14.124	40.323	1.00	33.32	C
ATOM	2067	CB	ILE	A	259	9.523	14.646	39.802	1.00	33.47	C
ATOM	2068	CG1	ILE	A	259	8.511	13.486	39.905	1.00	35.12	C
ATOM	2069	CD1	ILE	A	259	7.082	13.868	39.969	1.00	37.39	C
ATOM	2070	CG2	ILE	A	259	9.638	15.080	38.356	1.00	30.26	C
ATOM	2071	C	ILE	A	259	12.140	14.789	39.707	1.00	33.37	C
ATOM	2072	O	ILE	A	259	12.829	14.181	38.833	1.00	32.48	O
ATOM	2073	N	VAL	A	260	12.488	16.002	40.174	1.00	31.92	N
ATOM	2074	CA	VAL	A	260	13.665	16.624	39.573	1.00	30.84	C
ATOM	2075	CB	VAL	A	260	13.997	18.052	40.113	1.00	31.16	C
ATOM	2076	CG1	VAL	A	260	15.340	18.546	39.510	1.00	30.06	C
ATOM	2077	CG2	VAL	A	260	12.875	19.038	39.815	1.00	28.07	C
ATOM	2078	C	VAL	A	260	14.848	15.690	39.750	1.00	30.24	C
ATOM	2079	O	VAL	A	260	15.535	15.393	38.785	1.00	30.14	O
ATOM	2080	N	ARG	A	261	15.038	15.188	40.978	1.00	30.19	N
ATOM	2081	CA	ARG	A	261	16.202	14.363	41.344	1.00	29.99	C
ATOM	2082	CB	ARG	A	261	16.280	14.169	42.858	1.00	30.77	C
ATOM	2083	CG	ARG	A	261	17.027	15.331	43.599	1.00	37.31	C
ATOM	2084	CD	ARG	A	261	16.369	15.758	44.964	1.00	48.99	C
ATOM	2085	NE	ARG	A	261	16.832	17.067	45.521	1.00	55.00	N
ATOM	2086	CZ	ARG	A	261	16.454	18.304	45.089	1.00	56.95	C
ATOM	2087	NH1	ARG	A	261	15.605	18.487	44.064	1.00	57.23	N
ATOM	2088	NH2	ARG	A	261	16.955	19.376	45.683	1.00	56.62	N
ATOM	2089	C	ARG	A	261	16.241	13.018	40.586	1.00	28.88	C
ATOM	2090	O	ARG	A	261	17.337	12.551	40.154	1.00	28.49	O
ATOM	2091	N	ARG	A	262	15.061	12.416	40.362	1.00	26.25	N
ATOM	2092	CA	ARG	A	262	15.043	11.186	39.571	1.00	24.69	C
ATOM	2093	CB	ARG	A	262	13.726	10.426	39.683	1.00	25.43	C
ATOM	2094	CG	ARG	A	262	13.751	9.053	39.038	1.00	26.17	C
ATOM	2095	CD	ARG	A	262	14.476	7.919	39.782	1.00	24.92	C
ATOM	2096	NE	ARG	A	262	14.134	6.611	39.188	1.00	22.17	N
ATOM	2097	CZ	ARG	A	262	14.883	5.963	38.283	1.00	22.83	C
ATOM	2098	NH1	ARG	A	262	16.049	6.466	37.896	1.00	17.65	N
ATOM	2099	NH2	ARG	A	262	14.467	4.794	37.765	1.00	19.57	N
ATOM	2100	C	ARG	A	262	15.354	11.486	38.136	1.00	23.79	C
ATOM	2101	O	ARG	A	262	16.069	10.718	37.510	1.00	22.36	O
ATOM	2102	N	PHE	A	263	14.874	12.640	37.651	1.00	23.30	N
ATOM	2103	CA	PHE	A	263	15.188	13.072	36.329	1.00	23.64	C
ATOM	2104	CB	PHE	A	263	14.390	14.322	35.934	1.00	22.73	C
ATOM	2105	CG	PHE	A	263	14.607	14.723	34.469	1.00	22.71	C
ATOM	2106	CD1	PHE	A	263	13.964	14.028	33.447	1.00	18.84	C
ATOM	2107	CE1	PHE	A	263	14.140	14.363	32.082	1.00	20.04	C
ATOM	2108	CZ	PHE	A	263	14.957	15.406	31.705	1.00	19.05	C
ATOM	2109	CE2	PHE	A	263	15.657	16.123	32.730	1.00	24.61	C
ATOM	2110	CD2	PHE	A	263	15.495	15.759	34.117	1.00	23.48	C
ATOM	2111	C	PHE	A	263	16.701	13.295	36.138	1.00	24.87	C
ATOM	2112	O	PHE	A	263	17.323	12.790	35.190	1.00	25.68	O
ATOM	2113	N	LEU	A	264	17.293	14.100	37.008	1.00	25.79	N
ATOM	2114	CA	LEU	A	264	18.739	14.301	36.968	1.00	25.94	C
ATOM	2115	CB	LEU	A	264	19.152	15.073	38.208	1.00	25.48	C
ATOM	2116	CG	LEU	A	264	18.665	16.505	38.145	1.00	24.23	C
ATOM	2117	CD1	LEU	A	264	19.103	17.310	39.402	1.00	25.19	C
ATOM	2118	CD2	LEU	A	264	19.166	17.121	36.763	1.00	25.71	C
ATOM	2119	C	LEU	A	264	19.469	12.976	36.959	1.00	27.03	C
ATOM	2120	O	LEU	A	264	20.374	12.750	36.157	1.00	26.99	O
ATOM	2121	N	ASN	A	265	19.070	12.098	37.878	1.00	27.75	N
ATOM	2122	CA	ASN	A	265	19.735	10.800	38.047	1.00	28.08	C
ATOM	2123	CB	ASN	A	265	19.143	10.114	39.281	1.00	27.71	C
ATOM	2124	CG	ASN	A	265	19.390	8.614	39.321	1.00	29.77	C
ATOM	2125	OD1	ASN	A	265	18.538	7.818	38.877	1.00	28.58	O
ATOM	2126	ND2	ASN	A	265	20.545	8.210	39.885	1.00	28.45	N
ATOM	2127	C	ASN	A	265	19.611	9.944	36.796	1.00	27.97	C
ATOM	2128	O	ASN	A	265	20.556	9.310	36.411	1.00	29.56	O
ATOM	2129	N	ILE	A	266	18.451	9.939	36.155	1.00	27.72	N
ATOM	2130	CA	ILE	A	266	18.272	9.264	34.874	1.00	27.43	C
ATOM	2131	CB	ILE	A	266	16.764	9.318	34.387	1.00	27.09	C
ATOM	2132	CG1	ILE	A	266	15.903	8.450	35.302	1.00	24.67	C
ATOM	2133	CD1	ILE	A	266	14.411	8.920	35.477	1.00	22.89	C
ATOM	2134	CG2	ILE	A	266	16.637	8.852	32.888	1.00	22.91	C
ATOM	2135	C	ILE	A	266	19.221	9.801	33.797	1.00	28.75	C
ATOM	2136	O	ILE	A	266	19.894	9.010	33.110	1.00	29.64	O
ATOM	2137	N	CYS	A	267	19.298	11.135	33.659	1.00	29.82	N
ATOM	2138	CA	CYS	A	267	20.094	11.732	32.571	1.00	30.23	C
ATOM	2139	CB	CYS	A	267	19.643	13.150	32.192	1.00	29.11	C
ATOM	2140	SG	CYS	A	267	17.883	13.155	31.972	1.00	30.61	S
ATOM	2141	C	CYS	A	267	21.574	11.632	32.831	1.00	30.73	C
ATOM	2142	O	CYS	A	267	22.399	11.555	31.890	1.00	31.62	O
ATOM	2143	N	GLU	A	268	21.922	11.609	34.101	1.00	31.75	N
ATOM	2144	CA	GLU	A	268	23.318	11.528	34.463	1.00	32.58	C
ATOM	2145	CB	GLU	A	268	23.514	11.982	35.900	1.00	31.69	C
ATOM	2146	CG	GLU	A	268	23.590	13.457	36.087	1.00	29.64	C
ATOM	2147	CD	GLU	A	268	23.137	13.905	37.468	1.00	32.21	C
ATOM	2148	OE1	GLU	A	268	22.900	13.025	38.337	1.00	32.99	O
ATOM	2149	OE2	GLU	A	268	23.021	15.156	37.701	1.00	32.37	O
ATOM	2150	C	GLU	A	268	23.807	10.084	34.240	1.00	34.08	C
ATOM	2151	O	GLU	A	268	24.967	9.875	33.936	1.00	34.79	O
ATOM	2152	N	ASN	A	269	22.928	9.091	34.359	1.00	35.31	N
ATOM	2153	CA	ASN	A	269	23.404	7.712	34.353	1.00	36.46	C
ATOM	2154	CB	ASN	A	269	22.877	6.928	35.578	1.00	36.54	C
ATOM	2155	CG	ASN	A	269	23.394	7.516	36.897	1.00	37.53	C
ATOM	2156	OD1	ASN	A	269	24.602	7.657	37.087	1.00	37.87	O
ATOM	2157	ND2	ASN	A	269	22.473	7.909	37.788	1.00	34.48	N
ATOM	2158	C	ASN	A	269	23.156	6.966	33.060	1.00	37.25	C
ATOM	2159	O	ASN	A	269	23.554	5.800	32.930	1.00	37.33	O
ATOM	2160	N	THR	A	270	22.493	7.634	32.116	1.00	38.07	N
ATOM	2161	CA	THR	A	270	22.181	7.023	30.820	1.00	38.56	C
ATOM	2162	CB	THR	A	270	20.727	7.459	30.346	1.00	38.64	C
ATOM	2163	OG1	THR	A	270	20.282	6.653	29.241	1.00	39.90	O
ATOM	2164	CG2	THR	A	270	20.716	8.844	29.804	1.00	38.79	C
ATOM	2165	C	THR	A	270	23.329	7.313	29.831	1.00	38.44	C
ATOM	2166	O	THR	A	270	24.016	8.340	29.990	1.00	37.92	O
ATOM	2167	N	GLU	A	271	23.592	6.423	28.852	1.00	38.52	N
ATOM	2168	CA	GLU	A	271	24.832	6.618	28.038	1.00	38.99	C
ATOM	2169	CB	GLU	A	271	25.495	5.316	27.585	1.00	39.60	C
ATOM	2170	CG	GLU	A	271	26.889	5.138	28.186	1.00	44.95	C
ATOM	2171	CD	GLU	A	271	26.990	3.887	29.076	1.00	53.61	C
ATOM	2172	OE1	GLU	A	271	26.316	3.843	30.144	1.00	55.28	O
ATOM	2173	OE2	GLU	A	271	27.724	2.922	28.700	1.00	56.66	O
ATOM	2174	C	GLU	A	271	24.882	7.685	26.923	1.00	37.61	C
ATOM	2175	O	GLU	A	271	25.876	8.377	26.820	1.00	37.56	O
ATOM	2176	N	GLY	A	272	23.850	7.797	26.086	1.00	36.48	N
ATOM	2177	CA	GLY	A	272	23.789	8.877	25.094	1.00	34.76	C
ATOM	2178	C	GLY	A	272	22.536	9.753	25.267	1.00	33.52	C
ATOM	2179	O	GLY	A	272	22.256	10.237	26.376	1.00	32.95	O
ATOM	2180	N	ALA	A	273	21.744	9.895	24.201	1.00	31.04	N
ATOM	2181	CA	ALA	A	273	20.674	10.870	24.211	1.00	29.58	C
ATOM	2182	CB	ALA	A	273	20.396	11.388	22.805	1.00	29.41	C
ATOM	2183	C	ALA	A	273	19.399	10.466	24.977	1.00	29.57	C
ATOM	2184	O	ALA	A	273	19.077	9.257	25.140	1.00	30.10	O
ATOM	2185	N	ILE	A	274	18.723	11.473	25.537	1.00	28.07	N
ATOM	2186	CA	ILE	A	274	17.456	11.266	26.239	1.00	26.92	C
ATOM	2187	CB	ILE	A	274	17.501	11.801	27.714	1.00	26.71	C
ATOM	2188	CG1	ILE	A	274	18.649	11.195	28.516	1.00	26.40	C
ATOM	2189	CD1	ILE	A	274	19.761	12.230	28.830	1.00	28.28	C
ATOM	2190	CG2	ILE	A	274	16.168	11.575	28.487	1.00	26.66	C
ATOM	2191	C	ILE	A	274	16.411	12.034	25.417	1.00	27.28	C
ATOM	2192	O	ILE	A	274	16.576	13.215	25.121	1.00	27.82	O
ATOM	2193	N	ALA	A	275	15.364	11.328	25.007	1.00	27.11	N
ATOM	2194	CA	ALA	A	275	14.207	11.880	24.340	1.00	25.37	C
ATOM	2195	CB	ALA	A	275	13.769	10.913	23.272	1.00	25.99	C
ATOM	2196	C	ALA	A	275	13.147	11.995	25.408	1.00	25.03	C
ATOM	2197	O	ALA	A	275	12.789	10.975	26.045	1.00	25.22	O
ATOM	2198	N	VAL	A	276	12.685	13.224	25.653	1.00	23.73	N
ATOM	2199	CA	VAL	A	276	11.738	13.507	26.737	1.00	23.38	C
ATOM	2200	CB	VAL	A	276	12.322	14.607	27.713	1.00	23.75	C
ATOM	2201	CG1	VAL	A	276	11.316	15.047	28.819	1.00	20.32	C
ATOM	2202	CG2	VAL	A	276	13.597	14.086	28.342	1.00	20.65	C
ATOM	2203	C	VAL	A	276	10.421	13.973	26.153	1.00	24.51	C
ATOM	2204	O	VAL	A	276	10.434	14.814	25.250	1.00	23.65	O
ATOM	2205	N	HIS	A	277	9.288	13.433	26.642	1.00	25.56	N
ATOM	2206	CA	HIS	A	277	7.990	13.971	26.210	1.00	26.31	C
ATOM	2207	CB	HIS	A	277	7.358	13.182	25.037	1.00	27.21	C
ATOM	2208	CG	HIS	A	277	6.820	11.828	25.412	1.00	27.05	C
ATOM	2209	ND1	HIS	A	277	5.580	11.650	25.990	1.00	27.12	N
ATOM	2210	CE1	HIS	A	277	5.384	10.357	26.208	1.00	25.84	C
ATOM	2211	NE2	HIS	A	277	6.455	9.696	25.793	1.00	22.78	N
ATOM	2212	CD2	HIS	A	277	7.359	10.589	25.285	1.00	23.62	C
ATOM	2213	C	HIS	A	277	7.016	14.097	27.297	1.00	26.54	C
ATOM	2214	O	HIS	A	277	7.133	13.429	28.317	1.00	27.98	O
ATOM	2215	N	CYS	A	278	6.069	15.012	27.104	1.00	27.54	N
ATOM	2216	CA	CYS	A	278	4.803	14.966	27.804	1.00	27.10	C
ATOM	2217	CB	CYS	A	278	4.612	16.194	28.674	1.00	27.51	C
ATOM	2218	SG	CYS	A	278	5.254	17.706	27.937	1.00	29.54	S
ATOM	2219	C	CYS	A	278	3.691	14.759	26.738	1.00	27.18	C
ATOM	2220	O	CYS	A	278	3.762	13.843	25.915	1.00	26.85	O
ATOM	2221	N	LYS	A	279	2.660	15.568	26.730	1.00	27.77	N
ATOM	2222	CA	LYS	A	279	1.682	15.440	25.618	1.00	29.27	C
ATOM	2223	CB	LYS	A	279	0.300	16.018	26.025	1.00	28.72	C
ATOM	2224	CG	LYS	A	279	−0.874	15.522	25.242	1.00	32.93	C
ATOM	2225	CD	LYS	A	279	−2.119	15.405	26.206	1.00	43.60	C
ATOM	2226	CE	LYS	A	279	−1.711	15.163	27.751	1.00	44.22	C
ATOM	2227	NZ	LYS	A	279	−2.214	16.261	28.672	1.00	44.01	N
ATOM	2228	C	LYS	A	279	2.228	16.171	24.363	1.00	27.26	C
ATOM	2229	O	LYS	A	279	2.372	15.587	23.316	1.00	26.12	O
ATOM	2230	N	ALA	A	280	2.498	17.464	24.517	1.00	28.21	N
ATOM	2231	CA	ALA	A	280	3.022	18.354	23.442	1.00	28.48	C
ATOM	2232	CB	ALA	A	280	2.313	19.711	23.490	1.00	27.53	C
ATOM	2233	C	ALA	A	280	4.560	18.521	23.492	1.00	28.26	C
ATOM	2234	O	ALA	A	280	5.130	19.057	22.571	1.00	29.70	O
ATOM	2235	N	GLY	A	281	5.215	18.037	24.554	1.00	27.46	N
ATOM	2236	CA	GLY	A	281	6.653	18.178	24.729	1.00	26.71	C
ATOM	2237	C	GLY	A	281	7.142	19.607	24.975	1.00	26.35	C
ATOM	2238	O	GLY	A	281	8.279	19.955	24.589	1.00	26.47	O
ATOM	2239	N	LEU	A	282	6.304	20.415	25.625	1.00	24.58	N
ATOM	2240	CA	LEU	A	282	6.583	21.825	25.849	1.00	24.44	C
ATOM	2241	CB	LEU	A	282	5.424	22.690	25.337	1.00	24.07	C
ATOM	2242	CG	LEU	A	282	5.287	23.309	23.930	1.00	25.60	C
ATOM	2243	CD1	LEU	A	282	6.055	22.615	22.782	1.00	19.91	C
ATOM	2244	CD2	LEU	A	282	3.771	23.469	23.613	1.00	22.25	C
ATOM	2245	C	LEU	A	282	6.829	22.167	27.339	1.00	23.73	C
ATOM	2246	O	LEU	A	282	7.904	22.637	27.689	1.00	22.83	O
ATOM	2247	N	GLY	A	283	5.822	21.951	28.194	1.00	23.40	N
ATOM	2248	CA	GLY	A	283	5.844	22.485	29.545	1.00	22.27	C
ATOM	2249	C	GLY	A	283	6.738	21.671	30.435	1.00	21.96	C
ATOM	2250	O	GLY	A	283	7.848	22.063	30.792	1.00	22.22	O
ATOM	2251	N	ARG	A	284	6.248	20.504	30.784	1.00	22.52	N
ATOM	2252	CA	ARG	A	284	6.889	19.608	31.743	1.00	23.41	C
ATOM	2253	CB	ARG	A	284	6.021	18.369	31.918	1.00	23.96	C
ATOM	2254	CG	ARG	A	284	4.765	18.661	32.728	1.00	26.31	C
ATOM	2255	CD	ARG	A	284	3.811	17.545	32.753	1.00	29.52	C
ATOM	2256	NE	ARG	A	284	3.016	17.507	31.527	1.00	34.12	N
ATOM	2257	CZ	ARG	A	284	2.004	16.672	31.322	1.00	35.39	C
ATOM	2258	NH1	ARG	A	284	1.674	15.835	32.307	1.00	37.21	N
ATOM	2259	NH2	ARG	A	284	1.305	16.691	30.161	1.00	33.18	N
ATOM	2260	C	ARG	A	284	8.202	19.202	31.162	1.00	23.93	C
ATOM	2261	O	ARG	A	284	9.245	19.206	31.845	1.00	24.51	O
ATOM	2262	N	THR	A	285	8.153	18.875	29.874	1.00	24.20	N
ATOM	2263	CA	THR	A	285	9.329	18.502	29.119	1.00	24.46	C
ATOM	2264	CB	THR	A	285	8.933	18.271	27.659	1.00	24.48	C
ATOM	2265	OG1	THR	A	285	8.176	17.058	27.609	1.00	24.78	O
ATOM	2266	CG2	THR	A	285	10.169	17.986	26.739	1.00	23.96	C
ATOM	2267	C	THR	A	285	10.463	19.522	29.238	1.00	24.65	C
ATOM	2268	O	THR	A	285	11.563	19.199	29.729	1.00	25.01	O
ATOM	2269	N	GLY	A	286	10.201	20.730	28.766	1.00	23.81	N
ATOM	2270	CA	GLY	A	286	11.212	21.765	28.773	1.00	22.58	C
ATOM	2271	C	GLY	A	286	11.541	22.134	30.188	1.00	21.56	C
ATOM	2272	O	GLY	A	286	12.663	22.508	30.439	1.00	20.38	O
ATOM	2273	N	THR	A	287	10.594	21.999	31.114	1.00	20.80	N
ATOM	2274	CA	THR	A	287	10.950	22.257	32.506	1.00	21.40	C
ATOM	2275	CB	THR	A	287	9.729	22.318	33.397	1.00	21.58	C
ATOM	2276	OG1	THR	A	287	8.949	23.458	32.982	1.00	21.94	O
ATOM	2277	CG2	THR	A	287	10.131	22.614	34.884	1.00	16.63	C
ATOM	2278	C	THR	A	287	12.047	21.324	33.077	1.00	22.39	C
ATOM	2279	O	THR	A	287	13.062	21.806	33.661	1.00	23.25	O
ATOM	2280	N	LEU	A	288	11.882	20.010	32.909	1.00	21.73	N
ATOM	2281	CA	LEU	A	288	12.908	19.089	33.420	1.00	21.17	C
ATOM	2282	CB	LEU	A	288	12.411	17.646	33.428	1.00	21.17	C
ATOM	2283	CG	LEU	A	288	11.334	17.443	34.496	1.00	21.85	C
ATOM	2284	CD1	LEU	A	288	10.975	15.992	34.421	1.00	21.26	C
ATOM	2285	CD2	LEU	A	288	11.910	17.821	35.850	1.00	16.90	C
ATOM	2286	C	LEU	A	288	14.244	19.197	32.695	1.00	20.31	C
ATOM	2287	O	LEU	A	288	15.296	19.029	33.322	1.00	20.94	O
ATOM	2288	N	ILE	A	289	14.222	19.467	31.389	1.00	19.36	N
ATOM	2289	CA	ILE	A	289	15.451	19.485	30.601	1.00	18.68	C
ATOM	2290	CB	ILE	A	289	15.205	19.556	29.127	1.00	18.04	C
ATOM	2291	CG1	ILE	A	289	14.671	18.210	28.629	1.00	16.59	C
ATOM	2292	CD1	ILE	A	289	14.154	18.282	27.183	1.00	11.62	C
ATOM	2293	CG2	ILE	A	289	16.532	20.043	28.322	1.00	18.05	C
ATOM	2294	C	ILE	A	289	16.196	20.699	31.036	1.00	20.66	C
ATOM	2295	O	ILE	A	289	17.422	20.644	31.183	1.00	20.84	O
ATOM	2296	N	ALA	A	290	15.438	21.780	31.249	1.00	21.68	N
ATOM	2297	CA	ALA	A	290	15.921	23.042	31.766	1.00	22.16	C
ATOM	2298	CB	ALA	A	290	14.760	23.941	31.940	1.00	22.74	C
ATOM	2299	C	ALA	A	290	16.635	22.878	33.116	1.00	23.34	C
ATOM	2300	O	ALA	A	290	17.703	23.495	33.335	1.00	22.51	O
ATOM	2301	N	CYS	A	291	16.072	22.027	33.997	1.00	22.67	N
ATOM	2302	CA	CYS	A	291	16.675	21.824	35.293	1.00	22.31	C
ATOM	2303	CB	CYS	A	291	15.827	20.931	36.166	1.00	21.32	C
ATOM	2304	SG	CYS	A	291	14.340	21.678	36.841	1.00	21.82	S
ATOM	2305	C	CYS	A	291	18.074	21.231	35.111	1.00	23.11	C
ATOM	2306	O	CYS	A	291	19.014	21.698	35.732	1.00	24.51	O
ATOM	2307	N	TYR	A	292	18.200	20.205	34.287	1.00	23.44	N
ATOM	2308	CA	TYR	A	292	19.473	19.537	34.033	1.00	23.61	C
ATOM	2309	CB	TYR	A	292	19.280	18.350	33.064	1.00	23.51	C
ATOM	2310	CG	TYR	A	292	20.567	17.604	32.710	1.00	24.39	C
ATOM	2311	CD1	TYR	A	292	20.859	16.335	33.271	1.00	23.02	C
ATOM	2312	CE1	TYR	A	292	22.063	15.660	32.954	1.00	20.92	C
ATOM	2313	CZ	TYR	A	292	22.957	16.272	32.081	1.00	23.22	C
ATOM	2314	OH	TYR	A	292	24.154	15.653	31.706	1.00	27.67	O
ATOM	2315	CE2	TYR	A	292	22.683	17.529	31.527	1.00	23.95	C
ATOM	2316	CD2	TYR	A	292	21.512	18.176	31.836	1.00	24.84	C
ATOM	2317	C	TYR	A	292	20.496	20.472	33.455	1.00	23.95	C
ATOM	2318	O	TYR	A	292	21.675	20.398	33.813	1.00	25.48	O
ATOM	2319	N	VAL	A	293	20.080	21.367	32.572	1.00	23.92	N
ATOM	2320	CA	VAL	A	293	21.036	22.260	31.934	1.00	24.80	C
ATOM	2321	CB	VAL	A	293	20.505	22.840	30.545	1.00	25.94	C
ATOM	2322	CG1	VAL	A	293	21.393	23.985	30.004	1.00	23.60	C
ATOM	2323	CG2	VAL	A	293	20.421	21.733	29.514	1.00	25.40	C
ATOM	2324	C	VAL	A	293	21.440	23.357	32.903	1.00	24.28	C
ATOM	2325	O	VAL	A	293	22.535	23.794	32.892	1.00	24.58	O
ATOM	2326	N	MET	A	294	20.553	23.814	33.750	1.00	25.37	N
ATOM	2327	CA	MET	A	294	20.989	24.761	34.769	1.00	26.38	C
ATOM	2328	CB	MET	A	294	19.827	25.343	35.516	1.00	26.19	C
ATOM	2329	CG	MET	A	294	18.841	26.100	34.670	1.00	26.19	C
ATOM	2330	SD	MET	A	294	17.570	26.782	35.777	1.00	32.59	S
ATOM	2331	CE	MET	A	294	16.323	26.009	35.326	1.00	31.42	C
ATOM	2332	C	MET	A	294	21.987	24.141	35.754	1.00	27.49	C
ATOM	2333	O	MET	A	294	22.983	24.783	36.116	1.00	28.91	O
ATOM	2334	N	LYS	A	295	21.756	22.898	36.182	1.00	28.77	N
ATOM	2335	CA	LYS	A	295	22.733	22.171	37.042	1.00	28.47	C
ATOM	2336	CB	LYS	A	295	22.162	20.821	37.474	1.00	28.58	C
ATOM	2337	CG	LYS	A	295	23.132	20.014	38.299	1.00	28.90	C
ATOM	2338	CD	LYS	A	295	22.548	18.710	38.724	1.00	32.79	C
ATOM	2339	CE	LYS	A	295	23.622	17.834	39.449	1.00	32.66	C
ATOM	2340	NZ	LYS	A	295	23.010	16.618	40.078	1.00	34.26	N
ATOM	2341	C	LYS	A	295	24.088	21.939	36.349	1.00	28.51	C
ATOM	2342	O	LYS	A	295	25.144	22.267	36.868	1.00	28.43	O
ATOM	2343	N	HIS	A	296	24.052	21.358	35.162	1.00	29.10	N
ATOM	2344	CA	HIS	A	296	25.288	20.916	34.529	1.00	29.17	C
ATOM	2345	CB	HIS	A	296	25.026	19.614	33.719	1.00	29.20	C
ATOM	2346	CG	HIS	A	296	24.790	18.437	34.621	1.00	29.76	C
ATOM	2347	ND1	HIS	A	296	25.825	17.767	35.243	1.00	29.56	N
ATOM	2348	CE1	HIS	A	296	25.324	16.833	36.043	1.00	32.53	C
ATOM	2349	NE2	HIS	A	296	24.001	16.898	35.995	1.00	30.90	N
ATOM	2350	CD2	HIS	A	296	23.643	17.913	35.132	1.00	31.50	C
ATOM	2351	C	HIS	A	296	26.113	22.000	33.801	1.00	29.32	C
ATOM	2352	O	HIS	A	296	27.342	21.836	33.621	1.00	29.52	O
ATOM	2353	N	TYR	A	297	25.440	23.088	33.396	1.00	29.04	N
ATOM	2354	CA	TYR	A	297	26.037	24.165	32.607	1.00	28.73	C
ATOM	2355	CB	TYR	A	297	25.427	24.215	31.217	1.00	27.99	C
ATOM	2356	CG	TYR	A	297	25.692	22.959	30.444	1.00	29.27	C
ATOM	2357	CD1	TYR	A	297	26.811	22.863	29.587	1.00	29.35	C
ATOM	2358	CE1	TYR	A	297	27.060	21.669	28.864	1.00	31.53	C
ATOM	2359	CZ	TYR	A	297	26.185	20.580	29.023	1.00	33.60	C
ATOM	2360	OH	TYR	A	297	26.409	19.399	28.331	1.00	35.63	O
ATOM	2361	CE2	TYR	A	297	25.079	20.676	29.886	1.00	28.76	C
ATOM	2362	CD2	TYR	A	297	24.863	21.841	30.595	1.00	27.15	C
ATOM	2363	C	TYR	A	297	25.871	25.527	33.261	1.00	29.51	C
ATOM	2364	O	TYR	A	297	26.384	26.534	32.738	1.00	30.54	O
ATOM	2365	N	ARG	A	298	25.150	25.591	34.381	1.00	29.30	N
ATOM	2366	CA	ARG	A	298	25.054	26.858	35.069	1.00	30.65	C
ATOM	2367	CB	ARG	A	298	26.487	27.343	35.428	1.00	31.37	C
ATOM	2368	CG	ARG	A	298	26.663	27.825	36.855	1.00	37.22	C
ATOM	2369	CD	ARG	A	298	27.959	27.352	37.543	1.00	44.77	C
ATOM	2370	NE	ARG	A	298	27.757	27.088	38.980	1.00	50.22	N
ATOM	2371	CZ	ARG	A	298	27.801	28.010	39.966	1.00	50.84	C
ATOM	2372	NH1	ARG	A	298	28.040	29.293	39.702	1.00	51.31	N
ATOM	2373	NH2	ARG	A	298	27.601	27.640	41.237	1.00	51.31	N
ATOM	2374	C	ARG	A	298	24.333	27.972	34.258	1.00	29.40	C
ATOM	2375	O	ARG	A	298	24.667	29.138	34.414	1.00	30.05	O
ATOM	2376	N	PHE	A	299	23.390	27.637	33.384	1.00	27.64	N
ATOM	2377	CA	PHE	A	299	22.555	28.662	32.755	1.00	26.17	C
ATOM	2378	CB	PHE	A	299	21.531	28.030	31.806	1.00	25.34	C
ATOM	2379	CG	PHE	A	299	22.071	27.687	30.435	1.00	25.93	C
ATOM	2380	CD1	PHE	A	299	23.197	26.887	30.283	1.00	25.32	C
ATOM	2381	CE1	PHE	A	299	23.662	26.569	29.046	1.00	26.13	C
ATOM	2382	CZ	PHE	A	299	22.999	27.040	27.892	1.00	28.92	C
ATOM	2383	CE2	PHE	A	299	21.876	27.831	28.013	1.00	24.49	C
ATOM	2384	CD2	PHE	A	299	21.414	28.143	29.286	1.00	27.94	C
ATOM	2385	C	PHE	A	299	21.794	29.334	33.891	1.00	25.36	C
ATOM	2386	O	PHE	A	299	21.601	28.696	34.935	1.00	25.87	O
ATOM	2387	N	THR	A	300	21.388	30.588	33.708	1.00	23.89	N
ATOM	2388	CA	THR	A	300	20.384	31.179	34.557	1.00	24.99	C
ATOM	2389	CB	THR	A	300	20.447	32.719	34.558	1.00	25.07	C
ATOM	2390	OG1	THR	A	300	20.228	33.212	33.225	1.00	27.44	O
ATOM	2391	CG2	THR	A	300	21.893	33.273	34.970	1.00	24.30	C
ATOM	2392	C	THR	A	300	18.996	30.706	34.061	1.00	25.91	C
ATOM	2393	O	THR	A	300	18.877	30.102	33.000	1.00	25.20	O
ATOM	2394	N	HIS	A	301	17.954	30.974	34.830	1.00	25.99	N
ATOM	2395	CA	HIS	A	301	16.639	30.650	34.369	1.00	27.68	C
ATOM	2396	CB	HIS	A	301	15.606	30.967	35.440	1.00	26.16	C
ATOM	2397	CG	HIS	A	301	15.612	32.396	35.876	1.00	29.73	C
ATOM	2398	ND1	HIS	A	301	14.654	33.309	35.469	1.00	31.73	N
ATOM	2399	CE1	HIS	A	301	14.921	34.491	36.007	1.00	28.49	C
ATOM	2400	NE2	HIS	A	301	16.020	34.378	36.738	1.00	30.38	N
ATOM	2401	CD2	HIS	A	301	16.469	33.082	36.679	1.00	29.77	C
ATOM	2402	C	HIS	A	301	16.358	31.413	33.030	1.00	28.75	C
ATOM	2403	O	HIS	A	301	15.688	30.888	32.124	1.00	28.59	O
ATOM	2404	N	ALA	A	302	16.883	32.635	32.907	1.00	29.01	N
ATOM	2405	CA	ALA	A	302	16.526	33.478	31.748	1.00	28.38	C
ATOM	2406	CB	ALA	A	302	16.968	34.964	31.962	1.00	28.05	C
ATOM	2407	C	ALA	A	302	17.132	32.906	30.500	1.00	26.94	C
ATOM	2408	O	ALA	A	302	16.461	32.743	29.495	1.00	26.12	O
ATOM	2409	N	GLU	A	303	18.408	32.570	30.599	1.00	26.60	N
ATOM	2410	CA	GLU	A	303	19.162	31.992	29.477	1.00	26.59	C
ATOM	2411	CB	GLU	A	303	20.615	31.783	29.898	1.00	27.08	C
ATOM	2412	CG	GLU	A	303	21.403	33.071	30.072	1.00	30.49	C
ATOM	2413	CD	GLU	A	303	22.668	32.911	30.906	1.00	31.79	C
ATOM	2414	OE1	GLU	A	303	22.993	31.789	31.386	1.00	35.13	O
ATOM	2415	OE2	GLU	A	303	23.332	33.941	31.097	1.00	34.11	O
ATOM	2416	C	GLU	A	303	18.648	30.643	28.991	1.00	25.89	C
ATOM	2417	O	GLU	A	303	18.729	30.343	27.793	1.00	25.38	O
ATOM	2418	N	ILE	A	304	18.199	29.812	29.941	1.00	24.31	N
ATOM	2419	CA	ILE	A	304	17.749	28.488	29.632	1.00	23.08	C
ATOM	2420	CB	ILE	A	304	17.887	27.479	30.876	1.00	22.75	C
ATOM	2421	CG1	ILE	A	304	17.767	26.064	30.358	1.00	22.51	C
ATOM	2422	CD1	ILE	A	304	18.648	25.847	29.070	1.00	22.88	C
ATOM	2423	CG2	ILE	A	304	16.836	27.724	31.975	1.00	23.09	C
ATOM	2424	C	ILE	A	304	16.324	28.535	29.033	1.00	22.61	C
ATOM	2425	O	ILE	A	304	16.028	27.853	28.050	1.00	21.59	O
ATOM	2426	N	ILE	A	305	15.457	29.358	29.619	1.00	22.28	N
ATOM	2427	CA	ILE	A	305	14.134	29.563	29.061	1.00	21.28	C
ATOM	2428	CB	ILE	A	305	13.279	30.412	29.943	1.00	20.28	C
ATOM	2429	CG1	ILE	A	305	12.883	29.628	31.221	1.00	19.47	C
ATOM	2430	CD1	ILE	A	305	11.972	30.461	32.183	1.00	17.33	C
ATOM	2431	CG2	ILE	A	305	12.032	30.866	29.170	1.00	21.08	C
ATOM	2432	C	ILE	A	305	14.215	30.091	27.608	1.00	21.56	C
ATOM	2433	O	ILE	A	305	13.497	29.586	26.748	1.00	21.61	O
ATOM	2434	N	ALA	A	306	15.118	31.041	27.343	1.00	21.22	N
ATOM	2435	CA	ALA	A	306	15.409	31.488	25.976	1.00	21.38	C
ATOM	2436	CB	ALA	A	306	16.422	32.706	25.927	1.00	20.97	C
ATOM	2437	C	ALA	A	306	15.923	30.342	25.130	1.00	21.00	C
ATOM	2438	O	ALA	A	306	15.340	30.052	24.084	1.00	21.91	O
ATOM	2439	N	TRP	A	307	16.989	29.675	25.567	1.00	20.08	N
ATOM	2440	CA	TRP	A	307	17.560	28.594	24.761	1.00	19.20	C
ATOM	2441	CB	TRP	A	307	18.732	27.890	25.434	1.00	19.01	C
ATOM	2442	CG	TRP	A	307	19.309	26.900	24.464	1.00	21.98	C
ATOM	2443	CD1	TRP	A	307	19.382	25.536	24.603	1.00	18.19	C
ATOM	2444	NE1	TRP	A	307	19.927	24.985	23.453	1.00	20.57	N
ATOM	2445	CE2	TRP	A	307	20.158	25.974	22.525	1.00	19.53	C
ATOM	2446	CD2	TRP	A	307	19.808	27.197	23.125	1.00	20.75	C
ATOM	2447	CE3	TRP	A	307	19.995	28.383	22.383	1.00	22.62	C
ATOM	2448	CZ3	TRP	A	307	20.533	28.318	21.090	1.00	18.34	C
ATOM	2449	CH2	TRP	A	307	20.878	27.093	20.536	1.00	19.76	C
ATOM	2450	CZ2	TRP	A	307	20.692	25.905	21.227	1.00	21.01	C
ATOM	2451	C	TRP	A	307	16.515	27.551	24.304	1.00	19.74	C
ATOM	2452	O	TRP	A	307	16.429	27.250	23.116	1.00	20.13	O
ATOM	2453	N	ILE	A	308	15.743	27.006	25.248	1.00	19.15	N
ATOM	2454	CA	ILE	A	308	14.748	26.002	24.953	1.00	19.52	C
ATOM	2455	CB	ILE	A	308	14.238	25.283	26.268	1.00	18.70	C
ATOM	2456	CG1	ILE	A	308	15.462	24.700	26.996	1.00	19.28	C
ATOM	2457	CD1	ILE	A	308	15.199	23.972	28.266	1.00	20.94	C
ATOM	2458	CG2	ILE	A	308	13.193	24.135	25.937	1.00	17.18	C
ATOM	2459	C	ILE	A	308	13.627	26.577	24.098	1.00	20.56	C
ATOM	2460	O	ILE	A	308	13.157	25.936	23.150	1.00	21.92	O
ATOM	2461	N	ARG	A	309	13.168	27.770	24.412	1.00	20.98	N
ATOM	2462	CA	ARG	A	309	12.130	28.341	23.555	1.00	21.38	C
ATOM	2463	CB	ARG	A	309	11.500	29.609	24.154	1.00	21.45	C
ATOM	2464	CG	ARG	A	309	10.789	29.334	25.473	1.00	19.52	C
ATOM	2465	CD	ARG	A	309	9.799	30.383	25.820	1.00	19.37	C
ATOM	2466	NE	ARG	A	309	9.132	30.140	27.105	1.00	22.32	N
ATOM	2467	CZ	ARG	A	309	8.727	31.122	27.924	1.00	23.03	C
ATOM	2468	NH1	ARG	A	309	8.907	32.401	27.554	1.00	17.74	N
ATOM	2469	NH2	ARG	A	309	8.151	30.828	29.092	1.00	20.69	N
ATOM	2470	C	ARG	A	309	12.602	28.573	22.129	1.00	21.36	C
ATOM	2471	O	ARG	A	309	11.838	28.363	21.199	1.00	22.73	O
ATOM	2472	N	ILE	A	310	13.838	29.020	21.950	1.00	21.30	N
ATOM	2473	CA	ILE	A	310	14.405	29.159	20.618	1.00	20.35	C
ATOM	2474	CB	ILE	A	310	15.726	29.893	20.661	1.00	20.06	C
ATOM	2475	CG1	ILE	A	310	15.481	31.335	21.122	1.00	17.43	C
ATOM	2476	CD1	ILE	A	310	16.796	32.058	21.545	1.00	18.77	C
ATOM	2477	CG2	ILE	A	310	16.410	29.874	19.275	1.00	17.77	C
ATOM	2478	C	ILE	A	310	14.557	27.849	19.881	1.00	21.38	C
ATOM	2479	O	ILE	A	310	14.250	27.807	18.668	1.00	22.62	O
ATOM	2480	N	CYS	A	311	15.037	26.799	20.552	1.00	21.48	N
ATOM	2481	CA	CYS	A	311	15.012	25.451	19.959	1.00	22.97	C
ATOM	2482	CB	CYS	A	311	15.682	24.423	20.866	1.00	23.11	C
ATOM	2483	SG	CYS	A	311	17.433	24.682	20.927	1.00	21.87	S
ATOM	2484	C	CYS	A	311	13.616	24.943	19.634	1.00	23.86	C
ATOM	2485	O	CYS	A	311	13.374	24.412	18.557	1.00	24.95	O
ATOM	2486	N	ARG	A	312	12.697	25.129	20.567	1.00	23.24	N
ATOM	2487	CA	ARG	A	312	11.396	24.531	20.476	1.00	22.66	C
ATOM	2488	CB	ARG	A	312	11.464	23.257	21.297	1.00	22.04	C
ATOM	2489	CG	ARG	A	312	10.202	22.528	21.564	1.00	20.09	C
ATOM	2490	CD	ARG	A	312	10.461	21.029	21.770	1.00	16.73	C
ATOM	2491	NE	ARG	A	312	9.193	20.349	21.930	1.00	17.38	N
ATOM	2492	CZ	ARG	A	312	8.453	19.845	20.921	1.00	19.68	C
ATOM	2493	NH1	ARG	A	312	8.892	19.915	19.655	1.00	18.80	N
ATOM	2494	NH2	ARG	A	312	7.261	19.277	21.183	1.00	14.23	N
ATOM	2495	C	ARG	A	312	10.400	25.543	21.074	1.00	23.34	C
ATOM	2496	O	ARG	A	312	10.159	25.540	22.306	1.00	24.46	O
ATOM	2497	N	PRO	A	313	9.864	26.442	20.237	1.00	21.93	N
ATOM	2498	CA	PRO	A	313	8.873	27.408	20.697	1.00	21.72	C
ATOM	2499	CB	PRO	A	313	8.302	27.958	19.376	1.00	19.84	C
ATOM	2500	CG	PRO	A	313	9.494	27.995	18.540	1.00	19.85	C
ATOM	2501	CD	PRO	A	313	10.160	26.647	18.812	1.00	21.54	C
ATOM	2502	C	PRO	A	313	7.768	26.817	21.580	1.00	21.78	C
ATOM	2503	O	PRO	A	313	7.321	25.702	21.274	1.00	22.83	O
ATOM	2504	N	GLY	A	314	7.348	27.576	22.605	1.00	20.96	N
ATOM	2505	CA	GLY	A	314	6.244	27.265	23.496	1.00	21.48	C
ATOM	2506	C	GLY	A	314	6.671	26.578	24.793	1.00	22.87	C
ATOM	2507	O	GLY	A	314	5.889	26.493	25.722	1.00	23.29	O
ATOM	2508	N	SER	A	315	7.916	26.112	24.856	1.00	23.03	N
ATOM	2509	CA	SER	A	315	8.460	25.432	26.026	1.00	23.98	C
ATOM	2510	CB	SER	A	315	9.912	25.035	25.759	1.00	22.83	C
ATOM	2511	OG	SER	A	315	9.963	24.271	24.581	1.00	25.14	O
ATOM	2512	C	SER	A	315	8.392	26.191	27.367	1.00	24.02	C
ATOM	2513	O	SER	A	315	8.808	27.357	27.425	1.00	24.80	O
ATOM	2514	N	ILE	A	316	7.958	25.501	28.442	1.00	22.84	N
ATOM	2515	CA	ILE	A	316	8.123	26.007	29.815	1.00	23.04	C
ATOM	2516	CB	ILE	A	316	9.542	26.691	30.066	1.00	22.94	C
ATOM	2517	CG1	ILE	A	316	10.724	25.804	29.631	1.00	22.36	C
ATOM	2518	CD1	ILE	A	316	12.063	26.518	29.851	1.00	20.74	C
ATOM	2519	CG2	ILE	A	316	9.733	27.162	31.550	1.00	22.71	C
ATOM	2520	C	ILE	A	316	7.045	27.033	30.010	1.00	23.25	C
ATOM	2521	O	ILE	A	316	7.217	28.184	29.573	1.00	24.13	O
ATOM	2522	N	ILE	A	317	5.937	26.622	30.617	1.00	22.59	N
ATOM	2523	CA	ILE	A	317	4.710	27.426	30.647	1.00	23.70	C
ATOM	2524	CB	ILE	A	317	3.503	26.642	30.007	1.00	23.03	C
ATOM	2525	CG1	ILE	A	317	3.719	26.395	28.476	1.00	24.69	C
ATOM	2526	CD1	ILE	A	317	3.088	25.017	27.913	1.00	21.11	C
ATOM	2527	CG2	ILE	A	317	2.218	27.383	30.227	1.00	20.39	C
ATOM	2528	C	ILE	A	317	4.332	27.765	32.087	1.00	24.71	C
ATOM	2529	O	ILE	A	317	4.508	26.923	32.952	1.00	24.80	O
ATOM	2530	N	GLY	A	318	3.782	28.973	32.309	1.00	25.80	N
ATOM	2531	CA	GLY	A	318	3.171	29.418	33.555	1.00	25.70	C
ATOM	2532	C	GLY	A	318	4.075	29.350	34.784	1.00	27.49	C
ATOM	2533	O	GLY	A	318	5.173	29.974	34.804	1.00	27.87	O
ATOM	2534	N	PRO	A	319	3.668	28.560	35.795	1.00	27.14	N
ATOM	2535	CA	PRO	A	319	4.427	28.503	37.067	1.00	26.56	C
ATOM	2536	CB	PRO	A	319	3.535	27.667	38.017	1.00	26.49	C
ATOM	2537	CG	PRO	A	319	2.247	27.241	37.207	1.00	27.13	C
ATOM	2538	CD	PRO	A	319	2.481	27.686	35.781	1.00	26.95	C
ATOM	2539	C	PRO	A	319	5.798	27.881	36.884	1.00	26.11	C
ATOM	2540	O	PRO	A	319	6.738	28.138	37.669	1.00	25.62	O
ATOM	2541	N	GLN	A	320	5.926	27.064	35.835	1.00	26.11	N
ATOM	2542	CA	GLN	A	320	7.221	26.437	35.491	1.00	24.92	C
ATOM	2543	CB	GLN	A	320	7.049	25.429	34.370	1.00	24.70	C
ATOM	2544	CG	GLN	A	320	5.881	24.461	34.546	1.00	20.70	C
ATOM	2545	CD	GLN	A	320	5.639	23.616	33.289	1.00	24.98	C
ATOM	2546	OE1	GLN	A	320	5.979	24.022	32.142	1.00	28.44	O
ATOM	2547	NE2	GLN	A	320	5.086	22.444	33.484	1.00	24.69	N
ATOM	2548	C	GLN	A	320	8.297	27.449	35.130	1.00	25.20	C
ATOM	2549	O	GLN	A	320	9.476	27.234	35.385	1.00	24.41	O
ATOM	2550	N	GLN	A	321	7.887	28.591	34.586	1.00	26.34	N
ATOM	2551	CA	GLN	A	321	8.851	29.697	34.413	1.00	26.50	C
ATOM	2552	CB	GLN	A	321	8.214	30.894	33.716	1.00	26.11	C
ATOM	2553	CG	GLN	A	321	7.553	30.574	32.409	1.00	25.65	C
ATOM	2554	CD	GLN	A	321	6.754	31.729	31.873	1.00	23.31	C
ATOM	2555	OE1	GLN	A	321	7.122	32.311	30.847	1.00	23.14	O
ATOM	2556	NE2	GLN	A	321	5.651	32.059	32.544	1.00	17.67	N
ATOM	2557	C	GLN	A	321	9.473	30.152	35.747	1.00	27.41	C
ATOM	2558	O	GLN	A	321	10.704	30.151	35.870	1.00	27.71	O
ATOM	2559	N	HIS	A	322	8.620	30.600	36.688	1.00	27.47	N
ATOM	2560	CA	HIS	A	322	9.030	31.138	37.975	1.00	28.75	C
ATOM	2561	CB	HIS	A	322	7.840	31.718	38.728	1.00	27.95	C
ATOM	2562	CG	HIS	A	322	7.106	32.763	37.952	1.00	29.42	C
ATOM	2563	ND1	HIS	A	322	7.627	34.025	37.713	1.00	25.63	N
ATOM	2564	CE1	HIS	A	322	6.765	34.711	36.983	1.00	28.78	C
ATOM	2565	NE2	HIS	A	322	5.724	33.936	36.713	1.00	30.15	N
ATOM	2566	CD2	HIS	A	322	5.906	32.718	37.318	1.00	29.51	C
ATOM	2567	C	HIS	A	322	9.723	30.078	38.831	1.00	29.92	C
ATOM	2568	O	HIS	A	322	10.660	30.390	39.592	1.00	30.91	O
ATOM	2569	N	PHE	A	323	9.273	28.832	38.677	1.00	30.41	N
ATOM	2570	CA	PHE	A	323	9.885	27.686	39.314	1.00	30.38	C
ATOM	2571	CB	PHE	A	323	9.115	26.400	38.944	1.00	30.15	C
ATOM	2572	CG	PHE	A	323	9.885	25.125	39.211	1.00	30.39	C
ATOM	2573	CD1	PHE	A	323	9.937	24.583	40.494	1.00	30.76	C
ATOM	2574	CE1	PHE	A	323	10.644	23.417	40.745	1.00	31.31	C
ATOM	2575	CZ	PHE	A	323	11.349	22.776	39.686	1.00	32.02	C
ATOM	2576	CE2	PHE	A	323	11.316	23.340	38.397	1.00	30.55	C
ATOM	2577	CD2	PHE	A	323	10.588	24.490	38.175	1.00	29.96	C
ATOM	2578	C	PHE	A	323	11.392	27.618	38.992	1.00	31.03	C
ATOM	2579	O	PHE	A	323	12.227	27.419	39.916	1.00	31.65	O
ATOM	2580	N	LEU	A	324	11.775	27.803	37.724	1.00	30.84	N
ATOM	2581	CA	LEU	A	324	13.223	27.734	37.402	1.00	31.48	C
ATOM	2582	CB	LEU	A	324	13.486	27.602	35.902	1.00	31.19	C
ATOM	2583	CG	LEU	A	324	12.899	26.345	35.186	1.00	30.00	C
ATOM	2584	CD1	LEU	A	324	12.917	26.559	33.697	1.00	22.58	C
ATOM	2585	CD2	LEU	A	324	13.592	25.038	35.608	1.00	25.53	C
ATOM	2586	C	LEU	A	324	14.054	28.876	38.001	1.00	32.49	C
ATOM	2587	O	LEU	A	324	15.191	28.667	38.378	1.00	31.83	O
ATOM	2588	N	GLU	A	325	13.487	30.081	38.083	1.00	34.21	N
ATOM	2589	CA	GLU	A	325	14.159	31.204	38.734	1.00	35.98	C
ATOM	2590	CB	GLU	A	325	13.308	32.496	38.694	1.00	36.92	C
ATOM	2591	CG	GLU	A	325	13.797	33.638	39.609	1.00	40.78	C
ATOM	2592	CD	GLU	A	325	13.345	35.028	39.156	1.00	47.61	C
ATOM	2593	OE1	GLU	A	325	12.320	35.124	38.423	1.00	49.04	O
ATOM	2594	OE2	GLU	A	325	14.029	36.034	39.514	1.00	49.33	O
ATOM	2595	C	GLU	A	325	14.419	30.804	40.168	1.00	36.55	C
ATOM	2596	O	GLU	A	325	15.499	31.105	40.730	1.00	36.55	O
ATOM	2597	N	GLU	A	326	13.419	30.137	40.754	1.00	37.02	N
ATOM	2598	CA	GLU	A	326	13.468	29.753	42.163	1.00	38.44	C
ATOM	2599	CB	GLU	A	326	12.097	29.341	42.629	1.00	38.24	C
ATOM	2600	CG	GLU	A	326	11.974	29.364	44.128	1.00	46.60	C
ATOM	2601	CD	GLU	A	326	11.204	28.154	44.671	1.00	56.34	C
ATOM	2602	OE1	GLU	A	326	9.997	28.304	45.056	1.00	55.91	O
ATOM	2603	OE2	GLU	A	326	11.821	27.051	44.711	1.00	61.04	O
ATOM	2604	C	GLU	A	326	14.545	28.679	42.499	1.00	37.49	C
ATOM	2605	O	GLU	A	326	15.241	28.827	43.487	1.00	38.16	O
ATOM	2606	N	LYS	A	327	14.691	27.646	41.660	1.00	36.35	N
ATOM	2607	CA	LYS	A	327	15.657	26.555	41.849	1.00	35.48	C
ATOM	2608	CB	LYS	A	327	15.189	25.297	41.085	1.00	36.09	C
ATOM	2609	CG	LYS	A	327	13.916	24.631	41.583	1.00	39.72	C
ATOM	2610	CD	LYS	A	327	14.094	23.872	42.889	1.00	45.35	C
ATOM	2611	CE	LYS	A	327	13.058	24.351	43.912	1.00	47.94	C
ATOM	2612	NZ	LYS	A	327	13.345	23.880	45.326	1.00	51.88	N
ATOM	2613	C	LYS	A	327	17.042	26.869	41.312	1.00	34.69	C
ATOM	2614	O	LYS	A	327	17.985	26.073	41.459	1.00	34.75	O
ATOM	2615	N	GLN	A	328	17.174	27.983	40.610	1.00	33.74	N
ATOM	2616	CA	GLN	A	328	18.426	28.258	39.989	1.00	33.00	C
ATOM	2617	CB	GLN	A	328	18.452	29.658	39.396	1.00	32.91	C
ATOM	2618	CG	GLN	A	328	19.763	29.951	38.655	1.00	32.48	C
ATOM	2619	CD	GLN	A	328	19.751	31.318	38.096	1.00	33.62	C
ATOM	2620	OE1	GLN	A	328	18.863	31.656	37.303	1.00	32.99	O
ATOM	2621	NE2	GLN	A	328	20.694	32.147	38.537	1.00	30.88	N
ATOM	2622	C	GLN	A	328	19.572	28.044	40.978	1.00	33.13	C
ATOM	2623	O	GLN	A	328	20.415	27.209	40.714	1.00	33.14	O
ATOM	2624	N	ALA	A	329	19.604	28.754	42.118	1.00	33.32	N
ATOM	2625	CA	ALA	A	329	20.810	28.654	42.991	1.00	34.35	C
ATOM	2626	CB	ALA	A	329	20.822	29.738	44.175	1.00	34.37	C
ATOM	2627	C	ALA	A	329	21.003	27.216	43.523	1.00	33.13	C
ATOM	2628	O	ALA	A	329	22.093	26.671	43.556	1.00	31.93	O
ATOM	2629	N	SER	A	330	19.897	26.621	43.895	1.00	32.84	N
ATOM	2630	CA	SER	A	330	19.896	25.270	44.392	1.00	33.83	C
ATOM	2631	CB	SER	A	330	18.500	24.939	44.867	1.00	32.51	C
ATOM	2632	OG	SER	A	330	18.407	23.570	44.830	1.00	32.66	O
ATOM	2633	C	SER	A	330	20.389	24.220	43.368	1.00	34.50	C
ATOM	2634	O	SER	A	330	21.192	23.329	43.720	1.00	35.41	O
ATOM	2635	N	LEU	A	331	19.923	24.314	42.117	1.00	35.37	N
ATOM	2636	CA	LEU	A	331	20.424	23.449	41.023	1.00	35.72	C
ATOM	2637	CB	LEU	A	331	19.667	23.713	39.724	1.00	35.58	C
ATOM	2638	CG	LEU	A	331	18.179	23.354	39.709	1.00	35.06	C
ATOM	2639	CD1	LEU	A	331	17.461	24.003	38.579	1.00	36.01	C
ATOM	2640	CD2	LEU	A	331	18.063	21.844	39.614	1.00	38.47	C
ATOM	2641	C	LEU	A	331	21.894	23.676	40.774	1.00	36.94	C
ATOM	2642	O	LEU	A	331	22.619	22.759	40.463	1.00	37.72	O
ATOM	2643	N	TRP	A	332	22.342	24.913	40.909	1.00	38.52	N
ATOM	2644	CA	TRP	A	332	23.739	25.241	40.696	1.00	40.11	C
ATOM	2645	CB	TRP	A	332	23.914	26.766	40.649	1.00	40.56	C
ATOM	2646	CG	TRP	A	332	23.540	27.467	39.347	1.00	39.55	C
ATOM	2647	CD1	TRP	A	332	22.910	26.931	38.257	1.00	39.50	C
ATOM	2648	NE1	TRP	A	332	22.744	27.883	37.277	1.00	40.02	N
ATOM	2649	CE2	TRP	A	332	23.273	29.067	37.717	1.00	40.59	C
ATOM	2650	CD2	TRP	A	332	23.789	28.838	39.026	1.00	41.24	C
ATOM	2651	CE3	TRP	A	332	24.381	29.919	39.722	1.00	39.62	C
ATOM	2652	CZ3	TRP	A	332	24.444	31.170	39.099	1.00	40.71	C
ATOM	2653	CH2	TRP	A	332	23.945	31.357	37.779	1.00	42.82	C
ATOM	2654	CZ2	TRP	A	332	23.351	30.325	37.078	1.00	40.80	C
ATOM	2655	C	TRP	A	332	24.654	24.648	41.772	1.00	41.53	C
ATOM	2656	O	TRP	A	332	25.746	24.157	41.462	1.00	41.67	O
ATOM	2657	N	VAL	A	333	24.207	24.732	43.029	1.00	43.46	N
ATOM	2658	CA	VAL	A	333	24.898	24.158	44.186	1.00	45.50	C
ATOM	2659	CB	VAL	A	333	24.184	24.529	45.528	1.00	45.70	C
ATOM	2660	CG1	VAL	A	333	24.440	23.477	46.653	1.00	47.02	C
ATOM	2661	CG2	VAL	A	333	24.574	25.949	45.998	1.00	43.56	C
ATOM	2662	C	VAL	A	333	25.072	22.638	44.019	1.00	46.85	C
ATOM	2663	O	VAL	A	333	26.116	22.084	44.365	1.00	46.33	O
ATOM	2664	N	GLN	A	334	24.044	21.999	43.469	1.00	48.80	N
ATOM	2665	CA	GLN	A	334	24.074	20.593	43.099	1.00	50.76	C
ATOM	2666	CB	GLN	A	334	22.696	20.191	42.597	1.00	50.81	C
ATOM	2667	CG	GLN	A	334	21.684	19.706	43.625	1.00	52.47	C
ATOM	2668	CD	GLN	A	334	20.486	19.013	42.944	1.00	53.08	C
ATOM	2669	OE1	GLN	A	334	19.415	19.628	42.811	1.00	55.63	O
ATOM	2670	NE2	GLN	A	334	20.671	17.752	42.497	1.00	49.24	N
ATOM	2671	C	GLN	A	334	25.094	20.312	41.979	1.00	52.36	C
ATOM	2672	O	GLN	A	334	25.576	19.187	41.849	1.00	52.62	O
ATOM	2673	N	GLY	A	335	25.392	21.323	41.156	1.00	53.93	N
ATOM	2674	CA	GLY	A	335	26.309	21.169	40.040	1.00	56.09	C
ATOM	2675	C	GLY	A	335	27.755	21.416	40.425	1.00	57.55	C
ATOM	2676	O	GLY	A	335	28.681	21.254	39.627	1.00	57.14	O
ATOM	2677	N	ASP	A	336	27.937	21.801	41.677	1.00	59.72	N
ATOM	2678	CA	ASP	A	336	29.249	22.126	42.212	1.00	61.84	C
ATOM	2679	CB	ASP	A	336	29.133	23.191	43.314	1.00	62.12	C
ATOM	2680	CG	ASP	A	336	29.187	24.614	42.751	1.00	62.73	C
ATOM	2681	OD1	ASP	A	336	30.213	24.963	42.104	1.00	62.91	O
ATOM	2682	OD2	ASP	A	336	28.245	25.436	42.888	1.00	62.58	O
ATOM	2683	C	ASP	A	336	30.009	20.913	42.706	1.00	62.97	C
ATOM	2684	O	ASP	A	336	31.228	20.888	42.575	1.00	63.34	O
ATOM	2685	N	ILE	A	337	29.301	19.916	43.246	1.00	64.60	N
ATOM	2686	CA	ILE	A	337	29.943	18.668	43.691	1.00	66.91	C
ATOM	2687	CB	ILE	A	337	29.118	17.901	44.793	1.00	67.45	C
ATOM	2688	CG1	ILE	A	337	27.602	17.870	44.484	1.00	68.56	C
ATOM	2689	CD1	ILE	A	337	26.970	16.442	44.578	1.00	68.87	C
ATOM	2690	CG2	ILE	A	337	29.459	18.429	46.217	1.00	66.68	C
ATOM	2691	C	ILE	A	337	30.470	17.690	42.609	1.00	68.01	C
ATOM	2692	O	ILE	A	337	31.471	17.028	42.877	1.00	68.87	O
ATOM	2693	N	PHE	A	338	29.824	17.603	41.428	1.00	69.15	N
ATOM	2694	CA	PHE	A	338	30.276	16.806	40.235	1.00	70.03	C
ATOM	2695	CB	PHE	A	338	31.318	15.702	40.640	1.00	70.31	C
ATOM	2696	CG	PHE	A	338	31.676	14.627	39.552	1.00	73.39	C
ATOM	2697	CD1	PHE	A	338	32.996	14.124	39.482	1.00	74.60	C
ATOM	2698	CE1	PHE	A	338	33.367	13.127	38.529	1.00	73.26	C
ATOM	2699	CZ	PHE	A	338	32.415	12.581	37.660	1.00	74.78	C
ATOM	2700	CE2	PHE	A	338	31.085	13.038	37.716	1.00	76.35	C
ATOM	2701	CD2	PHE	A	338	30.717	14.058	38.671	1.00	75.91	C
ATOM	2702	C	PHE	A	338	29.074	16.256	39.394	1.00	70.28	C
ATOM	2703	O	PHE	A	338	28.021	16.903	39.185	1.00	70.08	O
ATOM	2704	OH2	HOH	X	1	30.392	44.817	5.609	1.00	15.49	O
ATOM	2705	OH2	HOH	X	2	12.479	42.639	25.190	1.00	21.91	O
ATOM	2706	OH2	HOH	X	3	1.933	40.117	24.460	1.00	10.78	O
ATOM	2707	OH2	HOH	X	4	8.721	45.606	21.026	1.00	14.59	O
ATOM	2708	OH2	HOH	X	5	9.444	10.576	11.676	1.00	23.82	O
ATOM	2709	OH2	HOH	X	6	5.498	29.114	26.844	1.00	19.62	O
ATOM	2710	OH2	HOH	X	7	10.354	30.633	21.043	1.00	14.93	O
ATOM	2711	OH2	HOH	X	8	12.208	43.248	10.092	1.00	24.81	O
ATOM	2712	OH2	HOH	X	9	7.539	29.107	14.472	1.00	19.31	O
ATOM	2713	OH2	HOH	X	10	9.981	31.125	15.007	1.00	18.08	O
ATOM	2714	OH2	HOH	X	11	2.120	9.839	24.658	1.00	24.10	O
ATOM	2715	OH2	HOH	X	12	0.036	32.702	25.407	1.00	30.47	O
ATOM	2716	OH2	HOH	X	13	3.274	20.669	26.828	1.00	17.68	O
ATOM	2717	OH2	HOH	X	14	27.479	44.460	0.903	1.00	34.85	O
ATOM	2718	OH2	HOH	X	15	10.125	26.950	11.563	1.00	14.24	O
ATOM	2719	OH2	HOH	X	16	9.810	40.477	12.846	1.00	20.12	O
ATOM	2720	OH2	HOH	X	17	6.687	36.789	13.629	1.00	17.24	O
ATOM	2721	OH2	HOH	X	18	3.551	33.912	34.465	1.00	24.01	O
ATOM	2722	OH2	HOH	X	19	16.083	19.978	15.859	1.00	19.07	O
ATOM	2723	OH2	HOH	X	20	19.197	48.185	−2.763	1.00	12.76	O
ATOM	2724	OH2	HOH	X	21	3.779	19.649	29.755	1.00	26.55	O
ATOM	2725	OH2	HOH	X	22	17.214	12.561	8.994	1.00	29.50	O
ATOM	2726	OH2	HOH	X	23	6.087	35.107	22.949	1.00	27.66	O
ATOM	2727	OH2	HOH	X	24	1.655	18.313	27.423	1.00	16.61	O
ATOM	2728	OH2	HOH	X	25	12.820	20.738	5.433	1.00	30.27	O
ATOM	2729	OH2	HOH	X	26	13.775	19.971	14.809	1.00	18.94	O
ATOM	2730	OH2	HOH	X	27	8.605	32.143	8.121	1.00	19.05	O
ATOM	2731	OH2	HOH	X	28	28.140	30.477	11.339	1.00	34.64	O
ATOM	2732	OH2	HOH	X	29	7.818	34.567	29.048	1.00	17.78	O
ATOM	2733	OH2	HOH	X	30	12.767	7.082	12.709	1.00	29.89	O
ATOM	2734	OH2	HOH	X	31	8.464	33.339	24.840	1.00	24.60	O
ATOM	2735	OH2	HOH	X	32	13.794	0.976	31.045	1.00	27.78	O
ATOM	2736	OH2	HOH	X	33	21.983	15.249	18.468	1.00	28.65	O
ATOM	2737	OH2	HOH	X	34	8.698	23.856	9.582	1.00	27.29	O
ATOM	2738	OH2	HOH	X	35	−3.848	3.911	24.474	1.00	33.30	O
ATOM	2739	OH2	HOH	X	36	7.401	24.078	19.387	1.00	13.57	O
ATOM	2740	OH2	HOH	X	37	23.748	23.485	15.061	1.00	29.29	O
ATOM	2741	OH2	HOH	X	38	16.583	8.136	10.462	1.00	32.15	O
ATOM	2742	OH2	HOH	X	39	19.593	54.974	7.869	1.00	35.19	O
ATOM	2743	OH2	HOH	X	40	10.733	21.392	25.560	1.00	20.33	O
ATOM	2744	OH2	HOH	X	41	9.181	23.299	17.795	1.00	14.83	O
ATOM	2745	OH2	HOH	X	42	20.133	35.689	33.599	1.00	31.37	O
ATOM	2746	OH2	HOH	X	43	−0.879	14.382	31.472	1.00	21.57	O
ATOM	2747	OH2	HOH	X	44	6.419	28.108	16.998	1.00	30.97	O
ATOM	2748	OH2	HOH	X	45	−5.292	36.071	28.744	1.00	29.29	O
ATOM	2749	OH2	HOH	X	46	21.987	39.391	−1.052	1.00	29.47	O
ATOM	2750	OH2	HOH	X	47	26.540	40.335	28.276	1.00	23.84	O
ATOM	2751	OH2	HOH	X	48	11.174	41.109	23.897	1.00	34.47	O
ATOM	2752	OH2	HOH	X	49	31.235	46.934	2.188	1.00	41.24	O
ATOM	2753	OH2	HOH	X	50	2.901	26.692	16.973	1.00	33.02	O
ATOM	2754	OH2	HOH	X	51	8.200	30.499	22.250	1.00	21.43	O
ATOM	2755	OH2	HOH	X	52	18.229	15.673	12.575	1.00	25.52	O
ATOM	2756	OH2	HOH	X	53	27.195	37.604	−1.067	1.00	40.56	O
ATOM	2757	OH2	HOH	X	54	21.789	10.462	41.779	1.00	26.17	O
ATOM	2758	OH2	HOH	X	55	14.945	51.976	15.909	1.00	32.78	O
ATOM	2759	OH2	HOH	X	56	17.339	27.449	44.743	1.00	36.67	O
ATOM	2760	OH2	HOH	X	57	24.378	28.490	43.957	1.00	34.99	O
ATOM	2761	OH2	HOH	X	58	23.795	56.412	3.230	1.00	37.51	O
ATOM	2762	OH2	HOH	X	59	0.979	42.476	17.580	1.00	17.89	O
ATOM	2763	OH2	HOH	X	60	2.548	36.119	16.447	1.00	22.93	O
ATOM	2764	OH2	HOH	X	61	19.332	57.131	1.158	1.00	27.06	O
ATOM	2765	OH2	HOH	X	62	−7.421	33.720	27.180	1.00	23.88	O
ATOM	2766	OH2	HOH	X	63	20.257	37.842	1.282	1.00	32.41	O
ATOM	2767	OH2	HOH	X	64	10.480	24.529	16.113	1.00	16.42	O
ATOM	2768	OH2	HOH	X	65	17.418	3.427	36.865	1.00	25.34	O
ATOM	2769	OH2	HOH	X	66	8.867	37.997	12.648	1.00	18.47	O
ATOM	2770	OH2	HOH	X	67	8.846	56.310	11.099	1.00	31.59	O
ATOM	2771	OH2	HOH	X	68	31.214	43.759	0.366	1.00	35.64	O
ATOM	2772	OH2	HOH	X	69	−2.109	35.228	19.095	1.00	27.26	O
ATOM	2773	OH2	HOH	X	70	21.858	13.896	40.580	1.00	29.98	O
ATOM	2774	OH2	HOH	X	71	3.522	21.534	12.712	1.00	28.15	O
ATOM	2775	OH2	HOH	X	72	1.842	32.743	12.431	1.00	26.77	O
ATOM	2776	OH2	HOH	X	73	31.373	37.111	16.604	1.00	39.52	O
ATOM	2777	OH2	HOH	X	74	5.765	16.863	41.129	1.00	42.22	O
ATOM	2778	OH2	HOH	X	75	24.850	25.175	8.189	1.00	25.14	O
ATOM	2779	OH2	HOH	X	76	30.581	35.933	8.351	1.00	39.39	O
ATOM	2780	OH2	HOH	X	77	30.453	32.913	14.167	1.00	37.72	O
ATOM	2781	OH2	HOH	X	78	29.920	39.998	9.172	1.00	38.13	O
ATOM	2782	OH2	HOH	X	79	33.114	42.201	22.842	1.00	44.59	O
ATOM	2783	OH2	HOH	X	80	15.986	31.586	3.922	1.00	21.34	O
ATOM	2784	OH2	HOH	X	81	30.333	−2.230	39.216	1.00	39.91	O
ATOM	2785	OH2	HOH	X	82	26.976	29.488	15.512	1.00	28.94	O
ATOM	2786	OH2	HOH	X	83	27.272	48.972	−3.939	1.00	36.49	O
ATOM	2787	OH2	HOH	X	84	26.454	41.583	−6.009	1.00	33.87	O
ATOM	2788	OH2	HOH	X	85	2.954	38.502	16.381	1.00	25.62	O
ATOM	2789	OH2	HOH	X	86	33.792	39.369	13.458	1.00	40.54	O
ATOM	2790	OH2	HOH	X	87	17.262	30.350	43.263	1.00	34.47	O
ATOM	2791	OH2	HOH	X	88	12.147	38.012	33.586	1.00	50.31	O
ATOM	2792	OH2	HOH	X	89	29.156	26.372	18.466	1.00	35.16	O
ATOM	2793	OH2	HOH	X	90	13.411	10.247	9.168	1.00	26.43	O
ATOM	2794	OH2	HOH	X	91	11.854	20.770	42.617	1.00	42.09	O
ATOM	2795	MG	MG	X	200	5.976	23.897	15.468	1.00	47.42	MG
ATOM	2796	MG	MG	X	201	−0.275	40.156	9.536	0.50	63.17	MG

A number of embodiments of the disclosure have been described. Nevertheless, it will be understood that various modifications may be made without departing from the spirit and scope of the disclosure. Accordingly, other embodiments are within the scope of the following claims.

All citations made in this disclosure are made with the understanding that the information contained in each such cited document is known to the skilled artisan; and each cited document is incorporated in its entirety herein by reference.

Claims

1. A method of modeling the interaction of a candidate binding agent and a cdc14A polypeptide, said method comprising: (a) modeling a cdc14A polypeptide, defined by a plurality of atomic coordinates; and (b) modeling the interaction of a candidate binding agent with said modeled cdc14A polypeptide.

2. The method of claim 1, wherein the cdc14A polypeptide is a human polypeptide.

3. The method of claim 1, wherein the cdc14A polypeptide has a sequence selected from the group consisting of: (a) SEQ ID NO: 2, 4, or 6; (b) conservative substitutions of (a); (c) variants of (a); (d) mutants of (a), (b), or (c); and (e) fragments of (a), (b), (c), or (d).

4. The method of claim 1, wherein said plurality of atomic coordinates are set forth in Table 2.

5. The method of claim 1, wherein the cdc14A polypeptide is a fragment that comprises the sequence as set forth in SEQ ID NO:2, 4, or 6 from about amino acids 277-285; and wherein the plurality of atomic coordinates comprises atoms 2205-2268 of Table 2.

6. The method of claim 1, wherein the candidate binding agent is selected from the group consisting of a peptide, an anti-cdc14A antibody, a peptidomimetic, and a small molecule.

7. The method of claim 1, further including the step of determining whether the binding agent forms a complex with cdc14A.

8. The method of claim 1, wherein the candidate binding agent is modeled using a computer algorithm to predict a three-dimensional representation of the candidate binding agent.

9. The method of claim 6, wherein the binding agent has a molecular weight less than 1000.

10. A method for identifying a candidate agent that modulates cdc14 polypeptide activity, comprising: (a) modeling a cdc14A polypeptide defined by a plurality of atomic coordinates of the cdc14A polypeptide; (b) modeling said agent's interaction with said modeled cdc14A polypeptide; and (c) determining whether an agent identified in step (b) interacts with cdc14A and modulates cdc14 polypeptide activity.

11. A computer program on a computer readable medium comprising instructions to cause a computer to: (a) define a cdc14A polypeptide or fragment thereof based on a plurality of atomic coordinates of the cdc14A polypeptide; and (b) model a potential binding agent that interacts with the cdc14A polypeptide.

12. The computer program of claim 11, wherein the plurality of atomic coordinates are as set forth in Table 2.

13. A crystalline cdc14A polypeptide comprising a sequence selected from the group consisting of: (a) SEQ ID NO: 2, 4, or 6; (b) conservative substitutions of (a); (c) variants of (a); (d) mutants of (a), (b), or (c); (e) fragments of (a), (b), (c), or (d); and (g) a sequence excluding amino acids 1-9 of SEQ ID NO: 2, 4, or 6.

14. The crystalline cdc14A polypeptide of claim 13, wherein the atomic coordinates of the atoms of the cdc14A polypeptide are selected from the atomic coordinates set forth in Table 2.

15. A crystalline structure selected from the group consisting of: (a) a crystalline polypeptide comprising approximately the following cell constants a=74 Å, b=81 Å, c=69 Å, and a space group of P21212; (b) a crystalline cdc14A polypeptide produced by the method of claim 16;(c) a heavy-atom derivative of a crystallized form of cdc14A polypeptide; (d) a crystalline complex comprising a cdc14A polypeptide and a candidate binding agent; and (e) a co-crystal of a cdc14A polypeptide and binding agent, wherein said cdc14A polypeptide has a sequence selected from the group consisting of SEQ ID NO: 2, 4 or 6.

16. A method of crystallizing cdc14A polypeptide comprising the steps of: (a) mixing an aqueous solution comprising substantially pure cdc14A polypeptide with a reservoir solution comprising a precipitant to form a mixed volume; and (b) subjecting the mixed volume to conditions and for a time sufficient for crystallization to occur.

17. The method of claim 16 wherein the cdc14A polypeptide is obtained from a eukaryotic cell.

18. The method of claim 16 wherein the aqueous solution of step (a) contains about 1 to 50 mg per ml of cdc14A polypeptide.

19. The method of claim 16 wherein the aqueous solution of step (a) contains about 5 to 15 mg per ml of cdc14A polypeptide.

20. The method of claim 16 wherein the precipitant is polyethylene glycol, sodium citrate, ammonium sulfate, sodium cacodylate, or a mixture thereof.

21. The method of claim 20 wherein the precipitant is polyethylene glycol buffered with sodium citrate or sodium cacodylate.

22. The method of claim 21 wherein the precipitant is present in the reservoir solution in an amount of about 16 to 18% of polyethylene glycol, and about 1 to 50 mM of sodium citrate, ammonium sulfate, or sodium cacodylate.

23. The method of claim 16 wherein the reservoir solution further comprises a detergent.

24. The method of claim 23 wherein the detergent is present in an amount of about 5 to 50 mM.

25. The method of claim 16 wherein the pH of the reservoir solution is about 4 to 10.

26. The method of claim 16 wherein step (b) is carried out by vapor diffusion crystallization, batch crystallization, liquid bridge crystallization, or dialysis crystallization.

27. The method of claim 16 wherein step (b) is carried out by vapor diffusion crystallization.

28. The method of claim 16 further comprising isolating the crystalline cdc14A polypeptide.

29. A method for determining a three-dimensional structure of a cdc14A polypeptide comprising: (a) obtaining crystalline cdc14A polypeptide; (b) irradiating the crystalline cdc14A polypeptide to obtain a diffraction pattern characteristic of the crystalline cdc14A polypeptide; and (c) transforming the diffraction pattern into the three-dimensional structure of the cdc14A polypeptide.

30. A method for determining at least a portion of a three-dimensional structure of a molecular complex, said complex comprising a cdc14A polypeptide and said method comprising the steps of: (a) determining the structural coordinates of a crystal of a cdc14A polypeptide; (b) calculating phases from the structural coordinates; (c) calculating an electron density map from the phases obtained in step (b); and (d) determining the structure of at least a portion of the complex based on said electron density map.

31. The method of claim 30, wherein the structural coordinates used in step (a) are substantially the same as those described in Table 2 or describe substantially the same crystal as the coordinates in Table 2.

32. A method for evaluating the ability of a chemical entity to associate with a cdc14A polypeptide or a complex thereof, the method comprising the steps of: (a) employing computational or experimental means to perform a fitting operation between the chemical entity and the cdc14A polypeptide or complex thereof, thereby obtaining data related to the association; and (b) analyzing the data obtained in step (a) to determine the characteristics of the association between the chemical entity and the cdc14A or complex thereof.

33. A method for determining the binding of a test compound to a cdc14 polypeptide, comprising: (a) introducing the test compound and a crystalline cdc14A polypeptide to conditions and for a time sufficient such that the test compound and crystalline cdc14A polypeptide form a complex; (b) analyzing the complex to determine whether the test compound binds thereto.

34. A method of identifying a binding agent for binding to a cdc14A polypeptide, comprising: (a) constructing a three-dimensional structure of the cdc14A polypeptide using a plurality of atomic coordinates selected from the group of atomic coordinates shown in Table 2, (b) performing structure-based design of said binding agent using said atomic coordinates of (a); and (c) identifying a binding agent predicted by said structure based design to bind to cdc14A polypeptide.

35. The method of claim 34, wherein the step of performing structure-based design is performed by computer-assisted means.

36. The method of claim 35, wherein the three-dimensional structure of cdc14A polypeptide is displayed visually by said computer-assisted means.

37. An electronic representation of a binding domain of a cdc14A polypeptide.

38. The electronic representation of claim 37, comprising a binding domain surface contour.

39. The electronic representation of claim 38, further comprising an electronic representation of a binding agent in a binding domain of cdc14A.

40. The electronic representation of claim 37, wherein the electronic representation uses a plurality of atomic coordinates selected from the group of atomic coordinates shown in Table 2.

41. A three-dimensional representation of a cdc14A polypeptide comprising a binding domain that is defined by atomic coordinates of at least one loop section comprising amino acids(a) 46-49 of SEQ ID NO:2; (b) 131-135 of SEQ ID NO:2; (c) 173-181 of SEQ ID NO:2; (d) 191-195 of SEQ ID NO:2; (e) 204-206 of SEQ ID NO:2; (f) 227-229 of SEQ ID NO:2; (g) 249-253 of SEQ ID NO:2; (h) 277-285 of SEQ ID NO:2; and (i) 312-320 of SEQ ID NO:2.