# Patent

## Title
Human laminin receptor crystal and uses thereof

## Abstract

A human laminin receptor crystal is disclosed. Methods are disclosed for using various computer and non-computer means in order to develop models for use in the development of novel therapeutics that block and/or mimic laminin receptor interactions in the setting of, among others, Alzheimer's disease, other neurological disorders, cancer, and viral and bacterial infections.

## Background
CROSS-REFERENCE TO RELATED APPLICATION
This application claims the benefit of and priority to U.S. Provisional Application Ser. No. 60/981,583, filed on Oct. 22, 2007, the entirety of this application hereby incorporated by reference.


STATEMENT REGARDING FEDERALLY SUPPORTED RESEARCH OR DEVELOPMENT
This invention was supported, in whole or in part, by U.S. Public Health Service grants CA100687 and CA68498 from the National Cancer Institute, National Institutes of Health, and Department of Health and Human Services. The Government has certain rights in the invention.


FIELD OF THE INVENTION
The present disclosure is directed to the crystal structure of a laminin receptor (hereinafter “LamR”), and furthermore is directed to developing novel therapeutics that block and/or mimic laminin receptor interactions in the setting of, among others, Alzheimer's Disease, other neurological disorders, cancers and viral and bacterial infections.
Throughout this Application, various publications are referenced by the lead author's name and date of publication. Full citations of these publications may be found in the References Cited. The disclosures of these publications are hereby incorporated by reference into this Application in, order to more fully describe the state of the art as of the date of the invention described and claimed herein.
BACKGROUND OF THE INVENTION
The LamR is a nonintegrin cell-surface protein that has been identified as the receptor for, among others, the extracellular matrix molecule laminin-1 (Rao 1983), pathogenic prion protein. (Gauczynski 2001), Sindbis virus (Wang 1992), Venezuelan equine encephalitis virus (VEE) (Ludwig 1996), cytotoxic necrotizing factor type I and II (McNichol 2007), and Adeno-associated virus serotypes 2, 3, 8 and 9 (Akache 2006). LamR binds to laminin with high affinity, mediating interactions between laminin and the extracellular environment that affect cell adhesion, tumor growth and metastasis.
Two types of LamR, the 67 kDa and the 37 kDa, are found on the surface of cells (Gauczynski 2001.). The 67 kDa laminin receptor may be formed by the dimerization of the 37 kDa laminin receptor. Phylogenetic analysis also suggests that the LamR is a ribosomal protein that acquired the additional novel function of the laminin receptor during evolution (Ardini 1998).
Structural characterization of the LamR may permit greater understanding of how the LamR interacts with its binding partners. This in turn may facilitate development of therapeutics that may block and/or mimic LamR interactions in the setting of, among others, AD, other neurological disorders, cancer, and viral and bacterial infections.
In addition, structural analysis of the LamR may provide insight into the development of therapeutics that aid in the prevention of various disease states, including tumor growth and metastasis.
Because of the role of LamR interaction, with laminin in normal and cancerous cells, as well as its role as a receptor for Sindbis virus, adeno-associated virus and pathogenic prion protein, it is desirable to study LamR using crystallographic methods.
SUMMARY OF THE INVENTION
The present disclosure provides a crystalline form of a human LamR, and provides methods for developing novel therapeutics that block and/or mimic LamR interactions in the setting of, among others, AD, other neurological disorders, cancer, and viral and bacterial infections.
According to aspects illustrated herein, a crystal is provided that includes at least a portion of a LamR. The term “at least, a portion” refers to a LamR having some or all residues of a LamR protein. In some aspects, the term “at least a portion” refers to a LamR having residues 1-220 of a full-length LamR.
According to aspects illustrated herein, a method is disclosed for identifying an agent that interacts with a LamR, that includes: providing at least a portion of the LamR as a crystal; and employing computational analysis to design or select an agent that interacts with the crystal.
According to further aspects illustrated herein, a method is disclosed for identifying an agent that interacts with a LamR that includes: providing at least a portion of the LamR as a crystal; generating a three-dimensional model of the crystal using a set of relative structural coordinates according to Appendix 1 with a root mean square deviation from residue backbone atoms being not more than 1.5 Å, the set of relative structural coordinates being based on the crystal; and employing the three-dimensional model to design or select an agent that interacts with the crystal.
According to further aspects illustrated herein, there is disclosed a method for identifying an activator or inhibitor of a molecule or molecular complex having an active binding site that includes: generating a three dimensional representation of the molecule or molecular complex including an active binding site using a set of relative structural coordinates of amino acid residues Leu25, Gly26, Gly27, Ile46, Arg80, Asp126, Arg128, Asn149, Asp151, Ser152, Asp164, Asp165, Lys166, Gln33, Gln35, Tyr36, Lys57, Ala137, Ser138, Asn141, Leu142, Pro143, Thr144, Met10, Leu19, His24, Ile49, Asn50, Leu51, Lys52, Gln9, Lys11, Trp55, Leu59, Glu181, Arg184, Met185 Arg191, Thr28, Ile46, Pro127, Ala129, Val15, Phe18, Leu25, Arg80 and Asn81, or any portion thereof, with a root mean square deviation from residue backbone atoms of the amino acid residues being not more than 1.5 Å; and selecting or designing a candidate activator or inhibitor by performing computer fitting analysis of the candidate activator or inhibitor with the three dimensional representation generated.
According to further aspects illustrated herein, there is disclosed a method for identifying a potential compound able to interact with a LamR family member that includes: selecting or designing the potential compound by performing rational drug design with a computer readable data storage material encoded with computer readable data including structure coordinates as listed in Appendix 1, wherein the selecting or designing is performed in conjunction with computer modeling; contacting the potential compound with at least a portion of a LamR; and detecting an ability of the potential compound to interact with the LamR family member.
According to yet further aspects illustrated herein, methods of identifying an agent that interacts with LamR, and/or identifying an activator or inhibitor of a molecule or molecular complex having an active binding site, and/or identifying a potential compound that is able to interact with a LamR family member may also be performed without the aid of a computer means. Indeed, the present invention includes manual and computational methods of determining and/or deriving the above, in accordance with a crystal of at least a portion of the LamR being provided.
According to even further aspects illustrated herein, there is disclosed a crystal that includes at least a portion of a p40 ribosomal protein, wherein the p40 ribosomal protein is in tetragonal space group P43212 and has unit cell dimensions a=75.7 Å, b=75.7 Å, and c=99 Å.
Applicants have also found that LamR interacts with many ligands including, but not limited to, laminin, prions, Sindbis virus, and EGCG (the major polyphenol in green tea).
LamR may also be implicated in the onset of Alzheimer's Disease (hereinafter “AD”) and certain dancers.
With respect to cancer, it has been observed that one of the ways EGCG may mediate anticancer effects is through binding to the LamR. Applicants have found that the Sindbis vector targets overexpressed LamR on tumor cells, resulting in the reduction of tumor load. Thus, targeted therapeutic design with respect to the LamR's interaction with its other binding partners will be efficacious.
For example, Applicants have discovered that blocking the interaction of certain ligands with the LamR will prevent internalization of a pathogen. This blocking prevents the removal of LamR from the cell surface. Together, these actions may very well effect disease progression.
With respect to AD, laminin has been shown to interact with the amyloid beta 1-40 peptide (hereinafter “Aβ”), thus blocking fibril formation and even inducing depolymerization of pre-formed fibrils. LamR may be of therapeutic interest for controlling the amyloidosis that occurs with AD.
Targeted therapeutic design against LamR's interaction with its other binding partners may also be efficacious. Further study of the structure of the LamR crystal provided herein will contribute to an understanding of how LamR interacts with its binding partners and aid in the development of therapeutics that can block and/or mimic LamR interactions in the setting of, among others, AD, other neurological disorders, cancers and viral and bacterial infections.
In addition, study of the LamR crystal structure may also lead to discovery of co-crystals representing the crystal forms and structures of the LamR when interacting with binding partners, which may further aid in the prevention or treatment of the types conditions noted above.



BRIEF DESCRIPTION OF THE DRAWINGS
The patent or application file contains at least one drawing executed in color. Copies of this patent or patent application publication with color drawing(s) will be provided by the Office upon request and payment of the necessary fee.
The presently disclosed embodiments will be further explained with reference to the attached drawings, wherein like structures are referred to by like numerals throughout the several views. The drawings are not necessarily to scale, the emphasis having instead been generally placed upon illustrating the principles of the presently disclosed embodiments.
FIG. 1 shows the sequence homology between the 37LRP/p40 orthologs and the H. sapien LamR-220 of the presently disclosed embodiments. Orthologs are C. elegans SA ribosomal protein (p40), S. cerevisiae S2p ribosomal protein, and A. fulgidus S2p ribosomal protein. Residue numbering is for human LamR-220.
FIGS. 2A and 2B show the bioactivity of LamR-220 of the presently disclosed embodiments, in vitro. FIG. 2A shows the in vitro LamR-220 binding affinity for laminin-1. (LamR-220 is illustrated by a solid black line and LamR-295 is illustrated by a dashed black line. n=3±SEM.) LamR-220 Kd=1.7 μM. LamR-295 Kd=0.7 μM. FIG. 2B shows Sindbis viral vector infection inhibition by LamR-220 in baby hamster kidney (hereinafter “BHK”) cells, SV=Sindbis vector (MOI=100), LamR=recombinant LamR-220. n=2±SEM. Statistical significance was calculated by a two-tailed student t-test (P<0.05).
FIGS. 3A, 3B-1, 3B-2 and, 3C show the crystal structure of human LamR-220 of the presently disclosed embodiments. FIG. 3A shows a ribbon diagram of LamR-220 with α helices labeled “A”, “B”, “C”, “D” and “E” and β strands, labeled “1”, “2”, “3”, “4”, “5”, “6” and “7”. FIGS. 3B-1 and 3B-2 show the superimposition of LamR-220 and A. fulgidus S2p (1VI6). Regions of divergence between the two structures are at residues 111-118 and 188-196. FIG. 3C shows a LamR-220 dimer. Residues in the dimer interface are labeled. The crystallographic two-fold axis is vertical.



While the above-identified drawings set forth presently disclosed embodiments, other embodiments are also contemplated, as noted in the discussion.
DETAILED DESCRIPTION OF THE INVENTION
As noted above, the embodiments disclosed herein relate to the three dimensional crystal structure of a LamR and to developing novel therapeutics that may block and/or mimic LamR interactions in the setting of, among others, AD, other neurological disorders, cancer, and viral and bacterial infections.
Atomic structural coordinates for the LamR of the presently disclosed embodiments were derived from the analysis of high resolution X-ray diffraction patterns of crystals of a 220-residue version LamR (hereinafter sometimes referred to as “LamR-220”). These atomic structural coordinates are given in Appendix 1.
Definitions
All scientific terms are given their ordinary meanings as understood by those of skill in the art, unless an alternate meaning is set forth below.
As used herein, the term “LamR” refers to the laminin receptor.
As used herein, the term “p40” refers to the p40 ribosome-associated protein.
As used herein, the term “molecular replacement” means a method of solving crystal structure using a set of atomic coordinates of a structurally related molecule.
As used herein, the term “binding site” or “binding pocket” refers to a region of a protein or protein/RNA complex or RNA that binds or interacts with a particular compound.
As used herein, the term “structural coordinates” refers to mathematical Cartesian coordinates corresponding to an atom's spatial relationship to other atoms in a molecule or molecular complex. Structural coordinates may be obtained using x-ray crystallography techniques or NMR techniques, or may be derived from mathematical equations related to the X-ray diffraction patterns obtained by diffracting X-rays off a crystal. The diffraction data are used to calculate an electron density map of the unit cell comprising the crystal; said maps are used to establish the positions of the atoms (e.g., the structure coordinates) within the unit cell. Various software programs allow for the graphical representation of a set of structural coordinates to obtain a three dimensional representation of a molecule or molecular complex. Those of skill in the art understand that a set of structure coordinates determined by X-ray crystallography contains standard errors.
As used herein, the term “β sheet” refers to two or more polypeptide chains (or beta strands) that run alongside each other and are linked in a regular manner by hydrogen bonds between the main chain C═O and N—H groups. Therefore all hydrogen bonds in a beta-sheet are between different segments of polypeptide. Most β-sheets in proteins are all-parallel (protein interiors) or all-antiparallel (one side facing solvent, the other facing the hydrophobic core). Hydrogen bonds in antiparallel sheets are perpendicular to the chain direction and spaced evenly as pairs between strands. Hydrogen bonds in parallel sheets are slanted with respect to the chains direction and spaced evenly between strands.
As used herein, the term “α helix” refers to the most abundant helical conformation found in globular proteins. The average length of an α helix is 10 residues. In, an α helix, all amide protons point toward the N-terminus and all carbonyl oxygens point toward the C-terminus. The repeating nature of the phi/psi pairs ensure this orientation. Hydrogen bonds within an α helix also display a repeating pattern in which the backbone C═O of residue X (wherein X refers to any amino acid) hydrogen bonds to the backbone HN of residue X+4. The α helix is a coiled structure characterized by 3.6. residues per turn, and translating along, its axis 1.5 Å per amino acid. Thus the pitch is 3.6×1.5 or 5.4 Å. The screw sense of alpha helices is always right-handed.
As used herein, the term “loop” refers to any other conformation of amino acids (i.e. not a helix, strand or sheet). Additionally, a loop may contain bond interactions between amino acid side chains, but not in a repetitive, regular fashion.
Amino acid residues in peptides are abbreviated as follows: Phenylalanine is Phe or F; Leucine is Leu or L; Isoleucine is Ile or I; Methionine is Met or M; Valine is Val or V; Serine is Ser or S; Proline is Pro or P; Threonine is Thr or T; Alanine is Ala or A; Tyrosine is Tyr or Y; Histidine is His or H; Glutamine is Gln or Q; Asparagine is Asn or N; Lysine is Lys or K; Aspartic Acid is Asp or D; Glutamic Acid is Glu or E; Cysteine is Cys or C; Tryptophan is Trp or W; Arginine is Arg or R; and Glycine is Gly or G.
As used herein, the term “root mean square deviation” is the square root of the arithmetic mean of the squares of the deviations from the mean, and is a way of expressing deviation or variation from the structural coordinates described herein. The present disclosure includes all embodiments comprising conservative substitutions of the noted amino acid residues resulting in same structural coordinates within the stated root mean square deviation.
As used herein, an “active site” refers to a region of a molecule or molecular complex that, as a result of its shape and charge potential, favorably interacts or associates with another agent (including, without limitation, a protein, polypeptide, peptide, nucleic acid, including DNA or RNA, molecule, compound or drug) via various covalent and/or non-covalent binding forces. An active site in accordance with the present disclosure may include, for example, the actual site of substrate binding with laminin receptor, as well as accessory binding sites adjacent or proximal to the actual binding site of substrate binding that nonetheless may affect laminin receptor activity upon interaction or association with a particular agent, either by direct interference with the actual site of substrate binding or by indirectly affecting the steric conformation or charge potential of the laminin receptor and thereby preventing or reducing binding of substrate to the laminin receptor at the actual site of substrate binding.
As used herein, an “agent” includes a protein, polypeptide, peptide, nucleic acid (including DNA or RNA), molecule, compound or drug.
As used herein, the terms “a target structural motif” or “target motif” refer to any rationally selected sequence or combination of sequences in which the sequence(s) are chosen based on a three-dimensional configuration or electron density map which is formed upon the folding of the target motif. There are a variety of target motifs known in the art. Protein target motifs include, but are not limited to, enzymatic active sites, structural subdomains, epitopes, functional domains and signal sequences.
Structural similarity may be inferred from, e.g., sequence similarity, which can be determined by one of ordinary skill through visual inspection and comparison of the sequences, or through the use of well-known alignment software programs such as CLUSTAL (Wilbur, W. J. and Lipman, D. J. Proc. Natl. Acad. Sci. USA, 80, 726 730 (1983)) or CLUSTAL W (Thompson, J. D., Higgins, D. G. and Gibson, T. J., CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice, Nucleic Acids Research, 22:4.673 4680 (1994)) or BLAST® (Altschul S F, Gish W, et al., J. Mol. Biol., October 5; 215(3):403 10 (1990)), a set of similarity search programs designed to explore all of the available sequence databases regardless of whether the query is protein or DNA. A residue within a first protein or nucleic acid sequence corresponds to a residue within a second protein, or nucleic acid sequence if the two residues occupy the same position when the first and second sequences are aligned.
LamR Binding Domains and Experimental Details
The region of LamR responsible for binding laminin-1 is between amino acid residues 161 and 180, and was found using a synthetic peptide called peptide G which corresponds to those amino acids. Specifically, the domain within laminin-1, the Tyr-Ile-Gly-Ser-Arg (YIGSR) peptide, is responsible for binding with LamR. In additions peptide G treatment of cells has been shown to increase and stabilize laminin binding on tumor cells. Peptide. G has also been shown to bind heparin sulfate proteoglycans (hereinafter “HSPG”) and it has been suggested that laminin-1 interactions with LamR may also be mediated by HSPG binding.
Another synthetic peptide comprised of corresponding amino acid residues 205-229 of the LamR, has been shown to interact with both laminin-1 and heparin sulfate. This indicates that two sites play a role in LamR interactions with laminin. The interaction domains between LamR and prion protein have also been characterized. Yeast two-hybrid system and cell-binding assays suggest that LamR, contains a primary prion protein-binding region between amino acids 144 and 179 and a secondary indirect binding site that is HSPG-dependent between amino acids 161 and 179.
A potential region for interaction between LamR and Sindbis virus E2 has been identified to lie within the C-terminus of LamR. In fact, Wang et al. determined that binding of monoclonal antibody 1C3 (MAb 1C3) to LamR in culture cells blocked Sindbis virus attachment (Wang 1992). MAb1C3 is a monoclonal antibody that is reactive with an epitope within the C-terminal 48 amino acids (residues 248 to 295) of the LamR. This indicates that Sindbis virus also binds somewhere in this C-terminal domain of LamR.
According to Applicants and others, these data also implicate LamR as the major cell-surface receptor for Sindbis virus in vertebrate cells, but the specific interaction domain between Sindbis virus E2 was heretofore unclear. Thus, X-ray crystallographic studies of the LamR are critical to understanding the precise structure of the LamR and to characterizing the LamR binding interaction with Sindbis virus, as well and other key binding partners and agents.
Discussion
In accordance with the present disclosure, a crystal form of the LamR has been produced. The LamR crystal has structure: and properties described in further detail below.
Thus, the presently disclosed embodiments describe the resolution of a three dimensional crystal structure of a 220-residue version of human LamR precursor protein (hereinafter “LamR-220”). LamR-220 binds laminin-1 in vitro, as shown in FIG. 2A, and inhibits Sindbis virus vector infection of BHK cells, as shown in FIG. 2B. These data demonstrate that the first 220 residues of LamR are sufficient for interacting with key binding partners, including Sindbis virus.
Crystals of LamR-220 were obtained at a pH 6.0 and belong to the tetragonal space group P43212 with one monomer in the asymmetric unit. The crystal structure of LamR-220 was determined by molecular replacement, using the crystal structure of the 30S ribosomal protein. S2p from Archaeoglobus fulgidus (PDB code 1VI6) (Badger 2005). Data collection and refinement statistics at 2.15 Å resolution are given in Appendix 1 and Table 1 below.








TABLE 1






LamR220


















Data collectio n




Space group
P43212



Cell dimensions




a, b, c (Å)
75.66, 75.66, 98.965



a, b, g (°)
90.00, 90.00, 90.00



Resolution (Å)
 50.0 (2.15)*



Rsym or Rmerge (%)
14.4 (47.7)



I/sI
5.0 (4.0)



Completeness (%)
100 (100)



Redundancy
9.4 (9.7)



Refinement




Resolution (Å)
30.0-2.15



No. reflections
14762



Rwork/Rfree (%)
18.8/24.1



No. atoms
1727



Protein
1563



Ligand/ion
0



Water
164



Average B-factor
22.0



R.m.s. deviations




Bond lengths (Å)
0.009



Bond angles (°)
1.17





*Values in parentheses are for highest-resolution shell (2.25-2.15 Å). One crystal was used for data collection.






Consistent with a sequence identity of 32% between the LamR and A. fulgidus S2p (residues 15-183 of FIG. 1), the two proteins share a similar overall architecture, classified (SCOP) as an α/β protein with a flavodoxin-like fold (see FIG. 3A). A central β sheet composed of five parallel β strands (β3-β7) is flanked by three α helices on one side (αB, αC and αE) and a single α helix (αD) on the other side. An N-terminal α helix (αA) and two anti-parallel β strands (β1-β2) pack against the α/β core of the protein. Residues 1-8 and 206-220 of LamR-220 are disordered in the structure.
FIGS. 3B-1 and 3B-2 show that the superimposition of the structures of LamR-220 and A. fulgidus S2p yields a root-mean-square deviation in Cα positions of just 0.9 Å (174 atoms) and reveals two areas in which the structures are divergent. The structures diverge at a segment between β4 and β5 (residues 111-118 in LamR) and a segment after the last α helix (αE) (residues 188-196 in LamR) in which LamR contains a five-residue insertion relative to A. fulgidis S2p. The segment between β4 and β5, contains an equal number of residues, in the two proteins. In A. fulgidis S2p, the segment is stabilized in a folded-back conformation via a salt bridge between Arg113 in this segment (Arg117 in LamR) and Asp93 (β4), the latter of which is not conserved in LamR, (Thr97). As shown in FIG. 3C, in the LamR-220 structure, this segment instead projects away from, the domain and packs against the same segment in a symmetry-related (two-fold) molecule. In this crystallographic dimer, Ala114 packs into a tight pocket in the symmetry related molecule formed by the β4-β5 segment and the end of αD, and Phe116 is in van der Waals contact with Tyr139 (αD). While Phe116 is generally conserved from S. cerevisiae through vertebrate species, Ala114 is conserved only in vertebrates. The total surface area buried in this interface is a modest 832 Å2 and LamR-220 runs as a monomer in solution but, in the context of a membrane attachment and a possible covalent dimerization linkage (Landowski 1995), this crystallographic dimer could be functionally significant.
The structural differences noted between LamR-220 and A. fulgidis S2p could be important for ribosomal protein function or the acquired function as the receptor for laminin. Analysis of the 3.0 Å-resolution structure of the 30S ribosomal subunit from Thermus thermophilus (PDB code 1J5E) (Wimberly 2000) indicates that the two major structural deviations between human LamR-220 and A. fulgidis S2p (between β4 and β5 and after αE) would not appear to affect ribosomal function, since no RNA or protein contacts are present in these regions. This suggests that the structural differences in human LamR versus A. fulgidis S2p are important for laminin binding.
Previously, peptide segments of LamR, utilized in binding assays implicated a segment, residues 161-180, known as peptide G, as a binding epitope for laminin. (Castronovo 1991). In the LamR-220 crystal structure of the presently disclosed embodiments, this stretch of residues comprises the linker between β7 and most of αE. The only portion of this sequence that, is solvent accessible are residues 165-169 in the β7-αE linker. Without being limited to any particular theory, it is conceivable that the C-terminal tail of LamR-220 undergoes a conformational change, exposing residues within this segment. It is desirable to determine if other peptide segments of LamR are possible for use in binding assays as a binding epitope for laminin. Previously, a short putative transmembrane segment, residues 86-102 was suggested as a binding epitope for laminin (Castronovo 1991). However, analysis of the LamR-220 of the presently disclosed embodiments shows that this segment, encompassing β4 and most of αC, is an integral part of the protein fold and is unlikely to serve as a transmembrane helix.
In addition, the presently disclosed embodiments permit the use of molecular design techniques (whether utilizing a computer or not) to design, identify and synthesize chemical entities and compounds, including inhibitory compounds, capable of binding anywhere on the LamR and/or LamR-related proteins. As such, the structure of the disclosed LamR crystal may be used to identify potential LamR ligands.
Appendix 1 shows the atomic coordinates/x-ray diffraction data of the LamR-220 of the presently disclosed embodiments. The atomic coordinates/x-ray diffraction data may be used to create a physical three-dimensional model which can then be used to design molecular models of compounds that interact and/or bind with LamR.
Alternatively, the atomic coordinates/x-ray diffraction data may be represented as atomic model output data on computer readable media which is then used in a computer modeling system to calculate different molecules expected to interact and/or bind with the LamR. For example, computer analysis of the data permits calculation of the three-dimensional interaction of the LamR and a ligand to confirm that the ligand binds to, or changes the conformation of, particular domain(s) or subdomain(s) of the LamR. Ligands identified from the analysis of the physical or computer model are then synthesized and tested for biological activity with an appropriate screen.
Although various computer programs are described herein which may be used in conjunction with the present invention, one of skill in the art could of course perform all of the analysis described herein using manual computational methods after having been provided the crystal structure of the LamR. Thus, the practice of the present invention is not limited to using only computer means, but includes and encompasses all forms of computational methods (computers or otherwise).
When using a computer means, however, the atomic coordinates/x-ray diffraction data of the presently disclosed embodiments are generally provided on computer readable media. A skilled artisan is able to access the data and analyze it for structure determination and/or rational ligand (e.g., inhibitor) design using a computer based system.
A typical computer system includes hardware means, software means, and data storage means. The hardware means typically includes a central processing unit (CPU), input means, output means and data storage means. One skilled in the art will readily appreciate which of the currently available computer-based systems are suitable for use in the practice of the presently disclosed embodiments.
As has been disclosed in U.S. patent application Ser. No. 10/885,190, a variety of commercially available software programs are available for conducting the analysis and comparison of data in the computer-based, system. One skilled in the art will readily recognize which of the available algorithms or implementing software packages for conducting computer analyses can be utilized or adapted for use in the computer-based system. A variety of structural formats for the input and output means can be used to input and output the information in the computer-based systems of the presently disclosed embodiments.
As has also been disclosed, in U.S. patent application Ser. No. 10/885,190, a variety of comparing means can be used to compare a target sequence or target motif with the data storage means to identify structural motifs or interpret electron density maps derived in part from the atomic coordinates/x-ray diffraction data. One skilled in the art can readily recognize any one of the publicly available computer modeling programs that can be used.
As has been further disclosed in U.S. patent application Ser. No. 10/885,190, suitable software that can be used to view, analyze, design, and/or model a protein include AlchemyTM, LabVisionTM, SybylTM, MolcaddTM, LeapfrogTM, MatchmakerTM, GenefoldTM and SitelTM (available from Tripos Inc., St. Louis, Mo.); QuantaTM, Cerius2TM, X-PlorTM, CNSTM, CatalystTM, ModellerTM, ChemXTM, LudiTM, InsightTM, DiscoverTM, CameleonTM and IditisTM (available from Accelrys Inc., Princeton, N.J.); RasmolTM (available from Glaxo Research and Development; Greenford, Middlesex, U.K.); MOETM (available from Chemical Computing Group, Montreal, Quebec, Canada); MaestroTM (available from Schrodinger Inc.); Midas/MidasPlusTM (available from UCSF, San Francisco, Calif.); VRML (webviewer—freeware on, the internet); Chime (MDL—freeware on the internet); MOIL, (available from University of Illinois, Urbana-Champaign, Ill.); MacroModelTM and GRASPTM (available: from Columbia University, New York, N.Y.); RibbonTM (available from University of Alabama, Tuscaloosa, Ala.); NAOMITM (available from Oxford University, Oxford, UK); Explorer EyechemTM (available from Silicon Graphics Inc., Mountain View, Calif.); UnivisionTM (available from Cray Research Inc., Seattle Wash.); MolscriptTM and O (available from Uppsala University, Uppsala, Sweden); Chem 3DTM and Protein ExpertTM (available from Cambridge Scientific); ChainTM (available from Baylor College of Medicine, Houston, Tex.); SpartanTM, MacSpartanTM and TitanTM (available from Wavefunction Inc., Irvine, Calif.); VMDTM (available from U. Illinois/Beckman Institute); SculptTM (available from Interactive Simulations, Inc., Portland, Oreg.); ProcheckTM (available from Brookhaven National Laboratory, Upton, N.Y.); DGEOM (available from QCPE—Quantum Chemistry Program Exchange, Indiana University Bloomington, Ind.); RE_VIEW (available from Brunel University, London, UK); Xmol (available from Minnesota Supercomputing Center, University of Minnesota, Minneapolis, Minn.); HyperchemTM (Available from Hypercube, Inc., Gainesville, Fla.); MDM Display (available from University of Washington, Seattle, Wash.); PKB (available from National Center for Biotechnblogy Information, NIH, Bethesda, Md.); Molecular Discovery Programmes (available from Molecular Discovery Limited, Mayfair, London); GrownolTM (available from Thistlesoft, Morris Township, N.J.); MICE (available from the San Diego Supercomputer Center, La Jolla, Calif.); Yummie and MCPro (available from Yale University, New Haven, Conn.); and upgraded versions thereof.
Another example of the type of software that a skilled artisan may use with the crystal structure of the LamR is software developed by Molsoft Technologies. Specifically, ICM Pro, ICM Browser Pro, ICM Homology and ICM VLS (hereinafter, collectively, “ICM”) together provide a solution for the viewing, analysis, modeling, design, and bonding simulation of proteins. ICM enables the analysis of a protein structure including, but not limited to, flagging problem regions, superimposing multiple structures, drug binding pocket and protein-protein interaction prediction, analysis of protein-ligand interactions, protein flexibility, distances and electrostatic properties. ICM also allows the full evaluation of the underlying crystallographic information contained within a Protein Databank file. One such function exhibits the full bio-molecular unit to see if crystal-crystal contacts have influenced the crystal structure. ICM's crystallographic capabilities include, but are not limited to: displaying the crystallographic cell, generating crystallographic neighbors, constructing biological units and applying transformations, and contouring and converting the electron density map to a grid energy map. ICM provides access to the chemical information and tools for accurate individual ligand-protein docking, peptide-protein docking and protein-protein docking, enabling rapid and accurate docking simulations. These tools provide scripting for small scale flexible ligand docking, procedures for protein-protein, and flexible peptide-receptor docking, and refinement of docking solutions in full atom representation. It also allows for the browsing of docking solutions, binding site analysis, visualization of grid potentials, adjustment of grid potential areas, and configurable preferences for ligand size and score thresholds. In application, ICM indexes and converts any chemical database to 3D, then docks and scores all molecules by estimated binding affinity. It separates binders and non-binders, and eliminates at least 99% of compounds that do not fit the protein or ligand pocket, and do not require experimental testing. One skilled in the art will appreciate that ICM (or similar software) may be used in order to determine what compounds can readily interact with the LamR.
Although the present invention is not limited to solely utilizing computers, computer simulation techniques may be advantageously used in connection with the. LamR crystal structure. In particular, the crystal structure of the LamR provides a means of discovering the characteristics and affinities of individual binding sites on the LamR. For example, EGCG is one such high-affinity compound whose specific binding sites with the LamR may be determined. Thus, the presently disclosed embodiments provide a means of accurately testing the effects of many molecular compounds on a given binding site which, in turn, may be used for the discovery and development of therapies for, but not limited to, cancer and AD. In addition, computer and/or other computational models may also be used for the discovery of inhibitors of LamR activity identified or designed by the methods of the presently disclosed embodiments. Once a potential ligand is identified from the analysis described above, the ligand can then be synthesized and tested for biological activity using an appropriate screening method discussed above and claimed below.
Analysis of the LamR crystal structure may also provide insights that aid in the development of novel therapeutics. In cancer, for example, the specific inhibition of the LamR function at the cell surface of tumor cells—either by binding of the catechin EGCG, which most likely competes with endogenous laminin, or by infection with Sindbis virus vector, which is internalized by receptor-mediated endocytosis—has been associated with anti-tumor effects (Tanaka 2000; Tachibana 2004; Tseng 2004; Cao 1999). Thus, both EGCG and Sindbis virus vectors, through two different mechanisms, reduce the ability of the LamR at the surface to interact with laminin.
Cancer cells invade the basement membranes through a process involving the binding of cell surface receptors like the LamR to laminin. While the presence of cancer invariably yields the overexpression of LamR, the expression of LamR has been particularly identified as correlating directly with increased invasiveness and the metastatic potential of tumors (Menard 1998). However, peptide G, for instance, has been identified as interfering with the binding of the LamR to laminin and therefore as effective in inhibiting tumor cell invasion. Similarly, as noted above, EGCG is well known to bind with the LamR, thereby precluding other binding from occurring. Study of the crystal structure of the LamR may permit precise determination of how these bindings occur.
Likewise, the crystal LamR may be used to further understand the role of the LamR in AD. With respect to AD, as previously noted, laminin has been shown to interact with the Aβ, thus blocking fibril formation and even inducing depolymerization of pre-formed fibrils. LamR may also be of therapeutic interest for controlling the amyloidosis that occurs with AD.
By way of a further background, AD is a progressive neurodegenerative disease, characterized by an early loss of memory as well as impairment of other intellectual functions, eventually resulting in the onset of dementia. The LamR may play a role in the progression of AD. Accordingly, study of the LamR crystal may play a role in treating and preventing AD.
The brains of humans afflicted with AD experience extensive neuronal loss in the hipocampus, neocortex, and other areas of the brain. Such brains have been found to be histopathologically characterized by numerous extracellular deposits, or lesions, comprising senile plaques and neurofibrillary tangles.
The interaction between laminin and the amyloid precursor protein (hereinafter “APP”)—which yields Aβ as a proteolytic fragment of APP—is, generally linked to the progressive development of the senile plaques (also known as amyloid plaques) which appear to disrupt the extracellular matrix when APP is overproduced. Aβ polymerizes into amyloid fibrils and is the major component of the plaques. These lesions have neurotoxic effects and are one of the causes, if not the primary cause, of neurodegeneration. AD brain tissue also has elevated expression of laminin compared to normal brain tissue.
Nonetheless, laminin has been found to be a potent inhibitor of the Aβ fibril formation responsible for the development of the plaques, as laminin has been shown to attenuate the neurotoxicity of amyloid. A chain containing the sequence IKVAV (a laminin-derived peptide), for example, has been found to inhibit amyloidogenesis by depolymerizing Aβ. This inhibition appears to be due to laminin's particular interaction with Aβ which results in the inducement of depolymerization of Aβ fibrils that are so instrumental in the onset and generation of AD and that are present in its telltale lesions. Laminin has also been shown to modulate the biogenesis of APP. Such interactions have also inhibited the toxic effects on rat primary hippocampal neurons.
Screening mechanisms as disclosed herein may also be used for the discovery and design of specific therapeutic drugs which treat various disease states by targeting the LamR. Once a drug is selected, the drug may then be produced through ordinary chemical synthesis. In addition, a pharmaceutically acceptable carrier may then be added thereto.
Accordingly, a method for producing a pharmaceutical composition which comprises a step of producing the drug obtainable by the above mentioned screening methods is within the scope of the presently disclosed embodiments.
As further disclosure of the presently disclosed embodiments, the, following Preparations and Examples are provided to illustrate specific embodiments and aspects of the presently disclosed embodiments. The illustration of specific embodiments and aspects, however, is not intended to limit the scope of this disclosure.
Materials And Methods
(i) Recombinant LamR Expression and Purification
Full-length human laminin receptor having residues 1-295 (LamR-295) was cloned into an E. coli expression vector that includes a TEV-cleavable, N-terminal 6×His-tag. The vector encoding LamR-295 was transformed into E. coli strain BL21 (DE3*) and cultures were grown in Luria broth media at 37° C. to an OD600 of 0.6. Protein expression was induced by the addition of isopropyl-thiogalactopyranoside (IPTG, 0.1 mM) for 12 hours at 20° C. Cells were harvested, resuspended in lysis buffer (50 mM Tris (pH 8.0), 300 mM NaCl, 0.1% Triton X-100, 10% glycerol, EDTA-free protease inhibitor tablet (Roche)) and lysed by French press. The lysate was centrifuged at 16,000 RPM for 30 minutes and the supernatant was collected. The soluble fraction was purified by Ni-NTA chromatography (Qiagen), followed by gel filtration chromatography (Superdex 75, Amersham). Protein was concentrated in spin concentrators (Amicon, Millipore).
Expression and purification of LamR-295 was verified by coomassie staining and Western blot using both anti-His and anti-LamR antibodies. Purification of LamR-295 resulted in an impure protein product which was evident by multiple bands in both the coomassie stain and Western blot. In order to crystallize a protein, an extremely high level of purity is necessary. Thus, various shorter-length LamRs were subcloned from the full-length human LamR-295 cDNA and expression and purification was tested.
Next, the following LamR constructs were tested for expression and purification for crystallography purposes: residues 1-198, 12-198, 1-220, 12-220, and 1-206. Constructs comprising residues 12-198 and 1-198 were tested due to a sequence alignment between T. thermophilus 40S ribosomal protein S0-A, which was solved by CryoEM structure. Residues 12-220 and 1-220 were tested because trypsin digestion of the full-length LamR construct corresponded to a stable protein of 25 kDa, which approximately corresponds to amino acids 1-220. In addition, N-terminal sequencing of LamR-295 confirmed that the full-length construct was not being degraded from the N-terminus.
Due to the highly pure protein product (>95%) obtained from the LamR-220 construct, to the LamR-220 construct was chosen for pursuing crystallization screenings Residues 1-220 of human 37 kDa LamR protein (LamR-220,) were subcloned from a full-length LamR cDNA into an E. coli expression vector that includes a TEV-cleavable, N-terminal 6×His-tag. The construct was verified by automated DNA sequencing. The vector encoding LamR-220 was transformed into E. coli strain BL21 (DE3*), and cultures were grown in Luria broth media at 37° C. to an OD600 of 0.6. Protein expression was induced by the addition of isopropyl-thiogalactopyranoside (IPTG, 0.1 mM) for 12 hours at 20° C. Cells were harvested, resuspended in lysis buffer (50 mM Tris (pH 8.0), 300 mM NaCl, 0.1% Triton X-100, 10% glycerol, EDTA-free protease inhibitor tablet (Roche)) and lysed by French press. The lysate was centrifuged at 16,000 RPM for 30 minutes and the supernatant was collected. The soluble fraction was purified by Ni-NTA chromatography (Qiagen), followed by gel filtration chromatography (Superdex 75, Amersham). Protein was concentrated in spin concentrators (Amicon, Millipore).
(ii) Crystallization and Data Collection
The most frequently used crystallization method is a vapor diffusion technique in which a 1 μl droplet of recombinant purified protein is mixed with an equal volume of the crystallizing solution that contains buffer, salt and precipitant. This droplet is placed on a siliconized glass cover slip which is inverted and sealed into place over a reservoir of 500 μl of the crystallization solution. The concentration difference between the drop and the reservoir drives the system to equilibrium by diffusion through the vapor phase.
Crystals of LamR-220 were grown at 17° C. by the hanging-drop vapor diffusion method in drops containing a 1:1 (v/v) ratio of protein solution at 10 mg/ml and reservoir solution containing 17% (w/v) PEG, 10 K, 120 mM sodium citrate, 100 mM MES [pH 6.0], and 5% (w/v) PEG 1.5 K. Crystals belong to the tetragonal space group P43212 with unit cell dimensions of a=75.666 Å, b=75.666 Å, and c=98.965 Å. Crystals were soaked briefly in crystallization buffer with 20% glycerol (v/v) and then flash frozen in liquid nitrogen. There is one LamR-220 molecule in the asymmetric unit with a solvent content of 56%. Diffraction data were collected to a resolution of 2.15 Å at X29 at the National Synchrotron Light Source at Brookhaven National Laboratory. Data were processed with the HKL2000 (Otwinowski 1997). A molecular replacement solution was found with AMoRE (Navaza 1994) using as a search model the structure of the A. fulgidus 30s ribosomal protein S2p [PDB code 1VI6, chain A] (Badger 2005). Rigid-body refinement, simulated annealing and positional and B-factor refinement were performed with CNS (Brunger 1998) and Refmac (Mushudov 1997). Coot was used for model building (Emsley 2004). According to PROCHECK (Laskowski 1993), 94.8% of the residues have backbone torsion angles in most favored regions and 5.2% in additional allowed regions.
(iii) In vitro Binding Affinity for Laminin-1
LamR-220 and LamR-295 were tested in vitro for their ability to bind with laminin-1. White polystyrene ELISA 96-well microplates, precoated with murine laminin-1 (NEBiolabs), were blocked O/N at 4° C. with blocking buffer (3.0% BSA, 0.1% sodium azide in PBS). Wells were incubated with increasing concentrations of LamR-220 or LamR-295, which was Ni-affinity purified as described, above for 1 hour at 37° C. Each well was washed three times with blocking buffer. Penta-His HRP conjugate (1:500) (Qiagen) was incubated for 2 hours at RT and wells were washed three times with blocking buffer. Substrate solution was added and incubated for approximately 15 minutes before reading fluorescent absorbance was detected at 490 nm on an ELISA plate reader (ELx800, Biotek Instruments, Inc.). Controls for buffer alone and nonspecific protein, BSA (NEBiolabs), were also tested. Experiments were performed in triplicate. A binding curve and Kd was generated for LamR-220 and LamR-295. The Kd was calculated using a one-site binding hyperbola and the equation Y=Bmax×X/(kd+X). Each group was tested in triplicate and binding affinity was determined by normalizing to background fluorescence. Results are shown in FIG. 2A.
(iv) Protocol for Protein Purification
A protocol for protein purification includes, but is not limited to, the following:
Expression:

    
    
        1. inoculate 100 ml LB+30 μg/ml Kanymycin O/N at 37° C.
        2. increase volume to 800-1000 mL LB+Kan in 2 L flask
        3. grow at 37° C. until OD600=0.4 to 0.6
        4. induce with 1 mM IPTG O/N at 20° C.
        5. spin down at 10,000 rpm for about 30 minutes and store pellets at −80° C. or Ni-purify
    
    


Nickel-Affinity Purification:

    
    
        1. resuspend 1 L pellet in 30 mL of lysis buffer with 1 tablet EDTA-free protease inhibitor (do this in ice bucket)
        
            a. dissolve protease tablet in lysis buffer before adding to protein pellet
        
        
        2. sonicate for about 20 minutes (3 seconds on, 12 seconds off, at level 3)
        
            a. in ice bucket
            b. OR French press two times
        
        
        3. spin down at 16,000 rpm for 30-45 minutes
        4. filter supernatant in 0.45 μm Millipore 150 ml sterile filters
        5. add 1 mL Ni-agarose beads/1 L original inoculation culture to large 20 mL disposable column
        
            a. add stop cock to control flow
        
        
        6. add 10 mL lysis buffer over beads and let flow through to wash
        7. add protein supernatant, collect flow through (FT)
        
            a. control flow so that it is fairly slow
        
        
        8. add 20 mL wash buffer and collect (W1)
        9. add another 20 mL wash buffer and collect (W2)
        10. add 5 mL elution buffer and, collect five 1 mL fractions (E1-5)
        11. run 10 μL of PC, FT, W1, W2, E1-5 in 15% SDS-PAGE
        12. stain with 0.025% coomassie stain for 15-30 minutes, destain
    
    


Size Exclusion Chromatography:

    
    
        1. collect fractions with most protein and concentrate to 2 mL, filter
        2. wash Superdex-75 column with S75 buffer
        3. run protein on Superdex-75 column and collect fractions
        4. run fractions in 15% SDS-PAGE
        5. concentrate to desired concentration
    
    


(v) In vitro Sindbis Virus Vector Inhibition
Three million (3×106) BHK-55 cells Were plated in a 12-well plate for 24 hours in αMEM (Cellgro) supplemented with 10% FBS. Sindbis virus vector that expressed a luciferin reporter upon replication (multiplicity of infection (MOI)=100) was incubated with control protein (BSA, NEBiolabs), LamR-220, or alone and rotated at room temperature for 1 hour. Cells were washed with Optimem (Gibco) and 300 μl of sample was added. Samples were incubated rotating gently for 1 hour at room temperature to allow Sindbis viral vector attachment. The supernatant was aspirated, cells were washed with PBS, and 1 ml of media was added. The cells were incubated O/N at 37° C. and media was aspirated the next day. 200 μl of unsupplemented media and 200 μl of luciferin substrate (SteadyGlo Luciferase Assay, Promega) was added. The cells were shaken vigorously for 15 minutes. The relative luciferase units (RLU), which correspond to infectivity of Sindbis virus vector, of each sample were read using a luminometer (Glomax 20/20, Promega). Experiments were performed in triplicate. A two-tailed student t-test was performed, (P<0.05) to determine statistical significance. Results are shown in FIG. 2B.
All patents, patent applications, and published references cited herein are hereby incorporated by reference in their, entirety. This disclosure presents illustrative embodiments by way of representation and not limitation. Numerous other modifications and embodiments may be devised by those skilled in the art which fall within the scope and spirit of the principles of the presently disclosed embodiments and the following claims.
REFERENCES CITED


    1. Jackers, P., Minoletti, F., Belotti, D., Clausse, N., Sozzi, G., Sobel, M. E., and Castronovo, V. (1996) Oncogene 13(3), 495-503;
    2. Ardini, E., Pesole, G., Tagliabue, E., Magnifico, A., Castronovo, V. Sobel, M. E., Colnaghi, M. I., and Menard, S. (1998) Mol Biol Evol 15 (8), 1017-1025;
    3. Rao, N. C., Barsky, S. H., Terranova, V. P., and Liotta, L. A., (,1983) Biochemical and biophysical research communications 111(3), 804-808;
    4. Gauczynski, S., Peyrin, J. M., Haik, S., Leucht, C., Hundt, C., Rieger, R., Krasemann, S., Deslys, J. P., Dormont, D., Lasmezas, C. I., and Weiss, S. (2001) Embo J 20(21), 5863-5875;
    5. Wang, K. S., Kuhn, R. J., Strauss, E. G., Ou, S., and Strauss, J. H. (1992) J Virol 66(8), 4992-5001;
    6. Ludwig, G. V., Kondig, J. P., and Smith, J. F. (1996) J Virol 70(8) 5592-5599;
    7. McNichol, B. A., Rasmussen, S. B., Carvalho, H. M., Meysick, K. C., and O'Brien A, D. (2007) Infect Immun; 
    8. Akache, B., Grimm, D., Pandey, K., Yant., S. R., Xu, H., and Kay, M. A. (2006) J Virol 80(19), 9831-9836;
    9. Landowski, T. H., Dratz, E. A., and Starkey, J. R. (1995) Biochemistry 34(35), 11276-11287;
    10. Menard, S., Tagliabue, E., and Colnaghi, M. I. (1998) Breast Cancer Res Treat 52(1-3), 137-145;
    11. Auth, D., and Brawerman, G. (1992) Proceedings of the National Academy of Sciences of the United States of America 89(10), 4368-4372;
    12. Sato, M., Kinoshita, K., Kaneda, U., Saeki, Y., Iwamatsu, A., and Tanaka, K. (1996) Biochemical and biophysical research communications 229(3), 896-901;
    13. Ford, C. L., Randal-Whitis, L., and Ellis, S. R. (1999) Cancer research 59(3), 704-710;
    14. Otwinowski, Z., and Minor, W. (19.97) Methods Enzymol. 276, 307-326;
    15. Navaza, J. (1994) Acta Crystallogr. A 50, 157-163;
    16. Badger, J., Sauder, J. M., Adams, J. M., Antonysamy, S., Bain, K., Bergseid, M. G., Buchanan, S. G., Buchanan, M. D., Batiyenko, Y., Christopher, J. A., Emtage, S., Eroshkina, A., Feil, I., Furlong, E. B., Gajiwala, K. S., Gao, X., He, D., Hendle, J., Huber, A., Hoda, K., Kearins, P., Kissinger, C., Laubert, B., Lewis, H. A., Lin, J., Loomis, K., Lorimer, D., Louie, G., Maletic, M., Marsh, C. D., Miller, I., Molinari, J., Muller-Dieckmann, H. J., Newman, J. M., Noland, B. W., Pagarigan, B., Park, F., Peat, T. S., Post, K. W., Radojicic, S., Ramos, A., Romero, R., Rutter, M. E., Sanderson, W. E., Schwinn, K. D., Tresser, J., Winhoven, J., Wright, T. A., Wu, L., Xu, J., and Harris, T. J. (,2005) Proteins 60(4), 787-796;
    17. Brunger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse-Kunstleve, R. W., Jiang, J. S., Kuszewski, J., Nilges, M., Pannu, N. S., Read, R. J., Rice, L. M., Simonson T., and Warren, G. L. (1998) Acta crystallographica 54(Pt 5), 905-921;
    18. Murshudov, G. N., Vagin, A. A., and Dodson, E. J. (1997) Acta crystallographica 53(Pt 3), 240-255;
    19. Emsley, P., and Cowtan, K. (2004) Acta crystallographica 60(Pt 12 Pt 1), 2126-2132;
    20. Laskowski, R., MacArthur, M. W., Moss, D. S., and Thornton, J. M. (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Cryst., 26, 283-291;
    21. Wimberly, B. T., Brodersen, D. E., Clemons, W. M., Jr., Morgan-Warren, R. J., Carter, A. P., Vonrhein, C., Hartsch, T., and Ramakrishnan, V. (2000) Nature 407(6802), 327-339;
    22. Castronovo, V., Taraboletti, G., and Sobel, M. E. (1991) J Biol Chem 266 (30), 20440-20446;
    23. Tanaka, M., Narumi, K., Isemura, M., Abe, M., Sato, Y., Abe, T., Saijo, Y., Nukiwa, T., and Satoh, K. (2000) Cancer Lett 153 (1-2), 161-168;
    24. Tachibana, H., Koga, K., Fujimura, Y., and Yamada, K. (2004) Nat Struct Mol Biol 11(4), 380-381;
    25. Tseng, J C., Levin, B., Hurtado, A., Yee, H., Perez de Castro, I., Jimenez, M., Shamamian, P., Jin R., Novick, R. P., Pellicler, A., and Meruelo, D. (2004) Nat Biotechnol 22(1), 70-77; and
    26. Cao, Y., and Cao, R. (1999) Nature 398(6726), 381.









APPENDIX 1





X-RAY DATA COORDINATES FOR LRP-220 (SEQ ID NO: 5)
















Unit cell:
75.666  75.666  98.965  90.00  90.00  90.00


Space Group:
P43212


















ATOM
1
N
GLN
X
9
32.089
42.564
44.187
1.00
39.73
N


ATOM
2
CA
GLN
X
9
32.301
44.031
44.338
1.00
39.55
C


ATOM
3
CB
GLN
X
9
32.131
44.729
42.990
1.00
39.97
C


ATOM
4
CG
GLN
X
9
32.703
46.131
42.948
1.00
41.74
C


ATOM
5
CD
GLN
X
9
31.798
47.087
42.215
1.00
43.97
C


ATOM
6
OE1
GLN
X
9
30.698
46.713
41.797
1.00
45.56
O


ATOM
7
NE2
GLN
X
9
32.244
48.335
42.062
1.00
44.38
N


ATOM
8
C
GLN
X
9
31.341
44.621
45.376
1.00
38.74
C


ATOM
9
O
GLN
X
9
31.550
45.728
45.883
1.00
38.77
O


ATOM
10
N
MET
X
10
30.285
43.872
45.679
1.00
37.79
N


ATOM
11
CA
MET
X
10
29.419
44.176
46.807
1.00
36.89
C


ATOM
12
CB
MET
X
10
28.177
43.277
46.769
1.00
37.05
C


ATOM
13
CG
MET
X
10
27.190
43.495
47.905
1.00
36.49
C


ATOM
14
SD
MET
X
10
25.593
42.715
47.601
1.00
37.00
S


ATOM
15
CE
MET
X
10
26.002
40.969
47.535
1.00
36.22
C


ATOM
16
C
MET
X
10
30.222
43.953
48.090
1.00
36.08
C


ATOM
17
O
MET
X
10
30.799
42.881
48.285
1.00
35.72
O


ATOM
18
N
LYS
X
11
30.270
44.968
48.947
1.00
35.03
N


ATOM
19
CA
LYS
X
11
31.070
44.896
50.163
1.00
34.37
C


ATOM
20
CB
LYS
X
11
31.573
46.284
50.571
1.00
34.63
C


ATOM
21
CG
LYS
X
11
32.737
46.797
49.708
1.00
34.83
C


ATOM
22
CD
LYS
X
11
33.164
48.201
50.118
1.00
35.43
C


ATOM
23
CE
LYS
X
11
34.298
48.740
49.230
1.00
37.13
C


ATOM
24
NZ
LYS
X
11
34.377
50.245
49.264
1.00
38.00
N


ATOM
25
C
LYS
X
11
30.334
44.201
51.310
1.00
33.41
C


ATOM
26
O
LYS
X
11
29.103
44.242
51.386
1.00
33.19
O


ATOM
27
N
GLU
X
12
31.112
43.560
52.185
1.00
32.40
N


ATOM
28
CA
GLU
X
12
30.603
42.748
53.296
1.00
31.60
C


ATOM
29
CB
GLU
X
12
31.765
42.159
54.113
1.00
31.72
C


ATOM
30
CG
GLU
X
12
32.593
41.085
53.398
1.00
32.86
C


ATOM
31
CD
GLU
X
12
33.959
40.834
54.062
1.00
33.84
C


ATOM
32
OE1
GLU
X
12
34.513
41.763
54.708
1.00
35.58
O


ATOM
33
OE2
GLU
X
12
34.482
39.698
53.936
1.00
36.48
O


ATOM
34
C
GLU
X
12
29.695
43.552
54.215
1.00
30.09
C


ATOM
35
O
GLU
X
12
28.652
43.063
54.652
1.00
29.50
O


ATOM
36
N
GLU
X
13
30.110
44.786
54.497
1.00
28.75
N


ATOM
37
CA
GLU
X
13
29.368
45.693
55.363
1.00
27.76
C


ATOM
38
CB
GLU
X
13
30.201
46.943
55.688
1.00
28.33
C


ATOM
39
CG
GLU
X
13
31.614
46.666
56.196
1.00
31.49
C


ATOM
40
CD
GLU
X
13
32.670
46.790
55.104
1.00
34.76
C


ATOM
41
OE1
GLU
X
13
32.827
45.844
54.295
1.00
35.71
O


ATOM
42
OE2
GLU
X
13
33.353
47.840
55.066
1.00
36.51
O


ATOM
43
C
GLU
X
13
28.034
46.111
54.742
1.00
25.85
C


ATOM
44
O
GLU
X
13
27.083
46.394
55.461
1.00
25.59
O


ATOM
45
N
ASP
X
14
27.976
46.155
53.411
1.00
24.16
N


ATOM
46
CA
ASP
X
14
26.740
46.506
52.703
1.00
22.20
C


ATOM
47
CB
ASP
X
14
27.023
46.949
51.268
1.00
22.02
C


ATOM
48
CG
ASP
X
14
27.631
48.353
51.193
1.00
21.77
C


ATOM
49
OD1
ASP
X
14
27.367
49.190
52.084
1.00
21.02
O


ATOM
50
OD2
ASP
X
14
28.369
48.623
50.230
1.00
20.85
O


ATOM
51
C
ASP
X
14
25.770
45.334
52.733
1.00
21.02
C


ATOM
52
O
ASP
X
14
24.564
45.525
52.896
1.00
20.55
O


ATOM
53
N
VAL
X
15
26.308
44.125
52.600
1.00
19.77
N


ATOM
54
CA
VAL
X
15
25.510
42.910
52.751
1.00
19.38
C


ATOM
55
CB
VAL
X
15
26.347
41.624
52.543
1.00
19.36
C


ATOM
56
CG1
VAL
X
15
25.496
40.377
52.830
1.00
19.68
C


ATOM
57
CG2
VAL
X
15
26.907
41.570
51.119
1.00
19.73
C


ATOM
58
C
VAL
X
15
24.831
42.888
54.124
1.00
18.45
C


ATOM
59
O
VAL
X
15
23.650
42.595
54.224
1.00
18.63
O


ATOM
60
N
LEU
X
16
25.577
43.230
55.172
1.00
17.93
N


ATOM
61
CA
LEU
X
16
25.030
43.237
56.534
1.00
17.17
C


ATOM
62
CB
LEU
X
16
26.152
43.372
57.569
1.00
17.29
C


ATOM
63
CG
LEU
X
16
27.107
42.181
57.710
1.00
17.24
C


ATOM
64
CD1
LEU
X
16
28.212
42.527
58.702
1.00
18.83
C


ATOM
65
CD2
LEU
X
16
26.363
40.935
58.147
1.00
17.49
C


ATOM
66
C
LEU
X
16
23.966
44.311
56.746
1.00
16.62
C


ATOM
67
O
LEU
X
16
23.010
44.097
57.488
1.00
16.22
O


ATOM
68
N
LYS
X
17
24.148
45.465
56.102
1.00
16.26
N


ATOM
69
CA
LYS
X
17
23.145
46.536
56.085
1.00
15.87
C


ATOM
70
CB
LYS
X
17
23.700
47.779
55.381
1.00
15.92
C


ATOM
71
CG
LYS
X
17
24.573
48.661
56.265
1.00
16.73
C


ATOM
72
CD
LYS
X
17
24.935
49.962
55.557
1.00
16.22
C


ATOM
73
CE
LYS
X
17
25.643
50.911
56.513
1.00
19.22
C


ATOM
74
NZ
LYS
X
17
26.950
50.349
56.984
1.00
19.58
N


ATOM
75
C
LYS
X
17
21.862
46.086
55.390
1.00
15.47
C


ATOM
76
O
LYS
X
17
20.762
46.266
55.921
1.00
15.51
O


ATOM
77
N
PHE
X
18
22.016
45.508
54.199
1.00
15.19
N


ATOM
78
CA
PHE
X
18
20.905
44.929
53.450
1.00
15.34
C


ATOM
79
CB
PHE
X
18
21.428
44.207
52.203
1.00
15.08
C


ATOM
80
CG
PHE
X
18
21.768
45.112
51.036
1.00
15.12
C


ATOM
81
CD1
PHE
X
18
20.991
46.227
50.727
1.00
14.63
C


ATOM
82
CE1
PHE
X
18
21.296
47.039
49.623
1.00
14.97
C


ATOM
83
CZ
PHE
X
18
22.386
46.729
48.817
1.00
15.27
C


ATOM
84
CE2
PHE
X
18
23.165
45.610
49.108
1.00
16.09
C


ATOM
85
CD2
PHE
X
18
22.847
44.805
50.214
1.00
15.18
C


ATOM
86
C
PHE
X
18
20.130
43.926
54.316
1.00
15.81
C


ATOM
87
O
PHE
X
18
18.894
43.961
54.385
1.00
15.46
O


ATOM
88
N
LEU
X
19
20.868
43.027
54.965
1.00
16.26
N


ATOM
89
CA
LEU
X
19
20.259
42.005
55.827
1.00
16.69
C


ATOM
90
CB
LEU
X
19
21.319
40.977
56.266
1.00
16.82
C


ATOM
91
CG
LEU
X
19
21.353
40.022
57.478
1.00
17.48
C


ATOM
92
CD1
LEU
X
19
20.113
39.951
58.393
1.00
17.46
C


ATOM
93
CD2
LEU
X
19
21.775
38.645
56.993
1.00
16.57
C


ATOM
94
C
LEU
X
19
19.468
42.588
56.994
1.00
16.54
C


ATOM
95
O
LEU
X
19
18.319
42.200
57.209
1.00
16.87
O


ATOM
96
N
ALA
X
20
20.068
43.533
57.717
1.00
16.46
N


ATOM
97
CA
ALA
X
20
19.408
44.199
58.849
1.00
16.22
C


ATOM
98
CB
ALA
X
20
20.374
45.177
59.541
1.00
16.21
C


ATOM
99
C
ALA
X
20
18.118
44.914
58.440
1.00
16.31
C


ATOM
100
O
ALA
X
20
17.133
44.907
59.191
1.00
16.26
O


ATOM
101
N
ALA
X
21
18.125
45.513
57.246
1.00
15.98
N


ATOM
102
CA
ALA
X
21
16.961
46.240
56.726
1.00
15.51
C


ATOM
103
CB
ALA
X
21
17.404
47.320
55.750
1.00
15.57
C


ATOM
104
C
ALA
X
21
15.923
45.336
56.070
1.00
15.27
C


ATOM
105
O
ALA
X
21
14.822
45.787
55.762
1.00
15.73
O


ATOM
106
N
GLY
X
22
16.273
44.068
55.855
1.00
14.77
N


ATOM
107
CA
GLY
X
22
15.408
43.130
55.144
1.00
14.09
C


ATOM
108
C
GLY
X
22
15.254
43.441
53.662
1.00
13.92
C


ATOM
109
O
GLY
X
22
14.189
43.241
53.093
1.00
13.77
O


ATOM
110
N
THR
X
23
16.323
43.915
53.029
1.00
13.85
N


ATOM
111
CA
THR
X
23
16.268
44.338
51.618
1.00
13.68
C


ATOM
112
CB
THR
X
23
17.522
45.161
51.240
1.00
13.54
C


ATOM
113
OG1
THR
X
23
17.609
46.295
52.118
1.00
12.71
O


ATOM
114
CG2
THR
X
23
17.464
45.654
49.782
1.00
13.41
C


ATOM
115
C
THR
X
23
15.994
43.164
50.649
1.00
13.97
C


ATOM
116
O
THR
X
23
15.357
43.337
49.593
1.00
13.34
O


ATOM
117
N
HIS
X
24
16.425
41.971
51.058
1.00
13.71
N


ATOM
118
CA
HIS
X
24
16.247
40.734
50.289
1.00
14.30
C


ATOM
119
CB
HIS
X
24
17.132
39.631
50.892
1.00
14.16
C


ATOM
120
CG
HIS
X
24
16.844
39.364
52.335
1.00
14.97
C


ATOM
121
ND1
HIS
X
24
16.114
38.273
52.761
1.00
16.93
N


ATOM
122
CE1
HIS
X
24
16.007
38.304
54.077
1.00
15.26
C


ATOM
123
NE2
HIS
X
24
16.627
39.382
54.520
1.00
15.35
N


ATOM
124
CD2
HIS
X
24
17.157
40.064
53.451
1.00
14.02
C


ATOM
125
C
HIS
X
24
14.806
40.226
50.268
1.00
14.30
C


ATOM
126
O
HIS
X
24
14.491
39.283
49.543
1.00
13.87
O


ATOM
127
N
LEU
X
25
13.943
40.834
51.078
1.00
14.73
N


ATOM
128
CA
LEU
X
25
12.592
40.330
51.264
1.00
15.36
C


ATOM
129
CB
LEU
X
25
12.061
40.685
52.661
1.00
15.55
C


ATOM
130
CG
LEU
X
25
12.652
39.923
53.848
1.00
16.91
C


ATOM
131
CD1
LEU
X
25
12.091
40.470
55.160
1.00
19.07
C


ATOM
132
CD2
LEU
X
25
12.398
38.410
53.737
1.00
18.51
C


ATOM
133
C
LEU
X
25
11.638
40.823
50.185
1.00
15.63
C


ATOM
134
O
LEU
X
25
11.312
42.004
50.121
1.00
15.72
O


ATOM
135
N
GLY
X
26
11.209
39.907
49.326
1.00
16.10
N


ATOM
136
CA
GLY
X
26
10.210
40.217
48.319
1.00
16.93
C


ATOM
137
C
GLY
X
26
8.854
39.855
48.874
1.00
17.73
C


ATOM
138
O
GLY
X
26
8.695
39.668
50.093
1.00
17.81
O


ATOM
139
N
GLY
X
27
7.877
39.722
47.983
1.00
18.17
N


ATOM
140
CA
GLY
X
27
6.539
39.289
48.374
1.00
18.99
C


ATOM
141
C
GLY
X
27
6.245
37.900
47.842
1.00
19.48
C


ATOM
142
O
GLY
X
27
7.140
37.213
47.359
1.00
19.37
O


ATOM
143
N
THR
X
28
4.987
37.489
47.933
1.00
19.94
N


ATOM
144
CA
THR
X
28
4.594
36.158
47.481
1.00
20.79
C


ATOM
145
CB
THR
X
28
3.406
35.610
48.309
1.00
20.95
C


ATOM
146
OG1
THR
X
28
2.292
36.498
48.182
1.00
21.19
O


ATOM
147
CG2
THR
X
28
3.791
35.506
49.778
1.00
21.28
C


ATOM
148
C
THR
X
28
4.278
36.106
45.983
1.00
20.78
C


ATOM
149
O
THR
X
28
4.208
35.024
45.400
1.00
21.53
O


ATOM
150
N
ASN
X
29
4.096
37.268
45.360
1.00
20.74
N


ATOM
151
CA
ASN
X
29
3.851
37.336
43.915
1.00
20.58
C


ATOM
152
CB
ASN
X
29
2.637
38.220
43.600
1.00
20.72
C


ATOM
153
CG
ASN
X
29
1.342
37.667
44.182
1.00
21.81
C


ATOM
154
OD1
ASN
X
29
0.556
38.399
44.769
1.00
23.20
O


ATOM
155
ND2
ASN
X
29
1.129
36.368
44.035
1.00
22.09
N


ATOM
156
C
ASN
X
29
5.067
37.807
43.123
1.00
20.50
C


ATOM
157
O
ASN
X
29
5.863
38.625
43.605
1.00
20.32
O


ATOM
158
N
LEU
X
30
5.195
37.287
41.904
1.00
20.02
N


ATOM
159
CA
LEU
X
30
6.341
37.562
41.064
1.00
20.09
C


ATOM
160
CB
LEU
X
30
7.237
36.322
40.962
1.00
19.88
C


ATOM
161
CG
LEU
X
30
8.521
36.381
40.122
1.00
19.08
C


ATOM
162
CD1
LEU
X
30
9.545
37.339
40.725
1.00
16.09
C


ATOM
163
CD2
LEU
X
30
9.115
34.973
39.968
1.00
19.47
C


ATOM
164
C
LEU
X
30
5.923
38.034
39.674
1.00
20.50
C


ATOM
165
O
LEU
X
30
5.246
37.310
38.932
1.00
20.79
O


ATOM
166
N
ASP
X
31
6.324
39.256
39.341
1.00
20.38
N


ATOM
167
CA
ASP
X
31
6.194
39.779
37.991
1.00
20.64
C


ATOM
168
CB
ASP
X
31
6.471
41.285
37.985
1.00
20.84
C


ATOM
169
CG
ASP
X
31
6.192
41.916
36.639
1.00
21.00
C


ATOM
170
OD1
ASP
X
31
7.080
41.876
35.763
1.00
20.07
O


ATOM
171
OD2
ASP
X
31
5.070
42.435
36.463
1.00
22.23
O


ATOM
172
C
ASP
X
31
7.195
39.056
37.096
1.00
20.79
C


ATOM
173
O
ASP
X
31
8.330
38.805
37.511
1.00
20.52
O


ATOM
174
N
PHE
X
32
6.785
38.717
35.874
1.00
21.02
N


ATOM
175
CA
PHE
X
32
7.645
37.926
34.984
1.00
21.44
C


ATOM
176
CB
PHE
X
32
6.906
37.497
33.695
1.00
22.33
C


ATOM
177
CG
PHE
X
32
6.743
38.594
32.666
1.00
24.17
C


ATOM
178
CD1
PHE
X
32
7.513
38.594
31.506
1.00
25.79
C


ATOM
179
CE1
PHE
X
32
7.358
39.601
30.538
1.00
25.74
C


ATOM
180
CZ
PHE
X
32
6.424
40.610
30.729
1.00
24.87
C


ATOM
181
CE2
PHE
X
32
5.637
40.619
31.880
1.00
25.78
C


ATOM
182
CD2
PHE
X
32
5.796
39.610
32.838
1.00
26.21
C


ATOM
183
C
PHE
X
32
8.992
38.603
34.693
1.00
20.92
C


ATOM
184
O
PHE
X
32
10.004
37.932
34.499
1.00
20.47
O


ATOM
185
N
GLN
X
33
9.003
39.933
34.695
1.00
20.63
N


ATOM
186
CA
GLN
X
33
10.237
40.676
34.471
1.00
20.36
C


ATOM
187
CB
GLN
X
33
9.944
42.054
33.877
1.00
20.69
C


ATOM
188
CG
GLN
X
33
9.423
42.010
32.436
1.00
20.63
C


ATOM
189
CD
GLN
X
33
9.380
43.389
31.796
1.00
20.80
C


ATOM
190
OE1
GLN
X
33
8.513
44.204
32.106
1.00
21.44
O


ATOM
191
NE2
GLN
X
33
10.330
43.658
30.909
1.00
20.99
N


ATOM
192
C
GLN
X
33
11.117
40.781
35.723
1.00
19.86
C


ATOM
193
O
GLN
X
33
12.277
41.182
35.631
1.00
20.34
O


ATOM
194
N
MET
X
34
10.579
40.393
36.878
1.00
19.10
N


ATOM
195
CA
MET
X
34
11.354
40.381
38.127
1.00
18.63
C


ATOM
196
CB
MET
X
34
10.488
40.816
39.310
1.00
18.41
C


ATOM
197
CG
MET
X
34
10.126
42.316
39.316
1.00
19.19
C


ATOM
198
SD
MET
X
34
11.552
43.413
39.463
1.00
20.47
S


ATOM
199
CE
MET
X
34
12.166
42.944
41.084
1.00
17.02
C


ATOM
200
C
MET
X
34
12.022
39.030
38.421
1.00
18.36
C


ATOM
201
O
MET
X
34
12.887
38.937
39.298
1.00
18.26
O


ATOM
202
N
GLU
X
35
11.618
37.994
37.685
1.00
17.82
N


ATOM
203
CA
GLU
X
35
12.170
36.642
37.836
1.00
17.39
C


ATOM
204
CB
GLU
X
35
11.550
35.704
36.795
1.00
17.70
C


ATOM
205
CG
GLU
X
35
12.027
34.254
36.892
1.00
17.81
C


ATOM
206
CD
GLU
X
35
11.389
33.378
35.829
1.00
17.94
C


ATOM
207
OE1
GLU
X
35
10.451
32.639
36.179
1.00
21.18
O


ATOM
208
OE2
GLU
X
35
11.800
33.454
34.647
1.00
17.38
O


ATOM
209
C
GLU
X
35
13.696
36.618
37.723
1.00
16.83
C


ATOM
210
O
GLU
X
35
14.371
35.920
38.479
1.00
16.31
O


ATOM
211
N
GLN
X
36
14.236
37.409
36.796
1.00
16.08
N


ATOM
212
CA
GLN
X
36
15.683
37.514
36.610
1.00
15.59
C


ATOM
213
CB
GLN
X
36
15.991
38.389
35.391
1.00
16.04
C


ATOM
214
CG
GLN
X
36
15.618
39.873
35.563
1.00
15.36
C


ATOM
215
CD
GLN
X
36
15.634
40.641
34.251
1.00
16.46
C


ATOM
216
OE1
GLN
X
36
14.598
41.159
33.810
1.00
19.47
O


ATOM
217
NE2
GLN
X
36
16.796
40.710
33.618
1.00
14.17
N


ATOM
218
C
GLN
X
36
16.440
38.053
37.836
1.00
15.31
C


ATOM
219
O
GLN
X
36
17.664
37.941
37.897
1.00
15.21
O


ATOM
220
N
TYR
X
37
15.718
38.622
38.802
1.00
15.03
N


ATOM
221
CA
TYR
X
37
16.348
39.258
39.966
1.00
15.39
C


ATOM
222
CB
TYR
X
37
15.865
40.705
40.128
1.00
15.46
C


ATOM
223
CG
TYR
X
37
16.080
41.585
38.917
1.00
15.82
C


ATOM
224
CD1
TYR
X
37
17.351
41.750
38.370
1.00
16.70
C


ATOM
225
CE1
TYR
X
37
17.555
42.558
37.262
1.00
16.54
C


ATOM
226
CZ
TYR
X
37
16.485
43.223
36.694
1.00
16.10
C


ATOM
227
OH
TYR
X
37
16.707
44.023
35.596
1.00
17.59
O


ATOM
228
CE2
TYR
X
37
15.213
43.085
37.213
1.00
15.68
C


ATOM
229
CD2
TYR
X
37
15.017
42.265
38.328
1.00
15.46
C


ATOM
230
C
TYR
X
37
16.137
38.515
41.290
1.00
15.38
C


ATOM
231
O
TYR
X
37
16.695
38.904
42.309
1.00
15.60
O


ATOM
232
N
ILE
X
38
15.317
37.471
41.287
1.00
15.50
N


ATOM
233
CA
ILE
X
38
15.089
36.707
42.514
1.00
15.21
C


ATOM
234
CB
ILE
X
38
13.597
36.289
42.698
1.00
15.28
C


ATOM
235
CG1
ILE
X
38
13.089
35.425
41.538
1.00
14.69
C


ATOM
236
CD1
ILE
X
38
13.431
33.960
41.673
1.00
14.29
C


ATOM
237
CG2
ILE
X
38
12.714
37.517
42.868
1.00
14.60
C


ATOM
238
C
ILE
X
38
16.072
35.529
42.607
1.00
15.56
C


ATOM
239
O
ILE
X
38
16.654
35.113
41.605
1.00
15.11
O


ATOM
240
N
TYR
X
39
16.279
35.028
43.818
1.00
15.67
N


ATOM
241
CA
TYR
X
39
17.228
33.950
44.042
1.00
15.96
C


ATOM
242
CB
TYR
X
39
18.187
34.303
45.189
1.00
16.07
C


ATOM
243
CG
TYR
X
39
19.314
33.315
45.370
1.00
16.45
C


ATOM
244
CD1
TYR
X
39
20.390
33.287
44.493
1.00
15.53
C


ATOM
245
CE1
TYR
X
39
21.435
32.370
44.652
1.00
16.33
C


ATOM
246
CZ
TYR
X
39
21.406
31.467
45.709
1.00
16.89
C


ATOM
247
OH
TYR
X
39
22.434
30.559
45.882
1.00
17.23
O


ATOM
248
CE2
TYR
X
39
20.346
31.474
46.598
1.00
18.39
C


ATOM
249
CD2
TYR
X
39
19.299
32.400
46.423
1.00
17.79
C


ATOM
250
C
TYR
X
39
16.486
32.656
44.326
1.00
16.39
C


ATOM
251
O
TYR
X
39
16.754
31.635
43.698
1.00
16.56
O


ATOM
252
N
LYS
X
40
15.538
32.709
45.255
1.00
16.77
N


ATOM
253
CA
LYS
X
40
14.749
31.542
45.619
1.00
18.18
C


ATOM
254
CB
LYS
X
40
15.553
30.572
46.508
1.00
17.81
C


ATOM
255
CG
LYS
X
40
16.002
31.115
47.861
1.00
19.20
C


ATOM
256
CD
LYS
X
40
16.748
30.032
48.639
1.00
20.03
C


ATOM
257
CE
LYS
X
40
17.819
30.608
49.544
1.00
23.88
C


ATOM
258
NZ
LYS
X
40
17.274
31.054
50.853
1.00
27.30
N


ATOM
259
C
LYS
X
40
13.452
31.939
46.301
1.00
18.48
C


ATOM
260
O
LYS
X
40
13.217
33.116
46.591
1.00
18.10
O


ATOM
261
N
ARG
X
41
12.614
30.941
46.545
1.00
19.31
N


ATOM
262
CA
ARG
X
41
11.348
31.141
47.209
1.00
20.40
C


ATOM
263
CB
ARG
X
41
10.195
30.819
46.255
1.00
20.38
C


ATOM
264
CG
ARG
X
41
8.848
31.278
46.746
1.00
20.74
C


ATOM
265
CD
ARG
X
41
7.710
30.805
45.855
1.00
21.62
C


ATOM
266
NE
ARG
X
41
6.526
31.626
46.106
1.00
22.97
N


ATOM
267
CZ
ARG
X
41
5.346
31.478
45.506
1.00
24.70
C


ATOM
268
NH1
ARG
X
41
5.158
30.515
44.604
1.00
24.36
N


ATOM
269
NH2
ARG
X
41
4.347
32.301
45.816
1.00
23.10
N


ATOM
270
C
ARG
X
41
11.316
30.246
48.441
1.00
21.24
C


ATOM
271
O
ARG
X
41
11.756
29.100
48.394
1.00
21.61
O


ATOM
272
N
LYS
X
42
10.826
30.794
49.545
1.00
22.35
N


ATOM
273
CA
LYS
X
42
10.681
30.067
50.802
1.00
23.26
C


ATOM
274
CB
LYS
X
42
10.827
31.052
51.971
1.00
23.59
C


ATOM
275
CG
LYS
X
42
12.228
31.651
52.133
1.00
25.84
C


ATOM
276
CD
LYS
X
42
13.248
30.571
52.524
1.00
27.90
C


ATOM
277
CE
LYS
X
42
14.568
31.194
52.942
1.00
30.69
C


ATOM
278
NZ
LYS
X
42
15.575
30.186
53.410
1.00
30.76
N


ATOM
279
C
LYS
X
42
9.318
29.365
50.872
1.00
23.30
C


ATOM
280
O
LYS
X
42
8.410
29.685
50.095
1.00
23.09
O


ATOM
281
N
SER
X
43
9.169
28.428
51.814
1.00
23.50
N


ATOM
282
CA
SER
X
43
7.908
27.695
51.989
1.00
23.42
C


ATOM
283
CB
SER
X
43
8.049
26.560
53.010
1.00
23.74
C


ATOM
284
OG
SER
X
43
8.248
27.068
54.317
1.00
23.90
O


ATOM
285
C
SER
X
43
6.737
28.609
52.357
1.00
23.27
C


ATOM
286
O
SER
X
43
5.589
28.311
52.011
1.00
23.41
O


ATOM
287
N
ASP
X
44
7.020
29.730
53.028
1.00
22.61
N


ATOM
288
CA
ASP
X
44
5.976
30.734
53.285
1.00
22.23
C


ATOM
289
CB
ASP
X
44
6.345
31.679
54.445
1.00
22.20
C


ATOM
290
CG
ASP
X
44
7.537
32.597
54.136
1.00
22.55
C


ATOM
291
OD1
ASP
X
44
8.189
32.457
53.077
1.00
22.52
O


ATOM
292
OD2
ASP
X
44
7.825
33.472
54.982
1.00
22.35
O


ATOM
293
C
ASP
X
44
5.568
31.518
52.033
1.00
22.07
C


ATOM
294
O
ASP
X
44
4.736
32.426
52.108
1.00
22.37
O


ATOM
295
N
GLY
X
45
6.153
31.164
50.890
1.00
21.50
N


ATOM
296
CA
GLY
X
45
5.794
31.773
49.609
1.00
21.11
C


ATOM
297
C
GLY
X
45
6.583
33.021
49.241
1.00
20.57
C


ATOM
298
O
GLY
X
45
6.484
33.503
48.117
1.00
20.80
O


ATOM
299
N
ILE
X
46
7.371
33.533
50.184
1.00
20.14
N


ATOM
300
CA
ILE
X
46
8.111
34.777
50.001
1.00
19.66
C


ATOM
301
CB
ILE
X
46
8.604
35.356
51.371
1.00
19.98
C


ATOM
302
CG1
ILE
X
46
7.420
35.761
52.259
1.00
20.97
C


ATOM
303
CD1
ILE
X
46
6.553
36.913
51.710
1.00
23.35
C


ATOM
304
CG2
ILE
X
46
9.539
36.547
51.184
1.00
20.10
C


ATOM
305
C
ILE
X
46
9.286
34.561
49.048
1.00
19.00
C


ATOM
306
O
ILE
X
46
10.089
33.643
49.238
1.00
18.99
O


ATOM
307
N
TYR
X
47
9.364
35.392
48.010
1.00
18.11
N


ATOM
308
CA
TYR
X
47
10.515
35.391
47.103
1.00
17.53
C


ATOM
309
CB
TYR
X
47
10.138
36.007
45.748
1.00
17.56
C


ATOM
310
CG
TYR
X
47
9.407
35.050
44.833
1.00
17.37
C


ATOM
311
CD1
TYR
X
47
10.105
34.085
44.108
1.00
16.49
C


ATOM
312
CE1
TYR
X
47
9.450
33.203
43.273
1.00
17.17
C


ATOM
313
CZ
TYR
X
47
8.072
33.270
43.148
1.00
17.59
C


ATOM
314
OH
TYR
X
47
7.432
32.389
42.310
1.00
18.79
O


ATOM
315
CE2
TYR
X
47
7.347
34.211
43.854
1.00
17.39
C


ATOM
316
CD2
TYR
X
47
8.023
35.101
44.698
1.00
17.42
C


ATOM
317
C
TYR
X
47
11.696
36.139
47.715
1.00
16.85
C


ATOM
318
O
TYR
X
47
11.536
37.249
48.223
1.00
17.33
O


ATOM
319
N
ILE
X
48
12.874
35.523
47.673
1.00
16.11
N


ATOM
320
CA
ILE
X
48
14.098
36.150
48.153
1.00
15.38
C


ATOM
321
CB
ILE
X
48
15.071
35.132
48.821
1.00
15.62
C


ATOM
322
CG1
ILE
X
48
14.403
34.388
49.998
1.00
15.96
C


ATOM
323
CD1
ILE
X
48
13.777
35.287
51.092
1.00
16.52
C


ATOM
324
CG2
ILE
X
48
16.367
35.813
49.263
1.00
14.67
C


ATOM
325
C
ILE
X
48
14.791
36.835
46.977
1.00
14.88
C


ATOM
326
O
ILE
X
48
15.053
36.204
45.954
1.00
14.80
O


ATOM
327
N
ILE
X
49
15.088
38.121
47.141
1.00
13.89
N


ATOM
328
CA
ILE
X
49
15.728
38.929
46.097
1.00
13.24
C


ATOM
329
CB
ILE
X
49
15.343
40.451
46.230
1.00
12.69
C


ATOM
330
CG1
ILE
X
49
13.830
40.614
46.035
1.00
13.47
C


ATOM
331
CD1
ILE
X
49
13.267
41.935
46.489
1.00
13.63
C


ATOM
332
CG2
ILE
X
49
16.090
41.313
45.203
1.00
12.29
C


ATOM
333
C
ILE
X
49
17.242
38.727
46.109
1.00
12.73
C


ATOM
334
O
ILE
X
49
17.871
38.772
47.163
1.00
12.68
O


ATOM
335
N
ASN
X
50
17.818
38.504
44.930
1.00
12.16
N


ATOM
336
CA
ASN
X
50
19.262
38.393
44.785
1.00
12.01
C


ATOM
337
CB
ASN
X
50
19.611
37.753
43.432
1.00
11.98
C


ATOM
338
CG
ASN
X
50
21.079
37.331
43.320
1.00
11.89
C


ATOM
339
OD1
ASN
X
50
21.404
36.384
42.600
1.00
15.09
O


ATOM
340
ND2
ASN
X
50
21.960
38.018
44.025
1.00
9.56
N


ATOM
341
C
ASN
X
50
19.918
39.780
44.929
1.00
12.37
C


ATOM
342
O
ASN
X
50
19.870
40.605
44.004
1.00
11.20
O


ATOM
343
N
LEU
X
51
20.538
40.004
46.090
1.00
12.23
N


ATOM
344
CA
LEU
X
51
21.182
41.277
46.440
1.00
13.15
C


ATOM
345
CB
LEU
X
51
21.624
41.252
47.902
1.00
13.20
C


ATOM
346
CG
LEU
X
51
20.766
41.890
49.001
1.00
15.03
C


ATOM
347
CD1
LEU
X
51
19.297
42.120
48.658
1.00
14.89
C


ATOM
348
CD2
LEU
X
51
20.920
41.148
50.315
1.00
15.20
C


ATOM
349
C
LEU
X
51
22.360
41.684
45.555
1.00
13.09
C


ATOM
350
O
LEU
X
51
22.717
42.860
45.495
1.00
13.04
O


ATOM
351
N
LYS
X
52
22.975
40.721
44.882
1.00
13.36
N


ATOM
352
CA
LYS
X
52
23.986
41.046
43.876
1.00
14.10
C


ATOM
353
CB
LYS
X
52
24.653
39.779
43.329
1.00
14.53
C


ATOM
354
CG
LYS
X
52
25.619
39.113
44.309
1.00
16.50
C


ATOM
355
CD
LYS
X
52
25.517
37.577
44.252
1.00
20.60
C


ATOM
356
CE
LYS
X
52
26.405
36.971
43.201
1.00
22.69
C


ATOM
357
NZ
LYS
X
52
26.297
35.476
43.131
1.00
23.72
N


ATOM
358
C
LYS
X
52
23.349
41.867
42.745
1.00
13.64
C


ATOM
359
O
LYS
X
52
23.946
42.828
42.260
1.00
13.63
O


ATOM
360
N
ARG
X
53
22.130
41.497
42.353
1.00
13.36
N


ATOM
361
CA
ARG
X
53
21.369
42.255
41.355
1.00
13.56
C


ATOM
362
CB
ARG
X
53
20.117
41.489
40.896
1.00
13.45
C


ATOM
363
CG
ARG
X
53
20.372
40.050
40.410
1.00
14.27
C


ATOM
364
CD
ARG
X
53
21.123
40.001
39.089
1.00
16.18
C


ATOM
365
NE
ARG
X
53
22.574
40.044
39.260
1.00
18.49
N


ATOM
366
CZ
ARG
X
53
23.343
38.984
39.506
1.00
20.09
C


ATOM
367
NH1
ARG
X
53
22.810
37.774
39.625
1.00
21.57
N


ATOM
368
NH2
ARG
X
53
24.657
39.135
39.639
1.00
21.70
N


ATOM
369
C
ARG
X
53
20.980
43.631
41.891
1.00
13.43
C


ATOM
370
O
ARG
X
53
21.130
44.629
41.187
1.00
14.11
O


ATOM
371
N
THR
X
54
20.478
43.677
43.125
1.00
13.10
N


ATOM
372
CA
THR
X
54
20.211
44.945
43.823
1.00
12.92
C


ATOM
373
CB
THR
X
54
19.922
44.718
45.334
1.00
12.81
C


ATOM
374
OG1
THR
X
54
18.834
43.803
45.479
1.00
11.60
O


ATOM
375
CG2
THR
X
54
19.571
46.037
46.059
1.00
12.38
C


ATOM
376
C
THR
X
54
21.408
45.885
43.660
1.00
13.18
C


ATOM
377
O
THR
X
54
21.251
47.019
43.188
1.00
13.06
O


ATOM
378
N
TRP
X
55
22.597
45.386
44.007
1.00
13.14
N


ATOM
379
CA
TRP
X
55
23.834
46.177
43.975
1.00
13.60
C


ATOM
380
CB
TRP
X
55
24.991
45.418
44.642
1.00
14.08
C


ATOM
381
CG
TRP
X
55
26.302
46.143
44.585
1.00
14.58
C


ATOM
382
CD1
TRP
X
55
27.410
45.786
43.866
1.00
15.56
C


ATOM
383
NE1
TRP
X
55
28.417
46.699
44.063
1.00
15.28
N


ATOM
384
CE2
TRP
X
55
27.976
47.669
44.925
1.00
15.31
C


ATOM
385
CD2
TRP
X
55
26.643
47.351
45.276
1.00
15.17
C


ATOM
386
CE3
TRP
X
55
25.948
48.199
46.155
1.00
15.54
C


ATOM
387
CZ3
TRP
X
55
26.600
49.324
46.650
1.00
15.72
C


ATOM
388
CH2
TRP
X
55
27.932
49.617
46.275
1.00
15.84
C


ATOM
389
CZ2
TRP
X
55
28.631
48.803
45.416
1.00
15.28
C


ATOM
390
C
TRP
X
55
24.232
46.637
42.572
1.00
13.85
C


ATOM
391
O
TRP
X
55
24.554
47.807
42.382
1.00
13.66
O


ATOM
392
N
GLU
X
56
24.210
45.717
41.606
1.00
14.15
N


ATOM
393
CA
GLU
X
56
24.508
46.040
40.204
1.00
15.20
C


ATOM
394
CB
GLU
X
56
24.413
44.790
39.326
1.00
15.32
C


ATOM
395
CG
GLU
X
56
25.568
43.814
39.528
1.00
18.48
C


ATOM
396
CD
GLU
X
56
25.240
42.386
39.086
1.00
22.64
C


ATOM
397
OE1
GLU
X
56
24.247
42.186
38.337
1.00
22.16
O


ATOM
398
OE2
GLU
X
56
25.995
41.466
39.485
1.00
23.38
O


ATOM
399
C
GLU
X
56
23.595
47.133
39.641
1.00
15.01
C


ATOM
400
O
GLU
X
56
24.061
48.052
38.966
1.00
15.02
O


ATOM
401
N
LYS
X
57
22.300
47.024
39.929
1.00
15.07
N


ATOM
402
CA
LYS
X
57
21.301
47.966
39.421
1.00
15.43
C


ATOM
403
CB
LYS
X
57
19.895
47.381
39.561
1.00
15.35
C


ATOM
404
CG
LYS
X
57
19.644
46.192
38.645
1.00
16.72
C


ATOM
405
CD
LYS
X
57
20.010
46.521
37.202
1.00
17.47
C


ATOM
406
CE
LYS
X
57
19.612
45.391
36.285
1.00
19.69
C


ATOM
407
NZ
LYS
X
57
20.159
45.554
34.911
1.00
21.09
N


ATOM
408
C
LYS
X
57
21.389
49.322
40.110
1.00
15.45
C


ATOM
409
O
LYS
X
57
21.097
50.357
39.513
1.00
15.28
O


ATOM
410
N
LEU
X
58
21.802
49.304
41.370
1.00
15.48
N


ATOM
411
CA
LEU
X
58
22.019
50.522
42.121
1.00
16.23
C


ATOM
412
CB
LEU
X
58
22.405
50.146
43.543
1.00
17.25
C


ATOM
413
CG
LEU
X
58
21.910
50.978
44.706
1.00
19.86
C


ATOM
414
CD1
LEU
X
58
21.822
50.054
45.930
1.00
21.77
C


ATOM
415
CD2
LEU
X
58
22.918
52.098
44.920
1.00
23.61
C


ATOM
416
C
LEU
X
58
23.135
51.343
41.465
1.00
15.84
C


ATOM
417
O
LEU
X
58
23.023
52.564
41.329
1.00
15.44
O


ATOM
418
N
LEU
X
59
24.197
50.650
41.050
1.00
15.30
N


ATOM
419
CA
LEU
X
59
25.343
51.274
40.381
1.00
15.32
C


ATOM
420
CB
LEU
X
59
26.525
50.298
40.299
1.00
15.39
C


ATOM
421
CG
LEU
X
59
27.225
49.909
41.609
1.00
16.30
C


ATOM
422
CD1
LEU
X
59
28.361
48.954
41.304
1.00
17.87
C


ATOM
423
CD2
LEU
X
59
27.759
51.147
42.346
1.00
17.69
C


ATOM
424
C
LEU
X
59
24.984
51.781
38.990
1.00
14.82
C


ATOM
425
O
LEU
X
59
25.414
52.862
38.596
1.00
14.71
O


ATOM
426
N
LEU
X
60
24.200
50.990
38.258
1.00
14.35
N


ATOM
427
CA
LEU
X
60
23.679
51.394
36.956
1.00
14.01
C


ATOM
428
CB
LEU
X
60
22.914
50.241
36.303
1.00
14.39
C


ATOM
429
CG
LEU
X
60
22.455
50.460
34.858
1.00
16.16
C


ATOM
430
CD1
LEU
X
60
23.637
50.340
33.877
1.00
18.26
C


ATOM
431
CD2
LEU
X
60
21.356
49.482
34.489
1.00
18.54
C


ATOM
432
C
LEU
X
60
22.786
52.642
37.079
1.00
13.61
C


ATOM
433
O
LEU
X
60
22.914
53.578
36.287
1.00
13.71
O


ATOM
434
N
ALA
X
61
21.897
52.655
38.073
1.00
12.97
N


ATOM
435
CA
ALA
X
61
21.060
53.822
38.350
1.00
13.04
C


ATOM
436
CB
ALA
X
61
20.036
53.513
39.434
1.00
12.61
C


ATOM
437
C
ALA
X
61
21.877
55.066
38.719
1.00
13.02
C


ATOM
438
O
ALA
X
61
21.594
56.151
38.222
1.00
13.00
O


ATOM
439
N
ALA
X
62
22.885
54.898
39.578
1.00
13.18
N


ATOM
440
CA
ALA
X
62
23.757
56.007
40.009
1.00
13.51
C


ATOM
441
CB
ALA
X
62
24.732
55.538
41.105
1.00
12.76
C


ATOM
442
C
ALA
X
62
24.520
56.616
38.831
1.00
13.73
C


ATOM
443
O
ALA
X
62
24.645
57.834
38.728
1.00
14.07
O


ATOM
444
N
ARG
X
63
25.010
55.752
37.946
1.00
14.22
N


ATOM
445
CA
ARG
X
63
25.668
56.151
36.709
1.00
15.34
C


ATOM
446
CB
ARG
X
63
26.095
54.903
35.946
1.00
15.87
C


ATOM
447
CG
ARG
X
63
27.355
55.055
35.133
1.00
20.75
C


ATOM
448
CD
ARG
X
63
27.822
53.685
34.630
1.00
27.61
C


ATOM
449
NE
ARG
X
63
28.044
52.743
35.733
1.00
31.32
N


ATOM
450
CZ
ARG
X
63
27.836
51.430
35.658
1.00
33.90
C


ATOM
451
NH1
ARG
X
63
27.385
50.879
34.533
1.00
35.78
N


ATOM
452
NH2
ARG
X
63
28.070
50.662
36.714
1.00
34.66
N


ATOM
453
C
ARG
X
63
24.760
57.011
35.836
1.00
14.90
C


ATOM
454
O
ARG
X
63
25.177
58.068
35.357
1.00
15.56
O


ATOM
455
N
ALA
X
64
23.520
56.561
35.647
1.00
14.15
N


ATOM
456
CA
ALA
X
64
22.511
57.289
34.861
1.00
13.71
C


ATOM
457
CB
ALA
X
64
21.251
56.435
34.699
1.00
13.54
C


ATOM
458
C
ALA
X
64
22.148
58.638
35.478
1.00
13.18
C


ATOM
459
O
ALA
X
64
21.916
59.619
34.766
1.00
12.87
O


ATOM
460
N
ILE
X
65
22.079
58.668
36.804
1.00
12.69
N


ATOM
461
CA
ILE
X
65
21.784
59.892
37.550
1.00
12.18
C


ATOM
462
CB
ILE
X
65
21.468
59.566
39.040
1.00
12.27
C


ATOM
463
CG1
ILE
X
65
20.078
58.909
39.159
1.00
11.23
C


ATOM
464
CD1
ILE
X
65
19.843
58.174
40.493
1.00
11.69
C


ATOM
465
CG2
ILE
X
65
21.583
60.823
39.921
1.00
10.47
C


ATOM
466
C
ILE
X
65
22.939
60.897
37.416
1.00
12.50
C


ATOM
467
O
ILE
X
65
22.713
62.084
37.162
1.00
12.85
O


ATOM
468
N
VAL
X
66
24.166
60.401
37.544
1.00
12.58
N


ATOM
469
CA
VAL
X
66
25.378
61.223
37.451
1.00
12.76
C


ATOM
470
CB
VAL
X
66
26.639
60.425
37.937
1.00
12.82
C


ATOM
471
CG1
VAL
X
66
27.954
61.116
37.565
1.00
14.01
C


ATOM
472
CG2
VAL
X
66
26.581
60.210
39.452
1.00
12.58
C


ATOM
473
C
VAL
X
66
25.555
61.847
36.047
1.00
13.21
C


ATOM
474
O
VAL
X
66
26.067
62.965
35.925
1.00
13.31
O


ATOM
475
N
ALA
X
67
25.104
61.139
35.007
1.00
13.01
N


ATOM
476
CA
ALA
X
67
25.190
61.637
33.630
1.00
13.38
C


ATOM
477
CB
ALA
X
67
24.905
60.515
32.623
1.00
12.82
C


ATOM
478
C
ALA
X
67
24.307
62.863
33.336
1.00
13.48
C


ATOM
479
O
ALA
X
67
24.474
63.505
32.300
1.00
14.15
O


ATOM
480
N
ILE
X
68
23.368
63.168
34.225
1.00
13.54
N


ATOM
481
CA
ILE
X
68
22.514
64.349
34.071
1.00
13.57
C


ATOM
482
CB
ILE
X
68
21.162
64.209
34.824
1.00
13.49
C


ATOM
483
CG1
ILE
X
68
20.448
62.901
34.446
1.00
12.37
C


ATOM
484
CD1
ILE
X
68
20.133
62.737
32.955
1.00
11.55
C


ATOM
485
CG2
ILE
X
68
20.266
65.423
34.558
1.00
13.63
C


ATOM
486
C
ILE
X
68
23.281
65.566
34.573
1.00
13.94
C


ATOM
487
O
ILE
X
68
23.572
65.677
35.769
1.00
13.16
O


ATOM
488
N
GLU
X
69
23.595
66.466
33.639
1.00
14.41
N


ATOM
489
CA
GLU
X
69
24.566
67.544
33.850
1.00
15.27
C


ATOM
490
CB
GLU
X
69
24.909
68.221
32.518
1.00
15.50
C


ATOM
491
CG
GLU
X
69
25.639
67.334
31.504
1.00
16.60
C


ATOM
492
CD
GLU
X
69
24.703
66.604
30.543
1.00
17.99
C


ATOM
493
OE1
GLU
X
69
23.567
66.236
30.933
1.00
19.61
O


ATOM
494
OE2
GLU
X
69
25.109
66.388
29.384
1.00
18.22
O


ATOM
495
C
GLU
X
69
24.121
68.584
34.886
1.00
15.47
C


ATOM
496
O
GLU
X
69
24.940
69.068
35.672
1.00
15.95
O


ATOM
497
N
ASN
X
70
22.836
68.933
34.882
1.00
15.17
N


ATOM
498
CA
ASN
X
70
22.275
69.751
35.949
1.00
15.17
C


ATOM
499
CB
ASN
X
70
21.362
70.836
35.367
1.00
15.33
C


ATOM
500
CG
ASN
X
70
20.632
71.646
36.432
1.00
15.56
C


ATOM
501
OD1
ASN
X
70
20.926
71.565
37.620
1.00
15.17
O


ATOM
502
ND2
ASN
X
70
19.676
72.446
35.993
1.00
17.62
N


ATOM
503
C
ASN
X
70
21.544
68.860
36.967
1.00
14.90
C


ATOM
504
O
ASN
X
70
20.503
68.285
36.650
1.00
14.79
O


ATOM
505
N
PRO
X
71
22.089
68.753
38.198
1.00
14.79
N


ATOM
506
CA
PRO
X
71
21.547
67.844
39.229
1.00
14.65
C


ATOM
507
CB
PRO
X
71
22.345
68.215
40.485
1.00
14.84
C


ATOM
508
CG
PRO
X
71
23.598
68.814
39.977
1.00
15.24
C


ATOM
509
CD
PRO
X
71
23.256
69.508
38.692
1.00
14.41
C


ATOM
510
C
PRO
X
71
20.048
68.032
39.488
1.00
14.30
C


ATOM
511
O
PRO
X
71
19.350
67.070
39.814
1.00
13.78
O


ATOM
512
N
ALA
X
72
19.561
69.261
39.327
1.00
14.03
N


ATOM
513
CA
ALA
X
72
18.148
69.576
39.557
1.00
13.57
C


ATOM
514
CB
ALA
X
72
17.938
71.093
39.614
1.00
13.64
C


ATOM
515
C
ALA
X
72
17.210
68.940
38.529
1.00
13.40
C


ATOM
516
O
ALA
X
72
16.008
68.825
38.781
1.00
13.23
O


ATOM
517
N
ASP
X
73
17.762
68.539
37.379
1.00
13.19
N


ATOM
518
CA
ASP
X
73
16.992
67.870
36.320
1.00
13.44
C


ATOM
519
CB
ASP
X
73
17.671
68.055
34.960
1.00
13.55
C


ATOM
520
CG
ASP
X
73
17.528
69.477
34.437
1.00
14.70
C


ATOM
521
OD1
ASP
X
73
16.559
70.147
34.841
1.00
16.45
O


ATOM
522
OD2
ASP
X
73
18.368
69.922
33.628
1.00
15.65
O


ATOM
523
C
ASP
X
73
16.697
66.387
36.591
1.00
13.25
C


ATOM
524
O
ASP
X
73
16.021
65.727
35.797
1.00
13.01
O


ATOM
525
N
VAL
X
74
17.209
65.880
37.711
1.00
12.99
N


ATOM
526
CA
VAL
X
74
16.795
64.586
38.237
1.00
12.95
C


ATOM
527
CB
VAL
X
74
17.971
63.819
38.895
1.00
13.13
C


ATOM
528
CG1
VAL
X
74
17.539
62.414
39.346
1.00
12.75
C


ATOM
529
CG2
VAL
X
74
19.169
63.731
37.938
1.00
12.47
C


ATOM
530
C
VAL
X
74
15.671
64.841
39.251
1.00
13.27
C


ATOM
531
O
VAL
X
74
15.836
65.580
40.226
1.00
13.05
O


ATOM
532
N
SER
X
75
14.517
64.245
38.997
1.00
13.48
N


ATOM
533
CA
SER
X
75
13.410
64.310
39.943
1.00
14.21
C


ATOM
534
CB
SER
X
75
12.126
64.728
39.231
1.00
13.94
C


ATOM
535
OG
SER
X
75
10.986
64.155
39.843
1.00
17.96
O


ATOM
536
C
SER
X
75
13.266
62.989
40.705
1.00
13.94
C


ATOM
537
O
SER
X
75
13.394
61.896
40.128
1.00
13.38
O


ATOM
538
N
VAL
X
76
13.060
63.104
42.015
1.00
14.01
N


ATOM
539
CA
VAL
X
76
13.006
61.945
42.903
1.00
14.17
C


ATOM
540
CB
VAL
X
76
14.258
61.840
43.833
1.00
14.24
C


ATOM
541
CG1
VAL
X
76
15.510
61.544
43.024
1.00
13.27
C


ATOM
542
CG2
VAL
X
76
14.470
63.113
44.659
1.00
14.71
C


ATOM
543
C
VAL
X
76
11.697
61.946
43.688
1.00
14.94
C


ATOM
544
O
VAL
X
76
11.314
62.960
44.290
1.00
15.09
O


ATOM
545
N
ILE
X
77
11.014
60.806
43.674
1.00
15.08
N


ATOM
546
CA
ILE
X
77
9.609
60.757
44.050
1.00
16.01
C


ATOM
547
CB
ILE
X
77
8.717
60.627
42.769
1.00
16.14
C


ATOM
548
CG1
ILE
X
77
8.608
61.995
42.082
1.00
16.19
C


ATOM
549
CD1
ILE
X
77
7.766
62.027
40.836
1.00
16.94
C


ATOM
550
CG2
ILE
X
77
7.342
60.053
43.094
1.00
16.76
C


ATOM
551
C
ILE
X
77
9.261
59.679
45.088
1.00
16.04
C


ATOM
552
O
ILE
X
77
9.762
58.556
45.028
1.00
15.42
O


ATOM
553
N
SER
X
78
8.418
60.062
46.051
1.00
16.33
N


ATOM
554
CA
SER
X
78
7.701
59.114
46.899
1.00
16.87
C


ATOM
555
CB
SER
X
78
8.521
58.707
48.128
1.00
16.62
C


ATOM
556
OG
SER
X
78
7.830
57.701
48.858
1.00
16.57
O


ATOM
557
C
SER
X
78
6.358
59.684
47.346
1.00
17.55
C


ATOM
558
O
SER
X
78
6.314
60.640
48.124
1.00
17.61
O


ATOM
559
N
SER
X
79
5.267
59.096
46.858
1.00
18.08
N


ATOM
560
CA
SER
X
79
3.942
59.458
47.347
1.00
19.01
C


ATOM
561
CB
SER
X
79
2.848
58.949
46.405
1.00
18.84
C


ATOM
562
OG
SER
X
79
2.953
57.547
46.234
1.00
19.69
O


ATOM
563
C
SER
X
79
3.743
58.903
48.759
1.00
19.52
C


ATOM
564
O
SER
X
79
3.237
59.598
49.640
1.00
19.93
O


ATOM
565
N
ARG
X
80
4.157
57.651
48.964
1.00
19.99
N


ATOM
566
CA
ARG
X
80
4.089
57.001
50.271
1.00
20.49
C


ATOM
567
CB
ARG
X
80
4.571
55.554
50.179
1.00
20.42
C


ATOM
568
CG
ARG
X
80
3.621
54.609
49.468
1.00
21.68
C


ATOM
569
CD
ARG
X
80
4.310
53.283
49.195
1.00
22.90
C


ATOM
570
NE
ARG
X
80
4.730
52.633
50.438
1.00
23.52
N


ATOM
571
CZ
ARG
X
80
5.811
51.863
50.565
1.00
23.95
C


ATOM
572
NH1
ARG
X
80
6.602
51.639
49.520
1.00
23.31
N


ATOM
573
NH2
ARG
X
80
6.101
51.320
51.743
1.00
22.97
N


ATOM
574
C
ARG
X
80
4.940
57.717
51.299
1.00
20.48
C


ATOM
575
O
ARG
X
80
6.076
58.110
51.005
1.00
20.45
O


ATOM
576
N
ASN
X
81
4.396
57.853
52.507
1.00
20.64
N


ATOM
577
CA
ASN
X
81
5.142
58.389
53.654
1.00
21.24
C


ATOM
578
CB
ASN
X
81
4.277
58.390
54.934
1.00
21.91
C


ATOM
579
CG
ASN
X
81
3.675
57.020
55.258
1.00
24.36
C


ATOM
580
OD1
ASN
X
81
3.899
56.027
54.548
1.00
26.64
O


ATOM
581
ND2
ASN
X
81
2.888
56.964
56.344
1.00
27.50
N


ATOM
582
C
ASN
X
81
6.472
57.678
53.901
1.00
20.73
C


ATOM
583
O
ASN
X
81
7.453
58.306
54.297
1.00
20.84
O


ATOM
584
N
THR
X
82
6.485
56.371
53.637
1.00
20.42
N


ATOM
585
CA
THR
X
82
7.645
55.499
53.820
1.00
20.15
C


ATOM
586
CB
THR
X
82
7.341
54.095
53.257
1.00
20.31
C


ATOM
587
OG1
THR
X
82
6.038
53.671
53.690
1.00
20.62
O


ATOM
588
CG2
THR
X
82
8.378
53.085
53.707
1.00
20.00
C


ATOM
589
C
THR
X
82
8.927
56.034
53.165
1.00
19.82
C


ATOM
590
O
THR
X
82
10.017
55.909
53.730
1.00
20.22
O


ATOM
591
N
GLY
X
83
8.799
56.636
51.984
1.00
19.24
N


ATOM
592
CA
GLY
X
83
9.968
57.147
51.264
1.00
18.71
C


ATOM
593
C
GLY
X
83
10.131
58.655
51.220
1.00
18.35
C


ATOM
594
O
GLY
X
83
11.050
59.160
50.577
1.00
18.24
O


ATOM
595
N
GLN
X
84
9.248
59.385
51.901
1.00
18.52
N


ATOM
596
CA
GLN
X
84
9.240
60.849
51.791
1.00
18.57
C


ATOM
597
CB
GLN
X
84
7.937
61.456
52.333
1.00
18.49
C


ATOM
598
CG
GLN
X
84
6.709
61.203
51.438
1.00
18.33
C


ATOM
599
CD
GLN
X
84
5.432
61.846
51.970
1.00
19.54
C


ATOM
600
OE1
GLN
X
84
5.485
62.836
52.698
1.00
22.21
O


ATOM
601
NE2
GLN
X
84
4.277
61.289
51.603
1.00
19.68
N


ATOM
602
C
GLN
X
84
10.487
61.486
52.413
1.00
18.38
C


ATOM
603
O
GLN
X
84
11.149
62.299
51.774
1.00
18.47
O


ATOM
604
N
ARG
X
85
10.827
61.097
53.639
1.00
18.38
N


ATOM
605
CA
ARG
X
85
12.042
61.608
54.287
1.00
18.16
C


ATOM
606
CB
ARG
X
85
12.153
61.069
55.714
1.00
18.58
C


ATOM
607
CG
ARG
X
85
13.389
61.544
56.468
1.00
21.55
C


ATOM
608
CD
ARG
X
85
13.255
61.267
57.955
1.00
26.37
C


ATOM
609
NE
ARG
X
85
14.539
61.396
58.636
1.00
30.42
N


ATOM
610
CZ
ARG
X
85
15.000
62.517
59.181
1.00
33.44
C


ATOM
611
NH1
ARG
X
85
14.275
63.637
59.144
1.00
34.31
N


ATOM
612
NH2
ARG
X
85
16.194
62.514
59.771
1.00
34.23
N


ATOM
613
C
ARG
X
85
13.289
61.250
53.474
1.00
17.61
C


ATOM
614
O
ARG
X
85
14.173
62.093
53.271
1.00
17.47
O


ATOM
615
N
ALA
X
86
13.336
60.001
53.006
1.00
16.99
N


ATOM
616
CA
ALA
X
86
14.429
59.496
52.176
1.00
16.60
C


ATOM
617
CB
ALA
X
86
14.199
58.028
51.844
1.00
16.58
C


ATOM
618
C
ALA
X
86
14.646
60.312
50.896
1.00
16.51
C


ATOM
619
O
ALA
X
86
15.781
60.671
50.588
1.00
16.15
O


ATOM
620
N
VAL
X
87
13.577
60.603
50.147
1.00
16.60
N


ATOM
621
CA
VAL
X
87
13.745
61.381
48.899
1.00
16.58
C


ATOM
622
CB
VAL
X
87
12.530
61.292
47.907
1.00
16.59
C


ATOM
623
CG1
VAL
X
87
12.280
59.849
47.481
1.00
16.75
C


ATOM
624
CG2
VAL
X
87
11.262
61.918
48.475
1.00
17.46
C


ATOM
625
C
VAL
X
87
14.157
62.833
49.178
1.00
16.27
C


ATOM
626
O
VAL
X
87
14.949
63.404
48.442
1.00
15.37
O


ATOM
627
N
LEU
X
88
13.633
63.401
50.264
1.00
16.52
N


ATOM
628
CA
LEU
X
88
14.032
64.735
50.720
1.00
16.66
C


ATOM
629
CB
LEU
X
88
13.129
65.222
51.870
1.00
16.75
C


ATOM
630
CG
LEU
X
88
11.665
65.514
51.490
1.00
17.60
C


ATOM
631
CD1
LEU
X
88
10.788
65.714
52.728
1.00
18.52
C


ATOM
632
CD2
LEU
X
88
11.546
66.726
50.558
1.00
17.78
C


ATOM
633
C
LEU
X
88
15.511
64.790
51.099
1.00
16.61
C


ATOM
634
O
LEU
X
88
16.208
65.740
50.731
1.00
16.55
O


ATOM
635
N
LYS
X
89
15.990
63.761
51.802
1.00
16.68
N


ATOM
636
CA
LYS
X
89
17.409
63.653
52.162
1.00
17.00
C


ATOM
637
CB
LYS
X
89
17.630
62.549
53.213
1.00
17.52
C


ATOM
638
CG
LYS
X
89
17.007
62.819
54.594
1.00
19.55
C


ATOM
639
CD
LYS
X
89
17.681
63.987
55.327
1.00
24.32
C


ATOM
640
CE
LYS
X
89
18.978
63.552
56.009
1.00
27.24
C


ATOM
641
NZ
LYS
X
89
19.928
64.695
56.235
1.00
29.88
N


ATOM
642
C
LYS
X
89
18.293
63.398
50.929
1.00
16.68
C


ATOM
643
O
LYS
X
89
19.349
64.012
50.782
1.00
16.41
O


ATOM
644
N
PHE
X
90
17.853
62.501
50.044
1.00
16.21
N


ATOM
645
CA
PHE
X
90
18.581
62.222
48.796
1.00
15.79
C


ATOM
646
CB
PHE
X
90
17.848
61.167
47.950
1.00
14.97
C


ATOM
647
CG
PHE
X
90
18.538
60.845
46.644
1.00
14.54
C


ATOM
648
CD1
PHE
X
90
18.347
61.648
45.518
1.00
13.59
C


ATOM
649
CE1
PHE
X
90
18.988
61.358
44.308
1.00
13.40
C


ATOM
650
CZ
PHE
X
90
19.825
60.253
44.211
1.00
13.33
C


ATOM
651
CE2
PHE
X
90
20.027
59.442
45.326
1.00
13.79
C


ATOM
652
CD2
PHE
X
90
19.377
59.735
46.537
1.00
13.59
C


ATOM
653
C
PHE
X
90
18.750
63.513
47.997
1.00
15.78
C


ATOM
654
O
PHE
X
90
19.836
63.799
47.489
1.00
15.87
O


ATOM
655
N
ALA
X
91
17.671
64.284
47.893
1.00
15.93
N


ATOM
656
CA
ALA
X
91
17.677
65.534
47.133
1.00
16.60
C


ATOM
657
CB
ALA
X
91
16.265
66.091
47.005
1.00
16.62
C


ATOM
658
C
ALA
X
91
18.623
66.575
47.729
1.00
16.94
C


ATOM
659
O
ALA
X
91
19.407
67.184
47.001
1.00
17.28
O


ATOM
660
N
ALA
X
92
18.564
66.759
49.048
1.00
17.44
N


ATOM
661
CA
ALA
X
92
19.494
67.657
49.754
1.00
17.93
C


ATOM
662
CB
ALA
X
92
19.179
67.698
51.252
1.00
18.27
C


ATOM
663
C
ALA
X
92
20.946
67.254
49.529
1.00
18.02
C


ATOM
664
O
ALA
X
92
21.815
68.112
49.327
1.00
18.62
O


ATOM
665
N
ALA
X
93
21.200
65.947
49.534
1.00
17.75
N


ATOM
666
CA
ALA
X
93
22.553
65.420
49.377
1.00
17.34
C


ATOM
667
CB
ALA
X
93
22.613
63.982
49.878
1.00
17.36
C


ATOM
668
C
ALA
X
93
23.115
65.516
47.957
1.00
17.08
C


ATOM
669
O
ALA
X
93
24.318
65.681
47.773
1.00
17.15
O


ATOM
670
N
THR
X
94
22.249
65.406
46.954
1.00
17.27
N


ATOM
671
CA
THR
X
94
22.704
65.254
45.565
1.00
16.60
C


ATOM
672
CB
THR
X
94
22.144
63.967
44.917
1.00
16.86
C


ATOM
673
OG1
THR
X
94
20.719
64.076
44.788
1.00
14.77
O


ATOM
674
CG2
THR
X
94
22.513
62.729
45.739
1.00
16.99
C


ATOM
675
C
THR
X
94
22.361
66.424
44.643
1.00
16.72
C


ATOM
676
O
THR
X
94
22.928
66.536
43.556
1.00
16.53
O


ATOM
677
N
GLY
X
95
21.428
67.272
45.070
1.00
16.73
N


ATOM
678
CA
GLY
X
95
20.979
68.408
44.262
1.00
16.94
C


ATOM
679
C
GLY
X
95
19.783
68.106
43.369
1.00
17.04
C


ATOM
680
O
GLY
X
95
19.370
68.953
42.570
1.00
16.56
O


ATOM
681
N
ALA
X
96
19.230
66.898
43.505
1.00
16.94
N


ATOM
682
CA
ALA
X
96
18.031
66.484
42.766
1.00
16.84
C


ATOM
683
CB
ALA
X
96
17.851
64.970
42.864
1.00
16.42
C


ATOM
684
C
ALA
X
96
16.775
67.207
43.278
1.00
16.99
C


ATOM
685
O
ALA
X
96
16.772
67.750
44.382
1.00
16.89
O


ATOM
686
N
THR
X
97
15.712
67.203
42.476
1.00
16.97
N


ATOM
687
CA
THR
X
97
14.460
67.872
42.839
1.00
17.29
C


ATOM
688
CB
THR
X
97
13.852
68.646
41.629
1.00
17.32
C


ATOM
689
OG1
THR
X
97
14.832
69.545
41.097
1.00
16.92
O


ATOM
690
CG2
THR
X
97
12.619
69.448
42.043
1.00
17.35
C


ATOM
691
C
THR
X
97
13.457
66.857
43.380
1.00
17.63
C


ATOM
692
O
THR
X
97
13.065
65.942
42.657
1.00
17.32
O


ATOM
693
N
PRO
X
98
13.041
67.010
44.657
1.00
17.99
N


ATOM
694
CA
PRO
X
98
12.136
66.017
45.229
1.00
18.76
C


ATOM
695
CB
PRO
X
98
12.488
66.052
46.719
1.00
18.80
C


ATOM
696
CG
PRO
X
98
12.880
67.521
46.972
1.00
18.29
C


ATOM
697
CD
PRO
X
98
13.380
68.074
45.631
1.00
18.26
C


ATOM
698
C
PRO
X
98
10.658
66.350
45.042
1.00
19.44
C


ATOM
699
O
PRO
X
98
10.273
67.522
45.071
1.00
19.77
O


ATOM
700
N
ILE
X
99
9.843
65.317
44.846
1.00
19.98
N


ATOM
701
CA
ILE
X
99
8.400
65.440
45.017
1.00
20.65
C


ATOM
702
CB
ILE
X
99
7.605
65.276
43.696
1.00
20.55
C


ATOM
703
CG1
ILE
X
99
8.132
66.222
42.608
1.00
20.58
C


ATOM
704
CD1
ILE
X
99
7.378
66.115
41.267
1.00
21.08
C


ATOM
705
CG2
ILE
X
99
6.112
65.513
43.949
1.00
20.67
C


ATOM
706
C
ILE
X
99
7.949
64.406
46.042
1.00
20.95
C


ATOM
707
O
ILE
X
99
7.700
63.239
45.710
1.00
21.31
O


ATOM
708
N
ALA
X
100
7.869
64.844
47.295
1.00
21.40
N


ATOM
709
CA
ALA
X
100
7.403
64.010
48.397
1.00
21.67
C


ATOM
710
CB
ALA
X
100
8.216
64.307
49.662
1.00
21.55
C


ATOM
711
C
ALA
X
100
5.925
64.281
48.640
1.00
21.93
C


ATOM
712
O
ALA
X
100
5.504
65.439
48.737
1.00
22.20
O


ATOM
713
N
GLY
X
101
5.140
63.216
48.738
1.00
22.03
N


ATOM
714
CA
GLY
X
101
3.711
63.346
48.965
1.00
22.51
C


ATOM
715
C
GLY
X
101
2.942
63.342
47.658
1.00
22.75
C


ATOM
716
O
GLY
X
101
3.298
62.620
46.724
1.00
22.69
O


ATOM
717
N
ARG
X
102
1.894
64.160
47.588
1.00
22.86
N


ATOM
718
CA
ARG
X
102
0.992
64.146
46.437
1.00
23.05
C


ATOM
719
CB
ARG
X
102
−0.275
64.963
46.702
1.00
23.67
C


ATOM
720
CG
ARG
X
102
−1.432
64.587
45.760
1.00
27.17
C


ATOM
721
CD
ARG
X
102
−2.557
65.621
45.778
1.00
33.00
C


ATOM
722
NE
ARG
X
102
−3.551
65.360
44.731
1.00
36.11
N


ATOM
723
CZ
ARG
X
102
−3.790
66.168
43.700
1.00
37.86
C


ATOM
724
NH1
ARG
X
102
−3.115
67.310
43.565
1.00
38.62
N


ATOM
725
NH2
ARG
X
102
−4.714
65.835
42.804
1.00
38.84
N


ATOM
726
C
ARG
X
102
1.663
64.616
45.156
1.00
22.14
C


ATOM
727
O
ARG
X
102
2.343
65.634
45.128
1.00
22.60
O


ATOM
728
N
PHE
X
103
1.474
63.843
44.100
1.00
21.51
N


ATOM
729
CA
PHE
X
103
1.874
64.238
42.764
1.00
20.69
C


ATOM
730
CB
PHE
X
103
2.571
63.064
42.064
1.00
20.07
C


ATOM
731
CG
PHE
X
103
3.002
63.348
40.647
1.00
19.32
C


ATOM
732
CD1
PHE
X
103
2.163
63.055
39.575
1.00
17.50
C


ATOM
733
CE1
PHE
X
103
2.565
63.302
38.269
1.00
17.80
C


ATOM
734
CZ
PHE
X
103
3.819
63.844
38.021
1.00
18.07
C


ATOM
735
CE2
PHE
X
103
4.662
64.143
39.085
1.00
17.29
C


ATOM
736
CD2
PHE
X
103
4.256
63.889
40.384
1.00
17.28
C


ATOM
737
C
PHE
X
103
0.579
64.626
42.058
1.00
20.64
C


ATOM
738
O
PHE
X
103
−0.308
63.794
41.874
1.00
20.75
O


ATOM
739
N
THR
X
104
0.464
65.901
41.700
1.00
20.41
N


ATOM
740
CA
THR
X
104
−0.708
66.402
40.982
1.00
20.68
C


ATOM
741
CB
THR
X
104
−0.745
67.951
40.979
1.00
20.76
C


ATOM
742
OG1
THR
X
104
−0.695
68.425
42.328
1.00
21.58
O


ATOM
743
CG2
THR
X
104
−2.018
68.469
40.306
1.00
21.15
C


ATOM
744
C
THR
X
104
−0.710
65.882
39.547
1.00
20.16
C


ATOM
745
O
THR
X
104
0.244
66.108
38.813
1.00
20.15
O


ATOM
746
N
PRO
X
105
−1.781
65.175
39.147
1.00
20.15
N


ATOM
747
CA
PRO
X
105
−1.871
64.682
37.768
1.00
20.04
C


ATOM
748
CB
PRO
X
105
−3.275
64.069
37.707
1.00
19.98
C


ATOM
749
CG
PRO
X
105
−3.564
63.675
39.143
1.00
20.49
C


ATOM
750
CD
PRO
X
105
−2.953
64.781
39.952
1.00
20.10
C


ATOM
751
C
PRO
X
105
−1.719
65.825
36.758
1.00
20.02
C


ATOM
752
O
PRO
X
105
−2.322
66.879
36.934
1.00
19.57
O


ATOM
753
N
GLY
X
106
−0.896
65.616
35.732
1.00
20.06
N


ATOM
754
CA
GLY
X
106
−0.598
66.658
34.752
1.00
20.30
C


ATOM
755
C
GLY
X
106
0.703
67.406
35.013
1.00
20.84
C


ATOM
756
O
GLY
X
106
1.119
68.225
34.198
1.00
20.54
O


ATOM
757
N
THR
X
107
1.349
67.140
36.145
1.00
21.12
N


ATOM
758
CA
THR
X
107
2.638
67.778
36.462
1.00
21.98
C


ATOM
759
CB
THR
X
107
3.228
67.252
37.797
1.00
21.60
C


ATOM
760
OG1
THR
X
107
2.318
67.541
38.861
1.00
21.06
O


ATOM
761
CG2
THR
X
107
4.575
67.899
38.116
1.00
22.08
C


ATOM
762
C
THR
X
107
3.637
67.606
35.313
1.00
22.66
C


ATOM
763
O
THR
X
107
4.340
68.558
34.951
1.00
22.79
O


ATOM
764
N
PHE
X
108
3.678
66.405
34.735
1.00
23.33
N


ATOM
765
CA
PHE
X
108
4.544
66.128
33.597
1.00
24.37
C


ATOM
766
CB
PHE
X
108
5.146
64.712
33.669
1.00
23.71
C


ATOM
767
CG
PHE
X
108
6.058
64.479
34.856
1.00
22.65
C


ATOM
768
CD1
PHE
X
108
6.694
65.540
35.501
1.00
20.74
C


ATOM
769
CE1
PHE
X
108
7.542
65.317
36.583
1.00
21.37
C


ATOM
770
CZ
PHE
X
108
7.771
64.016
37.029
1.00
22.32
C


ATOM
771
CE2
PHE
X
108
7.151
62.946
36.384
1.00
21.63
C


ATOM
772
CD2
PHE
X
108
6.305
63.184
35.302
1.00
21.95
C


ATOM
773
C
PHE
X
108
3.849
66.360
32.247
1.00
25.79
C


ATOM
774
O
PHE
X
108
4.422
67.003
31.374
1.00
26.35
O


ATOM
775
N
THR
X
109
2.628
65.849
32.077
1.00
27.27
N


ATOM
776
CA
THR
X
109
1.922
65.940
30.780
1.00
28.86
C


ATOM
777
CB
THR
X
109
0.732
64.950
30.677
1.00
28.57
C


ATOM
778
OG1
THR
X
109
−0.196
65.190
31.740
1.00
28.28
O


ATOM
779
CG2
THR
X
109
1.209
63.498
30.739
1.00
28.18
C


ATOM
780
C
THR
X
109
1.433
67.356
30.412
1.00
30.37
C


ATOM
781
O
THR
X
109
1.350
67.698
29.232
1.00
30.35
O


ATOM
782
N
ASN
X
110
1.098
68.162
31.417
1.00
32.08
N


ATOM
783
CA
ASN
X
110
0.687
69.553
31.201
1.00
34.07
C


ATOM
784
CB
ASN
X
110
−0.083
70.068
32.419
1.00
34.27
C


ATOM
785
CG
ASN
X
110
−1.571
69.980
32.252
1.00
35.53
C


ATOM
786
OD1
ASN
X
110
−2.180
70.876
31.681
1.00
38.58
O


ATOM
787
ND2
ASN
X
110
−2.178
68.926
32.782
1.00
36.18
N


ATOM
788
C
ASN
X
110
1.899
70.447
30.958
1.00
35.02
C


ATOM
789
O
ASN
X
110
2.430
71.048
31.888
1.00
35.57
O


ATOM
790
N
GLN
X
111
2.352
70.534
29.716
1.00
36.38
N


ATOM
791
CA
GLN
X
111
3.563
71.296
29.451
1.00
37.55
C


ATOM
792
CB
GLN
X
111
4.713
70.375
29.047
1.00
37.86
C


ATOM
793
CG
GLN
X
111
6.095
71.025
29.121
1.00
39.62
C


ATOM
794
CD
GLN
X
111
6.402
71.623
30.483
1.00
41.90
C


ATOM
795
OE1
GLN
X
111
6.579
70.896
31.470
1.00
42.33
O


ATOM
796
NE2
GLN
X
111
6.470
72.961
30.544
1.00
41.48
N


ATOM
797
C
GLN
X
111
3.369
72.420
28.445
1.00
37.98
C


ATOM
798
O
GLN
X
111
2.883
72.203
27.335
1.00
38.21
O


ATOM
799
N
ILE
X
112
3.776
73.619
28.860
1.00
38.65
N


ATOM
800
CA
ILE
X
112
3.606
74.851
28.084
1.00
39.07
C


ATOM
801
CB
ILE
X
112
3.508
76.088
29.018
1.00
39.13
C


ATOM
802
CG1
ILE
X
112
4.823
76.288
29.793
1.00
39.83
C


ATOM
803
CD1
ILE
X
112
4.848
77.481
30.741
1.00
39.68
C


ATOM
804
CG2
ILE
X
112
2.305
75.943
29.964
1.00
39.97
C


ATOM
805
C
ILE
X
112
4.726
75.066
27.062
1.00
38.69
C


ATOM
806
O
ILE
X
112
4.609
75.922
26.169
1.00
39.27
O


ATOM
807
N
GLN
X
113
5.802
74.289
27.195
1.00
37.82
N


ATOM
808
CA
GLN
X
113
6.989
74.443
26.361
1.00
36.64
C


ATOM
809
CB
GLN
X
113
8.093
75.184
27.123
1.00
37.01
C


ATOM
810
CG
GLN
X
113
8.202
76.660
26.774
1.00
38.82
C


ATOM
811
CD
GLN
X
113
8.131
77.561
27.987
1.00
41.43
C


ATOM
812
OE1
GLN
X
113
8.776
77.310
29.010
1.00
42.62
O


ATOM
813
NE2
GLN
X
113
7.333
78.626
27.881
1.00
42.06
N


ATOM
814
C
GLN
X
113
7.508
73.109
25.849
1.00
35.43
C


ATOM
815
O
GLN
X
113
7.676
72.157
26.607
1.00
35.25
O


ATOM
816
N
ALA
X
114
7.753
73.059
24.546
1.00
33.91
N


ATOM
817
CA
ALA
X
114
8.380
71.913
23.902
1.00
32.18
C


ATOM
818
CB
ALA
X
114
8.214
72.037
22.402
1.00
32.43
C


ATOM
819
C
ALA
X
114
9.867
71.827
24.251
1.00
30.68
C


ATOM
820
O
ALA
X
114
10.418
70.737
24.419
1.00
30.39
O


ATOM
821
N
ALA
X
115
10.500
72.992
24.359
1.00
29.00
N


ATOM
822
CA
ALA
X
115
11.949
73.098
24.490
1.00
27.55
C


ATOM
823
CB
ALA
X
115
12.434
74.411
23.870
1.00
27.22
C


ATOM
824
C
ALA
X
115
12.417
72.988
25.940
1.00
26.49
C


ATOM
825
O
ALA
X
115
11.735
73.462
26.849
1.00
26.04
O


ATOM
826
N
PHE
X
116
13.583
72.362
26.130
1.00
25.25
N


ATOM
827
CA
PHE
X
116
14.278
72.280
27.432
1.00
24.37
C


ATOM
828
CB
PHE
X
116
14.855
73.642
27.838
1.00
24.42
C


ATOM
829
CG
PHE
X
116
15.704
74.256
26.770
1.00
24.56
C


ATOM
830
CD1
PHE
X
116
17.005
73.825
26.573
1.00
24.63
C


ATOM
831
CE1
PHE
X
116
17.786
74.373
25.562
1.00
25.42
C


ATOM
832
CZ
PHE
X
116
17.258
75.350
24.734
1.00
24.56
C


ATOM
833
CE2
PHE
X
116
15.953
75.774
24.911
1.00
24.23
C


ATOM
834
CD2
PHE
X
116
15.183
75.228
25.925
1.00
24.58
C


ATOM
835
C
PHE
X
116
13.406
71.671
28.514
1.00
23.76
C


ATOM
836
O
PHE
X
116
13.328
72.152
29.650
1.00
23.31
O


ATOM
837
N
ARG
X
117
12.764
70.583
28.116
1.00
22.95
N


ATOM
838
CA
ARG
X
117
11.836
69.836
28.932
1.00
22.58
C


ATOM
839
CB
ARG
X
117
11.229
68.739
28.063
1.00
23.11
C


ATOM
840
CG
ARG
X
117
10.381
67.786
28.801
1.00
26.40
C


ATOM
841
CD
ARG
X
117
9.223
67.388
27.956
1.00
31.69
C


ATOM
842
NE
ARG
X
117
8.079
67.243
28.829
1.00
35.88
N


ATOM
843
CZ
ARG
X
117
6.862
67.673
28.540
1.00
38.16
C


ATOM
844
NH1
ARG
X
117
6.624
68.282
27.380
1.00
38.49
N


ATOM
845
NH2
ARG
X
117
5.891
67.494
29.422
1.00
39.18
N


ATOM
846
C
ARG
X
117
12.480
69.246
30.193
1.00
21.31
C


ATOM
847
O
ARG
X
117
13.551
68.636
30.140
1.00
21.06
O


ATOM
848
N
GLU
X
118
11.804
69.437
31.321
1.00
20.15
N


ATOM
849
CA
GLU
X
118
12.299
69.005
32.618
1.00
19.48
C


ATOM
850
CB
GLU
X
118
12.835
70.213
33.407
1.00
19.54
C


ATOM
851
CG
GLU
X
118
14.101
70.874
32.785
1.00
20.03
C


ATOM
852
CD
GLU
X
118
14.407
72.255
33.371
1.00
20.32
C


ATOM
853
OE1
GLU
X
118
13.702
73.220
33.011
1.00
20.60
O


ATOM
854
OE2
GLU
X
118
15.354
72.382
34.190
1.00
21.21
O


ATOM
855
C
GLU
X
118
11.163
68.317
33.379
1.00
18.61
C


ATOM
856
O
GLU
X
118
9.990
68.672
33.182
1.00
18.67
O


ATOM
857
N
PRO
X
119
11.489
67.318
34.236
1.00
17.43
N


ATOM
858
CA
PRO
X
119
12.808
66.702
34.476
1.00
16.34
C


ATOM
859
CB
PRO
X
119
12.548
65.736
35.641
1.00
16.16
C


ATOM
860
CG
PRO
X
119
11.102
65.507
35.639
1.00
16.78
C


ATOM
861
CD
PRO
X
119
10.454
66.742
35.108
1.00
16.78
C


ATOM
862
C
PRO
X
119
13.356
65.922
33.280
1.00
15.31
C


ATOM
863
O
PRO
X
119
12.632
65.646
32.325
1.00
14.60
O


ATOM
864
N
ARG
X
120
14.641
65.592
33.349
1.00
14.55
N


ATOM
865
CA
ARG
X
120
15.301
64.782
32.329
1.00
14.10
C


ATOM
866
CB
ARG
X
120
16.705
65.330
32.048
1.00
14.08
C


ATOM
867
CG
ARG
X
120
16.724
66.721
31.427
1.00
13.92
C


ATOM
868
CD
ARG
X
120
18.152
67.134
31.105
1.00
14.02
C


ATOM
869
NE
ARG
X
120
18.705
66.304
30.043
1.00
13.76
N


ATOM
870
CZ
ARG
X
120
19.992
66.008
29.906
1.00
15.31
C


ATOM
871
NH1
ARG
X
120
20.883
66.464
30.777
1.00
14.55
N


ATOM
872
NH2
ARG
X
120
20.387
65.236
28.895
1.00
17.13
N


ATOM
873
C
ARG
X
120
15.391
63.327
32.768
1.00
13.55
C


ATOM
874
O
ARG
X
120
15.600
62.440
31.953
1.00
13.14
O


ATOM
875
N
LEU
X
121
15.227
63.089
34.064
1.00
13.36
N


ATOM
876
CA
LEU
X
121
15.255
61.737
34.613
1.00
13.20
C


ATOM
877
CB
LEU
X
121
16.690
61.319
34.958
1.00
13.15
C


ATOM
878
CG
LEU
X
121
16.957
59.917
35.532
1.00
13.48
C


ATOM
879
CD1
LEU
X
121
16.618
58.803
34.528
1.00
12.75
C


ATOM
880
CD2
LEU
X
121
18.404
59.808
35.967
1.00
13.17
C


ATOM
881
C
LEU
X
121
14.355
61.665
35.845
1.00
13.02
C


ATOM
882
O
LEU
X
121
14.327
62.584
36.672
1.00
13.22
O


ATOM
883
N
LEU
X
122
13.617
60.571
35.953
1.00
12.73
N


ATOM
884
CA
LEU
X
122
12.721
60.361
37.073
1.00
12.88
C


ATOM
885
CB
LEU
X
122
11.274
60.250
36.577
1.00
13.01
C


ATOM
886
CG
LEU
X
122
10.217
59.856
37.614
1.00
13.55
C


ATOM
887
CD1
LEU
X
122
10.104
60.923
38.694
1.00
12.85
C


ATOM
888
CD2
LEU
X
122
8.867
59.587
36.953
1.00
12.51
C


ATOM
889
C
LEU
X
122
13.117
59.117
37.871
1.00
13.13
C


ATOM
890
O
LEU
X
122
13.364
58.048
37.306
1.00
12.99
O


ATOM
891
N
VAL
X
123
13.206
59.266
39.187
1.00
13.02
N


ATOM
892
CA
VAL
X
123
13.380
58.101
40.043
1.00
13.06
C


ATOM
893
CB
VAL
X
123
14.895
57.858
40.471
1.00
13.01
C


ATOM
894
CG1
VAL
X
123
15.740
59.116
40.419
1.00
13.47
C


ATOM
895
CG2
VAL
X
123
15.045
57.072
41.765
1.00
13.75
C


ATOM
896
C
VAL
X
123
12.300
58.002
41.135
1.00
13.24
C


ATOM
897
O
VAL
X
123
12.051
58.960
41.875
1.00
13.28
O


ATOM
898
N
VAL
X
124
11.620
56.858
41.176
1.00
13.15
N


ATOM
899
CA
VAL
X
124
10.482
56.661
42.078
1.00
13.12
C


ATOM
900
CB
VAL
X
124
9.117
56.447
41.328
1.00
13.16
C


ATOM
901
CG1
VAL
X
124
8.872
57.539
40.282
1.00
12.38
C


ATOM
902
CG2
VAL
X
124
9.041
55.066
40.687
1.00
12.89
C


ATOM
903
C
VAL
X
124
10.709
55.527
43.079
1.00
13.18
C


ATOM
904
O
VAL
X
124
11.514
54.619
42.847
1.00
12.76
O


ATOM
905
N
THR
X
125
9.976
55.598
44.186
1.00
13.18
N


ATOM
906
CA
THR
X
125
10.116
54.654
45.286
1.00
13.79
C


ATOM
907
CB
THR
X
125
9.684
55.325
46.617
1.00
13.80
C


ATOM
908
OG1
THR
X
125
10.532
56.455
46.864
1.00
14.25
O


ATOM
909
CG2
THR
X
125
9.769
54.358
47.796
1.00
13.19
C


ATOM
910
C
THR
X
125
9.338
53.356
45.065
1.00
13.98
C


ATOM
911
O
THR
X
125
9.751
52.304
45.541
1.00
13.85
O


ATOM
912
N
ASP
X
126
8.225
53.427
44.336
1.00
14.60
N


ATOM
913
CA
ASP
X
126
7.270
52.319
44.286
1.00
15.58
C


ATOM
914
CB
ASP
X
126
6.406
52.356
45.565
1.00
15.59
C


ATOM
915
CG
ASP
X
126
5.375
51.218
45.657
1.00
16.75
C


ATOM
916
OD1
ASP
X
126
5.034
50.575
44.644
1.00
17.08
O


ATOM
917
OD2
ASP
X
126
4.887
50.981
46.782
1.00
18.47
O


ATOM
918
C
ASP
X
126
6.418
52.463
43.032
1.00
16.06
C


ATOM
919
O
ASP
X
126
5.566
53.342
42.976
1.00
16.09
O


ATOM
920
N
PRO
X
127
6.645
51.606
42.016
1.00
16.67
N


ATOM
921
CA
PRO
X
127
5.917
51.738
40.750
1.00
17.51
C


ATOM
922
CB
PRO
X
127
6.471
50.580
39.903
1.00
17.42
C


ATOM
923
CG
PRO
X
127
7.794
50.297
40.483
1.00
17.16
C


ATOM
924
CD
PRO
X
127
7.594
50.483
41.961
1.00
16.89
C


ATOM
925
C
PRO
X
127
4.401
51.612
40.883
1.00
18.08
C


ATOM
926
O
PRO
X
127
3.671
52.136
40.042
1.00
18.48
O


ATOM
927
N
ARG
X
128
3.951
50.928
41.935
1.00
18.42
N


ATOM
928
CA
ARG
X
128
2.533
50.747
42.236
1.00
19.55
C


ATOM
929
CB
ARG
X
128
2.374
49.541
43.187
1.00
20.14
C


ATOM
930
CG
ARG
X
128
0.951
49.042
43.542
1.00
24.68
C


ATOM
931
CD
ARG
X
128
0.144
48.414
42.369
1.00
31.10
C


ATOM
932
NE
ARG
X
128
0.541
47.092
41.821
1.00
33.70
N


ATOM
933
CZ
ARG
X
128
1.310
46.159
42.396
1.00
34.27
C


ATOM
934
NH1
ARG
X
128
1.838
46.322
43.601
1.00
34.54
N


ATOM
935
NH2
ARG
X
128
1.549
45.031
41.739
1.00
34.73
N


ATOM
936
C
ARG
X
128
1.960
52.055
42.812
1.00
18.79
C


ATOM
937
O
ARG
X
128
1.043
52.636
42.240
1.00
18.93
O


ATOM
938
N
ALA
X
129
2.526
52.538
43.914
1.00
18.15
N


ATOM
939
CA
ALA
X
129
2.052
53.771
44.539
1.00
17.79
C


ATOM
940
CB
ALA
X
129
2.625
53.915
45.933
1.00
17.72
C


ATOM
941
C
ALA
X
129
2.366
55.017
43.699
1.00
17.52
C


ATOM
942
O
ALA
X
129
1.605
55.981
43.697
1.00
17.04
O


ATOM
943
N
ASP
X
130
3.491
54.983
42.991
1.00
17.23
N


ATOM
944
CA
ASP
X
130
3.935
56.117
42.188
1.00
17.23
C


ATOM
945
CB
ASP
X
130
5.428
56.372
42.433
1.00
17.10
C


ATOM
946
CG
ASP
X
130
5.725
56.714
43.882
1.00
17.70
C


ATOM
947
OD1
ASP
X
130
4.993
57.561
44.441
1.00
18.36
O


ATOM
948
OD2
ASP
X
130
6.677
56.145
44.466
1.00
16.55
O


ATOM
949
C
ASP
X
130
3.635
55.911
40.707
1.00
17.03
C


ATOM
950
O
ASP
X
130
4.374
56.375
39.846
1.00
16.69
O


ATOM
951
N
HIS
X
131
2.535
55.219
40.416
1.00
17.32
N


ATOM
952
CA
HIS
X
131
2.159
54.916
39.039
1.00
17.64
C


ATOM
953
CB
HIS
X
131
0.936
53.987
38.998
1.00
18.00
C


ATOM
954
CG
HIS
X
131
−0.354
54.683
39.299
1.00
19.71
C


ATOM
955
ND1
HIS
X
131
−0.868
54.777
49.576
1.00
21.28
N


ATOM
956
CE1
HIS
X
131
−1.997
55.464
40.545
1.00
22.13
C


ATOM
957
NE2
HIS
X
131
−2.233
55.820
39.294
1.00
23.52
N


ATOM
958
CD2
HIS
X
131
−1.220
55.344
38.494
1.00
20.68
C


ATOM
959
C
HIS
X
131
1.897
56.177
38.201
1.00
17.25
C


ATOM
960
O
HIS
X
131
2.167
56.183
36.997
1.00
17.72
O


ATOM
961
N
GLN
X
132
1.368
57.231
38.830
1.00
16.69
N


ATOM
962
CA
GLN
X
132
0.979
58.443
38.095
1.00
16.49
C


ATOM
963
CB
GLN
X
132
0.175
59.428
38.969
1.00
16.53
C


ATOM
964
CG
GLN
X
132
−0.312
60.706
38.239
1.00
16.83
C


ATOM
965
CD
GLN
X
132
−1.490
60.452
37.299
1.00
17.26
C


ATOM
966
OE1
GLN
X
132
−2.359
59.630
37.585
1.00
19.31
O


ATOM
967
NE2
GLN
X
132
−1.524
61.162
36.179
1.00
15.76
N


ATOM
968
C
GLN
X
132
2.181
59.111
37.406
1.00
16.10
C


ATOM
969
O
GLN
X
132
2.157
59.255
36.188
1.00
16.02
O


ATOM
970
N
PRO
X
133
3.229
59.514
38.174
1.00
15.88
N


ATOM
971
CA
PRO
X
133
4.436
60.074
37.536
1.00
15.39
C


ATOM
972
CB
PRO
X
133
5.405
60.294
38.711
1.00
15.57
C


ATOM
973
CG
PRO
X
133
4.829
59.557
39.862
1.00
16.05
C


ATOM
974
CD
PRO
X
133
3.350
59.520
39.645
1.00
15.63
C


ATOM
975
C
PRO
X
133
5.085
59.161
36.503
1.00
14.99
C


ATOM
976
O
PRO
X
133
5.538
59.652
35.478
1.00
15.33
O


ATOM
977
N
LEU
X
134
5.130
57.856
36.772
1.00
14.60
N


ATOM
978
CA
LEU
X
134
5.691
56.889
35.837
1.00
14.62
C


ATOM
979
CB
LEU
X
134
5.780
55.485
36.462
1.00
14.13
C


ATOM
980
CG
LEU
X
134
6.857
55.209
37.520
1.00
14.87
C


ATOM
981
CD1
LEU
X
134
6.728
53.784
38.025
1.00
13.28
C


ATOM
982
CD2
LEU
X
134
8.271
55.445
36.995
1.00
11.76
C


ATOM
983
C
LEU
X
134
4.898
56.822
34.539
1.00
14.42
C


ATOM
984
O
LEU
X
134
5.479
56.719
33.470
1.00
14.32
O


ATOM
985
N
THR
X
135
3.572
56.861
34.634
1.00
14.68
N


ATOM
986
CA
THR
X
135
2.752
56.780
33.431
1.00
14.87
C


ATOM
987
CB
THR
X
135
1.281
56.455
33.743
1.00
14.78
C


ATOM
988
OG1
THR
X
135
1.227
55.306
34.594
1.00
16.39
O


ATOM
989
CG2
THR
X
135
0.511
56.155
32.461
1.00
14.96
C


ATOM
990
C
THR
X
135
2.879
58.075
32.640
1.00
14.75
C


ATOM
991
O
THR
X
135
3.002
58.040
31.423
1.00
14.14
O


ATOM
992
N
GLU
X
136
2.876
59.207
33.347
1.00
14.94
N


ATOM
993
CA
GLU
X
136
3.068
60.506
32.709
1.00
15.53
C


ATOM
994
CB
GLU
X
136
2.861
61.666
33.701
1.00
15.40
C


ATOM
995
CG
GLU
X
136
1.420
61.797
34.192
1.00
16.02
C


ATOM
996
CD
GLU
X
136
1.098
63.150
34.818
1.00
16.58
C


ATOM
997
OE1
GLU
X
136
1.778
64.155
34.508
1.00
17.87
O


ATOM
998
OE2
GLU
X
136
0.149
63.203
35.627
1.00
17.77
O


ATOM
999
C
GLU
X
136
4.442
60.577
32.049
1.00
15.56
C


ATOM
1000
O
GLU
X
136
4.562
61.979
30.935
1.00
15.79
O


ATOM
1001
N
ALA
X
137
5.463
60.045
32.727
1.00
15.57
N


ATOM
1002
CA
ALA
X
137
6.819
59.965
32.175
1.00
16.00
C


ATOM
1003
CB
ALA
X
137
7.767
59.301
33.173
1.00
15.62
C


ATOM
1004
C
ALA
X
137
6.862
59.219
30.842
1.00
16.37
C


ATOM
1005
O
ALA
X
137
7.570
59.625
29.916
1.00
16.31
O


ATOM
1006
N
SER
X
138
6.115
58.120
30.763
1.00
16.92
N


ATOM
1007
CA
SER
X
138
6.014
57.344
29.532
1.00
18.02
C


ATOM
1008
CB
SER
X
138
5.191
56.079
29.748
1.00
18.15
C


ATOM
1009
OG
SER
X
138
5.486
55.160
28.709
1.00
22.02
O


ATOM
1010
C
SER
X
138
5.404
58.154
28.391
1.00
17.61
C


ATOM
1011
O
SER
X
138
5.863
58.053
27.254
1.00
18.11
O


ATOM
1012
N
TYR
X
139
4.377
58.949
28.700
1.00
17.08
N


ATOM
1013
CA
TYR
X
139
3.731
59.827
27.713
1.00
16.78
C


ATOM
1014
CB
TYR
X
139
2.561
60.592
28.352
1.00
16.51
C


ATOM
1015
CG
TYR
X
139
1.251
59.842
28.403
1.00
16.85
C


ATOM
1016
CD1
TYR
X
139
1.211
58.465
28.644
1.00
17.24
C


ATOM
1017
CE1
TYR
X
139
0.000
57.783
28.700
1.00
16.10
C


ATOM
1018
CZ
TYR
X
139
−1.175
58.475
28.530
1.00
15.99
C


ATOM
1019
OH
TYR
X
139
−2.365
57.801
28.585
1.00
16.80
O


ATOM
1020
CE2
TYR
X
139
−1.166
59.836
28.302
1.00
16.70
C


ATOM
1021
CD2
TYR
X
139
0.043
60.513
28.245
1.00
16.75
C


ATOM
1022
C
TYR
X
139
4.696
60.843
27.120
1.00
16.51
C


ATOM
1023
O
TYR
X
139
4.581
61.191
25.952
1.00
16.27
O


ATOM
1024
N
VAL
X
140
5.640
61.323
27.932
1.00
16.43
N


ATOM
1025
CA
VAL
X
140
6.535
62.412
27.506
1.00
16.24
C


ATOM
1026
CB
VAL
X
140
6.489
63.629
28.501
1.00
16.11
C


ATOM
1027
CG1
VAL
X
140
5.067
64.193
28.598
1.00
16.15
C


ATOM
1028
CG2
VAL
X
140
7.006
63.245
29.894
1.00
15.19
C


ATOM
1029
C
VAL
X
140
7.983
61.970
27.222
1.00
16.22
C


ATOM
1030
O
VAL
X
140
8.869
62.815
27.080
1.00
16.85
O


ATOM
1031
N
ASN
X
141
8.206
60.657
27.129
1.00
16.23
N


ATOM
1032
CA
ASN
X
141
9.540
60.066
26.927
1.00
16.12
C


ATOM
1033
CB
ASN
X
141
10.080
60.353
25.510
1.00
16.81
C


ATOM
1034
CG
ASN
X
141
9.140
59.874
24.405
1.00
18.10
C


ATOM
1035
OD1
ASN
X
141
8.430
58.882
24.558
1.00
21.41
O


ATOM
1036
ND2
ASN
X
141
9.146
60.579
23.284
1.00
19.83
N


ATOM
1037
C
ASN
X
141
10.566
60.491
28.001
1.00
15.49
C


ATOM
1038
O
ASN
X
141
11.721
60.799
27.700
1.00
15.25
O


ATOM
1039
N
LEU
X
142
10.120
60.514
29.252
1.00
14.66
N


ATOM
1040
CA
LEU
X
142
10.995
60.776
30.382
1.00
13.74
C


ATOM
1041
CB
LEU
X
142
10.224
61.539
31.463
1.00
13.57
C


ATOM
1042
CG
LEU
X
142
10.825
61.692
32.868
1.00
13.66
C


ATOM
1043
CD1
LEU
X
142
12.170
62.397
32.820
1.00
11.49
C


ATOM
1044
CD2
LEU
X
142
9.858
62.428
33.774
1.00
13.24
C


ATOM
1045
C
LEU
X
142
11.510
59.422
30.900
1.00
13.56
C


ATOM
1046
O
LEU
X
142
10.712
58.586
31.327
1.00
13.44
O


ATOM
1047
N
PRO
X
143
12.837
59.187
30.832
1.00
13.26
N


ATOM
1048
CA
PRO
X
143
13.386
57.916
31.331
1.00
12.95
C


ATOM
1049
CB
PRO
X
143
14.883
58.028
31.019
1.00
13.14
C


ATOM
1050
CG
PRO
X
143
14.968
59.082
29.927
1.00
13.92
C


ATOM
1051
CD
PRO
X
143
13.896
60.060
30.299
1.00
13.17
C


ATOM
1052
C
PRO
X
143
13.180
57.755
32.832
1.00
12.52
C


ATOM
1053
O
PRO
X
143
13.219
58.741
33.574
1.00
11.53
O


ATOM
1054
N
THR
X
144
12.981
56.516
33.278
1.00
12.24
N


ATOM
1055
CA
THR
X
144
12.633
56.282
34.674
1.00
12.51
C


ATOM
1056
CB
THR
X
144
11.169
55.837
34.837
1.00
12.44
C


ATOM
1057
OG1
THR
X
144
10.997
54.577
34.189
1.00
13.50
O


ATOM
1058
CG2
THR
X
144
10.219
56.844
34.220
1.00
12.05
C


ATOM
1059
C
THR
X
144
13.506
55.239
35.342
1.00
12.57
C


ATOM
1060
O
THR
X
144
14.054
54.340
34.686
1.00
13.12
O


ATOM
1061
N
ILE
X
145
13.599
55.369
36.661
1.00
11.86
N


ATOM
1062
CA
ILE
X
145
14.301
54.432
37.528
1.00
11.40
C


ATOM
1063
CB
ILE
X
145
15.642
55.011
38.047
1.00
11.28
C


ATOM
1064
CG1
ILE
X
145
16.557
55.385
36.869
1.00
11.42
C


ATOM
1065
CD1
ILE
X
145
17.819
56.141
37.244
1.00
11.39
C


ATOM
1066
CG2
ILE
X
145
16.327
54.013
38.997
1.00
11.28
C


ATOM
1067
C
ILE
X
145
13.366
54.206
38.698
1.00
11.06
C


ATOM
1068
O
ILE
X
145
12.713
55.139
39.159
1.00
11.09
O


ATOM
1069
N
ALA
X
146
13.276
52.970
39.171
1.00
10.74
N


ATOM
1070
CA
ALA
X
146
12.411
52.690
40.308
1.00
10.92
C


ATOM
1071
CB
ALA
X
146
11.000
52.297
39.848
1.00
9.62
C


ATOM
1072
C
ALA
X
146
12.993
51.605
41.183
1.00
10.87
C


ATOM
1073
O
ALA
X
146
13.660
50.699
40.701
1.00
10.77
O


ATOM
1074
N
LEU
X
147
12.728
51.731
42.474
1.00
11.43
N


ATOM
1075
CA
LEU
X
147
12.900
50.649
43.424
1.00
12.11
C


ATOM
1076
CB
LEU
X
147
12.810
51.188
44.859
1.00
11.61
C


ATOM
1077
CG
LEU
X
147
13.823
52.263
45.282
1.00
11.49
C


ATOM
1078
CD1
LEU
X
147
13.646
52.592
46.768
1.00
10.96
C


ATOM
1079
CD2
LEU
X
147
15.267
51.829
44.982
1.00
9.30
C


ATOM
1080
C
LEU
X
147
11.772
49.663
43.163
1.00
12.57
C


ATOM
1081
O
LEU
X
147
10.599
50.024
43.254
1.00
13.01
O


ATOM
1082
N
CYS
X
148
12.120
48.425
42.834
1.00
13.23
N


ATOM
1083
CA
CYS
X
148
11.120
47.457
42.398
1.00
13.55
C


ATOM
1084
CB
CYS
X
148
11.357
47.064
40.941
1.00
13.85
C


ATOM
1085
SG
CYS
X
148
11.109
48.395
39.766
1.00
14.86
S


ATOM
1086
C
CYS
X
148
11.107
46.210
43.260
1.00
13.86
C


ATOM
1087
O
CYS
X
148
12.135
45.536
43.418
1.00
14.09
O


ATOM
1088
N
ASN
X
149
9.933
45.910
43.803
1.00
13.71
N


ATOM
1089
CA
ASN
X
149
9.699
44.676
44.532
1.00
14.37
C


ATOM
1090
CB
ASN
X
149
8.567
44.863
45.555
1.00
13.99
C


ATOM
1091
CG
ASN
X
149
8.790
44.056
46.828
1.00
14.12
C


ATOM
1092
OD1
ASN
X
149
9.282
42.930
46.781
1.00
13.09
O


ATOM
1093
ND2
ASN
X
149
8.426
44.629
47.968
1.00
13.05
N


ATOM
1094
C
ASN
X
149
9.376
43.545
43.551
1.00
14.94
C


ATOM
1095
O
ASN
X
149
9.238
43.784
42.346
1.00
14.75
O


ATOM
1096
N
THR
X
150
9.249
42.320
44.058
1.00
15.51
N


ATOM
1097
CA
THR
X
150
9.016
41.159
43.183
1.00
16.22
C


ATOM
1098
CB
THR
X
150
9.097
39.818
43.953
1.00
16.08
C


ATOM
1099
OG1
THR
X
150
8.102
39.796
44.982
1.00
15.68
O


ATOM
1100
CG2
THR
X
150
10.477
39.646
44.563
1.00
15.55
C


ATOM
1101
C
THR
X
150
7.701
41.231
42.405
1.00
16.74
C


ATOM
1102
O
THR
X
150
7.619
40.733
41.286
1.00
16.41
O


ATOM
1103
N
ASP
X
151
6.687
41.859
42.995
1.00
17.93
N


ATOM
1104
CA
ASP
X
151
5.398
42.032
42.328
1.00
19.59
C


ATOM
1105
CB
ASP
X
151
4.254
41.705
43.288
1.00
20.07
C


ATOM
1106
CG
ASP
X
151
4.158
42.690
44.438
1.00
22.98
C


ATOM
1107
OD1
ASP
X
151
3.104
42.715
45.116
1.00
27.10
O


ATOM
1108
OD2
ASP
X
151
5.135
43.429
44.686
1.00
25.50
O


ATOM
1109
C
ASP
X
151
5.193
43.436
41.745
1.00
19.86
C


ATOM
1110
O
ASP
X
151
4.067
43.797
41.381
1.00
20.26
O


ATOM
1111
N
SER
X
152
6.264
44.226
41.668
1.00
19.95
N


ATOM
1112
CA
SER
X
152
6.185
45.559
41.063
1.00
19.88
C


ATOM
1113
CB
SER
X
152
7.465
46.361
41.299
1.00
19.46
C


ATOM
1114
OG
SER
X
152
7.505
46.882
42.616
1.00
19.58
O


ATOM
1115
C
SER
X
152
5.935
45.431
39.575
1.00
19.99
C


ATOM
1116
O
SER
X
152
6.546
44.589
38.916
1.00
20.27
O


ATOM
1117
N
PRO
X
153
5.019
46.253
39.038
1.00
20.10
N


ATOM
1118
CA
PRO
X
153
4.888
46.328
37.583
1.00
20.13
C


ATOM
1119
CB
PRO
X
153
3.572
47.095
37.397
1.00
20.02
C


ATOM
1120
CG
PRO
X
153
3.467
47.960
38.620
1.00
20.52
C


ATOM
1121
CD
PRO
X
153
4.060
47.132
39.737
1.00
20.09
C


ATOM
1122
C
PRO
X
153
6.068
47.100
36.974
1.00
20.13
C


ATOM
1123
O
PRO
X
153
6.397
48.201
37.442
1.00
20.58
O


ATOM
1124
N
LEU
X
154
6.701
46.527
35.953
1.00
19.88
N


ATOM
1125
CA
LEU
X
154
7.877
47.140
35.340
1.00
19.68
C


ATOM
1126
CB
LEU
X
154
9.006
46.116
35.137
1.00
19.67
C


ATOM
1127
CG
LEU
X
154
9.708
45.441
36.325
1.00
19.69
C


ATOM
1128
CD1
LEU
X
154
11.099
44.947
35.932
1.00
18.97
C


ATOM
1129
CD2
LEU
X
154
9.814
46.371
37.505
1.00
19.52
C


ATOM
1130
C
LEU
X
154
7.556
47.822
34.016
1.00
19.52
C


ATOM
1131
O
LEU
X
154
8.455
48.298
33.324
1.00
19.51
O


ATOM
1132
N
ARG
X
155
6.273
47.855
33.669
1.00
19.21
N


ATOM
1133
CA
ARG
X
155
5.807
48.440
32.414
1.00
18.99
C


ATOM
1134
CB
ARG
X
155
4.280
48.525
32.420
1.00
19.06
C


ATOM
1135
CG
ARG
X
155
3.690
49.105
31.143
1.00
20.28
C


ATOM
1136
CD
ARG
X
155
2.234
48.738
31.015
1.00
22.06
C


ATOM
1137
NE
ARG
X
155
2.086
47.302
30.790
1.00
22.67
N


ATOM
1138
CZ
ARG
X
155
0.966
46.619
30.985
1.00
23.37
C


ATOM
1139
NH1
ARG
X
155
−0.130
47.229
31.415
1.00
23.18
N


ATOM
1140
NH2
ARG
X
155
0.951
45.310
30.758
1.00
24.79
N


ATOM
1141
C
ARG
X
155
6.409
49.820
32.100
1.00
18.45
C


ATOM
1142
O
ARG
X
155
6.827
50.076
30.968
1.00
18.62
O


ATOM
1143
N
TYR
X
156
6.446
50.693
33.106
1.00
17.73
N


ATOM
1144
CA
TYR
X
156
6.878
52.085
32.939
1.00
16.79
C


ATOM
1145
CB
TYR
X
156
5.847
53.023
33.571
1.00
16.48
C


ATOM
1146
CG
TYR
X
156
4.451
52.845
33.010
1.00
16.91
C


ATOM
1147
CD1
TYR
X
156
4.178
53.106
31.666
1.00
16.32
C


ATOM
1148
CE1
TYR
X
156
2.898
52.940
31.144
1.00
15.84
C


ATOM
1149
CZ
TYR
X
156
1.878
52.504
31.965
1.00
16.74
C


ATOM
1150
OH
TYR
X
156
0.610
52.348
31.456
1.00
16.88
O


ATOM
1151
CE2
TYR
X
156
2.120
52.230
33.302
1.00
17.26
C


ATOM
1152
CD2
TYR
X
156
3.405
52.402
33.818
1.00
17.69
C


ATOM
1153
C
TYR
X
156
8.264
52.348
33.526
1.00
16.33
C


ATOM
1154
O
TYR
X
156
8.699
53.504
33.631
1.00
16.24
O


ATOM
1155
N
VAL
X
157
8.951
51.273
33.896
1.00
15.40
N


ATOM
1156
CA
VAL
X
157
10.264
51.363
34.529
1.00
15.08
C


ATOM
1157
CB
VAL
X
157
10.365
50.408
35.768
1.00
14.94
C


ATOM
1158
CG1
VAL
X
157
11.780
50.436
36.362
1.00
14.49
C


ATOM
1159
CG2
VAL
X
157
9.324
50.769
36.830
1.00
13.72
C


ATOM
1160
C
VAL
X
157
11.342
51.001
33.505
1.00
15.43
C


ATOM
1161
O
VAL
X
157
11.306
49.903
32.942
1.00
15.27
O


ATOM
1162
N
ASP
X
158
12.286
51.918
33.268
1.00
15.20
N


ATOM
1163
CA
ASP
X
158
13.423
51.656
32.372
1.00
15.42
C


ATOM
1164
CB
ASP
X
158
13.912
52.946
31.685
1.00
15.78
C


ATOM
1165
CG
ASP
X
158
12.840
53.602
30.811
1.00
17.28
C


ATOM
1166
OD1
ASP
X
158
12.315
52.959
29.869
1.00
18.93
O


ATOM
1167
OD2
ASP
X
158
12.530
54.780
31.057
1.00
18.99
O


ATOM
1168
C
ASP
X
158
14.590
50.973
33.106
1.00
15.10
C


ATOM
1169
O
ASP
X
158
15.176
50.005
32.598
1.00
15.16
O


ATOM
1170
N
ILE
X
159
14.942
51.488
34.282
1.00
14.23
N


ATOM
1171
CA
ILE
X
159
15.939
50.838
35.125
1.00
13.89
C


ATOM
1172
CB
ILE
X
159
17.174
51.732
35.426
1.00
14.16
C


ATOM
1173
CG1
ILE
X
159
17.942
52.079
34.139
1.00
13.81
C


ATOM
1174
CD1
ILE
X
159
18.986
53.186
34.338
1.00
13.96
C


ATOM
1175
CG2
ILE
X
159
18.101
51.034
36.446
1.00
13.94
C


ATOM
1176
C
ILE
X
159
15.285
50.416
36.432
1.00
13.63
C


ATOM
1177
O
ILE
X
159
14.884
51.267
37.238
1.00
13.47
O


ATOM
1178
N
ALA
X
160
15.168
49.102
36.618
1.00
13.06
N


ATOM
1179
CA
ALA
X
160
14.592
48.513
37.828
1.00
13.00
C


ATOM
1180
CB
ALA
X
160
13.784
47.269
37.476
1.00
12.71
C


ATOM
1181
C
ALA
X
160
15.687
48.159
38.822
1.00
12.72
C


ATOM
1182
O
ALA
X
160
16.635
47.448
38.480
1.00
13.40
O


ATOM
1183
N
ILE
X
161
15.566
48.673
40.040
1.00
12.22
N


ATOM
1184
CA
ILE
X
161
16.452
48.295
41.126
1.00
12.07
C


ATOM
1185
CB
ILE
X
161
16.933
49.525
41.952
1.00
11.98
C


ATOM
1186
CG1
ILE
X
161
17.521
50.607
41.038
1.00
11.82
C


ATOM
1187
CD1
ILE
X
161
17.733
51.946
41.727
1.00
11.76
C


ATOM
1188
CG2
ILE
X
161
17.979
49.097
42.968
1.00
12.04
C


ATOM
1189
C
ILE
X
161
15.679
47.310
42.024
1.00
12.00
C


ATOM
1190
O
ILE
X
161
14.774
47.719
42.749
1.00
11.80
O


ATOM
1191
N
PRO
X
162
16.018
46.008
41.955
1.00
12.25
N


ATOM
1192
CA
PRO
X
162
15.244
45.021
42.712
1.00
12.11
C


ATOM
1193
CB
PRO
X
162
15.699
43.686
42.121
1.00
12.20
C


ATOM
1194
CG
PRO
X
162
17.072
43.946
41.591
1.00
11.87
C


ATOM
1195
CD
PRO
X
162
17.107
45.385
41.175
1.00
12.06
C


ATOM
1196
C
PRO
X
162
15.544
45.099
44.201
1.00
12.22
C


ATOM
1197
O
PRO
X
162
16.711
45.093
44.597
1.00
12.32
O


ATOM
1198
N
CYS
X
163
14.495
45.202
45.013
1.00
12.31
N


ATOM
1199
CA
CYS
X
163
14.650
45.339
46.455
1.00
13.05
C


ATOM
1200
CB
CYS
X
163
15.315
46.685
46.787
1.00
13.19
C


ATOM
1201
SG
CYS
X
163
14.357
48.091
46.189
1.00
14.37
S


ATOM
1202
C
CYS
X
163
13.302
45.258
47.166
1.00
13.21
C


ATOM
1203
O
CYS
X
163
12.244
45.352
46.532
1.00
12.99
O


ATOM
1204
N
ASN
X
164
13.355
45.070
48.484
1.00
13.29
N


ATOM
1205
CA
ASN
X
164
12.220
45.353
49.355
1.00
13.54
C


ATOM
1206
CB
ASN
X
164
12.531
44.883
50.783
1.00
13.28
C


ATOM
1207
CG
ASN
X
164
11.386
45.130
51.769
1.00
13.91
C


ATOM
1208
OD1
ASN
X
164
10.380
45.756
51.444
1.00
14.80
O


ATOM
1209
ND2
ASN
X
164
11.553
44.638
52.994
1.00
13.95
N


ATOM
1210
C
ASN
X
164
11.987
46.871
49.319
1.00
13.94
C


ATOM
1211
O
ASN
X
164
12.741
47.640
49.926
1.00
14.14
O


ATOM
1212
N
ASN
X
165
10.970
47.293
48.579
1.00
14.20
N


ATOM
1213
CA
ASN
X
165
10.604
48.701
48.514
1.00
15.18
C


ATOM
1214
CB
ASN
X
165
10.377
49.144
47.059
1.00
14.77
C


ATOM
1215
CG
ASN
X
165
9.096
48.581
46.462
1.00
15.34
C


ATOM
1216
OD1
ASN
X
165
8.433
47.737
47.061
1.00
17.22
O


ATOM
1217
ND2
ASN
X
165
8.741
49.052
45.274
1.00
16.27
N


ATOM
1218
C
ASN
X
165
9.360
48.988
49.364
1.00
15.88
C


ATOM
1219
O
ASN
X
165
8.702
50.011
49.175
1.00
16.07
O


ATOM
1220
N
LYS
X
166
9.049
48.074
50.284
1.00
16.53
N


ATOM
1221
CA
LYS
X
166
7.898
48.202
51.169
1.00
17.51
C


ATOM
1222
CB
LYS
X
166
7.095
46.896
51.176
1.00
17.80
C


ATOM
1223
CG
LYS
X
166
5.864
46.935
52.080
1.00
21.27
C


ATOM
1224
CD
LYS
X
166
5.281
45.548
52.301
1.00
26.08
C


ATOM
1225
CE
LYS
K
166
4.165
45.584
53.340
1.00
29.90
C


ATOM
1226
NZ
LYS
X
166
3.050
46.503
52.943
1.00
32.28
N


ATOM
1227
C
LYS
X
166
8.302
48.596
52.599
1.00
17.32
C


ATOM
1228
O
LYS
X
166
7.784
49.564
53.156
1.00
17.63
O


ATOM
1229
N
GLY
X
167
9.226
47.846
53.190
1.00
17.29
N


ATOM
1230
CA
GLY
X
167
9.652
48.098
54.569
1.00
16.94
C


ATOM
1231
C
GLY
X
167
10.373
49.424
54.690
1.00
16.73
C


ATOM
1232
O
GLY
X
167
11.108
49.820
53.782
1.00
16.04
O


ATOM
1233
N
ALA
X
168
10.168
50.102
55.820
1.00
16.45
N


ATOM
1234
CA
ALA
X
168
10.729
51.437
56.050
1.00
16.34
C


ATOM
1235
CB
ALA
X
168
10.155
52.050
57.339
1.00
16.64
C


ATOM
1236
C
ALA
X
168
12.257
51.488
56.068
1.00
16.30
C


ATOM
1237
O
ALA
X
168
12.858
52.397
55.483
1.00
15.90
O


ATOM
1238
N
HIS
X
169
12.886
50.522
56.738
1.00
16.23
N


ATOM
1239
CA
HIS
X
169
14.350
50.485
56.818
1.00
16.44
C


ATOM
1240
CB
HIS
X
169
14.823
49.424
57.812
1.00
17.20
C


ATOM
1241
CG
HIS
X
169
14.662
49.818
59.248
1.00
20.89
C


ATOM
1242
ND1
HIS
X
169
15.450
49.296
60.250
1.00
24.67
N


ATOM
1243
CE1
HIS
X
169
15.084
49.814
61.411
1.00
25.88
C


ATOM
1244
NE2
HIS
X
169
14.091
50.658
61.197
1.00
25.28
N


ATOM
1245
CD2
HIS
X
169
13.809
50.681
59.852
1.00
23.96
C


ATOM
1246
C
HIS
X
169
14.983
50.240
55.451
1.00
15.63
C


ATOM
1247
O
HIS
X
169
15.973
50.882
55.096
1.00
15.48
O


ATOM
1248
N
SER
X
170
14.398
49.320
54.692
1.00
14.82
N


ATOM
1249
CA
SER
X
170
14.895
48.982
53.360
1.00
14.35
C


ATOM
1250
CB
SER
X
170
14.211
47.724
52.827
1.00
14.25
C


ATOM
1251
OG
SER
X
170
14.739
47.364
51.560
1.00
15.22
O


ATOM
1252
C
SER
X
170
14.737
50.145
52.381
1.00
13.75
C


ATOM
1253
O
SER
X
170
15.668
50.455
51.647
1.00
13.52
O


ATOM
1254
N
VAL
X
171
13.569
50.788
52.375
1.00
13.45
N


ATOM
1255
CA
VAL
X
171
13.360
51.973
51.523
1.00
13.20
C


ATOM
1256
CB
VAL
X
171
11.933
52.544
51.640
1.00
12.91
C


ATOM
1257
CG1
VAL
X
171
11.823
53.920
50.950
1.00
13.68
C


ATOM
1258
CG2
VAL
X
171
10.926
51.581
51.061
1.00
13.64
C


ATOM
1259
C
VAL
X
171
14.386
53.057
51.850
1.00
12.85
C


ATOM
1260
O
VAL
X
171
15.026
53.605
50.951
1.00
12.45
O


ATOM
1261
N
GLY
X
172
14.542
53.356
53.137
1.00
12.67
N


ATOM
1262
CA
GLY
X
172
15.489
54.386
53.577
1.00
12.48
C


ATOM
1263
C
GLY
X
172
16.921
54.052
53.199
1.00
12.33
C


ATOM
1264
O
GLY
X
172
17.664
54.914
52.719
1.00
12.19
O


ATOM
1265
N
LEU
X
173
17.297
52.792
53.402
1.00
12.45
N


ATOM
1266
CA
LEU
X
173
18.639
52.313
53.075
1.00
12.79
C


ATOM
1267
CB
LEU
X
173
18.847
50.875
53.560
1.00
12.76
C


ATOM
1268
CG
LEU
X
173
20.166
50.183
53.164
1.00
13.27
C


ATOM
1269
CD1
LEU
X
173
21.357
50.818
53.885
1.00
13.69
C


ATOM
1270
CD2
LEU
X
173
20.104
48.675
53.440
1.00
12.89
C


ATOM
1271
C
LEU
X
173
18.918
52.397
51.579
1.00
12.76
C


ATOM
1272
O
LEU
X
173
20.017
52.778
51.176
1.00
13.12
O


ATOM
1273
N
MET
X
174
17.929
52.034
50.763
1.00
12.59
N


ATOM
1274
CA
MET
X
174
18.102
52.059
49.308
1.00
12.69
C


ATOM
1275
CB
MET
X
174
16.875
51.479
48.591
1.00
12.53
C


ATOM
1276
CG
MET
X
174
16.734
49.947
48.706
1.00
12.61
C


ATOM
1277
SD
MET
X
174
18.170
48.973
48.177
1.00
13.33
S


ATOM
1278
CE
MET
X
174
18.237
49.361
46.425
1.00
11.52
C


ATOM
1279
C
MET
X
174
18.421
53.471
48.809
1.00
12.66
C


ATOM
1280
O
MET
X
174
19.379
53.667
48.048
1.00
12.36
O


ATOM
1281
N
TRP
X
175
17.628
54.446
49.258
1.00
12.66
N


ATOM
1282
CA
TRP
X
175
17.836
55.850
48.896
1.00
13.00
C


ATOM
1283
CB
TRP
X
175
16.670
56.711
49.395
1.00
12.45
C


ATOM
1284
CG
TRP
X
175
15.474
56.665
48.486
1.00
11.86
C


ATOM
1285
CD1
TRP
X
175
14.280
56.046
48.722
1.00
10.69
C


ATOM
1286
NE1
TRP
X
175
13.431
56.225
47.653
1.00
10.74
N


ATOM
1287
CE2
TRP
X
175
14.076
56.970
46.698
1.00
11.46
C


ATOM
1288
CD2
TRP
X
175
15.365
57.269
47.193
1.00
11.64
C


ATOM
1289
CE3
TRP
X
175
16.240
58.027
46.397
1.00
11.84
C


ATOM
1290
CZ3
TRP
X
175
15.796
58.474
45.158
1.00
11.34
C


ATOM
1291
CH2
TRP
X
175
14.500
58.164
44.696
1.00
11.34
C


ATOM
1292
CZ2
TRP
X
175
13.632
57.413
45.444
1.00
11.62
C


ATOM
1293
C
TRP
X
175
19.175
56.379
49.412
1.00
13.57
C


ATOM
1294
O
TRP
X
175
19.878
57.098
48.706
1.00
14.02
O


ATOM
1295
N
TRP
X
176
19.527
55.998
50.638
1.00
14.79
N


ATOM
1296
CA
TRP
X
176
20.838
56.320
51.223
1.00
15.57
C


ATOM
1297
CB
TRP
X
176
20.904
55.819
52.677
1.00
15.95
C


ATOM
1298
CG
TRP
X
176
22.234
56.003
53.351
1.00
16.75
C


ATOM
1299
CD1
TRP
X
176
22.640
57.084
54.089
1.00
17.25
C


ATOM
1300
NE1
TRP
X
176
23.924
56.886
54.551
1.00
16.59
N


ATOM
1301
CE2
TRP
X
176
24.369
55.664
54.121
1.00
16.79
C


ATOM
1302
CD2
TRP
X
176
23.326
55.073
53.365
1.00
17.27
C


ATOM
1303
CE3
TRP
X
176
23.528
53.798
52.811
1.00
16.82
C


ATOM
1304
CZ3
TRP
X
176
24.752
53.159
53.025
1.00
16.49
C


ATOM
1305
CH2
TRP
X
176
25.768
53.775
53.785
1.00
17.43
C


ATOM
1306
CZ2
TRP
X
176
25.595
55.022
54.339
1.00
17.22
C


ATOM
1307
C
TRP
X
176
21.986
55.745
50.385
1.00
15.71
C


ATOM
1308
O
TRP
X
176
22.953
56.446
50.069
1.00
15.13
O


ATOM
1309
N
MET
X
177
21.867
54.474
50.008
1.00
16.31
N


ATOM
1310
CA
MET
X
177
22.900
53.831
49.199
1.00
17.65
C


ATOM
1311
CB
MET
X
177
22.677
52.329
49.130
1.00
17.44
C


ATOM
1312
CG
MET
X
177
23.975
51.559
49.074
1.00
19.87
C


ATOM
1313
SD
MET
X
177
23.742
49.791
49.294
1.00
22.04
S


ATOM
1314
CE
MET
X
177
23.557
49.637
51.067
1.00
21.57
C


ATOM
1315
C
MET
X
177
23.013
54.425
47.791
1.00
16.68
C


ATOM
1316
O
MET
X
177
24.119
54.573
47.263
1.00
16.13
O


ATOM
1317
N
LEU
X
178
21.866
54.755
47.196
1.00
16.39
N


ATOM
1318
CA
LEU
X
178
21.831
55.439
45.905
1.00
16.64
C


ATOM
1319
CB
LEU
X
178
20.392
55.740
45.469
1.00
16.45
C


ATOM
1320
CG
LEU
X
178
19.930
55.495
44.020
1.00
18.25
C


ATOM
1321
CD1
LEU
X
178
18.855
56.495
43.575
1.00
16.38
C


ATOM
1322
CD2
LEU
X
178
21.057
55.389
42.991
1.00
16.98
C


ATOM
1323
C
LEU
X
178
22.603
56.747
46.016
1.00
16.16
C


ATOM
1324
O
LEU
X
178
23.482
57.007
45.208
1.00
16.08
O


ATOM
1325
N
ALA
X
179
22.265
57.548
47.028
1.00
16.24
N


ATOM
1326
CA
ALA
X
179
22.939
58.832
47.300
1.00
16.51
C


ATOM
1327
CB
ALA
X
179
22.335
59.510
48.542
1.00
16.39
C


ATOM
1328
C
ALA
X
179
24.443
58.678
47.460
1.00
16.51
C


ATOM
1329
O
ALA
X
179
25.215
59.402
46.829
1.00
16.60
O


ATOM
1330
N
ARG
X
180
24.855
57.726
48.297
1.00
16.59
N


ATOM
1331
CA
ARG
X
180
26.277
57.453
48.526
1.00
16.53
C


ATOM
1332
CB
ARG
X
180
26.437
56.270
49.490
1.00
16.40
C


ATOM
1333
CG
ARG
X
180
27.846
56.088
50.056
1.00
16.13
C


ATOM
1334
CD
ARG
X
180
27.952
54.790
50.850
1.00
16.00
C


ATOM
1335
NE
ARG
X
180
27.730
53.637
49.988
1.00
17.01
N


ATOM
1336
CZ
ARG
X
180
27.668
52.370
50.395
1.00
18.18
C


ATOM
1337
NH1
ARG
X
180
27.817
52.052
51.675
1.00
19.33
N


ATOM
1338
NH2
ARG
X
180
27.467
51.413
49.507
1.00
18.03
N


ATOM
1339
C
ARG
X
180
27.026
57.170
47.221
1.00
16.69
C


ATOM
1340
O
ARG
X
180
28.132
57.681
47.008
1.00
17.18
O


ATOM
1341
N
GLU
X
181
26.423
56.357
46.353
1.00
16.97
N


ATOM
1342
CA
GLU
X
181
27.056
55.970
45.090
1.00
17.18
C


ATOM
1343
CB
GLU
X
181
26.392
54.725
44.483
1.00
16.83
C


ATOM
1344
CG
GLU
X
181
26.595
53.443
45.306
1.00
19.23
C


ATOM
1345
CD
GLU
X
181
28.046
53.213
45.726
1.00
19.32
C


ATOM
1346
OE1
GLU
X
181
28.947
53.223
44.862
1.00
20.23
O


ATOM
1347
OE2
GLU
X
181
28.280
53.009
46.926
1.00
21.36
O


ATOM
1348
C
GLU
X
181
27.083
57.106
44.072
1.00
16.79
C


ATOM
1349
O
GLU
X
181
28.018
57.200
43.282
1.00
16.37
O


ATOM
1350
N
VAL
X
182
26.053
57.948
44.081
1.00
16.86
N


ATOM
1351
CA
VAL
X
182
26.052
59.152
43.238
1.00
17.35
C


ATOM
1352
CB
VAL
X
182
24.693
59.895
43.286
1.00
17.24
C


ATOM
1353
CG1
VAL
X
182
24.818
61.300
42.706
1.00
17.18
C


ATOM
1354
CG2
VAL
X
182
23.620
59.096
42.539
1.00
17.12
C


ATOM
1355
C
VAL
X
182
27.208
60.069
43.660
1.00
17.37
C


ATOM
1356
O
VAL
X
182
28.003
60.501
42.827
1.00
16.87
O


ATOM
1357
N
LEU
X
183
27.306
60.326
44.961
1.00
18.04
N


ATOM
1358
CA
LEU
X
183
28.365
61.177
45.520
1.00
19.17
C


ATOM
1359
CB
LEU
X
183
28.119
61.446
47.008
1.00
18.96
C


ATOM
1360
CG
LEU
X
183
26.871
62.282
47.331
1.00
19.49
C


ATOM
1361
CD1
LEU
X
183
26.695
62.445
48.833
1.00
19.23
C


ATOM
1362
CD2
LEU
X
183
26.911
63.650
46.633
1.00
19.34
C


ATOM
1363
C
LEU
X
183
29.766
60.610
45.307
1.00
19.85
C


ATOM
1364
O
LEU
X
183
30.712
61.366
45.088
1.00
20.20
O


ATOM
1365
N
ARG
X
184
29.895
59.286
45.379
1.00
20.45
N


ATOM
1366
CA
ARG
X
184
31.168
58.630
45.093
1.00
21.70
C


ATOM
1367
CB
ARG
X
184
31.134
57.155
45.504
1.00
21.78
C


ATOM
1368
CG
ARG
X
184
31.334
56.918
46.995
1.00
22.18
C


ATOM
1369
CD
ARG
X
184
31.159
55.442
47.339
1.00
22.57
C


ATOM
1370
NE
ARG
X
184
31.547
55.136
48.715
1.00
23.68
N


ATOM
1371
CZ
ARG
X
184
31.359
53.957
49.306
1.00
25.29
C


ATOM
1372
NH1
ARG
X
184
30.769
52.958
48.651
1.00
25.15
N


ATOM
1373
NH2
ARG
X
184
31.755
53.779
50.561
1.00
26.01
N


ATOM
1374
C
ARG
X
184
31.567
58.764
43.620
1.00
22.01
C


ATOM
1375
O
ARG
X
184
32.728
59.025
43.308
1.00
22.30
O


ATOM
1376
N
MET
X
185
30.607
58.588
42.719
1.00
22.36
N


ATOM
1377
CA
MET
X
185
30.887
58.685
41.288
1.00
23.07
C


ATOM
1378
CB
MET
X
185
29.689
58.212
40.468
1.00
22.89
C


ATOM
1379
CG
MET
X
185
29.402
56.735
40.640
1.00
23.31
C


ATOM
1380
SD
MET
X
185
28.182
56.149
39.465
1.00
23.73
S


ATOM
1381
CE
MET
X
185
28.238
54.384
39.799
1.00
22.03
C


ATOM
1382
C
MET
X
185
31.304
60.098
40.886
1.00
23.37
C


ATOM
1383
O
MET
X
185
32.194
60.273
40.052
1.00
23.40
O


ATOM
1384
N
ARG
X
186
30.674
61.091
41.511
1.00
23.70
N


ATOM
1385
CA
ARG
X
186
31.020
62.503
41.327
1.00
24.39
C


ATOM
1386
CB
ARG
X
186
29.917
63.390
41.908
1.00
23.94
C


ATOM
1387
CG
ARG
X
186
28.626
63.399
41.099
1.00
22.89
C


ATOM
1388
CD
ARG
X
186
27.633
64.341
41.727
1.00
20.94
C


ATOM
1389
NE
ARG
X
186
26.332
64.337
41.062
1.00
19.69
N


ATOM
1390
CZ
ARG
X
186
25.212
64.781
41.627
1.00
17.82
C


ATOM
1391
NH1
ARG
X
186
25.233
65.239
42.874
1.00
17.83
N


ATOM
1392
NH2
ARG
X
186
24.067
64.749
40.959
1.00
15.96
N


ATOM
1393
C
ARG
X
186
32.364
62.899
41.953
1.00
25.26
C


ATOM
1394
O
ARG
X
186
32.916
63.951
41.625
1.00
25.21
O


ATOM
1395
N
GLY
X
187
32.873
62.061
42.855
1.00
26.07
N


ATOM
1396
CA
GLY
X
187
34.102
62.350
43.589
1.00
27.26
C


ATOM
1397
C
GLY
X
187
33.860
63.316
44.730
1.00
28.25
C


ATOM
1398
O
GLY
X
187
34.797
63.950
45.216
1.00
28.55
O


ATOM
1399
N
THR
X
188
32.599
63.435
45.147
1.00
28.80
N


ATOM
1400
CA
THR
X
188
32.201
64.330
46.230
1.00
29.74
C


ATOM
1401
CB
THR
X
188
30.675
64.593
46.200
1.00
29.52
C


ATOM
1402
OG1
THR
X
188
30.307
65.134
44.924
1.00
29.63
O


ATOM
1403
CG2
THR
X
188
30.250
65.564
47.302
1.00
29.67
C


ATOM
1404
C
THR
X
188
32.608
63.757
47.594
1.00
30.65
C


ATOM
1405
O
THR
X
188
32.975
64.505
48.505
1.00
30.74
O


ATOM
1406
N
ILE
X
189
32.520
62.434
47.726
1.00
31.59
N


ATOM
1407
CA
ILE
X
189
32.952
61.731
48.931
1.00
32.51
C


ATOM
1408
CB
ILE
X
189
31.761
61.166
49.167
1.00
32.45
C


ATOM
1409
CG1
ILE
X
189
31.003
60.074
48.991
1.00
31.89
C


ATOM
1410
CD1
ILE
X
189
29.990
59.295
49.824
1.00
32.04
C


ATOM
1411
CG2
ILE
X
189
30.842
62.298
50.244
1.00
32.02
C


ATOM
1412
C
ILE
X
189
33.905
60.600
48.565
1.00
33.74
C


ATOM
1413
O
ILE
X
189
33.996
60.200
47.401
1.00
33.49
O


ATOM
1414
N
SER
X
190
34.603
60.088
49.573
1.00
35.56
N


ATOM
1415
CA
SER
X
190
35.582
59.020
49.393
1.00
37.44
C


ATOM
1416
CB
SER
X
190
36.366
58.788
50.685
1.00
37.26
C


ATOM
1417
OG
SER
X
190
37.180
57.630
50.578
1.00
38.17
O


ATOM
1418
C
SER
X
190
34.957
57.707
48.924
1.00
38.68
C


ATOM
1419
O
SER
X
190
33.913
57.274
49.425
1.00
38.89
O


ATOM
1420
N
ARG
X
191
35.636
57.078
47.972
1.00
40.35
N


ATOM
1421
CA
ARG
X
191
35.216
55.820
47.375
1.00
42.05
C


ATOM
1422
CB
ARG
X
191
35.837
55.712
45.981
1.00
42.21
C


ATOM
1423
CG
ARG
X
191
34.941
55.114
44.924
1.00
43.86
C


ATOM
1424
CD
ARG
X
191
35.428
55.482
43.524
1.00
46.98
C


ATOM
1425
NE
ARG
X
191
35.514
56.931
43.320
1.00
48.37
N


ATOM
1426
CZ
ARG
X
191
35.511
57.530
42.130
1.00
49.47
C


ATOM
1427
NH1
ARG
X
191
35.419
56.812
41.016
1.00
49.92
N


ATOM
1428
NH2
ARG
X
191
35.593
58.854
42.052
1.00
49.66
N


ATOM
1429
C
ARG
X
191
35.660
54.631
48.235
1.00
42.95
C


ATOM
1430
O
ARG
X
191
35.143
53.517
48.087
1.00
43.12
O


ATOM
1431
N
GLU
X
192
36.612
54.876
49.136
1.00
44.02
N


ATOM
1432
CA
GLU
X
192
37.237
53.805
49.920
1.00
45.03
C


ATOM
1433
CB
GLU
X
192
38.759
53.997
49.991
1.00
45.27
C


ATOM
1434
CG
GLU
X
192
39.514
53.573
48.722
1.00
46.86
C


ATOM
1435
CD
GLU
X
192
39.505
54.633
47.619
1.00
49.21
C


ATOM
1436
OE1
GLU
X
192
39.390
55.841
47.937
1.00
50.44
O


ATOM
1437
OE2
GLU
X
192
39.622
54.257
46.429
1.00
49.88
O


ATOM
1438
C
GLU
X
192
36.641
53.590
51.320
1.00
45.20
C


ATOM
1439
O
GLU
X
192
36.235
52.469
51.649
1.00
45.52
O


ATOM
1440
N
HIS
X
193
36.589
54.647
52.136
1.00
45.32
N


ATOM
1441
CA
HIS
X
193
36.067
54.530
53.508
1.00
45.33
C


ATOM
1442
CB
HIS
X
193
36.903
55.343
54.519
1.00
45.76
C


ATOM
1443
CG
HIS
X
193
36.728
56.830
54.423
1.00
47.14
C


ATOM
1444
ND1
HIS
X
193
35.675
57.498
55.014
1.00
48.11
N


ATOM
1445
CE1
HIS
X
193
35.788
58.794
54.777
1.00
48.61
C


ATOM
1446
NE2
HIS
X
193
36.886
58.994
54.069
1.00
48.65
N


ATOM
1447
CD2
HIS
X
193
37.496
57.783
53.841
1.00
48.49
C


ATOM
1448
C
HIS
X
193
34.567
54.847
53.617
1.00
44.88
C


ATOM
1449
O
HIS
X
193
34.028
55.576
52.779
1.00
44.95
O


ATOM
1450
N
PRO
X
194
33.887
54.274
54.636
1.00
44.30
N


ATOM
1451
CA
PRO
X
194
32.461
54.508
54.881
1.00
43.71
C


ATOM
1452
CB
PRO
X
194
32.249
53.908
56.272
1.00
43.81
C


ATOM
1453
CG
PRO
X
194
33.240
52.809
56.343
1.00
44.02
C


ATOM
1454
CD
PRO
X
194
34.451
53.324
55.618
1.00
44.29
C


ATOM
1455
C
PRO
X
194
32.061
55.984
54.885
1.00
43.07
C


ATOM
1456
O
PRO
X
194
32.853
56.846
55.277
1.00
42.96
O


ATOM
1457
N
TRP
X
195
30.830
56.245
54.451
1.00
42.19
N


ATOM
1458
CA
TRP
X
195
30.264
57.590
54.380
1.00
41.46
C


ATOM
1459
CB
TRP
X
195
29.054
57.583
53.433
1.00
40.37
C


ATOM
1460
CG
TRP
X
195
28.438
58.928
53.110
1.00
39.32
C


ATOM
1461
CD1
TRP
X
195
29.039
60.156
53.173
1.00
38.23
C


ATOM
1462
NE1
TRP
X
195
28.158
61.139
52.781
1.00
37.52
N


ATOM
1463
CE2
TRP
X
195
26.967
60.557
52.435
1.00
37.76
C


ATOM
1464
CD2
TRP
X
195
27.107
59.162
52.619
1.00
38.28
C


ATOM
1465
CE3
TRP
X
195
26.015
58.329
52.333
1.00
37.46
C


ATOM
1466
CZ3
TRP
X
195
24.833
58.907
51.875
1.00
37.85
C


ATOM
1467
CH2
TRP
X
195
24.728
60.297
51.701
1.00
38.37
C


ATOM
1468
CZ2
TRP
X
195
25.780
61.137
51.975
1.00
38.03
C


ATOM
1469
C
TRP
X
195
29.864
58.091
55.767
1.00
41.67
C


ATOM
1470
O
TRP
X
195
29.347
57.324
56.584
1.00
41.85
O


ATOM
1471
N
GLU
X
196
30.110
59.381
56.007
1.00
41.79
N


ATOM
1472
CA
GLU
X
196
29.788
60.068
57.265
1.00
41.88
C


ATOM
1473
CB
GLU
X
196
30.214
61.548
57.171
1.00
42.20
C


ATOM
1474
CG
GLU
X
196
29.283
62.434
56.318
1.00
43.93
C


ATOM
1475
CD
GLU
X
196
30.009
63.428
55.412
1.00
45.98
C


ATOM
1476
OE1
GLU
X
196
29.649
64.627
55.450
1.00
46.79
O


ATOM
1477
OE2
GLU
X
196
30.917
63.018
54.650
1.00
46.73
O


ATOM
1478
C
GLU
X
196
28.308
59.950
57.673
1.00
41.33
C


ATOM
1479
O
GLU
X
196
27.996
59.714
58.843
1.00
41.42
O


ATOM
1480
N
VAL
X
197
27.414
60.110
56.697
1.00
40.67
N


ATOM
1481
CA
VAL
X
197
25.964
60.085
56.908
1.00
39.71
C


ATOM
1482
CB
VAL
X
197
25.214
60.688
55.683
1.00
39.76
C


ATOM
1483
CG1
VAL
X
197
23.701
60.599
55.846
1.00
39.02
C


ATOM
1484
CG2
VAL
X
197
25.642
62.136
55.458
1.00
39.49
C


ATOM
1485
C
VAL
X
197
25.484
58.661
57.190
1.00
39.35
C


ATOM
1486
O
VAL
X
198
25.827
57.727
56.462
1.00
39.19
O


ATOM
1487
N
MET
X
198
24.710
58.510
58.264
1.00
38.79
N


ATOM
1488
CA
MET
X
198
24.122
57.228
58.643
1.00
38.71
C


ATOM
1489
CB
MET
X
198
23.902
57.156
60.157
1.00
38.67
C


ATOM
1490
CG
MET
X
198
25.182
57.054
60.988
1.00
40.04
C


ATOM
1491
SD
MET
X
198
24.856
56.740
62.744
1.00
42.11
S


ATOM
1492
CE
MET
X
198
23.934
58.216
63.213
1.00
41.75
C


ATOM
1493
C
MET
X
198
22.794
56.993
57.923
1.00
37.14
C


ATOM
1494
O
MET
X
198
22.029
57.938
57.715
1.00
36.78
O


ATOM
1495
N
PRO
X
199
22.521
55.731
57.531
1.00
36.06
N


ATOM
1496
CA
PRO
X
199
21.247
55.353
56.915
1.00
35.29
C


ATOM
1497
CB
PRO
X
199
21.331
53.825
56.857
1.00
35.14
C


ATOM
1498
CG
PRO
X
199
22.786
53.549
56.744
1.00
35.18
C


ATOM
1499
CD
PRO
X
199
23.446
54.583
57.606
1.00
35.80
C


ATOM
1500
C
PRO
X
199
19.997
55.795
57.683
1.00
34.70
C


ATOM
1501
O
PRO
X
199
19.013
56.175
57.053
1.00
34.06
O


ATOM
1502
N
ASP
X
200
20.038
55.759
59.017
1.00
34.37
N


ATOM
1503
CA
ASP
X
200
18.851
56.064
59.835
1.00
34.36
C


ATOM
1504
CB
ASP
X
200
19.066
55.719
61.323
1.00
34.77
C


ATOM
1505
CG
ASP
X
200
20.318
56.353
61.908
1.00
35.96
C


ATOM
1506
OD1
ASP
X
200
20.520
57.578
61.757
1.00
36.32
O


ATOM
1507
OD2
ASP
X
200
21.100
55.614
62.546
1.00
38.55
O


ATOM
1508
C
ASP
X
200
18.294
57.484
59.661
1.00
33.81
C


ATOM
1509
O
ASP
X
200
17.142
57.752
60.012
1.00
33.78
O


ATOM
1510
N
LEU
X
201
19.107
58.379
59.104
1.00
33.23
N


ATOM
1511
CA
LEU
X
201
18.654
59.721
58.732
1.00
32.90
C


ATOM
1512
CB
LEU
X
201
19.855
60.602
58.351
1.00
33.14
C


ATOM
1513
CG
LEU
X
201
20.646
61.383
59.424
1.00
33.94
C


ATOM
1514
CD1
LEU
X
201
20.907
60.605
60.718
1.00
34.33
C


ATOM
1515
CD2
LEU
X
201
21.965
61.886
58.857
1.00
33.61
C


ATOM
1516
C
LEU
X
201
17.622
59.679
57.595
1.00
32.28
C


ATOM
1517
O
LEU
X
201
16.834
60.608
57.430
1.00
32.29
O


ATOM
1518
N
TYR
X
202
17.622
58.587
56.832
1.00
31.44
N


ATOM
1519
CA
TYR
X
202
16.721
58.410
55.688
1.00
30.77
C


ATOM
1520
CB
TYR
X
202
17.450
57.674
54.556
1.00
29.63
C


ATOM
1521
CG
TYR
X
202
18.407
58.530
53.759
1.00
28.57
C


ATOM
1522
CD1
TYR
X
202
19.514
59.133
54.361
1.00
27.58
C


ATOM
1523
CE1
TYR
X
202
20.389
59.925
53.628
1.00
26.51
C


ATOM
1524
CZ
TYR
X
202
20.170
60.107
52.273
1.00
27.26
C


ATOM
1525
OH
TYR
X
202
21.036
60.880
51.539
1.00
27.46
O


ATOM
1526
CE2
TYR
X
202
19.087
59.516
51.650
1.00
26.92
C


ATOM
1527
CD2
TYR
X
202
18.212
58.732
52.392
1.00
27.09
C


ATOM
1528
C
TYR
X
202
15.430
57.664
56.044
1.00
31.15
C


ATOM
1529
O
TYR
X
202
14.497
57.616
55.235
1.00
30.65
O


ATOM
1530
N
PHE
X
203
15.377
57.096
57.251
1.00
32.02
N


ATOM
1531
CA
PHE
X
203
14.262
56.229
57.657
1.00
33.09
C


ATOM
1532
CB
PHE
X
203
14.651
55.269
58.802
1.00
32.95
C


ATOM
1533
CG
PHE
X
203
15.769
54.303
58.475
1.00
32.93
C


ATOM
1534
CD1
PHE
X
203
16.303
54.202
57.193
1.00
32.79
C


ATOM
1535
CE1
PHE
X
203
17.332
53.303
56.917
1.00
33.35
C


ATOM
1536
CZ
PHE
X
203
17.828
52.472
57.930
1.00
33.35
C


ATOM
1537
CE2
PHE
X
203
17.300
52.556
59.206
1.00
33.16
C


ATOM
1538
CD2
PHE
X
203
16.271
53.465
59.472
1.00
33.62
C


ATOM
1539
C
PHE
X
203
13.031
57.012
58.096
1.00
33.78
C


ATOM
1540
O
PHE
X
203
13.129
57.957
58.876
1.00
33.94
O


ATOM
1541
N
TYR
X
204
11.875
56.599
57.593
1.00
34.96
N


ATOM
1542
CA
TYR
X
204
10.591
57.032
58.124
1.00
36.43
C


ATOM
1543
CB
TYR
X
204
9.480
56.775
57.103
1.00
36.63
C


ATOM
1544
CG
TYR
X
204
8.075
56.885
57.662
1.00
36.91
C


ATOM
1545
CD1
TYR
X
204
7.522
58.126
57.975
1.00
36.88
C


ATOM
1546
CE1
TYR
X
204
6.231
58.232
58.487
1.00
37.29
C


ATOM
1547
CZ
TYR
X
204
5.483
57.084
58.685
1.00
37.32
C


ATOM
1548
OH
TYR
X
204
4.210
57.181
59.193
1.00
37.95
O


ATOM
1549
CE2
TYR
X
204
6.007
55.838
58.378
1.00
37.62
C


ATOM
1550
CD2
TYR
X
204
7.296
55.745
57.866
1.00
31.39
C


ATOM
1551
C
TYR
X
204
10.312
56.254
59.407
1.00
37.42
C


ATOM
1552
O
TYR
X
204
10.431
55.024
59.434
1.00
37.79
O


ATOM
1553
N
ARG
X
205
9.940
56.968
60.465
1.00
38.43
N


ATOM
1554
CA
ARG
X
205
9.665
56.348
61.767
1.00
39.46
C


ATOM
1555
CB
ARG
X
205
9.767
57.378
62.901
1.00
39.76
C


ATOM
1556
CG
ARG
X
205
11.014
58.268
62.864
1.00
41.74
C


ATOM
1557
CD
ARG
X
205
10.913
59.357
61.791
1.00
44.07
C


ATOM
1558
NE
ARG
X
205
12.076
60.240
61.801
1.00
46.72
N


ATOM
1559
CZ
ARG
X
205
12.019
61.562
61.939
1.00
48.19
C


ATOM
1560
NH1
ARG
X
205
10.848
62.179
62.064
1.00
48.90
N


ATOM
1561
NH2
ARG
X
205
13.140
62.274
61.940
1.00
49.01
N


ATOM
1562
C
ARG
X
205
8.295
55.665
61.795
1.00
39.44
C


ATOM
1563
O
ARG
X
205
7.258
56.324
61.900
1.00
39.65
O


ATOM
1564
OW0
HOH
W
1
17.328
30.841
41.342
1.00
13.55
O


ATOM
1565
OW0
HOH
W
2
6.080
55.905
47.160
1.00
13.76
O


ATOM
1566
OW0
HOH
W
3
4.048
59.906
43.347
1.00
14.05
O


ATOM
1567
OW0
HOH
W
4
0.704
57.513
41.713
1.00
15.24
O


ATOM
1568
OW0
HOH
W
5
5.651
50.433
35.931
1.00
17.32
O


ATOM
1569
OW0
HOH
W
6
23.026
64.481
38.188
1.00
10.96
O


ATOM
1570
OW0
HOH
W
7
12.555
37.870
34.182
1.00
19.82
O


ATOM
1571
OW0
HOH
W
8
11.922
54.852
55.497
1.00
18.27
O


ATOM
1572
OW0
HOH
W
9
8.818
43.207
50.381
1.00
14.96
O


ATOM
1573
OW0
HOH
W
10
27.800
66.142
44.438
1.00
26.20
O


ATOM
1574
OW0
HOH
W
11
11.787
57.813
54.420
1.00
19.92
O


ATOM
1575
OW0
HOH
W
12
3.596
40.091
46.527
1.00
22.31
O


ATOM
1576
OW0
HOH
W
13
29.206
53.589
53.969
1.00
21.19
O


ATOM
1577
OW0
HOH
W
14
3.076
67.750
41.467
1.00
22.33
O


ATOM
1578
OW0
HOH
W
15
26.620
64.484
38.091
1.00
17.05
O


ATOM
1579
OW0
HOH
W
16
19.359
34.768
41.035
1.00
15.57
O


ATOM
1580
OW0
HOH
W
17
21.010
64.857
40.624
1.00
16.67
O


ATOM
1581
OW0
HOH
W
18
19.888
36.931
39.432
1.00
23.52
O


ATOM
1582
OW0
HOH
W
19
27.622
58.662
34.483
1.00
19.48
O


ATOM
1583
OW0
HOH
W
20
12.579
47.128
55.855
1.00
16.64
O


ATOM
1584
OW0
HOH
W
21
5.023
62.006
44.777
1.00
17.04
O


ATOM
1585
OW0
HOH
W
22
12.419
69.310
25.291
1.00
22.84
O


ATOM
1586
OW0
HOH
W
23
18.045
48.671
59.395
1.00
34.19
O


ATOM
1587
OW0
HOH
W
24
21.204
72.606
40.012
1.00
19.76
O


ATOM
1588
OW0
HOH
W
25
8.025
55.157
31.622
1.00
19.49
O


ATOM
1589
OW0
HOH
W
26
21.198
59.382
32.295
1.00
16.12
O


ATOM
1590
OW0
HOH
W
27
26.059
47.843
37.230
1.00
20.06
O


ATOM
1591
OW0
HOH
W
28
23.148
42.497
59.773
1.00
20.86
O


ATOM
1592
OW0
HOH
W
29
15.204
68.185
50.111
1.00
23.32
O


ATOM
1593
OW0
HOH
W
30
13.652
67.881
37.933
1.00
24.96
O


ATOM
1594
OW0
HOH
W
31
7.882
66.774
31.839
1.00
28.46
O


ATOM
1595
OW0
HOH
W
32
20.646
71.206
42.370
1.00
16.13
O


ATOM
1596
OW0
HOH
W
33
28.643
37.966
50.225
1.00
34.91
O


ATOM
1597
OW0
HOH
W
34
9.845
56.350
30.277
1.00
20.05
O


ATOM
1598
OW0
HOH
W
35
28.649
40.248
55.059
1.00
23.37
O


ATOM
1599
OW0
HOH
W
36
8.995
59.883
55.595
1.00
35.28
O


ATOM
1600
OW0
HOH
W
37
9.497
44.727
54.972
1.00
27.65
O


ATOM
1601
OW0
HOH
W
38
3.544
51.694
37.348
1.00
19.23
O


ATOM
1602
OW0
HOH
W
39
8.560
64.565
24.883
1.00
36.70
O


ATOM
1603
OW0
HOH
W
40
7.634
78.032
23.865
1.00
79.88
O


ATOM
1604
OW0
HOH
W
41
28.072
34.958
45.439
1.00
29.28
O


ATOM
1605
OW0
HOH
W
42
5.695
48.163
44.053
1.00
23.93
O


ATOM
1606
OW0
HOH
W
43
3.718
38.814
35.388
1.00
28.41
O


ATOM
1607
OW0
HOH
W
44
7.063
67.338
24.804
0.50
44.82
O


ATOM
1608
OW0
HOH
W
45
23.810
53.672
33.588
1.00
20.53
O


ATOM
1609
OW0
HOH
W
46
25.722
66.756
37.670
1.00
21.69
O


ATOM
1610
OW0
HOH
W
47
22.474
43.283
37.008
1.00
31.52
O


ATOM
1611
OW0
HOH
W
48
1.425
57.265
52.722
1.00
36.34
O


ATOM
1612
OW0
HOH
W
49
11.169
64.598
28.922
1.00
28.96
O


ATOM
1613
OW0
HOH
W
50
34.865
61.830
51.709
1.00
29.19
O


ATOM
1614
OW0
HOH
W
51
20.529
48.485
57.562
1.00
24.13
O


ATOM
1615
OW0
HOH
W
52
24.623
55.853
32.317
1.00
20.99
O


ATOM
1616
OW0
HOH
W
53
18.317
47.805
33.566
1.00
28.59
O


ATOM
1617
OW0
HOH
W
54
12.895
50.563
28.740
1.00
28.50
O


ATOM
1618
OW0
HOH
W
55
−6.406
62.362
36.578
1.00
29.56
O


ATOM
1619
OW0
HOH
W
56
9.486
71.154
31.652
1.00
30.54
O


ATOM
1620
OW0
HOH
W
57
4.077
66.859
46.968
1.00
23.74
O


ATOM
1621
OW0
HOH
W
58
6.314
42.630
49.426
1.00
38.02
O


ATOM
1622
OW0
HOH
W
59
7.069
33.565
57.902
1.00
33.17
O


ATOM
1623
OW0
HOH
W
60
10.022
65.589
31.172
1.00
25.32
O


ATOM
1624
OW0
HOH
W
61
−4.508
58.652
36.641
1.00
25.95
O


ATOM
1625
OW0
HOH
W
62
1.246
50.368
36.771
1.00
23.12
O


ATOM
1626
OW0
HOH
W
63
18.779
58.847
31.608
1.00
22.18
O


ATOM
1627
OW0
HOH
W
64
10.843
63.364
23.031
1.00
32.27
O


ATOM
1628
OW0
HOH
W
65
20.715
62.939
42.136
1.00
29.55
O


ATOM
1629
OW0
HOH
W
66
0.328
69.253
45.663
1.00
51.19
O


ATOM
1630
OW0
HOH
W
67
27.567
64.900
34.385
1.00
28.74
O


ATOM
1631
OW0
HOH
W
68
39.584
55.441
52.982
1.00
56.79
O


ATOM
1632
OW0
HOH
W
69
22.538
62.716
53.219
1.00
31.08
O


ATOM
1633
OW0
HOH
W
70
2.632
68.395
43.791
1.00
45.23
O


ATOM
1634
OW0
HOH
W
71
13.947
35.361
33.766
1.00
28.13
O


ATOM
1635
OW0
HOH
W
72
35.236
59.612
45.072
1.00
56.78
O


ATOM
1636
OW0
HOH
W
73
0.229
49.559
39.212
1.00
30.20
O


ATOM
1637
OW0
HOH
W
74
0.068
61.386
44.549
1.00
33.50
O


ATOM
1638
OW0
HOH
W
75
20.812
70.177
47.212
1.00
29.48
O


ATOM
1639
OW0
HOH
W
76
33.222
41.166
46.547
1.00
102.49
O


ATOM
1640
OW0
HOH
W
77
32.816
57.977
51.761
1.00
40.60
O


ATOM
1641
OW0
HOH
W
78
6.562
43.845
33.931
1.00
35.81
O


ATOM
1642
OW0
HOH
W
79
18.456
56.610
32.498
1.00
28.33
O


ATOM
1643
OW0
HOH
W
80
27.538
69.465
35.257
1.00
32.01
O


ATOM
1644
OW0
HOH
W
81
26.080
52.220
32.438
1.00
41.15
O


ATOM
1645
OW0
HOH
W
82
27.106
47.009
58.301
1.00
34.89
O


ATOM
1646
OW0
HOH
W
83
23.231
64.872
28.117
1.00
31.34
O


ATOM
1647
OW0
HOH
W
84
24.934
64.631
52.680
1.00
31.24
O


ATOM
1648
OW0
HOH
W
85
3.258
42.665
38.698
1.00
31.19
O


ATOM
1649
OW0
HOH
W
86
18.392
36.517
33.372
1.00
30.32
O


ATOM
1650
OW0
HOH
W
87
24.722
46.488
59.681
1.00
35.45
O


ATOM
1651
OW0
HOH
W
88
16.606
65.079
28.152
1.00
29.22
O


ATOM
1652
OW0
HOH
W
89
8.072
43.179
52.938
1.00
33.09
O


ATOM
1653
OW0
HOH
W
90
−1.402
61.539
41.769
1.00
34.63
O


ATOM
1654
OW0
HOH
W
91
34.094
43.537
51.724
1.00
38.99
O


ATOM
1655
OW0
HOH
W
92
17.093
54.167
30.473
1.00
36.50
O


ATOM
1656
OW0
HOH
W
93
8.340
67.613
47.745
1.00
28.60
O


ATOM
1657
OW0
HOH
W
94
6.149
52.606
56.112
1.00
37.53
O


ATOM
1658
OW0
HOH
W
95
2.948
40.454
40.144
1.00
30.02
O


ATOM
1659
OW0
HOH
W
96
28.110
49.723
54.553
1.00
38.42
O


ATOM
1660
OW0
HOH
W
97
22.675
57.203
31.092
1.00
29.09
O


ATOM
1661
OW0
HOH
W
98
30.410
50.169
49.746
1.00
35.38
O


ATOM
1662
OW0
HOH
W
99
20.420
54.974
31.004
1.00
36.31
O


ATOM
1663
OW0
HOH
W
100
−4.624
67.662
37.763
1.00
29.29
O


ATOM
1664
OW0
HOH
W
101
32.903
59.925
53.842
1.00
57.65
O


ATOM
1665
OW0
HOH
W
102
8.251
48.921
57.957
1.00
32.56
O


ATOM
1666
OW0
HOH
W
103
9.529
69.708
43.742
1.00
34.52
O


ATOM
1667
OW0
HOH
W
104
−1.125
51.287
33.096
1.00
51.90
O


ATOM
1668
OW0
HOH
W
105
22.008
61.060
30.191
1.00
33.62
O


ATOM
1669
OW0
HOH
W
106
7.453
59.198
61.616
1.00
70.12
O


ATOM
1670
OW0
HOH
W
107
−0.874
51.284
40.694
1.00
35.22
O


ATOM
1671
OW0
HOH
W
108
20.943
41.645
35.526
1.00
32.26
O


ATOM
1672
OW0
HOH
W
109
5.620
70.636
25.877
1.00
61.44
O


ATOM
1673
OW0
HOH
W
110
22.275
54.122
60.734
1.00
36.32
O


ATOM
1674
OW0
HOH
W
111
26.307
66.084
49.785
1.00
34.11
O


ATOM
1675
OW0
HOH
W
112
11.407
48.301
58.411
1.00
29.02
O


ATOM
1676
OW0
HOH
W
113
26.806
63.460
31.122
1.00
34.71
O


ATOM
1677
OW0
HOH
W
114
8.884
30.582
40.992
1.00
36.30
O


ATOM
1678
OW0
HOH
W
115
11.479
63.554
59.426
1.00
56.37
O


ATOM
1679
OW0
HOH
W
116
14.803
63.347
29.162
1.00
39.68
O


ATOM
1680
OW0
HOH
W
117
12.150
53.474
60.742
1.00
41.19
O


ATOM
1681
OW0
HOH
W
118
28.575
47.112
48.173
1.00
34.99
O


ATOM
1682
OW0
HOH
W
119
10.076
30.133
34.488
1.00
47.15
O


ATOM
1683
OW0
HOH
W
120
28.402
61.033
31.016
1.00
39.73
O


ATOM
1684
OW0
HOH
W
121
25.479
67.945
46.049
1.00
39.36
O


ATOM
1685
OW0
HOH
W
122
0.734
56.578
47.909
1.00
38.00
O


ATOM
1686
OW0
HOH
W
123
9.395
49.839
30.508
1.00
35.16
O


ATOM
1687
OW0
HOH
W
124
31.550
49.603
47.391
1.00
32.71
O


ATOM
1688
OW0
HOH
W
125
0.816
41.368
43.751
1.00
35.22
O


ATOM
1689
OW0
HOH
W
126
5.486
47.377
47.613
1.00
44.89
O


ATOM
1690
OW0
HOH
W
127
31.113
51.669
45.682
1.00
38.04
O


ATOM
1691
OW0
HOH
W
128
1.436
59.923
42.862
1.00
26.88
O


ATOM
1692
OW0
HOH
W
129
18.586
43.366
33.846
1.00
38.47
O


ATOM
1693
OW0
HOH
W
130
16.561
69.834
48.474
1.00
32.88
O


ATOM
1694
OW0
HOH
W
131
34.295
43.982
47.100
1.00
68.28
O


ATOM
1695
OW0
HOH
W
132
5.298
34.689
38.229
1.00
49.39
O


ATOM
1696
OW0
HOH
W
133
3.300
35.280
40.898
1.00
35.60
O


ATOM
1697
OW0
HOH
W
134
12.437
70.145
37.142
1.00
40.97
O


ATOM
1698
OW0
HOH
W
135
27.766
65.255
29.010
1.00
36.38
O


ATOM
1699
OW0
HOH
W
136
6.084
41.962
46.625
1.00
47.13
O


ATOM
1700
OW0
HOH
W
137
5.960
49.922
55.359
1.00
34.78
O


ATOM
1701
OW0
HOH
W
138
19.695
36.565
36.333
1.00
37.61
O


ATOM
1702
OW0
HOH
W
139
26.815
55.165
58.919
1.00
61.16
O


ATOM
1703
OW0
HOH
W
140
21.895
52.796
31.863
1.00
42.17
O


ATOM
1704
OW0
HOH
W
141
1.460
65.803
50.346
1.00
40.26
O


ATOM
1705
OW0
HOH
W
142
4.323
46.032
44.857
1.00
37.04
O


ATOM
1706
OW0
HOH
W
143
13.181
47.109
33.427
1.00
40.11
O


ATOM
1707
OW0
HOH
W
144
18.021
60.476
62.244
1.00
58.10
O


ATOM
1708
OW0
HOH
W
145
34.229
42.239
57.157
1.00
45.39
O


ATOM
1709
OW0
HOH
W
146
22.591
48.081
59.775
1.00
32.69
O


ATOM
1710
OW0
HOH
W
147
7.290
34.657
36.557
1.00
38.37
O


ATOM
1711
OW0
HOH
W
148
30.205
51.763
38.560
1.00
43.21
O


ATOM
1712
OW0
HOH
W
149
9.512
60.561
58.672
1.00
47.60
O


ATOM
1713
OW0
HOH
W
150
1.012
47.871
35.078
1.00
33.28
O


ATOM
1714
OW0
HOH
W
151
28.668
53.537
56.609
1.00
43.90
O


ATOM
1715
OW0
HOH
W
152
29.440
57.784
36.320
1.00
46.19
O


ATOM
1716
OW0
HOH
W
153
14.716
41.521
57.984
1.00
42.10
O


ATOM
1717
OW0
HOH
W
154
2.405
29.431
51.398
1.00
54.51
O


ATOM
1718
OW0
HOH
W
155
15.742
47.273
34.380
1.00
32.73
O


ATOM
1719
OW0
HOH
W
156
−0.872
51.922
36.097
1.00
28.11
O


ATOM
1720
OW0
HOH
W
157
31.688
65.491
39.530
1.00
39.88
O


ATOM
1721
OW0
HOH
W
158
21.560
46.873
62.631
1.00
38.78
O


ATOM
1722
OW0
HOH
W
159
−0.474
56.276
45.289
1.00
46.96
O


ATOM
1723
OW0
HOH
W
160
6.427
28.246
48.315
1.00
36.54
O


ATOM
1724
OW0
HOH
W
161
31.532
37.651
51.492
1.00
56.31
O


ATOM
1725
OW0
HOH
W
162
9.015
29.318
55.310
1.00
42.95
O


ATOM
1726
OW0
HOH
W
163
28.298
64.095
52.742
1.00
50.08
O


ATOM
1727
OW0
HOH
W
164
−0.594
60.533
46.930
1.00
41.52
O

## Claims

1. A laminin receptor (LamR) crystal comprising residues 1-220 of the full-length human 37 kDa LamR protein, wherein said protein is in the tetragonal spacegroup P43212 and has unit cell dimensions of a=75.7 Angstroms, b=75.7 Angstroms and c=99.0 Angstroms.

2. The LamR crystal of claim 1 having atomic structure coordinates listed in Appendix 1, or any part thereof.

3. The LamR crystal of claim 1 having an active site including relative structural coordinates of amino acid residues Leu25, Gly26, Gly27 Ile46, Arg80, Asp126, Arg128, Asn149, Asp151, Ser152, Asp164, Asp165, Lys166, Gln33, Gln35, Tyr36, Lys57, Ala137, Ser138, Asn141, Leu142, Pro143, Thr144, Met10, Leu19, His24, Ile49, Asn50, Leu51, Lys52, Gln9, Lys11, Trp55, Leu59, Glu181, Arg184, Met185 and Arg191, or any portion thereof, and having a root mean square deviation from residue backbone atoms of said amino acid residues of not more than 1.5 Å.

4. The LamR crystal of claim 3, wherein
said active site is complexed with a compound,
said active site includes, relative structural coordinates of amino acid residues: Leu25, Gly26, Gly27, Thr28, Ile46, Asp126, Pro127, Arg128, Ala129, Asn149, Asp151, Ser152, Asn164, Asn165, Lys166, Val15, Phe18, Leu19, His24, Leu25, Ile49, Asn50, Leu51, and Lys52, Arg80 and Asn81, or any portion thereof, and
a root mean square deviation from residue backbone atoms of said amino acid residues being not more than 1.5 Å.

5. The LamR crystal of claim 3, wherein
said active site is complexed with a protein or peptide,
said active site includes relative structural coordinates of amino acid residues: Gln33, Leu60, Arg63, Ala64, Ala67, Asn70, Pro71, Ala72, Asp73, Val74, Ser75, Ala91, Ala92, Ala93, Thr94, Gly95, Ala96, Thr97, Pro98, Ile99, Arg102, Phe103, Thr104, Pro105, Gly106, Thr107, Phe108, Thr109, Asn110, Gln111, Ile112, Gln113, Ala114, Ala115, Phe116, Arg117, Glu118, Pro119, Arg120, Leu121, Leu134, Ala137, Ser138, Asn141, Leu142, Pro143, Thr144, Ile145, Leu154, Arg155, Tyr156, Val157, Asp158, Ile159, Leu183, Arg186, or any portion thereof, and
a root mean square deviation from residue backbone atoms of said amino acid residues being not more than 1.5 Å.

6. The LamR crystal of claim 3, wherein
said active site is complexed with a protein or peptide,
said active site includes relative structural coordinates of amino acid, residues: Ala72, Asp73, Val74, Ser75, Thr97, Ile99, Thr104, Pro105, Gly106, Thr107, Phe108, Asn110, Gln111, Ile112, Gln113, Ala114, Ala115, Phe116, Arg117, Glu118, Pro119, or any portion thereof, and
a root mean square deviation from residue backbone atoms of said amino acid residues being not more than 1.5 Å.