# Patent

## Title
Crystal of GTP Cyclohydrolase Type IB

## Abstract

This invention relates to a novel, bacterial GTP Cyclohydrolase Type IB enzyme, and the crystal structure thereof.

## Background
RELATED APPLICATIONS
The present application is a continuation-in-part of U.S. patent application Ser. No. 12/670,438, filed Jan. 25, 2010; which is a U.S. national phase application of PCT/US08/71358, filed Jul. 28, 2008; and which is related to and claims the priority benefit of U.S. Provisional Patent Application Ser. No. 60/935,124, “entitled Novel GTP Cyclohydrolase Type IB,” filed Jul. 26, 2007.


This invention was made with United States government support under Grant R01 GM70641-01 awarded by the National Institutes of Health, and Award No. MCB-0516948 awarded by the National Science Foundation. The Stanford Synchrotron Research Laboratory Structural Molecular Biology Program is supported by the Department of Energy, National Institutes of Health, and the National Institute of General Medical Sciences. The government has certain rights in the invention.


BACKGROUND
Bacterial diseases, such as those caused by Neisseria gonorrhea and Staphylococcus aureus, pose significant disease and health risks. N. gonorrhoeae is the causative agent of the sexually transmitted disease gonorrhea (infection of the genitalia, and urinary tract) and cause of pelvic inflammatory disease and infertility in one million women a year. Worldwide, there are an estimated 62 million new cases a year, with an average of 22 million cases at any given time. About 0.8 million new gonorrhea infections are reported each year in the U.S. primarily among teenage females and African Americans, costing $1.1 billion/year in treatment and related expenses. Importantly, gonorrhea infections increase the transmission and susceptibility to human immunodeficiency virus infection. Moreover, gonorrhea has become resistant to traditional treatments with quinolone (ciprofloxacin), tetracycline, penicillin, and sulfonamides. Currently, twenty percent of reported gonorrhea cases in the U.S. and Europe are resistant to all of these drugs, with the highest resistance seen among homosexual males. Although gonorrhea can now be treated with ultra high doses of azithromycin, resistance to that antibiotic is also emerging.
The S. aureus bacterium currently causes the most common and serious infections that occur in hospitalized patients. In recent years, S. aureus has become resistant to antibiotics (thus named Multidrug- or Methicillin-Resistant S. aureus, MRSA), causing a serious public health problem in the United States and worldwide. Sixty percent of intensive-care-unit infections in the U.S. are caused by MRSA, leading to significant mortality. The MRSA “superbug” multiplies very rapidly in the bloodstream causing toxic shock syndrome, and/or on the skin causing furuncles. Once an infection occurs, it is almost impossible to treat with existing antibiotics, especially in immune-compromised and elderly patients. When an incurable MRSA infection reaches the heart, it often causes fatal endocarditis.
Hence, there is a growing need for alternative treatments against such bacterial pathogens.
SUMMARY OF THE INVENTION
An object of the present invention provides for a novel avenue for combating bacterial pathogens by targeting specific enzymes that archaea and bacteria, but not eukarya, require. One embodiment of the present invention presents a novel, purified bacterial enzyme, GTP Cyclohydrolase Type IB (GCYH-IB).
Another embodiment provides for the crystalline structure of GCYH-IB. A related embodiments provides a GCYH-IB crystal. Yet another related embodiment provides for a computer-readable medium having GTP Cyclohydrolase Type IB crystal structure information stored thereon.



DESCRIPTION OF THE DRAWINGS
FIG. 1 presents a diagram of the reaction catalyzed by GTP Cyclohydrolase Type I (GCYH-I), and the metabolic fate of H2NTP.
FIG. 2 shows the overall structure of GTP Cyclohydrolase Type IB (GCYH-IB). Panel 2A is a ribbon diagram showing a side view (left) and a top view (right) of the full biological tetramer. Panel 2B is a stereo view of a FOM-weighted experimental electron density map (resolution 2.2 Å, contour level 1.5 σ), calculated after solvent flattening, in the β-sheet region. The map is superimposed on the refined model. The figure was prepared with BobScript software. Esnouf, 55(4) Acta Crystallogr. D Biol. Crystallogr. 938-40 (1999).
FIG. 3 depicts the topology of the GCYH-IB monomer and structural comparison with other T-fold enzymes. Panel 3A presents topology diagrams of N. gonorrhoeae GCYH-IB. Panel 3B: of A. flavus urate oxidase; Panel 3C: of E. coli GCYH-IA. Michalopoulos et al., 32 Nucleic Acids Res. D251-54 (2004). The N- and C-terminal modules of the core bimodular T-fold are colored in gray and light gray, respectively. Cα trace superpositions of the N- (gray) and C-terminal (light gray) modules of GCYH-IB with corresponding enzymes are shown in Panel B and panel C. Secondary structure nomenclature is shown for the two GCYH-I enzymes.
FIG. 4 presents structure-guided multi-sequence alignment of GCYH-IA and GCYH-IB in the shared T-fold region. For clarity, only four sequences are shown from each subfamily. Residue labels and secondary structure elements (from the crystal structures) are shown above and below the sequence alignment for enzyme subfamilies A and B, respectively. Secondary structure nomenclature is as in FIG. 3. Residues conserved between the two subfamilies are vertically outlined, with the strictly conserved residues (the substrate binding Glu and zinc binding Cys) highlighted in dark gray. Conserved regions within GCYH-IB subfamily are boxed. The zinc ion-liganding side chains in each subfamily are labeled with gray stars. The Mn-liganding side chains in GCYH-IB are labeled with black stars. # indicates a zinc liganding side chain from the neighboring subunit. Ec: Escherichia coli (SEQ ID NO: 1), Tt: Thermus thermophilus (SEQ ID NO: 2), Hs: Homo sapien (SEQ ID NO: 3), Rn: Rattus norvegicus (SEQ ID NO: 4), Tm: Thermotoga maritime (SEQ ID NO: 5), Bs: Bacillus subtilis (SEQ ID NO: 6), Sa: Staphylococcus aureus (SEQ ID NO: 7), Ng: Neisseria gonorrhoeae (SEQ ID NO: 8).
FIG. 5 depicts the metal site in GCYH-IB. Panel A shows a stereoview of annealed Fo-Fc electron density map (1500 K, 2.2 Å, 2.5 σ, Zn2+ and its ligands omitted from the phase calculation) superimposed on the model. Panel B shows the Mn2+-occupied metal site in the GCYH-IB.Mn2+ complex. Stereoview of annealed omit Fo-Fc electron density map (1500 K, 2.04 Å, 2.5 σ, Mn2+ and its ligands omitted from phase calculation) superposed on the model. Metal ions and water molecules are shown as spheres. Secondary structure elements in GCYH-IB are labeled.
FIG. 6 presents a 3D alignment of GCYH-IB (regular labels) and T. thermophilus GCYH-IA (italic labels) in the active-site region. Strictly conserved Cys149 in the metal binding loop of GCYH-IB is shown although it does not interact with the bound metal.
FIG. 7 illustrates the physical clustering of GCYH-IB (labeled COG1469) encoding genes with folate biosynthetic genes, such as folK, folP, and folM (an alternative dihydrofolate reductase gene). Rebelo et al., 326(2) J. Mol. Biol. 503-16 (2003).
FIG. 8 depicts various complementation data of the dT auxotrophy on LB (Panel A) or the slow growth phenotype on LB dT (Panel B) of the E. coli folE::KanR by pBAD derivatives expressing the GCYH-IB genes from B. subtilis (BsfolE2) and A. baylyi (AcfolE2). Panel C shows complementation of the slow growth on LB in the presence of dT of the E. coli folE::KanR by a plasmid expressing TM0039 (TmfolE2). The control is folE::KanR transformed by pBAD24. The plates were incubated at 37° C. for 48 h. Panel D presents PCR amplification to check for the presence of the folE::KanR allele (lanes 2, 4, 6, and 8) and to check for the presence of an insert of the expected size in the pBAD derivatives (lanes 3, 5, 7, and 9) was performed on the folE::KanR strain transformed with plasmids expressing AcfolE2 (lanes 2 and 3), BsfolE2 (lanes 4 and 5), and TmfolE2 (lanes 6 and 7) and with the pBAD24 control (lanes 8 and 9). The expected size of the PCR product detecting folE::KanR is about 3.5 kb, whereas the same primers amplify a 2.5-kb product in the wild type strain. The sizes of the PCR products resulting from having AcfolE2, BsfolE2, or TmfolE2 in pBAD24 are 1072, 1105, and 960 bp, respectively.
FIG. 9 graphically depicts GCYH-I activity assays. Panel 9A shows UV-visible spectra of cyclohydrolase assays. Line a, E. coli FolE; b, GCYH-IB protein from N. gonorrhoeae; c, GCYH-IB protein from B. subtilis; d, no enzyme. Panel 9B reflects fluorescence spectra of authentic neopterin and cyclohydrolase assays following post-reaction dephosphorylation and oxidation. Fluorescence was measured with excitation at 365 nm. Line a, T. maritima GCYH-IB; b, B. subtilis GCYH-IB; line c, E. coli FolE; d, authentic neopterin; e, N. gonorrhoeae GCYH-IB. Panel 9C presents HPLC chromatograms of authentic neopterin (line a) and cyclohydrolase assays with E. coli FolE (line b), B. subtilis GCYH-IB added to authentic neopterin (line c), and B. subtilis GCYH-IB alone (line d). Enzyme assays were subjected to postreaction dephosphorylation and oxidation.
FIG. 10 presents B. subtilis GCYH-IB enzymatic activity versus [Mn2+] (◯) or [Zn2+] (●). Each data point represents the average of four sets of triplicate assays.
FIG. 11 reflects GCYH-IB-dependent complementation of the B. subtilis ΔfolE mutant strain. Growth curves in rich medium of wild type (WT) and mutant B. subtilis strains expressing either type of GCYH-I. Strains and their corresponding expressed GCYH-I isozyme are listed.
FIG. 12 shows data from X-ray emission and fluorescence scans of bound metals in GCYH-IB crystals. Panel A reflects the fluorescence spectrum from GCYH-IB crystal taken near the zinc absorption edge. Panels B and C are emission scan and fluorescence spectrum, respectively, from GCYH-IB.Mn2+ crystal taken near the manganese K-shell absorption edge. Inflection points in the fluorescence spectra are indicated with vertical lines. The large peak in panel B corresponds to scattering from the main beam.
FIG. 13 is a Table of candidate Zur-binding sites upstream of folE2 in bacterial genomes. Distance is given in nucleotides relative to the start codon of the downstream gene. The Table contains candidate Zur-binding sites for the following bacterial genomes: PROTEOBACTERIA Consensus Zur-binding site (SEQ ID NO: 9); Serratia marcescens (SEQ ID NO: 10); Klebsiella pneumonia (SEQ ID NO: 11); Acinetobacter sp. ADP I (SEQ ID NO: 12); Methylococcus capsulatus (SEQ ID NO: 13); Chromohalobacter salexigens DSM 3043 (SEQ ID NO: 14); Hahella chejuensis KCTC 2396 (SEQ ID NO: 15); Pseudoalteromonas atlantica T6c (SEQ ID NO: 16); Pseudomonas aeruginosa (SEQ ID NO: 17); Pseudomonas entomophila L48 (SEQ ID NO: 18); Pseudomonas fluorescens Pf 5 (SEQ ID NO: 19); Pseudomonas syringae (SEQ ID NO: 20); Pseudomonas putida (SEQ ID NO: 21); Azotobacter vinelandii (SEQ ID NO: 22); Xanthomonas axonopodis (SEQ ID NO: 23); Xanthomonas campestris (SEQ ID NO: 24); Xylella fastidiosa (SEQ ID NO: 25); Burkholderia cepacia R18194 (SEQ ID NO: 26); Burkholderia cenocepacia AU 1054 (SEQ ID NO: 27); Ralstonia metallidurans (SEQ ID NO: 28); BACILLI Consensus Zur-binding site (SEQ ID NO: 29); Bacillus subtilis (SEQ ID NO: 30); Bacillus licheniformis (SEQ ID NO: 31); Bacillus halodurans (SEQ ID NO: 32).



DETAILED DESCRIPTION
It should be understood that this invention is not limited to the particular methodology, protocols, and reagents, etc., described herein and as such may vary. The terminology used herein is for the purpose of describing particular embodiments only, and is not intended to limit the scope of the present invention, which is defined solely by the claims.
As used herein and in the claims, the singular forms “a,” “an,” and “the” include the plural reference and equivalents known to those skilled in the art unless the context clearly indicates otherwise. Other than in the operating examples, or where otherwise indicated, all numbers expressing quantities of ingredients or reaction conditions used herein should be understood as modified in all instances by the term “about.”
All patents and other publications identified are incorporated herein by reference for the purpose of describing and disclosing, for example, the methodologies described in such publications that might be used in connection with the present invention, but are not to provide definitions of terms inconsistent with those presented herein. These publications are provided solely for their disclosure prior to the filing date of the present application. Nothing in this regard should be construed as an admission that the inventors are not entitled to antedate such disclosure by virtue of prior invention or for any other reason. All statements as to the date or representation as to the contents of these documents is based on information available to the applicants and do not constitute any admission as to the correctness of the dates or contents of these documents.
Unless defined otherwise, all technical and scientific terms used herein have the same meaning as those commonly understood to one of ordinary skill in the art to which this invention pertains. When COG1469 is used in the context of a protein or gene family, it is synonymous with GCYH-IB protein or gene family.
Folic acid or folate is an essential metabolite in all life forms. It is used by all cells for the biosynthesis of purines (building blocks of DNA and RNA), amino acids, and vitamins. Unlike humans, who need folic acid as a dietary supplement, bacteria and yeast biosynthesize folic acid de novo. As a result, folate biosynthesis in bacteria and yeast has become an attractive target in antibacterial therapeutics. For example, sulfonamides, the first synthetic drugs developed with broad antibacterial activity, target a late step in the bacterial folate biosynthetic pathways. Emerging resistance to existing antibiotics spurs the quest for new and more effective target points along the pathway. One such point is the first step in folate biosynthesis: the conversion of GTP to 7,8-dihydroneopterin triphosphate by the enzyme GTP cyclohydrolase I (GCYH-I). The presence in humans of a homologous enzyme (required for making biopterin, another metabolic co-factor distinct from folate), complicated the development of bacterial GCYH-I as a drug target.
The present invention provides for a novel GCYH-I family of enzymes, called GCYH-IB, that has been identified in pathogenic bacteria. El Yacoubi et al., 281(49) J. Biol. Chem. 37586-93 (2006), incorporated fully herein by this reference. Importantly, GCYH-IB is absent in humans. The present invention identifies the biochemical properties and crystal structure of GCYH-IB from the pathogenic bacterium N. gonorrhoeae. The unique structure of the active center and the new metal dependency of this cyclohydrolase suggest an enzymatic mechanism distinct from that of the canonical GCYH-I. The differences in the active-site architecture and enzymatic mechanism of the two subtypes of GCYH-I enzymes can be exploited for the design of selective inhibitors of the bacteria-specific enzyme. Realization of such a goal allows for development of GCYH-IB as a therapeutic target for antibacterial pharmaceuticals. Furthermore, the presence of GCYH-IB as the sole GTP-cyclohydrolase in two clinically important human pathogens, N. gonorrhoeae and S. aureus, allows investigations of this enzyme as a potential drug target against the antibiotic resistant forms of gonorrhea and MRSA infections.
More specifically, regarding folate biosynthesis, folic acid in the form of various tetrahydrofolate (THF) derivatives serves as a cofactor in one-carbon transfer reactions during the synthesis of purines, thymidylate, pantothenate, glycine, serine and methionine, in all kingdoms of life. Nichol et al., 54 Ann. Rev. Biochem. 729-64 (1985). In bacteria, THF is also involved in the biosynthesis of the initiator formylmethionyl-tRNA. Clark & Marker, 17(2) J. Mol. Biol. 394-406 (1966). Plants, fungi, and most bacteria synthesize THF de novo from GTP and p-aminobenzoic acid (pABA). Green et al., in E. COLI & SALMONELLA, CELLULAR & MOLECULAR BIOL. 665-73 (Neidhart, ed., Am. Soc. Micro., Washington, D.C., 1996); Cossins & Chen, 45(3) Phytochem. 437-52 (1997); Hanson & Gregory, 5(3) Curr. Opin. Plant Biol. 244-49 (2002). Animals lack key enzymes of the folate biosynthetic pathway, and thus require a dietary source of folate for normal growth and development. Lucock, 71(1) Mol. Genet. Metab. 121-38 (2000).
GTP cyclohydrolase I (GCYH-I; EC 3.5.4.16) is the first enzyme of the de novo THF pathway (FIG. 1). Nichol et al., 1985. It is encoded in E. coli by the folE gene (Katzenmeier et al., 372(11) Biol. Chem. Hoppe Seyler 991-97 (1991); Schoedon et al., 210(2) Eur. J. Biochem. 561-68 (1992)), and catalyzes a complex reaction that begins with hydrolytic ring opening of the purine ring at C8 to generate an N-formyl intermediate, which is then the site for a second hydrolysis with concomitant loss of C8 as formic acid. Yim & Brown 251(16) J. Biol. Chem. 5087-94 (1976). In the subsequent steps of the reaction, the ribosyl moiety undergoes ring-opening and an Amidori rearrangement, followed by cyclization to generate the pterin ring in THF (FIG. 1). The product of GCYH-I, 7,8-dihydroneopterin triphosphate (H2NTP), is subsequently dephosphorylated to 7,8-dihydroneopterin by both specific and non specific phosphatases (Klaus et al., 280(7) J. Biol. Chem. 5274-80 (2005)), and the remainder of THF biosynthesis carried out by the enzymes encoded by the folBKPCA genes (in E. coli). Green et al., 1996.
The folate pathway has a storied history as an important target in antibacterial therapeutics and cancer chemotherapy. Dihydropteroate synthase is the target of the sulfonamides (Huovinen et al., 39(2) Antimicrobial Agents & Chemotherapeutics, 279-89 (1995)), and dihydrofolate reductase is the target of methotrexate, the first anticancer chemotherapy developed. A homologous GCYH-I is found in mammals and other higher eukaryotes, however, where it catalyzes the first step of the biopterin (BH4) pathway (FIG. 1), an essential cofactor in aromatic amino acid oxidation in the biosynthesis of tyrosine and neurotransmitters such as serotonin and L-DOPA. Thony et al., 347(1) Biochem. J. 1-16 (2000); Bonafe et al., 69(2) Am. J. Human Genet. 269-77 (2001). Although several enzymes in the folate pathway have proved important antimicrobial targets (Huovinen et al., 1995), the presence of homologous GCYH-I enzymes in both humans and bacteria has precluded the development of GCYH-I as a viable target.
The role of folate as an essential cofactor, coupled with the historical importance of the pathway in the development of antibacterial, antiparasitic, and anticancer therapies (Hoffbrand & Weir, 113(3) Brit. J. Haematol 579-89 (2001)), has led to folate metabolism being an especially well-characterized area of biology. The discovery of a novel, widely distributed folate biosynthetic enzyme, as described herein, illustrates the power of comparative genomic approaches to link genes and function. The signature genes of the de novo folate pathway, folP and folK, encode dihydropteroate synthase and 6-hydromethyl-7,8-dihydropterin pyrophosphokinase, respectively. All organisms that possess these two genes should have a homolog of the folE gene, because none of the metabolic intermediates from 7,8-dihydropterin triphosphate to 7,8-dihydro-hydroxymethylpterin pyrophosphate, are transported in bacteria. Skold, 3(3) Drug Resistance Update, 155-60 (2000).
The distribution of the folE/folE2 genes among the sequenced organisms in the SEED database (26 archaeal, 363 bacterial, and 29 eukaryeal more or less complete genomes) were analyzed. No FolE2 homolog was identified in the eukaryotic genomes, and there was significant variation in the distribution of the FolE/FolE2 genes among bacteria. Analysis of the distribution of the folE gene among all sequenced genomes that possessed folKP homologs revealed a large class of organisms that lacked folE homologs (Table 1), suggesting that folE was “locally missing” in these organisms. See also Koonin et al., 12(9) Trends Genet. 334-36 (1996); Suppl. data for El Yacoubi et al., 2006, available at JBC Online.







TABLE 1







Distribution of FolE, COG1469, FolK, and FolP homologs


in a subset of sequenced genomes. The genomes used in


the phylogenetic pattern search are in bold.











Organism
FolE
COG1469
FolK
FolP





Escherichia coli K12
+

+
+


Bacillus subtilis subsp. subtilis str. 168
+
+
+
+


Acinetobacter baylyi
+
+
+
+


  RB50

+
+
+


  FA 1090

+
+
+


  MC58

+
+
+


  FAM18

+
+
+


  ST-640

+
+
+


  ATC 19718

+
+
+


  HTE831

+
+
+


  subsp.   

+
+
+


MW2






  JCSC1435

+
+
+


 

+
+
+


  MSB8

+
+
+


  LSv54

+
+
+


 

+
+
+


  sp. 255-15

+
+
+


  PCA

+
+
+


  GS-15

+
+
+


  sp. MC-1

+
+
+


  KT

+
+
+


Silicobacter sp. TM1040[B]

+
+
+


  2.4.1

+
+
+


Idiomarina loihiensis L2TR

+
+
+


Oceanicola batsensis HTCC2597

+
+
+


Rhodobacterales bacterium HTCC2654

+
+
+


Roseovarius nubinhibens ISM [B]

+
+
+


Loktanella vestifoldensis SKA53

+
+
+


Thiomicrospira crunogena XCL-2

+
+
+


Sulfitobacter sp. EE-36

+
+
+


Roseobacter sp. MED193

+
+
+


 

+
+
+









Using a SEED tool that allows identification of protein families that follow a defined phylogenetic distribution profile, a search was conducted of the available genomes for protein families that were present in organisms that lack folE homologs (Table 1, in bold) and absent in E. coli. Five protein families fulfilled those phylogenetic criteria, one of which, COG1469, was of unknown function. Members of this family clustered physically with folate metabolism genes in several organisms. The combination of phylogenetic distribution and clustering suggested that the COG1469 family might encode the missing GCYH-I enzyme.
Further regarding the variation of the distribution, the first and largest group, which includes E. coli, has only a folE homolog. A second group, which includes S. aureus and N. gonorrhoeae, has only a folE2 homolog. A third group, including B. subtilis and A. baylyi, has a homolog of each gene, whereas a fourth group can possess multiple copies of the two genes (e.g. Pseudomonas aeruginosa has two folE genes and one folE2 gene). The need for several genes encoding type I cyclohydrolase enzymes in many organisms may be due to differential expression under specific environmental conditions or their involvement in pathways other than folate biosynthesis: for example, a GTP cyclohydrolase has been implicated in the biosynthesis of 7-deazaguanosine derivatives, such as the modified tRNA nucleoside queuosine (Kuchino et al., 3 Nucl. Acids. Res. 393-98 (1976)), and the secondary metabolites toyocamycin and tubercidin. Suhadolnik & Uematsu, 245(17) J. Biol. Chem. 4365-71 (1970); Smulson & Suhadolnik, 242(12) J. Biol. Chem. 2872-76 (1967). In B. subtilis, it has been shown that the yciA gene is not essential (Gaballa et al., 184 J. Bacteriol. 6508-14 (2002)), because a folE gene (mtrA) is also present in this organism. Yakhin & Babitze, 64(3) Appl. Microbiol. Biotech. 382-86 (2004). No folE2 deletions are available in bacteria that do not have another identified folE gene; but construction of the corresponding S. aureus mutant is possible.
Most archaeal genomes possess either a folE or a folE2 homolog. See El Yacoubi et al., 2006, Suppl. Data. Several GTP-derived metabolites are synthesized in Archaea, including folate in the halophiles and Sulfolobii (White, 170(10) J. Bacteriol. 4608-12 (1988)), tetrahydromethanopterin in the methanogens (Graham et al., 41(50) Biochem. 15074-84 (2002)), and the 7-deazaguanosine tRNA-modified nucleoside archaeosine (Gregson et al., 268(14) J. Biol. Chem. 10076-86 (1993)), which is found in the majority of archaeal tRNA. The archaeal folE/folE2 genes may be involved in one or more of these biosynthetic pathways.
As noted above, GCYH-IB has been identified in a wide variety of bacteria using the techniques described herein. Table 2 illustrates some of this distribution:







TABLE 2







Distribution of genes encoding GCYH-1B in prokaryotes.


Genome and gene ids are found in the SEED database.









Genome ID
Organism
GCYH-IB












272557.1
Aeropyrum pernix K1 [A]
1635


224325.1
Archaeoglobus fulgidus DSM 4304 [A]
1168


64091.1
Halobacterium sp. NRC-1 [A]
1638


348780.3
Nitrosamonas pharaonis DSM 2160 [A]
1042


18420.1
Methanothermobacter thermautotrophicus str.
1179



Delta H [A]



243232.1
Methanocaldococcus jannaschii DSM 2661
797



[A]



267377.1
Methanococcus maripaludis S2 [A]
34


259564.1
Methanococcoides burtonii DSM 6242 [A]
34


188937.1
Methanosarcina acetivorans C2A [A]
4403


269797.3
Methanosarcina barkeri str. fusaro [A]
1194


2208.1
Methanosarcina barkeri [A]
3612


192952.1
Methanosarcina mazei Go1 [A]
1222


190192.1
Methanopyrus kandleri AV19 [A]
483


272844.1
Pyrococcus abyssi GE5 [A]
362


18497.1
Pyrococcus furiosus DSM 3638 [A]
1881


69014.3
Thermococcus kodakaraensis [A]
1153


263820.1
Picrophilus torridus DSM 9790 [A]
1009


273116.1
Thermoplasma volcanium GSS1 [A]
1214


273075.1
Thermoplasma acidophilum DSM 1728 [A]
1117









Importantly, in addition to S. aureus and N. gonorrhoeae, there are significant pathogens that have GCYH-IB but do not have GCYH-IA, as shown in Table 3:







TABLE 3







Clinically important pathogens with GCYH-IB and lacking GCYH-IA.








Organism
Pathogenic Indication





Bordetella parapertussis 12822
Mammalian pathogen,


Bordetella parapertussis 12822
respiratory tract infection


Bordetella pertussis Tohama I



Neisseria gonorrhoeae FA 1090
Human pathogen, genital and



urinary tract infection


Neisseria meningitidis FAM18
Human pathogen, meningitis


Neisseria meningitidis MC58



Neisseria meningitidis ZZ491



Staphylococcus aureus RF122
Human pathogen, blood and


Staphylococcus aureus subsp. aureus COL; subsp.
skin infection, toxic shock


aureus JH1; subsp. aureus MRSA252; subsp. aureus
syndrome


MSSA476; subsp. aureus MW2; subsp. aureus Mu50;



subsp. aureus N315; subsp. aureus NCTC 8325; subsp.



aureus USA300; subsp. Aureus



Staphylococcus epidermidis ATCC 12228
Human pathogen, blood, skin,


Staphylococcus epidermidis RP62A
and catheter infection


Staphylococcus haemolyticus JCSC1435
Human pathogen, skin infection


Staphylococcus saprophyticus subsp. ATCC 15305
Human pathogen, acute urinary



tract infection









The primary structure of GCYH-IB proteins presents no homology to any other known protein family. Direct alignment of GCYH-IB and GCYH-IA sequences yields no detectable similarity. Protein fold recognition analysis using 1- and 3-dimensional sequence profiles, however, coupled with secondary structure and solvation potential information (using the 3D-PSSM server available on-line from the Structural Bioinformatics Group at the Imperial College, UK; Kelley et al., 299(2) J. Mol. Biol. 499-520 (2000)), indicates potential three-dimensional structural homology with two tunnel-fold (T-fold) enzymes, a structural superfamily of enzymes that includes GCYH-IA. Colloc'h et al., 39(2) Proteins 142-54 (2000). T-fold enzymes bind planar purine and pterin-like substrates but catalyze disparate reactions (id.), and although they characteristically exhibit low sequence homology, their tertiary structural homology is very high.
Using the N. gonorrhoeae sequence as a bait, the N-terminal half of GCYH-IB is most similar in predicted tertiary structure to 7,8-dihydroneopterin triphosphate epimerase (Protein Data Bank code 1B9L (44), PSSM E value 0.39), whereas the C-terminal half is similar to 7,8-dihydroneopterin aldolase (DHNA; Protein Data Bank code 1NBU (45), PSSM E value 0.3). These were the only PSSM hits with a qualifying E value (i.e., lower than the detection threshold E value of 1.00). Both hits are folate biosynthetic enzymes with homo-octameric structures. Both the size of GCYH-IB proteins (250-300 amino acids) and the fact that two T-fold domains can be detected in their sequences suggest that GCYH-IB members belong to the bimodular subfamily of the T-fold superfamily, which includes urate oxidase (Colloc'h et al., 4(11) Nat. Struct'l Biol. 947-52 (1997)), the plant GCYH-IA enzyme (Basset et al., 99(19) PNAS 12489-94 (2002)), and the novel nitrile oxidoreductase (class 2; e.g. YqcD from E. coli) recently reported. Van Lanen et al., 102(2) PNAS 4264-69 (2005). Preliminary sedimentation velocity and crystallographic analyses of N. gonorrhoeae GCYH-IB suggest either a trimeric or a tetrameric quaternary structure.
Of the enzymes involved in folate and biopterin biosynthesis, GCYH-IA has attracted particular attention (Nar et al., 1995; Tanaka et al., 138(3) J. Biochem. (Tokyo) 263-75 (2005); Schramek et al., 316(3) J. Mol. Biol. 829-38 (2002); Bracher et al., 273(43) J. Biol. Chem. 28132-141 (1998); Wolf & Brown, 192(3) Biochem. Biophys. Acta 468-78 (1969)), due to the mechanistic complexity inherent in the conversion of GTP to H2NTP. GCYH-IA activity is dependent on a catalytic Zn2+ atom (Auerbach et al., 97(25) PNAS 13567-72 (2000)), which functions as a Lewis acid in activating a water molecule for nucleophilic attack at C-8 of GTP in the initial hydrolytic step of the reaction. The Zn2+ further serves to facilitate nucleophilic attack of the second water molecule by polarizing the resulting amide carbonyl. The zinc-binding site in GCYH-IA is made up of Cys110, His113, and Cys181 (E. coli numbering), with water occupying the fourth coordination site.
Hence, GCYH-IB was discovered in microbes (20% of bacteria and most archaea) that do not encode the canonical GCYH-I (renamed GCYH-IA), including several clinically important pathogens such as N. gonorrhoeae and S. aureus. El Yacoubi et al., 2006. Importantly, GCYH-IB is absent in eukarya, including humans. A prediction of the 3D structure of GCYH-IB showed that, like GCYH-IA, GCYH-IB enzymes are members of the tunnel-fold (T-fold) structural superfamily. GCYH-IB enzymes from T. maritima, N. gonorrhoeae, and B. subtilis have been cloned and functionally characterized in vitro. The metal dependency of GCYH-IB was analyzed in vitro and was found to be distinct from that of GCYH-IA, with manganese as the preferred metal cofactor. The preference for manganese of the N. gonorrhoeae enzyme is consistent with the fact that this pathogen had evolved unique and complex manganese-based cellular mechanisms for coping with the high oxidative stress environment imposed on it by the innate immune response of the female urogenital tract. Seib et al., 70(2) Bio. Reviews 344-61 (2006). The primary defenses used by N. gonorrhoeae against oxidative stress include the intracellular accumulation of manganese by the MntABC transport system and the unusually high manganese-dependent catalase and peroxidase activities. The discovery of a manganese-dependent folate biosynthesis enzyme in N. gonorrhoeae paves the way to a new approach in targeting the folate biosynthesis pathway for the development of anti-gonorrhea antibiotics.
The present invention provides for the crystal structures of N. gonorrhoeae GCYH-IB and of the manganese-remetallated form of the enzyme. The aspect of the present invention reveals the enyzme's active center, including a metal binding site, which are distinct from those of the canonical enzyme. The structural differences between human GCYH-IA and bacterial GCYH-IB in the active center; including those in the metal binding site, suggest distinct enzymatic mechanisms. These differences offer the unique opportunity to design and test inhibitors specific to the bacterial enzyme (GCYH-IB) that will not inhibit the human enzyme.
As noted above, the Zn2+-dependent enzyme GTP cyclohydrolase I (GCYH-I; EC 3.5.4.16) is the first enzyme of the de novo tetrahydrofolate (THF) biosynthesis pathway (FIG. 1). Nichol et al., 54 Ann. Rev. Biochem. 729-64 (1985). THF is an essential cofactor in one-carbon transfer reactions in the synthesis of purines, thymidylate, pantothenate, glycine, serine, and methionine in all kingdoms of life (id.) and formylmethionyl-tRNA in bacteria. Clark & Marcker, 17 J. Mol. Biol. 394-406 (1966). GCYH-I is encoded in E. coli by the folE gene (Katzenmeier et al., 372 Biol. Chem. Hoppe Seyler 991-97 (1991)), and catalyzes the conversion of GTP to 7,8-dihydroneopterin triphosphate, a complex reaction that begins with hydrolytic opening of the purine ring at C-8 of GTP to generate an N-formyl intermediate, followed by deformylation and subsequent rearrangement and cyclization of the ribosyl moiety to generate the pterin ring in THF (FIG. 1). Yim & Brown, 251 J. Biol. Chem. 5087-94 (1976). An active-site Zn2+ activates a water molecule for nucleophilic attack at C-8 in the first step of the reaction.
The distribution of folE (gene product renamed GCYH-IA) and folE2 (GCYH-IB) in microbes is diverse. El Yacoubi et al, 326 J. Mol. Biol. 503-516 (2006). The majority of organisms possess either a folE (65%, e.g., E. coli) or a folE2 gene (14%, e.g., N. gonorrhoeae). A significant number (12%, e.g., B. subtilis) possess both genes (a subset of 50 bacterial species is shown in FIG. 13), and 9% lack both genes, although members of the latter group are mainly intracellular or symbiotic bacteria that rely on external sources of folate.







TABLE 4







Distribution and candidate Zur-dependent regulation


of alternative GCYH-I genes in bacteriaa











Organism
folE
18 folE2






Enterobacteria
+
−



Escherichia coli
+
−



Salmonella typhimurium
+
−



Yersinia pestis
+
+



Klebsiella pneumoniaeb
+
+



Serratia marcescens
+
−



Erwinia carotovora
+
−



Photorhabdus luminiscens
+
−



Proteus mirabilis
+
−



Gamma-proteobacteria





Vibrio cholerae
+
−



Acinetobacter sp. ADP1
+
+



Pseudomonas aeruginosa
+
+



Pseudomonas entomophila L48
+
+



Pseudomonas syringae
+
+



Pseudomonas putida
+
+



Hahella chejuensis KCTC 2396
+
+



Chromohalobacter salexigens
+
+



DSM 3043





Methylococcus capsulatus
+
+



Xanthomonas axonopodis
+
+



Xanthomonas campestris
+
+



Xylella fastidiosa
+
+



 
−
+



Colwellia psychrerythraea
+
+



Pseudoalteromonas atlantica T6c
+
+



Pseudoalteromonas haloplanktis
+
+



TAC125





Alteromonas macleodi
+
−



Nitrosococcus oceani
+
+



Legionella pneumophila
+
−



Francisella tularensis
+
−



Beta-proteobacteria





Chromobacterium violaceum
+
−



 
−
+



Burkholderia cepacia R18194
+
+



Burkholderia cenocepacia AU
+
+



1054





Burkholderia xenovorans
+
−



Burkholderia mallei
+
−



 
−
+



Ralstonia eutropha JMP134
+
−



Ralstonia metallidurans
+
+



Ralstonia solanacearum
+
−



 
−
+



 
−
+



Azoarcus sp.
+
+



Bacilli/Clostridia





Bacillus subtilisd
+
+



Bacillus licheniformis
+
+



Bacillus cereus
+
−



Bacillus halodurans s
+
+



Bacillus clausii
+
−



Geobacillu kaustophilus
+
−



 
−
+



 
−
+





aGenes that are preceded by candidate Zur binding sites are on grey background;


bZur-regulated cluster ison the virulence plasmid pLVPK;


cExamples of organisms with no folE genes are in bold;


dZn-dependent regulation of B. subtilis folE2 by Zur was experimentally verified (Gaballa et al., 2002).






Expression of the folE2 B. subtilis gene, yciA, is controlled by the Zn-dependent Zur repressor and should thus be up-regulated under Zn-limiting conditions. Gaballa et al. 184 J. Bacteriol., 6508-6514 (2002). Hence, the GCYH-IB family might utilize a metal other than Zn to allow growth in Zn-limiting environments. The metal dependence of B. subtilis GCYH-IB in vitro and in vivo was explored, revealing that that in organisms that contain both isozymes such as B. subtilis, only the Zn-dependent enzyme is expressed unless Zn becomes limiting. To gain a structural understanding of the metal dependence of GCYH-IB, the high-resolution crystal structures of Zn2+- and Mn2+-metallated forms of the N. gonorrhoeae ortholog were determined. The results shed light on the regulation of folate biosynthesis in organisms exposed to different metal environments and offer a structural understanding of this regulation.
GCYH-IB and GCYH-IA have different metal requirements in vitro. It is well established that GCYH-IA uses a bound Zn2+ ion for activity. Nichol et al., 1985. To investigate the metal dependence of GCYH-IB, the purified recombinant B. subtilis enzyme was assayed for activity in the presence of a variety of metal ions or EDTA. Although no activity was observed in the presence of EDTA, the presence of several metal ions supported catalysis. To obtain unambiguous, quantitative data on the effect of various metal ions on catalytic activity, the enzyme was first demetallated by dialyzing against an EDTA/Chelex-containing buffer to generate the apoenzyme, which was then assayed in the presence of specific metal ions over a broad concentration range. As shown in Table 5, catalysis is supported by the metal ions Mn2+, Fe2+, Mg2+, Co2+, Zn2+, and Ni2+, conversely Ca2+, Cd2+, Cu2+, Co3+, and Fe3+ fail to support activity:







TABLE 5







Metal dependence of B. subtilis GCYH-IB enzymatic activity











Metal
[Metal]a (μM)
Relative Activity (%)














No Metal
0
0



Mn(II)
500
100 



Fe(II)
1000
75 ± 8



Mg(II)
100
43 ± 4



Co(II)
100
24 ± 3



Zn(II)
50
14 ± 1



Ni(II)
100
 9.8 ± 1.3



Ca(II)
NAb
0



Cd(II)
NA
0



Cu(II)
NA
0



Co(III)
NA
0



Fe(III)
NA
0





aThe metal concentration for optimal activity.


bNA refers to no activity detected regardless of metal concentration.






Notably, although the enzyme exhibits some activity in the presence of Zn2+, catalysis is significantly higher in the presence of Mn2+, and to a lesser extent Fe2+ and Mg2+. Interestingly, the optimum metal concentration required for catalysis is roughly 10-fold lower for Zn2+ than it is for Mn2+ (FIG. 10, Table 5), suggesting that although Mn2+ is more effective in supporting catalysis, it binds with lower affinity than does Zn2+.
The presence of both Zn2+ and Mn2+ in a reaction assay results in diminished activity (i.e. Zn2+ is an inhibitor versus Mn2+, Table 6). All of the metals bind the enzymes with low affinity, such that running the protein over a G-25 column or dialyzing against metal free buffer removed the protein bound metal.







TABLE 6







The effect of zinc upon B. subtilis and N. gonorrhoeae GCYH-IB


activity when assayed in the presence of 600 μM Mn(II).


Data expressed as relative activity (%).









[zinc] μM
B. subtilis
N. gonorrhoeae












0
100
100


0.5
84
93


1
41
68


2
34
57


4
35
47


10
35
53


20
26
45


40
23
45









To understand the structural basis of the unique metal requirement of GCYH-IB, the crystal structure in two forms: one of the recombinant enzyme purified in solutions lacking added metal (GCYH-IB, PDB ID 3D1T), and one of the apoenzyme remetallated with manganese (GCYH-IB.Mn, PDB ID 3D2O) were determined. Enzymes from both B. subtilis and N. gonorrhoeae were pursued for crystallization, but only the N. gonorrhoeae ortholog produced diffracting crystals. The two orthologs are 64% similar and 35% identical in sequence and possess similar biochemical properties in vitro.
The crystal structure of GCYH-IB was determined by seleno-MAD methods (FIG. 2, Tables 7 and 9). Two monomers, A and B, were identified in the asymmetric unit. The final structure is missing residues 1-13 of monomer A and residues 1-14 of monomer B of the total 257 amino acids in each monomer, and contains two Zn2+ ions and one acetate molecule. A homotetrameric complex representing the biological state of the enzyme. El Yacoubi et al. 281 J. Biol. Chem., 37586-37593 (2006) could be generated from the asymmetric-unit dimer by a crystallographic 2-fold rotation operation (FIG. 2A). (32% of the total monomeric surface is buried in the homotetramer). The monomer is a globular subunit composed of 9 β-strands and 6 α-helices (FIG. 3A), of which 8 sequential antiparallel β-strands (β1-β6, β8 and β9) and four antiparallel α-helices (α1, α2, α4 and α6) form a core with the classic tunneling fold (T-fold) architecture characteristic of bimodular pterin and purine binding enzymes. Colloc'h et al. 39 Proteins, 142-154 (2000). In this core, a highly twisted eight-stranded β-sheet is layered on its concave side with four antiparallel α-helices. The dimer of the asymmetric unit is constructed by a cyclic arrangement of the two eight-stranded β-sheets from the two monomers to form a sixteen-stranded antiparallel β-barrel. In the biological homotetramer, two β-barrels join together head-to-head to form a central tunnel that is 60 Å long and 17 Å in diameter (FIG. 2A).
A search for similar structures was done using the DALI search engine and the FSSP database (fold classification based on structure-structure alignment of proteins). Holm & Sander 233 J. Mol. Biol. 123-38 (1993). Several bimodular T-fold enzymes were identified, as well as GCYH-IA (FIG. 3C), a unimodular T-fold enzyme. The best fit was to A. flavus urate oxidase. Retailleau et al., 60 Acta Crystallogr. D 453-62 (2004) (PDB ID 1UOX, r.m.s.d. 3.4 Å over 197 Cα atoms, FIG. 3B) that follows a similar β8α4 topology.
Comparison of GCYH-IA and GCYH-IB structures shows that GCYH-IB is a homotetramer built around a bimodular β8α4 T-fold core and GCYH-IA is a homodecamer β4α2 unimodular T-fold enzyme. Pairwise structural comparison of the monomeric subunits of GCYH-IB and E. coli GCYH-IA (Rebelo et al., 326 J. Mol. Biol. 503-16 (2003)) (PDB ID 1FBX) using the DaliLite server (Holm & Park 16 Bioinformatics, 566-567 (2000)) yielded an alignment strictly in the four β-strands and two α-helices (β2, β3, β6, β7, α6, α7 of GCYH-IA, and β5, β6, β8, β9, α4, α6 of GCYH-IB) of the T-fold (r.m.s.d. 3.2 Å over 94 Cα atoms, FIG. 3C). Based on this alignment, a multi-sequence alignment of the two enzyme subfamilies in the shared core region was generated (15 sequences of each, FIG. 4). With the exception of a conserved cysteine involved in metal binding in both subfamilies (Cys147 in GCYH-IB), the new alignment differs significantly from previously reported alignment that was based on sequence information and predicted tertiary structure.
In the current alignment, the two subfamilies exhibit 28% sequence similarity and only two invariant residues; the metal and substrate liganding residues Cys147 and Glu216 (N. gonorrhoeae numbers), respectively. This unusually low primary structure homology, compared with 7%-17% identity and 39%-53% similarity between T-fold enzymes in general, explains improper annotation of GCYH-IB genes in genomic databases and limited success in previous attempts to generate a model of the tertiary structure by sequence-based homology modeling (El Yacoubi et al, 2006).
In addition to the absence in GCYH-IB of the N- and C-terminal domains found in GCYH-IA (FIGS. 3A and 3C), the following functionally important differences are seen in the T-fold domain, specifically in the active site: (a) insertion in GCYH-IB of a two turn α-helix (α3) between the first two strands (β5 and β6) of the common T-fold β-sheet (FIGS. 3A, 3C and FIG. 4). This change results in the loss of the Zn2+ binding loop C110EHH113 found in GCYH-IA, with the exception of the Cys (FIG. 4); (b) Insertion in GCYH-IB of a β-strand (β7) and α-helix (α5) between the two α-helices (α4 and α6) of the T-fold (FIGS. 3A, 3C and FIG. 4). β7 and α5 are part of the inter-subunit interface that harbors the active site. Significantly, α5 provides the strictly conserved Glu201 as a carboxylate ligand to the active-site metal ion in GCYH-IB; and (c) Deletion in GCYH-IB of helix α8 found in the T-fold domain of GCYH-IA (FIGS. 3A, 3C, and FIG. 4). Importantly, α8 contains the second Cys ligand to Zn2+ in GCYH-IA. This Cys is missing in GCYH-IB and the helix is replaced with a β-turn containing strictly conserved Glu243, His246 and His248.
Rearranged metal binding site and accommodation of Mn2÷; as in GCYH-IA, the active site of GCYH-IB is located at the interface between three subunits (Table 10 and Table 11). Two of the four active sites in the GCYH-IB homotetramer are partially disordered in the crystal. The active site encompasses the metal binding site and the putative GTP binding pocket with the conserved Glu216 that serves to anchor the substrate guanine moiety, a characteristic feature of all T-fold proteins (Colloc'h et al, 2000).
The presence of bound Zn2+ in the GCYH-IB crystal (grown with no additional Zn in the crystallization buffer) was confirmed by an X-ray fluorescence scan near the Zn absorption edge (see FIG. 12A) and an omit Fo-Fc map (FIG. 5A). Zn2+ is bound in a trigonal bipyramidal geometry and is coordinated by the thiol group of Cys147, side-chain oxygen atom of Glu201 from the neighboring subunit, and an oxygen atom from a bound acetate molecule (present in the protein sample at 50 mM) as equatorial ligands, and Nε of His159 and a water molecule as the bottom and top axial ligands, respectively (FIGS. 5A and 6 and Table 10). The average Zn2+-to-ligand distance is 2.4 Å. In its current position, the acetate molecule may mimic one of the cyclohydrolase reaction transition states that are subsequent of the opening of the substrate guanosine ring. The liganding side chains, their positions in the Zn2+ coordination sphere and the protein secondary structure elements in which they lie are different from those seen in GCYH-IA (FIGS. 4, 6, and Table 10). In T. thermophilus and E. coli GCYH-IA (PDB ID 1WM9, Rebelo et al., 326 J. Mol. Biol. 503-516 (2003); Tanaka et al., 138 J. Biochem. 263-275 (2005)), Zn2+ is coordinated by two thiol groups and a histidine side chain (Cys110, Cys181, His113 in E. coli residue numbers), all from the same subunit. These side chains come from the loop between the first two β-strands of the T-fold (β2 and β3 in Ec-GCYH-IA nomenclature) and a short α-helix (α8) (FIG. 4). In GCYH-IB, the metal binding site is formed by the helix-loop insertion (α3) between the first two β strands of the T-fold (β5 and β6) and the helical insertion α5 from the neighboring subunit.
Crystals of GCYH-IB remetallated with Mn2+ (GCYH-IB.Mn) were grown using Zn-free reagents. The presence of bound Mn2+ was confirmed with an X-ray emission spectrum and fluorescence scan near the Mn absorption edge following a wash and 1-hr back-soak of the crystal in metal-free solution (see FIGS. 12B and 12C). The crystal structure was determined by difference Fourier methods using model phases from the Zn2+-metallated structure (Tables 7 and 9 and Table 11). The two structures are similar and superpose with r.m.s.d. 0.3 Å over 486 Ca atoms. Metal coordination and distances are also similar except for the replacement of acetate with azide (added to the acetate-free protein sample at 12 mM concentration prior to crystallization) as an equatorial ligand to Mn2+ (FIG. 5B and Table 11).
The Zur dependent regulation of folE2 is conserved across bacterial species. The biochemical and structural analyses of B. subtilis and N. gonorrhoeae GCYH-IB suggest that Zn is not the physiological metal for this family of cyclohydrolases. The expression of GCYH-IB in B. subtilis is controlled by the Zn-dependent Zur repressor and is thus up-regulated under Zn-limiting conditions. Gelfand et al., 1 Brief Bioinform 357-71 (2000). To check if orthologs of folE2 in other bacteria are similarly subject to Zur-mediated control, bacterial regulons were analyzed using a comparative genomics approach. Gelfand et al, 2000; Rodionov, 107 Chem. Rev. 3467-97 (2007). Annotation of the folE and folE2 genes in available genomes had been performed previously. Two position-specific weight matrices (PWMs) were constructed for known Zur binding sites from Gram-positive and Gram-negative bacteria (Panina et al., 100 Proc Natl Acad Sci USA 9912-17 (2003)), and were used to scan for candidate Zur binding sites in 5′-untranslated regions (UTRs) of folE2 and neighbor genes in bacterial genomes. To account for possible operon structures, UTRs of genes located immediately upstream of folE2 in the genomes were also analyzed.
Strong Zur operator sites were identified upstream of folE2 genes in twenty-one bacterial genomes (Table 4, FIG. 13). This unique regulatory feature is conserved across phyla including examples in fifteen γ-proteobacteria (Pseudomonadales, Xanthomonadales, some Enterobacteria, and other lineages), three β-proteobacteria (some Burkholderiales), and three Bacillus species. Notably, all organisms that have the Zur-regulated folE2 gene also contain a copy of folE (e.g., B. subtilis). Similarly, no Zur regulatory sites were found upstream of folE2 genes in those organisms that lack the Zn-dependent GCYH-IA isozyme (e.g., N. gonorrhoeae). These results show that Zur regulation of GCYH-IB is widespread and suggest that, in some bacteria, the GCYH-IB isozyme is expressed under Zn-limiting conditions to replace the Zn-dependent GCYH-IA.
GCYH-IB can functionally replace GCYH-IA in B. subtilis, which has both the folE and folE2 genes (also known as mtrA and yciA, respectively). To determine whether GCYH-IB can functionally replace GCYH-IA, a B. subtilis ΔfolE mutant strain was constructed and its complementation with GCYH-IB investigated. Wild-type B. subtilis grows well in rich (LB) medium (FIG. 11, diamonds). As reported previously (Babitzke et al., 174 J, Bacteriol. 2059-64 (1992)), the ΔfolE mutant strain, expressing only GCYH-IB, is a thymidine (dT) auxotroph. In the absence of dT, it grows only with a reproducible lag in rich medium (FIG. 11, squares). Poor growth of the ΔfolE mutant strain in log phase is consistent with repression of GCYH-IB expression under these conditions. Growth commences in stationary phase and reflects derepression of GCYH-IB when cells become Zn-starved and Zur repression is released. Indeed, deleting the zur gene, as in the Δzur ΔfolE double mutant where GCYH-IB is constitutively expressed, eliminates the growth lag in rich medium (FIG. 11, triangles). As expected, the ΔfolE Δzur ΔfolE2 triple mutant strain, expressing no GCYH-I, is unable to grow (FIG. 11, closed circles), nor is the ΔfolE ΔfolE2 double mutant strain. For either strain, growth can only be partially restored by the addition of dT (FIG. 11, open circles) or all of the folate-derived metabolites. The rather poor dT rescue of these two mutant strains may be due to deficient formylated methionine biosynthesis. These results indicate that GCYH-IB functionally replaces GCYH-IA in B. subtilis under Zn-limiting conditions.
Sequence conservation indicates that metal-dependent catalysis is a property of the GCYH-IB enzyme family in general, with Mn2+, not Zn2+, possibly the preferred metal in vitro. Indeed, metal catalysis has been observed with GCYH-IB orthologs from N. gonorrhoeae and T. maritima, and from M. jannaschii (Grochowski et al., 46 Biochem. 6658-67 (2007)), which exhibits optimal activity in the presence of Fe2+. The structural differences between GCYH-IA and -IB enzymes in the active-site region contribute to creating a new metal functionality in GCYH-IB. For example, the introduction of an acidic side chain (Glu201) in the metal site of GCYH-IB allows accommodation of Mn2+ which favors oxygen ligands more than Zn2+. Further, the contribution of a neighboring subunit to the metal site suggests possible posttranslational regulation by metal-induced oligomerization as seen in DHNA. Goulding et al., 349 J. Mol. Biol. 61-72 (2005). The metal ion likely serves to activate the nucleophile water molecule in the first step of the reaction and to stabilize the formyl intermediate, as in GCYH-IA. Tanaka et al, 2005.
The differences in the active-site architecture and associated metal dependence between GCYH-IA and -IB may reflect differences in catalytic strategies for the two enzyme families. The presence of acetate and azide as exogenous metal ligands in the Zn2+- and Mn2+-metallated enzyme structures, respectively, is a result of sample preparation conditions and does not reflect specificity to the type of metal. The acetate ligand may mimic the reaction formyl intermediate or formic acid as a leaving group. The azide ligand may represent a moiety in a transition-state intermediate occurring in a later step, e.g., during the Amadori rearrangement that takes place after guanine and ribose ring opening.
Zinc is an essential cofactor for numerous proteins. In Bacteria and Eukaryotes, cellular Zn2+ levels are sensed by specific transcription factors (the repressor Zur in B. subtilis and E. coli, the activator Zap1p in S. cerevisiae). Hantke, 8 Curr. Opin. Microbiol. 196-202 (2005); Lyons et al., 97 Proc. Nat'l Acad. Sci. USA 7957-62 (2000); Moore & Heimann, 8 Curr. Opin. Microbiol. 188-195 (2005). Cellular responses to low Zn2+ conditions include increased expression of high-affinity Zn2+ transporters such as ZnuABC, and substitution of Zn2+-dependent enzymes with alternative isozymes that do not rely on this metal ion as a cofactor. Examples of the latter strategy include Zn2+-dependent regulation of the alcohol dehydrogenase isozyme ADH4 in yeast (Lyons et al., 2000), and paralogs of ribosomal proteins (e.g., L31 and L33) in B. subtilis and Streptomyces coelicolor. Nanamiya et al., 52 Mol. Microbiol. 273-83 (2004); Panina et al, 2003; Shin et al., 189 J. Bacteriol. 4070-77 (2007).
Similarly, results from the work presented herein indicate that the upregulation of B. subtilis GCYH-IB when Zn2+ is low serves to allow utilization of metal ions other than Zn2+ for folate synthesis. On the other hand, N. gonorrhoeae (and several other pathogens) do not possess the Zn-dependent GCYH-IA isozyme and instead rely solely on GCYH-IB for folate synthesis. Consistently, they do not have Zur regulatory sites upstream of the folE2 gene. N. gonorrhoeae live in the highly oxidizing environment created by the host immune response and, to survive in this challenging environment, they accumulate millimolar levels of manganese, an effective scavenger of reactive oxygen species (ROS), in the cytoplasm. Seib et al., 70 Microbiol. Mol. Biol. Rev. 344-61 (2006). A similar utilization of Mn to fight ROS damage resulting from radiation exposure occurs in D. radiodurans. Daly et al., 306 Science 1025-28 (2004). Presumably, the ready availability of Mn2+ makes a Mn-dependent folate biosynthesis pathway more advantageous for these organisms. Further, a recent report shows that the innate immune system in mice fights S. aureus infections by inhibiting microbial growth in tissue abscesses through chelation of Mn2+ and Zn2+ by the neutrophil-derived protein calprotectin, depriving the bacteria of essential nutrients. Corbin et al., 319 Science 962-65 (2008). It is possible that this defense strategy targets, among other cellular processes, folate synthesis in S. aureus, an organism that depends solely on GCYH-IB for folate synthesis and lacks GCYH-IA (FIG. 13). Hence, the distinct structure and metal dependence of GCYH-IB and its absence in humans may make it an attractive target for the development of new antibiotic agents.
The structural information disclosed herein is useful analysis of binding interactions with a ligand, e.g., for discovery of small molecule antibiotic agents. Such data is useful for a number of purposes, including the generation of structures to analyse the mechanisms of action and/or to discover or perform rational drug design of active compounds. For example, a search of several small-molecule structural data bases such as Available Chemicals Directory, Cambridge Crystallographic Database, Fine Chemical Database and CONCORD database is carried out using parameters derived from the crystal structure. The search can be 2-dimensional, 3-dimensional or both and can be done using a combination of software such as UNITY version 2.3.1 (Tripos, Inc.), MACCS 3D, CAVEAT and DOCK. Conformational flexibility of the small molecules is allowed. The strategy for conducting the search takes into account conformations and/or key residues in the combining site.
As discussed above, the structural information can be stored on a computer-readable medium. The invention therefore provides systems, particularly a computer system, the systems containing the atomic co-ordinate data of any one of the tables below, or selected co-ordinates thereof. The computer system may comprise: (i) a computer-readable data storage medium comprising data storage material encoded with the computer-readable data; (ii) a working memory for storing instructions for processing said computer-readable data; and (iii) a central-processing unit coupled to said working memory and to the computer-readable data storage medium for processing said computer-readable data and thereby generating structures and/or performing rational drug design. The computer system may further comprise a display coupled to the central-processing unit for displaying said structures. The computer system may contain one or more remote devices. The remote device may comprise e.g. a computer system or computer readable media of one of the previous aspects of the invention. The device may be in a different country or jurisdiction from where the computer-readable data is received. The communication with a remote device may be via the internet, intranet, e-mail etc, transmitted through wires or by wireless means such as by terrestrial radio or by satellite. Typically the communication will be electronic in nature, but some, or all, of the communication pathway may be optical, for example, over optical fibers. The data received may then be used in a computer-based method for the analysis of the interaction of a ligand as discussed above.
EXAMPLES
Example 1
Bioinformatics
Analysis of the folate subsystem was performed in the SEED data base (Overbeek et al., 33(17) Nucl. Acids Res. 5691-5702 (2005)) with SEED version cvs.1144925141 (05:45:41 on Apr. 13, 2006) (available on the internet at, for example, the “.org” site of the National Microbial Pathogen Data Resource (NMPDR). Results are made available in the “Folate Biosynthesis Subsystem” on the publicly available server (available on the internet at the SEED cite of the University of Chicago). The phylogenetic pattern search was performed on the SEED server located on the NMPDR website.
Example 2
Cloning of Thermotoga maritima, Neisseria gonorrhoeae, and Bacillus subtilis COG1469 Genes for GCYH-IB Protein Expression
The COG1469 genes from T. maritima (TM0039; GenBankTM accession number gi|15642814), N. gonorrhoeae (ngo0387; GenBankTM accession number gi|59800831), and B. subtilis (yciA; GenBankTM accession number gi|2632620) were amplified by PCR from genomic DNA of the respective organisms. The primers have been included in Ser. No. 60/935,124 and published in El Yacoubi et al., 2006.
The PCRs contained 500 ng of genomic DNA, 200 μM dNTPs, 50 pmol of the sense and antisense primers, 1×Pfu Ultra buffer (supplied by the manufacturer), and 2.5 units of Pfu Ultra DNA polymerase in a final volume of 50 μl. A three-step PCR thermocycling protocol was utilized: (1) 94° C. for 1 min; (2) 30 cycles of denaturation at 94° C. for 1 min, annealing at 50° C. for 2 min, and extension at 72° C. for 1 min; (3) 72° C. for 4 min. The PCR product was purified from a 1% agarose gel containing ethidium bromide using the Qiagen Inc. PCR purification kit and cloned into a linearized pET-30 Xa/LIC expression vector (Novagen). The primary structures of the resulting constructs, pSAB-7-189 (T. maritima), pSAB-8-142 (N. gonorrhoeae), and pSAB-9-61 (B. subtilis), were confirmed by sequencing.
Example 3
Cloning of the T. maritima, Acinetobacter baylyi, and B. subtilis COG1469 Genes for Complementation
pTM0039 expressing the TM0039 gene under PBAD control (Klock et al., 6(2-3) J. Struct. Genomics 89-94 (2005)) was a kind gift of the Joint Center for Structural Genomics (La Jolla, Calif.). The COG1469 genes from B. subtilis (yciA) and A. baylyi (ACIAD1740 gi|50084892) were cloned in pBAD24. Guzman et al., 177(14) J. Bact. 4121-30 (1995). The primers have been included in Ser. No. 60/935,124 and published in El Yacoubi et al., 2006. PCR products were obtained and purified as described above and then digested with NcoI/XbaI before ligation into plasmid pBAD24 (Guzman et al., 1995) digested with the same endonucleases and transformed into Topo10 cells (Invitrogen). The primary structures of the resulting constructs, pBY142.1 (expressing A. baylyi ACIAD1740) and pBY143.1 (expressing B. subtilis yciA), were confirmed by sequencing.
These plasmids, as well as pBAD24 and pTM0039, were transformed into the E. coli folE::KanR strain. Klaus et al., 280(46) J. Biol. Chem. 38457-63 (2005). The transformants were plated on LB supplemented with dT, ampicillin and kanamycin, and screened for the capacity to grow on LB without dT in the presence of various concentrations of arabinose. To confirm the presence of the folE::KanR allele and of the pBAD derivatives in the transformants, the colonies were analyzed by PCR using the oligonucleotides located upstream and downstream from the folE gene and ChkDfolE-ol2 or located upstream and downstream of the polylinker in the pBAD derivatives and pBADol5 as described in Ser. No. 60/935,124 and published in El Yacoubi et al., 2006.
Example 4
Purification and Overexpression of Recombinant T. maritima, N. gonorrhoeae, and B. subtilis GCYH-IB Proteins
The plasmids pSAB-7-189, pSAB-8-142, and pSAB-9-61 were transformed into E. coli BL21 (DE3) for expression of His6 tag (SEQ ID NO: 33) fusion proteins. Cultures of the transformed cells were grown at 37° C. with shaking (250 rpm) until an A600 of 0.9 was attained. Isopropyl-D-thiogalactopyranoside was added to a final concentration of 0.1 mM, and the cultures were incubated for an additional 4 h at 37° C. with shaking (250 rpm). The cells were harvested by centrifugation at 5000×g for 10 min at 4° C. The cell paste was flash frozen in liquid nitrogen and stored at −80° C. until needed.
Frozen cell paste was thawed and suspended in lysis buffer (50 mM Tris acetate (pH 8.0), 50 mM KCl, and 1 mM-mercaptoethanol) at a concentration of 250 mg/ml. The cells were lysed by the addition of lysozyme and DNase to a final concentration of 0.25 mg/ml and 10 μg/ml, respectively. The lysate was centrifuged at 15,000×g for 30 min at 4° C., and the resulting supernatant was filtered (low protein binding, 0.45 μm). The cell-free extract was loaded onto an Ni2+-nitrilotriacetic acid-agarose column (Qiagen) that had been equilibrated with Buffer A (100 mM Tris-acetate (pH 8.0), 300 mM KCl, 2 mM β-mercaptoethanol, 1% Triton X-100, 1 mM phenylmethylsulfonyl fluoride, and 10% glycerol). The column was washed with five column volumes of Buffer A, five column volumes of Buffer B (100 mM Tris acetate (pH 8.0), 300 mM KCl, 2 mM β-mercaptoethanol, 1% Triton X-100, 1 mM phenylmethylsulfonyl fluoride, 10% glycerol, and 20 mM imidazole), and finally five column volumes of Buffer C (100 mM Tris acetate (pH 8.0), 300 mM KCl, 2 mM-mercaptoethanol, 10% glycerol, and 20 mM imidazole). The protein was eluted from the column with ten column volumes of Buffer C containing 250 mM imidazole. The protein was concentrated in a Centricon YM-10 ultracentrifugation device and dialyzed at 4° C. against 50 mM Tris acetate (pH 8.0), 50 mM KCl, and 4 mM dithiothreitol.
The His6 tag (SEQ ID NO: 33) was cleaved from the T. maritima, N. gonorrhoeae, and B. subtilis GCYH-IB proteins in reactions that contained fusion protein (20 mg), Factor Xa protease (20 μg), 50 mM Tris acetate (pH 8.0), 100 mM KCl, 2 mM CaCl2 in a final volume of 1 ml. After incubating for 20 h at room temperature, the reactions were loaded onto a column containing 2 ml of Ni2+-nitrilotriacetic acid-agarose equilibrated in Buffer A. Wild-type protein was eluted from the column with ten column volumes of Buffer A. The protein was concentrated and dialyzed against 50 mM Tris acetate (pH 8.0), 50 mM KCl, and 10% glycerol.
Example 5
COG1469 Genes Complement an E. coli folE Mutant
Because folate is not transported in most bacteria (Skold et al., 2000), it can not be supplied in the medium to enable growth of a folate auxotroph. On rich medium, however, all of the folate-derived metabolites are present in sufficient quantities except for dT, allowing a folE mutant to be maintained on LB/dT. Klaus et al., 2005; Yakhin & Babitzke, 2004. Nevertheless, the E. coli folE::KanR strain has a slow growth phenotype on LB/dT (colonies take two days instead of one day to form at 37° C.), presumably due to the absence of formylation of the initiator tRNA. The folE::KanR strain was transformed with pBAD derivatives expressing the COG1469 homolog from T. maritime (TM0039).
Although complementation of both the dT auxotrophy and the slow growth phenotype was observed (FIG. 8C), was not robust, and depended on high arabinose levels. This is not surprising because T. maritima is a thermophile, and many of the enzymes from thermophiles exhibit low activity at 37° C. To achieve better complementation, the COG1469 orthologs from the mesophiles B. subtilis and A. baylyi (formally known as Acinetobacter sp. ADP1) were cloned and transformed into the E. coli folE::KanR strain. Robust complementation of dT auxotrophy (FIG. 8A) and poor growth (FIG. 8B) were observed with these constructs, which is consistent with GCYH-IB family proteins catalyzing GCYH-I activity.
Example 6
GCYH-IB Proteins have GCYH-I Activity In Vitro
In parallel with the in vivo experiments, COG1469 genes were cloned into protein expression vectors to allow unambiguous assignment of catalytic function through the direct investigation of putative GTP cyclohydrolase I activity with in vitro enzymatic assays of purified proteins. Thus, the genes encoding GCYH-IB proteins from T. maritima, N. gonorrhoeae, and B. subtilis were cloned from genomic DNA into the pET30 system, and the recombinant His6 fusion proteins were overproduced and purified. All three of the recombinant proteins were obtained as soluble, active enzymes both as the His6 fusion and the cleaved wild type.
Radiochemical assays using [8-14C]GTP (Yim et al., 1976), of each of the GCYH-IB proteins, along with E. coli FolE as a positive control, demonstrated that [14C]formate was released in each assay and that its production was both time- and enzyme-dependent, consistent with enzyme-catalyzed hydrolytic ring opening and deformylation at C-8 of GTP. From these data, specific activities of 2.3 min−1 mg−1 to 5.3 nmol min mg−1 were calculated for the GCYH-IB proteins, roughly an order of magnitude lower than that reported for FolE (Bracher et al., 274 J. Biol. Chem. 16727-35 (1999); Kolinsky & Gross, 279(39) J. Biol. Chem. 40677-82 (2004); Rebelo et al., 326(2) J. Mol. Biol. 503-16 (2003)) and the FolE control. To confirm that the product of the GCYH-IB catalyzed reactions was in fact 7,8-dihydroneopterin triphosphate, the enzyme assays were analyzed with UV-visible (Bracher et al., 40(26) Biochem. 7896-902 (2001)) and fluorescence spectroscopy. (Hatakeyama & Yoneyama, 100 Methods Mol. Biol. 265-72 (1998)). FIG. 9A shows UV-visible spectra for enzyme assays of E. coli FolE and GCYH-IB proteins under standard GTP cyclohydrolase 1 assay conditions. The spectra are essentially identical, with the characteristic absorption spectrum of GTP replaced by that of H2NTP. Bracher et al., 2001. When enzyme assays were subjected to post-reaction dephosphorylation and oxidation to convert the putative enzymatically produced H2NTP to the fluorescent neopterin, the fluorescent spectra from the GCYH-IB assays were identical to the spectrum of the E. coli FolE assay (FIG. 9B) and to that of authentic neopterin. Hatakeyama & Yoneyama, 1998.
Furthermore, HPLC analysis of the enzyme assays after dephosphorylation showed that the product from each enzyme-catalyzed reaction had the same retention time as authentic neopterin (under the analysis conditions dihydroneopterin is oxidized to neopterin) (FIG. 9C). Finally, mass spectrometry analysis of the E. coli FolE and N. gonorrhoeae GCYH-IB reactions revealed identical constituents, with ions corresponding to GTP (m/z 522, M-H−; m/z 544, M-2H−+Na+; m/z 566, M-3H−+2Na+), neopterin triphosphate (m/z 492, M-H−; under the conditions of the analysis dihydroneopterin is oxidized to neopterin), and neopterin cyclic monophosphate (m/z 314, M-H−; it has been previously documented that under the alkaline conditions of the work-up neopterin triphosphate is converted to the cyclic monophosphate. Basset et al., 99(19) PNAS 12489-94 (2002); Cone & Guroff, 246(4) J. Biol. Chem. 979-85 (1971); Plowman et al., 249(17) J. Biol. Chem. 5559-64 (1974).
Taken together, the data clearly demonstrate that the GCYH-IB proteins catalyze GTP cyclohydrolase I activity, and thus they represent a new structural class of GTP cyclohydrolase enzymes, distinct from the canonical GCYH-I enzyme exemplified by human and E. coli FolE. To differentiate these two cyclohydrolase families, the canonical type I cyclohydrolase may be renamed GCYH-IA, that the COG1469 family be named GCYH-IB, and that their corresponding genes be denoted as folE and folE2, respectively.
Example 7
Over-Expression and Purification of Selenomethionine (SeMet)-Labeled N. gonorrhoeae GCYH-IB (Ng-GCYH-IB)
Ng-GCYH-IB was cloned in pET-30 Xa/LIC expression vector (Novagen, San Diego, Calif.) as described previously. El Yacoubi et al., 2006. SeMet-labeled Ng-GCYH-IB was over-expressed in the E. coli methionine auxotroph B834(DE3) (Novagen) following standard methods. Hendrickson et al., 9(5) Eur. Mole. Biol. Org. J. 1665-72 (1990). The His6-tagged protein (SEQ ID NO: 33) was purified on Ni-NTA resin (washed with Tris acetate (100 mM, pH 8.0), KCl (300 mM), β-mercaptoethariol (2 mM), glycerol (10%), and imidazole (20 mM)), and eluted with the same buffer containing 250 mM imidazole. After concentration and dialysis against Tris acetate (50 mM, pH 8.0), KCl (50 mM), and dithiothreitol (4 mM), the His6 tag (SEQ ID NO: 33) was cleaved from the enzyme with Factor Xa as described previously (E1 Yacoubi et al., 2006) and SeMet-labeled wild-type Ng-GCYH-1B was further purified on a Ni-NTA column and eluted with ten column volumes of Tris-acetate (100 mM, pH 8.0), KCl (300 mM), β-mercaptoethanol (2 mM), Triton X-100 (1%), phenylmethylsulfonyl fluoride (1 mM), and glycerol (10%). After concentrating to 5.5 mg/mL, the protein was dialyzed against Tris-Acetate (50 mM, pH 8.0), KCl (100 mM) and β-mercaptoethanol (5 mM) and further concentrated to 9 mg/mL. Selenium substitution was verified with mass spectrometry using MALDI-TOF analysis.
Example 8
Crystallization and X-Ray Data Collection
SeMet-labeled GCYH-IB was crystallized at 20° C. by vapor diffusion in 2 μL sitting drops containing enzyme (9 mg/mL in 50 mM Tris-Acetate, 100 mM KCl, 5 mM BME, pH 8.0), polyethylene glycol 6000 (10-16%), LiCl (1-1.4 M), Tris (50 mM, pH 9.0) and Tris-HCl (50 mM, pH 7.0). The Mn-reconstituted enzyme (10 mg/mL in 50 mM Tris-HCl, 50 mM KCl, 1 mM DTT, pH 8.0) was crystallized under similar conditions but using metal-free reagents (Chelex-100-pretreated Milli-Q water and ultra pure reagents from Hampton, Inc.) with 1-10 mM MnCl2 and 12 mM sodium azide (as a preservative) added to the protein solution prior to crystallization. Crystals were cryo-protected in mother liquor plus ethylene glycol (25%) and flash cooled in liquid nitrogen. For the SeMet-labelled enzyme, a three-wavelength selenium dataset was collected at the Advanced Light Source (ALS, Berkeley, Calif.) beamline 8.2.2. For the GCYH-IB.Mn2+ complex, crystals were back-soaked in metal-free reservoir solution for 1 hr prior to cryo protection and a single-wavelength dataset was collected from a single crystal at the Stanford Synchrotron Radiation Laboratory (SSRL, Stanford, Calif.) beamline 7-1. X-ray data were processed in HKL2000. Otwinowski, Z. & Minor, W. 276 Methods Enzymol., 307-326 (1997).
Example 9
Structure Determination
The crystal structure of Ng-GCYH-IB was determined by the multi-wavelength anomalous dispersion (MAD) method using selenium as the anomalous scatterer. An initial heavy-atom substructure consisting of 15 selenium sites was identified using the Phenix-hyss program. Adams et al., 11 J. Synchrotron Rad. 53-55 (2004). Heavy atom positions, occupancies, and atomic displacement parameters were then refined in the SHARP maximum likelihood program (Maximum-likelihood heavy atom parameter refinement in the MIR and MAD methods, in METHODS IN ENZYMOLOGY (de La Fortelle & Bricogne, eds., Acad. Press, San Diego, Calif., 1997)), and initial phases were calculated using all Se sites. Phases were improved by density modification with DM (Cowtan, 31 Joint CCP4 & ESF-EACBM Newslett. Protein Crystallography, 34-38 (1994)), and SOLOMON (Abrahams & Leslie, 52 Acta Crystallographica 30-42 (1996)), of the CCP4 suite (Collaborative Computational Proj., N.4, D50 Acta Crystallographica 760-63 (1994)), using data in the resolution range 50 Å to 2.2 Å and solvent content of 47%.
With solvent flattening, the mean figure of merit increased from 0.34 to 0.85. The 2.2 Å FoFOM map was calculated and auto-traced in ARP/wARP (Perrakis et al., 6 Nature Structural Bio. 458-63 (1999)), where 418 of the 514 residues in the asymmetric unit were built. The model was manually completed and partially rebuilt in COOT (Emsley & Cowtan, D60 Acta Crystallographica 2126-32 (2004)), utilizing the two-fold non-crystallographic symmetry (NCS) relation. Subsequent crystallographic refinement was carried out with Phenix-refine (Adams et al. 11 J. Synchr. Radiat., 53-55 (2004)), using NCS restraints and Twin Lattice Symmetry parameterization that included 3 domains per monomer. (Isotropic B-group constraints were applied to disordered parts of the model). Finally, the f and f′ were refined in Phenix to final values of −6.4 and 5.6, −5.4 and 4.9, and −5.6 and 3.5, for the peak, inflection, and remote wavelength, respectively. Solvent molecules and ions were added, the structure was further refined in Crystallography and NMR Systems (CNS, Adams et al., 8(5) Curr. Opin. Struct. Biol. 606-11 (1998)), after removal of NCS restraints, and was validated using Procheck software. Vaguine et al., 55 Acta Crystallographica D, 191-205 (1999). The electron density for residues 146-160 and 188-210 of monomer A was weak with refined b-factors >60 Å2, indicating that this region is disordered.
The crystal structure of the GCYH-IB.Mn2+ complex was determined by direct difference Fourier calculation in which a protein model based on the crystal structure of the Zn2+-metallated enzyme was used to calculate phases. The structure was rigid-body refined in CNS, then refined in the program refmac from CCP4 (Michalopoulos, et al. 32 Nucl. Acids Res., 251-254 (2004)) while applying NCS restraints and solvent flattening. NCS restraints were removed in a second refmac run. Ligands and solvent molecules were modeled in Coot (Emsley, P. & Cowtan, K. 60 Acta Crystallogr. Biol. Crystallogr. D, 2126-2132 (2004)) and final refinement in refmac.










TABLE 7





Dataset
Sepeak
Seinflection
Seremote















GCYH-IB X-ray data collection and phasing statistics


Data collection










Unit cell (Å)
91.7, 100.3, 114.1
91.7, 100.2, 114.0
91.8, 100.4, 114.1


Wavelength (Å)
0.9793
0.9795
0.9747


Resolution (Å)
50.0-2.20
50.0-2.20
50.0-2.20


Unique reflections (ano)
 26,689 (26,567)1
26,724 (26,675)
26,490 (25,691)


Completeness (%)
99.8 (99.0)
 99.8 (100.0)
99.0 (92.0)


Redundancy
5.7 (5.0)
5.8 (5.7)
5.4 (3.5)


Rmerge (%)2
8.7 (61) 
 7.5 (36.9)
  84 (89.1)


<I/σ(I)>
16.3
17.6
15.0







X-ray data collection, phasing, and structure refinement statistics (con't)


Phasing statistics (29-2.30 Å)










Rder3
0.0744
0.137



Ranom5
0.069
0.059
0.058


Rcullis6 (iso4/ano)
0.49/0.73
0.83/0.72
0.84/0.86


Phasing power7





Centric
0.06
0.11
0.16


Acentric iso4
0.06
0.09
0.15


Acentric ano
1.20
1.46
1.10


FOM8, overall
0.34




after DM
0.83




after Solomon
0.85




Number of Se sites
15





1Highest-resolution shell (2.2-2.28 Å) information in parentheses.


2Rmerge = 100 × (Σh Σi|<I(h)> − I(h)i|)/Σh Σi I(h)i, where I(h)i is the ith observation of reflection h and <I(h)> is the mean intensity of all observations of reflection h.


3Rder = Σh|FPH − FP|/Σh|FP|, where |FP| and |FPH| are the observed structure factor amplitudes of the native and the derivative, respectively.


4The dispersive differences were treated as isomorphous replacement information where the data collected at wavelength 0.9747 Å are treated as native data (Terwilliger 1994).


5Ranom = Σh|FPH+ − FPH−|/Σh|<FPH>|, where |FPH+| and |FPH−| are the Friedel-pair observed structure factor amplitudes of the derivative at a given wavelength, and <FPH> is their average.


φ6RCullis = Σh[|FH| − (|FPH| − |FP|)]/Σh(|FPH| − |FP|), where |FH| is the calculated heavy-atom structure factor for reflection h.


7PPdisp = (1/Nrefl) Σh [||FPH| − |FP||/∫02π (|FPH − FPHcalc|) P(φ) d(φ)], where P(φ) is the probability of a phase value of φ for reflection h. PPano = (1/Nrefl) Σh [|ΔobsANO|/∫02π (|ΔobsANO − ΔcalcANO|) P(φ), d(), where ΔobsANO and ΔcalcANO are the Friedel-pair differences in the observed and calculated structure-factor amplitudes, respectively, for reflection h.


8FOM: figure of merit.













TABLE 8





GCYH-IB•Mn2+ X-ray data collection


GCYH-IB•Mn2+


















Spacegroup
C2221



Dataset




Unit cell (Å)
92.2, 100.4, 113.9



Wavelength (Å)
0.97607



Resolution (Å)
30.33-2.04



Unique reflections (ano)
33,675 (3,314)1 



Completeness (%)
99.8 (99.9)



Redundancy
4.5 (4.5)



Rmerge (%)
 7.1 (42.8)



<I/σ(I)>
11.0





1Highest-resolution shell (2.04-2.11 Å) information in parentheses.













TABLE 9







Structure refinement of GCYH-IB and GCYH-IB•Mn2+


Structure refinement










GCYH-IB
GCYH-IB•Mn2+





Resolution range
45.9-2.2 Å9
30.33-2.04


Number of reflections




working/free
42,83310/4,631 10 
31,937/1,710 


Number of atoms




protein/water
3,829/133  
3,829/261  


active site metal ions
2
2


other ions
1
2


other ligands
4
3


R-cryst11/R-free12 (%)
0.20/0.25
0.19/0.26


Rmsd bond lengths (Å)
0.007
0.019


Rmsd bond angles (Å)
0.825
1.754


Ramachandran Plot (%)




favored
93.2
96.9


allowed
6.8
3.1


Wilson B-factor (Å2)
40.3
37.4





9During density modification, structure factors were calculated for remote-wavelength data in the resolution range 2.3-2.2 Å.


10Anomalous pairs treated as separate reflections.


11Crystallographic R-factor = 100 × (Σh||Fobs(h)| − |Fcalc(h)||)/Σh |Fobs(h)|, where Fobs(h) and Fcalc(h) are the observed structure factor amplitude and the structurefactor amplitude calculated from the model, respectively.


12The free R-factor was calculated by using 90% and 95% of the data for GCYH-IB and GCYH-IB•Mn2+, respectively.













TABLE 10





Three-Dimensional Coordinates of Neisseria gonorrhoeae GCYH-IB (SEQ. ID. No. 8)
























ATOM
1
N
ARG
14
50.990
37.265
26.073
1.00
56.18


ATOM
2
CA
ARG
14
50.011
36.185
25.960
1.00
93.83


ATOM
3
C
ARG
14
49.059
36.319
24.779
1.00
0.95


ATOM
4
O
ARG
14
48.591
37.409
24.432
1.00
0.99


ATOM
5
CB
ARG
14
49.303
35.895
27.281
1.00
91.72


ATOM
6
CG
ARG
14
49.942
34.713
27.967
1.00
98.01


ATOM
7
CD
ARG
14
51.285
34.426
27.304
1.00
0.59


ATOM
8
NE
ARG
14
51.414
33.039
26.865
1.00
0.30


ATOM
9
CZ
ARG
14
52.447
32.573
26.171
1.00
0.57


ATOM
10
NH1
ARG
14
53.439
33.390
25.833
1.00
0.47


ATOM
11
NH2
ARG
14
52.489
31.293
25.814
1.00
0.76


ATOM
12
N
ASN
15
48.763
35.156
24.216
1.00
0.82


ATOM
13
CA
ASN
15
48.731
34.960
22.775
1.00
0.69


ATOM
14
C
ASN
15
47.386
34.873
22.064
1.00
0.82


ATOM
15
O
ASN
15
47.347
34.785
20.840
1.00
0.58


ATOM
16
CB
ASN
15
49.542
33.711
22.446
1.00
0.43


ATOM
17
CG
ASN
15
50.905
34.038
21.890
1.00
0.83


ATOM
18
OD1
ASN
15
51.045
34.928
21.057
1.00
0.77


ATOM
19
ND2
ASN
15
51.914
33.309
22.326
1.00
0.18


ATOM
20
N
LEU
16
46.303
34.863
22.829
1.00
93.09


ATOM
21
CA
LEU
16
44.939
34.936
22.298
1.00
61.91


ATOM
22
C
LEU
16
44.622
34.166
21.008
1.00
56.02


ATOM
23
O
LEU
16
45.138
34.469
19.932
1.00
38.84


ATOM
24
CB
LEU
16
44.489
36.387
22.186
1.00
59.10


ATOM
25
CG
LEU
16
43.830
36.989
23.430
1.00
70.01


ATOM
26
CD1
LEU
16
44.738
36.859
24.627
1.00
95.51


ATOM
27
CD2
LEU
16
43.495
38.446
23.180
1.00
64.01


ATOM
28
N
PRO
17
43.757
33.151
21.121
1.00
46.50


ATOM
29
CA
PRO
17
43.251
32.480
19.919
1.00
51.15


ATOM
30
C
PRO
17
42.355
33.456
19.159
1.00
50.11


ATOM
31
O
PRO
17
41.764
34.343
19.781
1.00
53.59


ATOM
32
CB
PRO
17
42.371
31.359
20.477
1.00
48.36


ATOM
33
CG
PRO
17
42.657
31.288
21.920
1.00
47.75


ATOM
34
CD
PRO
17
43.193
32.595
22.362
1.00
35.50


ATOM
35
N
ILE
18
42.269
33.309
17.840
1.00
37.05


ATOM
36
CA
ILE
18
41.329
34.091
17.045
1.00
44.06


ATOM
37
C
ILE
18
40.165
33.183
16.623
1.00
37.56


ATOM
38
O
ILE
18
40.365
32.151
15.989
1.00
33.36


ATOM
39
CB
ILE
18
42.022
34.736
15.835
1.00
40.66


ATOM
40
CG1
ILE
18
43.083
35.747
16.310
1.00
47.12


ATOM
41
CG2
ILE
18
41.009
35.427
14.932
1.00
45.97


ATOM
42
CD1
ILE
18
44.084
36.146
15.235
1.00
36.80


ATOM
43
N
LEU
51
42.102
30.092
14.708
1.00
39.41


ATOM
44
CA
LEU
51
43.542
30.191
14.783
1.00
40.03


ATOM
45
C
LEU
51
43.945
30.049
16.241
1.00
49.59


ATOM
46
O
LEU
51
43.620
30.892
17.048
1.00
35.47


ATOM
47
CB
LEU
51
44.031
31.523
14.227
1.00
43.30


ATOM
48
CG
LEU
51
45.544
31.592
14.050
1.00
47.56


ATOM
49
CD1
LEU
51
45.938
30.629
12.934
1.00
46.53


ATOM
50
CD2
LEU
51
46.047
33.017
13.741
1.00
36.00


ATOM
51
N
PRO
52
44.626
28.949
16.581
1.00
47.01


ATOM
52
CA
PRO
52
45.190
28.656
17.906
1.00
54.47


ATOM
53
C
PRO
52
46.064
29.798
18.441
1.00
47.94


ATOM
54
O
PRO
52
46.671
30.515
17.665
1.00
42.41


ATOM
55
CB
PRO
52
46.074
27.435
17.643
1.00
45.04


ATOM
56
CG
PRO
52
45.583
26.838
16.384
1.00
58.50


ATOM
57
CD
PRO
52
45.024
27.960
15.569
1.00
44.63


ATOM
58
N
ALA
53
46.140
29.938
19.754
1.00
48.98


ATOM
59
CA
ALA
53
46.895
31.025
20.372
1.00
58.53


ATOM
60
C
ALA
53
48.293
31.269
19.809
1.00
62.49


ATOM
61
O
ALA
53
48.705
32.414
19.618
1.00
65.81


ATOM
62
CB
ALA
53
46.968
30.817
21.866
1.00
53.72


ATOM
63
N
GLU
54
49.045
30.206
19.556
1.00
72.43


ATOM
64
CA
GLU
54
50.444
30.426
19.208
1.00
0.41


ATOM
65
C
GLU
54
50.782
30.220
17.740
1.00
90.42


ATOM
66
O
GLU
54
51.950
30.167
17.369
1.00
95.32


ATOM
67
CB
GLU
54
51.388
29.642
20.125
1.00
0.46


ATOM
68
CG
GLU
54
51.661
28.215
19.713
1.00
0.78


ATOM
69
CD
GLU
54
52.565
27.509
20.707
1.00
0.22


ATOM
70
OE1
GLU
54
52.165
27.386
21.885
1.00
0.86


ATOM
71
OE2
GLU
54
53.675
27.080
20.317
1.00
0.17


ATOM
72
N
GLN
55
49.757
30.122
16.905
1.00
74.01


ATOM
73
CA
GLN
55
49.960
30.205
15.468
1.00
65.50


ATOM
74
C
GLN
55
49.842
31.683
15.100
1.00
60.70


ATOM
75
O
GLN
55
48.917
32.349
15.541
1.00
63.86


ATOM
76
CB
GLN
55
48.915
29.362
14.736
1.00
64.04


ATOM
77
CG
GLN
55
49.232
29.077
13.274
1.00
67.10


ATOM
78
CD
GLN
55
48.245
28.102
12.656
1.00
78.01


ATOM
79
OE1
GLN
55
47.694
27.243
13.344
1.00
86.83


ATOM
80
NE2
GLN
55
48.020
28.230
11.349
1.00
66.25


ATOM
81
N
LYS
56
50.785
32.197
14.316
1.00
58.08


ATOM
82
CA
LYS
56
50.833
33.629
14.040
1.00
68.32


ATOM
83
C
LYS
56
49.826
34.047
12.981
1.00
68.10


ATOM
84
O
LYS
56
49.327
35.168
13.007
1.00
70.15


ATOM
85
CB
LYS
56
52.240
34.063
13.606
1.00
86.98


ATOM
86
CG
LYS
56
52.324
35.528
13.177
1.00
0.17


ATOM
87
CD
LYS
56
53.736
35.934
12.796
1.00
0.61


ATOM
88
CE
LYS
56
54.133
35.369
11.443
1.00
0.08


ATOM
89
NZ
LYS
56
55.504
35.801
11.051
1.00
0.69


ATOM
90
N
GLY
57
49.550
33.142
12.044
1.00
53.87


ATOM
91
CA
GLY
57
48.726
33.462
10.893
1.00
62.82


ATOM
92
C
GLY
57
48.122
32.238
10.237
1.00
69.86


ATOM
93
O
GLY
57
48.528
31.114
10.513
1.00
61.08


ATOM
94
N
THR
58
47.134
32.456
9.376
1.00
69.78


ATOM
95
CA
THR
58
46.546
31.375
8.602
1.00
71.47


ATOM
96
C
THR
58
47.141
31.433
7.205
1.00
55.97


ATOM
97
O
THR
58
48.036
32.244
6.951
1.00
59.93


ATOM
98
CB
THR
58
44.996
31.491
8.551
1.00
71.04


ATOM
99
OG1
THR
58
44.438
30.260
8.090
1.00
77.37


ATOM
100
CG2
THR
58
44.553
32.634
7.635
1.00
65.11


ATOM
101
N
HIS
59
46.646
30.597
6.297
1.00
58.22


ATOM
102
CA
HIS
59
47.133
30.614
4.921
1.00
64.81


ATOM
103
C
HIS
59
46.042
31.111
3.982
1.00
61.25


ATOM
104
O
HIS
59
45.196
30.337
3.553
1.00
68.43


ATOM
105
CB
HIS
59
47.617
29.219
4.529
1.00
66.44


ATOM
106
CG
HIS
59
48.517
28.597
5.553
1.00
72.69


ATOM
107
ND1
HIS
59
48.032
27.906
6.639
1.00
76.25


ATOM
108
CD2
HIS
59
49.864
28.598
5.667
1.00
76.00


ATOM
109
CE1
HIS
59
49.048
27.489
7.377
1.00
85.64


ATOM
110
NE2
HIS
59
50.168
27.892
6.811
1.00
86.98


ATOM
111
N
MSE
60
46.076
32.402
3.661
1.00
65.09


ATOM
112
CA
MSE
60
44.944
33.083
3.033
1.00
58.00


ATOM
113
C
MSE
60
44.570
32.565
1.654
1.00
50.50


ATOM
114
O
MSE
60
43.381
32.500
1.314
1.00
53.78


ATOM
115
CB
MSE
60
45.194
34.591
2.971
1.00
62.77


ATOM
116
CG
MSE
60
45.200
35.270
4.331
1.00
87.09


ATOM
117
SE
MSE
60
43.419
35.392
5.187
1.00
78.03


ATOM
118
CE
MSE
60
43.904
36.431
6.770
1.00
92.20


ATOM
119
N
SER
61
45.581
32.191
0.870
1.00
45.42


ATOM
120
CA
SER
61
45.372
31.744
−0.512
1.00
47.54


ATOM
121
C
SER
61
44.668
30.391
−0.647
1.00
55.39


ATOM
122
O
SER
61
44.049
30.106
−1.677
1.00
61.05


ATOM
123
CB
SER
61
46.682
31.749
−1.310
1.00
57.85


ATOM
124
OG
SER
61
47.430
30.578
−1.078
1.00
61.24


ATOM
125
N
ARG
62
44.750
29.559
0.383
1.00
50.58


ATOM
126
CA
ARG
62
44.031
28.279
0.363
1.00
51.01


ATOM
127
C
ARG
62
42.498
28.410
0.275
1.00
41.04


ATOM
128
O
ARG
62
41.844
27.611
−0.363
1.00
44.23


ATOM
129
CB
ARG
62
44.429
27.432
1.569
1.00
50.03


ATOM
130
CG
ARG
62
45.869
26.931
1.485
1.00
50.73


ATOM
131
CD
ARG
62
46.291
26.230
2.754
1.00
47.50


ATOM
132
NE
ARG
62
47.747
26.097
2.827
1.00
72.17


ATOM
133
CZ
ARG
62
48.391
25.436
3.779
1.00
68.28


ATOM
134
NH1
ARG
62
47.707
24.837
4.742
1.00
59.95


ATOM
135
NH2
ARG
62
49.714
25.375
3.768
1.00
79.31


ATOM
136
N
PHE
63
41.940
29.427
0.917
1.00
41.97


ATOM
137
CA
PHE
63
40.503
29.668
0.879
1.00
44.58


ATOM
138
C
PHE
63
40.028
29.808
−0.557
1.00
49.40


ATOM
139
O
PHE
63
39.061
29.168
−0.957
1.00
39.22


ATOM
140
CB
PHE
63
40.142
30.920
1.655
1.00
40.89


ATOM
141
CG
PHE
63
40.396
30.816
3.121
1.00
28.93


ATOM
142
CD1
PHE
63
39.581
30.031
3.914
1.00
38.88


ATOM
143
CD2
PHE
63
41.431
31.517
3.706
1.00
35.68


ATOM
144
CE1
PHE
63
39.790
29.946
5.262
1.00
36.00


ATOM
145
CE2
PHE
63
41.649
31.445
5.051
1.00
44.36


ATOM
146
CZ
PHE
63
40.829
30.669
5.838
1.00
30.89


ATOM
147
N
ALA
65
41.881
28.991
−3.386
1.00
31.61


ATOM
148
CA
ALA
65
42.210
27.754
−4.104
1.00
46.10


ATOM
149
C
ALA
65
41.122
26.698
−3.901
1.00
50.34


ATOM
150
O
ALA
65
40.794
25.957
−4.815
1.00
45.89


ATOM
151
CB
ALA
65
43.597
27.186
−3.664
1.00
43.69


ATOM
152
N
LEU
89
42.214
21.349
4.987
1.00
56.45


ATOM
153
CA
LEU
89
43.163
22.013
4.115
1.00
52.29


ATOM
154
C
LEU
89
43.946
23.137
4.829
1.00
59.53


ATOM
155
O
LEU
89
45.146
23.299
4.615
1.00
40.19


ATOM
156
CB
LEU
89
42.421
22.578
2.905
1.00
53.20


ATOM
157
CG
LEU
89
43.248
23.410
1.928
1.00
60.26


ATOM
158
CD1
LEU
89
44.138
22.497
1.126
1.00
43.38


ATOM
159
CD2
LEU
89
42.353
24.204
1.011
1.00
58.43


ATOM
160
N
LEU
90
43.268
23.916
5.666
1.00
49.78


ATOM
161
CA
LEU
90
43.935
24.970
6.421
1.00
62.35


ATOM
162
C
LEU
90
44.539
24.469
7.733
1.00
64.62


ATOM
163
O
LEU
90
45.059
25.243
8.539
1.00
60.89


ATOM
164
CB
LEU
90
42.973
26.124
6.657
1.00
47.33


ATOM
165
CG
LEU
90
43.040
27.025
5.431
1.00
59.03


ATOM
166
CD1
LEU
90
41.833
26.865
4.532
1.00
36.20


ATOM
167
CD2
LEU
90
43.199
28.447
5.854
1.00
69.47


ATOM
168
N
ASP
91
44.466
23.159
7.928
1.00
62.53


ATOM
169
CA
ASP
91
45.047
22.520
9.096
1.00
74.18


ATOM
170
C
ASP
91
44.501
23.155
10.370
1.00
64.49


ATOM
171
O
ASP
91
45.269
23.640
11.196
1.00
49.15


ATOM
172
CB
ASP
91
46.574
22.632
9.041
1.00
79.82


ATOM
173
CG
ASP
91
47.201
21.658
8.051
1.00
0.54


ATOM
174
OD1
ASP
91
46.457
20.880
7.417
1.00
0.33


ATOM
175
OD2
ASP
91
48.445
21.657
7.918
1.00
0.26


ATOM
176
N
SER
92
43.176
23.153
10.523
1.00
57.69


ATOM
177
CA
SER
92
42.553
23.776
11.687
1.00
45.90


ATOM
178
C
SER
92
41.470
22.934
12.389
1.00
51.56


ATOM
179
O
SER
92
40.897
22.048
11.805
1.00
45.21


ATOM
180
CB
SER
92
41.987
25.143
11.299
1.00
50.32


ATOM
181
OG
SER
92
41.420
25.786
12.424
1.00
54.21


ATOM
182
N
ARG
105
35.965
63.521
15.017
1.00
33.07


ATOM
183
CA
ARG
105
36.979
63.849
15.997
1.00
29.88


ATOM
184
C
ARG
105
38.125
64.607
15.317
1.00
32.84


ATOM
185
O
ARG
105
38.619
64.208
14.260
1.00
36.69


ATOM
186
CB
ARG
105
37.493
62.590
16.668
1.00
29.04


ATOM
187
CG
ARG
105
38.351
62.846
17.863
1.00
48.37


ATOM
188
CD
ARG
105
39.092
61.594
18.287
1.00
47.10


ATOM
189
NE
ARG
105
39.543
61.665
19.671
1.00
44.80


ATOM
190
CZ
ARG
105
40.409
60.822
20.222
1.00
56.34


ATOM
191
NH1
ARG
105
40.945
59.847
19.494
1.00
36.07


ATOM
192
NH2
ARG
105
40.747
60.953
21.503
1.00
43.89


ATOM
193
N
LYS
106
38.492
65.735
15.908
1.00
38.84


ATOM
194
CA
LYS
106
39.620
66.529
15.447
1.00
52.88


ATOM
195
C
LYS
106
40.929
65.782
15.718
1.00
42.47


ATOM
196
O
LYS
106
41.179
65.301
16.828
1.00
53.64


ATOM
197
CB
LYS
106
39.610
67.901
16.128
1.00
46.81


ATOM
198
CG
LYS
106
40.099
69.022
15.248
1.00
69.34


ATOM
199
CD
LYS
106
39.127
70.188
15.285
1.00
90.51


ATOM
200
CE
LYS
106
39.855
71.518
15.320
1.00
0.04


ATOM
201
NZ
LYS
106
40.925
71.586
14.292
1.00
0.37


ATOM
202
N
LYS
107
41.732
65.658
14.670
1.00
34.97


ATOM
203
CA
LYS
107
43.065
65.060
14.759
1.00
52.25


ATOM
204
C
LYS
107
44.181
66.034
14.370
1.00
51.78


ATOM
205
O
LYS
107
43.937
67.035
13.709
1.00
50.24


ATOM
206
CB
LYS
107
43.145
63.819
13.880
1.00
46.87


ATOM
207
CG
LYS
107
42.805
62.570
14.628
1.00
73.11


ATOM
208
CD
LYS
107
41.862
61.713
13.838
1.00
52.85


ATOM
209
CE
LYS
107
42.594
60.754
12.936
1.00
74.85


ATOM
210
NZ
LYS
107
43.478
59.816
13.679
1.00
60.74


ATOM
211
N
THR
108
45.406
65.706
14.768
1.00
39.92


ATOM
212
CA
THR
108
46.595
66.510
14.453
1.00
51.78


ATOM
213
C
THR
108
47.620
65.753
13.599
1.00
56.01


ATOM
214
O
THR
108
48.046
64.670
13.972
1.00
48.49


ATOM
215
CB
THR
108
47.265
66.962
15.743
1.00
58.98


ATOM
216
OG1
THR
108
46.367
67.820
16.453
1.00
76.08


ATOM
217
CG2
THR
108
48.565
67.713
15.439
1.00
63.78


ATOM
218
N
ALA
109
48.009
66.319
12.457
1.00
51.19


ATOM
219
CA
ALA
109
48.981
65.674
11.577
1.00
47.51


ATOM
220
C
ALA
109
50.292
65.456
12.332
1.00
56.59


ATOM
221
O
ALA
109
50.692
66.287
13.122
1.00
58.26


ATOM
222
CB
ALA
109
49.198
66.489
10.318
1.00
52.79


ATOM
223
N
PRO
110
50.940
64.306
12.120
1.00
60.88


ATOM
224
CA
PRO
110
52.063
63.857
12.954
1.00
54.80


ATOM
225
C
PRO
110
53.369
64.686
12.855
1.00
73.41


ATOM
226
O
PRO
110
54.163
64.643
13.794
1.00
94.80


ATOM
227
CB
PRO
110
52.284
62.420
12.469
1.00
59.86


ATOM
228
CG
PRO
110
51.694
62.406
11.099
1.00
62.30


ATOM
229
CD
PRO
110
50.486
63.240
11.220
1.00
65.45


ATOM
230
N
VAL
111
53.586
65.414
11.759
1.00
63.03


ATOM
231
CA
VAL
111
54.752
66.292
11.640
1.00
67.64


ATOM
232
C
VAL
111
54.375
67.780
11.620
1.00
74.71


ATOM
233
O
VAL
111
54.850
68.549
12.447
1.00
70.73


ATOM
234
CB
VAL
111
55.618
65.937
10.406
1.00
71.63


ATOM
235
CG1
VAL
111
56.663
67.006
10.150
1.00
85.60


ATOM
236
CG2
VAL
111
56.284
64.605
10.607
1.00
80.10


ATOM
237
N
SER
112
53.508
68.170
10.689
1.00
78.75


ATOM
238
CA
SER
112
53.131
69.567
10.506
1.00
75.70


ATOM
239
C
SER
112
52.215
70.105
11.605
1.00
69.51


ATOM
240
O
SER
112
52.104
71.327
11.801
1.00
49.35


ATOM
241
CB
SER
112
52.460
69.758
9.146
1.00
52.06


ATOM
242
OG
SER
112
51.115
69.326
9.190
1.00
56.21


ATOM
243
N
GLY
113
51.551
69.189
12.304
1.00
52.71


ATOM
244
CA
GLY
113
50.584
69.545
13.330
1.00
53.69


ATOM
245
C
GLY
113
49.263
70.121
12.828
1.00
57.78


ATOM
246
O
GLY
113
48.436
70.534
13.636
1.00
46.82


ATOM
247
N
ILE
114
49.067
70.165
11.509
1.00
48.95


ATOM
248
CA
ILE
114
47.827
70.689
10.954
1.00
62.98


ATOM
249
C
ILE
114
46.650
69.813
11.372
1.00
62.30


ATOM
250
O
ILE
114
46.718
68.582
11.321
1.00
62.97


ATOM
251
CB
ILE
114
47.875
70.826
9.417
1.00
74.53


ATOM
252
CG1
ILE
114
49.070
71.677
8.990
1.00
89.66


ATOM
253
CG2
ILE
114
46.597
71.473
8.904
1.00
60.35


ATOM
254
CD1
ILE
114
49.088
71.999
7.508
1.00
0.82


ATOM
255
N
ARG
115
45.581
70.461
11.809
1.00
58.21


ATOM
256
CA
ARG
115
44.416
69.765
12.333
1.00
66.68


ATOM
257
C
ARG
115
43.330
69.540
11.287
1.00
57.62


ATOM
258
O
ARG
115
43.135
70.350
10.377
1.00
46.10


ATOM
259
CB
ARG
115
43.858
70.514
13.536
1.00
68.26


ATOM
260
CG
ARG
115
44.883
70.668
14.648
1.00
96.72


ATOM
261
CD
ARG
115
44.398
71.606
15.733
1.00
0.68


ATOM
262
NE
ARG
115
43.474
70.954
16.653
1.00
0.03


ATOM
263
CZ
ARG
115
42.717
71.604
17.530
1.00
0.61


ATOM
264
NH1
ARG
115
42.768
72.927
17.601
1.00
0.15


ATOM
265
NH2
ARG
115
41.903
70.932
18.331
1.00
0.32


ATOM
266
N
SER
116
42.647
68.407
11.413
1.00
42.68


ATOM
267
CA
SER
116
41.529
68.076
10.535
1.00
43.53


ATOM
268
C
SER
116
40.657
67.039
11.224
1.00
43.72


ATOM
269
O
SER
116
41.096
66.350
12.142
1.00
45.98


ATOM
270
CB
SER
116
42.026
67.562
9.184
1.00
62.92


ATOM
271
OG
SER
116
42.807
66.390
9.331
1.00
72.92


ATOM
272
N
LEU
117
39.411
66.949
10.796
1.00
45.79


ATOM
273
CA
LEU
117
38.468
66.030
11.393
1.00
41.01


ATOM
274
C
LEU
117
38.604
64.680
10.718
1.00
30.98


ATOM
275
O
LEU
117
38.923
64.602
9.534
1.00
36.37


ATOM
276
CB
LEU
117
37.051
66.528
11.164
1.00
27.67


ATOM
277
CG
LEU
117
36.540
67.797
11.834
1.00
46.81


ATOM
278
CD1
LEU
117
35.225
68.156
11.179
1.00
42.43


ATOM
279
CD2
LEU
117
36.379
67.617
13.334
1.00
33.79


ATOM
280
N
LEU
118
38.363
63.616
11.471
1.00
36.49


ATOM
281
CA
LEU
118
38.123
62.309
10.869
1.00
34.89


ATOM
282
C
LEU
118
36.754
61.798
11.335
1.00
43.06


ATOM
283
O
LEU
118
36.329
62.065
12.465
1.00
27.18


ATOM
284
CB
LEU
118
39.216
61.307
11.257
1.00
37.46


ATOM
285
CG
LEU
118
39.256
60.025
10.399
1.00
51.69


ATOM
286
CD1
LEU
118
39.805
60.313
9.021
1.00
47.89


ATOM
287
CD2
LEU
118
40.055
58.916
11.031
1.00
55.80


ATOM
288
N
PRO
142
38.424
53.420
10.783
1.00
23.25


ATOM
289
CA
PRO
142
39.252
53.150
9.606
1.00
26.43


ATOM
290
C
PRO
142
40.728
53.367
9.970
1.00
33.52


ATOM
291
O
PRO
142
41.004
54.347
10.649
1.00
34.13


ATOM
292
CB
PRO
142
38.856
54.257
8.632
1.00
33.09


ATOM
293
CG
PRO
142
37.937
55.197
9.398
1.00
36.83


ATOM
294
CD
PRO
142
37.951
54.809
10.830
1.00
33.30


ATOM
295
N
VAL
143
41.629
52.489
9.535
1.00
29.80


ATOM
296
CA
VAL
143
43.062
52.644
9.755
1.00
29.02


ATOM
297
C
VAL
143
43.816
52.138
8.533
1.00
37.92


ATOM
298
O
VAL
143
43.207
51.728
7.551
1.00
42.12


ATOM
299
CB
VAL
143
43.547
51.867
10.977
1.00
45.56


ATOM
300
CG1
VAL
143
42.719
52.247
12.211
1.00
32.69


ATOM
301
CG2
VAL
143
43.500
50.365
10.696
1.00
46.28


ATOM
302
N
THR
144
45.145
52.193
8.601
1.00
40.29


ATOM
303
CA
THR
144
46.019
51.692
7.543
1.00
58.11


ATOM
304
C
THR
144
46.639
50.402
8.022
1.00
45.82


ATOM
305
O
THR
144
47.059
50.298
9.178
1.00
41.15


ATOM
306
CB
THR
144
47.182
52.666
7.239
1.00
76.98


ATOM
307
OG1
THR
144
46.679
53.997
7.072
1.00
84.02


ATOM
308
CG2
THR
144
47.933
52.234
5.985
1.00
83.55


ATOM
309
N
SER
145
46.701
49.415
7.145
1.00
36.24


ATOM
310
CA
SER
145
47.395
48.183
7.473
1.00
52.43


ATOM
311
C
SER
145
48.464
47.925
6.424
1.00
54.50


ATOM
312
O
SER
145
48.248
48.158
5.250
1.00
43.53


ATOM
313
CB
SER
145
46.416
47.009
7.539
1.00
64.86


ATOM
314
OG
SER
145
45.730
46.851
6.309
1.00
68.39


ATOM
315
N
LEU
146
49.621
47.452
6.852
1.00
56.00


ATOM
316
CA
LEU
146
50.691
47.139
5.919
1.00
62.10


ATOM
317
C
LEU
146
51.116
45.682
6.109
1.00
44.80


ATOM
318
O
LEU
146
51.243
45.211
7.229
1.00
49.94


ATOM
319
CB
LEU
146
51.872
48.103
6.111
1.00
66.77


ATOM
320
CG
LEU
146
53.014
47.984
5.089
1.00
65.46


ATOM
321
CD1
LEU
146
53.480
49.346
4.611
1.00
57.34


ATOM
322
CD2
LEU
146
54.166
47.156
5.653
1.00
61.66


ATOM
323
N
CYS
147
51.339
44.976
5.012
1.00
33.12


ATOM
324
CA
CYS
147
51.537
43.531
5.062
1.00
53.22


ATOM
325
C
CYS
147
52.978
43.105
5.361
1.00
49.05


ATOM
326
O
CYS
147
53.874
43.354
4.568
1.00
43.23


ATOM
327
CB
CYS
147
51.095
42.891
3.753
1.00
44.07


ATOM
328
SG
CYS
147
51.253
41.076
3.766
1.00
43.71


ATOM
329
N
PRO
148
53.185
42.411
6.485
1.00
76.53


ATOM
330
CA
PRO
148
54.521
41.952
6.877
1.00
83.85


ATOM
331
C
PRO
148
55.120
40.977
5.869
1.00
74.03


ATOM
332
O
PRO
148
56.284
41.115
5.550
1.00
61.76


ATOM
333
CB
PRO
148
54.274
41.256
8.215
1.00
84.26


ATOM
334
CG
PRO
148
52.968
41.783
8.690
1.00
73.26


ATOM
335
CD
PRO
148
52.165
42.004
7.458
1.00
71.33


ATOM
336
N
CYS
149
54.340
40.025
5.369
1.00
75.80


ATOM
337
CA
CYS
149
54.833
39.072
4.379
1.00
74.27


ATOM
338
C
CYS
149
55.272
39.756
3.091
1.00
78.06


ATOM
339
O
CYS
149
56.307
39.421
2.536
1.00
46.90


ATOM
340
CB
CYS
149
53.772
38.010
4.067
1.00
95.66


ATOM
341
SG
CYS
149
54.170
36.925
2.670
1.00
84.40


ATOM
342
N
SER
150
54.470
40.706
2.625
1.00
80.75


ATOM
343
CA
SER
150
54.775
41.480
1.431
1.00
64.38


ATOM
344
C
SER
150
56.102
42.224
1.569
1.00
54.94


ATOM
345
O
SER
150
56.914
42.224
0.646
1.00
38.94


ATOM
346
CB
SER
150
53.651
42.484
1.173
1.00
69.77


ATOM
347
OG
SER
150
53.899
43.263
0.023
1.00
33.31


ATOM
348
N
LYS
151
56.300
42.885
2.708
1.00
33.12


ATOM
349
CA
LYS
151
57.547
43.593
2.989
1.00
68.45


ATOM
350
C
LYS
151
58.748
42.633
3.032
1.00
66.78


ATOM
351
O
LYS
151
59.751
42.833
2.357
1.00
57.85


ATOM
352
CB
LYS
151
57.428
44.328
4.320
1.00
71.24


ATOM
353
CG
LYS
151
58.697
45.032
4.746
1.00
76.97


ATOM
354
CD
LYS
151
58.592
45.599
6.148
1.00
68.20


ATOM
355
CE
LYS
151
59.889
46.271
6.539
1.00
58.17


ATOM
356
NZ
LYS
151
59.812
46.823
7.902
1.00
59.77


ATOM
357
N
GLU
152
58.613
41.585
3.829
1.00
78.41


ATOM
358
CA
GLU
152
59.640
40.561
4.021
1.00
92.52


ATOM
359
C
GLU
152
60.153
39.905
2.735
1.00
79.43


ATOM
360
O
GLU
152
61.339
39.649
2.602
1.00
69.31


ATOM
361
CB
GLU
152
59.091
39.489
4.962
1.00
0.08


ATOM
362
CG
GLU
152
60.011
38.331
5.246
1.00
0.79


ATOM
363
CD
GLU
152
59.323
37.258
6.072
1.00
0.24


ATOM
364
OE1
GLU
152
58.216
36.827
5.688
1.00
0.23


ATOM
365
OE2
GLU
152
59.884
36.848
7.108
1.00
0.86


ATOM
366
N
ILE
153
59.262
39.634
1.790
1.00
89.96


ATOM
367
CA
ILE
153
59.642
38.882
0.597
1.00
92.18


ATOM
368
C
ILE
153
60.114
39.737
−0.576
1.00
88.22


ATOM
369
O
ILE
153
60.802
39.239
−1.457
1.00
82.43


ATOM
370
CB
ILE
153
58.513
37.932
0.108
1.00
86.38


ATOM
371
CG1
ILE
153
57.298
38.733
−0.386
1.00
77.79


ATOM
372
CG2
ILE
153
58.133
36.944
1.202
1.00
83.92


ATOM
373
CD1
ILE
153
56.227
37.894
−1.037
1.00
62.29


ATOM
374
N
SER
154
59.745
41.013
−0.609
1.00
88.01


ATOM
375
CA
SER
154
60.133
41.853
−1.742
1.00
86.91


ATOM
376
C
SER
154
61.351
42.710
−1.418
1.00
67.99


ATOM
377
O
SER
154
61.612
43.017
−0.263
1.00
52.76


ATOM
378
CB
SER
154
58.960
42.701
−2.253
1.00
78.98


ATOM
379
OG
SER
154
58.304
43.363
−1.197
1.00
77.89


ATOM
380
N
GLN
155
62.102
43.079
−2.448
1.00
68.23


ATOM
381
CA
GLN
155
63.334
43.837
−2.252
1.00
87.17


ATOM
382
C
GLN
155
63.032
45.299
−1.942
1.00
86.25


ATOM
383
O
GLN
155
63.870
46.020
−1.408
1.00
67.23


ATOM
384
CB
GLN
155
64.269
43.704
−3.460
1.00
96.47


ATOM
385
CG
GLN
155
63.654
44.106
−4.786
1.00
0.52


ATOM
386
CD
GLN
155
64.638
44.006
−5.936
1.00
0.43


ATOM
387
OE1
GLN
155
65.818
44.328
−5.789
1.00
0.25


ATOM
388
NE2
GLN
155
64.156
43.559
−7.090
1.00
0.08


ATOM
389
N
TYR
156
61.822
45.723
−2.284
1.00
82.97


ATOM
390
CA
TYR
156
61.318
47.030
−1.884
1.00
80.96


ATOM
391
C
TYR
156
59.800
47.062
−1.963
1.00
80.92


ATOM
392
O
TYR
156
59.193
46.208
−2.600
1.00
47.73


ATOM
393
CB
TYR
156
61.929
48.158
−2.723
1.00
65.47


ATOM
394
CG
TYR
156
62.164
47.832
−4.181
1.00
85.68


ATOM
395
CD1
TYR
156
61.111
47.526
−5.027
1.00
77.03


ATOM
396
CD2
TYR
156
63.447
47.853
−4.715
1.00
90.55


ATOM
397
CE1
TYR
156
61.328
47.238
−6.361
1.00
99.10


ATOM
398
CE2
TYR
156
63.672
47.566
−6.044
1.00
96.22


ATOM
399
CZ
TYR
156
62.611
47.260
−6.862
1.00
0.08


ATOM
400
OH
TYR
156
62.837
46.976
−8.186
1.00
90.79


ATOM
401
N
GLY
157
59.196
48.044
−1.304
1.00
72.73


ATOM
402
CA
GLY
157
57.754
48.188
−1.307
1.00
58.71


ATOM
403
C
GLY
157
57.062
47.167
−0.424
1.00
52.06


ATOM
404
O
GLY
157
57.631
46.138
−0.078
1.00
47.90


ATOM
405
N
ALA
158
55.824
47.471
−0.046
1.00
33.39


ATOM
406
CA
ALA
158
54.953
46.536
0.669
1.00
56.02


ATOM
407
C
ALA
158
53.518
46.951
0.406
1.00
62.89


ATOM
408
O
ALA
158
53.168
48.113
0.567
1.00
42.34


ATOM
409
CB
ALA
158
55.239
46.546
2.164
1.00
50.98


ATOM
410
N
HIS
159
52.675
46.023
−0.016
1.00
53.10


ATOM
411
CA
HIS
159
51.307
46.421
−0.280
1.00
50.36


ATOM
412
C
HIS
159
50.642
46.805
1.043
1.00
46.60


ATOM
413
O
HIS
159
50.840
46.156
2.077
1.00
42.85


ATOM
414
CB
HIS
159
50.528
45.359
−1.061
1.00
69.62


ATOM
415
CG
HIS
159
50.007
44.242
−0.218
1.00
64.17


ATOM
416
ND1
HIS
159
48.869
44.363
0.549
1.00
65.54


ATOM
417
CD2
HIS
159
50.456
42.985
−0.031
1.00
51.87


ATOM
418
CE1
HIS
159
48.648
43.223
1.182
1.00
52.61


ATOM
419
NE2
HIS
159
49.595
42.373
0.846
1.00
61.55


ATOM
420
N
ASN
160
49.913
47.915
1.011
1.00
39.47


ATOM
421
CA
ASN
160
49.141
48.362
2.156
1.00
41.24


ATOM
422
C
ASN
160
47.750
48.703
1.673
1.00
36.77


ATOM
423
O
ASN
160
47.495
48.705
0.481
1.00
37.08


ATOM
424
CB
ASN
160
49.819
49.545
2.865
1.00
40.95


ATOM
425
CG
ASN
160
50.298
50.619
1.900
1.00
68.88


ATOM
426
OD1
ASN
160
51.460
50.618
1.484
1.00
66.81


ATOM
427
ND2
ASN
160
49.411
51.546
1.545
1.00
28.56


ATOM
428
N
GLN
161
46.855
49.012
2.591
1.00
26.40


ATOM
429
CA
GLN
161
45.458
49.252
2.236
1.00
43.83


ATOM
430
C
GLN
161
44.713
49.794
3.417
1.00
49.46


ATOM
431
O
GLN
161
45.198
49.738
4.542
1.00
43.92


ATOM
432
CB
GLN
161
44.775
47.962
1.777
1.00
57.27


ATOM
433
CG
GLN
161
44.857
46.852
2.784
1.00
60.87


ATOM
434
CD
GLN
161
46.158
46.068
2.695
1.00
52.87


ATOM
435
OE1
GLN
161
46.634
45.738
1.601
1.00
41.97


ATOM
436
NE2
GLN
161
46.725
45.746
3.850
1.00
38.64


ATOM
437
N
ARG
162
43.522
50.312
3.158
1.00
52.54


ATOM
438
CA
ARG
162
42.648
50.738
4.232
1.00
46.71


ATOM
439
C
ARG
162
42.082
49.501
4.904
1.00
59.05


ATOM
440
O
ARG
162
41.814
48.496
4.270
1.00
42.45


ATOM
441
CB
ARG
162
41.524
51.644
3.711
1.00
54.51


ATOM
442
CG
ARG
162
41.034
52.664
4.718
1.00
71.10


ATOM
443
CD
ARG
162
39.975
53.579
4.129
1.00
86.06


ATOM
444
NE
ARG
162
40.524
54.548
3.190
1.00
68.39


ATOM
445
CZ
ARG
162
39.800
55.199
2.290
1.00
75.71


ATOM
446
NH1
ARG
162
38.499
54.973
2.206
1.00
62.22


ATOM
447
NH2
ARG
162
40.375
56.065
1.471
1.00
70.75


ATOM
448
N
SER
163
41.938
49.587
6.211
1.00
37.48


ATOM
449
CA
SER
163
41.365
48.527
7.016
1.00
34.90


ATOM
450
C
SER
163
40.248
49.125
7.885
1.00
42.81


ATOM
451
O
SER
163
40.317
50.265
8.350
1.00
29.13


ATOM
452
CB
SER
163
42.466
47.877
7.862
1.00
43.38


ATOM
453
OG
SER
163
41.956
47.004
8.840
1.00
73.12


ATOM
454
N
HIS
164
39.167
48.383
8.050
1.00
25.58


ATOM
455
CA
HIS
164
38.147
48.793
9.003
1.00
27.06


ATOM
456
C
HIS
164
38.230
47.893
10.208
1.00
36.62


ATOM
457
O
HIS
164
38.126
46.676
10.089
1.00
35.13


ATOM
458
CB
HIS
164
36.748
48.713
8.377
1.00
33.69


ATOM
459
CG
HIS
164
36.524
49.686
7.266
1.00
64.30


ATOM
460
ND1
HIS
164
35.667
49.443
6.221
1.00
73.91


ATOM
461
CD2
HIS
164
37.058
50.917
7.034
1.00
61.84


ATOM
462
CE1
HIS
164
35.671
50.475
5.393
1.00
72.47


ATOM
463
NE2
HIS
164
36.512
51.379
5.866
1.00
59.98


ATOM
464
N
GLU
178
35.857
58.012
22.387
1.00
39.25


ATOM
465
CA
GLU
178
37.222
58.396
22.054
1.00
38.39


ATOM
466
C
GLU
178
38.207
57.420
22.669
1.00
48.57


ATOM
467
O
GLU
178
39.273
57.172
22.104
1.00
46.83


ATOM
468
CB
GLU
178
37.512
59.842
22.484
1.00
42.73


ATOM
469
CG
GLU
178
37.664
60.049
23.993
1.00
64.81


ATOM
470
CD
GLU
178
36.370
59.881
24.781
1.00
66.63


ATOM
471
OE1
GLU
178
35.270
60.027
24.197
1.00
60.52


ATOM
472
OE2
GLU
178
36.461
59.611
25.997
1.00
61.01


ATOM
473
N
GLU
179
37.840
56.840
23.808
1.00
37.21


ATOM
474
CA
GLU
179
38.661
55.782
24.407
1.00
40.17


ATOM
475
C
GLU
179
38.751
54.560
23.517
1.00
36.90


ATOM
476
O
GLU
179
39.825
53.985
23.374
1.00
51.37


ATOM
477
CB
GLU
179
38.129
55.350
25.773
1.00
43.49


ATOM
478
CG
GLU
179
38.141
56.416
26.843
1.00
57.74


ATOM
479
CD
GLU
179
37.805
55.843
28.214
1.00
74.66


ATOM
480
OE1
GLU
179
38.687
55.202
28.841
1.00
60.84


ATOM
481
OE2
GLU
179
36.653
56.032
28.660
1.00
68.81


ATOM
482
N
ILE
181
38.345
54.507
20.306
1.00
27.44


ATOM
483
CA
ILE
181
39.097
54.884
19.126
1.00
29.36


ATOM
484
C
ILE
181
40.614
54.834
19.407
1.00
50.07


ATOM
485
O
ILE
181
41.397
54.383
18.564
1.00
40.42


ATOM
486
CB
ILE
181
38.699
56.265
18.613
1.00
30.81


ATOM
487
CG1
ILE
181
37.266
56.212
18.047
1.00
37.62


ATOM
488
CG2
ILE
181
39.754
56.774
17.599
1.00
29.95


ATOM
489
CD1
ILE
181
36.677
57.558
17.652
1.00
39.81


ATOM
490
N
ASP
182
41.004
55.282
20.598
1.00
29.14


ATOM
491
CA
ASP
182
42.401
55.313
21.019
1.00
37.82


ATOM
492
C
ASP
182
42.982
53.891
21.154
1.00
43.42


ATOM
493
O
ASP
182
44.074
53.610
20.662
1.00
47.73


ATOM
494
CB
ASP
182
42.558
56.092
22.331
1.00
36.01


ATOM
495
CG
ASP
182
42.444
57.614
22.149
1.00
52.83


ATOM
496
OD1
ASP
182
42.697
58.124
21.032
1.00
49.45


ATOM
497
OD2
ASP
182
42.108
58.306
23.144
1.00
54.83


ATOM
498
N
TYR
183
42.257
52.988
21.807
1.00
37.63


ATOM
499
CA
TYR
183
42.705
51.598
21.887
1.00
25.05


ATOM
500
C
TYR
183
43.036
51.059
20.493
1.00
47.61


ATOM
501
O
TYR
183
43.943
50.254
20.326
1.00
41.37


ATOM
502
CB
TYR
183
41.645
50.700
22.527
1.00
33.40


ATOM
503
CG
TYR
183
41.497
50.812
24.026
1.00
47.28


ATOM
504
CD1
TYR
183
42.600
50.998
24.836
1.00
56.26


ATOM
505
CD2
TYR
183
40.252
50.681
24.633
1.00
38.98


ATOM
506
CE1
TYR
183
42.477
51.075
26.207
1.00
67.80


ATOM
507
CE2
TYR
183
40.115
50.753
26.001
1.00
55.22


ATOM
508
CZ
TYR
183
41.233
50.955
26.789
1.00
67.84


ATOM
509
OH
TYR
183
41.117
51.036
28.160
1.00
69.73


ATOM
510
N
VAL
184
42.294
51.485
19.480
1.00
32.30


ATOM
511
CA
VAL
184
42.513
50.910
18.168
1.00
34.08


ATOM
512
C
VAL
184
43.614
51.617
17.387
1.00
36.57


ATOM
513
O
VAL
184
44.448
50.970
16.789
1.00
35.67


ATOM
514
CB
VAL
184
41.228
50.851
17.308
1.00
40.81


ATOM
515
CG1
VAL
184
41.578
50.500
15.876
1.00
41.01


ATOM
516
CG2
VAL
184
40.222
49.820
17.875
1.00
29.23


ATOM
517
N
GLU
185
43.610
52.941
17.391
1.00
40.28


ATOM
518
CA
GLU
185
44.548
53.689
16.562
1.00
39.88


ATOM
519
C
GLU
185
45.993
53.527
17.037
1.00
49.88


ATOM
520
O
GLU
185
46.913
53.496
16.236
1.00
56.83


ATOM
521
CB
GLU
185
44.119
55.154
16.470
1.00
28.85


ATOM
522
CG
GLU
185
42.883
55.365
15.585
1.00
48.56


ATOM
523
CD
GLU
185
42.538
56.833
15.405
1.00
52.66


ATOM
524
OE1
GLU
185
42.974
57.633
16.251
1.00
43.17


ATOM
525
OE2
GLU
185
41.836
57.191
14.430
1.00
39.75


ATOM
526
N
THR
186
46.158
53.416
18.348
1.00
56.19


ATOM
527
CA
THR
186
47.419
53.065
18.988
1.00
60.74


ATOM
528
C
THR
186
48.080
51.839
18.356
1.00
54.76


ATOM
529
O
THR
186
49.286
51.803
18.152
1.00
53.36


ATOM
530
CB
THR
186
47.188
52.794
20.494
1.00
59.55


ATOM
531
OG1
THR
186
47.159
54.038
21.195
1.00
64.84


ATOM
532
CG2
THR
186
48.287
51.920
21.078
1.00
66.33


ATOM
533
N
GLN
187
47.274
50.843
18.028
1.00
54.99


ATOM
534
CA
GLN
187
47.774
49.561
17.551
1.00
53.27


ATOM
535
C
GLN
187
47.868
49.431
16.034
1.00
47.18


ATOM
536
O
GLN
187
48.309
48.411
15.541
1.00
56.60


ATOM
537
CB
GLN
187
46.862
48.446
18.054
1.00
45.99


ATOM
538
CG
GLN
187
46.659
48.444
19.536
1.00
53.53


ATOM
539
CD
GLN
187
47.920
48.065
20.252
1.00
60.81


ATOM
540
OE1
GLN
187
48.807
47.435
19.670
1.00
55.31


ATOM
541
NE2
GLN
187
48.015
48.432
21.520
1.00
47.26


ATOM
542
N
ALA
188
47.427
50.426
15.283
1.00
44.02


ATOM
543
CA
ALA
188
47.445
50.290
13.834
1.00
52.84


ATOM
544
C
ALA
188
48.853
50.496
13.242
1.00
61.50


ATOM
545
O
ALA
188
49.666
51.203
13.820
1.00
45.67


ATOM
546
CB
ALA
188
46.466
51.254
13.219
1.00
42.42


ATOM
547
N
SER
189
49.135
49.860
12.103
1.00
36.67


ATOM
548
CA
SER
189
50.352
50.130
11.336
1.00
49.39


ATOM
549
C
SER
189
50.511
51.630
11.189
1.00
62.48


ATOM
550
O
SER
189
51.589
52.169
11.411
1.00
51.33


ATOM
551
CB
SER
189
50.289
49.483
9.953
1.00
35.57


ATOM
552
OG
SER
189
50.524
48.091
10.040
1.00
49.82


ATOM
553
N
CYS
190
49.420
52.285
10.796
1.00
43.06


ATOM
554
CA
CYS
190
49.286
53.728
10.919
1.00
42.62


ATOM
555
C
CYS
190
47.816
54.169
10.820
1.00
49.00


ATOM
556
O
CYS
190
46.973
53.488
10.259
1.00
43.56


ATOM
557
CB
CYS
190
50.158
54.486
9.912
1.00
80.65


ATOM
558
SG
CYS
190
50.699
56.108
10.542
1.00
74.68


ATOM
559
N
GLN
191
47.510
55.311
11.396
1.00
39.65


ATOM
560
CA
GLN
191
46.148
55.797
11.388
1.00
60.24


ATOM
561
C
GLN
191
45.908
56.730
10.210
1.00
52.12


ATOM
562
O
GLN
191
46.837
57.102
9.515
1.00
49.03


ATOM
563
CB
GLN
191
45.831
56.475
12.715
1.00
61.86


ATOM
564
CG
GLN
191
46.995
57.198
13.327
1.00
60.94


ATOM
565
CD
GLN
191
46.670
57.707
14.698
1.00
63.14


ATOM
566
OE1
GLN
191
45.933
58.674
14.849
1.00
54.80


ATOM
567
NE2
GLN
191
47.211
57.055
15.713
1.00
66.82


ATOM
568
N
LEU
192
44.655
57.086
9.984
1.00
50.72


ATOM
569
CA
LEU
192
44.289
57.926
8.860
1.00
41.55


ATOM
570
C
LEU
192
44.159
59.371
9.315
1.00
50.00


ATOM
571
O
LEU
192
43.876
59.621
10.475
1.00
36.32


ATOM
572
CB
LEU
192
42.966
57.446
8.255
1.00
39.35


ATOM
573
CG
LEU
192
42.940
56.019
7.727
1.00
46.42


ATOM
574
CD1
LEU
192
41.593
55.684
7.117
1.00
41.02


ATOM
575
CD2
LEU
192
44.044
55.836
6.701
1.00
49.16


ATOM
576
N
TYR
193
44.386
60.307
8.394
1.00
41.05


ATOM
577
CA
TYR
193
44.156
61.731
8.618
1.00
41.75


ATOM
578
C
TYR
193
43.434
62.327
7.416
1.00
45.03


ATOM
579
O
TYR
193
43.612
61.860
6.290
1.00
56.48


ATOM
580
CB
TYR
193
45.482
62.471
8.851
1.00
46.33


ATOM
581
CG
TYR
193
46.279
61.953
10.022
1.00
52.84


ATOM
582
CD1
TYR
193
46.090
62.483
11.290
1.00
47.66


ATOM
583
CD2
TYR
193
47.222
60.925
9.863
1.00
49.49


ATOM
584
CE1
TYR
193
46.804
62.018
12.366
1.00
57.04


ATOM
585
CE2
TYR
193
47.944
60.452
10.941
1.00
51.34


ATOM
586
CZ
TYR
193
47.730
61.010
12.187
1.00
59.22


ATOM
587
OH
TYR
193
48.427
60.569
13.273
1.00
45.64


ATOM
588
N
GLY
194
42.625
63.357
7.649
1.00
47.68


ATOM
589
CA
GLY
194
41.953
64.039
6.563
1.00
45.00


ATOM
590
C
GLY
194
42.902
64.941
5.783
1.00
55.57


ATOM
591
O
GLY
194
42.802
65.059
4.562
1.00
73.94


ATOM
592
N
LEU
195
43.828
65.576
6.495
1.00
56.69


ATOM
593
CA
LEU
195
44.748
66.545
5.903
1.00
68.95


ATOM
594
C
LEU
195
46.190
66.203
6.238
1.00
68.24


ATOM
595
O
LEU
195
46.552
66.162
7.408
1.00
53.14


ATOM
596
CB
LEU
195
44.431
67.941
6.431
1.00
55.82


ATOM
597
CG
LEU
195
44.860
69.144
5.603
1.00
63.65


ATOM
598
CD1
LEU
195
44.173
70.395
6.124
1.00
53.17


ATOM
599
CD2
LEU
195
46.371
69.303
5.634
1.00
83.63


ATOM
600
N
LEU
196
47.000
65.960
5.208
1.00
49.64


ATOM
601
CA
LEU
196
48.437
65.714
5.370
1.00
47.59


ATOM
602
C
LEU
196
49.267
66.548
4.411
1.00
55.36


ATOM
603
O
LEU
196
48.957
66.624
3.222
1.00
59.50


ATOM
604
CB
LEU
196
48.768
64.246
5.111
1.00
47.54


ATOM
605
CG
LEU
196
48.082
63.238
6.027
1.00
58.31


ATOM
606
CD1
LEU
196
48.266
61.841
5.517
1.00
54.87


ATOM
607
CD2
LEU
196
48.630
63.386
7.419
1.00
37.88


ATOM
608
N
LYS
197
50.338
67.146
4.923
1.00
48.39


ATOM
609
CA
LYS
197
51.311
67.836
4.083
1.00
75.76


ATOM
610
C
LYS
197
52.429
66.865
3.703
1.00
71.25


ATOM
611
O
LYS
197
52.485
65.749
4.228
1.00
49.06


ATOM
612
CB
LYS
197
51.880
69.060
4.807
1.00
81.92


ATOM
613
CG
LYS
197
50.855
70.153
5.073
1.00
88.40


ATOM
614
CD
LYS
197
49.784
70.161
3.999
1.00
0.78


ATOM
615
CE
LYS
197
49.135
71.520
3.846
1.00
0.41


ATOM
616
NZ
LYS
197
49.905
72.367
2.897
1.00
0.26


ATOM
617
N
ARG
198
53.307
67.287
2.795
1.00
61.35


ATOM
618
CA
ARG
198
54.429
66.455
2.340
1.00
78.19


ATOM
619
C
ARG
198
55.195
65.744
3.462
1.00
75.65


ATOM
620
O
ARG
198
55.372
64.533
3.408
1.00
52.93


ATOM
621
CB
ARG
198
55.403
67.271
1.491
1.00
91.33


ATOM
622
CG
ARG
198
55.218
67.126
−0.001
1.00
0.83


ATOM
623
CD
ARG
198
56.126
68.092
−0.738
1.00
0.91


ATOM
624
NE
ARG
198
56.610
67.533
−1.995
1.00
0.29


ATOM
625
CZ
ARG
198
57.805
66.973
−2.152
1.00
0.90


ATOM
626
NH1
ARG
198
58.646
66.902
−1.128
1.00
0.09


ATOM
627
NH2
ARG
198
58.162
66.488
−3.334
1.00
0.42


ATOM
628
N
PRO
199
55.669
66.494
4.471
1.00
70.03


ATOM
629
CA
PRO
199
56.397
65.866
5.579
1.00
66.36


ATOM
630
C
PRO
199
55.541
64.867
6.351
1.00
71.38


ATOM
631
O
PRO
199
56.103
63.892
6.843
1.00
55.95


ATOM
632
CB
PRO
199
56.757
67.059
6.482
1.00
64.71


ATOM
633
CG
PRO
199
55.798
68.123
6.082
1.00
73.47


ATOM
634
CD
PRO
199
55.666
67.957
4.609
1.00
77.02


ATOM
635
N
ASP
200
54.227
65.115
6.456
1.00
60.82


ATOM
636
CA
ASP
200
53.290
64.211
7.142
1.00
63.99


ATOM
637
C
ASP
200
53.146
62.886
6.410
1.00
61.39


ATOM
638
O
ASP
200
53.208
61.814
7.003
1.00
53.71


ATOM
639
CB
ASP
200
51.899
64.838
7.228
1.00
50.68


ATOM
640
CG
ASP
200
51.852
66.035
8.145
1.00
70.50


ATOM
641
OD1
ASP
200
52.439
65.955
9.241
1.00
53.74


ATOM
642
OD2
ASP
200
51.215
67.045
7.773
1.00
75.96


ATOM
643
N
GLU
201
52.926
62.986
5.109
1.00
44.34


ATOM
644
CA
GLU
201
52.811
61.827
4.255
1.00
68.64


ATOM
645
C
GLU
201
54.094
61.003
4.267
1.00
64.75


ATOM
646
O
GLU
201
54.046
59.787
4.319
1.00
40.48


ATOM
647
CB
GLU
201
52.469
62.247
2.830
1.00
44.67


ATOM
648
CG
GLU
201
52.608
61.122
1.836
1.00
71.92


ATOM
649
CD
GLU
201
51.777
61.334
0.595
1.00
76.03


ATOM
650
OE1
GLU
201
51.495
62.494
0.255
1.00
87.45


ATOM
651
OE2
GLU
201
51.404
60.336
−0.043
1.00
64.60


ATOM
652
N
LYS
202
55.243
61.661
4.206
1.00
50.01


ATOM
653
CA
LYS
202
56.513
60.957
4.314
1.00
53.02


ATOM
654
C
LYS
202
56.564
60.157
5.628
1.00
42.78


ATOM
655
O
LYS
202
56.876
58.973
5.640
1.00
43.49


ATOM
656
CB
LYS
202
57.685
61.948
4.227
1.00
45.02


ATOM
657
CG
LYS
202
59.008
61.344
4.615
1.00
59.66


ATOM
658
CD
LYS
202
60.147
62.359
4.555
1.00
54.22


ATOM
659
CE
LYS
202
61.395
61.732
5.112
1.00
46.69


ATOM
660
NZ
LYS
202
62.492
62.730
5.135
1.00
0.21


ATOM
661
N
TYR
203
56.261
60.827
6.729
1.00
53.09


ATOM
662
CA
TYR
203
56.204
60.202
8.045
1.00
64.50


ATOM
663
C
TYR
203
55.245
59.002
8.106
1.00
61.81


ATOM
664
O
TYR
203
55.568
57.969
8.685
1.00
65.84


ATOM
665
CB
TYR
203
55.783
61.245
9.075
1.00
67.81


ATOM
666
CG
TYR
203
55.679
60.723
10.477
1.00
64.72


ATOM
667
CD1
TYR
203
56.748
60.819
11.345
1.00
52.12


ATOM
668
CD2
TYR
203
54.513
60.137
10.940
1.00
53.63


ATOM
669
CE1
TYR
203
56.664
60.356
12.633
1.00
60.02


ATOM
670
CE2
TYR
203
54.421
59.662
12.241
1.00
64.08


ATOM
671
CZ
TYR
203
55.506
59.781
13.079
1.00
69.98


ATOM
672
OH
TYR
203
55.444
59.316
14.365
1.00
69.48


ATOM
673
N
VAL
204
54.068
59.141
7.506
1.00
60.20


ATOM
674
CA
VAL
204
53.038
58.088
7.576
1.00
78.24


ATOM
675
C
VAL
204
53.422
56.850
6.723
1.00
47.17


ATOM
676
O
VAL
204
53.315
55.712
7.181
1.00
43.11


ATOM
677
CB
VAL
204
51.612
58.669
7.250
1.00
43.63


ATOM
678
CG1
VAL
204
51.277
58.534
5.775
1.00
47.36


ATOM
679
CG2
VAL
204
50.563
58.049
8.102
1.00
71.25


ATOM
680
N
THR
205
53.905
57.086
5.506
1.00
44.47


ATOM
681
CA
THR
205
54.461
56.047
4.633
1.00
52.60


ATOM
682
C
THR
205
55.540
55.208
5.338
1.00
57.12


ATOM
683
O
THR
205
55.508
53.963
5.330
1.00
41.28


ATOM
684
CB
THR
205
55.107
56.681
3.363
1.00
61.74


ATOM
685
OG1
THR
205
54.153
57.493
2.669
1.00
49.23


ATOM
686
CG2
THR
205
55.642
55.616
2.418
1.00
57.92


ATOM
687
N
GLU
206
56.501
55.905
5.939
1.00
51.43


ATOM
688
CA
GLU
206
57.652
55.270
6.587
1.00
49.67


ATOM
689
C
GLU
206
57.274
54.507
7.859
1.00
42.78


ATOM
690
O
GLU
206
57.708
53.380
8.056
1.00
46.60


ATOM
691
CB
GLU
206
58.753
56.312
6.872
1.00
32.43


ATOM
692
CG
GLU
206
59.406
56.840
5.608
1.00
67.25


ATOM
693
CD
GLU
206
60.333
58.014
5.874
1.00
94.44


ATOM
694
OE1
GLU
206
60.462
58.439
7.044
1.00
0.36


ATOM
695
OE2
GLU
206
60.933
58.514
4.904
1.00
89.69


ATOM
696
N
LYS
207
56.460
55.129
8.703
1.00
46.45


ATOM
697
CA
LYS
207
56.052
54.550
9.968
1.00
62.72


ATOM
698
C
LYS
207
55.270
53.262
9.746
1.00
63.15


ATOM
699
O
LYS
207
55.445
52.296
10.483
1.00
51.88


ATOM
700
CB
LYS
207
55.237
55.571
10.776
1.00
72.67


ATOM
701
CG
LYS
207
54.342
54.977
11.858
1.00
0.74


ATOM
702
CD
LYS
207
55.121
54.624
13.113
1.00
0.57


ATOM
703
CE
LYS
207
54.183
54.307
14.272
1.00
0.12


ATOM
704
NZ
LYS
207
54.926
54.061
15.540
1.00
0.37


ATOM
705
N
ALA
208
54.419
53.247
8.721
1.00
51.93


ATOM
706
CA
ALA
208
53.653
52.046
8.383
1.00
52.25


ATOM
707
C
ALA
208
54.595
50.951
7.896
1.00
57.98


ATOM
708
O
ALA
208
54.459
49.779
8.252
1.00
36.09


ATOM
709
CB
ALA
208
52.598
52.353
7.319
1.00
38.82


ATOM
710
N
TYR
209
55.565
51.343
7.077
1.00
52.31


ATOM
711
CA
TYR
209
56.567
50.407
6.594
1.00
56.68


ATOM
712
C
TYR
209
57.336
49.761
7.761
1.00
64.16


ATOM
713
O
TYR
209
57.634
48.581
7.726
1.00
52.26


ATOM
714
CB
TYR
209
57.510
51.099
5.615
1.00
51.72


ATOM
715
CG
TYR
209
58.410
50.162
4.833
1.00
63.67


ATOM
716
CD1
TYR
209
57.999
49.632
3.608
1.00
59.18


ATOM
717
CD2
TYR
209
59.667
49.813
5.309
1.00
67.39


ATOM
718
CE1
TYR
209
58.809
48.792
2.885
1.00
74.90


ATOM
719
CE2
TYR
209
60.490
48.966
4.586
1.00
55.98


ATOM
720
CZ
TYR
209
60.053
48.459
3.378
1.00
78.85


ATOM
721
OH
TYR
209
60.859
47.615
2.659
1.00
69.89


ATOM
722
N
GLU
210
57.623
50.527
8.806
1.00
59.87


ATOM
723
CA
GLU
210
58.365
50.004
9.952
1.00
55.94


ATOM
724
C
GLU
210
57.461
49.241
10.920
1.00
69.29


ATOM
725
O
GLU
210
57.948
48.571
11.819
1.00
56.02


ATOM
726
CB
GLU
210
59.066
51.136
10.702
1.00
55.80


ATOM
727
CG
GLU
210
59.989
51.979
9.849
1.00
71.30


ATOM
728
CD
GLU
210
60.235
53.368
10.426
1.00
87.58


ATOM
729
OE1
GLU
210
59.759
53.668
11.546
1.00
73.11


ATOM
730
OE2
GLU
210
60.903
54.171
9.748
1.00
93.13


ATOM
731
N
ASN
211
56.144
49.348
10.751
1.00
52.95


ATOM
732
CA
ASN
211
55.228
48.666
11.660
1.00
72.66


ATOM
733
C
ASN
211
54.204
47.800
10.915
1.00
72.42


ATOM
734
O
ASN
211
53.002
48.024
11.008
1.00
55.20


ATOM
735
CB
ASN
211
54.537
49.677
12.586
1.00
82.34


ATOM
736
CG
ASN
211
53.763
49.010
13.711
1.00
96.40


ATOM
737
OD1
ASN
211
54.164
47.965
14.228
1.00
0.40


ATOM
738
ND2
ASN
211
52.645
49.617
14.097
1.00
93.22


ATOM
739
N
PRO
212
54.685
46.797
10.171
1.00
55.52


ATOM
740
CA
PRO
212
53.771
45.938
9.417
1.00
50.78


ATOM
741
C
PRO
212
52.908
45.098
10.357
1.00
62.47


ATOM
742
O
PRO
212
53.390
44.658
11.396
1.00
43.99


ATOM
743
CB
PRO
212
54.717
45.020
8.633
1.00
44.67


ATOM
744
CG
PRO
212
56.099
45.617
8.786
1.00
53.75


ATOM
745
CD
PRO
212
56.078
46.322
10.087
1.00
52.24


ATOM
746
N
LYS
213
51.647
44.889
10.000
1.00
50.06


ATOM
747
CA
LYS
213
50.733
44.089
10.821
1.00
60.06


ATOM
748
C
LYS
213
49.698
43.345
9.986
1.00
37.78


ATOM
749
O
LYS
213
48.985
43.940
9.184
1.00
49.66


ATOM
750
CB
LYS
213
50.019
44.947
11.877
1.00
59.67


ATOM
751
CG
LYS
213
50.842
45.204
13.119
1.00
67.39


ATOM
752
CD
LYS
213
50.009
45.756
14.255
1.00
71.54


ATOM
753
CE
LYS
213
50.909
46.303
15.349
1.00
66.53


ATOM
754
NZ
LYS
213
50.180
46.690
16.586
1.00
54.59


ATOM
755
N
PHE
214
49.644
42.037
10.189
1.00
44.37


ATOM
756
CA
PHE
214
48.577
41.197
9.666
1.00
57.67


ATOM
757
C
PHE
214
47.257
41.532
10.339
1.00
50.58


ATOM
758
O
PHE
214
47.235
42.124
11.414
1.00
52.80


ATOM
759
CB
PHE
214
48.882
39.721
9.950
1.00
53.34


ATOM
760
CG
PHE
214
49.983
39.148
9.112
1.00
60.66


ATOM
761
CD1
PHE
214
49.924
39.198
7.730
1.00
75.57


ATOM
762
CD2
PHE
214
51.063
38.528
9.708
1.00
74.87


ATOM
763
CE1
PHE
214
50.932
38.660
6.959
1.00
68.54


ATOM
764
CE2
PHE
214
52.075
37.984
8.943
1.00
73.49


ATOM
765
CZ
PHE
214
52.009
38.051
7.565
1.00
65.16


ATOM
766
N
VAL
215
46.161
41.102
9.721
1.00
50.21


ATOM
767
CA
VAL
215
44.838
41.218
10.332
1.00
32.24


ATOM
768
C
VAL
215
44.760
40.429
11.663
1.00
39.63


ATOM
769
O
VAL
215
44.097
40.842
12.616
1.00
34.93


ATOM
770
CB
VAL
215
43.736
40.829
9.328
1.00
49.44


ATOM
771
CG1
VAL
215
43.564
39.327
9.245
1.00
40.48


ATOM
772
CG2
VAL
215
42.442
41.477
9.698
1.00
43.26


ATOM
773
N
GLU
216
45.483
39.315
11.741
1.00
31.87


ATOM
774
CA
GLU
216
45.604
38.551
12.985
1.00
37.07


ATOM
775
C
GLU
216
46.236
39.343
14.124
1.00
42.58


ATOM
776
O
GLU
216
45.774
39.286
15.267
1.00
37.19


ATOM
777
CB
GLU
216
46.392
37.253
12.760
1.00
37.27


ATOM
778
CG
GLU
216
45.753
36.309
11.734
1.00
55.63


ATOM
779
CD
GLU
216
46.293
36.491
10.315
1.00
64.24


ATOM
780
OE1
GLU
216
46.794
37.581
9.987
1.00
72.74


ATOM
781
OE2
GLU
216
46.212
35.541
9.514
1.00
72.11


ATOM
782
N
ASP
217
47.297
40.082
13.821
1.00
42.79


ATOM
783
CA
ASP
217
47.967
40.880
14.846
1.00
48.33


ATOM
784
C
ASP
217
47.118
42.054
15.292
1.00
43.56


ATOM
785
O
ASP
217
47.070
42.373
16.475
1.00
45.97


ATOM
786
CB
ASP
217
49.316
41.364
14.338
1.00
53.19


ATOM
787
CG
ASP
217
50.191
40.226
13.902
1.00
69.65


ATOM
788
OD1
ASP
217
50.265
39.231
14.662
1.00
73.54


ATOM
789
OD2
ASP
217
50.782
40.314
12.801
1.00
68.83


ATOM
790
N
MSE
218
46.443
42.682
14.336
1.00
37.35


ATOM
791
CA
MSE
218
45.542
43.788
14.634
1.00
39.78


ATOM
792
C
MSE
218
44.546
43.395
15.734
1.00
24.72


ATOM
793
O
MSE
218
44.499
44.012
16.796
1.00
29.59


ATOM
794
CB
MSE
218
44.810
44.241
13.362
1.00
58.79


ATOM
795
CG
MSE
218
44.073
45.573
13.480
1.00
77.38


ATOM
796
SE
MSE
218
45.130
46.991
14.337
1.00
0.47


ATOM
797
CE
MSE
218
44.023
48.546
13.914
1.00
0.92


ATOM
798
N
VAL
219
43.774
42.337
15.494
1.00
29.59


ATOM
799
CA
VAL
219
42.719
41.980
16.429
1.00
26.43


ATOM
800
C
VAL
219
43.272
41.489
17.751
1.00
27.62


ATOM
801
O
VAL
219
42.717
41.787
18.809
1.00
32.99


ATOM
802
CB
VAL
219
41.705
40.955
15.837
1.00
36.95


ATOM
803
CG1
VAL
219
41.063
41.525
14.612
1.00
35.83


ATOM
804
CG2
VAL
219
42.391
39.657
15.492
1.00
30.34


ATOM
805
N
ARG
220
44.362
40.734
17.691
1.00
30.45


ATOM
806
CA
ARG
220
45.024
40.300
18.917
1.00
43.29


ATOM
807
C
ARG
220
45.473
41.480
19.757
1.00
39.78


ATOM
808
O
ARG
220
45.241
41.506
20.961
1.00
49.09


ATOM
809
CB
ARG
220
46.204
39.392
18.606
1.00
37.68


ATOM
810
CG
ARG
220
45.787
37.957
18.434
1.00
41.30


ATOM
811
CD
ARG
220
46.922
37.107
17.877
1.00
37.85


ATOM
812
NE
ARG
220
46.562
35.704
18.004
1.00
44.94


ATOM
813
CZ
ARG
220
47.039
34.723
17.253
1.00
47.83


ATOM
814
NH1
ARG
220
47.911
34.976
16.293
1.00
39.44


ATOM
815
NH2
ARG
220
46.630
33.483
17.468
1.00
46.76


ATOM
816
N
ASP
221
46.091
42.466
19.116
1.00
30.84


ATOM
817
CA
ASP
221
46.593
43.628
19.863
1.00
39.37


ATOM
818
C
ASP
221
45.487
44.506
20.456
1.00
39.67


ATOM
819
O
ASP
221
45.582
44.958
21.584
1.00
44.32


ATOM
820
CB
ASP
221
47.527
44.451
18.990
1.00
50.33


ATOM
821
CG
ASP
221
48.803
43.695
18.628
1.00
76.67


ATOM
822
OD1
ASP
221
49.064
42.623
19.227
1.00
84.23


ATOM
823
OD2
ASP
221
49.549
44.170
17.741
1.00
61.34


ATOM
824
N
VAL
222
44.411
44.721
19.707
1.00
35.67


ATOM
825
CA
VAL
222
43.286
45.490
20.242
1.00
37.76


ATOM
826
C
VAL
222
42.568
44.737
21.366
1.00
32.07


ATOM
827
O
VAL
222
42.181
45.332
22.366
1.00
38.73


ATOM
828
CB
VAL
222
42.265
45.817
19.163
1.00
30.54


ATOM
829
CG1
VAL
222
41.055
46.485
19.798
1.00
34.98


ATOM
830
CG2
VAL
222
42.880
46.682
18.116
1.00
31.33


ATOM
831
N
ALA
223
42.408
43.424
21.189
1.00
27.50


ATOM
832
CA
ALA
223
41.684
42.595
22.152
1.00
38.49


ATOM
833
C
ALA
223
42.393
42.585
23.496
1.00
41.28


ATOM
834
O
ALA
223
41.755
42.586
24.540
1.00
35.49


ATOM
835
CB
ALA
223
41.531
41.189
21.634
1.00
32.48


ATOM
836
N
THR
224
43.722
42.571
23.457
1.00
38.65


ATOM
837
CA
THR
224
44.515
42.572
24.679
1.00
41.10


ATOM
838
C
THR
224
44.251
43.847
25.487
1.00
40.22


ATOM
839
O
THR
224
44.079
43.801
26.702
1.00
44.23


ATOM
840
CB
THR
224
45.997
42.444
24.361
1.00
34.72


ATOM
841
OG1
THR
224
46.230
41.196
23.701
1.00
47.19


ATOM
842
CG2
THR
224
46.809
42.504
25.634
1.00
51.18


ATOM
843
N
SER
225
44.206
44.985
24.803
1.00
35.60


ATOM
844
CA
SER
225
43.861
46.250
25.456
1.00
47.00


ATOM
845
C
SER
225
42.478
46.229
26.070
1.00
45.84


ATOM
846
O
SER
225
42.288
46.755
27.161
1.00
42.17


ATOM
847
CB
SER
225
43.921
47.413
24.479
1.00
42.92


ATOM
848
OG
SER
225
45.122
47.392
23.754
1.00
48.51


ATOM
849
N
LEU
226
41.518
45.629
25.370
1.00
37.09


ATOM
850
CA
LEU
226
40.133
45.605
25.853
1.00
36.24


ATOM
851
C
LEU
226
40.008
44.659
27.036
1.00
37.89


ATOM
852
O
LEU
226
39.325
44.973
28.006
1.00
43.78


ATOM
853
CB
LEU
226
39.165
45.210
24.729
1.00
34.97


ATOM
854
CG
LEU
226
39.134
46.090
23.479
1.00
33.84


ATOM
855
CD1
LEU
226
38.220
45.489
22.430
1.00
50.41


ATOM
856
CD2
LEU
226
38.715
47.542
23.789
1.00
39.51


ATOM
857
N
ILE
227
40.697
43.517
26.953
1.00
36.57


ATOM
858
CA
ILE
227
40.717
42.519
28.015
1.00
45.24


ATOM
859
C
ILE
227
41.250
43.119
29.305
1.00
47.23


ATOM
860
O
ILE
227
40.767
42.806
30.391
1.00
49.27


ATOM
861
CB
ILE
227
41.584
41.309
27.644
1.00
47.34


ATOM
862
CG1
ILE
227
40.827
40.398
26.683
1.00
43.33


ATOM
863
CG2
ILE
227
42.004
40.532
28.913
1.00
38.95


ATOM
864
CD1
ILE
227
41.690
39.392
26.055
1.00
47.18


ATOM
865
N
ALA
228
42.242
43.995
29.169
1.00
33.22


ATOM
866
CA
ALA
228
42.793
44.696
30.316
1.00
51.83


ATOM
867
C
ALA
228
41.791
45.649
30.994
1.00
62.10


ATOM
868
O
ALA
228
41.712
45.706
32.215
1.00
60.35


ATOM
869
CB
ALA
228
44.061
45.427
29.931
1.00
49.81


ATOM
870
N
ASP
229
41.017
46.383
30.207
1.00
48.90


ATOM
871
CA
ASP
229
40.031
47.312
30.765
1.00
44.21


ATOM
872
C
ASP
229
38.912
46.607
31.570
1.00
52.96


ATOM
873
O
ASP
229
38.167
45.795
31.024
1.00
56.32


ATOM
874
CB
ASP
229
39.422
48.142
29.638
1.00
63.61


ATOM
875
CG
ASP
229
38.777
49.411
30.137
1.00
71.21


ATOM
876
OD1
ASP
229
37.992
49.364
31.117
1.00
54.93


ATOM
877
OD2
ASP
229
39.065
50.462
29.541
1.00
59.40


ATOM
878
N
LYS
230
38.797
46.931
32.858
1.00
59.01


ATOM
879
CA
LYS
230
37.898
46.203
33.757
1.00
60.43


ATOM
880
C
LYS
230
36.423
46.579
33.583
1.00
51.76


ATOM
881
O
LYS
230
35.540
45.878
34.083
1.00
60.37


ATOM
882
CB
LYS
230
38.306
46.402
35.220
1.00
66.12


ATOM
883
CG
LYS
230
39.779
46.128
35.521
1.00
90.89


ATOM
884
CD
LYS
230
40.171
44.685
35.229
1.00
94.28


ATOM
885
CE
LYS
230
41.592
44.381
35.704
1.00
89.21


ATOM
886
NZ
LYS
230
42.710
44.902
34.842
1.00
72.91


ATOM
887
N
ASN
241
40.511
43.782
6.157
1.00
35.37


ATOM
888
CA
ASN
241
41.557
44.396
5.336
1.00
35.84


ATOM
889
C
ASN
241
41.181
44.360
3.868
1.00
44.30


ATOM
890
O
ASN
241
41.131
43.285
3.277
1.00
35.87


ATOM
891
CB
ASN
241
42.846
43.596
5.458
1.00
59.50


ATOM
892
CG
ASN
241
43.834
44.211
6.385
1.00
74.07


ATOM
893
OD1
ASN
241
45.033
44.132
6.144
1.00
83.92


ATOM
894
ND2
ASN
241
43.353
44.817
7.461
1.00
73.43


ATOM
895
N
PHE
242
40.947
45.512
3.261
1.00
34.18


ATOM
896
CA
PHE
242
40.648
45.561
1.835
1.00
54.06


ATOM
897
C
PHE
242
41.932
45.486
1.029
1.00
43.36


ATOM
898
O
PHE
242
42.298
46.430
0.319
1.00
42.57


ATOM
899
CB
PHE
242
39.837
46.812
1.491
1.00
49.71


ATOM
900
CG
PHE
242
38.579
46.943
2.307
1.00
54.48


ATOM
901
CD1
PHE
242
37.400
46.327
1.899
1.00
48.92


ATOM
902
CD2
PHE
242
38.587
47.658
3.500
1.00
50.08


ATOM
903
CE1
PHE
242
36.249
46.426
2.662
1.00
44.33


ATOM
904
CE2
PHE
242
37.446
47.768
4.265
1.00
56.26


ATOM
905
CZ
PHE
242
36.269
47.147
3.847
1.00
48.67


ATOM
906
N
GLU
243
42.603
44.341
1.149
1.00
43.70


ATOM
907
CA
GLU
243
43.938
44.146
0.598
1.00
53.80


ATOM
908
C
GLU
243
44.041
44.634
−0.836
1.00
54.72


ATOM
909
O
GLU
243
43.155
44.399
−1.662
1.00
36.12


ATOM
910
CB
GLU
243
44.409
42.691
0.753
1.00
62.42


ATOM
911
CG
GLU
243
43.409
41.659
0.338
1.00
98.18


ATOM
912
CD
GLU
243
43.956
40.259
0.486
1.00
0.38


ATOM
913
OE1
GLU
243
43.160
39.296
0.471
1.00
0.85


ATOM
914
OE2
GLU
243
45.189
40.123
0.625
1.00
0.45


ATOM
915
N
SER
244
45.126
45.345
−1.110
1.00
48.15


ATOM
916
CA
SER
244
45.254
46.091
−2.349
1.00
48.27


ATOM
917
C
SER
244
45.764
45.216
−3.487
1.00
43.29


ATOM
918
O
SER
244
45.999
45.711
−4.582
1.00
54.30


ATOM
919
CB
SER
244
46.178
47.290
−2.154
1.00
50.70


ATOM
920
OG
SER
244
47.495
46.834
−1.924
1.00
57.31


ATOM
921
N
ILE
245
45.938
43.921
−3.225
1.00
38.50


ATOM
922
CA
ILE
245
46.367
42.985
−4.273
1.00
54.46


ATOM
923
C
ILE
245
45.290
41.961
−4.654
1.00
49.60


ATOM
924
O
ILE
245
45.474
41.190
−5.595
1.00
39.53


ATOM
925
CB
ILE
245
47.658
42.234
−3.879
1.00
54.37


ATOM
926
CG1
ILE
245
47.401
41.334
−2.669
1.00
54.44


ATOM
927
CG2
ILE
245
48.758
43.216
−3.577
1.00
37.95


ATOM
928
CD1
ILE
245
48.629
40.583
−2.192
1.00
73.40


ATOM
929
N
HIS
246
44.188
41.940
−3.908
1.00
43.91


ATOM
930
CA
HIS
246
43.058
41.050
−4.206
1.00
49.94


ATOM
931
C
HIS
246
41.770
41.862
−4.355
1.00
57.65


ATOM
932
O
HIS
246
41.754
43.043
−4.058
1.00
47.46


ATOM
933
CB
HIS
246
42.893
40.005
−3.104
1.00
40.63


ATOM
934
CG
HIS
246
44.038
39.038
−3.001
1.00
63.27


ATOM
935
ND1
HIS
246
44.749
38.845
−1.831
1.00
58.15


ATOM
936
CD2
HIS
246
44.585
38.202
−3.912
1.00
61.44


ATOM
937
CE1
HIS
246
45.683
37.933
−2.032
1.00
69.99


ATOM
938
NE2
HIS
246
45.609
37.532
−3.288
1.00
70.61


ATOM
939
N
ASN
247
40.699
41.241
−4.831
1.00
45.02


ATOM
940
CA
ASN
247
39.407
41.904
−4.820
1.00
41.42


ATOM
941
C
ASN
247
38.445
41.358
−3.747
1.00
46.46


ATOM
942
O
ASN
247
37.230
41.355
−3.930
1.00
59.35


ATOM
943
CB
ASN
247
38.748
41.892
−6.206
1.00
48.65


ATOM
944
CG
ASN
247
37.673
42.965
−6.343
1.00
49.46


ATOM
945
OD1
ASN
247
37.815
44.041
−5.800
1.00
34.71


ATOM
946
ND2
ASN
247
36.602
42.670
−7.065
1.00
32.52


TER











ATOM
947
ZN
ZN2 B
258
50.203
40.407
1.793
1.00
35.76


ATOM
948
C
ACY B
259
47.704
37.868
1.932
1.00
65.42


ATOM
949
O
ACY B
259
47.758
37.530
3.162
1.00
54.29


ATOM
950
OXT
ACY B
259
48.249
38.912
1.482
1.00
52.67


ATOM
951
CH3
ACY B
259
46.973
37.009
0.925
1.00
47.10


TER











ATOM
952
N
ARG
14
50.990
63.026
−26.073
1.00
56.18


ATOM
953
CA
ARG
14
50.011
64.106
−25.960
1.00
93.83


ATOM
954
C
ARG
14
49.059
63.972
−24.779
1.00
0.95


ATOM
955
O
ARG
14
48.591
62.882
−24.432
1.00
0.99


ATOM
956
CB
ARG
14
49.303
64.396
−27.281
1.00
91.72


ATOM
957
CG
ARG
14
49.942
65.578
−27.967
1.00
98.01


ATOM
958
CD
ARG
14
51.285
65.865
−27.304
1.00
0.59


ATOM
959
NE
ARG
14
51.414
67.252
−26.865
1.00
0.30


ATOM
960
CZ
ARG
14
52.447
67.718
−26.171
1.00
0.57


ATOM
961
NH1
ARG
14
53.439
66.901
−25.833
1.00
0.47


ATOM
962
NH2
ARG
14
52.489
68.998
−25.814
1.00
0.76


ATOM
963
N
ASN
15
48.763
65.135
−24.216
1.00
0.82


ATOM
964
CA
ASN
15
48.731
65.331
−22.775
1.00
0.69


ATOM
965
C
ASN
15
47.386
65.418
−22.064
1.00
0.82


ATOM
966
O
ASN
15
47.347
65.506
−20.840
1.00
0.58


ATOM
967
CB
ASN
15
49.542
66.580
−22.446
1.00
0.43


ATOM
968
CG
ASN
15
50.905
66.253
−21.890
1.00
0.83


ATOM
969
OD1
ASN
15
51.045
65.363
−21.057
1.00
0.77


ATOM
970
ND2
ASN
15
51.914
66.982
−22.326
1.00
0.18


ATOM
971
N
LEU
16
46.303
65.428
−22.829
1.00
93.09


ATOM
972
CA
LEU
16
44.939
65.355
−22.298
1.00
61.91


ATOM
973
C
LEU
16
44.622
66.125
−21.008
1.00
56.02


ATOM
974
O
LEU
16
45.138
65.822
−19.932
1.00
38.84


ATOM
975
CB
LEU
16
44.489
63.904
−22.186
1.00
59.10


ATOM
976
CG
LEU
16
43.830
63.302
−23.430
1.00
70.01


ATOM
977
CD1
LEU
16
44.738
63.432
−24.627
1.00
95.51


ATOM
978
CD2
LEU
16
43.495
61.845
−23.180
1.00
64.01


ATOM
979
N
PRO
17
43.757
67.140
−21.121
1.00
46.50


ATOM
980
CA
PRO
17
43.251
67.811
−19.919
1.00
51.15


ATOM
981
C
PRO
17
42.355
66.835
−19.159
1.00
50.11


ATOM
982
O
PRO
17
41.764
65.948
−19.781
1.00
53.59


ATOM
983
CB
PRO
17
42.371
68.932
−20.477
1.00
48.36


ATOM
984
CG
PRO
17
42.657
69.003
−21.920
1.00
47.75


ATOM
985
CD
PRO
17
43.193
67.696
−22.362
1.00
35.50


ATOM
986
N
ILE
18
42.269
66.982
−17.840
1.00
37.05


ATOM
987
CA
ILE
18
41.329
66.200
−17.045
1.00
44.06


ATOM
988
C
ILE
18
40.165
67.108
−16.623
1.00
37.56


ATOM
989
O
ILE
18
40.365
68.140
−15.989
1.00
33.36


ATOM
990
CB
ILE
18
42.022
65.555
−15.835
1.00
40.66


ATOM
991
CG1
ILE
18
43.083
64.544
−16.310
1.00
47.12


ATOM
992
CG2
ILE
18
41.009
64.864
−14.932
1.00
45.97


ATOM
993
CD1
ILE
18
44.084
64.145
−15.235
1.00
36.80


ATOM
994
N
ASN
19
38.963
66.745
−17.035
1.00
32.51


ATOM
995
CA
ASN
19
37.764
67.513
−16.705
1.00
35.21


ATOM
996
C
ASN
19
37.639
67.863
−15.230
1.00
40.29


ATOM
997
O
ASN
19
37.423
69.016
−14.893
1.00
34.49


ATOM
998
CB
ASN
19
36.511
66.771
−17.157
1.00
47.76


ATOM
999
CG
ASN
19
36.476
66.555
−18.648
1.00
51.75


ATOM
1000
OD1
ASN
19
35.652
67.140
−19.335
1.00
61.29


ATOM
1001
ND2
ASN
19
37.372
65.715
−19.160
1.00
31.66


ATOM
1002
N
GLN
20
37.795
66.879
−14.348
1.00
36.73


ATOM
1003
CA
GLN
20
37.707
67.140
−12.919
1.00
33.67


ATOM
1004
C
GLN
20
38.670
66.226
−12.183
1.00
35.95


ATOM
1005
O
GLN
20
38.703
65.023
−12.421
1.00
30.38


ATOM
1006
CB
GLN
20
36.272
66.916
−12.376
1.00
35.50


ATOM
1007
CG
GLN
20
35.140
67.729
−13.030
1.00
36.99


ATOM
1008
CD
GLN
20
35.230
69.213
−12.750
1.00
47.86


ATOM
1009
OE1
GLN
20
35.841
69.622
−11.771
1.00
44.72


ATOM
1010
NE2
GLN
20
34.636
70.029
−13.622
1.00
48.95


ATOM
1011
N
VAL
21
39.437
66.796
−11.267
1.00
30.12


ATOM
1012
CA
VAL
21
40.238
65.974
−10.397
1.00
34.50


ATOM
1013
C
VAL
21
40.183
66.600
−9.031
1.00
38.21


ATOM
1014
O
VAL
21
40.161
67.827
−8.905
1.00
43.19


ATOM
1015
CB
VAL
21
41.699
65.873
−10.883
1.00
38.43


ATOM
1016
CG1
VAL
21
42.278
67.249
−11.082
1.00
32.73


ATOM
1017
CG2
VAL
21
42.535
65.141
−9.876
1.00
35.82


ATOM
1018
N
GLY
22
40.160
65.758
−8.010
1.00
28.80


ATOM
1019
CA
GLY
22
40.140
66.202
−6.630
1.00
28.65


ATOM
1020
C
GLY
22
39.756
65.068
−5.713
1.00
41.36


ATOM
1021
O
GLY
22
40.296
63.954
−5.820
1.00
37.38


ATOM
1022
N
ILE
23
38.813
65.339
−4.822
1.00
28.55


ATOM
1023
CA
ILE
23
38.422
64.370
−3.802
1.00
30.09


ATOM
1024
C
ILE
23
36.941
64.073
−3.808
1.00
32.04


ATOM
1025
O
ILE
23
36.112
64.890
−4.211
1.00
34.87


ATOM
1026
CB
ILE
23
38.819
64.839
−2.378
1.00
28.66


ATOM
1027
CG1
ILE
23
38.014
66.074
−1.975
1.00
30.62


ATOM
1028
CG2
ILE
23
40.303
65.120
−2.308
1.00
40.70


ATOM
1029
CD1
ILE
23
38.023
66.347
−0.511
1.00
43.09


ATOM
1030
N
THR
48
36.389
69.073
−6.903
1.00
24.29


ATOM
1031
CA
THR
48
37.274
68.785
−8.006
1.00
31.42


ATOM
1032
C
THR
48
37.590
70.085
−8.785
1.00
41.99


ATOM
1033
O
THR
48
36.853
71.081
−8.699
1.00
34.59


ATOM
1034
CB
THR
48
36.617
67.751
−8.950
1.00
43.46


ATOM
1035
OG1
THR
48
35.426
68.302
−9.502
1.00
43.17


ATOM
1036
CG2
THR
48
36.281
66.445
−8.216
1.00
41.57


ATOM
1037
N
VAL
49
38.683
70.085
−9.537
1.00
34.12


ATOM
1038
CA
VAL
49
38.973
71.194
−10.463
1.00
29.96


ATOM
1039
C
VAL
49
39.461
70.666
−11.801
1.00
39.64


ATOM
1040
O
VAL
49
39.885
69.522
−11.914
1.00
34.16


ATOM
1041
CB
VAL
49
40.050
72.148
−9.917
1.00
28.70


ATOM
1042
CG1
VAL
49
39.613
72.760
−8.609
1.00
34.65


ATOM
1043
CG2
VAL
49
41.401
71.413
−9.736
1.00
34.78


ATOM
1044
N
TYR
50
39.410
71.515
−12.811
1.00
35.35


ATOM
1045
CA
TYR
50
39.965
71.222
−14.128
1.00
36.36


ATOM
1046
C
TYR
50
41.498
71.212
−14.090
1.00
30.60


ATOM
1047
O
TYR
50
42.117
72.076
−13.476
1.00
48.28


ATOM
1048
CB
TYR
50
39.477
72.281
−15.104
1.00
43.69


ATOM
1049
CG
TYR
50
40.034
72.207
−16.498
1.00
44.11


ATOM
1050
CD1
TYR
50
39.424
71.435
−17.459
1.00
35.06


ATOM
1051
CD2
TYR
50
41.138
72.972
−16.871
1.00
47.58


ATOM
1052
CE1
TYR
50
39.915
71.378
−18.761
1.00
48.54


ATOM
1053
CE2
TYR
50
41.642
72.926
−18.166
1.00
60.18


ATOM
1054
CZ
TYR
50
41.024
72.130
−19.108
1.00
64.39


ATOM
1055
OH
TYR
50
41.514
72.087
−20.393
1.00
57.90


ATOM
1056
N
LEU
51
42.102
70.199
−14.708
1.00
39.41


ATOM
1057
CA
LEU
51
43.542
70.100
−14.783
1.00
40.03


ATOM
1058
C
LEU
51
43.945
70.242
−16.241
1.00
49.59


ATOM
1059
O
LEU
51
43.620
69.399
−17.048
1.00
35.47


ATOM
1060
CB
LEU
51
44.031
68.768
−14.227
1.00
43.30


ATOM
1061
CG
LEU
51
45.544
68.699
−14.050
1.00
47.56


ATOM
1062
CD1
LEU
51
45.938
69.662
−12.934
1.00
46.53


ATOM
1063
CD2
LEU
51
46.047
67.274
−13.741
1.00
36.00


ATOM
1064
N
PRO
52
44.626
71.342
−16.581
1.00
47.01


ATOM
1065
CA
PRO
52
45.190
71.635
−17.906
1.00
54.47


ATOM
1066
C
PRO
52
46.064
70.493
−18.441
1.00
47.94


ATOM
1067
O
PRO
52
46.671
69.776
−17.665
1.00
42.41


ATOM
1068
CB
PRO
52
46.074
72.856
−17.643
1.00
45.04


ATOM
1069
CG
PRO
52
45.583
73.453
−16.384
1.00
58.50


ATOM
1070
CD
PRO
52
45.024
72.331
−15.569
1.00
44.63


ATOM
1071
N
ALA
53
46.140
70.353
−19.754
1.00
48.98


ATOM
1072
CA
ALA
53
46.895
69.266
−20.372
1.00
58.53


ATOM
1073
C
ALA
53
48.293
69.022
−19.809
1.00
62.49


ATOM
1074
O
ALA
53
48.705
67.877
−19.618
1.00
65.81


ATOM
1075
CB
ALA
53
46.968
69.474
−21.866
1.00
53.72


ATOM
1076
N
GLU
54
49.045
70.085
−19.556
1.00
72.43


ATOM
1077
CA
GLU
54
50.444
69.865
−19.208
1.00
0.41


ATOM
1078
C
GLU
54
50.782
70.071
−17.740
1.00
90.42


ATOM
1079
O
GLU
54
51.950
70.124
−17.369
1.00
95.32


ATOM
1080
CB
GLU
54
51.388
70.649
−20.125
1.00
0.46


ATOM
1081
CG
GLU
54
51.661
72.076
−19.713
1.00
0.78


ATOM
1082
CD
GLU
54
52.565
72.782
−20.707
1.00
0.22


ATOM
1083
OE1
GLU
54
52.165
72.905
−21.885
1.00
0.86


ATOM
1084
OE2
GLU
54
53.675
73.211
−20.317
1.00
0.17


ATOM
1085
N
GLN
55
49.757
70.169
−16.905
1.00
74.01


ATOM
1086
CA
GLN
55
49.960
70.086
−15.468
1.00
65.50


ATOM
1087
C
GLN
55
49.842
68.608
−15.100
1.00
60.70


ATOM
1088
O
GLN
55
48.917
67.942
−15.541
1.00
63.86


ATOM
1089
CB
GLN
55
48.915
70.929
−14.736
1.00
64.04


ATOM
1090
CG
GLN
55
49.232
71.214
−13.274
1.00
67.10


ATOM
1091
CD
GLN
55
48.245
72.189
−12.656
1.00
78.01


ATOM
1092
OE1
GLN
55
47.694
73.048
−13.344
1.00
86.83


ATOM
1093
NE2
GLN
55
48.020
72.061
−11.349
1.00
66.25


ATOM
1094
N
LYS
56
50.785
68.094
−14.316
1.00
58.08


ATOM
1095
CA
LYS
56
50.833
66.662
−14.040
1.00
68.32


ATOM
1096
C
LYS
56
49.826
66.244
−12.981
1.00
68.10


ATOM
1097
O
LYS
56
49.327
65.123
−13.007
1.00
70.15


ATOM
1098
CB
LYS
56
52.240
66.228
−13.606
1.00
86.98


ATOM
1099
CG
LYS
56
52.324
64.763
−13.177
1.00
0.17


ATOM
1100
CD
LYS
56
53.736
64.357
−12.796
1.00
0.61


ATOM
1101
CE
LYS
56
54.133
64.922
−11.443
1.00
0.08


ATOM
1102
NZ
LYS
56
55.504
64.490
−11.051
1.00
0.69


ATOM
1103
N
GLY
57
49.550
67.149
−12.044
1.00
53.87


ATOM
1104
CA
GLY
57
48.726
66.829
−10.893
1.00
62.82


ATOM
1105
C
GLY
57
48.122
68.053
−10.237
1.00
69.86


ATOM
1106
O
GLY
57
48.528
69.177
−10.513
1.00
61.08


ATOM
1107
N
THR
58
47.134
67.835
−9.376
1.00
69.78


ATOM
1108
CA
THR
58
46.546
68.916
−8.602
1.00
71.47


ATOM
1109
C
THR
58
47.141
68.858
−7.205
1.00
55.97


ATOM
1110
O
THR
58
48.036
68.047
−6.951
1.00
59.93


ATOM
1111
CB
THR
58
44.996
68.800
−8.551
1.00
71.04


ATOM
1112
OG1
THR
58
44.438
70.031
−8.090
1.00
77.37


ATOM
1113
CG2
THR
58
44.553
67.657
−7.635
1.00
65.11


ATOM
1114
N
HIS
59
46.646
69.694
−6.297
1.00
58.22


ATOM
1115
CA
HIS
59
47.133
69.677
−4.921
1.00
64.81


ATOM
1116
C
HIS
59
46.042
69.180
−3.982
1.00
61.25


ATOM
1117
O
HIS
59
45.196
69.954
−3.553
1.00
68.43


ATOM
1118
CB
HIS
59
47.617
71.072
−4.529
1.00
66.44


ATOM
1119
CG
HIS
59
48.517
71.694
−5.553
1.00
72.69


ATOM
1120
ND1
HIS
59
48.032
72.385
−6.639
1.00
76.25


ATOM
1121
CD2
HIS
59
49.864
71.693
−5.667
1.00
76.00


ATOM
1122
CE1
HIS
59
49.048
72.802
−7.377
1.00
85.64


ATOM
1123
NE2
HIS
59
50.168
72.399
−6.811
1.00
86.98


ATOM
1124
N
MSE
60
46.076
67.889
−3.661
1.00
65.09


ATOM
1125
CA
MSE
60
44.944
67.208
−3.033
1.00
58.00


ATOM
1126
C
MSE
60
44.570
67.726
−1.654
1.00
50.50


ATOM
1127
O
MSE
60
43.381
67.791
−1.314
1.00
53.78


ATOM
1128
CB
MSE
60
45.194
65.700
−2.971
1.00
62.77


ATOM
1129
CG
MSE
60
45.200
65.021
−4.331
1.00
87.09


ATOM
1130
SE
MSE
60
43.419
64.899
−5.187
1.00
78.03


ATOM
1131
CE
MSE
60
43.904
63.860
−6.770
1.00
92.20


ATOM
1132
N
SER
61
45.581
68.100
−0.870
1.00
45.42


ATOM
1133
CA
SER
61
45.372
68.547
0.512
1.00
47.54


ATOM
1134
C
SER
61
44.668
69.900
0.647
1.00
55.39


ATOM
1135
O
SER
61
44.049
70.185
1.677
1.00
61.05


ATOM
1136
CB
SER
61
46.682
68.542
1.310
1.00
57.85


ATOM
1137
OG
SER
61
47.430
69.713
1.078
1.00
61.24


ATOM
1138
N
ARG
62
44.750
70.732
−0.383
1.00
50.58


ATOM
1139
CA
ARG
62
44.031
72.012
−0.363
1.00
51.01


ATOM
1140
C
ARG
62
42.498
71.881
−0.275
1.00
41.04


ATOM
1141
O
ARG
62
41.844
72.680
0.363
1.00
44.23


ATOM
1142
CB
ARG
62
44.429
72.859
−1.569
1.00
50.03


ATOM
1143
CG
ARG
62
45.869
73.360
−1.485
1.00
50.73


ATOM
1144
CD
ARG
62
46.291
74.061
−2.754
1.00
47.50


ATOM
1145
NE
ARG
62
47.747
74.194
−2.827
1.00
72.17


ATOM
1146
CZ
ARG
62
48.391
74.855
−3.779
1.00
68.28


ATOM
1147
NH1
ARG
62
47.707
75.454
−4.742
1.00
59.95


ATOM
1148
NH2
ARG
62
49.714
74.916
−3.768
1.00
79.31


ATOM
1149
N
PHE
63
41.940
70.864
−0.917
1.00
41.97


ATOM
1150
CA
PHE
63
40.503
70.623
−0.879
1.00
44.58


ATOM
1151
C
PHE
63
40.028
70.483
0.557
1.00
49.40


ATOM
1152
O
PHE
63
39.061
71.123
0.957
1.00
39.22


ATOM
1153
CB
PHE
63
40.142
69.371
−1.655
1.00
40.89


ATOM
1154
CG
PHE
63
40.396
69.475
−3.121
1.00
28.93


ATOM
1155
CD1
PHE
63
39.581
70.260
−3.914
1.00
38.88


ATOM
1156
CD2
PHE
63
41.431
68.774
−3.706
1.00
35.68


ATOM
1157
CE1
PHE
63
39.790
70.345
−5.262
1.00
36.00


ATOM
1158
CE2
PHE
63
41.649
68.846
−5.051
1.00
44.36


ATOM
1159
CZ
PHE
63
40.829
69.622
−5.838
1.00
30.89


ATOM
1160
N
VAL
64
40.732
69.655
1.321
1.00
38.51


ATOM
1161
CA
VAL
64
40.438
69.431
2.723
1.00
36.46


ATOM
1162
C
VAL
64
40.702
70.690
3.547
1.00
44.40


ATOM
1163
O
VAL
64
39.850
71.084
4.335
1.00
40.10


ATOM
1164
CB
VAL
64
41.266
68.289
3.305
1.00
54.00


ATOM
1165
CG1
VAL
64
40.964
68.118
4.766
1.00
60.44


ATOM
1166
CG2
VAL
64
40.994
67.015
2.546
1.00
63.75


ATOM
1167
N
ALA
65
41.881
71.300
3.386
1.00
31.61


ATOM
1168
CA
ALA
65
42.210
72.537
4.104
1.00
46.10


ATOM
1169
C
ALA
65
41.122
73.593
3.901
1.00
50.34


ATOM
1170
O
ALA
65
40.794
74.334
4.815
1.00
45.89


ATOM
1171
CB
ALA
65
43.597
73.105
3.664
1.00
43.69


ATOM
1172
N
LEU
66
40.574
73.650
2.691
1.00
43.19


ATOM
1173
CA
LEU
66
39.556
74.640
2.360
1.00
41.61


ATOM
1174
C
LEU
66
38.341
74.405
3.250
1.00
55.17


ATOM
1175
O
LEU
66
37.801
75.328
3.841
1.00
52.31


ATOM
1176
CB
LEU
66
39.194
74.538
0.883
1.00
58.42


ATOM
1177
CG
LEU
66
38.117
75.513
0.426
1.00
64.87


ATOM
1178
CD1
LEU
66
38.717
76.886
0.319
1.00
65.34


ATOM
1179
CD2
LEU
66
37.506
75.098
−0.901
1.00
68.63


ATOM
1180
N
MSE
67
37.948
73.147
3.386
1.00
52.78


ATOM
1181
CA
MSE
67
36.836
72.771
4.261
1.00
43.01


ATOM
1182
C
MSE
67
37.085
73.021
5.746
1.00
48.38


ATOM
1183
O
MSE
67
36.207
73.512
6.447
1.00
45.66


ATOM
1184
CB
MSE
67
36.457
71.301
4.053
1.00
47.95


ATOM
1185
CG
MSE
67
35.691
71.069
2.776
1.00
70.03


ATOM
1186
SE
MSE
67
34.340
72.453
2.495
1.00
0.69


ATOM
1187
CE
MSE
67
33.466
71.739
0.906
1.00
0.86


ATOM
1188
N
GLU
68
38.267
72.661
6.231
1.00
40.76


ATOM
1189
CA
GLU
68
38.577
72.843
7.641
1.00
48.85


ATOM
1190
C
GLU
68
38.543
74.316
8.043
1.00
60.66


ATOM
1191
O
GLU
68
38.178
74.657
9.173
1.00
58.50


ATOM
1192
CB
GLU
68
39.937
72.238
7.979
1.00
54.20


ATOM
1193
CG
GLU
68
40.048
70.756
7.675
1.00
71.81


ATOM
1194
CD
GLU
68
39.261
69.901
8.646
1.00
93.47


ATOM
1195
OE1
GLU
68
38.577
70.470
9.522
1.00
92.19


ATOM
1196
OE2
GLU
68
39.323
68.658
8.535
1.00
0.36


ATOM
1197
N
GLN
69
38.904
75.188
7.108
1.00
76.80


ATOM
1198
CA
GLN
69
39.078
76.602
7.419
1.00
92.12


ATOM
1199
C
GLN
69
37.768
77.374
7.328
1.00
88.66


ATOM
1200
O
GLN
69
37.662
78.502
7.804
1.00
92.08


ATOM
1201
CB
GLN
69
40.112
77.231
6.492
1.00
0.48


ATOM
1202
CG
GLN
69
40.744
78.483
7.064
1.00
0.89


ATOM
1203
CD
GLN
69
41.389
79.351
6.003
1.00
0.27


ATOM
1204
OE1
GLN
69
40.999
79.315
4.834
1.00
0.95


ATOM
1205
NE2
GLN
69
42.378
80.145
6.407
1.00
0.89


ATOM
1206
N
HIS
70
36.771
76.758
6.712
1.00
88.30


ATOM
1207
CA
HIS
70
35.480
77.402
6.522
1.00
91.96


ATOM
1208
C
HIS
70
34.461
76.908
7.543
1.00
90.90


ATOM
1209
O
HIS
70
33.859
75.852
7.374
1.00
0.38


ATOM
1210
CB
HIS
70
34.994
77.164
5.092
1.00
0.30


ATOM
1211
CG
HIS
70
33.507
77.153
4.946
1.00
0.41


ATOM
1212
ND1
HIS
70
32.749
76.030
5.177
1.00
0.00


ATOM
1213
CD2
HIS
70
32.641
78.125
4.574
1.00
0.21


ATOM
1214
CE1
HIS
70
31.475
76.309
4.967
1.00
0.57


ATOM
1215
NE2
HIS
70
31.383
77.573
4.597
1.00
0.16


ATOM
1216
N
ALA
84
34.316
79.531
−5.688
1.00
33.25


ATOM
1217
CA
ALA
84
35.233
80.497
−6.283
1.00
48.28


ATOM
1218
C
ALA
84
36.546
80.459
−5.531
1.00
39.13


ATOM
1219
O
ALA
84
37.599
80.477
−6.121
1.00
50.56


ATOM
1220
CB
ALA
84
34.646
81.896
−6.227
1.00
31.09


ATOM
1221
N
GLU
85
36.455
80.428
−4.207
1.00
35.63


ATOM
1222
CA
GLU
85
37.616
80.417
−3.351
1.00
37.98


ATOM
1223
C
GLU
85
38.447
79.157
−3.599
1.00
46.30


ATOM
1224
O
GLU
85
39.666
79.170
−3.460
1.00
53.61


ATOM
1225
CB
GLU
85
37.171
80.501
−1.896
1.00
42.29


ATOM
1226
CG
GLU
85
38.298
80.701
−0.924
1.00
80.83


ATOM
1227
CD
GLU
85
37.814
81.190
0.415
1.00
0.90


ATOM
1228
OE1
GLU
85
36.587
81.377
0.562
1.00
0.66


ATOM
1229
OE2
GLU
85
38.658
81.390
1.316
1.00
0.63


ATOM
1230
N
MSE
86
37.777
78.073
−3.981
1.00
34.35


ATOM
1231
CA
MSE
86
38.455
76.797
−4.253
1.00
38.80


ATOM
1232
C
MSE
86
39.232
76.811
−5.562
1.00
43.36


ATOM
1233
O
MSE
86
40.388
76.407
−5.585
1.00
49.32


ATOM
1234
CB
MSE
86
37.471
75.622
−4.279
1.00
32.54


ATOM
1235
CG
MSE
86
38.089
74.354
−4.852
1.00
44.97


ATOM
1236
SE
MSE
86
36.780
72.927
−5.113
1.00
63.68


ATOM
1237
CE
MSE
86
36.010
73.458
−6.821
1.00
28.92


ATOM
1238
N
VAL
87
38.600
77.253
−6.651
1.00
38.65


ATOM
1239
CA
VAL
87
39.295
77.311
−7.933
1.00
34.36


ATOM
1240
C
VAL
87
40.490
78.256
−7.825
1.00
47.21


ATOM
1241
O
VAL
87
41.540
78.009
−8.444
1.00
48.22


ATOM
1242
CB
VAL
87
38.391
77.728
−9.107
1.00
46.20


ATOM
1243
CG1
VAL
87
37.200
76.772
−9.251
1.00
40.79


ATOM
1244
CG2
VAL
87
37.909
79.116
−8.920
1.00
49.33


ATOM
1245
N
ALA
88
40.345
79.313
−7.021
1.00
37.66


ATOM
1246
CA
ALA
88
41.443
80.285
−6.838
1.00
52.91


ATOM
1247
C
ALA
88
42.581
79.670
−6.038
1.00
61.51


ATOM
1248
O
ALA
88
43.749
79.856
−6.360
1.00
60.52


ATOM
1249
CB
ALA
88
40.957
81.523
−6.135
1.00
46.70


ATOM
1250
N
LEU
89
42.214
78.942
−4.987
1.00
56.45


ATOM
1251
CA
LEU
89
43.163
78.278
−4.115
1.00
52.29


ATOM
1252
C
LEU
89
43.946
77.154
−4.829
1.00
59.53


ATOM
1253
O
LEU
89
45.146
76.992
−4.615
1.00
40.19


ATOM
1254
CB
LEU
89
42.421
77.713
−2.905
1.00
53.20


ATOM
1255
CG
LEU
89
43.248
76.881
−1.928
1.00
60.26


ATOM
1256
CD1
LEU
89
44.138
77.794
−1.126
1.00
43.38


ATOM
1257
CD2
LEU
89
42.353
76.087
−1.011
1.00
58.43


ATOM
1258
N
LEU
90
43.268
76.375
−5.666
1.00
49.78


ATOM
1259
CA
LEU
90
43.935
75.321
−6.421
1.00
62.35


ATOM
1260
C
LEU
90
44.539
75.822
−7.733
1.00
64.62


ATOM
1261
O
LEU
90
45.059
75.048
−8.539
1.00
60.89


ATOM
1262
CB
LEU
90
42.973
74.167
−6.657
1.00
47.33


ATOM
1263
CG
LEU
90
43.040
73.266
−5.431
1.00
59.03


ATOM
1264
CD1
LEU
90
41.833
73.426
−4.532
1.00
36.20


ATOM
1265
CD2
LEU
90
43.199
71.844
−5.854
1.00
69.47


ATOM
1266
N
ASP
91
44.466
77.132
−7.928
1.00
62.53


ATOM
1267
CA
ASP
91
45.047
77.771
−9.096
1.00
74.18


ATOM
1268
C
ASP
91
44.501
77.136
−10.370
1.00
64.49


ATOM
1269
O
ASP
91
45.269
76.651
−11.196
1.00
49.15


ATOM
1270
CB
ASP
91
46.574
77.659
−9.041
1.00
79.82


ATOM
1271
CG
ASP
91
47.201
78.633
−8.051
1.00
0.54


ATOM
1272
OD1
ASP
91
46.457
79.411
−7.417
1.00
0.33


ATOM
1273
OD2
ASP
91
48.445
78.634
−7.918
1.00
0.26


ATOM
1274
N
SER
92
43.176
77.138
−10.523
1.00
57.69


ATOM
1275
CA
SER
92
42.553
76.515
−11.687
1.00
45.90


ATOM
1276
C
SER
92
41.470
77.357
−12.389
1.00
51.56


ATOM
1277
O
SER
92
40.897
78.243
−11.805
1.00
45.21


ATOM
1278
CB
SER
92
41.987
75.148
−11.299
1.00
50.32


ATOM
1279
OG
SER
92
41.420
74.505
−12.424
1.00
54.21


ATOM
1280
N
ARG
93
41.174
77.010
−13.637
1.00
60.08


ATOM
1281
CA
ARG
93
40.214
77.712
−14.486
1.00
47.03


ATOM
1282
C
ARG
93
38.743
77.357
−14.182
1.00
59.53


ATOM
1283
O
ARG
93
37.830
78.115
−14.507
1.00
62.26


ATOM
1284
CB
ARG
93
40.534
77.354
−15.942
1.00
60.51


ATOM
1285
CG
ARG
93
39.779
78.116
−16.998
1.00
79.56


ATOM
1286
CD
ARG
93
40.076
77.548
−18.388
1.00
92.42


ATOM
1287
NE
ARG
93
39.647
76.158
−18.521
1.00
86.05


ATOM
1288
CZ
ARG
93
38.374
75.770
−18.603
1.00
96.18


ATOM
1289
NH1
ARG
93
37.396
76.668
−18.554
1.00
94.70


ATOM
1290
NH2
ARG
93
38.070
74.482
−18.725
1.00
84.26


ATOM
1291
N
ALA
94
38.517
76.204
−13.558
1.00
39.54


ATOM
1292
CA
ALA
94
37.175
75.667
−13.380
1.00
49.91


ATOM
1293
C
ALA
94
37.143
74.595
−12.295
1.00
36.89


ATOM
1294
O
ALA
94
38.170
74.050
−11.919
1.00
57.00


ATOM
1295
CB
ALA
94
36.661
75.101
−14.684
1.00
45.18


ATOM
1296
N
GLY
95
35.950
74.288
−11.804
1.00
48.07


ATOM
1297
CA
GLY
95
35.800
73.287
−10.765
1.00
43.22


ATOM
1298
C
GLY
95
34.370
73.116
−10.281
1.00
49.89


ATOM
1299
O
GLY
95
33.492
73.863
−10.670
1.00
43.58


ATOM
1300
N
ASP
130
35.219
79.330
−15.968
1.00
90.21


ATOM
1301
CA
ASP
130
35.821
80.546
−16.514
1.00
96.62


ATOM
1302
C
ASP
130
35.339
81.803
−15.804
1.00
88.70


ATOM
1303
O
ASP
130
35.222
82.857
−16.416
1.00
82.77


ATOM
1304
CB
ASP
130
35.548
80.668
−18.015
1.00
0.95


ATOM
1305
CG
ASP
130
36.445
79.773
−18.843
1.00
0.53


ATOM
1306
OD1
ASP
130
35.915
79.058
−19.724
1.00
0.60


ATOM
1307
OD2
ASP
130
37.676
79.784
−18.606
1.00
0.00


ATOM
1308
N
GLY
131
35.073
81.693
−14.509
1.00
89.33


ATOM
1309
CA
GLY
131
34.571
82.821
−13.752
1.00
78.51


ATOM
1310
C
GLY
131
33.054
82.867
−13.776
1.00
75.79


ATOM
1311
O
GLY
131
32.443
83.619
−13.016
1.00
71.46


ATOM
1312
N
LYS
107
41.732
34.633
−14.670
1.00
34.97


ATOM
1313
CA
LYS
107
43.065
35.231
−14.759
1.00
52.25


ATOM
1314
C
LYS
107
44.181
34.257
−14.370
1.00
51.78


ATOM
1315
O
LYS
107
43.937
33.256
−13.709
1.00
50.24


ATOM
1316
CB
LYS
107
43.145
36.472
−13.880
1.00
46.87


ATOM
1317
CG
LYS
107
42.805
37.721
−14.628
1.00
73.11


ATOM
1318
CD
LYS
107
41.862
38.578
−13.838
1.00
52.85


ATOM
1319
CE
LYS
107
42.594
39.537
−12.936
1.00
74.85


ATOM
1320
NZ
LYS
107
43.478
40.475
−13.679
1.00
60.74


ATOM
1321
N
THR
108
45.406
34.585
−14.768
1.00
39.92


ATOM
1322
CA
THR
108
46.595
33.781
−14.453
1.00
51.78


ATOM
1323
C
THR
108
47.620
34.538
−13.599
1.00
56.01


ATOM
1324
O
THR
108
48.046
35.621
−13.972
1.00
48.49


ATOM
1325
CB
THR
108
47.265
33.329
−15.743
1.00
58.98


ATOM
1326
OG1
THR
108
46.367
32.471
−16.453
1.00
76.08


ATOM
1327
CG2
THR
108
48.565
32.578
−15.439
1.00
63.78


ATOM
1328
N
ALA
109
48.009
33.972
−12.457
1.00
51.19


ATOM
1329
CA
ALA
109
48.981
34.617
−11.577
1.00
47.51


ATOM
1330
C
ALA
109
50.292
34.835
−12.332
1.00
56.59


ATOM
1331
O
ALA
109
50.692
34.004
−13.122
1.00
58.26


ATOM
1332
CB
ALA
109
49.198
33.802
−10.318
1.00
52.79


ATOM
1333
N
PRO
110
50.940
35.985
−12.120
1.00
60.88


ATOM
1334
CA
PRO
110
52.063
36.434
−12.954
1.00
54.80


ATOM
1335
C
PRO
110
53.369
35.605
−12.855
1.00
73.41


ATOM
1336
O
PRO
110
54.163
35.648
−13.794
1.00
94.80


ATOM
1337
CB
PRO
110
52.284
37.871
−12.469
1.00
59.86


ATOM
1338
CG
PRO
110
51.694
37.885
−11.099
1.00
62.30


ATOM
1339
CD
PRO
110
50.486
37.051
−11.220
1.00
65.45


ATOM
1340
N
VAL
111
53.586
34.877
−11.759
1.00
63.03


ATOM
1341
CA
VAL
111
54.752
33.999
−11.640
1.00
67.64


ATOM
1342
C
VAL
111
54.375
32.511
−11.620
1.00
74.71


ATOM
1343
O
VAL
111
54.850
31.742
−12.447
1.00
70.73


ATOM
1344
CB
VAL
111
55.618
34.354
−10.406
1.00
71.63


ATOM
1345
CG1
VAL
111
56.663
33.285
−10.150
1.00
85.60


ATOM
1346
CG2
VAL
111
56.284
35.686
−10.607
1.00
80.10


ATOM
1347
N
SER
112
53.508
32.121
−10.689
1.00
78.75


ATOM
1348
CA
SER
112
53.131
30.724
−10.506
1.00
75.70


ATOM
1349
C
SER
112
52.215
30.186
−11.605
1.00
69.51


ATOM
1350
O
SER
112
52.104
28.964
−11.801
1.00
49.35


ATOM
1351
CB
SER
112
52.460
30.533
−9.146
1.00
52.06


ATOM
1352
OG
SER
112
51.115
30.965
−9.190
1.00
56.21


ATOM
1353
N
GLY
113
51.551
31.102
−12.304
1.00
52.71


ATOM
1354
CA
GLY
113
50.584
30.746
−13.330
1.00
53.69


ATOM
1355
C
GLY
113
49.263
30.170
−12.828
1.00
57.78


ATOM
1356
O
GLY
113
48.436
29.757
−13.636
1.00
46.82


ATOM
1357
N
ILE
114
49.067
30.126
−11.509
1.00
48.95


ATOM
1358
CA
ILE
114
47.827
29.602
−10.954
1.00
62.98


ATOM
1359
C
ILE
114
46.650
30.478
−11.372
1.00
62.30


ATOM
1360
O
ILE
114
46.718
31.709
−11.321
1.00
62.97


ATOM
1361
CB
ILE
114
47.875
29.465
−9.417
1.00
74.53


ATOM
1362
CG1
ILE
114
49.070
28.614
−8.990
1.00
89.66


ATOM
1363
CG2
ILE
114
46.597
28.818
−8.904
1.00
60.35


ATOM
1364
CD1
ILE
114
49.088
28.292
−7.508
1.00
0.82


ATOM
1365
N
ARG
115
45.581
29.830
−11.809
1.00
58.21


ATOM
1366
CA
ARG
115
44.416
30.526
−12.333
1.00
66.68


ATOM
1367
C
ARG
115
43.330
30.751
−11.287
1.00
57.62


ATOM
1368
O
ARG
115
43.135
29.941
−10.377
1.00
46.10


ATOM
1369
CB
ARG
115
43.858
29.777
−13.536
1.00
68.26


ATOM
1370
CG
ARG
115
44.883
29.623
−14.648
1.00
96.72


ATOM
1371
CD
ARG
115
44.398
28.685
−15.733
1.00
0.68


ATOM
1372
NE
ARG
115
43.474
29.337
−16.653
1.00
0.03


ATOM
1373
CZ
ARG
115
42.717
28.687
−17.530
1.00
0.61


ATOM
1374
NH1
ARG
115
42.768
27.364
−17.601
1.00
0.15


ATOM
1375
NH2
ARG
115
41.903
29.359
−18.331
1.00
0.32


ATOM
1376
N
SER
116
42.647
31.884
−11.413
1.00
42.68


ATOM
1377
CA
SER
116
41.529
32.215
−10.535
1.00
43.53


ATOM
1378
C
SER
116
40.657
33.252
−11.224
1.00
43.72


ATOM
1379
O
SER
116
41.096
33.941
−12.142
1.00
45.98


ATOM
1380
CB
SER
116
42.026
32.729
−9.184
1.00
62.92


ATOM
1381
OG
SER
116
42.807
33.901
−9.331
1.00
72.92


ATOM
1382
N
PRO
142
38.424
46.871
−10.783
1.00
23.25


ATOM
1383
CA
PRO
142
39.252
47.141
−9.606
1.00
26.43


ATOM
1384
C
PRO
142
40.728
46.924
−9.970
1.00
33.52


ATOM
1385
O
PRO
142
41.004
45.944
−10.649
1.00
34.13


ATOM
1386
CB
PRO
142
38.856
46.034
−8.632
1.00
33.09


ATOM
1387
CG
PRO
142
37.937
45.094
−9.398
1.00
36.83


ATOM
1388
CD
PRO
142
37.951
45.482
−10.830
1.00
33.30


ATOM
1389
N
VAL
143
41.629
47.802
−9.535
1.00
29.80


ATOM
1390
CA
VAL
143
43.062
47.647
−9.755
1.00
29.02


ATOM
1391
C
VAL
143
43.816
48.153
−8.533
1.00
37.92


ATOM
1392
O
VAL
143
43.207
48.563
−7.551
1.00
42.12


ATOM
1393
CB
VAL
143
43.547
48.424
−10.977
1.00
45.56


ATOM
1394
CG1
VAL
143
42.719
48.044
−12.211
1.00
32.69


ATOM
1395
CG2
VAL
143
43.500
49.926
−10.696
1.00
46.28


ATOM
1396
N
THR
144
45.145
48.098
−8.601
1.00
40.29


ATOM
1397
CA
THR
144
46.019
48.599
−7.543
1.00
58.11


ATOM
1398
C
THR
144
46.639
49.889
−8.022
1.00
45.82


ATOM
1399
O
THR
144
47.059
49.993
−9.178
1.00
41.15


ATOM
1400
CB
THR
144
47.182
47.625
−7.239
1.00
76.98


ATOM
1401
OG1
THR
144
46.679
46.294
−7.072
1.00
84.02


ATOM
1402
CG2
THR
144
47.933
48.057
−5.985
1.00
83.55


ATOM
1403
N
SER
145
46.701
50.876
−7.145
1.00
36.24


ATOM
1404
CA
SER
145
47.395
52.108
−7.473
1.00
52.43


ATOM
1405
C
SER
145
48.464
52.366
−6.424
1.00
54.50


ATOM
1406
O
SER
145
48.248
52.133
−5.250
1.00
43.53


ATOM
1407
CB
SER
145
46.416
53.282
−7.539
1.00
64.86


ATOM
1408
OG
SER
145
45.730
53.440
−6.309
1.00
68.39


ATOM
1409
N
LEU
146
49.621
52.839
−6.852
1.00
56.00


ATOM
1410
CA
LEU
146
50.691
53.152
−5.919
1.00
62.10


ATOM
1411
C
LEU
146
51.116
54.609
−6.109
1.00
44.80


ATOM
1412
O
LEU
146
51.243
55.080
−7.229
1.00
49.94


ATOM
1413
CB
LEU
146
51.872
52.188
−6.111
1.00
66.77


ATOM
1414
CG
LEU
146
53.014
52.307
−5.089
1.00
65.46


ATOM
1415
CD1
LEU
146
53.480
50.945
−4.611
1.00
57.34


ATOM
1416
CD2
LEU
146
54.166
53.135
−5.653
1.00
61.66


ATOM
1417
N
CYS
147
51.339
55.315
−5.012
1.00
33.12


ATOM
1418
CA
CYS
147
51.537
56.760
−5.062
1.00
53.22


ATOM
1419
C
CYS
147
52.978
57.186
−5.361
1.00
49.05


ATOM
1420
O
CYS
147
53.874
56.937
−4.568
1.00
43.23


ATOM
1421
CB
CYS
147
51.095
57.400
−3.753
1.00
44.07


ATOM
1422
SG
CYS
147
51.253
59.215
−3.766
1.00
43.71


ATOM
1423
N
PRO
148
53.185
57.880
−6.485
1.00
76.53


ATOM
1424
CA
PRO
148
54.521
58.339
−6.877
1.00
83.85


ATOM
1425
C
PRO
148
55.120
59.314
−5.869
1.00
74.03


ATOM
1426
O
PRO
148
56.284
59.176
−5.550
1.00
61.76


ATOM
1427
CB
PRO
148
54.274
59.035
−8.215
1.00
84.26


ATOM
1428
CG
PRO
148
52.968
58.508
−8.690
1.00
73.26


ATOM
1429
CD
PRO
148
52.165
58.287
−7.458
1.00
71.33


ATOM
1430
N
CYS
149
54.340
60.266
−5.369
1.00
75.80


ATOM
1431
CA
CYS
149
54.833
61.219
−4.379
1.00
74.27


ATOM
1432
C
CYS
149
55.272
60.535
−3.091
1.00
78.06


ATOM
1433
O
CYS
149
56.307
60.870
−2.536
1.00
46.90


ATOM
1434
CB
CYS
149
53.772
62.281
−4.067
1.00
95.66


ATOM
1435
SG
CYS
149
54.170
63.366
−2.670
1.00
84.40


ATOM
1436
N
SER
150
54.470
59.585
−2.625
1.00
80.75


ATOM
1437
CA
SER
150
54.775
58.811
−1.431
1.00
64.38


ATOM
1438
C
SER
150
56.102
58.067
−1.569
1.00
54.94


ATOM
1439
O
SER
150
56.914
58.067
−0.646
1.00
38.94


ATOM
1440
CB
SER
150
53.651
57.807
−1.173
1.00
69.77


ATOM
1441
OG
SER
150
53.899
57.028
−0.023
1.00
33.31


ATOM
1442
N
LYS
151
56.300
57.406
−2.708
1.00
33.12


ATOM
1443
CA
LYS
151
57.547
56.698
−2.989
1.00
68.45


ATOM
1444
C
LYS
151
58.748
57.658
−3.032
1.00
66.78


ATOM
1445
O
LYS
151
59.751
57.458
−2.357
1.00
57.85


ATOM
1446
CB
LYS
151
57.428
55.963
−4.320
1.00
71.24


ATOM
1447
CG
LYS
151
58.697
55.259
−4.746
1.00
76.97


ATOM
1448
CD
LYS
151
58.592
54.692
−6.148
1.00
68.20


ATOM
1449
CE
LYS
151
59.889
54.020
−6.539
1.00
58.17


ATOM
1450
NZ
LYS
151
59.812
53.468
−7.902
1.00
59.77


ATOM
1451
N
GLU
152
58.613
58.706
−3.829
1.00
78.41


ATOM
1452
CA
GLU
152
59.640
59.730
−4.021
1.00
92.52


ATOM
1453
C
GLU
152
60.153
60.386
−2.735
1.00
79.43


ATOM
1454
O
GLU
152
61.339
60.642
−2.602
1.00
69.31


ATOM
1455
CB
GLU
152
59.091
60.802
−4.962
1.00
0.08


ATOM
1456
CG
GLU
152
60.011
61.960
−5.246
1.00
0.79


ATOM
1457
CD
GLU
152
59.323
63.033
−6.072
1.00
0.24


ATOM
1458
OE1
GLU
152
58.216
63.464
−5.688
1.00
0.23


ATOM
1459
OE2
GLU
152
59.884
63.443
−7.108
1.00
0.86


ATOM
1460
N
ILE
153
59.262
60.657
−1.790
1.00
89.96


ATOM
1461
CA
ILE
153
59.642
61.409
−0.597
1.00
92.18


ATOM
1462
C
ILE
153
60.114
60.554
0.576
1.00
88.22


ATOM
1463
O
ILE
153
60.802
61.052
1.457
1.00
82.43


ATOM
1464
CB
ILE
153
58.513
62.359
−0.108
1.00
86.38


ATOM
1465
CG1
ILE
153
57.298
61.558
0.386
1.00
77.79


ATOM
1466
CG2
ILE
153
58.133
63.347
−1.202
1.00
83.92


ATOM
1467
CD1
ILE
153
56.227
62.397
1.037
1.00
62.29


ATOM
1468
N
SER
154
59.745
59.278
0.609
1.00
88.01


ATOM
1469
CA
SER
154
60.133
58.438
1.742
1.00
86.91


ATOM
1470
C
SER
154
61.351
57.581
1.418
1.00
67.99


ATOM
1471
O
SER
154
61.612
57.274
0.263
1.00
52.76


ATOM
1472
CB
SER
154
58.960
57.590
2.253
1.00
78.98


ATOM
1473
OG
SER
154
58.304
56.928
1.197
1.00
77.89


ATOM
1474
N
GLN
155
62.102
57.212
2.448
1.00
68.23


ATOM
1475
CA
GLN
155
63.334
56.454
2.252
1.00
87.17


ATOM
1476
C
GLN
155
63.032
54.992
1.942
1.00
86.25


ATOM
1477
O
GLN
155
63.870
54.271
1.408
1.00
67.23


ATOM
1478
CB
GLN
155
64.269
56.587
3.460
1.00
96.47


ATOM
1479
CG
GLN
155
63.654
56.185
4.786
1.00
0.52


ATOM
1480
CD
GLN
155
64.638
56.285
5.936
1.00
0.43


ATOM
1481
OE1
GLN
155
65.818
55.963
5.789
1.00
0.25


ATOM
1482
NE2
GLN
155
64.156
56.732
7.090
1.00
0.08


ATOM
1483
N
TYR
156
61.822
54.568
2.284
1.00
82.97


ATOM
1484
CA
TYR
156
61.318
53.261
1.884
1.00
80.96


ATOM
1485
C
TYR
156
59.800
53.229
1.963
1.00
80.92


ATOM
1486
O
TYR
156
59.193
54.083
2.600
1.00
47.73


ATOM
1487
CB
TYR
156
61.929
52.133
2.723
1.00
65.47


ATOM
1488
CG
TYR
156
62.164
52.459
4.181
1.00
85.68


ATOM
1489
CD1
TYR
156
61.111
52.765
5.027
1.00
77.03


ATOM
1490
CD2
TYR
156
63.447
52.438
4.715
1.00
90.55


ATOM
1491
CE1
TYR
156
61.328
53.053
6.361
1.00
99.10


ATOM
1492
CE2
TYR
156
63.672
52.725
6.044
1.00
96.22


ATOM
1493
CZ
TYR
156
62.611
53.031
6.862
1.00
0.08


ATOM
1494
OH
TYR
156
62.837
53.315
8.186
1.00
90.79


ATOM
1495
N
GLY
157
59.196
52.247
1.304
1.00
72.73


ATOM
1496
CA
GLY
157
57.754
52.103
1.307
1.00
58.71


ATOM
1497
C
GLY
157
57.062
53.124
0.424
1.00
52.06


ATOM
1498
O
GLY
157
57.631
54.153
0.078
1.00
47.90


ATOM
1499
N
ALA
158
55.824
52.820
0.046
1.00
33.39


ATOM
1500
CA
ALA
158
54.953
53.755
−0.669
1.00
56.02


ATOM
1501
C
ALA
158
53.518
53.340
−0.406
1.00
62.89


ATOM
1502
O
ALA
158
53.168
52.178
−0.567
1.00
42.34


ATOM
1503
CB
ALA
158
55.239
53.745
−2.164
1.00
50.98


ATOM
1504
N
HIS
159
52.675
54.268
0.016
1.00
53.10


ATOM
1505
CA
HIS
159
51.307
53.870
0.280
1.00
50.36


ATOM
1506
C
HIS
159
50.642
53.486
−1.043
1.00
46.60


ATOM
1507
O
HIS
159
50.840
54.135
−2.077
1.00
42.85


ATOM
1508
CB
HIS
159
50.528
54.932
1.061
1.00
69.62


ATOM
1509
CG
HIS
159
50.007
56.049
0.218
1.00
64.17


ATOM
1510
ND1
HIS
159
48.869
55.928
−0.549
1.00
65.54


ATOM
1511
CD2
HIS
159
50.456
57.306
0.031
1.00
51.87


ATOM
1512
CE1
HIS
159
48.648
57.068
−1.182
1.00
52.61


ATOM
1513
NE2
HIS
159
49.595
57.918
−0.846
1.00
61.55


ATOM
1514
N
ASN
160
49.913
52.376
−1.011
1.00
39.47


ATOM
1515
CA
ASN
160
49.141
51.929
−2.156
1.00
41.24


ATOM
1516
C
ASN
160
47.750
51.588
−1.673
1.00
36.77


ATOM
1517
O
ASN
160
47.495
51.586
−0.481
1.00
37.08


ATOM
1518
CB
ASN
160
49.819
50.746
−2.865
1.00
40.95


ATOM
1519
CG
ASN
160
50.298
49.672
−1.900
1.00
68.88


ATOM
1520
OD1
ASN
160
51.460
49.673
−1.484
1.00
66.81


ATOM
1521
ND2
ASN
160
49.411
48.745
−1.545
1.00
28.56


ATOM
1522
N
GLN
161
46.855
51.279
−2.591
1.00
26.40


ATOM
1523
CA
GLN
161
45.458
51.039
−2.236
1.00
43.83


ATOM
1524
C
GLN
161
44.713
50.497
−3.417
1.00
49.46


ATOM
1525
O
GLN
161
45.198
50.553
−4.542
1.00
43.92


ATOM
1526
CB
GLN
161
44.775
52.329
−1.777
1.00
57.27


ATOM
1527
CG
GLN
161
44.857
53.439
−2.784
1.00
60.87


ATOM
1528
CD
GLN
161
46.158
54.223
−2.695
1.00
52.87


ATOM
1529
OE1
GLN
161
46.634
54.553
−1.601
1.00
41.97


ATOM
1530
NE2
GLN
161
46.725
54.545
−3.850
1.00
38.64


ATOM
1531
N
ARG
162
43.522
49.979
−3.158
1.00
52.54


ATOM
1532
CA
ARG
162
42.648
49.553
−4.232
1.00
46.71


ATOM
1533
C
ARG
162
42.082
50.790
−4.904
1.00
59.05


ATOM
1534
O
ARG
162
41.814
51.795
−4.270
1.00
42.45


ATOM
1535
CB
ARG
162
41.524
48.647
−3.711
1.00
54.51


ATOM
1536
CG
ARG
162
41.034
47.627
−4.718
1.00
71.10


ATOM
1537
CD
ARG
162
39.975
46.712
−4.129
1.00
86.06


ATOM
1538
NE
ARG
162
40.524
45.743
−3.190
1.00
68.39


ATOM
1539
CZ
ARG
162
39.800
45.092
−2.290
1.00
75.71


ATOM
1540
NH1
ARG
162
38.499
45.318
−2.206
1.00
62.22


ATOM
1541
NH2
ARG
162
40.375
44.226
−1.471
1.00
70.75


ATOM
1542
N
SER
163
41.938
50.704
−6.211
1.00
37.48


ATOM
1543
CA
SER
163
41.365
51.764
−7.016
1.00
34.90


ATOM
1544
C
SER
163
40.248
51.166
−7.885
1.00
42.81


ATOM
1545
O
SER
163
40.317
50.026
−8.350
1.00
29.13


ATOM
1546
CB
SER
163
42.466
52.414
−7.862
1.00
43.38


ATOM
1547
OG
SER
163
41.956
53.287
−8.840
1.00
73.12


ATOM
1548
N
HIS
164
39.167
51.908
−8.050
1.00
25.58


ATOM
1549
CA
HIS
164
38.147
51.498
−9.003
1.00
27.06


ATOM
1550
C
HIS
164
38.230
52.398
−10.208
1.00
36.62


ATOM
1551
O
HIS
164
38.126
53.615
−10.089
1.00
35.13


ATOM
1552
CB
HIS
164
36.748
51.578
−8.377
1.00
33.69


ATOM
1553
CG
HIS
164
36.524
50.605
−7.266
1.00
64.30


ATOM
1554
ND1
HIS
164
35.667
50.848
−6.221
1.00
73.91


ATOM
1555
CD2
HIS
164
37.058
49.374
−7.034
1.00
61.84


ATOM
1556
CE1
HIS
164
35.671
49.816
−5.393
1.00
72.47


ATOM
1557
NE2
HIS
164
36.512
48.912
−5.866
1.00
59.98


ATOM
1558
N
ILE
181
38.345
45.784
−20.306
1.00
27.44


ATOM
1559
CA
ILE
181
39.097
45.407
−19.126
1.00
29.36


ATOM
1560
C
ILE
181
40.614
45.457
−19.407
1.00
50.07


ATOM
1561
O
ILE
181
41.397
45.908
−18.564
1.00
40.42


ATOM
1562
CB
ILE
181
38.699
44.026
−18.613
1.00
30.81


ATOM
1563
CG1
ILE
181
37.266
44.079
−18.047
1.00
37.62


ATOM
1564
CG2
ILE
181
39.754
43.517
−17.599
1.00
29.95


ATOM
1565
CD1
ILE
181
36.677
42.733
−17.652
1.00
39.81


ATOM
1566
N
ASP
182
41.004
45.009
−20.598
1.00
29.14


ATOM
1567
CA
ASP
182
42.401
44.978
−21.019
1.00
37.82


ATOM
1568
C
ASP
182
42.982
46.400
−21.154
1.00
43.42


ATOM
1569
O
ASP
182
44.074
46.681
−20.662
1.00
47.73


ATOM
1570
CB
ASP
182
42.558
44.199
−22.331
1.00
36.01


ATOM
1571
CG
ASP
182
42.444
42.677
−22.149
1.00
52.83


ATOM
1572
OD1
ASP
182
42.697
42.167
−21.032
1.00
49.45


ATOM
1573
OD2
ASP
182
42.108
41.985
−23.144
1.00
54.83


ATOM
1574
N
TYR
183
42.257
47.303
−21.807
1.00
37.63


ATOM
1575
CA
TYR
183
42.705
48.693
−21.887
1.00
25.05


ATOM
1576
C
TYR
183
43.036
49.232
−20.493
1.00
47.61


ATOM
1577
O
TYR
183
43.943
50.037
−20.326
1.00
41.37


ATOM
1578
CB
TYR
183
41.645
49.591
−22.527
1.00
33.40


ATOM
1579
CG
TYR
183
41.497
49.479
−24.026
1.00
47.28


ATOM
1580
CD1
TYR
183
42.600
49.293
−24.836
1.00
56.26


ATOM
1581
CD2
TYR
183
40.252
49.610
−24.633
1.00
38.98


ATOM
1582
CE1
TYR
183
42.477
49.216
−26.207
1.00
67.80


ATOM
1583
CE2
TYR
183
40.115
49.538
−26.001
1.00
55.22


ATOM
1584
CZ
TYR
183
41.233
49.336
−26.789
1.00
67.84


ATOM
1585
OH
TYR
183
41.117
49.255
−28.160
1.00
69.73


ATOM
1586
N
VAL
184
42.294
48.806
−19.480
1.00
32.30


ATOM
1587
CA
VAL
184
42.513
49.381
−18.168
1.00
34.08


ATOM
1588
C
VAL
184
43.614
48.674
−17.387
1.00
36.57


ATOM
1589
O
VAL
184
44.448
49.321
−16.789
1.00
35.67


ATOM
1590
CB
VAL
184
41.228
49.440
−17.308
1.00
40.81


ATOM
1591
CG1
VAL
184
41.578
49.791
−15.876
1.00
41.01


ATOM
1592
CG2
VAL
184
40.222
50.471
−17.875
1.00
29.23


ATOM
1593
N
GLU
185
43.610
47.350
−17.391
1.00
40.28


ATOM
1594
CA
GLU
185
44.548
46.602
−16.562
1.00
39.88


ATOM
1595
C
GLU
185
45.993
46.764
−17.037
1.00
49.88


ATOM
1596
O
GLU
185
46.913
46.795
−16.236
1.00
56.83


ATOM
1597
CB
GLU
185
44.119
45.137
−16.470
1.00
28.85


ATOM
1598
CG
GLU
185
42.883
44.926
−15.585
1.00
48.56


ATOM
1599
CD
GLU
185
42.538
43.458
−15.405
1.00
52.66


ATOM
1600
OE1
GLU
185
42.974
42.658
−16.251
1.00
43.17


ATOM
1601
OE2
GLU
185
41.836
43.100
−14.430
1.00
39.75


ATOM
1602
N
THR
186
46.158
46.875
−18.348
1.00
56.19


ATOM
1603
CA
THR
186
47.419
47.226
−18.988
1.00
60.74


ATOM
1604
C
THR
186
48.080
48.452
−18.356
1.00
54.76


ATOM
1605
O
THR
186
49.286
48.488
−18.152
1.00
53.36


ATOM
1606
CB
THR
186
47.188
47.497
−20.494
1.00
59.55


ATOM
1607
OG1
THR
186
47.159
46.253
−21.195
1.00
64.84


ATOM
1608
CG2
THR
186
48.287
48.371
−21.078
1.00
66.33


ATOM
1609
N
GLN
187
47.274
49.448
−18.028
1.00
54.99


ATOM
1610
CA
GLN
187
47.774
50.730
−17.551
1.00
53.27


ATOM
1611
C
GLN
187
47.868
50.860
−16.034
1.00
47.18


ATOM
1612
O
GLN
187
48.309
51.880
−15.541
1.00
56.60


ATOM
1613
CB
GLN
187
46.862
51.845
−18.054
1.00
45.99


ATOM
1614
CG
GLN
187
46.659
51.847
−19.536
1.00
53.53


ATOM
1615
CD
GLN
187
47.920
52.226
−20.252
1.00
60.81


ATOM
1616
OE1
GLN
187
48.807
52.856
−19.670
1.00
55.31


ATOM
1617
NE2
GLN
187
48.015
51.859
−21.520
1.00
47.26


ATOM
1618
N
ALA
188
47.427
49.865
−15.283
1.00
44.02


ATOM
1619
CA
ALA
188
47.445
50.001
−13.834
1.00
52.84


ATOM
1620
C
ALA
188
48.853
49.795
−13.242
1.00
61.50


ATOM
1621
O
ALA
188
49.666
49.088
−13.820
1.00
45.67


ATOM
1622
CB
ALA
188
46.466
49.037
−13.219
1.00
42.42


ATOM
1623
N
SER
189
49.135
50.431
−12.103
1.00
36.67


ATOM
1624
CA
SER
189
50.352
50.161
−11.336
1.00
49.39


ATOM
1625
C
SER
189
50.511
48.661
−11.189
1.00
62.48


ATOM
1626
O
SER
189
51.589
48.122
−11.411
1.00
51.33


ATOM
1627
CB
SER
189
50.289
50.808
−9.953
1.00
35.57


ATOM
1628
OG
SER
189
50.524
52.200
−10.040
1.00
49.82


ATOM
1629
N
CYS
190
49.420
48.006
−10.796
1.00
43.06


ATOM
1630
CA
CYS
190
49.286
46.563
−10.919
1.00
42.62


ATOM
1631
C
CYS
190
47.816
46.122
−10.820
1.00
49.00


ATOM
1632
O
CYS
190
46.973
46.803
−10.259
1.00
43.56


ATOM
1633
CB
CYS
190
50.158
45.805
−9.912
1.00
80.65


ATOM
1634
SG
CYS
190
50.699
44.183
−10.542
1.00
74.68


ATOM
1635
N
GLN
191
47.510
44.980
−11.396
1.00
39.65


ATOM
1636
CA
GLN
191
46.148
44.494
−11.388
1.00
60.24


ATOM
1637
C
GLN
191
45.908
43.561
−10.210
1.00
52.12


ATOM
1638
O
GLN
191
46.837
43.189
−9.515
1.00
49.03


ATOM
1639
CB
GLN
191
45.831
43.816
−12.715
1.00
61.86


ATOM
1640
CG
GLN
191
46.995
43.093
−13.327
1.00
60.94


ATOM
1641
CD
GLN
191
46.670
42.584
−14.698
1.00
63.14


ATOM
1642
OE1
GLN
191
45.933
41.617
−14.849
1.00
54.80


ATOM
1643
NE2
GLN
191
47.211
43.236
−15.713
1.00
66.82


ATOM
1644
N
LEU
192
44.655
43.205
−9.984
1.00
50.72


ATOM
1645
CA
LEU
192
44.289
42.365
−8.860
1.00
41.55


ATOM
1646
C
LEU
192
44.159
40.920
−9.315
1.00
50.00


ATOM
1647
O
LEU
192
43.876
40.670
−10.475
1.00
36.32


ATOM
1648
CB
LEU
192
42.966
42.845
−8.255
1.00
39.35


ATOM
1649
CG
LEU
192
42.940
44.272
−7.727
1.00
46.42


ATOM
1650
CD1
LEU
192
41.593
44.607
−7.117
1.00
41.02


ATOM
1651
CD2
LEU
192
44.044
44.455
−6.701
1.00
49.16


ATOM
1652
N
TYR
193
44.386
39.984
−8.394
1.00
41.05


ATOM
1653
CA
TYR
193
44.156
38.560
−8.618
1.00
41.75


ATOM
1654
C
TYR
193
43.434
37.964
−7.416
1.00
45.03


ATOM
1655
O
TYR
193
43.612
38.431
−6.290
1.00
56.48


ATOM
1656
CB
TYR
193
45.482
37.820
−8.851
1.00
46.33


ATOM
1657
CG
TYR
193
46.279
38.338
−10.022
1.00
52.84


ATOM
1658
CD1
TYR
193
46.090
37.808
−11.290
1.00
47.66


ATOM
1659
CD2
TYR
193
47.222
39.366
−9.863
1.00
49.49


ATOM
1660
CE1
TYR
193
46.804
38.273
−12.366
1.00
57.04


ATOM
1661
CE2
TYR
193
47.944
39.839
−10.941
1.00
51.34


ATOM
1662
CZ
TYR
193
47.730
39.281
−12.187
1.00
59.22


ATOM
1663
OH
TYR
193
48.427
39.722
−13.273
1.00
45.64


ATOM
1664
N
GLY
194
42.625
36.934
−7.649
1.00
47.68


ATOM
1665
CA
GLY
194
41.953
36.252
−6.563
1.00
45.00


ATOM
1666
C
GLY
194
42.902
35.350
−5.783
1.00
55.57


ATOM
1667
O
GLY
194
42.802
35.232
−4.562
1.00
73.94


ATOM
1668
N
LEU
195
43.828
34.715
−6.495
1.00
56.69


ATOM
1669
CA
LEU
195
44.748
33.746
−5.903
1.00
68.95


ATOM
1670
C
LEU
195
46.190
34.088
−6.238
1.00
68.24


ATOM
1671
O
LEU
195
46.552
34.129
−7.408
1.00
53.14


ATOM
1672
CB
LEU
195
44.431
32.350
−6.431
1.00
55.82


ATOM
1673
CG
LEU
195
44.860
31.147
−5.603
1.00
63.65


ATOM
1674
CD1
LEU
195
44.173
29.896
−6.124
1.00
53.17


ATOM
1675
CD2
LEU
195
46.371
30.988
−5.634
1.00
83.63


ATOM
1676
N
LEU
196
47.000
34.331
−5.208
1.00
49.64


ATOM
1677
CA
LEU
196
48.437
34.577
−5.370
1.00
47.59


ATOM
1678
C
LEU
196
49.267
33.743
−4.411
1.00
55.36


ATOM
1679
O
LEU
196
48.957
33.667
−3.222
1.00
59.50


ATOM
1680
CB
LEU
196
48.768
36.045
−5.111
1.00
47.54


ATOM
1681
CG
LEU
196
48.082
37.053
−6.027
1.00
58.31


ATOM
1682
CD1
LEU
196
48.266
38.450
−5.517
1.00
54.87


ATOM
1683
CD2
LEU
196
48.630
36.905
−7.419
1.00
37.88


ATOM
1684
N
LYS
197
50.338
33.145
−4.923
1.00
48.39


ATOM
1685
CA
LYS
197
51.311
32.455
−4.083
1.00
75.76


ATOM
1686
C
LYS
197
52.429
33.426
−3.703
1.00
71.25


ATOM
1687
O
LYS
197
52.485
34.542
−4.228
1.00
49.06


ATOM
1688
CB
LYS
197
51.880
31.231
−4.807
1.00
81.92


ATOM
1689
CG
LYS
197
50.855
30.138
−5.073
1.00
88.40


ATOM
1690
CD
LYS
197
49.784
30.130
−3.999
1.00
0.78


ATOM
1691
CE
LYS
197
49.135
28.771
−3.846
1.00
0.41


ATOM
1692
NZ
LYS
197
49.905
27.924
−2.897
1.00
0.26


ATOM
1693
N
ARG
198
53.307
33.004
−2.795
1.00
61.35


ATOM
1694
CA
ARG
198
54.429
33.836
−2.340
1.00
78.19


ATOM
1695
C
ARG
198
55.195
34.547
−3.462
1.00
75.65


ATOM
1696
O
ARG
198
55.372
35.758
−3.408
1.00
52.93


ATOM
1697
CB
ARG
198
55.403
33.020
−1.491
1.00
91.33


ATOM
1698
CG
ARG
198
55.218
33.165
0.001
1.00
0.83


ATOM
1699
CD
ARG
198
56.126
32.199
0.738
1.00
0.91


ATOM
1700
NE
ARG
198
56.610
32.758
1.995
1.00
0.29


ATOM
1701
CZ
ARG
198
57.805
33.318
2.152
1.00
0.90


ATOM
1702
NH1
ARG
198
58.646
33.389
1.128
1.00
0.09


ATOM
1703
NH2
ARG
198
58.162
33.803
3.334
1.00
0.42


ATOM
1704
N
PRO
199
55.669
33.797
−4.471
1.00
70.03


ATOM
1705
CA
PRO
199
56.397
34.425
−5.579
1.00
66.36


ATOM
1706
C
PRO
199
55.541
35.424
−6.351
1.00
71.38


ATOM
1707
O
PRO
199
56.103
36.399
−6.843
1.00
55.95


ATOM
1708
CB
PRO
199
56.757
33.232
−6.482
1.00
64.71


ATOM
1709
CG
PRO
199
55.798
32.168
−6.082
1.00
73.47


ATOM
1710
CD
PRO
199
55.666
32.334
−4.609
1.00
77.02


ATOM
1711
N
ASP
200
54.227
35.176
−6.456
1.00
60.82


ATOM
1712
CA
ASP
200
53.290
36.080
−7.142
1.00
63.99


ATOM
1713
C
ASP
200
53.146
37.405
−6.410
1.00
61.39


ATOM
1714
O
ASP
200
53.208
38.477
−7.003
1.00
53.71


ATOM
1715
CB
ASP
200
51.899
35.453
−7.228
1.00
50.68


ATOM
1716
CG
ASP
200
51.852
34.256
−8.145
1.00
70.50


ATOM
1717
OD1
ASP
200
52.439
34.336
−9.241
1.00
53.74


ATOM
1718
OD2
ASP
200
51.215
33.246
−7.773
1.00
75.96


ATOM
1719
N
GLU
201
52.926
37.305
−5.109
1.00
44.34


ATOM
1720
CA
GLU
201
52.811
38.464
−4.255
1.00
68.64


ATOM
1721
C
GLU
201
54.094
39.288
−4.267
1.00
64.75


ATOM
1722
O
GLU
201
54.046
40.504
−4.319
1.00
40.48


ATOM
1723
CB
GLU
201
52.469
38.044
−2.830
1.00
44.67


ATOM
1724
CG
GLU
201
52.608
39.169
−1.836
1.00
71.92


ATOM
1725
CD
GLU
201
51.777
38.957
−0.595
1.00
76.03


ATOM
1726
OE1
GLU
201
51.495
37.797
−0.255
1.00
87.45


ATOM
1727
OE2
GLU
201
51.404
39.955
0.043
1.00
64.60


ATOM
1728
N
LYS
202
55.243
38.630
−4.206
1.00
50.01


ATOM
1729
CA
LYS
202
56.513
39.334
−4.314
1.00
53.02


ATOM
1730
C
LYS
202
56.564
40.134
−5.628
1.00
42.78


ATOM
1731
O
LYS
202
56.876
41.318
−5.640
1.00
43.49


ATOM
1732
CB
LYS
202
57.685
38.343
−4.227
1.00
45.02


ATOM
1733
CG
LYS
202
59.008
38.947
−4.615
1.00
59.66


ATOM
1734
CD
LYS
202
60.147
37.932
−4.555
1.00
54.22


ATOM
1735
CE
LYS
202
61.395
38.559
−5.112
1.00
46.69


ATOM
1736
NZ
LYS
202
62.492
37.561
−5.135
1.00
0.21


ATOM
1737
N
TYR
203
56.261
39.464
−6.729
1.00
53.09


ATOM
1738
CA
TYR
203
56.204
40.089
−8.045
1.00
64.50


ATOM
1739
C
TYR
203
55.245
41.289
−8.106
1.00
61.81


ATOM
1740
O
TYR
203
55.568
42.322
−8.685
1.00
65.84


ATOM
1741
CB
TYR
203
55.783
39.046
−9.075
1.00
67.81


ATOM
1742
CG
TYR
203
55.679
39.568
−10.477
1.00
64.72


ATOM
1743
CD1
TYR
203
56.748
39.472
−11.345
1.00
52.12


ATOM
1744
CD2
TYR
203
54.513
40.154
−10.940
1.00
53.63


ATOM
1745
CE1
TYR
203
56.664
39.935
−12.633
1.00
60.02


ATOM
1746
CE2
TYR
203
54.421
40.629
−12.241
1.00
64.08


ATOM
1747
CZ
TYR
203
55.506
40.510
−13.079
1.00
69.98


ATOM
1748
OH
TYR
203
55.444
40.975
−14.365
1.00
69.48


ATOM
1749
N
VAL
204
54.068
41.150
−7.506
1.00
60.20


ATOM
1750
CA
VAL
204
53.038
42.203
−7.576
1.00
78.24


ATOM
1751
C
VAL
204
53.422
43.441
−6.723
1.00
47.17


ATOM
1752
O
VAL
204
53.315
44.579
−7.181
1.00
43.11


ATOM
1753
CB
VAL
204
51.612
41.622
−7.250
1.00
43.63


ATOM
1754
CG1
VAL
204
51.277
41.757
−5.775
1.00
47.36


ATOM
1755
CG2
VAL
204
50.563
42.242
−8.102
1.00
71.25


ATOM
1756
N
THR
205
53.905
43.205
−5.506
1.00
44.47


ATOM
1757
CA
THR
205
54.461
44.244
−4.633
1.00
52.60


ATOM
1758
C
THR
205
55.540
45.083
−5.338
1.00
57.12


ATOM
1759
O
THR
205
55.508
46.328
−5.330
1.00
41.28


ATOM
1760
CB
THR
205
55.107
43.610
−3.363
1.00
61.74


ATOM
1761
OG1
THR
205
54.153
42.798
−2.669
1.00
49.23


ATOM
1762
CG2
THR
205
55.642
44.675
−2.418
1.00
57.92


ATOM
1763
N
GLU
206
56.501
44.386
−5.939
1.00
51.43


ATOM
1764
CA
GLU
206
57.652
45.021
−6.587
1.00
49.67


ATOM
1765
C
GLU
206
57.274
45.784
−7.859
1.00
42.78


ATOM
1766
O
GLU
206
57.708
46.911
−8.056
1.00
46.60


ATOM
1767
CB
GLU
206
58.753
43.979
−6.872
1.00
32.43


ATOM
1768
CG
GLU
206
59.406
43.451
−5.608
1.00
67.25


ATOM
1769
CD
GLU
206
60.333
42.277
−5.874
1.00
94.44


ATOM
1770
OE1
GLU
206
60.462
41.852
−7.044
1.00
0.36


ATOM
1771
OE2
GLU
206
60.933
41.777
−4.904
1.00
89.69


ATOM
1772
N
LYS
207
56.460
45.162
−8.703
1.00
46.45


ATOM
1773
CA
LYS
207
56.052
45.741
−9.968
1.00
62.72


ATOM
1774
C
LYS
207
55.270
47.029
−9.746
1.00
63.15


ATOM
1775
O
LYS
207
55.445
47.995
−10.483
1.00
51.88


ATOM
1776
CB
LYS
207
55.237
44.720
−10.776
1.00
72.67


ATOM
1777
CG
LYS
207
54.342
45.314
−11.858
1.00
0.74


ATOM
1778
CD
LYS
207
55.121
45.667
−13.113
1.00
0.57


ATOM
1779
CE
LYS
207
54.183
45.984
−14.272
1.00
0.12


ATOM
1780
NZ
LYS
207
54.926
46.230
−15.540
1.00
0.37


ATOM
1781
N
ALA
208
54.419
47.044
−8.721
1.00
51.93


ATOM
1782
CA
ALA
208
53.653
48.245
−8.383
1.00
52.25


ATOM
1783
C
ALA
208
54.595
49.340
−7.896
1.00
57.98


ATOM
1784
O
ALA
208
54.459
50.512
−8.252
1.00
36.09


ATOM
1785
CB
ALA
208
52.598
47.938
−7.319
1.00
38.82


ATOM
1786
N
TYR
209
55.565
48.948
−7.077
1.00
52.31


ATOM
1787
CA
TYR
209
56.567
49.884
−6.594
1.00
56.68


ATOM
1788
C
TYR
209
57.336
50.530
−7.761
1.00
64.16


ATOM
1789
O
TYR
209
57.634
51.710
−7.726
1.00
52.26


ATOM
1790
CB
TYR
209
57.510
49.192
−5.615
1.00
51.72


ATOM
1791
CG
TYR
209
58.410
50.129
−4.833
1.00
63.67


ATOM
1792
CD1
TYR
209
57.999
50.659
−3.608
1.00
59.18


ATOM
1793
CD2
TYR
209
59.667
50.478
−5.309
1.00
67.39


ATOM
1794
CE1
TYR
209
58.809
51.499
−2.885
1.00
74.90


ATOM
1795
CE2
TYR
209
60.490
51.325
−4.586
1.00
55.98


ATOM
1796
CZ
TYR
209
60.053
51.832
−3.378
1.00
78.85


ATOM
1797
OH
TYR
209
60.859
52.676
−2.659
1.00
69.89


ATOM
1798
N
GLU
210
57.623
49.764
−8.806
1.00
59.87


ATOM
1799
CA
GLU
210
58.365
50.287
−9.952
1.00
55.94


ATOM
1800
C
GLU
210
57.461
51.050
−10.920
1.00
69.29


ATOM
1801
O
GLU
210
57.948
51.720
−11.819
1.00
56.02


ATOM
1802
CB
GLU
210
59.066
49.155
−10.702
1.00
55.80


ATOM
1803
CG
GLU
210
59.989
48.312
−9.849
1.00
71.30


ATOM
1804
CD
GLU
210
60.235
46.923
−10.426
1.00
87.58


ATOM
1805
OE1
GLU
210
59.759
46.623
−11.546
1.00
73.11


ATOM
1806
OE2
GLU
210
60.903
46.120
−9.748
1.00
93.13


ATOM
1807
N
ASN
211
56.144
50.943
−10.751
1.00
52.95


ATOM
1808
CA
ASN
211
55.228
51.625
−11.660
1.00
72.66


ATOM
1809
C
ASN
211
54.204
52.491
−10.915
1.00
72.42


ATOM
1810
O
ASN
211
53.002
52.267
−11.008
1.00
55.20


ATOM
1811
CB
ASN
211
54.537
50.614
−12.586
1.00
82.34


ATOM
1812
CG
ASN
211
53.763
51.281
−13.711
1.00
96.40


ATOM
1813
OD1
ASN
211
54.164
52.326
−14.228
1.00
0.40


ATOM
1814
ND2
ASN
211
52.645
50.674
−14.097
1.00
93.22


ATOM
1815
N
PRO
212
54.685
53.494
−10.171
1.00
55.52


ATOM
1816
CA
PRO
212
53.771
54.353
−9.417
1.00
50.78


ATOM
1817
C
PRO
212
52.908
55.193
−10.357
1.00
62.47


ATOM
1818
O
PRO
212
53.390
55.633
−11.396
1.00
43.99


ATOM
1819
CB
PRO
212
54.717
55.271
−8.633
1.00
44.67


ATOM
1820
CG
PRO
212
56.099
54.674
−8.786
1.00
53.75


ATOM
1821
CD
PRO
212
56.078
53.969
−10.087
1.00
52.24


ATOM
1822
N
LYS
213
51.647
55.402
−10.000
1.00
50.06


ATOM
1823
CA
LYS
213
50.733
56.202
−10.821
1.00
60.06


ATOM
1824
C
LYS
213
49.698
56.946
−9.986
1.00
37.78


ATOM
1825
O
LYS
213
48.985
56.351
−9.184
1.00
49.66


ATOM
1826
CB
LYS
213
50.019
55.344
−11.877
1.00
59.67


ATOM
1827
CG
LYS
213
50.842
55.087
−13.119
1.00
67.39


ATOM
1828
CD
LYS
213
50.009
54.535
−14.255
1.00
71.54


ATOM
1829
CE
LYS
213
50.909
53.988
−15.349
1.00
66.53


ATOM
1830
NZ
LYS
213
50.180
53.601
−16.586
1.00
54.59


ATOM
1831
N
PHE
214
49.644
58.254
−10.189
1.00
44.37


ATOM
1832
CA
PHE
214
48.577
59.094
−9.666
1.00
57.67


ATOM
1833
C
PHE
214
47.257
58.759
−10.339
1.00
50.58


ATOM
1834
O
PHE
214
47.235
58.167
−11.414
1.00
52.80


ATOM
1835
CB
PHE
214
48.882
60.570
−9.950
1.00
53.34


ATOM
1836
CG
PHE
214
49.983
61.143
−9.112
1.00
60.66


ATOM
1837
CD1
PHE
214
49.924
61.093
−7.730
1.00
75.57


ATOM
1838
CD2
PHE
214
51.063
61.763
−9.708
1.00
74.87


ATOM
1839
CE1
PHE
214
50.932
61.631
−6.959
1.00
68.54


ATOM
1840
CE2
PHE
214
52.075
62.307
−8.943
1.00
73.49


ATOM
1841
CZ
PHE
214
52.009
62.240
−7.565
1.00
65.16


ATOM
1842
N
VAL
215
46.161
59.189
−9.721
1.00
50.21


ATOM
1843
CA
VAL
215
44.838
59.073
−10.332
1.00
32.24


ATOM
1844
C
VAL
215
44.760
59.862
−11.663
1.00
39.63


ATOM
1845
O
VAL
215
44.097
59.449
−12.616
1.00
34.93


ATOM
1846
CB
VAL
215
43.736
59.462
−9.328
1.00
49.44


ATOM
1847
CG1
VAL
215
43.564
60.964
−9.245
1.00
40.48


ATOM
1848
CG2
VAL
215
42.442
58.814
−9.698
1.00
43.26


ATOM
1849
N
GLU
216
45.483
60.976
−11.741
1.00
31.87


ATOM
1850
CA
GLU
216
45.604
61.740
−12.985
1.00
37.07


ATOM
1851
C
GLU
216
46.236
60.948
−14.124
1.00
42.58


ATOM
1852
O
GLU
216
45.774
61.005
−15.267
1.00
37.19


ATOM
1853
CB
GLU
216
46.392
63.038
−12.760
1.00
37.27


ATOM
1854
CG
GLU
216
45.753
63.982
−11.734
1.00
55.63


ATOM
1855
CD
GLU
216
46.293
63.800
−10.315
1.00
64.24


ATOM
1856
OE1
GLU
216
46.794
62.710
−9.987
1.00
72.74


ATOM
1857
OE2
GLU
216
46.212
64.750
−9.514
1.00
72.11


ATOM
1858
N
ASP
217
47.297
60.209
−13.821
1.00
42.79


ATOM
1859
CA
ASP
217
47.967
59.411
−14.846
1.00
48.33


ATOM
1860
C
ASP
217
47.118
58.237
−15.292
1.00
43.56


ATOM
1861
O
ASP
217
47.070
57.918
−16.475
1.00
45.97


ATOM
1862
CB
ASP
217
49.316
58.927
−14.338
1.00
53.19


ATOM
1863
CG
ASP
217
50.191
60.065
−13.902
1.00
69.65


ATOM
1864
OD1
ASP
217
50.265
61.060
−14.662
1.00
73.54


ATOM
1865
OD2
ASP
217
50.782
59.977
−12.801
1.00
68.83


ATOM
1866
N
MSE
218
46.443
57.609
−14.336
1.00
37.35


ATOM
1867
CA
MSE
218
45.542
56.503
−14.634
1.00
39.78


ATOM
1868
C
MSE
218
44.546
56.896
−15.734
1.00
24.72


ATOM
1869
O
MSE
218
44.499
56.279
−16.796
1.00
29.59


ATOM
1870
CB
MSE
218
44.810
56.050
−13.362
1.00
58.79


ATOM
1871
CG
MSE
218
44.073
54.718
−13.480
1.00
77.38


ATOM
1872
SE
MSE
218
45.130
53.300
−14.337
1.00
0.47


ATOM
1873
CE
MSE
218
44.023
51.745
−13.914
1.00
0.92


ATOM
1874
N
VAL
219
43.774
57.954
−15.494
1.00
29.59


ATOM
1875
CA
VAL
219
42.719
58.311
−16.429
1.00
26.43


ATOM
1876
C
VAL
219
43.272
58.802
−17.751
1.00
27.62


ATOM
1877
O
VAL
219
42.717
58.504
−18.809
1.00
32.99


ATOM
1878
CB
VAL
219
41.705
59.336
−15.837
1.00
36.95


ATOM
1879
CG1
VAL
219
41.063
58.766
−14.612
1.00
35.83


ATOM
1880
CG2
VAL
219
42.391
60.634
−15.492
1.00
30.34


ATOM
1881
N
ARG
220
44.362
59.557
−17.691
1.00
30.45


ATOM
1882
CA
ARG
220
45.024
59.991
−18.917
1.00
43.29


ATOM
1883
C
ARG
220
45.473
58.811
−19.757
1.00
39.78


ATOM
1884
O
ARG
220
45.241
58.785
−20.961
1.00
49.09


ATOM
1885
CB
ARG
220
46.204
60.899
−18.606
1.00
37.68


ATOM
1886
CG
ARG
220
45.787
62.334
−18.434
1.00
41.30


ATOM
1887
CD
ARG
220
46.922
63.184
−17.877
1.00
37.85


ATOM
1888
NE
ARG
220
46.562
64.587
−18.004
1.00
44.94


ATOM
1889
CZ
ARG
220
47.039
65.568
−17.253
1.00
47.83


ATOM
1890
NH1
ARG
220
47.911
65.315
−16.293
1.00
39.44


ATOM
1891
NH2
ARG
220
46.630
66.808
−17.468
1.00
46.76


ATOM
1892
N
ASP
221
46.091
57.825
−19.116
1.00
30.84


ATOM
1893
CA
ASP
221
46.593
56.663
−19.863
1.00
39.37


ATOM
1894
C
ASP
221
45.487
55.785
−20.456
1.00
39.67


ATOM
1895
O
ASP
221
45.582
55.333
−21.584
1.00
44.32


ATOM
1896
CB
ASP
221
47.527
55.840
−18.990
1.00
50.33


ATOM
1897
CG
ASP
221
48.803
56.596
−18.628
1.00
76.67


ATOM
1898
OD1
ASP
221
49.064
57.668
−19.227
1.00
84.23


ATOM
1899
OD2
ASP
221
49.549
56.121
−17.741
1.00
61.34


ATOM
1900
N
VAL
222
44.411
55.570
−19.707
1.00
35.67


ATOM
1901
CA
VAL
222
43.286
54.801
−20.242
1.00
37.76


ATOM
1902
C
VAL
222
42.568
55.554
−21.366
1.00
32.07


ATOM
1903
O
VAL
222
42.181
54.959
−22.366
1.00
38.73


ATOM
1904
CB
VAL
222
42.265
54.474
−19.163
1.00
30.54


ATOM
1905
CG1
VAL
222
41.055
53.806
−19.798
1.00
34.98


ATOM
1906
CG2
VAL
222
42.880
53.609
−18.116
1.00
31.33


ATOM
1907
N
ALA
223
42.408
56.867
−21.189
1.00
27.50


ATOM
1908
CA
ALA
223
41.684
57.696
−22.152
1.00
38.49


ATOM
1909
C
ALA
223
42.393
57.706
−23.496
1.00
41.28


ATOM
1910
O
ALA
223
41.755
57.705
−24.540
1.00
35.49


ATOM
1911
CB
ALA
223
41.531
59.102
−21.634
1.00
32.48


ATOM
1912
N
THR
224
43.722
57.720
−23.457
1.00
38.65


ATOM
1913
CA
THR
224
44.515
57.719
−24.679
1.00
41.10


ATOM
1914
C
THR
224
44.251
56.444
−25.487
1.00
40.22


ATOM
1915
O
THR
224
44.079
56.490
−26.702
1.00
44.23


ATOM
1916
CB
THR
224
45.997
57.847
−24.361
1.00
34.72


ATOM
1917
OG1
THR
224
46.230
59.095
−23.701
1.00
47.19


ATOM
1918
CG2
THR
224
46.809
57.787
−25.634
1.00
51.18


ATOM
1919
N
SER
225
44.206
55.306
−24.803
1.00
35.60


ATOM
1920
CA
SER
225
43.861
54.041
−25.456
1.00
47.00


ATOM
1921
C
SER
225
42.478
54.062
−26.070
1.00
45.84


ATOM
1922
O
SER
225
42.288
53.536
−27.161
1.00
42.17


ATOM
1923
CB
SER
225
43.921
52.878
−24.479
1.00
42.92


ATOM
1924
OG
SER
225
45.122
52.899
−23.754
1.00
48.51


ATOM
1925
N
LEU
226
41.518
54.662
−25.370
1.00
37.09


ATOM
1926
CA
LEU
226
40.133
54.686
−25.853
1.00
36.24


ATOM
1927
C
LEU
226
40.008
55.632
−27.036
1.00
37.89


ATOM
1928
O
LEU
226
39.325
55.318
−28.006
1.00
43.78


ATOM
1929
CB
LEU
226
39.165
55.081
−24.729
1.00
34.97


ATOM
1930
CG
LEU
226
39.134
54.201
−23.479
1.00
33.84


ATOM
1931
CD1
LEU
226
38.220
54.802
−22.430
1.00
50.41


ATOM
1932
CD2
LEU
226
38.715
52.749
−23.789
1.00
39.51


ATOM
1933
N
ILE
227
40.697
56.774
−26.953
1.00
36.57


ATOM
1934
CA
ILE
227
40.717
57.772
−28.015
1.00
45.24


ATOM
1935
C
ILE
227
41.250
57.172
−29.305
1.00
47.23


ATOM
1936
O
ILE
227
40.767
57.485
−30.391
1.00
49.27


ATOM
1937
CB
ILE
227
41.584
58.982
−27.644
1.00
47.34


ATOM
1938
CG1
ILE
227
40.827
59.893
−26.683
1.00
43.33


ATOM
1939
CG2
ILE
227
42.004
59.759
−28.913
1.00
38.95


ATOM
1940
CD1
ILE
227
41.690
60.899
−26.055
1.00
47.18


ATOM
1941
N
ALA
228
42.242
56.296
−29.169
1.00
33.22


ATOM
1942
CA
ALA
228
42.793
55.595
−30.316
1.00
51.83


ATOM
1943
C
ALA
228
41.791
54.642
−30.994
1.00
62.10


ATOM
1944
O
ALA
228
41.712
54.585
−32.215
1.00
60.35


ATOM
1945
CB
ALA
228
44.061
54.864
−29.931
1.00
49.81


ATOM
1946
N
ASP
229
41.017
53.908
−30.207
1.00
48.90


ATOM
1947
CA
ASP
229
40.031
52.979
−30.765
1.00
44.21


ATOM
1948
C
ASP
229
38.912
53.684
−31.570
1.00
52.96


ATOM
1949
O
ASP
229
38.167
54.496
−31.024
1.00
56.32


ATOM
1950
CB
ASP
229
39.422
52.149
−29.638
1.00
63.61


ATOM
1951
CG
ASP
229
38.777
50.880
−30.137
1.00
71.21


ATOM
1952
OD1
ASP
229
37.992
50.927
−31.117
1.00
54.93


ATOM
1953
OD2
ASP
229
39.065
49.829
−29.541
1.00
59.40


ATOM
1954
N
SER
239
38.540
57.458
−12.331
1.00
32.02


ATOM
1955
CA
SER
239
39.261
56.623
−11.403
1.00
36.49


ATOM
1956
C
SER
239
39.027
57.122
−9.984
1.00
38.44


ATOM
1957
O
SER
239
39.101
58.312
−9.694
1.00
36.92


ATOM
1958
CB
SER
239
40.740
56.592
−11.742
1.00
34.93


ATOM
1959
OG
SER
239
41.417
55.702
−10.880
1.00
60.83


ATOM
1960
N
GLU
240
38.691
56.205
−9.102
1.00
23.58


ATOM
1961
CA
GLU
240
38.605
56.532
−7.698
1.00
29.00


ATOM
1962
C
GLU
240
39.659
55.781
−6.871
1.00
42.70


ATOM
1963
O
GLU
240
39.693
54.562
−6.885
1.00
34.93


ATOM
1964
CB
GLU
240
37.206
56.221
−7.195
1.00
21.31


ATOM
1965
CG
GLU
240
37.038
56.469
−5.723
1.00
44.72


ATOM
1966
CD
GLU
240
35.586
56.521
−5.345
1.00
61.73


ATOM
1967
OE1
GLU
240
34.730
56.323
−6.244
1.00
55.18


ATOM
1968
OE2
GLU
240
35.301
56.770
−4.156
1.00
62.28


ATOM
1969
N
ASN
241
40.511
56.509
−6.157
1.00
35.37


ATOM
1970
CA
ASN
241
41.557
55.895
−5.336
1.00
35.84


ATOM
1971
C
ASN
241
41.181
55.931
−3.868
1.00
44.30


ATOM
1972
O
ASN
241
41.131
57.006
−3.277
1.00
35.87


ATOM
1973
CB
ASN
241
42.846
56.695
−5.458
1.00
59.50


ATOM
1974
CG
ASN
241
43.834
56.080
−6.385
1.00
74.07


ATOM
1975
OD1
ASN
241
45.033
56.159
−6.144
1.00
83.92


ATOM
1976
ND2
ASN
241
43.353
55.474
−7.461
1.00
73.43


ATOM
1977
N
PHE
242
40.947
54.779
−3.261
1.00
34.18


ATOM
1978
CA
PHE
242
40.648
54.730
−1.835
1.00
54.06


ATOM
1979
C
PHE
242
41.932
54.805
−1.029
1.00
43.36


ATOM
1980
O
PHE
242
42.298
53.861
−0.319
1.00
42.57


ATOM
1981
CB
PHE
242
39.837
53.479
−1.491
1.00
49.71


ATOM
1982
CG
PHE
242
38.579
53.348
−2.307
1.00
54.48


ATOM
1983
CD1
PHE
242
37.400
53.964
−1.899
1.00
48.92


ATOM
1984
CD2
PHE
242
38.587
52.633
−3.500
1.00
50.08


ATOM
1985
CE1
PHE
242
36.249
53.865
−2.662
1.00
44.33


ATOM
1986
CE2
PHE
242
37.446
52.523
−4.265
1.00
56.26


ATOM
1987
CZ
PHE
242
36.269
53.144
−3.847
1.00
48.67


ATOM
1988
N
GLU
243
42.603
55.950
−1.149
1.00
43.70


ATOM
1989
CA
GLU
243
43.938
56.145
−0.598
1.00
53.80


ATOM
1990
C
GLU
243
44.041
55.657
0.836
1.00
54.72


ATOM
1991
O
GLU
243
43.155
55.892
1.662
1.00
36.12


ATOM
1992
CB
GLU
243
44.409
57.600
−0.753
1.00
62.42


ATOM
1993
CG
GLU
243
43.409
58.632
−0.338
1.00
98.18


ATOM
1994
CD
GLU
243
43.956
60.032
−0.486
1.00
0.38


ATOM
1995
OE1
GLU
243
43.160
60.995
−0.471
1.00
0.85


ATOM
1996
OE2
GLU
243
45.189
60.168
−0.625
1.00
0.45


ATOM
1997
N
SER
244
45.126
54.946
1.110
1.00
48.15


ATOM
1998
CA
SER
244
45.254
54.200
2.349
1.00
48.27


ATOM
1999
C
SER
244
45.764
55.075
3.487
1.00
43.29


ATOM
2000
O
SER
244
45.999
54.580
4.582
1.00
54.30


ATOM
2001
CB
SER
244
46.178
53.001
2.154
1.00
50.70


ATOM
2002
OG
SER
244
47.495
53.457
1.924
1.00
57.31


ATOM
2003
N
ILE
245
45.938
56.370
3.225
1.00
38.50


ATOM
2004
CA
ILE
245
46.367
57.306
4.273
1.00
54.46


ATOM
2005
C
ILE
245
45.290
58.330
4.654
1.00
49.60


ATOM
2006
O
ILE
245
45.474
59.101
5.595
1.00
39.53


ATOM
2007
CB
ILE
245
47.658
58.057
3.879
1.00
54.37


ATOM
2008
CG1
ILE
245
47.401
58.957
2.669
1.00
54.44


ATOM
2009
CG2
ILE
245
48.758
57.075
3.577
1.00
37.95


ATOM
2010
CD1
ILE
245
48.629
59.708
2.192
1.00
73.40


ATOM
2011
N
HIS
246
44.188
58.351
3.908
1.00
43.91


ATOM
2012
CA
HIS
246
43.058
59.241
4.206
1.00
49.94


ATOM
2013
C
HIS
246
41.770
58.429
4.355
1.00
57.65


ATOM
2014
O
HIS
246
41.754
57.248
4.058
1.00
47.46


ATOM
2015
CB
HIS
246
42.893
60.286
3.104
1.00
40.63


ATOM
2016
CG
HIS
246
44.038
61.253
3.001
1.00
63.27


ATOM
2017
ND1
HIS
246
44.749
61.446
1.831
1.00
58.15


ATOM
2018
CD2
HIS
246
44.585
62.089
3.912
1.00
61.44


ATOM
2019
CE1
HIS
246
45.683
62.358
2.032
1.00
69.99


ATOM
2020
NE2
HIS
246
45.609
62.759
3.288
1.00
70.61


ATOM
2021
N
ASN
247
40.699
59.050
4.831
1.00
45.02


ATOM
2022
CA
ASN
247
39.407
58.387
4.820
1.00
41.42


ATOM
2023
C
ASN
247
38.445
58.933
3.747
1.00
46.46


ATOM
2024
O
ASN
247
37.230
58.936
3.930
1.00
59.35


ATOM
2025
CB
ASN
247
38.748
58.399
6.206
1.00
48.65


ATOM
2026
CG
ASN
247
37.673
57.326
6.343
1.00
49.46


ATOM
2027
OD1
ASN
247
37.815
56.250
5.800
1.00
34.71


ATOM
2028
ND2
ASN
247
36.602
57.621
7.065
1.00
32.52


ATOM
2029
N
HIS
248
39.003
59.394
2.636
1.00
43.29


ATOM
2030
CA
HIS
248
38.225
59.817
1.479
1.00
37.63


ATOM
2031
C
HIS
248
39.022
59.392
0.266
1.00
32.12


ATOM
2032
O
HIS
248
40.113
58.841
0.402
1.00
33.44


ATOM
2033
CB
HIS
248
38.002
61.334
1.461
1.00
24.97


ATOM
2034
CG
HIS
248
39.263
62.130
1.604
1.00
40.81


ATOM
2035
ND1
HIS
248
39.979
62.602
0.523
1.00
37.83


ATOM
2036
CD2
HIS
248
39.942
62.535
2.702
1.00
40.18


ATOM
2037
CE1
HIS
248
41.038
63.258
0.949
1.00
38.94


ATOM
2038
NE2
HIS
248
41.036
63.240
2.269
1.00
39.85


ATOM
2039
N
SER
249
38.501
59.662
−0.921
1.00
31.92


ATOM
2040
CA
SER
249
39.118
59.158
−2.132
1.00
28.87


ATOM
2041
C
SER
249
39.662
60.283
−2.973
1.00
31.05


ATOM
2042
O
SER
249
39.077
61.355
−3.026
1.00
37.57


ATOM
2043
CB
SER
249
38.081
58.383
−2.967
1.00
34.29


ATOM
2044
OG
SER
249
37.538
57.285
−2.250
1.00
37.64


ATOM
2045
N
ALA
250
40.762
60.012
−3.661
1.00
28.85


ATOM
2046
CA
ALA
250
41.194
60.819
−4.764
1.00
33.19


ATOM
2047
C
ALA
250
40.330
60.391
−5.934
1.00
28.86


ATOM
2048
O
ALA
250
39.959
59.240
−6.049
1.00
34.36


ATOM
2049
CB
ALA
250
42.673
60.554
−5.065
1.00
31.23


ATOM
2050
N
TYR
251
40.036
61.321
−6.826
1.00
33.24


ATOM
2051
CA
TYR
251
39.093
61.057
−7.876
1.00
29.01


ATOM
2052
C
TYR
251
39.442
61.887
−9.119
1.00
33.92


ATOM
2053
O
TYR
251
39.828
63.038
−8.993
1.00
33.45


ATOM
2054
CB
TYR
251
37.699
61.414
−7.347
1.00
32.19


ATOM
2055
CG
TYR
251
36.610
61.299
−8.361
1.00
32.91


ATOM
2056
CD1
TYR
251
36.196
60.054
−8.816
1.00
29.52


ATOM
2057
CD2
TYR
251
35.964
62.429
−8.847
1.00
47.96


ATOM
2058
CE1
TYR
251
35.180
59.933
−9.755
1.00
39.22


ATOM
2059
CE2
TYR
251
34.941
62.319
−9.780
1.00
46.77


ATOM
2060
CZ
TYR
251
34.562
61.066
−10.237
1.00
43.34


ATOM
2061
OH
TYR
251
33.557
60.940
−11.171
1.00
54.07


ATOM
2062
N
ALA
252
39.310
61.309
−10.310
1.00
30.32


ATOM
2063
CA
ALA
252
39.456
62.078
−11.543
1.00
26.10


ATOM
2064
C
ALA
252
38.605
61.518
−12.650
1.00
33.82


ATOM
2065
O
ALA
252
38.286
60.340
−12.647
1.00
33.50


ATOM
2066
CB
ALA
252
40.884
62.096
−11.983
1.00
24.77


ATOM
2067
N
TYR
253
38.232
62.365
−13.604
1.00
23.03


ATOM
2068
CA
TYR
253
37.575
61.855
−14.792
1.00
34.29


ATOM
2069
C
TYR
253
37.791
62.664
−16.044
1.00
34.76


ATOM
2070
O
TYR
253
37.999
63.864
−15.990
1.00
37.04


ATOM
2071
CB
TYR
253
36.078
61.662
−14.551
1.00
39.33


ATOM
2072
CG
TYR
253
35.200
62.866
−14.735
1.00
44.29


ATOM
2073
CD1
TYR
253
35.007
63.439
−15.859
1.00
47.98


ATOM
2074
CD2
TYR
253
34.487
63.346
−13.801
1.00
71.67


ATOM
2075
CE1
TYR
253
34.171
64.535
−16.015
1.00
64.14


ATOM
2076
CE2
TYR
253
33.654
64.444
−13.979
1.00
82.86


ATOM
2077
CZ
TYR
253
33.494
65.031
−15.080
1.00
89.73


ATOM
2078
OH
TYR
253
32.658
66.122
−15.240
1.00
0.58


TER











ATOM
2079
ZN
ZN2 B
258
50.203
59.884
−1.793
1.00
35.76


ATOM
2080
C
ACY B
259
47.704
62.423
−1.932
1.00
65.42


ATOM
2081
O
ACY B
259
47.758
62.761
−3.162
1.00
54.29


ATOM
2082
OXT
ACY B
259
48.249
61.379
−1.482
1.00
52.67


ATOM
2083
CH3
ACY B
259
46.973
63.282
−0.925
1.00
47.10


TER











ENDMDL











MODEL
2










TER











ATOM
1
N
ARG
105
12.838
31.677
−7.753
1.00
37.32


ATOM
2
CA
ARG
105
11.823
30.638
−7.695
1.00
33.40


ATOM
3
C
ARG
105
10.667
30.993
−8.623
1.00
41.58


ATOM
4
O
ARG
105
10.117
32.098
−8.581
1.00
51.52


ATOM
5
CB
ARG
105
11.326
30.437
−6.269
1.00
40.89


ATOM
6
CG
ARG
105
10.462
29.204
−6.112
1.00
58.44


ATOM
7
CD
ARG
105
9.698
29.219
−4.804
1.00
56.99


ATOM
8
NE
ARG
105
9.230
27.881
−4.437
1.00
57.40


ATOM
9
CZ
ARG
105
8.424
27.637
−3.416
1.00
59.07


ATOM
10
NH1
ARG
105
7.994
28.656
−2.684
1.00
44.70


ATOM
11
NH2
ARG
105
8.046
26.390
−3.134
1.00
57.95


ATOM
12
N
LYS
106
10.322
30.047
−9.482
1.00
43.60


ATOM
13
CA
LYS
106
9.176
30.219
−10.367
1.00
57.50


ATOM
14
C
LYS
106
7.853
30.213
−9.582
1.00
51.91


ATOM
15
O
LYS
106
7.597
29.322
−8.776
1.00
64.57


ATOM
16
CB
LYS
106
9.181
29.140
−11.447
1.00
55.51


ATOM
17
CG
LYS
106
8.667
29.611
−12.791
1.00
73.50


ATOM
18
CD
LYS
106
9.636
29.195
−13.884
1.00
89.56


ATOM
19
CE
LYS
106
8.911
28.719
−15.117
1.00
99.85


ATOM
20
NZ
LYS
106
7.842
29.667
−15.491
1.00
0.62


ATOM
21
N
LYS
107
7.039
31.237
−9.816
1.00
54.02


ATOM
22
CA
LYS
107
5.719
31.359
−9.197
1.00
55.18


ATOM
23
C
LYS
107
4.623
31.427
−10.238
1.00
64.44


ATOM
24
O
LYS
107
4.890
31.709
−11.408
1.00
67.36


ATOM
25
CB
LYS
107
5.645
32.591
−8.293
1.00
59.17


ATOM
26
CG
LYS
107
6.076
32.289
−6.871
1.00
78.01


ATOM
27
CD
LYS
107
7.044
33.323
−6.340
1.00
42.27


ATOM
28
CE
LYS
107
6.290
34.470
−5.703
1.00
76.76


ATOM
29
NZ
LYS
107
5.410
34.007
−4.585
1.00
63.95


ATOM
30
N
THR
108
3.391
31.175
−9.794
1.00
52.40


ATOM
31
CA
THR
108
2.216
31.207
−10.661
1.00
54.45


ATOM
32
C
THR
108
1.188
32.249
−10.194
1.00
68.79


ATOM
33
O
THR
108
0.785
32.251
−9.030
1.00
66.08


ATOM
34
CB
THR
108
1.551
29.818
−10.712
1.00
69.12


ATOM
35
OG1
THR
108
2.462
28.875
−11.294
1.00
81.63


ATOM
36
CG2
THR
108
0.254
29.851
−11.508
1.00
60.33


ATOM
37
N
ALA
109
0.768
33.129
−11.103
1.00
59.63


ATOM
38
CA
ALA
109
−0.208
34.158
−10.780
1.00
55.61


ATOM
39
C
ALA
109
−1.539
33.521
−10.335
1.00
71.15


ATOM
40
O
ALA
109
−1.987
32.530
−10.911
1.00
77.38


ATOM
41
CB
ALA
109
−0.414
35.084
−11.970
1.00
64.89


ATOM
42
N
PRO
110
−2.167
34.088
−9.292
1.00
77.07


ATOM
43
CA
PRO
110
−3.301
33.451
−8.607
1.00
60.99


ATOM
44
C
PRO
110
−4.581
33.254
−9.428
1.00
75.83


ATOM
45
O
PRO
110
−5.376
32.386
−9.075
1.00
0.83


ATOM
46
CB
PRO
110
−3.554
34.398
−7.428
1.00
69.05


ATOM
47
CG
PRO
110
−2.920
35.694
−7.844
1.00
73.14


ATOM
48
CD
PRO
110
−1.683
35.259
−8.540
1.00
70.35


ATOM
49
N
VAL
111
−4.796
34.046
−10.475
1.00
76.98


ATOM
50
CA
VAL
111
−5.969
33.867
−11.326
1.00
75.05


ATOM
51
C
VAL
111
−5.617
33.407
−12.751
1.00
83.25


ATOM
52
O
VAL
111
−6.118
32.386
−13.221
1.00
84.58


ATOM
53
CB
VAL
111
−6.859
35.146
−11.386
1.00
80.99


ATOM
54
CG1
VAL
111
−7.935
35.014
−12.477
1.00
89.81


ATOM
55
CG2
VAL
111
−7.508
35.409
−10.036
1.00
90.98


ATOM
56
N
SER
112
−4.763
34.164
−13.431
1.00
87.92


ATOM
57
CA
SER
112
−4.384
33.866
−14.813
1.00
84.89


ATOM
58
C
SER
112
−3.470
32.637
−14.961
1.00
80.23


ATOM
59
O
SER
112
−3.417
32.026
−16.035
1.00
72.07


ATOM
60
CB
SER
112
−3.710
35.086
−15.455
1.00
64.52


ATOM
61
OG
SER
112
−2.361
35.214
−15.020
1.00
67.63


ATOM
62
N
GLY
113
−2.740
32.293
−13.896
1.00
65.30


ATOM
63
CA
GLY
113
−1.815
31.176
−13.934
1.00
57.14


ATOM
64
C
GLY
113
−0.484
31.488
−14.595
1.00
71.26


ATOM
65
O
GLY
113
0.410
30.631
−14.638
1.00
69.71


ATOM
66
N
ILE
114
−0.330
32.710
−15.103
1.00
73.22


ATOM
67
CA
ILE
114
0.934
33.108
−15.738
1.00
69.42


ATOM
68
C
ILE
114
2.125
33.020
−14.779
1.00
68.09


ATOM
69
O
ILE
114
2.077
33.509
−13.650
1.00
76.48


ATOM
70
CB
ILE
114
0.869
34.517
−16.368
1.00
73.91


ATOM
71
CG1
ILE
114
−0.334
34.628
−17.303
1.00
89.92


ATOM
72
CG2
ILE
114
2.138
34.798
−17.152
1.00
63.39


ATOM
73
CD1
ILE
114
−0.366
35.918
−18.089
1.00
0.56


ATOM
74
N
ARG
115
3.193
32.389
−15.248
1.00
61.46


ATOM
75
CA
ARG
115
4.354
32.117
−14.415
1.00
70.33


ATOM
76
C
ARG
115
5.449
33.180
−14.551
1.00
64.45


ATOM
77
O
ARG
115
5.670
33.747
−15.625
1.00
63.87


ATOM
78
CB
ARG
115
4.903
30.716
−14.718
1.00
74.16


ATOM
79
CG
ARG
115
3.876
29.607
−14.512
1.00
97.70


ATOM
80
CD
ARG
115
4.378
28.283
−15.043
1.00
0.22


ATOM
81
NE
ARG
115
5.317
27.638
−14.130
1.00
0.87


ATOM
82
CZ
ARG
115
6.084
26.605
−14.460
1.00
0.60


ATOM
83
NH1
ARG
115
6.032
26.101
−15.685
1.00
0.46


ATOM
84
NH2
ARG
115
6.907
26.077
−13.567
1.00
0.52


ATOM
85
N
SER
116
6.112
33.459
−13.440
1.00
46.36


ATOM
86
CA
SER
116
7.241
34.376
−13.437
1.00
58.82


ATOM
87
C
SER
116
8.116
34.069
−12.239
1.00
52.50


ATOM
88
O
SER
116
7.667
33.429
−11.292
1.00
69.05


ATOM
89
CB
SER
116
6.757
35.822
−13.386
1.00
72.93


ATOM
90
OG
SER
116
6.002
36.061
−12.213
1.00
83.93


ATOM
91
N
LEU
117
9.365
34.518
−12.295
1.00
50.22


ATOM
92
CA
LEU
117
10.334
34.282
−11.237
1.00
47.85


ATOM
93
C
LEU
117
10.235
35.354
−10.178
1.00
44.22


ATOM
94
O
LEU
117
9.949
36.505
−10.480
1.00
49.25


ATOM
95
CB
LEU
117
11.739
34.333
−11.809
1.00
39.11


ATOM
96
CG
LEU
117
12.192
33.272
−12.799
1.00
51.74


ATOM
97
CD1
LEU
117
13.513
33.721
−13.367
1.00
48.04


ATOM
98
CD2
LEU
117
12.331
31.936
−12.105
1.00
46.33


ATOM
99
N
LEU
118
10.475
34.980
−8.930
1.00
47.30


ATOM
100
CA
LEU
118
10.672
35.969
−7.891
1.00
38.20


ATOM
101
C
LEU
118
12.022
35.699
−7.285
1.00
43.03


ATOM
102
O
LEU
118
12.460
34.561
−7.267
1.00
38.94


ATOM
103
CB
LEU
118
9.584
35.909
−6.813
1.00
48.88


ATOM
104
CG
LEU
118
9.555
37.141
−5.883
1.00
59.07


ATOM
105
CD1
LEU
118
8.998
38.351
−6.609
1.00
50.36


ATOM
106
CD2
LEU
118
8.775
36.905
−4.595
1.00
64.70


ATOM
107
N
PRO
142
10.324
38.919
0.478
1.00
35.84


ATOM
108
CA
PRO
142
9.506
40.128
0.335
1.00
26.02


ATOM
109
C
PRO
142
8.056
39.748
0.236
1.00
44.44


ATOM
110
O
PRO
142
7.763
38.820
−0.506
1.00
49.76


ATOM
111
CB
PRO
142
9.947
40.718
−1.014
1.00
38.65


ATOM
112
CG
PRO
142
10.918
39.705
−1.641
1.00
43.31


ATOM
113
CD
PRO
142
10.869
38.445
−0.805
1.00
41.46


ATOM
114
N
VAL
143
7.177
40.433
0.968
1.00
38.87


ATOM
115
CA
VAL
143
5.740
40.182
0.923
1.00
40.60


ATOM
116
C
VAL
143
4.983
41.496
0.993
1.00
45.08


ATOM
117
O
VAL
143
5.574
42.567
1.073
1.00
57.65


ATOM
118
CB
VAL
143
5.270
39.281
2.083
1.00
54.37


ATOM
119
CG1
VAL
143
6.160
38.046
2.195
1.00
39.31


ATOM
120
CG2
VAL
143
5.283
40.049
3.384
1.00
52.85


ATOM
121
N
THR
144
3.670
41.401
0.931
1.00
46.10


ATOM
122
CA
THR
144
2.772
42.549
1.090
1.00
66.56


ATOM
123
C
THR
144
2.120
42.531
2.467
1.00
68.98


ATOM
124
O
THR
144
1.621
41.494
2.916
1.00
67.59


ATOM
125
CB
THR
144
1.608
42.519
0.073
1.00
79.38


ATOM
126
OG1
THR
144
2.116
42.247
−1.237
1.00
90.84


ATOM
127
CG2
THR
144
0.848
43.849
0.073
1.00
84.80


ATOM
128
N
SER
145
2.112
43.673
3.138
1.00
92.35


ATOM
129
CA
SER
145
1.414
43.763
4.403
1.00
92.76


ATOM
130
C
SER
145
0.348
44.831
4.281
1.00
93.23


ATOM
131
O
SER
145
0.560
45.856
3.638
1.00
93.67


ATOM
132
CB
SER
145
2.387
44.082
5.536
1.00
93.44


ATOM
133
OG
SER
145
3.120
45.259
5.253
1.00
94.25


ATOM
134
N
LEU
146
−0.811
44.578
4.875
1.00
93.12


ATOM
135
CA
LEU
146
−1.886
45.558
4.883
1.00
93.52


ATOM
136
C
LEU
146
−2.293
45.854
6.323
1.00
94.04


ATOM
137
O
LEU
146
−2.412
44.943
7.135
1.00
93.70


ATOM
138
CB
LEU
146
−3.069
45.066
4.048
1.00
92.85


ATOM
139
CG
LEU
146
−4.193
46.079
3.829
1.00
93.13


ATOM
140
CD1
LEU
146
−4.655
46.067
2.381
1.00
92.61


ATOM
141
CD2
LEU
146
−5.349
45.825
4.792
1.00
93.10


ATOM
142
N
CYS
147
−2.491
47.129
6.639
1.00
94.85


ATOM
143
CA
CYS
147
−2.704
47.545
8.023
1.00
95.44


ATOM
144
C
CYS
147
−4.145
47.388
8.502
1.00
95.11


ATOM
145
O
CYS
147
−5.049
48.015
7.955
1.00
95.12


ATOM
146
CB
CYS
147
−2.269
49.000
8.216
1.00
96.58


ATOM
147
SG
CYS
147
−2.408
49.540
9.928
1.00
97.39


ATOM
148
N
PRO
148
−4.354
46.570
9.550
1.00
94.79


ATOM
149
CA
PRO
148
−5.687
46.343
10.123
1.00
94.46


ATOM
150
C
PRO
148
−6.311
47.616
10.712
1.00
95.13


ATOM
151
O
PRO
148
−7.500
47.853
10.497
1.00
94.91


ATOM
152
CB
PRO
148
−5.425
45.315
11.233
1.00
94.10


ATOM
153
CG
PRO
148
−4.110
44.703
10.900
1.00
93.98


ATOM
154
CD
PRO
148
−3.320
45.797
10.256
1.00
94.69


ATOM
155
N
CYS
149
−5.524
48.414
11.438
1.00
95.97


ATOM
156
CA
CYS
149
−6.015
49.657
12.031
1.00
96.73


ATOM
157
C
CYS
149
−6.454
50.656
10.961
1.00
97.03


ATOM
158
O
CYS
149
−7.487
51.309
11.100
1.00
97.11


ATOM
159
CB
CYS
149
−4.953
50.289
12.937
1.00
0.39


ATOM
160
SG
CYS
149
−5.365
51.972
13.513
1.00
98.92


ATOM
161
N
SER
150
−5.661
50.766
9.897
1.00
97.14


ATOM
162
CA
SER
150
−5.968
51.645
8.773
1.00
97.32


ATOM
163
C
SER
150
−7.297
51.284
8.122
1.00
96.45


ATOM
164
O
SER
150
−8.116
52.156
7.844
1.00
96.62


ATOM
165
CB
SER
150
−4.853
51.566
7.731
1.00
97.36


ATOM
166
OG
SER
150
−5.142
52.369
6.603
1.00
97.43


ATOM
167
N
LYS
151
−7.494
49.991
7.874
1.00
95.57


ATOM
168
CA
LYS
151
−8.742
49.474
7.308
1.00
94.80


ATOM
169
C
LYS
151
−9.939
49.737
8.227
1.00
94.79


ATOM
170
O
LYS
151
−10.957
50.290
7.802
1.00
94.68


ATOM
171
CB
LYS
151
−8.611
47.970
7.039
1.00
94.03


ATOM
172
CG
LYS
151
−9.884
47.324
6.534
1.00
93.37


ATOM
173
CD
LYS
151
−9.763
45.813
6.462
1.00
92.78


ATOM
174
CE
LYS
151
−11.067
45.208
5.973
1.00
92.30


ATOM
175
NZ
LYS
151
−11.016
43.734
5.900
1.00
91.85


ATOM
176
N
GLU
152
−9.789
49.335
9.486
1.00
94.88


ATOM
177
CA
GLU
152
−10.808
49.477
10.524
1.00
99.88


ATOM
178
C
GLU
152
−11.333
50.906
10.726
1.00
95.41


ATOM
179
O
GLU
152
−12.530
51.111
10.933
1.00
95.13


ATOM
180
CB
GLU
152
−10.246
48.940
11.842
1.00
0.77


ATOM
181
CG
GLU
152
−11.165
49.055
13.038
1.00
0.86


ATOM
182
CD
GLU
152
−10.473
48.628
14.318
1.00
0.48


ATOM
183
OE1
GLU
152
−9.369
49.144
14.596
1.00
0.36


ATOM
184
OE2
GLU
152
−11.028
47.776
15.043
1.00
0.55


ATOM
185
N
ILE
153
−10.440
51.891
10.668
1.00
98.72


ATOM
186
CA
ILE
153
−10.815
53.268
10.987
1.00
0.24


ATOM
187
C
ILE
153
−11.296
54.104
9.797
1.00
97.15


ATOM
188
O
ILE
153
−11.995
55.100
9.988
1.00
97.36


ATOM
189
CB
ILE
153
−9.682
54.036
11.722
1.00
98.13


ATOM
190
CG1
ILE
153
−8.480
54.248
10.800
1.00
98.60


ATOM
191
CG2
ILE
153
−9.289
53.320
13.006
1.00
98.08


ATOM
192
CD1
ILE
153
−7.425
55.156
11.380
1.00
99.90


ATOM
193
N
SER
154
−10.928
53.719
8.579
1.00
96.66


ATOM
194
CA
SER
154
−11.331
54.502
7.411
1.00
96.63


ATOM
195
C
SER
154
−12.547
53.901
6.712
1.00
95.64


ATOM
196
O
SER
154
−12.783
52.693
6.793
1.00
94.99


ATOM
197
CB
SER
154
−10.164
54.702
6.436
1.00
96.93


ATOM
198
OG
SER
154
−9.523
53.481
6.138
1.00
96.38


ATOM
199
N
GLN
155
−13.323
54.750
6.043
1.00
95.57


ATOM
200
CA
GLN
155
−14.556
54.309
5.394
1.00
94.71


ATOM
201
C
GLN
155
−14.265
53.543
4.110
1.00
94.12


ATOM
202
O
GLN
155
−15.114
52.804
3.607
1.00
93.43


ATOM
203
CB
GLN
155
−15.493
55.490
5.126
1.00
0.29


ATOM
204
CG
GLN
155
−14.877
56.622
4.320
1.00
0.53


ATOM
205
CD
GLN
155
−15.866
57.739
4.039
1.00
0.79


ATOM
206
OE1
GLN
155
−17.047
57.492
3.786
1.00
0.94


ATOM
207
NE2
GLN
155
−15.387
58.976
4.080
1.00
0.95


ATOM
208
N
TYR
156
−13.058
53.733
3.586
1.00
94.45


ATOM
209
CA
TYR
156
−12.548
52.923
2.483
1.00
93.90


ATOM
210
C
TYR
156
−11.030
52.991
2.429
1.00
95.21


ATOM
211
O
TYR
156
−10.417
53.882
3.023
1.00
95.22


ATOM
212
CB
TYR
156
−13.154
53.337
1.136
1.00
93.42


ATOM
213
CG
TYR
156
−13.397
54.821
0.969
1.00
96.29


ATOM
214
CD1
TYR
156
−12.340
55.724
0.952
1.00
94.61


ATOM
215
CD2
TYR
156
−14.688
55.316
0.804
1.00
93.79


ATOM
216
CE1
TYR
156
−12.565
57.086
0.793
1.00
0.99


ATOM
217
CE2
TYR
156
−14.923
56.671
0.643
1.00
0.56


ATOM
218
CZ
TYR
156
−13.859
57.554
0.638
1.00
0.71


ATOM
219
OH
TYR
156
−14.088
58.902
0.475
1.00
0.86


ATOM
220
N
GLY
157
−10.430
52.039
1.721
1.00
93.87


ATOM
221
CA
GLY
157
−8.989
51.991
1.574
1.00
94.19


ATOM
222
C
GLY
157
−8.289
51.501
2.826
1.00
94.61


ATOM
223
O
GLY
157
−8.860
51.502
3.914
1.00
94.83


ATOM
224
N
ALA
158
−7.044
51.068
2.658
1.00
94.67


ATOM
225
CA
ALA
158
−6.180
50.692
3.770
1.00
95.10


ATOM
226
C
ALA
158
−4.752
50.803
3.273
1.00
95.37


ATOM
227
O
ALA
158
−4.422
50.276
2.213
1.00
94.74


ATOM
228
CB
ALA
158
−6.473
49.274
4.229
1.00
94.43


ATOM
229
N
HIS
159
−3.899
51.503
4.008
1.00
96.33


ATOM
230
CA
HIS
159
−2.535
51.633
3.536
1.00
96.64


ATOM
231
C
HIS
159
−1.857
50.268
3.619
1.00
95.96


ATOM
232
O
HIS
159
−2.001
49.541
4.602
1.00
95.83


ATOM
233
CB
HIS
159
−1.756
52.732
4.276
1.00
97.98


ATOM
234
CG
HIS
159
−1.206
52.306
5.598
1.00
98.41


ATOM
235
ND1
HIS
159
−0.055
51.560
5.717
1.00
98.28


ATOM
236
CD2
HIS
159
−1.641
52.534
6.855
1.00
98.92


ATOM
237
CE1
HIS
159
0.190
51.333
6.996
1.00
98.69


ATOM
238
NE2
HIS
159
−0.758
51.915
7.704
1.00
99.08


ATOM
239
N
ASN
160
−1.173
49.911
2.541
1.00
95.46


ATOM
240
CA
ASN
160
−0.370
48.706
2.495
1.00
94.85


ATOM
241
C
ASN
160
1.022
49.070
2.001
1.00
95.19


ATOM
242
O
ASN
160
1.264
50.211
1.603
1.00
95.86


ATOM
243
CB
ASN
160
−1.025
47.634
1.613
1.00
93.70


ATOM
244
CG
ASN
160
−1.510
48.175
0.286
1.00
93.37


ATOM
245
OD1
ASN
160
−2.673
48.552
0.146
1.00
93.31


ATOM
246
ND2
ASN
160
−0.626
48.206
−0.699
1.00
93.09


ATOM
247
N
GLN
161
1.941
48.113
2.045
1.00
94.75


ATOM
248
CA
GLN
161
3.318
48.378
1.664
1.00
95.04


ATOM
249
C
GLN
161
4.075
47.079
1.518
1.00
94.19


ATOM
250
O
GLN
161
3.591
46.011
1.909
1.00
93.54


ATOM
251
CB
GLN
161
4.010
49.243
2.717
1.00
96.35


ATOM
252
CG
GLN
161
3.950
48.667
4.121
1.00
96.52


ATOM
253
CD
GLN
161
2.646
48.992
4.833
1.00
96.74


ATOM
254
OE1
GLN
161
2.166
50.125
4.783
1.00
97.47


ATOM
255
NE2
GLN
161
2.069
47.998
5.504
1.00
96.11


ATOM
256
N
ARG
162
5.267
47.176
0.948
1.00
94.19


ATOM
257
CA
ARG
162
6.137
46.029
0.884
1.00
93.45


ATOM
258
C
ARG
162
6.698
45.798
2.278
1.00
94.02


ATOM
259
O
ARG
162
6.983
46.742
3.020
1.00
95.15


ATOM
260
CB
ARG
162
7.251
46.234
−0.145
1.00
93.25


ATOM
261
CG
ARG
162
7.743
44.935
−0.778
1.00
92.02


ATOM
262
CD
ARG
162
8.796
45.188
−1.840
1.00
0.01


ATOM
263
NE
ARG
162
8.231
45.757
−3.059
1.00
91.42


ATOM
264
CZ
ARG
162
8.945
46.401
−3.976
1.00
93.79


ATOM
265
NH1
ARG
162
10.251
46.567
−3.806
1.00
91.78


ATOM
266
NH2
ARG
162
8.353
46.885
−5.059
1.00
91.03


ATOM
267
N
SER
163
6.811
44.524
2.632
1.00
47.09


ATOM
268
CA
SER
163
7.414
44.106
3.886
1.00
43.85


ATOM
269
C
SER
163
8.524
43.090
3.595
1.00
48.09


ATOM
270
O
SER
163
8.397
42.276
2.694
1.00
43.99


ATOM
271
CB
SER
163
6.325
43.515
4.786
1.00
51.94


ATOM
272
OG
SER
163
6.868
42.925
5.949
1.00
81.97


ATOM
273
N
HIS
164
9.624
43.166
4.336
1.00
37.14


ATOM
274
CA
HIS
164
10.651
42.146
4.270
1.00
35.94


ATOM
275
C
HIS
164
10.540
41.311
5.529
1.00
43.89


ATOM
276
O
HIS
164
10.570
41.836
6.643
1.00
42.93


ATOM
277
CB
HIS
164
12.044
42.772
4.153
1.00
49.63


ATOM
278
CG
HIS
164
12.264
43.502
2.857
1.00
73.84


ATOM
279
ND1
HIS
164
13.125
44.582
2.748
1.00
79.92


ATOM
280
CD2
HIS
164
11.732
43.318
1.632
1.00
68.49


ATOM
281
CE1
HIS
164
13.114
45.016
1.501
1.00
79.23


ATOM
282
NE2
HIS
164
12.279
44.271
0.797
1.00
71.70


ATOM
283
N
GLU
178
13.020
26.531
−0.097
1.00
46.89


ATOM
284
CA
GLU
178
11.633
26.683
−0.524
1.00
46.96


ATOM
285
C
GLU
178
10.657
26.422
0.622
1.00
50.17


ATOM
286
O
GLU
178
9.596
27.029
0.679
1.00
54.75


ATOM
287
CB
GLU
178
11.331
25.803
−1.744
1.00
44.87


ATOM
288
CG
GLU
178
11.198
24.305
−1.443
1.00
70.11


ATOM
289
CD
GLU
178
12.503
23.640
−1.010
1.00
73.32


ATOM
290
OE1
GLU
178
13.597
24.158
−1.347
1.00
65.34


ATOM
291
OE2
GLU
178
12.423
22.588
−0.339
1.00
68.91


ATOM
292
N
GLU
179
11.035
25.555
1.554
1.00
41.96


ATOM
293
CA
GLU
179
10.211
25.309
2.743
1.00
45.73


ATOM
294
C
GLU
179
10.130
26.536
3.642
1.00
38.32


ATOM
295
O
GLU
179
9.075
26.827
4.202
1.00
50.81


ATOM
296
CB
GLU
179
10.750
24.149
3.585
1.00
42.76


ATOM
297
CG
GLU
179
10.771
22.791
2.920
1.00
64.32


ATOM
298
CD
GLU
179
11.114
21.682
3.911
1.00
77.87


ATOM
299
OE1
GLU
179
10.229
21.300
4.717
1.00
65.15


ATOM
300
OE2
GLU
179
12.270
21.195
3.887
1.00
62.58


ATOM
301
N
VAL
180
11.254
27.239
3.814
1.00
33.17


ATOM
302
CA
VAL
180
11.223
28.446
4.624
1.00
34.71


ATOM
303
C
VAL
180
10.415
29.555
3.927
1.00
41.23


ATOM
304
O
VAL
180
9.639
30.264
4.553
1.00
37.41


ATOM
305
CB
VAL
180
12.630
28.940
5.018
1.00
41.02


ATOM
306
CG1
VAL
180
12.522
30.238
5.761
1.00
39.39


ATOM
307
CG2
VAL
180
13.319
27.924
5.867
1.00
44.36


ATOM
308
N
ILE
181
10.571
29.676
2.622
1.00
38.53


ATOM
309
CA
ILE
181
9.757
30.616
1.864
1.00
36.63


ATOM
310
C
ILE
181
8.243
30.322
2.002
1.00
51.18


ATOM
311
O
ILE
181
7.433
31.246
2.155
1.00
44.19


ATOM
312
CB
ILE
181
10.171
30.637
0.377
1.00
35.04


ATOM
313
CG1
ILE
181
11.587
31.220
0.239
1.00
31.82


ATOM
314
CG2
ILE
181
9.132
31.388
−0.457
1.00
30.75


ATOM
315
CD1
ILE
181
12.198
31.128
−1.161
1.00
38.43


ATOM
316
N
ASP
182
7.879
29.038
1.964
1.00
40.80


ATOM
317
CA
ASP
182
6.476
28.607
2.095
1.00
38.01


ATOM
318
C
ASP
182
5.902
28.943
3.478
1.00
44.33


ATOM
319
O
ASP
182
4.818
29.503
3.578
1.00
43.19


ATOM
320
CB
ASP
182
6.324
27.116
1.775
1.00
37.87


ATOM
321
CG
ASP
182
6.455
26.819
0.275
1.00
61.34


ATOM
322
OD1
ASP
182
6.189
27.723
−0.553
1.00
62.93


ATOM
323
OD2
ASP
182
6.823
25.677
−0.086
1.00
58.69


ATOM
324
N
TYR
183
6.643
28.636
4.539
1.00
37.99


ATOM
325
CA
TYR
183
6.211
29.031
5.878
1.00
39.70


ATOM
326
C
TYR
183
5.865
30.510
5.957
1.00
52.99


ATOM
327
O
TYR
183
4.984
30.910
6.708
1.00
53.89


ATOM
328
CB
TYR
183
7.279
28.739
6.934
1.00
39.65


ATOM
329
CG
TYR
183
7.415
27.289
7.330
1.00
55.07


ATOM
330
CD1
TYR
183
6.300
26.457
7.413
1.00
60.10


ATOM
331
CD2
TYR
183
8.655
26.756
7.651
1.00
44.43


ATOM
332
CE1
TYR
183
6.421
25.130
7.783
1.00
73.20


ATOM
333
CE2
TYR
183
8.787
25.438
8.028
1.00
60.20


ATOM
334
CZ
TYR
183
7.667
24.625
8.092
1.00
70.47


ATOM
335
OH
TYR
183
7.796
23.310
8.471
1.00
74.31


ATOM
336
N
VAL
184
6.571
31.335
5.201
1.00
40.52


ATOM
337
CA
VAL
184
6.324
32.765
5.295
1.00
41.20


ATOM
338
C
VAL
184
5.186
33.230
4.386
1.00
41.72


ATOM
339
O
VAL
184
4.304
33.957
4.826
1.00
46.40


ATOM
340
CB
VAL
184
7.604
33.624
5.056
1.00
39.23


ATOM
341
CG1
VAL
184
7.230
35.090
4.946
1.00
44.52


ATOM
342
CG2
VAL
184
8.605
33.419
6.185
1.00
37.38


ATOM
343
N
GLU
185
5.203
32.810
3.131
1.00
37.33


ATOM
344
CA
GLU
185
4.293
33.381
2.156
1.00
40.53


ATOM
345
C
GLU
185
2.849
32.980
2.472
1.00
58.15


ATOM
346
O
GLU
185
1.911
33.744
2.225
1.00
63.95


ATOM
347
CB
GLU
185
4.712
32.994
0.739
1.00
37.22


ATOM
348
CG
GLU
185
5.944
33.751
0.253
1.00
56.36


ATOM
349
CD
GLU
185
6.302
33.436
−1.188
1.00
58.49


ATOM
350
OE1
GLU
185
5.913
32.355
−1.673
1.00
54.54


ATOM
351
OE2
GLU
185
6.981
34.265
−1.837
1.00
55.30


ATOM
352
N
THR
186
2.705
31.785
3.040
1.00
58.75


ATOM
353
CA
THR
186
1.442
31.267
3.556
1.00
61.49


ATOM
354
C
THR
186
0.776
32.254
4.505
1.00
55.72


ATOM
355
O
THR
186
−0.429
32.446
4.459
1.00
61.05


ATOM
356
CB
THR
186
1.684
29.940
4.309
1.00
61.83


ATOM
357
OG1
THR
186
1.715
28.860
3.369
1.00
68.11


ATOM
358
CG2
THR
186
0.603
29.690
5.335
1.00
71.42


ATOM
359
N
GLN
187
1.581
32.898
5.339
1.00
77.31


ATOM
360
CA
GLN
187
1.078
33.768
6.393
1.00
77.26


ATOM
361
C
GLN
187
0.934
35.245
6.009
1.00
76.67


ATOM
362
O
GLN
187
0.447
36.044
6.804
1.00
76.96


ATOM
363
CB
GLN
187
2.001
33.671
7.606
1.00
76.96


ATOM
364
CG
GLN
187
2.215
32.274
8.095
1.00
77.69


ATOM
365
CD
GLN
187
0.969
31.712
8.695
1.00
79.02


ATOM
366
OE1
GLN
187
0.067
32.456
9.079
1.00
79.37


ATOM
367
NE2
GLN
187
0.901
30.393
8.786
1.00
80.11


ATOM
368
N
ALA
188
1.372
35.626
4.818
1.00
76.11


ATOM
369
CA
ALA
188
1.357
37.045
4.464
1.00
75.76


ATOM
370
C
ALA
188
−0.046
37.533
4.083
1.00
76.42


ATOM
371
O
ALA
188
−0.874
36.743
3.629
1.00
76.99


ATOM
372
CB
ALA
188
2.356
37.333
3.344
1.00
75.21


ATOM
373
N
SER
189
−0.303
38.828
4.291
1.00
76.61


ATOM
374
CA
SER
189
−1.531
39.468
3.819
1.00
77.40


ATOM
375
C
SER
189
−1.704
39.111
2.359
1.00
79.46


ATOM
376
O
SER
189
−2.789
38.688
1.933
1.00
77.83


ATOM
377
CB
SER
189
−1.461
40.989
3.965
1.00
77.73


ATOM
378
OG
SER
189
−1.641
41.380
5.308
1.00
78.51


ATOM
379
N
CYS
190
−0.625
39.300
1.602
1.00
76.27


ATOM
380
CA
CYS
190
−0.481
38.684
0.291
1.00
76.02


ATOM
381
C
CYS
190
0.975
38.648
−0.155
1.00
75.41


ATOM
382
O
CYS
190
1.801
39.427
0.313
1.00
75.21


ATOM
383
CB
CYS
190
−1.348
39.366
−0.766
1.00
91.77


ATOM
384
SG
CYS
190
−1.875
38.213
−2.080
1.00
98.91


ATOM
385
N
GLN
191
1.288
37.729
−1.057
1.00
75.45


ATOM
386
CA
GLN
191
2.659
37.583
−1.525
1.00
75.31


ATOM
387
C
GLN
191
2.889
38.390
−2.799
1.00
75.40


ATOM
388
O
GLN
191
1.942
38.898
−3.402
1.00
75.47


ATOM
389
CB
GLN
191
2.998
36.104
−1.730
1.00
75.73


ATOM
390
CG
GLN
191
1.820
35.273
−2.190
1.00
76.28


ATOM
391
CD
GLN
191
2.140
33.805
−2.240
1.00
80.40


ATOM
392
OE1
GLN
191
2.850
33.343
−3.133
1.00
77.60


ATOM
393
NE2
GLN
191
1.612
33.055
−1.280
1.00
81.30


ATOM
394
N
LEU
192
4.153
38.514
−3.192
1.00
75.60


ATOM
395
CA
LEU
192
4.528
39.279
−4.379
1.00
75.98


ATOM
396
C
LEU
192
4.661
38.382
−5.608
1.00
76.53


ATOM
397
O
LEU
192
4.959
37.193
−5.494
1.00
76.85


ATOM
398
CB
LEU
192
5.842
40.025
−4.138
1.00
76.39


ATOM
399
CG
LEU
192
5.866
40.989
−2.956
1.00
76.19


ATOM
400
CD1
LEU
192
7.208
41.684
−2.866
1.00
76.97


ATOM
401
CD2
LEU
192
4.755
42.001
−3.089
1.00
76.14


ATOM
402
N
TYR
193
4.425
38.961
−6.781
1.00
76.83


ATOM
403
CA
TYR
193
4.630
38.265
−8.048
1.00
77.60


ATOM
404
C
TYR
193
5.343
39.205
−9.011
1.00
78.30


ATOM
405
O
TYR
193
5.185
40.423
−8.930
1.00
78.11


ATOM
406
CB
TYR
193
3.297
37.800
−8.653
1.00
77.49


ATOM
407
CG
TYR
193
2.511
36.841
−7.782
1.00
77.25


ATOM
408
CD1
TYR
193
2.701
35.469
−7.877
1.00
78.00


ATOM
409
CD2
TYR
193
1.572
37.311
−6.865
1.00
76.63


ATOM
410
CE1
TYR
193
1.984
34.591
−7.083
1.00
78.10


ATOM
411
CE2
TYR
193
0.853
36.439
−6.066
1.00
76.74


ATOM
412
CZ
TYR
193
1.064
35.081
−6.183
1.00
77.46


ATOM
413
OH
TYR
193
0.356
34.211
−5.395
1.00
77.87


ATOM
414
N
GLY
194
6.138
38.640
−9.913
1.00
79.42


ATOM
415
CA
GLY
194
6.809
39.436
−10.923
1.00
80.46


ATOM
416
C
GLY
194
5.856
39.875
−12.024
1.00
80.39


ATOM
417
O
GLY
194
5.953
40.991
−12.538
1.00
90.26


ATOM
418
N
LEU
195
4.923
38.992
−12.375
1.00
80.09


ATOM
419
CA
LEU
195
3.999
39.222
−13.483
1.00
80.50


ATOM
420
C
LEU
195
2.545
39.011
−13.058
1.00
87.63


ATOM
421
O
LEU
195
2.166
37.913
−12.639
1.00
79.12


ATOM
422
CB
LEU
195
4.334
38.281
−14.641
1.00
81.47


ATOM
423
CG
LEU
195
3.877
38.671
−16.046
1.00
82.08


ATOM
424
CD1
LEU
195
4.554
37.777
−17.068
1.00
83.80


ATOM
425
CD2
LEU
195
2.368
38.595
−16.186
1.00
91.32


ATOM
426
N
LEU
196
1.737
40.062
−13.180
1.00
78.72


ATOM
427
CA
LEU
196
0.314
39.992
−12.863
1.00
78.17


ATOM
428
C
LEU
196
−0.524
40.617
−13.969
1.00
78.46


ATOM
429
O
LEU
196
−0.206
41.698
−14.467
1.00
78.70


ATOM
430
CB
LEU
196
0.015
40.713
−11.548
1.00
77.52


ATOM
431
CG
LEU
196
0.682
40.179
−10.285
1.00
77.15


ATOM
432
CD1
LEU
196
0.482
41.140
−9.125
1.00
76.76


ATOM
433
CD2
LEU
196
0.132
38.806
−9.961
1.00
77.20


ATOM
434
N
LYS
197
−1.600
39.937
−14.347
1.00
78.62


ATOM
435
CA
LYS
197
−2.579
40.508
−15.265
1.00
86.92


ATOM
436
C
LYS
197
−3.697
41.188
−14.471
1.00
84.36


ATOM
437
O
LYS
197
−3.750
41.064
−13.250
1.00
78.30


ATOM
438
CB
LYS
197
−3.149
39.426
−16.187
1.00
87.85


ATOM
439
CG
LYS
197
−2.125
38.825
−17.140
1.00
97.73


ATOM
440
CD
LYS
197
−1.043
39.843
−17.481
1.00
0.65


ATOM
441
CE
LYS
197
−0.395
39.561
−18.825
1.00
0.58


ATOM
442
NZ
LYS
197
−1.184
40.154
−19.939
1.00
0.14


ATOM
443
N
ARG
198
−4.582
41.901
−15.165
1.00
79.02


ATOM
444
CA
ARG
198
−5.703
42.597
−14.523
1.00
88.62


ATOM
445
C
ARG
198
−6.465
41.778
−13.475
1.00
90.64


ATOM
446
O
ARG
198
−6.648
42.239
−12.349
1.00
79.37


ATOM
447
CB
ARG
198
−6.685
43.120
−15.572
1.00
95.76


ATOM
448
CG
ARG
198
−6.523
44.581
−15.908
1.00
0.91


ATOM
449
CD
ARG
198
−7.421
44.960
−17.070
1.00
0.94


ATOM
450
NE
ARG
198
−7.901
46.332
−16.953
1.00
0.52


ATOM
451
CZ
ARG
198
−9.089
46.662
−16.457
1.00
0.91


ATOM
452
NH1
ARG
198
−9.919
45.714
−16.039
1.00
0.67


ATOM
453
NH2
ARG
198
−9.448
47.938
−16.381
1.00
0.24


ATOM
454
N
PRO
199
−6.933
40.572
−13.848
1.00
79.78


ATOM
455
CA
PRO
199
−7.649
39.730
−12.883
1.00
80.54


ATOM
456
C
PRO
199
−6.782
39.325
−11.684
1.00
83.44


ATOM
457
O
PRO
199
−7.316
39.187
−10.584
1.00
79.98


ATOM
458
CB
PRO
199
−8.028
38.494
−13.717
1.00
81.05


ATOM
459
CG
PRO
199
−7.080
38.518
−14.878
1.00
84.72


ATOM
460
CD
PRO
199
−6.956
39.969
−15.192
1.00
83.17


ATOM
461
N
ASP
200
−5.479
39.139
−11.899
1.00
78.96


ATOM
462
CA
ASP
200
−4.541
38.786
−10.831
1.00
78.42


ATOM
463
C
ASP
200
−4.407
39.908
−9.822
1.00
79.19


ATOM
464
O
ASP
200
−4.465
39.688
−8.611
1.00
77.91


ATOM
465
CB
ASP
200
−3.155
38.515
−11.407
1.00
78.13


ATOM
466
CG
ASP
200
−3.103
37.261
−12.223
1.00
82.28


ATOM
467
OD1
ASP
200
−3.716
36.265
−11.799
1.00
79.46


ATOM
468
OD2
ASP
200
−2.441
37.268
−13.280
1.00
87.15


ATOM
469
N
GLU
201
−4.191
41.111
−10.343
1.00
77.87


ATOM
470
CA
GLU
201
−4.068
42.309
−9.527
1.00
88.08


ATOM
471
C
GLU
201
−5.343
42.577
−8.731
1.00
82.38


ATOM
472
O
GLU
201
−5.280
42.941
−7.557
1.00
78.63


ATOM
473
CB
GLU
201
−3.725
43.516
−10.397
1.00
78.07


ATOM
474
CG
GLU
201
−3.905
44.822
−9.680
1.00
82.77


ATOM
475
CD
GLU
201
−3.066
45.919
−10.263
1.00
86.32


ATOM
476
OE1
GLU
201
−2.758
45.880
−11.473
1.00
94.84


ATOM
477
OE2
GLU
201
−2.716
46.823
−9.491
1.00
79.42


ATOM
478
N
LYS
202
−6.497
42.401
−9.370
1.00
79.23


ATOM
479
CA
LYS
202
−7.769
42.529
−8.673
1.00
80.32


ATOM
480
C
LYS
202
−7.821
41.552
−7.497
1.00
80.40


ATOM
481
O
LYS
202
−8.153
41.932
−6.374
1.00
80.99


ATOM
482
CB
LYS
202
−8.931
42.277
−9.630
1.00
81.23


ATOM
483
CG
LYS
202
−10.249
42.104
−8.921
1.00
82.74


ATOM
484
CD
LYS
202
−11.374
41.804
−9.885
1.00
83.85


ATOM
485
CE
LYS
202
−12.645
41.477
−9.126
1.00
85.72


ATOM
486
NZ
LYS
202
−13.745
41.122
−10.052
1.00
0.18


ATOM
487
N
TYR
203
−7.468
40.299
−7.767
1.00
80.02


ATOM
488
CA
TYR
203
−7.406
39.253
−6.751
1.00
80.20


ATOM
489
C
TYR
203
−6.462
39.590
−5.590
1.00
79.44


ATOM
490
O
TYR
203
−6.804
39.384
−4.429
1.00
79.97


ATOM
491
CB
TYR
203
−6.983
37.931
−7.399
1.00
80.10


ATOM
492
CG
TYR
203
−6.890
36.768
−6.439
1.00
80.53


ATOM
493
CD1
TYR
203
−7.977
35.925
−6.231
1.00
82.06


ATOM
494
CD2
TYR
203
−5.717
36.512
−5.740
1.00
79.65


ATOM
495
CE1
TYR
203
−7.900
34.862
−5.356
1.00
82.73


ATOM
496
CE2
TYR
203
−5.629
35.449
−4.858
1.00
80.16


ATOM
497
CZ
TYR
203
−6.724
34.626
−4.673
1.00
82.73


ATOM
498
OH
TYR
203
−6.644
33.570
−3.798
1.00
82.87


ATOM
499
N
VAL
204
−5.276
40.101
−5.909
1.00
78.40


ATOM
500
CA
VAL
204
−4.255
40.392
−4.897
1.00
87.71


ATOM
501
C
VAL
204
−4.627
41.607
−4.013
1.00
78.27


ATOM
502
O
VAL
204
−4.436
41.585
−2.795
1.00
78.34


ATOM
503
CB
VAL
204
−2.831
40.525
−5.553
1.00
76.92


ATOM
504
CG1
VAL
204
−2.497
41.967
−5.901
1.00
76.96


ATOM
505
CG2
VAL
204
−1.766
39.942
−4.663
1.00
76.41


ATOM
506
N
THR
205
−5.180
42.647
−4.639
1.00
78.84


ATOM
507
CA
THR
205
−5.709
43.825
−3.945
1.00
79.87


ATOM
508
C
THR
205
−6.769
43.443
−2.913
1.00
81.00


ATOM
509
O
THR
205
−6.703
43.850
−1.752
1.00
81.54


ATOM
510
CB
THR
205
−6.358
44.817
−4.951
1.00
80.67


ATOM
511
OG1
THR
205
−5.397
45.218
−5.934
1.00
79.91


ATOM
512
CG2
THR
205
−6.887
46.051
−4.241
1.00
82.14


ATOM
513
N
GLU
206
−7.746
42.657
−3.361
1.00
81.59


ATOM
514
CA
GLU
206
−8.880
42.244
−2.539
1.00
83.15


ATOM
515
C
GLU
206
−8.497
41.283
−1.417
1.00
82.92


ATOM
516
O
GLU
206
−8.919
41.462
−0.280
1.00
84.05


ATOM
517
CB
GLU
206
−9.965
41.628
−3.420
1.00
84.07


ATOM
518
CG
GLU
206
−10.610
42.636
−4.353
1.00
84.78


ATOM
519
CD
GLU
206
−11.558
42.005
−5.361
1.00
0.42


ATOM
520
OE1
GLU
206
−11.678
40.758
−5.384
1.00
0.46


ATOM
521
OE2
GLU
206
−12.182
42.763
−6.136
1.00
98.72


ATOM
522
N
LYS
207
−7.699
40.269
−1.744
1.00
81.67


ATOM
523
CA
LYS
207
−7.228
39.284
−0.769
1.00
81.45


ATOM
524
C
LYS
207
−6.425
39.920
0.378
1.00
80.95


ATOM
525
O
LYS
207
−6.573
39.531
1.535
1.00
81.57


ATOM
526
CB
LYS
207
−6.403
38.194
−1.471
1.00
82.62


ATOM
527
CG
LYS
207
−5.506
37.363
−0.558
1.00
0.81


ATOM
528
CD
LYS
207
−6.286
36.288
0.185
1.00
0.19


ATOM
529
CE
LYS
207
−5.345
35.303
0.866
1.00
0.78


ATOM
530
NZ
LYS
207
−6.089
34.185
1.511
1.00
0.10


ATOM
531
N
ALA
208
−5.577
40.893
0.054
1.00
80.02


ATOM
532
CA
ALA
208
−4.814
41.607
1.072
1.00
79.80


ATOM
533
C
ALA
208
−5.747
42.421
1.965
1.00
81.46


ATOM
534
O
ALA
208
−5.570
42.469
3.184
1.00
81.88


ATOM
535
CB
ALA
208
−3.767
42.508
0.420
1.00
78.93


ATOM
536
N
TYR
209
−6.740
43.056
1.344
1.00
82.59


ATOM
537
CA
TYR
209
−7.751
43.825
2.067
1.00
84.67


ATOM
538
C
TYR
209
−8.516
42.947
3.062
1.00
85.92


ATOM
539
O
TYR
209
−8.824
43.390
4.166
1.00
87.37


ATOM
540
CB
TYR
209
−8.716
44.510
1.090
1.00
85.82


ATOM
541
CG
TYR
209
−9.615
45.562
1.713
1.00
88.27


ATOM
542
CD1
TYR
209
−9.200
46.883
1.815
1.00
88.83


ATOM
543
CD2
TYR
209
−10.885
45.235
2.184
1.00
90.41


ATOM
544
CE1
TYR
209
−10.016
47.849
2.376
1.00
91.44


ATOM
545
CE2
TYR
209
−11.711
46.194
2.745
1.00
93.05


ATOM
546
CZ
TYR
209
−11.271
47.502
2.838
1.00
94.48


ATOM
547
OH
TYR
209
−12.080
48.472
3.394
1.00
96.54


ATOM
548
N
GLU
210
−8.805
41.705
2.677
1.00
85.61


ATOM
549
CA
GLU
210
−9.536
40.773
3.540
1.00
87.08


ATOM
550
C
GLU
210
−8.646
40.101
4.590
1.00
86.22


ATOM
551
O
GLU
210
−9.142
39.463
5.520
1.00
87.58


ATOM
552
CB
GLU
210
−10.225
39.692
2.704
1.00
87.52


ATOM
553
CG
GLU
210
−11.164
40.223
1.643
1.00
88.48


ATOM
554
CD
GLU
210
−11.399
39.226
0.522
1.00
0.19


ATOM
555
OE1
GLU
210
−10.915
38.075
0.625
1.00
87.54


ATOM
556
OE2
GLU
210
−12.070
39.599
−0.467
1.00
0.58


ATOM
557
N
ASN
211
−7.332
40.238
4.440
1.00
84.16


ATOM
558
CA
ASN
211
−6.404
39.611
5.372
1.00
83.31


ATOM
559
C
ASN
211
−5.378
40.610
5.917
1.00
87.15


ATOM
560
O
ASN
211
−4.177
40.455
5.694
1.00
80.86


ATOM
561
CB
ASN
211
−5.707
38.415
4.705
1.00
89.00


ATOM
562
CG
ASN
211
−4.924
37.566
5.692
1.00
0.16


ATOM
563
OD1
ASN
211
−5.325
37.402
6.848
1.00
0.17


ATOM
564
ND2
ASN
211
−3.799
37.018
5.236
1.00
99.78


ATOM
565
N
PRO
212
−5.853
41.642
6.641
1.00
83.90


ATOM
566
CA
PRO
212
−4.944
42.647
7.205
1.00
83.57


ATOM
567
C
PRO
212
−4.058
42.036
8.296
1.00
82.85


ATOM
568
O
PRO
212
−4.523
41.194
9.062
1.00
83.56


ATOM
569
CB
PRO
212
−5.901
43.685
7.817
1.00
85.91


ATOM
570
CG
PRO
212
−7.256
43.349
7.287
1.00
87.27


ATOM
571
CD
PRO
212
−7.244
41.882
7.051
1.00
86.29


ATOM
572
N
LYS
213
−2.796
42.447
8.356
1.00
81.66


ATOM
573
CA
LYS
213
−1.879
41.932
9.368
1.00
81.02


ATOM
574
C
LYS
213
−0.847
42.956
9.811
1.00
80.90


ATOM
575
O
LYS
213
−0.140
43.545
8.996
1.00
80.25


ATOM
576
CB
LYS
213
−1.174
40.659
8.888
1.00
79.48


ATOM
577
CG
LYS
213
−1.990
39.393
9.075
1.00
80.00


ATOM
578
CD
LYS
213
−1.147
38.133
8.942
1.00
80.38


ATOM
579
CE
LYS
213
−2.048
36.915
8.819
1.00
79.77


ATOM
580
NZ
LYS
213
−1.310
35.630
8.798
1.00
79.21


ATOM
581
N
PHE
214
−0.777
43.159
11.117
1.00
81.78


ATOM
582
CA
PHE
214
0.279
43.940
11.712
1.00
81.81


ATOM
583
C
PHE
214
1.610
43.197
11.578
1.00
80.07


ATOM
584
O
PHE
214
1.666
41.997
11.322
1.00
79.06


ATOM
585
CB
PHE
214
−0.011
44.168
13.199
1.00
83.28


ATOM
586
CG
PHE
214
−1.127
45.146
13.477
1.00
85.59


ATOM
587
CD1
PHE
214
−1.079
46.442
12.980
1.00
88.35


ATOM
588
CD2
PHE
214
−2.205
44.780
14.265
1.00
87.15


ATOM
589
CE1
PHE
214
−2.096
47.345
13.248
1.00
89.02


ATOM
590
CE2
PHE
214
−3.217
45.680
14.536
1.00
89.66


ATOM
591
CZ
PHE
214
−3.163
46.962
14.027
1.00
90.59


ATOM
592
N
VAL
215
2.690
43.924
11.777
1.00
50.17


ATOM
593
CA
VAL
215
4.001
43.320
11.876
1.00
41.74


ATOM
594
C
VAL
215
4.075
42.335
13.059
1.00
47.63


ATOM
595
O
VAL
215
4.762
41.314
12.985
1.00
45.88


ATOM
596
CB
VAL
215
5.105
44.420
11.916
1.00
50.90


ATOM
597
CG1
VAL
215
5.318
44.942
13.325
1.00
44.79


ATOM
598
CG2
VAL
215
6.377
43.890
11.342
1.00
44.27


ATOM
599
N
GLU
216
3.350
42.626
14.133
1.00
38.86


ATOM
600
CA
GLU
216
3.280
41.716
15.267
1.00
45.56


ATOM
601
C
GLU
216
2.645
40.375
14.884
1.00
44.87


ATOM
602
O
GLU
216
3.128
39.318
15.290
1.00
42.87


ATOM
603
CB
GLU
216
2.519
42.347
16.431
1.00
49.41


ATOM
604
CG
GLU
216
3.149
43.630
16.979
1.00
63.76


ATOM
605
CD
GLU
216
2.569
44.897
16.362
1.00
68.55


ATOM
606
OE1
GLU
216
2.046
44.833
15.233
1.00
69.32


ATOM
607
OE2
GLU
216
2.638
45.966
17.008
1.00
75.24


ATOM
608
N
ASP
217
1.582
40.416
14.088
1.00
45.69


ATOM
609
CA
ASP
217
0.909
39.184
13.681
1.00
47.86


ATOM
610
C
ASP
217
1.749
38.388
12.716
1.00
53.47


ATOM
611
O
ASP
217
1.778
37.164
12.780
1.00
61.34


ATOM
612
CB
ASP
217
−0.454
39.468
13.071
1.00
56.10


ATOM
613
CG
ASP
217
−1.341
40.215
14.015
1.00
74.86


ATOM
614
OD1
ASP
217
−1.385
39.803
15.200
1.00
74.32


ATOM
615
OD2
ASP
217
−1.963
41.218
13.578
1.00
80.99


ATOM
616
N
MSE
218
2.447
39.088
11.828
1.00
48.18


ATOM
617
CA
MSE
218
3.335
38.430
10.876
1.00
48.13


ATOM
618
C
MSE
218
4.367
37.519
11.572
1.00
44.35


ATOM
619
O
MSE
218
4.451
36.316
11.295
1.00
44.73


ATOM
620
CB
MSE
218
4.043
39.482
10.013
1.00
67.17


ATOM
621
CG
MSE
218
4.792
38.920
8.792
1.00
78.71


ATOM
622
SE
MSE
218
3.762
37.588
7.728
1.00
0.04


ATOM
623
CE
MSE
218
4.841
37.553
6.111
1.00
0.62


ATOM
624
N
VAL
219
5.153
38.090
12.479
1.00
38.53


ATOM
625
CA
VAL
219
6.170
37.311
13.154
1.00
34.39


ATOM
626
C
VAL
219
5.567
36.223
14.048
1.00
37.70


ATOM
627
O
VAL
219
6.082
35.110
14.104
1.00
41.68


ATOM
628
CB
VAL
219
7.162
38.186
13.952
1.00
44.91


ATOM
629
CG1
VAL
219
7.886
39.169
13.008
1.00
51.70


ATOM
630
CG2
VAL
219
6.458
38.927
15.067
1.00
34.05


ATOM
631
N
ARG
220
4.485
36.532
14.750
1.00
38.89


ATOM
632
CA
ARG
220
3.850
35.506
15.578
1.00
45.03


ATOM
633
C
ARG
220
3.434
34.298
14.742
1.00
49.38


ATOM
634
O
ARG
220
3.726
33.158
15.099
1.00
54.21


ATOM
635
CB
ARG
220
2.675
36.066
16.369
1.00
44.05


ATOM
636
CG
ARG
220
3.115
36.735
17.641
1.00
46.49


ATOM
637
CD
ARG
220
2.038
37.571
18.249
1.00
46.91


ATOM
638
NE
ARG
220
2.410
37.910
19.605
1.00
48.02


ATOM
639
CZ
ARG
220
1.898
38.925
20.279
1.00
55.99


ATOM
640
NH1
ARG
220
0.979
39.703
19.716
1.00
44.26


ATOM
641
NH2
ARG
220
2.305
39.152
21.519
1.00
53.88


ATOM
642
N
ASP
221
2.795
34.555
13.607
1.00
43.66


ATOM
643
CA
ASP
221
2.279
33.478
12.760
1.00
41.62


ATOM
644
C
ASP
221
3.400
32.639
12.130
1.00
50.60


ATOM
645
O
ASP
221
3.305
31.413
12.090
1.00
44.79


ATOM
646
CB
ASP
221
1.350
34.039
11.691
1.00
46.23


ATOM
647
CG
ASP
221
0.080
34.656
12.287
1.00
78.89


ATOM
648
OD1
ASP
221
−0.171
34.471
13.503
1.00
87.03


ATOM
649
OD2
ASP
221
−0.667
35.328
11.545
1.00
63.65


ATOM
650
N
VAL
222
4.471
33.289
11.658
1.00
40.55


ATOM
651
CA
VAL
222
5.611
32.547
11.110
1.00
39.97


ATOM
652
C
VAL
222
6.353
31.754
12.189
1.00
40.25


ATOM
653
O
VAL
222
6.749
30.618
11.969
1.00
43.37


ATOM
654
CB
VAL
222
6.641
33.466
10.424
1.00
40.52


ATOM
655
CG1
VAL
222
7.854
32.663
10.029
1.00
40.76


ATOM
656
CG2
VAL
222
6.044
34.136
9.216
1.00
39.98


ATOM
657
N
ALA
223
6.558
32.365
13.350
1.00
42.74


ATOM
658
CA
ALA
223
7.248
31.712
14.462
1.00
38.34


ATOM
659
C
ALA
223
6.516
30.454
14.951
1.00
48.36


ATOM
660
O
ALA
223
7.137
29.450
15.296
1.00
53.21


ATOM
661
CB
ALA
223
7.427
32.680
15.606
1.00
45.59


ATOM
662
N
THR
224
5.193
30.509
14.972
1.00
44.31


ATOM
663
CA
THR
224
4.393
29.338
15.339
1.00
43.02


ATOM
664
C
THR
224
4.677
28.152
14.414
1.00
45.58


ATOM
665
O
THR
224
4.851
27.031
14.871
1.00
49.95


ATOM
666
CB
THR
224
2.905
29.682
15.329
1.00
42.71


ATOM
667
OG1
THR
224
2.659
30.725
16.279
1.00
53.74


ATOM
668
CG2
THR
224
2.085
28.478
15.691
1.00
50.78


ATOM
669
N
SER
225
4.746
28.420
13.115
1.00
41.80


ATOM
670
CA
SER
225
5.075
27.389
12.142
1.00
51.93


ATOM
671
C
SER
225
6.481
26.839
12.386
1.00
52.55


ATOM
672
O
SER
225
6.711
25.633
12.275
1.00
52.97


ATOM
673
CB
SER
225
4.988
27.922
10.707
1.00
50.08


ATOM
674
OG
SER
225
3.762
28.589
10.467
1.00
64.07


ATOM
675
N
LEU
226
7.430
27.715
12.708
1.00
43.70


ATOM
676
CA
LEU
226
8.819
27.270
12.875
1.00
41.18


ATOM
677
C
LEU
226
9.005
26.498
14.182
1.00
49.52


ATOM
678
O
LEU
226
9.774
25.549
14.249
1.00
48.99


ATOM
679
CB
LEU
226
9.817
28.440
12.812
1.00
35.26


ATOM
680
CG
LEU
226
9.817
29.332
11.577
1.00
41.80


ATOM
681
CD1
LEU
226
10.725
30.527
11.814
1.00
43.92


ATOM
682
CD2
LEU
226
10.225
28.566
10.330
1.00
38.82


ATOM
683
N
ILE
227
8.308
26.932
15.221
1.00
44.77


ATOM
684
CA
ILE
227
8.303
26.231
16.499
1.00
46.88


ATOM
685
C
ILE
227
7.765
24.810
16.353
1.00
51.88


ATOM
686
O
ILE
227
8.255
23.893
17.004
1.00
54.76


ATOM
687
CB
ILE
227
7.422
26.966
17.508
1.00
52.15


ATOM
688
CG1
ILE
227
8.152
28.188
18.052
1.00
53.45


ATOM
689
CG2
ILE
227
7.072
26.084
18.664
1.00
38.00


ATOM
690
CD1
ILE
227
7.233
29.100
18.818
1.00
47.15


ATOM
691
N
ALA
228
6.764
24.635
15.496
1.00
47.59


ATOM
692
CA
ALA
228
6.186
23.315
15.236
1.00
54.10


ATOM
693
C
ALA
228
7.189
22.370
14.557
1.00
63.76


ATOM
694
O
ALA
228
7.263
21.200
14.912
1.00
56.69


ATOM
695
CB
ALA
228
4.914
23.441
14.405
1.00
50.72


ATOM
696
N
ASP
229
7.973
22.882
13.605
1.00
57.62


ATOM
697
CA
ASP
229
8.941
22.062
12.867
1.00
50.20


ATOM
698
C
ASP
229
10.052
21.540
13.783
1.00
53.28


ATOM
699
O
ASP
229
10.788
22.315
14.380
1.00
55.26


ATOM
700
CB
ASP
229
9.523
22.857
11.694
1.00
62.28


ATOM
701
CG
ASP
229
10.189
21.974
10.660
1.00
69.82


ATOM
702
OD1
ASP
229
11.076
21.183
11.048
1.00
51.12


ATOM
703
OD2
ASP
229
9.837
22.081
9.460
1.00
58.63


ATOM
704
N
LYS
230
10.175
20.222
13.888
1.00
58.48


ATOM
705
CA
LYS
230
11.084
19.605
14.857
1.00
53.49


ATOM
706
C
LYS
230
12.558
19.649
14.425
1.00
56.06


ATOM
707
O
LYS
230
13.456
19.411
15.234
1.00
48.87


ATOM
708
CB
LYS
230
10.668
18.153
15.141
1.00
68.41


ATOM
709
CG
LYS
230
9.187
17.952
15.488
1.00
89.06


ATOM
710
CD
LYS
230
8.784
18.696
16.761
1.00
95.42


ATOM
711
CE
LYS
230
7.366
18.329
17.220
1.00
92.94


ATOM
712
NZ
LYS
230
6.250
18.989
16.461
1.00
71.70


ATOM
713
N
ASN
241
8.276
46.463
8.105
1.00
42.17


ATOM
714
CA
ASN
241
7.235
47.043
7.269
1.00
43.83


ATOM
715
C
ASN
241
7.582
48.432
6.808
1.00
51.54


ATOM
716
O
ASN
241
7.578
49.346
7.620
1.00
52.46


ATOM
717
CB
ASN
241
5.955
47.182
8.075
1.00
60.29


ATOM
718
CG
ASN
241
4.965
46.097
7.784
1.00
76.81


ATOM
719
OD1
ASN
241
3.765
46.346
7.766
1.00
80.52


ATOM
720
ND2
ASN
241
5.451
44.883
7.553
1.00
79.98


ATOM
721
N
PHE
242
7.845
48.615
5.517
1.00
50.46


ATOM
722
CA
PHE
242
8.149
49.962
5.009
1.00
66.54


ATOM
723
C
PHE
242
6.862
50.760
4.825
1.00
56.00


ATOM
724
O
PHE
242
6.502
51.144
3.714
1.00
54.94


ATOM
725
CB
PHE
242
8.972
49.901
3.719
1.00
55.87


ATOM
726
CG
PHE
242
10.225
49.076
3.851
1.00
58.67


ATOM
727
CD1
PHE
242
11.398
49.654
4.299
1.00
54.65


ATOM
728
CD2
PHE
242
10.218
47.717
3.547
1.00
54.51


ATOM
729
CE1
PHE
242
12.546
48.899
4.432
1.00
56.56


ATOM
730
CE2
PHE
242
11.360
46.955
3.670
1.00
56.59


ATOM
731
CZ
PHE
242
12.526
47.542
4.116
1.00
56.20


ATOM
732
N
GLU
243
6.186
50.995
5.946
1.00
52.01


ATOM
733
CA
GLU
243
4.849
51.565
5.946
1.00
59.99


ATOM
734
C
GLU
243
4.747
52.767
5.025
1.00
64.49


ATOM
735
O
GLU
243
5.620
53.648
5.016
1.00
57.32


ATOM
736
CB
GLU
243
4.390
51.905
7.366
1.00
67.73


ATOM
737
CG
GLU
243
5.399
52.658
8.197
1.00
99.15


ATOM
738
CD
GLU
243
4.861
52.972
9.575
1.00
0.05


ATOM
739
OE1
GLU
243
5.665
53.302
10.472
1.00
0.86


ATOM
740
OE2
GLU
243
3.627
52.882
9.758
1.00
0.90


ATOM
741
N
SER
244
3.672
52.779
4.243
1.00
53.45


ATOM
742
CA
SER
244
3.523
53.732
3.154
1.00
53.27


ATOM
743
C
SER
244
3.021
55.097
3.625
1.00
55.37


ATOM
744
O
SER
244
2.754
55.969
2.800
1.00
62.63


ATOM
745
CB
SER
244
2.589
53.174
2.074
1.00
58.33


ATOM
746
OG
SER
244
1.267
53.101
2.564
1.00
72.38


ATOM
747
N
ILE
245
2.887
55.278
4.936
1.00
45.75


ATOM
748
CA
ILE
245
2.430
56.553
5.482
1.00
59.96


ATOM
749
C
ILE
245
3.505
57.255
6.314
1.00
53.42


ATOM
750
O
ILE
245
3.319
58.398
6.741
1.00
58.48


ATOM
751
CB
ILE
245
1.131
56.400
6.323
1.00
61.54


ATOM
752
CG1
ILE
245
1.395
55.530
7.550
1.00
63.07


ATOM
753
CG2
ILE
245
−0.003
55.821
5.479
1.00
53.03


ATOM
754
CD1
ILE
245
0.187
55.356
8.429
1.00
78.07


ATOM
755
N
HIS
246
4.619
56.564
6.557
1.00
50.73


ATOM
756
CA
HIS
246
5.736
57.142
7.299
1.00
53.43


ATOM
757
C
HIS
246
7.027
57.010
6.499
1.00
64.72


ATOM
758
O
HIS
246
7.071
56.289
5.509
1.00
62.83


ATOM
759
CB
HIS
246
5.905
56.448
8.646
1.00
49.66


ATOM
760
CG
HIS
246
4.773
56.673
9.600
1.00
65.04


ATOM
761
ND1
HIS
246
4.062
55.635
10.162
1.00
65.95


ATOM
762
CD2
HIS
246
4.238
57.812
10.101
1.00
64.99


ATOM
763
CE1
HIS
246
3.137
56.124
10.969
1.00
77.08


ATOM
764
NE2
HIS
246
3.219
57.443
10.948
1.00
73.91


ATOM
765
N
ASN
247
8.085
57.698
6.923
1.00
56.86


ATOM
766
CA
ASN
247
9.385
57.471
6.291
1.00
52.91


ATOM
767
C
ASN
247
10.353
56.631
7.152
1.00
50.50


ATOM
768
O
ASN
247
11.566
56.789
7.087
1.00
66.31


ATOM
769
CB
ASN
247
10.035
58.774
5.808
1.00
55.98


ATOM
770
CG
ASN
247
11.118
58.521
4.744
1.00
59.98


ATOM
771
OD1
ASN
247
10.980
57.614
3.910
1.00
49.10


ATOM
772
ND2
ASN
247
12.199
59.309
4.779
1.00
48.52


ATOM
773
N
ASN
15
0.218
32.086
22.240
1.00
0.61


ATOM
774
CA
ASN
15
0.186
33.528
22.018
1.00
0.98


ATOM
775
C
ASN
15
1.535
34.235
21.874
1.00
0.70


ATOM
776
O
ASN
15
1.568
35.421
21.554
1.00
0.18


ATOM
777
CB
ASN
15
−0.630
34.213
23.111
1.00
0.60


ATOM
778
CG
ASN
15
−1.982
34.679
22.621
1.00
0.45


ATOM
779
OD1
ASN
15
−2.111
35.186
21.513
1.00
0.18


ATOM
780
ND2
ASN
15
−2.995
34.526
23.454
1.00
0.78


ATOM
781
N
LEU
16
2.627
33.518
22.133
1.00
94.87


ATOM
782
CA
LEU
16
4.002
34.005
21.882
1.00
68.59


ATOM
783
C
LEU
16
4.304
35.483
22.181
1.00
62.20


ATOM
784
O
LEU
16
3.765
36.386
21.537
1.00
47.59


ATOM
785
CB
LEU
16
4.440
33.654
20.458
1.00
58.51


ATOM
786
CG
LEU
16
5.071
32.271
20.284
1.00
71.98


ATOM
787
CD1
LEU
16
4.166
31.193
20.815
1.00
95.09


ATOM
788
CD2
LEU
16
5.387
32.009
18.826
1.00
66.90


ATOM
789
N
PRO
17
5.172
35.727
23.174
1.00
59.11


ATOM
790
CA
PRO
17
5.692
37.076
23.383
1.00
56.32


ATOM
791
C
PRO
17
6.546
37.470
22.172
1.00
53.83


ATOM
792
O
PRO
17
7.090
36.599
21.490
1.00
55.40


ATOM
793
CB
PRO
17
6.593
36.929
24.615
1.00
49.67


ATOM
794
CG
PRO
17
6.313
35.601
25.173
1.00
57.25


ATOM
795
CD
PRO
17
5.780
34.751
24.087
1.00
51.52


ATOM
796
N
ILE
18
6.635
38.764
21.898
1.00
44.93


ATOM
797
CA
ILE
18
7.572
39.262
20.914
1.00
40.29


ATOM
798
C
ILE
18
8.729
39.970
21.625
1.00
42.04


ATOM
799
O
ILE
18
8.521
40.914
22.379
1.00
43.41


ATOM
800
CB
ILE
18
6.889
40.190
19.902
1.00
38.13


ATOM
801
CG1
ILE
18
5.875
39.414
19.075
1.00
45.13


ATOM
802
CG2
ILE
18
7.929
40.830
18.976
1.00
48.42


ATOM
803
CD1
ILE
18
4.852
40.278
18.363
1.00
47.95


ATOM
804
N
TYR
50
9.472
45.033
24.568
1.00
48.54


ATOM
805
CA
TYR
50
8.939
43.690
24.720
1.00
42.54


ATOM
806
C
TYR
50
7.415
43.706
24.665
1.00
38.18


ATOM
807
O
TYR
50
6.765
44.559
25.274
1.00
59.47


ATOM
808
CB
TYR
50
9.421
43.125
26.063
1.00
48.65


ATOM
809
CG
TYR
50
8.877
41.770
26.439
1.00
46.41


ATOM
810
CD1
TYR
50
9.495
40.601
26.002
1.00
48.12


ATOM
811
CD2
TYR
50
7.780
41.656
27.288
1.00
45.63


ATOM
812
CE1
TYR
50
9.005
39.351
26.369
1.00
49.82


ATOM
813
CE2
TYR
50
7.282
40.418
27.658
1.00
64.78


ATOM
814
CZ
TYR
50
7.891
39.267
27.200
1.00
66.95


ATOM
815
OH
TYR
50
7.378
38.038
27.576
1.00
63.72


ATOM
816
N
LEU
51
6.845
42.762
23.925
1.00
41.19


ATOM
817
CA
LEU
51
5.392
42.650
23.852
1.00
45.35


ATOM
818
C
LEU
51
4.944
41.327
24.477
1.00
59.79


ATOM
819
O
LEU
51
5.234
40.259
23.953
1.00
57.86


ATOM
820
CB
LEU
51
4.903
42.786
22.407
1.00
41.63


ATOM
821
CG
LEU
51
3.390
42.955
22.268
1.00
57.45


ATOM
822
CD1
LEU
51
3.024
44.309
22.804
1.00
53.37


ATOM
823
CD2
LEU
51
2.896
42.786
20.817
1.00
46.74


ATOM
824
N
PRO
52
4.252
41.404
25.620
1.00
50.41


ATOM
825
CA
PRO
52
3.698
40.238
26.327
1.00
60.78


ATOM
826
C
PRO
52
2.845
39.355
25.412
1.00
55.59


ATOM
827
O
PRO
52
2.252
39.850
24.464
1.00
45.38


ATOM
828
CB
PRO
52
2.799
40.873
27.398
1.00
51.53


ATOM
829
CG
PRO
52
3.307
42.272
27.560
1.00
54.38


ATOM
830
CD
PRO
52
3.795
42.675
26.204
1.00
47.05


ATOM
831
N
ALA
53
2.787
38.061
25.706
1.00
65.72


ATOM
832
CA
ALA
53
2.046
37.103
24.882
1.00
66.94


ATOM
833
C
ALA
53
0.629
37.544
24.490
1.00
71.17


ATOM
834
O
ALA
53
0.223
37.378
23.341
1.00
71.46


ATOM
835
CB
ALA
53
1.998
35.748
25.564
1.00
66.90


ATOM
836
N
GLU
54
−0.130
38.108
25.424
1.00
75.20


ATOM
837
CA
GLU
54
−1.535
38.373
25.120
1.00
0.50


ATOM
838
C
GLU
54
−1.871
39.834
24.827
1.00
90.42


ATOM
839
O
GLU
54
−3.039
40.201
24.744
1.00
95.12


ATOM
840
CB
GLU
54
−2.466
37.767
26.176
1.00
0.71


ATOM
841
CG
GLU
54
−2.722
38.621
27.397
1.00
0.20


ATOM
842
CD
GLU
54
−3.621
37.920
28.398
1.00
0.17


ATOM
843
OE1
GLU
54
−3.217
36.856
28.908
1.00
0.84


ATOM
844
OE2
GLU
54
−4.728
38.427
28.672
1.00
0.50


ATOM
845
N
GLN
55
−0.845
40.659
24.656
1.00
78.83


ATOM
846
CA
GLN
55
−1.035
41.995
24.104
1.00
68.58


ATOM
847
C
GLN
55
−0.918
41.857
22.589
1.00
58.44


ATOM
848
O
GLN
55
0.009
41.221
22.092
1.00
65.77


ATOM
849
CB
GLN
55
0.011
42.970
24.658
1.00
58.13


ATOM
850
CG
GLN
55
−0.321
44.447
24.474
1.00
67.08


ATOM
851
CD
GLN
55
0.672
45.362
25.189
1.00
79.71


ATOM
852
OE1
GLN
55
1.214
45.006
26.235
1.00
88.70


ATOM
853
NE2
GLN
55
0.912
46.547
24.625
1.00
63.58


ATOM
854
N
LYS
56
−1.859
42.436
21.852
1.00
61.67


ATOM
855
CA
LYS
56
−1.921
42.230
20.410
1.00
65.88


ATOM
856
C
LYS
56
−0.919
43.095
19.648
1.00
73.54


ATOM
857
O
LYS
56
−0.438
42.707
18.578
1.00
73.26


ATOM
858
CB
LYS
56
−3.326
42.503
19.872
1.00
88.06


ATOM
859
CG
LYS
56
−3.413
42.433
18.349
1.00
0.53


ATOM
860
CD
LYS
56
−4.837
42.642
17.847
1.00
0.29


ATOM
861
CE
LYS
56
−5.261
44.101
17.948
1.00
0.17


ATOM
862
NZ
LYS
56
−6.636
44.318
17.419
1.00
0.56


ATOM
863
N
GLY
57
−0.613
44.266
20.205
1.00
63.39


ATOM
864
CA
GLY
57
0.166
45.280
19.520
1.00
60.23


ATOM
865
C
GLY
57
0.775
46.299
20.465
1.00
67.31


ATOM
866
O
GLY
57
0.404
46.397
21.628
1.00
65.95


ATOM
867
N
THR
58
1.747
47.048
19.964
1.00
71.54


ATOM
868
CA
THR
58
2.338
48.127
20.736
1.00
72.16


ATOM
869
C
THR
58
1.743
49.429
20.216
1.00
61.69


ATOM
870
O
THR
58
0.837
49.406
19.387
1.00
61.90


ATOM
871
CB
THR
58
3.879
48.132
20.619
1.00
69.56


ATOM
872
OG1
THR
58
4.439
48.979
21.629
1.00
79.35


ATOM
873
CG2
THR
58
4.316
48.611
19.244
1.00
68.68


ATOM
874
N
HIS
59
2.246
50.562
20.695
1.00
71.58


ATOM
875
CA
HIS
59
1.724
51.852
20.259
1.00
69.19


ATOM
876
C
HIS
59
2.798
52.593
19.487
1.00
62.91


ATOM
877
O
HIS
59
3.641
53.268
20.075
1.00
74.03


ATOM
878
CB
HIS
59
1.246
52.655
21.466
1.00
67.89


ATOM
879
CG
HIS
59
0.355
51.877
22.386
1.00
73.78


ATOM
880
ND1
HIS
59
0.848
51.082
23.406
1.00
79.21


ATOM
881
CD2
HIS
59
−0.988
51.758
22.440
1.00
74.77


ATOM
882
CE1
HIS
59
−0.155
50.522
24.049
1.00
81.43


ATOM
883
NE2
HIS
59
−1.283
50.913
23.482
1.00
82.11


ATOM
884
N
MSE
60
2.754
52.467
18.164
1.00
69.20


ATOM
885
CA
MSE
60
3.889
52.836
17.308
1.00
64.49


ATOM
886
C
MSE
60
4.271
54.314
17.333
1.00
57.44


ATOM
887
O
MSE
60
5.453
54.663
17.259
1.00
55.33


ATOM
888
CB
MSE
60
3.626
52.396
15.866
1.00
68.93


ATOM
889
CG
MSE
60
3.645
50.886
15.670
1.00
88.07


ATOM
890
SE
MSE
60
5.452
50.082
15.726
1.00
90.92


ATOM
891
CE
MSE
60
4.956
48.218
15.352
1.00
91.55


ATOM
892
N
SER
61
3.265
55.177
17.436
1.00
49.65


ATOM
893
CA
SER
61
3.490
56.624
17.384
1.00
52.54


ATOM
894
C
SER
61
4.202
57.193
18.627
1.00
57.67


ATOM
895
O
SER
61
4.824
58.251
18.555
1.00
63.02


ATOM
896
CB
SER
61
2.158
57.360
17.127
1.00
60.89


ATOM
897
OG
SER
61
1.418
57.470
18.313
1.00
63.53


ATOM
898
N
ARG
62
4.112
56.495
19.757
1.00
58.58


ATOM
899
CA
ARG
62
4.804
56.928
20.970
1.00
54.99


ATOM
900
C
ARG
62
6.330
56.959
20.816
1.00
47.98


ATOM
901
O
ARG
62
6.992
57.829
21.385
1.00
58.75


ATOM
902
CB
ARG
62
4.407
56.069
22.169
1.00
48.24


ATOM
903
CG
ARG
62
2.980
56.278
22.584
1.00
54.45


ATOM
904
CD
ARG
62
2.567
55.281
23.663
1.00
53.24


ATOM
905
NE
ARG
62
1.122
55.256
23.836
1.00
68.95


ATOM
906
CZ
ARG
62
0.492
54.612
24.808
1.00
67.76


ATOM
907
NH1
ARG
62
1.186
53.948
25.719
1.00
58.36


ATOM
908
NH2
ARG
62
−0.838
54.642
24.869
1.00
72.93


ATOM
909
N
PHE
63
6.879
56.017
20.049
1.00
45.59


ATOM
910
CA
PHE
63
8.317
55.990
19.800
1.00
51.33


ATOM
911
C
PHE
63
8.788
57.305
19.200
1.00
57.30


ATOM
912
O
PHE
63
9.781
57.895
19.641
1.00
55.44


ATOM
913
CB
PHE
63
8.688
54.840
18.866
1.00
49.40


ATOM
914
CG
PHE
63
8.439
53.498
19.449
1.00
44.13


ATOM
915
CD1
PHE
63
9.233
53.021
20.474
1.00
41.09


ATOM
916
CD2
PHE
63
7.394
52.718
18.995
1.00
50.77


ATOM
917
CE1
PHE
63
9.008
51.782
21.018
1.00
39.25


ATOM
918
CE2
PHE
63
7.161
51.471
19.543
1.00
57.73


ATOM
919
CZ
PHE
63
7.977
50.996
20.546
1.00
41.41


ATOM
920
N
VAL
64
8.065
57.751
18.180
1.00
47.97


ATOM
921
CA
VAL
64
8.375
59.013
17.524
1.00
55.02


ATOM
922
C
VAL
64
8.125
60.197
18.472
1.00
53.37


ATOM
923
O
VAL
64
9.000
61.047
18.648
1.00
45.07


ATOM
924
CB
VAL
64
7.537
59.188
16.238
1.00
69.71


ATOM
925
CG1
VAL
64
7.874
60.505
15.564
1.00
71.34


ATOM
926
CG2
VAL
64
7.770
58.025
15.293
1.00
71.51


ATOM
927
N
ALA
65
6.935
60.248
19.081
1.00
43.65


ATOM
928
CA
ALA
65
6.603
61.331
20.017
1.00
45.85


ATOM
929
C
ALA
65
7.693
61.470
21.074
1.00
55.77


ATOM
930
O
ALA
65
8.040
62.575
21.480
1.00
62.71


ATOM
931
CB
ALA
65
5.251
61.081
20.673
1.00
51.78


ATOM
932
N
ALA
88
8.534
53.005
30.061
1.00
37.50


ATOM
933
CA
ALA
88
7.456
53.494
30.916
1.00
51.61


ATOM
934
C
ALA
88
6.339
54.012
30.058
1.00
56.02


ATOM
935
O
ALA
88
5.185
53.700
30.295
1.00
63.47


ATOM
936
CB
ALA
88
7.943
54.591
31.853
1.00
50.46


ATOM
937
N
LEU
89
6.697
54.794
29.047
1.00
57.64


ATOM
938
CA
LEU
89
5.730
55.400
28.124
1.00
59.78


ATOM
939
C
LEU
89
4.942
54.357
27.315
1.00
53.97


ATOM
940
O
LEU
89
3.743
54.487
27.119
1.00
56.91


ATOM
941
CB
LEU
89
6.451
56.368
27.181
1.00
57.63


ATOM
942
CG
LEU
89
5.628
57.042
26.094
1.00
56.32


ATOM
943
CD1
LEU
89
4.718
58.084
26.716
1.00
42.44


ATOM
944
CD2
LEU
89
6.536
57.676
25.055
1.00
61.18


ATOM
945
N
LEU
90
5.612
53.321
26.837
1.00
54.16


ATOM
946
CA
LEU
90
4.924
52.266
26.111
1.00
63.18


ATOM
947
C
LEU
90
4.361
51.189
27.032
1.00
67.68


ATOM
948
O
LEU
90
3.870
50.160
26.575
1.00
65.17


ATOM
949
CB
LEU
90
5.844
51.657
25.065
1.00
54.20


ATOM
950
CG
LEU
90
5.801
52.540
23.824
1.00
61.73


ATOM
951
CD1
LEU
90
7.055
53.389
23.699
1.00
41.72


ATOM
952
CD2
LEU
90
5.595
51.690
22.601
1.00
75.98


ATOM
953
N
ASP
91
4.432
51.443
28.332
1.00
62.55


ATOM
954
CA
ASP
91
3.870
50.543
29.329
1.00
74.29


ATOM
955
C
ASP
91
4.407
49.124
29.159
1.00
64.93


ATOM
956
O
ASP
91
3.634
48.184
29.035
1.00
56.16


ATOM
957
CB
ASP
91
2.333
50.539
29.242
1.00
84.05


ATOM
958
CG
ASP
91
1.698
51.810
29.813
1.00
0.91


ATOM
959
OD1
ASP
91
2.435
52.672
30.332
1.00
0.11


ATOM
960
OD2
ASP
91
0.456
51.944
29.753
1.00
98.46


ATOM
961
N
SER
92
5.730
48.970
29.156
1.00
57.68


ATOM
962
CA
SER
92
6.349
47.662
28.929
1.00
40.55


ATOM
963
C
SER
92
7.432
47.291
29.952
1.00
52.93


ATOM
964
O
SER
92
7.981
48.149
30.636
1.00
58.12


ATOM
965
CB
SER
92
6.909
47.602
27.509
1.00
47.88


ATOM
966
OG
SER
92
7.480
46.339
27.226
1.00
53.37


ATOM
967
N
ARG
93
7.744
46.001
30.016
1.00
53.73


ATOM
968
CA
ARG
93
8.714
45.427
30.946
1.00
47.19


ATOM
969
C
ARG
93
10.185
45.602
30.507
1.00
61.56


ATOM
970
O
ARG
93
11.110
45.546
31.327
1.00
57.47


ATOM
971
CB
ARG
93
8.417
43.934
31.073
1.00
57.38


ATOM
972
CG
ARG
93
9.157
43.215
32.169
1.00
80.07


ATOM
973
CD
ARG
93
8.893
41.714
32.098
1.00
91.35


ATOM
974
NE
ARG
93
9.315
41.137
30.822
1.00
84.96


ATOM
975
CZ
ARG
93
10.584
40.930
30.474
1.00
95.02


ATOM
976
NH1
ARG
93
11.571
41.262
31.296
1.00
95.51


ATOM
977
NH2
ARG
93
10.872
40.398
29.297
1.00
81.77


ATOM
978
ZN
ZN2
258
−1.421
51.727
9.888
1.00
71.07


ATOM
979
N
LYS
107
7.039
69.054
9.816
1.00
54.02


ATOM
980
CA
LYS
107
5.719
68.932
9.197
1.00
55.18


ATOM
981
C
LYS
107
4.623
68.864
10.238
1.00
64.44


ATOM
982
O
LYS
107
4.890
68.582
11.408
1.00
67.36


ATOM
983
CB
LYS
107
5.645
67.700
8.293
1.00
59.17


ATOM
984
CG
LYS
107
6.076
68.002
6.871
1.00
78.01


ATOM
985
CD
LYS
107
7.044
66.968
6.340
1.00
42.27


ATOM
986
CE
LYS
107
6.290
65.821
5.703
1.00
76.76


ATOM
987
NZ
LYS
107
5.410
66.284
4.585
1.00
63.95


ATOM
988
N
THR
108
3.391
69.116
9.794
1.00
52.40


ATOM
989
CA
THR
108
2.216
69.084
10.661
1.00
54.45


ATOM
990
C
THR
108
1.188
68.042
10.194
1.00
68.79


ATOM
991
O
THR
108
0.785
68.040
9.030
1.00
66.08


ATOM
992
CB
THR
108
1.551
70.473
10.712
1.00
69.12


ATOM
993
OG1
THR
108
2.462
71.416
11.294
1.00
81.63


ATOM
994
CG2
THR
108
0.254
70.440
11.508
1.00
60.33


ATOM
995
N
ALA
109
0.768
67.162
11.103
1.00
59.63


ATOM
996
CA
ALA
109
−0.208
66.133
10.780
1.00
55.61


ATOM
997
C
ALA
109
−1.539
66.770
10.335
1.00
71.15


ATOM
998
O
ALA
109
−1.987
67.761
10.911
1.00
77.38


ATOM
999
CB
ALA
109
−0.414
65.207
11.970
1.00
64.89


ATOM
1000
N
PRO
110
−2.167
66.203
9.292
1.00
77.07


ATOM
1001
CA
PRO
110
−3.301
66.840
8.607
1.00
60.99


ATOM
1002
C
PRO
110
−4.581
67.037
9.428
1.00
75.83


ATOM
1003
O
PRO
110
−5.376
67.905
9.075
1.00
0.83


ATOM
1004
CB
PRO
110
−3.554
65.893
7.428
1.00
69.05


ATOM
1005
CG
PRO
110
−2.920
64.597
7.844
1.00
73.14


ATOM
1006
CD
PRO
110
−1.683
65.032
8.540
1.00
70.35


ATOM
1007
N
VAL
111
−4.796
66.245
10.475
1.00
76.98


ATOM
1008
CA
VAL
111
−5.969
66.424
11.326
1.00
75.05


ATOM
1009
C
VAL
111
−5.617
66.884
12.751
1.00
83.25


ATOM
1010
O
VAL
111
−6.118
67.905
13.221
1.00
84.58


ATOM
1011
CB
VAL
111
−6.859
65.145
11.386
1.00
80.99


ATOM
1012
CG1
VAL
111
−7.935
65.277
12.477
1.00
89.81


ATOM
1013
CG2
VAL
111
−7.508
64.882
10.036
1.00
90.98


ATOM
1014
N
SER
112
−4.763
66.127
13.431
1.00
87.92


ATOM
1015
CA
SER
112
−4.384
66.425
14.813
1.00
84.89


ATOM
1016
C
SER
112
−3.470
67.654
14.961
1.00
80.23


ATOM
1017
O
SER
112
−3.417
68.265
16.035
1.00
72.07


ATOM
1018
CB
SER
112
−3.710
65.205
15.455
1.00
64.52


ATOM
1019
OG
SER
112
−2.361
65.077
15.020
1.00
67.63


ATOM
1020
N
GLY
113
−2.740
67.998
13.896
1.00
65.30


ATOM
1021
CA
GLY
113
−1.815
69.115
13.934
1.00
57.14


ATOM
1022
C
GLY
113
−0.484
68.803
14.595
1.00
71.26


ATOM
1023
O
GLY
113
0.410
69.660
14.638
1.00
69.71


ATOM
1024
N
ILE
114
−0.330
67.581
15.103
1.00
73.22


ATOM
1025
CA
ILE
114
0.934
67.183
15.738
1.00
69.42


ATOM
1026
C
ILE
114
2.125
67.271
14.779
1.00
68.09


ATOM
1027
O
ILE
114
2.077
66.782
13.650
1.00
76.48


ATOM
1028
CB
ILE
114
0.869
65.774
16.368
1.00
73.91


ATOM
1029
CG1
ILE
114
−0.334
65.663
17.303
1.00
89.92


ATOM
1030
CG2
ILE
114
2.138
65.493
17.152
1.00
63.39


ATOM
1031
CD1
ILE
114
−0.366
64.373
18.089
1.00
0.56


ATOM
1032
N
ARG
115
3.193
67.902
15.248
1.00
61.46


ATOM
1033
CA
ARG
115
4.354
68.174
14.415
1.00
70.33


ATOM
1034
C
ARG
115
5.449
67.111
14.551
1.00
64.45


ATOM
1035
O
ARG
115
5.670
66.544
15.625
1.00
63.87


ATOM
1036
CB
ARG
115
4.903
69.575
14.718
1.00
74.16


ATOM
1037
CG
ARG
115
3.876
70.684
14.512
1.00
97.70


ATOM
1038
CD
ARG
115
4.378
72.008
15.043
1.00
0.22


ATOM
1039
NE
ARG
115
5.317
72.653
14.130
1.00
0.87


ATOM
1040
CZ
ARG
115
6.084
73.686
14.460
1.00
0.60


ATOM
1041
NH1
ARG
115
6.032
74.190
15.685
1.00
0.46


ATOM
1042
NH2
ARG
115
6.907
74.214
13.567
1.00
0.52


ATOM
1043
N
SER
116
6.112
66.832
13.440
1.00
46.36


ATOM
1044
CA
SER
116
7.241
65.915
13.437
1.00
58.82


ATOM
1045
C
SER
116
8.116
66.222
12.239
1.00
52.50


ATOM
1046
O
SER
116
7.667
66.862
11.292
1.00
69.05


ATOM
1047
CB
SER
116
6.757
64.469
13.386
1.00
72.93


ATOM
1048
OG
SER
116
6.002
64.230
12.213
1.00
83.93


ATOM
1049
N
PRO
142
10.324
61.372
−0.478
1.00
35.84


ATOM
1050
CA
PRO
142
9.506
60.163
−0.335
1.00
26.02


ATOM
1051
C
PRO
142
8.056
60.543
−0.236
1.00
44.44


ATOM
1052
O
PRO
142
7.763
61.471
0.506
1.00
49.76


ATOM
1053
CB
PRO
142
9.947
59.573
1.014
1.00
38.65


ATOM
1054
CG
PRO
142
10.918
60.586
1.641
1.00
43.31


ATOM
1055
CD
PRO
142
10.869
61.846
0.805
1.00
41.46


ATOM
1056
N
VAL
143
7.177
59.858
−0.968
1.00
38.87


ATOM
1057
CA
VAL
143
5.740
60.109
−0.923
1.00
40.60


ATOM
1058
C
VAL
143
4.983
58.795
−0.993
1.00
45.08


ATOM
1059
O
VAL
143
5.574
57.724
−1.073
1.00
57.65


ATOM
1060
CB
VAL
143
5.270
61.010
−2.083
1.00
54.37


ATOM
1061
CG1
VAL
143
6.160
62.245
−2.195
1.00
39.31


ATOM
1062
CG2
VAL
143
5.283
60.242
−3.384
1.00
52.85


ATOM
1063
N
THR
144
3.670
58.890
−0.931
1.00
46.10


ATOM
1064
CA
THR
144
2.772
57.742
−1.090
1.00
66.56


ATOM
1065
C
THR
144
2.120
57.760
−2.467
1.00
68.98


ATOM
1066
O
THR
144
1.621
58.797
−2.916
1.00
67.59


ATOM
1067
CB
THR
144
1.608
57.772
−0.073
1.00
79.38


ATOM
1068
OG1
THR
144
2.116
58.044
1.237
1.00
90.84


ATOM
1069
CG2
THR
144
0.848
56.442
−0.073
1.00
84.80


ATOM
1070
N
SER
145
2.112
56.618
−3.138
1.00
92.35


ATOM
1071
CA
SER
145
1.414
56.528
−4.403
1.00
92.76


ATOM
1072
C
SER
145
0.348
55.460
−4.281
1.00
93.23


ATOM
1073
O
SER
145
0.560
54.435
−3.638
1.00
93.67


ATOM
1074
CB
SER
145
2.387
56.209
−5.536
1.00
93.44


ATOM
1075
OG
SER
145
3.120
55.032
−5.253
1.00
94.25


ATOM
1076
N
LEU
146
−0.811
55.713
−4.875
1.00
93.12


ATOM
1077
CA
LEU
146
−1.886
54.733
−4.883
1.00
93.52


ATOM
1078
C
LEU
146
−2.293
54.437
−6.323
1.00
94.04


ATOM
1079
O
LEU
146
−2.412
55.348
−7.135
1.00
93.70


ATOM
1080
CB
LEU
146
−3.069
55.225
−4.048
1.00
92.85


ATOM
1081
CG
LEU
146
−4.193
54.212
−3.829
1.00
93.13


ATOM
1082
CD1
LEU
146
−4.655
54.224
−2.381
1.00
92.61


ATOM
1083
CD2
LEU
146
−5.349
54.466
−4.792
1.00
93.10


ATOM
1084
N
CYS
147
−2.491
53.162
−6.639
1.00
94.85


ATOM
1085
CA
CYS
147
−2.704
52.746
−8.023
1.00
95.44


ATOM
1086
C
CYS
147
−4.145
52.903
−8.502
1.00
95.11


ATOM
1087
O
CYS
147
−5.049
52.276
−7.955
1.00
95.12


ATOM
1088
CB
CYS
147
−2.269
51.291
−8.216
1.00
96.58


ATOM
1089
SG
CYS
147
−2.408
50.751
−9.928
1.00
97.39


ATOM
1090
N
PRO
148
−4.354
53.721
−9.550
1.00
94.79


ATOM
1091
CA
PRO
148
−5.687
53.948
−10.123
1.00
94.46


ATOM
1092
C
PRO
148
−6.311
52.675
−10.712
1.00
95.13


ATOM
1093
O
PRO
148
−7.500
52.438
−10.497
1.00
94.91


ATOM
1094
CB
PRO
148
−5.425
54.976
−11.233
1.00
94.10


ATOM
1095
CG
PRO
148
−4.110
55.588
−10.900
1.00
93.98


ATOM
1096
CD
PRO
148
−3.320
54.494
−10.256
1.00
94.69


ATOM
1097
N
CYS
149
−5.524
51.877
−11.438
1.00
95.97


ATOM
1098
CA
CYS
149
−6.015
50.634
−12.031
1.00
96.73


ATOM
1099
C
CYS
149
−6.454
49.635
−10.961
1.00
97.03


ATOM
1100
O
CYS
149
−7.487
48.982
−11.100
1.00
97.11


ATOM
1101
CB
CYS
149
−4.953
50.002
−12.937
1.00
0.39


ATOM
1102
SG
CYS
149
−5.365
48.319
−13.513
1.00
98.92


ATOM
1103
N
SER
150
−5.661
49.525
−9.897
1.00
97.14


ATOM
1104
CA
SER
150
−5.968
48.646
−8.773
1.00
97.32


ATOM
1105
C
SER
150
−7.297
49.007
−8.122
1.00
96.45


ATOM
1106
O
SER
150
−8.116
48.135
−7.844
1.00
96.62


ATOM
1107
CB
SER
150
−4.853
48.725
−7.731
1.00
97.36


ATOM
1108
OG
SER
150
−5.142
47.922
−6.603
1.00
97.43


ATOM
1109
N
LYS
151
−7.494
50.300
−7.874
1.00
95.57


ATOM
1110
CA
LYS
151
−8.742
50.817
−7.308
1.00
94.80


ATOM
1111
C
LYS
151
−9.939
50.554
−8.227
1.00
94.79


ATOM
1112
O
LYS
151
−10.957
50.001
−7.802
1.00
94.68


ATOM
1113
CB
LYS
151
−8.611
52.321
−7.039
1.00
94.03


ATOM
1114
CG
LYS
151
−9.884
52.967
−6.534
1.00
93.37


ATOM
1115
CD
LYS
151
−9.763
54.478
−6.462
1.00
92.78


ATOM
1116
CE
LYS
151
−11.067
55.083
−5.973
1.00
92.30


ATOM
1117
NZ
LYS
151
−11.016
56.557
−5.900
1.00
91.85


ATOM
1118
N
GLU
152
−9.789
50.956
−9.486
1.00
94.88


ATOM
1119
CA
GLU
152
−10.808
50.814
−10.524
1.00
99.88


ATOM
1120
C
GLU
152
−11.333
49.385
−10.726
1.00
95.41


ATOM
1121
O
GLU
152
−12.530
49.180
−10.933
1.00
95.13


ATOM
1122
CB
GLU
152
−10.246
51.351
−11.842
1.00
0.77


ATOM
1123
CG
GLU
152
−11.165
51.236
−13.038
1.00
0.86


ATOM
1124
CD
GLU
152
−10.473
51.663
−14.318
1.00
0.48


ATOM
1125
OE1
GLU
152
−9.369
51.147
−14.596
1.00
0.36


ATOM
1126
OE2
GLU
152
−11.028
52.515
−15.043
1.00
0.55


ATOM
1127
N
ILE
153
−10.440
48.400
−10.668
1.00
98.72


ATOM
1128
CA
ILE
153
−10.815
47.023
−10.987
1.00
0.24


ATOM
1129
C
ILE
153
−11.296
46.187
−9.797
1.00
97.15


ATOM
1130
O
ILE
153
−11.995
45.191
−9.988
1.00
97.36


ATOM
1131
CB
ILE
153
−9.682
46.255
−11.722
1.00
98.13


ATOM
1132
CG1
ILE
153
−8.480
46.043
−10.800
1.00
98.60


ATOM
1133
CG2
ILE
153
−9.289
46.971
−13.006
1.00
98.08


ATOM
1134
CD1
ILE
153
−7.425
45.135
−11.380
1.00
99.90


ATOM
1135
N
SER
154
−10.928
46.572
−8.579
1.00
96.66


ATOM
1136
CA
SER
154
−11.331
45.789
−7.411
1.00
96.63


ATOM
1137
C
SER
154
−12.547
46.390
−6.712
1.00
95.64


ATOM
1138
O
SER
154
−12.783
47.598
−6.793
1.00
94.99


ATOM
1139
CB
SER
154
−10.164
45.589
−6.436
1.00
96.93


ATOM
1140
OG
SER
154
−9.523
46.810
−6.138
1.00
96.38


ATOM
1141
N
GLN
155
−13.323
45.541
−6.043
1.00
95.57


ATOM
1142
CA
GLN
155
−14.556
45.982
−5.394
1.00
94.71


ATOM
1143
C
GLN
155
−14.265
46.748
−4.110
1.00
94.12


ATOM
1144
O
GLN
155
−15.114
47.487
−3.607
1.00
93.43


ATOM
1145
CB
GLN
155
−15.493
44.801
−5.126
1.00
0.29


ATOM
1146
CG
GLN
155
−14.877
43.669
−4.320
1.00
0.53


ATOM
1147
CD
GLN
155
−15.866
42.552
−4.039
1.00
0.79


ATOM
1148
OE1
GLN
155
−17.047
42.799
−3.786
1.00
0.94


ATOM
1149
NE2
GLN
155
−15.387
41.315
−4.080
1.00
0.95


ATOM
1150
N
TYR
156
−13.058
46.558
−3.586
1.00
94.45


ATOM
1151
CA
TYR
156
−12.548
47.368
−2.483
1.00
93.90


ATOM
1152
C
TYR
156
−11.030
47.300
−2.429
1.00
95.21


ATOM
1153
O
TYR
156
−10.417
46.409
−3.023
1.00
95.22


ATOM
1154
CB
TYR
156
−13.154
46.954
−1.136
1.00
93.42


ATOM
1155
CG
TYR
156
−13.397
45.470
−0.969
1.00
96.29


ATOM
1156
CD1
TYR
156
−12.340
44.567
−0.952
1.00
94.61


ATOM
1157
CD2
TYR
156
−14.688
44.975
−0.804
1.00
93.79


ATOM
1158
CE1
TYR
156
−12.565
43.205
−0.793
1.00
0.99


ATOM
1159
CE2
TYR
156
−14.923
43.620
−0.643
1.00
0.56


ATOM
1160
CZ
TYR
156
−13.859
42.737
−0.638
1.00
0.71


ATOM
1161
OH
TYR
156
−14.088
41.389
−0.475
1.00
0.86


ATOM
1162
N
GLY
157
−10.430
48.252
−1.721
1.00
93.87


ATOM
1163
CA
GLY
157
−8.989
48.300
−1.574
1.00
94.19


ATOM
1164
C
GLY
157
−8.289
48.790
−2.826
1.00
94.61


ATOM
1165
O
GLY
157
−8.860
48.789
−3.914
1.00
94.83


ATOM
1166
N
ALA
158
−7.044
49.223
−2.658
1.00
94.67


ATOM
1167
CA
ALA
158
−6.180
49.599
−3.770
1.00
95.10


ATOM
1168
C
ALA
158
−4.752
49.488
−3.273
1.00
95.37


ATOM
1169
O
ALA
158
−4.422
50.015
−2.213
1.00
94.74


ATOM
1170
CB
ALA
158
−6.473
51.017
−4.229
1.00
94.43


ATOM
1171
N
HIS
159
−3.899
48.788
−4.008
1.00
96.33


ATOM
1172
CA
HIS
159
−2.535
48.658
−3.536
1.00
96.64


ATOM
1173
C
HIS
159
−1.857
50.023
−3.619
1.00
95.96


ATOM
1174
O
HIS
159
−2.001
50.750
−4.602
1.00
95.83


ATOM
1175
CB
HIS
159
−1.756
47.559
−4.276
1.00
97.98


ATOM
1176
CG
HIS
159
−1.206
47.985
−5.598
1.00
98.41


ATOM
1177
ND1
HIS
159
−0.055
48.731
−5.717
1.00
98.28


ATOM
1178
CD2
HIS
159
−1.641
47.757
−6.855
1.00
98.92


ATOM
1179
CE1
HIS
159
0.190
48.958
−6.996
1.00
98.69


ATOM
1180
NE2
HIS
159
−0.758
48.376
−7.704
1.00
99.08


ATOM
1181
N
ASN
160
−1.173
50.380
−2.541
1.00
95.46


ATOM
1182
CA
ASN
160
−0.370
51.585
−2.495
1.00
94.85


ATOM
1183
C
ASN
160
1.022
51.221
−2.001
1.00
95.19


ATOM
1184
O
ASN
160
1.264
50.080
−1.603
1.00
95.86


ATOM
1185
CB
ASN
160
−1.025
52.657
−1.613
1.00
93.70


ATOM
1186
CG
ASN
160
−1.510
52.116
−0.286
1.00
93.37


ATOM
1187
OD1
ASN
160
−2.673
51.739
−0.146
1.00
93.31


ATOM
1188
ND2
ASN
160
−0.626
52.085
0.699
1.00
93.09


ATOM
1189
N
GLN
161
1.941
52.178
−2.045
1.00
94.75


ATOM
1190
CA
GLN
161
3.318
51.913
−1.664
1.00
95.04


ATOM
1191
C
GLN
161
4.075
53.212
−1.518
1.00
94.19


ATOM
1192
O
GLN
161
3.591
54.280
−1.909
1.00
93.54


ATOM
1193
CB
GLN
161
4.010
51.048
−2.717
1.00
96.35


ATOM
1194
CG
GLN
161
3.950
51.624
−4.121
1.00
96.52


ATOM
1195
CD
GLN
161
2.646
51.299
−4.833
1.00
96.74


ATOM
1196
OE1
GLN
161
2.166
50.166
−4.783
1.00
97.47


ATOM
1197
NE2
GLN
161
2.069
52.293
−5.504
1.00
96.11


ATOM
1198
N
ARG
162
5.267
53.115
−0.948
1.00
94.19


ATOM
1199
CA
ARG
162
6.137
54.262
−0.884
1.00
93.45


ATOM
1200
C
ARG
162
6.698
54.493
−2.278
1.00
94.02


ATOM
1201
O
ARG
162
6.983
53.549
−3.020
1.00
95.15


ATOM
1202
CB
ARG
162
7.251
54.057
0.145
1.00
93.25


ATOM
1203
CG
ARG
162
7.743
55.356
0.778
1.00
92.02


ATOM
1204
CD
ARG
162
8.796
55.103
1.840
1.00
0.01


ATOM
1205
NE
ARG
162
8.231
54.534
3.059
1.00
91.42


ATOM
1206
CZ
ARG
162
8.945
53.890
3.976
1.00
93.79


ATOM
1207
NH1
ARG
162
10.251
53.724
3.806
1.00
91.78


ATOM
1208
NH2
ARG
162
8.353
53.406
5.059
1.00
91.03


ATOM
1209
N
SER
163
6.811
55.767
−2.632
1.00
47.09


ATOM
1210
CA
SER
163
7.414
56.185
−3.886
1.00
43.85


ATOM
1211
C
SER
163
8.524
57.201
−3.595
1.00
48.09


ATOM
1212
O
SER
163
8.397
58.015
−2.694
1.00
43.99


ATOM
1213
CB
SER
163
6.325
56.776
−4.786
1.00
51.94


ATOM
1214
OG
SER
163
6.868
57.366
−5.949
1.00
81.97


ATOM
1215
N
HIS
164
9.624
57.125
−4.336
1.00
37.14


ATOM
1216
CA
HIS
164
10.651
58.145
−4.270
1.00
35.94


ATOM
1217
C
HIS
164
10.540
58.980
−5.529
1.00
43.89


ATOM
1218
O
HIS
164
10.570
58.455
−6.643
1.00
42.93


ATOM
1219
CB
HIS
164
12.044
57.519
−4.153
1.00
49.63


ATOM
1220
CG
HIS
164
12.264
56.789
−2.857
1.00
73.84


ATOM
1221
ND1
HIS
164
13.125
55.709
−2.748
1.00
79.92


ATOM
1222
CD2
HIS
164
11.732
56.973
−1.632
1.00
68.49


ATOM
1223
CE1
HIS
164
13.114
55.275
−1.501
1.00
79.23


ATOM
1224
NE2
HIS
164
12.279
56.020
−0.797
1.00
71.70


ATOM
1225
N
ILE
181
10.571
70.615
−2.622
1.00
38.53


ATOM
1226
CA
ILE
181
9.757
69.675
−1.864
1.00
36.63


ATOM
1227
C
ILE
181
8.243
69.969
−2.002
1.00
51.18


ATOM
1228
O
ILE
181
7.433
69.045
−2.155
1.00
44.19


ATOM
1229
CB
ILE
181
10.171
69.654
−0.377
1.00
35.04


ATOM
1230
CG1
ILE
181
11.587
69.071
−0.239
1.00
31.82


ATOM
1231
CG2
ILE
181
9.132
68.903
0.457
1.00
30.75


ATOM
1232
CD1
ILE
181
12.198
69.163
1.161
1.00
38.43


ATOM
1233
N
ASP
182
7.879
71.253
−1.964
1.00
40.80


ATOM
1234
CA
ASP
182
6.476
71.684
−2.095
1.00
38.01


ATOM
1235
C
ASP
182
5.902
71.348
−3.478
1.00
44.33


ATOM
1236
O
ASP
182
4.818
70.788
−3.578
1.00
43.19


ATOM
1237
CB
ASP
182
6.324
73.175
−1.775
1.00
37.87


ATOM
1238
CG
ASP
182
6.455
73.472
−0.275
1.00
61.34


ATOM
1239
OD1
ASP
182
6.189
72.568
0.553
1.00
62.93


ATOM
1240
OD2
ASP
182
6.823
74.614
0.086
1.00
58.69


ATOM
1241
N
TYR
183
6.643
71.655
−4.539
1.00
37.99


ATOM
1242
CA
TYR
183
6.211
71.260
−5.878
1.00
39.70


ATOM
1243
C
TYR
183
5.865
69.781
−5.957
1.00
52.99


ATOM
1244
O
TYR
183
4.984
69.381
−6.708
1.00
53.89


ATOM
1245
CB
TYR
183
7.279
71.552
−6.934
1.00
39.65


ATOM
1246
CG
TYR
183
7.415
73.002
−7.330
1.00
55.07


ATOM
1247
CD1
TYR
183
6.300
73.834
−7.413
1.00
60.10


ATOM
1248
CD2
TYR
183
8.655
73.535
−7.651
1.00
44.43


ATOM
1249
CE1
TYR
183
6.421
75.161
−7.783
1.00
73.20


ATOM
1250
CE2
TYR
183
8.787
74.853
−8.028
1.00
60.20


ATOM
1251
CZ
TYR
183
7.667
75.666
−8.092
1.00
70.47


ATOM
1252
OH
TYR
183
7.796
76.981
−8.471
1.00
74.31


ATOM
1253
N
VAL
184
6.571
68.956
−5.201
1.00
40.52


ATOM
1254
CA
VAL
184
6.324
67.526
−5.295
1.00
41.20


ATOM
1255
C
VAL
184
5.186
67.061
−4.386
1.00
41.72


ATOM
1256
O
VAL
184
4.304
66.334
−4.826
1.00
46.40


ATOM
1257
CB
VAL
184
7.604
66.667
−5.056
1.00
39.23


ATOM
1258
CG1
VAL
184
7.230
65.201
−4.946
1.00
44.52


ATOM
1259
CG2
VAL
184
8.605
66.872
−6.185
1.00
37.38


ATOM
1260
N
GLU
185
5.203
67.481
−3.131
1.00
37.33


ATOM
1261
CA
GLU
185
4.293
66.910
−2.156
1.00
40.53


ATOM
1262
C
GLU
185
2.849
67.311
−2.472
1.00
58.15


ATOM
1263
O
GLU
185
1.911
66.547
−2.225
1.00
63.95


ATOM
1264
CB
GLU
185
4.712
67.297
−0.739
1.00
37.22


ATOM
1265
CG
GLU
185
5.944
66.540
−0.253
1.00
56.36


ATOM
1266
CD
GLU
185
6.302
66.855
1.188
1.00
58.49


ATOM
1267
OE1
GLU
185
5.913
67.936
1.673
1.00
54.54


ATOM
1268
OE2
GLU
185
6.981
66.026
1.837
1.00
55.30


ATOM
1269
N
THR
186
2.705
68.506
−3.040
1.00
58.75


ATOM
1270
CA
THR
186
1.442
69.024
−3.556
1.00
61.49


ATOM
1271
C
THR
186
0.776
68.037
−4.505
1.00
55.72


ATOM
1272
O
THR
186
−0.429
67.845
−4.459
1.00
61.05


ATOM
1273
CB
THR
186
1.684
70.351
−4.309
1.00
61.83


ATOM
1274
OG1
THR
186
1.715
71.431
−3.369
1.00
68.11


ATOM
1275
CG2
THR
186
0.603
70.601
−5.335
1.00
71.42


ATOM
1276
N
GLN
187
1.581
67.393
−5.339
1.00
77.31


ATOM
1277
CA
GLN
187
1.078
66.523
−6.393
1.00
77.26


ATOM
1278
C
GLN
187
0.934
65.046
−6.009
1.00
76.67


ATOM
1279
O
GLN
187
0.447
64.247
−6.804
1.00
76.96


ATOM
1280
CB
GLN
187
2.001
66.620
−7.606
1.00
76.96


ATOM
1281
CG
GLN
187
2.215
68.017
−8.095
1.00
77.69


ATOM
1282
CD
GLN
187
0.969
68.579
−8.695
1.00
79.02


ATOM
1283
OE1
GLN
187
0.067
67.835
−9.079
1.00
79.37


ATOM
1284
NE2
GLN
187
0.901
69.898
−8.786
1.00
80.11


ATOM
1285
N
ALA
188
1.372
64.665
−4.818
1.00
76.11


ATOM
1286
CA
ALA
188
1.357
63.246
−4.464
1.00
75.76


ATOM
1287
C
ALA
188
−0.046
62.758
−4.083
1.00
76.42


ATOM
1288
O
ALA
188
−0.874
63.548
−3.629
1.00
76.99


ATOM
1289
CB
ALA
188
2.356
62.958
−3.344
1.00
75.21


ATOM
1290
N
SER
189
−0.303
61.463
−4.291
1.00
76.61


ATOM
1291
CA
SER
189
−1.531
60.823
−3.819
1.00
77.40


ATOM
1292
C
SER
189
−1.704
61.180
−2.359
1.00
79.46


ATOM
1293
O
SER
189
−2.789
61.603
−1.933
1.00
77.83


ATOM
1294
CB
SER
189
−1.461
59.302
−3.965
1.00
77.73


ATOM
1295
OG
SER
189
−1.641
58.911
−5.308
1.00
78.51


ATOM
1296
N
CYS
190
−0.625
60.991
−1.602
1.00
76.27


ATOM
1297
CA
CYS
190
−0.481
61.607
−0.291
1.00
76.02


ATOM
1298
C
CYS
190
0.975
61.643
0.155
1.00
75.41


ATOM
1299
O
CYS
190
1.801
60.864
−0.313
1.00
75.21


ATOM
1300
CB
CYS
190
−1.348
60.925
0.766
1.00
91.77


ATOM
1301
SG
CYS
190
−1.875
62.078
2.080
1.00
98.91


ATOM
1302
N
GLN
191
1.288
62.562
1.057
1.00
75.45


ATOM
1303
CA
GLN
191
2.659
62.708
1.525
1.00
75.31


ATOM
1304
C
GLN
191
2.889
61.901
2.799
1.00
75.40


ATOM
1305
O
GLN
191
1.942
61.393
3.402
1.00
75.47


ATOM
1306
CB
GLN
191
2.998
64.187
1.730
1.00
75.73


ATOM
1307
CG
GLN
191
1.820
65.018
2.190
1.00
76.28


ATOM
1308
CD
GLN
191
2.140
66.486
2.240
1.00
80.40


ATOM
1309
OE1
GLN
191
2.850
66.948
3.133
1.00
77.60


ATOM
1310
NE2
GLN
191
1.612
67.236
1.280
1.00
81.30


ATOM
1311
N
LEU
192
4.153
61.777
3.192
1.00
75.60


ATOM
1312
CA
LEU
192
4.528
61.012
4.379
1.00
75.98


ATOM
1313
C
LEU
192
4.661
61.909
5.608
1.00
76.53


ATOM
1314
O
LEU
192
4.959
63.098
5.494
1.00
76.85


ATOM
1315
CB
LEU
192
5.842
60.266
4.138
1.00
76.39


ATOM
1316
CG
LEU
192
5.866
59.302
2.956
1.00
76.19


ATOM
1317
CD1
LEU
192
7.208
58.607
2.866
1.00
76.97


ATOM
1318
CD2
LEU
192
4.755
58.290
3.089
1.00
76.14


ATOM
1319
N
TYR
193
4.425
61.330
6.781
1.00
76.83


ATOM
1320
CA
TYR
193
4.630
62.026
8.048
1.00
77.60


ATOM
1321
C
TYR
193
5.343
61.086
9.011
1.00
78.30


ATOM
1322
O
TYR
193
5.185
59.868
8.930
1.00
78.11


ATOM
1323
CB
TYR
193
3.297
62.491
8.653
1.00
77.49


ATOM
1324
CG
TYR
193
2.511
63.450
7.782
1.00
77.25


ATOM
1325
CD1
TYR
193
2.701
64.822
7.877
1.00
78.00


ATOM
1326
CD2
TYR
193
1.572
62.980
6.865
1.00
76.63


ATOM
1327
CE1
TYR
193
1.984
65.700
7.083
1.00
78.10


ATOM
1328
CE2
TYR
193
0.853
63.852
6.066
1.00
76.74


ATOM
1329
CZ
TYR
193
1.064
65.210
6.183
1.00
77.46


ATOM
1330
OH
TYR
193
0.356
66.080
5.395
1.00
77.87


ATOM
1331
N
GLY
194
6.138
61.651
9.913
1.00
79.42


ATOM
1332
CA
GLY
194
6.809
60.855
10.923
1.00
80.46


ATOM
1333
C
GLY
194
5.856
60.416
12.024
1.00
80.39


ATOM
1334
O
GLY
194
5.953
59.300
12.538
1.00
90.26


ATOM
1335
N
LEU
195
4.923
61.299
12.375
1.00
80.09


ATOM
1336
CA
LEU
195
3.999
61.069
13.483
1.00
80.50


ATOM
1337
C
LEU
195
2.545
61.280
13.058
1.00
87.63


ATOM
1338
O
LEU
195
2.166
62.378
12.639
1.00
79.12


ATOM
1339
CB
LEU
195
4.334
62.010
14.641
1.00
81.47


ATOM
1340
CG
LEU
195
3.877
61.620
16.046
1.00
82.08


ATOM
1341
CD1
LEU
195
4.554
62.514
17.068
1.00
83.80


ATOM
1342
CD2
LEU
195
2.368
61.696
16.186
1.00
91.32


ATOM
1343
N
LEU
196
1.737
60.229
13.180
1.00
78.72


ATOM
1344
CA
LEU
196
0.314
60.299
12.863
1.00
78.17


ATOM
1345
C
LEU
196
−0.524
59.674
13.969
1.00
78.46


ATOM
1346
O
LEU
196
−0.206
58.593
14.467
1.00
78.70


ATOM
1347
CB
LEU
196
0.015
59.578
11.548
1.00
77.52


ATOM
1348
CG
LEU
196
0.682
60.112
10.285
1.00
77.15


ATOM
1349
CD1
LEU
196
0.482
59.151
9.125
1.00
76.76


ATOM
1350
CD2
LEU
196
0.132
61.485
9.961
1.00
77.20


ATOM
1351
N
LYS
197
−1.600
60.354
14.347
1.00
78.62


ATOM
1352
CA
LYS
197
−2.579
59.783
15.265
1.00
86.92


ATOM
1353
C
LYS
197
−3.697
59.103
14.471
1.00
84.36


ATOM
1354
O
LYS
197
−3.750
59.227
13.250
1.00
78.30


ATOM
1355
CB
LYS
197
−3.149
60.865
16.187
1.00
87.85


ATOM
1356
CG
LYS
197
−2.125
61.466
17.140
1.00
97.73


ATOM
1357
CD
LYS
197
−1.043
60.448
17.481
1.00
0.65


ATOM
1358
CE
LYS
197
−0.395
60.730
18.825
1.00
0.58


ATOM
1359
NZ
LYS
197
−1.184
60.137
19.939
1.00
0.14


ATOM
1360
N
ARG
198
−4.582
58.390
15.165
1.00
79.02


ATOM
1361
CA
ARG
198
−5.703
57.694
14.523
1.00
88.62


ATOM
1362
C
ARG
198
−6.465
58.513
13.475
1.00
90.64


ATOM
1363
O
ARG
198
−6.648
58.052
12.349
1.00
79.37


ATOM
1364
CB
ARG
198
−6.685
57.171
15.572
1.00
95.76


ATOM
1365
CG
ARG
198
−6.523
55.710
15.908
1.00
0.91


ATOM
1366
CD
ARG
198
−7.421
55.331
17.070
1.00
0.94


ATOM
1367
NE
ARG
198
−7.901
53.959
16.953
1.00
0.52


ATOM
1368
CZ
ARG
198
−9.089
53.629
16.457
1.00
0.91


ATOM
1369
NH1
ARG
198
−9.919
54.577
16.039
1.00
0.67


ATOM
1370
NH2
ARG
198
−9.448
52.353
16.381
1.00
0.24


ATOM
1371
N
PRO
199
−6.933
59.719
13.848
1.00
79.78


ATOM
1372
CA
PRO
199
−7.649
60.561
12.883
1.00
80.54


ATOM
1373
C
PRO
199
−6.782
60.966
11.684
1.00
83.44


ATOM
1374
O
PRO
199
−7.316
61.104
10.584
1.00
79.98


ATOM
1375
CB
PRO
199
−8.028
61.797
13.717
1.00
81.05


ATOM
1376
CG
PRO
199
−7.080
61.773
14.878
1.00
84.72


ATOM
1377
CD
PRO
199
−6.956
60.322
15.192
1.00
83.17


ATOM
1378
N
ASP
200
−5.479
61.152
11.899
1.00
78.96


ATOM
1379
CA
ASP
200
−4.541
61.505
10.831
1.00
78.42


ATOM
1380
C
ASP
200
−4.407
60.383
9.822
1.00
79.19


ATOM
1381
O
ASP
200
−4.465
60.603
8.611
1.00
77.91


ATOM
1382
CB
ASP
200
−3.155
61.776
11.407
1.00
78.13


ATOM
1383
CG
ASP
200
−3.103
63.030
12.223
1.00
82.28


ATOM
1384
OD1
ASP
200
−3.716
64.026
11.799
1.00
79.46


ATOM
1385
OD2
ASP
200
−2.441
63.023
13.280
1.00
87.15


ATOM
1386
N
GLU
201
−4.191
59.180
10.343
1.00
77.87


ATOM
1387
CA
GLU
201
−4.068
57.982
9.527
1.00
88.08


ATOM
1388
C
GLU
201
−5.343
57.714
8.731
1.00
82.38


ATOM
1389
O
GLU
201
−5.280
57.350
7.557
1.00
78.63


ATOM
1390
CB
GLU
201
−3.725
56.775
10.397
1.00
78.07


ATOM
1391
CG
GLU
201
−3.905
55.469
9.680
1.00
82.77


ATOM
1392
CD
GLU
201
−3.066
54.372
10.263
1.00
86.32


ATOM
1393
OE1
GLU
201
−2.758
54.411
11.473
1.00
94.84


ATOM
1394
OE2
GLU
201
−2.716
53.468
9.491
1.00
79.42


ATOM
1395
N
LYS
202
−6.497
57.890
9.370
1.00
79.23


ATOM
1396
CA
LYS
202
−7.769
57.762
8.673
1.00
80.32


ATOM
1397
C
LYS
202
−7.821
58.739
7.497
1.00
80.40


ATOM
1398
O
LYS
202
−8.153
58.359
6.374
1.00
80.99


ATOM
1399
CB
LYS
202
−8.931
58.014
9.630
1.00
81.23


ATOM
1400
CG
LYS
202
−10.249
58.187
8.921
1.00
82.74


ATOM
1401
CD
LYS
202
−11.374
58.487
9.885
1.00
83.85


ATOM
1402
CE
LYS
202
−12.645
58.814
9.126
1.00
85.72


ATOM
1403
NZ
LYS
202
−13.745
59.169
10.052
1.00
0.18


ATOM
1404
N
TYR
203
−7.468
59.992
7.767
1.00
80.02


ATOM
1405
CA
TYR
203
−7.406
61.038
6.751
1.00
80.20


ATOM
1406
C
TYR
203
−6.462
60.701
5.590
1.00
79.44


ATOM
1407
O
TYR
203
−6.804
60.907
4.429
1.00
79.97


ATOM
1408
CB
TYR
203
−6.983
62.360
7.399
1.00
80.10


ATOM
1409
CG
TYR
203
−6.890
63.523
6.439
1.00
80.53


ATOM
1410
CD1
TYR
203
−7.977
64.366
6.231
1.00
82.06


ATOM
1411
CD2
TYR
203
−5.717
63.779
5.740
1.00
79.65


ATOM
1412
CE1
TYR
203
−7.900
65.429
5.356
1.00
82.73


ATOM
1413
CE2
TYR
203
−5.629
64.842
4.858
1.00
80.16


ATOM
1414
CZ
TYR
203
−6.724
65.665
4.673
1.00
82.73


ATOM
1415
OH
TYR
203
−6.644
66.721
3.798
1.00
82.87


ATOM
1416
N
VAL
204
−5.276
60.190
5.909
1.00
78.40


ATOM
1417
CA
VAL
204
−4.255
59.899
4.897
1.00
87.71


ATOM
1418
C
VAL
204
−4.627
58.684
4.013
1.00
78.27


ATOM
1419
O
VAL
204
−4.436
58.706
2.795
1.00
78.34


ATOM
1420
CB
VAL
204
−2.831
59.766
5.553
1.00
76.92


ATOM
1421
CG1
VAL
204
−2.497
58.324
5.901
1.00
76.96


ATOM
1422
CG2
VAL
204
−1.766
60.349
4.663
1.00
76.41


ATOM
1423
N
THR
205
−5.180
57.644
4.639
1.00
78.84


ATOM
1424
CA
THR
205
−5.709
56.466
3.945
1.00
79.87


ATOM
1425
C
THR
205
−6.769
56.848
2.913
1.00
81.00


ATOM
1426
O
THR
205
−6.703
56.441
1.752
1.00
81.54


ATOM
1427
CB
THR
205
−6.358
55.474
4.951
1.00
80.67


ATOM
1428
OG1
THR
205
−5.397
55.073
5.934
1.00
79.91


ATOM
1429
CG2
THR
205
−6.887
54.240
4.241
1.00
82.14


ATOM
1430
N
GLU
206
−7.746
57.634
3.361
1.00
81.59


ATOM
1431
CA
GLU
206
−8.880
58.047
2.539
1.00
83.15


ATOM
1432
C
GLU
206
−8.497
59.008
1.417
1.00
82.92


ATOM
1433
O
GLU
206
−8.919
58.829
0.280
1.00
84.05


ATOM
1434
CB
GLU
206
−9.965
58.663
3.420
1.00
84.07


ATOM
1435
CG
GLU
206
−10.610
57.655
4.353
1.00
84.78


ATOM
1436
CD
GLU
206
−11.558
58.286
5.361
1.00
0.42


ATOM
1437
OE1
GLU
206
−11.678
59.533
5.384
1.00
0.46


ATOM
1438
OE2
GLU
206
−12.182
57.528
6.136
1.00
98.72


ATOM
1439
N
LYS
207
−7.699
60.022
1.744
1.00
81.67


ATOM
1440
CA
LYS
207
−7.228
61.007
0.769
1.00
81.45


ATOM
1441
C
LYS
207
−6.425
60.371
−0.378
1.00
80.95


ATOM
1442
O
LYS
207
−6.573
60.760
−1.535
1.00
81.57


ATOM
1443
CB
LYS
207
−6.403
62.097
1.471
1.00
82.62


ATOM
1444
CG
LYS
207
−5.506
62.928
0.558
1.00
0.81


ATOM
1445
CD
LYS
207
−6.286
64.003
−0.185
1.00
0.19


ATOM
1446
CE
LYS
207
−5.345
64.988
−0.866
1.00
0.78


ATOM
1447
NZ
LYS
207
−6.089
66.106
−1.511
1.00
0.10


ATOM
1448
N
ALA
208
−5.577
59.398
−0.054
1.00
80.02


ATOM
1449
CA
ALA
208
−4.814
58.684
−1.072
1.00
79.80


ATOM
1450
C
ALA
208
−5.747
57.870
−1.965
1.00
81.46


ATOM
1451
O
ALA
208
−5.570
57.822
−3.184
1.00
81.88


ATOM
1452
CB
ALA
208
−3.767
57.783
−0.420
1.00
78.93


ATOM
1453
N
TYR
209
−6.740
57.235
−1.344
1.00
82.59


ATOM
1454
CA
TYR
209
−7.751
56.466
−2.067
1.00
84.67


ATOM
1455
C
TYR
209
−8.516
57.344
−3.062
1.00
85.92


ATOM
1456
O
TYR
209
−8.824
56.901
−4.166
1.00
87.37


ATOM
1457
CB
TYR
209
−8.716
55.781
−1.090
1.00
85.82


ATOM
1458
CG
TYR
209
−9.615
54.729
−1.713
1.00
88.27


ATOM
1459
CD1
TYR
209
−9.200
53.408
−1.815
1.00
88.83


ATOM
1460
CD2
TYR
209
−10.885
55.056
−2.184
1.00
90.41


ATOM
1461
CE1
TYR
209
−10.016
52.442
−2.376
1.00
91.44


ATOM
1462
CE2
TYR
209
−11.711
54.097
−2.745
1.00
93.05


ATOM
1463
CZ
TYR
209
−11.271
52.789
−2.838
1.00
94.48


ATOM
1464
OH
TYR
209
−12.080
51.819
−3.394
1.00
96.54


ATOM
1465
N
GLU
210
−8.805
58.586
−2.677
1.00
85.61


ATOM
1466
CA
GLU
210
−9.536
59.518
−3.540
1.00
87.08


ATOM
1467
C
GLU
210
−8.646
60.190
−4.590
1.00
86.22


ATOM
1468
O
GLU
210
−9.142
60.828
−5.520
1.00
87.58


ATOM
1469
CB
GLU
210
−10.225
60.599
−2.704
1.00
87.52


ATOM
1470
CG
GLU
210
−11.164
60.068
−1.643
1.00
88.48


ATOM
1471
CD
GLU
210
−11.399
61.065
−0.522
1.00
0.19


ATOM
1472
OE1
GLU
210
−10.915
62.216
−0.625
1.00
87.54


ATOM
1473
OE2
GLU
210
−12.070
60.692
0.467
1.00
0.58


ATOM
1474
N
ASN
211
−7.332
60.053
−4.440
1.00
84.16


ATOM
1475
CA
ASN
211
−6.404
60.680
−5.372
1.00
83.31


ATOM
1476
C
ASN
211
−5.378
59.681
−5.917
1.00
87.15


ATOM
1477
O
ASN
211
−4.177
59.836
−5.694
1.00
80.86


ATOM
1478
CB
ASN
211
−5.707
61.876
−4.705
1.00
89.00


ATOM
1479
CG
ASN
211
−4.924
62.725
−5.692
1.00
0.16


ATOM
1480
OD1
ASN
211
−5.325
62.889
−6.848
1.00
0.17


ATOM
1481
ND2
ASN
211
−3.799
63.273
−5.236
1.00
99.78


ATOM
1482
N
PRO
212
−5.853
58.649
−6.641
1.00
83.90


ATOM
1483
CA
PRO
212
−4.944
57.644
−7.205
1.00
83.57


ATOM
1484
C
PRO
212
−4.058
58.255
−8.296
1.00
82.85


ATOM
1485
O
PRO
212
−4.523
59.097
−9.062
1.00
83.56


ATOM
1486
CB
PRO
212
−5.901
56.606
−7.817
1.00
85.91


ATOM
1487
CG
PRO
212
−7.256
56.942
−7.287
1.00
87.27


ATOM
1488
CD
PRO
212
−7.244
58.409
−7.051
1.00
86.29


ATOM
1489
N
LYS
213
−2.796
57.844
−8.356
1.00
81.66


ATOM
1490
CA
LYS
213
−1.879
58.359
−9.368
1.00
81.02


ATOM
1491
C
LYS
213
−0.847
57.335
−9.811
1.00
80.90


ATOM
1492
O
LYS
213
−0.140
56.746
−8.996
1.00
80.25


ATOM
1493
CB
LYS
213
−1.174
59.632
−8.888
1.00
79.48


ATOM
1494
CG
LYS
213
−1.990
60.898
−9.075
1.00
80.00


ATOM
1495
CD
LYS
213
−1.147
62.158
−8.942
1.00
80.38


ATOM
1496
CE
LYS
213
−2.048
63.376
−8.819
1.00
79.77


ATOM
1497
NZ
LYS
213
−1.310
64.661
−8.798
1.00
79.21


ATOM
1498
N
PHE
214
−0.777
57.132
−11.117
1.00
81.78


ATOM
1499
CA
PHE
214
0.279
56.351
−11.712
1.00
81.81


ATOM
1500
C
PHE
214
1.610
57.094
−11.578
1.00
80.07


ATOM
1501
O
PHE
214
1.666
58.294
−11.322
1.00
79.06


ATOM
1502
CB
PHE
214
−0.011
56.123
−13.199
1.00
83.28


ATOM
1503
CG
PHE
214
−1.127
55.145
−13.477
1.00
85.59


ATOM
1504
CD1
PHE
214
−1.079
53.849
−12.980
1.00
88.35


ATOM
1505
CD2
PHE
214
−2.205
55.511
−14.265
1.00
87.15


ATOM
1506
CE1
PHE
214
−2.096
52.946
−13.248
1.00
89.02


ATOM
1507
CE2
PHE
214
−3.217
54.611
−14.536
1.00
89.66


ATOM
1508
CZ
PHE
214
−3.163
53.329
−14.027
1.00
90.59


ATOM
1509
N
VAL
215
2.690
56.367
−11.777
1.00
50.17


ATOM
1510
CA
VAL
215
4.001
56.971
−11.876
1.00
41.74


ATOM
1511
C
VAL
215
4.075
57.956
−13.059
1.00
47.63


ATOM
1512
O
VAL
215
4.762
58.977
−12.985
1.00
45.88


ATOM
1513
CB
VAL
215
5.105
55.871
−11.916
1.00
50.90


ATOM
1514
CG1
VAL
215
5.318
55.349
−13.325
1.00
44.79


ATOM
1515
CG2
VAL
215
6.377
56.401
−11.342
1.00
44.27


ATOM
1516
N
GLU
216
3.350
57.665
−14.133
1.00
38.86


ATOM
1517
CA
GLU
216
3.280
58.575
−15.267
1.00
45.56


ATOM
1518
C
GLU
216
2.645
59.916
−14.884
1.00
44.87


ATOM
1519
O
GLU
216
3.128
60.973
−15.290
1.00
42.87


ATOM
1520
CB
GLU
216
2.519
57.944
−16.431
1.00
49.41


ATOM
1521
CG
GLU
216
3.149
56.661
−16.979
1.00
63.76


ATOM
1522
CD
GLU
216
2.569
55.394
−16.362
1.00
68.55


ATOM
1523
OE1
GLU
216
2.046
55.458
−15.233
1.00
69.32


ATOM
1524
OE2
GLU
216
2.638
54.325
−17.008
1.00
75.24


ATOM
1525
N
ASP
217
1.582
59.875
−14.088
1.00
45.69


ATOM
1526
CA
ASP
217
0.909
61.107
−13.681
1.00
47.86


ATOM
1527
C
ASP
217
1.749
61.903
−12.716
1.00
53.47


ATOM
1528
O
ASP
217
1.778
63.127
−12.780
1.00
61.34


ATOM
1529
CB
ASP
217
−0.454
60.823
−13.071
1.00
56.10


ATOM
1530
CG
ASP
217
−1.341
60.076
−14.015
1.00
74.86


ATOM
1531
OD1
ASP
217
−1.385
60.488
−15.200
1.00
74.32


ATOM
1532
OD2
ASP
217
−1.963
59.073
−13.578
1.00
80.99


ATOM
1533
N
MSE
218
2.447
61.203
−11.828
1.00
48.18


ATOM
1534
CA
MSE
218
3.335
61.861
−10.876
1.00
48.13


ATOM
1535
C
MSE
218
4.367
62.772
−11.572
1.00
44.35


ATOM
1536
O
MSE
218
4.451
63.975
−11.295
1.00
44.73


ATOM
1537
CB
MSE
218
4.043
60.809
−10.013
1.00
67.17


ATOM
1538
CG
MSE
218
4.792
61.371
−8.792
1.00
78.71


ATOM
1539
SE
MSE
218
3.762
62.703
−7.728
1.00
0.04


ATOM
1540
CE
MSE
218
4.841
62.738
−6.111
1.00
0.62


ATOM
1541
N
VAL
219
5.153
62.201
−12.479
1.00
38.53


ATOM
1542
CA
VAL
219
6.170
62.980
−13.154
1.00
34.39


ATOM
1543
C
VAL
219
5.567
64.068
−14.048
1.00
37.70


ATOM
1544
O
VAL
219
6.082
65.181
−14.104
1.00
41.68


ATOM
1545
CB
VAL
219
7.162
62.105
−13.952
1.00
44.91


ATOM
1546
CG1
VAL
219
7.886
61.122
−13.008
1.00
51.70


ATOM
1547
CG2
VAL
219
6.458
61.364
−15.067
1.00
34.05


ATOM
1548
N
ARG
220
4.485
63.759
−14.750
1.00
38.89


ATOM
1549
CA
ARG
220
3.850
64.785
−15.578
1.00
45.03


ATOM
1550
C
ARG
220
3.434
65.993
−14.742
1.00
49.38


ATOM
1551
O
ARG
220
3.726
67.133
−15.099
1.00
54.21


ATOM
1552
CB
ARG
220
2.675
64.225
−16.369
1.00
44.05


ATOM
1553
CG
ARG
220
3.115
63.556
−17.641
1.00
46.49


ATOM
1554
CD
ARG
220
2.038
62.720
−18.249
1.00
46.91


ATOM
1555
NE
ARG
220
2.410
62.381
−19.605
1.00
48.02


ATOM
1556
CZ
ARG
220
1.898
61.366
−20.279
1.00
55.99


ATOM
1557
NH1
ARG
220
0.979
60.588
−19.716
1.00
44.26


ATOM
1558
NH2
ARG
220
2.305
61.139
−21.519
1.00
53.88


ATOM
1559
N
ASP
221
2.795
65.736
−13.607
1.00
43.66


ATOM
1560
CA
ASP
221
2.279
66.813
−12.760
1.00
41.62


ATOM
1561
C
ASP
221
3.400
67.652
−12.130
1.00
50.60


ATOM
1562
O
ASP
221
3.305
68.878
−12.090
1.00
44.79


ATOM
1563
CB
ASP
221
1.350
66.252
−11.691
1.00
46.23


ATOM
1564
CG
ASP
221
0.080
65.635
−12.287
1.00
78.89


ATOM
1565
OD1
ASP
221
−0.171
65.820
−13.503
1.00
87.03


ATOM
1566
OD2
ASP
221
−0.667
64.963
−11.545
1.00
63.65


ATOM
1567
N
VAL
222
4.471
67.002
−11.658
1.00
40.55


ATOM
1568
CA
VAL
222
5.611
67.744
−11.110
1.00
39.97


ATOM
1569
C
VAL
222
6.353
68.537
−12.189
1.00
40.25


ATOM
1570
O
VAL
222
6.749
69.673
−11.969
1.00
43.37


ATOM
1571
CB
VAL
222
6.641
66.825
−10.424
1.00
40.52


ATOM
1572
CG1
VAL
222
7.854
67.628
−10.029
1.00
40.76


ATOM
1573
CG2
VAL
222
6.044
66.155
−9.216
1.00
39.98


ATOM
1574
N
ALA
223
6.558
67.926
−13.350
1.00
42.74


ATOM
1575
CA
ALA
223
7.248
68.579
−14.462
1.00
38.34


ATOM
1576
C
ALA
223
6.516
69.837
−14.951
1.00
48.36


ATOM
1577
O
ALA
223
7.137
70.841
−15.296
1.00
53.21


ATOM
1578
CB
ALA
223
7.427
67.611
−15.606
1.00
45.59


ATOM
1579
N
THR
224
5.193
69.782
−14.972
1.00
44.31


ATOM
1580
CA
THR
224
4.393
70.953
−15.339
1.00
43.02


ATOM
1581
C
THR
224
4.677
72.139
−14.414
1.00
45.58


ATOM
1582
O
THR
224
4.851
73.260
−14.871
1.00
49.95


ATOM
1583
CB
THR
224
2.905
70.609
−15.329
1.00
42.71


ATOM
1584
OG1
THR
224
2.659
69.566
−16.279
1.00
53.74


ATOM
1585
CG2
THR
224
2.085
71.813
−15.691
1.00
50.78


ATOM
1586
N
SER
225
4.746
71.871
−13.115
1.00
41.80


ATOM
1587
CA
SER
225
5.075
72.902
−12.142
1.00
51.93


ATOM
1588
C
SER
225
6.481
73.452
−12.386
1.00
52.55


ATOM
1589
O
SER
225
6.711
74.658
−12.275
1.00
52.97


ATOM
1590
CB
SER
225
4.988
72.369
−10.707
1.00
50.08


ATOM
1591
OG
SER
225
3.762
71.702
−10.467
1.00
64.07


ATOM
1592
N
LEU
226
7.430
72.576
−12.708
1.00
43.70


ATOM
1593
CA
LEU
226
8.819
73.021
−12.875
1.00
41.18


ATOM
1594
C
LEU
226
9.005
73.793
−14.182
1.00
49.52


ATOM
1595
O
LEU
226
9.774
74.742
−14.249
1.00
48.99


ATOM
1596
CB
LEU
226
9.817
71.851
−12.812
1.00
35.26


ATOM
1597
CG
LEU
226
9.817
70.959
−11.577
1.00
41.80


ATOM
1598
CD1
LEU
226
10.725
69.764
−11.814
1.00
43.92


ATOM
1599
CD2
LEU
226
10.225
71.725
−10.330
1.00
38.82


ATOM
1600
N
ILE
227
8.308
73.359
−15.221
1.00
44.77


ATOM
1601
CA
ILE
227
8.303
74.060
−16.499
1.00
46.88


ATOM
1602
C
ILE
227
7.765
75.481
−16.353
1.00
51.88


ATOM
1603
O
ILE
227
8.255
76.398
−17.004
1.00
54.76


ATOM
1604
CB
ILE
227
7.422
73.325
−17.508
1.00
52.15


ATOM
1605
CG1
ILE
227
8.152
72.103
−18.052
1.00
53.45


ATOM
1606
CG2
ILE
227
7.072
74.207
−18.664
1.00
38.00


ATOM
1607
CD1
ILE
227
7.233
71.191
−18.818
1.00
47.15


ATOM
1608
N
ALA
228
6.764
75.656
−15.496
1.00
47.59


ATOM
1609
CA
ALA
228
6.186
76.976
−15.236
1.00
54.10


ATOM
1610
C
ALA
228
7.189
77.921
−14.557
1.00
63.76


ATOM
1611
O
ALA
228
7.263
79.091
−14.912
1.00
56.69


ATOM
1612
CB
ALA
228
4.914
76.850
−14.405
1.00
50.72


ATOM
1613
N
ASP
229
7.973
77.409
−13.605
1.00
57.62


ATOM
1614
CA
ASP
229
8.941
78.229
−12.867
1.00
50.20


ATOM
1615
C
ASP
229
10.052
78.751
−13.783
1.00
53.28


ATOM
1616
O
ASP
229
10.788
77.976
−14.380
1.00
55.26


ATOM
1617
CB
ASP
229
9.523
77.434
−11.694
1.00
62.28


ATOM
1618
CG
ASP
229
10.189
78.317
−10.660
1.00
69.82


ATOM
1619
OD1
ASP
229
11.076
79.108
−11.048
1.00
51.12


ATOM
1620
OD2
ASP
229
9.837
78.210
−9.460
1.00
58.63


ATOM
1621
N
SER
239
10.316
59.328
−11.007
1.00
33.39


ATOM
1622
CA
SER
239
9.562
58.739
−9.923
1.00
37.64


ATOM
1623
C
SER
239
9.770
57.242
−9.947
1.00
41.56


ATOM
1624
O
SER
239
9.717
56.603
−10.999
1.00
40.74


ATOM
1625
CB
SER
239
8.066
59.088
−10.029
1.00
39.51


ATOM
1626
OG
SER
239
7.366
58.601
−8.908
1.00
58.13


ATOM
1627
N
GLU
240
10.028
56.688
−8.776
1.00
36.90


ATOM
1628
CA
GLU
240
10.164
55.253
−8.629
1.00
41.05


ATOM
1629
C
GLU
240
9.111
54.745
−7.646
1.00
48.68


ATOM
1630
O
GLU
240
9.046
55.178
−6.505
1.00
44.51


ATOM
1631
CB
GLU
240
11.576
54.886
−8.176
1.00
33.98


ATOM
1632
CG
GLU
240
11.769
53.430
−7.885
1.00
52.95


ATOM
1633
CD
GLU
240
13.243
53.043
−7.821
1.00
68.35


ATOM
1634
OE1
GLU
240
14.102
53.961
−7.886
1.00
66.40


ATOM
1635
OE2
GLU
240
13.531
51.822
−7.709
1.00
63.55


ATOM
1636
N
ASN
241
8.276
53.828
−8.105
1.00
42.17


ATOM
1637
CA
ASN
241
7.235
53.248
−7.269
1.00
43.83


ATOM
1638
C
ASN
241
7.582
51.859
−6.808
1.00
51.54


ATOM
1639
O
ASN
241
7.578
50.945
−7.620
1.00
52.46


ATOM
1640
CB
ASN
241
5.955
53.109
−8.075
1.00
60.29


ATOM
1641
CG
ASN
241
4.965
54.194
−7.784
1.00
76.81


ATOM
1642
OD1
ASN
241
3.765
53.945
−7.766
1.00
80.52


ATOM
1643
ND2
ASN
241
5.451
55.408
−7.553
1.00
79.98


ATOM
1644
N
PHE
242
7.845
51.676
−5.517
1.00
50.46


ATOM
1645
CA
PHE
242
8.149
50.329
−5.009
1.00
66.54


ATOM
1646
C
PHE
242
6.862
49.531
−4.825
1.00
56.00


ATOM
1647
O
PHE
242
6.502
49.147
−3.714
1.00
54.94


ATOM
1648
CB
PHE
242
8.972
50.390
−3.719
1.00
55.87


ATOM
1649
CG
PHE
242
10.225
51.215
−3.851
1.00
58.67


ATOM
1650
CD1
PHE
242
11.398
50.637
−4.299
1.00
54.65


ATOM
1651
CD2
PHE
242
10.218
52.574
−3.547
1.00
54.51


ATOM
1652
CE1
PHE
242
12.546
51.392
−4.432
1.00
56.56


ATOM
1653
CE2
PHE
242
11.360
53.336
−3.670
1.00
56.59


ATOM
1654
CZ
PHE
242
12.526
52.749
−4.116
1.00
56.20


ATOM
1655
N
GLU
243
6.186
49.296
−5.946
1.00
52.01


ATOM
1656
CA
GLU
243
4.849
48.726
−5.946
1.00
59.99


ATOM
1657
C
GLU
243
4.747
47.524
−5.025
1.00
64.49


ATOM
1658
O
GLU
243
5.620
46.643
−5.016
1.00
57.32


ATOM
1659
CB
GLU
243
4.390
48.386
−7.366
1.00
67.73


ATOM
1660
CG
GLU
243
5.399
47.633
−8.197
1.00
99.15


ATOM
1661
CD
GLU
243
4.861
47.319
−9.575
1.00
0.05


ATOM
1662
OE1
GLU
243
5.665
46.989
−10.472
1.00
0.86


ATOM
1663
OE2
GLU
243
3.627
47.409
−9.758
1.00
0.90


ATOM
1664
N
SER
244
3.672
47.512
−4.243
1.00
53.45


ATOM
1665
CA
SER
244
3.523
46.559
−3.154
1.00
53.27


ATOM
1666
C
SER
244
3.021
45.194
−3.625
1.00
55.37


ATOM
1667
O
SER
244
2.754
44.322
−2.800
1.00
62.63


ATOM
1668
CB
SER
244
2.589
47.117
−2.074
1.00
58.33


ATOM
1669
OG
SER
244
1.267
47.190
−2.564
1.00
72.38


ATOM
1670
N
ILE
245
2.887
45.013
−4.936
1.00
45.75


ATOM
1671
CA
ILE
245
2.430
43.738
−5.482
1.00
59.96


ATOM
1672
C
ILE
245
3.505
43.036
−6.314
1.00
53.42


ATOM
1673
O
ILE
245
3.319
41.893
−6.741
1.00
58.48


ATOM
1674
CB
ILE
245
1.131
43.891
−6.323
1.00
61.54


ATOM
1675
CG1
ILE
245
1.395
44.761
−7.550
1.00
63.07


ATOM
1676
CG2
ILE
245
−0.003
44.470
−5.479
1.00
53.03


ATOM
1677
CD1
ILE
245
0.187
44.935
−8.429
1.00
78.07


ATOM
1678
N
HIS
246
4.619
43.727
−6.557
1.00
50.73


ATOM
1679
CA
HIS
246
5.736
43.149
−7.299
1.00
53.43


ATOM
1680
C
HIS
246
7.027
43.281
−6.499
1.00
64.72


ATOM
1681
O
HIS
246
7.071
44.002
−5.509
1.00
62.83


ATOM
1682
CB
HIS
246
5.905
43.843
−8.646
1.00
49.66


ATOM
1683
CG
HIS
246
4.773
43.618
−9.600
1.00
65.04


ATOM
1684
ND1
HIS
246
4.062
44.656
−10.162
1.00
65.95


ATOM
1685
CD2
HIS
246
4.238
42.479
−10.101
1.00
64.99


ATOM
1686
CE1
HIS
246
3.137
44.167
−10.969
1.00
77.08


ATOM
1687
NE2
HIS
246
3.219
42.848
−10.948
1.00
73.91


ATOM
1688
N
ASN
247
8.085
42.593
−6.923
1.00
56.86


ATOM
1689
CA
ASN
247
9.385
42.820
−6.291
1.00
52.91


ATOM
1690
C
ASN
247
10.353
43.660
−7.152
1.00
50.50


ATOM
1691
O
ASN
247
11.566
43.502
−7.087
1.00
66.31


ATOM
1692
CB
ASN
247
10.035
41.517
−5.808
1.00
55.98


ATOM
1693
CG
ASN
247
11.118
41.770
−4.744
1.00
59.98


ATOM
1694
OD1
ASN
247
10.980
42.677
−3.910
1.00
49.10


ATOM
1695
ND2
ASN
247
12.199
40.982
−4.779
1.00
48.52


ATOM
1696
N
HIS
248
9.792
44.549
−7.958
1.00
46.70


ATOM
1697
CA
HIS
248
10.564
45.518
−8.725
1.00
45.58


ATOM
1698
C
HIS
248
9.778
46.828
−8.712
1.00
43.64


ATOM
1699
O
HIS
248
8.694
46.904
−8.130
1.00
49.26


ATOM
1700
CB
HIS
248
10.789
45.045
−10.163
1.00
35.45


ATOM
1701
CG
HIS
248
9.529
44.638
−10.863
1.00
47.99


ATOM
1702
ND1
HIS
248
8.828
45.493
−11.689
1.00
54.22


ATOM
1703
CD2
HIS
248
8.830
43.477
−10.842
1.00
46.59


ATOM
1704
CE1
HIS
248
7.758
44.875
−12.150
1.00
51.61


ATOM
1705
NE2
HIS
248
7.735
43.649
−11.659
1.00
55.20


ATOM
1706
N
SER
249
10.318
47.849
−9.351
1.00
39.68


ATOM
1707
CA
SER
249
9.715
49.166
−9.284
1.00
46.54


ATOM
1708
C
SER
249
9.181
49.632
−10.625
1.00
37.56


ATOM
1709
O
SER
249
9.766
49.357
−11.653
1.00
43.92


ATOM
1710
CB
SER
249
10.740
50.194
−8.784
1.00
43.78


ATOM
1711
OG
SER
249
11.184
49.896
−7.473
1.00
57.17


ATOM
1712
N
ALA
250
8.075
50.357
−10.598
1.00
36.21


ATOM
1713
CA
ALA
250
7.637
51.113
−11.743
1.00
34.75


ATOM
1714
C
ALA
250
8.476
52.369
−11.719
1.00
36.51


ATOM
1715
O
ALA
250
8.838
52.865
−10.661
1.00
45.60


ATOM
1716
CB
ALA
250
6.182
51.465
−11.612
1.00
37.23


ATOM
1717
N
TYR
251
8.773
52.909
−12.886
1.00
35.78


ATOM
1718
CA
TYR
251
9.763
53.968
−12.989
1.00
31.65


ATOM
1719
C
TYR
251
9.449
54.882
−14.175
1.00
34.60


ATOM
1720
O
TYR
251
9.086
54.400
−15.231
1.00
39.05


ATOM
1721
CB
TYR
251
11.155
53.318
−13.140
1.00
33.30


ATOM
1722
CG
TYR
251
12.262
54.313
−13.345
1.00
33.98


ATOM
1723
CD1
TYR
251
12.662
55.157
−12.309
1.00
37.10


ATOM
1724
CD2
TYR
251
12.910
54.414
−14.566
1.00
39.17


ATOM
1725
CE1
TYR
251
13.679
56.080
−12.486
1.00
38.91


ATOM
1726
CE2
TYR
251
13.936
55.326
−14.754
1.00
46.69


ATOM
1727
CZ
TYR
251
14.314
56.152
−13.715
1.00
46.28


ATOM
1728
OH
TYR
251
15.317
57.062
−13.900
1.00
60.47


ATOM
1729
N
ALA
252
9.569
56.196
−14.002
1.00
37.22


ATOM
1730
CA
ALA
252
9.398
57.099
−15.124
1.00
31.12


ATOM
1731
C
ALA
252
10.255
58.324
−14.985
1.00
37.45


ATOM
1732
O
ALA
252
10.575
58.740
−13.878
1.00
37.06


ATOM
1733
CB
ALA
252
7.956
57.501
−15.300
1.00
32.57


ATOM
1734
N
TYR
253
10.622
58.943
−16.098
1.00
29.71


ATOM
1735
CA
TYR
253
11.326
60.221
−15.963
1.00
39.30


ATOM
1736
C
TYR
253
11.165
61.127
−17.156
1.00
36.10


ATOM
1737
O
TYR
253
10.963
60.680
−18.277
1.00
40.44


ATOM
1738
CB
TYR
253
12.824
59.989
−15.661
1.00
46.73


ATOM
1739
CG
TYR
253
13.734
59.833
−16.858
1.00
49.56


ATOM
1740
CD1
TYR
253
13.812
58.756
−17.504
1.00
56.37


ATOM
1741
CD2
TYR
253
14.537
60.749
−17.280
1.00
65.68


ATOM
1742
CE1
TYR
253
14.640
58.593
−18.575
1.00
75.03


ATOM
1743
CE2
TYR
253
15.363
60.567
−18.365
1.00
78.78


ATOM
1744
CZ
TYR
253
15.421
59.488
−19.013
1.00
93.20


ATOM
1745
OH
TYR
253
16.262
59.296
−20.105
1.00
0.44


ATOM
1746
ZN
ZN2
258
−1.421
48.564
−9.888
1.00
71.07


ATOM
1747
N
ASN
15
0.218
68.205
−22.240
1.00
0.61


ATOM
1748
CA
ASN
15
0.186
66.763
−22.018
1.00
0.98


ATOM
1749
C
ASN
15
1.535
66.056
−21.874
1.00
0.70


ATOM
1750
O
ASN
15
1.568
64.870
−21.554
1.00
0.18


ATOM
1751
CB
ASN
15
−0.630
66.078
−23.111
1.00
0.60


ATOM
1752
CG
ASN
15
−1.982
65.612
−22.621
1.00
0.45


ATOM
1753
OD1
ASN
15
−2.111
65.105
−21.513
1.00
0.18


ATOM
1754
ND2
ASN
15
−2.995
65.765
−23.454
1.00
0.78


ATOM
1755
N
LEU
16
2.627
66.773
−22.133
1.00
94.87


ATOM
1756
CA
LEU
16
4.002
66.286
−21.882
1.00
68.59


ATOM
1757
C
LEU
16
4.304
64.808
−22.181
1.00
62.20


ATOM
1758
O
LEU
16
3.765
63.905
−21.537
1.00
47.59


ATOM
1759
CB
LEU
16
4.440
66.637
−20.458
1.00
58.51


ATOM
1760
CG
LEU
16
5.071
68.020
−20.284
1.00
71.98


ATOM
1761
CD1
LEU
16
4.166
69.098
−20.815
1.00
95.09


ATOM
1762
CD2
LEU
16
5.387
68.282
−18.826
1.00
66.90


ATOM
1763
N
PRO
17
5.172
64.564
−23.174
1.00
59.11


ATOM
1764
CA
PRO
17
5.692
63.215
−23.383
1.00
56.32


ATOM
1765
C
PRO
17
6.546
62.821
−22.172
1.00
53.83


ATOM
1766
O
PRO
17
7.090
63.692
−21.490
1.00
55.40


ATOM
1767
CB
PRO
17
6.593
63.362
−24.615
1.00
49.67


ATOM
1768
CG
PRO
17
6.313
64.690
−25.173
1.00
57.25


ATOM
1769
CD
PRO
17
5.780
65.540
−24.087
1.00
51.52


ATOM
1770
N
ILE
18
6.635
61.527
−21.898
1.00
44.93


ATOM
1771
CA
ILE
18
7.572
61.029
−20.914
1.00
40.29


ATOM
1772
C
ILE
18
8.729
60.321
−21.625
1.00
42.04


ATOM
1773
O
ILE
18
8.521
59.377
−22.379
1.00
43.41


ATOM
1774
CB
ILE
18
6.889
60.101
−19.902
1.00
38.13


ATOM
1775
CG1
ILE
18
5.875
60.877
−19.075
1.00
45.13


ATOM
1776
CG2
ILE
18
7.929
59.461
−18.976
1.00
48.42


ATOM
1777
CD1
ILE
18
4.852
60.013
−18.363
1.00
47.95


ATOM
1778
N
ASN
19
9.946
60.803
−21.377
1.00
38.56


ATOM
1779
CA
ASN
19
11.151
60.265
−22.005
1.00
45.65


ATOM
1780
C
ASN
19
11.296
58.752
−21.879
1.00
49.75


ATOM
1781
O
ASN
19
11.592
58.067
−22.855
1.00
53.42


ATOM
1782
CB
ASN
19
12.407
60.935
−21.440
1.00
48.95


ATOM
1783
CG
ASN
19
12.450
62.410
−21.714
1.00
54.49


ATOM
1784
OD1
ASN
19
13.260
62.892
−22.513
1.00
68.59


ATOM
1785
ND2
ASN
19
11.586
63.141
−21.048
1.00
35.74


ATOM
1786
N
GLN
20
11.101
58.241
−20.671
1.00
46.80


ATOM
1787
CA
GLN
20
11.192
56.807
−20.435
1.00
38.04


ATOM
1788
C
GLN
20
10.243
56.403
−19.325
1.00
38.60


ATOM
1789
O
GLN
20
10.218
57.007
−18.259
1.00
41.07


ATOM
1790
CB
GLN
20
12.635
56.383
−20.038
1.00
33.85


ATOM
1791
CG
GLN
20
13.749
56.734
−21.029
1.00
34.91


ATOM
1792
CD
GLN
20
13.680
55.963
−22.344
1.00
56.22


ATOM
1793
OE1
GLN
20
13.058
54.904
−22.429
1.00
49.36


ATOM
1794
NE2
GLN
20
14.322
56.501
−23.380
1.00
56.75


ATOM
1795
N
VAL
21
9.461
55.371
−19.574
1.00
37.98


ATOM
1796
CA
VAL
21
8.625
54.813
−18.532
1.00
36.09


ATOM
1797
C
VAL
21
8.640
53.314
−18.683
1.00
49.71


ATOM
1798
O
VAL
21
8.605
52.800
−19.800
1.00
43.59


ATOM
1799
CB
VAL
21
7.176
55.332
−18.615
1.00
47.00


ATOM
1800
CG1
VAL
21
6.612
55.089
−19.972
1.00
42.94


ATOM
1801
CG2
VAL
21
6.292
54.635
−17.580
1.00
46.40


ATOM
1802
N
GLY
22
8.703
52.616
−17.556
1.00
43.61


ATOM
1803
CA
GLY
22
8.784
51.173
−17.557
1.00
35.97


ATOM
1804
C
GLY
22
9.120
50.661
−16.173
1.00
42.16


ATOM
1805
O
GLY
22
8.507
51.064
−15.177
1.00
41.03


ATOM
1806
N
ILE
23
10.092
49.757
−16.107
1.00
27.58


ATOM
1807
CA
ILE
23
10.433
49.117
−14.851
1.00
28.73


ATOM
1808
C
ILE
23
11.926
49.234
−14.573
1.00
34.99


ATOM
1809
O
ILE
23
12.750
49.357
−15.484
1.00
36.46


ATOM
1810
CB
ILE
23
10.049
47.609
−14.835
1.00
37.25


ATOM
1811
CG1
ILE
23
10.915
46.827
−15.823
1.00
43.10


ATOM
1812
CG2
ILE
23
8.530
47.392
−15.108
1.00
33.88


ATOM
1813
CD1
ILE
23
10.871
45.338
−15.634
1.00
54.70


ATOM
1814
N
THR
48
12.474
50.488
−20.323
1.00
29.81


ATOM
1815
CA
THR
48
11.604
51.653
−20.402
1.00
30.70


ATOM
1816
C
THR
48
11.352
51.979
−21.873
1.00
42.96


ATOM
1817
O
THR
48
12.134
51.579
−22.746
1.00
36.92


ATOM
1818
CB
THR
48
12.283
52.868
−19.734
1.00
49.92


ATOM
1819
OG1
THR
48
13.497
53.165
−20.433
1.00
50.87


ATOM
1820
CG2
THR
48
12.627
52.597
−18.233
1.00
36.60


ATOM
1821
N
VAL
49
10.263
52.695
−22.139
1.00
39.32


ATOM
1822
CA
VAL
49
9.940
53.162
−23.485
1.00
40.47


ATOM
1823
C
VAL
49
9.428
54.590
−23.429
1.00
47.31


ATOM
1824
O
VAL
49
8.994
55.065
−22.393
1.00
39.62


ATOM
1825
CB
VAL
49
8.827
52.307
−24.190
1.00
39.46


ATOM
1826
CG1
VAL
49
9.252
50.874
−24.353
1.00
38.61


ATOM
1827
CG2
VAL
49
7.464
52.427
−23.453
1.00
32.61


ATOM
1828
N
TYR
50
9.472
55.258
−24.568
1.00
48.54


ATOM
1829
CA
TYR
50
8.939
56.601
−24.720
1.00
42.54


ATOM
1830
C
TYR
50
7.415
56.585
−24.665
1.00
38.18


ATOM
1831
O
TYR
50
6.765
55.732
−25.274
1.00
59.47


ATOM
1832
CB
TYR
50
9.421
57.166
−26.063
1.00
48.65


ATOM
1833
CG
TYR
50
8.877
58.521
−26.439
1.00
46.41


ATOM
1834
CD1
TYR
50
9.495
59.690
−26.002
1.00
48.12


ATOM
1835
CD2
TYR
50
7.780
58.635
−27.288
1.00
45.63


ATOM
1836
CE1
TYR
50
9.005
60.940
−26.369
1.00
49.82


ATOM
1837
CE2
TYR
50
7.282
59.873
−27.658
1.00
64.78


ATOM
1838
CZ
TYR
50
7.891
61.024
−27.200
1.00
66.95


ATOM
1839
OH
TYR
50
7.378
62.253
−27.576
1.00
63.72


ATOM
1840
N
LEU
51
6.845
57.529
−23.925
1.00
41.19


ATOM
1841
CA
LEU
51
5.392
57.641
−23.852
1.00
45.35


ATOM
1842
C
LEU
51
4.944
58.964
−24.477
1.00
59.79


ATOM
1843
O
LEU
51
5.234
60.032
−23.953
1.00
57.86


ATOM
1844
CB
LEU
51
4.903
57.505
−22.407
1.00
41.63


ATOM
1845
CG
LEU
51
3.390
57.336
−22.268
1.00
57.45


ATOM
1846
CD1
LEU
51
3.024
55.982
−22.804
1.00
53.37


ATOM
1847
CD2
LEU
51
2.896
57.505
−20.817
1.00
46.74


ATOM
1848
N
PRO
52
4.252
58.887
−25.620
1.00
50.41


ATOM
1849
CA
PRO
52
3.698
60.053
−26.327
1.00
60.78


ATOM
1850
C
PRO
52
2.845
60.936
−25.412
1.00
55.59


ATOM
1851
O
PRO
52
2.252
60.441
−24.464
1.00
45.38


ATOM
1852
CB
PRO
52
2.799
59.418
−27.398
1.00
51.53


ATOM
1853
CG
PRO
52
3.307
58.019
−27.560
1.00
54.38


ATOM
1854
CD
PRO
52
3.795
57.616
−26.204
1.00
47.05


ATOM
1855
N
ALA
53
2.787
62.230
−25.706
1.00
65.72


ATOM
1856
CA
ALA
53
2.046
63.188
−24.882
1.00
66.94


ATOM
1857
C
ALA
53
0.629
62.747
−24.490
1.00
71.17


ATOM
1858
O
ALA
53
0.223
62.913
−23.341
1.00
71.46


ATOM
1859
CB
ALA
53
1.998
64.543
−25.564
1.00
66.90


ATOM
1860
N
GLU
54
−0.130
62.183
−25.424
1.00
75.20


ATOM
1861
CA
GLU
54
−1.535
61.918
−25.120
1.00
0.50


ATOM
1862
C
GLU
54
−1.871
60.457
−24.827
1.00
90.42


ATOM
1863
O
GLU
54
−3.039
60.090
−24.744
1.00
95.12


ATOM
1864
CB
GLU
54
−2.466
62.524
−26.176
1.00
0.71


ATOM
1865
CG
GLU
54
−2.722
61.670
−27.397
1.00
0.20


ATOM
1866
CD
GLU
54
−3.621
62.371
−28.398
1.00
0.17


ATOM
1867
OE1
GLU
54
−3.217
63.435
−28.908
1.00
0.84


ATOM
1868
OE2
GLU
54
−4.728
61.864
−28.672
1.00
0.50


ATOM
1869
N
GLN
55
−0.845
59.632
−24.656
1.00
78.83


ATOM
1870
CA
GLN
55
−1.035
58.296
−24.104
1.00
68.58


ATOM
1871
C
GLN
55
−0.918
58.434
−22.589
1.00
58.44


ATOM
1872
O
GLN
55
0.009
59.070
−22.092
1.00
65.77


ATOM
1873
CB
GLN
55
0.011
57.321
−24.658
1.00
58.13


ATOM
1874
CG
GLN
55
−0.321
55.844
−24.474
1.00
67.08


ATOM
1875
CD
GLN
55
0.672
54.929
−25.189
1.00
79.71


ATOM
1876
OE1
GLN
55
1.214
55.285
−26.235
1.00
88.70


ATOM
1877
NE2
GLN
55
0.912
53.744
−24.625
1.00
63.58


ATOM
1878
N
LYS
56
−1.859
57.855
−21.852
1.00
61.67


ATOM
1879
CA
LYS
56
−1.921
58.061
−20.410
1.00
65.88


ATOM
1880
C
LYS
56
−0.919
57.196
−19.648
1.00
73.54


ATOM
1881
O
LYS
56
−0.438
57.584
−18.578
1.00
73.26


ATOM
1882
CB
LYS
56
−3.326
57.788
−19.872
1.00
88.06


ATOM
1883
CG
LYS
56
−3.413
57.858
−18.349
1.00
0.53


ATOM
1884
CD
LYS
56
−4.837
57.649
−17.847
1.00
0.29


ATOM
1885
CE
LYS
56
−5.261
56.190
−17.948
1.00
0.17


ATOM
1886
NZ
LYS
56
−6.636
55.973
−17.419
1.00
0.56


ATOM
1887
N
GLY
57
−0.613
56.025
−20.205
1.00
63.39


ATOM
1888
CA
GLY
57
0.166
55.011
−19.520
1.00
60.23


ATOM
1889
C
GLY
57
0.775
53.992
−20.465
1.00
67.31


ATOM
1890
O
GLY
57
0.404
53.894
−21.628
1.00
65.95


ATOM
1891
N
THR
58
1.747
53.243
−19.964
1.00
71.54


ATOM
1892
CA
THR
58
2.338
52.164
−20.736
1.00
72.16


ATOM
1893
C
THR
58
1.743
50.862
−20.216
1.00
61.69


ATOM
1894
O
THR
58
0.837
50.885
−19.387
1.00
61.90


ATOM
1895
CB
THR
58
3.879
52.159
−20.619
1.00
69.56


ATOM
1896
OG1
THR
58
4.439
51.312
−21.629
1.00
79.35


ATOM
1897
CG2
THR
58
4.316
51.680
−19.244
1.00
68.68


ATOM
1898
N
HIS
59
2.246
49.729
−20.695
1.00
71.58


ATOM
1899
CA
HIS
59
1.724
48.439
−20.259
1.00
69.19


ATOM
1900
C
HIS
59
2.798
47.698
−19.487
1.00
62.91


ATOM
1901
O
HIS
59
3.641
47.023
−20.075
1.00
74.03


ATOM
1902
CB
HIS
59
1.246
47.636
−21.466
1.00
67.89


ATOM
1903
CG
HIS
59
0.355
48.414
−22.386
1.00
73.78


ATOM
1904
ND1
HIS
59
0.848
49.209
−23.406
1.00
79.21


ATOM
1905
CD2
HIS
59
−0.988
48.533
−22.440
1.00
74.77


ATOM
1906
CE1
HIS
59
−0.155
49.769
−24.049
1.00
81.43


ATOM
1907
NE2
HIS
59
−1.283
49.378
−23.482
1.00
82.11


ATOM
1908
N
MSE
60
2.754
47.824
−18.164
1.00
69.20


ATOM
1909
CA
MSE
60
3.889
47.455
−17.308
1.00
64.49


ATOM
1910
C
MSE
60
4.271
45.977
−17.333
1.00
57.44


ATOM
1911
O
MSE
60
5.453
45.628
−17.259
1.00
55.33


ATOM
1912
CB
MSE
60
3.626
47.895
−15.866
1.00
68.93


ATOM
1913
CG
MSE
60
3.645
49.405
−15.670
1.00
88.07


ATOM
1914
SE
MSE
60
5.452
50.209
−15.726
1.00
90.92


ATOM
1915
CE
MSE
60
4.956
52.073
−15.352
1.00
91.55


ATOM
1916
N
SER
61
3.265
45.114
−17.436
1.00
49.65


ATOM
1917
CA
SER
61
3.490
43.667
−17.384
1.00
52.54


ATOM
1918
C
SER
61
4.202
43.098
−18.627
1.00
57.67


ATOM
1919
O
SER
61
4.824
42.040
−18.555
1.00
63.02


ATOM
1920
CB
SER
61
2.158
42.931
−17.127
1.00
60.89


ATOM
1921
OG
SER
61
1.418
42.821
−18.313
1.00
63.53


ATOM
1922
N
ARG
62
4.112
43.796
−19.757
1.00
58.58


ATOM
1923
CA
ARG
62
4.804
43.363
−20.970
1.00
54.99


ATOM
1924
C
ARG
62
6.330
43.332
−20.816
1.00
47.98


ATOM
1925
O
ARG
62
6.992
42.462
−21.385
1.00
58.75


ATOM
1926
CB
ARG
62
4.407
44.222
−22.169
1.00
48.24


ATOM
1927
CG
ARG
62
2.980
44.013
−22.584
1.00
54.45


ATOM
1928
CD
ARG
62
2.567
45.010
−23.663
1.00
53.24


ATOM
1929
NE
ARG
62
1.122
45.035
−23.836
1.00
68.95


ATOM
1930
CZ
ARG
62
0.492
45.679
−24.808
1.00
67.76


ATOM
1931
NH1
ARG
62
1.186
46.343
−25.719
1.00
58.36


ATOM
1932
NH2
ARG
62
−0.838
45.649
−24.869
1.00
72.93


ATOM
1933
N
PHE
63
6.879
44.274
−20.049
1.00
45.59


ATOM
1934
CA
PHE
63
8.317
44.301
−19.800
1.00
51.33


ATOM
1935
C
PHE
63
8.788
42.986
−19.200
1.00
57.30


ATOM
1936
O
PHE
63
9.781
42.396
−19.641
1.00
55.44


ATOM
1937
CB
PHE
63
8.688
45.451
−18.866
1.00
49.40


ATOM
1938
CG
PHE
63
8.439
46.793
−19.449
1.00
44.13


ATOM
1939
CD1
PHE
63
9.233
47.270
−20.474
1.00
41.09


ATOM
1940
CD2
PHE
63
7.394
47.573
−18.995
1.00
50.77


ATOM
1941
CE1
PHE
63
9.008
48.509
−21.018
1.00
39.25


ATOM
1942
CE2
PHE
63
7.161
48.820
−19.543
1.00
57.73


ATOM
1943
CZ
PHE
63
7.977
49.295
−20.546
1.00
41.41


ATOM
1944
N
VAL
64
8.065
42.540
−18.180
1.00
47.97


ATOM
1945
CA
VAL
64
8.375
41.278
−17.524
1.00
55.02


ATOM
1946
C
VAL
64
8.125
40.094
−18.472
1.00
53.37


ATOM
1947
O
VAL
64
9.000
39.244
−18.648
1.00
45.07


ATOM
1948
CB
VAL
64
7.537
41.103
−16.238
1.00
69.71


ATOM
1949
CG1
VAL
64
7.874
39.786
−15.564
1.00
71.34


ATOM
1950
CG2
VAL
64
7.770
42.266
−15.293
1.00
71.51


ATOM
1951
N
ALA
65
6.935
40.043
−19.081
1.00
43.65


ATOM
1952
CA
ALA
65
6.603
38.960
−20.017
1.00
45.85


ATOM
1953
C
ALA
65
7.693
38.821
−21.074
1.00
55.77


ATOM
1954
O
ALA
65
8.040
37.716
−21.480
1.00
62.71


ATOM
1955
CB
ALA
65
5.251
39.210
−20.673
1.00
51.78


ATOM
1956
N
LEU
66
8.246
39.951
−21.498
1.00
48.51


ATOM
1957
CA
LEU
66
9.263
39.949
−22.523
1.00
43.71


ATOM
1958
C
LEU
66
10.473
39.169
−22.012
1.00
59.09


ATOM
1959
O
LEU
66
11.024
38.322
−22.717
1.00
63.51


ATOM
1960
CB
LEU
66
9.645
41.382
−22.900
1.00
57.57


ATOM
1961
CG
LEU
66
10.720
41.475
−23.984
1.00
65.50


ATOM
1962
CD1
LEU
66
10.131
41.113
−25.331
1.00
62.26


ATOM
1963
CD2
LEU
66
11.344
42.854
−24.030
1.00
66.51


ATOM
1964
N
MSE
67
10.863
39.435
−20.768
1.00
56.08


ATOM
1965
CA
MSE
67
11.995
38.730
−20.156
1.00
50.31


ATOM
1966
C
MSE
67
11.739
37.245
−19.931
1.00
57.07


ATOM
1967
O
MSE
67
12.615
36.424
−20.190
1.00
56.89


ATOM
1968
CB
MSE
67
12.389
39.382
−18.829
1.00
60.46


ATOM
1969
CG
MSE
67
13.175
40.665
−19.002
1.00
70.04


ATOM
1970
SE
MSE
67
14.532
40.440
−20.393
1.00
0.01


ATOM
1971
CE
MSE
67
15.381
42.197
−20.260
1.00
0.53


ATOM
1972
N
GLU
68
10.548
36.900
−19.437
1.00
43.15


ATOM
1973
CA
GLU
68
10.235
35.514
−19.126
1.00
52.89


ATOM
1974
C
GLU
68
10.264
34.643
−20.374
1.00
66.07


ATOM
1975
O
GLU
68
10.597
33.455
−20.312
1.00
65.29


ATOM
1976
CB
GLU
68
8.854
35.414
−18.459
1.00
60.06


ATOM
1977
CG
GLU
68
8.743
36.180
−17.138
1.00
77.68


ATOM
1978
CD
GLU
68
9.549
35.547
−16.007
1.00
95.66


ATOM
1979
OE1
GLU
68
10.258
34.545
−16.254
1.00
95.42


ATOM
1980
OE2
GLU
68
9.472
36.052
−14.866
1.00
0.24


ATOM
1981
N
GLN
69
9.916
35.245
−21.507
1.00
80.73


ATOM
1982
CA
GLN
69
9.751
34.495
−22.744
1.00
93.63


ATOM
1983
C
GLN
69
11.061
34.321
−23.493
1.00
89.35


ATOM
1984
O
GLN
69
11.165
33.485
−24.386
1.00
94.28


ATOM
1985
CB
GLN
69
8.735
35.176
−23.655
1.00
0.97


ATOM
1986
CG
GLN
69
8.083
34.221
−24.639
1.00
0.88


ATOM
1987
CD
GLN
69
7.454
34.936
−25.812
1.00
0.36


ATOM
1988
OE1
GLN
69
7.850
36.048
−26.162
1.00
0.96


ATOM
1989
NE2
GLN
69
6.471
34.297
−26.433
1.00
0.47


ATOM
1990
N
HIS
70
12.059
35.114
−23.128
1.00
87.50


ATOM
1991
CA
HIS
70
13.355
35.066
−23.793
1.00
91.35


ATOM
1992
C
HIS
70
14.373
34.251
−22.988
1.00
93.16


ATOM
1993
O
HIS
70
14.977
34.751
−22.039
1.00
0.23


ATOM
1994
CB
HIS
70
13.849
36.491
−24.045
1.00
0.10


ATOM
1995
CG
HIS
70
15.339
36.630
−24.061
1.00
0.47


ATOM
1996
ND1
HIS
70
16.086
36.773
−22.911
1.00
0.14


ATOM
1997
CD2
HIS
70
16.218
36.673
−25.089
1.00
0.88


ATOM
1998
CE1
HIS
70
17.365
36.882
−23.229
1.00
0.10


ATOM
1999
NE2
HIS
70
17.471
36.829
−24.544
1.00
0.29


ATOM
2000
N
ALA
84
14.585
45.967
−29.802
1.00
39.91


ATOM
2001
CA
ALA
84
13.671
46.186
−30.913
1.00
51.43


ATOM
2002
C
ALA
84
12.362
45.463
−30.642
1.00
49.14


ATOM
2003
O
ALA
84
11.285
46.009
−30.853
1.00
53.26


ATOM
2004
CB
ALA
84
14.281
45.707
−32.223
1.00
36.81


ATOM
2005
N
GLU
85
12.470
44.232
−30.156
1.00
43.56


ATOM
2006
CA
GLU
85
11.296
43.422
−29.859
1.00
48.49


ATOM
2007
C
GLU
85
10.448
44.096
−28.778
1.00
46.67


ATOM
2008
O
GLU
85
9.222
44.003
−28.785
1.00
56.68


ATOM
2009
CB
GLU
85
11.724
42.022
−29.434
1.00
49.28


ATOM
2010
CG
GLU
85
10.587
41.034
−29.353
1.00
80.44


ATOM
2011
CD
GLU
85
11.069
39.600
−29.385
1.00
0.75


ATOM
2012
OE1
GLU
85
12.298
39.399
−29.519
1.00
0.01


ATOM
2013
OE2
GLU
85
10.223
38.680
−29.283
1.00
0.82


ATOM
2014
N
MSE
86
11.110
44.803
−27.866
1.00
40.52


ATOM
2015
CA
MSE
86
10.417
45.484
−26.786
1.00
39.51


ATOM
2016
C
MSE
86
9.631
46.703
−27.235
1.00
44.35


ATOM
2017
O
MSE
86
8.460
46.850
−26.896
1.00
50.93


ATOM
2018
CB
MSE
86
11.365
45.906
−25.682
1.00
40.42


ATOM
2019
CG
MSE
86
10.708
46.867
−24.705
1.00
48.85


ATOM
2020
SE
MSE
86
11.954
47.555
−23.380
1.00
71.76


ATOM
2021
CE
MSE
86
12.844
48.922
−24.467
1.00
36.65


ATOM
2022
N
VAL
87
10.277
47.597
−27.972
1.00
44.35


ATOM
2023
CA
VAL
87
9.589
48.791
−28.442
1.00
45.24


ATOM
2024
C
VAL
87
8.398
48.392
−29.329
1.00
44.79


ATOM
2025
O
VAL
87
7.382
49.081
−29.339
1.00
48.45


ATOM
2026
CB
VAL
87
10.508
49.762
−29.222
1.00
49.52


ATOM
2027
CG1
VAL
87
11.666
50.235
−28.352
1.00
37.17


ATOM
2028
CG2
VAL
87
11.008
49.119
−30.499
1.00
53.31


ATOM
2029
N
ALA
88
8.534
47.286
−30.061
1.00
37.50


ATOM
2030
CA
ALA
88
7.456
46.797
−30.916
1.00
51.61


ATOM
2031
C
ALA
88
6.339
46.279
−30.058
1.00
56.02


ATOM
2032
O
ALA
88
5.185
46.591
−30.295
1.00
63.47


ATOM
2033
CB
ALA
88
7.943
45.700
−31.853
1.00
50.46


ATOM
2034
N
LEU
89
6.697
45.497
−29.047
1.00
57.64


ATOM
2035
CA
LEU
89
5.730
44.891
−28.124
1.00
59.78


ATOM
2036
C
LEU
89
4.942
45.934
−27.315
1.00
53.97


ATOM
2037
O
LEU
89
3.743
45.804
−27.119
1.00
56.91


ATOM
2038
CB
LEU
89
6.451
43.923
−27.181
1.00
57.63


ATOM
2039
CG
LEU
89
5.628
43.249
−26.094
1.00
56.32


ATOM
2040
CD1
LEU
89
4.718
42.207
−26.716
1.00
42.44


ATOM
2041
CD2
LEU
89
6.536
42.615
−25.055
1.00
61.18


ATOM
2042
N
LEU
90
5.612
46.970
−26.837
1.00
54.16


ATOM
2043
CA
LEU
90
4.924
48.025
−26.111
1.00
63.18


ATOM
2044
C
LEU
90
4.361
49.102
−27.032
1.00
67.68


ATOM
2045
O
LEU
90
3.870
50.131
−26.575
1.00
65.17


ATOM
2046
CB
LEU
90
5.844
48.634
−25.065
1.00
54.20


ATOM
2047
CG
LEU
90
5.801
47.751
−23.824
1.00
61.73


ATOM
2048
CD1
LEU
90
7.055
46.902
−23.699
1.00
41.72


ATOM
2049
CD2
LEU
90
5.595
48.601
−22.601
1.00
75.98


ATOM
2050
N
ASP
91
4.432
48.848
−28.332
1.00
62.55


ATOM
2051
CA
ASP
91
3.870
49.748
−29.329
1.00
74.29


ATOM
2052
C
ASP
91
4.407
51.167
−29.159
1.00
64.93


ATOM
2053
O
ASP
91
3.634
52.107
−29.035
1.00
56.16


ATOM
2054
CB
ASP
91
2.333
49.752
−29.242
1.00
84.05


ATOM
2055
CG
ASP
91
1.698
48.481
−29.813
1.00
0.91


ATOM
2056
OD1
ASP
91
2.435
47.619
−30.332
1.00
0.11


ATOM
2057
OD2
ASP
91
0.456
48.347
−29.753
1.00
98.46


ATOM
2058
N
SER
92
5.730
51.321
−29.156
1.00
57.68


ATOM
2059
CA
SER
92
6.349
52.629
−28.929
1.00
40.55


ATOM
2060
C
SER
92
7.432
53.000
−29.952
1.00
52.93


ATOM
2061
O
SER
92
7.981
52.142
−30.636
1.00
58.12


ATOM
2062
CB
SER
92
6.909
52.689
−27.509
1.00
47.88


ATOM
2063
OG
SER
92
7.480
53.952
−27.226
1.00
53.37


ATOM
2064
N
ARG
93
7.744
54.290
−30.016
1.00
53.73


ATOM
2065
CA
ARG
93
8.714
54.864
−30.946
1.00
47.19


ATOM
2066
C
ARG
93
10.185
54.689
−30.507
1.00
61.56


ATOM
2067
O
ARG
93
11.110
54.745
−31.327
1.00
57.47


ATOM
2068
CB
ARG
93
8.417
56.357
−31.073
1.00
57.38


ATOM
2069
CG
ARG
93
9.157
57.076
−32.169
1.00
80.07


ATOM
2070
CD
ARG
93
8.893
58.577
−32.098
1.00
91.35


ATOM
2071
NE
ARG
93
9.315
59.154
−30.822
1.00
84.96


ATOM
2072
CZ
ARG
93
10.584
59.361
−30.474
1.00
95.02


ATOM
2073
NH1
ARG
93
11.571
59.029
−31.296
1.00
95.51


ATOM
2074
NH2
ARG
93
10.872
59.893
−29.297
1.00
81.77


ATOM
2075
N
ALA
94
10.396
54.497
−29.210
1.00
48.21


ATOM
2076
CA
ALA
94
11.749
54.469
−28.642
1.00
54.64


ATOM
2077
C
ALA
94
11.768
53.778
−27.293
1.00
43.02


ATOM
2078
O
ALA
94
10.722
53.561
−26.681
1.00
51.06


ATOM
2079
CB
ALA
94
12.297
55.883
−28.505
1.00
43.30


ATOM
2080
N
GLY
95
12.966
53.446
−26.817
1.00
49.26


ATOM
2081
CA
GLY
95
13.115
52.824
−25.518
1.00
35.71


ATOM
2082
C
GLY
95
14.522
52.335
−25.225
1.00
55.15


ATOM
2083
O
GLY
95
15.394
52.348
−26.092
1.00
48.14


TER











ENDMDL
















TABLE 11





Three-Dimensional Coordinates of Neisseria gonorrhoeae GCYH-IB·Mn2+


(SEQ. ID. No. 8)
























ATOM
1
N
LYS
106
10.392
70.600
9.408
1.00
39.71


ATOM
2
CA
LYS
106
9.306
70.423
10.391
1.00
42.95


ATOM
3
C
LYS
106
7.939
70.297
9.736
1.00
43.79


ATOM
4
O
LYS
106
7.463
71.233
9.099
1.00
44.80


ATOM
5
CB
LYS
106
9.305
71.577
11.392
1.00
43.80


ATOM
6
CG
LYS
106
8.686
71.208
12.748
1.00
48.36


ATOM
7
CD
LYS
106
9.747
71.087
13.838
1.00
53.64


ATOM
8
CE
LYS
106
9.171
70.635
15.168
1.00
55.97


ATOM
9
NZ
LYS
106
8.461
69.303
15.127
1.00
59.34


ATOM
10
N
LYS
107
7.304
69.138
9.880
1.00
44.36


ATOM
11
CA
LYS
107
5.973
68.949
9.312
1.00
44.70


ATOM
12
C
LYS
107
4.898
68.958
10.414
1.00
45.13


ATOM
13
O
LYS
107
5.213
68.843
11.615
1.00
44.87


ATOM
14
CB
LYS
107
5.919
67.670
8.473
1.00
44.28


ATOM
15
CG
LYS
107
7.016
67.604
7.384
1.00
43.47


ATOM
16
CD
LYS
107
6.748
66.456
6.423
1.00
41.18


ATOM
17
CE
LYS
107
5.476
66.755
5.604
1.00
42.21


ATOM
18
NZ
LYS
107
5.334
65.886
4.400
1.00
40.46


ATOM
19
N
THR
108
3.641
69.114
9.996
1.00
45.84


ATOM
20
CA
THR
108
2.494
69.116
10.901
1.00
46.81


ATOM
21
C
THR
108
1.453
68.111
10.397
1.00
47.68


ATOM
22
O
THR
108
1.123
68.099
9.198
1.00
47.71


ATOM
23
CB
THR
108
1.900
70.564
11.037
1.00
47.35


ATOM
24
OG1
THR
108
2.963
71.502
11.302
1.00
47.19


ATOM
25
CG2
THR
108
0.851
70.649
12.172
1.00
47.03


ATOM
26
N
ALA
109
0.950
67.260
11.299
1.00
48.80


ATOM
27
CA
ALA
109
−0.043
66.235
10.948
1.00
50.14


ATOM
28
C
ALA
109
−1.364
66.869
10.468
1.00
51.03


ATOM
29
O
ALA
109
−1.770
67.916
11.004
1.00
51.15


ATOM
30
CB
ALA
109
−0.284
65.278
12.127
1.00
50.35


ATOM
31
N
PRO
110
−2.009
66.268
9.427
1.00
51.43


ATOM
32
CA
PRO
110
−3.180
66.907
8.859
1.00
51.94


ATOM
33
C
PRO
110
−4.394
67.037
9.798
1.00
52.99


ATOM
34
O
PRO
110
−5.175
67.962
9.609
1.00
52.84


ATOM
35
CB
PRO
110
−3.517
66.029
7.639
1.00
51.48


ATOM
36
CG
PRO
110
−2.880
64.767
7.863
1.00
51.48


ATOM
37
CD
PRO
110
−1.654
65.036
8.684
1.00
51.45


ATOM
38
N
VAL
111
−4.578
66.145
10.780
1.00
53.92


ATOM
39
CA
VAL
111
−5.756
66.302
11.660
1.00
55.03


ATOM
40
C
VAL
111
−5.429
66.827
13.057
1.00
55.25


ATOM
41
O
VAL
111
−5.957
67.878
13.469
1.00
55.19


ATOM
42
CB
VAL
111
−6.709
65.062
11.692
1.00
55.46


ATOM
43
CG1
VAL
111
−7.959
65.351
12.557
1.00
54.84


ATOM
44
CG2
VAL
111
−7.125
64.682
10.262
1.00
55.47


ATOM
45
N
SER
112
−4.559
66.102
13.764
1.00
55.19


ATOM
46
CA
SER
112
−4.113
66.499
15.099
1.00
55.31


ATOM
47
C
SER
112
−3.377
67.852
15.158
1.00
54.97


ATOM
48
O
SER
112
−3.518
68.577
16.147
1.00
54.91


ATOM
49
CB
SER
112
−3.256
65.399
15.742
1.00
55.47


ATOM
50
OG
SER
112
−2.087
65.121
14.963
1.00
56.21


ATOM
51
N
GLY
113
−2.614
68.189
14.106
1.00
54.62


ATOM
52
CA
GLY
113
−1.646
69.315
14.149
1.00
53.64


ATOM
53
C
GLY
113
−0.355
69.022
14.943
1.00
53.03


ATOM
54
O
GLY
113
0.471
69.929
15.166
1.00
52.84


ATOM
55
N
ILE
114
−0.174
67.772
15.384
1.00
52.24


ATOM
56
CA
ILE
114
1.092
67.361
16.020
1.00
52.01


ATOM
57
C
ILE
114
2.254
67.467
14.992
1.00
51.48


ATOM
58
O
ILE
114
2.100
67.114
13.808
1.00
50.80


ATOM
59
CB
ILE
114
1.024
65.935
16.667
1.00
52.23


ATOM
60
CG1
ILE
114
−0.088
65.851
17.722
1.00
53.68


ATOM
61
CG2
ILE
114
2.337
65.584
17.370
1.00
51.30


ATOM
62
CD1
ILE
114
−0.418
64.414
18.174
1.00
53.39


ATOM
63
N
ARG
115
3.393
67.989
15.450
1.00
50.22


ATOM
64
CA
ARG
115
4.520
68.263
14.576
1.00
49.39


ATOM
65
C
ARG
115
5.561
67.156
14.723
1.00
47.82


ATOM
66
O
ARG
115
5.733
66.586
15.820
1.00
46.47


ATOM
67
CB
ARG
115
5.159
69.625
14.893
1.00
50.41


ATOM
68
CG
ARG
115
4.234
70.839
14.773
1.00
53.80


ATOM
69
CD
ARG
115
4.782
71.939
15.657
1.00
58.84


ATOM
70
NE
ARG
115
5.550
72.917
14.885
1.00
64.83


ATOM
71
CZ
ARG
115
6.714
73.450
15.257
1.00
61.10


ATOM
72
NH1
ARG
115
7.313
73.074
16.394
1.00
65.93


ATOM
73
NH2
ARG
115
7.300
74.341
14.454
1.00
66.59


ATOM
74
N
SER
116
6.238
66.869
13.609
1.00
45.50


ATOM
75
CA
SER
116
7.398
65.999
13.565
1.00
44.28


ATOM
76
C
SER
116
8.251
66.377
12.346
1.00
43.63


ATOM
77
O
SER
116
7.748
67.050
11.418
1.00
43.82


ATOM
78
CB
SER
116
6.977
64.524
13.499
1.00
44.12


ATOM
79
OG
SER
116
6.181
64.263
12.365
1.00
44.28


ATOM
80
N
LEU
117
9.513
65.929
12.343
1.00
41.18


ATOM
81
CA
LEU
117
10.420
66.162
11.222
1.00
39.32


ATOM
82
C
LEU
117
10.214
65.130
10.135
1.00
38.39


ATOM
83
O
LEU
117
9.828
64.006
10.421
1.00
37.25


ATOM
84
CB
LEU
117
11.869
66.098
11.684
1.00
38.72


ATOM
85
CG
LEU
117
12.234
67.020
12.841
1.00
38.20


ATOM
86
CD1
LEU
117
13.674
66.792
13.245
1.00
37.30


ATOM
87
CD2
LEU
117
11.986
68.492
12.494
1.00
37.50


ATOM
88
N
PRO
142
10.478
61.583
−0.479
1.00
31.78


ATOM
89
CA
PRO
142
9.695
60.360
−0.363
1.00
32.72


ATOM
90
C
PRO
142
8.237
60.743
−0.204
1.00
34.76


ATOM
91
O
PRO
142
7.899
61.618
0.638
1.00
35.43


ATOM
92
CB
PRO
142
10.240
59.663
0.917
1.00
32.41


ATOM
93
CG
PRO
142
10.949
60.785
1.722
1.00
32.83


ATOM
94
CD
PRO
142
11.041
62.043
0.817
1.00
31.61


ATOM
95
N
VAL
143
7.390
60.112
−1.006
1.00
34.49


ATOM
96
CA
VAL
143
5.966
60.332
−0.977
1.00
36.54


ATOM
97
C
VAL
143
5.257
58.987
−0.907
1.00
37.50


ATOM
98
O
VAL
143
5.873
57.931
−1.010
1.00
37.31


ATOM
99
CB
VAL
143
5.435
61.127
−2.220
1.00
36.15


ATOM
100
CG1
VAL
143
6.186
62.446
−2.420
1.00
36.77


ATOM
101
CG2
VAL
143
5.542
60.303
−3.443
1.00
35.72


ATOM
102
N
THR
144
3.957
59.043
−0.692
1.00
40.85


ATOM
103
CA
THR
144
3.070
57.890
−0.876
1.00
43.22


ATOM
104
C
THR
144
2.496
57.940
−2.296
1.00
45.07


ATOM
105
O
THR
144
2.017
59.013
−2.764
1.00
44.61


ATOM
106
CB
THR
144
1.904
57.920
0.137
1.00
43.97


ATOM
107
OG1
THR
144
2.430
58.174
1.451
1.00
45.02


ATOM
108
CG2
THR
144
1.090
56.604
0.134
1.00
43.92


ATOM
109
N
SER
145
2.564
56.789
−2.974
1.00
46.62


ATOM
110
CA
SER
145
1.899
56.587
−4.274
1.00
48.13


ATOM
111
C
SER
145
0.841
55.504
−4.119
1.00
48.74


ATOM
112
O
SER
145
1.058
54.516
−3.417
1.00
48.82


ATOM
113
CB
SER
145
2.886
56.201
−5.384
1.00
48.45


ATOM
114
OG
SER
145
3.671
55.067
−5.036
1.00
50.19


ATOM
115
N
LEU
146
−0.314
55.720
−4.746
1.00
49.98


ATOM
116
CA
LEU
146
−1.427
54.755
−4.705
1.00
50.76


ATOM
117
C
LEU
146
−1.915
54.476
−6.134
1.00
51.52


ATOM
118
O
LEU
146
−2.141
55.419
−6.927
1.00
51.71


ATOM
119
CB
LEU
146
−2.560
55.248
−3.800
1.00
50.62


ATOM
120
CG
LEU
146
−3.742
54.279
−3.605
1.00
50.27


ATOM
121
CD1
LEU
146
−4.266
54.208
−2.164
1.00
49.21


ATOM
122
CD2
LEU
146
−4.852
54.635
−4.576
1.00
50.20


ATOM
123
N
CYS
147
−2.050
53.195
−6.469
1.00
51.52


ATOM
124
CA
CYS
147
−2.304
52.802
−7.849
1.00
52.46


ATOM
125
C
CYS
147
−3.773
52.944
−8.331
1.00
53.73


ATOM
126
O
CYS
147
−4.690
52.294
−7.788
1.00
53.40


ATOM
127
CB
CYS
147
−1.804
51.375
−8.098
1.00
52.50


ATOM
128
SG
CYS
147
−2.131
50.800
−9.803
1.00
51.33


ATOM
129
N
PRO
148
−3.988
53.744
−9.400
1.00
54.93


ATOM
130
CA
PRO
148
−5.373
53.975
−9.860
1.00
55.87


ATOM
131
C
PRO
148
−6.026
52.699
−10.446
1.00
56.77


ATOM
132
O
PRO
148
−7.222
52.445
−10.198
1.00
56.68


ATOM
133
CB
PRO
148
−5.243
55.099
−10.909
1.00
55.91


ATOM
134
CG
PRO
148
−3.778
55.216
−11.232
1.00
55.66


ATOM
135
CD
PRO
148
−2.970
54.424
−10.237
1.00
55.10


ATOM
136
N
CYS
149
−5.232
51.900
−11.172
1.00
57.41


ATOM
137
CA
CYS
149
−5.692
50.637
−11.765
1.00
57.40


ATOM
138
C
CYS
149
−6.185
49.651
−10.685
1.00
57.29


ATOM
139
O
CYS
149
−7.265
49.043
−10.819
1.00
56.51


ATOM
140
CB
CYS
149
−4.577
50.006
−12.613
1.00
57.61


ATOM
141
SG
CYS
149
−5.106
48.508
−13.511
1.00
59.83


ATOM
142
N
SER
150
−5.389
49.517
−9.621
1.00
57.10


ATOM
143
CA
SER
150
−5.755
48.730
−8.438
1.00
57.37


ATOM
144
C
SER
150
−7.159
49.087
−7.927
1.00
57.54


ATOM
145
O
SER
150
−8.069
48.243
−7.942
1.00
56.90


ATOM
146
CB
SER
150
−4.699
48.908
−7.315
1.00
57.56


ATOM
147
OG
SER
150
−4.960
48.056
−6.196
1.00
56.24


ATOM
148
N
LYS
151
−7.325
50.335
−7.480
1.00
58.20


ATOM
149
CA
LYS
151
−8.614
50.826
−6.980
1.00
58.78


ATOM
150
C
LYS
151
−9.768
50.518
−7.953
1.00
59.60


ATOM
151
O
LYS
151
−10.820
49.980
−7.548
1.00
59.74


ATOM
152
CB
LYS
151
−8.530
52.335
−6.737
1.00
58.67


ATOM
153
CG
LYS
151
−9.859
52.996
−6.372
1.00
57.80


ATOM
154
CD
LYS
151
−9.711
54.513
−6.375
1.00
57.00


ATOM
155
CE
LYS
151
−10.975
55.191
−5.868
1.00
56.13


ATOM
156
NZ
LYS
151
−10.706
56.603
−5.487
1.00
54.37


ATOM
157
N
GLU
152
−9.526
50.867
−9.222
1.00
60.08


ATOM
158
CA
GLU
152
−10.491
50.858
−10.326
1.00
60.84


ATOM
159
C
GLU
152
−11.066
49.467
−10.619
1.00
60.69


ATOM
160
O
GLU
152
−12.257
49.323
−10.912
1.00
60.54


ATOM
161
CB
GLU
152
−9.782
51.379
−11.572
1.00
61.06


ATOM
162
CG
GLU
152
−10.668
51.860
−12.727
1.00
64.00


ATOM
163
CD
GLU
152
−9.947
52.910
−13.573
1.00
65.38


ATOM
164
OE1
GLU
152
−8.784
52.679
−13.986
1.00
65.59


ATOM
165
OE2
GLU
152
−10.537
53.987
−13.794
1.00
67.79


ATOM
166
N
ILE
153
−10.199
48.459
−10.551
1.00
60.40


ATOM
167
CA
ILE
153
−10.560
47.088
−10.885
1.00
59.97


ATOM
168
C
ILE
153
−11.005
46.287
−9.649
1.00
59.93


ATOM
169
O
ILE
153
−11.676
45.255
−9.806
1.00
59.92


ATOM
170
CB
ILE
153
−9.396
46.345
−11.633
1.00
60.11


ATOM
171
CG1
ILE
153
−8.231
46.011
−10.666
1.00
59.91


ATOM
172
CG2
ILE
153
−8.954
47.141
−12.886
1.00
59.57


ATOM
173
CD1
ILE
153
−7.180
45.087
−11.244
1.00
59.73


ATOM
174
N
SER
154
−10.639
46.762
−8.442
1.00
59.44


ATOM
175
CA
SER
154
−10.934
46.046
−7.191
1.00
59.16


ATOM
176
C
SER
154
−12.228
46.524
−6.536
1.00
59.11


ATOM
177
O
SER
154
−12.506
47.729
−6.506
1.00
58.66


ATOM
178
CB
SER
154
−9.777
46.159
−6.179
1.00
59.05


ATOM
179
OG
SER
154
−8.528
45.889
−6.786
1.00
58.46


ATOM
180
N
GLN
155
−12.998
45.574
−5.992
1.00
59.19


ATOM
181
CA
GLN
155
−14.252
45.887
−5.279
1.00
59.20


ATOM
182
C
GLN
155
−13.990
46.642
−3.969
1.00
58.56


ATOM
183
O
GLN
155
−14.872
47.344
−3.441
1.00
58.43


ATOM
184
CB
GLN
155
−15.103
44.620
−5.037
1.00
59.42


ATOM
185
CG
GLN
155
−14.478
43.547
−4.109
1.00
59.96


ATOM
186
CD
GLN
155
−15.294
42.235
−4.047
1.00
60.84


ATOM
187
OE1
GLN
155
−16.514
42.259
−3.833
1.00
63.53


ATOM
188
NE2
GLN
155
−14.613
41.090
−4.221
1.00
61.62


ATOM
189
N
TYR
156
−12.775
46.479
−3.447
1.00
57.89


ATOM
190
CA
TYR
156
−12.301
47.244
−2.290
1.00
57.36


ATOM
191
C
TYR
156
−10.756
47.310
−2.288
1.00
56.68


ATOM
192
O
TYR
156
−10.080
46.428
−2.857
1.00
55.91


ATOM
193
CB
TYR
156
−12.874
46.699
−0.957
1.00
57.64


ATOM
194
CG
TYR
156
−13.016
45.174
−0.860
1.00
59.03


ATOM
195
CD1
TYR
156
−11.895
44.325
−0.994
1.00
59.96


ATOM
196
CD2
TYR
156
−14.268
44.578
−0.624
1.00
60.16


ATOM
197
CE1
TYR
156
−12.014
42.918
−0.915
1.00
59.50


ATOM
198
CE2
TYR
156
−14.399
43.161
−0.535
1.00
60.74


ATOM
199
CZ
TYR
156
−13.260
42.346
−0.684
1.00
59.41


ATOM
200
OH
TYR
156
−13.355
40.974
−0.586
1.00
58.74


ATOM
201
N
GLY
157
−10.224
48.381
−1.686
1.00
55.88


ATOM
202
CA
GLY
157
−8.782
48.552
−1.486
1.00
54.70


ATOM
203
C
GLY
157
−8.046
48.941
−2.750
1.00
53.87


ATOM
204
O
GLY
157
−8.628
48.988
−3.838
1.00
53.85


ATOM
205
N
ALA
158
−6.753
49.211
−2.600
1.00
53.06


ATOM
206
CA
ALA
158
−5.889
49.638
−3.704
1.00
52.34


ATOM
207
C
ALA
158
−4.458
49.573
−3.233
1.00
51.79


ATOM
208
O
ALA
158
−4.116
50.133
−2.176
1.00
51.74


ATOM
209
CB
ALA
158
−6.210
51.065
−4.162
1.00
52.30


ATOM
210
N
HIS
159
−3.601
48.919
−4.006
1.00
50.50


ATOM
211
CA
HIS
159
−2.245
48.777
−3.514
1.00
49.70


ATOM
212
C
HIS
159
−1.569
50.148
−3.570
1.00
49.57


ATOM
213
O
HIS
159
−1.826
50.969
−4.477
1.00
49.86


ATOM
214
CB
HIS
159
−1.439
47.699
−4.251
1.00
48.45


ATOM
215
CG
HIS
159
−0.801
48.164
−5.524
1.00
45.98


ATOM
216
ND1
HIS
159
0.410
48.828
−5.551
1.00
43.16


ATOM
217
CD2
HIS
159
−1.178
48.011
−6.819
1.00
42.93


ATOM
218
CE1
HIS
159
0.738
49.088
−6.808
1.00
42.42


ATOM
219
NE2
HIS
159
−0.194
48.579
−7.595
1.00
39.71


ATOM
220
N
ASN
160
−0.746
50.384
−2.560
1.00
49.49


ATOM
221
CA
ASN
160
0.054
51.594
−2.464
1.00
48.81


ATOM
222
C
ASN
160
1.412
51.224
−1.879
1.00
48.38


ATOM
223
O
ASN
160
1.642
50.069
−1.462
1.00
47.84


ATOM
224
CB
ASN
160
−0.673
52.701
−1.658
1.00
48.67


ATOM
225
CG
ASN
160
−1.276
52.196
−0.336
1.00
48.57


ATOM
226
OD1
ASN
160
−2.384
51.659
−0.308
1.00
49.39


ATOM
227
ND2
ASN
160
−0.557
52.409
0.762
1.00
47.12


ATOM
228
N
GLN
161
2.316
52.203
−1.878
1.00
47.92


ATOM
229
CA
GLN
161
3.710
51.989
−1.502
1.00
47.53


ATOM
230
C
GLN
161
4.428
53.326
−1.401
1.00
47.31


ATOM
231
O
GLN
161
3.974
54.353
−1.960
1.00
47.48


ATOM
232
CB
GLN
161
4.425
51.114
−2.542
1.00
47.08


ATOM
233
CG
GLN
161
4.320
51.651
−3.982
1.00
47.63


ATOM
234
CD
GLN
161
3.004
51.296
−4.648
1.00
48.13


ATOM
235
OE1
GLN
161
2.504
50.166
−4.487
1.00
47.49


ATOM
236
NE2
GLN
161
2.426
52.249
−5.397
1.00
48.31


ATOM
237
N
ARG
162
5.536
53.313
−0.668
1.00
46.28


ATOM
238
CA
ARG
162
6.427
54.435
−0.704
1.00
45.81


ATOM
239
C
ARG
162
7.032
54.593
−2.125
1.00
45.47


ATOM
240
O
ARG
162
7.245
53.605
−2.901
1.00
44.60


ATOM
241
CB
ARG
162
7.495
54.348
0.389
1.00
45.64


ATOM
242
CG
ARG
162
7.999
55.693
0.859
1.00
45.77


ATOM
243
CD
ARG
162
9.102
55.488
1.931
1.00
46.20


ATOM
244
NE
ARG
162
8.617
54.789
3.121
1.00
43.09


ATOM
245
CZ
ARG
162
9.405
54.167
4.011
1.00
45.13


ATOM
246
NH1
ARG
162
10.739
54.160
3.862
1.00
43.75


ATOM
247
NH2
ARG
162
8.864
53.570
5.077
1.00
44.59


ATOM
248
N
SER
163
7.246
55.858
−2.479
1.00
44.43


ATOM
249
CA
SER
163
7.914
56.146
−3.716
1.00
43.91


ATOM
250
C
SER
163
8.854
57.331
−3.548
1.00
42.32


ATOM
251
O
SER
163
8.597
58.236
−2.760
1.00
43.00


ATOM
252
CB
SER
163
6.887
56.300
−4.856
1.00
44.01


ATOM
253
OG
SER
163
6.306
57.569
−4.855
1.00
47.10


ATOM
254
N
ILE
181
10.703
70.756
−2.585
1.00
27.65


ATOM
255
CA
ILE
181
9.879
69.847
−1.798
1.00
28.15


ATOM
256
C
ILE
181
8.375
70.134
−1.999
1.00
29.61


ATOM
257
O
ILE
181
7.584
69.196
−2.237
1.00
30.26


ATOM
258
CB
ILE
181
10.259
69.876
−0.283
1.00
28.11


ATOM
259
CG1
ILE
181
11.633
69.233
−0.105
1.00
25.88


ATOM
260
CG2
ILE
181
9.239
69.090
0.517
1.00
26.16


ATOM
261
CD1
ILE
181
12.443
69.751
1.114
1.00
27.81


ATOM
262
N
ASP
182
7.974
71.413
−1.900
1.00
30.08


ATOM
263
CA
ASP
182
6.555
71.756
−2.064
1.00
31.00


ATOM
264
C
ASP
182
6.038
71.466
−3.464
1.00
31.45


ATOM
265
O
ASP
182
4.964
70.923
−3.592
1.00
32.21


ATOM
266
CB
ASP
182
6.253
73.205
−1.669
1.00
31.45


ATOM
267
CG
ASP
182
6.358
73.420
−0.194
1.00
33.00


ATOM
268
OD1
ASP
182
6.060
72.499
0.589
1.00
38.70


ATOM
269
OD2
ASP
182
6.807
74.473
0.202
1.00
33.35


ATOM
270
N
TYR
183
6.801
71.776
−4.512
1.00
31.67


ATOM
271
CA
TYR
183
6.346
71.379
−5.878
1.00
31.88


ATOM
272
C
TYR
183
5.996
69.892
−6.001
1.00
31.33


ATOM
273
O
TYR
183
5.079
69.513
−6.769
1.00
31.50


ATOM
274
CB
TYR
183
7.407
71.695
−6.959
1.00
32.44


ATOM
275
CG
TYR
183
7.509
73.139
−7.389
1.00
32.80


ATOM
276
CD1
TYR
183
6.354
73.909
−7.666
1.00
34.47


ATOM
277
CD2
TYR
183
8.759
73.729
−7.578
1.00
32.37


ATOM
278
CE1
TYR
183
6.468
75.247
−8.101
1.00
33.02


ATOM
279
CE2
TYR
183
8.889
75.045
−7.983
1.00
31.79


ATOM
280
CZ
TYR
183
7.731
75.807
−8.253
1.00
33.92


ATOM
281
OH
TYR
183
7.879
77.117
−8.689
1.00
34.75


ATOM
282
N
VAL
184
6.739
69.036
−5.299
1.00
31.13


ATOM
283
CA
VAL
184
6.472
67.566
−5.349
1.00
30.51


ATOM
284
C
VAL
184
5.338
67.145
−4.441
1.00
31.17


ATOM
285
O
VAL
184
4.415
66.457
−4.858
1.00
31.57


ATOM
286
CB
VAL
184
7.746
66.711
−4.997
1.00
30.57


ATOM
287
CG1
VAL
184
7.398
65.190
−5.041
1.00
29.99


ATOM
288
CG2
VAL
184
8.844
67.002
−5.995
1.00
31.45


ATOM
289
N
GLU
185
5.420
67.543
−3.173
1.00
31.99


ATOM
290
CA
GLU
185
4.476
67.096
−2.159
1.00
33.75


ATOM
291
C
GLU
185
3.061
67.540
−2.469
1.00
35.59


ATOM
292
O
GLU
185
2.087
66.813
−2.163
1.00
34.88


ATOM
293
CB
GLU
185
4.923
67.550
−0.764
1.00
33.52


ATOM
294
CG
GLU
185
6.124
66.727
−0.249
1.00
34.66


ATOM
295
CD
GLU
185
6.472
67.088
1.180
1.00
37.62


ATOM
296
OE1
GLU
185
6.132
68.250
1.552
1.00
34.07


ATOM
297
OE2
GLU
185
7.071
66.223
1.905
1.00
39.40


ATOM
298
N
THR
186
2.962
68.703
−3.113
1.00
37.29


ATOM
299
CA
THR
186
1.671
69.219
−3.581
1.00
39.44


ATOM
300
C
THR
186
0.997
68.210
−4.470
1.00
39.55


ATOM
301
O
THR
186
−0.216
68.035
−4.416
1.00
39.96


ATOM
302
CB
THR
186
1.831
70.510
−4.351
1.00
39.43


ATOM
303
OG1
THR
186
1.926
71.571
−3.413
1.00
41.26


ATOM
304
CG2
THR
186
0.608
70.760
−5.263
1.00
42.27


ATOM
305
N
GLN
187
1.809
67.527
−5.263
1.00
40.30


ATOM
306
CA
GLN
187
1.310
66.644
−6.305
1.00
40.35


ATOM
307
C
GLN
187
1.120
65.204
−5.847
1.00
40.86


ATOM
308
O
GLN
187
0.467
64.414
−6.546
1.00
40.53


ATOM
309
CB
GLN
187
2.233
66.690
−7.547
1.00
40.36


ATOM
310
CG
GLN
187
2.314
68.075
−8.228
1.00
39.80


ATOM
311
CD
GLN
187
0.947
68.577
−8.653
1.00
39.36


ATOM
312
OE1
GLN
187
0.005
67.783
−8.777
1.00
39.91


ATOM
313
NE2
GLN
187
0.828
69.887
−8.887
1.00
35.15


ATOM
314
N
ALA
188
1.671
64.843
−4.691
1.00
41.85


ATOM
315
CA
ALA
188
1.614
63.438
−4.252
1.00
43.17


ATOM
316
C
ALA
188
0.192
62.942
−4.004
1.00
43.55


ATOM
317
O
ALA
188
−0.660
63.715
−3.577
1.00
43.98


ATOM
318
CB
ALA
188
2.520
63.199
−2.984
1.00
43.74


ATOM
319
N
SER
189
−0.068
61.656
−4.297
1.00
44.60


ATOM
320
CA
SER
189
−1.298
60.977
−3.803
1.00
45.06


ATOM
321
C
SER
189
−1.502
61.373
−2.327
1.00
45.29


ATOM
322
O
SER
189
−2.600
61.760
−1.911
1.00
45.23


ATOM
323
CB
SER
189
−1.173
59.435
−3.887
1.00
45.28


ATOM
324
OG
SER
189
−1.596
58.905
−5.133
1.00
44.89


ATOM
325
N
CYS
190
−0.429
61.225
−1.550
1.00
45.95


ATOM
326
CA
CYS
190
−0.320
61.796
−0.189
1.00
46.60


ATOM
327
C
CYS
190
1.148
61.866
0.259
1.00
46.70


ATOM
328
O
CYS
190
1.985
61.031
−0.126
1.00
46.76


ATOM
329
CB
CYS
190
−1.153
61.017
0.841
1.00
46.68


ATOM
330
SG
CYS
190
−1.465
61.939
2.425
1.00
48.51


ATOM
331
N
GLN
191
1.450
62.873
1.064
1.00
46.03


ATOM
332
CA
GLN
191
2.796
63.026
1.622
1.00
46.34


ATOM
333
C
GLN
191
2.995
62.247
2.921
1.00
45.74


ATOM
334
O
GLN
191
2.041
61.751
3.533
1.00
45.80


ATOM
335
CB
GLN
191
3.115
64.501
1.856
1.00
46.24


ATOM
336
CG
GLN
191
1.986
65.240
2.522
1.00
46.12


ATOM
337
CD
GLN
191
2.257
66.708
2.616
1.00
45.71


ATOM
338
OE1
GLN
191
3.128
67.120
3.362
1.00
42.50


ATOM
339
NE2
GLN
191
1.513
67.518
1.839
1.00
47.50


ATOM
340
N
LEU
192
4.251
62.176
3.341
1.00
45.93


ATOM
341
CA
LEU
192
4.634
61.393
4.508
1.00
45.42


ATOM
342
C
LEU
192
4.759
62.259
5.762
1.00
45.84


ATOM
343
O
LEU
192
5.036
63.474
5.694
1.00
45.09


ATOM
344
CB
LEU
192
5.940
60.636
4.234
1.00
45.16


ATOM
345
CG
LEU
192
5.993
59.679
3.044
1.00
43.78


ATOM
346
CD1
LEU
192
7.329
58.955
3.016
1.00
43.93


ATOM
347
CD2
LEU
192
4.893
58.657
3.093
1.00
43.70


ATOM
348
N
TYR
193
4.520
61.615
6.906
1.00
45.73


ATOM
349
CA
TYR
193
4.756
62.218
8.203
1.00
45.73


ATOM
350
C
TYR
193
5.404
61.167
9.120
1.00
46.31


ATOM
351
O
TYR
193
5.035
59.967
9.095
1.00
45.28


ATOM
352
CB
TYR
193
3.445
62.738
8.812
1.00
45.20


ATOM
353
CG
TYR
193
2.638
63.691
7.907
1.00
44.11


ATOM
354
CD1
TYR
193
2.823
65.078
7.964
1.00
43.87


ATOM
355
CD2
TYR
193
1.683
63.186
6.998
1.00
44.60


ATOM
356
CE1
TYR
193
2.068
65.944
7.143
1.00
43.56


ATOM
357
CE2
TYR
193
0.930
64.029
6.190
1.00
42.74


ATOM
358
CZ
TYR
193
1.133
65.409
6.273
1.00
42.90


ATOM
359
OH
TYR
193
0.401
66.227
5.474
1.00
44.37


ATOM
360
N
GLY
194
6.385
61.623
9.896
1.00
47.12


ATOM
361
CA
GLY
194
6.981
60.801
10.936
1.00
48.68


ATOM
362
C
GLY
194
5.913
60.387
11.934
1.00
49.53


ATOM
363
O
GLY
194
5.722
59.183
12.171
1.00
49.81


ATOM
364
N
LEU
195
5.188
61.368
12.482
1.00
50.33


ATOM
365
CA
LEU
195
4.240
61.095
13.579
1.00
51.06


ATOM
366
C
LEU
195
2.784
61.345
13.193
1.00
52.16


ATOM
367
O
LEU
195
2.389
62.489
12.837
1.00
51.75


ATOM
368
CB
LEU
195
4.612
61.889
14.840
1.00
50.86


ATOM
369
CG
LEU
195
3.940
61.618
16.195
1.00
50.48


ATOM
370
CD1
LEU
195
4.719
62.355
17.275
1.00
49.39


ATOM
371
CD2
LEU
195
2.516
62.141
16.207
1.00
51.52


ATOM
372
N
LEU
196
1.990
60.277
13.290
1.00
53.08


ATOM
373
CA
LEU
196
0.583
60.340
12.936
1.00
55.19


ATOM
374
C
LEU
196
−0.282
59.778
14.069
1.00
56.77


ATOM
375
O
LEU
196
0.000
58.705
14.604
1.00
56.95


ATOM
376
CB
LEU
196
0.326
59.604
11.612
1.00
54.79


ATOM
377
CG
LEU
196
0.949
60.235
10.346
1.00
55.32


ATOM
378
CD1
LEU
196
0.931
59.273
9.136
1.00
54.75


ATOM
379
CD2
LEU
196
0.317
61.613
9.990
1.00
54.04


ATOM
380
N
LYS
197
−1.314
60.519
14.463
1.00
58.59


ATOM
381
CA
LYS
197
−2.334
59.933
15.353
1.00
60.40


ATOM
382
C
LYS
197
−3.393
59.174
14.545
1.00
60.81


ATOM
383
O
LYS
197
−3.364
59.195
13.294
1.00
60.59


ATOM
384
CB
LYS
197
−2.941
60.970
16.316
1.00
60.82


ATOM
385
CG
LYS
197
−2.344
60.884
17.753
1.00
63.00


ATOM
386
CD
LYS
197
−0.793
60.988
17.781
1.00
64.23


ATOM
387
CE
LYS
197
−0.195
60.868
19.202
1.00
64.55


ATOM
388
NZ
LYS
197
−0.184
59.471
19.739
1.00
64.56


ATOM
389
N
ARG
198
−4.289
58.479
15.256
1.00
61.03


ATOM
390
CA
ARG
198
−5.388
57.746
14.631
1.00
61.98


ATOM
391
C
ARG
198
−6.168
58.558
13.574
1.00
61.01


ATOM
392
O
ARG
198
−6.279
58.122
12.435
1.00
60.94


ATOM
393
CB
ARG
198
−6.332
57.144
15.690
1.00
62.12


ATOM
394
CG
ARG
198
−6.388
55.616
15.679
1.00
64.00


ATOM
395
CD
ARG
198
−6.848
54.991
17.028
1.00
64.71


ATOM
396
NE
ARG
198
−7.001
53.536
16.895
1.00
70.51


ATOM
397
CZ
ARG
198
−8.173
52.893
16.895
1.00
71.39


ATOM
398
NH1
ARG
198
−9.309
53.569
17.049
1.00
74.34


ATOM
399
NH2
ARG
198
−8.216
51.570
16.745
1.00
73.50


ATOM
400
N
PRO
199
−6.712
59.735
13.949
1.00
60.31


ATOM
401
CA
PRO
199
−7.394
60.542
12.926
1.00
59.80


ATOM
402
C
PRO
199
−6.506
60.946
11.725
1.00
59.02


ATOM
403
O
PRO
199
−6.975
60.893
10.582
1.00
58.60


ATOM
404
CB
PRO
199
−7.891
61.778
13.706
1.00
60.10


ATOM
405
CG
PRO
199
−7.149
61.780
15.009
1.00
60.56


ATOM
406
CD
PRO
199
−6.771
60.356
15.291
1.00
60.60


ATOM
407
N
ASP
200
−5.247
61.316
11.978
1.00
58.37


ATOM
408
CA
ASP
200
−4.289
61.627
10.889
1.00
58.09


ATOM
409
C
ASP
200
−4.123
60.454
9.932
1.00
57.97


ATOM
410
O
ASP
200
−4.210
60.623
8.707
1.00
58.11


ATOM
411
CB
ASP
200
−2.916
62.014
11.440
1.00
57.41


ATOM
412
CG
ASP
200
−2.987
63.149
12.416
1.00
56.87


ATOM
413
OD1
ASP
200
−3.551
64.204
12.044
1.00
56.53


ATOM
414
OD2
ASP
200
−2.471
62.986
13.545
1.00
54.07


ATOM
415
N
GLU
201
−3.876
59.271
10.498
1.00
57.96


ATOM
416
CA
GLU
201
−3.801
58.036
9.707
1.00
58.04


ATOM
417
C
GLU
201
−5.089
57.778
8.868
1.00
57.99


ATOM
418
O
GLU
201
−5.010
57.296
7.717
1.00
57.08


ATOM
419
CB
GLU
201
−3.411
56.822
10.577
1.00
58.12


ATOM
420
CG
GLU
201
−3.762
55.479
9.910
1.00
59.81


ATOM
421
CD
GLU
201
−2.850
54.339
10.275
1.00
59.25


ATOM
422
OE1
GLU
201
−2.353
54.293
11.424
1.00
61.24


ATOM
423
OE2
GLU
201
−2.653
53.472
9.394
1.00
61.33


ATOM
424
N
LYS
202
−6.258
58.106
9.444
1.00
58.11


ATOM
425
CA
LYS
202
−7.538
58.002
8.733
1.00
58.01


ATOM
426
C
LYS
202
−7.538
58.940
7.519
1.00
57.58


ATOM
427
O
LYS
202
−7.884
58.514
6.416
1.00
57.11


ATOM
428
CB
LYS
202
−8.729
58.282
9.670
1.00
58.00


ATOM
429
CG
LYS
202
−10.094
58.289
8.991
1.00
58.29


ATOM
430
CD
LYS
202
−11.235
58.423
10.025
1.00
58.66


ATOM
431
CE
LYS
202
−12.517
59.076
9.442
1.00
58.41


ATOM
432
NZ
LYS
202
−12.846
58.760
8.009
1.00
59.05


ATOM
433
N
TYR
203
−7.132
60.198
7.752
1.00
57.29


ATOM
434
CA
TYR
203
−7.027
61.255
6.731
1.00
56.76


ATOM
435
C
TYR
203
−6.051
60.847
5.622
1.00
55.73


ATOM
436
O
TYR
203
−6.365
60.900
4.439
1.00
55.19


ATOM
437
CB
TYR
203
−6.594
62.584
7.391
1.00
57.82


ATOM
438
CG
TYR
203
−6.403
63.759
6.431
1.00
57.69


ATOM
439
CD1
TYR
203
−7.378
64.778
6.304
1.00
59.41


ATOM
440
CD2
TYR
203
−5.257
63.838
5.633
1.00
59.00


ATOM
441
CE1
TYR
203
−7.192
65.857
5.410
1.00
59.51


ATOM
442
CE2
TYR
203
−5.065
64.889
4.745
1.00
60.75


ATOM
443
CZ
TYR
203
−6.017
65.900
4.636
1.00
58.13


ATOM
444
OH
TYR
203
−5.754
66.922
3.740
1.00
60.67


ATOM
445
N
VAL
204
−4.866
60.422
6.026
1.00
54.95


ATOM
446
CA
VAL
204
−3.835
60.017
5.072
1.00
54.58


ATOM
447
C
VAL
204
−4.290
58.782
4.213
1.00
53.79


ATOM
448
O
VAL
204
−4.091
58.758
2.986
1.00
52.60


ATOM
449
CB
VAL
204
−2.469
59.851
5.822
1.00
54.92


ATOM
450
CG1
VAL
204
−1.523
58.898
5.116
1.00
56.19


ATOM
451
CG2
VAL
204
−1.820
61.233
6.087
1.00
53.61


ATOM
452
N
THR
205
−4.949
57.801
4.851
1.00
53.09


ATOM
453
CA
THR
205
−5.456
56.626
4.132
1.00
52.58


ATOM
454
C
THR
205
−6.437
57.018
3.017
1.00
53.09


ATOM
455
O
THR
205
−6.340
56.514
1.878
1.00
52.50


ATOM
456
CB
THR
205
−6.109
55.579
5.091
1.00
52.24


ATOM
457
OG1
THR
205
−5.109
55.049
5.976
1.00
50.47


ATOM
458
CG2
THR
205
−6.716
54.420
4.305
1.00
51.46


ATOM
459
N
GLU
206
−7.352
57.929
3.365
1.00
53.01


ATOM
460
CA
GLU
206
−8.444
58.355
2.489
1.00
53.57


ATOM
461
C
GLU
206
−7.956
59.243
1.363
1.00
53.60


ATOM
462
O
GLU
206
−8.280
58.979
0.203
1.00
53.68


ATOM
463
CB
GLU
206
−9.563
59.021
3.295
1.00
53.31


ATOM
464
CG
GLU
206
−10.150
58.061
4.283
1.00
54.66


ATOM
465
CD
GLU
206
−11.279
58.627
5.124
1.00
55.83


ATOM
466
OE1
GLU
206
−11.449
59.865
5.199
1.00
58.27


ATOM
467
OE2
GLU
206
−11.993
57.802
5.731
1.00
57.86


ATOM
468
N
LYS
207
−7.171
60.270
1.714
1.00
53.98


ATOM
469
CA
LYS
207
−6.504
61.175
0.746
1.00
54.40


ATOM
470
C
LYS
207
−5.834
60.360
−0.379
1.00
54.04


ATOM
471
O
LYS
207
−6.116
60.553
−1.572
1.00
53.03


ATOM
472
CB
LYS
207
−5.463
62.044
1.481
1.00
54.50


ATOM
473
CG
LYS
207
−4.727
63.081
0.646
1.00
56.04


ATOM
474
CD
LYS
207
−3.784
63.911
1.522
1.00
58.59


ATOM
475
CE
LYS
207
−3.018
64.957
0.713
1.00
59.46


ATOM
476
NZ
LYS
207
−2.119
65.730
1.635
1.00
58.18


ATOM
477
N
ALA
208
−4.973
59.429
0.029
1.00
54.31


ATOM
478
CA
ALA
208
−4.238
58.613
−0.900
1.00
55.01


ATOM
479
C
ALA
208
−5.226
57.838
−1.799
1.00
55.58


ATOM
480
O
ALA
208
−5.072
57.834
−3.021
1.00
55.47


ATOM
481
CB
ALA
208
−3.292
57.663
−0.130
1.00
55.20


ATOM
482
N
TYR
209
−6.243
57.217
−1.183
1.00
57.15


ATOM
483
CA
TYR
209
−7.312
56.466
−1.915
1.00
56.96


ATOM
484
C
TYR
209
−8.039
57.342
−2.964
1.00
56.61


ATOM
485
O
TYR
209
−8.230
56.916
−4.130
1.00
56.39


ATOM
486
CB
TYR
209
−8.321
55.842
−0.925
1.00
57.07


ATOM
487
CG
TYR
209
−9.265
54.766
−1.483
1.00
57.70


ATOM
488
CD1
TYR
209
−8.809
53.454
−1.731
1.00
58.72


ATOM
489
CD2
TYR
209
−10.631
55.048
−1.719
1.00
58.01


ATOM
490
CE1
TYR
209
−9.689
52.458
−2.216
1.00
59.35


ATOM
491
CE2
TYR
209
−11.506
54.068
−2.208
1.00
57.42


ATOM
492
CZ
TYR
209
−11.026
52.777
−2.451
1.00
55.90


ATOM
493
OH
TYR
209
−11.881
51.806
−2.917
1.00
58.74


ATOM
494
N
GLU
210
−8.389
58.570
−2.558
1.00
56.26


ATOM
495
CA
GLU
210
−9.155
59.505
−3.411
1.00
56.42


ATOM
496
C
GLU
210
−8.343
60.109
−4.566
1.00
56.04


ATOM
497
O
GLU
210
−8.907
60.607
−5.553
1.00
56.04


ATOM
498
CB
GLU
210
−9.743
60.642
−2.566
1.00
56.91


ATOM
499
CG
GLU
210
−10.701
60.175
−1.446
1.00
58.24


ATOM
500
CD
GLU
210
−10.842
61.207
−0.337
1.00
61.03


ATOM
501
OE1
GLU
210
−10.317
62.342
−0.514
1.00
63.30


ATOM
502
OE2
GLU
210
−11.480
60.889
0.700
1.00
60.60


ATOM
503
N
ASN
211
−7.021
60.028
−4.434
1.00
54.85


ATOM
504
CA
ASN
211
−6.079
60.747
−5.277
1.00
54.55


ATOM
505
C
ASN
211
−5.033
59.735
−5.879
1.00
53.11


ATOM
506
O
ASN
211
−3.831
59.980
−5.806
1.00
52.60


ATOM
507
CB
ASN
211
−5.479
61.894
−4.393
1.00
55.22


ATOM
508
CG
ASN
211
−4.332
62.682
−5.055
1.00
58.06


ATOM
509
OD1
ASN
211
−4.018
62.510
−6.243
1.00
60.91


ATOM
510
ND2
ASN
211
−3.692
63.565
−4.261
1.00
59.82


ATOM
511
N
PRO
212
−5.496
58.597
−6.491
1.00
51.64


ATOM
512
CA
PRO
212
−4.515
57.628
−6.998
1.00
50.32


ATOM
513
C
PRO
212
−3.784
58.231
−8.212
1.00
49.35


ATOM
514
O
PRO
212
−4.417
58.916
−9.022
1.00
48.96


ATOM
515
CB
PRO
212
−5.386
56.455
−7.461
1.00
50.49


ATOM
516
CG
PRO
212
−6.674
57.098
−7.891
1.00
51.04


ATOM
517
CD
PRO
212
−6.876
58.180
−6.826
1.00
51.68


ATOM
518
N
LYS
213
−2.479
57.973
−8.318
1.00
47.51


ATOM
519
CA
LYS
213
−1.648
58.498
−9.375
1.00
46.52


ATOM
520
C
LYS
213
−0.638
57.445
−9.769
1.00
46.02


ATOM
521
O
LYS
213
0.019
56.851
−8.906
1.00
46.15


ATOM
522
CB
LYS
213
−0.893
59.737
−8.909
1.00
46.06


ATOM
523
CG
LYS
213
−1.769
60.976
−8.686
1.00
45.94


ATOM
524
CD
LYS
213
−1.021
62.289
−9.006
1.00
42.30


ATOM
525
CE
LYS
213
−1.946
63.481
−8.706
1.00
42.12


ATOM
526
NZ
LYS
213
−1.223
64.796
−8.755
1.00
41.19


ATOM
527
N
PHE
214
−0.534
57.201
−11.073
1.00
45.52


ATOM
528
CA
PHE
214
0.540
56.384
−11.634
1.00
45.58


ATOM
529
C
PHE
214
1.875
57.134
−11.471
1.00
43.76


ATOM
530
O
PHE
214
1.897
58.364
−11.285
1.00
43.89


ATOM
531
CB
PHE
214
0.299
56.150
−13.141
1.00
46.89


ATOM
532
CG
PHE
214
−0.840
55.212
−13.471
1.00
48.64


ATOM
533
CD1
PHE
214
−0.830
53.881
−13.033
1.00
51.01


ATOM
534
CD2
PHE
214
−1.890
55.646
−14.309
1.00
50.55


ATOM
535
CE1
PHE
214
−1.876
52.991
−13.378
1.00
52.20


ATOM
536
CE2
PHE
214
−2.938
54.788
−14.672
1.00
50.78


ATOM
537
CZ
PHE
214
−2.938
53.451
−14.199
1.00
51.48


ATOM
538
N
VAL
215
2.986
56.408
−11.572
1.00
41.22


ATOM
539
CA
VAL
215
4.268
57.060
−11.753
1.00
39.38


ATOM
540
C
VAL
215
4.255
58.075
−12.936
1.00
38.44


ATOM
541
O
VAL
215
4.831
59.167
−12.830
1.00
37.18


ATOM
542
CB
VAL
215
5.451
56.045
−11.859
1.00
39.18


ATOM
543
CG1
VAL
215
5.390
55.182
−13.135
1.00
37.11


ATOM
544
CG2
VAL
215
6.681
56.782
−11.833
1.00
39.54


ATOM
545
N
GLU
216
3.578
57.712
−14.035
1.00
37.54


ATOM
546
CA
GLU
216
3.430
58.603
−15.200
1.00
36.83


ATOM
547
C
GLU
216
2.775
59.953
−14.819
1.00
36.37


ATOM
548
O
GLU
216
3.271
61.013
−15.164
1.00
35.59


ATOM
549
CB
GLU
216
2.592
57.931
−16.287
1.00
36.59


ATOM
550
CG
GLU
216
3.269
56.750
−17.002
1.00
36.95


ATOM
551
CD
GLU
216
2.843
55.395
−16.448
1.00
36.23


ATOM
552
OE1
GLU
216
2.424
55.387
−15.285
1.00
35.17


ATOM
553
OE2
GLU
216
2.953
54.341
−17.152
1.00
36.48


ATOM
554
N
ASP
217
1.666
59.879
−14.096
1.00
37.46


ATOM
555
CA
ASP
217
0.924
61.055
−13.575
1.00
37.41


ATOM
556
C
ASP
217
1.763
61.917
−12.679
1.00
36.40


ATOM
557
O
ASP
217
1.733
63.152
−12.781
1.00
35.80


ATOM
558
CB
ASP
217
−0.305
60.587
−12.782
1.00
39.17


ATOM
559
CG
ASP
217
−1.379
59.979
−13.689
1.00
42.59


ATOM
560
OD1
ASP
217
−1.611
60.541
−14.803
1.00
44.14


ATOM
561
OD2
ASP
217
−1.972
58.946
−13.294
1.00
45.24


ATOM
562
N
MET
218
2.523
61.279
−11.793
1.00
36.11


ATOM
563
CA
MET
218
3.384
62.025
−10.895
1.00
35.43


ATOM
564
C
MET
218
4.516
62.729
−11.624
1.00
33.47


ATOM
565
O
MET
218
4.761
63.892
−11.387
1.00
32.57


ATOM
566
CB
MET
218
3.919
61.129
−9.744
1.00
36.86


ATOM
567
CG
MET
218
4.835
61.863
−8.686
1.00
39.05


ATOM
568
SD
MET
218
4.098
63.050
−7.489
1.00
48.15


ATOM
569
CE
MET
218
2.385
62.882
−7.908
1.00
47.14


ATOM
570
N
VAL
219
5.233
62.058
−12.507
1.00
32.53


ATOM
571
CA
VAL
219
6.310
62.816
−13.169
1.00
32.64


ATOM
572
C
VAL
219
5.758
64.016
−13.970
1.00
32.02


ATOM
573
O
VAL
219
6.383
65.105
−13.996
1.00
30.73


ATOM
574
CB
VAL
219
7.290
61.951
−14.026
1.00
32.81


ATOM
575
CG1
VAL
219
8.108
61.031
−13.124
1.00
33.18


ATOM
576
CG2
VAL
219
6.570
61.164
−15.095
1.00
33.07


ATOM
577
N
ARG
220
4.613
63.799
−14.631
1.00
32.42


ATOM
578
CA
ARG
220
3.940
64.851
−15.425
1.00
32.49


ATOM
579
C
ARG
220
3.445
66.069
−14.650
1.00
33.39


ATOM
580
O
ARG
220
3.745
67.221
−15.037
1.00
34.66


ATOM
581
CB
ARG
220
2.814
64.264
−16.220
1.00
32.42


ATOM
582
CG
ARG
220
3.309
63.496
−17.434
1.00
31.64


ATOM
583
CD
ARG
220
2.123
62.782
−18.065
1.00
32.29


ATOM
584
NE
ARG
220
2.428
62.444
−19.436
1.00
34.95


ATOM
585
CZ
ARG
220
1.932
61.391
−20.059
1.00
35.09


ATOM
586
NH1
ARG
220
1.120
60.547
−19.417
1.00
33.56


ATOM
587
NH2
ARG
220
2.268
61.180
−21.319
1.00
36.65


ATOM
588
N
ASP
221
2.717
65.830
−13.566
1.00
34.07


ATOM
589
CA
ASP
221
2.290
66.894
−12.636
1.00
33.76


ATOM
590
C
ASP
221
3.446
67.711
−12.069
1.00
33.51


ATOM
591
O
ASP
221
3.342
68.931
−11.968
1.00
33.79


ATOM
592
CB
ASP
221
1.453
66.265
−11.505
1.00
34.70


ATOM
593
CG
ASP
221
0.124
65.715
−12.009
1.00
36.94


ATOM
594
OD1
ASP
221
−0.162
65.982
−13.197
1.00
40.28


ATOM
595
OD2
ASP
221
−0.626
65.034
−11.263
1.00
36.36


ATOM
596
N
VAL
222
4.559
67.058
−11.697
1.00
32.83


ATOM
597
CA
VAL
222
5.737
67.797
−11.232
1.00
31.91


ATOM
598
C
VAL
222
6.418
68.561
−12.389
1.00
32.92


ATOM
599
O
VAL
222
6.823
69.731
−12.243
1.00
32.48


ATOM
600
CB
VAL
222
6.756
66.875
−10.431
1.00
31.86


ATOM
601
CG1
VAL
222
8.053
67.588
−10.118
1.00
29.78


ATOM
602
CG2
VAL
222
6.119
66.313
−9.133
1.00
28.77


ATOM
603
N
ALA
223
6.553
67.923
−13.549
1.00
32.41


ATOM
604
CA
ALA
223
7.218
68.622
−14.660
1.00
32.79


ATOM
605
C
ALA
223
6.469
69.921
−15.061
1.00
32.87


ATOM
606
O
ALA
223
7.092
70.971
−15.365
1.00
32.40


ATOM
607
CB
ALA
223
7.311
67.714
−15.851
1.00
33.64


ATOM
608
N
THR
224
5.138
69.838
−15.076
1.00
33.30


ATOM
609
CA
THR
224
4.311
71.039
−15.348
1.00
34.28


ATOM
610
C
THR
224
4.709
72.191
−14.426
1.00
33.80


ATOM
611
O
THR
224
4.883
73.312
−14.896
1.00
32.18


ATOM
612
CB
THR
224
2.834
70.753
−15.250
1.00
34.79


ATOM
613
OG1
THR
224
2.527
69.657
−16.107
1.00
34.54


ATOM
614
CG2
THR
224
2.009
71.981
−15.738
1.00
38.37


ATOM
615
N
SER
225
4.876
71.926
−13.115
1.00
34.23


ATOM
616
CA
SER
225
5.217
73.008
−12.194
1.00
34.27


ATOM
617
C
SER
225
6.582
73.547
−12.546
1.00
34.88


ATOM
618
O
SER
225
6.833
74.788
−12.517
1.00
34.49


ATOM
619
CB
SER
225
5.208
72.552
−10.736
1.00
34.83


ATOM
620
OG
SER
225
3.879
72.289
−10.317
1.00
36.16


ATOM
621
N
LEU
226
7.499
72.638
−12.887
1.00
34.32


ATOM
622
CA
LEU
226
8.863
73.093
−13.123
1.00
34.58


ATOM
623
C
LEU
226
9.034
73.818
−14.480
1.00
35.09


ATOM
624
O
LEU
226
9.871
74.718
−14.624
1.00
35.39


ATOM
625
CB
LEU
226
9.867
71.920
−12.956
1.00
34.96


ATOM
626
CG
LEU
226
9.770
71.026
−11.699
1.00
33.32


ATOM
627
CD1
LEU
226
10.737
69.840
−11.796
1.00
29.72


ATOM
628
CD2
LEU
226
10.017
71.850
−10.444
1.00
31.90


ATOM
629
N
ILE
227
8.285
73.410
−15.499
1.00
35.24


ATOM
630
CA
ILE
227
8.359
74.134
−16.791
1.00
34.80


ATOM
631
C
ILE
227
7.912
75.610
−16.620
1.00
35.08


ATOM
632
O
ILE
227
8.456
76.548
−17.253
1.00
34.52


ATOM
633
CB
ILE
227
7.486
73.438
−17.862
1.00
35.35


ATOM
634
CG1
ILE
227
8.228
72.188
−18.401
1.00
35.35


ATOM
635
CG2
ILE
227
7.131
74.418
−18.992
1.00
35.51


ATOM
636
CD1
ILE
227
7.329
71.149
−19.011
1.00
35.08


ATOM
637
N
ALA
228
6.950
75.792
−15.727
1.00
35.42


ATOM
638
CA
ALA
228
6.324
77.073
−15.459
1.00
36.53


ATOM
639
C
ALA
228
7.183
78.037
−14.640
1.00
36.58


ATOM
640
O
ALA
228
7.024
79.270
−14.741
1.00
37.14


ATOM
641
CB
ALA
228
4.984
76.835
−14.774
1.00
36.82


ATOM
642
N
ASP
229
8.109
77.505
−13.850
1.00
36.37


ATOM
643
CA
ASP
229
8.973
78.352
−13.018
1.00
36.10


ATOM
644
C
ASP
229
10.034
78.994
−13.915
1.00
37.32


ATOM
645
O
ASP
229
10.792
78.279
−14.572
1.00
37.73


ATOM
646
CB
ASP
229
9.585
77.499
−11.897
1.00
35.82


ATOM
647
CG
ASP
229
10.310
78.324
−10.861
1.00
35.00


ATOM
648
OD1
ASP
229
11.209
79.106
−11.240
1.00
32.09


ATOM
649
OD2
ASP
229
9.966
78.202
−9.653
1.00
34.51


ATOM
650
N
PHE
242
7.931
51.871
−5.327
1.00
42.06


ATOM
651
CA
PHE
242
8.328
50.538
−4.849
1.00
43.01


ATOM
652
C
PHE
242
7.099
49.620
−4.761
1.00
43.06


ATOM
653
O
PHE
242
6.628
49.305
−3.649
1.00
41.83


ATOM
654
CB
PHE
242
9.160
50.645
−3.539
1.00
42.80


ATOM
655
CG
PHE
242
10.470
51.378
−3.748
1.00
43.34


ATOM
656
CD1
PHE
242
11.578
50.701
−4.232
1.00
43.78


ATOM
657
CD2
PHE
242
10.565
52.770
−3.542
1.00
43.59


ATOM
658
CE1
PHE
242
12.781
51.376
−4.457
1.00
45.11


ATOM
659
CE2
PHE
242
11.767
53.451
−3.755
1.00
42.03


ATOM
660
CZ
PHE
242
12.872
52.752
−4.214
1.00
43.33


ATOM
661
N
GLU
243
6.591
49.235
−5.947
1.00
42.20


ATOM
662
CA
GLU
243
5.313
48.530
−6.091
1.00
43.24


ATOM
663
C
GLU
243
5.193
47.503
−4.975
1.00
42.95


ATOM
664
O
GLU
243
6.100
46.664
−4.795
1.00
41.58


ATOM
665
CB
GLU
243
5.176
47.817
−7.456
1.00
43.53


ATOM
666
CG
GLU
243
5.166
48.729
−8.686
1.00
47.74


ATOM
667
CD
GLU
243
4.045
49.790
−8.672
1.00
53.02


ATOM
668
OE1
GLU
243
2.909
49.485
−9.111
1.00
56.85


ATOM
669
OE2
GLU
243
4.313
50.950
−8.262
1.00
54.32


ATOM
670
N
SER
244
4.109
47.621
−4.205
1.00
42.95


ATOM
671
CA
SER
244
3.917
46.786
−3.017
1.00
43.67


ATOM
672
C
SER
244
3.492
45.363
−3.422
1.00
44.11


ATOM
673
O
SER
244
3.430
44.503
−2.559
1.00
43.54


ATOM
674
CB
SER
244
2.872
47.385
−2.062
1.00
43.70


ATOM
675
OG
SER
244
1.608
47.538
−2.714
1.00
43.76


ATOM
676
N
ILE
245
3.247
45.151
−4.732
1.00
44.53


ATOM
677
CA
ILE
245
2.762
43.878
−5.305
1.00
44.90


ATOM
678
C
ILE
245
3.796
43.050
−6.114
1.00
44.98


ATOM
679
O
ILE
245
3.579
41.858
−6.399
1.00
45.25


ATOM
680
CB
ILE
245
1.446
44.092
−6.131
1.00
45.08


ATOM
681
CG1
ILE
245
1.678
45.000
−7.340
1.00
45.82


ATOM
682
CG2
ILE
245
0.327
44.676
−5.234
1.00
45.11


ATOM
683
CD1
ILE
245
0.563
44.940
−8.372
1.00
45.19


ATOM
684
N
HIS
246
4.912
43.691
−6.467
1.00
44.82


ATOM
685
CA
HIS
246
6.046
43.056
−7.170
1.00
44.40


ATOM
686
C
HIS
246
7.299
43.248
−6.337
1.00
43.85


ATOM
687
O
HIS
246
7.274
43.929
−5.290
1.00
43.92


ATOM
688
CB
HIS
246
6.306
43.733
−8.529
1.00
45.24


ATOM
689
CG
HIS
246
5.125
43.746
−9.448
1.00
45.19


ATOM
690
ND1
HIS
246
4.574
44.916
−9.935
1.00
47.43


ATOM
691
CD2
HIS
246
4.390
42.735
−9.968
1.00
44.55


ATOM
692
CE1
HIS
246
3.557
44.616
−10.729
1.00
47.01


ATOM
693
NE2
HIS
246
3.423
43.299
−10.761
1.00
45.51


TER











ATOM
694
MN
MN2 A
258
−0.987
48.653
−9.777
1.00
49.60


TER











ATOM
695
N
ASN
15
−0.055
68.475
−21.743
1.00
57.77


ATOM
696
CA
ASN
15
0.077
66.987
−21.573
1.00
57.60


ATOM
697
C
ASN
15
1.474
66.516
−21.106
1.00
56.17


ATOM
698
O
ASN
15
1.638
66.048
−19.944
1.00
57.59


ATOM
699
CB
ASN
15
−0.349
66.258
−22.857
1.00
58.61


ATOM
700
CG
ASN
15
−1.826
65.843
−22.840
1.00
61.05


ATOM
701
OD1
ASN
15
−2.439
65.713
−21.763
1.00
62.70


ATOM
702
ND2
ASN
15
−2.407
65.626
−24.045
1.00
62.68


ATOM
703
N
LEU
16
2.466
66.657
−21.989
1.00
53.16


ATOM
704
CA
LEU
16
3.873
66.273
−21.715
1.00
49.45


ATOM
705
C
LEU
16
4.265
64.821
−22.049
1.00
46.26


ATOM
706
O
LEU
16
3.774
63.857
−21.428
1.00
45.34


ATOM
707
CB
LEU
16
4.286
66.643
−20.281
1.00
50.00


ATOM
708
CG
LEU
16
5.106
67.898
−20.015
1.00
50.00


ATOM
709
CD1
LEU
16
4.760
69.101
−20.907
1.00
49.39


ATOM
710
CD2
LEU
16
5.019
68.235
−18.515
1.00
49.75


ATOM
711
N
PRO
17
5.144
64.662
−23.051
1.00
43.37


ATOM
712
CA
PRO
17
5.673
63.318
−23.272
1.00
42.01


ATOM
713
C
PRO
17
6.630
62.898
−22.123
1.00
39.49


ATOM
714
O
PRO
17
7.206
63.762
−21.457
1.00
38.46


ATOM
715
CB
PRO
17
6.387
63.410
−24.638
1.00
41.94


ATOM
716
CG
PRO
17
6.625
64.921
−24.889
1.00
42.78


ATOM
717
CD
PRO
17
5.660
65.673
−24.004
1.00
43.71


ATOM
718
N
ILE
18
6.757
61.587
−21.888
1.00
37.20


ATOM
719
CA
ILE
18
7.707
61.060
−20.889
1.00
34.81


ATOM
720
C
ILE
18
8.860
60.366
−21.617
1.00
34.48


ATOM
721
O
ILE
18
8.658
59.400
−22.359
1.00
33.94


ATOM
722
CB
ILE
18
7.007
60.115
−19.844
1.00
35.33


ATOM
723
CG1
ILE
18
5.742
60.779
−19.284
1.00
34.34


ATOM
724
CG2
ILE
18
7.994
59.691
−18.733
1.00
34.30


ATOM
725
CD1
ILE
18
4.965
60.057
−18.195
1.00
33.50


ATOM
726
N
TYR
50
9.592
55.233
−24.510
1.00
32.49


ATOM
727
CA
TYR
50
9.011
56.572
−24.698
1.00
33.92


ATOM
728
C
TYR
50
7.472
56.559
−24.508
1.00
34.74


ATOM
729
O
TYR
50
6.795
55.620
−24.894
1.00
34.44


ATOM
730
CB
TYR
50
9.391
57.083
−26.100
1.00
34.27


ATOM
731
CG
TYR
50
8.732
58.354
−26.497
1.00
34.16


ATOM
732
CD1
TYR
50
9.239
59.573
−26.086
1.00
34.55


ATOM
733
CD2
TYR
50
7.621
58.344
−27.334
1.00
34.69


ATOM
734
CE1
TYR
50
8.612
60.776
−26.451
1.00
34.91


ATOM
735
CE2
TYR
50
7.008
59.513
−27.724
1.00
34.31


ATOM
736
CZ
TYR
50
7.497
60.717
−27.280
1.00
34.93


ATOM
737
OH
TYR
50
6.858
61.883
−27.670
1.00
37.56


ATOM
738
N
LEU
51
6.920
57.574
−23.856
1.00
36.01


ATOM
739
CA
LEU
51
5.459
57.628
−23.743
1.00
38.06


ATOM
740
C
LEU
51
4.970
58.946
−24.359
1.00
38.71


ATOM
741
O
LEU
51
5.357
60.033
−23.891
1.00
38.72


ATOM
742
CB
LEU
51
4.966
57.508
−22.293
1.00
38.26


ATOM
743
CG
LEU
51
3.483
57.129
−22.071
1.00
39.97


ATOM
744
CD1
LEU
51
3.196
55.722
−22.569
1.00
41.59


ATOM
745
CD2
LEU
51
3.106
57.206
−20.601
1.00
39.18


ATOM
746
N
PRO
52
4.132
58.851
−25.410
1.00
39.27


ATOM
747
CA
PRO
52
3.607
60.049
−26.084
1.00
40.56


ATOM
748
C
PRO
52
2.762
60.931
−25.170
1.00
40.53


ATOM
749
O
PRO
52
2.094
60.428
−24.289
1.00
39.33


ATOM
750
CB
PRO
52
2.720
59.470
−27.209
1.00
40.48


ATOM
751
CG
PRO
52
3.168
58.035
−27.390
1.00
40.75


ATOM
752
CD
PRO
52
3.626
57.600
−26.013
1.00
39.83


ATOM
753
N
ALA
53
2.808
62.240
−25.420
1.00
42.43


ATOM
754
CA
ALA
53
2.081
63.263
−24.663
1.00
44.05


ATOM
755
C
ALA
53
0.632
62.937
−24.238
1.00
46.03


ATOM
756
O
ALA
53
0.269
63.114
−23.079
1.00
45.37


ATOM
757
CB
ALA
53
2.158
64.611
−25.400
1.00
44.31


ATOM
758
N
GLU
54
−0.201
62.432
−25.147
1.00
48.17


ATOM
759
CA
GLU
54
−1.588
62.156
−24.742
1.00
50.27


ATOM
760
C
GLU
54
−1.866
60.696
−24.298
1.00
50.27


ATOM
761
O
GLU
54
−3.005
60.374
−23.975
1.00
50.60


ATOM
762
CB
GLU
54
−2.627
62.696
−25.771
1.00
50.47


ATOM
763
CG
GLU
54
−2.726
61.898
−27.079
1.00
52.14


ATOM
764
CD
GLU
54
−3.853
62.381
−28.041
1.00
52.30


ATOM
765
OE1
GLU
54
−3.510
63.067
−29.047
1.00
53.98


ATOM
766
OE2
GLU
54
−5.059
62.074
−27.795
1.00
52.76


ATOM
767
N
GLN
55
−0.842
59.833
−24.264
1.00
49.80


ATOM
768
CA
GLN
55
−1.008
58.463
−23.723
1.00
49.67


ATOM
769
C
GLN
55
−0.821
58.421
−22.204
1.00
49.52


ATOM
770
O
GLN
55
0.162
58.960
−21.673
1.00
48.68


ATOM
771
CB
GLN
55
−0.060
57.476
−24.415
1.00
49.73


ATOM
772
CG
GLN
55
−0.274
55.997
−24.053
1.00
49.02


ATOM
773
CD
GLN
55
0.539
55.065
−24.963
1.00
50.64


ATOM
774
OE1
GLN
55
0.798
55.402
−26.127
1.00
50.76


ATOM
775
NE2
GLN
55
0.928
53.872
−24.442
1.00
50.99


ATOM
776
N
LYS
56
−1.761
57.772
−21.514
1.00
49.80


ATOM
777
CA
LYS
56
−1.878
57.919
−20.046
1.00
50.35


ATOM
778
C
LYS
56
−0.832
57.125
−19.269
1.00
48.93


ATOM
779
O
LYS
56
−0.302
57.610
−18.259
1.00
48.73


ATOM
780
CB
LYS
56
−3.292
57.572
−19.523
1.00
50.57


ATOM
781
CG
LYS
56
−3.464
57.835
−18.019
1.00
51.80


ATOM
782
CD
LYS
56
−4.918
57.915
−17.578
1.00
53.30


ATOM
783
CE
LYS
56
−5.380
56.598
−16.954
1.00
55.68


ATOM
784
NZ
LYS
56
−6.597
56.015
−17.633
1.00
59.22


ATOM
785
N
GLY
57
−0.585
55.903
−19.747
1.00
47.49


ATOM
786
CA
GLY
57
0.319
54.958
−19.131
1.00
45.82


ATOM
787
C
GLY
57
0.834
53.928
−20.127
1.00
45.53


ATOM
788
O
GLY
57
0.337
53.804
−21.261
1.00
44.75


ATOM
789
N
THR
58
1.867
53.202
−19.715
1.00
44.32


ATOM
790
CA
THR
58
2.451
52.188
−20.551
1.00
43.57


ATOM
791
C
THR
58
1.880
50.881
−20.016
1.00
44.18


ATOM
792
O
THR
58
0.915
50.906
−19.236
1.00
43.92


ATOM
793
CB
THR
58
4.020
52.240
−20.514
1.00
43.34


ATOM
794
OG1
THR
58
4.567
51.259
−21.411
1.00
42.06


ATOM
795
CG2
THR
58
4.552
51.995
−19.087
1.00
41.24


ATOM
796
N
HIS
59
2.484
49.759
−20.416
1.00
44.36


ATOM
797
CA
HIS
59
1.990
48.432
−20.089
1.00
44.59


ATOM
798
C
HIS
59
3.042
47.682
−19.315
1.00
43.83


ATOM
799
O
HIS
59
3.780
46.885
−19.885
1.00
42.81


ATOM
800
CB
HIS
59
1.636
47.699
−21.380
1.00
45.60


ATOM
801
CG
HIS
59
0.703
48.482
−22.252
1.00
48.60


ATOM
802
ND1
HIS
59
1.144
49.285
−23.288
1.00
51.29


ATOM
803
CD2
HIS
59
−0.637
48.661
−22.180
1.00
50.27


ATOM
804
CE1
HIS
59
0.109
49.887
−23.847
1.00
51.31


ATOM
805
NE2
HIS
59
−0.984
49.521
−23.198
1.00
52.01


ATOM
806
N
MET
60
3.060
47.922
−18.003
1.00
43.45


ATOM
807
CA
MET
60
4.118
47.452
−17.111
1.00
43.58


ATOM
808
C
MET
60
4.408
45.950
−17.126
1.00
42.81


ATOM
809
O
MET
60
5.568
45.558
−17.000
1.00
43.78


ATOM
810
CB
MET
60
3.826
47.903
−15.662
1.00
44.75


ATOM
811
CG
MET
60
3.874
49.424
−15.481
1.00
45.80


ATOM
812
SD
MET
60
5.554
50.030
−15.559
1.00
47.38


ATOM
813
CE
MET
60
5.341
51.725
−15.015
1.00
46.89


ATOM
814
N
SER
61
3.378
45.104
−17.240
1.00
41.77


ATOM
815
CA
SER
61
3.580
43.646
−17.190
1.00
40.55


ATOM
816
C
SER
61
4.316
43.095
−18.401
1.00
40.20


ATOM
817
O
SER
61
4.872
41.980
−18.354
1.00
39.73


ATOM
818
CB
SER
61
2.253
42.915
−17.058
1.00
40.87


ATOM
819
OG
SER
61
1.535
42.951
−18.286
1.00
42.74


ATOM
820
N
ARG
62
4.306
43.848
−19.502
1.00
38.76


ATOM
821
CA
ARG
62
4.907
43.356
−20.760
1.00
37.81


ATOM
822
C
ARG
62
6.430
43.334
−20.708
1.00
36.60


ATOM
823
O
ARG
62
7.053
42.553
−21.407
1.00
35.27


ATOM
824
CB
ARG
62
4.471
44.223
−21.946
1.00
38.07


ATOM
825
CG
ARG
62
2.986
44.333
−22.103
1.00
37.78


ATOM
826
CD
ARG
62
2.650
44.941
−23.453
1.00
37.88


ATOM
827
NE
ARG
62
1.202
45.064
−23.598
1.00
37.07


ATOM
828
CZ
ARG
62
0.569
45.715
−24.579
1.00
37.18


ATOM
829
NH1
ARG
62
1.229
46.323
−25.571
1.00
37.21


ATOM
830
NH2
ARG
62
−0.745
45.735
−24.564
1.00
35.43


ATOM
831
N
PHE
63
7.029
44.222
−19.900
1.00
36.09


ATOM
832
CA
PHE
63
8.464
44.216
−19.720
1.00
35.73


ATOM
833
C
PHE
63
8.893
42.871
−19.109
1.00
36.45


ATOM
834
O
PHE
63
9.793
42.213
−19.617
1.00
36.12


ATOM
835
CB
PHE
63
8.934
45.382
−18.850
1.00
35.41


ATOM
836
CG
PHE
63
8.621
46.727
−19.413
1.00
34.78


ATOM
837
CD1
PHE
63
9.340
47.217
−20.503
1.00
32.25


ATOM
838
CD2
PHE
63
7.598
47.499
−18.852
1.00
33.93


ATOM
839
CE1
PHE
63
9.074
48.487
−21.031
1.00
32.28


ATOM
840
CE2
PHE
63
7.303
48.777
−19.376
1.00
34.29


ATOM
841
CZ
PHE
63
8.050
49.274
−20.464
1.00
33.57


ATOM
842
N
VAL
64
8.236
42.472
−18.020
1.00
37.27


ATOM
843
CA
VAL
64
8.517
41.190
−17.375
1.00
37.13


ATOM
844
C
VAL
64
8.161
40.006
−18.267
1.00
38.00


ATOM
845
O
VAL
64
8.928
39.046
−18.346
1.00
38.05


ATOM
846
CB
VAL
64
7.771
41.072
−15.995
1.00
37.68


ATOM
847
CG1
VAL
64
7.969
39.680
−15.348
1.00
35.90


ATOM
848
CG2
VAL
64
8.246
42.118
−15.051
1.00
35.99


ATOM
849
N
ALA
65
6.995
40.064
−18.920
1.00
39.07


ATOM
850
CA
ALA
65
6.604
39.084
−19.959
1.00
39.65


ATOM
851
C
ALA
65
7.709
38.860
−20.985
1.00
39.89


ATOM
852
O
ALA
65
8.040
37.714
−21.288
1.00
40.81


ATOM
853
CB
ALA
65
5.314
39.527
−20.661
1.00
39.83


ATOM
854
N
ALA
88
8.500
47.251
−29.983
1.00
37.69


ATOM
855
CA
ALA
88
7.412
46.662
−30.793
1.00
39.22


ATOM
856
C
ALA
88
6.275
46.238
−29.879
1.00
39.76


ATOM
857
O
ALA
88
5.118
46.646
−30.063
1.00
40.54


ATOM
858
CB
ALA
88
7.930
45.445
−31.529
1.00
39.27


ATOM
859
N
LEU
89
6.607
45.422
−28.880
1.00
39.88


ATOM
860
CA
LEU
89
5.615
44.873
−27.936
1.00
40.55


ATOM
861
C
LEU
89
4.903
45.956
−27.096
1.00
39.98


ATOM
862
O
LEU
89
3.701
45.889
−26.799
1.00
40.50


ATOM
863
CB
LEU
89
6.293
43.838
−27.020
1.00
40.81


ATOM
864
CG
LEU
89
5.482
43.171
−25.912
1.00
41.42


ATOM
865
CD1
LEU
89
4.311
42.388
−26.507
1.00
43.86


ATOM
866
CD2
LEU
89
6.373
42.242
−25.071
1.00
41.85


ATOM
867
N
LEU
90
5.634
46.969
−26.699
1.00
39.63


ATOM
868
CA
LEU
90
4.988
48.003
−25.934
1.00
39.66


ATOM
869
C
LEU
90
4.345
49.029
−26.854
1.00
39.64


ATOM
870
O
LEU
90
3.830
50.045
−26.394
1.00
40.47


ATOM
871
CB
LEU
90
5.975
48.630
−24.943
1.00
38.91


ATOM
872
CG
LEU
90
5.850
47.641
−23.753
1.00
40.39


ATOM
873
CD1
LEU
90
7.044
46.740
−23.526
1.00
36.51


ATOM
874
CD2
LEU
90
5.400
48.294
−22.503
1.00
38.67


ATOM
875
N
ASP
91
4.389
48.771
−28.159
1.00
40.21


ATOM
876
CA
ASP
91
3.915
49.746
−29.157
1.00
39.95


ATOM
877
C
ASP
91
4.453
51.174
−28.929
1.00
38.80


ATOM
878
O
ASP
91
3.678
52.138
−28.926
1.00
38.19


ATOM
879
CB
ASP
91
2.355
49.735
−29.285
1.00
40.89


ATOM
880
CG
ASP
91
1.796
48.482
−30.023
1.00
43.50


ATOM
881
OD1
ASP
91
2.494
47.945
−30.931
1.00
46.25


ATOM
882
OD2
ASP
91
0.645
48.039
−29.723
1.00
42.88


ATOM
883
N
SER
92
5.775
51.327
−28.785
1.00
38.12


ATOM
884
CA
SER
92
6.384
52.673
−28.609
1.00
37.45


ATOM
885
C
SER
92
7.380
53.024
−29.694
1.00
38.08


ATOM
886
O
SER
92
7.959
52.116
−30.317
1.00
38.79


ATOM
887
CB
SER
92
7.087
52.787
−27.263
1.00
37.32


ATOM
888
OG
SER
92
7.773
54.032
−27.125
1.00
36.68


ATOM
889
N
LYS
107
7.304
31.282
−9.880
1.00
44.36


ATOM
890
CA
LYS
107
5.973
31.471
−9.312
1.00
44.70


ATOM
891
C
LYS
107
4.898
31.462
−10.414
1.00
45.13


ATOM
892
O
LYS
107
5.213
31.577
−11.615
1.00
44.87


ATOM
893
CB
LYS
107
5.919
32.750
−8.473
1.00
44.28


ATOM
894
CG
LYS
107
7.016
32.816
−7.384
1.00
43.47


ATOM
895
CD
LYS
107
6.748
33.964
−6.423
1.00
41.18


ATOM
896
CE
LYS
107
5.476
33.665
−5.604
1.00
42.21


ATOM
897
NZ
LYS
107
5.334
34.534
−4.400
1.00
40.46


ATOM
898
N
THR
108
3.641
31.306
−9.996
1.00
45.84


ATOM
899
CA
THR
108
2.494
31.304
−10.901
1.00
46.81


ATOM
900
C
THR
108
1.453
32.309
−10.397
1.00
47.68


ATOM
901
O
THR
108
1.123
32.321
−9.198
1.00
47.71


ATOM
902
CB
THR
108
1.900
29.856
−11.037
1.00
47.35


ATOM
903
OG1
THR
108
2.963
28.918
−11.302
1.00
47.19


ATOM
904
CG2
THR
108
0.851
29.771
−12.172
1.00
47.03


ATOM
905
N
ALA
109
0.950
33.160
−11.299
1.00
48.80


ATOM
906
CA
ALA
109
−0.043
34.185
−10.948
1.00
50.14


ATOM
907
C
ALA
109
−1.364
33.551
−10.468
1.00
51.03


ATOM
908
O
ALA
109
−1.770
32.504
−11.004
1.00
51.15


ATOM
909
CB
ALA
109
−0.284
35.142
−12.127
1.00
50.35


ATOM
910
N
PRO
110
−2.009
34.152
−9.427
1.00
51.43


ATOM
911
CA
PRO
110
−3.180
33.513
−8.859
1.00
51.94


ATOM
912
C
PRO
110
−4.394
33.383
−9.798
1.00
52.99


ATOM
913
O
PRO
110
−5.175
32.458
−9.609
1.00
52.84


ATOM
914
CB
PRO
110
−3.517
34.391
−7.639
1.00
51.48


ATOM
915
CG
PRO
110
−2.880
35.653
−7.863
1.00
51.48


ATOM
916
CD
PRO
110
−1.654
35.384
−8.684
1.00
51.45


ATOM
917
N
VAL
111
−4.578
34.275
−10.780
1.00
53.92


ATOM
918
CA
VAL
111
−5.756
34.118
−11.660
1.00
55.03


ATOM
919
C
VAL
111
−5.429
33.593
−13.057
1.00
55.25


ATOM
920
O
VAL
111
−5.957
32.542
−13.469
1.00
55.19


ATOM
921
CB
VAL
111
−6.709
35.358
−11.692
1.00
55.46


ATOM
922
CG1
VAL
111
−7.959
35.069
−12.557
1.00
54.84


ATOM
923
CG2
VAL
111
−7.125
35.738
−10.262
1.00
55.47


ATOM
924
N
SER
112
−4.559
34.318
−13.764
1.00
55.19


ATOM
925
CA
SER
112
−4.113
33.921
−15.099
1.00
55.31


ATOM
926
C
SER
112
−3.377
32.568
−15.158
1.00
54.97


ATOM
927
O
SER
112
−3.518
31.843
−16.147
1.00
54.91


ATOM
928
CB
SER
112
−3.256
35.021
−15.742
1.00
55.47


ATOM
929
OG
SER
112
−2.087
35.299
−14.963
1.00
56.21


ATOM
930
N
GLY
113
−2.614
32.231
−14.106
1.00
54.62


ATOM
931
CA
GLY
113
−1.646
31.105
−14.149
1.00
53.64


ATOM
932
C
GLY
113
−0.355
31.398
−14.943
1.00
53.03


ATOM
933
O
GLY
113
0.471
30.491
−15.166
1.00
52.84


ATOM
934
N
ILE
114
−0.174
32.648
−15.384
1.00
52.24


ATOM
935
CA
ILE
114
1.092
33.059
−16.020
1.00
52.01


ATOM
936
C
ILE
114
2.254
32.953
−14.992
1.00
51.48


ATOM
937
O
ILE
114
2.100
33.306
−13.808
1.00
50.80


ATOM
938
CB
ILE
114
1.024
34.485
−16.667
1.00
52.23


ATOM
939
CG1
ILE
114
−0.088
34.569
−17.722
1.00
53.68


ATOM
940
CG2
ILE
114
2.337
34.836
−17.370
1.00
51.30


ATOM
941
CD1
ILE
114
−0.418
36.006
−18.174
1.00
53.39


ATOM
942
N
ARG
115
3.393
32.431
−15.450
1.00
50.22


ATOM
943
CA
ARG
115
4.520
32.157
−14.576
1.00
49.39


ATOM
944
C
ARG
115
5.561
33.264
−14.723
1.00
47.82


ATOM
945
O
ARG
115
5.733
33.834
−15.820
1.00
46.47


ATOM
946
CB
ARG
115
5.159
30.795
−14.893
1.00
50.41


ATOM
947
CG
ARG
115
4.234
29.581
−14.773
1.00
53.80


ATOM
948
CD
ARG
115
4.782
28.481
−15.657
1.00
58.84


ATOM
949
NE
ARG
115
5.550
27.503
−14.885
1.00
64.83


ATOM
950
CZ
ARG
115
6.714
26.970
−15.257
1.00
61.10


ATOM
951
NH1
ARG
115
7.313
27.346
−16.394
1.00
65.93


ATOM
952
NH2
ARG
115
7.300
26.079
−14.454
1.00
66.59


ATOM
953
N
SER
116
6.238
33.551
−13.609
1.00
45.50


ATOM
954
CA
SER
116
7.398
34.421
−13.565
1.00
44.28


ATOM
955
C
SER
116
8.251
34.043
−12.346
1.00
43.63


ATOM
956
O
SER
116
7.748
33.370
−11.418
1.00
43.82


ATOM
957
CB
SER
116
6.977
35.896
−13.499
1.00
44.12


ATOM
958
OG
SER
116
6.181
36.157
−12.365
1.00
44.28


ATOM
959
N
VAL
143
7.390
40.308
1.006
1.00
34.49


ATOM
960
CA
VAL
143
5.966
40.088
0.977
1.00
36.54


ATOM
961
C
VAL
143
5.257
41.433
0.907
1.00
37.50


ATOM
962
O
VAL
143
5.873
42.489
1.010
1.00
37.31


ATOM
963
CB
VAL
143
5.435
39.293
2.220
1.00
36.15


ATOM
964
CG1
VAL
143
6.186
37.974
2.420
1.00
36.77


ATOM
965
CG2
VAL
143
5.542
40.117
3.443
1.00
35.72


ATOM
966
N
THR
144
3.957
41.377
0.692
1.00
40.85


ATOM
967
CA
THR
144
3.070
42.530
0.876
1.00
43.22


ATOM
968
C
THR
144
2.496
42.480
2.296
1.00
45.07


ATOM
969
O
THR
144
2.017
41.407
2.764
1.00
44.61


ATOM
970
CB
THR
144
1.904
42.500
−0.137
1.00
43.97


ATOM
971
OG1
THR
144
2.430
42.246
−1.451
1.00
45.02


ATOM
972
CG2
THR
144
1.090
43.816
−0.134
1.00
43.92


ATOM
973
N
SER
145
2.564
43.631
2.974
1.00
46.62


ATOM
974
CA
SER
145
1.899
43.833
4.274
1.00
48.13


ATOM
975
C
SER
145
0.841
44.916
4.119
1.00
48.74


ATOM
976
O
SER
145
1.058
45.904
3.417
1.00
48.82


ATOM
977
CB
SER
145
2.886
44.219
5.384
1.00
48.45


ATOM
978
OG
SER
145
3.671
45.353
5.036
1.00
50.19


ATOM
979
N
LEU
146
−0.314
44.700
4.746
1.00
49.98


ATOM
980
CA
LEU
146
−1.427
45.665
4.705
1.00
50.76


ATOM
981
C
LEU
146
−1.915
45.944
6.134
1.00
51.52


ATOM
982
O
LEU
146
−2.141
45.001
6.927
1.00
51.71


ATOM
983
CB
LEU
146
−2.560
45.172
3.800
1.00
50.62


ATOM
984
CG
LEU
146
−3.742
46.141
3.605
1.00
50.27


ATOM
985
CD1
LEU
146
−4.266
46.212
2.164
1.00
49.21


ATOM
986
CD2
LEU
146
−4.852
45.785
4.576
1.00
50.20


ATOM
987
N
CYS
147
−2.050
47.225
6.469
1.00
51.52


ATOM
988
CA
CYS
147
−2.304
47.618
7.849
1.00
52.46


ATOM
989
C
CYS
147
−3.773
47.476
8.331
1.00
53.73


ATOM
990
O
CYS
147
−4.690
48.126
7.788
1.00
53.40


ATOM
991
CB
CYS
147
−1.804
49.045
8.098
1.00
52.50


ATOM
992
SG
CYS
147
−2.131
49.620
9.803
1.00
51.33


ATOM
993
N
PRO
148
−3.988
46.676
9.400
1.00
54.93


ATOM
994
CA
PRO
148
−5.373
46.445
9.860
1.00
55.87


ATOM
995
C
PRO
148
−6.026
47.721
10.446
1.00
56.77


ATOM
996
O
PRO
148
−7.222
47.975
10.198
1.00
56.68


ATOM
997
CB
PRO
148
−5.243
45.321
10.909
1.00
55.91


ATOM
998
CG
PRO
148
−3.778
45.204
11.232
1.00
55.66


ATOM
999
CD
PRO
148
−2.970
45.996
10.237
1.00
55.10


ATOM
1000
N
CYS
149
−5.232
48.520
11.172
1.00
57.41


ATOM
1001
CA
CYS
149
−5.692
49.783
11.765
1.00
57.40


ATOM
1002
C
CYS
149
−6.185
50.769
10.685
1.00
57.29


ATOM
1003
O
CYS
149
−7.265
51.377
10.819
1.00
56.51


ATOM
1004
CB
CYS
149
−4.577
50.414
12.613
1.00
57.61


ATOM
1005
SG
CYS
149
−5.106
51.912
13.511
1.00
59.83


ATOM
1006
N
SER
150
−5.389
50.903
9.621
1.00
57.10


ATOM
1007
CA
SER
150
−5.755
51.690
8.438
1.00
57.37


ATOM
1008
C
SER
150
−7.159
51.333
7.927
1.00
57.54


ATOM
1009
O
SER
150
−8.069
52.177
7.942
1.00
56.90


ATOM
1010
CB
SER
150
−4.699
51.512
7.315
1.00
57.56


ATOM
1011
OG
SER
150
−4.960
52.364
6.196
1.00
56.24


ATOM
1012
N
LYS
151
−7.325
50.085
7.480
1.00
58.20


ATOM
1013
CA
LYS
151
−8.614
49.594
6.980
1.00
58.78


ATOM
1014
C
LYS
151
−9.768
49.902
7.953
1.00
59.60


ATOM
1015
O
LYS
151
−10.820
50.440
7.548
1.00
59.74


ATOM
1016
CB
LYS
151
−8.530
48.085
6.737
1.00
58.67


ATOM
1017
CG
LYS
151
−9.859
47.424
6.372
1.00
57.80


ATOM
1018
CD
LYS
151
−9.711
45.907
6.375
1.00
57.00


ATOM
1019
CE
LYS
151
−10.975
45.229
5.868
1.00
56.13


ATOM
1020
NZ
LYS
151
−10.706
43.817
5.487
1.00
54.37


ATOM
1021
N
GLU
152
−9.526
49.553
9.222
1.00
60.08


ATOM
1022
CA
GLU
152
−10.491
49.562
10.326
1.00
60.84


ATOM
1023
C
GLU
152
−11.066
50.953
10.619
1.00
60.69


ATOM
1024
O
GLU
152
−12.257
51.097
10.912
1.00
60.54


ATOM
1025
CB
GLU
152
−9.782
49.041
11.572
1.00
61.06


ATOM
1026
CG
GLU
152
−10.668
48.560
12.727
1.00
64.00


ATOM
1027
CD
GLU
152
−9.947
47.510
13.573
1.00
65.38


ATOM
1028
OE1
GLU
152
−8.784
47.741
13.986
1.00
65.59


ATOM
1029
OE2
GLU
152
−10.537
46.433
13.794
1.00
67.79


ATOM
1030
N
ILE
153
−10.199
51.961
10.551
1.00
60.40


ATOM
1031
CA
ILE
153
−10.560
53.332
10.885
1.00
59.97


ATOM
1032
C
ILE
153
−11.005
54.133
9.649
1.00
59.93


ATOM
1033
O
ILE
153
−11.676
55.165
9.806
1.00
59.92


ATOM
1034
CB
ILE
153
−9.396
54.075
11.633
1.00
60.11


ATOM
1035
CG1
ILE
153
−8.231
54.409
10.666
1.00
59.91


ATOM
1036
CG2
ILE
153
−8.954
53.279
12.886
1.00
59.57


ATOM
1037
CD1
ILE
153
−7.180
55.333
11.244
1.00
59.73


ATOM
1038
N
SER
154
−10.639
53.658
8.442
1.00
59.44


ATOM
1039
CA
SER
154
−10.934
54.374
7.191
1.00
59.16


ATOM
1040
C
SER
154
−12.228
53.896
6.536
1.00
59.11


ATOM
1041
O
SER
154
−12.506
52.691
6.506
1.00
58.66


ATOM
1042
CB
SER
154
−9.777
54.261
6.179
1.00
59.05


ATOM
1043
OG
SER
154
−8.528
54.531
6.786
1.00
58.46


ATOM
1044
N
GLN
155
−12.998
54.846
5.992
1.00
59.19


ATOM
1045
CA
GLN
155
−14.252
54.533
5.279
1.00
59.20


ATOM
1046
C
GLN
155
−13.990
53.778
3.969
1.00
58.56


ATOM
1047
O
GLN
155
−14.872
53.076
3.441
1.00
58.43


ATOM
1048
CB
GLN
155
−15.103
55.800
5.037
1.00
59.42


ATOM
1049
CG
GLN
155
−14.478
56.873
4.109
1.00
59.96


ATOM
1050
CD
GLN
155
−15.294
58.185
4.047
1.00
60.84


ATOM
1051
OE1
GLN
155
−16.514
58.161
3.833
1.00
63.53


ATOM
1052
NE2
GLN
155
−14.613
59.330
4.221
1.00
61.62


ATOM
1053
N
TYR
156
−12.775
53.941
3.447
1.00
57.89


ATOM
1054
CA
TYR
156
−12.301
53.176
2.290
1.00
57.36


ATOM
1055
C
TYR
156
−10.756
53.110
2.288
1.00
56.68


ATOM
1056
O
TYR
156
−10.080
53.992
2.857
1.00
55.91


ATOM
1057
CB
TYR
156
−12.874
53.721
0.957
1.00
57.64


ATOM
1058
CG
TYR
156
−13.016
55.246
0.860
1.00
59.03


ATOM
1059
CD1
TYR
156
−11.895
56.095
0.994
1.00
59.96


ATOM
1060
CD2
TYR
156
−14.268
55.842
0.624
1.00
60.16


ATOM
1061
CE1
TYR
156
−12.014
57.502
0.915
1.00
59.50


ATOM
1062
CE2
TYR
156
−14.399
57.259
0.535
1.00
60.74


ATOM
1063
CZ
TYR
156
−13.260
58.074
0.684
1.00
59.41


ATOM
1064
OH
TYR
156
−13.355
59.446
0.586
1.00
58.74


ATOM
1065
N
GLY
157
−10.224
52.039
1.686
1.00
55.88


ATOM
1066
CA
GLY
157
−8.782
51.868
1.486
1.00
54.70


ATOM
1067
C
GLY
157
−8.046
51.479
2.750
1.00
53.87


ATOM
1068
O
GLY
157
−8.628
51.432
3.838
1.00
53.85


ATOM
1069
N
ALA
158
−6.753
51.209
2.600
1.00
53.06


ATOM
1070
CA
ALA
158
−5.889
50.782
3.704
1.00
52.34


ATOM
1071
C
ALA
158
−4.458
50.847
3.233
1.00
51.79


ATOM
1072
O
ALA
158
−4.116
50.287
2.176
1.00
51.74


ATOM
1073
CB
ALA
158
−6.210
49.355
4.162
1.00
52.30


ATOM
1074
N
HIS
159
−3.601
51.501
4.006
1.00
50.50


ATOM
1075
CA
HIS
159
−2.245
51.643
3.514
1.00
49.70


ATOM
1076
C
HIS
159
−1.569
50.272
3.570
1.00
49.57


ATOM
1077
O
HIS
159
−1.826
49.451
4.477
1.00
49.86


ATOM
1078
CB
HIS
159
−1.439
52.721
4.251
1.00
48.45


ATOM
1079
CG
HIS
159
−0.801
52.256
5.524
1.00
45.98


ATOM
1080
ND1
HIS
159
0.410
51.592
5.551
1.00
43.16


ATOM
1081
CD2
HIS
159
−1.178
52.409
6.819
1.00
42.93


ATOM
1082
CE1
HIS
159
0.738
51.332
6.808
1.00
42.42


ATOM
1083
NE2
HIS
159
−0.194
51.841
7.595
1.00
39.71


ATOM
1084
N
ASN
160
−0.746
50.036
2.560
1.00
49.49


ATOM
1085
CA
ASN
160
0.054
48.826
2.464
1.00
48.81


ATOM
1086
C
ASN
160
1.412
49.196
1.879
1.00
48.38


ATOM
1087
O
ASN
160
1.642
50.351
1.462
1.00
47.84


ATOM
1088
CB
ASN
160
−0.673
47.719
1.658
1.00
48.67


ATOM
1089
CG
ASN
160
−1.276
48.224
0.336
1.00
48.57


ATOM
1090
OD1
ASN
160
−2.384
48.761
0.308
1.00
49.39


ATOM
1091
ND2
ASN
160
−0.557
48.011
−0.762
1.00
47.12


ATOM
1092
N
GLN
161
2.316
48.217
1.878
1.00
47.92


ATOM
1093
CA
GLN
161
3.710
48.431
1.502
1.00
47.53


ATOM
1094
C
GLN
161
4.428
47.094
1.401
1.00
47.31


ATOM
1095
O
GLN
161
3.974
46.067
1.960
1.00
47.48


ATOM
1096
CB
GLN
161
4.425
49.306
2.542
1.00
47.08


ATOM
1097
CG
GLN
161
4.320
48.769
3.982
1.00
47.63


ATOM
1098
CD
GLN
161
3.004
49.124
4.648
1.00
48.13


ATOM
1099
OE1
GLN
161
2.504
50.254
4.487
1.00
47.49


ATOM
1100
NE2
GLN
161
2.426
48.171
5.397
1.00
48.31


ATOM
1101
N
ARG
162
5.536
47.107
0.668
1.00
46.28


ATOM
1102
CA
ARG
162
6.427
45.985
0.704
1.00
45.81


ATOM
1103
C
ARG
162
7.032
45.827
2.125
1.00
45.47


ATOM
1104
O
ARG
162
7.245
46.815
2.901
1.00
44.60


ATOM
1105
CB
ARG
162
7.495
46.072
−0.389
1.00
45.64


ATOM
1106
CG
ARG
162
7.999
44.727
−0.859
1.00
45.77


ATOM
1107
CD
ARG
162
9.102
44.932
−1.931
1.00
46.20


ATOM
1108
NE
ARG
162
8.617
45.631
−3.121
1.00
43.09


ATOM
1109
CZ
ARG
162
9.405
46.253
−4.011
1.00
45.13


ATOM
1110
NH1
ARG
162
10.739
46.260
−3.862
1.00
43.75


ATOM
1111
NH2
ARG
162
8.864
46.850
−5.077
1.00
44.59


ATOM
1112
N
SER
163
7.246
44.562
2.479
1.00
44.43


ATOM
1113
CA
SER
163
7.914
44.274
3.716
1.00
43.91


ATOM
1114
C
SER
163
8.854
43.089
3.548
1.00
42.32


ATOM
1115
O
SER
163
8.597
42.184
2.760
1.00
43.00


ATOM
1116
CB
SER
163
6.887
44.120
4.856
1.00
44.01


ATOM
1117
OG
SER
163
6.306
42.851
4.855
1.00
47.10


ATOM
1118
N
ASP
182
7.974
29.007
1.900
1.00
30.08


ATOM
1119
CA
ASP
182
6.555
28.664
2.064
1.00
31.00


ATOM
1120
C
ASP
182
6.038
28.954
3.464
1.00
31.45


ATOM
1121
O
ASP
182
4.964
29.497
3.592
1.00
32.21


ATOM
1122
CB
ASP
182
6.253
27.215
1.669
1.00
31.45


ATOM
1123
CG
ASP
182
6.358
27.000
0.194
1.00
33.00


ATOM
1124
OD1
ASP
182
6.060
27.921
−0.589
1.00
38.70


ATOM
1125
OD2
ASP
182
6.807
25.947
−0.202
1.00
33.35


ATOM
1126
N
TYR
183
6.801
28.644
4.512
1.00
31.67


ATOM
1127
CA
TYR
183
6.346
29.041
5.878
1.00
31.88


ATOM
1128
C
TYR
183
5.996
30.528
6.001
1.00
31.33


ATOM
1129
O
TYR
183
5.079
30.907
6.769
1.00
31.50


ATOM
1130
CB
TYR
183
7.407
28.725
6.959
1.00
32.44


ATOM
1131
CG
TYR
183
7.509
27.281
7.389
1.00
32.80


ATOM
1132
CD1
TYR
183
6.354
26.511
7.666
1.00
34.47


ATOM
1133
CD2
TYR
183
8.759
26.691
7.578
1.00
32.37


ATOM
1134
CE1
TYR
183
6.468
25.173
8.101
1.00
33.02


ATOM
1135
CE2
TYR
183
8.889
25.375
7.983
1.00
31.79


ATOM
1136
CZ
TYR
183
7.731
24.613
8.253
1.00
33.92


ATOM
1137
OH
TYR
183
7.879
23.303
8.689
1.00
34.75


ATOM
1138
N
VAL
184
6.739
31.384
5.299
1.00
31.13


ATOM
1139
CA
VAL
184
6.472
32.854
5.349
1.00
30.51


ATOM
1140
C
VAL
184
5.338
33.275
4.441
1.00
31.17


ATOM
1141
O
VAL
184
4.415
33.963
4.858
1.00
31.57


ATOM
1142
CB
VAL
184
7.746
33.709
4.997
1.00
30.57


ATOM
1143
CG1
VAL
184
7.398
35.230
5.041
1.00
29.99


ATOM
1144
CG2
VAL
184
8.844
33.418
5.995
1.00
31.45


ATOM
1145
N
GLU
185
5.420
32.877
3.173
1.00
31.99


ATOM
1146
CA
GLU
185
4.476
33.324
2.159
1.00
33.75


ATOM
1147
C
GLU
185
3.061
32.880
2.469
1.00
35.59


ATOM
1148
O
GLU
185
2.087
33.607
2.163
1.00
34.88


ATOM
1149
CB
GLU
185
4.923
32.870
0.764
1.00
33.52


ATOM
1150
CG
GLU
185
6.124
33.693
0.249
1.00
34.66


ATOM
1151
CD
GLU
185
6.472
33.332
−1.180
1.00
37.62


ATOM
1152
OE1
GLU
185
6.132
32.170
−1.552
1.00
34.07


ATOM
1153
OE2
GLU
185
7.071
34.197
−1.905
1.00
39.40


ATOM
1154
N
THR
186
2.962
31.717
3.113
1.00
37.29


ATOM
1155
CA
THR
186
1.671
31.201
3.581
1.00
39.44


ATOM
1156
C
THR
186
0.997
32.210
4.470
1.00
39.55


ATOM
1157
O
THR
186
−0.216
32.385
4.416
1.00
39.96


ATOM
1158
CB
THR
186
1.831
29.910
4.351
1.00
39.43


ATOM
1159
OG1
THR
186
1.926
28.849
3.413
1.00
41.26


ATOM
1160
CG2
THR
186
0.608
29.660
5.263
1.00
42.27


ATOM
1161
N
GLN
187
1.809
32.893
5.263
1.00
40.30


ATOM
1162
CA
GLN
187
1.310
33.776
6.305
1.00
40.35


ATOM
1163
C
GLN
187
1.120
35.216
5.847
1.00
40.86


ATOM
1164
O
GLN
187
0.467
36.006
6.546
1.00
40.53


ATOM
1165
CB
GLN
187
2.233
33.730
7.547
1.00
40.36


ATOM
1166
CG
GLN
187
2.314
32.345
8.228
1.00
39.80


ATOM
1167
CD
GLN
187
0.947
31.843
8.653
1.00
39.36


ATOM
1168
OE1
GLN
187
0.005
32.637
8.777
1.00
39.91


ATOM
1169
NE2
GLN
187
0.828
30.533
8.887
1.00
35.15


ATOM
1170
N
ALA
188
1.671
35.577
4.691
1.00
41.85


ATOM
1171
CA
ALA
188
1.614
36.982
4.252
1.00
43.17


ATOM
1172
C
ALA
188
0.192
37.478
4.004
1.00
43.55


ATOM
1173
O
ALA
188
−0.660
36.705
3.577
1.00
43.98


ATOM
1174
CB
ALA
188
2.520
37.221
2.984
1.00
43.74


ATOM
1175
N
SER
189
−0.068
38.764
4.297
1.00
44.60


ATOM
1176
CA
SER
189
−1.298
39.443
3.803
1.00
45.06


ATOM
1177
C
SER
189
−1.502
39.047
2.327
1.00
45.29


ATOM
1178
O
SER
189
−2.600
38.660
1.911
1.00
45.23


ATOM
1179
CB
SER
189
−1.173
40.985
3.887
1.00
45.28


ATOM
1180
OG
SER
189
−1.596
41.515
5.133
1.00
44.89


ATOM
1181
N
CYS
190
−0.429
39.195
1.550
1.00
45.95


ATOM
1182
CA
CYS
190
−0.320
38.624
0.189
1.00
46.60


ATOM
1183
C
CYS
190
1.148
38.554
−0.259
1.00
46.70


ATOM
1184
O
CYS
190
1.985
39.389
0.126
1.00
46.76


ATOM
1185
CB
CYS
190
−1.153
39.403
−0.841
1.00
46.68


ATOM
1186
SG
CYS
190
−1.465
38.481
−2.425
1.00
48.51


ATOM
1187
N
GLN
191
1.450
37.547
−1.064
1.00
46.03


ATOM
1188
CA
GLN
191
2.796
37.394
−1.622
1.00
46.34


ATOM
1189
C
GLN
191
2.995
38.173
−2.921
1.00
45.74


ATOM
1190
O
GLN
191
2.041
38.669
−3.533
1.00
45.80


ATOM
1191
CB
GLN
191
3.115
35.919
−1.856
1.00
46.24


ATOM
1192
CG
GLN
191
1.986
35.180
−2.522
1.00
46.12


ATOM
1193
CD
GLN
191
2.257
33.712
−2.616
1.00
45.71


ATOM
1194
OE1
GLN
191
3.128
33.300
−3.362
1.00
42.50


ATOM
1195
NE2
GLN
191
1.513
32.902
−1.839
1.00
47.50


ATOM
1196
N
LEU
192
4.251
38.244
−3.341
1.00
45.93


ATOM
1197
CA
LEU
192
4.634
39.027
−4.508
1.00
45.42


ATOM
1198
C
LEU
192
4.759
38.161
−5.762
1.00
45.84


ATOM
1199
O
LEU
192
5.036
36.946
−5.694
1.00
45.09


ATOM
1200
CB
LEU
192
5.940
39.784
−4.234
1.00
45.16


ATOM
1201
CG
LEU
192
5.993
40.741
−3.044
1.00
43.78


ATOM
1202
CD1
LEU
192
7.329
41.465
−3.016
1.00
43.93


ATOM
1203
CD2
LEU
192
4.893
41.763
−3.093
1.00
43.70


ATOM
1204
N
TYR
193
4.520
38.805
−6.906
1.00
45.73


ATOM
1205
CA
TYR
193
4.756
38.202
−8.203
1.00
45.73


ATOM
1206
C
TYR
193
5.404
39.253
−9.120
1.00
46.31


ATOM
1207
O
TYR
193
5.035
40.453
−9.095
1.00
45.28


ATOM
1208
CB
TYR
193
3.445
37.682
−8.812
1.00
45.20


ATOM
1209
CG
TYR
193
2.638
36.729
−7.907
1.00
44.11


ATOM
1210
CD1
TYR
193
2.823
35.342
−7.964
1.00
43.87


ATOM
1211
CD2
TYR
193
1.683
37.234
−6.998
1.00
44.60


ATOM
1212
CE1
TYR
193
2.068
34.476
−7.143
1.00
43.56


ATOM
1213
CE2
TYR
193
0.930
36.391
−6.190
1.00
42.74


ATOM
1214
CZ
TYR
193
1.133
35.011
−6.273
1.00
42.90


ATOM
1215
OH
TYR
193
0.401
34.193
−5.474
1.00
44.37


ATOM
1216
N
GLY
194
6.385
38.797
−9.896
1.00
47.12


ATOM
1217
CA
GLY
194
6.981
39.619
−10.936
1.00
48.68


ATOM
1218
C
GLY
194
5.913
40.033
−11.934
1.00
49.53


ATOM
1219
O
GLY
194
5.722
41.237
−12.171
1.00
49.81


ATOM
1220
N
LEU
195
5.188
39.052
−12.482
1.00
50.33


ATOM
1221
CA
LEU
195
4.240
39.325
−13.579
1.00
51.06


ATOM
1222
C
LEU
195
2.784
39.075
−13.193
1.00
52.16


ATOM
1223
O
LEU
195
2.389
37.931
−12.837
1.00
51.75


ATOM
1224
CB
LEU
195
4.612
38.531
−14.840
1.00
50.86


ATOM
1225
CG
LEU
195
3.940
38.802
−16.195
1.00
50.48


ATOM
1226
CD1
LEU
195
4.719
38.065
−17.275
1.00
49.39


ATOM
1227
CD2
LEU
195
2.516
38.279
−16.207
1.00
51.52


ATOM
1228
N
LEU
196
1.990
40.143
−13.290
1.00
53.08


ATOM
1229
CA
LEU
196
0.583
40.080
−12.936
1.00
55.19


ATOM
1230
C
LEU
196
−0.282
40.642
−14.069
1.00
56.77


ATOM
1231
O
LEU
196
0.000
41.715
−14.604
1.00
56.95


ATOM
1232
CB
LEU
196
0.326
40.816
−11.612
1.00
54.79


ATOM
1233
CG
LEU
196
0.949
40.185
−10.346
1.00
55.32


ATOM
1234
CD1
LEU
196
0.931
41.147
−9.136
1.00
54.75


ATOM
1235
CD2
LEU
196
0.317
38.807
−9.990
1.00
54.04


ATOM
1236
N
LYS
197
−1.314
39.901
−14.463
1.00
58.59


ATOM
1237
CA
LYS
197
−2.334
40.487
−15.353
1.00
60.40


ATOM
1238
C
LYS
197
−3.393
41.246
−14.545
1.00
60.81


ATOM
1239
O
LYS
197
−3.364
41.225
−13.294
1.00
60.59


ATOM
1240
CB
LYS
197
−2.941
39.450
−16.316
1.00
60.82


ATOM
1241
CG
LYS
197
−2.344
39.536
−17.753
1.00
63.00


ATOM
1242
CD
LYS
197
−0.793
39.432
−17.781
1.00
64.23


ATOM
1243
CE
LYS
197
−0.195
39.552
−19.202
1.00
64.55


ATOM
1244
NZ
LYS
197
−0.184
40.949
−19.739
1.00
64.56


ATOM
1245
N
ARG
198
−4.289
41.941
−15.256
1.00
61.03


ATOM
1246
CA
ARG
198
−5.388
42.674
−14.631
1.00
61.98


ATOM
1247
C
ARG
198
−6.168
41.862
−13.574
1.00
61.01


ATOM
1248
O
ARG
198
−6.279
42.298
−12.435
1.00
60.94


ATOM
1249
CB
ARG
198
−6.332
43.276
−15.690
1.00
62.12


ATOM
1250
CG
ARG
198
−6.388
44.804
−15.679
1.00
64.00


ATOM
1251
CD
ARG
198
−6.848
45.429
−17.028
1.00
64.71


ATOM
1252
NE
ARG
198
−7.001
46.884
−16.895
1.00
70.51


ATOM
1253
CZ
ARG
198
−8.173
47.527
−16.895
1.00
71.39


ATOM
1254
NH1
ARG
198
−9.309
46.851
−17.049
1.00
74.34


ATOM
1255
NH2
ARG
198
−8.216
48.850
−16.745
1.00
73.50


ATOM
1256
N
PRO
199
−6.712
40.685
−13.949
1.00
60.31


ATOM
1257
CA
PRO
199
−7.394
39.878
−12.926
1.00
59.80


ATOM
1258
C
PRO
199
−6.506
39.474
−11.725
1.00
59.02


ATOM
1259
O
PRO
199
−6.975
39.527
−10.582
1.00
58.60


ATOM
1260
CB
PRO
199
−7.891
38.642
−13.706
1.00
60.10


ATOM
1261
CG
PRO
199
−7.149
38.640
−15.009
1.00
60.56


ATOM
1262
CD
PRO
199
−6.771
40.064
−15.291
1.00
60.60


ATOM
1263
N
ASP
200
−5.247
39.104
−11.978
1.00
58.37


ATOM
1264
CA
ASP
200
−4.289
38.793
−10.889
1.00
58.09


ATOM
1265
C
ASP
200
−4.123
39.966
−9.932
1.00
57.97


ATOM
1266
O
ASP
200
−4.210
39.797
−8.707
1.00
58.11


ATOM
1267
CB
ASP
200
−2.916
38.406
−11.440
1.00
57.41


ATOM
1268
CG
ASP
200
−2.987
37.271
−12.416
1.00
56.87


ATOM
1269
OD1
ASP
200
−3.551
36.216
−12.044
1.00
56.53


ATOM
1270
OD2
ASP
200
−2.471
37.434
−13.545
1.00
54.07


ATOM
1271
N
GLU
201
−3.876
41.149
−10.498
1.00
57.96


ATOM
1272
CA
GLU
201
−3.801
42.384
−9.707
1.00
58.04


ATOM
1273
C
GLU
201
−5.089
42.642
−8.868
1.00
57.99


ATOM
1274
O
GLU
201
−5.010
43.124
−7.717
1.00
57.08


ATOM
1275
CB
GLU
201
−3.411
43.598
−10.577
1.00
58.12


ATOM
1276
CG
GLU
201
−3.762
44.941
−9.910
1.00
59.81


ATOM
1277
CD
GLU
201
−2.850
46.081
−10.275
1.00
59.25


ATOM
1278
OE1
GLU
201
−2.353
46.127
−11.424
1.00
61.24


ATOM
1279
OE2
GLU
201
−2.653
46.948
−9.394
1.00
61.33


ATOM
1280
N
LYS
202
−6.258
42.314
−9.444
1.00
58.11


ATOM
1281
CA
LYS
202
−7.538
42.418
−8.733
1.00
58.01


ATOM
1282
C
LYS
202
−7.538
41.480
−7.519
1.00
57.58


ATOM
1283
O
LYS
202
−7.884
41.906
−6.416
1.00
57.11


ATOM
1284
CB
LYS
202
−8.729
42.138
−9.670
1.00
58.00


ATOM
1285
CG
LYS
202
−10.094
42.131
−8.991
1.00
58.29


ATOM
1286
CD
LYS
202
−11.235
41.997
−10.025
1.00
58.66


ATOM
1287
CE
LYS
202
−12.517
41.344
−9.442
1.00
58.41


ATOM
1288
NZ
LYS
202
−12.846
41.660
−8.009
1.00
59.05


ATOM
1289
N
TYR
203
−7.132
40.222
−7.752
1.00
57.29


ATOM
1290
CA
TYR
203
−7.027
39.165
−6.731
1.00
56.76


ATOM
1291
C
TYR
203
−6.051
39.573
−5.622
1.00
55.73


ATOM
1292
O
TYR
203
−6.365
39.520
−4.439
1.00
55.19


ATOM
1293
CB
TYR
203
−6.594
37.836
−7.391
1.00
57.82


ATOM
1294
CG
TYR
203
−6.403
36.661
−6.431
1.00
57.69


ATOM
1295
CD1
TYR
203
−7.378
35.642
−6.304
1.00
59.41


ATOM
1296
CD2
TYR
203
−5.257
36.582
−5.633
1.00
59.00


ATOM
1297
CE1
TYR
203
−7.192
34.563
−5.410
1.00
59.51


ATOM
1298
CE2
TYR
203
−5.065
35.531
−4.745
1.00
60.75


ATOM
1299
CZ
TYR
203
−6.017
34.520
−4.636
1.00
58.13


ATOM
1300
OH
TYR
203
−5.754
33.498
−3.740
1.00
60.67


ATOM
1301
N
VAL
204
−4.866
39.998
−6.026
1.00
54.95


ATOM
1302
CA
VAL
204
−3.835
40.403
−5.072
1.00
54.58


ATOM
1303
C
VAL
204
−4.290
41.638
−4.213
1.00
53.79


ATOM
1304
O
VAL
204
−4.091
41.662
−2.986
1.00
52.60


ATOM
1305
CB
VAL
204
−2.469
40.569
−5.822
1.00
54.92


ATOM
1306
CG1
VAL
204
−1.523
41.522
−5.116
1.00
56.19


ATOM
1307
CG2
VAL
204
−1.820
39.187
−6.087
1.00
53.61


ATOM
1308
N
THR
205
−4.949
42.619
−4.851
1.00
53.09


ATOM
1309
CA
THR
205
−5.456
43.794
−4.132
1.00
52.58


ATOM
1310
C
THR
205
−6.437
43.402
−3.017
1.00
53.09


ATOM
1311
O
THR
205
−6.340
43.906
−1.878
1.00
52.50


ATOM
1312
CB
THR
205
−6.109
44.841
−5.091
1.00
52.24


ATOM
1313
OG1
THR
205
−5.109
45.371
−5.976
1.00
50.47


ATOM
1314
CG2
THR
205
−6.716
46.000
−4.305
1.00
51.46


ATOM
1315
N
GLU
206
−7.352
42.491
−3.365
1.00
53.01


ATOM
1316
CA
GLU
206
−8.444
42.065
−2.489
1.00
53.57


ATOM
1317
C
GLU
206
−7.956
41.177
−1.363
1.00
53.60


ATOM
1318
O
GLU
206
−8.280
41.441
−0.203
1.00
53.68


ATOM
1319
CB
GLU
206
−9.563
41.399
−3.295
1.00
53.31


ATOM
1320
CG
GLU
206
−10.150
42.359
−4.283
1.00
54.66


ATOM
1321
CD
GLU
206
−11.279
41.793
−5.124
1.00
55.83


ATOM
1322
OE1
GLU
206
−11.449
40.555
−5.199
1.00
58.27


ATOM
1323
OE2
GLU
206
−11.993
42.618
−5.731
1.00
57.86


ATOM
1324
N
LYS
207
−7.171
40.150
−1.714
1.00
53.98


ATOM
1325
CA
LYS
207
−6.504
39.245
−0.746
1.00
54.40


ATOM
1326
C
LYS
207
−5.834
40.060
0.379
1.00
54.04


ATOM
1327
O
LYS
207
−6.116
39.867
1.572
1.00
53.03


ATOM
1328
CB
LYS
207
−5.463
38.376
−1.481
1.00
54.50


ATOM
1329
CG
LYS
207
−4.727
37.339
−0.646
1.00
56.04


ATOM
1330
CD
LYS
207
−3.784
36.509
−1.522
1.00
58.59


ATOM
1331
CE
LYS
207
−3.018
35.463
−0.713
1.00
59.46


ATOM
1332
NZ
LYS
207
−2.119
34.690
−1.635
1.00
58.18


ATOM
1333
N
ALA
208
−4.973
40.991
−0.029
1.00
54.31


ATOM
1334
CA
ALA
208
−4.238
41.807
0.900
1.00
55.01


ATOM
1335
C
ALA
208
−5.226
42.582
1.799
1.00
55.58


ATOM
1336
O
ALA
208
−5.072
42.586
3.021
1.00
55.47


ATOM
1337
CB
ALA
208
−3.292
42.757
0.130
1.00
55.20


ATOM
1338
N
TYR
209
−6.243
43.203
1.183
1.00
57.15


ATOM
1339
CA
TYR
209
−7.312
43.954
1.915
1.00
56.96


ATOM
1340
C
TYR
209
−8.039
43.078
2.964
1.00
56.61


ATOM
1341
O
TYR
209
−8.230
43.504
4.130
1.00
56.39


ATOM
1342
CB
TYR
209
−8.321
44.578
0.925
1.00
57.07


ATOM
1343
CG
TYR
209
−9.265
45.654
1.483
1.00
57.70


ATOM
1344
CD1
TYR
209
−8.809
46.966
1.731
1.00
58.72


ATOM
1345
CD2
TYR
209
−10.631
45.372
1.719
1.00
58.01


ATOM
1346
CE1
TYR
209
−9.689
47.962
2.216
1.00
59.35


ATOM
1347
CE2
TYR
209
−11.506
46.352
2.208
1.00
57.42


ATOM
1348
CZ
TYR
209
−11.026
47.643
2.451
1.00
55.90


ATOM
1349
OH
TYR
209
−11.881
48.614
2.917
1.00
58.74


ATOM
1350
N
GLU
210
−8.389
41.850
2.558
1.00
56.26


ATOM
1351
CA
GLU
210
−9.155
40.915
3.411
1.00
56.42


ATOM
1352
C
GLU
210
−8.343
40.311
4.566
1.00
56.04


ATOM
1353
O
GLU
210
−8.907
39.813
5.553
1.00
56.04


ATOM
1354
CB
GLU
210
−9.743
39.778
2.566
1.00
56.91


ATOM
1355
CG
GLU
210
−10.701
40.245
1.446
1.00
58.24


ATOM
1356
CD
GLU
210
−10.842
39.213
0.337
1.00
61.03


ATOM
1357
OE1
GLU
210
−10.317
38.078
0.514
1.00
63.30


ATOM
1358
OE2
GLU
210
−11.480
39.531
−0.700
1.00
60.60


ATOM
1359
N
ASN
211
−7.021
40.392
4.434
1.00
54.85


ATOM
1360
CA
ASN
211
−6.079
39.673
5.277
1.00
54.55


ATOM
1361
C
ASN
211
−5.033
40.685
5.879
1.00
53.11


ATOM
1362
O
ASN
211
−3.831
40.440
5.806
1.00
52.60


ATOM
1363
CB
ASN
211
−5.479
38.526
4.393
1.00
55.22


ATOM
1364
CG
ASN
211
−4.332
37.738
5.055
1.00
58.06


ATOM
1365
OD1
ASN
211
−4.018
37.910
6.243
1.00
60.91


ATOM
1366
ND2
ASN
211
−3.692
36.855
4.261
1.00
59.82


ATOM
1367
N
PRO
212
−5.496
41.823
6.491
1.00
51.64


ATOM
1368
CA
PRO
212
−4.515
42.792
6.998
1.00
50.32


ATOM
1369
C
PRO
212
−3.784
42.189
8.212
1.00
49.35


ATOM
1370
O
PRO
212
−4.417
41.504
9.022
1.00
48.96


ATOM
1371
CB
PRO
212
−5.386
43.965
7.461
1.00
50.49


ATOM
1372
CG
PRO
212
−6.674
43.322
7.891
1.00
51.04


ATOM
1373
CD
PRO
212
−6.876
42.240
6.826
1.00
51.68


ATOM
1374
N
LYS
213
−2.479
42.447
8.318
1.00
47.51


ATOM
1375
CA
LYS
213
−1.648
41.922
9.375
1.00
46.52


ATOM
1376
C
LYS
213
−0.638
42.975
9.769
1.00
46.02


ATOM
1377
O
LYS
213
0.019
43.569
8.906
1.00
46.15


ATOM
1378
CB
LYS
213
−0.893
40.683
8.909
1.00
46.06


ATOM
1379
CG
LYS
213
−1.769
39.444
8.686
1.00
45.94


ATOM
1380
CD
LYS
213
−1.021
38.131
9.006
1.00
42.30


ATOM
1381
CE
LYS
213
−1.946
36.939
8.706
1.00
42.12


ATOM
1382
NZ
LYS
213
−1.223
35.624
8.755
1.00
41.19


ATOM
1383
N
PHE
214
−0.534
43.219
11.073
1.00
45.52


ATOM
1384
CA
PHE
214
0.540
44.036
11.634
1.00
45.58


ATOM
1385
C
PHE
214
1.875
43.286
11.471
1.00
43.76


ATOM
1386
O
PHE
214
1.897
42.056
11.285
1.00
43.89


ATOM
1387
CB
PHE
214
0.299
44.270
13.141
1.00
46.89


ATOM
1388
CG
PHE
214
−0.840
45.208
13.471
1.00
48.64


ATOM
1389
CD1
PHE
214
−0.830
46.539
13.033
1.00
51.01


ATOM
1390
CD2
PHE
214
−1.890
44.774
14.309
1.00
50.55


ATOM
1391
CE1
PHE
214
−1.876
47.429
13.378
1.00
52.20


ATOM
1392
CE2
PHE
214
−2.938
45.632
14.672
1.00
50.78


ATOM
1393
CZ
PHE
214
−2.938
46.969
14.199
1.00
51.48


ATOM
1394
N
VAL
215
2.986
44.012
11.572
1.00
41.22


ATOM
1395
CA
VAL
215
4.268
43.360
11.753
1.00
39.38


ATOM
1396
C
VAL
215
4.255
42.345
12.936
1.00
38.44


ATOM
1397
O
VAL
215
4.831
41.253
12.830
1.00
37.18


ATOM
1398
CB
VAL
215
5.451
44.375
11.859
1.00
39.18


ATOM
1399
CG1
VAL
215
5.390
45.238
13.135
1.00
37.11


ATOM
1400
CG2
VAL
215
6.681
43.638
11.833
1.00
39.54


ATOM
1401
N
GLU
216
3.578
42.708
14.035
1.00
37.54


ATOM
1402
CA
GLU
216
3.430
41.817
15.200
1.00
36.83


ATOM
1403
C
GLU
216
2.775
40.467
14.819
1.00
36.37


ATOM
1404
O
GLU
216
3.271
39.407
15.164
1.00
35.59


ATOM
1405
CB
GLU
216
2.592
42.489
16.287
1.00
36.59


ATOM
1406
CG
GLU
216
3.269
43.670
17.002
1.00
36.95


ATOM
1407
CD
GLU
216
2.843
45.025
16.448
1.00
36.23


ATOM
1408
OE1
GLU
216
2.424
45.033
15.285
1.00
35.17


ATOM
1409
OE2
GLU
216
2.953
46.079
17.152
1.00
36.48


ATOM
1410
N
ASP
217
1.666
40.541
14.096
1.00
37.46


ATOM
1411
CA
ASP
217
0.924
39.365
13.575
1.00
37.41


ATOM
1412
C
ASP
217
1.763
38.503
12.679
1.00
36.40


ATOM
1413
O
ASP
217
1.733
37.268
12.781
1.00
35.80


ATOM
1414
CB
ASP
217
−0.305
39.833
12.782
1.00
39.17


ATOM
1415
CG
ASP
217
−1.379
40.441
13.689
1.00
42.59


ATOM
1416
OD1
ASP
217
−1.611
39.879
14.803
1.00
44.14


ATOM
1417
OD2
ASP
217
−1.972
41.474
13.294
1.00
45.24


ATOM
1418
N
MET
218
2.523
39.141
11.793
1.00
36.11


ATOM
1419
CA
MET
218
3.384
38.395
10.895
1.00
35.43


ATOM
1420
C
MET
218
4.516
37.691
11.624
1.00
33.47


ATOM
1421
O
MET
218
4.761
36.528
11.387
1.00
32.57


ATOM
1422
CB
MET
218
3.919
39.291
9.744
1.00
36.86


ATOM
1423
CG
MET
218
4.835
38.557
8.686
1.00
39.05


ATOM
1424
SD
MET
218
4.098
37.370
7.489
1.00
48.15


ATOM
1425
CE
MET
218
2.385
37.538
7.908
1.00
47.14


ATOM
1426
N
VAL
219
5.233
38.362
12.507
1.00
32.53


ATOM
1427
CA
VAL
219
6.310
37.604
13.169
1.00
32.64


ATOM
1428
C
VAL
219
5.758
36.404
13.970
1.00
32.02


ATOM
1429
O
VAL
219
6.383
35.315
13.996
1.00
30.73


ATOM
1430
CB
VAL
219
7.290
38.469
14.026
1.00
32.81


ATOM
1431
CG1
VAL
219
8.108
39.389
13.124
1.00
33.18


ATOM
1432
CG2
VAL
219
6.570
39.256
15.095
1.00
33.07


ATOM
1433
N
ARG
220
4.613
36.621
14.631
1.00
32.42


ATOM
1434
CA
ARG
220
3.940
35.569
15.425
1.00
32.49


ATOM
1435
C
ARG
220
3.445
34.351
14.650
1.00
33.39


ATOM
1436
O
ARG
220
3.745
33.199
15.037
1.00
34.66


ATOM
1437
CB
ARG
220
2.814
36.156
16.220
1.00
32.42


ATOM
1438
CG
ARG
220
3.309
36.924
17.434
1.00
31.64


ATOM
1439
CD
ARG
220
2.123
37.638
18.065
1.00
32.29


ATOM
1440
NE
ARG
220
2.428
37.976
19.436
1.00
34.95


ATOM
1441
CZ
ARG
220
1.932
39.029
20.059
1.00
35.09


ATOM
1442
NH1
ARG
220
1.120
39.873
19.417
1.00
33.56


ATOM
1443
NH2
ARG
220
2.268
39.240
21.319
1.00
36.65


ATOM
1444
N
ASP
221
2.717
34.590
13.566
1.00
34.07


ATOM
1445
CA
ASP
221
2.290
33.526
12.636
1.00
33.76


ATOM
1446
C
ASP
221
3.446
32.709
12.069
1.00
33.51


ATOM
1447
O
ASP
221
3.342
31.489
11.968
1.00
33.79


ATOM
1448
CB
ASP
221
1.453
34.155
11.505
1.00
34.70


ATOM
1449
CG
ASP
221
0.124
34.705
12.009
1.00
36.94


ATOM
1450
OD1
ASP
221
−0.162
34.438
13.197
1.00
40.28


ATOM
1451
OD2
ASP
221
−0.626
35.386
11.263
1.00
36.36


ATOM
1452
N
VAL
222
4.559
33.362
11.697
1.00
32.83


ATOM
1453
CA
VAL
222
5.737
32.623
11.232
1.00
31.91


ATOM
1454
C
VAL
222
6.418
31.859
12.389
1.00
32.92


ATOM
1455
O
VAL
222
6.823
30.689
12.243
1.00
32.48


ATOM
1456
CB
VAL
222
6.756
33.545
10.431
1.00
31.86


ATOM
1457
CG1
VAL
222
8.053
32.832
10.118
1.00
29.78


ATOM
1458
CG2
VAL
222
6.119
34.107
9.133
1.00
28.77


ATOM
1459
N
ALA
223
6.553
32.497
13.549
1.00
32.41


ATOM
1460
CA
ALA
223
7.218
31.798
14.660
1.00
32.79


ATOM
1461
C
ALA
223
6.469
30.499
15.061
1.00
32.87


ATOM
1462
O
ALA
223
7.092
29.449
15.365
1.00
32.40


ATOM
1463
CB
ALA
223
7.311
32.706
15.851
1.00
33.64


ATOM
1464
N
THR
224
5.138
30.582
15.076
1.00
33.30


ATOM
1465
CA
THR
224
4.311
29.381
15.348
1.00
34.28


ATOM
1466
C
THR
224
4.709
28.229
14.426
1.00
33.80


ATOM
1467
O
THR
224
4.883
27.108
14.896
1.00
32.18


ATOM
1468
CB
THR
224
2.834
29.667
15.250
1.00
34.79


ATOM
1469
OG1
THR
224
2.527
30.763
16.107
1.00
34.54


ATOM
1470
CG2
THR
224
2.009
28.439
15.738
1.00
38.37


ATOM
1471
N
SER
225
4.876
28.494
13.115
1.00
34.23


ATOM
1472
CA
SER
225
5.217
27.412
12.194
1.00
34.27


ATOM
1473
C
SER
225
6.582
26.873
12.546
1.00
34.88


ATOM
1474
O
SER
225
6.833
25.632
12.517
1.00
34.49


ATOM
1475
CB
SER
225
5.208
27.868
10.736
1.00
34.83


ATOM
1476
OG
SER
225
3.879
28.131
10.317
1.00
36.16


ATOM
1477
N
LEU
226
7.499
27.782
12.887
1.00
34.32


ATOM
1478
CA
LEU
226
8.863
27.327
13.123
1.00
34.58


ATOM
1479
C
LEU
226
9.034
26.602
14.480
1.00
35.09


ATOM
1480
O
LEU
226
9.871
25.702
14.624
1.00
35.39


ATOM
1481
CB
LEU
226
9.867
28.500
12.956
1.00
34.96


ATOM
1482
CG
LEU
226
9.770
29.394
11.699
1.00
33.32


ATOM
1483
CD1
LEU
226
10.737
30.580
11.796
1.00
29.72


ATOM
1484
CD2
LEU
226
10.017
28.570
10.444
1.00
31.90


ATOM
1485
N
ILE
227
8.285
27.010
15.499
1.00
35.24


ATOM
1486
CA
ILE
227
8.359
26.286
16.791
1.00
34.80


ATOM
1487
C
ILE
227
7.912
24.810
16.620
1.00
35.08


ATOM
1488
O
ILE
227
8.456
23.872
17.253
1.00
34.52


ATOM
1489
CB
ILE
227
7.486
26.982
17.862
1.00
35.35


ATOM
1490
CG1
ILE
227
8.228
28.232
18.401
1.00
35.35


ATOM
1491
CG2
ILE
227
7.131
26.002
18.992
1.00
35.51


ATOM
1492
CD1
ILE
227
7.329
29.271
19.011
1.00
35.08


ATOM
1493
N
ALA
228
6.950
24.628
15.727
1.00
35.42


ATOM
1494
CA
ALA
228
6.324
23.347
15.459
1.00
36.53


ATOM
1495
C
ALA
228
7.183
22.383
14.640
1.00
36.58


ATOM
1496
O
ALA
228
7.024
21.150
14.741
1.00
37.14


ATOM
1497
CB
ALA
228
4.984
23.585
14.774
1.00
36.82


ATOM
1498
N
ASP
229
8.109
22.915
13.850
1.00
36.37


ATOM
1499
CA
ASP
229
8.973
22.068
13.018
1.00
36.10


ATOM
1500
C
ASP
229
10.034
21.426
13.915
1.00
37.32


ATOM
1501
O
ASP
229
10.792
22.141
14.572
1.00
37.73


ATOM
1502
CB
ASP
229
9.585
22.921
11.897
1.00
35.82


ATOM
1503
CG
ASP
229
10.310
22.096
10.861
1.00
35.00


ATOM
1504
OD1
ASP
229
11.209
21.314
11.240
1.00
32.09


ATOM
1505
OD2
ASP
229
9.966
22.218
9.653
1.00
34.51


ATOM
1506
N
ASN
241
8.407
46.451
7.910
1.00
38.75


ATOM
1507
CA
ASN
241
7.350
46.945
7.062
1.00
40.86


ATOM
1508
C
ASN
241
7.685
48.355
6.625
1.00
41.84


ATOM
1509
O
ASN
241
7.708
49.260
7.459
1.00
41.53


ATOM
1510
CB
ASN
241
6.035
47.019
7.831
1.00
41.45


ATOM
1511
CG
ASN
241
5.404
45.673
8.066
1.00
45.01


ATOM
1512
OD1
ASN
241
4.426
45.578
8.807
1.00
50.80


ATOM
1513
ND2
ASN
241
5.938
44.623
7.443
1.00
47.80


ATOM
1514
N
PHE
242
7.931
48.549
5.327
1.00
42.06


ATOM
1515
CA
PHE
242
8.328
49.882
4.849
1.00
43.01


ATOM
1516
C
PHE
242
7.099
50.800
4.761
1.00
43.06


ATOM
1517
O
PHE
242
6.628
51.115
3.649
1.00
41.83


ATOM
1518
CB
PHE
242
9.160
49.775
3.539
1.00
42.80


ATOM
1519
CG
PHE
242
10.470
49.042
3.748
1.00
43.34


ATOM
1520
CD1
PHE
242
11.578
49.719
4.232
1.00
43.78


ATOM
1521
CD2
PHE
242
10.565
47.650
3.542
1.00
43.59


ATOM
1522
CE1
PHE
242
12.781
49.044
4.457
1.00
45.11


ATOM
1523
CE2
PHE
242
11.767
46.969
3.755
1.00
42.03


ATOM
1524
CZ
PHE
242
12.872
47.668
4.214
1.00
43.33


ATOM
1525
N
GLU
243
6.591
51.185
5.947
1.00
42.20


ATOM
1526
CA
GLU
243
5.313
51.890
6.091
1.00
43.24


ATOM
1527
C
GLU
243
5.193
52.917
4.975
1.00
42.95


ATOM
1528
O
GLU
243
6.100
53.756
4.795
1.00
41.58


ATOM
1529
CB
GLU
243
5.176
52.603
7.456
1.00
43.53


ATOM
1530
CG
GLU
243
5.166
51.691
8.686
1.00
47.74


ATOM
1531
CD
GLU
243
4.045
50.630
8.672
1.00
53.02


ATOM
1532
OE1
GLU
243
2.909
50.935
9.111
1.00
56.85


ATOM
1533
OE2
GLU
243
4.313
49.470
8.262
1.00
54.32


ATOM
1534
N
SER
244
4.109
52.799
4.205
1.00
42.95


ATOM
1535
CA
SER
244
3.917
53.634
3.017
1.00
43.67


ATOM
1536
C
SER
244
3.492
55.057
3.422
1.00
44.11


ATOM
1537
O
SER
244
3.430
55.917
2.559
1.00
43.54


ATOM
1538
CB
SER
244
2.872
53.035
2.062
1.00
43.70


ATOM
1539
OG
SER
244
1.608
52.882
2.714
1.00
43.76


ATOM
1540
N
ILE
245
3.247
55.269
4.732
1.00
44.53


ATOM
1541
CA
ILE
245
2.762
56.542
5.305
1.00
44.90


ATOM
1542
C
ILE
245
3.796
57.370
6.114
1.00
44.98


ATOM
1543
O
ILE
245
3.579
58.562
6.399
1.00
45.25


ATOM
1544
CB
ILE
245
1.446
56.328
6.131
1.00
45.08


ATOM
1545
CG1
ILE
245
1.678
55.420
7.340
1.00
45.82


ATOM
1546
CG2
ILE
245
0.327
55.744
5.234
1.00
45.11


ATOM
1547
CD1
ILE
245
0.563
55.480
8.372
1.00
45.19


ATOM
1548
N
HIS
246
4.912
56.729
6.467
1.00
44.82


ATOM
1549
CA
HIS
246
6.046
57.364
7.170
1.00
44.40


ATOM
1550
C
HIS
246
7.299
57.172
6.337
1.00
43.85


ATOM
1551
O
HIS
246
7.274
56.491
5.290
1.00
43.92


ATOM
1552
CB
HIS
246
6.306
56.687
8.529
1.00
45.24


ATOM
1553
CG
HIS
246
5.125
56.674
9.448
1.00
45.19


ATOM
1554
ND1
HIS
246
4.574
55.504
9.935
1.00
47.43


ATOM
1555
CD2
HIS
246
4.390
57.685
9.968
1.00
44.55


ATOM
1556
CE1
HIS
246
3.557
55.804
10.729
1.00
47.01


ATOM
1557
NE2
HIS
246
3.423
57.121
10.761
1.00
45.51


ATOM
1558
N
ASN
247
8.409
57.740
6.798
1.00
42.26


ATOM
1559
CA
ASN
247
9.689
57.458
6.151
1.00
40.75


ATOM
1560
C
ASN
247
10.617
56.602
7.022
1.00
39.27


ATOM
1561
O
ASN
247
11.858
56.641
6.871
1.00
39.39


ATOM
1562
CB
ASN
247
10.388
58.753
5.655
1.00
41.37


ATOM
1563
CG
ASN
247
11.418
58.491
4.526
1.00
41.38


ATOM
1564
OD1
ASN
247
11.262
57.564
3.727
1.00
42.55


ATOM
1565
ND2
ASN
247
12.482
59.322
4.475
1.00
40.83


ATOM
1566
N
TYR
251
8.983
47.503
12.864
1.00
31.14


ATOM
1567
CA
TYR
251
9.911
46.418
12.972
1.00
31.17


ATOM
1568
C
TYR
251
9.549
45.501
14.174
1.00
31.66


ATOM
1569
O
TYR
251
9.072
45.965
15.166
1.00
31.06


ATOM
1570
CB
TYR
251
11.325
46.995
13.106
1.00
30.79


ATOM
1571
CG
TYR
251
12.393
45.981
13.307
1.00
30.68


ATOM
1572
CD1
TYR
251
12.814
45.139
12.251
1.00
29.05


ATOM
1573
CD2
TYR
251
12.998
45.830
14.566
1.00
30.94


ATOM
1574
CE1
TYR
251
13.793
44.182
12.450
1.00
30.88


ATOM
1575
CE2
TYR
251
13.994
44.862
14.766
1.00
33.74


ATOM
1576
CZ
TYR
251
14.389
44.058
13.702
1.00
31.97


ATOM
1577
OH
TYR
251
15.362
43.101
13.900
1.00
35.58


TER











ATOM
1578
MN
MN2 C
258
−0.987
51.767
9.777
1.00
49.60


TER











ATOM
1579
N
ASN
15
−0.055
31.945
21.743
1.00
57.77


ATOM
1580
CA
ASN
15
0.077
33.433
21.573
1.00
57.60


ATOM
1581
C
ASN
15
1.474
33.904
21.106
1.00
56.17


ATOM
1582
O
ASN
15
1.638
34.372
19.944
1.00
57.59


ATOM
1583
CB
ASN
15
−0.349
34.162
22.857
1.00
58.61


ATOM
1584
CG
ASN
15
−1.826
34.577
22.840
1.00
61.05


ATOM
1585
OD1
ASN
15
−2.439
34.707
21.763
1.00
62.70


ATOM
1586
ND2
ASN
15
−2.407
34.794
24.045
1.00
62.68


ATOM
1587
N
LEU
16
2.466
33.763
21.989
1.00
53.16


ATOM
1588
CA
LEU
16
3.873
34.147
21.715
1.00
49.45


ATOM
1589
C
LEU
16
4.265
35.599
22.049
1.00
46.26


ATOM
1590
O
LEU
16
3.774
36.563
21.428
1.00
45.34


ATOM
1591
CB
LEU
16
4.286
33.777
20.281
1.00
50.00


ATOM
1592
CG
LEU
16
5.106
32.522
20.015
1.00
50.00


ATOM
1593
CD1
LEU
16
4.760
31.319
20.907
1.00
49.39


ATOM
1594
CD2
LEU
16
5.019
32.185
18.515
1.00
49.75


ATOM
1595
N
PRO
17
5.144
35.758
23.051
1.00
43.37


ATOM
1596
CA
PRO
17
5.673
37.102
23.272
1.00
42.01


ATOM
1597
C
PRO
17
6.630
37.522
22.123
1.00
39.49


ATOM
1598
O
PRO
17
7.206
36.658
2.1.457
1.00
38.46


ATOM
1599
CB
PRO
17
6.387
37.010
24.638
1.00
41.94


ATOM
1600
CG
PRO
17
6.625
35.499
24.889
1.00
42.78


ATOM
1601
CD
PRO
17
5.660
34.747
24.004
1.00
43.71


ATOM
1602
N
ILE
18
6.757
38.833
21.888
1.00
37.20


ATOM
1603
CA
ILE
18
7.707
39.360
20.889
1.00
34.81


ATOM
1604
C
ILE
18
8.860
40.054
21.617
1.00
34.48


ATOM
1605
O
ILE
18
8.658
41.020
22.359
1.00
33.94


ATOM
1606
CB
ILE
18
7.007
40.305
19.844
1.00
35.33


ATOM
1607
CG1
ILE
18
5.742
39.641
19.284
1.00
34.34


ATOM
1608
CG2
ILE
18
7.994
40.729
18.733
1.00
34.30


ATOM
1609
CD1
ILE
18
4.965
40.363
18.195
1.00
33.50


ATOM
1610
N
ASN
19
10.077
39.554
21.388
1.00
34.14


ATOM
1611
CA
ASN
19
11.282
40.096
22.001
1.00
33.65


ATOM
1612
C
ASN
19
11.389
41.597
21.857
1.00
33.26


ATOM
1613
O
ASN
19
11.644
42.306
22.834
1.00
32.04


ATOM
1614
CB
ASN
19
12.539
39.407
21.443
1.00
34.52


ATOM
1615
CG
ASN
19
12.552
37.950
21.744
1.00
36.27


ATOM
1616
OD1
ASN
19
13.318
37.480
22.582
1.00
42.25


ATOM
1617
ND2
ASN
19
11.678
37.229
21.114
1.00
35.29


ATOM
1618
N
GLY
22
8.798
47.783
17.427
1.00
30.37


ATOM
1619
CA
GLY
22
8.928
49.238
17.433
1.00
29.76


ATOM
1620
C
GLY
22
9.283
49.783
16.066
1.00
30.75


ATOM
1621
O
GLY
22
8.767
49.302
15.054
1.00
31.28


ATOM
1622
N
VAL
49
10.256
47.847
22.103
1.00
29.99


ATOM
1623
CA
VAL
49
9.882
47.350
23.439
1.00
30.64


ATOM
1624
C
VAL
49
9.500
45.862
23.366
1.00
31.81


ATOM
1625
O
VAL
49
9.173
45.339
22.282
1.00
31.69


ATOM
1626
CB
VAL
49
8.711
48.165
24.139
1.00
30.27


ATOM
1627
CG1
VAL
49
9.066
49.625
24.338
1.00
27.05


ATOM
1628
CG2
VAL
49
7.386
48.097
23.369
1.00
28.65


ATOM
1629
N
TYR
50
9.592
45.187
24.510
1.00
32.49


ATOM
1630
CA
TYR
50
9.011
43.848
24.698
1.00
33.92


ATOM
1631
C
TYR
50
7.472
43.861
24.508
1.00
34.74


ATOM
1632
O
TYR
50
6.795
44.800
24.894
1.00
34.44


ATOM
1633
CB
TYR
50
9.391
43.337
26.100
1.00
34.27


ATOM
1634
CG
TYR
50
8.732
42.066
26.497
1.00
34.16


ATOM
1635
CD1
TYR
50
9.239
40.847
26.086
1.00
34.55


ATOM
1636
CD2
TYR
50
7.621
42.076
27.334
1.00
34.69


ATOM
1637
CE1
TYR
50
8.612
39.644
26.451
1.00
34.91


ATOM
1638
CE2
TYR
50
7.008
40.907
27.724
1.00
34.31


ATOM
1639
CZ
TYR
50
7.497
39.703
27.280
1.00
34.93


ATOM
1640
OH
TYR
50
6.858
38.537
27.670
1.00
37.56


ATOM
1641
N
LEU
51
6.920
42.846
23.856
1.00
36.01


ATOM
1642
CA
LEU
51
5.459
42.792
23.743
1.00
38.06


ATOM
1643
C
LEU
51
4.970
41.474
24.359
1.00
38.71


ATOM
1644
O
LEU
51
5.357
40.387
23.891
1.00
38.72


ATOM
1645
CB
LEU
51
4.966
42.912
22.293
1.00
38.26


ATOM
1646
CG
LEU
51
3.483
43.291
22.071
1.00
39.97


ATOM
1647
CD1
LEU
51
3.196
44.698
22.569
1.00
41.59


ATOM
1648
CD2
LEU
51
3.106
43.214
20.601
1.00
39.18


ATOM
1649
N
PRO
52
4.132
41.569
25.410
1.00
39.27


ATOM
1650
CA
PRO
52
3.607
40.371
26.084
1.00
40.56


ATOM
1651
C
PRO
52
2.762
39.489
25.170
1.00
40.53


ATOM
1652
O
PRO
52
2.094
39.992
24.289
1.00
39.33


ATOM
1653
CB
PRO
52
2.720
40.950
27.209
1.00
40.48


ATOM
1654
CG
PRO
52
3.168
42.385
27.390
1.00
40.75


ATOM
1655
CD
PRO
52
3.626
42.820
26.013
1.00
39.83


ATOM
1656
N
ALA
53
2.808
38.180
25.420
1.00
42.43


ATOM
1657
CA
ALA
53
2.081
37.157
24.663
1.00
44.05


ATOM
1658
C
ALA
53
0.632
37.483
24.238
1.00
46.03


ATOM
1659
O
ALA
53
0.269
37.306
23.079
1.00
45.37


ATOM
1660
CB
ALA
53
2.158
35.809
25.400
1.00
44.31


ATOM
1661
N
GLU
54
−0.201
37.988
25.147
1.00
48.17


ATOM
1662
CA
GLU
54
−1.588
38.264
24.742
1.00
50.27


ATOM
1663
C
GLU
54
−1.866
39.724
24.298
1.00
50.27


ATOM
1664
O
GLU
54
−3.005
40.046
23.975
1.00
50.60


ATOM
1665
CB
GLU
54
−2.627
37.724
25.771
1.00
50.47


ATOM
1666
CG
GLU
54
−2.726
38.522
27.079
1.00
52.14


ATOM
1667
CD
GLU
54
−3.853
38.039
28.041
1.00
52.30


ATOM
1668
OE1
GLU
54
−3.510
37.353
29.047
1.00
53.98


ATOM
1669
OE2
GLU
54
−5.059
38.346
27.795
1.00
52.76


ATOM
1670
N
GLN
55
−0.842
40.587
24.264
1.00
49.80


ATOM
1671
CA
GLN
55
−1.008
41.957
23.723
1.00
49.67


ATOM
1672
C
GLN
55
−0.821
41.999
22.204
1.00
49.52


ATOM
1673
O
GLN
55
0.162
41.460
21.673
1.00
48.68


ATOM
1674
CB
GLN
55
−0.060
42.944
24.415
1.00
49.73


ATOM
1675
CG
GLN
55
−0.274
44.423
24.053
1.00
49.02


ATOM
1676
CD
GLN
55
0.539
45.355
24.963
1.00
50.64


ATOM
1677
OE1
GLN
55
0.798
45.018
26.127
1.00
50.76


ATOM
1678
NE2
GLN
55
0.928
46.548
24.442
1.00
50.99


ATOM
1679
N
LYS
56
−1.761
42.648
21.514
1.00
49.80


ATOM
1680
CA
LYS
56
−1.878
42.501
20.046
1.00
50.35


ATOM
1681
C
LYS
56
−0.832
43.295
19.269
1.00
48.93


ATOM
1682
O
LYS
56
−0.302
42.810
18.259
1.00
48.73


ATOM
1683
CB
LYS
56
−3.292
42.848
19.523
1.00
50.57


ATOM
1684
CG
LYS
56
−3.464
42.585
18.019
1.00
51.80


ATOM
1685
CD
LYS
56
−4.918
42.505
17.578
1.00
53.30


ATOM
1686
CE
LYS
56
−5.380
43.822
16.954
1.00
55.68


ATOM
1687
NZ
LYS
56
−6.597
44.405
17.633
1.00
59.22


ATOM
1688
N
GLY
57
−0.585
44.517
19.747
1.00
47.49


ATOM
1689
CA
GLY
57
0.319
45.462
19.131
1.00
45.82


ATOM
1690
C
GLY
57
0.834
46.492
20.127
1.00
45.53


ATOM
1691
O
GLY
57
0.337
46.616
21.261
1.00
44.75


ATOM
1692
N
THR
58
1.867
47.218
19.715
1.00
44.32


ATOM
1693
CA
THR
58
2.451
48.232
20.551
1.00
43.57


ATOM
1694
C
THR
58
1.880
49.539
20.016
1.00
44.18


ATOM
1695
O
THR
58
0.915
49.514
19.236
1.00
43.92


ATOM
1696
CB
THR
58
4.020
48.180
20.514
1.00
43.34


ATOM
1697
OG1
THR
58
4.567
49.161
21.411
1.00
42.06


ATOM
1698
CG2
THR
58
4.552
48.425
19.087
1.00
41.24


ATOM
1699
N
HIS
59
2.484
50.661
20.416
1.00
44.36


ATOM
1700
CA
HIS
59
1.990
51.988
20.089
1.00
44.59


ATOM
1701
C
HIS
59
3.042
52.738
19.315
1.00
43.83


ATOM
1702
O
HIS
59
3.780
53.535
19.885
1.00
42.81


ATOM
1703
CB
HIS
59
1.636
52.721
21.380
1.00
45.60


ATOM
1704
CG
HIS
59
0.703
51.938
22.252
1.00
48.60


ATOM
1705
ND1
HIS
59
1.144
51.135
23.288
1.00
51.29


ATOM
1706
CD2
HIS
59
−0.637
51.759
22.180
1.00
50.27


ATOM
1707
CE1
HIS
59
0.109
50.533
23.847
1.00
51.31


ATOM
1708
NE2
HIS
59
−0.984
50.899
23.198
1.00
52.01


ATOM
1709
N
MET
60
3.060
52.498
18.003
1.00
43.45


ATOM
1710
CA
MET
60
4.118
52.968
17.111
1.00
43.58


ATOM
1711
C
MET
60
4.408
54.470
17.126
1.00
42.81


ATOM
1712
O
MET
60
5.568
54.862
17.000
1.00
43.78


ATOM
1713
CB
MET
60
3.826
52.517
15.662
1.00
44.75


ATOM
1714
CG
MET
60
3.874
50.996
15.481
1.00
45.80


ATOM
1715
SD
MET
60
5.554
50.390
15.559
1.00
47.38


ATOM
1716
CE
MET
60
5.341
48.695
15.015
1.00
46.89


ATOM
1717
N
SER
61
3.378
55.316
17.240
1.00
41.77


ATOM
1718
CA
SER
61
3.580
56.774
17.190
1.00
40.55


ATOM
1719
C
SER
61
4.316
57.325
18.401
1.00
40.20


ATOM
1720
O
SER
61
4.872
58.440
18.354
1.00
39.73


ATOM
1721
CB
SER
61
2.253
57.505
17.058
1.00
40.87


ATOM
1722
OG
SER
61
1.535
57.469
18.286
1.00
42.74


ATOM
1723
N
ARG
62
4.306
56.572
19.502
1.00
38.76


ATOM
1724
CA
ARG
62
4.907
57.064
20.760
1.00
37.81


ATOM
1725
C
ARG
62
6.430
57.086
20.708
1.00
36.60


ATOM
1726
O
ARG
62
7.053
57.867
21.407
1.00
35.27


ATOM
1727
CB
ARG
62
4.471
56.197
21.946
1.00
38.07


ATOM
1728
CG
ARG
62
2.986
56.087
22.103
1.00
37.78


ATOM
1729
CD
ARG
62
2.650
55.479
23.453
1.00
37.88


ATOM
1730
NE
ARG
62
1.202
55.356
23.598
1.00
37.07


ATOM
1731
CZ
ARG
62
0.569
54.705
24.579
1.00
37.18


ATOM
1732
NH1
ARG
62
1.229
54.097
25.571
1.00
37.21


ATOM
1733
NH2
ARG
62
−0.745
54.685
24.564
1.00
35.43


ATOM
1734
N
PHE
63
7.029
56.198
19.900
1.00
36.09


ATOM
1735
CA
PHE
63
8.464
56.204
19.720
1.00
35.73


ATOM
1736
C
PHE
63
8.893
57.549
19.109
1.00
36.45


ATOM
1737
O
PHE
63
9.793
58.207
19.617
1.00
36.12


ATOM
1738
CB
PHE
63
8.934
55.038
18.850
1.00
35.41


ATOM
1739
CG
PHE
63
8.621
53.693
19.413
1.00
34.78


ATOM
1740
CD1
PHE
63
9.340
53.203
20.503
1.00
32.25


ATOM
1741
CD2
PHE
63
7.598
52.921
18.852
1.00
33.93


ATOM
1742
CE1
PHE
63
9.074
51.933
21.031
1.00
32.28


ATOM
1743
CE2
PHE
63
7.303
51.643
19.376
1.00
34.29


ATOM
1744
CZ
PHE
63
8.050
51.146
20.464
1.00
33.57


ATOM
1745
N
VAL
64
8.236
57.948
18.020
1.00
37.27


ATOM
1746
CA
VAL
64
8.517
59.230
17.375
1.00
37.13


ATOM
1747
C
VAL
64
8.161
60.414
18.267
1.00
38.00


ATOM
1748
O
VAL
64
8.928
61.374
18.346
1.00
38.05


ATOM
1749
CB
VAL
64
7.771
59.348
15.995
1.00
37.68


ATOM
1750
CG1
VAL
64
7.969
60.740
15.348
1.00
35.90


ATOM
1751
CG2
VAL
64
8.246
58.302
15.051
1.00
35.99


ATOM
1752
N
ALA
65
6.995
60.356
18.920
1.00
39.07


ATOM
1753
CA
ALA
65
6.604
61.336
19.959
1.00
39.65


ATOM
1754
C
ALA
65
7.709
61.560
20.985
1.00
39.89


ATOM
1755
O
ALA
65
8.040
62.706
21.288
1.00
40.81


ATOM
1756
CB
ALA
65
5.314
60.893
20.661
1.00
39.83


ATOM
1757
N
LEU
66
8.289
60.476
21.511
1.00
39.65


ATOM
1758
CA
LEU
66
9.366
60.572
22.481
1.00
39.87


ATOM
1759
C
LEU
66
10.574
61.353
21.914
1.00
41.30


ATOM
1760
O
LEU
66
11.115
62.244
22.594
1.00
40.47


ATOM
1761
CB
LEU
66
9.791
59.179
22.920
1.00
40.26


ATOM
1762
CG
LEU
66
10.824
59.054
24.047
1.00
40.85


ATOM
1763
CD1
LEU
66
10.177
59.321
25.386
1.00
40.55


ATOM
1764
CD2
LEU
66
11.503
57.695
24.065
1.00
39.84


ATOM
1765
N
GLU
68
10.766
63.558
19.363
1.00
46.22


ATOM
1766
CA
GLU
68
10.381
64.976
19.114
1.00
48.69


ATOM
1767
C
GLU
68
10.315
65.841
20.391
1.00
50.90


ATOM
1768
O
GLU
68
10.662
67.033
20.349
1.00
51.17


ATOM
1769
CB
GLU
68
9.037
65.069
18.353
1.00
48.22


ATOM
1770
CG
GLU
68
8.992
64.362
16.978
1.00
46.41


ATOM
1771
CD
GLU
68
9.820
65.064
15.886
1.00
47.69


ATOM
1772
OE1
GLU
68
10.263
66.237
16.080
1.00
45.80


ATOM
1773
OE2
GLU
68
10.032
64.419
14.824
1.00
47.66


ATOM
1774
N
GLN
69
9.878
65.225
21.502
1.00
53.44


ATOM
1775
CA
GLN
69
9.737
65.894
22.821
1.00
55.64


ATOM
1776
C
GLN
69
11.066
66.234
23.455
1.00
56.51


ATOM
1777
O
GLN
69
11.205
67.300
24.052
1.00
56.81


ATOM
1778
CB
GLN
69
8.960
65.033
23.819
1.00
56.03


ATOM
1779
CG
GLN
69
7.481
65.390
23.982
1.00
59.13


ATOM
1780
CD
GLN
69
6.553
64.171
23.830
1.00
61.60


ATOM
1781
OE1
GLN
69
6.731
63.130
24.489
1.00
63.56


ATOM
1782
NE2
GLN
69
5.565
64.296
22.941
1.00
62.80


ATOM
1783
N
GLU
85
12.285
56.401
29.960
1.00
35.51


ATOM
1784
CA
GLU
85
11.043
57.106
29.645
1.00
36.75


ATOM
1785
C
GLU
85
10.286
56.367
28.558
1.00
36.10


ATOM
1786
O
GLU
85
9.063
56.381
28.509
1.00
35.56


ATOM
1787
CB
GLU
85
11.345
58.521
29.186
1.00
37.91


ATOM
1788
CG
GLU
85
10.511
59.561
29.872
1.00
45.60


ATOM
1789
CD
GLU
85
10.938
60.971
29.494
1.00
51.33


ATOM
1790
OE1
GLU
85
11.946
61.450
30.082
1.00
56.31


ATOM
1791
OE2
GLU
85
10.262
61.599
28.612
1.00
57.98


ATOM
1792
N
MET
86
11.027
55.701
27.682
1.00
34.68


ATOM
1793
CA
MET
86
10.396
54.953
26.610
1.00
33.27


ATOM
1794
C
MET
86
9.602
53.755
27.109
1.00
32.94


ATOM
1795
O
MET
86
8.444
53.580
26.743
1.00
31.87


ATOM
1796
CB
MET
86
11.438
54.437
25.623
1.00
31.72


ATOM
1797
CG
MET
86
10.773
53.653
24.513
1.00
29.97


ATOM
1798
SD
MET
86
11.938
52.947
23.321
1.00
32.42


ATOM
1799
CE
MET
86
12.806
51.729
24.284
1.00
23.54


ATOM
1800
N
VAL
87
10.244
52.890
27.888
1.00
34.25


ATOM
1801
CA
VAL
87
9.560
51.671
28.364
1.00
35.93


ATOM
1802
C
VAL
87
8.348
52.052
29.271
1.00
36.89


ATOM
1803
O
VAL
87
7.303
51.369
29.273
1.00
36.38


ATOM
1804
CB
VAL
87
10.512
50.648
29.024
1.00
36.17


ATOM
1805
CG1
VAL
87
11.577
50.146
28.033
1.00
36.15


ATOM
1806
CG2
VAL
87
11.181
51.186
30.300
1.00
37.44


ATOM
1807
N
ALA
88
8.500
53.169
29.983
1.00
37.69


ATOM
1808
CA
ALA
88
7.412
53.758
30.793
1.00
39.22


ATOM
1809
C
ALA
88
6.275
54.182
29.879
1.00
39.76


ATOM
1810
O
ALA
88
5.118
53.774
30.063
1.00
40.54


ATOM
1811
CB
ALA
88
7.930
54.975
31.529
1.00
39.27


ATOM
1812
N
LEU
89
6.607
54.998
28.880
1.00
39.88


ATOM
1813
CA
LEU
89
5.615
55.547
27.936
1.00
40.55


ATOM
1814
C
LEU
89
4.903
54.464
27.096
1.00
39.98


ATOM
1815
O
LEU
89
3.701
54.531
26.799
1.00
40.50


ATOM
1816
CB
LEU
89
6.293
56.582
27.020
1.00
40.81


ATOM
1817
CG
LEU
89
5.482
57.249
25.912
1.00
41.42


ATOM
1818
CD1
LEU
89
4.311
58.032
26.507
1.00
43.86


ATOM
1819
CD2
LEU
89
6.373
58.178
25.071
1.00
41.85


ATOM
1820
N
LEU
90
5.634
53.451
26.699
1.00
39.63


ATOM
1821
CA
LEU
90
4.988
52.417
25.934
1.00
39.66


ATOM
1822
C
LEU
90
4.345
51.391
26.854
1.00
39.64


ATOM
1823
O
LEU
90
3.830
50.375
26.394
1.00
40.47


ATOM
1824
CB
LEU
90
5.975
51.790
24.943
1.00
38.91


ATOM
1825
CG
LEU
90
5.850
52.779
23.753
1.00
40.39


ATOM
1826
CD1
LEU
90
7.044
53.680
23.526
1.00
36.51


ATOM
1827
CD2
LEU
90
5.400
52.126
22.503
1.00
38.67


ATOM
1828
N
ASP
91
4.389
51.649
28.159
1.00
40.21


ATOM
1829
CA
ASP
91
3.915
50.674
29.157
1.00
39.95


ATOM
1830
C
ASP
91
4.453
49.246
28.929
1.00
38.80


ATOM
1831
O
ASP
91
3.678
48.282
28.926
1.00
38.19


ATOM
1832
CB
ASP
91
2.355
50.685
29.285
1.00
40.89


ATOM
1833
CG
ASP
91
1.796
51.938
30.023
1.00
43.50


ATOM
1834
OD1
ASP
91
2.494
52.475
30.931
1.00
46.25


ATOM
1835
OD2
ASP
91
0.645
52.381
29.723
1.00
42.88


ATOM
1836
N
SER
92
5.775
49.093
28.785
1.00
38.12


ATOM
1837
CA
SER
92
6.384
47.747
28.609
1.00
37.45


ATOM
1838
C
SER
92
7.380
47.396
29.694
1.00
38.08


ATOM
1839
O
SER
92
7.959
48.304
30.317
1.00
38.79


ATOM
1840
CB
SER
92
7.087
47.633
27.263
1.00
37.32


ATOM
1841
OG
SER
92
7.773
46.388
27.125
1.00
36.68


ATOM
1842
N
ARG
93
7.604
46.097
29.905
1.00
38.34


ATOM
1843
CA
ARG
93
8.632
45.629
30.871
1.00
39.41


ATOM
1844
C
ARG
93
10.085
45.856
30.407
1.00
38.10


ATOM
1845
O
ARG
93
11.001
45.895
31.225
1.00
35.83


ATOM
1846
CB
ARG
93
8.453
44.139
31.247
1.00
41.31


ATOM
1847
CG
ARG
93
8.978
43.121
30.205
1.00
44.67


ATOM
1848
CD
ARG
93
9.790
41.938
30.865
1.00
50.90


ATOM
1849
NE
ARG
93
10.206
40.824
29.954
1.00
51.36


ATOM
1850
CZ
ARG
93
11.437
40.590
29.478
1.00
51.92


ATOM
1851
NH1
ARG
93
12.467
41.370
29.790
1.00
54.64


ATOM
1852
NH2
ARG
93
11.641
39.537
28.689
1.00
53.40


ATOM
1853
N
ALA
94
10.292
45.964
29.082
1.00
36.95


ATOM
1854
CA
ALA
94
11.653
46.011
28.533
1.00
35.38


ATOM
1855
C
ALA
94
11.703
46.705
27.171
1.00
35.03


ATOM
1856
O
ALA
94
10.680
46.841
26.484
1.00
33.23


ATOM
1857
CB
ALA
94
12.245
44.572
28.431
1.00
34.91


TER











ENDMDL











MODEL
2










TER











ATOM
1
N
ARG
14
51.699
63.155
−25.990
1.00
59.94


ATOM
2
CA
ARG
14
50.569
64.101
−25.839
1.00
60.10


ATOM
3
C
ARG
14
49.765
63.744
−24.590
1.00
59.52


ATOM
4
O
ARG
14
49.543
62.552
−24.283
1.00
59.50


ATOM
5
CB
ARG
14
49.727
64.169
−27.117
1.00
60.86


ATOM
6
CG
ARG
14
50.102
65.332
−28.041
1.00
62.47


ATOM
7
CD
ARG
14
51.596
65.658
−28.056
1.00
66.68


ATOM
8
NE
ARG
14
52.030
66.690
−27.094
1.00
66.83


ATOM
9
CZ
ARG
14
52.974
66.531
−26.153
1.00
74.89


ATOM
10
NH1
ARG
14
53.616
65.358
−25.985
1.00
70.24


ATOM
11
NH2
ARG
14
53.281
67.559
−25.359
1.00
70.54


ATOM
12
N
ASN
15
49.332
64.800
−23.892
1.00
58.31


ATOM
13
CA
ASN
15
49.230
64.790
−22.425
1.00
56.79


ATOM
14
C
ASN
15
47.825
64.669
−21.839
1.00
54.53


ATOM
15
O
ASN
15
47.622
63.943
−20.862
1.00
55.84


ATOM
16
CB
ASN
15
49.946
66.021
−21.842
1.00
57.64


ATOM
17
CG
ASN
15
51.363
65.720
−21.380
1.00
58.56


ATOM
18
OD1
ASN
15
51.644
64.656
−20.812
1.00
59.64


ATOM
19
ND2
ASN
15
52.266
66.681
−21.597
1.00
59.50


ATOM
20
N
LEU
16
46.876
65.374
−22.445
1.00
50.71


ATOM
21
CA
LEU
16
45.451
65.266
−22.128
1.00
45.72


ATOM
22
C
LEU
16
45.008
66.059
−20.897
1.00
42.62


ATOM
23
O
LEU
16
45.480
65.849
−19.781
1.00
41.21


ATOM
24
CB
LEU
16
44.990
63.823
−22.066
1.00
46.03


ATOM
25
CG
LEU
16
44.014
63.129
−23.024
1.00
45.53


ATOM
26
CD1
LEU
16
44.094
63.555
−24.479
1.00
46.94


ATOM
27
CD2
LEU
16
44.289
61.658
−22.907
1.00
42.24


ATOM
28
N
PRO
17
44.091
66.999
−21.118
1.00
39.73


ATOM
29
CA
PRO
17
43.589
67.732
−19.976
1.00
37.59


ATOM
30
C
PRO
17
42.594
66.792
−19.285
1.00
35.06


ATOM
31
O
PRO
17
41.991
65.908
−19.928
1.00
34.66


ATOM
32
CB
PRO
17
42.862
68.914
−20.612
1.00
37.49


ATOM
33
CG
PRO
17
42.391
68.361
−21.904
1.00
38.46


ATOM
34
CD
PRO
17
43.431
67.395
−22.375
1.00
39.21


ATOM
35
N
ILE
18
42.450
66.965
−17.988
1.00
32.48


ATOM
36
CA
ILE
18
41.485
66.174
−17.234
1.00
29.75


ATOM
37
C
ILE
18
40.315
67.048
−16.866
1.00
28.71


ATOM
38
O
ILE
18
40.492
68.138
−16.313
1.00
29.46


ATOM
39
CB
ILE
18
42.172
65.505
−16.010
1.00
29.27


ATOM
40
CG1
ILE
18
43.186
64.487
−16.555
1.00
28.75


ATOM
41
CG2
ILE
18
41.139
64.819
−15.144
1.00
26.93


ATOM
42
CD1
ILE
18
44.188
64.021
−15.568
1.00
29.65


ATOM
43
N
ASN
19
39.124
66.588
−17.218
1.00
27.84


ATOM
44
CA
ASN
19
37.917
67.332
−17.011
1.00
28.72


ATOM
45
C
ASN
19
37.791
67.749
−15.535
1.00
29.30


ATOM
46
O
ASN
19
37.556
68.901
−15.230
1.00
29.67


ATOM
47
CB
ASN
19
36.692
66.523
−17.443
1.00
27.56


ATOM
48
CG
ASN
19
36.566
66.383
−18.934
1.00
30.11


ATOM
49
OD1
ASN
19
35.628
66.910
−19.537
1.00
35.03


ATOM
50
ND2
ASN
19
37.457
65.617
−19.541
1.00
26.59


ATOM
51
N
GLY
22
40.265
65.648
−8.214
1.00
25.74


ATOM
52
CA
GLY
22
40.312
66.105
−6.847
1.00
25.43


ATOM
53
C
GLY
22
39.912
65.005
−5.893
1.00
25.13


ATOM
54
O
GLY
22
40.462
63.857
−5.962
1.00
24.40


ATOM
55
N
TYR
50
39.658
71.451
−12.980
1.00
30.77


ATOM
56
CA
TYR
50
40.097
71.065
−14.333
1.00
31.30


ATOM
57
C
TYR
50
41.584
71.055
−14.291
1.00
31.89


ATOM
58
O
TYR
50
42.174
71.917
−13.663
1.00
31.71


ATOM
59
CB
TYR
50
39.619
72.128
−15.301
1.00
32.58


ATOM
60
CG
TYR
50
40.188
72.091
−16.695
1.00
33.26


ATOM
61
CD1
TYR
50
39.629
71.282
−17.651
1.00
32.16


ATOM
62
CD2
TYR
50
41.235
72.942
−17.067
1.00
34.15


ATOM
63
CE1
TYR
50
40.135
71.254
−18.975
1.00
35.06


ATOM
64
CE2
TYR
50
41.748
72.932
−18.387
1.00
34.47


ATOM
65
CZ
TYR
50
41.182
72.084
−19.318
1.00
34.05


ATOM
66
OH
TYR
50
41.636
72.058
−20.629
1.00
36.34


ATOM
67
N
LEU
51
42.199
70.064
−14.925
1.00
32.43


ATOM
68
CA
LEU
51
43.649
69.995
−15.047
1.00
33.24


ATOM
69
C
LEU
51
44.061
70.148
−16.526
1.00
33.57


ATOM
70
O
LEU
51
43.695
69.305
−17.330
1.00
31.07


ATOM
71
CB
LEU
51
44.161
68.642
−14.528
1.00
32.42


ATOM
72
CG
LEU
51
45.656
68.642
−14.277
1.00
33.30


ATOM
73
CD1
LEU
51
46.001
69.646
−13.207
1.00
32.77


ATOM
74
CD2
LEU
51
46.156
67.251
−13.840
1.00
33.73


ATOM
75
N
PRO
52
44.803
71.240
−16.884
1.00
35.48


ATOM
76
CA
PRO
52
45.196
71.393
−18.303
1.00
36.24


ATOM
77
C
PRO
52
46.242
70.341
−18.713
1.00
37.08


ATOM
78
O
PRO
52
46.981
69.804
−17.867
1.00
35.03


ATOM
79
CB
PRO
52
45.803
72.800
−18.378
1.00
36.44


ATOM
80
CG
PRO
52
46.191
73.152
−16.968
1.00
37.84


ATOM
81
CD
PRO
52
45.255
72.361
−16.042
1.00
35.65


ATOM
82
N
ALA
53
46.312
70.068
−20.008
1.00
39.26


ATOM
83
CA
ALA
53
47.259
69.078
−20.509
1.00
41.52


ATOM
84
C
ALA
53
48.632
69.158
−19.902
1.00
43.70


ATOM
85
O
ALA
53
49.213
68.120
−19.542
1.00
44.05


ATOM
86
CB
ALA
53
47.343
69.125
−22.028
1.00
41.87


ATOM
87
N
GLU
54
49.176
70.369
−19.770
1.00
46.18


ATOM
88
CA
GLU
54
50.595
70.473
−19.416
1.00
48.84


ATOM
89
C
GLU
54
50.950
70.231
−17.960
1.00
48.48


ATOM
90
O
GLU
54
52.143
70.110
−17.626
1.00
48.68


ATOM
91
CB
GLU
54
51.290
71.741
−19.988
1.00
49.42


ATOM
92
CG
GLU
54
50.930
73.116
−19.376
1.00
51.16


ATOM
93
CD
GLU
54
51.905
74.263
−19.853
1.00
52.55


ATOM
94
OE1
GLU
54
51.600
75.467
−19.611
1.00
55.01


ATOM
95
OE2
GLU
54
52.984
73.964
−20.462
1.00
56.97


ATOM
96
N
GLN
55
49.943
70.156
−17.098
1.00
47.97


ATOM
97
CA
GLN
55
50.192
70.024
−15.657
1.00
48.24


ATOM
98
C
GLN
55
50.070
68.560
−15.229
1.00
47.26


ATOM
99
O
GLN
55
49.114
67.887
−15.588
1.00
46.59


ATOM
100
CB
GLN
55
49.222
70.920
−14.877
1.00
48.23


ATOM
101
CG
GLN
55
49.460
70.937
−13.359
1.00
49.79


ATOM
102
CD
GLN
55
48.669
72.024
−12.661
1.00
49.97


ATOM
103
OE1
GLN
55
48.367
73.045
−13.266
1.00
53.57


ATOM
104
NE2
GLN
55
48.337
71.819
−11.382
1.00
50.86


ATOM
105
N
LYS
56
51.043
68.068
−14.471
1.00
47.46


ATOM
106
CA
LYS
56
51.091
66.651
−14.130
1.00
48.23


ATOM
107
C
LYS
56
49.978
66.288
−13.149
1.00
47.43


ATOM
108
O
LYS
56
49.311
65.270
−13.323
1.00
47.38


ATOM
109
CB
LYS
56
52.461
66.246
−13.542
1.00
48.49


ATOM
110
CG
LYS
56
52.559
64.719
−13.239
1.00
50.23


ATOM
111
CD
LYS
56
53.838
64.316
−12.483
1.00
51.07


ATOM
112
CE
LYS
56
54.040
65.144
−11.199
1.00
54.39


ATOM
113
NZ
LYS
56
55.448
65.054
−10.676
1.00
56.64


ATOM
114
N
GLY
57
49.801
67.120
−12.124
1.00
46.67


ATOM
115
CA
GLY
57
48.811
66.866
−11.099
1.00
46.24


ATOM
116
C
GLY
57
48.282
68.107
−10.412
1.00
46.03


ATOM
117
O
GLY
57
48.843
69.212
−10.570
1.00
46.27


ATOM
118
N
THR
58
47.195
67.911
−9.654
1.00
45.17


ATOM
119
CA
THR
58
46.597
68.937
−8.810
1.00
43.95


ATOM
120
C
THR
58
47.170
68.864
−7.387
1.00
43.93


ATOM
121
O
THR
58
48.149
68.150
−7.156
1.00
43.84


ATOM
122
CB
THR
58
45.031
68.866
−8.784
1.00
43.76


ATOM
123
OG1
THR
58
44.529
70.079
−8.239
1.00
42.58


ATOM
124
CG2
THR
58
44.481
67.663
−7.957
1.00
41.26


ATOM
125
N
HIS
59
46.542
69.590
−6.456
1.00
42.61


ATOM
126
CA
HIS
59
47.038
69.729
−5.097
1.00
42.55


ATOM
127
C
HIS
59
46.006
69.244
−4.075
1.00
41.58


ATOM
128
O
HIS
59
45.185
70.018
−3.565
1.00
40.93


ATOM
129
CB
HIS
59
47.431
71.174
−4.868
1.00
43.03


ATOM
130
CG
HIS
59
48.369
71.688
−5.915
1.00
46.13


ATOM
131
ND1
HIS
59
47.926
72.295
−7.076
1.00
48.89


ATOM
132
CD2
HIS
59
49.716
71.610
−6.019
1.00
48.32


ATOM
133
CE1
HIS
59
48.966
72.593
−7.840
1.00
48.82


ATOM
134
NE2
HIS
59
50.063
72.187
−7.222
1.00
50.35


ATOM
135
N
MET
60
46.054
67.949
−3.790
1.00
40.23


ATOM
136
CA
MET
60
44.936
67.253
−3.145
1.00
38.85


ATOM
137
C
MET
60
44.631
67.691
−1.718
1.00
37.25


ATOM
138
O
MET
60
43.465
67.703
−1.303
1.00
37.16


ATOM
139
CB
MET
60
45.147
65.734
−3.231
1.00
40.07


ATOM
140
CG
MET
60
45.182
65.202
−4.688
1.00
40.71


ATOM
141
SD
MET
60
43.511
64.820
−5.252
1.00
45.21


ATOM
142
CE
MET
60
43.801
63.999
−6.813
1.00
42.50


ATOM
143
N
SER
61
45.652
68.067
−0.956
1.00
36.21


ATOM
144
CA
SER
61
45.423
68.452
0.429
1.00
35.39


ATOM
145
C
SER
61
44.706
69.789
0.540
1.00
35.50


ATOM
146
O
SER
61
44.116
70.095
1.581
1.00
35.82


ATOM
147
CB
SER
61
46.719
68.519
1.204
1.00
36.22


ATOM
148
OG
SER
61
47.456
69.699
0.911
1.00
36.27


ATOM
149
N
ARG
62
44.724
70.576
−0.533
1.00
34.65


ATOM
150
CA
ARG
62
44.188
71.946
−0.507
1.00
34.67


ATOM
151
C
ARG
62
42.670
71.915
−0.519
1.00
33.66


ATOM
152
O
ARG
62
42.029
72.852
−0.064
1.00
33.93


ATOM
153
CB
ARG
62
44.700
72.765
−1.718
1.00
35.39


ATOM
154
CG
ARG
62
46.213
73.028
−1.757
1.00
35.71


ATOM
155
CD
ARG
62
46.596
73.881
−2.992
1.00
36.59


ATOM
156
NE
ARG
62
48.060
73.991
−3.152
1.00
40.81


ATOM
157
CZ
ARG
62
48.673
74.793
−4.030
1.00
42.85


ATOM
158
NH1
ARG
62
47.947
75.568
−4.833
1.00
42.89


ATOM
159
NH2
ARG
62
50.010
74.829
−4.101
1.00
39.58


ATOM
160
N
PHE
63
42.080
70.851
−1.073
1.00
31.76


ATOM
161
CA
PHE
63
40.621
70.685
−1.039
1.00
29.77


ATOM
162
C
PHE
63
40.169
70.511
0.413
1.00
29.97


ATOM
163
O
PHE
63
39.205
71.121
0.833
1.00
29.60


ATOM
164
CB
PHE
63
40.155
69.450
−1.815
1.00
29.04


ATOM
165
CG
PHE
63
40.440
69.502
−3.280
1.00
24.94


ATOM
166
CD1
PHE
63
39.661
70.280
−4.105
1.00
25.06


ATOM
167
CD2
PHE
63
41.475
68.758
−3.828
1.00
25.62


ATOM
168
CE1
PHE
63
39.904
70.352
−5.464
1.00
25.26


ATOM
169
CE2
PHE
63
41.738
68.810
−5.202
1.00
27.19


ATOM
170
CZ
PHE
63
40.938
69.618
−6.022
1.00
26.37


ATOM
171
N
VAL
64
40.880
69.691
1.178
1.00
29.57


ATOM
172
CA
VAL
64
40.513
69.476
2.578
1.00
29.55


ATOM
173
C
VAL
64
40.837
70.749
3.361
1.00
30.87


ATOM
174
O
VAL
64
40.065
71.110
4.227
1.00
30.92


ATOM
175
CB
VAL
64
41.256
68.306
3.207
1.00
29.58


ATOM
176
CG1
VAL
64
40.690
68.037
4.582
1.00
30.02


ATOM
177
CG2
VAL
64
41.126
67.008
2.311
1.00
27.42


ATOM
178
N
ALA
65
41.967
71.415
3.068
1.00
31.39


ATOM
179
CA
ALA
65
42.338
72.696
3.733
1.00
32.56


ATOM
180
C
ALA
65
41.193
73.717
3.642
1.00
33.22


ATOM
181
O
ALA
65
40.842
74.399
4.620
1.00
33.73


ATOM
182
CB
ALA
65
43.688
73.301
3.097
1.00
32.21


ATOM
183
N
LEU
66
40.610
73.829
2.448
1.00
33.30


ATOM
184
CA
LEU
66
39.528
74.760
2.226
1.00
32.82


ATOM
185
C
LEU
66
38.364
74.505
3.196
1.00
33.60


ATOM
186
O
LEU
66
37.849
75.424
3.856
1.00
32.31


ATOM
187
CB
LEU
66
39.061
74.662
0.775
1.00
31.90


ATOM
188
CG
LEU
66
37.995
75.668
0.377
1.00
32.41


ATOM
189
CD1
LEU
66
38.590
77.115
0.361
1.00
35.12


ATOM
190
CD2
LEU
66
37.421
75.285
−0.955
1.00
31.49


ATOM
191
N
VAL
87
38.796
77.246
−6.771
1.00
36.21


ATOM
192
CA
VAL
87
39.569
77.287
−8.040
1.00
37.84


ATOM
193
C
VAL
87
40.803
78.166
−7.905
1.00
39.36


ATOM
194
O
VAL
87
41.838
77.892
−8.531
1.00
40.24


ATOM
195
CB
VAL
87
38.730
77.746
−9.245
1.00
38.61


ATOM
196
CG1
VAL
87
37.639
76.748
−9.519
1.00
37.63


ATOM
197
CG2
VAL
87
38.122
79.147
−9.011
1.00
37.58


ATOM
198
N
ALA
88
40.699
79.210
−7.071
1.00
39.92


ATOM
199
CA
ALA
88
41.823
80.128
−6.824
1.00
40.37


ATOM
200
C
ALA
88
42.893
79.477
−5.987
1.00
40.95


ATOM
201
O
ALA
88
44.082
79.564
−6.326
1.00
41.91


ATOM
202
CB
ALA
88
41.339
81.398
−6.156
1.00
40.29


ATOM
203
N
LEU
89
42.467
78.793
−4.917
1.00
40.06


ATOM
204
CA
LEU
89
43.380
78.086
−4.017
1.00
40.50


ATOM
205
C
LEU
89
44.174
76.985
−4.745
1.00
39.98


ATOM
206
O
LEU
89
45.363
76.752
−4.462
1.00
38.44


ATOM
207
CB
LEU
89
42.588
77.469
−2.848
1.00
40.68


ATOM
208
CG
LEU
89
43.370
76.638
−1.820
1.00
41.74


ATOM
209
CD1
LEU
89
44.363
77.552
−1.059
1.00
44.04


ATOM
210
CD2
LEU
89
42.426
75.936
−0.818
1.00
40.51


ATOM
211
N
LEU
90
43.494
76.319
−5.678
1.00
40.31


ATOM
212
CA
LEU
90
44.053
75.180
−6.402
1.00
40.41


ATOM
213
C
LEU
90
44.739
75.607
−7.709
1.00
41.69


ATOM
214
O
LEU
90
45.256
74.765
−8.483
1.00
40.27


ATOM
215
CB
LEU
90
42.955
74.186
−6.699
1.00
39.60


ATOM
216
CG
LEU
90
43.070
73.338
−5.455
1.00
38.10


ATOM
217
CD1
LEU
90
41.936
73.564
−4.502
1.00
33.65


ATOM
218
CD2
LEU
90
43.272
71.963
−5.834
1.00
34.46


ATOM
219
N
ASP
91
44.738
76.926
−7.925
1.00
41.99


ATOM
220
CA
ASP
91
45.381
77.552
−9.110
1.00
42.31


ATOM
221
C
ASP
91
44.863
76.971
−10.409
1.00
41.35


ATOM
222
O
ASP
91
45.669
76.497
−11.225
1.00
42.00


ATOM
223
CB
ASP
91
46.900
77.345
−9.073
1.00
42.72


ATOM
224
CG
ASP
91
47.545
77.948
−7.880
1.00
46.18


ATOM
225
OD1
ASP
91
47.169
79.083
−7.503
1.00
52.04


ATOM
226
OD2
ASP
91
48.439
77.296
−7.313
1.00
48.88


ATOM
227
N
SER
92
43.543
76.994
−10.605
1.00
40.27


ATOM
228
CA
SER
92
42.920
76.417
−11.793
1.00
39.39


ATOM
229
C
SER
92
41.864
77.332
−12.372
1.00
40.36


ATOM
230
O
SER
92
41.378
78.237
−11.699
1.00
42.15


ATOM
231
CB
SER
92
42.236
75.078
−11.488
1.00
39.41


ATOM
232
OG
SER
92
41.483
74.625
−12.630
1.00
34.46


ATOM
233
N
ARG
93
41.454
77.042
−13.594
1.00
40.29


ATOM
234
CA
ARG
93
40.521
77.885
−14.309
1.00
42.05


ATOM
235
C
ARG
93
39.068
77.472
−14.088
1.00
40.68


ATOM
236
O
ARG
93
38.152
78.227
−14.428
1.00
41.97


ATOM
237
CB
ARG
93
40.847
77.844
−15.799
1.00
42.19


ATOM
238
CG
ARG
93
39.854
77.034
−16.613
1.00
45.63


ATOM
239
CD
ARG
93
40.382
76.504
−17.978
1.00
46.18


ATOM
240
NE
ARG
93
39.617
75.295
−18.363
1.00
54.20


ATOM
241
CZ
ARG
93
38.309
75.266
−18.680
1.00
54.69


ATOM
242
NH1
ARG
93
37.576
76.384
−18.686
1.00
58.29


ATOM
243
NH2
ARG
93
37.720
74.113
−18.984
1.00
56.33


ATOM
244
N
ARG
105
36.120
36.645
−15.040
1.00
26.77


ATOM
245
CA
ARG
105
37.159
36.313
−15.992
1.00
29.12


ATOM
246
C
ARG
105
38.248
35.521
−15.275
1.00
30.18


ATOM
247
O
ARG
105
38.650
35.872
−14.149
1.00
30.90


ATOM
248
CB
ARG
105
37.726
37.566
−16.629
1.00
28.06


ATOM
249
CG
ARG
105
38.582
37.254
−17.864
1.00
30.28


ATOM
250
CD
ARG
105
39.194
38.513
−18.372
1.00
32.89


ATOM
251
NE
ARG
105
39.735
38.397
−19.720
1.00
34.73


ATOM
252
CZ
ARG
105
40.665
39.201
−20.218
1.00
33.07


ATOM
253
NH1
ARG
105
41.174
40.185
−19.454
1.00
33.32


ATOM
254
NH2
ARG
105
41.061
39.029
−21.482
1.00
31.76


ATOM
255
N
LYS
106
38.708
34.443
−15.909
1.00
31.12


ATOM
256
CA
LYS
106
39.798
33.620
−15.380
1.00
32.80


ATOM
257
C
LYS
106
41.145
34.298
−15.628
1.00
32.96


ATOM
258
O
LYS
106
41.449
34.697
−16.783
1.00
33.18


ATOM
259
CB
LYS
106
39.757
32.229
−16.041
1.00
34.65


ATOM
260
CG
LYS
106
40.696
31.185
−15.401
1.00
39.55


ATOM
261
CD
LYS
106
40.008
30.232
−14.406
1.00
47.35


ATOM
262
CE
LYS
106
38.963
29.324
−15.070
1.00
49.33


ATOM
263
NZ
LYS
106
39.461
28.601
−16.300
1.00
54.56


ATOM
264
N
LYS
107
41.930
34.484
−14.557
1.00
31.08


ATOM
265
CA
LYS
107
43.263
35.059
−14.676
1.00
30.55


ATOM
266
C
LYS
107
44.327
34.034
−14.279
1.00
30.89


ATOM
267
O
LYS
107
44.023
33.035
−13.627
1.00
31.02


ATOM
268
CB
LYS
107
43.437
36.302
−13.789
1.00
30.30


ATOM
269
CG
LYS
107
42.291
37.283
−13.910
1.00
30.97


ATOM
270
CD
LYS
107
42.610
38.648
−13.245
1.00
29.55


ATOM
271
CE
LYS
107
43.721
39.346
−13.925
1.00
27.26


ATOM
272
NZ
LYS
107
43.937
40.678
−13.259
1.00
25.91


ATOM
273
N
THR
108
45.561
34.339
−14.645
1.00
31.14


ATOM
274
CA
THR
108
46.746
33.518
−14.404
1.00
32.51


ATOM
275
C
THR
108
47.714
34.323
−13.548
1.00
32.54


ATOM
276
O
THR
108
48.188
35.392
−13.983
1.00
33.24


ATOM
277
CB
THR
108
47.397
33.254
−15.779
1.00
32.61


ATOM
278
OG1
THR
108
46.422
32.634
−16.589
1.00
35.34


ATOM
279
CG2
THR
108
48.586
32.351
−15.699
1.00
33.31


ATOM
280
N
ALA
109
48.002
33.854
−12.335
1.00
33.07


ATOM
281
CA
ALA
109
49.018
34.514
−11.498
1.00
33.80


ATOM
282
C
ALA
109
50.355
34.702
−12.250
1.00
34.89


ATOM
283
O
ALA
109
50.734
33.856
−13.083
1.00
34.88


ATOM
284
CB
ALA
109
49.209
33.734
−10.195
1.00
34.10


ATOM
285
N
PRO
110
51.057
35.844
−11.991
1.00
35.11


ATOM
286
CA
PRO
110
52.171
36.240
−12.837
1.00
35.19


ATOM
287
C
PRO
110
53.463
35.436
−12.693
1.00
35.83


ATOM
288
O
PRO
110
54.287
35.522
−13.615
1.00
36.44


ATOM
289
CB
PRO
110
52.426
37.698
−12.426
1.00
35.24


ATOM
290
CG
PRO
110
51.888
37.802
−11.047
1.00
35.53


ATOM
291
CD
PRO
110
50.757
36.844
−10.945
1.00
33.91


ATOM
292
N
VAL
111
53.642
34.688
−11.579
1.00
34.87


ATOM
293
CA
VAL
111
54.845
33.859
−11.401
1.00
34.55


ATOM
294
C
VAL
111
54.480
32.371
−11.361
1.00
34.44


ATOM
295
O
VAL
111
54.889
31.613
−12.217
1.00
34.73


ATOM
296
CB
VAL
111
55.721
34.316
−10.201
1.00
35.20


ATOM
297
CG1
VAL
111
56.926
33.367
−10.018
1.00
35.13


ATOM
298
CG2
VAL
111
56.258
35.758
−10.458
1.00
33.36


ATOM
299
N
SER
112
53.644
31.975
−10.411
1.00
34.36


ATOM
300
CA
SER
112
53.171
30.591
−10.301
1.00
33.65


ATOM
301
C
SER
112
52.276
30.124
−11.430
1.00
34.37


ATOM
302
O
SER
112
52.205
28.898
−11.716
1.00
34.40


ATOM
303
CB
SER
112
52.457
30.385
−8.980
1.00
33.85


ATOM
304
OG
SER
112
51.195
31.061
−8.954
1.00
32.93


ATOM
305
N
GLY
113
51.573
31.072
−12.067
1.00
33.94


ATOM
306
CA
GLY
113
50.585
30.736
−13.125
1.00
32.54


ATOM
307
C
GLY
113
49.345
30.023
−12.624
1.00
33.41


ATOM
308
O
GLY
113
48.569
29.470
−13.442
1.00
32.86


ATOM
309
N
ILE
114
49.131
30.036
−11.289
1.00
33.45


ATOM
310
CA
ILE
114
47.931
29.430
−10.697
1.00
34.24


ATOM
311
C
ILE
114
46.768
30.282
−11.217
1.00
34.53


ATOM
312
O
ILE
114
46.890
31.519
−11.331
1.00
33.15


ATOM
313
CB
ILE
114
47.910
29.455
−9.134
1.00
35.17


ATOM
314
CG1
ILE
114
49.151
28.779
−8.519
1.00
38.77


ATOM
315
CG2
ILE
114
46.701
28.738
−8.582
1.00
33.39


ATOM
316
CD1
ILE
114
49.226
27.332
−8.731
1.00
42.74


ATOM
317
N
ARG
115
45.664
29.624
−11.562
1.00
34.61


ATOM
318
CA
ARG
115
44.558
30.341
−12.189
1.00
35.62


ATOM
319
C
ARG
115
43.499
30.661
−11.134
1.00
33.87


ATOM
320
O
ARG
115
43.329
29.908
−10.171
1.00
32.92


ATOM
321
CB
ARG
115
43.976
29.576
−13.399
1.00
35.86


ATOM
322
CG
ARG
115
45.049
29.195
−14.495
1.00
39.50


ATOM
323
CD
ARG
115
44.457
29.202
−15.918
1.00
41.37


ATOM
324
NE
ARG
115
44.156
30.581
−16.349
1.00
49.17


ATOM
325
CZ
ARG
115
43.421
30.934
−17.420
1.00
50.07


ATOM
326
NH1
ARG
115
42.877
30.002
−18.205
1.00
52.25


ATOM
327
NH2
ARG
115
43.228
32.238
−17.705
1.00
50.44


ATOM
328
N
SER
116
42.829
31.808
−11.305
1.00
32.49


ATOM
329
CA
SER
116
41.712
32.164
−10.444
1.00
31.24


ATOM
330
C
SER
116
40.804
33.216
−11.123
1.00
30.84


ATOM
331
O
SER
116
41.201
33.934
−12.080
1.00
31.63


ATOM
332
CB
SER
116
42.218
32.585
−9.021
1.00
31.35


ATOM
333
OG
SER
116
42.970
33.795
−9.062
1.00
29.62


ATOM
334
N
LEU
117
39.573
33.282
−10.665
1.00
29.03


ATOM
335
CA
LEU
117
38.620
34.242
−11.222
1.00
28.26


ATOM
336
C
LEU
117
38.876
35.615
−10.633
1.00
27.66


ATOM
337
O
LEU
117
39.382
35.753
−9.495
1.00
27.40


ATOM
338
CB
LEU
117
37.170
33.830
−10.922
1.00
27.18


ATOM
339
CG
LEU
117
36.731
32.487
−11.525
1.00
27.76


ATOM
340
CD1
LEU
117
35.345
32.155
−11.063
1.00
26.57


ATOM
341
CD2
LEU
117
36.831
32.452
−13.070
1.00
28.10


ATOM
342
N
LEU
118
38.495
36.637
−11.388
1.00
26.69


ATOM
343
CA
LEU
118
38.297
37.963
−10.773
1.00
25.88


ATOM
344
C
LEU
118
36.918
38.468
−11.237
1.00
24.69


ATOM
345
O
LEU
118
36.471
38.091
−12.322
1.00
22.82


ATOM
346
CB
LEU
118
39.392
38.921
−11.221
1.00
26.05


ATOM
347
CG
LEU
118
39.524
40.162
−10.290
1.00
27.63


ATOM
348
CD1
LEU
118
40.096
39.788
−8.861
1.00
29.00


ATOM
349
CD2
LEU
118
40.387
41.128
−10.945
1.00
27.18


ATOM
350
N
PRO
142
38.636
46.847
−10.939
1.00
23.23


ATOM
351
CA
PRO
142
39.398
47.173
−9.753
1.00
23.79


ATOM
352
C
PRO
142
40.866
46.809
−9.963
1.00
24.65


ATOM
353
O
PRO
142
41.162
45.753
−10.563
1.00
25.09


ATOM
354
CB
PRO
142
38.715
46.295
−8.699
1.00
24.09


ATOM
355
CG
PRO
142
38.391
44.964
−9.539
1.00
23.27


ATOM
356
CD
PRO
142
37.978
45.519
−10.870
1.00
23.22


ATOM
357
N
VAL
143
41.771
47.687
−9.512
1.00
24.51


ATOM
358
CA
VAL
143
43.210
47.555
−9.769
1.00
25.26


ATOM
359
C
VAL
143
43.912
48.079
−8.527
1.00
26.54


ATOM
360
O
VAL
143
43.270
48.615
−7.611
1.00
25.34


ATOM
361
CB
VAL
143
43.698
48.366
−11.032
1.00
24.57


ATOM
362
CG1
VAL
143
42.985
47.887
−12.322
1.00
25.48


ATOM
363
CG2
VAL
143
43.463
49.910
−10.826
1.00
23.63


ATOM
364
N
THR
144
45.225
47.878
−8.503
1.00
27.67


ATOM
365
CA
THR
144
46.106
48.449
−7.510
1.00
27.19


ATOM
366
C
THR
144
46.653
49.802
−8.005
1.00
27.74


ATOM
367
O
THR
144
47.110
49.884
−9.150
1.00
27.09


ATOM
368
CB
THR
144
47.302
47.525
−7.281
1.00
27.10


ATOM
369
OG1
THR
144
46.827
46.219
−6.909
1.00
24.38


ATOM
370
CG2
THR
144
48.174
48.091
−6.162
1.00
28.95


ATOM
371
N
SER
145
46.572
50.851
−7.157
1.00
26.89


ATOM
372
CA
SER
145
47.241
52.127
−7.442
1.00
27.89


ATOM
373
C
SER
145
48.318
52.371
−6.381
1.00
28.66


ATOM
374
O
SER
145
48.130
52.002
−5.237
1.00
28.16


ATOM
375
CB
SER
145
46.217
53.288
−7.504
1.00
28.02


ATOM
376
OG
SER
145
45.570
53.460
−6.232
1.00
26.68


ATOM
377
N
LEU
146
49.460
52.952
−6.756
1.00
29.89


ATOM
378
CA
LEU
146
50.545
53.212
−5.789
1.00
29.68


ATOM
379
C
LEU
146
51.070
54.633
−5.993
1.00
30.59


ATOM
380
O
LEU
146
51.229
55.058
−7.132
1.00
28.81


ATOM
381
CB
LEU
146
51.662
52.183
−5.962
1.00
29.41


ATOM
382
CG
LEU
146
52.892
52.265
−5.020
1.00
29.93


ATOM
383
CD1
LEU
146
53.407
50.894
−4.667
1.00
27.71


ATOM
384
CD2
LEU
146
54.018
53.136
−5.659
1.00
28.67


ATOM
385
N
CYS
147
51.337
55.375
−4.903
1.00
31.66


ATOM
386
CA
CYS
147
51.527
56.839
−5.043
1.00
31.98


ATOM
387
C
CYS
147
52.968
57.271
−5.421
1.00
31.99


ATOM
388
O
CYS
147
53.908
57.022
−4.649
1.00
31.52


ATOM
389
CB
CYS
147
51.081
57.556
−3.767
1.00
31.07


ATOM
390
SG
CYS
147
51.160
59.374
−3.962
1.00
34.30


ATOM
391
N
PRO
148
53.160
57.932
−6.599
1.00
32.55


ATOM
392
CA
PRO
148
54.563
58.342
−6.962
1.00
33.44


ATOM
393
C
PRO
148
55.189
59.356
−5.986
1.00
34.23


ATOM
394
O
PRO
148
56.410
59.363
−5.794
1.00
34.47


ATOM
395
CB
PRO
148
54.420
58.991
−8.350
1.00
33.47


ATOM
396
CG
PRO
148
53.058
58.526
−8.878
1.00
33.36


ATOM
397
CD
PRO
148
52.191
58.286
−7.641
1.00
32.15


ATOM
398
N
CYS
149
54.353
60.186
−5.358
1.00
35.48


ATOM
399
CA
CYS
149
54.815
61.208
−4.420
1.00
34.64


ATOM
400
C
CYS
149
55.291
60.533
−3.120
1.00
33.98


ATOM
401
O
CYS
149
56.400
60.836
−2.588
1.00
33.37


ATOM
402
CB
CYS
149
53.683
62.215
−4.164
1.00
34.81


ATOM
403
SG
CYS
149
54.068
63.434
−2.863
1.00
41.23


ATOM
404
N
SER
150
54.474
59.586
−2.636
1.00
32.17


ATOM
405
CA
SER
150
54.840
58.743
−1.498
1.00
31.42


ATOM
406
C
SER
150
56.187
57.998
−1.673
1.00
31.54


ATOM
407
O
SER
150
57.066
58.051
−0.783
1.00
31.16


ATOM
408
CB
SER
150
53.698
57.728
−1.218
1.00
31.09


ATOM
409
OG
SER
150
54.012
56.905
−0.114
1.00
28.82


ATOM
410
N
LYS
151
56.340
57.283
−2.787
1.00
30.89


ATOM
411
CA
LYS
151
57.609
56.647
−3.108
1.00
32.75


ATOM
412
C
LYS
151
58.783
57.685
−3.082
1.00
34.08


ATOM
413
O
LYS
151
59.806
57.498
−2.380
1.00
35.64


ATOM
414
CB
LYS
151
57.521
55.977
−4.506
1.00
31.90


ATOM
415
CG
LYS
151
58.790
55.268
−4.942
1.00
31.20


ATOM
416
CD
LYS
151
58.619
54.627
−6.326
1.00
31.30


ATOM
417
CE
LYS
151
59.952
54.049
−6.776
1.00
33.03


ATOM
418
NZ
LYS
151
59.848
53.308
−8.026
1.00
30.24


ATOM
419
N
GLU
152
58.639
58.749
−3.850
1.00
35.50


ATOM
420
CA
GLU
152
59.707
59.745
−4.032
1.00
38.06


ATOM
421
C
GLU
152
60.216
60.387
−2.718
1.00
38.25


ATOM
422
O
GLU
152
61.426
60.523
−2.526
1.00
39.41


ATOM
423
CB
GLU
152
59.253
60.823
−5.017
1.00
39.11


ATOM
424
CG
GLU
152
60.091
62.096
−4.985
1.00
45.31


ATOM
425
CD
GLU
152
59.694
63.051
−6.069
1.00
52.84


ATOM
426
OE1
GLU
152
58.956
64.019
−5.769
1.00
57.04


ATOM
427
OE2
GLU
152
60.086
62.806
−7.237
1.00
57.07


ATOM
428
N
ILE
153
59.302
60.775
−1.824
1.00
37.49


ATOM
429
CA
ILE
153
59.688
61.492
−0.608
1.00
37.01


ATOM
430
C
ILE
153
60.152
60.522
0.517
1.00
37.61


ATOM
431
O
ILE
153
60.871
60.943
1.429
1.00
37.14


ATOM
432
CB
ILE
153
58.543
62.463
−0.113
1.00
37.48


ATOM
433
CG1
ILE
153
57.332
61.670
0.436
1.00
37.02


ATOM
434
CG2
ILE
153
58.110
63.473
−1.257
1.00
35.87


ATOM
435
CD1
ILE
153
56.064
62.465
0.708
1.00
36.43


ATOM
436
N
SER
154
59.742
59.236
0.451
1.00
36.39


ATOM
437
CA
SER
154
59.982
58.295
1.561
1.00
36.06


ATOM
438
C
SER
154
61.247
57.527
1.398
1.00
36.42


ATOM
439
O
SER
154
61.594
57.143
0.288
1.00
36.52


ATOM
440
CB
SER
154
58.810
57.316
1.733
1.00
34.92


ATOM
441
OG
SER
154
57.623
58.073
1.874
1.00
34.60


ATOM
442
N
GLN
155
61.952
57.274
2.491
1.00
37.31


ATOM
443
CA
GLN
155
63.209
56.510
2.338
1.00
39.20


ATOM
444
C
GLN
155
62.959
55.059
2.004
1.00
38.30


ATOM
445
O
GLN
155
63.840
54.363
1.475
1.00
37.74


ATOM
446
CB
GLN
155
64.129
56.635
3.565
1.00
40.45


ATOM
447
CG
GLN
155
63.556
56.180
4.895
1.00
42.35


ATOM
448
CD
GLN
155
64.560
56.373
6.021
1.00
42.99


ATOM
449
OE1
GLN
155
65.753
56.075
5.856
1.00
45.28


ATOM
450
NE2
GLN
155
64.086
56.879
7.171
1.00
46.69


ATOM
451
N
TYR
156
61.739
54.610
2.305
1.00
37.89


ATOM
452
CA
TYR
156
61.285
53.248
1.997
1.00
36.80


ATOM
453
C
TYR
156
59.761
53.190
2.042
1.00
36.04


ATOM
454
O
TYR
156
59.130
54.076
2.647
1.00
36.63


ATOM
455
CB
TYR
156
61.934
52.218
2.936
1.00
36.72


ATOM
456
CG
TYR
156
62.101
52.631
4.392
1.00
36.70


ATOM
457
CD1
TYR
156
61.034
53.108
5.141
1.00
37.81


ATOM
458
CD2
TYR
156
63.346
52.526
5.026
1.00
38.83


ATOM
459
CE1
TYR
156
61.201
53.472
6.492
1.00
37.24


ATOM
460
CE2
TYR
156
63.520
52.874
6.405
1.00
38.26


ATOM
461
CZ
TYR
156
62.456
53.334
7.110
1.00
37.10


ATOM
462
OH
TYR
156
62.629
53.656
8.447
1.00
37.14


ATOM
463
N
GLY
157
59.159
52.204
1.365
1.00
34.75


ATOM
464
CA
GLY
157
57.687
52.157
1.303
1.00
33.03


ATOM
465
C
GLY
157
57.048
53.125
0.316
1.00
31.76


ATOM
466
O
GLY
157
57.700
54.071
−0.178
1.00
30.74


ATOM
467
N
ALA
158
55.778
52.870
0.010
1.00
30.83


ATOM
468
CA
ALA
158
54.967
53.774
−0.799
1.00
31.12


ATOM
469
C
ALA
158
53.511
53.422
−0.556
1.00
30.73


ATOM
470
O
ALA
158
53.158
52.234
−0.675
1.00
31.76


ATOM
471
CB
ALA
158
55.327
53.625
−2.295
1.00
30.85


ATOM
472
N
HIS
159
52.661
54.390
−0.177
1.00
28.96


ATOM
473
CA
HIS
159
51.271
54.002
0.084
1.00
27.54


ATOM
474
C
HIS
159
50.593
53.588
−1.198
1.00
26.90


ATOM
475
O
HIS
159
50.909
54.116
−2.264
1.00
27.11


ATOM
476
CB
HIS
159
50.445
55.046
0.843
1.00
27.56


ATOM
477
CG
HIS
159
49.942
56.201
0.023
1.00
27.53


ATOM
478
ND1
HIS
159
48.771
56.137
−0.707
1.00
28.80


ATOM
479
CD2
HIS
159
50.386
57.483
−0.080
1.00
25.15


ATOM
480
CE1
HIS
159
48.537
57.311
−1.261
1.00
26.96


ATOM
481
NE2
HIS
159
49.509
58.145
−0.905
1.00
27.80


ATOM
482
N
ASN
160
49.683
52.626
−1.076
1.00
25.77


ATOM
483
CA
ASN
160
49.021
52.005
−2.233
1.00
24.99


ATOM
484
C
ASN
160
47.670
51.560
−1.744
1.00
25.23


ATOM
485
O
ASN
160
47.413
51.549
−0.501
1.00
25.07


ATOM
486
CB
ASN
160
49.886
50.887
−2.882
1.00
24.72


ATOM
487
CG
ASN
160
50.412
49.837
−1.905
1.00
26.68


ATOM
488
OD1
ASN
160
51.537
49.971
−1.397
1.00
31.21


ATOM
489
ND2
ASN
160
49.665
48.741
−1.721
1.00
22.78


ATOM
490
N
GLN
161
46.763
51.287
−2.659
1.00
24.62


ATOM
491
CA
GLN
161
45.373
51.074
−2.282
1.00
25.62


ATOM
492
C
GLN
161
44.660
50.437
−3.461
1.00
25.75


ATOM
493
O
GLN
161
45.160
50.509
−4.567
1.00
25.66


ATOM
494
CB
GLN
161
44.663
52.390
−1.948
1.00
24.86


ATOM
495
CG
GLN
161
44.856
53.512
−3.004
1.00
25.88


ATOM
496
CD
GLN
161
46.155
54.290
−2.795
1.00
26.01


ATOM
497
OE1
GLN
161
46.542
54.608
−1.652
1.00
25.80


ATOM
498
NE2
GLN
161
46.835
54.609
−3.899
1.00
24.43


ATOM
499
N
ARG
162
43.511
49.814
−3.202
1.00
25.37


ATOM
500
CA
ARG
162
42.654
49.399
−4.265
1.00
26.23


ATOM
501
C
ARG
162
42.032
50.654
−4.913
1.00
26.60


ATOM
502
O
ARG
162
41.775
51.671
−4.252
1.00
25.80


ATOM
503
CB
ARG
162
41.556
48.495
−3.741
1.00
26.40


ATOM
504
CG
ARG
162
40.992
47.552
−4.879
1.00
29.11


ATOM
505
CD
ARG
162
39.866
46.616
−4.360
1.00
27.52


ATOM
506
NE
ARG
162
40.374
45.658
−3.381
1.00
26.18


ATOM
507
CZ
ARG
162
39.603
45.119
−2.453
1.00
19.53


ATOM
508
NH1
ARG
162
38.283
45.457
−2.374
1.00
23.76


ATOM
509
NH2
ARG
162
40.179
44.253
−1.612
1.00
23.47


ATOM
510
N
SER
163
41.787
50.544
−6.208
1.00
26.65


ATOM
511
CA
SER
163
41.244
51.627
−6.987
1.00
27.57


ATOM
512
C
SER
163
40.155
51.052
−7.909
1.00
26.82


ATOM
513
O
SER
163
40.152
49.843
−8.235
1.00
26.70


ATOM
514
CB
SER
163
42.423
52.376
−7.657
1.00
27.35


ATOM
515
OG
SER
163
42.151
52.643
−9.023
1.00
35.69


ATOM
516
N
HIS
164
39.122
51.841
−8.156
1.00
24.51


ATOM
517
CA
HIS
164
38.004
51.427
−9.015
1.00
24.40


ATOM
518
C
HIS
164
38.080
52.287
−10.243
1.00
23.64


ATOM
519
O
HIS
164
37.868
53.506
−10.154
1.00
23.83


ATOM
520
CB
HIS
164
36.623
51.581
−8.342
1.00
22.54


ATOM
521
CG
HIS
164
36.351
50.532
−7.265
1.00
26.02


ATOM
522
ND1
HIS
164
35.215
50.544
−6.470
1.00
26.46


ATOM
523
CD2
HIS
164
37.072
49.449
−6.864
1.00
24.91


ATOM
524
CE1
HIS
164
35.273
49.536
−5.602
1.00
27.18


ATOM
525
NE2
HIS
164
36.379
48.844
−5.837
1.00
23.87


ATOM
526
N
GLU
178
36.025
42.070
−22.347
1.00
27.67


ATOM
527
CA
GLU
178
37.377
41.730
−21.959
1.00
27.98


ATOM
528
C
GLU
178
38.387
42.678
−22.559
1.00
27.24


ATOM
529
O
GLU
178
39.453
42.873
−21.988
1.00
25.70


ATOM
530
CB
GLU
178
37.685
40.262
−22.280
1.00
28.97


ATOM
531
CG
GLU
178
37.779
39.941
−23.817
1.00
32.86


ATOM
532
CD
GLU
178
36.465
40.133
−24.630
1.00
33.62


ATOM
533
OE1
GLU
178
35.328
39.936
−24.092
1.00
34.70


ATOM
534
OE2
GLU
178
36.596
40.482
−25.829
1.00
31.93


ATOM
535
N
GLU
179
38.056
43.272
−23.720
1.00
26.74


ATOM
536
CA
GLU
179
38.884
44.273
−24.302
1.00
26.64


ATOM
537
C
GLU
179
39.000
45.480
−23.395
1.00
25.61


ATOM
538
O
GLU
179
40.060
46.034
−23.237
1.00
26.26


ATOM
539
CB
GLU
179
38.303
44.699
−25.661
1.00
27.63


ATOM
540
CG
GLU
179
38.361
43.565
−26.687
1.00
30.31


ATOM
541
CD
GLU
179
38.099
44.069
−28.094
1.00
32.92


ATOM
542
OE1
GLU
179
39.042
44.622
−28.702
1.00
33.44


ATOM
543
OE2
GLU
179
36.964
43.925
−28.543
1.00
32.90


ATOM
544
N
VAL
180
37.883
45.905
−22.809
1.00
25.11


ATOM
545
CA
VAL
180
37.896
47.086
−21.946
1.00
23.45


ATOM
546
C
VAL
180
38.719
46.745
−20.705
1.00
23.67


ATOM
547
O
VAL
180
39.508
47.555
−20.236
1.00
23.44


ATOM
548
CB
VAL
180
36.480
47.466
−21.502
1.00
24.00


ATOM
549
CG1
VAL
180
36.479
48.682
−20.487
1.00
21.69


ATOM
550
CG2
VAL
180
35.579
47.700
−22.690
1.00
21.64


ATOM
551
N
ILE
181
38.506
45.553
−20.151
1.00
22.91


ATOM
552
CA
ILE
181
39.317
45.101
−18.995
1.00
23.75


ATOM
553
C
ILE
181
40.825
45.159
−19.310
1.00
26.04


ATOM
554
O
ILE
181
41.638
45.674
−18.478
1.00
27.11


ATOM
555
CB
ILE
181
38.911
43.630
−18.555
1.00
23.88


ATOM
556
CG1
ILE
181
37.430
43.577
−18.071
1.00
21.17


ATOM
557
CG2
ILE
181
39.925
43.030
−17.477
1.00
21.79


ATOM
558
CD1
ILE
181
36.943
42.131
−17.780
1.00
20.98


ATOM
559
N
ASP
182
41.225
44.643
−20.488
1.00
26.54


ATOM
560
CA
ASP
182
42.657
44.616
−20.814
1.00
26.69


ATOM
561
C
ASP
182
43.199
46.024
−20.957
1.00
25.88


ATOM
562
O
ASP
182
44.296
46.286
−20.514
1.00
26.00


ATOM
563
CB
ASP
182
42.995
43.772
−22.070
1.00
27.60


ATOM
564
CG
ASP
182
42.783
42.263
−21.860
1.00
30.47


ATOM
565
OD1
ASP
182
42.991
41.759
−20.746
1.00
31.48


ATOM
566
OD2
ASP
182
42.373
41.576
−22.814
1.00
33.73


ATOM
567
N
TYR
183
42.452
46.930
−21.589
1.00
26.54


ATOM
568
CA
TYR
183
42.882
48.337
−21.703
1.00
26.51


ATOM
569
C
TYR
183
43.281
48.920
−20.323
1.00
27.37


ATOM
570
O
TYR
183
44.284
49.646
−20.180
1.00
28.29


ATOM
571
CB
TYR
183
41.761
49.172
−22.358
1.00
27.89


ATOM
572
CG
TYR
183
41.688
49.124
−23.877
1.00
27.72


ATOM
573
CD1
TYR
183
42.832
49.062
−24.634
1.00
31.11


ATOM
574
CD2
TYR
183
40.457
49.185
−24.546
1.00
27.18


ATOM
575
CE1
TYR
183
42.777
49.054
−26.075
1.00
32.80


ATOM
576
CE2
TYR
183
40.377
49.157
−25.943
1.00
31.64


ATOM
577
CZ
TYR
183
41.555
49.102
−26.706
1.00
31.01


ATOM
578
OH
TYR
183
41.507
49.115
−28.099
1.00
33.34


ATOM
579
N
VAL
184
42.476
48.626
−19.307
1.00
26.40


ATOM
580
CA
VAL
184
42.668
49.212
−17.997
1.00
24.57


ATOM
581
C
VAL
184
43.796
48.478
−17.240
1.00
25.20


ATOM
582
O
VAL
184
44.694
49.099
−16.708
1.00
25.99


ATOM
583
CB
VAL
184
41.309
49.197
−17.190
1.00
23.34


ATOM
584
CG1
VAL
184
41.538
49.434
−15.671
1.00
24.07


ATOM
585
CG2
VAL
184
40.331
50.295
−17.729
1.00
21.77


ATOM
586
N
GLU
185
43.711
47.159
−17.177
1.00
25.17


ATOM
587
CA
GLU
185
44.647
46.338
−16.391
1.00
25.55


ATOM
588
C
GLU
185
46.078
46.559
−16.857
1.00
27.14


ATOM
589
O
GLU
185
47.019
46.547
−16.027
1.00
26.38


ATOM
590
CB
GLU
185
44.185
44.872
−16.421
1.00
25.17


ATOM
591
CG
GLU
185
42.920
44.621
−15.549
1.00
23.68


ATOM
592
CD
GLU
185
42.609
43.139
−15.318
1.00
26.50


ATOM
593
OE1
GLU
185
42.984
42.320
−16.171
1.00
24.21


ATOM
594
OE2
GLU
185
41.987
42.784
−14.288
1.00
26.85


ATOM
595
N
THR
186
46.230
46.823
−18.172
1.00
27.44


ATOM
596
CA
THR
186
47.548
47.060
−18.780
1.00
29.10


ATOM
597
C
THR
186
48.130
48.338
−18.223
1.00
28.82


ATOM
598
O
THR
186
49.335
48.470
−18.137
1.00
29.57


ATOM
599
CB
THR
186
47.488
47.249
−20.331
1.00
28.74


ATOM
600
OG1
THR
186
46.989
46.059
−20.926
1.00
31.76


ATOM
601
CG2
THR
186
48.900
47.440
−20.950
1.00
31.01


ATOM
602
N
GLN
187
47.266
49.282
−17.880
1.00
27.63


ATOM
603
CA
GLN
187
47.734
50.582
−17.463
1.00
27.72


ATOM
604
C
GLN
187
47.895
50.719
−15.963
1.00
27.83


ATOM
605
O
GLN
187
48.495
51.676
−15.524
1.00
29.63


ATOM
606
CB
GLN
187
46.797
51.676
−17.974
1.00
27.75


ATOM
607
CG
GLN
187
46.783
51.841
−19.519
1.00
26.73


ATOM
608
CD
GLN
187
48.157
52.026
−20.097
1.00
27.76


ATOM
609
OE1
GLN
187
49.015
52.720
−19.533
1.00
30.15


ATOM
610
NE2
GLN
187
48.378
51.441
−21.239
1.00
28.32


ATOM
611
N
ALA
188
47.356
49.795
−15.176
1.00
27.23


ATOM
612
CA
ALA
188
47.369
49.946
−13.725
1.00
27.88


ATOM
613
C
ALA
188
48.791
49.798
−13.135
1.00
28.74


ATOM
614
O
ALA
188
49.614
49.086
−13.715
1.00
28.55


ATOM
615
CB
ALA
188
46.445
48.903
−13.118
1.00
27.58


ATOM
616
N
SER
189
49.102
50.485
−12.010
1.00
28.35


ATOM
617
CA
SER
189
50.358
50.203
−11.299
1.00
28.39


ATOM
618
C
SER
189
50.551
48.679
−11.159
1.00
28.75


ATOM
619
O
SER
189
51.626
48.161
−11.474
1.00
29.75


ATOM
620
CB
SER
189
50.435
50.919
−9.947
1.00
28.00


ATOM
621
OG
SER
189
50.545
52.349
−10.203
1.00
31.33


ATOM
622
N
CYS
190
49.503
47.986
−10.730
1.00
28.89


ATOM
623
CA
CYS
190
49.416
46.536
−10.865
1.00
29.72


ATOM
624
C
CYS
190
47.958
46.096
−10.868
1.00
29.12


ATOM
625
O
CYS
190
47.134
46.656
−10.176
1.00
29.39


ATOM
626
CB
CYS
190
50.183
45.813
−9.738
1.00
29.28


ATOM
627
SG
CYS
190
50.602
44.059
−10.127
1.00
31.60


ATOM
628
N
GLN
191
47.637
45.079
−11.649
1.00
28.56


ATOM
629
CA
GLN
191
46.306
44.513
−11.624
1.00
28.62


ATOM
630
C
GLN
191
46.093
43.539
−10.431
1.00
28.18


ATOM
631
O
GLN
191
47.055
43.115
−9.816
1.00
30.09


ATOM
632
CB
GLN
191
46.007
43.833
−12.982
1.00
27.91


ATOM
633
CG
GLN
191
46.917
42.657
−13.269
1.00
29.69


ATOM
634
CD
GLN
191
46.745
42.128
−14.681
1.00
28.05


ATOM
635
OE1
GLN
191
45.815
41.379
−14.953
1.00
26.08


ATOM
636
NE2
GLN
191
47.663
42.480
−15.563
1.00
27.88


ATOM
637
N
LEU
192
44.838
43.159
−10.165
1.00
27.13


ATOM
638
CA
LEU
192
44.458
42.247
−9.084
1.00
26.58


ATOM
639
C
LEU
192
44.288
40.777
−9.519
1.00
26.86


ATOM
640
O
LEU
192
43.984
40.493
−10.665
1.00
26.33


ATOM
641
CB
LEU
192
43.123
42.692
−8.459
1.00
25.94


ATOM
642
CG
LEU
192
42.975
44.148
−8.007
1.00
25.68


ATOM
643
CD1
LEU
192
41.595
44.361
−7.442
1.00
24.34


ATOM
644
CD2
LEU
192
44.038
44.511
−6.967
1.00
25.68


ATOM
645
N
TYR
193
44.460
39.880
−8.550
1.00
26.29


ATOM
646
CA
TYR
193
44.264
38.410
−8.677
1.00
27.06


ATOM
647
C
TYR
193
43.652
37.912
−7.373
1.00
27.76


ATOM
648
O
TYR
193
43.991
38.458
−6.293
1.00
28.41


ATOM
649
CB
TYR
193
45.624
37.737
−8.820
1.00
26.43


ATOM
650
CG
TYR
193
46.409
38.226
−10.009
1.00
26.85


ATOM
651
CD1
TYR
193
46.305
37.586
−11.260
1.00
26.58


ATOM
652
CD2
TYR
193
47.243
39.344
−9.887
1.00
28.66


ATOM
653
CE1
TYR
193
47.035
38.045
−12.367
1.00
24.85


ATOM
654
CE2
TYR
193
47.967
39.818
−10.959
1.00
26.95


ATOM
655
CZ
TYR
193
47.841
39.172
−12.187
1.00
26.61


ATOM
656
OH
TYR
193
48.580
39.668
−13.189
1.00
26.01


ATOM
657
N
GLY
194
42.805
36.879
−7.430
1.00
27.45


ATOM
658
CA
GLY
194
42.219
36.368
−6.211
1.00
28.39


ATOM
659
C
GLY
194
43.250
35.477
−5.558
1.00
29.37


ATOM
660
O
GLY
194
43.404
35.433
−4.351
1.00
29.71


ATOM
661
N
LEU
195
43.997
34.760
−6.377
1.00
30.72


ATOM
662
CA
LEU
195
44.913
33.749
−5.828
1.00
30.71


ATOM
663
C
LEU
195
46.347
34.064
−6.172
1.00
29.77


ATOM
664
O
LEU
195
46.736
34.103
−7.330
1.00
28.47


ATOM
665
CB
LEU
195
44.495
32.356
−6.282
1.00
30.93


ATOM
666
CG
LEU
195
44.897
31.120
−5.459
1.00
33.19


ATOM
667
CD1
LEU
195
44.301
29.867
−6.174
1.00
33.40


ATOM
668
CD2
LEU
195
46.381
31.012
−5.430
1.00
35.11


ATOM
669
N
LEU
196
47.125
34.301
−5.120
1.00
29.88


ATOM
670
CA
LEU
196
48.509
34.678
−5.234
1.00
31.16


ATOM
671
C
LEU
196
49.300
33.837
−4.255
1.00
32.87


ATOM
672
O
LEU
196
48.981
33.824
−3.049
1.00
31.79


ATOM
673
CB
LEU
196
48.716
36.158
−4.891
1.00
30.65


ATOM
674
CG
LEU
196
48.111
37.202
−5.856
1.00
31.74


ATOM
675
CD1
LEU
196
48.363
38.544
−5.281
1.00
32.71


ATOM
676
CD2
LEU
196
48.735
37.132
−7.252
1.00
32.09


ATOM
677
N
LYS
197
50.312
33.151
−4.790
1.00
33.78


ATOM
678
CA
LYS
197
51.318
32.493
−3.980
1.00
36.74


ATOM
679
C
LYS
197
52.431
33.510
−3.573
1.00
36.95


ATOM
680
O
LYS
197
52.487
34.658
−4.085
1.00
37.20


ATOM
681
CB
LYS
197
51.883
31.254
−4.722
1.00
37.53


ATOM
682
CG
LYS
197
50.885
30.079
−4.822
1.00
39.92


ATOM
683
CD
LYS
197
50.542
29.675
−3.378
1.00
44.49


ATOM
684
CE
LYS
197
49.503
28.600
−3.289
1.00
49.11


ATOM
685
NZ
LYS
197
50.033
27.283
−3.746
1.00
51.33


ATOM
686
N
ARG
198
53.316
33.087
−2.673
1.00
36.70


ATOM
687
CA
ARG
198
54.337
33.976
−2.112
1.00
37.70


ATOM
688
C
ARG
198
55.200
34.587
−3.247
1.00
36.39


ATOM
689
O
ARG
198
55.469
35.791
−3.250
1.00
35.97


ATOM
690
CB
ARG
198
55.148
33.225
−1.021
1.00
37.77


ATOM
691
CG
ARG
198
56.366
33.946
−0.404
1.00
40.32


ATOM
692
CD
ARG
198
57.175
32.979
0.517
1.00
41.88


ATOM
693
NE
ARG
198
58.574
33.393
0.649
1.00
49.67


ATOM
694
CZ
ARG
198
59.170
33.718
1.802
1.00
51.87


ATOM
695
NH1
ARG
198
58.489
33.677
2.947
1.00
53.30


ATOM
696
NH2
ARG
198
60.453
34.087
1.808
1.00
51.58


ATOM
697
N
PRO
199
55.623
33.776
−4.241
1.00
35.71


ATOM
698
CA
PRO
199
56.383
34.445
−5.318
1.00
34.81


ATOM
699
C
PRO
199
55.516
35.443
−6.110
1.00
35.08


ATOM
700
O
PRO
199
56.055
36.446
−6.651
1.00
34.43


ATOM
701
CB
PRO
199
56.823
33.291
−6.208
1.00
34.84


ATOM
702
CG
PRO
199
55.836
32.170
−5.874
1.00
35.30


ATOM
703
CD
PRO
199
55.517
32.321
−4.440
1.00
35.36


ATOM
704
N
ASP
200
54.201
35.173
−6.175
1.00
34.66


ATOM
705
CA
ASP
200
53.252
36.049
−6.906
1.00
35.25


ATOM
706
C
ASP
200
53.062
37.348
−6.146
1.00
35.17


ATOM
707
O
ASP
200
53.055
38.437
−6.722
1.00
35.34


ATOM
708
CB
ASP
200
51.908
35.366
−7.035
1.00
35.09


ATOM
709
CG
ASP
200
51.976
34.109
−7.874
1.00
35.57


ATOM
710
OD1
ASP
200
52.551
34.160
−8.989
1.00
33.86


ATOM
711
OD2
ASP
200
51.410
33.089
−7.420
1.00
35.70


ATOM
712
N
GLU
201
52.943
37.224
−4.831
1.00
35.17


ATOM
713
CA
GLU
201
52.823
38.397
−3.976
1.00
34.49


ATOM
714
C
GLU
201
54.086
39.284
−4.066
1.00
34.61


ATOM
715
O
GLU
201
53.997
40.507
−4.171
1.00
32.47


ATOM
716
CB
GLU
201
52.492
38.022
−2.523
1.00
34.51


ATOM
717
CG
GLU
201
52.407
39.289
−1.648
1.00
34.40


ATOM
718
CD
GLU
201
51.698
39.072
−0.353
1.00
36.89


ATOM
719
OE1
GLU
201
51.475
37.926
0.017
1.00
40.24


ATOM
720
OE2
GLU
201
51.344
40.059
0.298
1.00
36.83


ATOM
721
N
LYS
202
55.260
38.656
−4.042
1.00
34.91


ATOM
722
CA
LYS
202
56.499
39.369
−4.256
1.00
35.18


ATOM
723
C
LYS
202
56.511
40.155
−5.589
1.00
34.53


ATOM
724
O
LYS
202
56.870
41.335
−5.584
1.00
33.52


ATOM
725
CB
LYS
202
57.704
38.404
−4.144
1.00
36.19


ATOM
726
CG
LYS
202
58.953
38.888
−4.837
1.00
36.45


ATOM
727
CD
LYS
202
60.187
37.956
−4.538
1.00
36.73


ATOM
728
CE
LYS
202
61.352
38.334
−5.420
1.00
38.08


ATOM
729
NZ
LYS
202
62.094
39.558
−5.001
1.00
38.27


ATOM
730
N
TYR
203
56.132
39.496
−6.695
1.00
34.14


ATOM
731
CA
TYR
203
56.081
40.077
−8.049
1.00
34.26


ATOM
732
C
TYR
203
55.182
41.362
−8.081
1.00
33.41


ATOM
733
O
TYR
203
55.545
42.408
−8.591
1.00
32.66


ATOM
734
CB
TYR
203
55.507
39.040
−9.034
1.00
34.85


ATOM
735
CG
TYR
203
55.420
39.550
−10.446
1.00
36.49


ATOM
736
CD1
TYR
203
56.444
39.292
−11.371
1.00
37.59


ATOM
737
CD2
TYR
203
54.323
40.333
−10.869
1.00
36.73


ATOM
738
CE1
TYR
203
56.386
39.791
−12.694
1.00
38.56


ATOM
739
CE2
TYR
203
54.267
40.841
−12.195
1.00
38.63


ATOM
740
CZ
TYR
203
55.309
40.546
−13.091
1.00
37.44


ATOM
741
OH
TYR
203
55.280
41.022
−14.372
1.00
40.73


ATOM
742
N
VAL
204
54.002
41.216
−7.518
1.00
32.56


ATOM
743
CA
VAL
204
52.952
42.234
−7.520
1.00
32.86


ATOM
744
C
VAL
204
53.349
43.472
−6.664
1.00
32.32


ATOM
745
O
VAL
204
53.162
44.628
−7.075
1.00
32.22


ATOM
746
CB
VAL
204
51.675
41.454
−7.117
1.00
33.17


ATOM
747
CG1
VAL
204
50.933
41.971
−5.882
1.00
33.70


ATOM
748
CG2
VAL
204
50.855
40.953
−8.375
1.00
31.96


ATOM
749
N
THR
205
53.936
43.214
−5.498
1.00
32.24


ATOM
750
CA
THR
205
54.428
44.259
−4.608
1.00
31.51


ATOM
751
C
THR
205
55.481
45.129
−5.321
1.00
31.55


ATOM
752
O
THR
205
55.359
46.388
−5.363
1.00
30.90


ATOM
753
CB
THR
205
54.970
43.608
−3.295
1.00
31.73


ATOM
754
OG1
THR
205
53.875
42.946
−2.591
1.00
30.86


ATOM
755
CG2
THR
205
55.646
44.659
−2.411
1.00
31.29


ATOM
756
N
GLU
206
56.491
44.454
−5.892
1.00
31.37


ATOM
757
CA
GLU
206
57.593
45.095
−6.652
1.00
32.61


ATOM
758
C
GLU
206
57.142
45.761
−7.949
1.00
32.07


ATOM
759
O
GLU
206
57.573
46.855
−8.226
1.00
31.97


ATOM
760
CB
GLU
206
58.753
44.123
−6.930
1.00
32.31


ATOM
761
CG
GLU
206
59.419
43.619
−5.654
1.00
33.50


ATOM
762
CD
GLU
206
60.435
42.484
−5.897
1.00
34.50


ATOM
763
OE1
GLU
206
60.604
42.040
−7.066
1.00
38.19


ATOM
764
OE2
GLU
206
61.035
42.032
−4.917
1.00
31.10


ATOM
765
N
LYS
207
56.281
45.110
−8.721
1.00
31.90


ATOM
766
CA
LYS
207
55.750
45.712
−9.952
1.00
32.07


ATOM
767
C
LYS
207
55.029
47.049
−9.645
1.00
32.17


ATOM
768
O
LYS
207
55.321
48.081
−10.253
1.00
32.06


ATOM
769
CB
LYS
207
54.804
44.732
−10.670
1.00
32.80


ATOM
770
CG
LYS
207
54.356
45.155
−12.090
1.00
36.71


ATOM
771
CD
LYS
207
55.577
45.529
−12.935
1.00
43.40


ATOM
772
CE
LYS
207
55.461
45.108
−14.453
1.00
46.89


ATOM
773
NZ
LYS
207
56.763
45.323
−15.135
1.00
47.00


ATOM
774
N
ALA
208
54.094
47.030
−8.690
1.00
30.86


ATOM
775
CA
ALA
208
53.376
48.257
−8.340
1.00
30.32


ATOM
776
C
ALA
208
54.366
49.365
−7.984
1.00
30.56


ATOM
777
O
ALA
208
54.272
50.500
−8.483
1.00
29.36


ATOM
778
CB
ALA
208
52.364
48.005
−7.163
1.00
28.98


ATOM
779
N
TYR
209
55.321
49.017
−7.116
1.00
31.34


ATOM
780
CA
TYR
209
56.333
49.945
−6.618
1.00
32.07


ATOM
781
C
TYR
209
57.240
50.482
−7.739
1.00
32.83


ATOM
782
O
TYR
209
57.700
51.637
−7.691
1.00
32.54


ATOM
783
CB
TYR
209
57.154
49.253
−5.554
1.00
32.73


ATOM
784
CG
TYR
209
58.158
50.135
−4.853
1.00
33.75


ATOM
785
CD1
TYR
209
57.787
50.864
−3.703
1.00
34.84


ATOM
786
CD2
TYR
209
59.483
50.223
−5.299
1.00
33.51


ATOM
787
CE1
TYR
209
58.718
51.662
−3.031
1.00
34.86


ATOM
788
CE2
TYR
209
60.438
51.049
−4.623
1.00
34.90


ATOM
789
CZ
TYR
209
60.032
51.759
−3.486
1.00
33.05


ATOM
790
OH
TYR
209
60.932
52.575
−2.791
1.00
35.66


ATOM
791
N
GLU
210
57.463
49.666
−8.762
1.00
34.05


ATOM
792
CA
GLU
210
58.206
50.124
−9.956
1.00
34.62


ATOM
793
C
GLU
210
57.331
50.963
−10.902
1.00
35.41


ATOM
794
O
GLU
210
57.848
51.629
−11.824
1.00
34.97


ATOM
795
CB
GLU
210
58.758
48.924
−10.696
1.00
35.86


ATOM
796
CG
GLU
210
59.770
48.085
−9.883
1.00
36.13


ATOM
797
CD
GLU
210
59.917
46.646
−10.388
1.00
38.52


ATOM
798
OE1
GLU
210
59.209
46.222
−11.326
1.00
38.33


ATOM
799
OE2
GLU
210
60.761
45.923
−9.805
1.00
40.89


ATOM
800
N
ASN
211
56.010
50.925
−10.701
1.00
34.65


ATOM
801
CA
ASN
211
55.071
51.615
−11.625
1.00
35.17


ATOM
802
C
ASN
211
54.033
52.471
−10.929
1.00
33.23


ATOM
803
O
ASN
211
52.844
52.319
−11.179
1.00
34.24


ATOM
804
CB
ASN
211
54.387
50.656
−12.597
1.00
35.24


ATOM
805
CG
ASN
211
55.388
49.871
−13.414
1.00
38.14


ATOM
806
OD1
ASN
211
55.927
48.833
−12.954
1.00
41.46


ATOM
807
ND2
ASN
211
55.681
50.367
−14.617
1.00
36.20


ATOM
808
N
PRO
212
54.503
53.427
−10.110
1.00
32.10


ATOM
809
CA
PRO
212
53.583
54.274
−9.385
1.00
31.76


ATOM
810
C
PRO
212
52.823
55.163
−10.356
1.00
31.38


ATOM
811
O
PRO
212
53.380
55.633
−11.353
1.00
30.16


ATOM
812
CB
PRO
212
54.490
55.103
−8.486
1.00
30.78


ATOM
813
CG
PRO
212
55.845
55.134
−9.224
1.00
31.04


ATOM
814
CD
PRO
212
55.922
53.801
−9.893
1.00
31.09


ATOM
815
N
LYS
213
51.562
55.406
−10.036
1.00
30.99


ATOM
816
CA
LYS
213
50.761
56.346
−10.818
1.00
31.42


ATOM
817
C
LYS
213
49.766
57.072
−9.955
1.00
31.15


ATOM
818
O
LYS
213
49.074
56.467
−9.116
1.00
31.01


ATOM
819
CB
LYS
213
49.986
55.603
−11.911
1.00
30.59


ATOM
820
CG
LYS
213
50.911
55.017
−12.959
1.00
29.40


ATOM
821
CD
LYS
213
50.177
54.712
−14.282
1.00
27.87


ATOM
822
CE
LYS
213
51.127
54.020
−15.275
1.00
29.06


ATOM
823
NZ
LYS
213
50.269
53.473
−16.416
1.00
29.60


ATOM
824
N
PHE
214
49.736
58.380
−10.165
1.00
31.08


ATOM
825
CA
PHE
214
48.631
59.232
−9.699
1.00
31.02


ATOM
826
C
PHE
214
47.336
58.851
−10.398
1.00
29.28


ATOM
827
O
PHE
214
47.336
58.200
−11.486
1.00
28.86


ATOM
828
CB
PHE
214
48.962
60.715
−10.011
1.00
31.33


ATOM
829
CG
PHE
214
50.110
61.273
−9.193
1.00
33.17


ATOM
830
CD1
PHE
214
50.029
61.331
−7.785
1.00
34.17


ATOM
831
CD2
PHE
214
51.254
61.777
−9.826
1.00
31.80


ATOM
832
CE1
PHE
214
51.118
61.848
−7.014
1.00
36.33


ATOM
833
CE2
PHE
214
52.323
62.291
−9.087
1.00
32.91


ATOM
834
CZ
PHE
214
52.258
62.343
−7.665
1.00
33.95


ATOM
835
N
VAL
215
46.226
59.269
−9.796
1.00
27.85


ATOM
836
CA
VAL
215
44.911
59.108
−10.377
1.00
28.62


ATOM
837
C
VAL
215
44.878
59.813
−11.762
1.00
28.57


ATOM
838
O
VAL
215
44.295
59.280
−12.682
1.00
27.90


ATOM
839
CB
VAL
215
43.749
59.519
−9.352
1.00
28.94


ATOM
840
CG1
VAL
215
43.721
61.018
−9.060
1.00
29.40


ATOM
841
CG2
VAL
215
42.428
59.073
−9.813
1.00
29.76


ATOM
842
N
GLU
216
45.546
60.970
−11.872
1.00
28.34


ATOM
843
CA
GLU
216
45.735
61.768
−13.131
1.00
29.82


ATOM
844
C
GLU
216
46.364
60.930
−14.235
1.00
28.79


ATOM
845
O
GLU
216
45.822
60.801
−15.311
1.00
28.87


ATOM
846
CB
GLU
216
46.608
63.020
−12.835
1.00
28.86


ATOM
847
CG
GLU
216
45.872
64.035
−11.934
1.00
32.94


ATOM
848
CD
GLU
216
46.306
63.994
−10.455
1.00
34.70


ATOM
849
OE1
GLU
216
46.537
62.903
−9.914
1.00
35.44


ATOM
850
OE2
GLU
216
46.400
65.073
−9.820
1.00
37.76


ATOM
851
N
ASP
217
47.483
60.303
−13.892
1.00
29.08


ATOM
852
CA
ASP
217
48.235
59.389
−14.751
1.00
28.86


ATOM
853
C
ASP
217
47.386
58.235
−15.203
1.00
28.38


ATOM
854
O
ASP
217
47.338
57.916
−16.408
1.00
27.02


ATOM
855
CB
ASP
217
49.437
58.850
−14.000
1.00
29.76


ATOM
856
CG
ASP
217
50.398
59.919
−13.603
1.00
31.99


ATOM
857
OD1
ASP
217
50.489
60.928
−14.298
1.00
38.26


ATOM
858
OD2
ASP
217
51.084
59.766
−12.591
1.00
34.15


ATOM
859
N
MET
218
46.696
57.589
−14.261
1.00
28.36


ATOM
860
CA
MET
218
45.812
56.492
−14.647
1.00
29.64


ATOM
861
C
MET
218
44.706
56.862
−15.656
1.00
28.41


ATOM
862
O
MET
218
44.492
56.145
−16.636
1.00
26.63


ATOM
863
CB
MET
218
45.176
55.791
−13.422
1.00
30.96


ATOM
864
CG
MET
218
44.319
54.575
−13.861
1.00
35.70


ATOM
865
SD
MET
218
45.273
53.140
−14.514
1.00
45.47


ATOM
866
CE
MET
218
46.456
53.050
−13.190
1.00
46.95


ATOM
867
N
VAL
219
43.962
57.941
−15.405
1.00
28.22


ATOM
868
CA
VAL
219
42.869
58.262
−16.337
1.00
28.10


ATOM
869
C
VAL
219
43.427
58.690
−17.690
1.00
27.11


ATOM
870
O
VAL
219
42.857
58.342
−18.725
1.00
27.29


ATOM
871
CB
VAL
219
41.773
59.259
−15.749
1.00
28.69


ATOM
872
CG1
VAL
219
41.164
58.645
−14.457
1.00
29.54


ATOM
873
CG2
VAL
219
42.347
60.643
−15.445
1.00
27.60


ATOM
874
N
ARG
220
44.529
59.424
−17.692
1.00
27.25


ATOM
875
CA
ARG
220
45.171
59.840
−18.986
1.00
29.06


ATOM
876
C
ARG
220
45.667
58.643
−19.743
1.00
28.85


ATOM
877
O
ARG
220
45.464
58.585
−20.955
1.00
30.55


ATOM
878
CB
ARG
220
46.331
60.821
−18.797
1.00
27.73


ATOM
879
CG
ARG
220
45.901
62.272
−18.483
1.00
29.78


ATOM
880
CD
ARG
220
47.100
63.094
−17.937
1.00
29.72


ATOM
881
NE
ARG
220
46.730
64.494
−18.068
1.00
33.92


ATOM
882
CZ
ARG
220
47.200
65.477
−17.324
1.00
32.61


ATOM
883
NH1
ARG
220
48.094
65.214
−16.410
1.00
33.13


ATOM
884
NH2
ARG
220
46.761
66.725
−17.514
1.00
34.32


ATOM
885
N
ASP
221
46.313
57.712
−19.036
1.00
28.07


ATOM
886
CA
ASP
221
46.889
56.471
−19.662
1.00
28.23


ATOM
887
C
ASP
221
45.801
55.599
−20.281
1.00
27.79


ATOM
888
O
ASP
221
45.901
55.153
−21.453
1.00
28.28


ATOM
889
CB
ASP
221
47.746
55.697
−18.645
1.00
27.76


ATOM
890
CG
ASP
221
49.112
56.318
−18.449
1.00
29.80


ATOM
891
OD1
ASP
221
49.405
57.309
−19.147
1.00
30.61


ATOM
892
OD2
ASP
221
49.902
55.850
−17.583
1.00
32.40


ATOM
893
N
VAL
222
44.730
55.358
−19.532
1.00
25.93


ATOM
894
CA
VAL
222
43.588
54.659
−20.109
1.00
25.63


ATOM
895
C
VAL
222
42.893
55.417
−21.279
1.00
26.39


ATOM
896
O
VAL
222
42.539
54.788
−22.285
1.00
26.70


ATOM
897
CB
VAL
222
42.517
54.272
−19.058
1.00
24.90


ATOM
898
CG1
VAL
222
41.313
53.621
−19.773
1.00
25.51


ATOM
899
CG2
VAL
222
43.098
53.309
−18.028
1.00
24.07


ATOM
900
N
ALA
223
42.664
56.732
−21.126
1.00
25.77


ATOM
901
CA
ALA
223
41.954
57.535
−22.148
1.00
26.96


ATOM
902
C
ALA
223
42.728
57.519
−23.503
1.00
27.41


ATOM
903
O
ALA
223
42.141
57.449
−24.555
1.00
27.99


ATOM
904
CB
ALA
223
41.761
58.976
−21.674
1.00
24.19


ATOM
905
N
THR
224
44.042
57.579
−23.440
1.00
29.50


ATOM
906
CA
THR
224
44.885
57.497
−24.635
1.00
30.83


ATOM
907
C
THR
224
44.640
56.163
−25.358
1.00
31.18


ATOM
908
O
THR
224
44.426
56.153
−26.568
1.00
31.47


ATOM
909
CB
THR
224
46.353
57.671
−24.266
1.00
31.10


ATOM
910
OG1
THR
224
46.515
58.940
−23.611
1.00
32.84


ATOM
911
CG2
THR
224
47.176
57.728
−25.503
1.00
32.78


ATOM
912
N
SER
225
44.589
55.061
−24.612
1.00
31.19


ATOM
913
CA
SER
225
44.306
53.722
−25.208
1.00
32.14


ATOM
914
C
SER
225
42.957
53.650
−25.930
1.00
31.64


ATOM
915
O
SER
225
42.830
53.046
−26.990
1.00
32.34


ATOM
916
CB
SER
225
44.323
52.656
−24.141
1.00
32.10


ATOM
917
OG
SER
225
45.639
52.349
−23.727
1.00
33.71


ATOM
918
N
LEU
226
41.937
54.263
−25.346
1.00
31.46


ATOM
919
CA
LEU
226
40.571
54.266
−25.908
1.00
31.10


ATOM
920
C
LEU
226
40.437
55.192
−27.121
1.00
31.71


ATOM
921
O
LEU
226
39.721
54.868
−28.084
1.00
31.22


ATOM
922
CB
LEU
226
39.570
54.742
−24.815
1.00
30.41


ATOM
923
CG
LEU
226
39.527
53.888
−23.517
1.00
28.65


ATOM
924
CD1
LEU
226
38.528
54.473
−22.550
1.00
26.39


ATOM
925
CD2
LEU
226
39.099
52.494
−23.861
1.00
26.47


ATOM
926
N
ILE
227
41.083
56.357
−27.053
1.00
32.52


ATOM
927
CA
ILE
227
41.131
57.262
−28.223
1.00
34.66


ATOM
928
C
ILE
227
41.711
56.576
−29.449
1.00
34.68


ATOM
929
O
ILE
227
41.198
56.725
−30.533
1.00
36.02


ATOM
930
CB
ILE
227
41.928
58.555
−27.959
1.00
35.04


ATOM
931
CG1
ILE
227
41.168
59.408
−26.956
1.00
34.54


ATOM
932
CG2
ILE
227
42.124
59.326
−29.307
1.00
35.53


ATOM
933
CD1
ILE
227
42.062
60.418
−26.261
1.00
35.14


ATOM
934
N
ALA
228
42.764
55.808
−29.247
1.00
35.83


ATOM
935
CA
ALA
228
43.345
54.957
−30.266
1.00
36.33


ATOM
936
C
ALA
228
42.442
53.813
−30.810
1.00
36.87


ATOM
937
O
ALA
228
42.849
53.109
−31.733
1.00
36.87


ATOM
938
CB
ALA
228
44.625
54.367
−29.715
1.00
35.72


ATOM
939
N
ASP
229
41.284
53.556
−30.200
1.00
36.77


ATOM
940
CA
ASP
229
40.461
52.454
−30.644
1.00
37.00


ATOM
941
C
ASP
229
39.408
53.150
−31.459
1.00
38.22


ATOM
942
O
ASP
229
38.582
53.892
−30.903
1.00
37.95


ATOM
943
CB
ASP
229
39.842
51.696
−29.446
1.00
36.82


ATOM
944
CG
ASP
229
39.075
50.427
−29.856
1.00
35.61


ATOM
945
OD1
ASP
229
38.303
50.430
−30.845
1.00
32.28


ATOM
946
OD2
ASP
229
39.234
49.400
−29.166
1.00
36.47


ATOM
947
N
LYS
230
39.439
52.952
−32.785
1.00
39.74


ATOM
948
CA
LYS
230
38.611
53.794
−33.663
1.00
40.81


ATOM
949
C
LYS
230
37.141
53.311
−33.702
1.00
40.52


ATOM
950
O
LYS
230
36.284
54.023
−34.227
1.00
41.73


ATOM
951
CB
LYS
230
39.210
53.987
−35.107
1.00
41.71


ATOM
952
CG
LYS
230
40.744
54.405
−35.297
1.00
43.63


ATOM
953
CD
LYS
230
41.364
55.367
−34.210
1.00
44.04


ATOM
954
CE
LYS
230
42.910
55.731
−34.504
1.00
40.84


ATOM
955
NZ
LYS
230
44.069
54.838
−33.927
1.00
29.08


ATOM
956
N
GLU
240
38.629
56.109
−9.090
1.00
26.04


ATOM
957
CA
GLU
240
38.563
56.440
−7.677
1.00
25.79


ATOM
958
C
GLU
240
39.604
55.580
−6.918
1.00
26.33


ATOM
959
O
GLU
240
39.581
54.323
−7.008
1.00
26.15


ATOM
960
CB
GLU
240
37.133
56.189
−7.133
1.00
25.72


ATOM
961
CG
GLU
240
36.967
56.616
−5.663
1.00
25.21


ATOM
962
CD
GLU
240
35.532
56.595
−5.146
1.00
26.43


ATOM
963
OE1
GLU
240
34.604
56.243
−5.902
1.00
27.62


ATOM
964
OE2
GLU
240
35.322
56.973
−3.967
1.00
26.61


ATOM
965
N
ASN
241
40.534
56.239
−6.207
1.00
26.14


ATOM
966
CA
ASN
241
41.553
55.525
−5.458
1.00
25.32


ATOM
967
C
ASN
241
41.235
55.691
−3.974
1.00
25.25


ATOM
968
O
ASN
241
41.123
56.826
−3.494
1.00
23.38


ATOM
969
CB
ASN
241
42.918
56.080
−5.756
1.00
26.66


ATOM
970
CG
ASN
241
43.291
55.967
−7.253
1.00
29.90


ATOM
971
OD1
ASN
241
44.408
56.313
−7.640
1.00
36.12


ATOM
972
ND2
ASN
241
42.386
55.453
−8.072
1.00
27.28


ATOM
973
N
PHE
242
41.063
54.564
−3.277
1.00
23.13


ATOM
974
CA
PHE
242
40.624
54.548
−1.896
1.00
24.91


ATOM
975
C
PHE
242
41.842
54.769
−1.023
1.00
25.54


ATOM
976
O
PHE
242
42.315
53.851
−0.388
1.00
25.14


ATOM
977
CB
PHE
242
39.830
53.259
−1.586
1.00
24.91


ATOM
978
CG
PHE
242
38.557
53.179
−2.379
1.00
25.60


ATOM
979
CD1
PHE
242
37.410
53.824
−1.922
1.00
26.78


ATOM
980
CD2
PHE
242
38.544
52.570
−3.650
1.00
25.71


ATOM
981
CE1
PHE
242
36.201
53.800
−2.691
1.00
29.47


ATOM
982
CE2
PHE
242
37.364
52.585
−4.469
1.00
24.56


ATOM
983
CZ
PHE
242
36.193
53.174
−3.984
1.00
26.86


ATOM
984
N
GLU
243
42.356
56.005
−1.066
1.00
25.28


ATOM
985
CA
GLU
243
43.638
56.383
−0.503
1.00
27.20


ATOM
986
C
GLU
243
43.891
55.714
0.844
1.00
26.88


ATOM
987
O
GLU
243
43.133
55.939
1.776
1.00
27.26


ATOM
988
CB
GLU
243
43.754
57.907
−0.342
1.00
28.44


ATOM
989
CG
GLU
243
43.600
58.669
−1.660
1.00
30.04


ATOM
990
CD
GLU
243
44.744
58.326
−2.585
1.00
32.00


ATOM
991
OE1
GLU
243
44.617
57.383
−3.389
1.00
30.26


ATOM
992
OE2
GLU
243
45.815
58.944
−2.446
1.00
35.21


ATOM
993
N
SER
244
44.962
54.926
0.945
1.00
27.02


ATOM
994
CA
SER
244
45.160
54.124
2.185
1.00
27.90


ATOM
995
C
SER
244
45.582
54.978
3.363
1.00
28.54


ATOM
996
O
SER
244
45.551
54.508
4.525
1.00
29.90


ATOM
997
CB
SER
244
46.139
52.988
1.959
1.00
26.85


ATOM
998
OG
SER
244
47.413
53.524
1.761
1.00
25.99


ATOM
999
N
ILE
245
45.936
56.242
3.097
1.00
28.99


ATOM
1000
CA
ILE
245
46.325
57.173
4.192
1.00
28.75


ATOM
1001
C
ILE
245
45.263
58.213
4.615
1.00
28.22


ATOM
1002
O
ILE
245
45.454
58.973
5.589
1.00
28.72


ATOM
1003
CB
ILE
245
47.619
57.930
3.832
1.00
28.52


ATOM
1004
CG1
ILE
245
47.395
58.849
2.619
1.00
27.33


ATOM
1005
CG2
ILE
245
48.795
56.924
3.645
1.00
26.82


ATOM
1006
CD1
ILE
245
48.584
59.899
2.445
1.00
28.82


ATOM
1007
N
HIS
246
44.184
58.275
3.849
1.00
27.14


ATOM
1008
CA
HIS
246
43.062
59.140
4.132
1.00
26.06


ATOM
1009
C
HIS
246
41.827
58.311
4.349
1.00
26.53


ATOM
1010
O
HIS
246
41.870
57.070
4.164
1.00
25.05


ATOM
1011
CB
HIS
246
42.806
60.041
2.962
1.00
26.37


ATOM
1012
CG
HIS
246
43.931
60.957
2.686
1.00
27.22


ATOM
1013
ND1
HIS
246
44.492
61.076
1.432
1.00
29.18


ATOM
1014
CD2
HIS
246
44.608
61.803
3.496
1.00
26.14


ATOM
1015
CE1
HIS
246
45.470
61.961
1.482
1.00
27.29


ATOM
1016
NE2
HIS
246
45.572
62.409
2.722
1.00
28.61


ATOM
1017
N
ASN
247
40.747
58.982
4.800
1.00
25.55


ATOM
1018
CA
ASN
247
39.419
58.329
4.806
1.00
25.30


ATOM
1019
C
ASN
247
38.497
58.880
3.718
1.00
25.63


ATOM
1020
O
ASN
247
37.262
58.817
3.835
1.00
24.99


ATOM
1021
CB
ASN
247
38.719
58.368
6.211
1.00
24.56


ATOM
1022
CG
ASN
247
37.661
57.281
6.348
1.00
25.15


ATOM
1023
OD1
ASN
247
37.853
56.171
5.856
1.00
27.25


ATOM
1024
ND2
ASN
247
36.531
57.594
6.973
1.00
25.75


ATOM
1025
N
SER
249
38.626
59.597
−0.930
1.00
24.78


ATOM
1026
CA
SER
249
39.213
59.045
−2.180
1.00
24.32


ATOM
1027
C
SER
249
39.808
60.130
−3.013
1.00
24.05


ATOM
1028
O
SER
249
39.310
61.225
−2.945
1.00
25.10


ATOM
1029
CB
SER
249
38.100
58.361
−2.967
1.00
23.81


ATOM
1030
OG
SER
249
37.687
57.149
−2.322
1.00
24.81


ATOM
1031
N
ALA
250
40.875
59.846
−3.763
1.00
24.15


ATOM
1032
CA
ALA
250
41.299
60.666
−4.900
1.00
24.78


ATOM
1033
C
ALA
250
40.460
60.222
−6.086
1.00
25.30


ATOM
1034
O
ALA
250
40.141
59.036
−6.212
1.00
25.56


ATOM
1035
CB
ALA
250
42.799
60.442
−5.181
1.00
25.32


ATOM
1036
N
TYR
251
40.095
61.159
−6.971
1.00
24.61


ATOM
1037
CA
TYR
251
39.171
60.879
−8.041
1.00
24.59


ATOM
1038
C
TYR
251
39.481
61.721
−9.294
1.00
25.35


ATOM
1039
O
TYR
251
39.807
62.903
−9.169
1.00
25.44


ATOM
1040
CB
TYR
251
37.739
61.192
−7.534
1.00
25.31


ATOM
1041
CG
TYR
251
36.650
61.072
−8.575
1.00
24.55


ATOM
1042
CD1
TYR
251
36.232
59.831
−9.035
1.00
23.76


ATOM
1043
CD2
TYR
251
36.033
62.228
−9.120
1.00
27.05


ATOM
1044
CE1
TYR
251
35.218
59.714
−10.015
1.00
23.94


ATOM
1045
CE2
TYR
251
35.009
62.121
−10.113
1.00
26.38


ATOM
1046
CZ
TYR
251
34.626
60.872
−10.547
1.00
25.70


ATOM
1047
OH
TYR
251
33.644
60.763
−11.508
1.00
30.46


ATOM
1048
MN
MN2
258
50.065
59.976
−1.837
1.00
31.39


ATOM
1049
N1
AZI
261
48.108
61.800
−2.111
0.50
29.51


ATOM
1050
N2
AZI
261
47.484
62.346
−1.282
0.50
23.78


ATOM
1051
N3
AZI
261
47.000
62.868
−0.349
0.50
33.34


ATOM
1052
N
ARG
14
51.699
37.265
25.990
1.00
59.94


ATOM
1053
CA
ARG
14
50.569
36.319
25.839
1.00
60.10


ATOM
1054
C
ARG
14
49.765
36.676
24.590
1.00
59.52


ATOM
1055
O
ARG
14
49.543
37.868
24.283
1.00
59.50


ATOM
1056
CB
ARG
14
49.727
36.251
27.117
1.00
60.86


ATOM
1057
CG
ARG
14
50.102
35.088
28.041
1.00
62.47


ATOM
1058
CD
ARG
14
51.596
34.762
28.056
1.00
66.68


ATOM
1059
NE
ARG
14
52.030
33.730
27.094
1.00
66.83


ATOM
1060
CZ
ARG
14
52.974
33.889
26.153
1.00
74.89


ATOM
1061
NH1
ARG
14
53.616
35.062
25.985
1.00
70.24


ATOM
1062
NH2
ARG
14
53.281
32.861
25.359
1.00
70.54


ATOM
1063
N
ASN
15
49.332
35.620
23.892
1.00
58.31


ATOM
1064
CA
ASN
15
49.230
35.630
22.425
1.00
56.79


ATOM
1065
C
ASN
15
47.825
35.751
21.839
1.00
54.53


ATOM
1066
O
ASN
15
47.622
36.477
20.862
1.00
55.84


ATOM
1067
CB
ASN
15
49.946
34.399
21.842
1.00
57.64


ATOM
1068
CG
ASN
15
51.363
34.700
21.380
1.00
58.56


ATOM
1069
OD1
ASN
15
51.644
35.764
20.812
1.00
59.64


ATOM
1070
ND2
ASN
15
52.266
33.739
21.597
1.00
59.50


ATOM
1071
N
LEU
16
46.876
35.046
22.445
1.00
50.71


ATOM
1072
CA
LEU
16
45.451
35.154
22.128
1.00
45.72


ATOM
1073
C
LEU
16
45.008
34.361
20.897
1.00
42.62


ATOM
1074
O
LEU
16
45.480
34.571
19.781
1.00
41.21


ATOM
1075
CB
LEU
16
44.990
36.597
22.066
1.00
46.03


ATOM
1076
CG
LEU
16
44.014
37.291
23.024
1.00
45.53


ATOM
1077
CD1
LEU
16
44.094
36.865
24.479
1.00
46.94


ATOM
1078
CD2
LEU
16
44.289
38.762
22.907
1.00
42.24


ATOM
1079
N
PRO
17
44.091
33.421
21.118
1.00
39.73


ATOM
1080
CA
PRO
17
43.589
32.688
19.976
1.00
37.59


ATOM
1081
C
PRO
17
42.594
33.628
19.285
1.00
35.06


ATOM
1082
O
PRO
17
41.991
34.512
19.928
1.00
34.66


ATOM
1083
CB
PRO
17
42.862
31.506
20.612
1.00
37.49


ATOM
1084
CG
PRO
17
42.391
32.059
21.904
1.00
38.46


ATOM
1085
CD
PRO
17
43.431
33.025
22.375
1.00
39.21


ATOM
1086
N
ILE
18
42.450
33.455
17.988
1.00
32.48


ATOM
1087
CA
ILE
18
41.485
34.246
17.234
1.00
29.75


ATOM
1088
C
ILE
18
40.315
33.372
16.866
1.00
28.71


ATOM
1089
O
ILE
18
40.492
32.282
16.313
1.00
29.46


ATOM
1090
CB
ILE
18
42.172
34.915
16.010
1.00
29.27


ATOM
1091
CG1
ILE
18
43.186
35.933
16.555
1.00
28.75


ATOM
1092
CG2
ILE
18
41.139
35.601
15.144
1.00
26.93


ATOM
1093
CD1
ILE
18
44.188
36.399
15.568
1.00
29.65


ATOM
1094
N
ASN
19
39.124
33.832
17.218
1.00
27.84


ATOM
1095
CA
ASN
19
37.917
33.088
17.011
1.00
28.72


ATOM
1096
C
ASN
19
37.791
32.671
15.535
1.00
29.30


ATOM
1097
O
ASN
19
37.556
31.519
15.230
1.00
29.67


ATOM
1098
CB
ASN
19
36.692
33.897
17.443
1.00
27.56


ATOM
1099
CG
ASN
19
36.566
34.037
18.934
1.00
30.11


ATOM
1100
OD1
ASN
19
35.628
33.510
19.537
1.00
35.03


ATOM
1101
ND2
ASN
19
37.457
34.803
19.541
1.00
26.59


ATOM
1102
N
GLN
20
37.946
33.633
14.625
1.00
28.21


ATOM
1103
CA
GLN
20
37.823
33.346
13.200
1.00
27.61


ATOM
1104
C
GLN
20
38.739
34.277
12.456
1.00
26.93


ATOM
1105
O
GLN
20
38.727
35.468
12.704
1.00
25.53


ATOM
1106
CB
GLN
20
36.387
33.587
12.738
1.00
27.40


ATOM
1107
CG
GLN
20
35.289
32.662
13.323
1.00
28.89


ATOM
1108
CD
GLN
20
35.392
31.156
12.907
1.00
29.01


ATOM
1109
OE1
GLN
20
36.015
30.793
11.917
1.00
24.93


ATOM
1110
NE2
GLN
20
34.725
30.299
13.677
1.00
33.39


ATOM
1111
N
VAL
21
39.523
33.726
11.534
1.00
28.44


ATOM
1112
CA
VAL
21
40.353
34.521
10.641
1.00
28.39


ATOM
1113
C
VAL
21
40.302
33.901
9.231
1.00
28.96


ATOM
1114
O
VAL
21
40.332
32.653
9.084
1.00
28.04


ATOM
1115
CB
VAL
21
41.813
34.603
11.139
1.00
29.27


ATOM
1116
CG1
VAL
21
42.432
33.163
11.302
1.00
30.86


ATOM
1117
CG2
VAL
21
42.630
35.412
10.182
1.00
26.64


ATOM
1118
N
GLY
22
40.265
34.772
8.214
1.00
25.74


ATOM
1119
CA
GLY
22
40.312
34.315
6.847
1.00
25.43


ATOM
1120
C
GLY
22
39.912
35.415
5.893
1.00
25.13


ATOM
1121
O
GLY
22
40.462
36.563
5.962
1.00
24.40


ATOM
1122
N
ILE
23
39.006
35.087
4.967
1.00
24.91


ATOM
1123
CA
ILE
23
38.654
36.061
3.894
1.00
24.29


ATOM
1124
C
ILE
23
37.205
36.429
3.946
1.00
24.19


ATOM
1125
O
ILE
23
36.368
35.647
4.382
1.00
22.43


ATOM
1126
CB
ILE
23
39.055
35.617
2.460
1.00
24.57


ATOM
1127
CG1
ILE
23
38.314
34.325
2.043
1.00
25.55


ATOM
1128
CG2
ILE
23
40.562
35.500
2.383
1.00
27.03


ATOM
1129
CD1
ILE
23
38.356
33.909
0.539
1.00
26.06


ATOM
1130
N
THR
48
36.553
31.379
7.054
1.00
25.33


ATOM
1131
CA
THR
48
37.449
31.661
8.177
1.00
26.30


ATOM
1132
C
THR
48
37.736
30.379
8.969
1.00
27.67


ATOM
1133
O
THR
48
36.880
29.443
8.981
1.00
27.40


ATOM
1134
CB
THR
48
36.811
32.640
9.156
1.00
25.92


ATOM
1135
OG1
THR
48
35.570
32.127
9.604
1.00
27.43


ATOM
1136
CG2
THR
48
36.580
34.048
8.541
1.00
25.73


ATOM
1137
N
VAL
49
38.895
30.322
9.648
1.00
28.21


ATOM
1138
CA
VAL
49
39.164
29.202
10.595
1.00
27.79


ATOM
1139
C
VAL
49
39.600
29.805
11.956
1.00
29.96


ATOM
1140
O
VAL
49
39.931
30.991
12.055
1.00
29.84


ATOM
1141
CB
VAL
49
40.301
28.306
10.065
1.00
27.06


ATOM
1142
CG1
VAL
49
39.910
27.547
8.745
1.00
24.24


ATOM
1143
CG2
VAL
49
41.593
29.120
9.884
1.00
26.20


ATOM
1144
N
TYR
50
39.658
28.969
12.980
1.00
30.77


ATOM
1145
CA
TYR
50
40.097
29.355
14.333
1.00
31.30


ATOM
1146
C
TYR
50
41.584
29.365
14.291
1.00
31.89


ATOM
1147
O
TYR
50
42.174
28.503
13.663
1.00
31.71


ATOM
1148
CB
TYR
50
39.619
28.292
15.301
1.00
32.58


ATOM
1149
CG
TYR
50
40.188
28.329
16.695
1.00
33.26


ATOM
1150
CD1
TYR
50
39.629
29.138
17.651
1.00
32.16


ATOM
1151
CD2
TYR
50
41.235
27.478
17.067
1.00
34.15


ATOM
1152
CE1
TYR
50
40.135
29.166
18.975
1.00
35.06


ATOM
1153
CE2
TYR
50
41.748
27.488
18.387
1.00
34.47


ATOM
1154
CZ
TYR
50
41.182
28.336
19.318
1.00
34.05


ATOM
1155
OH
TYR
50
41.636
28.362
20.629
1.00
36.34


ATOM
1156
N
LEU
51
42.199
30.356
14.925
1.00
32.43


ATOM
1157
CA
LEU
51
43.649
30.425
15.047
1.00
33.24


ATOM
1158
C
LEU
51
44.061
30.272
16.526
1.00
33.57


ATOM
1159
O
LEU
51
43.695
31.115
17.330
1.00
31.07


ATOM
1160
CB
LEU
51
44.161
31.778
14.528
1.00
32.42


ATOM
1161
CG
LEU
51
45.656
31.778
14.277
1.00
33.30


ATOM
1162
CD1
LEU
51
46.001
30.774
13.207
1.00
32.77


ATOM
1163
CD2
LEU
51
46.156
33.169
13.840
1.00
33.73


ATOM
1164
N
PRO
52
44.803
29.180
16.884
1.00
35.48


ATOM
1165
CA
PRO
52
45.196
29.027
18.303
1.00
36.24


ATOM
1166
C
PRO
52
46.242
30.079
18.713
1.00
37.08


ATOM
1167
O
PRO
52
46.981
30.616
17.867
1.00
35.03


ATOM
1168
CB
PRO
52
45.803
27.620
18.378
1.00
36.44


ATOM
1169
CG
PRO
52
46.191
27.268
16.968
1.00
37.84


ATOM
1170
CD
PRO
52
45.255
28.059
16.042
1.00
35.65


ATOM
1171
N
ALA
53
46.312
30.352
20.008
1.00
39.26


ATOM
1172
CA
ALA
53
47.259
31.342
20.509
1.00
41.52


ATOM
1173
C
ALA
53
48.632
31.262
19.902
1.00
43.70


ATOM
1174
O
ALA
53
49.213
32.300
19.542
1.00
44.05


ATOM
1175
CB
ALA
53
47.343
31.295
22.028
1.00
41.87


ATOM
1176
N
GLU
54
49.176
30.051
19.770
1.00
46.18


ATOM
1177
CA
GLU
54
50.595
29.947
19.416
1.00
48.84


ATOM
1178
C
GLU
54
50.950
30.189
17.960
1.00
48.48


ATOM
1179
O
GLU
54
52.143
30.310
17.626
1.00
48.68


ATOM
1180
CB
GLU
54
51.290
28.679
19.988
1.00
49.42


ATOM
1181
CG
GLU
54
50.930
27.304
19.376
1.00
51.16


ATOM
1182
CD
GLU
54
51.905
26.157
19.853
1.00
52.55


ATOM
1183
OE1
GLU
54
51.600
24.953
19.611
1.00
55.01


ATOM
1184
OE2
GLU
54
52.984
26.456
20.462
1.00
56.97


ATOM
1185
N
GLN
55
49.943
30.264
17.098
1.00
47.97


ATOM
1186
CA
GLN
55
50.192
30.396
15.657
1.00
48.24


ATOM
1187
C
GLN
55
50.070
31.860
15.229
1.00
47.26


ATOM
1188
O
GLN
55
49.114
32.533
15.588
1.00
46.59


ATOM
1189
CB
GLN
55
49.222
29.500
14.877
1.00
48.23


ATOM
1190
CG
GLN
55
49.460
29.483
13.359
1.00
49.79


ATOM
1191
CD
GLN
55
48.669
28.396
12.661
1.00
49.97


ATOM
1192
OE1
GLN
55
48.367
27.375
13.266
1.00
53.57


ATOM
1193
NE2
GLN
55
48.337
28.601
11.382
1.00
50.86


ATOM
1194
N
LYS
56
51.043
32.352
14.471
1.00
47.46


ATOM
1195
CA
LYS
56
51.091
33.769
14.130
1.00
48.23


ATOM
1196
C
LYS
56
49.978
34.132
13.149
1.00
47.43


ATOM
1197
O
LYS
56
49.311
35.150
13.323
1.00
47.38


ATOM
1198
CB
LYS
56
52.461
34.174
13.542
1.00
48.49


ATOM
1199
CG
LYS
56
52.559
35.701
13.239
1.00
50.23


ATOM
1200
CD
LYS
56
53.838
36.104
12.483
1.00
51.07


ATOM
1201
CE
LYS
56
54.040
35.276
11.199
1.00
54.39


ATOM
1202
NZ
LYS
56
55.448
35.366
10.676
1.00
56.64


ATOM
1203
N
GLY
57
49.801
33.300
12.124
1.00
46.67


ATOM
1204
CA
GLY
57
48.811
33.554
11.099
1.00
46.24


ATOM
1205
C
GLY
57
48.282
32.313
10.412
1.00
46.03


ATOM
1206
O
GLY
57
48.843
31.208
10.570
1.00
46.27


ATOM
1207
N
THR
58
47.195
32.509
9.654
1.00
45.17


ATOM
1208
CA
THR
58
46.597
31.483
8.810
1.00
43.95


ATOM
1209
C
THR
58
47.170
31.556
7.387
1.00
43.93


ATOM
1210
O
THR
58
48.149
32.270
7.156
1.00
43.84


ATOM
1211
CB
THR
58
45.031
31.554
8.784
1.00
43.76


ATOM
1212
OG1
THR
58
44.529
30.341
8.239
1.00
42.58


ATOM
1213
CG2
THR
58
44.481
32.757
7.957
1.00
41.26


ATOM
1214
N
HIS
59
46.542
30.830
6.456
1.00
42.61


ATOM
1215
CA
HIS
59
47.038
30.691
5.097
1.00
42.55


ATOM
1216
C
HIS
59
46.006
31.176
4.075
1.00
41.58


ATOM
1217
O
HIS
59
45.185
30.402
3.565
1.00
40.93


ATOM
1218
CB
HIS
59
47.431
29.246
4.868
1.00
43.03


ATOM
1219
CG
HIS
59
48.369
28.732
5.915
1.00
46.13


ATOM
1220
ND1
HIS
59
47.926
28.125
7.076
1.00
48.89


ATOM
1221
CD2
HIS
59
49.716
28.810
6.019
1.00
48.32


ATOM
1222
CE1
HIS
59
48.966
27.827
7.840
1.00
48.82


ATOM
1223
NE2
HIS
59
50.063
28.233
7.222
1.00
50.35


ATOM
1224
N
MET
60
46.054
32.471
3.790
1.00
40.23


ATOM
1225
CA
MET
60
44.936
33.167
3.145
1.00
38.85


ATOM
1226
C
MET
60
44.631
32.729
1.718
1.00
37.25


ATOM
1227
O
MET
60
43.465
32.717
1.303
1.00
37.16


ATOM
1228
CB
MET
60
45.147
34.686
3.231
1.00
40.07


ATOM
1229
CG
MET
60
45.182
35.218
4.688
1.00
40.71


ATOM
1230
SD
MET
60
43.511
35.600
5.252
1.00
45.21


ATOM
1231
CE
MET
60
43.801
36.421
6.813
1.00
42.50


ATOM
1232
N
SER
61
45.652
32.353
0.956
1.00
36.21


ATOM
1233
CA
SER
61
45.423
31.968
−0.429
1.00
35.39


ATOM
1234
C
SER
61
44.706
30.631
−0.540
1.00
35.50


ATOM
1235
O
SER
61
44.116
30.325
−1.581
1.00
35.82


ATOM
1236
CB
SER
61
46.719
31.901
−1.204
1.00
36.22


ATOM
1237
OG
SER
61
47.456
30.721
−0.911
1.00
36.27


ATOM
1238
N
ARG
62
44.724
29.844
0.533
1.00
34.65


ATOM
1239
CA
ARG
62
44.188
28.474
0.507
1.00
34.67


ATOM
1240
C
ARG
62
42.670
28.505
0.519
1.00
33.66


ATOM
1241
O
ARG
62
42.029
27.568
0.064
1.00
33.93


ATOM
1242
CB
ARG
62
44.700
27.655
1.718
1.00
35.39


ATOM
1243
CG
ARG
62
46.213
27.392
1.757
1.00
35.71


ATOM
1244
CD
ARG
62
46.596
26.539
2.992
1.00
36.59


ATOM
1245
NE
ARG
62
48.060
26.429
3.152
1.00
40.81


ATOM
1246
CZ
ARG
62
48.673
25.627
4.030
1.00
42.85


ATOM
1247
NH1
ARG
62
47.947
24.852
4.833
1.00
42.89


ATOM
1248
NH2
ARG
62
50.010
25.591
4.101
1.00
39.58


ATOM
1249
N
PHE
63
42.080
29.569
1.073
1.00
31.76


ATOM
1250
CA
PHE
63
40.621
29.735
1.039
1.00
29.77


ATOM
1251
C
PHE
63
40.169
29.909
−0.413
1.00
29.97


ATOM
1252
O
PHE
63
39.205
29.299
−0.833
1.00
29.60


ATOM
1253
CB
PHE
63
40.155
30.970
1.815
1.00
29.04


ATOM
1254
CG
PHE
63
40.440
30.918
3.280
1.00
24.94


ATOM
1255
CD1
PHE
63
39.661
30.140
4.105
1.00
25.06


ATOM
1256
CD2
PHE
63
41.475
31.662
3.828
1.00
25.62


ATOM
1257
CE1
PHE
63
39.904
30.068
5.464
1.00
25.26


ATOM
1258
CE2
PHE
63
41.738
31.610
5.202
1.00
27.19


ATOM
1259
CZ
PHE
63
40.938
30.802
6.022
1.00
26.37


ATOM
1260
N
VAL
64
40.880
30.729
−1.178
1.00
29.57


ATOM
1261
CA
VAL
64
40.513
30.944
−2.578
1.00
29.55


ATOM
1262
C
VAL
64
40.837
29.671
−3.361
1.00
30.87


ATOM
1263
O
VAL
64
40.065
29.310
−4.227
1.00
30.92


ATOM
1264
CB
VAL
64
41.256
32.114
−3.207
1.00
29.58


ATOM
1265
CG1
VAL
64
40.690
32.383
−4.582
1.00
30.02


ATOM
1266
CG2
VAL
64
41.126
33.412
−2.311
1.00
27.42


ATOM
1267
N
ALA
65
41.967
29.005
−3.068
1.00
31.39


ATOM
1268
CA
ALA
65
42.338
27.724
−3.733
1.00
32.56


ATOM
1269
C
ALA
65
41.193
26.703
−3.642
1.00
33.22


ATOM
1270
O
ALA
65
40.842
26.021
−4.620
1.00
33.73


ATOM
1271
CB
ALA
65
43.688
27.119
−3.097
1.00
32.21


ATOM
1272
N
LEU
66
40.610
26.591
−2.448
1.00
33.30


ATOM
1273
CA
LEU
66
39.528
25.660
−2.226
1.00
32.82


ATOM
1274
C
LEU
66
38.364
25.915
−3.196
1.00
33.60


ATOM
1275
O
LEU
66
37.849
24.996
−3.856
1.00
32.31


ATOM
1276
CB
LEU
66
39.061
25.758
−0.775
1.00
31.90


ATOM
1277
CG
LEU
66
37.995
24.752
−0.377
1.00
32.41


ATOM
1278
CD1
LEU
66
38.590
23.305
−0.361
1.00
35.12


ATOM
1279
CD2
LEU
66
37.421
25.135
0.955
1.00
31.49


ATOM
1280
N
GLU
68
38.341
27.610
−6.063
1.00
37.55


ATOM
1281
CA
GLU
68
38.771
27.390
−7.422
1.00
40.89


ATOM
1282
C
GLU
68
38.784
25.887
−7.739
1.00
43.79


ATOM
1283
O
GLU
68
38.320
25.502
−8.793
1.00
42.72


ATOM
1284
CB
GLU
68
40.128
28.049
−7.679
1.00
40.31


ATOM
1285
CG
GLU
68
40.090
29.562
−7.438
1.00
38.64


ATOM
1286
CD
GLU
68
39.309
30.285
−8.518
1.00
38.78


ATOM
1287
OE1
GLU
68
39.045
29.632
−9.551
1.00
36.65


ATOM
1288
OE2
GLU
68
38.971
31.505
−8.366
1.00
38.57


ATOM
1289
N
GLN
69
39.247
25.068
−6.786
1.00
47.57


ATOM
1290
CA
GLN
69
39.388
23.612
−6.988
1.00
52.47


ATOM
1291
C
GLN
69
38.048
22.908
−7.080
1.00
53.85


ATOM
1292
O
GLN
69
37.912
21.936
−7.810
1.00
54.85


ATOM
1293
CB
GLN
69
40.200
22.961
−5.857
1.00
52.64


ATOM
1294
CG
GLN
69
41.709
22.868
−6.141
1.00
55.16


ATOM
1295
CD
GLN
69
42.618
22.724
−4.878
1.00
55.40


ATOM
1296
OE1
GLN
69
42.147
22.602
−3.726
1.00
59.00


ATOM
1297
NE2
GLN
69
43.931
22.746
−5.114
1.00
57.66


ATOM
1298
N
GLU
85
36.599
20.020
4.284
1.00
34.50


ATOM
1299
CA
GLU
85
37.788
20.139
3.477
1.00
36.41


ATOM
1300
C
GLU
85
38.564
21.421
3.793
1.00
35.63


ATOM
1301
O
GLU
85
39.804
21.403
3.868
1.00
36.27


ATOM
1302
CB
GLU
85
37.430
20.063
2.005
1.00
37.22


ATOM
1303
CG
GLU
85
38.661
19.976
1.159
1.00
44.97


ATOM
1304
CD
GLU
85
38.432
19.342
−0.195
1.00
52.91


ATOM
1305
OE1
GLU
85
37.489
18.508
−0.323
1.00
54.95


ATOM
1306
OE2
GLU
85
39.214
19.693
−1.131
1.00
55.69


ATOM
1307
N
MET
86
37.842
22.524
4.012
1.00
33.82


ATOM
1308
CA
MET
86
38.514
23.766
4.412
1.00
33.23


ATOM
1309
C
MET
86
39.369
23.647
5.676
1.00
34.16


ATOM
1310
O
MET
86
40.527
24.057
5.679
1.00
34.95


ATOM
1311
CB
MET
86
37.507
24.910
4.647
1.00
32.36


ATOM
1312
CG
MET
86
38.202
26.275
4.769
1.00
31.48


ATOM
1313
SD
MET
86
37.050
27.565
5.210
1.00
29.78


ATOM
1314
CE
MET
86
36.275
27.008
6.773
1.00
22.03


ATOM
1315
N
VAL
87
38.796
23.174
6.771
1.00
36.21


ATOM
1316
CA
VAL
87
39.569
23.133
8.040
1.00
37.84


ATOM
1317
C
VAL
87
40.803
22.254
7.905
1.00
39.36


ATOM
1318
O
VAL
87
41.838
22.528
8.531
1.00
40.24


ATOM
1319
CB
VAL
87
38.730
22.674
9.245
1.00
38.61


ATOM
1320
CG1
VAL
87
37.639
23.672
9.519
1.00
37.63


ATOM
1321
CG2
VAL
87
38.122
21.273
9.011
1.00
37.58


ATOM
1322
N
ALA
88
40.699
21.210
7.071
1.00
39.92


ATOM
1323
CA
ALA
88
41.823
20.292
6.824
1.00
40.37


ATOM
1324
C
ALA
88
42.893
20.943
5.987
1.00
40.95


ATOM
1325
O
ALA
88
44.082
20.856
6.326
1.00
41.91


ATOM
1326
CB
ALA
88
41.339
19.022
6.156
1.00
40.29


ATOM
1327
N
LEU
89
42.467
21.627
4.917
1.00
40.06


ATOM
1328
CA
LEU
89
43.380
22.334
4.017
1.00
40.50


ATOM
1329
C
LEU
89
44.174
23.435
4.745
1.00
39.98


ATOM
1330
O
LEU
89
45.363
23.668
4.462
1.00
38.44


ATOM
1331
CB
LEU
89
42.588
22.951
2.848
1.00
40.68


ATOM
1332
CG
LEU
89
43.370
23.782
1.820
1.00
41.74


ATOM
1333
CD1
LEU
89
44.363
22.868
1.059
1.00
44.04


ATOM
1334
CD2
LEU
89
42.426
24.484
0.818
1.00
40.51


ATOM
1335
N
LEU
90
43.494
24.101
5.678
1.00
40.31


ATOM
1336
CA
LEU
90
44.053
25.240
6.402
1.00
40.41


ATOM
1337
C
LEU
90
44.739
24.813
7.709
1.00
41.69


ATOM
1338
O
LEU
90
45.256
25.655
8.483
1.00
40.27


ATOM
1339
CB
LEU
90
42.955
26.234
6.699
1.00
39.60


ATOM
1340
CG
LEU
90
43.070
27.082
5.455
1.00
38.10


ATOM
1341
CD1
LEU
90
41.936
26.856
4.502
1.00
33.65


ATOM
1342
CD2
LEU
90
43.272
28.457
5.834
1.00
34.46


ATOM
1343
N
ASP
91
44.738
23.494
7.925
1.00
41.99


ATOM
1344
CA
ASP
91
45.381
22.868
9.110
1.00
42.31


ATOM
1345
C
ASP
91
44.863
23.449
10.409
1.00
41.35


ATOM
1346
O
ASP
91
45.669
23.923
11.225
1.00
42.00


ATOM
1347
CB
ASP
91
46.900
23.075
9.073
1.00
42.72


ATOM
1348
CG
ASP
91
47.545
22.472
7.880
1.00
46.18


ATOM
1349
OD1
ASP
91
47.169
21.337
7.503
1.00
52.04


ATOM
1350
OD2
ASP
91
48.439
23.124
7.313
1.00
48.88


ATOM
1351
N
SER
92
43.543
23.426
10.605
1.00
40.27


ATOM
1352
CA
SER
92
42.920
24.003
11.793
1.00
39.39


ATOM
1353
C
SER
92
41.864
23.088
12.372
1.00
40.36


ATOM
1354
O
SER
92
41.378
22.183
11.699
1.00
42.15


ATOM
1355
CB
SER
92
42.236
25.342
11.488
1.00
39.41


ATOM
1356
OG
SER
92
41.483
25.795
12.630
1.00
34.46


ATOM
1357
N
ARG
93
41.454
23.378
13.594
1.00
40.29


ATOM
1358
CA
ARG
93
40.521
22.535
14.309
1.00
42.05


ATOM
1359
C
ARG
93
39.068
22.948
14.088
1.00
40.68


ATOM
1360
O
ARG
93
38.152
22.193
14.428
1.00
41.97


ATOM
1361
CB
ARG
93
40.847
22.576
15.799
1.00
42.19


ATOM
1362
CG
ARG
93
39.854
23.386
16.613
1.00
45.63


ATOM
1363
CD
ARG
93
40.382
23.916
17.978
1.00
46.18


ATOM
1364
NE
ARG
93
39.617
25.125
18.363
1.00
54.20


ATOM
1365
CZ
ARG
93
38.309
25.154
18.680
1.00
54.69


ATOM
1366
NH1
ARG
93
37.576
24.036
18.686
1.00
58.29


ATOM
1367
NH2
ARG
93
37.720
26.307
18.984
1.00
56.33


ATOM
1368
N
ALA
94
38.842
24.151
13.541
1.00
37.80


ATOM
1369
CA
ALA
94
37.501
24.726
13.516
1.00
35.70


ATOM
1370
C
ALA
94
37.410
25.833
12.474
1.00
34.21


ATOM
1371
O
ALA
94
38.389
26.471
12.193
1.00
33.40


ATOM
1372
CB
ALA
94
37.134
25.284
14.843
1.00
34.97


ATOM
1373
N
LYS
106
38.708
65.977
15.909
1.00
31.12


ATOM
1374
CA
LYS
106
39.798
66.800
15.380
1.00
32.80


ATOM
1375
C
LYS
106
41.145
66.122
15.628
1.00
32.96


ATOM
1376
O
LYS
106
41.449
65.723
16.783
1.00
33.18


ATOM
1377
CB
LYS
106
39.757
68.191
16.041
1.00
34.65


ATOM
1378
CG
LYS
106
40.696
69.235
15.401
1.00
39.55


ATOM
1379
CD
LYS
106
40.008
70.188
14.406
1.00
47.35


ATOM
1380
CE
LYS
106
38.963
71.096
15.070
1.00
49.33


ATOM
1381
NZ
LYS
106
39.461
71.819
16.300
1.00
54.56


ATOM
1382
N
LYS
107
41.930
65.936
14.557
1.00
31.08


ATOM
1383
CA
LYS
107
43.263
65.361
14.676
1.00
30.55


ATOM
1384
C
LYS
107
44.327
66.386
14.279
1.00
30.89


ATOM
1385
O
LYS
107
44.023
67.385
13.627
1.00
31.02


ATOM
1386
CB
LYS
107
43.437
64.118
13.789
1.00
30.30


ATOM
1387
CG
LYS
107
42.291
63.137
13.910
1.00
30.97


ATOM
1388
CD
LYS
107
42.610
61.772
13.245
1.00
29.55


ATOM
1389
CE
LYS
107
43.721
61.074
13.925
1.00
27.26


ATOM
1390
NZ
LYS
107
43.937
59.742
13.259
1.00
25.91


ATOM
1391
N
THR
108
45.561
66.081
14.645
1.00
31.14


ATOM
1392
CA
THR
108
46.746
66.902
14.404
1.00
32.51


ATOM
1393
C
THR
108
47.714
66.097
13.548
1.00
32.54


ATOM
1394
O
THR
108
48.188
65.028
13.983
1.00
33.24


ATOM
1395
CB
THR
108
47.397
67.166
15.779
1.00
32.61


ATOM
1396
OG1
THR
108
46.422
67.786
16.589
1.00
35.34


ATOM
1397
CG2
THR
108
48.586
68.069
15.699
1.00
33.31


ATOM
1398
N
ALA
109
48.002
66.566
12.335
1.00
33.07


ATOM
1399
CA
ALA
109
49.018
65.906
11.498
1.00
33.80


ATOM
1400
C
ALA
109
50.355
65.718
12.250
1.00
34.89


ATOM
1401
O
ALA
109
50.734
66.564
13.083
1.00
34.88


ATOM
1402
CB
ALA
109
49.209
66.686
10.195
1.00
34.10


ATOM
1403
N
PRO
110
51.057
64.576
11.991
1.00
35.11


ATOM
1404
CA
PRO
110
52.171
64.180
12.837
1.00
35.19


ATOM
1405
C
PRO
110
53.463
64.984
12.693
1.00
35.83


ATOM
1406
O
PRO
110
54.287
64.898
13.615
1.00
36.44


ATOM
1407
CB
PRO
110
52.426
62.722
12.426
1.00
35.24


ATOM
1408
CG
PRO
110
51.888
62.618
11.047
1.00
35.53


ATOM
1409
CD
PRO
110
50.757
63.576
10.945
1.00
33.91


ATOM
1410
N
VAL
111
53.642
65.732
11.579
1.00
34.87


ATOM
1411
CA
VAL
111
54.845
66.561
11.401
1.00
34.55


ATOM
1412
C
VAL
111
54.480
68.049
11.361
1.00
34.44


ATOM
1413
O
VAL
111
54.889
68.807
12.217
1.00
34.73


ATOM
1414
CB
VAL
111
55.721
66.104
10.201
1.00
35.20


ATOM
1415
CG1
VAL
111
56.926
67.053
10.018
1.00
35.13


ATOM
1416
CG2
VAL
111
56.258
64.662
10.458
1.00
33.36


ATOM
1417
N
SER
112
53.644
68.445
10.411
1.00
34.36


ATOM
1418
CA
SER
112
53.171
69.829
10.301
1.00
33.65


ATOM
1419
C
SER
112
52.276
70.296
11.430
1.00
34.37


ATOM
1420
O
SER
112
52.205
71.522
11.716
1.00
34.40


ATOM
1421
CB
SER
112
52.457
70.035
8.980
1.00
33.85


ATOM
1422
OG
SER
112
51.195
69.359
8.954
1.00
32.93


ATOM
1423
N
GLY
113
51.573
69.348
12.067
1.00
33.94


ATOM
1424
CA
GLY
113
50.585
69.684
13.125
1.00
32.54


ATOM
1425
C
GLY
113
49.345
70.397
12.624
1.00
33.41


ATOM
1426
O
GLY
113
48.569
70.950
13.442
1.00
32.86


ATOM
1427
N
ILE
114
49.131
70.384
11.289
1.00
33.45


ATOM
1428
CA
ILE
114
47.931
70.990
10.697
1.00
34.24


ATOM
1429
C
ILE
114
46.768
70.138
11.217
1.00
34.53


ATOM
1430
O
ILE
114
46.890
68.901
11.331
1.00
33.15


ATOM
1431
CB
ILE
114
47.910
70.965
9.134
1.00
35.17


ATOM
1432
CG1
ILE
114
49.151
71.641
8.519
1.00
38.77


ATOM
1433
CG2
ILE
114
46.701
71.682
8.582
1.00
33.39


ATOM
1434
CD1
ILE
114
49.226
73.088
8.731
1.00
42.74


ATOM
1435
N
ARG
115
45.664
70.796
11.562
1.00
34.61


ATOM
1436
CA
ARG
115
44.558
70.079
12.189
1.00
35.62


ATOM
1437
C
ARG
115
43.499
69.759
11.134
1.00
33.87


ATOM
1438
O
ARG
115
43.329
70.512
10.171
1.00
32.92


ATOM
1439
CB
ARG
115
43.976
70.844
13.399
1.00
35.86


ATOM
1440
CG
ARG
115
45.049
71.225
14.495
1.00
39.50


ATOM
1441
CD
ARG
115
44.457
71.218
15.918
1.00
41.37


ATOM
1442
NE
ARG
115
44.156
69.839
16.349
1.00
49.17


ATOM
1443
CZ
ARG
115
43.421
69.486
17.420
1.00
50.07


ATOM
1444
NH1
ARG
115
42.877
70.418
18.205
1.00
52.25


ATOM
1445
NH2
ARG
115
43.228
68.182
17.705
1.00
50.44


ATOM
1446
N
SER
116
42.829
68.612
11.305
1.00
32.49


ATOM
1447
CA
SER
116
41.712
68.256
10.444
1.00
31.24


ATOM
1448
C
SER
116
40.804
67.204
11.123
1.00
30.84


ATOM
1449
O
SER
116
41.201
66.486
12.080
1.00
31.63


ATOM
1450
CB
SER
116
42.218
67.835
9.021
1.00
31.35


ATOM
1451
OG
SER
116
42.970
66.625
9.062
1.00
29.62


ATOM
1452
N
PRO
142
38.636
53.573
10.939
1.00
23.23


ATOM
1453
CA
PRO
142
39.398
53.247
9.753
1.00
23.79


ATOM
1454
C
PRO
142
40.866
53.611
9.963
1.00
24.65


ATOM
1455
O
PRO
142
41.162
54.667
10.563
1.00
25.09


ATOM
1456
CB
PRO
142
38.715
54.125
8.699
1.00
24.09


ATOM
1457
CG
PRO
142
38.391
55.456
9.539
1.00
23.27


ATOM
1458
CD
PRO
142
37.978
54.901
10.870
1.00
23.22


ATOM
1459
N
VAL
143
41.771
52.733
9.512
1.00
24.51


ATOM
1460
CA
VAL
143
43.210
52.865
9.769
1.00
25.26


ATOM
1461
C
VAL
143
43.912
52.341
8.527
1.00
26.54


ATOM
1462
O
VAL
143
43.270
51.805
7.611
1.00
25.34


ATOM
1463
CB
VAL
143
43.698
52.054
11.032
1.00
24.57


ATOM
1464
CG1
VAL
143
42.985
52.533
12.322
1.00
25.48


ATOM
1465
CG2
VAL
143
43.463
50.510
10.826
1.00
23.63


ATOM
1466
N
THR
144
45.225
52.542
8.503
1.00
27.67


ATOM
1467
CA
THR
144
46.106
51.971
7.510
1.00
27.19


ATOM
1468
C
THR
144
46.653
50.618
8.005
1.00
27.74


ATOM
1469
O
THR
144
47.110
50.536
9.150
1.00
27.09


ATOM
1470
CB
THR
144
47.302
52.895
7.281
1.00
27.10


ATOM
1471
OG1
THR
144
46.827
54.201
6.909
1.00
24.38


ATOM
1472
CG2
THR
144
48.174
52.329
6.162
1.00
28.95


ATOM
1473
N
SER
145
46.572
49.569
7.157
1.00
26.89


ATOM
1474
CA
SER
145
47.241
48.293
7.442
1.00
27.89


ATOM
1475
C
SER
145
48.318
48.049
6.381
1.00
28.66


ATOM
1476
O
SER
145
48.130
48.418
5.237
1.00
28.16


ATOM
1477
CB
SER
145
46.217
47.132
7.504
1.00
28.02


ATOM
1478
OG
SER
145
45.570
46.960
6.232
1.00
26.68


ATOM
1479
N
LEU
146
49.460
47.468
6.756
1.00
29.89


ATOM
1480
CA
LEU
146
50.545
47.208
5.789
1.00
29.68


ATOM
1481
C
LEU
146
51.070
45.787
5.993
1.00
30.59


ATOM
1482
O
LEU
146
51.229
45.362
7.132
1.00
28.81


ATOM
1483
CB
LEU
146
51.662
48.237
5.962
1.00
29.41


ATOM
1484
CG
LEU
146
52.892
48.155
5.020
1.00
29.93


ATOM
1485
CD1
LEU
146
53.407
49.526
4.667
1.00
27.71


ATOM
1486
CD2
LEU
146
54.018
47.284
5.659
1.00
28.67


ATOM
1487
N
CYS
147
51.337
45.045
4.903
1.00
31.66


ATOM
1488
CA
CYS
147
51.527
43.581
5.043
1.00
31.98


ATOM
1489
C
CYS
147
52.968
43.149
5.421
1.00
31.99


ATOM
1490
O
CYS
147
53.908
43.398
4.649
1.00
31.52


ATOM
1491
CB
CYS
147
51.081
42.864
3.767
1.00
31.07


ATOM
1492
SG
CYS
147
51.160
41.046
3.962
1.00
34.30


ATOM
1493
N
PRO
148
53.160
42.488
6.599
1.00
32.55


ATOM
1494
CA
PRO
148
54.563
42.078
6.962
1.00
33.44


ATOM
1495
C
PRO
148
55.189
41.064
5.986
1.00
34.23


ATOM
1496
O
PRO
148
56.410
41.057
5.794
1.00
34.47


ATOM
1497
CB
PRO
148
54.420
41.429
8.350
1.00
33.47


ATOM
1498
CG
PRO
148
53.058
41.894
8.878
1.00
33.36


ATOM
1499
CD
PRO
148
52.191
42.134
7.641
1.00
32.15


ATOM
1500
N
CYS
149
54.353
40.234
5.358
1.00
35.48


ATOM
1501
CA
CYS
149
54.815
39.212
4.420
1.00
34.64


ATOM
1502
C
CYS
149
55.291
39.887
3.120
1.00
33.98


ATOM
1503
O
CYS
149
56.400
39.584
2.588
1.00
33.37


ATOM
1504
CB
CYS
149
53.683
38.205
4.164
1.00
34.81


ATOM
1505
SG
CYS
149
54.068
36.986
2.863
1.00
41.23


ATOM
1506
N
SER
150
54.474
40.834
2.636
1.00
32.17


ATOM
1507
CA
SER
150
54.840
41.677
1.498
1.00
31.42


ATOM
1508
C
SER
150
56.187
42.422
1.673
1.00
31.54


ATOM
1509
O
SER
150
57.066
42.369
0.783
1.00
31.16


ATOM
1510
CB
SER
150
53.698
42.692
1.218
1.00
31.09


ATOM
1511
OG
SER
150
54.012
43.515
0.114
1.00
28.82


ATOM
1512
N
LYS
151
56.340
43.137
2.787
1.00
30.89


ATOM
1513
CA
LYS
151
57.609
43.773
3.108
1.00
32.75


ATOM
1514
C
LYS
151
58.783
42.735
3.082
1.00
34.08


ATOM
1515
O
LYS
151
59.806
42.922
2.380
1.00
35.64


ATOM
1516
CB
LYS
151
57.521
44.443
4.506
1.00
31.90


ATOM
1517
CG
LYS
151
58.790
45.152
4.942
1.00
31.20


ATOM
1518
CD
LYS
151
58.619
45.793
6.326
1.00
31.30


ATOM
1519
CE
LYS
151
59.952
46.371
6.776
1.00
33.03


ATOM
1520
NZ
LYS
151
59.848
47.112
8.026
1.00
30.24


ATOM
1521
N
GLU
152
58.639
41.671
3.850
1.00
35.50


ATOM
1522
CA
GLU
152
59.707
40.675
4.032
1.00
38.06


ATOM
1523
C
GLU
152
60.216
40.033
2.718
1.00
38.25


ATOM
1524
O
GLU
152
61.426
39.897
2.526
1.00
39.41


ATOM
1525
CB
GLU
152
59.253
39.597
5.017
1.00
39.11


ATOM
1526
CG
GLU
152
60.091
38.324
4.985
1.00
45.31


ATOM
1527
CD
GLU
152
59.694
37.369
6.069
1.00
52.84


ATOM
1528
OE1
GLU
152
58.956
36.401
5.769
1.00
57.04


ATOM
1529
OE2
GLU
152
60.086
37.614
7.237
1.00
57.07


ATOM
1530
N
ILE
153
59.302
39.645
1.824
1.00
37.49


ATOM
1531
CA
ILE
153
59.688
38.928
0.608
1.00
37.01


ATOM
1532
C
ILE
153
60.152
39.898
−0.517
1.00
37.61


ATOM
1533
O
ILE
153
60.871
39.477
−1.429
1.00
37.14


ATOM
1534
CB
ILE
153
58.543
37.957
0.113
1.00
37.48


ATOM
1535
CG1
ILE
153
57.332
38.750
−0.436
1.00
37.02


ATOM
1536
CG2
ILE
153
58.110
36.947
1.257
1.00
35.87


ATOM
1537
CD1
ILE
153
56.064
37.955
−0.708
1.00
36.43


ATOM
1538
N
SER
154
59.742
41.184
−0.451
1.00
36.39


ATOM
1539
CA
SER
154
59.982
42.125
−1.561
1.00
36.06


ATOM
1540
C
SER
154
61.247
42.893
−1.398
1.00
36.42


ATOM
1541
O
SER
154
61.594
43.277
−0.288
1.00
36.52


ATOM
1542
CB
SER
154
58.810
43.104
−1.733
1.00
34.92


ATOM
1543
OG
SER
154
57.623
42.347
−1.874
1.00
34.60


ATOM
1544
N
GLN
155
61.952
43.146
−2.491
1.00
37.31


ATOM
1545
CA
GLN
155
63.209
43.910
−2.338
1.00
39.20


ATOM
1546
C
GLN
155
62.959
45.361
−2.004
1.00
38.30


ATOM
1547
O
GLN
155
63.840
46.057
−1.475
1.00
37.74


ATOM
1548
CB
GLN
155
64.129
43.785
−3.565
1.00
40.45


ATOM
1549
CG
GLN
155
63.556
44.240
−4.895
1.00
42.35


ATOM
1550
CD
GLN
155
64.560
44.047
−6.021
1.00
42.99


ATOM
1551
OE1
GLN
155
65.753
44.345
−5.856
1.00
45.28


ATOM
1552
NE2
GLN
155
64.086
43.541
−7.171
1.00
46.69


ATOM
1553
N
TYR
156
61.739
45.810
−2.305
1.00
37.89


ATOM
1554
CA
TYR
156
61.285
47.172
−1.997
1.00
36.80


ATOM
1555
C
TYR
156
59.761
47.230
−2.042
1.00
36.04


ATOM
1556
O
TYR
156
59.130
46.344
−2.647
1.00
36.63


ATOM
1557
CB
TYR
156
61.934
48.202
−2.936
1.00
36.72


ATOM
1558
CG
TYR
156
62.101
47.789
−4.392
1.00
36.70


ATOM
1559
CD1
TYR
156
61.034
47.312
−5.141
1.00
37.81


ATOM
1560
CD2
TYR
156
63.346
47.894
−5.026
1.00
38.83


ATOM
1561
CE1
TYR
156
61.201
46.948
−6.492
1.00
37.24


ATOM
1562
CE2
TYR
156
63.520
47.546
−6.405
1.00
38.26


ATOM
1563
CZ
TYR
156
62.456
47.086
−7.110
1.00
37.10


ATOM
1564
OH
TYR
156
62.629
46.764
−8.447
1.00
37.14


ATOM
1565
N
GLY
157
59.159
48.216
−1.365
1.00
34.75


ATOM
1566
CA
GLY
157
57.687
48.263
−1.303
1.00
33.03


ATOM
1567
C
GLY
157
57.048
47.295
−0.316
1.00
31.76


ATOM
1568
O
GLY
157
57.700
46.349
0.178
1.00
30.74


ATOM
1569
N
ALA
158
55.778
47.550
−0.010
1.00
30.83


ATOM
1570
CA
ALA
158
54.967
46.646
0.799
1.00
31.12


ATOM
1571
C
ALA
158
53.511
46.998
0.556
1.00
30.73


ATOM
1572
O
ALA
158
53.158
48.186
0.675
1.00
31.76


ATOM
1573
CB
ALA
158
55.327
46.795
2.295
1.00
30.85


ATOM
1574
N
HIS
159
52.661
46.030
0.177
1.00
28.96


ATOM
1575
CA
HIS
159
51.271
46.418
−0.084
1.00
27.54


ATOM
1576
C
HIS
159
50.593
46.832
1.198
1.00
26.90


ATOM
1577
O
HIS
159
50.909
46.304
2.264
1.00
27.11


ATOM
1578
CB
HIS
159
50.445
45.374
−0.843
1.00
27.56


ATOM
1579
CG
HIS
159
49.942
44.219
−0.023
1.00
27.53


ATOM
1580
ND1
HIS
159
48.771
44.283
0.707
1.00
28.80


ATOM
1581
CD2
HIS
159
50.386
42.937
0.080
1.00
25.15


ATOM
1582
CE1
HIS
159
48.537
43.109
1.261
1.00
26.96


ATOM
1583
NE2
HIS
159
49.509
42.275
0.905
1.00
27.80


ATOM
1584
N
ASN
160
49.683
47.794
1.076
1.00
25.77


ATOM
1585
CA
ASN
160
49.021
48.415
2.233
1.00
24.99


ATOM
1586
C
ASN
160
47.670
48.860
1.744
1.00
25.23


ATOM
1587
O
ASN
160
47.413
48.871
0.501
1.00
25.07


ATOM
1588
CB
ASN
160
49.886
49.533
2.882
1.00
24.72


ATOM
1589
CG
ASN
160
50.412
50.583
1.905
1.00
26.68


ATOM
1590
OD1
ASN
160
51.537
50.449
1.397
1.00
31.21


ATOM
1591
ND2
ASN
160
49.665
51.679
1.721
1.00
22.78


ATOM
1592
N
GLN
161
46.763
49.133
2.659
1.00
24.62


ATOM
1593
CA
GLN
161
45.373
49.346
2.282
1.00
25.62


ATOM
1594
C
GLN
161
44.660
49.983
3.461
1.00
25.75


ATOM
1595
O
GLN
161
45.160
49.911
4.567
1.00
25.66


ATOM
1596
CB
GLN
161
44.663
48.030
1.948
1.00
24.86


ATOM
1597
CG
GLN
161
44.856
46.908
3.004
1.00
25.88


ATOM
1598
CD
GLN
161
46.155
46.130
2.795
1.00
26.01


ATOM
1599
OE1
GLN
161
46.542
45.812
1.652
1.00
25.80


ATOM
1600
NE2
GLN
161
46.835
45.811
3.899
1.00
24.43


ATOM
1601
N
ARG
162
43.511
50.606
3.202
1.00
25.37


ATOM
1602
CA
ARG
162
42.654
51.021
4.265
1.00
26.23


ATOM
1603
C
ARG
162
42.032
49.766
4.913
1.00
26.60


ATOM
1604
O
ARG
162
41.775
48.749
4.252
1.00
25.80


ATOM
1605
CB
ARG
162
41.556
51.925
3.741
1.00
26.40


ATOM
1606
CG
ARG
162
40.992
52.868
4.879
1.00
29.11


ATOM
1607
CD
ARG
162
39.866
53.804
4.360
1.00
27.52


ATOM
1608
NE
ARG
162
40.374
54.762
3.381
1.00
26.18


ATOM
1609
CZ
ARG
162
39.603
55.301
2.453
1.00
19.53


ATOM
1610
NH1
ARG
162
38.283
54.963
2.374
1.00
23.76


ATOM
1611
NH2
ARG
162
40.179
56.167
1.612
1.00
23.47


ATOM
1612
N
SER
163
41.787
49.876
6.208
1.00
26.65


ATOM
1613
CA
SER
163
41.244
48.793
6.987
1.00
27.57


ATOM
1614
C
SER
163
40.155
49.368
7.909
1.00
26.82


ATOM
1615
O
SER
163
40.152
50.577
8.235
1.00
26.70


ATOM
1616
CB
SER
163
42.423
48.044
7.657
1.00
27.35


ATOM
1617
OG
SER
163
42.151
47.777
9.023
1.00
35.69


ATOM
1618
N
ILE
181
38.506
54.867
20.151
1.00
22.91


ATOM
1619
CA
ILE
181
39.317
55.319
18.995
1.00
23.75


ATOM
1620
C
ILE
181
40.825
55.261
19.310
1.00
26.04


ATOM
1621
O
ILE
181
41.638
54.746
18.478
1.00
27.11


ATOM
1622
CB
ILE
181
38.911
56.790
18.555
1.00
23.88


ATOM
1623
CG1
ILE
181
37.430
56.843
18.071
1.00
21.17


ATOM
1624
CG2
ILE
181
39.925
57.390
17.477
1.00
21.79


ATOM
1625
CD1
ILE
181
36.943
58.289
17.780
1.00
20.98


ATOM
1626
N
ASP
182
41.225
55.777
20.488
1.00
26.54


ATOM
1627
CA
ASP
182
42.657
55.804
20.814
1.00
26.69


ATOM
1628
C
ASP
182
43.199
54.396
20.957
1.00
25.88


ATOM
1629
O
ASP
182
44.296
54.134
20.514
1.00
26.00


ATOM
1630
CB
ASP
182
42.995
56.648
22.070
1.00
27.60


ATOM
1631
CG
ASP
182
42.783
58.157
21.860
1.00
30.47


ATOM
1632
OD1
ASP
182
42.991
58.661
20.746
1.00
31.48


ATOM
1633
OD2
ASP
182
42.373
58.844
22.814
1.00
33.73


ATOM
1634
N
TYR
183
42.452
53.490
21.589
1.00
26.54


ATOM
1635
CA
TYR
183
42.882
52.083
21.703
1.00
26.51


ATOM
1636
C
TYR
183
43.281
51.500
20.323
1.00
27.37


ATOM
1637
O
TYR
183
44.284
50.774
20.180
1.00
28.29


ATOM
1638
CB
TYR
183
41.761
51.248
22.358
1.00
27.89


ATOM
1639
CG
TYR
183
41.688
51.296
23.877
1.00
27.72


ATOM
1640
CD1
TYR
183
42.832
51.358
24.634
1.00
31.11


ATOM
1641
CD2
TYR
183
40.457
51.235
24.546
1.00
27.18


ATOM
1642
CE1
TYR
183
42.777
51.366
26.075
1.00
32.80


ATOM
1643
CE2
TYR
183
40.377
51.263
25.943
1.00
31.64


ATOM
1644
CZ
TYR
183
41.555
51.318
26.706
1.00
31.01


ATOM
1645
OH
TYR
183
41.507
51.305
28.099
1.00
33.34


ATOM
1646
N
VAL
184
42.476
51.794
19.307
1.00
26.40


ATOM
1647
CA
VAL
184
42.668
51.208
17.997
1.00
24.57


ATOM
1648
C
VAL
184
43.796
51.942
17.240
1.00
25.20


ATOM
1649
O
VAL
184
44.694
51.321
16.708
1.00
25.99


ATOM
1650
CB
VAL
184
41.309
51.223
17.190
1.00
23.34


ATOM
1651
CG1
VAL
184
41.538
50.986
15.671
1.00
24.07


ATOM
1652
CG2
VAL
184
40.331
50.125
17.729
1.00
21.77


ATOM
1653
N
GLU
185
43.711
53.261
17.177
1.00
25.17


ATOM
1654
CA
GLU
185
44.647
54.082
16.391
1.00
25.55


ATOM
1655
C
GLU
185
46.078
53.861
16.857
1.00
27.14


ATOM
1656
O
GLU
185
47.019
53.873
16.027
1.00
26.38


ATOM
1657
CB
GLU
185
44.185
55.548
16.421
1.00
25.17


ATOM
1658
CG
GLU
185
42.920
55.799
15.549
1.00
23.68


ATOM
1659
CD
GLU
185
42.609
57.281
15.318
1.00
26.50


ATOM
1660
OE1
GLU
185
42.984
58.100
16.171
1.00
24.21


ATOM
1661
OE2
GLU
185
41.987
57.636
14.288
1.00
26.85


ATOM
1662
N
THR
186
46.230
53.597
18.172
1.00
27.44


ATOM
1663
CA
THR
186
47.548
53.360
18.780
1.00
29.10


ATOM
1664
C
THR
186
48.130
52.082
18.223
1.00
28.82


ATOM
1665
O
THR
186
49.335
51.950
18.137
1.00
29.57


ATOM
1666
CB
THR
186
47.488
53.171
20.331
1.00
28.74


ATOM
1667
OG1
THR
186
46.989
54.361
20.926
1.00
31.76


ATOM
1668
CG2
THR
186
48.900
52.980
20.950
1.00
31.01


ATOM
1669
N
GLN
187
47.266
51.138
17.880
1.00
27.63


ATOM
1670
CA
GLN
187
47.734
49.838
17.463
1.00
27.72


ATOM
1671
C
GLN
187
47.895
49.701
15.963
1.00
27.83


ATOM
1672
O
GLN
187
48.495
48.744
15.524
1.00
29.63


ATOM
1673
CB
GLN
187
46.797
48.744
17.974
1.00
27.75


ATOM
1674
CG
GLN
187
46.783
48.579
19.519
1.00
26.73


ATOM
1675
CD
GLN
187
48.157
48.394
20.097
1.00
27.76


ATOM
1676
OE1
GLN
187
49.015
47.700
19.533
1.00
30.15


ATOM
1677
NE2
GLN
187
48.378
48.979
21.239
1.00
28.32


ATOM
1678
N
ALA
188
47.356
50.625
15.176
1.00
27.23


ATOM
1679
CA
ALA
188
47.369
50.474
13.725
1.00
27.88


ATOM
1680
C
ALA
188
48.791
50.622
13.135
1.00
28.74


ATOM
1681
O
ALA
188
49.614
51.334
13.715
1.00
28.55


ATOM
1682
CB
ALA
188
46.445
51.517
13.118
1.00
27.58


ATOM
1683
N
SER
189
49.102
49.935
12.010
1.00
28.35


ATOM
1684
CA
SER
189
50.358
50.217
11.299
1.00
28.39


ATOM
1685
C
SER
189
50.551
51.741
11.159
1.00
28.75


ATOM
1686
O
SER
189
51.626
52.259
11.474
1.00
29.75


ATOM
1687
CB
SER
189
50.435
49.501
9.947
1.00
28.00


ATOM
1688
OG
SER
189
50.545
48.071
10.203
1.00
31.33


ATOM
1689
N
CYS
190
49.503
52.434
10.730
1.00
28.89


ATOM
1690
CA
CYS
190
49.416
53.884
10.865
1.00
29.72


ATOM
1691
C
CYS
190
47.958
54.324
10.868
1.00
29.12


ATOM
1692
O
CYS
190
47.134
53.764
10.176
1.00
29.39


ATOM
1693
CB
CYS
190
50.183
54.607
9.738
1.00
29.28


ATOM
1694
SG
CYS
190
50.602
56.361
10.127
1.00
31.60


ATOM
1695
N
GLN
191
47.637
55.341
11.649
1.00
28.56


ATOM
1696
CA
GLN
191
46.306
55.907
11.624
1.00
28.62


ATOM
1697
C
GLN
191
46.093
56.881
10.431
1.00
28.18


ATOM
1698
O
GLN
191
47.055
57.305
9.816
1.00
30.09


ATOM
1699
CB
GLN
191
46.007
56.587
12.982
1.00
27.91


ATOM
1700
CG
GLN
191
46.917
57.763
13.269
1.00
29.69


ATOM
1701
CD
GLN
191
46.745
58.292
14.681
1.00
28.05


ATOM
1702
OE1
GLN
191
45.815
59.041
14.953
1.00
26.08


ATOM
1703
NE2
GLN
191
47.663
57.940
15.563
1.00
27.88


ATOM
1704
N
LEU
192
44.838
57.261
10.165
1.00
27.13


ATOM
1705
CA
LEU
192
44.458
58.173
9.084
1.00
26.58


ATOM
1706
C
LEU
192
44.288
59.643
9.519
1.00
26.86


ATOM
1707
O
LEU
192
43.984
59.927
10.665
1.00
26.33


ATOM
1708
CB
LEU
192
43.123
57.728
8.459
1.00
25.94


ATOM
1709
CG
LEU
192
42.975
56.272
8.007
1.00
25.68


ATOM
1710
CD1
LEU
192
41.595
56.059
7.442
1.00
24.34


ATOM
1711
CD2
LEU
192
44.038
55.909
6.967
1.00
25.68


ATOM
1712
N
TYR
193
44.460
60.540
8.550
1.00
26.29


ATOM
1713
CA
TYR
193
44.264
62.010
8.677
1.00
27.06


ATOM
1714
C
TYR
193
43.652
62.508
7.373
1.00
27.76


ATOM
1715
O
TYR
193
43.991
61.962
6.293
1.00
28.41


ATOM
1716
CB
TYR
193
45.624
62.683
8.820
1.00
26.43


ATOM
1717
CG
TYR
193
46.409
62.194
10.009
1.00
26.85


ATOM
1718
CD1
TYR
193
46.305
62.834
11.260
1.00
26.58


ATOM
1719
CD2
TYR
193
47.243
61.076
9.887
1.00
28.66


ATOM
1720
CE1
TYR
193
47.035
62.375
12.367
1.00
24.85


ATOM
1721
CE2
TYR
193
47.967
60.602
10.959
1.00
26.95


ATOM
1722
CZ
TYR
193
47.841
61.248
12.187
1.00
26.61


ATOM
1723
OH
TYR
193
48.580
60.752
13.189
1.00
26.01


ATOM
1724
N
GLY
194
42.805
63.541
7.430
1.00
27.45


ATOM
1725
CA
GLY
194
42.219
64.052
6.211
1.00
28.39


ATOM
1726
C
GLY
194
43.250
64.943
5.558
1.00
29.37


ATOM
1727
O
GLY
194
43.404
64.987
4.351
1.00
29.71


ATOM
1728
N
LEU
195
43.997
65.660
6.377
1.00
30.72


ATOM
1729
CA
LEU
195
44.913
66.671
5.828
1.00
30.71


ATOM
1730
C
LEU
195
46.347
66.356
6.172
1.00
29.77


ATOM
1731
O
LEU
195
46.736
66.317
7.330
1.00
28.47


ATOM
1732
CB
LEU
195
44.495
68.064
6.282
1.00
30.93


ATOM
1733
CG
LEU
195
44.897
69.300
5.459
1.00
33.19


ATOM
1734
CD1
LEU
195
44.301
70.553
6.174
1.00
33.40


ATOM
1735
CD2
LEU
195
46.381
69.408
5.430
1.00
35.11


ATOM
1736
N
LEU
196
47.125
66.119
5.120
1.00
29.88


ATOM
1737
CA
LEU
196
48.509
65.742
5.234
1.00
31.16


ATOM
1738
C
LEU
196
49.300
66.583
4.255
1.00
32.87


ATOM
1739
O
LEU
196
48.981
66.596
3.049
1.00
31.79


ATOM
1740
CB
LEU
196
48.716
64.262
4.891
1.00
30.65


ATOM
1741
CG
LEU
196
48.111
63.218
5.856
1.00
31.74


ATOM
1742
CD1
LEU
196
48.363
61.876
5.281
1.00
32.71


ATOM
1743
CD2
LEU
196
48.735
63.288
7.252
1.00
32.09


ATOM
1744
N
LYS
197
50.312
67.269
4.790
1.00
33.78


ATOM
1745
CA
LYS
197
51.318
67.927
3.980
1.00
36.74


ATOM
1746
C
LYS
197
52.431
66.910
3.573
1.00
36.95


ATOM
1747
O
LYS
197
52.487
65.762
4.085
1.00
37.20


ATOM
1748
CB
LYS
197
51.883
69.166
4.722
1.00
37.53


ATOM
1749
CG
LYS
197
50.885
70.341
4.822
1.00
39.92


ATOM
1750
CD
LYS
197
50.542
70.745
3.378
1.00
44.49


ATOM
1751
CE
LYS
197
49.503
71.820
3.289
1.00
49.11


ATOM
1752
NZ
LYS
197
50.033
73.137
3.746
1.00
51.33


ATOM
1753
N
ARG
198
53.316
67.333
2.673
1.00
36.70


ATOM
1754
CA
ARG
198
54.337
66.444
2.112
1.00
37.70


ATOM
1755
C
ARG
198
55.200
65.833
3.247
1.00
36.39


ATOM
1756
O
ARG
198
55.469
64.629
3.250
1.00
35.97


ATOM
1757
CB
ARG
198
55.148
67.195
1.021
1.00
37.77


ATOM
1758
CG
ARG
198
56.366
66.474
0.404
1.00
40.32


ATOM
1759
CD
ARG
198
57.175
67.441
−0.517
1.00
41.88


ATOM
1760
NE
ARG
198
58.574
67.027
−0.649
1.00
49.67


ATOM
1761
CZ
ARG
198
59.170
66.702
−1.802
1.00
51.87


ATOM
1762
NH1
ARG
198
58.489
66.743
−2.947
1.00
53.30


ATOM
1763
NH2
ARG
198
60.453
66.333
−1.808
1.00
51.58


ATOM
1764
N
PRO
199
55.623
66.644
4.241
1.00
35.71


ATOM
1765
CA
PRO
199
56.383
65.975
5.318
1.00
34.81


ATOM
1766
C
PRO
199
55.516
64.977
6.110
1.00
35.08


ATOM
1767
O
PRO
199
56.055
63.974
6.651
1.00
34.43


ATOM
1768
CB
PRO
199
56.823
67.129
6.208
1.00
34.84


ATOM
1769
CG
PRO
199
55.836
68.250
5.874
1.00
35.30


ATOM
1770
CD
PRO
199
55.517
68.099
4.440
1.00
35.36


ATOM
1771
N
ASP
200
54.201
65.247
6.175
1.00
34.66


ATOM
1772
CA
ASP
200
53.252
64.371
6.906
1.00
35.25


ATOM
1773
C
ASP
200
53.062
63.072
6.146
1.00
35.17


ATOM
1774
O
ASP
200
53.055
61.983
6.722
1.00
35.34


ATOM
1775
CB
ASP
200
51.908
65.054
7.035
1.00
35.09


ATOM
1776
CG
ASP
200
51.976
66.311
7.874
1.00
35.57


ATOM
1777
OD1
ASP
200
52.551
66.260
8.989
1.00
33.86


ATOM
1778
OD2
ASP
200
51.410
67.331
7.420
1.00
35.70


ATOM
1779
N
GLU
201
52.943
63.196
4.831
1.00
35.17


ATOM
1780
CA
GLU
201
52.823
62.023
3.976
1.00
34.49


ATOM
1781
C
GLU
201
54.086
61.136
4.066
1.00
34.61


ATOM
1782
O
GLU
201
53.997
59.913
4.171
1.00
32.47


ATOM
1783
CB
GLU
201
52.492
62.398
2.523
1.00
34.51


ATOM
1784
CG
GLU
201
52.407
61.131
1.648
1.00
34.40


ATOM
1785
CD
GLU
201
51.698
61.348
0.353
1.00
36.89


ATOM
1786
OE1
GLU
201
51.475
62.494
−0.017
1.00
40.24


ATOM
1787
OE2
GLU
201
51.344
60.361
−0.298
1.00
36.83


ATOM
1788
N
LYS
202
55.260
61.764
4.042
1.00
34.91


ATOM
1789
CA
LYS
202
56.499
61.051
4.256
1.00
35.18


ATOM
1790
C
LYS
202
56.511
60.265
5.589
1.00
34.53


ATOM
1791
O
LYS
202
56.870
59.085
5.584
1.00
33.52


ATOM
1792
CB
LYS
202
57.704
62.016
4.144
1.00
36.19


ATOM
1793
CG
LYS
202
58.953
61.532
4.837
1.00
36.45


ATOM
1794
CD
LYS
202
60.187
62.464
4.538
1.00
36.73


ATOM
1795
CE
LYS
202
61.352
62.086
5.420
1.00
38.08


ATOM
1796
NZ
LYS
202
62.094
60.862
5.001
1.00
38.27


ATOM
1797
N
TYR
203
56.132
60.924
6.695
1.00
34.14


ATOM
1798
CA
TYR
203
56.081
60.343
8.049
1.00
34.26


ATOM
1799
C
TYR
203
55.182
59.058
8.081
1.00
33.41


ATOM
1800
O
TYR
203
55.545
58.012
8.591
1.00
32.66


ATOM
1801
CB
TYR
203
55.507
61.380
9.034
1.00
34.85


ATOM
1802
CG
TYR
203
55.420
60.870
10.446
1.00
36.49


ATOM
1803
CD1
TYR
203
56.444
61.128
11.371
1.00
37.59


ATOM
1804
CD2
TYR
203
54.323
60.087
10.869
1.00
36.73


ATOM
1805
CE1
TYR
203
56.386
60.629
12.694
1.00
38.56


ATOM
1806
CE2
TYR
203
54.267
59.579
12.195
1.00
38.63


ATOM
1807
CZ
TYR
203
55.309
59.874
13.091
1.00
37.44


ATOM
1808
OH
TYR
203
55.280
59.398
14.372
1.00
40.73


ATOM
1809
N
VAL
204
54.002
59.204
7.518
1.00
32.56


ATOM
1810
CA
VAL
204
52.952
58.186
7.520
1.00
32.86


ATOM
1811
C
VAL
204
53.349
56.948
6.664
1.00
32.32


ATOM
1812
O
VAL
204
53.162
55.792
7.075
1.00
32.22


ATOM
1813
CB
VAL
204
51.675
58.966
7.117
1.00
33.17


ATOM
1814
CG1
VAL
204
50.933
58.449
5.882
1.00
33.70


ATOM
1815
CG2
VAL
204
50.855
59.467
8.375
1.00
31.96


ATOM
1816
N
THR
205
53.936
57.206
5.498
1.00
32.24


ATOM
1817
CA
THR
205
54.428
56.161
4.608
1.00
31.51


ATOM
1818
C
THR
205
55.481
55.291
5.321
1.00
31.55


ATOM
1819
O
THR
205
55.359
54.032
5.363
1.00
30.90


ATOM
1820
CB
THR
205
54.970
56.812
3.295
1.00
31.73


ATOM
1821
OG1
THR
205
53.875
57.474
2.591
1.00
30.86


ATOM
1822
CG2
THR
205
55.646
55.761
2.411
1.00
31.29


ATOM
1823
N
GLU
206
56.491
55.966
5.892
1.00
31.37


ATOM
1824
CA
GLU
206
57.593
55.325
6.652
1.00
32.61


ATOM
1825
C
GLU
206
57.142
54.659
7.949
1.00
32.07


ATOM
1826
O
GLU
206
57.573
53.565
8.226
1.00
31.97


ATOM
1827
CB
GLU
206
58.753
56.297
6.930
1.00
32.31


ATOM
1828
CG
GLU
206
59.419
56.801
5.654
1.00
33.50


ATOM
1829
CD
GLU
206
60.435
57.936
5.897
1.00
34.50


ATOM
1830
OE1
GLU
206
60.604
58.380
7.066
1.00
38.19


ATOM
1831
OE2
GLU
206
61.035
58.388
4.917
1.00
31.10


ATOM
1832
N
LYS
207
56.281
55.310
8.721
1.00
31.90


ATOM
1833
CA
LYS
207
55.750
54.708
9.952
1.00
32.07


ATOM
1834
C
LYS
207
55.029
53.371
9.645
1.00
32.17


ATOM
1835
O
LYS
207
55.321
52.339
10.253
1.00
32.06


ATOM
1836
CB
LYS
207
54.804
55.688
10.670
1.00
32.80


ATOM
1837
CG
LYS
207
54.356
55.265
12.090
1.00
36.71


ATOM
1838
CD
LYS
207
55.577
54.891
12.935
1.00
43.40


ATOM
1839
CE
LYS
207
55.461
55.312
14.453
1.00
46.89


ATOM
1840
NZ
LYS
207
56.763
55.097
15.135
1.00
47.00


ATOM
1841
N
ALA
208
54.094
53.390
8.690
1.00
30.86


ATOM
1842
CA
ALA
208
53.376
52.163
8.340
1.00
30.32


ATOM
1843
C
ALA
208
54.366
51.055
7.984
1.00
30.56


ATOM
1844
O
ALA
208
54.272
49.920
8.483
1.00
29.36


ATOM
1845
CB
ALA
208
52.364
52.415
7.163
1.00
28.98


ATOM
1846
N
TYR
209
55.321
51.403
7.116
1.00
31.34


ATOM
1847
CA
TYR
209
56.333
50.475
6.618
1.00
32.07


ATOM
1848
C
TYR
209
57.240
49.938
7.739
1.00
32.83


ATOM
1849
O
TYR
209
57.700
48.783
7.691
1.00
32.54


ATOM
1850
CB
TYR
209
57.154
51.167
5.554
1.00
32.73


ATOM
1851
CG
TYR
209
58.158
50.285
4.853
1.00
33.75


ATOM
1852
CD1
TYR
209
57.787
49.556
3.703
1.00
34.84


ATOM
1853
CD2
TYR
209
59.483
50.197
5.299
1.00
33.51


ATOM
1854
CE1
TYR
209
58.718
48.758
3.031
1.00
34.86


ATOM
1855
CE2
TYR
209
60.438
49.371
4.623
1.00
34.90


ATOM
1856
CZ
TYR
209
60.032
48.661
3.486
1.00
33.05


ATOM
1857
OH
TYR
209
60.932
47.845
2.791
1.00
35.66


ATOM
1858
N
GLU
210
57.463
50.754
8.762
1.00
34.05


ATOM
1859
CA
GLU
210
58.206
50.296
9.956
1.00
34.62


ATOM
1860
C
GLU
210
57.331
49.457
10.902
1.00
35.41


ATOM
1861
O
GLU
210
57.848
48.791
11.824
1.00
34.97


ATOM
1862
CB
GLU
210
58.758
51.496
10.696
1.00
35.86


ATOM
1863
CG
GLU
210
59.770
52.335
9.883
1.00
36.13


ATOM
1864
CD
GLU
210
59.917
53.774
10.388
1.00
38.52


ATOM
1865
OE1
GLU
210
59.209
54.198
11.326
1.00
38.33


ATOM
1866
OE2
GLU
210
60.761
54.497
9.805
1.00
40.89


ATOM
1867
N
ASN
211
56.010
49.495
10.701
1.00
34.65


ATOM
1868
CA
ASN
211
55.071
48.805
11.625
1.00
35.17


ATOM
1869
C
ASN
211
54.033
47.949
10.929
1.00
33.23


ATOM
1870
O
ASN
211
52.844
48.101
11.179
1.00
34.24


ATOM
1871
CB
ASN
211
54.387
49.764
12.597
1.00
35.24


ATOM
1872
CG
ASN
211
55.388
50.549
13.414
1.00
38.14


ATOM
1873
OD1
ASN
211
55.927
51.587
12.954
1.00
41.46


ATOM
1874
ND2
ASN
211
55.681
50.053
14.617
1.00
36.20


ATOM
1875
N
PRO
212
54.503
46.993
10.110
1.00
32.10


ATOM
1876
CA
PRO
212
53.583
46.146
9.385
1.00
31.76


ATOM
1877
C
PRO
212
52.823
45.257
10.356
1.00
31.38


ATOM
1878
O
PRO
212
53.380
44.787
11.353
1.00
30.16


ATOM
1879
CB
PRO
212
54.490
45.317
8.486
1.00
30.78


ATOM
1880
CG
PRO
212
55.845
45.286
9.224
1.00
31.04


ATOM
1881
CD
PRO
212
55.922
46.619
9.893
1.00
31.09


ATOM
1882
N
LYS
213
51.562
45.014
10.036
1.00
30.99


ATOM
1883
CA
LYS
213
50.761
44.074
10.818
1.00
31.42


ATOM
1884
C
LYS
213
49.766
43.348
9.955
1.00
31.15


ATOM
1885
O
LYS
213
49.074
43.953
9.116
1.00
31.01


ATOM
1886
CB
LYS
213
49.986
44.817
11.911
1.00
30.59


ATOM
1887
CG
LYS
213
50.911
45.403
12.959
1.00
29.40


ATOM
1888
CD
LYS
213
50.177
45.708
14.282
1.00
27.87


ATOM
1889
CE
LYS
213
51.127
46.400
15.275
1.00
29.06


ATOM
1890
NZ
LYS
213
50.269
46.947
16.416
1.00
29.60


ATOM
1891
N
PHE
214
49.736
42.040
10.165
1.00
31.08


ATOM
1892
CA
PHE
214
48.631
41.188
9.699
1.00
31.02


ATOM
1893
C
PHE
214
47.336
41.569
10.398
1.00
29.28


ATOM
1894
O
PHE
214
47.336
42.220
11.486
1.00
28.86


ATOM
1895
CB
PHE
214
48.962
39.705
10.011
1.00
31.33


ATOM
1896
CG
PHE
214
50.110
39.147
9.193
1.00
33.17


ATOM
1897
CD1
PHE
214
50.029
39.089
7.785
1.00
34.17


ATOM
1898
CD2
PHE
214
51.254
38.643
9.826
1.00
31.80


ATOM
1899
CE1
PHE
214
51.118
38.572
7.014
1.00
36.33


ATOM
1900
CE2
PHE
214
52.323
38.129
9.087
1.00
32.91


ATOM
1901
CZ
PHE
214
52.258
38.077
7.665
1.00
33.95


ATOM
1902
N
VAL
215
46.226
41.151
9.796
1.00
27.85


ATOM
1903
CA
VAL
215
44.911
41.312
10.377
1.00
28.62


ATOM
1904
C
VAL
215
44.878
40.607
11.762
1.00
28.57


ATOM
1905
O
VAL
215
44.295
41.140
12.682
1.00
27.90


ATOM
1906
CB
VAL
215
43.749
40.901
9.352
1.00
28.94


ATOM
1907
CG1
VAL
215
43.721
39.402
9.060
1.00
29.40


ATOM
1908
CG2
VAL
215
42.428
41.347
9.813
1.00
29.76


ATOM
1909
N
GLU
216
45.546
39.450
11.872
1.00
28.34


ATOM
1910
CA
GLU
216
45.735
38.652
13.131
1.00
29.82


ATOM
1911
C
GLU
216
46.364
39.490
14.235
1.00
28.79


ATOM
1912
O
GLU
216
45.822
39.619
15.311
1.00
28.87


ATOM
1913
CB
GLU
216
46.608
37.400
12.835
1.00
28.86


ATOM
1914
CG
GLU
216
45.872
36.385
11.934
1.00
32.94


ATOM
1915
CD
GLU
216
46.306
36.426
10.455
1.00
34.70


ATOM
1916
OE1
GLU
216
46.537
37.517
9.914
1.00
35.44


ATOM
1917
OE2
GLU
216
46.400
35.347
9.820
1.00
37.76


ATOM
1918
N
ASP
217
47.483
40.117
13.892
1.00
29.08


ATOM
1919
CA
ASP
217
48.235
41.031
14.751
1.00
28.86


ATOM
1920
C
ASP
217
47.386
42.185
15.203
1.00
28.38


ATOM
1921
O
ASP
217
47.338
42.504
16.408
1.00
27.02


ATOM
1922
CB
ASP
217
49.437
41.570
14.000
1.00
29.76


ATOM
1923
CG
ASP
217
50.398
40.501
13.603
1.00
31.99


ATOM
1924
OD1
ASP
217
50.489
39.492
14.298
1.00
38.26


ATOM
1925
OD2
ASP
217
51.084
40.654
12.591
1.00
34.15


ATOM
1926
N
MET
218
46.696
42.831
14.261
1.00
28.36


ATOM
1927
CA
MET
218
45.812
43.928
14.647
1.00
29.64


ATOM
1928
C
MET
218
44.706
43.558
15.656
1.00
28.41


ATOM
1929
O
MET
218
44.492
44.275
16.636
1.00
26.63


ATOM
1930
CB
MET
218
45.176
44.629
13.422
1.00
30.96


ATOM
1931
CG
MET
218
44.319
45.845
13.861
1.00
35.70


ATOM
1932
SD
MET
218
45.273
47.280
14.514
1.00
45.47


ATOM
1933
CE
MET
218
46.456
47.370
13.190
1.00
46.95


ATOM
1934
N
VAL
219
43.962
42.479
15.405
1.00
28.22


ATOM
1935
CA
VAL
219
42.869
42.158
16.337
1.00
28.10


ATOM
1936
C
VAL
219
43.427
41.730
17.690
1.00
27.11


ATOM
1937
O
VAL
219
42.857
42.078
18.725
1.00
27.29


ATOM
1938
CB
VAL
219
41.773
41.161
15.749
1.00
28.69


ATOM
1939
CG1
VAL
219
41.164
41.775
14.457
1.00
29.54


ATOM
1940
CG2
VAL
219
42.347
39.777
15.445
1.00
27.60


ATOM
1941
N
ARG
220
44.529
40.996
17.692
1.00
27.25


ATOM
1942
CA
ARG
220
45.171
40.580
18.986
1.00
29.06


ATOM
1943
C
ARG
220
45.667
41.777
19.743
1.00
28.85


ATOM
1944
O
ARG
220
45.464
41.835
20.955
1.00
30.55


ATOM
1945
CB
ARG
220
46.331
39.599
18.797
1.00
27.73


ATOM
1946
CG
ARG
220
45.901
38.148
18.483
1.00
29.78


ATOM
1947
CD
ARG
220
47.100
37.326
17.937
1.00
29.72


ATOM
1948
NE
ARG
220
46.730
35.926
18.068
1.00
33.92


ATOM
1949
CZ
ARG
220
47.200
34.943
17.324
1.00
32.61


ATOM
1950
NH1
ARG
220
48.094
35.206
16.410
1.00
33.13


ATOM
1951
NH2
ARG
220
46.761
33.695
17.514
1.00
34.32


ATOM
1952
N
ASP
221
46.313
42.708
19.036
1.00
28.07


ATOM
1953
CA
ASP
221
46.889
43.949
19.662
1.00
28.23


ATOM
1954
C
ASP
221
45.801
44.821
20.281
1.00
27.79


ATOM
1955
O
ASP
221
45.901
45.267
21.453
1.00
28.28


ATOM
1956
CB
ASP
221
47.746
44.723
18.645
1.00
27.76


ATOM
1957
CG
ASP
221
49.112
44.102
18.449
1.00
29.80


ATOM
1958
OD1
ASP
221
49.405
43.111
19.147
1.00
30.61


ATOM
1959
OD2
ASP
221
49.902
44.570
17.583
1.00
32.40


ATOM
1960
N
VAL
222
44.730
45.062
19.532
1.00
25.93


ATOM
1961
CA
VAL
222
43.588
45.761
20.109
1.00
25.63


ATOM
1962
C
VAL
222
42.893
45.003
21.279
1.00
26.39


ATOM
1963
O
VAL
222
42.539
45.632
22.285
1.00
26.70


ATOM
1964
CB
VAL
222
42.517
46.148
19.058
1.00
24.90


ATOM
1965
CG1
VAL
222
41.313
46.799
19.773
1.00
25.51


ATOM
1966
CG2
VAL
222
43.098
47.111
18.028
1.00
24.07


ATOM
1967
N
ALA
223
42.664
43.688
21.126
1.00
25.77


ATOM
1968
CA
ALA
223
41.954
42.885
22.148
1.00
26.96


ATOM
1969
C
ALA
223
42.728
42.901
23.503
1.00
27.41


ATOM
1970
O
ALA
223
42.141
42.971
24.555
1.00
27.99


ATOM
1971
CB
ALA
223
41.761
41.444
21.674
1.00
24.19


ATOM
1972
N
THR
224
44.042
42.841
23.440
1.00
29.50


ATOM
1973
CA
THR
224
44.885
42.923
24.635
1.00
30.83


ATOM
1974
C
THR
224
44.640
44.257
25.358
1.00
31.18


ATOM
1975
O
THR
224
44.426
44.267
26.568
1.00
31.47


ATOM
1976
CB
THR
224
46.353
42.749
24.266
1.00
31.10


ATOM
1977
OG1
THR
224
46.515
41.480
23.611
1.00
32.84


ATOM
1978
CG2
THR
224
47.176
42.692
25.503
1.00
32.78


ATOM
1979
N
SER
225
44.589
45.359
24.612
1.00
31.19


ATOM
1980
CA
SER
225
44.306
46.698
25.208
1.00
32.14


ATOM
1981
C
SER
225
42.957
46.770
25.930
1.00
31.64


ATOM
1982
O
SER
225
42.830
47.374
26.990
1.00
32.34


ATOM
1983
CB
SER
225
44.323
47.764
24.141
1.00
32.10


ATOM
1984
OG
SER
225
45.639
48.071
23.727
1.00
33.71


ATOM
1985
N
LEU
226
41.937
46.157
25.346
1.00
31.46


ATOM
1986
CA
LEU
226
40.571
46.154
25.908
1.00
31.10


ATOM
1987
C
LEU
226
40.437
45.228
27.121
1.00
31.71


ATOM
1988
O
LEU
226
39.721
45.552
28.084
1.00
31.22


ATOM
1989
CB
LEU
226
39.570
45.678
24.815
1.00
30.41


ATOM
1990
CG
LEU
226
39.527
46.532
23.517
1.00
28.65


ATOM
1991
CD1
LEU
226
38.528
45.947
22.550
1.00
26.39


ATOM
1992
CD2
LEU
226
39.099
47.926
23.861
1.00
26.47


ATOM
1993
N
ILE
227
41.083
44.063
27.053
1.00
32.52


ATOM
1994
CA
ILE
227
41.131
43.158
28.223
1.00
34.66


ATOM
1995
C
ILE
227
41.711
43.844
29.449
1.00
34.68


ATOM
1996
O
ILE
227
41.198
43.695
30.533
1.00
36.02


ATOM
1997
CB
ILE
227
41.928
41.865
27.959
1.00
35.04


ATOM
1998
CG1
ILE
227
41.168
41.012
26.956
1.00
34.54


ATOM
1999
CG2
ILE
227
42.124
41.094
29.307
1.00
35.53


ATOM
2000
CD1
ILE
227
42.062
40.002
26.261
1.00
35.14


ATOM
2001
N
ALA
228
42.764
44.612
29.247
1.00
35.83


ATOM
2002
CA
ALA
228
43.345
45.463
30.266
1.00
36.33


ATOM
2003
C
ALA
228
42.442
46.607
30.810
1.00
36.87


ATOM
2004
O
ALA
228
42.849
47.311
31.733
1.00
36.87


ATOM
2005
CB
ALA
228
44.625
46.053
29.715
1.00
35.72


ATOM
2006
N
ASP
229
41.284
46.864
30.200
1.00
36.77


ATOM
2007
CA
ASP
229
40.461
47.966
30.644
1.00
37.00


ATOM
2008
C
ASP
229
39.408
47.270
31.459
1.00
38.22


ATOM
2009
O
ASP
229
38.582
46.528
30.903
1.00
37.95


ATOM
2010
CB
ASP
229
39.842
48.724
29.446
1.00
36.82


ATOM
2011
CG
ASP
229
39.075
49.993
29.856
1.00
35.61


ATOM
2012
OD1
ASP
229
38.303
49.990
30.845
1.00
32.28


ATOM
2013
OD2
ASP
229
39.234
51.020
29.166
1.00
36.47


ATOM
2014
N
GLU
240
38.629
44.311
9.090
1.00
26.04


ATOM
2015
CA
GLU
240
38.563
43.980
7.677
1.00
25.79


ATOM
2016
C
GLU
240
39.604
44.840
6.918
1.00
26.33


ATOM
2017
O
GLU
240
39.581
46.097
7.008
1.00
26.15


ATOM
2018
CB
GLU
240
37.133
44.231
7.133
1.00
25.72


ATOM
2019
CG
GLU
240
36.967
43.804
5.663
1.00
25.21


ATOM
2020
CD
GLU
240
35.532
43.825
5.146
1.00
26.43


ATOM
2021
OE1
GLU
240
34.604
44.177
5.902
1.00
27.62


ATOM
2022
OE2
GLU
240
35.322
43.447
3.967
1.00
26.61


ATOM
2023
N
ASN
241
40.534
44.181
6.207
1.00
26.14


ATOM
2024
CA
ASN
241
41.553
44.895
5.458
1.00
25.32


ATOM
2025
C
ASN
241
41.235
44.729
3.974
1.00
25.25


ATOM
2026
O
ASN
241
41.123
43.594
3.494
1.00
23.38


ATOM
2027
CB
ASN
241
42.918
44.340
5.756
1.00
26.66


ATOM
2028
CG
ASN
241
43.291
44.453
7.253
1.00
29.90


ATOM
2029
OD1
ASN
241
44.408
44.107
7.640
1.00
36.12


ATOM
2030
ND2
ASN
241
42.386
44.967
8.072
1.00
27.28


ATOM
2031
N
PHE
242
41.063
45.856
3.277
1.00
23.13


ATOM
2032
CA
PHE
242
40.624
45.872
1.896
1.00
24.91


ATOM
2033
C
PHE
242
41.842
45.651
1.023
1.00
25.54


ATOM
2034
O
PHE
242
42.315
46.569
0.388
1.00
25.14


ATOM
2035
CB
PHE
242
39.830
47.161
1.586
1.00
24.91


ATOM
2036
CG
PHE
242
38.557
47.241
2.379
1.00
25.60


ATOM
2037
CD1
PHE
242
37.410
46.596
1.922
1.00
26.78


ATOM
2038
CD2
PHE
242
38.544
47.850
3.650
1.00
25.71


ATOM
2039
CE1
PHE
242
36.201
46.620
2.691
1.00
29.47


ATOM
2040
CE2
PHE
242
37.364
47.835
4.469
1.00
24.56


ATOM
2041
CZ
PHE
242
36.193
47.246
3.984
1.00
26.86


ATOM
2042
N
GLU
243
42.356
44.415
1.066
1.00
25.28


ATOM
2043
CA
GLU
243
43.638
44.037
0.503
1.00
27.20


ATOM
2044
C
GLU
243
43.891
44.706
−0.844
1.00
26.88


ATOM
2045
O
GLU
243
43.133
44.481
−1.776
1.00
27.26


ATOM
2046
CB
GLU
243
43.754
42.513
0.342
1.00
28.44


ATOM
2047
CG
GLU
243
43.600
41.751
1.660
1.00
30.04


ATOM
2048
CD
GLU
243
44.744
42.094
2.585
1.00
32.00


ATOM
2049
OE1
GLU
243
44.617
43.037
3.389
1.00
30.26


ATOM
2050
OE2
GLU
243
45.815
41.476
2.446
1.00
35.21


ATOM
2051
N
SER
244
44.962
45.494
−0.945
1.00
27.02


ATOM
2052
CA
SER
244
45.160
46.296
−2.185
1.00
27.90


ATOM
2053
C
SER
244
45.582
45.442
−3.363
1.00
28.54


ATOM
2054
O
SER
244
45.551
45.912
−4.525
1.00
29.90


ATOM
2055
CB
SER
244
46.139
47.432
−1.959
1.00
26.85


ATOM
2056
OG
SER
244
47.413
46.896
−1.761
1.00
25.99


ATOM
2057
N
ILE
245
45.936
44.178
−3.097
1.00
28.99


ATOM
2058
CA
ILE
245
46.325
43.247
−4.192
1.00
28.75


ATOM
2059
C
ILE
245
45.263
42.207
−4.615
1.00
28.22


ATOM
2060
O
ILE
245
45.454
41.447
−5.589
1.00
28.72


ATOM
2061
CB
ILE
245
47.619
42.490
−3.832
1.00
28.52


ATOM
2062
CG1
ILE
245
47.395
41.571
−2.619
1.00
27.33


ATOM
2063
CG2
ILE
245
48.795
43.496
−3.645
1.00
26.82


ATOM
2064
CD1
ILE
245
48.584
40.521
−2.445
1.00
28.82


ATOM
2065
N
HIS
246
44.184
42.145
−3.849
1.00
27.14


ATOM
2066
CA
HIS
246
43.062
41.280
−4.132
1.00
26.06


ATOM
2067
C
HIS
246
41.827
42.109
−4.349
1.00
26.53


ATOM
2068
O
HIS
246
41.870
43.350
−4.164
1.00
25.05


ATOM
2069
CB
HIS
246
42.806
40.379
−2.962
1.00
26.37


ATOM
2070
CG
HIS
246
43.931
39.463
−2.686
1.00
27.22


ATOM
2071
ND1
HIS
246
44.492
39.344
−1.432
1.00
29.18


ATOM
2072
CD2
HIS
246
44.608
38.617
−3.496
1.00
26.14


ATOM
2073
CE1
HIS
246
45.470
38.459
−1.482
1.00
27.29


ATOM
2074
NE2
HIS
246
45.572
38.011
−2.722
1.00
28.61


ATOM
2075
N
ASN
247
40.747
41.438
−4.800
1.00
25.55


ATOM
2076
CA
ASN
247
39.419
42.091
−4.806
1.00
25.30


ATOM
2077
C
ASN
247
38.497
41.540
−3.718
1.00
25.63


ATOM
2078
O
ASN
247
37.262
41.603
−3.835
1.00
24.99


ATOM
2079
CB
ASN
247
38.719
42.052
−6.211
1.00
24.56


ATOM
2080
CG
ASN
247
37.661
43.139
−6.348
1.00
25.15


ATOM
2081
OD1
ASN
247
37.853
44.249
−5.856
1.00
27.25


ATOM
2082
ND2
ASN
247
36.531
42.826
−6.973
1.00
25.75


ATOM
2083
N
HIS
248
39.094
41.004
−2.644
1.00
24.93


ATOM
2084
CA
HIS
248
38.331
40.606
−1.484
1.00
24.20


ATOM
2085
C
HIS
248
39.165
41.050
−0.265
1.00
24.68


ATOM
2086
O
HIS
248
40.280
41.561
−0.416
1.00
23.64


ATOM
2087
CB
HIS
248
38.116
39.080
−1.470
1.00
24.81


ATOM
2088
CG
HIS
248
39.397
38.297
−1.527
1.00
22.23


ATOM
2089
ND1
HIS
248
40.078
37.886
−0.404
1.00
26.19


ATOM
2090
CD2
HIS
248
40.115
37.849
−2.579
1.00
22.16


ATOM
2091
CE1
HIS
248
41.186
37.259
−0.757
1.00
21.82


ATOM
2092
NE2
HIS
248
41.208
37.186
−2.077
1.00
24.48


ATOM
2093
N
SER
249
38.626
40.823
0.930
1.00
24.78


ATOM
2094
CA
SER
249
39.213
41.375
2.180
1.00
24.32


ATOM
2095
C
SER
249
39.808
40.290
3.013
1.00
24.05


ATOM
2096
O
SER
249
39.310
39.195
2.945
1.00
25.10


ATOM
2097
CB
SER
249
38.100
42.059
2.967
1.00
23.81


ATOM
2098
OG
SER
249
37.687
43.271
2.322
1.00
24.81


ATOM
2099
N
ALA
250
40.875
40.574
3.763
1.00
24.15


ATOM
2100
CA
ALA
250
41.299
39.754
4.900
1.00
24.78


ATOM
2101
C
ALA
250
40.460
40.198
6.086
1.00
25.30


ATOM
2102
O
ALA
250
40.141
41.384
6.212
1.00
25.56


ATOM
2103
CB
ALA
250
42.799
39.978
5.181
1.00
25.32


ATOM
2104
N
TYR
251
40.095
39.261
6.971
1.00
24.61


ATOM
2105
CA
TYR
251
39.171
39.541
8.041
1.00
24.59


ATOM
2106
C
TYR
251
39.481
38.699
9.294
1.00
25.35


ATOM
2107
O
TYR
251
39.807
37.517
9.169
1.00
25.44


ATOM
2108
CB
TYR
251
37.739
39.228
7.534
1.00
25.31


ATOM
2109
CG
TYR
251
36.650
39.348
8.575
1.00
24.55


ATOM
2110
CD1
TYR
251
36.232
40.589
9.035
1.00
23.76


ATOM
2111
CD2
TYR
251
36.033
38.192
9.120
1.00
27.05


ATOM
2112
CE1
TYR
251
35.218
40.706
10.015
1.00
23.94


ATOM
2113
CE2
TYR
251
35.009
38.299
10.113
1.00
26.38


ATOM
2114
CZ
TYR
251
34.626
39.548
10.547
1.00
25.70


ATOM
2115
OH
TYR
251
33.644
39.657
11.508
1.00
30.46


ATOM
2116
N
ALA
252
39.332
39.252
10.484
1.00
25.78


ATOM
2117
CA
ALA
252
39.476
38.425
11.698
1.00
26.50


ATOM
2118
C
ALA
252
38.616
38.996
12.773
1.00
27.38


ATOM
2119
O
ALA
252
38.245
40.160
12.707
1.00
27.79


ATOM
2120
CB
ALA
252
40.915
38.388
12.137
1.00
25.42


ATOM
2121
MN
MN2
258
50.065
40.444
1.837
1.00
31.39


ATOM
2122
N1
AZI
261
48.108
38.620
2.111
0.50
29.51


ATOM
2123
N2
AZI
261
47.484
38.074
1.282
0.50
23.78


ATOM
2124
N3
AZI
261
47.000
37.552
0.349
0.50
33.34


TER











ENDMDL









Example 10
Metal Dependencies of GCYH-IB
Enzyme Activity Assays: All chemicals were of analytical, metal-free grade from Sigma or Fisher. All solutions were prepared with Milli-Q water (18.2 MΩ) and treated with Chelex-100 (BioRad) to remove contaminating metals. Glassware were soaked in nitric acid (10%), then EDTA (5 mM) and rinsed liberally with Chelex-treated Milli-Q water before use. Activity assays were conducted as described previously (El Yacoubi et al, 2006) using either variable concentrations of metal or EDTA (5 mM), and 0.1 mM GTP.
Apoenzyme Preparation: Metal ions were removed from B. subtilis and N. gonorrhoeae GCYH-IB by incubating the purified, recombinant protein (0.5 ml) with EDTA (5 mM, 1 hr, 21° C.) followed by dialysis thrice against a 4-liter solution of Tris-HCl (50 mM, pH 8.0), KCl (50 mM), EDTA (5 mM) and a few grams of Chelex-100. The resulting apoenzyme was dialyzed thrice against 3 L of Tris-HCl (50 mM, pH 8.0), KCl (50 mM), and Chelex-100 to remove EDTA and passed through Chelex-100 resin (5 ml protein solution per 3 ml resin) prior to activity assays. Protein concentrations were determined spectrophotometrically.
Metal Activation Studies: The B. subtilis apoenzyme (2 μM) was incubated with varying concentrations (0.1 μM-4 mM) of metal chlorides (MnCl2, ZnCl2, MgCl2, NiCl2, CaCl2, CdCl2, CoCl2, CuCl2, CoCl3, FeCl3) or Fe(SO4) in standard buffer (100 mM HEPES, pH 8.0, 100 mM KCl) for 10 min at 37 C, and assayed for activity as described above. All assays involving Fe2+ were conducted in an anaerobic chamber with degassed and N2-purged buffers.
Reconstitution of N. gonorrhoeae GCYH-IB with Mn: The apoenzyme was incubated in the presence of 2-7 molar equivalents of MnCl2 in standard buffer containing 2 mM DTT for 60 min at 25° C. Loosely bound metal was removed either by dialysis twice against Tris-HCl (50 mM, pH 8.0), KCl (50 mM) and DTT (1 mM) for 4 hr at 4° C., filtration on a Sephadex G-25 column, or extensive washing with buffer in an Amicon ultra-centrifugal device. The enzyme was assayed for activity as described above and the metal content analyzed by ICP-MS.
Example 11
Zinc-Dependent Regulation of GCYH-IB
Bioinformatics: Analysis of the folE/folE2 gene distribution was performed using the SEED annotation environment. The results of the analysis are provided by Table I. Candidate Zur binding sites were identified using the Genome Explorer software (Mironov et al., 2000) by scanning bacterial genomes with two PWMs constructed using the training sets of two different sets of known Zur binding sites in proteobacteria and firmicutes. Panina et al. 100 Proc. Natl. Acad. Sci. USA, 9912-9917 (2003).
B. subtilis strain construction and growth conditions: All strains were derived from the B. subtilis 168 trpc2attSPβwild-type strain, CU1065, and were grown in LB. Growth curves were done using a Bioscreen CMBR system for 24 hours with OD600 measurements every 10 min. Liquid overnight cultures with antibiotics were used to start pre-cultures that were diluted at mid-log to a normalized OD600 of 0.01 in a volume of 200 μl in a 100-well honeycomb microtiter plate at which point the growth curve was started. Cultures were incubated at 37° C. with shaking at 200 rpm. For selection, antibiotics were added at the following concentrations: erythromycin (1 μg/ml) and lincomycin (25 μg/ml) (for selecting for macrolide-lincosamide-streptogramin B resistance), spectinomycin (100 μg/ml), kanamycin (15 μg/ml).
Mutants in folE, folE2 and zur were constructed using long-flanking-homology polymerase chain reaction (LFH-PCR) as previously described (Butcher & Helmann, 2006). LFH-PCR and chromosomal DNA transformation were used to generate strains expressing various combinations of GCYH-I enzymes. Specifically, strain HB6788 CU1065folE::mls) lacks GCYH-IA while its GCYH-IB is repressed, but its gene is still present (designated ΔfolE). This strain was used for construction of other strains. Strain HB6791 (CU1065 folE::mls zur::kan) expresses only GCYH-IB (designated ΔfolE Δzur). Strain HB6852 (CU1065 folE::mls zur::kan folE2::spc) lacks both GCYH-I isozymes (designated ΔfolE Δzur ΔfolE2).

## Claims

1. A crystal of a GTP Cyclohydrolase Type-IB (GCYH-IB) polypeptide, wherein the GCYH-IB polypeptide comprises the amino acid sequence of SEQ ID NO: 8, wherein the GCYH-IB crystal is characterized by space group C2221 and unit cell dimension values: a=91.7 Å; b=100.3 Å; and c=114.1 Å.

2. A crystal of a GCYH-IB polypeptide in complex with Mn2+ (GCYH-IB.Mn2+), wherein the GCYH-IB polypeptide comprises the amino acid sequence of SEQ ID NO: 8, wherein the GCYH-IB.Mn2+ crystal is characterized by space group C2221 and unit cell dimension values: a=92.2 Å; b=100.4 Å; and c=113.9 Å.

3. A method of preparing a crystal of a GCYH-IB polypeptide, comprising the steps of:
a) preparing a crystallizable composition that comprises a solution comprising: a selenomethionine (SeMet)-labeled GCYH-IB polypeptide that comprises the amino acid sequence of SEQ ID NO: 8; 10-16% polyethylene glycol 6000; 1-1.4 M LiCl; 50 mM Tris buffer, pH 9.0; and 50 mM Tris-HCl buffer, pH 7.0,
b) subjecting the crystallizable composition to conditions which promote crystallization, and
c) obtaining a crystal having space group C2221 and the unit cell dimension values: a=91.7 Å; b=100.3 Å; and c=114.1 Å.

4. The method of claim 3, wherein the SeMet-labeled GCYH-IB polypeptide is added to the crystallizable composition from a solution comprising 9 mg/ml of SeMet-labeled GCYH-IB polypeptide, 50 mM Tris-Acetate, 100 mM KCl, and 5 mM 2-mercaptoethanol (BME), and wherein the solution has a pH of 8.0.

5. A method of preparing a crystal of a GCYH-IB polypeptide in complex with Mn2+ (GCYH-IB.Mn2+), comprising the steps of:
a) preparing a crystallizable composition that comprises a solution comprising: a GCYH-IB polypeptide that comprises the amino acid sequence of SEQ ID NO: 8; 10-16% polyethylene glycol 6000; 1-1.4 M LiCl; 50 mM Tris buffer, pH 9.0; 50 mM Tris-HCl buffer, pH 7.0; and MnCl2,
b) subjecting the crystallizable composition to conditions which promote crystallization, and
c) obtaining a crystal that forms in space group C2221 and the unit cell dimension values: a=92.2 Å; b=100.4 Å; and c=113.9 Å.

6. The method of claim 5, wherein the GCYH-IB polypeptide is added to the crystallizable composition from a solution comprising 10 mg/ml of GCYH-IB polypeptide, 50 mM Tris-HCl, 50 mM KCl, and 1 mM dithiothreitol (DTT), and 1 to 10 mM MnCl2, and wherein the solution has a pH of 8.0.