# Patent

## Title
Anti-bacterial drug targeting of genome maintenance interfaces

## Abstract

The present invention provides methods for the design and identification of novel antimicrobial compounds, and provides antimicrobial compounds identified using these methods. These antimicrobial compounds inhibit the binding of a prokaryotic single-stranded DNA binding protein to a polypeptide that binds to the prokaryotic single-stranded DNA binding protein. In some examples, the prokaryotic single-stranded DNA binding protein is prokaryotic Exonuclease I. In one embodiment, the antimicrobial compound has the structure




    
    
        wherein Y is selected from the group consisting of CH2, O, and NH,
        R1 is selected from the group consisting of H, F, Cl, Br, and I,
        R2 is selected from the group consisting of H and CF3,
        R3 is selected from the group consisting of H and CO2H,
        R4 is selected from the group consisting of H and OH, and
        R5 is selected from the group consisting of H, alkoxy, and NO2.

## Background
CROSS-REFERENCE TO RELATED APPLICATIONS
This invention claims priority to U.S. Provisional Patent Application Ser. No. 60/931,411, filed May 22, 2007, which is herein incorporated by reference.


GOVERNMENT INTERESTS
This invention was made with United States government support awarded by the National Institutes of Health, grant No. GM068061. The United States government has certain rights in this invention.


FIELD OF THE INVENTION
The present invention relates generally to the field of screening for novel antimicrobial compounds.
BACKGROUND
Antibiotic resistant strains of bacteria as well as emerging bacterial pathogens pose a growing threat to world health, and the development of antibiotics necessary to counter these threats has dramatically slowed over the previous decades, leaving the population more vulnerable to these risks (Katz et al., 2006, Nat. Biotech. 24: 1529-1531; Payne et al., 2007, Nat. Rev. Drug Discovery 6: 29-40). Most newly developed antibiotics merely target one of the proven vulnerable pathways previously exploited by prior generations of antibiotics. While these drugs are effective, resistance to them is rising at an alarming rate, suggesting the need for antibiotics that target additional bacterial molecules or cellular processes.
Single-stranded DNA-binding proteins (SSBs) in bacteria form essential intermolecular complexes with at least a dozen other DNA replication, DNA recombination, and DNA repair proteins (Molineux and Gefter, 1975, J. Mol. Biol. 98: 811-825; Butland et al., 2005, Nature 433: 531-537). In addition, SSB proteins play important organizational roles through their interactions with many different genome maintenance proteins. Several, if not all, of these interactions are known to be mediated by the carboxy-terminal-most 8-10 residues from SSB, which form a peptide sequence that is highly conserved among bacterial SSBs but is not found in eukaryotic SSBs (Sandigursky et al., 1996, Radiation Res. 145: 619-623; Curth et al., 1996, Nucleic Acids Res. 24: 2706-2711; Genschel et al., 2000, Biol. Chem. 381: 183-192). Previous studies have shown that mutations within, or deletions of, this interaction sequence from SSB, have drastic effects on bacterial viability, indicating that formation of proper protein interactions with this site is critical for bacterial growth.
SSBs are a conserved protein family found throughout all forms of life, playing a variety of essential roles in nearly all aspects of DNA metabolism. SSBs bind and protect sensitive single-stranded DNA (ssDNA) intermediates that occur during DNA replication, recombination, and repair. SSBs recruit genome maintenance proteins to ssDNA, and play instrumental regulatory roles in ssDNA degradation, replication initiation, initiation of homologous recombination, relaxation of supercoiled DNA, and numerous other genome maintenance processes. Deletions of SSBs have been shown to be lethal and since all known SSBs play similar roles in cells, finding compounds that inhibit bacterial SSBs could have similar effects on eukaryotic cells.
BRIEF SUMMARY
It has been discovered that interfaces involving SSBs may be used as targets to generate promising new classes of antimicrobial compounds. Methods are provided that include reacting polypeptides comprising prokaryotic single-stranded DNA binding proteins, polypeptides that bind to the prokaryotic single-stranded DNA binding proteins, and candidate compounds, and assaying for binding of the polypeptides comprising the prokaryotic single-stranded DNA binding proteins to the polypeptides that bind to the prokaryotic single-stranded DNA binding proteins, where a decrease in binding, relative to the binding of the polypeptides comprising the prokaryotic single-stranded DNA binding proteins to the polypeptides that bind to the prokaryotic single-stranded DNA binding proteins in absence of the candidate compounds, identifies the candidate compounds as antimicrobial compounds. In the practice of the methods, the polypeptides comprising the prokaryotic single-stranded DNA binding proteins may include carboxy-tails that are at least 90% identical to the carboxy-tails of the polypeptides with an amino acid sequence of SEQ ID NO:2, or to the carboxy-tails of the polypeptides with an amino acid sequence of SEQ ID NO:2 having 1 to 4 conservative amino acid substitutions. The polypeptides comprising the prokaryotic single-stranded DNA binding proteins polypeptides may include carboxy-tails comprising the amino acid sequence Asp-Ile-Pro-Phe (SEQ ID NO:5), or the amino acid sequence Asp-Ile-Pro-Phe (SEQ ID NO:5) having 1 to 2 conservative amino acid substitutions.
In the practice of the methods, the polypeptides that bind to the prokaryotic single-stranded DNA binding proteins may include exonucleases, DNA polymerase subunits, primases, helicases, topoisomerases, DNA repair enzymes, etc. In one example, the polypeptides that bind to the prokaryotic single-stranded DNA binding proteins include Exonuclease I. The polypeptides that bind to the prokaryotic single-stranded DNA binding proteins may be at least 90% identical to the amino acid sequence of SEQ ID NO:4. The methods may include assaying that comprises measuring fluorescence polarization.
Methods of inhibiting the binding of SSB-binding proteins to the C-terminal tails of prokaryotic SSBs are provided. The methods include contacting the antimicrobial compounds identified as described above with the SSB-binding proteins and with the C-terminal tails of prokaryotic SSBs, where the antimicrobial compounds inhibit the binding of the prokaryotic SSBs to the SSB-binding proteins. The SSB-binding proteins may be exonucleases, and in some embodiments the SSB-binding proteins may be prokaryotic Exonuclease I.
Methods of inhibiting the growth of microorganisms are provided, which include contacting the antimicrobial compounds identified as described above with the microorganisms, thereby inhibiting the growth of the microorganisms.
Three-dimensional models of crystal structures of prokaryotic Exonucleases I bound to the C-terminal tails of prokaryotic SSBs are provided. In one embodiment, the models substantially represent the atomic coordinates specified in the Protein Data Bank under the accession code 3C94. Methods are provided, which include: a) identifying candidate compounds using three-dimensional models of crystal structures of Exonuclease I bound to C-terminal tails of prokaryotic single-stranded DNA binding proteins, where the models substantially represent the atomic coordinates specified in the Protein Data Bank under the accession code 3C94; b) contacting the candidate compounds with polypeptides comprising the prokaryotic single-stranded DNA binding proteins and with polypeptides that bind to the prokaryotic single-stranded DNA binding proteins; and c) assaying for binding of the polypeptides comprising the prokaryotic single-stranded DNA binding proteins to the polypeptides that bind to the prokaryotic single-stranded DNA binding proteins; where a decrease in binding, relative to the binding of the polypeptides comprising the prokaryotic single-stranded DNA binding proteins to the polypeptides that bind to the prokaryotic single-stranded DNA binding proteins in absence of the candidate compounds, identifies the candidate compounds as antimicrobial compounds. The contacting may be performed in solution. Alternatively, the contacting may be simulated in silico. The methods may also include the step (d) of administering the identified antimicrobial compounds to subjects to determine if the compounds reduce growth of microorganisms in the subjects. Compounds identified by these methods are provided. Antimicrobial pharmaceutical compositions that include as active agents the compounds identified by these methods are also provided.
Methods of inhibiting the binding of prokaryotic Exonucleases I to the C-terminal tails of prokaryotic SSBs are provided, which include: a) designing candidate compounds using three-dimensional models of crystal structures of the prokaryotic Exonucleases I bound to the C-terminal tails of the prokaryotic SSBs, where the models substantially represent the atomic coordinates specified in the Protein Data Bank under the accession code 3C94; and b) contacting the candidate compounds with the Exonucleases I and with the prokaryotic SSBs, where the candidate compounds inhibit the binding of the prokaryotic Exonucleases I to the prokaryotic SSBs. The contacting may be performed in solution. Alternatively, the contacting may be simulated in silico.
Three-dimensional models of crystal structures of prokaryotic Exonuclease I bound to compounds identified according to the present invention are provided. For example, the three-dimensional model of crystal structure of prokaryotic Exonuclease I bound to compound 9 is provided, where the models substantially represent the atomic coordinates specified in Table 6. As well, the three-dimensional models of crystal structure of prokaryotic Exonuclease I bound to compound 10 is provided, where the models substantially represent the atomic coordinates specified in Table 7. Methods are provided, which include: a) identifying candidate compounds using three-dimensional models of crystal structures of Exonuclease I bound to compound 9 or compound 10, where the models substantially represent the atomic coordinates specified in Tables 7 and 8, respectively; b) contacting the candidate compounds with polypeptides comprising the prokaryotic single-stranded DNA binding proteins and with polypeptides that bind to the prokaryotic single-stranded DNA binding proteins; and c) assaying for binding of the polypeptides comprising the prokaryotic single-stranded DNA binding proteins to the polypeptides that bind to the prokaryotic single-stranded DNA binding proteins; where a decrease in binding, relative to the binding of the polypeptides comprising the prokaryotic single-stranded DNA binding proteins to the polypeptides that bind to the prokaryotic single-stranded DNA binding proteins in absence of the candidate compounds, identifies the candidate compounds as antimicrobial compounds. The contacting may be performed in solution. Alternatively, the contacting may be simulated in silico. The methods may also include the step (d) of administering the identified antimicrobial compounds to subjects to determine if the compounds reduce growth of microorganisms in the subjects. Compounds identified by these methods are provided. Antimicrobial pharmaceutical compositions that include as active agents the compounds identified by these methods are also provided.
Methods of inhibiting the growth of microorganisms are provided, which include contacting the antimicrobial compounds identified as described herein with the microorganisms, thereby inhibiting the growth of the microorganisms.
Antimicrobial pharmaceutical compositions comprising as the active agent the antimicrobial compounds identified as described herein are provided. Also provided are methods of treating subjects that have microbial infections, which include the step of administering to the subjects therapeutically effective amounts of these novel pharmaceutical compositions.



BRIEF DESCRIPTION OF THE DRAWINGS
FIG. 1 is a graph showing peptide binding inhibition by inhibitor 3.
FIG. 2 is a graph showing peptide binding inhibition by inhibitor 9.
FIG. 3 is a graph showing peptide binding inhibition by inhibitor 10.
FIG. 4 is a graph showing peptide binding inhibition by inhibitor 32.
FIG. 5 is a graph showing peptide binding inhibition by inhibitor 37.
FIG. 6 is a graph showing peptide binding inhibition by inhibitor 46 vs. peptide binding inhibition by inhibitor 31.
FIG. 7 is a graph showing peptide binding inhibition by the WT peptide.
FIG. 8 is a graph showing the inhibition of Escherichia coli 4213 growth by inhibitor 3.
FIG. 9 is a graph showing the inhibition of Escherichia coli 4213 growth by inhibitor 8.
FIG. 10 is a graph showing the inhibition of Escherichia coli 4213 growth by inhibitor 9.
FIG. 11 is a graph showing the inhibition of Escherichia coli 4213 growth by inhibitor 10.
FIG. 12 is a graph showing the inhibition of Escherichia coli 4213 growth by inhibitor 28.
FIG. 13 is a graph showing the inhibition of Escherichia coli 4213 growth by inhibitor 29.
FIG. 14 is a graph showing the inhibition of Escherichia coli 4213 growth by inhibitor 31.
FIG. 15 is a graph showing the inhibition of Escherichia coli 4213 growth by inhibitor 32.
FIG. 16 is a graph showing the inhibition of Escherichia coli 4213 growth by inhibitor 37.
FIG. 17 is a graph showing the inhibition of Staphylococcus aureus growth by inhibitor 3.
FIG. 18 is a graph showing the inhibition of Staphylococcus aureus growth by inhibitor 8.
FIG. 19 is a graph showing the inhibition of Staphylococcus aureus growth by inhibitor 9.
FIG. 20 is a graph showing the inhibition of Staphylococcus aureus growth by inhibitor 10.
FIG. 21 is a graph showing the inhibition of Staphylococcus aureus growth by inhibitor 32.
FIG. 22 is a graph showing the inhibition of Staphylococcus aureus growth by inhibitor 37.
FIG. 23 is a graph showing the inhibition of Staphylococcus aureus growth by inhibitor 42.
FIG. 24 is a graph showing Topoisomerase III peptide binding in the absence and in the presence of various inhibitors.
FIG. 25 illustrates the structure of the E. coli ExoI/SSB-Ct complex.
FIG. 26 illustrates equilibrium binding highlights the roles of the peptide-A-binding site and the basic ridge in SSB-Ct binding.
FIG. 27 illustrates how ExoI/SSB physical interaction is essential for SSB stimulation of ExoI activity.
FIG. 28 is a stereo diagram displaying Fo-Fc omit electron-density map for SSB-Ct peptides A and B.
FIG. 29 illustrates the crystallographic association of two glutamine residues from the ExoI helical domain associate with the SSB-Ct peptide A.
FIG. 30 illustrates the similarity of the ExoI SSB-Ct binding site (A) and a site on the surface of the E. coli RecQ winged-helix domain (B).



DETAILED DESCRIPTION OF THE PRESENTLY PREFERRED EMBODIMENTS
Novel and selective targets for antibiotic development are provided. The compounds and assays of the present invention can be used for identification of molecules that selectively inhibit interaction between SSB and its target proteins. Such molecules may be used as novel, broad-spectrum antibiotics. Alternatively, such molecules may be chemically modified, i.e. they may be used as starting points for the development of novel, broad-spectrum antibiotics. The compositions of the present invention find use in methods to inhibit the growth of microorganisms. They find use as disinfectants. They find use as active agents that can be used in pharmaceutical compositions, and they also find use in methods of treating subjects with microbial infections. The term “subject” is intended to include patients, normal volunteers, non-human mammals such as primates, and also other animals.
In one aspect, the present invention relates to novel antimicrobial compounds and to methods of identifying same. An “antimicrobial” is a substance that kills or inhibits the growth of microbes such as bacteria (antibacterial activity), fungi (antifungal activity), viruses (antiviral activity), or parasites (anti-parasitic activity). “Antibiotic” is an antimicrobial substance that is generally used to treat bacterial infections.
The invention is particularly well-suited for the identification of antimicrobial compounds in the form of small molecules that can inhibit the growth of bacteria. In some examples, the bacteria whose growth is inhibited using the compounds of the present invention are Gram-negative bacteria, e.g. Escherichia coli. In other examples, the bacteria whose growth is inhibited using the compounds of the present invention are Gram-positive bacteria, e.g. Staphylococcus aureus. The present invention may be practiced with bacteria that are not necessarily classified as Gram-positive or Gram-negative, e.g. Deinococcus radiodurans and Mycobactedia such as Mycobacterium tuberculosis, and also with any other bacteria that have conserved C-terminal residues as described herein.
In one embodiment, the present invention provides for the identification of compounds that inhibit protein complex formation mediated by the single-stranded DNA binding protein's highly conserved C-terminal tail, which could lead to a novel class of chemotherapeutics. The term “SSB” refers to a single-stranded DNA-binding protein. In some embodiments of the present invention, the E. coli SSB has the nucleotide sequence of SEQ ID NO:1, and has the amino acid sequence of SEQ ID NO:2.
Prokaryotic SSBs of the present invention include polypeptides that are polymorphic variants, mutants, and interspecies homologs of SEQ ID NO:2. Prokaryotic SSBs of the present invention also include functional equivalents or fragments of SEQ ID NO:2. A “functional fragment” or “functional equivalent” or “functional homolog” of a polypeptide of the present invention is a polypeptide that is homologous to the specified polypeptide but has one or more amino acid differences from the specified polypeptide. A functional fragment or equivalent of a polypeptide retains at least some, if not all, of the activity of the specified polypeptide.
The term “genome maintenance” as used herein refers to the maintenance of the structure and integrity of a genome. Proteins such as the single-stranded DNA-binding protein (SSB) may be involved in genome maintenance.
“Carboxy tail” (also known as the carboxy-tail, carboxyl-terminus, carboxy-terminus, C-terminal end, C-terminus, or COOH-terminus) of a protein or polypeptide is the end of the amino acid chain terminated by a free carboxyl group (—COOH). For purposes of the present invention, the C-terminus of a protein encompasses approximately 10-20 amino acids of the C-terminus of a protein. The SSB's C-terminus is herein also referred to as SSB-Ct.
The canonical prokaryotic SSBs are homotetramers composed of four identical subunits, with each monomeric unit consisting of an oligonucleotide/oligosaccharide binding (OB)-fold followed by a disordered C-terminal tail. The final ten amino acids of the C-terminal tail are very highly conserved among bacteria, and are essential for viability in E. coli, yet they are notably absent from both eukaryotic and mitochondrial SSBs. The C-terminal tail of E. coli SSB is the primary interaction site between SSB and many, if not all, of its functional partners including Topoisomerase III, PriA DNA helicase, Chi subunit of DNA polymerase III, RecQ DNA helicase, and Exonuclease I. Removal of the C-terminal tail of SSB has little effect on SSB's DNA binding capabilities, but it is nonetheless lethal to E. coli. 
Methods are provided for the identification of compounds that inhibit protein-protein interactions mediated by the C-terminal tail of SSB. The present invention also provides compounds that are identified using these methods, which compounds can inhibit protein-protein interactions mediated by the C-terminal tail of SSB. These compounds can serve as broad-spectrum antibiotics by disrupting the formation of genome maintenance protein complexes in prokaryotes, and in particular in bacteria. These compounds are not detrimental to eukaryotic genome maintenance complexes since eukaryotic RPA (Replication Protein A) does not contain a similar C-terminal tail, and likely uses a distinct method to recruit binding partners.
Alignment of SSB Tails from Different Prokaryotic Organisms
The alignment of the carboxy-tails of approximately 280 prokaryotic SSBs is shown in Table 1, which shows the conservation of the approximately ten amino acid residues that comprise the carboxy-tails of prokaryotic SSBs. In particular, the alignment of the C-terminal 20 residues of approximately 280 prokaryotic SSBs shows that the four extreme C-terminal residues (DIPF, i.e. Asp-Ile-Pro-Phe; also shown in SEQ ID NO:5) are the most highly conserved residues in the carboxy-tail of these prokaryotic SSBs (Table 1). These final C-terminal residues from the carboxy-tail of prokaryotic SSBs appear to be the most important for binding of proteins.
The present invention contemplates the use of polypeptides with carboxy-tails as shown in Table 1. The present invention contemplates the use of polypeptides with carboxy-tails homologous to the carboxy-tails shown in Table 1. For example, other useful polypeptides may have carboxy-tails as indicated in Table 1 with amino acid sequences comprising one or more conservative amino acid substitutions.







TABLE 1





Alignment of the carboxy-tails (C-termini)


of known prokaryotic SSBs















Desulfovibrio_desulfuricans--------FDDLGPAFPSEVSGMDDVPF (SEQ ID


NO: 9)


 


Desulfovibrio_vulgaris-------------DDDLGPAFPSEASGMDDVPF (SEQ ID


NO: 10)


 


Lawsonia_intracellularis----------GFEDISP-FPSEASGMDDVPF (SEQ ID


NO: 11)


 


Deinococcus_geothermalis-----------GLDIDQGLDDFPPEEEDLPF (SEQ ID


NO: 12)


 


Deinococcus_radiodurans------------GLDIDQGLDDFPPEEDDLPF (SEQ ID


NO: 13)


 


Thermus_thermophilus--------------GGVDIDEGLEDFPPEE-DLPF (SEQ ID


NO: 14)


 


Streptococcus_pneumoniae-----------ENNAGQDLADLVLEEEELPF (SEQ ID


NO: 15)


 


Caldicellulosiruptor_saccharol-----DIGTSSKLDLDENPEDDLPF (SEQ ID


NO: 16)


 


Streptococcus_pyogenes-------------NTSSLADSMPDYGPEPDLPF (SEQ ID


NO: 17)


 


Bacteroides_thetaiotaomicron-------QAQPSQAQPIQDNPADDLPF (SEQ ID


NO: 18)


 


Bacteroides_fragilis---------------SQQPQQPVSSQDNSADDLPF (SEQ ID


NO: 19)


 


Gramella_forsetii------------------NFANKNEFYSQDEEEDDLPF (SEQ ID


NO: 20)


 


Escherichia_coli_K12------------SAPAAPSNEPPMD---FDDDIPF (SEQ ID


NO: 21)


 


Shigella_dysenteriae_Sd197------SAPAAPSNEPPMD---FDDDIPF (SEQ ID


NO: 22)


 


Shigella_flexneri---------------SAPAAPSNEPPMD---FDDDIPF (SEQ ID


NO: 23)


 


Shigella_sonnei_Ss046-----------SAPAAPSNEPPMD---FDDDIPF (SEQ ID


NO: 24)


 


Shigella_boydii_Sb227-----------SAPAAPSNEPPMD---FDDDIPF (SEQ ID


NO: 25)


 


Haemophilus_influenzae-----------QQAAPQAEPPMDG--FDDDIPF (SEQ ID


NO: 26)


 


Pseudoalteromonas_atlantica-----QNKPAPMAEPDFD---FDDDIPF (SEQ ID


NO: 27)


 


Mannheimia_succiniciproducens----TRPAPAAEPAMDN--FDDDIPF (SEQ ID


NO: 28)


 


Pasteurella_mult-------------------PAPQNEPPMDMGFEBDNIPF (SEQ ID


NO: 29)


 


Salmonella_enterica-------------QSAPAPSNEPPMD---FDDDIPF (SEQ ID


NO: 30)


 


Salmonella_typhimurium----------QSAPAPSNEPPMD---FDDDIPF (SEQ ID


NO: 31)


 


Sodalis_glossinidius------------NSAPAPSNEPPMD---FDDDIPF (SEQ ID


NO: 32)


 


Erwinia_carotovora--------------NNAPAQSNEPPMD---FDDDIPF (SEQ ID


NO: 33)


 


Aeromonas_hydrophila------------QSAPPVYNEPPMD---FDDDIPF (SEQ ID


NO: 34)


 


Aeromonas_salmonicida-----------QSAPPVYNEPPMD---FDDDIPF (SEQ ID


NO: 35)


 


Vibrio_parahaemolyticus---------QQPQQQYNEPPMD---FDDDIPF (SEQ ID


NO: 36)


 


Photobacterium_profundum--------QQPQQQYNEPPMD---FDDDIPF (SEQ ID


NO: 37)


 


Vibrio_cholerae-----------------QYSQPQYNEPPMD---FDDDIPF (SEQ ID


NO: 38)


 


Vibrio_vulnificus---------------MQSQPQYNEPPMD---FDDDIPF (SEQ ID


NO: 39)


 


Vibrio_fischeri-----------------QAAQPQYNEPPMD---FDDDIPF (SEQ ID


NO: 40)


 


Psychromonas_ingrahamii---------QPTQTQYNEPSMD---FDDDIPF (SEQ ID


NO: 41)


 


Yersinia_enterocolitica---------AAQPQGGNEPPMD---FDDDIPF (SEQ ID


NO: 42)


 


Shewanella_oneidensis-------------QPQQNFTPDLDDG-WDDDIPF (SEQ ID


NO: 43)


 


Shewanella_loihica----------------QPQQNFTPDLDDG-WDDDIPF (SEQ ID


NO: 44)


 


Shewanella_putrefaciens-----------QPQQNFTPDLDDG-WDDDIPF (SEQ ID


NO: 45)


 


Shewanella_baltica----------------QPQQNFTPDLDDG-WDDDIPF (SEQ ID


NO: 46)


 


Shewanella_amazonensis------------PQQQNYTPDLDDG-WDDDIPF (SEQ ID


NO: 47)


 


Xanthomonas_campestris------------PAQQQSAPPMDDF-ADDDIPF (SEQ ID


NO: 48)


 


Xanthomonas_axonopodis------------PAQQQSAPPMDDF-ADDDIPF (SEQ ID


NO: 49)


 


Xanthomonas_oryzae----------------PAQQQSVPPMDDF-ADDDIPF (SEQ ID


NO: 50)


 


Xylella_fastidiosa----------------QSPQSSPPPMDDF-ADDDIPF (SEQ ID


NO: 51)


 


Hahella_chejuensis----------------QQPKPPMPEPMDD-FDDDIPF (SEQ ID


NO: 52)


 


Marinobacter_aquaeolei------------QQQGGGMPEPIDD-FDDDIPF (SEQ ID


NO: 53)


 


Alcanivorax_borkumensis---------TNQGGGFSGPADD---FDDDIPF (SEQ ID


NO: 54)


 


Magnetococcus_MC-1-------------FSSPADTFN-EGPD---FDDDIPF (SEQ ID


NO: 55)


 


Geobacter_metallireducens-------FGGGPAYDEPAFN---PDDDIPF (SEQ ID


NO: 56)


 


Geobacter_sulfurreducens-------GFGG-PSYDEPAFN---PDDDIPF (SEQ ID


NO: 57)


 


Pelobacter_carbinolicus---------QPQQNQYEEPPFN---PDDDIPF (SEQ ID


NO: 58)


 


Syntrophobacter_fumaroxidans----SRADELPPHPGGG---PDDDIPF (SEQ ID


NO: 59)


 


Leptospira_borgpetersenii-------SSSPESYNPPAPD---GDDDIPF (SEQ ID


NO: 60)


 


Buchnera_aphidicola----------------PKKIEKIDSSEIDFDDEIPF (SEQ ID


NO: 61)


 


Coxiella_burnetii------------------QTPTAGDDSSVADFDDDIPF (SEQ ID


NO: 62)


 


Photorhabdus_luminescens-----------SSVPPRGSEPPIDFDELIPF (SEQ ID


NO: 63)


 


Nitrosococcus_oceani-------------PRPSAPPSSSND--DFEDDIPF (SEQ ID


NO: 64)


 


Colwellia_psychrerythraea----------QAPKVNPQEPSIDFDDDIPF (SEQ ID


NO: 65)


 


Pseudoalteromonas_haloplanktis-----QGGASNPMEPTIDFDDDIPF (SEQ ID


NO: 66)


 


Wigglesworthia_glossinidia---------KESKKNKIEEEINFDDDIPF (SEQ ID


NO: 67)


 


Pseudomonas_entomophila------------QQPAPQPAADFDSFDDDIPF (SEQ ID


NO: 68)


 


Pseudomonas_putida-----------------QQPAPQPAADFDSFDDDIPF (SEQ ID


NO: 69)


 


Pseudomonas_syringae---------------QQQAPQPAADFDSFDDDIPF (SEQ ID


NO: 70)


 


Pseudomonas_fluorescens------------QQAAPQPAPDFDSFDDDIPF (SEQ ID


NO: 71)


 


Pseudomonas_aeruginosa-------------QQPAPQPAQDYDSFDDDIPF (SEQ ID


NO: 72)


 


Pseudomonas_stutzeri---------------PAARQQPAPDYDSEDDDIPF (SEQ ID


NO: 73)


 


Pseudomonas_mendocina--------------APQQAQPAPDYDSFDDDIPF (SEQ ID


NO: 74)


 


Saccharophagus_degradans-----------PAPAAPPAPDMDSFDDDIPF (SEQ ID


NO: 75)


 


Methylibium_petroleiphilum---------RQQARQPATAGDGFDDEIPF (SEQ ID


NO: 76)


 


Thiomicrospira_crunogena-----------PAQQVPAYTANDFDDDDVPF (SEQ ID


NO: 77)


 


Solibacter_usitatus---------------APAQHNDDFNQG-ITDDDVPF (SEQ ID


NO: 78)


 


Idiomarina_loihiensis-------------KPAEPAPFSPDNDF-DDDIPF (SEQ ID


NO: 79)


 


Burkholderia_383-------------------SRPSAPAGGGFDEMDDDIPF (SEQ ID


NO: 80)


 


Burkholderia_cepacia---------------SRPSAPAGGGFDEMDDDIPF (SEQ ID


NO: 81)


 


Burkholderia_pseudomallei----------SRPSAPAGGGFDEMDDDIPF (SEQ ID


NO: 82)


 


Burkholderia_mallei----------------SRPSAPAGGGFDEMDDDIPF (SEQ ID


NO: 83)


 


Burkholderia_cenocepacia-----------SRPSAPAGGGFDEMDDDIPF (SEQ ID


NO: 84)


 


Burkhoideria_xenovorans------------SRPSAPAGGGFDEMDDDIPF (SEQ ID


NO: 85)


 


Burkholderia_vietnamiensis---------SRPSAPAGGGFDEMDDDIPF (SEQ ID


NO: 86)


 


Acidovorax_avenae------------------AAQAPRAASGFDDMDDDIPF (SEQ ID


NO: 87)


 


Verminephrobacter_eiseniae---------AAPGPRAASGFDDMDDDIPF (SEQ ID


NO: 88)


 


Polaromonas_JS666------------------APAPTKAASGFDDMDDDIPF (SEQ ID


NO: 89)


 


Rhodoferax_ferrireducens-----------APAQAKPSSGFDDMDDDIPF (SEQ ID


NO: 90)


 


Thiobacillus_denitrificans---------AGSQRPASSGFDDMDDDIPF (SEQ ID


NO: 91)


 


Polaromonas_naphthalenivorans------PAASRASPSGFDDMDDDIPF (SEQ ID


NO: 92)


 


Nitrosomonas_eutropha--------------KTGTTGSSTGFDDMEDDIPF (SEQ ID


NO: 93)


 


Nitrosomonas_europaea--------------STPPAKSNTGFDDMEDDIPF (SEQ ID


NO: 94)


 


Nitrosospira_multiformis-----------GRAPARSSTGFDDMDDDIPF (SEQ ID


NO: 95)


 


Azoarcus_EbN1----------------------KAPTKSSGAGFGDFDDDIPF (SEQ ID


NO: 96)


 


Methylobacillus_flagellatus--------AASKPAGGSNFDDFEDDIPF (SEQ ID


NO: 97)


 


Rhodospirillum_rubrum-------------TAPASGPAGGP-VDMDDDIPF (SEQ ID


NO: 98)


 


Ralstonia_eutropha----------------RRQQQAPSNGF-EDMDDDIPF (SEQ ID


NO: 99)


 


Ralstonia_solanacearum------------ARRQQAPSNGF-EDMDDDIPF (SEQ ID


NO: 100)


 


Agrobacterium_tumefaciens----------RGGGQPSGGFSNDMDDDIPF (SEQ ID


NO: 101)


 


Neisseria_gonorrhoeae--------------RRQPVPAAAPVEDIDDDIPF (SEQ ID


NO: 102)


 


Neisseria_meningitidis-------------RRQPVPAAAPVEDIDDDIPF (SEQ ID


NO: 103)


 


Herminiimonas_arsenicoxydans-------RPAAKPAASNFNDMDDDIPF (SEQ ID


NO: 104)


 


Nitrobacter_hamburgensis-----------PRRTVAAGARRSDMDDDIPF (SEQ ID


NO: 105)


 


Nitrobacter_winogradskyi-----------PRRAAPASSHRGDMDDDIPF (SEQ ID


NO: 106)


 


Bordetella_parapertussis-----------PAPQAAPAANLADMDDDIPF (SEQ ID


NO: 107)


 


Bordetella_pertussis---------------PAPQAAPAANLADMDDDIPF (SEQ ID


NO: 108)


 


Bordetelia_bronchiseptica----------PAPQAAPAANLADMDDDIPF (SEQ ID


NO: 109)


 


Polynucleobacter_QLW-P1DMWA-1------SAPSASNAASLGAMDDDIPF (SEQ ID


NO: 110)


 


Acidobacteria_bacterium------------NDFDSAPAASTGITDDDIPF (SEQ ID


NO: 111)


 


Candidatus_pelagibacter-----------ANNFEDSPQTSN-DMDDEIPF (SEQ ID


NO: 112)


 


Psychrobacter_arcticus-------------PAQSKPTAMLDGPVDDDIPF (SEQ ID


NO: 113)


 


Psychrobacter_cryohalolentis-------PAQSKPTAMPDGPVDDDIPF (SEQ ID


NO: 114)


 


Haemophilus_ducreyi----------------NKSSKKSTTQQPEVDDDIPF (SEQ ID


NO: 115)


 


Dechloromonas_aromatica------------APPKNKPKPSFDDLGDDIPF (SEQ ID


NO: 116)


 


Neorickettsia_sennetsu-----------DLGTPTNHVNDTLDD--DDIPF (SEQ ID


NO: 117)


 


Baumannia_cicadellinicola---------NKILQDMGNEQPIEFDDEIPF (SEQ ID


NO: 118)


 


Bdellovibrio_bacteriovorus---------FNFQDFGPEPSFNSNDEIPF (SEQ ID


NO: 119)


 


Chromohalobacter_salexigens--------DNYGAPNPGNFDDFDDEIPF (SEQ ID


NO: 120)


 


Dichelobacter_nodosus------------SSPDYGP--DGAFDDPDDEIPF (SEQ ID


NO: 121)


 


Aquifex_aeolicus-------------------EKLGKEEEKPFTDEEDEIPF (SEQ ID


NO: 122)


 


Hyphomonas_neptunium--------------QQMSGPKESFS-QDLDDEIPF (SEQ ID


NO: 123)


 


Caulobacter_crescentus------------SQPSGPRESES-ADLDDEIPF (SEQ ID


NO: 124)


 


Maricaulis_mans--------------------SMDGPKEDFRNADLDDEIPF (SEQ ID


NO: 125)


 


Rickettsia_felis-------------------HPEAKNHSFDHSDLDDEIPF (SEQ ID


NO: 126)


 


Rickettsia_conorii-----------------HPETKNHSFDHSDLDDEIPF (SEQ ID


NO: 127)


 


Rickettsia_typhi-------------------YPEIKNHSFDHSDLDDEIPF (SEQ ID


NO: 128)


 


Rickettsia_prowazekii--------------YPETKNHSFDHSDLDDEIPF (SEQ ID


NO: 129)


 


Rickettsia_bellii------------------EYKHSKPSFDHSDLDDEIPF (SEQ ID


NO: 130)


 


Halorhodospira_halophila-----------GSGGGGMQEAPADFDDDIPF (SEQ ID


NO: 131)


 


Paracoccus_denitrificans-----------SGGGGGQSQSRPDFDDDIPF (SEQ ID


NO: 132)


 


Rhodopseudomonas_palustris---------RPMPASSGGGRSDMDDDIPF (SEQ ID


NO: 133)


 


Bradyrhizobium_japonicum-----------RAVAAGGGGRNSDMDDDIPF (SEQ ID


NO: 134)


 


Granulibacter_bethesdensis--------SGGSGWEPSHGG-DLDDEIPF (SEQ ID


NO: 135)


 


Rhodobacter_sphaeroides-----------RGNAPSGCGRRS-DLDDEIPF (SEQ ID


NO: 136)


 


Silicibacter_pomeroyi-------------GGGRGRGPASGG-IDDDEIPF (SEQ ID


NO: 137)


 


Roseobacter_denitrificans---------GGGNAPSPAPSR-DLDDEIPF (SEQ ID


NO: 138)


 


Magnetospirillum_magneticum-------GGGCGQSWEPPA-DLDDEIPF (SEQ ID


NO: 139)


 


Mesorhizobium_BNC1----------------PAESGGGGGHSR-DLDDEIPF (SEQ ID


NO: 140)


 


Mesorhizobium_loti----------------APRGGGGGGSSR-ELDDEIPF (SEQ ID


NO: 141)


 


Brucella_melitensis---------------GPSSGSSGGFSR-DLDDEIPF (SEQ ID


NO: 142)


 


Brucella_suis---------------------GPSSGSSGGFSR-DLDDEIPF (SEQ ID


NO: 143)


 


Brucella_abortus------------------GPSSGSSGGFSR-DLDDEIPF (SEQ ID


NO: 144)


 


Jannaschia_CCS1--------------------SGGGYGGGGGSSDLDDEIPF (SEQ ID


NO: 145)


 


Silicibacter_TM1040---------------NRGGGYGSGSQSID-DDEIPF (SEQ ID


NO: 146)


 


Novosphingobium_aromaticivoran----NQGGGSGGGFGD-DLDDDIPF (SEQ ID


NO: 147)


 


Myxococcus_xanthus-------------PPDDMGGGHGGGNGD----DDIPF (SEQ ID


NO: 148)


 


Erythrobacter_litoralis-----------GGSGGGGGSNYD-DLDDDIPF (SEQ ID


NO: 149)


 


Anaeromyxobacter_dehalogenans-----GPGFGSGGGAGG-GGPDDIPF (SEQ ID


NO: 150)


 


Desulfotomaculum_reducens--------SGSGSGFGSEISF-NG-DDIPF (SEQ ID


NO: 151)


 


Sphingopyxis_alaskensis-----------GAPGGGR-PPFDDDLDDDVPF (SEQ ID


NO: 152)


 


Pelobacter_propionicus----------AGTSGGGYEPPPFQD---DDIPF (SEQ ID


NO: 153)


 


Gluconobacter_oxydans--------------GSNGGWDAPPDNDLDDEIPF (SEQ ID


NO: 154)


 


Bartonella_quintana----------------QNNSQSEESFSHKLDDDVPF (SEQ ID


NO: 155)


 


Bartonella_henselae----------------SNNSQLGESFSHKLDDDVPF (SEQ ID


NO: 156)


 


Bartonella_bacilliformis-----------QNNNQSGGSFSHQLDDDVPF (SEQ ID


NO: 157)


 


Rhizobium_etli---------------------SSNRGGGGNFSRDLDDDIPF (SEQ ID


NO: 158)


 


Rhizobium_leguminosarum------------SRGGGGGGNFSRDLDDDIPF (SEQ ID


NO: 159)


 


Sinorhizobium_meliloti-------------SNQPNQGGNFSRDLDDDIPF (SEQ ID


NO: 160)


 


Desulfitobacteriurn_hafniense------HTASGEAYGHEMSLDDDIPF (SEQ ID


NO: 161)


 


Shewanella_denitrificans-----------KSHLVDSTSKIDFDDEDIPF (SEQ ID


NO: 162)


 


Candidatus_blochmannia------------NNHELNSESILVNFNEDDIPF (SEQ ID


NO: 163)


 


Wolbachia_endosyinbiont------------QYENFDSEVKEELIDDEIPF (SEQ ID


NO: 164)


 


Tropheryma_whipplei----------------KVLVGDNVSYEDFDSDEVPF (SEQ ID


NO: 165)


 


Ehrlichia_chaffeensis--------------KENSLNSSCDDIIIDDEIPF (SEQ ID


NO: 166)


 


Ehrlichia_canis--------------------KENFQDSSCDDIIIDDEIPF (SEQ ID


NO: 167)


 


Ehrlichia_ruminantium--------------NKMPFQNSCEDVIIDDEIPF (SEQ ID


NO: 168)


 


Helicobacter_acinonychis-----------PSKYQNSVPEINIDEEEIPF (SEQ ID


NO: 169)


 


Helicobacter_pylori----------------PSKYQNSVPEINIDEEEIPF (SEQ ID


NO: 170)


 


Thiomicrospira_denitrificans-------QMPSNSSIPEIDIDEDEIPF (SEQ ID


NO: 171)


 


Wolinella_succinogenes-------------APYKEPQIPEINIDDDEIPF (SEQ ID


NO: 172)


 


Helicobacter_hepaticus-------------TGNYPQNIPEINIDDEDIPF (SEQ ID


NO: 173)


 


Campylobacter_fetus----------------RQNKPKQNIDVNIDDEEIPF (SEQ ID


NO: 174)


 


Dehalococcoides_ethenogenes-----MDARDDDNGGGELEP---EDIPF (SEQ ID


NO: 175)


 


Dehalococcoides_CBDB1-----------IDAREDDNGGGELEP---EDIPF (SEQ ID


NO: 176)


 


Symbiobacterium_thermophilum-------RREDGMGSELTLGDDEDVPF (SEQ ID


NO: 177)


 


Clostridium_novyi------------------IFDQGYDEEITPIDDGDIPF (SEQ ID


NO: 178)


 


Clostridium_acetobutylicum---------DFGVPVQEDITPVDNSDIPF (SEQ ID


NO: 179)


 


Clostridium_perfringens------------DSSFNSNDDMTPIDDGDIPF (SEQ ID


NO: 180)


 


Clostridium_tetani-----------------NNEDNYNDDITPVDEGEVPF (SEQ ID


NO: 181)


 


Borrelia_afzelii-------------------EDVIKDIDIVDDKFNEDIPF (SEQ ID


NO: 182)


 


Borrelia_burgdorferi---------------EDVVKDIDIVDDKFSEDIPF (SEQ ID


NO: 183)


 


Borrelia_garinii-------------------EDAIKNIDIVDDKFNEDIPF (SEQ ID


NO: 184)


 


Syntrophomonas_wolfei--------------EVNMDNIDLVDQHEDEDIPF (SEQ ID


NO: 185)


 


Anapiasma_marginale----------------ENAIVEEVSFADEDMDEIPF (SEQ ID


NO: 186)


 


Anaplasma_phagocytophilum----------AGSFGGGVDFLDPDVDEIPF (SEQ ID


NO: 187)


 


Treponema_pallidum-----------------ATSSLDEADFSSSDLDTVPF (SEQ ID


NO: 188)


 


Rubrobacter_xylanophilus-----------GRGAGDEVDINESDFDDIPF (SEQ ID


NO: 189)


 


Treponema_denticola----------------PSYDDYQPDMGNSDLDNIPF (SEQ ID


NO: 190)


 


Mycoplasma_penetrans---------------DDEDPDQVVSNLDWLDEFKF (SEQ ID


NO: 191)


 


Candidatus_ruthia------------------PVLDPIAPVDNSEFDDDIPF (SEQ ID


NO: 192)


 


Acidovorax_JS42--------------------PVLDPIAPVDNSEFDDDIPF (SEQ ID


NO: 193)


 


Francisella_tularensis-------------DNMPDFAEINSSNFDDDIPF (SEQ ID


NO: 194)


 


Porphyromonas_gingivalis-----------SSVRDTAKEESSEPPSDLPF (SEQ ID


NO: 195)


 


Acinetobacter_ADP1---------------YVPKAPQQP--APADLDDDLPF (SEQ ID


NO: 196)


 


Acinetobacter_baumannii------------PKAPQQPASAPADLDDDLPF (SEQ ID


NO: 197)


 


Synechococcus_elongates------------GSRRDQEGGMAPRDPDSDLF (SEQ ID


NO: 198)


 


Clostridium_thermocellum----------EPENTDGEGFFPAE-DDELPF (SEQ ID


NO: 199)


 


Clostridium_difficile-------------EPQGLDPQGFQAID-DDDIPF (SEQ ID


NO: 200)


 


Thermoanaerobacter_tengcongens-----DIPDDFDGFTPIESEDDLPF (SEQ ID


NO: 201)


 


Streptococcus_sanguinis----------DESPFGNSN--PMDISDDDLPF (SEQ ID


NO: 202)


 


Streptococcus_thermophilus------DESPFGNSN--PMDISDDDLPF (SEQ ID


NO: 203)


 


Streptococcus_agalactiae---------DESPFGNSN--PMDISDDDLPF (SEQ ID


NO: 204)


 


Streptococcus_mutans-------------DESPFGDSN--PMDISDDDLPF (SEQ ID


NO: 205)


 


Streptococcus_suis---------------EESPFGASN--PMDISDDDLPF (SEQ ID


NO: 206)


 


Lactococcus_lactis--------------QNNDSFG-SD--PMEISDDDLPF (SEQ ID


NO: 207)


 


Zymomonas_inobilis---------------SSNTNHDPF--GMDDLDDDVPF (SEQ ID


NO: 208)


 


Oenococcus_oeni------------------PFNTDTGND--SLDISDDDLPF (SEQ ID


NO: 209)


 


Carboxydothermus_hydrogenoform----DFDPSDFG-TEIEISDEDIPF (SEQ ID


NO: 210)


 


Moorella_therinoacetica-----------NQDFSDLG-TEVEIGEDDLPF (SEQ ID


NO: 211)


 


Geobacillus_kaustophilus----------DDPFANDG-QPIDISDDDLPF (SEQ ID


NO: 212)


 


Geobacillus_thermodenitrifican----EDPFANDG-QPIDISDDDLPF (SEQ ID


NO: 213)


 


Bacillus_licheniformis------------DDPFANDG-KPIDISDDDLPF (SEQ ID


NO: 214)


 


Bacillus_subtilis-----------------DDPFANDG-KPIDISDDDLPF (SEQ ID


NO: 215)


 


Bacillus_halodurans---------------EDPFANDG-KPIDISDDDLPF (SEQ ID


NO: 216)


 


Listeria_welshimeri---------------NDPFASDG-KPIDISDDDLPF (SEQ ID


NO: 217)


 


Lactobacillus_casei---------------PDPFANNG-KPIDISDDDLPF (SEQ ID


NO: 218)


 


Oceanobacillus_iheyensis----------EDPFKNNG-EPIDISDDDLPF (SEQ ID


NO: 219)


 


Bacillus_thuringiensis------------DDPFSNVG-QPIDISDDDLPF (SEQ ID


NO: 220)


 


Bacillus_anthracis----------------DDPFSNVG-QPIDISDDDLPF (SEQ ID


NO: 221)


 


Bacillus_cereus-------------------DDPFSNVG-QPIDISDDDLPF (SEQ ID


NO: 222)


 


Bacillus_clausii-----------------DNDPFSNDG--SIDISDDDLPF (SEQ ID


NO: 223)


 


Pediococcus_pentosaceus-----------NDPFANSG-QSIDISDDDLPF (SEQ ID


NO: 224)


 


Lactobacillus_plantarum-----------ADPFANNG-DQIDISDDDLPF (SEQ ID


NO: 225)


 


Lactobacillus_brevis--------------ADPFANSG-DSIDISDDDLPF (SEQ ID


NO: 226)


 


Lactobacillus_sakei---------------ADPFANNG-QAIDISDDDLPF (SEQ ID


NO: 227)


 


Lactobacillus_salivarius----------ADPFADNG-QSIDISDDDLPF (SEQ ID


NO: 228)


 


Leuconostoc_mesenteroides----------NPFAASGNTEIDISDDDLPF (SEQ ID


NO: 229)


 


Lactobacillus_gasseri-------------QDPFADSG-STIDISDDDLPF (SEQ ID


NO: 230)


 


Enterococcus_faecalis-------------SDPFGGSG-SSIDISDDDLPF (SEQ ID


NO: 231)


 


Staphylococcus_haemolyticus-------DNPFANAN-GPIDISDDDLPF (SEQ ID


NO: 232)


 


Staphylococcus_saprophyticus------DNPFANAN-GPIDISDDDLPF (SEQ ID


NO: 233)


 


Staphylococcus_epidermidis--------DNPFANAN-GPIDISDDDLPF (SEQ ID


NO: 234)


 


Listeria_innocua------------------SDSFANEG-KPIDINPDDLPF (SEQ ID


NO: 235)


 


Listeria_monocytogenes------------SDSFASEG-KPIDINEDDLPF (SEQ ID


NO: 236)


 


Prosthecochloris_vibrioformis------TSQPPSGPMIENNDKDDLPF (SEQ ID


NO: 237)


 


Pelodictyon_luteolum--------------PPQTAPSAPMIEN-DKDDLPF (SEQ ID


NO: 238)


 


Chlorobium_phaeobacteroides-------DYPQQSSGPMIES-EKDDLPF (SEQ ID


NO: 239)


 


Chlorobium_tepidum-----------------YGASPSSGGAQEFEKDDLPF (SEQ ID


NO: 240)


 


Chlorobium_chlorochromatii---------PPATPTVPTMIDTDKDDLPF (SEQ ID


NO: 241)


 


Staphylococcus_aureus--------------TQTGNNPFDNTEEDFSDLPF (SEQ ID


NO: 242)


 


Lactobacillus_delbrueckii----------TNPFDSSDDAINVSNDDLPF (SEQ ID


NO: 243)


 


Salinibacter_rubber----------------GGDGQPGSDETFEPDDDLPF (SEQ ID


NO: 244)


 


Cytophaga_hutchinsonii-------------AMESAGSFEPQTSGADDLPF (SEQ ID


NO: 245)


 


Methylococcus_capsulatus-----------GGSGAGSSQFDEGFDDDVPF (SEQ ID


NO: 246)


 


Alkalilimnicola_ehrlichei----------GGRQDNMGDDAGAFEDDIPF (SEQ ID


NO: 247)


 


Rhodopirellula_baltica-------------SSDSQPTGDGPGYDEPDIPF (SEQ ID


NO: 248)


 


Synechococcus_WH_8102-------------DNQEAAGSFG-GQASDEEIPF (SEQ ID


NO: 249)


 


Synechococcus_CC9902--------------DNQESGGNFG-GQASDEDIPF (SEQ ID


NO: 250)


 


Synechococcus_CC9311---------------SEAGSGGFGGGSPSDEEVPF (SEQ ID


NO: 251)


 


Prochlorococcus_marinus-----------ASNFGGGGFGDG-PSBEEVPF (SEQ ID


NO: 252)


 


Arthrobacter_aurescens-----------NPSANAGSSWGNS-P-DSEPPF (SEQ ID


NO: 253)


 


Arthrobacter_FB24----------------PGVSNAGGGWGNG-P-DSEPPF (SEQ ID


NO: 254)


 


Mycobacterium_tuberculosis------PWGSAPASGSFGGG---DDEPPF (SEQ ID


NO: 255)


 


Mycobacterium_avium-------------PWGSAPASGSFGGG---DDEPPF (SEQ ID


NO: 256)


 


Mycobacterium_bovis-------------PWGSAPASGSFGGG---DDEPPF (SEQ ID


NO: 257)


 


Mycobacterium_vanbaalenii-------PWGSAPASGSFGGA---DDEPPF (SEQ ID


NO: 258)


 


Mycobacterium_gilvum------------PWGSAPASGSFGGA---DDEPPF (SEQ ID


NO: 259)


 


Mycobacterium_smegmatis---------PWGSAPASGSFSGA---DDEPPF (SEQ ID


NO: 260)


 


Nocardia_farcinica----------------GSAPAAGSFGGGRM-DDEPPF (SEQ ID


NO: 261)


 


Mycobacterium_ulcerans---------DPWGSAPASGSFG-G---DDEPPF (SEQ ID


NO: 262)


 


Mycobacterium_leprae------------PWGSAPTSGSEGVG---DEEPPF (SEQ ID


NO: 263)


 


Corynebacterium_jeikeium-------DPWNSAPQSG-FGDG---DDEPPF (SEQ ID


NO: 264)


 


Corynebacterium_diphtheriae-----PWSSAPQAGGFGGA---EQDPPF (SEQ ID


NO: 265)


 


Salinispora_tropica---------------APAPSRGGSGGGNF-DEEPPF (SEQ ID


NO: 266)


 


Corynebacterium_efficiens---------NSAPPAGSGGFGGA-DDEPPF (SEQ ID


NO: 267)


 


Corynebacterium_glutamicum--------NSAPPAGSGGFGGA-DDEPPF (SEQ ID


NO: 268)


 


Rhodococcus_RHA1----------------APQASGSFGGSGGG---SDEPPF (SEQ ID


NO: 269)


 


Streptomyces_avermitilis---------GSSGGSSGGSGGG-Y-SDEPPF (SEQ ID


NO: 270)


 


Thermobifida_fusca--------------WATGGGGFGG-GGG-Y-SDEPPF (SEQ ID


NO: 271)


 


Frankia_CcI3---------------------APIDDPWSQPAGG--YSDEPPF (SEQ ID


NO: 272)


 


Nocardioides_JS614--------------SAPANDPWGAPGVG---SDEPPF (SEQ ID


NO: 273)


 


Acidothermus_cellulolyticus--------AEDPWAAGSATGNFSDEPPF (SEQ ID


NO: 274)


 


Propionibacterium_acnes-------ANRGGGVDPWASAQT-----DEPPF (SEQ ID


NO: 275)


 


Leifsonia_xyli------------------PSAGTDVWNTPGAYN---DSTPF (SEQ ID


NO: 276)


 


Aster_yellows_witches_broom--NKTATKVIVQKVIFLDNKDK (SEQ ID


NO: 277)


 


Onion_yellows_2--------------------VIVHKVIFLDNKSQTDNLPF (SEQ ID


NO: 278)


 


Anabaena_variabilis----------------EESTSTSLPNETQAVANANF (SEQ ID


NO: 279)


 


Nostoc_PCC_7120--------------------EESTSTSAPNETQAVANANF (SEQ ID


NO: 280)


 


Synechocystis_---------------------LLGSKRDNAEATMNNYPEEF (SEQ ID


NO: 281)


 


Trichodesinium_erythraeum----------ELLGSKRDSEQAALASYNEF (SEQ ID


NO: 282)


 


Flavobacterium_johnsoniae----------AKNTNFDAPSEGLPINDLPF (SEQ ID


NO: 283)


 


Thermotoga_maritime----------------LEIPEEDFSSDTFSEDEPPF (SEQ ID


NO: 284)


 


Syntrophus_aciditrophicus----------EGHFSPFNDLPPLPEDDVPF (SEQ ID


NO: 285)


 


Leptospira_interrogans-------------VVGQMIRFDGLPGKKEREVA (SEQ ID


NO: 286)


 


Desulfotalea_psychrophila----------SFPEPTGPDAYGGTGNDVPF (SEQ ID


NO: 287)


 


Onion_yellows_phytoplasma_OY-M-----CNNVQFLESKKNPDNAYDNF (SEQ ID


NO: 288)


 


Campylobacter_jejuni---------------EKLKEIDIDAYDSDDTNLPF (SEQ ID


NO: 289)


 


Thermosynechococcus_elongates-------LSSKRDTDPNAVPAGYVPEI (SEQ ID


NO: 290)


 


Shewanella_W3-18-1-----------------PADDASSQANWAQTYPEPDF (SEQ ID


NO: 291)


 


Gloeobacter_violaceus--------------KVDQLELLGRAARPDEPESF (SEQ ID


NO: 292)


 


Shewanella_ANA-3---------------------AQPQGGHQQNTQQQAYNYHR (SEQ ID


NO: 293)









In one aspect, the present invention relates to the determination of the previously unpublished high-resolution structure of the E. coli SSB bound to a target protein, Exonuclease I (Exo I) from Escherichia coli. The E. coli Exonuclease I was described by Lehman, 1960, J. Biol. Chem. 235: 1479-1487. Exonucleases, which can be found as individual enzymes, or as parts of larger enzyme complexes, are enzymes that cleave nucleotides one at a time from an end of a polynucleotide chain. The E. coli Exonuclease I has the nucleotide sequence of SEQ ID NO:3, and it has the amino acid sequence of SEQ ID NO:4. The atomic coordinates of the crystal structure of the E. coli Exonuclease I have been deposited in the Protein Data Bank under the accession code 3C95. The present invention contemplates the use of other prokaryotic exonucleases, and in particular the use of other prokaryotic homologs of the E. coli Exonuclease I.
Prokaryotic exonucleases of the present invention include polypeptides that are polymorphic variants, mutants, and interspecies homologs of SEQ ID NO:4. Prokaryotic exonucleases of the present invention also include functional equivalents or fragments of SEQ ID NO:4.
Methods are provided for assaying binding of a prokaryotic SSB to a “SSB-binding protein” (also referred to herein as a “target protein”). An SSB-binding protein is a protein that binds to SSB. The SSB may be a prokaryotic SSB, for example the SSB may be an E. coli SSB. The SSB-binding protein may be a prokaryotic SSB-binding protein, for example the SSB-binding protein may be Exonuclease. The Exonuclease may be prokaryotic Exonuclease, and in particular it may be Exonuclease I. The Exonuclease I may be an E. coli Exonuclease I.
Also provided are rapid fluorescence polarization methods for measuring the binding of SSB to Exonuclease I in solution. Fluorescence polarization (FP) is a technique that can measure the binding of a tagged molecule to a target molecule using polarized light and a fluorescent tracer. When excited with polarized light, tracers attached to molecules emit high levels of polarized fluorescence. Tracers attached to larger molecules are slower in rotations compared to tracers attached to smaller molecules. For example, fluorescein-labeled peptides can be used to detect specific binding of the peptides to a variety of molecules, since the fluorescein-labeled peptides are depolarized more slowly when bound to targets due to their slower tumbling rates relative to their free tumbling rates. In chemistry, fluorescence anisotropy assays the rotational diffusion of a molecule from the decorrelation of polarization in fluorescence, i.e., between the exciting and emitted (fluorescent) photons. From the rotational diffusion constants, one can estimate the shape of a macromolecule and use that information to design other molecules that may be drug candidates.
Given (1) the importance of protein interactions with SSBs, (2) the broad conservation of SSB protein-binding sequences across bacterial species, and (3) the apparent absence of SSB protein-binding sequences from eukaryotic (human) systems, these assays can be specific for the identification of compounds that selectively inhibit prokaryotic growth. Small molecules that selectively inhibit interaction between SSB and its target proteins are thus attractive, novel, broad-spectrum antibiotics. The present invention contemplates the use of the methods described herein for a high-throughput screen for small-molecule inhibitors of this interaction. Such inhibitors can serve as lead compounds for future biochemical and anti-microbial studies.
The methods of the present invention may be practiced in solution, i.e., in vitro. Thus, by conducting in vitro assays, it is possible to identify novel antimicrobial compounds according to the present invention. In another example, the methods of the present invention may be practiced in silico, i.e. through simulations using computer programs. Thus, using information on the crystal structures of the present invention, it is possible to design and/or to identify structures of novel antimicrobial compounds that can then be chemically synthesized using methods known in the art.
Examples of libraries of compounds that can be screened used in the practice of this invention include a variety of screening libraries that can be obtained from Maybridge (e.g., the HitFinder collection of 14,400 compounds); the 16,000 compound DIVERSet library from ChemBridge; the Chemdiversity library, Chemical Diversity Labs, Inc., etc. Any other candidate compounds can be used in the assays according to this invention. Candidate compounds do not have to be obtained from libraries in order to be screened. Candidate compounds can be synthesized using methods known in the art, and can then be used in the assays of the present invention. For example, candidate compounds can be designed in silico, using data on the crystal structures of the interacting proteins (e.g. SSB and Exonuclease). Once candidate compounds are designed in silico, these candidate compounds can be synthesized using known methods of synthetic chemistry, and can then be tested for their efficacy to inhibit or influence the interaction between the interacting proteins (e.g. SSB and Exonuclease).
In one example, the identification of compounds that inhibit SSB C-terminal tail mediated protein/protein interactions is assayed using a high throughput fluorescence polarization (FP) based screen. The inventors used an FP screen to identify compounds that inhibit binding of ExoI to the C-terminal tail of E. coli SSB. The use of ExoI-SSB C-terminal tail binding as a reporter for the high throughput screen has several advantages. First, binding between ExoI and SSB's C-terminal tail is quite strong in comparison to other known binding events allowing determination of an accurate Kd using FP and allowing screening of significant populations of ExoI-SSB-Ct complexes since complex formation can be saturated. Second, FP is very amenable to a high throughput platform, thus allowing for screening large numbers of compounds quickly. Third, the inventors' recent discovery of the crystal structures of Exonuclease I bound to the C-terminal tail of SSB has provided the first known high-resolution picture of the SSB C-terminal tail bound to a functional partner. The crystal structure suggests that the final amino acids of the C-terminal tail play vital roles in binding. These findings are supported by FP data indicating that mutation of the penultimate Pro residue of SSB to Ser eliminates the ability of the ExoI to bind the C-terminal tail of SSB. Not wanting to be bound by the following theory, it is possible that, given the extremely high conservation between the final four amino acids of SSB among disparate bacterial SSB homologs, this mode of protein binding may be a conserved mechanism of recruitment for proteins vital for genome maintenance.
By finding small molecules that inhibit these binding events, it is possible to disrupt the SSB-Exonuclease I interactions thus slowing bacterial growth or killing the bacteria. Furthermore, small molecules that inhibit binding may also inhibit binding between SSB C-terminal tail and other binding partners.
In one example, high throughput screens could be done looking for molecules that disrupt the interaction between SSB's C-terminal tail and other known SSB binding partners. For example, over a dozen SSB-interacting proteins have been already identified in E. coli (Butland et al., 2005, Nature 433: 531-537). Many of these interactions are mediated by contacts between the C-terminal tail of SSB and its heterotypic binding partners, e.g. ExoI (Sandigursky et al., 1996, Radiation Research 145: 619-623; Genschel et al., 2000, Biol. Chem. 381: 183-192), the χψ subunit of DNA polymerase III (Yuzhakov et al., 1999, Cell 96: 153-163; Witte et al., 2003, Nucleic Acids Res. 31: 4434-4440), uracil DNA glycosylase (Hanada et al., 2001, J. Biol. Chem. 276: 16992-16997), PriA DNA helicase (Cadman and McGlynn, 2004, Nucleic Acids Res. 32:6378-6387), and RecQ DNA helicase (Shereda et al., 2007, J. Biol. Chem. 282: 19247-19258). Since bacterial SSB proteins are predominantly homotetrameric (with four C-termini that can act as protein binding sites) and multiple SSB tetramers can bind to a single extended ssDNA region (Lohman and Ferrari, 1994, Annu. Rev. Biochem. 66: 527-570), utilization of SSB as a common target for many genome maintenance enzymes fosters efficient targeting and coordination of several DNA metabolic activities.
Order of Addition of Assay Components when Performing the Screen for Antimicrobial Compounds
The present invention contemplates variations of the screens for antimicrobial compounds described herein. As shown below, it is possible to screen libraries of compounds, to identify a number of hits that as candidate antimicrobial compounds. These candidate compounds can be mapped to a peptide-binding site in a crystal structure that represents the C-terminus of SSB bound to a SSB-binding protein (e.g. ExoI). In one example, it is possible to make a screen using a solution of fluorescently labeled C-terminal SSB peptide prebound to ExoI and titrate in compounds. Alternatively, it would be possible to conduct a screen by adding Exonuclease I (e.g. to 384 well plates), and then adding a single (e.g. different) candidate compound to each well. This would allow the compound some time to bind to the binding pocket is of ExoI. Fluorescently labeled peptide of the present invention can then be added. This fluorescently labeled peptide would compete for any compounds that were bound to the pocket/s. Not wanting to be bound by the following theory, it is possible that the latter would be a more physiologically relevant screen, since a drug in vivo would likely see its target before the target saw the SSB tail. While in the examples below the screen was conducted using ExoI and the peptide tail, there are numerous variations on this theme that could potentially be useful. The screen can also be performed using other targets from E. coli, e.g. Topoisomerase III, the Chi subunit of DNA polymerase, Gyrase, mixtures of these or other targets, etc. Furthermore, this screen could be done using proteins from another bacterium, including but not limited to Staphylococcus, Bacillus, Enterococcus, etc. These assays can be done using the entire protein or the C-terminal tail from the species that is being tested.
Using Docking Computer Programs to Identify and Improve Binding of Compounds
Computer modeling and docking procedures can be used to examine and improve the hits from small molecule screening libraries by analyzing the docking modes of known small molecules in the binding pocket. Docking starts with a crystal structure of the small molecule in the receptor pocket. It may happen that an initial hit from a database may not be an optimal structure for a drug. This can be tested by modeling the hit in the active site, then docking other molecules. A binding energy is calculated and compared to the known hits. Conformational fit is also an important part of the docking results and is usually examined by modeling.
After the initial crystal structure is determined for a bound small molecule, computational screening and docking programs such as AutoDock (Scripps research Institute, La Jolla, Calif.), FlexX (BioSolveIT GmbH, Sankt Augustin, Germany), and SLIDE (Michigan State University, East Lansing, Mich.) can be used to screen thousands of compounds from known databases. In this example, each molecule is allowed conformational flexibility to fit in the receptor site and scored on binding ability. In most cases, the receptor is also allowed flexibility. The top compounds from the databases are scored and ranked and the binding modes and binding energies are compared to actual hits from the small molecule assays. This ranks the reliability of both the chemical assay and the docking modes. This procedure leads to a group of molecules that can serve as starting molecules for optimizing the binding pocket with atom by atom de novo or by similar drug binding computer programs.
The methods described herein are amenable to this type of procedure. Indeed, the inventors of the present application have solved a number of crystal structures in which inhibitors are bound to the binding pocket. Using these tools, it is possible to search in silico (i.e., using computer programs) for molecules that bind as well or perhaps even better than the ones that have already been identified herein. In essence, appropriate computer software might be used to help identify the structure of a compound that will optimally inhibit peptide binding. The advantage of using the in silico techniques is the rapidity with which the potential candidate compounds can be screened, since this is a much faster way than doing thousands of binding assays in solution, i.e. in vitro.
Pharmaceutical Compositions that Include Identified Compounds
Pharmaceutical compositions are also provided, which include as active agents the antimicrobial compounds that are identified according to the present invention. The pharmaceutical compositions may be liquid or solid. The liquid composition may, for example, be an aqueous solution comprising one or more antimicrobial compounds. The solid composition may, for example, be a solid preparation obtainable by freeze-drying or spray-drying the above aqueous solution. In one embodiment the solid preparation is a lyophilizate. The aqueous preparation mentioned above includes an aqueous solution of such solid preparation. Still, the above solid composition may be in the form of a kit wherein the solid preparation and an infusion are formulated into separate preparations.
An example of the technology for producing the pharmaceutical compositions of this invention is described below. An aqueous solution can be produced by dissolving the antimicrobial compound in a conventional manner, in a solvent of choice. This aqueous solution may be alkaline, neutral, or basic; it is just sufficient that the antimicrobial compound is dissolved in the aqueous solution. The concentration of the antimicrobial compound in such an aqueous solution may for example be at concentrations consistent with measured minimal inhibitory concentrations (Table 3). In some embodiments, the concentration is chosen so that it permits successful lyophilization in a subsequent procedure. Referring to the manufacture of a solid pharmaceutical composition, a lyophilizate, for instance, can be produced by freeze-drying an aqueous solution that includes one or more antimicrobial compounds of the present invention. An exemplary procedure comprises freezing the aqueous solution at about −25° C. and, with the internal negative pressure of the freeze-dryer being maintained at about 0.1 Torr or less, increasing the plate temperature at a rate of about 5° C. to 20° C./hour to an ultimate temperature of about 25° C. to 40° C. Where lyophilization is carried out, a form regulator may be added to an aqueous solution of the antimicrobial compound for the purpose of improving the morphology of the lyophilizate. The form regulator may include various sugars (e.g. sugar alcohols such as mannitol, xylitol, inositol, sorbitol, etc., hexose-based disaccharides such as maltose, sucrose, lactose, etc., and monosaccharides such as glucose), neutral amino acids (e.g. glycine, alanine, proline, valine, methionine, etc.) and alkali metal salts of succinic acid (e.g. sodium succinate, etc.). Where a spray-dried preparation is the desired product, the aqueous solution described above is spray-dried by a per se known technique. An exemplary procedure comprises ejecting the aqueous solution in mist form from a spray dryer nozzle (e.g. a twin nozzle, a pressure nozzle, etc.) or rotary disk into its drying chamber at a flow rate of about 5-20 ml/minute (e.g. drying chamber inlet and out temperatures: about 80° C. to 120° C. and about 30° C. to 50° C., respectively; air flow rate about 70-100 kg/hour).
For insuring a further increase in drug absorption, a surfactant can be used concomitantly in the pharmaceutical compositions of this invention. Examples of suitable surfactants include nonionic surfactants such as sorbitan fatty acid esters (e.g. sorbitan monopalmitate, sorbitan sesquistearate, etc.), glycerin fatty acid esters (e.g. glyceryl monostearate, etc.), propylene glycol fatty acid esters (e.g. propylene glycol monostearate), polyoxyethylene glycerin fatty acid esters (e.g. polyoxyethylene glyceryl monostearate, etc.), polyethylene glycol fatty acid esters (e.g. polyoxyethylene monostearate, PEG distearate, etc.), polyoxyethylene alkyl ethers (e.g. polyoxyethylene lauryl ether, polyoxyethylene stearyl ether, etc.), polyoxyethylene hydrogenated castor oil, polyoxyethylene sorbitol beeswax derivatives, polyoxyethylene lanolin alcohol, polyoxyethylene sorbitol fatty acid esters, Pluronic series surfactants, anionic surfactants such as alkali metal dodecyl sulfates, alkali metal stearates, alkali metal palmitates, and liquid surfactants such as Tween 20 and Tween 80, among others. These surfactants can be used singly or plurally in a suitable ratio.
For improving the solubility or stability of the antimicrobial compound, a variety of salts (e.g. salts of organic acids such as sodium citrate, sodium tartrate, sodium benzoate, etc.) and/or stabilizers (e.g. basic inorganic salts such as magnesium carbonate, calcium carbonate, magnesium hydrogen carbonate, calcium hydrogen carbonate, etc.) may be incorporated or added to the compositions of this invention. If necessary, an isotonizing agent (e.g. sodium chloride) for osmotic pressure adjustment and/or a soothing or local anesthetic agent (e.g. glucose, sorbitol, mannitol, benzyl alcohol, mepivacaine hydrochloride, xylocaine hydrochloride, etc.) can also be employed.
A preservative and a pH control agent can be added in small amounts as required. The preservative includes parabens such as methyl p-hydroxybenzoate, propyl p-hydroxybenzoates, etc., alcohols such as chlorobutanol, quaternary ammonium salts such as benzalkonium chloride, benzethonium chloride, cetrimide, etc., sorbic acid, chlorhexidines, thimerosal and so on. The pH control agent includes various acids, e.g. inorganic acids such as hydrochloric acid, boric acid, phosphoric acid, carbonic acid, hydrogen carbonic acid, etc., organic acids such as mono- or polycarboxylic acids, amino acids, etc., and various bases, e.g. alkali metal hydroxides such as sodium hydroxide, potassium hydroxide, etc. and alkali metal (hydrogen) carbonates such as sodium hydrogen carbonate, sodium carbonate and so on. These additives can be used alone or in combination and can be added in a proportion of about 0.001-10 mg, preferably about 0.01-5 mg, per milligram of the antimicrobial compound.
The pharmaceutical compositions of this invention are generally administered orally or parenterally in a dosage form manufactured by formulating such an active ingredient with a pharmacologically acceptable carrier or excipient. The pharmaceutical composition of this invention can be put to use in the following manner. Taking a solid composition as an example, it can be extemporaneously dissolved in sterile distilled water or an infusion fluid (e.g. physiological saline, glucose infusion, etc.) and used as, for example, an intravenous, subcutaneous, intramuscular or intravenous drip injection or as an ophthalmic solution. Preparation of such an injection is preferably carried out by known aseptic procedures.
The dosage of the pharmaceutical composition of this invention is dependent on dosage form, therapeutic regimen, species of active compound and other factors. In some embodiments, the pharmaceutical composition may be administered once or divided into 2 to 3 times a day.
EXAMPLES
It is to be understood that this invention is not limited to the particular methodology, protocols, subjects, or reagents described, and as such may vary. It is also to be understood that 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 limited only by the claims. The following examples are offered to illustrate, but not to limit the claimed invention.
Structures of Compounds
Shown below are examples of compounds that were identified in the screens for compounds that inhibit SSB-Exonuclease I binding, according to this invention. For each of the compounds, the name of the compound, the chemical formula of the compound, the molecular weight of the compound (MW), and the chemical structure of the compound are shown. Also shown are the name of the company that provided the library from which the compound was identified, and the product code for the specific compound in the library. The Ki value is dissociation constant used to describe the affinity between a ligand (such as a drug, in the present case the tested inhibitory compound) and a peptide or a protein, i.e. how tightly a ligand (i.e., the tested inhibitory compound) binds to a particular peptide or protein. The IC50 value refers to the half maximal inhibitory concentration, i.e. the concentration of an inhibitory compound that is required for 50% inhibition of its target in vitro. It measures how much of a particular substance/molecule is needed to inhibit some biological process (e.g., bacterial growth in LB) by 50%.
Compound 3
Name: 2-[5-(3-bromobenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]-3-phenylpropanoic acid. Formula: C19H14BrNO3S2. MW: 448.36. Company: ChemBridge. Product Code: 6044448. Ki= ̃2.5 μM. IC50 E. coli 4213=5.5 μM. IC50 Staphylococcus aureus=10 μM.




Compound 8

Name: [5-(2-methyl-3-phenyl-2-propen-1-ylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl](phenyl)acetic acid. Formula: C21H17NO3S2. MW: 395.5. Company: ChemBridge. Product Code: 5767720. Ki= ̃4 μM. IC50 E. coli 4213=11 μM. IC50 Staphylococcus aureus=29 μM.




Compound 9

Name: 3-(tert-butyl)-1-(6-chloro-1,3-benzothiazol-2-yl)-4,5-dihydro-1H-pyrazol-5-one. Formula: C14H14ClN3OS. MW: 307.79766. Company: Maybridge. Product Code: SEW01297. Ki= ̃773 nM. IC50 E. coli 4213=6 μM. IC50 Staphylococcus aureus=5.5 μM.




Compound 10

Name: 2-[2-chloro-5-(trifluoromethyl)anilino]-5-methoxybenzoic acid. ACD Code: MFCD00175807. Formula: C15H11ClF3NO3. MW: 345.705449. Company: Maybridge. Product Code: S07197. Ki= ̃124.7 nM. IC50 E. coli 4213=30 μM. IC50 Staphylococcus aureus=18 μM.




Compound 28

Name: 1-(1,3-benzothiazol-2-yl)-3,4-dimethyl-1H-pyrazol-5-ol. Formula: C12H11N3OS. MW: 245.3. Company: Chembridge. Product Code: 9040944.




Compound 29

Name: 1-(1,3-benzothiazol-2-yl)-3-isopropyl-1H-pyrazol-5-ol. Formula: C13H13N3OS. MW: 259.33. Company: ChemBridge. Product Code: 9036389.




Compound 31

Name: 2-(1,3-benzothiazol-2-yl)-5-methyl-2,4-dihydro-3H-pyrazol-3-one. Formula: C11H9N3OS. MW: 231.27. Company: Chembridge. Product Code: 5108305.




Compound 32

Name: 2-[3-(trifluoromethyl)anilino]benzoic acid. Formula: C14H10F3NO2. MW: 281.234109. Company: Maybridge. Product Code: RJC02179.




Compound 37

Name: 5-[2-chloro-5-(trifluoromethyl)phenoxy]-2-nitrophenol. Formula: C13H7ClF3NO4. MW: 333.64. Company: ChemBridge. Product Code: 5524827.




Compound 42

Name: N-(6-chloro-1,3-benzothiazol-2-yl)-3,5-dimethyl-4-isoxazolecarboxamide. Formula: C13H10ClN3OS. MW: 307.7543. Company: Maybridge. Product Code: HTS08909.




Compound 46

Name: 1-(6-chloro-1,3-benzothiazol-2-yl)-3-methyl-4,5-dihydro-1H-pyrazol-5-one. Formula: C11H8ClN3OS. MW: 265.71702. Company: Maybridge. Product Code: SEW01296.




Peptides Corresponding to the C-Terminal Tail of SSB

Peptides corresponding to the C-terminal tail of SSB or variants thereof were synthesized and purified by the University of Wisconsin-Madison Biotechnology Center. “WT” peptide comprises an added N-terminal Trp (W) residue for quantification followed by the 9 C-terminal-most residues from E. coli SSB: Trp-Met-Asp-Phe-Asp-Asp-Asp-Ile-Pro-Phe (SEQ ID NO:6). Thus, the synthesized peptide was fluorescein-WMDFDDDIPF (i.e., fluorescein-SEQ ID NO:6). The Trp residue absorbs at 280 nm thus allowing accurate quantification of the peptide concentration. Alternatively, other residues or tags could be used for practicing the invention, so long as they can be used to accurately quantify the peptide concentration. In competitive binding experiments, the peptide WMDFDDDIPF (SEQ ID NO:6) was used without a fluorescent moiety.
A second peptide that was used, “F-WT”, comprises the same sequence but adds an N-terminal fluorescein moiety. Two additional peptides that alter the F-WT sequence were also synthesized: the first, “F-P176S”, substitutes a Ser residue for the penultimate Pro in the WT sequence, and the second, “F-mixed”, is a randomly-chosen sequence of the SSB-derived portion of the F-WT peptide sequence Trp-Asp-Phe-Met-Asp-Asp-Pro-Phe-Ile-Asp (SEQ ID NO:8). Other peptides that were used in the experiments described below were WDDIPF (SEQ ID NO:7) and WMDFDDDIPF (SEQ ID NO:6). Neither of these peptides was fluorescently labeled.
Peptide Binding Assay
Peptide binding assays were performed in solution, using the peptides from above, and Exonuclease I, in the absence or presence of various compounds. Different amounts of Exonuclease I (ExoI) were used in the peptide binding assays. Typically, 0.1-10,000 nM E. coli ExoI (or a variant) was incubated with 10 nM F-WT, F-P176S, or F-mixed peptide in 20 mM Tris-HCl, pH 8.0, 100 mM NaCl, 1 mM MgCl2, 4% (v/v) glycerol, 1 mM 2-mercaptoethanol, and 0.1 mg/ml bovine serum albumin (BSA) at room temperature for 10 minutes. Fluorescence polarization (FP) was measured at 25° C. in triplicate; the average FP value was plotted with standard deviation of the mean shown as error.
The data in Table 2 summarize the values of the dissociation constants (Ki) for several candidate compounds tested. Graphs showing peptide binding data for individual compounds (i.e., inhibitors) are shown in FIGS. 1-6. The data for the WT peptide control are shown in FIG. 7.







TABLE 2







Dissociation constant (Ki) estimates










Compound
Ki estimates














 3
2.5
μM



 8
4
μM



 9
2.2
μM



10
350
nM



32
1.5
μM



37
700
nM



46
1.5
μM



WT peptide
53
nM









In one example, it was noteworthy that the only difference between compounds (inhibitors) 46 and 31 was the presence of a Cl atom in the former. To examine the significance of one atom substitution, the peptide binding inhibition values of inhibitor 46 were plotted against the peptide binding inhibition values of inhibitor 31 (FIG. 6). Absence of the Cl atom resulted in much weaker binding (Table 3).
FIG. 7 shows which portions of the C-terminal peptide are important for binding to Exonuclease I. The principle of the experiment shown in FIG. 7 is very similar to the experiments performed with the inhibitors (FIGS. 1-6), but instead of titrating different inhibitors into a solution that has fluorescently tagged SSB C-terminal tail peptide bound to Exonuclease I, an unlabeled peptide, or an unlabeled peptide DDDIPF (SEQ ID NO:7) that has three amino acids residues (MDF) missing from the N-terminus was titrated. It should be again pointed out that the W is there only for quantitative purposes. If the missing residues play important roles in peptide binding then the truncated version of the peptide should compete more poorly than the full-length peptide. This is precisely what is seen in FIG. 7; it takes ten-fold more of the truncated peptide than the full-length peptide to titrate away the fluorescent peptide already bound to the protein. The fact that it is possible to titrate away the protein suggests that while those N-terminal three residues play a role in binding they are not the vital for binding since the truncated peptide competes, but does so more poorly.
The compounds 28, 29, and 31 did not inhibit binding (Table 3).
High Throughput Screen to Find Molecules that Inhibit SSB/Exonuclease I Interaction
Concentrated Exonuclease I was dialyzed overnight into 2 liters dilution buffer (DB) (20 mM Tris pH 8.0 HCl, 100 mM NaCl, 1 mM MgCl2, and 1 mM Beta-Mercaptoethanol). After dialysis, Exonuclease I was mixed with fluorescently labeled SSB C-terminal peptide, amino acid sequence (N-terminus) Fluorescein-WMDFDDDIPF, i.e. fluorescein-SEQ ID NO:6 (C-terminus), also previously diluted in DB. The final concentrations of the components of the Exonuclease I/SSB C-terminal peptide mixture after-adjustment with DB were 1 μM Exonuclease I, 10 nM fluorescently labeled SSB C-terminal peptide with 20 mM Tris pH 8.0 HCl, 100 mM NaCl, 1 mM MgCl2, and 1 mM Beta-Mercaptoethanol. After sitting at room temperature for 5 min, a liquid handling system was used to aliquot this solution into 384 well plates providing 30 microliters/well. One microliter of 1 mM compound was then added. The screened compounds were obtained from the ChemBridge DIVERSet library (ChemBridge Corporation, San Diego, Calif.), from the Maybridge HitFinder library (Thermo Fisher Scientific, Waltham, Mass.), from the ChemDiv library (Chemical Diversity Labs, San Diego, Calif.), or from the Known Bioactive Library—KBA01.
The FP (fluorescence polarization) values for each well were read using a (plate reader) 5 minutes after compound addition. Compounds that lowered the FP values were identified. This was typically done using three standard deviations. Compounds that were fluorescent or caused excessive precipitation were eliminated from consideration. Roughly 20 compounds that met these criteria were isolated and more stringently tested using a PanVera Beacon 2000 FP (PanVera Corp., Madison, Wis.). From these experiments 5 compounds were identified that were able to lower the FP values to a degree that suggested a complete inhibition of peptide binding thus allowing the determination of Ki.
To determine the Ki, a master mix was prepared similar to what was previously described above, using 1 μM Exonuclease I, 10 nM fluorescently labeled SSB C-terminal peptide with 20 mM Tris pH 8.0 HCl, 100 mM NaCl, 1 mM MgCl2, and 1 mM Beta-Mercaptoethanol. Increasing amounts of compound were titrated into peptide protein mixture until FP values were lowered to values given by only fluorescently labeled peptide alone. Ki values were determined using the Ki calculator for fluorescence-based competitive binding assays of Prof. Shaomeng Wang, University of Michigan (Nikolovska-Coleska et al., 2004, Anal. Biochem. 332: 261-273).
Bacterial Growth Assays
The candidate compounds were tested for their ability to inhibit bacterial growth, as shown in FIGS. 8-23 and in Table 3. For example, in FIGS. 8-16, the growth curves for E. coli 4213, a Gram-negative bacterium that has a compromised cell wall, are shown. FIGS. 8-16 show how individual candidate inhibitory compounds inhibit the growth of E. coli 4213. The compromised cell wall allows the chemicals to pass through it more readily. As well, FIGS. 17-23 show how individual candidate inhibitory compounds inhibit the growth of Staphylococcus aureus 12598, a Gram-positive bacterium.
100 μL of LB containing E. coli 1655, E. coli 4213, or S. aureus at A  ̃0.05 OD 600 was aliquoted in 96 well plates. One μL of compound in DMSO was added to final concentrations given. Plates were incubated at 37° C. with shaking at 250 RPM. Rate of growth was calculated by determining the average change in OD/hour that took place between hours 3 and 7 (log growth phase). The graphs shown herein are plots of this bacterial growth rate (change in OD/h) against inhibitor concentration in μM.
The data in Table 3 summarize the concentrations of selected compounds according to the present invention, which are necessary to reduce bacterial growth by 50% in liquid media.







TABLE 3







Concentrations of selected compounds necessary to reduce bacterial growth 50% in liquid media


















IC(50)







IC(50)
IC(50)
Human



Kia
E. coli
S.
cell
Hemolysis
MICc
Compound


Compound structure
(μM)
imp4213
aureus
line
b(μM)
(μg/ml)
name/info





















0.8
 6
6
>100
>800
9.0 (E. coli) 6.2 (B. subtilis)
Compound 9; also called BCBP.  Came from original Maybridge HTS collection.


 






 NDd
38
TBDe
TBD
>800
TBD
Compound 28. Derivative of compound 9.


 






ND
88
TBD
TBD
>800
TBD
Compound 29. Derivative of compound 9.


 






ND
50-100
TBD
TBD
>800
TBD
Compound 31. Derivative of compound 9.


 






TBD
TBD
9
TBD
>800
TBD
Compound 42. Derivative of compound 9.


 






1.5
TBD
TBD
TBD
>800
TBD
Compound 46. Derivative of compound 9.


 






0.1
30
20
>100
~800
12.3 (E. coli) 11.1 (B. subtilis)
Compound 10; also called CFAM. Came from original Maybridge HTS collection.


 






1.5
33
30
TBD
>800
TBD
Compound 32. Derivative of compound 10.


 






0.7
33
2.5
TBD
>800
TBD
Compound 37. Derivative of  compound 10.


 






2.5
 6
9
12
~100
3.6 (E. coli) 3.6 (B. subtilis.)
Compound 3; also called BOTP. Came from original Maybridge HTS collection. Bactericidal for B. subtilis


 






4  
11
29
>100
~200
4.0 (E.coli) 6.3 (B. subtilis)
Compound 8; also called MPTA. Came from original Maybridge HTS collection. Bactericidal for B. subtilis





aKi is the amount of compound needed to dissociate 50% of Exonuclease I/SSB-Ct complexes in vitro.


bHemolysis is the minimum concentration of compounded necessary to lyse red blood cells.


cMIC is the minimal concentration necessary to inhibit growth of E. coli (imp4213) or B. subtilis cells on solid media. Data are the same for either bacterial strain.


dNot detected; no dissociation of the Exonuclease I/SSB-Ct complex was observed even in the highest concentrations tested.


eTo be determined.






Data from the Escherichia coli inhibition experiments are summarized in Table 4.







TABLE 4







Inhibition of E. coli growth










Inhibitor
IC50 μM inhibitor













3
6



8
11



9
6



10
30



32
33



37
33



28
38



29
88



31
50-100



46









Data from the Staphylococcus aureus inhibition experiments are summarized in Table 5.







TABLE 5







Inhibition of S. aureus growth










Inhibitor
IC50 μM inhibitor













3
9



8
30



9
6



10
20



32
30



37
2.5



42
9









A number of the tested candidate compounds had profound inhibitory effects on bacterial growth. In addition, it was discovered that the identified drug compounds can slow the growth of a number of other Gram-positive bacterial species. For example, the growth of Bacillus subtilis and Enterococcus faecalis was inhibited when these bacteria were grown on agar plates containing 100 μM of either compound 9 or compound 10. Growth of Deinococcus radiodurans was also inhibited when tested in a similar manner.
Crystal Structures
Exonuclease I crystals were transferred to a soak solution containing 12% PEG 4000, 1 mM MgCl2, 20 mM Tris pH 8.0, and 5 mM compound. These solutions were allowed to soak in watch glasses for 5 days at which point the crystals were transferred to a cryo solution containing 12% PEG 4000, 1 mM MgCl2, 20 mM Tris pH 8.0, 5 mM compound, and 25% glycerol. Crystals were then flash frozen in liquid Nitrogen.
In spite of the noted importance of SSB interactions with heterologous proteins in cells, a structural and mechanistic understanding of interactions between SSB and its partner proteins has remained unclear. In one aspect, the present invention provides elucidation of the high-resolution structure of E. coli ExoI bound to the C-terminus of its cognate SSB. The crystal structures of apo and SSB peptide-bound forms of E. coli ExoI were determined, as were candidate compounds that bind in one of the binding pockets previously occupied by the C-terminal peptide tail of SSB in the crystal structure (Lu and Keck, 2008, Proc. Natl. Acad. Sci. USA, in press).
The crystal structure of E. coli ExoI bound to a peptide comprising the SSB-Ct element was determined. ExoI/SSB-Ct protein crystals diffracted to 2.7-Å resolution and the structure of the complex was determined by molecular replacement using the apo ExoI structure (Breyer and Matthews, 2000, Nat. Struct Biol. 7: 1125-1128) as a search model (Table 9). In addition, the 1.7-Å-resolution structure of E. coli ExoI crystallized in the absence of the SSB-Ct peptide (but otherwise under the same crystallization conditions as the peptide-bound form) was determined, for comparative structural analysis. As was described for the initial apo-ExoI structure, ExoI in both crystal forms is comprised of exonuclease (residues 1-201), SH3-like (residues 202-352), and helical (residues 360-476) domains (FIGS. 25A and 25B).
Inspection of difference electron-density maps from the SSB-Ct-bound ExoI crystals revealed features corresponding to the C-termini from two SSB-Ct peptides associated with the ExoI surface, as shown in FIGS. 25C, 25D, and FIG. 28. Both peptides bind at sites that are >20 Å from the active site. The first peptide (“peptide A”) binds between the exonuclease and SH3-like domains of ExoI (FIGS. 25C and 25E). Electron density is apparent for the C-terminal-most SSB residues of peptide A (174-177), but is missing for residues 169-173, consistent with the N-terminus being dynamic or disordered. The peptide-A binding site anchors the C-terminal-most SSB-Ct residue (Phe177) in a deep pocket comprised of evolutionarily conserved residues from ExoI. In this interaction, the hydrophobic Phe side chain is packed against Leu147, Leu204, and Tyr207 side chains from ExoI and its α-carboxyl oxygens form apparent ionic bonds with the Arg148 side chain. The more N-terminal region of peptide A packs against Ala310, Gln311, and Thr314 from ExoI with the exception of Asp174, which contacts ExoI residues Gln448 and Gln452 in an adjacent ExoI molecule within the crystal lattice (FIG. 29). SSB-Ct binding to site A is coincident with rearrangement of the ExoI Arg316 side chain, which orients toward the path of peptide A (FIG. 25E). This Arg316 rotamer position allows a non-active site Mg2+ ion to bind to an acidic pocket formed by Glu150, Glu318, and Asp319. In addition to these elements, a “basic ridge” formed by the Arg338 and Lys227 ExoI side chains presents a prominent electropositive patch near the N-terminus of peptide A (FIG. 25D). Given the presence of additional unresolved Asp residues on the SSB-Ct, this ridge could play a role in SSB-Ct binding that is not accounted for in the structure. This possibility was also tested.
Electron density for the second peptide, “peptide B”, includes SSB residues 175-177, which are bound entirely by the ExoI SH3-like domain (FIG. 25F). As with the peptide-A site, the peptide-B site binds primarily to Phe177 from the SSB-Ct, anchoring its side chain in a hydrophobic pocket (comprised of residues Trp245, Leu264, and Cys330) and binding its α-carboxyl oxygens in apparent ionic bonds formed with Arg327 from ExoI. ExoI residues Leu331, Leu334, and Pro338 contact more N-terminal regions of peptide B. Since prior solution studies indicated that ExoI/SSB complexes are stoichiometric (Genschel et al., 2000, Biol. Chem. 381: 183-192), finding two peptides bound to the surface of a single ExoI monomer was unexpected. Moreover, since peptide A is positioned between symmetrically-related ExoI molecules in the crystal lattice, there was a strong possibility that crystal packing could have influenced the structure of the complex. This structure was therefore used as a starting point to design experiments that evaluated the roles of ExoI residues in each site for SSB binding and enzymatic stimulation.
Solution SSB-Ct Binding Studies Define Important Features of the ExoI/SSB Complex
To examine ExoI/SSB-Ct complex formation in solution, an equilibrium fluorescence-anisotropy assay that measures ExoI binding to a fluorescein-labeled SSB-Ct peptide (F-SSB-Ct) was developed. ExoI binds F-SSB-Ct with an apparent equilibrium dissociation constant (Kd, app) of 136+/−11 nM in this assay (FIG. 26A). This binding is higher affinity than that observed for SSB-Ct peptide binding by PriA and RecQ, which associate with respective Kd, app values of 2 and 6 μM. To test whether this interaction was specific, ExoI binding to two control peptides was examined. The first, “F-P176S”, changes the penultimate Pro residue in the F-SSB-Ct sequence to Ser, which mimics the well studied ssb113 mutation that causes impaired cell growth due to defects in its interactions with cellular DNA replication machinery. The second control peptide, “F-mixed”, randomly mixes the arrangement of the residues in F-SSB-Ct. ExoI binding to both control peptides was minimal relative to the F-SSB-Ct peptide (FIG. 26A). Analogous specificities were observed for SSB-Ct peptide binding by PriA and RecQ. These results indicate that ExoI specifically interacts with the F-SSB-Ct peptide in solution, which is consistent with a previous study that examined ExoI binding to SSB-derived peptides in competition experiments (Lecointe et al., 2007, EMBO J. 26: 4239-4251).
A panel of ExoI variants was created in which surface-exposed residues forming the peptide-A (Arg148, Tyr207, Gln311 and Arg316) or peptide-B (Arg327 and Leu331) binding sites were individually mutated to alanine to assess the contributions of the two sites to SSB-Ct binding. Additional Ala variants were made to test whether the prominent “basic ridge” on ExoI (Lys227 and Arg338) and ExoI residues that bind Mg2+ in the presence of the SSB-Ct peptide (Glu150, Glu318 and Asp319) have roles in F-SSB-Ct binding. Finally, Ala variants altering residues from the helical domain (Gln448 and Gln452) that mediate inter-protein contacts with peptide A in the crystal structure were also created. Each ExoI variant was purified and tested for binding to the F-SSB-Ct peptide. Far UV circular dichroic spectra of the variants were indistinguishable from wild type ExoI, indicating that the mutations did not alter the secondary structure of the variants significantly.
Three of the peptide-A-site variants displayed dramatically reduced F-SSB-Ct binding (FIG. 26B and Table 10). Arg148, Tyr207, and Arg316 Ala variants bound the peptide  ̃10- to 100-fold more weakly than wild-type ExoI, with the Arg148 variant exhibiting the poorest binding. Kd, app values could not be derived for these variants since peptide binding was not saturated at the highest enzyme concentrations tested (10 μM). The Gln311 variant led to a more modest 2-fold binding defect relative to wild-type ExoI. In contrast to the peptide-A-site variants, neither of the peptide-B-site variants had measurable F-SSB-Ct binding defects (FIG. 26C). This was surprising given their direct contacts with Phe177 from peptide B and the strong defects displayed by analogous mutations in the peptide-A binding site.
Additional variants were used to test the roles of basic ridge, Mg2+-binding and helical domain surfaces in binding the F-SSB-Ct peptide in solution (FIG. 26D). The basic ridge variants had dramatic defects in peptide binding. ExoI Lys227 and Arg338 variants had 7- and 3-fold binding defects, respectively. These results indicate a significant role for the ExoI basic ridge in SSB-Ct binding. Two of the Mg2+-binding variants had  ̃2-fold enhanced binding relative to wild-type ExoI (Glu150 and Glu318), whereas the Asp319 variant had a 2-fold binding defect. Not wanting to be bound by the following theory, these modest effects suggested that Mg2+ binding observed in the crystal structure could be a consequence of the high concentration of the metal in the crystallization conditions rather than reflecting a major role for Mg2+ in SSB/ExoI complex formation. F-SSB-Ct binding by the Gln448 and Gln452 variants was indistinguishable from that of wild-type ExoI, suggesting that their association with the SSB-Ct peptide in the crystal structure was due to their proximity to the peptide through crystal packing but that they do not play a role in SSB-Ct binding in solution (FIG. 29).
ExoI/SSB Complex Formation is Essential for SSB stimulation of ExoI Activity
Early studies showed that E. coli SSB stimulates ExoI nuclease activity and that the two proteins physically interact. However, whether ExoI/SSB complex formation is required for this stimulation has not been tested. To examine this, a nuclease assay in which hydrolysis of a radiolabeled ssDNA substrate is catalyzed by ExoI in a reaction that can be stimulated  ̃4-fold with the addition of SSB was developed (FIG. 27A). SSB stimulation plateaus at 200 nM SSB, which is the concentration necessary to saturate the ssDNA with SSB.
To assess whether association with SSB is necessary for ExoI stimulation, two SSB variants wee substituted into the assay. The first, SSB113, is a well-characterized E. coli SSB variant with dramatically reduced ExoI binding affinity but wild type ssDNA binding attributes, and the second, SSB-mixed, is a variant with a mixed C-terminal sequence that matches the sequence used in the F-mixed peptide. SSB113 provided greatly reduced stimulation (<2-fold) compared to wild type SSB, whereas SSB-mixed entirely failed to stimulate ExoI activity (FIG. 27A). These results support the idea that ExoI/SSB interaction is critical for SSB stimulation. To test whether binding to the SSB-Ct element alone is sufficient to stimulate ExoI activity, the SSB-Ct peptide was titrated into the ExoI assay. The peptide had no apparent effect on ExoI nuclease activity even at concentrations well above the Kd, app for binding the enzyme (FIG. 27A). Together, these data are consistent with SSB-Ct/ExoI complex formation being necessary, but not sufficient, for SSB stimulation of ExoI activity.
The effects of Ala substitutions on SSB-stimulated ExoI nuclease activity were also tested. If SSB stimulates ExoI by recruiting the enzyme to its substrate, then ExoI variants that are defective for binding the SSB-Ct peptide would have parallel defects in SSB-stimulated activity. The peptide-A- and peptide-B-site variants matched this prediction remarkably well. Two of the peptide-A-site variants (Arg148 and Tyr207) appeared to be unaffected by the addition of SSB, maintaining wild-type levels of nuclease activity at all SSB concentrations tested (FIG. 27B); these variants also had the weakest F-SSB-Ct binding among the panel of ExoI mutant proteins (FIG. 26B). A third peptide-A-site variant, Arg316, had dramatically reduced SSB-dependent activity (<2-fold enhancement by SSB) relative to wild-type ExoI. As with the Arg148 and Tyr207 variants, the Arg316 variant also had impaired F-SSB-Ct binding affinity, although it appeared to bind with higher affinity than the former variants (FIG. 26B). Finally, the Gln311 variant had only a mildly reduced SSB-stimulation relative to wild-type ExoI, which paralleled its modest reduction in affinity for the F-SSB-Ct peptide. As would be predicted from these findings, the peptide-B-site and helical domain variants, which did not alter F-SSB-Ct binding in solution, also had wild-type SSB-dependent nuclease activity (FIG. 27C and FIG. 29).
The basic ridge and Mg2+-binding ExoI variants were also tested for SSB-dependent nuclease activities. The basic ridge variants (Lys227 and Arg338), which had defects in F-SSB-Ct binding, similarly had reduced stimulation by SSB (FIG. 27D). These results confirmed the importance of the basic ridge for coordinated activity with SSB. Two of the Mg2+-binding variants (Glu318 and Asp319) had wild-type levels of SSB-stimulated nuclease activity whereas the third (Glu150) had moderately elevated levels of both intrinsic (SSB-independent) and SSB-dependent activity. Although the maximal SSB-stimulated activity of the Glu150 variant exceeded that of wild-type ExoI, the fold stimulation by SSB was the same as with the wild-type enzyme. Thus the  ̃2-fold higher F-SSB-Ct binding affinity of the Glu150 and Glu318 variants did not result in enhanced SSB-stimulation of nuclease activity.
The atomic coordinates of the crystal structure of Escherichia coli Exonuclease I bound to the C-terminal peptide from E. coli SSB have been deposited in the Protein Data Bank under the accession code 3C94. Prokaryotic exonucleases that bind to SSBs and that upon binding have crystal structures whose models substantially represent the atomic coordinates specified in the model deposited in the Protein Data Bank under the accession code 3C94, can be used for practicing the present invention. As well, SSBs that bind to prokaryotic exonculeases and that upon binding have crystal structures whose models substantially represent the atomic coordinates specified in the model deposited in the Protein Data Bank under the accession code 3C94, can be used for practicing the present invention.
FIG. 25 illustrates the structure of the E. coli ExoI/SSB-Ct complex. FIG. 25(A): schematic diagram of E. coli ExoI and SSB's structural features (ExoI: Exonuclease domain; SH3-like domain, and helical domain; SSB: oligonucleotide-binding (OB) domain followed by  ̃60 disordered C-terminal residues). The bar graph depicts evolutionary conservation of the SSB C-terminus (SSB-Ct) sequence among 284 bacterial SSB proteins as percent identity. FIG. 25(B): ribbon diagram of ExoI bound to two SSB-Ct peptides. Dotted lines represent segments for which electron density was not observed. FIG. 25(C): surface representation depicting the binding sites for two SSB-Ct peptides (A and B) bound to ExoI. Selected ExoI residues are labeled. FIG. 25(D): surface representation as in (C) that models electropositive and electronegative potential. FIG. 25 (E and F): detailed views of the peptide-A and peptide-B sites. The Arg316 side chain from apo ExoI is superimposed.
FIG. 26 illustrates equilibrium binding highlights the roles of the peptide-A-binding site and the basic ridge in SSB-Ct binding. FIG. 26(A-D): equilibrium binding isotherms of F-SSB-Ct (or peptide variant) association with ExoI (or Ala variant) as monitored by fluorescence anisotropy. All data points are the average of three experiments. Error bars are one standard deviation from the mean. FIG. 26(A): F-SSB-Ct, F-P176S, and F-mixed ExoI binding isotherms. FIG. 26(B): F-SSB-Ct binding by peptide-A-site ExoI variants (R148A, Y207A, Q311A, and R316A). FIG. 26(C): F-SSB-Ct binding by peptide-B-site ExoI variants (L331A, R327A). FIG. 26(D): F-SSB-Ct binding by basic ridge (K227A, R338A) and Mg2+ binding site (E150A, E318A, D319A) ExoI variants. (E) Summary of ExoI variant F-SSB-Ct binding. The fold-change observed in F-SSB-Ct binding affinity relative to wild-type ExoI was: <1-fold binding changes (higher affinity), 1-2 fold, >2-5 fold, and >5 fold.
FIG. 27 illustrates how ExoI/SSB physical interaction is essential for SSB stimulation of ExoI activity. FIG. 27(A-D): ExoI specific activity is plotted as a function of SSB (or SSB variant). Data points are the mean of three experiments. Error bars are one standard deviation from the mean. Trend lines are shown for clarity. FIG. 27(A): ExoI activity on ssDNA is stimulated  ̃4 fold by the addition of SSB but not the SSB-Ct peptide alone. SSB-Ct peptide variants modestly stimulate (SSB113) or have no effect on (SSB-mixed) ExoI activity. FIG. 27(B): SSB-dependence of Peptide-A-site ExoI variant nuclease activities (R148A, Y207A, Q311A, and R316A). FIG. 27(C): SSB-dependence of Peptide-B-site ExoI variant nuclease activities (L331A, R327A). FIG. 27(D): SSB-dependence of basic ridge (K227A, R338A) and Mg2+-binding site (E150A, E318A, D319A) ExoI variants nuclease activity. FIG. 27(E): summary of the SSB dependence of ExoI variants nuclease activity.
FIG. 28 is a stereo diagram displaying Fo-Fc omit electron-density map (contoured at 2.8σ) for SSB-Ct peptides A and B.
FIG. 29 illustrates the crystallographic association of two glutamine residues from the ExoI helical domain associate with the SSB-Ct peptide A. FIG. 29(A): SSB-Ct peptide A associates with a symmetrically-related ExoI molecule (shown in ribbon form) in the crystal lattice via two Gin residues from the ExoI helical domain (Gln448 and Gln452. FIG. 29(B): close-up stereo diagram of the Gln-mediated interaction in the crystal lattice. FIG. 29(C): Gln448 and Gln452 Ala variants have no apparent F-SSB-Ct binding defects (Q448A, Q452A). FIG. 29(D): Gln448 and Gln452 Ala variants have wild-type SSB-dependent nuclease activities (Q448A, Q452A).
FIG. 30 illustrates the similarity of the ExoI SSB-Ct binding site (A) and a site on the surface of the E. coli RecQ winged-helix domain (B). The RecQ winged-helix domain binds the SSB-Ct element but the binding site has not been described. Regions on the RecQ domain with similar electrostatic features to those involved in ExoI/SSB-Ct binding are highlighted in (B).
Table 6 shows the coordinates of the crystal structure of E. coli ExoI bound to compound 9 that was identified in a screen according to the present invention. Compounds that bind prokaryotic exonucleases and that have crystal structures whose models substantially represent the atomic coordinates specified in Table 6, can be used for practicing the present invention.







TABLE 6





Coordinates of the crystal structure of E. coli Exol bound to compound 9

















HEADER
 ----
XX-XXX-XX  xxxx


COMPND
 ---


REMARK
3










REMARK
3
REFINEMENT.



REMARK
3
 PROGRAM
: REFMAC 5.2.0019


REMARK
3
 AUTHORS
: MURSHUDOV, VAGIN, DODSON


REMARK
3









REMARK
3
  REFINEMENT TARGET : MAXIMUM LIKELIHOOD


REMARK
3


REMARK
3
 DATA USED IN REFINEMENT.











REMARK
3
 RESOLUTION RANGE HIGH
(ANGSTROMS)
:   1.55


REMARK
3
 RESOLUTION RANGE LOW
(ANGSTROMS)
:  19.87


REMARK
3
 DATA CUTOFF
(SIGMA(F))
: NONE


REMARK
3
 COMPLETENESS FOR RANGE
(%)
:  92.76


REMARK
3
 NUMBER OF REFLECTIONS

:   68041


REMARK
3









REMARK
3
 FIT TO DATA USED IN REFINEMENT.










REMARK
3
 CROSS-VALIDATION METHOD
: THROUGHOUT


REMARK
3
 FREE R VALUE TEST SET SELECTION
: RANDOM











REMARK
3
 R VALUE
(WORKING + TEST SET)
: 0.21370


REMARK
3
 R VALUE
(WORKING SET)
:  0.21267










REMARK
3
 FREE R VALUE
:  0.23374











REMARK
3
 FREE R VALUE TEST SET SIZE
(%)
:  5.0


REMARK
3
 FREE R VALUE TEST SET COUNT

:  3592


REMARK
3









REMARK
3
 FIT IN THE HIGHEST RESOLUTION BIN.










REMARK
3
 TOTAL NUMBER OF BINS USED
:     20


REMARK
3
 BIN RESOLUTION RANGE HIGH
:   1.550


REMARK
3
 BIN RESOLUTION RANGE LOW
:   1.590











REMARK
3
 REFLECTION IN BIN
(WORKING SET)
:    4542


REMARK
3
 BIN COMPLETENESS
(WORKING + TEST) (%)
:   85.08


REMARK
3
 BIN R VALUE
(WORKING SET)
:   0.268










REMARK
3
 BIN FREE R VALUE SET COUNT
:     253


REMARK
3
 BIN FREE R VALUE
:   0.320


REMARK
3









REMARK
3
 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.










REMARK
3
 ALL ATOMS
:   4220


REMARK
3


REMARK
3
 B VALUES.











REMARK
3
 FROM WILSON PLOT
(A**2)
: NULL


REMARK
3
 MEAN B VALUE
(OVERALL, A**2)
:  24.107









REMARK
3
 OVERALL ANISOTROPIC B VALUE.


REMARK
3
  B11 (A**2) :   0.01


REMARK
3
  B22 (A**2) :   0.00


REMARK
3
  B33 (A**2) :   0.00


REMARK
3
  B12 (A**2) :   0.00


REMARK
3
  B13 (A**2) :   0.00


REMARK
3
  B23 (A**2) :   0.00


REMARK
3


REMARK
3
 ESTIMATED OVERALL COORDINATE ERROR.












REMARK
3
 ESU BASED ON R VALUE
(A):

 0.099


REMARK
3
 ESU BASED ON FREE R VALUE
(A):

 0.094


REMARK
3
 ESU BASED ON MAXIMUM LIKELIHOOD
(A):

 0.059


REMARK
3
 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD
(A**2):

 3.239


REMARK
3


REMARK
3
CORRELATION COEFFICIENTS.











REMARK
3
 CORRELATION COEFFICIENT FO-FC
:
0.954


REMARK
3
 CORRELATION COEFFICIENT FO-FC FREE
:
0.935


REMARK
3












REMARK
3
 RMS DEVIATIONS FROM IDEAL VALUES
COUNT
 RMS
 WEIGHT













REMARK
3
 BOND LENGTHS REFINED ATOMS
(A):
 3737 ;
 0.008 ;
 0.022


REMARK
3
 BOND ANGLES REFINED ATOMS
(DEGREES):
 5084 ;
 1.038 ;
 1.951


REMARK
3
 TORSION ANGLES, PERIOD 1
(DEGREES):
 442 ;
 5.149 ;
 5.000


REMARK
3
 TORSION ANGLES, PERIOD 2
(DEGREES):
 197 ;
32.714 ;
23.858


REMARK
3
 TORSION ANGLES, PERIOD 3
(DEGREES):
 606 ;
11.915 ;
15.000


REMARK
3
 TORSION ANGLES, PERIOD 4
(DEGREES):
  30 ;
12.440 ;
15.000


REMARK
3
 CHIRAL-CENTER RESTRAINTS
(A**3):
 545 ;
 0.057 ;
 0.200













REMARK
3
 GENERAL PLANES REFINED ATOMS
(A):
 2920 ;
 0.003 ;
 0.020


REMARK
3
 NON-BONDED CONTACTS REFINED ATOMS
(A):
 1836 ;
 0.196 ;
 0.200


REMARK
3
 NON-BONDED TORSION REFINED ATOMS
(A):
 2568 ;
 0.303 ;
 0.200


REMARK
3
 H-BOND (X . . . Y) REFINED ATOMS
(A):
 468 ;
 0.136 ;
 0.200


REMARK
3
 POTENTIAL METAL-ION REFINED ATOMS
(A):
  2 ;
 0.017 ;
 0.200


REMARK
3
 SYMMETRY VDW REFINED ATOMS
(A):
  39 ;
 0.225 ;
 0.200


REMARK
3
 SYMMETRY H-BOND REFINED ATOMS
(A):
  27 ;
 0.225 ;
 0.200


REMARK
3












REMARK
3
 ISOTROPIC THERMAL FACTOR RESTRAINTS.
 COUNT
 RMS
 WEIGHT













REMARK
3
 MAIN-CHAIN BOND REFINED ATOMS
(A**2):
 2305 ;
 0.433 ;
 1.500


REMARK
3
 MAIN-CHAIN ANGLE REFINED ATOMS
(A**2):
 3608 ;
 0.664 ;
 2.000


REMARK
3
 SIDE-CHAIN BOND REFINED ATOMS
(A**2):
 1709 ;
 1.021 ;
 3.000


REMARK
3
 SIDE-CHAIN ANGLE REFINED ATOMS
(A**2):
 1476 ;
 1.651 ;
 4.500


REMARK
3









REMARK
3
 NCS RESTRAINTS STATISTICS


REMARK
3
 NUMBER OF NCS GROUPS : NULL


REMARK
3


REMARK
3


REMARK
3
 TLS DETAILS


REMARK
3
 NUMBER OF TLS GROUPS :   3


REMARK
3
 ATOM RECORD CONTAINS RESIDUAL B FACTORS ONLY


REMARK
3


REMARK
3
 TLS GROUP :   1


REMARK
3
  NUMBER OF COMPONENTS GROUP :   1














REMARK
3
  COMPONENTS
C
SSSEQI
TO
C
SSSEQI


REMARK
3
  RESIDUE RANGE:
A
  1

A
 201









REMARK
3
  ORIGIN FOR THE GROUP (A):  30.6117  26.4458  31.1155


REMARK
3
  T TENSOR


REMARK
3
  T11:  −0.0145 T22:  −0.0126


REMARK
3
  T33:   0.0000 T12:  −0.0097


REMARK
3
  T13:   0.0041 T23:  −0.0023


REMARK
3
  L TENSOR


REMARK
3
  L11:   0.1747 L22:   0.2763


REMARK
3
  L33:   0.5243 L12:  −0.0803


REMARK
3
  L13:   0.1528 L23:  −0.2242


REMARK
3
  S TENSOR


REMARK
3
  S11:   0.0196 S12:   0.0055 S13:   0.0154


REMARK
3
  S21:  −0.0690 S22:   0.0139 S23:  −0.0222


REMARK
3
  S31:  −0.0123 S32:   0.0319 S33:  −0.0335


REMARK
3


REMARK
3
 TLS GROUP :   2


REMARK
3
  NUMBER OF COMPONENTS GROUP :   1














REMARK
3
  COMPONENTS
C
SSSEQI
TO
C
SSSEQI


REMARK
3
  RESIDUE RANGE:
A
 202

A
 354









REMARK
3
  ORIGIN FOR THE GROUP (A):  25.1747  4.7360  46.6329


REMARK
3
  T TENSOR


REMARK
3
  T11:  −0.0578 T22:  −0.0315


REMARK
3
  T33:  −0.0114 T12:  −0.0002


REMARK
3
  T13:   0.0088 T23:   0.0016


REMARK
3
  L TENSOR


REMARK
3
  L11:   0.6486 L22:   1.1345


REMARK
3
  L33:   0.9027 L12:   0.2886


REMARK
3
  L13:  −0.1969 L23:  −0.1079


REMARK
3
  S TENSOR


REMARK
3
  S11:  −0.0401 S12:   0.0041 S13:  −0.0065


REMARK
3
  S21:  −0.0122 S22:   0.0400 S23:   0.1062


REMARK
3
  S31:   0.0979 S32:  −0.0452 S33:   0.0001


REMARK
3


REMARK
3
 TLS GROUP :   3


REMARK
3
  NUMBER OF COMPONENTS GROUP :   1














REMARK
3
  COMPONENTS
C
SSSEQI
TO
C
SSSEQI


REMARK
3
  RESIDUE RANGE:
A
 355

A
 477









REMARK
3
  ORIGIN FOR THE GROUP (A):  12.6823  27.6878  16.5653


REMARK
3
  T TENSOR


REMARK
3
  T11:  −0.0330 T22:  −0.0129


REMARK
3
  T33:  −0.0882 T12:  −0.0147


REMARK
3
  T13:  −0.0325 T23:   0.0227


REMARK
3
  L TENSOR


REMARK
3
  L11:   0.5669 L22:   1.2815


REMARK
3
  L33:   1.0851 L12:   0.0040


REMARK
3
  L13:  −0.1252 L23:   0.5280


REMARK
3
  S TENSOR


REMARK
3
  S11:   0.0297 S12:   0.0777 S13:  −0.0305


REMARK
3
  S21:  −0.1022 S22:  −0.0153 S23:   0.1608


REMARK
3
  S31:  −0.0144 S32:  −0.1499 S33:  −0.0145


REMARK
3


REMARK
3


REMARK
3
 BULK SOLVENT MODELLING.


REMARK
3
 METHOD USED: BABINET MODEL WITH MASK


REMARK
3
 PARAMETERS FOR MASK CALCULATION










REMARK
3
 VDW PROBE RADIUS
:  1.20


REMARK
3
 ION PROBE RADIUS
:  0.80


REMARK
3
 SHRINKAGE RADIUS
:  0.80


REMARK
3









REMARK
3
 OTHER REFINEMENT REMARKS: NULL


REMARK
3













CISPEP
1
HIS A
177
SER A
178
0.00










LINK
SER A 178
ASP A 182
gap


LINK
ARG A 280
ALA A 295
gap


LINK
GLU A 353
SER A 360
gap








CRYST 1
53.823   91.966  106.280  90.00  90.00  90.00 P 21 21 21











SCALE 1
0.018579
0.000000
0.000000
0.00000


SCALE 2
0.000000
0.010874
0.000000
0.00000


SCALE 3
0.000000
0.000000
0.009409
0.00000


















ATOM
1
N
GLN
A
7
50.557
15.759
20.315
1.00
27.46
N


ATOM
2
CA
GLN
A
7
49.450
16.551
20.924
1.00
27.31
C


ATOM
3
CB
GLN
A
7
48.092
15.990
20.489
1.00
27.52
C


ATOM
4
CG
GLN
A
7
46.884
16.848
20.888
1.00
28.40
C


ATOM
5
CD
GLN
A
7
46.601
17.984
19.911
1.00
29.59
C


ATOM
6
OE1
GLN
A
7
47.389
18.258
19.002
1.00
30.56
O


ATOM
7
NE2
GLN
A
7
45.467
18.649
20.098
1.00
29.83
N


ATOM
8
C
GLN
A
7
49.558
16.553
22.448
1.00
26.84
C


ATOM
9
O
GLN
A
7
49.743
15.503
23.070
1.00
27.02
O


ATOM
10
N
GLN
A
8
49.450
17.739
23.041
1.00
26.18
N


ATOM
11
CA
GLN
A
8
49.483
17.879
24.495
1.00
25.51
C


ATOM
12
CB
GLN
A
8
50.193
19.175
24.902
1.00
25.77
C


ATOM
13
CG
GLN
A
8
49.479
20.452
24.463
1.00
26.77
C


ATOM
14
CD
GLN
A
8
50.023
21.697
25.134
1.00
27.43
C


ATOM
15
OE1
GLN
A
8
50.793
21.618
26.097
1.00
29.46
O


ATOM
16
NE2
GLN
A
8
49.616
22.862
24.633
1.00
29.00
N


ATOM
17
C
GLN
A
8
48.076
17.845
25.081
1.00
24.47
C


ATOM
18
O
GLN
A
8
47.104
18.220
24.416
1.00
24.29
O


ATOM
19
N
SER
A
9
47.974
17.390
26.327
1.00
23.25
N


ATOM
20
CA
SER
A
9
46.708
17.409
27.051
1.00
22.05
C


ATOM
21
CB
SER
A
9
46.786
16.528
28.299
1.00
22.13
C


ATOM
22
OG
SER
A
9
47.031
15.175
27.953
1.00
22.89
O


ATOM
23
C
SER
A
9
46.355
18.841
27.436
1.00
21.07
C


ATOM
24
O
SER
A
9
47.194
19.580
27.961
1.00
20.89
O


ATOM
25
N
THR
A
10
45.118
19.238
27.151
1.00
19.73
N


ATOM
26
CA
THR
A
10
44.658
20.583
27.480
1.00
18.69
C


ATOM
27
CB
THR
A
10
44.569
21.493
26.224
1.00
18.74
C


ATOM
28
OG1
THR
A
10
43.608
20.962
25.305
1.00
18.51
O


ATOM
29
CG2
THR
A
10
45.929
21.613
25.533
1.00
18.94
C


ATOM
30
C
THR
A
10
43.300
20.557
28.168
1.00
17.97
C


ATOM
31
O
THR
A
10
42.583
19.557
28.111
1.00
17.87
O


ATOM
32
N
PHE
A
11
42.973
21.660
28.836
1.00
16.92
N


ATOM
33
CA
PHE
A
11
41.638
21.890
29.371
1.00
16.34
C


ATOM
34
CB
PHE
A
11
41.716
22.339
30.830
1.00
16.30
C


ATOM
35
CG
PHE
A
11
42.156
21.265
31.777
1.00
16.20
C


ATOM
36
CD1
PHE
A
11
41.221
20.426
32.376
1.00
16.26
C


ATOM
37
CE1
PHE
A
11
41.619
19.431
33.261
1.00
16.26
C


ATOM
38
CZ
PHE
A
11
42.965
19.266
33.561
1.00
17.12
C


ATOM
39
CE2
PHE
A
11
43.911
20.101
32.973
1.00
17.27
C


ATOM
40
CD2
PHE
A
11
43.503
21.097
32.088
1.00
17.00
C


ATOM
41
C
PHE
A
11
40.959
22.974
28.559
1.00
15.81
C


ATOM
42
O
PHE
A
11
41.581
23.978
28.209
1.00
15.67
O


ATOM
43
N
LEU
A
12
39.684
22.775
28.255
1.00
15.13
N


ATOM
44
CA
LEU
A
12
38.883
23.837
27.673
1.00
14.78
C


ATOM
45
CB
LEU
A
12
38.307
23.429
26.315
1.00
14.84
C


ATOM
46
CG
LEU
A
12
37.592
24.535
25.525
1.00
15.52
C


ATOM
47
CD1
LEU
A
12
38.567
25.629
25.082
1.00
16.05
C


ATOM
48
CD2
LEU
A
12
36.863
23.962
24.333
1.00
15.62
C


ATOM
49
C
LEU
A
12
37.778
24.221
28.637
1.00
14.29
C


ATOM
50
O
LEU
A
12
36.763
23.530
28.743
1.00
14.07
O


ATOM
51
N
PHE
A
13
38.013
25.304
29.369
1.00
14.01
N


ATOM
52
CA
PHE
A
13
37.022
25.869
30.270
1.00
13.80
C


ATOM
53
CB
PHE
A
13
37.694
26.807
31.274
1.00
13.63
C


ATOM
54
CG
PHE
A
13
38.570
26.104
32.283
1.00
13.27
C


ATOM
55
CD1
PHE
A
13
38.078
25.784
33.548
1.00
13.35
C


ATOM
56
CE1
PHE
A
13
38.885
25.144
34.489
1.00
12.71
C


ATOM
57
CZ
PHE
A
13
40.204
24.820
34.166
1.00
12.95
C


ATOM
58
CE2
PHE
A
13
40.708
25.140
32.911
1.00
12.37
C


ATOM
59
CD2
PHE
A
13
39.892
25.777
31.975
1.00
12.95
C


ATOM
60
C
PHE
A
13
36.013
26.644
29.443
1.00
13.88
C


ATOM
61
O
PHE
A
13
36.391
27.396
28.548
1.00
14.05
O


ATOM
62
N
HIS
A
14
34.729
26.456
29.734
1.00
13.87
N


ATOM
63
CA
HIS
A
14
33.678
27.117
28.965
1.00
13.75
C


ATOM
64
CB
HIS
A
14
33.269
26.257
27.767
1.00
14.02
C


ATOM
65
CG
HIS
A
14
32.455
25.062
28.145
1.00
14.10
C


ATOM
66
ND1
HIS
A
14
31.105
24.968
27.888
1.00
15.76
N


ATOM
67
CE1
HIS
A
14
30.651
23.818
28.350
1.00
14.67
C


ATOM
68
NE2
HIS
A
14
31.656
23.167
28.907
1.00
16.74
N


ATOM
69
CD2
HIS
A
14
32.795
23.926
28.796
1.00
14.51
C


ATOM
70
C
HIS
A
14
32.451
27.420
29.816
1.00
13.65
C


ATOM
71
O
HIS
A
14
32.282
26.866
30.908
1.00
13.85
O


ATOM
72
N
ASP
A
15
31.593
28.290
29.290
1.00
13.54
N


ATOM
73
CA
ASP
A
15
30.356
28.674
29.952
1.00
13.85
C


ATOM
74
CB
ASP
A
15
30.640
29.713
31.042
1.00
13.93
C


ATOM
75
CG
ASP
A
15
29.424
30.009
31.900
1.00
15.01
C


ATOM
76
OD1
ASP
A
15
28.825
29.055
32.454
1.00
15.75
O


ATOM
77
OD2
ASP
A
15
29.073
31.198
32.039
1.00
17.02
O


ATOM
78
C
ASP
A
15
29.382
29.250
28.932
1.00
13.67
C


ATOM
79
O
ASP
A
15
29.786
29.996
28.039
1.00
13.73
O


ATOM
80
N
TYR
A
16
28.107
28.891
29.062
1.00
14.02
N


ATOM
81
CA
TYR
A
16
27.046
29.511
28.272
1.00
14.37
C


ATOM
82
CB
TYR
A
16
26.015
28.476
27.820
1.00
14.27
C


ATOM
83
CG
TYR
A
16
26.457
27.486
26.771
1.00
14.10
C


ATOM
84
CD1
TYR
A
16
26.364
27.788
25.409
1.00
14.43
C


ATOM
85
CE1
TYR
A
16
26.736
26.857
24.439
1.00
14.31
C


ATOM
86
CZ
TYR
A
16
27.183
25.603
24.832
1.00
14.50
C


ATOM
87
OH
TYR
A
16
27.547
24.671
23.889
1.00
14.16
O


ATOM
88
CE2
TYR
A
16
27.261
25.277
26.175
1.00
13.93
C


ATOM
89
CD2
TYR
A
16
26.889
26.212
27.134
1.00
14.54
C


ATOM
90
C
TYR
A
16
26.291
30.548
29.085
1.00
14.77
C


ATOM
91
O
TYR
A
16
26.019
30.347
30.275
1.00
14.91
O


ATOM
92
N
GLU
A
17
25.928
31.644
28.430
1.00
15.18
N


ATOM
93
CA
GLU
A
17
24.799
32.445
28.872
1.00
15.82
C


ATOM
94
CB
GLU
A
17
25.115
33.944
28.803
1.00
16.31
C


ATOM
95
CG
GLU
A
17
26.328
34.386
29.633
1.00
18.97
C


ATOM
96
CD
GLU
A
17
26.115
34.275
31.147
1.00
22.44
C


ATOM
97
OE1
GLU
A
17
24.980
34.008
31.591
1.00
24.46
O


ATOM
98
OE2
GLU
A
17
27.096
34.461
31.898
1.00
25.38
O


ATOM
99
C
GLU
A
17
23.646
32.098
27.949
1.00
15.59
C


ATOM
100
O
GLU
A
17
23.821
32.041
26.731
1.00
15.67
O


ATOM
101
N
THR
A
18
22.482
31.813
28.526
1.00
15.43
N


ATOM
102
CA
THR
A
18
21.321
31.413
27.731
1.00
15.37
C


ATOM
103
CB
THR
A
18
20.904
29.946
27.999
1.00
15.55
C


ATOM
104
OG1
THR
A
18
20.307
29.844
29.295
1.00
16.45
O


ATOM
105
CG2
THR
A
18
22.107
29.007
27.908
1.00
15.79
C


ATOM
106
C
THR
A
18
20.125
32.326
27.978
1.00
15.23
C


ATOM
107
O
THR
A
18
20.159
33.187
28.861
1.00
15.56
O


ATOM
108
N
PHE
A
19
19.070
32.129
27.193
1.00
15.09
N


ATOM
109
CA
PHE
A
19
17.858
32.930
27.312
1.00
14.91
C


ATOM
110
CB
PHE
A
19
17.279
33.237
25.928
1.00
14.79
C


ATOM
111
CG
PHE
A
19
18.037
34.296
25.175
1.00
14.13
C


ATOM
112
CD1
PHE
A
19
18.182
35.577
25.705
1.00
14.77
C


ATOM
113
CE1
PHE
A
19
18.878
36.565
25.009
1.00
14.06
C


ATOM
114
CZ
PHE
A
19
19.429
36.278
23.770
1.00
14.30
C


ATOM
115
CE2
PHE
A
19
19.286
35.008
23.223
1.00
14.16
C


ATOM
116
CD2
PHE
A
19
18.588
34.021
23.929
1.00
14.19
C


ATOM
117
C
PHE
A
19
16.805
32.262
28.196
1.00
15.28
C


ATOM
118
O
PHE
A
19
15.666
32.721
28.271
1.00
15.20
O


ATOM
119
N
GLY
A
20
17.197
31.189
28.877
1.00
15.71
N


ATOM
120
CA
GLY
A
20
16.289
30.508
29.789
1.00
16.41
C


ATOM
121
C
GLY
A
20
16.873
29.276
30.441
1.00
16.87
C


ATOM
122
O
GLY
A
20
17.980
28.849
30.113
1.00
16.68
O


ATOM
123
N
THR
A
21
16.096
28.690
31.347
1.00
17.63
N


ATOM
124
CA
THR
A
21
16.571
27.616
32.219
1.00
18.54
C


ATOM
125
CB
THR
A
21
15.754
27.555
33.532
1.00
18.77
C


ATOM
126
OG1
THR
A
21
14.374
27.333
33.227
1.00
20.19
O


ATOM
127
CG2
THR
A
21
15.892
28.859
34.318
1.00
19.50
C


ATOM
128
C
THR
A
21
16.543
26.234
31.559
1.00
18.69
C


ATOM
129
O
THR
A
21
17.235
25.315
32.007
1.00
18.83
O


ATOM
130
N
HIS
A
22
15.736
26.084
30.510
1.00
18.75
N


ATOM
131
CA
HIS
A
22
15.606
24.792
29.837
1.00
19.27
C


ATOM
132
CB
HIS
A
22
14.208
24.621
29.241
1.00
19.39
C


ATOM
133
CG
HIS
A
22
13.843
23.195
28.974
1.00
20.16
C


ATOM
134
ND1
HIS
A
22
12.795
22.562
29.608
1.00
21.93
N


ATOM
135
CE1
HIS
A
22
12.721
21.312
29.187
1.00
21.83
C


ATOM
136
NE2
HIS
A
22
13.689
21.108
28.312
1.00
22.15
N


ATOM
137
CD2
HIS
A
22
14.408
22.269
28.164
1.00
20.52
C


ATOM
138
C
HIS
A
22
16.676
24.606
28.756
1.00
19.53
C


ATOM
139
O
HIS
A
22
16.705
25.354
27.777
1.00
19.17
O


ATOM
140
N
PRO
A
23
17.546
23.588
28.921
1.00
19.58
N


ATOM
141
CA
PRO
A
23
18.676
23.383
28.003
1.00
19.95
C


ATOM
142
CB
PRO
A
23
19.424
22.192
28.616
1.00
20.08
C


ATOM
143
CG
PRO
A
23
18.910
22.066
30.005
1.00
20.23
C


ATOM
144
CD
PRO
A
23
17.515
22.569
29.985
1.00
19.70
C


ATOM
145
C
PRO
A
23
18.257
23.052
26.569
1.00
19.96
C


ATOM
146
O
PRO
A
23
19.047
23.243
25.641
1.00
20.25
O


ATOM
147
N
ALA
A
24
17.027
22.567
26.396
1.00
19.92
N


ATOM
148
CA
ALA
A
24
16.505
22.202
25.079
1.00
19.89
C


ATOM
149
CB
ALA
A
24
15.819
20.842
25.137
1.00
20.01
C


ATOM
150
C
ALA
A
24
15.551
23.252
24.511
1.00
19.82
C


ATOM
151
O
ALA
A
24
15.642
23.607
23.333
1.00
20.09
O


ATOM
152
N
LEU
A
25
14.644
23.745
25.354
1.00
19.43
N


ATOM
153
CA
LEU
A
25
13.538
24.597
24.900
1.00
19.28
C


ATOM
154
CB
LEU
A
25
12.261
24.295
25.690
1.00
19.47
C


ATOM
155
CG
LEU
A
25
11.674
22.888
25.528
1.00
20.18
C


ATOM
156
CD1
LEU
A
25
10.377
22.760
26.309
1.00
20.77
C


ATOM
157
CD2
LEU
A
25
11.457
22.536
24.060
1.00
21.08
C


ATOM
158
C
LEU
A
25
13.850
26.089
24.944
1.00
18.94
C


ATOM
159
O
LEU
A
25
13.148
26.895
24.326
1.00
19.13
O


ATOM
160
N
ASP
A
26
14.896
26.456
25.677
1.00
18.37
N


ATOM
161
CA
ASP
A
26
15.397
27.823
25.650
1.00
17.98
C


ATOM
162
CB
ASP
A
26
15.625
28.343
27.071
1.00
17.69
C


ATOM
163
CG
ASP
A
26
14.321
28.595
27.815
1.00
18.14
C


ATOM
164
OD1
ASP
A
26
13.507
29.412
27.334
1.00
17.60
O


ATOM
165
OD2
ASP
A
26
14.115
27.987
28.888
1.00
18.41
O


ATOM
166
C
ASP
A
26
16.678
27.896
24.825
1.00
17.72
C


ATOM
167
O
ASP
A
26
17.450
26.938
24.775
1.00
18.49
O


ATOM
168
N
ARG
A
27
16.894
29.031
24.168
1.00
16.86
N


ATOM
169
CA
ARG
A
27
18.006
29.167
23.228
1.00
16.22
C


ATOM
170
CB
ARG
A
27
17.592
30.017
22.019
1.00
16.09
C


ATOM
171
CG
ARG
A
27
16.238
29.659
21.425
1.00
16.52
C


ATOM
172
CD
ARG
A
27
16.260
28.368
20.612
1.00
16.60
C


ATOM
173
NE
ARG
A
27
14.902
27.860
20.429
1.00
17.60
N


ATOM
174
CZ
ARG
A
27
14.077
28.230
19.452
1.00
17.84
C


ATOM
175
NH1
ARG
A
27
14.468
29.105
18.525
1.00
17.82
N


ATOM
176
NH2
ARG
A
27
12.856
27.715
19.395
1.00
18.04
N


ATOM
177
C
ARG
A
27
19.239
29.772
23.894
1.00
15.87
C


ATOM
178
O
ARG
A
27
19.115
30.575
24.826
1.00
15.56
O


ATOM
179
N
PRO
A
28
20.440
29.389
23.417
1.00
15.52
N


ATOM
180
CA
PRO
A
28
21.668
29.978
23.942
1.00
15.49
C


ATOM
181
CB
PRO
A
28
22.764
29.122
23.307
1.00
15.36
C


ATOM
182
CG
PRO
A
28
22.155
28.610
22.047
1.00
15.52
C


ATOM
183
CD
PRO
A
28
20.712
28.388
22.365
1.00
15.47
C


ATOM
184
C
PRO
A
28
21.803
31.429
23.494
1.00
15.32
C


ATOM
185
O
PRO
A
28
21.260
31.807
22.450
1.00
15.54
O


ATOM
186
N
ALA
A
29
22.508
32.230
24.285
1.00
14.92
N


ATOM
187
CA
ALA
A
29
22.746
33.633
23.952
1.00
15.06
C


ATOM
188
CB
ALA
A
29
22.303
34.528
25.094
1.00
14.98
C


ATOM
189
C
ALA
A
29
24.215
33.876
23.634
1.00
14.92
C


ATOM
190
O
ALA
A
29
24.547
34.556
22.658
1.00
14.81
O


ATOM
191
N
GLN
A
30
25.093
33.312
24.462
1.00
14.93
N


ATOM
192
CA
GLN
A
30
26.525
33.567
24.368
1.00
15.30
C


ATOM
193
CB
GLN
A
30
26.892
34.783
25.227
1.00
15.18
C


ATOM
194
CG
GLN
A
30
28.320
35.283
25.073
1.00
16.92
C


ATOM
195
CD
GLN
A
30
28.708
36.258
26.167
1.00
17.27
C


ATOM
196
OE1
GLN
A
30
28.784
35.893
27.343
1.00
21.13
O


ATOM
197
NE2
GLN
A
30
28.960
37.508
25.787
1.00
20.44
N


ATOM
198
C
GLN
A
30
27.324
32.349
24.820
1.00
14.87
C


ATOM
199
O
GLN
A
30
26.937
31.660
25.763
1.00
15.19
O


ATOM
200
N
PHE
A
31
28.433
32.093
24.130
1.00
14.51
N


ATOM
201
CA
PHE
A
31
29.388
31.056
24.513
1.00
14.29
C


ATOM
202
CB
PHE
A
31
29.530
30.030
23.383
1.00
14.25
C


ATOM
203
CG
PHE
A
31
30.586
28.974
23.625
1.00
14.20
C


ATOM
204
CD1
PHE
A
31
30.260
27.765
24.239
1.00
14.04
C


ATOM
205
CE1
PHE
A
31
31.232
26.779
24.438
1.00
13.99
C


ATOM
206
CZ
PHE
A
31
32.537
26.995
24.002
1.00
13.88
C


ATOM
207
CE2
PHE
A
31
32.868
28.190
23.376
1.00
14.18
C


ATOM
208
CD2
PHE
A
31
31.895
29.169
23.188
1.00
13.96
C


ATOM
209
C
PHE
A
31
30.729
31.719
24.804
1.00
14.32
C


ATOM
210
O
PHE
A
31
31.167
32.598
24.064
1.00
14.16
O


ATOM
211
N
ALA
A
32
31.363
31.306
25.897
1.00
14.37
N


ATOM
212
CA
ALA
A
32
32.673
31.822
26.271
1.00
14.83
C


ATOM
213
CB
ALA
A
32
32.552
32.794
27.429
1.00
14.68
C


ATOM
214
C
ALA
A
32
33.569
30.661
26.645
1.00
14.99
C


ATOM
215
O
ALA
A
32
33.130
29.733
27.322
1.00
15.38
O


ATOM
216
N
ALA
A
33
34.819
30.705
26.194
1.00
15.45
N


ATOM
217
CA
ALA
A
33
35.768
29.635
26.482
1.00
15.71
C


ATOM
218
CB
ALA
A
33
35.554
28.458
25.536
1.00
15.98
C


ATOM
219
C
ALA
A
33
37.206
30.109
26.411
1.00
16.12
C


ATOM
220
O
ALA
A
33
37.517
31.089
25.730
1.00
16.43
O


ATOM
221
N
ILE
A
34
38.079
29.410
27.128
1.00
16.39
N


ATOM
222
CA
ILE
A
34
39.519
29.580
26.971
1.00
16.74
C


ATOM
223
CB
ILE
A
34
40.071
30.740
27.850
1.00
17.07
C


ATOM
224
CG1
ILE
A
34
41.369
31.304
27.257
1.00
17.60
C


ATOM
225
CD1
ILE
A
34
41.647
32.748
27.650
1.00
18.75
C


ATOM
226
CG2
ILE
A
34
40.241
30.302
29.298
1.00
16.97
C


ATOM
227
C
ILE
A
34
40.236
28.261
27.254
1.00
16.68
C


ATOM
228
O
ILE
A
34
39.808
27.477
28.108
1.00
16.42
O


ATOM
229
N
ARG
A
35
41.306
28.013
26.507
1.00
16.69
N


ATOM
230
CA
ARG
A
35
42.080
26.789
26.647
1.00
16.85
C


ATOM
231
CB
ARG
A
35
42.550
26.303
25.271
1.00
16.75
C


ATOM
232
CG
ARG
A
35
43.051
24.867
25.249
1.00
17.00
C


ATOM
233
CD
ARG
A
35
43.346
24.394
23.830
1.00
17.03
C


ATOM
234
NE
ARG
A
35
42.146
24.346
22.992
1.00
17.29
N


ATOM
235
CZ
ARG
A
35
41.310
23.311
22.921
1.00
17.56
C


ATOM
236
NH1
ARG
A
35
41.523
22.219
23.646
1.00
17.86
N


ATOM
237
NH2
ARG
A
35
40.255
23.370
22.121
1.00
17.90
N


ATOM
238
C
ARG
A
35
43.272
27.017
27.573
1.00
17.06
C


ATOM
239
O
ARG
A
35
43.894
28.085
27.546
1.00
17.08
O


ATOM
240
N
THR
A
36
43.564
26.022
28.413
1.00
17.31
N


ATOM
241
CA
THR
A
36
44.743
26.052
29.282
1.00
17.83
C


ATOM
242
CB
THR
A
36
44.370
26.175
30.793
1.00
18.01
C


ATOM
243
OG1
THR
A
36
43.932
24.906
31.296
1.00
18.26
O


ATOM
244
CG2
THR
A
36
43.289
27.226
31.025
1.00
17.90
C


ATOM
245
C
THR
A
36
45.570
24.783
29.100
1.00
18.08
C


ATOM
246
O
THR
A
36
45.066
23.775
28.599
1.00
17.81
O


ATOM
247
N
ASP
A
37
46.834
24.830
29.517
1.00
18.48
N


ATOM
248
CA
ASP
A
37
47.650
23.621
29.582
1.00
19.18
C


ATOM
249
CB
ASP
A
37
49.158
23.952
29.575
1.00
19.15
C


ATOM
250
CG
ASP
A
37
49.610
24.746
30.798
1.00
19.92
C


ATOM
251
OD1
ASP
A
37
48.833
24.894
31.765
1.00
20.67
O


ATOM
252
OD2
ASP
A
37
50.771
25.219
30.787
1.00
20.60
O


ATOM
253
C
ASP
A
37
47.257
22.774
30.797
1.00
19.55
C


ATOM
254
O
ASP
A
37
46.341
23.136
31.547
1.00
19.64
O


ATOM
255
N
SER
A
38
47.947
21.653
30.988
1.00
20.21
N


ATOM
256
CA
SER
A
38
47.623
20.716
32.066
1.00
20.94
C


ATOM
257
CB
SER
A
38
48.441
19.432
31.917
1.00
20.98
C


ATOM
258
OG
SER
A
38
49.829
19.713
31.908
1.00
21.79
O


ATOM
259
C
SER
A
38
47.824
21.313
33.462
1.00
21.25
C


ATOM
260
O
SER
A
38
47.371
20.741
34.457
1.00
21.58
O


ATOM
261
N
GLU
A
39
48.494
22.466
33.522
1.00
21.48
N


ATOM
262
CA
GLU
A
39
48.767
23.153
34.789
1.00
21.82
C


ATOM
263
CB
GLU
A
39
50.256
23.507
34.896
1.00
22.13
C


ATOM
264
CG
GLU
A
39
51.180
22.296
35.015
1.00
23.91
C


ATOM
265
CD
GLU
A
39
50.916
21.476
36.267
1.00
26.19
C


ATOM
266
OE1
GLU
A
39
50.905
22.057
37.373
1.00
27.78
O


ATOM
267
OE2
GLU
A
39
50.718
20.248
36.143
1.00
27.92
O


ATOM
268
C
GLU
A
39
47.901
24.405
34.972
1.00
21.65
C


ATOM
269
O
GLU
A
39
48.106
25.183
35.909
1.00
21.67
O


ATOM
270
N
PHE
A
40
46.930
24.576
34.072
1.00
21.49
N


ATOM
271
CA
PHE
A
40
45.956
25.683
34.112
1.00
21.58
C


ATOM
272
CB
PHE
A
40
45.230
25.759
35.469
1.00
21.41
C


ATOM
273
CG
PHE
A
40
44.506
24.493
35.841
1.00
21.31
C


ATOM
274
CD1
PHE
A
40
43.623
23.889
34.948
1.00
21.03
C


ATOM
275
CE1
PHE
A
40
42.954
22.716
35.289
1.00
20.68
C


ATOM
276
CZ
PHE
A
40
43.160
22.140
36.536
1.00
21.44
C


ATOM
277
CE2
PHE
A
40
44.032
22.736
37.438
1.00
21.87
C


ATOM
278
CD2
PHE
A
40
44.701
23.908
37.089
1.00
21.78
C


ATOM
279
C
PHE
A
40
46.511
27.052
33.698
1.00
21.77
C


ATOM
280
O
PHE
A
40
45.916
28.089
34.008
1.00
21.87
O


ATOM
281
N
ASN
A
41
47.641
27.045
32.992
1.00
22.05
N


ATOM
282
CA
ASN
A
41
48.137
28.245
32.320
1.00
22.27
C


ATOM
283
CB
ASN
A
41
49.645
28.150
32.056
1.00
22.41
C


ATOM
284
CG
ASN
A
41
50.438
27.769
33.292
1.00
22.55
C


ATOM
285
OD1
ASN
A
41
51.112
26.738
33.314
1.00
23.79
O


ATOM
286
ND2
ASN
A
41
50.363
28.596
34.327
1.00
23.32
N


ATOM
287
C
ASN
A
41
47.401
28.432
31.003
1.00
22.47
C


ATOM
288
O
ASN
A
41
47.337
27.510
30.188
1.00
22.33
O


ATOM
289
N
VAL
A
42
46.845
29.625
30.802
1.00
22.96
N


ATOM
290
CA
VAL
A
42
46.115
29.951
29.574
1.00
23.38
C


ATOM
291
CB
VAL
A
42
45.518
31.385
29.639
1.00
23.30
C


ATOM
292
CG1
VAL
A
42
44.983
31.817
28.284
1.00
23.40
C


ATOM
293
CG2
VAL
A
42
44.424
31.462
30.698
1.00
23.15
C


ATOM
294
C
VAL
A
42
47.030
29.815
28.356
1.00
23.84
C


ATOM
295
O
VAL
A
42
48.157
30.317
28.362
1.00
23.83
O


ATOM
296
N
ILE
A
43
46.556
29.115
27.326
1.00
24.38
N


ATOM
297
CA
ILE
A
43
47.357
28.921
26.108
1.00
25.12
C


ATOM
298
CB
ILE
A
43
47.824
27.443
25.918
1.00
25.11
C


ATOM
299
CG1
ILE
A
43
46.631
26.485
25.871
1.00
25.16
C


ATOM
300
CD1
ILE
A
43
47.007
25.063
25.503
1.00
25.21
C


ATOM
301
CG2
ILE
A
43
48.812
27.044
27.017
1.00
25.45
C


ATOM
302
C
ILE
A
43
46.712
29.462
24.825
1.00
25.54
C


ATOM
303
O
ILE
A
43
47.378
29.587
23.795
1.00
25.90
O


ATOM
304
N
GLY
A
44
45.425
29.786
24.889
1.00
25.87
N


ATOM
305
CA
GLY
A
44
44.735
30.348
23.733
1.00
26.38
C


ATOM
306
C
GLY
A
44
44.261
31.774
23.945
1.00
26.59
C


ATOM
307
O
GLY
A
44
44.393
32.332
25.039
1.00
26.91
O


ATOM
308
N
GLU
A
45
43.730
32.372
22.882
1.00
26.48
N


ATOM
309
CA
GLU
A
45
42.979
33.615
22.993
1.00
26.37
C


ATOM
310
CB
GLU
A
45
42.892
34.320
21.633
1.00
26.59
C


ATOM
311
CG
GLU
A
45
44.230
34.835
21.095
1.00
27.78
C


ATOM
312
CD
GLU
A
45
44.871
35.883
21.994
1.00
29.22
C


ATOM
313
OE1
GLU
A
45
44.152
36.792
22.468
1.00
30.39
O


ATOM
314
OE2
GLU
A
45
46.097
35.799
22.219
1.00
30.40
O


ATOM
315
C
GLU
A
45
41.577
33.286
23.501
1.00
25.89
C


ATOM
316
O
GLU
A
45
41.081
32.181
23.260
1.00
25.87
O


ATOM
317
N
PRO
A
46
40.936
34.235
24.216
1.00
25.47
N


ATOM
318
CA
PRO
A
46
39.554
34.018
24.645
1.00
25.05
C


ATOM
319
CB
PRO
A
46
39.207
35.315
25.390
1.00
25.19
C


ATOM
320
CG
PRO
A
46
40.521
35.900
25.775
1.00
25.39
C


ATOM
321
CD
PRO
A
46
41.454
35.537
24.673
1.00
25.43
C


ATOM
322
C
PRO
A
46
38.619
33.829
23.452
1.00
24.60
C


ATOM
323
O
PRO
A
46
38.751
34.527
22.440
1.00
24.34
O


ATOM
324
N
GLU
A
47
37.705
32.871
23.567
1.00
23.93
N


ATOM
325
CA
GLU
A
47
36.691
32.636
22.546
1.00
23.56
C


ATOM
326
CB
GLU
A
47
36.653
31.152
22.154
1.00
23.73
C


ATOM
327
CG
GLU
A
47
37.983
30.581
21.659
1.00
25.05
C


ATOM
328
CD
GLU
A
47
38.238
30.848
20.184
1.00
26.33
C


ATOM
329
OE1
GLU
A
47
37.274
31.162
19.448
1.00
27.07
O


ATOM
330
OE2
GLU
A
47
39.407
30.731
19.758
1.00
27.50
O


ATOM
331
C
GLU
A
47
35.331
33.059
23.086
1.00
22.90
C


ATOM
332
O
GLU
A
47
34.768
32.393
23.951
1.00
22.80
O


ATOM
333
N
VAL
A
48
34.818
34.183
22.590
1.00
22.04
N


ATOM
334
CA
VAL
A
48
33.505
34.686
23.005
1.00
21.35
C


ATOM
335
CB
VAL
A
48
33.618
35.928
23.945
1.00
21.57
C


ATOM
336
CG1
VAL
A
48
32.234
36.405
24.380
1.00
21.71
C


ATOM
337
CG2
VAL
A
48
34.471
35.613
25.167
1.00
21.88
C


ATOM
338
C
VAL
A
48
32.676
35.054
21.780
1.00
20.67
C


ATOM
339
O
VAL
A
48
33.097
35.879
20.964
1.00
20.73
O


ATOM
340
N
PHE
A
49
31.501
34.440
21.653
1.00
19.66
N


ATOM
341
CA
PHE
A
49
30.592
34.741
20.540
1.00
18.82
C


ATOM
342
CB
PHE
A
49
30.970
33.953
19.274
1.00
18.80
C


ATOM
343
CG
PHE
A
49
31.245
32.492
19.515
1.00
18.76
C


ATOM
344
CD1
PHE
A
49
30.229
31.553
19.400
1.00
18.52
C


ATOM
345
CE1
PHE
A
49
30.482
30.198
19.615
1.00
18.18
C


ATOM
346
CZ
PHE
A
49
31.769
29.776
19.935
1.00
18.18
C


ATOM
347
CE2
PHE
A
49
32.794
30.705
20.046
1.00
18.51
C


ATOM
348
CD2
PHE
A
49
32.531
32.056
19.834
1.00
19.00
C


ATOM
349
C
PHE
A
49
29.117
34.544
20.892
1.00
18.46
C


ATOM
350
O
PHE
A
49
28.780
33.815
21.828
1.00
17.58
O


ATOM
351
N
TYR
A
50
28.250
35.212
20.135
1.00
18.22
N


ATOM
352
CA
TYR
A
50
26.816
35.216
20.398
1.00
18.09
C


ATOM
353
CB
TYR
A
50
26.254
36.637
20.273
1.00
18.60
C


ATOM
354
CG
TYR
A
50
26.723
37.606
21.337
1.00
19.37
C


ATOM
355
CD1
TYR
A
50
26.026
37.742
22.536
1.00
20.46
C


ATOM
356
CE1
TYR
A
50
26.444
38.637
23.515
1.00
21.26
C


ATOM
357
CZ
TYR
A
50
27.567
39.415
23.296
1.00
21.36
C


ATOM
358
OH
TYR
A
50
27.978
40.303
24.269
1.00
22.46
O


ATOM
359
CE2
TYR
A
50
28.276
39.306
22.110
1.00
21.29
C


ATOM
360
CD2
TYR
A
50
27.849
38.405
21.135
1.00
20.77
C


ATOM
361
C
TYR
A
50
26.063
34.294
19.444
1.00
17.58
C


ATOM
362
O
TYR
A
50
26.562
33.948
18.364
1.00
17.36
O


ATOM
363
N
CYS
A
51
24.856
33.904
19.849
1.00
17.04
N


ATOM
364
CA
CYS
A
51
23.968
33.130
18.995
1.00
16.99
C


ATOM
365
CB
CYS
A
51
23.567
31.818
19.673
1.00
16.78
C


ATOM
366
SG
CYS
A
51
22.709
30.666
18.576
1.00
16.89
S


ATOM
367
C
CYS
A
51
22.722
33.933
18.664
1.00
17.11
C


ATOM
368
O
CYS
A
51
22.016
34.396
19.563
1.00
16.98
O


ATOM
369
N
LYS
A
52
22.463
34.103
17.370
1.00
17.43
N


ATOM
370
CA
LYS
A
52
21.241
34.744
16.906
1.00
18.04
C


ATOM
371
CB
LYS
A
52
21.341
35.057
15.409
1.00
18.17
C


ATOM
372
CG
LYS
A
52
20.124
35.756
14.829
1.00
19.34
C


ATOM
373
CD
LYS
A
52
20.271
35.964
13.328
1.00
20.17
C


ATOM
374
CE
LYS
A
52
19.036
36.630
12.746
1.00
22.70
C


ATOM
375
NZ
LYS
A
52
19.139
36.808
11.270
1.00
24.68
N


ATOM
376
C
LYS
A
52
20.040
33.836
17.189
1.00
17.92
C


ATOM
377
O
LYS
A
52
20.015
32.684
16.745
1.00
18.27
O


ATOM
378
N
PRO
A
53
19.055
34.341
17.956
1.00
18.06
N


ATOM
379
CA
PRO
A
53
17.838
33.564
18.180
1.00
18.09
C


ATOM
380
CB
PRO
A
53
17.218
34.233
19.408
1.00
18.04
C


ATOM
381
CG
PRO
A
53
17.685
35.652
19.343
1.00
18.12
C


ATOM
382
CD
PRO
A
53
19.032
35.636
18.667
1.00
18.06
C


ATOM
383
C
PRO
A
53
16.887
33.637
16.986
1.00
18.25
C


ATOM
384
O
PRO
A
53
16.646
34.723
16.450
1.00
18.68
O


ATOM
385
N
ALA
A
54
16.357
32.484
16.579
1.00
18.31
N


ATOM
386
CA
ALA
A
54
15.371
32.417
15.501
1.00
18.29
C


ATOM
387
CB
ALA
A
54
15.082
30.978
15.145
1.00
18.39
C


ATOM
388
C
ALA
A
54
14.078
33.142
15.882
1.00
18.36
C


ATOM
389
O
ALA
A
54
13.818
33.383
17.062
1.00
18.35
O


ATOM
390
N
ASP
A
55
13.265
33.475
14.882
1.00
18.43
N


ATOM
391
CA
ASP
A
55
12.073
34.295
15.110
1.00
18.66
C


ATOM
392
CB
ASP
A
55
11.730
35.128
13.861
1.00
19.05
C


ATOM
393
CG
ASP
A
55
11.266
34.278
12.683
1.00
20.25
C


ATOM
394
OD1
ASP
A
55
11.256
33.029
12.783
1.00
21.62
O


ATOM
395
OD2
ASP
A
55
10.908
34.873
11.646
1.00
22.14
O


ATOM
396
C
ASP
A
55
10.840
33.525
15.620
1.00
18.39
C


ATOM
397
O
ASP
A
55
9.716
34.029
15.555
1.00
18.35
O


ATOM
398
N
ASP
A
56
11.060
32.317
16.139
1.00
18.02
N


ATOM
399
CA
ASP
A
56
9.980
31.526
16.731
1.00
17.85
C


ATOM
400
CB
ASP
A
56
9.946
30.112
16.127
1.00
17.87
C


ATOM
401
CG
ASP
A
56
11.154
29.263
16.527
1.00
18.36
C


ATOM
402
OD1
ASP
A
56
12.229
29.830
16.825
1.00
18.82
O


ATOM
403
OD2
ASP
A
56
11.024
28.021
16.537
1.00
19.81
O


ATOM
404
C
ASP
A
56
10.100
31.458
18.256
1.00
17.49
C


ATOM
405
O
ASP
A
56
9.523
30.577
18.894
1.00
17.77
O


ATOM
406
N
TYR
A
57
10.831
32.407
18.834
1.00
17.09
N


ATOM
407
CA
TYR
A
57
11.226
32.310
20.234
1.00
16.68
C


ATOM
408
CB
TYR
A
57
12.593
31.619
20.334
1.00
16.45
C


ATOM
409
CG
TYR
A
57
13.141
31.500
21.741
1.00
16.16
C


ATOM
410
CD1
TYR
A
57
12.652
30.533
22.623
1.00
15.88
C


ATOM
411
CE1
TYR
A
57
13.156
30.419
23.916
1.00
16.09
C


ATOM
412
CZ
TYR
A
57
14.166
31.272
24.335
1.00
16.18
C


ATOM
413
OH
TYR
A
57
14.666
31.160
25.611
1.00
16.26
O


ATOM
414
CE2
TYR
A
57
14.673
32.236
23.475
1.00
15.81
C


ATOM
415
CD2
TYR
A
57
14.158
32.346
22.186
1.00
15.91
C


ATOM
416
C
TYR
A
57
11.273
33.658
20.939
1.00
16.54
C


ATOM
417
O
TYR
A
57
11.759
34.645
20.383
1.00
16.53
O


ATOM
418
N
LEU
A
58
10.761
33.686
22.169
1.00
16.33
N


ATOM
419
CA
LEU
A
58
10.957
34.815
23.072
1.00
16.43
C


ATOM
420
CB
LEU
A
58
9.616
35.427
23.489
1.00
16.46
C


ATOM
421
CG
LEU
A
58
8.817
36.202
22.440
1.00
16.58
C


ATOM
422
CD1
LEU
A
58
7.510
36.695
23.041
1.00
17.29
C


ATOM
423
CD2
LEU
A
58
9.622
37.367
21.896
1.00
17.31
C


ATOM
424
C
LEU
A
58
11.725
34.358
24.308
1.00
16.45
C


ATOM
425
O
LEU
A
58
11.401
33.318
24.890
1.00
16.17
O


ATOM
426
N
PRO
A
59
12.759
35.123
24.705
1.00
16.50
N


ATOM
427
CA
PRO
A
59
13.555
34.769
25.886
1.00
16.57
C


ATOM
428
CB
PRO
A
59
14.676
35.815
25.881
1.00
16.63
C


ATOM
429
CG
PRO
A
59
14.144
36.948
25.089
1.00
16.92
C


ATOM
430
CD
PRO
A
59
13.250
36.352
24.056
1.00
16.58
C


ATOM
431
C
PRO
A
59
12.768
34.872
27.186
1.00
16.86
C


ATOM
432
O
PRO
A
59
11.827
35.660
27.281
1.00
16.89
O


ATOM
433
N
GLN
A
60
13.153
34.074
28.178
1.00
16.97
N


ATOM
434
CA
GLN
A
60
12.611
34.229
29.523
1.00
17.66
C


ATOM
435
CB
GLN
A
60
13.008
33.048
30.410
1.00
17.54
C


ATOM
436
CG
GLN
A
60
12.432
31.705
29.978
1.00
18.84
C


ATOM
437
CD
GLN
A
60
12.727
30.588
30.973
1.00
19.43
C


ATOM
438
OE1
GLN
A
60
13.691
30.656
31.742
1.00
21.53
O


ATOM
439
NE2
GLN
A
60
11.897
29.549
30.957
1.00
21.90
N


ATOM
440
C
GLN
A
60
13.150
35.528
30.116
1.00
17.55
C


ATOM
441
O
GLN
A
60
14.365
35.718
30.178
1.00
17.29
O


ATOM
442
N
PRO
A
61
12.247
36.437
30.537
1.00
17.70
N


ATOM
443
CA
PRO
A
61
12.679
37.711
31.118
1.00
17.82
C


ATOM
444
CB
PRO
A
61
11.366
38.338
31.598
1.00
17.83
C


ATOM
445
CG
PRO
A
61
10.328
37.751
30.706
1.00
17.88
C


ATOM
446
CD
PRO
A
61
10.776
36.337
30.469
1.00
17.59
C


ATOM
447
C
PRO
A
61
13.670
37.547
32.281
1.00
17.86
C


ATOM
448
O
PRO
A
61
14.646
38.295
32.369
1.00
18.00
O


ATOM
449
N
GLY
A
62
13.434
36.562
33.147
1.00
18.02
N


ATOM
450
CA
GLY
A
62
14.322
36.305
34.282
1.00
18.01
C


ATOM
451
C
GLY
A
62
15.761
36.037
33.878
1.00
18.02
C


ATOM
452
O
GLY
A
62
16.700
36.513
34.528
1.00
18.40
O


ATOM
453
N
ALA
A
63
15.936
35.281
32.796
1.00
17.90
N


ATOM
454
CA
ALA
A
63
17.265
34.950
32.289
1.00
17.51
C


ATOM
455
CB
ALA
A
63
17.169
33.921
31.177
1.00
17.69
C


ATOM
456
C
ALA
A
63
18.011
36.190
31.808
1.00
17.37
C


ATOM
457
O
ALA
A
63
19.200
36.348
32.079
1.00
17.33
O


ATOM
458
N
VAL
A
64
17.301
37.064
31.097
1.00
17.23
N


ATOM
459
CA
VAL
A
64
17.880
38.305
30.577
1.00
17.18
C


ATOM
460
CB
VAL
A
64
16.917
39.010
29.582
1.00
17.00
C


ATOM
461
CG1
VAL
A
64
17.491
40.346
29.104
1.00
17.01
C


ATOM
462
CG2
VAL
A
64
16.627
38.096
28.394
1.00
17.42
C


ATOM
463
C
VAL
A
64
18.282
39.249
31.714
1.00
17.28
C


ATOM
464
O
VAL
A
64
19.290
39.942
31.621
1.00
17.15
O


ATOM
465
N
LEU
A
65
17.505
39.251
32.796
1.00
17.61
N


ATOM
466
CA
LEU
A
65
17.850
40.051
33.973
1.00
18.18
C


ATOM
467
CB
LEU
A
65
16.699
40.071
34.984
1.00
18.22
C


ATOM
468
CG
LEU
A
65
15.440
40.838
34.569
1.00
18.35
C


ATOM
469
CD1
LEU
A
65
14.403
40.795
35.680
1.00
19.16
C


ATOM
470
CD2
LEU
A
65
15.769
42.282
34.197
1.00
19.05
C


ATOM
471
C
LEU
A
65
19.141
39.570
34.638
1.00
18.47
C


ATOM
472
O
LEU
A
65
19.884
40.366
35.216
1.00
18.98
O


ATOM
473
N
ILE
A
66
19.399
38.268
34.547
1.00
18.79
N


ATOM
474
CA
ILE
A
66
20.634
37.682
35.064
1.00
19.06
C


ATOM
475
CB
ILE
A
66
20.492
36.143
35.271
1.00
19.18
C


ATOM
476
CG1
ILE
A
66
19.574
35.852
36.463
1.00
19.58
C


ATOM
477
CD1
ILE
A
66
19.065
34.424
36.520
1.00
20.67
C


ATOM
478
CG2
ILE
A
66
21.859
35.487
35.478
1.00
19.53
C


ATOM
479
C
ILE
A
66
21.832
37.997
34.158
1.00
19.02
C


ATOM
480
O
ILE
A
66
22.865
38.473
34.633
1.00
19.54
O


ATOM
481
N
THR
A
67
21.674
37.753
32.855
1.00
18.77
N


ATOM
482
CA
THR
A
67
22.793
37.823
31.905
1.00
18.49
C


ATOM
483
CB
THR
A
67
22.530
36.957
30.655
1.00
18.46
C


ATOM
484
OG1
THR
A
67
21.456
37.528
29.899
1.00
18.33
O


ATOM
485
CG2
THR
A
67
22.173
35.529
31.045
1.00
18.45
C


ATOM
486
C
THR
A
67
23.083
39.242
31.427
1.00
18.41
C


ATOM
487
O
THR
A
67
24.235
39.584
31.137
1.00
18.90
O


ATOM
488
N
GLY
A
68
22.034
40.053
31.314
1.00
18.06
N


ATOM
489
CA
GLY
A
68
22.158
41.394
30.748
1.00
17.48
C


ATOM
490
C
GLY
A
68
22.275
41.401
29.230
1.00
17.28
C


ATOM
491
O
GLY
A
68
22.572
42.438
28.630
1.00
17.58
O


ATOM
492
N
ILE
A
69
22.044
40.244
28.609
1.00
16.85
N


ATOM
493
CA
ILE
A
69
22.078
40.125
27.150
1.00
16.50
C


ATOM
494
CB
ILE
A
69
22.809
38.837
26.680
1.00
16.56
C


ATOM
495
CG1
ILE
A
69
24.216
38.750
27.280
1.00
16.54
C


ATOM
496
CD1
ILE
A
69
24.861
37.363
27.157
1.00
17.06
C


ATOM
497
CG2
ILE
A
69
22.872
38.785
25.145
1.00
16.48
C


ATOM
498
C
ILE
A
69
20.660
40.120
26.590
1.00
16.10
C


ATOM
499
O
ILE
A
69
19.892
39.184
26.826
1.00
16.02
O


ATOM
500
N
THR
A
70
20.321
41.173
25.853
1.00
15.70
N


ATOM
501
CA
THR
A
70
19.012
41.286
25.215
1.00
15.32
C


ATOM
502
CB
THR
A
70
18.698
42.744
24.825
1.00
15.31
C


ATOM
503
OG1
THR
A
70
19.668
43.208
23.876
1.00
15.64
O


ATOM
504
CG2
THR
A
70
18.711
43.648
26.050
1.00
15.43
C


ATOM
505
C
THR
A
70
18.971
40.425
23.954
1.00
15.06
C


ATOM
506
O
THR
A
70
20.015
40.135
23.371
1.00
14.70
O


ATOM
507
N
PRO
A
71
17.761
40.007
23.529
1.00
14.88
N


ATOM
508
CA
PRO
A
71
17.639
39.311
22.246
1.00
14.75
C


ATOM
509
CB
PRO
A
71
16.137
39.025
22.136
1.00
14.86
C


ATOM
510
CG
PRO
A
71
15.486
39.960
23.119
1.00
14.89
C


ATOM
511
CD
PRO
A
71
16.464
40.138
24.217
1.00
14.80
C


ATOM
512
C
PRO
A
71
18.119
40.173
21.070
1.00
14.66
C


ATOM
513
O
PRO
A
71
18.645
39.638
20.094
1.00
14.71
O


ATOM
514
N
GLN
A
72
17.956
41.493
21.182
1.00
14.69
N


ATOM
515
CA
GLN
A
72
18.452
42.428
20.165
1.00
14.86
C


ATOM
516
CB
GLN
A
72
18.028
43.867
20.479
1.00
14.82
C


ATOM
517
CG
GLN
A
72
16.529
44.127
20.387
1.00
14.90
C


ATOM
518
CD
GLN
A
72
15.826
44.050
21.731
1.00
15.27
C


ATOM
519
OE1
GLN
A
72
16.242
43.314
22.625
1.00
15.46
O


ATOM
520
NE2
GLN
A
72
14.752
44.818
21.877
1.00
15.57
N


ATOM
521
C
GLN
A
72
19.973
42.359
20.013
1.00
14.93
C


ATOM
522
O
GLN
A
72
20.492
42.350
18.892
1.00
14.77
O


ATOM
523
N
GLU
A
73
20.682
42.327
21.140
1.00
15.09
N


ATOM
524
CA
GLU
A
73
22.139
42.233
21.113
1.00
15.36
C


ATOM
525
CB
GLU
A
73
22.739
42.416
22.508
1.00
15.71
C


ATOM
526
CG
GLU
A
73
24.267
42.367
22.512
1.00
17.54
C


ATOM
527
CD
GLU
A
73
24.883
42.870
23.799
1.00
20.20
C


ATOM
528
OE1
GLU
A
73
24.331
42.579
24.883
1.00
21.84
O


ATOM
529
OE2
GLU
A
73
25.933
43.545
23.724
1.00
21.38
O


ATOM
530
C
GLU
A
73
22.607
40.915
20.496
1.00
15.01
C


ATOM
531
O
GLU
A
73
23.488
40.910
19.636
1.00
14.92
O


ATOM
532
N
ALA
A
74
22.011
39.803
20.927
1.00
14.76
N


ATOM
533
CA
ALA
A
74
22.388
38.488
20.400
1.00
14.83
C


ATOM
534
CB
ALA
A
74
21.705
37.381
21.180
1.00
14.82
C


ATOM
535
C
ALA
A
74
22.073
38.377
18.908
1.00
14.98
C


ATOM
536
O
ALA
A
74
22.842
37.791
18.145
1.00
14.87
O


ATOM
537
N
ARG
A
75
20.946
38.957
18.498
1.00
15.07
N


ATOM
538
CA
ARG
A
75
20.556
38.966
17.091
1.00
15.58
C


ATOM
539
CB
ARG
A
75
19.128
39.494
16.930
1.00
15.60
C


ATOM
540
CG
ARG
A
75
18.630
39.522
15.492
1.00
17.28
C


ATOM
541
CD
ARG
A
75
17.152
39.856
15.424
1.00
18.48
C


ATOM
542
NE
ARG
A
75
16.876
41.253
15.761
1.00
19.56
N


ATOM
543
CZ
ARG
A
75
15.672
41.818
15.690
1.00
20.65
C


ATOM
544
NH1
ARG
A
75
14.619
41.110
15.292
1.00
20.90
N


ATOM
545
NH2
ARG
A
75
15.518
43.095
16.015
1.00
21.36
N


ATOM
546
C
ARG
A
75
21.523
39.791
16.243
1.00
15.50
C


ATOM
547
O
ARG
A
75
21.913
39.372
15.152
1.00
15.79
O


ATOM
548
N
ALA
A
76
21.907
40.959
16.754
1.00
15.45
N


ATOM
549
CA
ALA
A
76
22.773
41.881
16.014
1.00
15.48
C


ATOM
550
CB
ALA
A
76
22.683
43.280
16.607
1.00
15.48
C


ATOM
551
C
ALA
A
76
24.229
41.417
15.961
1.00
15.72
C


ATOM
552
O
ALA
A
76
24.929
41.673
14.982
1.00
15.53
O


ATOM
553
N
LYS
A
77
24.678
40.733
17.011
1.00
16.04
N


ATOM
554
CA
LYS
A
77
26.091
40.375
17.147
1.00
16.47
C


ATOM
555
CB
LYS
A
77
26.616
40.787
18.521
1.00
16.57
C


ATOM
556
CG
LYS
A
77
26.624
42.278
18.746
1.00
17.11
C


ATOM
557
CD
LYS
A
77
27.172
42.613
20.106
1.00
18.65
C


ATOM
558
CE
LYS
A
77
27.189
44.108
20.327
1.00
19.06
C


ATOM
559
NZ
LYS
A
77
27.605
44.437
21.711
1.00
20.55
N


ATOM
560
C
LYS
A
77
26.391
38.902
16.905
1.00
16.78
C


ATOM
561
O
LYS
A
77
27.555
38.514
16.794
1.00
17.20
O


ATOM
562
N
GLY
A
78
25.348
38.084
16.825
1.00
16.93
N


ATOM
563
CA
GLY
A
78
25.529
36.645
16.717
1.00
17.28
C


ATOM
564
C
GLY
A
78
25.499
36.118
15.302
1.00
17.69
C


ATOM
565
O
GLY
A
78
25.157
36.834
14.361
1.00
17.94
O


ATOM
566
N
GLU
A
79
25.890
34.860
15.157
1.00
17.81
N


ATOM
567
CA
GLU
A
79
25.646
34.114
13.935
1.00
18.20
C


ATOM
568
CB
GLU
A
79
26.906
33.356
13.516
1.00
18.44
C


ATOM
569
CG
GLU
A
79
28.098
34.270
13.222
1.00
20.04
C


ATOM
570
CD
GLU
A
79
29.401
33.516
13.049
1.00
20.79
C


ATOM
571
OE1
GLU
A
79
29.618
32.516
13.770
1.00
24.47
O


ATOM
572
OE2
GLU
A
79
30.222
33.938
12.207
1.00
24.43
O


ATOM
573
C
GLU
A
79
24.502
33.152
14.215
1.00
17.52
C


ATOM
574
O
GLU
A
79
24.133
32.952
15.379
1.00
17.07
O


ATOM
575
N
ASN
A
80
23.920
32.573
13.167
1.00
16.85
N


ATOM
576
CA
ASN
A
80
22.838
31.612
13.367
1.00
16.48
C


ATOM
577
CB
ASN
A
80
22.139
31.235
12.040
1.00
16.69
C


ATOM
578
CG
ASN
A
80
23.062
30.534
11.041
1.00
17.13
C


ATOM
579
OD1
ASN
A
80
24.055
29.907
11.409
1.00
18.22
O


ATOM
580
ND2
ASN
A
80
22.710
30.623
9.762
1.00
17.57
N


ATOM
581
C
ASN
A
80
23.317
30.388
14.152
1.00
16.15
C


ATOM
582
O
ASN
A
80
24.523
30.170
14.296
1.00
15.83
O


ATOM
583
N
GLU
A
81
22.379
29.612
14.686
1.00
15.75
N


ATOM
584
CA
GLU
A
81
22.740
28.501
15.571
1.00
15.64
C


ATOM
585
CB
GLU
A
81
21.499
27.873
16.201
1.00
15.52
C


ATOM
586
CG
GLU
A
81
21.777
27.155
17.520
1.00
16.22
C


ATOM
587
CD
GLU
A
81
20.525
26.599
18.155
1.00
17.76
C


ATOM
588
OE1
GLU
A
81
19.950
25.640
17.595
1.00
18.33
O


ATOM
589
OE2
GLU
A
81
20.121
27.113
19.221
1.00
18.67
O


ATOM
590
C
GLU
A
81
23.602
27.441
14.876
1.00
15.66
C


ATOM
591
O
GLU
A
81
24.438
26.806
15.513
1.00
15.63
O


ATOM
592
N
ALA
A
82
23.408
27.274
13.567
1.00
15.63
N


ATOM
593
CA
ALA
A
82
24.240
26.370
12.771
1.00
15.67
C


ATOM
594
CB
ALA
A
82
23.764
26.343
11.314
1.00
15.81
C


ATOM
595
C
ALA
A
82
25.721
26.749
12.846
1.00
15.71
C


ATOM
596
O
ALA
A
82
26.580
25.891
13.062
1.00
15.65
O


ATOM
597
N
ALA
A
83
26.010
28.039
12.675
1.00
15.61
N


ATOM
598
CA
ALA
A
83
27.381
28.544
12.743
1.00
15.64
C


ATOM
599
CB
ALA
A
83
27.468
29.925
12.116
1.00
15.69
C


ATOM
600
C
ALA
A
83
27.898
28.569
14.182
1.00
15.62
C


ATOM
601
O
ALA
A
83
29.073
28.289
14.436
1.00
15.68
O


ATOM
602
N
PHE
A
84
27.005
28.915
15.109
1.00
15.41
N


ATOM
603
CA
PHE
A
84
27.264
28.854
16.548
1.00
15.46
C


ATOM
604
CB
PHE
A
84
25.981
29.252
17.298
1.00
15.20
C


ATOM
605
CG
PHE
A
84
26.163
29.489
18.777
1.00
14.93
C


ATOM
606
CD1
PHE
A
84
26.849
30.611
19.247
1.00
14.78
C


ATOM
607
CE1
PHE
A
84
26.986
30.842
20.619
1.00
14.63
C


ATOM
608
CZ
PHE
A
84
26.419
29.955
21.529
1.00
14.87
C


ATOM
609
CE2
PHE
A
84
25.718
28.843
21.071
1.00
14.51
C


ATOM
610
CD2
PHE
A
84
25.589
28.619
19.702
1.00
14.96
C


ATOM
611
C
PHE
A
84
27.712
27.433
16.932
1.00
15.58
C


ATOM
612
O
PHE
A
84
28.769
27.249
17.540
1.00
15.73
O


ATOM
613
N
ALA
A
85
26.917
26.439
16.532
1.00
15.68
N


ATOM
614
CA
ALA
A
85
27.236
25.025
16.760
1.00
15.90
C


ATOM
615
CB
ALA
A
85
26.117
24.137
16.228
1.00
15.88
C


ATOM
616
C
ALA
A
85
28.578
24.611
16.146
1.00
15.99
C


ATOM
617
O
ALA
A
85
29.346
23.871
16.764
1.00
16.13
O


ATOM
618
N
ALA
A
86
28.845
25.085
14.928
1.00
16.07
N


ATOM
619
CA
ALA
A
86
30.085
24.762
14.219
1.00
16.15
C


ATOM
620
CB
ALA
A
86
30.079
25.377
12.820
1.00
16.23
C


ATOM
621
C
ALA
A
86
31.329
25.202
14.988
1.00
16.20
C


ATOM
622
O
ALA
A
86
32.297
24.444
15.104
1.00
16.18
O


ATOM
623
N
ARG
A
87
31.294
26.426
15.513
1.00
16.27
N


ATOM
624
CA
ARG
A
87
32.424
26.986
16.250
1.00
16.59
C


ATOM
625
CB
ARG
A
87
32.181
28.460
16.578
1.00
16.76
C


ATOM
626
CG
ARG
A
87
32.208
29.388
15.378
1.00
18.66
C


ATOM
627
CD
ARG
A
87
32.229
30.846
15.817
1.00
21.18
C


ATOM
628
NE
ARG
A
87
33.477
31.203
16.493
1.00
23.62
N


ATOM
629
CZ
ARG
A
87
33.784
32.427
16.922
1.00
24.97
C


ATOM
630
NH1
ARG
A
87
32.934
33.431
16.757
1.00
26.02
N


ATOM
631
NH2
ARG
A
87
34.943
32.646
17.527
1.00
25.78
N


ATOM
632
C
ARG
A
87
32.695
26.210
17.533
1.00
16.14
C


ATOM
633
O
ARG
A
87
33.846
25.925
17.862
1.00
16.38
O


ATOM
634
N
ILE
A
88
31.629
25.879
18.256
1.00
15.87
N


ATOM
635
CA
ILE
A
88
31.746
25.122
19.501
1.00
15.59
C


ATOM
636
CB
ILE
A
88
30.402
25.109
20.285
1.00
15.46
C


ATOM
637
CG1
ILE
A
88
30.001
26.546
20.656
1.00
15.32
C


ATOM
638
CD1
ILE
A
88
28.570
26.697
21.133
1.00
15.40
C


ATOM
639
CG2
ILE
A
88
30.503
24.230
21.538
1.00
15.30
C


ATOM
640
C
ILE
A
88
32.256
23.701
19.234
1.00
15.79
C


ATOM
641
O
ILE
A
88
33.183
23.231
19.902
1.00
15.48
O


ATOM
642
N
HIS
A
89
31.674
23.042
18.232
1.00
16.14
N


ATOM
643
CA
HIS
A
89
32.102
21.700
17.837
1.00
16.63
C


ATOM
644
CB
HIS
A
89
31.258
21.181
16.667
1.00
16.67
C


ATOM
645
CG
HIS
A
89
31.509
19.745
16.332
1.00
17.60
C


ATOM
646
ND1
HIS
A
89
32.333
19.356
15.298
1.00
18.72
N


ATOM
647
CE1
HIS
A
89
32.367
18.037
15.237
1.00
18.96
C


ATOM
648
NE2
HIS
A
89
31.596
17.555
16.195
1.00
18.90
N


ATOM
649
CD2
HIS
A
89
31.048
18.602
16.895
1.00
18.05
C


ATOM
650
C
HIS
A
89
33.588
21.651
17.477
1.00
16.83
C


ATOM
651
O
HIS
A
89
34.284
20.703
17.840
1.00
16.85
O


ATOM
652
N
SER
A
90
34.071
22.679
16.777
1.00
17.23
N


ATOM
653
CA
SER
A
90
35.478
22.745
16.383
1.00
17.67
C


ATOM
654
CB
SER
A
90
35.727
23.927
15.442
1.00
17.88
C


ATOM
655
OG
SER
A
90
35.515
25.162
16.103
1.00
20.31
O


ATOM
656
C
SER
A
90
36.400
22.830
17.602
1.00
17.56
C


ATOM
657
O
SER
A
90
37.474
22.234
17.620
1.00
17.93
O


ATOM
658
N
LEU
A
91
35.967
23.571
18.620
1.00
17.26
N


ATOM
659
CA
LEU
A
91
36.736
23.710
19.854
1.00
17.08
C


ATOM
660
CB
LEU
A
91
36.204
24.883
20.684
1.00
17.15
C


ATOM
661
CG
LEU
A
91
36.336
26.291
20.095
1.00
17.75
C


ATOM
662
CD1
LEU
A
91
35.471
27.272
20.872
1.00
18.55
C


ATOM
663
CD2
LEU
A
91
37.793
26.750
20.075
1.00
18.09
C


ATOM
664
C
LEU
A
91
36.714
22.428
20.686
1.00
16.87
C


ATOM
665
O
LEU
A
91
37.739
22.015
21.238
1.00
16.55
O


ATOM
666
N
PHE
A
92
35.542
21.803
20.760
1.00
16.59
N


ATOM
667
CA
PHE
A
92
35.324
20.638
21.622
1.00
16.54
C


ATOM
668
CB
PHE
A
92
33.818
20.399
21.821
1.00
16.11
C


ATOM
669
CG
PHE
A
92
33.177
21.289
22.872
1.00
15.40
C


ATOM
670
CD1
PHE
A
92
33.810
22.446
23.330
1.00
15.34
C


ATOM
671
CE1
PHE
A
92
33.206
23.260
24.293
1.00
15.03
C


ATOM
672
CZ
PHE
A
92
31.955
22.928
24.795
1.00
15.29
C


ATOM
673
CE2
PHE
A
92
31.307
21.786
24.338
1.00
15.17
C


ATOM
674
CD2
PHE
A
92
31.917
20.975
23.378
1.00
14.73
C


ATOM
675
C
PHE
A
92
35.983
19.360
21.088
1.00
16.84
C


ATOM
676
O
PHE
A
92
36.227
18.421
21.851
1.00
17.26
O


ATOM
677
N
THR
A
93
36.258
19.322
19.783
1.00
16.91
N


ATOM
678
CA
THR
A
93
36.775
18.103
19.143
1.00
17.06
C


ATOM
679
CB
THR
A
93
36.017
17.764
17.833
1.00
16.85
C


ATOM
680
OG1
THR
A
93
36.057
18.885
16.946
1.00
17.15
O


ATOM
681
CG2
THR
A
93
34.565
17.401
18.127
1.00
17.01
C


ATOM
682
C
THR
A
93
38.287
18.128
18.887
1.00
17.14
C


ATOM
683
O
THR
A
93
38.833
17.217
18.249
1.00
17.47
O


ATOM
684
N
VAL
A
94
38.957
19.171
19.377
1.00
17.23
N


ATOM
685
CA
VAL
A
94
40.419
19.189
19.420
1.00
17.22
C


ATOM
686
CB
VAL
A
94
40.962
20.533
19.984
1.00
17.18
C


ATOM
687
CG1
VAL
A
94
42.476
20.470
20.210
1.00
17.25
C


ATOM
688
CG2
VAL
A
94
40.605
21.691
19.053
1.00
17.24
C


ATOM
689
C
VAL
A
94
40.880
18.017
20.294
1.00
17.23
C


ATOM
690
O
VAL
A
94
40.401
17.860
21.417
1.00
17.19
O


ATOM
691
N
PRO
A
95
41.773
17.160
19.760
1.00
17.25
N


ATOM
692
CA
PRO
A
95
42.222
15.975
20.497
1.00
17.20
C


ATOM
693
CB
PRO
A
95
43.290
15.376
19.576
1.00
17.22
C


ATOM
694
CG
PRO
A
95
42.906
15.838
18.221
1.00
17.29
C


ATOM
695
CD
PRO
A
95
42.381
17.227
18.418
1.00
17.27
C


ATOM
696
C
PRO
A
95
42.825
16.286
21.864
1.00
17.13
C


ATOM
697
O
PRO
A
95
43.418
17.353
22.057
1.00
17.08
O


ATOM
698
N
LYS
A
96
42.657
15.345
22.796
1.00
17.07
N


ATOM
699
CA
LYS
A
96
43.241
15.413
24.143
1.00
17.36
C


ATOM
700
CB
LYS
A
96
44.775
15.388
24.081
1.00
17.39
C


ATOM
701
CG
LYS
A
96
45.343
14.098
23.498
1.00
18.57
C


ATOM
702
CD
LYS
A
96
46.865
14.097
23.506
1.00
19.11
C


ATOM
703
CE
LYS
A
96
47.430
13.683
24.861
1.00
21.71
C


ATOM
704
NZ
LYS
A
96
47.230
12.228
25.141
1.00
23.87
N


ATOM
705
C
LYS
A
96
42.736
16.599
24.966
1.00
16.80
C


ATOM
706
O
LYS
A
96
43.462
17.148
25.800
1.00
17.10
O


ATOM
707
N
THR
A
97
41.482
16.976
24.728
1.00
16.26
N


ATOM
708
CA
THR
A
97
40.844
18.070
25.454
1.00
15.70
C


ATOM
709
CB
THR
A
97
39.980
18.941
24.507
1.00
15.74
C


ATOM
710
OG1
THR
A
97
40.801
19.500
23.476
1.00
16.12
O


ATOM
711
CG2
THR
A
97
39.297
20.072
25.273
1.00
15.72
C


ATOM
712
C
THR
A
97
39.949
17.535
26.570
1.00
15.33
C


ATOM
713
O
THR
A
97
39.110
16.664
26.340
1.00
15.17
O


ATOM
714
N
CYS
A
98
40.135
18.065
27.777
1.00
14.66
N


ATOM
715
CA
CYS
A
98
39.153
17.901
28.842
1.00
14.18
C


ATOM
716
CB
CYS
A
98
39.840
17.730
30.198
1.00
14.26
C


ATOM
717
SG
CYS
A
98
38.690
17.667
31.598
1.00
14.39
S


ATOM
718
C
CYS
A
98
38.244
19.124
28.852
1.00
13.77
C


ATOM
719
O
CYS
A
98
38.679
20.227
29.197
1.00
13.75
O


ATOM
720
N
ILE
A
99
36.994
18.934
28.430
1.00
13.80
N


ATOM
721
CA
ILE
A
99
36.020
20.022
28.392
1.00
13.84
C


ATOM
722
CB
ILE
A
99
34.928
19.802
27.299
1.00
13.91
C


ATOM
723
CG1
ILE
A
99
35.551
19.716
25.897
1.00
15.01
C


ATOM
724
CD1
ILE
A
99
35.910
18.306
25.454
1.00
15.61
C


ATOM
725
CG2
ILE
A
99
33.891
20.923
27.337
1.00
14.48
C


ATOM
726
C
ILE
A
99
35.354
20.140
29.753
1.00
13.65
C


ATOM
727
O
ILE
A
99
34.733
19.193
30.231
1.00
14.01
O


ATOM
728
N
LEU
A
100
35.491
21.299
30.384
1.00
13.55
N


ATOM
729
CA
LEU
A
100
34.952
21.477
31.729
1.00
13.40
C


ATOM
730
CB
LEU
A
100
36.007
21.129
32.792
1.00
13.38
C


ATOM
731
CG
LEU
A
100
37.158
22.096
33.102
1.00
13.15
C


ATOM
732
CD1
LEU
A
100
38.076
21.464
34.131
1.00
13.55
C


ATOM
733
CD2
LEU
A
100
37.954
22.486
31.850
1.00
12.90
C


ATOM
734
C
LEU
A
100
34.388
22.862
31.969
1.00
13.55
C


ATOM
735
O
LEU
A
100
34.626
23.792
31.198
1.00
13.66
O


ATOM
736
N
GLY
A
101
33.630
22.988
33.049
1.00
13.29
N


ATOM
737
CA
GLY
A
101
33.082
24.266
33.452
1.00
13.04
C


ATOM
738
C
GLY
A
101
32.659
24.216
34.894
1.00
12.69
C


ATOM
739
O
GLY
A
101
33.262
23.504
35.707
1.00
12.81
O


ATOM
740
N
TYR
A
102
31.619
24.978
35.212
1.00
12.78
N


ATOM
741
CA
TYR
A
102
31.070
25.006
36.552
1.00
12.71
C


ATOM
742
CB
TYR
A
102
31.383
26.341
37.239
1.00
12.74
C


ATOM
743
CG
TYR
A
102
31.322
26.247
38.739
1.00
12.16
C


ATOM
744
CD1
TYR
A
102
32.384
25.708
39.463
1.00
11.94
C


ATOM
745
CE1
TYR
A
102
32.332
25.601
40.850
1.00
11.78
C


ATOM
746
CZ
TYR
A
102
31.206
26.031
41.525
1.00
12.47
C


ATOM
747
OH
TYR
A
102
31.161
25.919
42.893
1.00
12.70
O


ATOM
748
CE2
TYR
A
102
30.131
26.572
40.829
1.00
12.43
C


ATOM
749
CD2
TYR
A
102
30.194
26.673
39.438
1.00
12.41
C


ATOM
750
C
TYR
A
102
29.570
24.773
36.470
1.00
13.14
C


ATOM
751
O
TYR
A
102
28.823
25.648
36.030
1.00
13.68
O


ATOM
752
N
ASN
A
103
29.150
23.580
36.891
1.00
13.63
N


ATOM
753
CA
ASN
A
103
27.786
23.075
36.677
1.00
13.94
C


ATOM
754
CB
ASN
A
103
26.720
24.047
37.212
1.00
14.21
C


ATOM
755
CG
ASN
A
103
25.376
23.369
37.445
1.00
14.49
C


ATOM
756
OD1
ASN
A
103
25.316
22.188
37.794
1.00
15.72
O


ATOM
757
ND2
ASN
A
103
24.291
24.110
37.234
1.00
16.28
N


ATOM
758
C
ASN
A
103
27.510
22.692
35.213
1.00
14.23
C


ATOM
759
O
ASN
A
103
26.349
22.617
34.784
1.00
14.23
O


ATOM
760
N
ASN
A
104
28.571
22.429
34.455
1.00
14.30
N


ATOM
761
CA
ASN
A
104
28.410
22.044
33.052
1.00
14.80
C


ATOM
762
CB
ASN
A
104
29.736
22.111
32.287
1.00
14.66
C


ATOM
763
CG
ASN
A
104
30.822
21.269
32.921
1.00
14.18
C


ATOM
764
OD1
ASN
A
104
31.268
21.551
34.029
1.00
13.93
O


ATOM
765
ND2
ASN
A
104
31.259
20.230
32.213
1.00
15.36
N


ATOM
766
C
ASN
A
104
27.747
20.687
32.859
1.00
15.56
C


ATOM
767
O
ASN
A
104
26.975
20.509
31.931
1.00
15.61
O


ATOM
768
N
VAL
A
105
28.034
19.736
33.744
1.00
16.33
N


ATOM
769
CA
VAL
A
105
27.477
18.388
33.598
1.00
17.10
C


ATOM
770
CB
VAL
A
105
28.037
17.411
34.666
1.00
17.09
C


ATOM
771
CG1
VAL
A
105
27.206
16.134
34.730
1.00
18.11
C


ATOM
772
CG2
VAL
A
105
29.482
17.077
34.354
1.00
17.71
C


ATOM
773
C
VAL
A
105
25.942
18.398
33.600
1.00
17.34
C


ATOM
774
O
VAL
A
105
25.310
17.712
32.787
1.00
17.57
O


ATOM
775
N
ARG
A
106
25.351
19.203
34.480
1.00
17.58
N


ATOM
776
CA
ARG
A
106
23.892
19.264
34.594
1.00
18.16
C


ATOM
777
CB
ARG
A
106
23.459
19.472
36.052
1.00
18.90
C


ATOM
778
CG
ARG
A
106
23.844
18.333
37.005
1.00
21.54
C


ATOM
779
CD
ARG
A
106
23.032
17.072
36.757
1.00
25.71
C


ATOM
780
NE
ARG
A
106
23.392
16.007
37.690
1.00
28.42
N


ATOM
781
CZ
ARG
A
106
22.921
14.762
37.635
1.00
30.09
C


ATOM
782
NH1
ARG
A
106
22.062
14.407
36.687
1.00
31.00
N


ATOM
783
NH2
ARG
A
106
23.316
13.868
38.534
1.00
30.81
N


ATOM
784
C
ARG
A
106
23.251
20.323
33.697
1.00
17.67
C


ATOM
785
O
ARG
A
106
22.075
20.203
33.343
1.00
17.93
O


ATOM
786
N
PHE
A
107
24.014
21.351
33.326
1.00
16.77
N


ATOM
787
CA
PHE
A
107
23.470
22.431
32.500
1.00
16.20
C


ATOM
788
CB
PHE
A
107
23.423
23.761
33.266
1.00
16.14
C


ATOM
789
CG
PHE
A
107
22.750
24.871
32.501
1.00
16.18
C


ATOM
790
CD1
PHE
A
107
21.374
24.845
32.280
1.00
16.71
C


ATOM
791
CE1
PHE
A
107
20.746
25.866
31.561
1.00
16.35
C


ATOM
792
CZ
PHE
A
107
21.499
26.926
31.064
1.00
16.54
C


ATOM
793
CE2
PHE
A
107
22.875
26.961
31.284
1.00
16.03
C


ATOM
794
CD2
PHE
A
107
23.492
25.934
31.997
1.00
16.50
C


ATOM
795
C
PHE
A
107
24.146
22.608
31.136
1.00
15.99
C


ATOM
796
O
PHE
A
107
23.547
22.303
30.109
1.00
16.02
O


ATOM
797
N
ASP
A
108
25.380
23.113
31.126
1.00
15.37
N


ATOM
798
CA
ASP
A
108
26.031
23.500
29.869
1.00
15.64
C


ATOM
799
CB
ASP
A
108
27.380
24.175
30.131
1.00
15.39
C


ATOM
800
CG
ASP
A
108
27.262
25.356
31.076
1.00
15.55
C


ATOM
801
OD1
ASP
A
108
27.311
26.515
30.604
1.00
14.99
O


ATOM
802
OD2
ASP
A
108
27.094
25.125
32.295
1.00
15.85
O


ATOM
803
C
ASP
A
108
26.180
22.338
28.884
1.00
15.81
C


ATOM
804
O
ASP
A
108
25.989
22.515
27.681
1.00
15.93
O


ATOM
805
N
ASP
A
109
26.505
21.153
29.397
1.00
16.16
N


ATOM
806
CA
ASP
A
109
26.644
19.971
28.545
1.00
16.50
C


ATOM
807
CB
ASP
A
109
27.241
18.793
29.322
1.00
17.00
C


ATOM
808
CG
ASP
A
109
28.701
19.018
29.711
1.00
18.58
C


ATOM
809
OD1
ASP
A
109
29.306
20.032
29.294
1.00
21.14
O


ATOM
810
OD2
ASP
A
109
29.245
18.170
30.448
1.00
21.53
O


ATOM
811
C
ASP
A
109
25.315
19.565
27.914
1.00
16.46
C


ATOM
812
O
ASP
A
109
25.291
19.043
26.802
1.00
16.35
O


ATOM
813
N
GLU
A
110
24.216
19.805
28.628
1.00
16.19
N


ATOM
814
CA
GLU
A
110
22.880
19.560
28.080
1.00
16.39
C


ATOM
815
CB
GLU
A
110
21.820
19.573
29.185
1.00
16.49
C


ATOM
816
CG
GLU
A
110
21.933
18.413
30.176
1.00
18.63
C


ATOM
817
CD
GLU
A
110
21.863
17.046
29.505
1.00
20.67
C


ATOM
818
OE1
GLU
A
110
20.972
16.839
28.653
1.00
22.32
O


ATOM
819
OE2
GLU
A
110
22.702
16.179
29.835
1.00
23.12
O


ATOM
820
C
GLU
A
110
22.536
20.572
26.987
1.00
15.99
C


ATOM
821
O
GLU
A
110
21.935
20.217
25.972
1.00
15.80
O


ATOM
822
N
VAL
A
111
22.934
21.826
27.192
1.00
15.23
N


ATOM
823
CA
VAL
A
111
22.814
22.855
26.156
1.00
14.93
C


ATOM
824
CB
VAL
A
111
23.297
24.244
26.668
1.00
14.62
C


ATOM
825
CG1
VAL
A
111
23.269
25.272
25.551
1.00
14.55
C


ATOM
826
CG2
VAL
A
111
22.433
24.710
27.835
1.00
15.01
C


ATOM
827
C
VAL
A
111
23.591
22.437
24.899
1.00
14.95
C


ATOM
828
O
VAL
A
111
23.049
22.465
23.788
1.00
15.06
O


ATOM
829
N
THR
A
112
24.847
22.026
25.092
1.00
14.81
N


ATOM
830
CA
THR
A
112
25.710
21.546
24.003
1.00
14.98
C


ATOM
831
CB
THR
A
112
27.100
21.109
24.540
1.00
14.98
C


ATOM
832
OG1
THR
A
112
27.763
22.234
25.132
1.00
14.96
O


ATOM
833
CG2
THR
A
112
27.973
20.546
23.421
1.00
15.49
C


ATOM
834
C
THR
A
112
25.077
20.382
23.239
1.00
15.13
C


ATOM
835
O
THR
A
112
25.028
20.394
22.006
1.00
14.99
O


ATOM
836
N
ARG
A
113
24.594
19.381
23.975
1.00
15.15
N


ATOM
837
CA
ARG
A
113
23.950
18.219
23.359
1.00
15.42
C


ATOM
838
CB
ARG
A
113
23.494
17.219
24.422
1.00
15.69
C


ATOM
839
CG
ARG
A
113
24.631
16.460
25.071
1.00
17.33
C


ATOM
840
CD
ARG
A
113
24.121
15.427
26.053
1.00
21.07
C


ATOM
841
NE
ARG
A
113
25.214
14.812
26.801
1.00
24.39
N


ATOM
842
CZ
ARG
A
113
25.055
13.882
27.739
1.00
25.95
C


ATOM
843
NH1
ARG
A
113
23.840
13.447
28.055
1.00
26.90
N


ATOM
844
NH2
ARG
A
113
26.115
13.385
28.361
1.00
27.24
N


ATOM
845
C
ARG
A
113
22.771
18.639
22.496
1.00
15.07
C


ATOM
846
O
ARG
A
113
22.596
18.134
21.383
1.00
15.01
O


ATOM
847
N
ASN
A
114
21.977
19.574
23.007
1.00
14.95
N


ATOM
848
CA
ASN
A
114
20.795
20.050
22.296
1.00
15.03
C


ATOM
849
CB
ASN
A
114
19.845
20.762
23.251
1.00
14.99
C


ATOM
850
CG
ASN
A
114
18.980
19.793
24.026
1.00
15.70
C


ATOM
851
OD1
ASN
A
114
19.190
19.563
25.221
1.00
17.72
O


ATOM
852
ND2
ASN
A
114
18.017
19.196
23.343
1.00
15.14
N


ATOM
853
C
ASN
A
114
21.111
20.916
21.079
1.00
15.03
C


ATOM
854
O
ASN
A
114
20.445
20.810
20.052
1.00
14.98
O


ATOM
855
N
ILE
A
115
22.132
21.763
21.198
1.00
15.18
N


ATOM
856
CA
ILE
A
115
22.614
22.559
20.064
1.00
15.62
C


ATOM
857
CB
ILE
A
115
23.729
23.557
20.494
1.00
15.76
C


ATOM
858
CG1
ILE
A
115
23.169
24.613
21.454
1.00
15.99
C


ATOM
859
CD1
ILE
A
115
24.231
25.510
22.069
1.00
16.53
C


ATOM
860
CG2
ILE
A
115
24.355
24.233
19.278
1.00
16.50
C


ATOM
861
C
ILE
A
115
23.127
21.648
18.940
1.00
15.53
C


ATOM
862
O
ILE
A
115
22.801
21.848
17.769
1.00
15.53
O


ATOM
863
N
PHE
A
116
23.915
20.640
19.308
1.00
15.29
N


ATOM
864
CA
PHE
A
116
24.461
19.691
18.337
1.00
15.31
C


ATOM
865
CB
PHE
A
116
25.482
18.770
19.012
1.00
15.21
C


ATOM
866
CG
PHE
A
116
26.809
19.439
19.317
1.00
15.36
C


ATOM
867
CD1
PHE
A
116
27.034
20.780
18.994
1.00
15.37
C


ATOM
868
CE1
PHE
A
116
28.256
21.394
19.285
1.00
15.42
C


ATOM
869
CZ
PHE
A
116
29.264
20.671
19.915
1.00
15.69
C


ATOM
870
CE2
PHE
A
116
29.051
19.339
20.248
1.00
15.68
C


ATOM
871
CD2
PHE
A
116
27.826
18.730
19.952
1.00
15.54
C


ATOM
872
C
PHE
A
116
23.336
18.880
17.687
1.00
15.22
C


ATOM
873
O
PHE
A
116
23.307
18.706
16.466
1.00
15.41
O


ATOM
874
N
TYR
A
117
22.405
18.418
18.521
1.00
15.26
N


ATOM
875
CA
TYR
A
117
21.207
17.687
18.093
1.00
15.33
C


ATOM
876
CB
TYR
A
117
20.373
17.345
19.337
1.00
15.37
C


ATOM
877
CG
TYR
A
117
18.947
16.891
19.109
1.00
15.35
C


ATOM
878
CD1
TYR
A
117
18.664
15.604
18.641
1.00
15.45
C


ATOM
879
CE1
TYR
A
117
17.349
15.177
18.468
1.00
15.76
C


ATOM
880
CZ
TYR
A
117
16.303
16.033
18.786
1.00
15.83
C


ATOM
881
OH
TYR
A
117
15.001
15.618
18.621
1.00
16.23
O


ATOM
882
CE2
TYR
A
117
16.560
17.306
19.274
1.00
15.24
C


ATOM
883
CD2
TYR
A
117
17.876
17.721
19.444
1.00
15.21
C


ATOM
884
C
TYR
A
117
20.379
18.463
17.060
1.00
15.39
C


ATOM
885
O
TYR
A
117
20.011
17.919
16.013
1.00
15.53
O


ATOM
886
N
ARG
A
118
20.111
19.736
17.345
1.00
15.21
N


ATOM
887
CA
ARG
A
118
19.320
20.583
16.443
1.00
15.27
C


ATOM
888
CB
ARG
A
118
18.921
21.890
17.131
1.00
15.22
C


ATOM
889
CG
ARG
A
118
17.867
21.730
18.209
1.00
15.72
C


ATOM
890
CD
ARG
A
118
17.214
23.058
18.554
1.00
16.48
C


ATOM
891
NE
ARG
A
118
18.135
24.014
19.176
1.00
16.31
N


ATOM
892
CZ
ARG
A
118
18.316
24.146
20.489
1.00
16.23
C


ATOM
893
NH1
ARG
A
118
17.664
23.363
21.341
1.00
16.71
N


ATOM
894
NH2
ARG
A
118
19.163
25.057
20.954
1.00
17.02
N


ATOM
895
C
ARG
A
118
20.029
20.898
15.127
1.00
15.44
C


ATOM
896
O
ARG
A
118
19.378
21.164
14.115
1.00
15.21
O


ATOM
897
N
ASN
A
119
21.358
20.870
15.141
1.00
15.55
N


ATOM
898
CA
ASN
A
119
22.140
21.345
13.997
1.00
15.92
C


ATOM
899
CB
ASN
A
119
22.957
22.572
14.395
1.00
15.86
C


ATOM
900
CG
ASN
A
119
22.080
23.719
14.834
1.00
15.91
C


ATOM
901
OD1
ASN
A
119
21.464
24.395
14.008
1.00
16.05
O


ATOM
902
ND2
ASN
A
119
21.986
23.925
16.143
1.00
15.71
N


ATOM
903
C
ASN
A
119
23.003
20.275
13.323
1.00
16.10
C


ATOM
904
O
ASN
A
119
24.002
20.585
12.656
1.00
16.16
O


ATOM
905
N
PHE
A
120
22.592
19.019
13.499
1.00
16.42
N


ATOM
906
CA
PHE
A
120
23.129
17.875
12.744
1.00
16.83
C


ATOM
907
CB
PHE
A
120
22.908
18.058
11.231
1.00
16.95
C


ATOM
908
CG
PHE
A
120
21.468
17.968
10.827
1.00
17.27
C


ATOM
909
CD1
PHE
A
120
20.961
16.793
10.285
1.00
17.40
C


ATOM
910
CE1
PHE
A
120
19.619
16.695
9.925
1.00
18.11
C


ATOM
911
CZ
PHE
A
120
18.770
17.775
10.115
1.00
18.05
C


ATOM
912
CE2
PHE
A
120
19.260
18.952
10.661
1.00
18.03
C


ATOM
913
CD2
PHE
A
120
20.605
19.045
11.016
1.00
17.09
C


ATOM
914
C
PHE
A
120
24.578
17.516
13.082
1.00
17.08
C


ATOM
915
O
PHE
A
120
25.327
17.000
12.239
1.00
17.37
O


ATOM
916
N
TYR
A
121
24.954
17.782
14.331
1.00
17.18
N


ATOM
917
CA
TYR
A
121
26.191
17.268
14.894
1.00
17.43
C


ATOM
918
CB
TYR
A
121
26.953
18.371
15.633
1.00
17.20
C


ATOM
919
CG
TYR
A
121
27.571
19.403
14.725
1.00
17.07
C


ATOM
920
CD1
TYR
A
121
28.815
19.181
14.133
1.00
16.79
C


ATOM
921
CE1
TYR
A
121
29.392
20.129
13.294
1.00
17.16
C


ATOM
922
CZ
TYR
A
121
28.723
21.315
13.042
1.00
16.99
C


ATOM
923
OH
TYR
A
121
29.289
22.253
12.206
1.00
17.30
O


ATOM
924
CE2
TYR
A
121
27.484
21.562
13.621
1.00
16.88
C


ATOM
925
CD2
TYR
A
121
26.918
20.606
14.461
1.00
16.73
C


ATOM
926
C
TYR
A
121
25.886
16.129
15.854
1.00
17.80
C


ATOM
927
O
TYR
A
121
24.825
16.107
16.488
1.00
17.95
O


ATOM
928
N
ASP
A
122
26.813
15.181
15.951
1.00
17.97
N


ATOM
929
CA
ASP
A
122
26.726
14.121
16.945
1.00
18.33
C


ATOM
930
CB
ASP
A
122
27.917
13.170
16.807
1.00
18.50
C


ATOM
931
CG
ASP
A
122
27.710
11.865
17.545
1.00
19.19
C


ATOM
932
OD1
ASP
A
122
27.535
11.891
18.784
1.00
19.38
O


ATOM
933
OD2
ASP
A
122
27.734
10.806
16.886
1.00
21.11
O


ATOM
934
C
ASP
A
122
26.699
14.752
18.340
1.00
18.48
C


ATOM
935
O
ASP
A
122
27.630
15.464
18.710
1.00
18.47
O


ATOM
936
N
PRO
A
123
25.610
14.519
19.105
1.00
18.60
N


ATOM
937
CA
PRO
A
123
25.468
15.160
20.418
1.00
18.98
C


ATOM
938
CB
PRO
A
123
24.016
14.837
20.816
1.00
18.96
C


ATOM
939
CG
PRO
A
123
23.350
14.360
19.550
1.00
18.81
C


ATOM
940
CD
PRO
A
123
24.437
13.692
18.779
1.00
18.92
C


ATOM
941
C
PRO
A
123
26.432
14.639
21.488
1.00
19.31
C


ATOM
942
O
PRO
A
123
26.592
15.287
22.526
1.00
19.38
O


ATOM
943
N
TYR
A
124
27.071
13.495
21.233
1.00
19.63
N


ATOM
944
CA
TYR
A
124
27.844
12.795
22.272
1.00
20.03
C


ATOM
945
CB
TYR
A
124
27.228
11.424
22.566
1.00
20.41
C


ATOM
946
CG
TYR
A
124
25.769
11.469
22.953
1.00
20.97
C


ATOM
947
CD1
TYR
A
124
25.380
11.821
24.249
1.00
21.42
C


ATOM
948
CE1
TYR
A
124
24.036
11.862
24.610
1.00
22.00
C


ATOM
949
CZ
TYR
A
124
23.066
11.547
23.669
1.00
21.78
C


ATOM
950
OH
TYR
A
124
21.737
11.584
24.019
1.00
22.38
O


ATOM
951
CE2
TYR
A
124
23.427
11.192
22.377
1.00
21.45
C


ATOM
952
CD2
TYR
A
124
24.774
11.153
22.028
1.00
21.08
C


ATOM
953
C
TYR
A
124
29.336
12.623
21.972
1.00
20.06
C


ATOM
954
O
TYR
A
124
30.164
12.689
22.885
1.00
20.26
O


ATOM
955
N
ALA
A
125
29.670
12.394
20.702
1.00
19.90
N


ATOM
956
CA
ALA
A
125
31.029
11.993
20.304
1.00
19.83
C


ATOM
957
CB
ALA
A
125
31.114
11.831
18.791
1.00
19.95
C


ATOM
958
C
ALA
A
125
32.136
12.925
20.804
1.00
19.78
C


ATOM
959
O
ALA
A
125
33.220
12.468
21.168
1.00
19.65
O


ATOM
960
N
TRP
A
126
31.849
14.226
20.828
1.00
19.70
N


ATOM
961
CA
TRP
A
126
32.829
15.250
21.210
1.00
19.77
C


ATOM
962
CB
TRP
A
126
32.169
16.634
21.238
1.00
19.66
C


ATOM
963
CG
TRP
A
126
31.005
16.736
22.195
1.00
19.81
C


ATOM
964
CD1
TRP
A
126
29.701
16.421
21.937
1.00
19.67
C


ATOM
965
NE1
TRP
A
126
28.928
16.644
23.051
1.00
19.31
N


ATOM
966
CE2
TRP
A
126
29.728
17.109
24.062
1.00
19.57
C


ATOM
967
CD2
TRP
A
126
31.047
17.180
23.559
1.00
19.35
C


ATOM
968
CE3
TRP
A
126
32.071
17.632
24.405
1.00
20.15
C


ATOM
969
CZ3
TRP
A
126
31.747
17.992
25.711
1.00
19.88
C


ATOM
970
CH2
TRP
A
126
30.423
17.910
26.182
1.00
19.60
C


ATOM
971
CZ2
TRP
A
126
29.403
17.473
25.375
1.00
19.46
C


ATOM
972
C
TRP
A
126
33.524
14.982
22.552
1.00
19.88
C


ATOM
973
O
TRP
A
126
34.700
15.320
22.725
1.00
19.92
O


ATOM
974
N
SER
A
127
32.799
14.364
23.485
1.00
19.81
N


ATOM
975
CA
SER
A
127
33.263
14.246
24.868
1.00
19.97
C


ATOM
976
CB
SER
A
127
32.073
14.181
25.834
1.00
20.00
C


ATOM
977
OG
SER
A
127
31.327
12.993
25.648
1.00
21.41
O


ATOM
978
C
SER
A
127
34.212
13.077
25.121
1.00
19.75
C


ATOM
979
O
SER
A
127
34.825
13.002
26.185
1.00
19.96
O


ATOM
980
N
TRP
A
128
34.334
12.164
24.156
1.00
19.47
N


ATOM
981
CA
TRP
A
128
35.167
10.972
24.356
1.00
19.35
C


ATOM
982
CB
TRP
A
128
34.308
9.748
24.711
1.00
19.21
C


ATOM
983
CG
TRP
A
128
33.365
9.314
23.628
1.00
19.16
C


ATOM
984
CD1
TRP
A
128
32.055
9.666
23.496
1.00
19.24
C


ATOM
985
NE1
TRP
A
128
31.512
9.065
22.386
1.00
19.59
N


ATOM
986
CE2
TRP
A
128
32.474
8.304
21.775
1.00
19.07
C


ATOM
987
CD2
TRP
A
128
33.658
8.432
22.533
1.00
19.12
C


ATOM
988
CE3
TRP
A
128
34.806
7.740
22.119
1.00
19.01
C


ATOM
989
CZ3
TRP
A
128
34.735
6.953
20.970
1.00
19.33
C


ATOM
990
CH2
TRP
A
128
33.541
6.847
20.238
1.00
19.10
C


ATOM
991
CZ2
TRP
A
128
32.403
7.512
20.622
1.00
19.29
C


ATOM
992
C
TRP
A
128
36.121
10.650
23.204
1.00
19.50
C


ATOM
993
O
TRP
A
128
37.146
9.998
23.412
1.00
19.27
O


ATOM
994
N
GLN
A
129
35.784
11.096
21.997
1.00
19.58
N


ATOM
995
CA
GLN
A
129
36.633
10.837
20.831
1.00
20.12
C


ATOM
996
CB
GLN
A
129
35.897
11.173
19.534
1.00
20.10
C


ATOM
997
CG
GLN
A
129
34.776
10.203
19.195
1.00
20.80
C


ATOM
998
CD
GLN
A
129
34.276
10.349
17.768
1.00
21.42
C


ATOM
999
OE1
GLN
A
129
34.455
11.392
17.131
1.00
21.82
O


ATOM
1000
NE2
GLN
A
129
33.638
9.301
17.261
1.00
21.57
N


ATOM
1001
C
GLN
A
129
37.941
11.615
20.915
1.00
20.31
C


ATOM
1002
O
GLN
A
129
37.989
12.694
21.504
1.00
20.52
O


ATOM
1003
N
HIS
A
130
38.997
11.053
20.322
1.00
20.55
N


ATOM
1004
CA
HIS
A
130
40.331
11.676
20.300
1.00
20.90
C


ATOM
1005
CB
HIS
A
130
40.314
13.008
19.527
1.00
21.05
C


ATOM
1006
CG
HIS
A
130
39.495
12.977
18.274
1.00
22.25
C


ATOM
1007
ND1
HIS
A
130
39.876
12.275
17.151
1.00
23.43
N


ATOM
1008
CE1
HIS
A
130
38.968
12.435
16.205
1.00
23.56
C


ATOM
1009
NE2
HIS
A
130
38.015
13.222
16.671
1.00
23.82
N


ATOM
1010
CD2
HIS
A
130
38.321
13.577
17.962
1.00
23.28
C


ATOM
1011
C
HIS
A
130
40.906
11.879
21.711
1.00
20.64
C


ATOM
1012
O
HIS
A
130
41.578
12.879
21.978
1.00
20.82
O


ATOM
1013
N
ASP
A
131
40.636
10.919
22.599
1.00
20.55
N


ATOM
1014
CA
ASP
A
131
41.098
10.949
24.000
1.00
20.38
C


ATOM
1015
CB
ASP
A
131
42.634
10.926
24.085
1.00
20.89
C


ATOM
1016
CG
ASP
A
131
43.219
9.581
23.704
1.00
22.29
C


ATOM
1017
OD1
ASP
A
131
42.707
8.546
24.183
1.00
24.53
O


ATOM
1018
OD2
ASP
A
131
44.200
9.560
22.930
1.00
24.56
O


ATOM
1019
C
ASP
A
131
40.526
12.110
24.819
1.00
19.67
C


ATOM
1020
O
ASP
A
131
41.102
12.514
25.835
1.00
19.86
O


ATOM
1021
N
ASN
A
132
39.385
12.635
24.386
1.00
18.50
N


ATOM
1022
CA
ASN
A
132
38.737
13.716
25.113
1.00
17.51
C


ATOM
1023
CB
ASN
A
132
37.792
14.506
24.196
1.00
17.56
C


ATOM
1024
CG
ASN
A
132
38.542
15.427
23.244
1.00
17.41
C


ATOM
1025
OD1
ASN
A
132
39.764
15.349
23.120
1.00
17.71
O


ATOM
1026
ND2
ASN
A
132
37.810
16.308
22.573
1.00
17.89
N


ATOM
1027
C
ASN
A
132
38.013
13.223
26.357
1.00
16.95
C


ATOM
1028
O
ASN
A
132
37.799
12.023
26.534
1.00
16.55
O


ATOM
1029
N
SER
A
133
37.665
14.158
27.233
1.00
16.16
N


ATOM
1030
CA
SER
A
133
36.934
13.843
28.451
1.00
15.87
C


ATOM
1031
CB
SER
A
133
37.890
13.362
29.550
1.00
15.85
C


ATOM
1032
OG
SER
A
133
38.746
14.409
29.982
1.00
15.85
O


ATOM
1033
C
SER
A
133
36.188
15.080
28.903
1.00
15.63
C


ATOM
1034
O
SER
A
133
36.307
16.146
28.293
1.00
15.32
O


ATOM
1035
N
ARG
A
134
35.402
14.935
29.960
1.00
15.54
N


ATOM
1036
CA
ARG
A
134
34.783
16.088
30.586
1.00
15.77
C


ATOM
1037
CB
ARG
A
134
33.298
16.205
30.209
1.00
16.43
C


ATOM
1038
CG
ARG
A
134
32.408
15.083
30.703
1.00
18.91
C


ATOM
1039
CD
ARG
A
134
30.954
15.464
30.493
1.00
22.85
C


ATOM
1040
NE
ARG
A
134
30.038
14.349
30.692
1.00
25.21
N


ATOM
1041
CZ
ARG
A
134
28.712
14.457
30.661
1.00
26.15
C


ATOM
1042
NH1
ARG
A
134
28.140
15.635
30.441
1.00
26.76
N


ATOM
1043
NH2
ARG
A
134
27.954
13.386
30.850
1.00
26.51
N


ATOM
1044
C
ARG
A
134
34.982
16.087
32.095
1.00
14.98
C


ATOM
1045
O
ARG
A
134
35.337
15.069
32.684
1.00
14.98
O


ATOM
1046
N
TRP
A
135
34.773
17.248
32.703
1.00
14.31
N


ATOM
1047
CA
TRP
A
135
34.861
17.401
34.144
1.00
13.77
C


ATOM
1048
CB
TRP
A
135
36.321
17.620
34.566
1.00
13.68
C


ATOM
1049
CG
TRP
A
135
36.644
17.220
35.998
1.00
13.12
C


ATOM
1050
CD1
TRP
A
135
35.948
16.345
36.795
1.00
12.79
C


ATOM
1051
NE1
TRP
A
135
36.560
16.230
38.021
1.00
13.20
N


ATOM
1052
CE2
TRP
A
135
37.683
17.017
38.032
1.00
13.03
C


ATOM
1053
CD2
TRP
A
135
37.770
17.650
36.768
1.00
13.01
C


ATOM
1054
CE3
TRP
A
135
38.842
18.521
36.520
1.00
13.64
C


ATOM
1055
CZ3
TRP
A
135
39.782
18.727
37.525
1.00
13.26
C


ATOM
1056
CH2
TRP
A
135
39.666
18.083
38.772
1.00
13.14
C


ATOM
1057
CZ2
TRP
A
135
38.629
17.228
39.043
1.00
13.19
C


ATOM
1058
C
TRP
A
135
33.986
18.580
34.551
1.00
13.57
C


ATOM
1059
O
TRP
A
135
33.445
19.284
33.697
1.00
13.88
O


ATOM
1060
N
ASP
A
136
33.829
18.783
35.851
1.00
13.21
N


ATOM
1061
CA
ASP
A
136
32.950
19.823
36.363
1.00
12.93
C


ATOM
1062
CB
ASP
A
136
31.514
19.290
36.458
1.00
13.00
C


ATOM
1063
CG
ASP
A
136
30.491
20.374
36.776
1.00
13.03
C


ATOM
1064
OD1
ASP
A
136
30.856
21.429
37.347
1.00
12.52
O


ATOM
1065
OD2
ASP
A
136
29.305
20.147
36.460
1.00
13.16
O


ATOM
1066
C
ASP
A
136
33.450
20.240
37.726
1.00
12.96
C


ATOM
1067
O
ASP
A
136
33.517
19.424
38.643
1.00
13.44
O


ATOM
1068
N
LEU
A
137
33.811
21.511
37.856
1.00
12.52
N


ATOM
1069
CA
LEU
A
137
34.396
22.004
39.100
1.00
12.63
C


ATOM
1070
CB
LEU
A
137
35.151
23.323
38.877
1.00
12.90
C


ATOM
1071
CG
LEU
A
137
36.644
23.259
38.514
1.00
14.10
C


ATOM
1072
CD1
LEU
A
137
37.468
22.555
39.600
1.00
14.95
C


ATOM
1073
CD2
LEU
A
137
36.854
22.598
37.169
1.00
15.29
C


ATOM
1074
C
LEU
A
137
33.388
22.158
40.230
1.00
12.44
C


ATOM
1075
O
LEU
A
137
33.778
22.284
41.390
1.00
12.54
O


ATOM
1076
N
LEU
A
138
32.096
22.141
39.906
1.00
12.19
N


ATOM
1077
CA
LEU
A
138
31.072
22.276
40.948
1.00
12.28
C


ATOM
1078
CB
LEU
A
138
29.664
22.381
40.349
1.00
12.13
C


ATOM
1079
CG
LEU
A
138
28.495
22.312
41.350
1.00
12.30
C


ATOM
1080
CD1
LEU
A
138
28.574
23.424
42.411
1.00
12.88
C


ATOM
1081
CD2
LEU
A
138
27.154
22.352
40.623
1.00
12.55
C


ATOM
1082
C
LEU
A
138
31.141
21.146
41.974
1.00
12.43
C


ATOM
1083
O
LEU
A
138
31.223
21.399
43.175
1.00
12.66
O


ATOM
1084
N
ASP
A
139
31.109
19.899
41.508
1.00
13.18
N


ATOM
1085
CA
ASP
A
139
31.163
18.776
42.440
1.00
13.57
C


ATOM
1086
CB
ASP
A
139
30.648
17.477
41.799
1.00
14.45
C


ATOM
1087
CG
ASP
A
139
29.116
17.383
41.805
1.00
16.60
C


ATOM
1088
OD1
ASP
A
139
28.452
18.247
42.419
1.00
17.94
O


ATOM
1089
OD2
ASP
A
139
28.574
16.435
41.194
1.00
19.38
O


ATOM
1090
C
ASP
A
139
32.560
18.604
43.051
1.00
13.11
C


ATOM
1091
O
ASP
A
139
32.698
18.002
44.112
1.00
13.17
O


ATOM
1092
N
VAL
A
140
33.580
19.156
42.390
1.00
12.51
N


ATOM
1093
CA
VAL
A
140
34.915
19.255
42.988
1.00
12.14
C


ATOM
1094
CB
VAL
A
140
35.972
19.774
41.980
1.00
12.06
C


ATOM
1095
CG1
VAL
A
140
37.318
19.996
42.673
1.00
12.35
C


ATOM
1096
CG2
VAL
A
140
36.119
18.793
40.816
1.00
12.44
C


ATOM
1097
C
VAL
A
140
34.880
20.141
44.236
1.00
12.04
C


ATOM
1098
O
VAL
A
140
35.380
19.748
45.294
1.00
11.91
O


ATOM
1099
N
MET
A
141
34.273
21.324
44.117
1.00
11.56
N


ATOM
1100
CA
MET
A
141
34.141
22.222
45.263
1.00
11.62
C


ATOM
1101
CB
MET
A
141
33.517
23.562
44.859
1.00
11.79
C


ATOM
1102
CG
MET
A
141
34.314
24.368
43.826
1.00
13.16
C


ATOM
1103
SD
MET
A
141
36.091
24.433
44.145
1.00
15.72
S


ATOM
1104
CE
MET
A
141
36.152
25.429
45.636
1.00
16.58
C


ATOM
1105
C
MET
A
141
33.313
21.573
46.364
1.00
11.24
C


ATOM
1106
O
MET
A
141
33.659
21.654
47.537
1.00
10.96
O


ATOM
1107
N
ARG
A
142
32.223
20.918
45.977
1.00
11.10
N


ATOM
1108
CA
ARG
A
142
31.383
20.214
46.944
1.00
11.33
C


ATOM
1109
CB
ARG
A
142
30.146
19.639
46.261
1.00
11.37
C


ATOM
1110
CG
ARG
A
142
29.109
20.676
45.894
1.00
11.94
C


ATOM
1111
CD
ARG
A
142
27.941
20.018
45.198
1.00
13.07
C


ATOM
1112
NE
ARG
A
142
26.823
20.935
45.001
1.00
15.27
N


ATOM
1113
CZ
ARG
A
142
25.991
20.880
43.965
1.00
15.36
C


ATOM
1114
NH1
ARG
A
142
26.170
19.973
43.012
1.00
15.39
N


ATOM
1115
NH2
ARG
A
142
24.988
21.740
43.873
1.00
17.10
N


ATOM
1116
C
ARG
A
142
32.146
19.105
47.661
1.00
11.50
C


ATOM
1117
O
ARG
A
142
32.022
18.947
48.883
1.00
11.32
O


ATOM
1118
N
ALA
A
143
32.941
18.350
46.901
1.00
11.95
N


ATOM
1119
CA
ALA
A
143
33.734
17.256
47.457
1.00
12.40
C


ATOM
1120
CB
ALA
A
143
34.379
16.440
46.345
1.00
12.65
C


ATOM
1121
C
ALA
A
143
34.792
17.781
48.421
1.00
12.80
C


ATOM
1122
O
ALA
A
143
35.046
17.180
49.466
1.00
12.91
O


ATOM
1123
N
CYS
A
144
35.397
18.912
48.067
1.00
13.36
N


ATOM
1124
CA
CYS
A
144
36.400
19.543
48.917
1.00
13.71
C


ATOM
1125
CB
CYS
A
144
37.023
20.748
48.216
1.00
13.89
C


ATOM
1126
SG
CYS
A
144
38.648
21.205
48.871
1.00
17.63
S


ATOM
1127
C
CYS
A
144
35.789
19.964
50.248
1.00
13.15
C


ATOM
1128
O
CYS
A
144
36.337
19.680
51.306
1.00
13.26
O


ATOM
1129
N
TYR
A
145
34.639
20.628
50.193
1.00
12.80
N


ATOM
1130
CA
TYR
A
145
33.959
21.037
51.417
1.00
12.99
C


ATOM
1131
CB
TYR
A
145
32.681
21.806
51.095
1.00
13.37
C


ATOM
1132
CG
TYR
A
145
31.838
22.082
52.318
1.00
13.87
C


ATOM
1133
CD1
TYR
A
145
32.068
23.212
53.108
1.00
16.64
C


ATOM
1134
CE1
TYR
A
145
31.302
23.456
54.248
1.00
14.79
C


ATOM
1135
CZ
TYR
A
145
30.296
22.563
54.598
1.00
15.17
C


ATOM
1136
OH
TYR
A
145
29.528
22.788
55.719
1.00
16.31
O


ATOM
1137
CE2
TYR
A
145
30.060
21.435
53.834
1.00
14.86
C


ATOM
1138
CD2
TYR
A
145
30.826
21.199
52.703
1.00
14.64
C


ATOM
1139
C
TYR
A
145
33.635
19.831
52.297
1.00
13.03
C


ATOM
1140
O
TYR
A
145
33.856
19.857
53.510
1.00
12.68
O


ATOM
1141
N
ALA
A
146
33.113
18.779
51.676
1.00
13.12
N


ATOM
1142
CA
ALA
A
146
32.661
17.602
52.406
1.00
13.42
C


ATOM
1143
CB
ALA
A
146
31.823
16.723
51.504
1.00
13.40
C


ATOM
1144
C
ALA
A
146
33.814
16.799
53.006
1.00
13.87
C


ATOM
1145
O
ALA
A
146
33.752
16.381
54.165
1.00
14.10
O


ATOM
1146
N
LEU
A
147
34.862
16.586
52.212
1.00
14.03
N


ATOM
1147
CA
LEU
A
147
35.916
15.630
52.567
1.00
14.65
C


ATOM
1148
CB
LEU
A
147
36.277
14.751
51.361
1.00
14.66
C


ATOM
1149
CG
LEU
A
147
35.145
13.997
50.651
1.00
15.56
C


ATOM
1150
CD1
LEU
A
147
35.665
13.307
49.401
1.00
16.43
C


ATOM
1151
CD2
LEU
A
147
34.482
12.991
51.584
1.00
16.71
C


ATOM
1152
C
LEU
A
147
37.182
16.266
53.146
1.00
14.97
C


ATOM
1153
O
LEU
A
147
37.757
15.738
54.099
1.00
15.49
O


ATOM
1154
N
ARG
A
148
37.622
17.380
52.557
1.00
14.86
N


ATOM
1155
CA
ARG
A
148
38.887
18.026
52.944
1.00
15.33
C


ATOM
1156
CB
ARG
A
148
40.035
17.566
52.025
1.00
15.51
C


ATOM
1157
CG
ARG
A
148
40.272
16.060
51.962
1.00
17.75
C


ATOM
1158
CD
ARG
A
148
40.914
15.529
53.236
1.00
20.53
C


ATOM
1159
NE
ARG
A
148
41.300
14.123
53.108
1.00
22.94
N


ATOM
1160
CZ
ARG
A
148
40.481
13.090
53.303
1.00
23.76
C


ATOM
1161
NH1
ARG
A
148
39.214
13.288
53.646
1.00
23.96
N


ATOM
1162
NH2
ARG
A
148
40.934
11.851
53.162
1.00
25.04
N


ATOM
1163
C
ARG
A
148
38.770
19.559
52.900
1.00
15.14
C


ATOM
1164
O
ARG
A
148
39.365
20.202
52.036
1.00
14.77
O


ATOM
1165
N
PRO
A
149
37.991
20.146
53.830
1.00
15.28
N


ATOM
1166
CA
PRO
A
149
37.684
21.584
53.790
1.00
15.60
C


ATOM
1167
CB
PRO
A
149
36.543
21.720
54.798
1.00
15.72
C


ATOM
1168
CG
PRO
A
149
36.776
20.609
55.772
1.00
15.40
C


ATOM
1169
CD
PRO
A
149
37.320
19.471
54.962
1.00
15.43
C


ATOM
1170
C
PRO
A
149
38.837
22.510
54.189
1.00
15.79
C


ATOM
1171
O
PRO
A
149
38.791
23.706
53.897
1.00
15.37
O


ATOM
1172
N
GLU
A
150
39.852
21.960
54.847
1.00
16.45
N


ATOM
1173
CA
GLU
A
150
40.928
22.762
55.427
1.00
17.32
C


ATOM
1174
CB
GLU
A
150
41.921
21.852
56.169
1.00
17.80
C


ATOM
1175
CG
GLU
A
150
41.278
20.923
57.233
1.00
20.75
C


ATOM
1176
CD
GLU
A
150
40.737
19.591
56.666
1.00
23.67
C


ATOM
1177
OE1
GLU
A
150
40.847
19.342
55.442
1.00
23.65
O


ATOM
1178
OE2
GLU
A
150
40.200
18.783
57.462
1.00
27.09
O


ATOM
1179
C
GLU
A
150
41.655
23.596
54.362
1.00
16.95
C


ATOM
1180
O
GLU
A
150
42.038
23.077
53.318
1.00
18.07
O


ATOM
1181
N
GLY
A
151
41.818
24.893
54.622
1.00
16.58
N


ATOM
1182
CA
GLY
A
151
42.584
25.766
53.725
1.00
16.00
C


ATOM
1183
C
GLY
A
151
41.763
26.676
52.826
1.00
15.79
C


ATOM
1184
O
GLY
A
151
42.275
27.665
52.305
1.00
15.47
O


ATOM
1185
N
ILE
A
152
40.491
26.333
52.630
1.00
15.42
N


ATOM
1186
CA
ILE
A
152
39.581
27.139
51.815
1.00
15.31
C


ATOM
1187
CB
ILE
A
152
38.966
26.301
50.651
1.00
15.16
C


ATOM
1188
CG1
ILE
A
152
40.059
25.904
49.652
1.00
15.23
C


ATOM
1189
CD1
ILE
A
152
39.622
24.895
48.608
1.00
15.70
C


ATOM
1190
CG2
ILE
A
152
37.843
27.076
49.936
1.00
14.93
C


ATOM
1191
C
ILE
A
152
38.482
27.728
52.698
1.00
15.20
C


ATOM
1192
O
ILE
A
152
38.013
27.074
53.629
1.00
15.54
O


ATOM
1193
N
ASN
A
153
38.100
28.971
52.417
1.00
15.16
N


ATOM
1194
CA
ASN
A
153
36.988
29.617
53.112
1.00
15.40
C


ATOM
1195
CB
ASN
A
153
37.163
31.134
53.115
1.00
15.88
C


ATOM
1196
CG
ASN
A
153
38.372
31.585
53.916
1.00
17.59
C


ATOM
1197
OD1
ASN
A
153
39.108
32.478
53.492
1.00
20.14
O


ATOM
1198
ND2
ASN
A
153
38.580
30.974
55.078
1.00
19.62
N


ATOM
1199
C
ASN
A
153
35.667
29.250
52.455
1.00
15.02
C


ATOM
1200
O
ASN
A
153
35.488
29.440
51.251
1.00
15.24
O


ATOM
1201
N
TRP
A
154
34.745
28.724
53.254
1.00
14.59
N


ATOM
1202
CA
TRP
A
154
33.486
28.207
52.731
1.00
14.62
C


ATOM
1203
CB
TRP
A
154
33.253
26.778
53.227
1.00
14.06
C


ATOM
1204
CG
TRP
A
154
34.336
25.853
52.791
1.00
13.57
C


ATOM
1205
CD1
TRP
A
154
35.358
25.368
53.556
1.00
13.37
C


ATOM
1206
NE1
TRP
A
154
36.180
24.567
52.797
1.00
14.01
N


ATOM
1207
CE2
TRP
A
154
35.701
24.530
51.513
1.00
12.87
C


ATOM
1208
CD2
TRP
A
154
34.540
25.335
51.471
1.00
13.08
C


ATOM
1209
CE3
TRP
A
154
33.851
25.465
50.257
1.00
12.93
C


ATOM
1210
CZ3
TRP
A
154
34.336
24.794
49.138
1.00
13.25
C


ATOM
1211
CH2
TRP
A
154
35.494
23.999
49.213
1.00
13.53
C


ATOM
1212
CZ2
TRP
A
154
36.188
23.856
50.388
1.00
13.49
C


ATOM
1213
C
TRP
A
154
32.323
29.117
53.100
1.00
14.88
C


ATOM
1214
O
TRP
A
154
31.899
29.146
54.260
1.00
15.50
O


ATOM
1215
N
PRO
A
155
31.802
29.869
52.108
1.00
15.42
N


ATOM
1216
CA
PRO
A
155
30.760
30.856
52.371
1.00
15.76
C


ATOM
1217
CB
PRO
A
155
30.678
31.637
51.054
1.00
15.95
C


ATOM
1218
CG
PRO
A
155
31.111
30.678
50.020
1.00
15.67
C


ATOM
1219
CD
PRO
A
155
32.164
29.819
50.678
1.00
15.41
C


ATOM
1220
C
PRO
A
155
29.418
30.209
52.679
1.00
16.21
C


ATOM
1221
O
PRO
A
155
29.143
29.100
52.218
1.00
15.87
O


ATOM
1222
N
GLU
A
156
28.608
30.900
53.476
1.00
17.18
N


ATOM
1223
CA
GLU
A
156
27.227
30.506
53.717
1.00
18.23
C


ATOM
1224
CB
GLU
A
156
26.864
30.676
55.196
1.00
18.44
C


ATOM
1225
CG
GLU
A
156
27.301
29.525
56.100
1.00
20.25
C


ATOM
1226
CD
GLU
A
156
26.828
29.690
57.544
1.00
20.90
C


ATOM
1227
OE1
GLU
A
156
26.141
30.693
57.851
1.00
24.13
O


ATOM
1228
OE2
GLU
A
156
27.140
28.811
58.374
1.00
24.81
O


ATOM
1229
C
GLU
A
156
26.303
31.366
52.869
1.00
18.22
C


ATOM
1230
O
GLU
A
156
26.566
32.553
52.664
1.00
18.66
O


ATOM
1231
N
ASN
A
157
25.223
30.772
52.371
1.00
17.87
N


ATOM
1232
CA
ASN
A
157
24.185
31.550
51.697
1.00
17.84
C


ATOM
1233
CB
ASN
A
157
23.411
30.694
50.682
1.00
17.67
C


ATOM
1234
CG
ASN
A
157
22.704
29.503
51.321
1.00
17.25
C


ATOM
1235
OD1
ASN
A
157
22.250
29.566
52.464
1.00
16.01
O


ATOM
1236
ND2
ASN
A
157
22.594
28.415
50.569
1.00
17.91
N


ATOM
1237
C
ASN
A
157
23.250
32.207
52.720
1.00
17.99
C


ATOM
1238
O
ASN
A
157
23.451
32.066
53.928
1.00
17.66
O


ATOM
1239
N
ASP
A
158
22.237
32.921
52.233
1.00
18.57
N


ATOM
1240
CA
ASP
A
158
21.319
33.659
53.109
1.00
19.21
C


ATOM
1241
CB
ASP
A
158
20.445
34.617
52.295
1.00
19.80
C


ATOM
1242
CG
ASP
A
158
21.207
35.839
51.816
1.00
22.26
C


ATOM
1243
OD1
ASP
A
158
22.238
36.190
52.433
1.00
24.52
O


ATOM
1244
OD2
ASP
A
158
20.768
36.452
50.821
1.00
25.31
O


ATOM
1245
C
ASP
A
158
20.444
32.764
53.992
1.00
18.79
C


ATOM
1246
O
ASP
A
158
19.833
33.238
54.955
1.00
19.15
O


ATOM
1247
N
ASP
A
159
20.390
31.475
53.669
1.00
18.01
N


ATOM
1248
CA
ASP
A
159
19.648
30.521
54.490
1.00
17.50
C


ATOM
1249
CB
ASP
A
159
18.976
29.454
53.616
1.00
17.76
C


ATOM
1250
CG
ASP
A
159
17.894
30.034
52.712
1.00
18.58
C


ATOM
1251
OD1
ASP
A
159
17.319
31.091
53.059
1.00
20.34
O


ATOM
1252
OD2
ASP
A
159
17.621
29.437
51.651
1.00
21.00
O


ATOM
1253
C
ASP
A
159
20.526
29.881
55.573
1.00
16.64
C


ATOM
1254
O
ASP
A
159
20.024
29.178
56.453
1.00
16.38
O


ATOM
1255
N
GLY
A
160
21.834
30.149
55.511
1.00
16.05
N


ATOM
1256
CA
GLY
A
160
22.780
29.689
56.534
1.00
15.43
C


ATOM
1257
C
GLY
A
160
23.413
28.348
56.220
1.00
15.36
C


ATOM
1258
O
GLY
A
160
23.950
27.679
57.107
1.00
15.56
O


ATOM
1259
N
LEU
A
161
23.353
27.967
54.948
1.00
15.03
N


ATOM
1260
CA
LEU
A
161
23.889
26.699
54.482
1.00
15.00
C


ATOM
1261
CB
LEU
A
161
22.816
25.938
53.694
1.00
15.45
C


ATOM
1262
CG
LEU
A
161
21.535
25.575
54.454
1.00
16.60
C


ATOM
1263
CD1
LEU
A
161
20.364
25.424
53.500
1.00
18.75
C


ATOM
1264
CD2
LEU
A
161
21.727
24.324
55.291
1.00
18.16
C


ATOM
1265
C
LEU
A
161
25.099
26.966
53.596
1.00
14.52
C


ATOM
1266
O
LEU
A
161
25.221
28.051
53.041
1.00
14.06
O


ATOM
1267
N
PRO
A
162
26.001
25.973
53.460
1.00
14.21
N


ATOM
1268
CA
PRO
A
162
27.166
26.179
52.598
1.00
14.32
C


ATOM
1269
CB
PRO
A
162
27.914
24.840
52.681
1.00
14.58
C


ATOM
1270
CG
PRO
A
162
26.929
23.867
53.205
1.00
15.14
C


ATOM
1271
CD
PRO
A
162
25.998
24.636
54.077
1.00
14.33
C


ATOM
1272
C
PRO
A
162
26.751
26.477
51.161
1.00
14.27
C


ATOM
1273
O
PRO
A
162
25.892
25.786
50.602
1.00
14.48
O


ATOM
1274
N
SER
A
163
27.337
27.525
50.593
1.00
14.20
N


ATOM
1275
CA
SER
A
163
27.048
27.935
49.230
1.00
14.41
C


ATOM
1276
CB
SER
A
163
26.849
29.445
49.159
1.00
14.49
C


ATOM
1277
OG
SER
A
163
26.619
29.860
47.824
1.00
15.65
O


ATOM
1278
C
SER
A
163
28.167
27.534
48.291
1.00
14.45
C


ATOM
1279
O
SER
A
163
29.350
27.640
48.632
1.00
14.57
O


ATOM
1280
N
PHE
A
164
27.787
27.094
47.097
1.00
14.45
N


ATOM
1281
CA
PHE
A
164
28.752
26.719
46.073
1.00
14.94
C


ATOM
1282
CB
PHE
A
164
28.697
25.212
45.826
1.00
14.65
C


ATOM
1283
CG
PHE
A
164
29.047
24.414
47.039
1.00
13.63
C


ATOM
1284
CD1
PHE
A
164
30.375
24.163
47.360
1.00
12.83
C


ATOM
1285
CE1
PHE
A
164
30.707
23.459
48.507
1.00
12.89
C


ATOM
1286
CZ
PHE
A
164
29.702
23.012
49.364
1.00
13.46
C


ATOM
1287
CE2
PHE
A
164
28.375
23.277
49.065
1.00
13.92
C


ATOM
1288
CD2
PHE
A
164
28.053
23.983
47.914
1.00
13.57
C


ATOM
1289
C
PHE
A
164
28.539
27.528
44.808
1.00
15.50
C


ATOM
1290
O
PHE
A
164
28.995
27.156
43.731
1.00
16.05
O


ATOM
1291
N
ARG
A
165
27.860
28.659
44.961
1.00
15.92
N


ATOM
1292
CA
ARG
A
165
27.745
29.631
43.888
1.00
16.71
C


ATOM
1293
CB
ARG
A
165
26.738
30.720
44.251
1.00
17.04
C


ATOM
1294
CG
ARG
A
165
25.309
30.216
44.320
1.00
19.09
C


ATOM
1295
CD
ARG
A
165
24.369
31.278
44.841
1.00
23.00
C


ATOM
1296
NE
ARG
A
165
24.014
32.257
43.818
1.00
26.05
N


ATOM
1297
CZ
ARG
A
165
23.240
33.321
44.032
1.00
27.94
C


ATOM
1298
NH1
ARG
A
165
22.737
33.557
45.240
1.00
28.81
N


ATOM
1299
NH2
ARG
A
165
22.970
34.153
43.034
1.00
29.25
N


ATOM
1300
C
ARG
A
165
29.111
30.230
43.618
1.00
16.87
C


ATOM
1301
O
ARG
A
165
29.832
30.614
44.545
1.00
16.55
O


ATOM
1302
N
LEU
A
166
29.464
30.287
42.340
1.00
17.35
N


ATOM
1303
CA
LEU
A
166
30.783
30.719
41.906
1.00
18.02
C


ATOM
1304
CB
LEU
A
166
30.850
30.695
40.376
1.00
18.00
C


ATOM
1305
CG
LEU
A
166
32.209
30.730
39.680
1.00
18.31
C


ATOM
1306
CD1
LEU
A
166
33.115
29.605
40.159
1.00
17.97
C


ATOM
1307
CD2
LEU
A
166
32.012
30.656
38.174
1.00
18.48
C


ATOM
1308
C
LEU
A
166
31.145
32.106
42.442
1.00
18.36
C


ATOM
1309
O
LEU
A
166
32.273
32.331
42.884
1.00
18.87
O


ATOM
1310
N
GLU
A
167
30.175
33.020
42.422
1.00
18.91
N


ATOM
1311
CA
GLU
A
167
30.379
34.383
42.919
1.00
19.19
C


ATOM
1312
CB
GLU
A
167
29.210
35.300
42.521
1.00
19.83
C


ATOM
1313
CG
GLU
A
167
27.842
34.875
43.061
1.00
21.88
C


ATOM
1314
CD
GLU
A
167
27.043
34.025
42.078
1.00
24.40
C


ATOM
1315
OE1
GLU
A
167
27.652
33.280
41.276
1.00
25.54
O


ATOM
1316
OE2
GLU
A
167
25.794
34.102
42.113
1.00
26.68
O


ATOM
1317
C
GLU
A
167
30.624
34.450
44.434
1.00
18.64
C


ATOM
1318
O
GLU
A
167
31.309
35.351
44.914
1.00
18.90
O


ATOM
1319
N
HIS
A
168
30.060
33.498
45.178
1.00
17.92
N


ATOM
1320
CA
HIS
A
168
30.275
33.437
46.623
1.00
17.49
C


ATOM
1321
CB
HIS
A
168
29.190
32.603
47.309
1.00
17.52
C


ATOM
1322
CG
HIS
A
168
27.830
33.231
47.280
1.00
18.42
C


ATOM
1323
ND1
HIS
A
168
26.679
32.524
47.554
1.00
18.79
N


ATOM
1324
CE1
HIS
A
168
25.635
33.328
47.452
1.00
19.62
C


ATOM
1325
NE2
HIS
A
168
26.067
34.530
47.116
1.00
19.64
N


ATOM
1326
CD2
HIS
A
168
27.436
34.497
47.002
1.00
19.62
C


ATOM
1327
C
HIS
A
168
31.646
32.871
46.957
1.00
16.82
C


ATOM
1328
O
HIS
A
168
32.319
33.354
47.870
1.00
17.05
O


ATOM
1329
N
LEU
A
169
32.053
31.844
46.216
1.00
16.25
N


ATOM
1330
CA
LEU
A
169
33.329
31.168
46.470
1.00
15.90
C


ATOM
1331
CB
LEU
A
169
33.408
29.849
45.700
1.00
15.86
C


ATOM
1332
CG
LEU
A
169
32.510
28.717
46.207
1.00
15.38
C


ATOM
1333
CD1
LEU
A
169
32.431
27.620
45.169
1.00
16.14
C


ATOM
1334
CD2
LEU
A
169
33.002
28.160
47.534
1.00
16.14
C


ATOM
1335
C
LEU
A
169
34.524
32.045
46.131
1.00
16.11
C


ATOM
1336
O
LEU
A
169
35.533
32.020
46.834
1.00
15.79
O


ATOM
1337
N
THR
A
170
34.413
32.806
45.045
1.00
16.60
N


ATOM
1338
CA
THR
A
170
35.469
33.746
44.667
1.00
17.15
C


ATOM
1339
CB
THR
A
170
35.226
34.372
43.271
1.00
17.17
C


ATOM
1340
OG1
THR
A
170
33.912
34.939
43.221
1.00
17.26
O


ATOM
1341
CG2
THR
A
170
35.370
33.325
42.175
1.00
17.25
C


ATOM
1342
C
THR
A
170
35.622
34.848
45.718
1.00
17.59
C


ATOM
1343
O
THR
A
170
36.724
35.089
46.218
1.00
17.52
O


ATOM
1344
N
LYS
A
171
34.507
35.488
46.073
1.00
18.04
N


ATOM
1345
CA
LYS
A
171
34.510
36.555
47.079
1.00
18.75
C


ATOM
1346
CB
LYS
A
171
33.093
37.113
47.275
1.00
19.02
C


ATOM
1347
CG
LYS
A
171
33.020
38.386
48.124
1.00
20.90
C


ATOM
1348
CD
LYS
A
171
33.512
39.597
47.345
1.00
23.93
C


ATOM
1349
CE
LYS
A
171
33.163
40.895
48.049
1.00
25.78
C


ATOM
1350
NZ
LYS
A
171
33.372
42.069
47.156
1.00
27.44
N


ATOM
1351
C
LYS
A
171
35.088
36.085
48.417
1.00
18.65
C


ATOM
1352
O
LYS
A
171
35.912
36.775
49.026
1.00
18.96
O


ATOM
1353
N
ALA
A
172
34.670
34.900
48.858
1.00
18.51
N


ATOM
1354
CA
ALA
A
172
35.088
34.367
50.156
1.00
18.61
C


ATOM
1355
CB
ALA
A
172
34.268
33.139
50.515
1.00
18.48
C


ATOM
1356
C
ALA
A
172
36.580
34.043
50.211
1.00
18.66
C


ATOM
1357
O
ALA
A
172
37.160
33.945
51.297
1.00
18.46
O


ATOM
1358
N
ASN
A
173
37.194
33.884
49.040
1.00
19.01
N


ATOM
1359
CA
ASN
A
173
38.591
33.465
48.953
1.00
19.64
C


ATOM
1360
CB
ASN
A
173
38.691
32.101
48.264
1.00
19.21
C


ATOM
1361
CG
ASN
A
173
38.117
30.987
49.112
1.00
18.39
C


ATOM
1362
OD1
ASN
A
173
36.981
30.543
48.899
1.00
18.47
O


ATOM
1363
ND2
ASN
A
173
38.882
30.549
50.103
1.00
15.58
N


ATOM
1364
C
ASN
A
173
39.516
34.494
48.293
1.00
20.56
C


ATOM
1365
O
ASN
A
173
40.628
34.165
47.879
1.00
20.71
O


ATOM
1366
N
GLY
A
174
39.047
35.737
48.207
1.00
21.57
N


ATOM
1367
CA
GLY
A
174
39.877
36.856
47.744
1.00
22.98
C


ATOM
1368
C
GLY
A
174
40.171
36.846
46.255
1.00
24.05
C


ATOM
1369
O
GLY
A
174
41.061
37.558
45.785
1.00
23.97
O


ATOM
1370
N
ILE
A
175
39.421
36.037
45.514
1.00
25.09
N


ATOM
1371
CA
ILE
A
175
39.580
35.944
44.070
1.00
26.48
C


ATOM
1372
CB
ILE
A
175
39.225
34.529
43.558
1.00
26.28
C


ATOM
1373
CG1
ILE
A
175
40.236
33.511
44.095
1.00
26.32
C


ATOM
1374
CD1
ILE
A
175
39.730
32.087
44.126
1.00
26.16
C


ATOM
1375
CG2
ILE
A
175
39.181
34.498
42.026
1.00
26.36
C


ATOM
1376
C
ILE
A
175
38.702
36.989
43.401
1.00
27.60
C


ATOM
1377
O
ILE
A
175
37.510
37.097
43.704
1.00
27.64
O


ATOM
1378
N
GLU
A
176
39.397
37.862
42.287
1.00
29.15
N


ATOM
1379
CA
GLU
A
176
38.476
38.953
41.895
1.00
30.68
C


ATOM
1380
CB
GLU
A
176
39.215
40.293
41.691
1.00
30.87
C


ATOM
1381
CG
GLU
A
176
38.779
41.134
40.550
1.00
32.20
C


ATOM
1382
CD
GLU
A
176
38.556
42.478
41.248
1.00
33.78
C


ATOM
1383
OE1
GLU
A
176
38.910
42.595
42.451
1.00
34.69
O


ATOM
1384
OE2
GLU
A
176
38.016
43.409
40.607
1.00
34.97
O


ATOM
1385
C
GLU
A
176
37.596
38.571
40.703
1.00
31.35
C


ATOM
1386
O
GLU
A
176
38.115
38.207
39.640
1.00
31.77
O


ATOM
1387
N
HIS
A
177
36.287
38.658
40.904
1.00
32.22
N


ATOM
1388
CA
HIS
A
177
35.315
38.246
39.895
1.00
33.00
C


ATOM
1389
CB
HIS
A
177
34.908
36.786
40.195
1.00
32.93
C


ATOM
1390
CG
HIS
A
177
33.778
36.229
39.513
1.00
33.16
C


ATOM
1391
ND1
HIS
A
177
32.675
35.626
40.082
1.00
33.42
N


ATOM
1392
CE1
HIS
A
177
31.884
35.168
39.127
1.00
33.35
C


ATOM
1393
NE2
HIS
A
177
32.436
35.447
37.960
1.00
33.29
N


ATOM
1394
CD2
HIS
A
177
33.626
36.105
38.173
1.00
33.10
C


ATOM
1395
C
HIS
A
177
34.114
39.189
39.917
1.00
33.51
C


ATOM
1396
O
HIS
A
177
33.329
39.184
40.876
1.00
33.83
O


ATOM
1397
N
SER
A
178
33.945
40.014
38.881
1.00
34.07
N


ATOM
1398
CA
SER
A
178
34.891
40.153
37.766
1.00
34.50
C


ATOM
1399
CB
SER
A
178
34.173
40.915
36.639
1.00
34.57
C


ATOM
1400
OG
SER
A
178
34.771
40.576
35.349
1.00
35.10
O


ATOM
1401
C
SER
A
178
36.178
40.871
38.165
1.00
34.67
C


ATOM
1402
O
SER
A
178
36.201
41.617
39.159
1.00
34.97
O


ATOM
1403
N
ASP
A
182
34.971
40.128
31.700
0.50
19.78
N


ATOM
1404
CA
ASP
A
182
33.575
40.540
31.602
0.50
19.66
C


ATOM
1405
CB
ASP
A
182
33.433
41.725
30.642
0.50
19.93
C


ATOM
1406
CG
ASP
A
182
32.169
42.540
30.893
0.50
20.54
C


ATOM
1407
OD1
ASP
A
182
31.159
41.971
31.364
0.50
21.52
O


ATOM
1408
OD2
ASP
A
182
32.186
43.757
30.611
0.50
21.53
O


ATOM
1409
C
ASP
A
182
32.701
39.375
31.141
0.50
19.23
C


ATOM
1410
O
ASP
A
182
32.099
38.679
31.958
0.50
19.38
O


ATOM
1411
N
ALA
A
183
32.625
39.176
29.829
0.50
18.71
N


ATOM
1412
CA
ALA
A
183
31.960
38.003
29.280
0.50
17.98
C


ATOM
1413
CB
ALA
A
183
31.836
38.121
27.771
0.50
18.08
C


ATOM
1414
C
ALA
A
183
32.758
36.761
29.656
0.50
17.41
C


ATOM
1415
O
ALA
A
183
32.250
35.640
29.618
0.50
17.33
O


ATOM
1416
N
MET
A
184
34.013
36.978
30.031
0.50
16.71
N


ATOM
1417
CA
MET
A
184
34.914
35.895
30.398
0.50
16.03
C


ATOM
1418
CB
MET
A
184
36.326
36.197
29.894
0.50
15.98
C


ATOM
1419
CG
MET
A
184
36.524
35.986
28.403
0.50
15.42
C


ATOM
1420
SD
MET
A
184
36.354
34.259
27.917
0.50
15.06
S


ATOM
1421
CE
MET
A
184
37.746
33.519
28.762
0.50
15.02
C


ATOM
1422
C
MET
A
184
34.941
35.669
31.908
0.50
15.85
C


ATOM
1423
O
MET
A
184
35.606
34.754
32.396
0.50
15.18
O


ATOM
1424
N
ALA
A
185
34.209
36.500
32.640
0.50
15.71
N


ATOM
1425
CA
ALA
A
185
34.250
36.487
34.103
0.50
16.04
C


ATOM
1426
CB
ALA
A
185
33.205
37.441
34.674
0.50
16.01
C


ATOM
1427
C
ALA
A
185
34.090
35.093
34.708
0.50
16.19
C


ATOM
1428
O
ALA
A
185
34.898
34.679
35.543
0.50
15.99
O


ATOM
1429
N
ASP
A
186
33.047
34.376
34.295
1.00
16.76
N


ATOM
1430
CA
ASP
A
186
32.747
33.065
34.871
1.00
17.17
C


ATOM
1431
CB
ASP
A
186
31.333
32.617
34.495
1.00
18.01
C


ATOM
1432
CG
ASP
A
186
30.253
33.385
35.250
1.00
20.53
C


ATOM
1433
OD1
ASP
A
186
29.093
33.383
34.788
1.00
24.87
O


ATOM
1434
OD2
ASP
A
186
30.558
33.984
36.304
1.00
22.76
O


ATOM
1435
C
ASP
A
186
33.776
31.999
34.489
1.00
16.71
C


ATOM
1436
O
ASP
A
186
34.112
31.135
35.300
1.00
16.63
O


ATOM
1437
N
VAL
A
187
34.277
32.069
33.258
1.00
16.07
N


ATOM
1438
CA
VAL
A
187
35.321
31.155
32.801
1.00
15.75
C


ATOM
1439
CB
VAL
A
187
35.603
31.314
31.281
1.00
15.57
C


ATOM
1440
CG1
VAL
A
187
36.850
30.536
30.876
1.00
15.34
C


ATOM
1441
CG2
VAL
A
187
34.399
30.850
30.466
1.00
16.27
C


ATOM
1442
C
VAL
A
187
36.607
31.338
33.620
1.00
15.65
C


ATOM
1443
O
VAL
A
187
37.185
30.361
34.109
1.00
15.26
O


ATOM
1444
N
TYR
A
188
37.039
32.588
33.782
1.00
15.72
N


ATOM
1445
CA
TYR
A
188
38.225
32.880
34.592
1.00
15.94
C


ATOM
1446
CB
TYR
A
188
38.624
34.355
34.486
1.00
16.66
C


ATOM
1447
CG
TYR
A
188
39.255
34.736
33.161
1.00
17.87
C


ATOM
1448
CD1
TYR
A
188
40.247
33.941
32.578
1.00
19.04
C


ATOM
1449
CE1
TYR
A
188
40.832
34.295
31.361
1.00
19.69
C


ATOM
1450
CZ
TYR
A
188
40.431
35.462
30.724
1.00
19.07
C


ATOM
1451
OH
TYR
A
188
41.004
35.821
29.528
1.00
19.55
O


ATOM
1452
CE2
TYR
A
188
39.463
36.273
31.291
1.00
19.42
C


ATOM
1453
CD2
TYR
A
188
38.879
35.907
32.503
1.00
18.86
C


ATOM
1454
C
TYR
A
188
38.043
32.478
36.055
1.00
15.58
C


ATOM
1455
O
TYR
A
188
38.977
31.979
36.684
1.00
15.53
O


ATOM
1456
N
ALA
A
189
36.840
32.684
36.588
1.00
15.26
N


ATOM
1457
CA
ALA
A
189
36.532
32.286
37.966
1.00
15.06
C


ATOM
1458
CB
ALA
A
189
35.171
32.818
38.389
1.00
15.29
C


ATOM
1459
C
ALA
A
189
36.597
30.770
38.149
1.00
15.16
C


ATOM
1460
O
ALA
A
189
37.005
30.284
39.203
1.00
15.23
O


ATOM
1461
N
THR
A
190
36.192
30.032
37.118
1.00
14.75
N


ATOM
1462
CA
THR
A
190
36.226
28.572
37.156
1.00
14.73
C


ATOM
1463
CB
THR
A
190
35.431
27.959
35.974
1.00
14.76
C


ATOM
1464
OG1
THR
A
190
34.093
28.472
35.985
1.00
15.21
O


ATOM
1465
CG2
THR
A
190
35.382
26.447
36.076
1.00
14.43
C


ATOM
1466
C
THR
A
190
37.671
28.064
37.173
1.00
14.68
C


ATOM
1467
O
THR
A
190
38.000
27.133
37.913
1.00
14.85
O


ATOM
1468
N
ILE
A
191
38.529
28.692
36.367
1.00
14.61
N


ATOM
1469
CA
ILE
A
191
39.963
28.389
36.376
1.00
14.67
C


ATOM
1470
CB
ILE
A
191
40.730
29.209
35.304
1.00
14.63
C


ATOM
1471
CG1
ILE
A
191
40.224
28.860
33.900
1.00
14.62
C


ATOM
1472
CD1
ILE
A
191
40.755
29.772
32.801
1.00
14.39
C


ATOM
1473
CG2
ILE
A
191
42.247
28.965
35.409
1.00
14.95
C


ATOM
1474
C
ILE
A
191
40.552
28.650
37.771
1.00
14.94
C


ATOM
1475
O
ILE
A
191
41.341
27.844
38.282
1.00
14.89
O


ATOM
1476
N
ALA
A
192
40.143
29.762
38.384
1.00
15.33
N


ATOM
1477
CA
ALA
A
192
40.577
30.112
39.740
1.00
15.80
C


ATOM
1478
CB
ALA
A
192
40.033
31.480
40.139
1.00
15.69
C


ATOM
1479
C
ALA
A
192
40.169
29.053
40.764
1.00
15.95
C


ATOM
1480
O
ALA
A
192
40.933
28.743
41.679
1.00
16.20
O


ATOM
1481
N
MET
A
193
38.968
28.498
40.607
1.00
15.93
N


ATOM
1482
CA
MET
A
193
38.505
27.406
41.471
1.00
16.48
C


ATOM
1483
CB
MET
A
193
37.054
27.034
41.155
1.00
16.66
C


ATOM
1484
CG
MET
A
193
36.047
28.132
41.420
1.00
19.01
C


ATOM
1485
SD
MET
A
193
35.912
28.590
43.159
1.00
23.55
S


ATOM
1486
CE
MET
A
193
37.193
29.824
43.319
1.00
22.77
C


ATOM
1487
C
MET
A
193
39.389
26.177
41.331
1.00
16.02
C


ATOM
1488
O
MET
A
193
39.757
25.552
42.326
1.00
15.82
O


ATOM
1489
N
ALA
A
194
39.727
25.836
40.089
1.00
15.74
N


ATOM
1490
CA
ALA
A
194
40.583
24.690
39.815
1.00
15.59
C


ATOM
1491
CB
ALA
A
194
40.731
24.480
38.310
1.00
15.59
C


ATOM
1492
C
ALA
A
194
41.948
24.851
40.479
1.00
15.77
C


ATOM
1493
O
ALA
A
194
42.438
23.928
41.130
1.00
15.72
O


ATOM
1494
N
LYS
A
195
42.545
26.032
40.324
1.00
15.85
N


ATOM
1495
CA
LYS
A
195
43.837
26.332
40.940
1.00
16.01
C


ATOM
1496
CB
LYS
A
195
44.345
27.700
40.487
1.00
16.03
C


ATOM
1497
CG
LYS
A
195
44.771
27.760
39.038
1.00
17.42
C


ATOM
1498
CD
LYS
A
195
45.332
29.132
38.706
1.00
19.39
C


ATOM
1499
CE
LYS
A
195
45.617
29.280
37.228
1.00
20.86
C


ATOM
1500
NZ
LYS
A
195
46.055
30.666
36.909
1.00
22.55
N


ATOM
1501
C
LYS
A
195
43.746
26.291
42.461
1.00
15.97
C


ATOM
1502
O
LYS
A
195
44.650
25.789
43.131
1.00
16.10
O


ATOM
1503
N
LEU
A
196
42.645
26.815
42.996
1.00
15.90
N


ATOM
1504
CA
LEU
A
196
42.406
26.842
44.437
1.00
15.96
C


ATOM
1505
CB
LEU
A
196
41.049
27.494
44.731
1.00
16.10
C


ATOM
1506
CG
LEU
A
196
40.684
27.857
46.170
1.00
16.88
C


ATOM
1507
CD1
LEU
A
196
41.606
28.941
46.710
1.00
17.76
C


ATOM
1508
CD2
LEU
A
196
39.243
28.314
46.223
1.00
16.73
C


ATOM
1509
C
LEU
A
196
42.476
25.440
45.045
1.00
15.73
C


ATOM
1510
O
LEU
A
196
43.244
25.198
45.973
1.00
15.76
O


ATOM
1511
N
VAL
A
197
41.692
24.514
44.502
1.00
15.45
N


ATOM
1512
CA
VAL
A
197
41.652
23.152
45.030
1.00
15.55
C


ATOM
1513
CB
VAL
A
197
40.411
22.373
44.524
1.00
15.51
C


ATOM
1514
CG1
VAL
A
197
40.378
20.971
45.110
1.00
16.33
C


ATOM
1515
CG2
VAL
A
197
39.141
23.114
44.899
1.00
16.27
C


ATOM
1516
C
VAL
A
197
42.950
22.383
44.746
1.00
15.19
C


ATOM
1517
O
VAL
A
197
43.438
21.648
45.606
1.00
14.93
O


ATOM
1518
N
LYS
A
198
43.515
22.566
43.553
1.00
15.09
N


ATOM
1519
CA
LYS
A
198
44.767
21.893
43.197
1.00
15.16
C


ATOM
1520
CB
LYS
A
198
45.174
22.220
41.757
1.00
15.27
C


ATOM
1521
CG
LYS
A
198
46.399
21.453
41.257
1.00
16.41
C


ATOM
1522
CD
LYS
A
198
46.867
21.994
39.921
1.00
18.29
C


ATOM
1523
CE
LYS
A
198
48.222
21.425
39.524
1.00
20.44
C


ATOM
1524
NZ
LYS
A
198
48.095
20.129
38.812
1.00
21.73
N


ATOM
1525
C
LYS
A
198
45.887
22.275
44.163
1.00
15.12
C


ATOM
1526
O
LYS
A
198
46.683
21.427
44.567
1.00
15.32
O


ATOM
1527
N
THR
A
199
45.928
23.551
44.535
1.00
15.06
N


ATOM
1528
CA
THR
A
199
46.977
24.077
45.414
1.00
15.20
C


ATOM
1529
CB
THR
A
199
47.052
25.628
45.323
1.00
15.37
C


ATOM
1530
OG1
THR
A
199
47.456
26.006
44.004
1.00
16.96
O


ATOM
1531
CG2
THR
A
199
48.045
26.197
46.330
1.00
16.37
C


ATOM
1532
C
THR
A
199
46.775
23.653
46.868
1.00
14.86
C


ATOM
1533
O
THR
A
199
47.733
23.306
47.562
1.00
14.71
O


ATOM
1534
N
ARG
A
200
45.528
23.679
47.324
1.00
14.28
N


ATOM
1535
CA
ARG
A
200
45.245
23.538
48.748
1.00
13.96
C


ATOM
1536
CB
ARG
A
200
44.224
24.592
49.191
1.00
14.35
C


ATOM
1537
CG
ARG
A
200
44.701
26.007
48.849
1.00
15.23
C


ATOM
1538
CD
ARG
A
200
43.936
27.087
49.560
1.00
16.46
C


ATOM
1539
NE
ARG
A
200
44.247
28.395
48.988
1.00
16.30
N


ATOM
1540
CZ
ARG
A
200
43.671
29.538
49.352
1.00
16.74
C


ATOM
1541
NH1
ARG
A
200
42.748
29.555
50.307
1.00
16.92
N


ATOM
1542
NH2
ARG
A
200
44.017
30.666
48.751
1.00
16.62
N


ATOM
1543
C
ARG
A
200
44.847
22.131
49.164
1.00
13.42
C


ATOM
1544
O
ARG
A
200
45.007
21.751
50.326
1.00
13.05
O


ATOM
1545
N
GLN
A
201
44.353
21.345
48.208
1.00
12.67
N


ATOM
1546
CA
GLN
A
201
44.092
19.924
48.447
1.00
12.15
C


ATOM
1547
CB
GLN
A
201
42.595
19.676
48.711
1.00
12.05
C


ATOM
1548
CG
GLN
A
201
42.079
20.263
50.033
1.00
12.51
C


ATOM
1549
CD
GLN
A
201
42.724
19.632
51.272
1.00
12.82
C


ATOM
1550
OE1
GLN
A
201
43.303
18.548
51.203
1.00
12.32
O


ATOM
1551
NE2
GLN
A
201
42.595
20.303
52.415
1.00
13.25
N


ATOM
1552
C
GLN
A
201
44.600
19.071
47.279
1.00
12.14
C


ATOM
1553
O
GLN
A
201
43.805
18.482
46.544
1.00
11.55
O


ATOM
1554
N
PRO
A
202
45.938
19.003
47.109
1.00
11.99
N


ATOM
1555
CA
PRO
A
202
46.554
18.376
45.931
1.00
12.33
C


ATOM
1556
CB
PRO
A
202
48.054
18.436
46.240
1.00
12.38
C


ATOM
1557
CG
PRO
A
202
48.201
19.521
47.228
1.00
12.21
C


ATOM
1558
CD
PRO
A
202
46.955
19.536
48.039
1.00
12.19
C


ATOM
1559
C
PRO
A
202
46.130
16.930
45.685
1.00
12.58
C


ATOM
1560
O
PRO
A
202
45.815
16.572
44.549
1.00
12.77
O


ATOM
1561
N
ARG
A
203
46.136
16.107
46.731
1.00
12.83
N


ATOM
1562
CA
ARG
A
203
45.833
14.681
46.579
1.00
13.37
C


ATOM
1563
CB
ARG
A
203
46.199
13.898
47.842
1.00
13.92
C


ATOM
1564
CG
ARG
A
203
47.676
13.923
48.189
1.00
17.16
C


ATOM
1565
CD
ARG
A
203
48.511
13.059
47.262
1.00
21.11
C


ATOM
1566
NE
ARG
A
203
49.938
13.210
47.546
1.00
23.96
N


ATOM
1567
CZ
ARG
A
203
50.915
12.664
46.827
1.00
25.59
C


ATOM
1568
NH1
ARG
A
203
50.630
11.920
45.764
1.00
26.84
N


ATOM
1569
NH2
ARG
A
203
52.180
12.865
47.171
1.00
26.99
N


ATOM
1570
C
ARG
A
203
44.368
14.452
46.221
1.00
13.27
C


ATOM
1571
O
ARG
A
203
44.057
13.613
45.379
1.00
13.36
O


ATOM
1572
N
LEU
A
204
43.474
15.200
46.863
1.00
12.94
N


ATOM
1573
CA
LEU
A
204
42.053
15.104
46.545
1.00
13.16
C


ATOM
1574
CB
LEU
A
204
41.206
15.907
47.539
1.00
13.02
C


ATOM
1575
CG
LEU
A
204
39.684
15.861
47.322
1.00
13.22
C


ATOM
1576
CD1
LEU
A
204
39.150
14.431
47.418
1.00
14.13
C


ATOM
1577
CD2
LEU
A
204
38.967
16.775
48.301
1.00
13.97
C


ATOM
1578
C
LEU
A
204
41.780
15.558
45.114
1.00
13.30
C


ATOM
1579
O
LEU
A
204
41.032
14.907
44.387
1.00
13.36
O


ATOM
1580
N
PHE
A
205
42.398
16.667
44.712
1.00
13.44
N


ATOM
1581
CA
PHE
A
205
42.255
17.170
43.347
1.00
13.82
C


ATOM
1582
CB
PHE
A
205
43.074
18.448
43.147
1.00
14.20
C


ATOM
1583
CG
PHE
A
205
42.727
19.198
41.889
1.00
15.23
C


ATOM
1584
CD1
PHE
A
205
41.625
20.046
41.852
1.00
16.70
C


ATOM
1585
CE1
PHE
A
205
41.296
20.743
40.692
1.00
16.75
C


ATOM
1586
CZ
PHE
A
205
42.076
20.599
39.558
1.00
16.27
C


ATOM
1587
CE2
PHE
A
205
43.178
19.755
39.577
1.00
16.65
C


ATOM
1588
CD2
PHE
A
205
43.501
19.059
40.744
1.00
16.46
C


ATOM
1589
C
PHE
A
205
42.656
16.110
42.320
1.00
13.90
C


ATOM
1590
O
PHE
A
205
41.916
15.846
41.368
1.00
13.72
O


ATOM
1591
N
ASP
A
206
43.820
15.497
42.532
1.00
14.18
N


ATOM
1592
CA
ASP
A
206
44.323
14.446
41.649
1.00
14.63
C


ATOM
1593
CB
ASP
A
206
45.718
14.002
42.094
1.00
15.26
C


ATOM
1594
CG
ASP
A
206
46.789
15.031
41.776
1.00
18.22
C


ATOM
1595
OD1
ASP
A
206
46.544
15.915
40.924
1.00
21.73
O


ATOM
1596
OD2
ASP
A
206
47.885
14.954
42.374
1.00
21.57
O


ATOM
1597
C
ASP
A
206
43.379
13.251
41.618
1.00
14.13
C


ATOM
1598
O
ASP
A
206
43.085
12.708
40.548
1.00
13.94
O


ATOM
1599
N
TYR
A
207
42.901
12.847
42.792
1.00
13.73
N


ATOM
1600
CA
TYR
A
207
41.947
11.746
42.885
1.00
13.33
C


ATOM
1601
CB
TYR
A
207
41.555
11.457
44.343
1.00
13.56
C


ATOM
1602
CG
TYR
A
207
40.488
10.390
44.448
1.00
13.43
C


ATOM
1603
CD1
TYR
A
207
40.832
9.040
44.508
1.00
13.64
C


ATOM
1604
CE1
TYR
A
207
39.857
8.055
44.583
1.00
13.66
C


ATOM
1605
CZ
TYR
A
207
38.516
8.418
44.586
1.00
14.26
C


ATOM
1606
OH
TYR
A
207
37.547
7.444
44.649
1.00
14.50
O


ATOM
1607
CE2
TYR
A
207
38.147
9.748
44.520
1.00
14.19
C


ATOM
1608
CD2
TYR
A
207
39.131
10.727
44.448
1.00
13.84
C


ATOM
1609
C
TYR
A
207
40.696
12.032
42.055
1.00
13.31
C


ATOM
1610
O
TYR
A
207
40.268
11.200
41.249
1.00
13.40
O


ATOM
1611
N
LEU
A
208
40.117
13.211
42.253
1.00
13.17
N


ATOM
1612
CA
LEU
A
208
38.884
13.572
41.557
1.00
13.25
C


ATOM
1613
CB
LEU
A
208
38.303
14.876
42.113
1.00
13.08
C


ATOM
1614
CG
LEU
A
208
37.833
14.811
43.573
1.00
13.39
C


ATOM
1615
CD1
LEU
A
208
37.542
16.202
44.101
1.00
13.36
C


ATOM
1616
CD2
LEU
A
208
36.609
13.903
43.745
1.00
14.58
C


ATOM
1617
C
LEU
A
208
39.081
13.647
40.043
1.00
13.37
C


ATOM
1618
O
LEU
A
208
38.236
13.172
39.276
1.00
13.64
O


ATOM
1619
N
PHE
A
209
40.206
14.218
39.615
1.00
13.50
N


ATOM
1620
CA
PHE
A
209
40.514
14.309
38.193
1.00
13.83
C


ATOM
1621
CB
PHE
A
209
41.785
15.131
37.964
1.00
13.80
C


ATOM
1622
CG
PHE
A
209
42.194
15.220
36.520
1.00
14.14
C


ATOM
1623
CD1
PHE
A
209
41.404
15.907
35.598
1.00
15.00
C


ATOM
1624
CE1
PHE
A
209
41.774
15.987
34.259
1.00
14.80
C


ATOM
1625
CZ
PHE
A
209
42.953
15.382
33.829
1.00
14.59
C


ATOM
1626
CE2
PHE
A
209
43.750
14.691
34.740
1.00
14.91
C


ATOM
1627
CD2
PHE
A
209
43.367
14.615
36.078
1.00
15.39
C


ATOM
1628
C
PHE
A
209
40.652
12.923
37.573
1.00
14.10
C


ATOM
1629
O
PHE
A
209
40.062
12.641
36.533
1.00
14.03
O


ATOM
1630
N
THR
A
210
41.409
12.053
38.232
1.00
14.49
N


ATOM
1631
CA
THR
A
210
41.620
10.698
37.732
1.00
15.15
C


ATOM
1632
CB
THR
A
210
42.648
9.940
38.602
1.00
15.28
C


ATOM
1633
OG1
THR
A
210
43.931
10.570
38.471
1.00
17.01
O


ATOM
1634
CG2
THR
A
210
42.763
8.480
38.173
1.00
16.94
C


ATOM
1635
C
THR
A
210
40.296
9.930
37.641
1.00
14.95
C


ATOM
1636
O
THR
A
210
40.066
9.175
36.692
1.00
15.26
O


ATOM
1637
N
HIS
A
211
39.411
10.164
38.601
1.00
14.91
N


ATOM
1638
CA
HIS
A
211
38.152
9.430
38.653
1.00
15.03
C


ATOM
1639
CB
HIS
A
211
37.768
9.130
40.101
1.00
15.04
C


ATOM
1640
CG
HIS
A
211
38.663
8.123
40.743
1.00
15.65
C


ATOM
1641
ND1
HIS
A
211
38.294
6.807
40.926
1.00
17.36
N


ATOM
1642
CE1
HIS
A
211
39.297
6.146
41.478
1.00
16.04
C


ATOM
1643
NE2
HIS
A
211
40.308
6.980
41.637
1.00
17.36
N


ATOM
1644
CD2
HIS
A
211
39.941
8.220
41.177
1.00
15.45
C


ATOM
1645
C
HIS
A
211
37.004
10.059
37.861
1.00
15.16
C


ATOM
1646
O
HIS
A
211
35.855
9.646
37.995
1.00
15.16
O


ATOM
1647
N
ARG
A
212
37.325
11.029
37.004
1.00
15.47
N


ATOM
1648
CA
ARG
A
212
36.362
11.500
36.010
1.00
15.93
C


ATOM
1649
CB
ARG
A
212
36.861
12.781
35.318
1.00
15.83
C


ATOM
1650
CG
ARG
A
212
37.836
12.560
34.167
1.00
15.45
C


ATOM
1651
CD
ARG
A
212
38.585
13.851
33.815
1.00
15.16
C


ATOM
1652
NE
ARG
A
212
39.478
13.685
32.666
1.00
14.75
N


ATOM
1653
CZ
ARG
A
212
40.663
13.076
32.709
1.00
14.33
C


ATOM
1654
NH1
ARG
A
212
41.115
12.555
33.845
1.00
13.79
N


ATOM
1655
NH2
ARG
A
212
41.398
12.981
31.608
1.00
14.22
N


ATOM
1656
C
ARG
A
212
36.105
10.381
34.990
1.00
16.76
C


ATOM
1657
O
ARG
A
212
35.056
10.340
34.343
1.00
17.51
O


ATOM
1658
N
ASN
A
213
37.075
9.473
34.883
1.00
17.38
N


ATOM
1659
CA
ASN
A
213
37.057
8.362
33.930
1.00
17.71
C


ATOM
1660
CB
ASN
A
213
38.497
7.850
33.736
1.00
18.26
C


ATOM
1661
CG
ASN
A
213
38.573
6.562
32.938
1.00
19.19
C


ATOM
1662
OD1
ASN
A
213
38.395
5.475
33.482
1.00
21.02
O


ATOM
1663
ND2
ASN
A
213
38.886
6.678
31.651
1.00
21.22
N


ATOM
1664
C
ASN
A
213
36.120
7.252
34.416
1.00
17.64
C


ATOM
1665
O
ASN
A
213
36.207
6.821
35.568
1.00
17.23
O


ATOM
1666
N
LYS
A
214
35.220
6.804
33.538
1.00
17.63
N


ATOM
1667
CA
LYS
A
214
34.179
5.837
33.922
1.00
17.91
C


ATOM
1668
CB
LYS
A
214
33.157
5.628
32.791
1.00
17.94
C


ATOM
1669
CG
LYS
A
214
33.705
4.960
31.533
1.00
19.15
C


ATOM
1670
CD
LYS
A
214
32.607
4.750
30.501
1.00
19.48
C


ATOM
1671
CE
LYS
A
214
33.054
3.808
29.394
1.00
21.33
C


ATOM
1672
NZ
LYS
A
214
32.047
3.736
28.295
1.00
22.45
N


ATOM
1673
C
LYS
A
214
34.728
4.496
34.411
1.00
17.51
C


ATOM
1674
O
LYS
A
214
34.127
3.865
35.272
1.00
17.26
O


ATOM
1675
N
HIS
A
215
35.869
4.071
33.869
1.00
17.45
N


ATOM
1676
CA
HIS
A
215
36.464
2.785
34.256
1.00
17.45
C


ATOM
1677
CB
HIS
A
215
37.553
2.353
33.266
1.00
17.81
C


ATOM
1678
CG
HIS
A
215
37.045
2.105
31.881
1.00
18.53
C


ATOM
1679
ND1
HIS
A
215
35.844
1.476
31.629
1.00
19.42
N


ATOM
1680
CE1
HIS
A
215
35.661
1.391
30.323
1.00
19.31
C


ATOM
1681
NE2
HIS
A
215
36.700
1.938
29.720
1.00
19.79
N


ATOM
1682
CD2
HIS
A
215
37.582
2.388
30.672
1.00
18.99
C


ATOM
1683
C
HIS
A
215
37.013
2.810
35.675
1.00
17.43
C


ATOM
1684
O
HIS
A
215
36.917
1.819
36.403
1.00
17.34
O


ATOM
1685
N
LYS
A
216
37.586
3.947
36.064
1.00
17.36
N


ATOM
1686
CA
LYS
A
216
38.030
4.154
37.436
1.00
17.25
C


ATOM
1687
CB
LYS
A
216
38.781
5.484
37.568
1.00
17.50
C


ATOM
1688
CG
LYS
A
216
40.127
5.528
36.831
1.00
18.65
C


ATOM
1689
CD
LYS
A
216
41.132
4.512
37.383
1.00
21.49
C


ATOM
1690
CE
LYS
A
216
41.701
4.939
38.732
1.00
23.17
C


ATOM
1691
NZ
LYS
A
216
42.760
4.001
39.210
1.00
24.87
N


ATOM
1692
C
LYS
A
216
36.842
4.117
38.393
1.00
16.90
C


ATOM
1693
O
LYS
A
216
36.931
3.551
39.480
1.00
16.78
O


ATOM
1694
N
LEU
A
217
35.728
4.712
37.975
1.00
16.80
N


ATOM
1695
CA
LEU
A
217
34.510
4.706
38.783
1.00
16.79
C


ATOM
1696
CB
LEU
A
217
33.483
5.698
38.233
1.00
16.55
C


ATOM
1697
CG
LEU
A
217
33.850
7.182
38.326
1.00
16.10
C


ATOM
1698
CD1
LEU
A
217
32.929
8.007
37.441
1.00
16.48
C


ATOM
1699
CD2
LEU
A
217
33.820
7.691
39.773
1.00
14.81
C


ATOM
1700
C
LEU
A
217
33.899
3.314
38.890
1.00
17.13
C


ATOM
1701
O
LEU
A
217
33.500
2.894
39.973
1.00
17.09
O


ATOM
1702
N
MET
A
218
33.844
2.598
37.766
1.00
17.56
N


ATOM
1703
CA
MET
A
218
33.296
1.236
37.740
1.00
18.68
C


ATOM
1704
CB
MET
A
218
33.277
0.687
36.314
1.00
18.70
C


ATOM
1705
CG
MET
A
218
32.299
1.386
35.385
1.00
20.24
C


ATOM
1706
SD
MET
A
218
32.570
0.886
33.679
1.00
23.07
S


ATOM
1707
CE
MET
A
218
31.807
2.211
32.778
1.00
23.31
C


ATOM
1708
C
MET
A
218
34.065
0.282
38.655
1.00
18.02
C


ATOM
1709
O
MET
A
218
33.477
−0.620
39.253
1.00
17.65
O


ATOM
1710
N
ALA
A
219
35.376
0.492
38.764
1.00
17.87
N


ATOM
1711
CA
ALA
A
219
36.224
−0.330
39.630
1.00
17.92
C


ATOM
1712
CB
ALA
A
219
37.687
0.064
39.471
1.00
18.12
C


ATOM
1713
C
ALA
A
219
35.800
−0.247
41.099
1.00
18.18
C


ATOM
1714
O
ALA
A
219
36.009
−1.191
41.865
1.00
18.31
O


ATOM
1715
N
LEU
A
220
35.189
0.879
41.472
1.00
18.33
N


ATOM
1716
CA
LEU
A
220
34.705
1.098
42.842
1.00
18.72
C


ATOM
1717
CB
LEU
A
220
34.525
2.596
43.117
1.00
18.59
C


ATOM
1718
CG
LEU
A
220
35.749
3.514
43.031
1.00
18.98
C


ATOM
1719
CD1
LEU
A
220
35.319
4.975
43.049
1.00
19.06
C


ATOM
1720
CD2
LEU
A
220
36.728
3.229
44.160
1.00
20.15
C


ATOM
1721
C
LEU
A
220
33.384
0.391
43.107
1.00
18.96
C


ATOM
1722
O
LEU
A
220
32.982
0.228
44.260
1.00
18.98
O


ATOM
1723
N
ILE
A
221
32.705
−0.009
42.037
1.00
19.39
N


ATOM
1724
CA
ILE
A
221
31.353
−0.547
42.137
1.00
20.11
C


ATOM
1725
CB
ILE
A
221
30.476
−0.093
40.936
1.00
20.08
C


ATOM
1726
CG1
ILE
A
221
30.308
1.435
40.957
1.00
20.97
C


ATOM
1727
CD1
ILE
A
221
29.762
2.031
39.673
1.00
21.54
C


ATOM
1728
CG2
ILE
A
221
29.116
−0.807
40.952
1.00
20.68
C


ATOM
1729
C
ILE
A
221
31.370
−2.069
42.267
1.00
20.09
C


ATOM
1730
O
ILE
A
221
31.838
−2.776
41.369
1.00
20.23
O


ATOM
1731
N
ASP
A
222
30.878
−2.557
43.406
1.00
20.05
N


ATOM
1732
CA
ASP
A
222
30.749
−3.989
43.658
1.00
20.18
C


ATOM
1733
CB
ASP
A
222
31.731
−4.444
44.746
1.00
20.32
C


ATOM
1734
CG
ASP
A
222
31.927
−5.958
44.775
1.00
21.08
C


ATOM
1735
OD1
ASP
A
222
30.973
−6.705
44.465
1.00
21.43
O


ATOM
1736
OD2
ASP
A
222
33.042
−6.403
45.120
1.00
22.80
O


ATOM
1737
C
ASP
A
222
29.311
−4.309
44.058
1.00
19.87
C


ATOM
1738
O
ASP
A
222
28.956
−4.281
45.241
1.00
19.86
O


ATOM
1739
N
VAL
A
223
28.493
−4.608
43.055
1.00
19.69
N


ATOM
1740
CA
VAL
A
223
27.071
−4.882
43.244
1.00
19.55
C


ATOM
1741
CB
VAL
A
223
26.315
−4.935
41.877
1.00
19.60
C


ATOM
1742
CG1
VAL
A
223
24.889
−5.412
42.055
1.00
19.80
C


ATOM
1743
CG2
VAL
A
223
26.338
−3.565
41.200
1.00
20.04
C


ATOM
1744
C
VAL
A
223
26.795
−6.145
44.093
1.00
19.53
C


ATOM
1745
O
VAL
A
223
25.989
−6.090
45.025
1.00
19.19
O


ATOM
1746
N
PRO
A
224
27.456
−7.285
43.773
1.00
19.47
N


ATOM
1747
CA
PRO
A
224
27.243
−8.494
44.579
1.00
19.68
C


ATOM
1748
CB
PRO
A
224
28.238
−9.496
43.977
1.00
19.61
C


ATOM
1749
CG
PRO
A
224
28.419
−9.038
42.578
1.00
19.85
C


ATOM
1750
CD
PRO
A
224
28.388
−7.542
42.656
1.00
19.51
C


ATOM
1751
C
PRO
A
224
27.514
−8.307
46.078
1.00
19.80
C


ATOM
1752
O
PRO
A
224
26.817
−8.900
46.904
1.00
19.94
O


ATOM
1753
N
GLN
A
225
28.507
−7.485
46.419
1.00
20.05
N


ATOM
1754
CA
GLN
A
225
28.867
−7.249
47.822
1.00
20.44
C


ATOM
1755
CB
GLN
A
225
30.376
−7.006
47.964
1.00
20.89
C


ATOM
1756
CG
GLN
A
225
31.263
−8.152
47.475
1.00
22.94
C


ATOM
1757
CD
GLN
A
225
31.117
−9.417
48.299
1.00
25.44
C


ATOM
1758
OE1
GLN
A
225
31.025
−9.369
49.527
1.00
27.59
O


ATOM
1759
NE2
GLN
A
225
31.107
−10.560
47.625
1.00
26.94
N


ATOM
1760
C
GLN
A
225
28.102
−6.073
48.431
1.00
20.09
C


ATOM
1761
O
GLN
A
225
28.182
−5.836
49.641
1.00
20.00
O


ATOM
1762
N
MET
A
226
27.363
−5.341
47.591
1.00
19.78
N


ATOM
1763
CA
MET
A
226
26.747
−4.065
47.985
1.00
19.76
C


ATOM
1764
CB
MET
A
226
25.530
−4.287
48.901
1.00
19.68
C


ATOM
1765
CG
MET
A
226
24.396
−5.089
48.282
1.00
20.20
C


ATOM
1766
SD
MET
A
226
22.960
−5.112
49.374
1.00
20.94
S


ATOM
1767
CE
MET
A
226
21.951
−6.384
48.614
1.00
20.50
C


ATOM
1768
C
MET
A
226
27.778
−3.165
48.675
1.00
19.40
C


ATOM
1769
O
MET
A
226
27.476
−2.506
49.672
1.00
19.22
O


ATOM
1770
N
LYS
A
227
28.997
−3.151
48.138
1.00
18.93
N


ATOM
1771
CA
LYS
A
227
30.110
−2.439
48.762
1.00
18.82
C


ATOM
1772
CB
LYS
A
227
31.404
−2.649
47.971
1.00
18.94
C


ATOM
1773
CG
LYS
A
227
32.648
−2.094
48.662
1.00
20.38
C


ATOM
1774
CD
LYS
A
227
33.930
−2.458
47.921
1.00
21.14
C


ATOM
1775
CE
LYS
A
227
34.078
−1.661
46.636
1.00
23.75
C


ATOM
1776
NZ
LYS
A
227
35.444
−1.783
46.052
1.00
26.02
N


ATOM
1777
C
LYS
A
227
29.804
−0.948
48.910
1.00
17.87
C


ATOM
1778
O
LYS
A
227
29.510
−0.271
47.920
1.00
17.45
O


ATOM
1779
N
PRO
A
228
29.854
−0.436
50.155
1.00
17.28
N


ATOM
1780
CA
PRO
A
228
29.503
0.957
50.416
1.00
16.78
C


ATOM
1781
CB
PRO
A
228
29.447
1.025
51.946
1.00
16.72
C


ATOM
1782
CG
PRO
A
228
30.361
−0.052
52.400
1.00
17.10
C


ATOM
1783
CD
PRO
A
228
30.227
−1.152
51.392
1.00
17.20
C


ATOM
1784
C
PRO
A
228
30.537
1.942
49.879
1.00
16.33
C


ATOM
1785
O
PRO
A
228
31.733
1.643
49.853
1.00
16.46
O


ATOM
1786
N
LEU
A
229
30.059
3.103
49.446
1.00
16.00
N


ATOM
1787
CA
LEU
A
229
30.916
4.159
48.934
1.00
15.53
C


ATOM
1788
CB
LEU
A
229
30.811
4.231
47.406
1.00
15.51
C


ATOM
1789
CG
LEU
A
229
31.265
3.017
46.589
1.00
15.86
C


ATOM
1790
CD1
LEU
A
229
30.859
3.189
45.132
1.00
16.73
C


ATOM
1791
CD2
LEU
A
229
32.774
2.795
46.707
1.00
16.88
C


ATOM
1792
C
LEU
A
229
30.475
5.485
49.516
1.00
15.49
C


ATOM
1793
O
LEU
A
229
29.295
5.673
49.813
1.00
15.72
O


ATOM
1794
N
VAL
A
230
31.413
6.413
49.671
1.00
15.38
N


ATOM
1795
CA
VAL
A
230
31.034
7.805
49.887
1.00
15.35
C


ATOM
1796
CB
VAL
A
230
32.135
8.633
50.627
1.00
15.63
C


ATOM
1797
CG1
VAL
A
230
33.421
8.670
49.846
1.00
17.35
C


ATOM
1798
CG2
VAL
A
230
31.642
10.049
50.913
1.00
16.44
C


ATOM
1799
C
VAL
A
230
30.663
8.431
48.541
1.00
14.90
C


ATOM
1800
O
VAL
A
230
31.346
8.221
47.535
1.00
14.97
O


ATOM
1801
N
HIS
A
231
29.556
9.164
48.528
1.00
14.44
N


ATOM
1802
CA
HIS
A
231
29.072
9.820
47.328
1.00
14.40
C


ATOM
1803
CB
HIS
A
231
27.843
9.064
46.785
1.00
14.52
C


ATOM
1804
CG
HIS
A
231
27.247
9.652
45.538
1.00
14.60
C


ATOM
1805
ND1
HIS
A
231
28.008
10.151
44.501
1.00
15.15
N


ATOM
1806
CE1
HIS
A
231
27.209
10.578
43.537
1.00
16.20
C


ATOM
1807
NE2
HIS
A
231
25.960
10.352
43.900
1.00
15.71
N


ATOM
1808
CD2
HIS
A
231
25.955
9.766
45.142
1.00
15.21
C


ATOM
1809
C
HIS
A
231
28.731
11.259
47.671
1.00
14.29
C


ATOM
1810
O
HIS
A
231
27.999
11.521
48.625
1.00
14.26
O


ATOM
1811
N
VAL
A
232
29.310
12.190
46.920
1.00
14.20
N


ATOM
1812
CA
VAL
A
232
28.996
13.606
47.060
1.00
14.34
C


ATOM
1813
CB
VAL
A
232
30.282
14.474
47.166
1.00
14.14
C


ATOM
1814
CG1
VAL
A
232
29.929
15.952
47.329
1.00
15.14
C


ATOM
1815
CG2
VAL
A
232
31.150
14.000
48.332
1.00
13.76
C


ATOM
1816
C
VAL
A
232
28.171
14.037
45.862
1.00
14.70
C


ATOM
1817
O
VAL
A
232
28.595
13.880
44.716
1.00
14.68
O


ATOM
1818
N
SER
A
233
26.984
14.571
46.133
1.00
15.02
N


ATOM
1819
CA
SER
A
233
26.034
14.910
45.086
1.00
15.78
C


ATOM
1820
CB
SER
A
233
25.188
13.685
44.730
1.00
16.03
C


ATOM
1821
OG
SER
A
233
24.145
14.023
43.831
1.00
17.78
O


ATOM
1822
C
SER
A
233
25.132
16.042
45.541
1.00
15.96
C


ATOM
1823
O
SER
A
233
24.666
16.051
46.683
1.00
15.66
O


ATOM
1824
N
GLY
A
234
24.879
16.989
44.639
1.00
16.47
N


ATOM
1825
CA
GLY
A
234
23.979
18.109
44.920
1.00
17.13
C


ATOM
1826
C
GLY
A
234
22.589
17.671
45.352
1.00
17.83
C


ATOM
1827
O
GLY
A
234
21.904
18.394
46.076
1.00
17.68
O


ATOM
1828
N
MET
A
235
22.184
16.477
44.917
1.00
18.31
N


ATOM
1829
CA
MET
A
235
20.874
15.916
45.270
1.00
19.90
C


ATOM
1830
CB
MET
A
235
20.604
14.633
44.479
1.00
19.87
C


ATOM
1831
CG
MET
A
235
20.636
14.806
42.971
1.00
22.46
C


ATOM
1832
SD
MET
A
235
19.943
13.392
42.091
1.00
26.93
S


ATOM
1833
CE
MET
A
235
18.184
13.616
42.377
1.00
27.02
C


ATOM
1834
C
MET
A
235
20.729
15.626
46.767
1.00
18.55
C


ATOM
1835
O
MET
A
235
19.607
15.581
47.289
1.00
18.66
O


ATOM
1836
N
PHE
A
236
21.853
15.425
47.456
1.00
17.54
N


ATOM
1837
CA
PHE
A
236
21.819
15.129
48.888
1.00
16.56
C


ATOM
1838
CB
PHE
A
236
23.113
14.448
49.355
1.00
16.45
C


ATOM
1839
CG
PHE
A
236
23.252
13.015
48.900
1.00
16.34
C


ATOM
1840
CD1
PHE
A
236
22.138
12.181
48.799
1.00
16.76
C


ATOM
1841
CE1
PHE
A
236
22.271
10.851
48.382
1.00
17.06
C


ATOM
1842
CZ
PHE
A
236
23.530
10.341
48.084
1.00
16.76
C


ATOM
1843
CE2
PHE
A
236
24.645
11.158
48.191
1.00
16.13
C


ATOM
1844
CD2
PHE
A
236
24.505
12.488
48.605
1.00
15.86
C


ATOM
1845
C
PHE
A
236
21.511
16.358
49.743
1.00
16.31
C


ATOM
1846
O
PHE
A
236
20.946
16.232
50.830
1.00
16.55
O


ATOM
1847
N
GLY
A
237
21.877
17.539
49.248
1.00
15.77
N


ATOM
1848
CA
GLY
A
237
21.524
18.796
49.915
1.00
15.30
C


ATOM
1849
C
GLY
A
237
22.636
19.375
50.771
1.00
15.02
C


ATOM
1850
O
GLY
A
237
23.373
18.641
51.438
1.00
15.15
O


ATOM
1851
N
ALA
A
238
22.737
20.702
50.762
1.00
14.97
N


ATOM
1852
CA
ALA
A
238
23.798
21.415
51.475
1.00
14.74
C


ATOM
1853
CB
ALA
A
238
23.750
22.907
51.144
1.00
15.08
C


ATOM
1854
C
ALA
A
238
23.756
21.201
52.990
1.00
14.89
C


ATOM
1855
O
ALA
A
238
24.783
21.301
53.663
1.00
14.56
O


ATOM
1856
N
TRP
A
239
22.573
20.882
53.513
1.00
14.88
N


ATOM
1857
CA
TRP
A
239
22.390
20.696
54.952
1.00
15.05
C


ATOM
1858
CB
TRP
A
239
20.907
20.551
55.297
1.00
15.08
C


ATOM
1859
CG
TRP
A
239
20.225
19.398
54.617
1.00
15.39
C


ATOM
1860
CD1
TRP
A
239
19.536
19.433
53.439
1.00
15.59
C


ATOM
1861
NE1
TRP
A
239
19.039
18.190
53.141
1.00
16.02
N


ATOM
1862
CE2
TRP
A
239
19.400
17.316
54.133
1.00
15.28
C


ATOM
1863
CD2
TRP
A
239
20.145
18.045
55.086
1.00
15.37
C


ATOM
1864
CE3
TRP
A
239
20.638
17.375
56.216
1.00
15.47
C


ATOM
1865
CZ3
TRP
A
239
20.365
16.014
56.359
1.00
16.08
C


ATOM
1866
CH2
TRP
A
239
19.620
15.319
55.390
1.00
16.34
C


ATOM
1867
CZ2
TRP
A
239
19.128
15.950
54.275
1.00
16.37
C


ATOM
1868
C
TRP
A
239
23.190
19.524
55.517
1.00
15.04
C


ATOM
1869
O
TRP
A
239
23.469
19.481
56.721
1.00
15.45
O


ATOM
1870
N
ARG
A
240
23.543
18.575
54.649
1.00
14.96
N


ATOM
1871
CA
ARG
A
240
24.451
17.484
55.016
1.00
14.68
C


ATOM
1872
CB
ARG
A
240
23.758
16.113
54.916
1.00
14.96
C


ATOM
1873
CG
ARG
A
240
22.962
15.873
53.638
1.00
14.45
C


ATOM
1874
CD
ARG
A
240
22.520
14.422
53.553
1.00
15.27
C


ATOM
1875
NE
ARG
A
240
21.453
14.221
52.579
1.00
16.23
N


ATOM
1876
CZ
ARG
A
240
20.980
13.030
52.222
1.00
16.62
C


ATOM
1877
NH1
ARG
A
240
21.486
11.923
52.753
1.00
16.98
N


ATOM
1878
NH2
ARG
A
240
20.004
12.945
51.328
1.00
17.49
N


ATOM
1879
C
ARG
A
240
25.728
17.510
54.173
1.00
14.43
C


ATOM
1880
O
ARG
A
240
26.334
16.470
53.909
1.00
14.51
O


ATOM
1881
N
GLY
A
241
26.128
18.708
53.750
1.00
14.21
N


ATOM
1882
CA
GLY
A
241
27.324
18.872
52.928
1.00
14.05
C


ATOM
1883
C
GLY
A
241
27.291
18.029
51.666
1.00
14.02
C


ATOM
1884
O
GLY
A
241
28.332
17.576
51.188
1.00
14.10
O


ATOM
1885
N
ASN
A
242
26.085
17.809
51.134
1.00
13.71
N


ATOM
1886
CA
ASN
A
242
25.901
17.098
49.863
1.00
13.99
C


ATOM
1887
CB
ASN
A
242
26.517
17.905
48.710
1.00
13.75
C


ATOM
1888
CG
ASN
A
242
25.844
19.247
48.515
1.00
14.13
C


ATOM
1889
OD1
ASN
A
242
24.635
19.323
48.312
1.00
14.64
O


ATOM
1890
ND2
ASN
A
242
26.630
20.315
48.568
1.00
14.19
N


ATOM
1891
C
ASN
A
242
26.455
15.674
49.866
1.00
14.06
C


ATOM
1892
O
ASN
A
242
26.785
15.128
48.813
1.00
14.29
O


ATOM
1893
N
THR
A
243
26.518
15.062
51.045
1.00
14.19
N


ATOM
1894
CA
THR
A
243
27.267
13.822
51.217
1.00
14.72
C


ATOM
1895
CB
THR
A
243
28.577
14.090
51.989
1.00
14.75
C


ATOM
1896
OG1
THR
A
243
29.384
14.993
51.229
1.00
15.13
O


ATOM
1897
CG2
THR
A
243
29.361
12.801
52.229
1.00
15.83
C


ATOM
1898
C
THR
A
243
26.470
12.722
51.905
1.00
14.74
C


ATOM
1899
O
THR
A
243
25.675
12.984
52.812
1.00
14.79
O


ATOM
1900
N
SER
A
244
26.684
11.488
51.457
1.00
14.75
N


ATOM
1901
CA
SER
A
244
26.176
10.317
52.158
1.00
15.02
C


ATOM
1902
CB
SER
A
244
24.695
10.092
51.840
1.00
15.21
C


ATOM
1903
OG
SER
A
244
24.100
9.263
52.825
1.00
15.64
O


ATOM
1904
C
SER
A
244
26.977
9.076
51.801
1.00
15.30
C


ATOM
1905
O
SER
A
244
27.822
9.102
50.899
1.00
15.29
O


ATOM
1906
N
TRP
A
245
26.724
7.996
52.531
1.00
15.34
N


ATOM
1907
CA
TRP
A
245
27.194
6.682
52.135
1.00
15.69
C


ATOM
1908
CB
TRP
A
245
27.535
5.833
53.358
1.00
16.05
C


ATOM
1909
CG
TRP
A
245
28.886
6.120
53.943
1.00
16.43
C


ATOM
1910
CD1
TRP
A
245
30.100
5.796
53.402
1.00
17.01
C


ATOM
1911
NE1
TRP
A
245
31.113
6.212
54.229
1.00
17.52
N


ATOM
1912
CE2
TRP
A
245
30.566
6.812
55.334
1.00
17.00
C


ATOM
1913
CD2
TRP
A
245
29.162
6.771
55.186
1.00
16.88
C


ATOM
1914
CE3
TRP
A
245
28.359
7.325
56.193
1.00
17.00
C


ATOM
1915
CZ3
TRP
A
245
28.977
7.895
57.301
1.00
16.84
C


ATOM
1916
CH2
TRP
A
245
30.379
7.918
57.420
1.00
16.85
C


ATOM
1917
CZ2
TRP
A
245
31.188
7.385
56.451
1.00
16.77
C


ATOM
1918
C
TRP
A
245
26.113
6.002
51.309
1.00
15.83
C


ATOM
1919
O
TRP
A
245
24.929
6.039
51.666
1.00
16.01
O


ATOM
1920
N
VAL
A
246
26.522
5.404
50.194
1.00
15.86
N


ATOM
1921
CA
VAL
A
246
25.600
4.704
49.302
1.00
16.17
C


ATOM
1922
CB
VAL
A
246
25.447
5.433
47.936
1.00
16.13
C


ATOM
1923
CG1
VAL
A
246
24.817
6.804
48.123
1.00
15.98
C


ATOM
1924
CG2
VAL
A
246
26.798
5.546
47.215
1.00
15.47
C


ATOM
1925
C
VAL
A
246
26.046
3.263
49.059
1.00
16.48
C


ATOM
1926
O
VAL
A
246
27.220
2.930
49.232
1.00
16.67
O


ATOM
1927
N
ALA
A
247
25.101
2.414
48.665
1.00
16.71
N


ATOM
1928
CA
ALA
A
247
25.421
1.048
48.251
1.00
17.14
C


ATOM
1929
CB
ALA
A
247
25.017
0.049
49.329
1.00
17.29
C


ATOM
1930
C
ALA
A
247
24.733
0.722
46.930
1.00
17.43
C


ATOM
1931
O
ALA
A
247
23.554
1.041
46.752
1.00
17.42
O


ATOM
1932
N
PRO
A
248
25.475
0.103
45.987
1.00
17.73
N


ATOM
1933
CA
PRO
A
248
24.898
−0.307
44.708
1.00
18.09
C


ATOM
1934
CB
PRO
A
248
26.130
−0.540
43.828
1.00
18.22
C


ATOM
1935
CG
PRO
A
248
27.192
−0.942
44.776
1.00
17.84
C


ATOM
1936
CD
PRO
A
248
26.914
−0.217
46.071
1.00
17.92
C


ATOM
1937
C
PRO
A
248
24.073
−1.586
44.833
1.00
18.53
C


ATOM
1938
O
PRO
A
248
24.560
−2.594
45.357
1.00
18.97
O


ATOM
1939
N
LEU
A
249
22.830
−1.531
44.366
1.00
18.90
N


ATOM
1940
CA
LEU
A
249
21.934
−2.687
44.412
1.00
19.29
C


ATOM
1941
CB
LEU
A
249
20.519
−2.261
44.806
1.00
19.62
C


ATOM
1942
CG
LEU
A
249
20.209
−1.960
46.272
1.00
20.98
C


ATOM
1943
CD1
LEU
A
249
18.718
−1.733
46.428
1.00
22.37
C


ATOM
1944
CD2
LEU
A
249
20.668
−3.086
47.186
1.00
22.46
C


ATOM
1945
C
LEU
A
249
21.883
−3.426
43.082
1.00
19.13
C


ATOM
1946
O
LEU
A
249
21.780
−4.654
43.048
1.00
19.16
O


ATOM
1947
N
ALA
A
250
21.926
−2.666
41.990
1.00
19.03
N


ATOM
1948
CA
ALA
A
250
21.832
−3.222
40.643
1.00
18.99
C


ATOM
1949
CB
ALA
A
250
20.463
−3.856
40.423
1.00
19.20
C


ATOM
1950
C
ALA
A
250
22.073
−2.134
39.613
1.00
18.99
C


ATOM
1951
O
ALA
A
250
22.049
−0.949
39.935
1.00
19.17
O


ATOM
1952
N
TRP
A
251
22.300
−2.545
38.372
1.00
18.96
N


ATOM
1953
CA
TRP
A
251
22.410
−1.611
37.267
1.00
19.14
C


ATOM
1954
CB
TRP
A
251
23.402
−2.133
36.232
1.00
19.09
C


ATOM
1955
CG
TRP
A
251
24.804
−2.019
36.701
1.00
19.05
C


ATOM
1956
CD1
TRP
A
251
25.477
−2.896
37.504
1.00
18.96
C


ATOM
1957
NE1
TRP
A
251
26.754
−2.441
37.735
1.00
18.93
N


ATOM
1958
CE2
TRP
A
251
26.923
−1.246
37.085
1.00
19.18
C


ATOM
1959
CD2
TRP
A
251
25.710
−0.948
36.426
1.00
18.63
C


ATOM
1960
CE3
TRP
A
251
25.618
0.234
35.677
1.00
18.82
C


ATOM
1961
CZ3
TRP
A
251
26.727
1.071
35.616
1.00
19.08
C


ATOM
1962
CH2
TRP
A
251
27.919
0.747
36.282
1.00
19.76
C


ATOM
1963
CZ2
TRP
A
251
28.037
−0.403
37.021
1.00
19.19
C


ATOM
1964
C
TRP
A
251
21.051
−1.348
36.636
1.00
19.55
C


ATOM
1965
O
TRP
A
251
20.180
−2.223
36.630
1.00
19.41
O


ATOM
1966
N
HIS
A
252
20.872
−0.131
36.128
1.00
20.04
N


ATOM
1967
CA
HIS
A
252
19.635
0.275
35.463
1.00
20.98
C


ATOM
1968
CB
HIS
A
252
19.780
1.705
34.934
1.00
20.99
C


ATOM
1969
CG
HIS
A
252
18.480
2.369
34.601
1.00
21.68
C


ATOM
1970
ND1
HIS
A
252
17.736
2.037
33.489
1.00
22.07
N


ATOM
1971
CE1
HIS
A
252
16.654
2.793
33.444
1.00
22.45
C


ATOM
1972
NE2
HIS
A
252
16.672
3.609
34.482
1.00
22.56
N


ATOM
1973
CD2
HIS
A
252
17.806
3.367
35.220
1.00
22.29
C


ATOM
1974
C
HIS
A
252
19.309
−0.689
34.315
1.00
21.35
C


ATOM
1975
O
HIS
A
252
20.181
−0.999
33.501
1.00
21.32
O


ATOM
1976
N
PRO
A
253
18.052
−1.178
34.256
1.00
21.99
N


ATOM
1977
CA
PRO
A
253
17.661
−2.187
33.259
1.00
22.43
C


ATOM
1978
CB
PRO
A
253
16.200
−2.493
33.621
1.00
22.38
C


ATOM
1979
CG
PRO
A
253
15.736
−1.308
34.390
1.00
22.25
C


ATOM
1980
CD
PRO
A
253
16.930
−0.822
35.144
1.00
21.98
C


ATOM
1981
C
PRO
A
253
17.764
−1.720
31.801
1.00
22.95
C


ATOM
1982
O
PRO
A
253
17.895
−2.554
30.900
1.00
23.24
O


ATOM
1983
N
GLU
A
254
17.706
−0.408
31.575
1.00
23.34
N


ATOM
1984
CA
GLU
A
254
17.765
0.139
30.216
1.00
23.86
C


ATOM
1985
CB
GLU
A
254
16.459
0.862
29.855
1.00
24.08
C


ATOM
1986
CG
GLU
A
254
15.205
−0.028
29.874
1.00
25.50
C


ATOM
1987
CD
GLU
A
254
15.238
−1.156
28.844
1.00
27.12
C


ATOM
1988
OE1
GLU
A
254
15.884
−0.994
27.784
1.00
28.18
O


ATOM
1989
OE2
GLU
A
254
14.602
−2.204
29.092
1.00
28.43
O


ATOM
1990
C
GLU
A
254
18.970
1.050
29.985
1.00
23.73
C


ATOM
1991
O
GLU
A
254
19.635
0.958
28.949
1.00
24.16
O


ATOM
1992
N
ASN
A
255
19.245
1.929
30.948
1.00
23.41
N


ATOM
1993
CA
ASN
A
255
20.369
2.857
30.849
1.00
22.98
C


ATOM
1994
CB
ASN
A
255
20.151
4.075
31.760
1.00
23.09
C


ATOM
1995
CG
ASN
A
255
21.168
5.193
31.514
1.00
23.12
C


ATOM
1996
OD1
ASN
A
255
22.264
4.960
31.004
1.00
23.00
O


ATOM
1997
ND2
ASN
A
255
20.801
6.413
31.890
1.00
23.76
N


ATOM
1998
C
ASN
A
255
21.691
2.164
31.174
1.00
22.78
C


ATOM
1999
O
ASN
A
255
21.954
1.813
32.324
1.00
22.55
O


ATOM
2000
N
ARG
A
256
22.517
1.989
30.146
1.00
22.49
N


ATOM
2001
CA
ARG
A
256
23.775
1.244
30.245
1.00
22.40
C


ATOM
2002
CB
ARG
A
256
24.401
1.101
28.849
1.00
22.38
C


ATOM
2003
CG
ARG
A
256
25.431
−0.013
28.718
1.00
23.43
C


ATOM
2004
CD
ARG
A
256
25.793
−0.267
27.258
1.00
23.57
C


ATOM
2005
NE
ARG
A
256
26.850
−1.270
27.121
1.00
25.65
N


ATOM
2006
CZ
ARG
A
256
27.287
−1.755
25.960
1.00
26.46
C


ATOM
2007
NH1
ARG
A
256
26.761
−1.339
24.814
1.00
26.98
N


ATOM
2008
NH2
ARG
A
256
28.252
−2.666
25.945
1.00
27.03
N


ATOM
2009
C
ARG
A
256
24.780
1.883
31.214
1.00
21.84
C


ATOM
2010
O
ARG
A
256
25.665
1.204
31.739
1.00
21.63
O


ATOM
2011
N
ASN
A
257
24.632
3.185
31.452
1.00
21.28
N


ATOM
2012
CA
ASN
A
257
25.610
3.941
32.237
1.00
20.85
C


ATOM
2013
CB
ASN
A
257
26.105
5.155
31.439
1.00
21.32
C


ATOM
2014
CG
ASN
A
257
26.792
4.761
30.144
1.00
22.40
C


ATOM
2015
OD1
ASN
A
257
26.311
5.074
29.051
1.00
24.76
O


ATOM
2016
ND2
ASN
A
257
27.915
4.058
30.258
1.00
24.27
N


ATOM
2017
C
ASN
A
257
25.123
4.374
33.624
1.00
20.06
C


ATOM
2018
O
ASN
A
257
25.797
5.140
34.312
1.00
20.29
O


ATOM
2019
N
ALA
A
258
23.962
3.874
34.038
1.00
19.22
N


ATOM
2020
CA
ALA
A
258
23.401
4.233
35.338
1.00
18.54
C


ATOM
2021
CB
ALA
A
258
22.021
4.865
35.172
1.00
18.61
C


ATOM
2022
C
ALA
A
258
23.333
3.044
36.288
1.00
18.22
C


ATOM
2023
O
ALA
A
258
22.813
1.983
35.936
1.00
17.88
O


ATOM
2024
N
VAL
A
259
23.873
3.230
37.489
1.00
17.80
N


ATOM
2025
CA
VAL
A
259
23.763
2.235
38.551
1.00
18.02
C


ATOM
2026
CB
VAL
A
259
25.159
1.904
39.190
1.00
18.16
C


ATOM
2027
CG1
VAL
A
259
25.795
3.136
39.817
1.00
19.20
C


ATOM
2028
CG2
VAL
A
259
25.051
0.765
40.199
1.00
18.50
C


ATOM
2029
C
VAL
A
259
22.742
2.701
39.597
1.00
17.69
C


ATOM
2030
O
VAL
A
259
22.644
3.896
39.894
1.00
17.39
O


ATOM
2031
N
ILE
A
260
21.958
1.759
40.115
1.00
17.65
N


ATOM
2032
CA
ILE
A
260
20.954
2.071
41.124
1.00
17.83
C


ATOM
2033
CB
ILE
A
260
19.723
1.133
41.033
1.00
17.76
C


ATOM
2034
CG1
ILE
A
260
19.160
1.117
39.607
1.00
17.88
C


ATOM
2035
CD1
ILE
A
260
18.193
−0.030
39.331
1.00
17.61
C


ATOM
2036
CG2
ILE
A
260
18.659
1.560
42.039
1.00
17.70
C


ATOM
2037
C
ILE
A
260
21.567
1.974
42.514
1.00
18.01
C


ATOM
2038
O
ILE
A
260
21.998
0.897
42.942
1.00
18.20
O


ATOM
2039
N
MET
A
261
21.614
3.111
43.206
1.00
18.18
N


ATOM
2040
CA
MET
A
261
22.194
3.198
44.541
1.00
18.49
C


ATOM
2041
CB
MET
A
261
23.139
4.397
44.629
1.00
18.95
C


ATOM
2042
CG
MET
A
261
24.328
4.323
43.705
1.00
20.24
C


ATOM
2043
SD
MET
A
261
25.596
3.232
44.346
1.00
21.93
S


ATOM
2044
CE
MET
A
261
27.037
3.847
43.478
1.00
21.25
C


ATOM
2045
C
MET
A
261
21.114
3.355
45.594
1.00
18.31
C


ATOM
2046
O
MET
A
261
20.047
3.901
45.320
1.00
18.35
O


ATOM
2047
N
VAL
A
262
21.403
2.881
46.802
1.00
17.89
N


ATOM
2048
CA
VAL
A
262
20.582
3.200
47.962
1.00
17.97
C


ATOM
2049
CB
VAL
A
262
20.172
1.927
48.753
1.00
18.03
C


ATOM
2050
CG1
VAL
A
262
19.474
2.297
50.057
1.00
18.35
C


ATOM
2051
CG2
VAL
A
262
19.270
1.062
47.916
1.00
19.01
C


ATOM
2052
C
VAL
A
262
21.349
4.161
48.862
1.00
17.61
C


ATOM
2053
O
VAL
A
262
22.535
3.955
49.138
1.00
17.21
O


ATOM
2054
N
ASP
A
263
20.679
5.232
49.279
1.00
17.43
N


ATOM
2055
CA
ASP
A
263
21.227
6.142
50.271
1.00
17.72
C


ATOM
2056
CB
ASP
A
263
20.490
7.487
50.231
1.00
17.57
C


ATOM
2057
CG
ASP
A
263
21.002
8.471
51.272
1.00
18.01
C


ATOM
2058
OD1
ASP
A
263
21.948
8.134
52.014
1.00
16.76
O


ATOM
2059
OD2
ASP
A
263
20.446
9.586
51.355
1.00
19.03
O


ATOM
2060
C
ASP
A
263
21.107
5.492
51.643
1.00
17.65
C


ATOM
2061
O
ASP
A
263
20.004
5.350
52.185
1.00
17.86
O


ATOM
2062
N
LEU
A
264
22.248
5.093
52.199
1.00
17.66
N


ATOM
2063
CA
LEU
A
264
22.268
4.346
53.458
1.00
17.44
C


ATOM
2064
CB
LEU
A
264
23.637
3.693
53.687
1.00
17.50
C


ATOM
2065
CG
LEU
A
264
24.048
2.611
52.682
1.00
17.27
C


ATOM
2066
CD1
LEU
A
264
25.487
2.196
52.905
1.00
17.83
C


ATOM
2067
CD2
LEU
A
264
23.124
1.399
52.756
1.00
17.33
C


ATOM
2068
C
LEU
A
264
21.857
5.179
54.672
1.00
17.58
C


ATOM
2069
O
LEU
A
264
21.546
4.628
55.726
1.00
17.30
O


ATOM
2070
N
ALA
A
265
21.850
6.503
54.513
1.00
17.57
N


ATOM
2071
CA
ALA
A
265
21.405
7.407
55.578
1.00
17.94
C


ATOM
2072
CB
ALA
A
265
22.032
8.785
55.404
1.00
17.98
C


ATOM
2073
C
ALA
A
265
19.884
7.514
55.629
1.00
18.21
C


ATOM
2074
O
ALA
A
265
19.325
8.098
56.560
1.00
18.28
O


ATOM
2075
N
GLY
A
266
19.218
6.943
54.628
1.00
18.49
N


ATOM
2076
CA
GLY
A
266
17.768
7.041
54.522
1.00
19.08
C


ATOM
2077
C
GLY
A
266
17.018
5.995
55.324
1.00
19.56
C


ATOM
2078
O
GLY
A
266
17.594
5.298
56.167
1.00
19.16
O


ATOM
2079
N
ASP
A
267
15.718
5.906
55.061
1.00
20.17
N


ATOM
2080
CA
ASP
A
267
14.847
4.907
55.668
1.00
20.83
C


ATOM
2081
CB
ASP
A
267
13.535
5.568
56.130
1.00
21.05
C


ATOM
2082
CG
ASP
A
267
12.546
4.575
56.749
1.00
21.59
C


ATOM
2083
OD1
ASP
A
267
12.894
3.388
56.934
1.00
22.94
O


ATOM
2084
OD2
ASP
A
267
11.409
4.995
57.057
1.00
22.79
O


ATOM
2085
C
ASP
A
267
14.571
3.829
54.627
1.00
21.36
C


ATOM
2086
O
ASP
A
267
13.876
4.075
53.639
1.00
21.41
O


ATOM
2087
N
ILE
A
268
15.130
2.640
54.843
1.00
21.86
N


ATOM
2088
CA
ILE
A
268
15.031
1.559
53.855
1.00
22.65
C


ATOM
2089
CB
ILE
A
268
16.318
0.686
53.801
1.00
22.62
C


ATOM
2090
CG1
ILE
A
268
16.551
−0.033
55.135
1.00
23.00
C


ATOM
2091
CD1
ILE
A
268
17.500
−1.215
55.041
1.00
23.11
C


ATOM
2092
CG2
ILE
A
268
17.532
1.535
53.390
1.00
22.46
C


ATOM
2093
C
ILE
A
268
13.797
0.673
54.041
1.00
23.23
C


ATOM
2094
O
ILE
A
268
13.590
−0.274
53.281
1.00
23.41
O


ATOM
2095
N
SER
A
269
12.978
0.995
55.042
1.00
24.01
N


ATOM
2096
CA
SER
A
269
11.737
0.253
55.306
1.00
24.89
C


ATOM
2097
CB
SER
A
269
10.979
0.848
56.499
1.00
24.91
C


ATOM
2098
OG
SER
A
269
11.690
0.640
57.706
1.00
25.77
O


ATOM
2099
C
SER
A
269
10.813
0.131
54.079
1.00
25.39
C


ATOM
2100
O
SER
A
269
10.347
−0.968
53.779
1.00
25.49
O


ATOM
2101
N
PRO
A
270
10.549
1.255
53.364
1.00
25.94
N


ATOM
2102
CA
PRO
A
270
9.733
1.173
52.143
1.00
26.40
C


ATOM
2103
CB
PRO
A
270
9.838
2.585
51.556
1.00
26.42
C


ATOM
2104
CG
PRO
A
270
10.100
3.454
52.721
1.00
26.43
C


ATOM
2105
CD
PRO
A
270
10.957
2.647
53.649
1.00
26.03
C


ATOM
2106
C
PRO
A
270
10.259
0.146
51.136
1.00
26.83
C


ATOM
2107
O
PRO
A
270
9.468
−0.534
50.483
1.00
26.72
O


ATOM
2108
N
LEU
A
271
11.584
0.037
51.024
1.00
27.26
N


ATOM
2109
CA
LEU
A
271
12.214
−0.914
50.104
1.00
27.95
C


ATOM
2110
CB
LEU
A
271
13.722
−0.649
50.000
1.00
27.98
C


ATOM
2111
CG
LEU
A
271
14.191
0.629
49.299
1.00
28.13
C


ATOM
2112
CD1
LEU
A
271
15.702
0.766
49.423
1.00
28.43
C


ATOM
2113
CD2
LEU
A
271
13.770
0.639
47.833
1.00
28.30
C


ATOM
2114
C
LEU
A
271
11.972
−2.366
50.508
1.00
28.41
C


ATOM
2115
O
LEU
A
271
11.920
−3.253
49.656
1.00
28.42
O


ATOM
2116
N
LEU
A
272
11.826
−2.600
51.809
1.00
29.14
N


ATOM
2117
CA
LEU
A
272
11.621
−3.948
52.330
1.00
30.02
C


ATOM
2118
CB
LEU
A
272
12.144
−4.058
53.769
1.00
29.91
C


ATOM
2119
CG
LEU
A
272
13.614
−3.712
54.045
1.00
30.10
C


ATOM
2120
CD1
LEU
A
272
13.877
−3.670
55.543
1.00
30.43
C


ATOM
2121
CD2
LEU
A
272
14.559
−4.690
53.361
1.00
30.27
C


ATOM
2122
C
LEU
A
272
10.153
−4.382
52.269
1.00
30.64
C


ATOM
2123
O
LEU
A
272
9.851
−5.516
51.888
1.00
30.75
O


ATOM
2124
N
GLU
A
273
9.248
−3.473
52.628
1.00
31.44
N


ATOM
2125
CA
GLU
A
273
7.847
−3.834
52.879
1.00
32.20
C


ATOM
2126
CB
GLU
A
273
7.392
−3.290
54.243
1.00
32.28
C


ATOM
2127
CG
GLU
A
273
7.360
−1.766
54.343
1.00
32.84
C


ATOM
2128
CD
GLU
A
273
7.446
−1.263
55.777
1.00
33.54
C


ATOM
2129
OE1
GLU
A
273
6.807
−0.235
56.084
1.00
34.30
O


ATOM
2130
OE2
GLU
A
273
8.153
−1.891
56.595
1.00
33.75
O


ATOM
2131
C
GLU
A
273
6.855
−3.426
51.776
1.00
32.67
C


ATOM
2132
O
GLU
A
273
5.672
−3.775
51.844
1.00
32.65
O


ATOM
2133
N
LEU
A
274
7.333
−2.701
50.767
1.00
33.22
N


ATOM
2134
CA
LEU
A
274
6.458
−2.236
49.684
1.00
33.80
C


ATOM
2135
CB
LEU
A
274
6.450
−0.704
49.606
1.00
33.74
C


ATOM
2136
CG
LEU
A
274
6.027
0.069
50.860
1.00
33.91
C


ATOM
2137
CD1
LEU
A
274
6.216
1.564
50.664
1.00
33.94
C


ATOM
2138
CD2
LEU
A
274
4.591
−0.249
51.259
1.00
33.97
C


ATOM
2139
C
LEU
A
274
6.834
−2.835
48.328
1.00
34.16
C


ATOM
2140
O
LEU
A
274
8.009
−3.087
48.054
1.00
34.25
O


ATOM
2141
N
ASP
A
275
5.825
−3.056
47.486
1.00
34.65
N


ATOM
2142
CA
ASP
A
275
6.033
−3.615
46.148
1.00
35.13
C


ATOM
2143
CB
ASP
A
275
4.726
−4.203
45.588
1.00
35.16
C


ATOM
2144
CG
ASP
A
275
3.606
−3.175
45.493
1.00
35.50
C


ATOM
2145
OD1
ASP
A
275
2.593
−3.335
46.206
1.00
35.93
O


ATOM
2146
OD2
ASP
A
275
3.732
−2.213
44.703
1.00
35.74
O


ATOM
2147
C
ASP
A
275
6.622
−2.586
45.182
1.00
35.37
C


ATOM
2148
O
ASP
A
275
6.596
−1.381
45.450
1.00
35.41
O


ATOM
2149
N
SER
A
276
7.138
−3.072
44.054
1.00
35.74
N


ATOM
2150
CA
SER
A
276
7.849
−2.233
43.084
1.00
36.09
C


ATOM
2151
CB
SER
A
276
8.480
−3.098
41.991
1.00
36.12
C


ATOM
2152
OG
SER
A
276
7.507
−3.905
41.348
1.00
36.24
O


ATOM
2153
C
SER
A
276
6.981
−1.136
42.456
1.00
36.27
C


ATOM
2154
O
SER
A
276
7.476
−0.050
42.147
1.00
36.29
O


ATOM
2155
N
ASP
A
277
5.694
−1.427
42.271
1.00
36.57
N


ATOM
2156
CA
ASP
A
277
4.758
−0.464
41.685
1.00
36.83
C


ATOM
2157
CB
ASP
A
277
3.431
−1.144
41.325
1.00
36.90
C


ATOM
2158
CG
ASP
A
277
3.539
−2.030
40.089
1.00
37.18
C


ATOM
2159
OD1
ASP
A
277
4.198
−1.621
39.107
1.00
37.30
O


ATOM
2160
OD2
ASP
A
277
2.950
−3.132
40.095
1.00
37.67
O


ATOM
2161
C
ASP
A
277
4.509
0.738
42.600
1.00
36.93
C


ATOM
2162
O
ASP
A
277
4.449
1.878
42.133
1.00
36.95
O


ATOM
2163
N
THR
A
278
4.373
0.475
43.900
1.00
37.08
N


ATOM
2164
CA
THR
A
278
4.133
1.527
44.893
1.00
37.21
C


ATOM
2165
CB
THR
A
278
3.707
0.934
46.260
1.00
37.24
C


ATOM
2166
OG1
THR
A
278
2.723
−0.090
46.057
1.00
37.26
O


ATOM
2167
CG2
THR
A
278
3.123
2.017
47.164
1.00
37.32
C


ATOM
2168
C
THR
A
278
5.365
2.420
45.080
1.00
37.33
C


ATOM
2169
O
THR
A
278
5.240
3.638
45.234
1.00
37.33
O


ATOM
2170
N
LEU
A
279
6.548
1.805
45.056
1.00
37.41
N


ATOM
2171
CA
LEU
A
279
7.813
2.532
45.199
1.00
37.52
C


ATOM
2172
CB
LEU
A
279
8.986
1.552
45.327
1.00
37.54
C


ATOM
2173
CG
LEU
A
279
9.101
0.718
46.608
1.00
37.62
C


ATOM
2174
CD1
LEU
A
279
9.966
−0.510
46.371
1.00
37.83
C


ATOM
2175
CD2
LEU
A
279
9.646
1.548
47.764
1.00
37.83
C


ATOM
2176
C
LEU
A
279
8.058
3.492
44.033
1.00
37.57
C


ATOM
2177
O
LEU
A
279
8.646
4.561
44.213
1.00
37.61
O


ATOM
2178
N
ARG
A
280
7.602
3.099
42.845
1.00
37.64
N


ATOM
2179
CA
ARG
A
280
7.757
3.904
41.634
1.00
37.73
C


ATOM
2180
CB
ARG
A
280
7.426
3.064
40.400
1.00
37.74
C


ATOM
2181
CG
ARG
A
280
7.876
3.676
39.078
1.00
37.84
C


ATOM
2182
CD
ARG
A
280
7.328
2.898
37.883
1.00
37.88
C


ATOM
2183
NE
ARG
A
280
7.781
1.505
37.868
1.00
38.18
N


ATOM
2184
CZ
ARG
A
280
7.022
0.460
38.195
1.00
38.31
C


ATOM
2185
NH1
ARG
A
280
5.755
0.636
38.553
1.00
38.32
N


ATOM
2186
NH2
ARG
A
280
7.526
−0.765
38.146
1.00
38.33
N


ATOM
2187
C
ARG
A
280
6.867
5.143
41.671
1.00
37.74
C


ATOM
2188
O
ARG
A
280
7.336
6.246
41.971
1.00
37.72
O


ATOM
2189
N
ALA
A
295
9.877
8.433
52.274
1.00
25.76
N


ATOM
2190
CA
ALA
A
295
10.781
8.783
51.185
1.00
25.58
C


ATOM
2191
CB
ALA
A
295
11.658
9.962
51.581
1.00
25.68
C


ATOM
2192
C
ALA
A
295
11.638
7.584
50.782
1.00
25.50
C


ATOM
2193
O
ALA
A
295
12.276
6.951
51.629
1.00
25.66
O


ATOM
2194
N
VAL
A
296
11.640
7.274
49.486
1.00
25.14
N


ATOM
2195
CA
VAL
A
296
12.369
6.119
48.966
1.00
24.66
C


ATOM
2196
CB
VAL
A
296
11.730
5.567
47.661
1.00
24.71
C


ATOM
2197
CG1
VAL
A
296
12.414
4.275
47.230
1.00
24.78
C


ATOM
2198
CG2
VAL
A
296
10.232
5.334
47.851
1.00
24.58
C


ATOM
2199
C
VAL
A
296
13.836
6.491
48.722
1.00
24.36
C


ATOM
2200
O
VAL
A
296
14.134
7.288
47.829
1.00
24.46
O


ATOM
2201
M
PRO
A
297
14.756
5.908
49.516
1.00
23.99
N


ATOM
2202
CA
PRO
A
297
16.163
6.305
49.483
1.00
23.74
C


ATOM
2203
CB
PRO
A
297
16.692
5.798
50.824
1.00
23.69
C


ATOM
2204
CG
PRO
A
297
15.882
4.580
51.099
1.00
23.75
C


ATOM
2205
CD
PRO
A
297
14.515
4.822
50.488
1.00
23.89
C


ATOM
2206
C
PRO
A
297
16.920
5.658
48.320
1.00
23.66
C


ATOM
2207
O
PRO
A
297
17.931
4.981
48.528
1.00
23.48
O


ATOM
2208
N
VAL
A
298
16.421
5.873
47.108
1.00
23.57
N


ATOM
2209
CA
VAL
A
298
17.029
5.322
45.905
1.00
23.75
C


ATOM
2210
CB
VAL
A
298
16.066
4.327
45.196
1.00
23.90
C


ATOM
2211
CG1
VAL
A
298
16.452
4.122
43.731
1.00
24.23
C


ATOM
2212
CG2
VAL
A
298
16.040
2.996
45.937
1.00
24.33
C


ATOM
2213
C
VAL
A
298
17.419
6.453
44.960
1.00
23.70
C


ATOM
2214
O
VAL
A
298
16.653
7.396
44.757
1.00
23.73
O


ATOM
2215
N
LYS
A
299
18.622
6.363
44.402
1.00
23.47
N


ATOM
2216
CA
LYS
A
299
19.066
7.326
43.406
1.00
23.55
C


ATOM
2217
CB
LYS
A
299
19.792
8.504
44.067
1.00
24.04
C


ATOM
2218
CG
LYS
A
299
21.161
8.167
44.649
1.00
25.38
C


ATOM
2219
CD
LYS
A
299
22.096
9.375
44.600
1.00
27.13
C


ATOM
2220
CE
LYS
A
299
22.269
9.881
43.168
1.00
28.37
C


ATOM
2221
NZ
LYS
A
299
23.271
10.975
43.052
1.00
28.89
N


ATOM
2222
C
LYS
A
299
19.947
6.678
42.346
1.00
22.95
C


ATOM
2223
O
LYS
A
299
20.664
5.711
42.623
1.00
23.10
O


ATOM
2224
N
LEU
A
300
19.879
7.210
41.132
1.00
22.36
N


ATOM
2225
CA
LEU
A
300
20.734
6.753
40.051
1.00
21.72
C


ATOM
2226
CB
LEU
A
300
20.057
6.963
38.695
1.00
21.88
C


ATOM
2227
CG
LEU
A
300
18.787
6.160
38.393
1.00
22.24
C


ATOM
2228
CD1
LEU
A
300
18.215
6.566
37.046
1.00
22.48
C


ATOM
2229
CD2
LEU
A
300
19.056
4.657
38.431
1.00
22.49
C


ATOM
2230
C
LEU
A
300
22.058
7.494
40.085
1.00
21.20
C


ATOM
2231
O
LEU
A
300
22.100
8.703
40.311
1.00
21.28
O


ATOM
2232
N
VAL
A
301
23.138
6.753
39.876
1.00
20.12
N


ATOM
2233
CA
VAL
A
301
24.452
7.345
39.673
1.00
19.53
C


ATOM
2234
CB
VAL
A
301
25.492
6.776
40.664
1.00
19.49
C


ATOM
2235
CG1
VAL
A
301
26.910
7.165
40.255
1.00
20.01
C


ATOM
2236
CG2
VAL
A
301
25.190
7.266
42.074
1.00
19.25
C


ATOM
2237
C
VAL
A
301
24.868
7.082
38.236
1.00
19.22
C


ATOM
2238
O
VAL
A
301
24.911
5.933
37.794
1.00
18.96
O


ATOM
2239
N
HIS
A
302
25.143
8.158
37.505
1.00
18.78
N


ATOM
2240
CA
HIS
A
302
25.494
8.069
36.096
1.00
18.73
C


ATOM
2241
CB
HIS
A
302
24.820
9.192
35.309
1.00
19.01
C


ATOM
2242
CG
HIS
A
302
23.327
9.161
35.380
1.00
19.89
C


ATOM
2243
ND1
HIS
A
302
22.623
9.658
36.455
1.00
21.67
N


ATOM
2244
CE1
HIS
A
302
21.329
9.490
36.245
1.00
21.22
C


ATOM
2245
NE2
HIS
A
302
21.170
8.897
35.077
1.00
22.02
N


ATOM
2246
CD2
HIS
A
302
22.404
8.678
34.516
1.00
20.67
C


ATOM
2247
C
HIS
A
302
27.000
8.143
35.939
1.00
18.54
C


ATOM
2248
O
HIS
A
302
27.601
9.195
36.155
1.00
17.95
O


ATOM
2249
N
ILE
A
303
27.605
7.021
35.556
1.00
18.41
N


ATOM
2250
CA
ILE
A
303
29.068
6.897
35.544
1.00
18.75
C


ATOM
2251
CB
ILE
A
303
29.530
5.425
35.403
1.00
18.89
C


ATOM
2252
CG1
ILE
A
303
28.977
4.810
34.111
1.00
19.75
C


ATOM
2253
CD1
ILE
A
303
29.151
3.324
34.014
1.00
20.54
C


ATOM
2254
CG2
ILE
A
303
29.151
4.617
36.658
1.00
19.75
C


ATOM
2255
C
ILE
A
303
29.745
7.757
34.477
1.00
18.39
C


ATOM
2256
O
ILE
A
303
30.956
7.964
34.521
1.00
17.99
O


ATOM
2257
N
ASN
A
304
28.959
8.251
33.523
1.00
18.32
N


ATOM
2258
CA
ASN
A
304
29.475
9.162
32.501
1.00
18.64
C


ATOM
2259
CB
ASN
A
304
28.827
8.880
31.129
1.00
19.11
C


ATOM
2260
CG
ASN
A
304
27.296
8.814
31.186
1.00
20.53
C


ATOM
2261
OD1
ASN
A
304
26.697
8.625
32.246
1.00
22.87
O


ATOM
2262
ND2
ASN
A
304
26.665
8.954
30.026
1.00
22.68
N


ATOM
2263
C
ASN
A
304
29.335
10.641
32.872
1.00
18.43
C


ATOM
2264
O
ASN
A
304
29.711
11.517
32.095
1.00
18.48
O


ATOM
2265
N
LYS
A
305
28.819
10.909
34.070
1.00
17.99
N


ATOM
2266
CA
LYS
A
305
28.513
12.280
34.490
1.00
17.91
C


ATOM
2267
CB
LYS
A
305
27.030
12.405
34.858
1.00
18.35
C


ATOM
2268
CG
LYS
A
305
26.094
12.276
33.669
1.00
19.69
C


ATOM
2269
CD
LYS
A
305
24.672
12.655
34.031
1.00
22.17
C


ATOM
2270
CE
LYS
A
305
23.787
12.684
32.791
1.00
24.13
C


ATOM
2271
NZ
LYS
A
305
22.386
13.066
33.110
1.00
26.24
N


ATOM
2272
C
LYS
A
305
29.401
12.774
35.638
1.00
17.56
C


ATOM
2273
O
LYS
A
305
28.974
13.593
36.453
1.00
17.40
O


ATOM
2274
N
CYS
A
306
30.638
12.277
35.681
1.00
17.12
N


ATOM
2275
CA
CYS
A
306
31.616
12.647
36.721
1.00
16.92
C


ATOM
2276
CB
CYS
A
306
32.221
14.029
36.441
1.00
17.16
C


ATOM
2277
SG
CYS
A
306
32.868
14.228
34.799
1.00
19.64
S


ATOM
2278
C
CYS
A
306
31.050
12.618
38.144
1.00
16.23
C


ATOM
2279
O
CYS
A
306
31.200
13.589
38.891
1.00
16.57
O


ATOM
2280
N
PRO
A
307
30.407
11.503
38.536
1.00
15.55
N


ATOM
2281
CA
PRO
A
307
29.928
11.435
39.913
1.00
15.21
C


ATOM
2282
CB
PRO
A
307
29.089
10.156
39.929
1.00
15.16
C


ATOM
2283
CG
PRO
A
307
29.690
9.305
38.854
1.00
14.99
C


ATOM
2284
CD
PRO
A
307
30.122
10.266
37.785
1.00
15.31
C


ATOM
2285
C
PRO
A
307
31.101
11.315
40.875
1.00
14.94
C


ATOM
2286
O
PRO
A
307
32.095
10.653
40.558
1.00
14.73
O


ATOM
2287
N
VAL
A
308
31.007
11.987
42.020
1.00
14.58
N


ATOM
2288
CA
VAL
A
308
32.041
11.880
43.039
1.00
14.38
C


ATOM
2289
CB
VAL
A
308
32.095
13.128
43.950
1.00
14.27
C


ATOM
2290
CG1
VAL
A
308
33.123
12.930
45.059
1.00
14.53
C


ATOM
2291
CG2
VAL
A
308
32.424
14.374
43.129
1.00
15.01
C


ATOM
2292
C
VAL
A
308
31.799
10.629
43.866
1.00
14.31
C


ATOM
2293
O
VAL
A
308
30.786
10.524
44.565
1.00
14.45
O


ATOM
2294
N
LEU
A
309
32.721
9.675
43.760
1.00
14.25
N


ATOM
2295
CA
LEU
A
309
32.628
8.408
44.485
1.00
14.24
C


ATOM
2296
CB
LEU
A
309
32.162
7.282
43.556
1.00
14.13
C


ATOM
2297
CG
LEU
A
309
30.734
7.295
43.002
1.00
14.20
C


ATOM
2298
CD1
LEU
A
309
30.584
6.216
41.932
1.00
14.78
C


ATOM
2299
CD2
LEU
A
309
29.696
7.108
44.103
1.00
15.11
C


ATOM
2300
C
LEU
A
309
33.983
8.037
45.045
1.00
14.61
C


ATOM
2301
O
LEU
A
309
35.007
8.228
44.385
1.00
14.41
O


ATOM
2302
N
ALA
A
310
33.986
7.488
46.253
1.00
15.14
N


ATOM
2303
CA
ALA
A
310
35.217
6.987
46.865
1.00
15.91
C


ATOM
2304
CB
ALA
A
310
35.956
8.114
47.581
1.00
16.02
C


ATOM
2305
C
ALA
A
310
34.916
5.850
47.829
1.00
16.86
C


ATOM
2306
O
ALA
A
310
33.774
5.678
48.258
1.00
16.58
O


ATOM
2307
N
GLN
A
311
35.945
5.075
48.169
1.00
17.85
N


ATOM
2308
CA
GLN
A
311
35.812
4.009
49.164
1.00
19.42
C


ATOM
2309
CB
GLN
A
311
37.169
3.342
49.436
1.00
19.58
C


ATOM
2310
CG
GLN
A
311
38.293
4.306
49.805
1.00
21.33
C


ATOM
2311
CD
GLN
A
311
39.614
3.605
50.088
1.00
22.30
C


ATOM
2312
OE1
GLN
A
311
39.776
2.414
49.816
1.00
26.55
O


ATOM
2313
NE2
GLN
A
311
40.571
4.350
50.638
1.00
25.81
N


ATOM
2314
C
GLN
A
311
35.210
4.558
50.457
1.00
19.41
C


ATOM
2315
O
GLN
A
311
35.450
5.710
50.819
1.00
18.91
O


ATOM
2316
N
ALA
A
312
34.418
3.730
51.136
1.00
20.15
N


ATOM
2317
CA
ALA
A
312
33.643
4.165
52.305
1.00
20.85
C


ATOM
2318
CB
ALA
A
312
32.865
2.994
52.894
1.00
20.99
C


ATOM
2319
C
ALA
A
312
34.478
4.857
53.389
1.00
21.47
C


ATOM
2320
O
ALA
A
312
34.021
5.821
54.003
1.00
21.38
O


ATOM
2321
N
ASN
A
313
35.700
4.372
53.612
1.00
22.21
N


ATOM
2322
CA
ASN
A
313
36.552
4.913
54.678
1.00
22.99
C


ATOM
2323
CB
ASN
A
313
37.631
3.898
55.097
1.00
23.35
C


ATOM
2324
CG
ASN
A
313
38.760
3.767
54.077
1.00
24.25
C


ATOM
2325
OD1
ASN
A
313
38.743
4.394
53.018
1.00
25.71
O


ATOM
2326
ND2
ASN
A
313
39.754
2.946
54.406
1.00
26.19
N


ATOM
2327
C
ASN
A
313
37.165
6.295
54.397
1.00
23.17
C


ATOM
2328
O
ASN
A
313
37.811
6.879
55.273
1.00
23.31
O


ATOM
2329
N
THR
A
314
36.956
6.813
53.184
1.00
23.21
N


ATOM
2330
CA
THR
A
314
37.395
8.169
52.819
1.00
23.60
C


ATOM
2331
CB
THR
A
314
37.095
8.484
51.333
1.00
23.64
C


ATOM
2332
OG1
THR
A
314
37.724
7.506
50.501
1.00
24.38
O


ATOM
2333
CG2
THR
A
314
37.609
9.873
50.947
1.00
23.80
C


ATOM
2334
C
THR
A
314
36.729
9.223
53.708
1.00
23.64
C


ATOM
2335
O
THR
A
314
37.332
10.253
54.029
1.00
23.91
O


ATOM
2336
N
LEU
A
315
35.481
8.960
54.086
1.00
23.65
N


ATOM
2337
CA
LEU
A
315
34.779
9.782
55.056
1.00
23.66
C


ATOM
2338
CB
LEU
A
315
33.293
9.902
54.689
1.00
23.52
C


ATOM
2339
CG
LEU
A
315
32.476
11.001
55.375
1.00
23.24
C


ATOM
2340
CD1
LEU
A
315
32.862
12.374
54.850
1.00
23.13
C


ATOM
2341
CD2
LEU
A
315
30.993
10.754
55.170
1.00
23.20
C


ATOM
2342
C
LEU
A
315
34.953
9.160
56.438
1.00
23.89
C


ATOM
2343
O
LEU
A
315
34.350
8.133
56.753
1.00
23.82
O


ATOM
2344
N
ARG
A
316
35.805
9.780
57.246
1.00
24.44
N


ATOM
2345
CA
ARG
A
316
36.149
9.256
58.563
1.00
24.97
C


ATOM
2346
CB
ARG
A
316
37.540
9.749
58.974
1.00
25.29
C


ATOM
2347
CG
ARG
A
316
38.667
9.171
58.119
1.00
26.77
C


ATOM
2348
CD
ARG
A
316
39.928
10.021
58.179
1.00
29.89
C


ATOM
2349
NE
ARG
A
316
39.798
11.261
57.409
1.00
31.75
N


ATOM
2350
CZ
ARG
A
316
40.818
12.042
57.063
1.00
33.02
C


ATOM
2351
NH1
ARG
A
316
42.060
11.720
57.409
1.00
33.79
N


ATOM
2352
NH2
ARG
A
316
40.598
13.149
56.370
1.00
34.00
N


ATOM
2353
C
ARG
A
316
35.088
9.652
59.594
1.00
24.93
C


ATOM
2354
O
ARG
A
316
34.334
10.598
59.366
1.00
24.77
O


ATOM
2355
N
PRO
A
317
34.997
8.903
60.716
1.00
25.05
N


ATOM
2356
CA
PRO
A
317
34.018
9.216
61.766
1.00
24.98
C


ATOM
2357
CB
PRO
A
317
34.500
8.386
62.971
1.00
24.96
C


ATOM
2358
CG
PRO
A
317
35.734
7.656
62.514
1.00
25.21
C


ATOM
2359
CD
PRO
A
317
35.768
7.691
61.037
1.00
25.07
C


ATOM
2360
C
PRO
A
317
33.944
10.703
62.130
1.00
25.00
C


ATOM
2361
O
PRO
A
317
32.847
11.229
62.331
1.00
24.83
O


ATOM
2362
N
GLU
A
318
35.097
11.370
62.200
1.00
25.02
N


ATOM
2363
CA
GLU
A
318
35.146
12.800
62.528
1.00
25.13
C


ATOM
2364
CB
GLU
A
318
36.572
13.235
62.918
1.00
25.38
C


ATOM
2365
CG
GLU
A
318
37.633
13.054
61.823
1.00
26.70
C


ATOM
2366
CD
GLU
A
318
38.376
11.722
61.909
1.00
28.26
C


ATOM
2367
OE1
GLU
A
318
37.827
10.748
62.472
1.00
28.57
O


ATOM
2368
OE2
GLU
A
318
39.518
11.654
61.403
1.00
29.44
O


ATOM
2369
C
GLU
A
318
34.589
13.684
61.403
1.00
24.84
C


ATOM
2370
O
GLU
A
318
34.036
14.755
61.664
1.00
24.73
O


ATOM
2371
N
ASP
A
319
34.736
13.225
60.159
1.00
24.57
N


ATOM
2372
CA
ASP
A
319
34.174
13.920
58.998
1.00
24.36
C


ATOM
2373
CB
ASP
A
319
34.741
13.345
57.695
1.00
24.59
C


ATOM
2374
CG
ASP
A
319
36.246
13.517
57.575
1.00
25.22
C


ATOM
2375
OD1
ASP
A
319
36.766
14.586
57.963
1.00
26.23
O


ATOM
2376
OD2
ASP
A
319
36.909
12.584
57.068
1.00
26.18
O


ATOM
2377
C
ASP
A
319
32.650
13.809
58.989
1.00
23.92
C


ATOM
2378
O
ASP
A
319
31.948
14.788
58.725
1.00
23.64
O


ATOM
2379
N
ALA
A
320
32.150
12.608
59.279
1.00
23.57
N


ATOM
2380
CA
ALA
A
320
30.710
12.362
59.358
1.00
23.46
C


ATOM
2381
CB
ALA
A
320
30.436
10.881
59.579
1.00
23.46
C


ATOM
2382
C
ALA
A
320
30.060
13.201
60.459
1.00
23.35
C


ATOM
2383
O
ALA
A
320
28.975
13.752
60.268
1.00
23.22
O


ATOM
2384
N
ASP
A
321
30.739
13.301
61.604
1.00
23.33
N


ATOM
2385
CA
ASP
A
321
30.255
14.106
62.729
1.00
23.33
C


ATOM
2386
CB
ASP
A
321
31.190
13.966
63.938
1.00
23.72
C


ATOM
2387
CG
ASP
A
321
31.140
12.578
64.564
1.00
25.17
C


ATOM
2388
OD1
ASP
A
321
30.175
11.828
64.300
1.00
27.19
O


ATOM
2389
OD2
ASP
A
321
32.072
12.238
65.324
1.00
27.12
O


ATOM
2390
C
ASP
A
321
30.115
15.575
62.341
1.00
22.91
C


ATOM
2391
O
ASP
A
321
29.114
16.217
62.666
1.00
22.72
O


ATOM
2392
N
ARG
A
322
31.120
16.091
61.634
1.00
22.49
N


ATOM
2393
CA
ARG
A
322
31.113
17.471
61.143
1.00
22.19
C


ATOM
2394
CB
ARG
A
322
32.437
17.792
60.432
1.00
22.22
C


ATOM
2395
CG
ARG
A
322
32.479
19.161
59.769
1.00
22.55
C


ATOM
2396
CD
ARG
A
322
33.768
19.378
58.999
1.00
23.30
C


ATOM
2397
NE
ARG
A
322
33.646
20.499
58.069
1.00
24.98
N


ATOM
2398
CZ
ARG
A
322
33.445
20.373
56.759
1.00
24.81
C


ATOM
2399
NH1
ARG
A
322
33.359
19.168
56.206
1.00
24.90
N


ATOM
2400
NH2
ARG
A
322
33.341
21.454
55.997
1.00
25.12
N


ATOM
2401
C
ARG
A
322
29.926
17.737
60.210
1.00
21.78
C


ATOM
2402
O
ARG
A
322
29.302
18.798
60.276
1.00
21.78
O


ATOM
2403
N
LEU
A
323
29.617
16.766
59.353
1.00
21.10
N


ATOM
2404
CA
LEU
A
323
28.533
16.906
58.378
1.00
20.82
C


ATOM
2405
CB
LEU
A
323
28.845
16.102
57.110
1.00
20.56
C


ATOM
2406
CG
LEU
A
323
30.109
16.485
56.333
1.00
20.41
C


ATOM
2407
CD1
LEU
A
323
30.343
15.517
55.188
1.00
20.38
C


ATOM
2408
CD2
LEU
A
323
30.032
17.921
55.819
1.00
20.70
C


ATOM
2409
C
LEU
A
323
27.171
16.494
58.942
1.00
20.63
C


ATOM
2410
O
LEU
A
323
26.145
16.640
58.273
1.00
20.55
O


ATOM
2411
N
GLY
A
324
27.171
15.977
60.169
1.00
20.56
N


ATOM
2412
CA
GLY
A
324
25.936
15.567
60.844
1.00
20.54
C


ATOM
2413
C
GLY
A
324
25.360
14.254
60.341
1.00
20.62
C


ATOM
2414
O
GLY
A
324
24.167
13.989
60.507
1.00
20.98
O


ATOM
2415
N
ILE
A
325
26.213
13.429
59.737
1.00
20.56
N


ATOM
2416
CA
ILE
A
325
25.791
12.143
59.180
1.00
20.60
C


ATOM
2417
CB
ILE
A
325
26.606
11.784
57.904
1.00
20.53
C


ATOM
2418
CG1
ILE
A
325
26.419
12.867
56.836
1.00
20.70
C


ATOM
2419
CD1
ILE
A
325
27.453
12.836
55.723
1.00
20.37
C


ATOM
2420
CG2
ILE
A
325
26.202
10.401
57.362
1.00
21.15
C


ATOM
2421
C
ILE
A
325
25.919
11.033
60.226
1.00
20.62
C


ATOM
2422
O
ILE
A
325
26.963
10.888
60.863
1.00
20.83
O


ATOM
2423
N
ASN
A
326
24.844
10.263
60.395
1.00
20.58
N


ATOM
2424
CA
ASN
A
326
24.817
9.141
61.335
1.00
20.69
C


ATOM
2425
CB
ASN
A
326
23.369
8.831
61.745
1.00
20.79
C


ATOM
2426
CG
ASN
A
326
23.274
7.952
62.997
1.00
21.31
C


ATOM
2427
OD1
ASN
A
326
22.289
8.023
63.735
1.00
23.24
O


ATOM
2428
ND2
ASN
A
326
24.284
7.120
63.230
1.00
21.17
N


ATOM
2429
C
ASN
A
326
25.486
7.904
60.733
1.00
20.40
C


ATOM
2430
O
ASN
A
326
24.861
7.143
59.989
1.00
20.45
O


ATOM
2431
N
ARG
A
327
26.761
7.716
61.070
1.00
20.25
N


ATOM
2432
CA
ARG
A
327
27.580
6.629
60.530
1.00
20.22
C


ATOM
2433
CB
ARG
A
327
29.027
6.775
61.017
1.00
20.28
C


ATOM
2434
CG
ARG
A
327
30.025
5.801
60.404
1.00
20.65
C


ATOM
2435
CD
ARG
A
327
31.431
6.110
60.896
1.00
20.96
C


ATOM
2436
NE
ARG
A
327
32.417
5.128
60.449
1.00
22.26
N


ATOM
2437
CZ
ARG
A
327
32.745
4.028
61.125
1.00
23.08
C


ATOM
2438
NH1
ARG
A
327
32.159
3.753
62.283
1.00
23.38
N


ATOM
2439
NH2
ARG
A
327
33.661
3.200
60.638
1.00
23.92
N


ATOM
2440
C
ARG
A
327
27.029
5.237
60.875
1.00
19.92
C


ATOM
2441
O
ARG
A
327
26.925
4.374
60.001
1.00
20.03
O


ATOM
2442
N
GLN
A
328
26.673
5.029
62.143
1.00
19.65
N


ATOM
2443
CA
GLN
A
328
26.159
3.732
62.587
1.00
19.32
C


ATOM
2444
CB
GLN
A
328
26.042
3.677
64.117
1.00
19.35
C


ATOM
2445
CG
GLN
A
328
25.840
2.263
64.677
1.00
19.94
C


ATOM
2446
CD
GLN
A
328
26.906
1.281
64.201
1.00
20.35
C


ATOM
2447
OE1
GLN
A
328
28.099
1.478
64.435
1.00
21.19
O


ATOM
2448
NE2
GLN
A
328
26.475
0.219
63.528
1.00
21.05
N


ATOM
2449
C
GLN
A
328
24.824
3.370
61.928
1.00
18.99
C


ATOM
2450
O
GLN
A
328
24.573
2.202
61.633
1.00
19.16
O


ATOM
2451
N
HIS
A
329
23.974
4.371
61.698
1.00
18.85
N


ATOM
2452
CA
HIS
A
329
22.712
4.150
60.991
1.00
18.74
C


ATOM
2453
CB
HIS
A
329
21.884
5.436
60.942
1.00
18.98
C


ATOM
2454
CG
HIS
A
329
20.599
5.299
60.184
1.00
19.79
C


ATOM
2455
ND1
HIS
A
329
19.485
4.682
60.712
1.00
21.92
N


ATOM
2456
CE1
HIS
A
329
18.506
4.711
59.824
1.00
22.02
C


ATOM
2457
NE2
HIS
A
329
18.945
5.326
58.740
1.00
21.91
N


ATOM
2458
CD2
HIS
A
329
20.250
5.704
58.940
1.00
21.39
C


ATOM
2459
C
HIS
A
329
22.960
3.619
59.578
1.00
18.57
C


ATOM
2460
O
HIS
A
329
22.260
2.717
59.114
1.00
18.41
O


ATOM
2461
N
CYS
A
330
23.962
4.184
58.904
1.00
18.22
N


ATOM
2462
CA
CYS
A
330
24.350
3.734
57.567
1.00
18.07
C


ATOM
2463
CB
CYS
A
330
25.386
4.681
56.959
1.00
18.07
C


ATOM
2464
SG
CYS
A
330
24.742
6.328
56.591
1.00
18.74
S


ATOM
2465
C
CYS
A
330
24.875
2.299
57.585
1.00
18.02
C


ATOM
2466
O
CYS
A
330
24.528
1.495
56.716
1.00
17.98
O


ATOM
2467
N
LEU
A
331
25.707
1.986
58.580
1.00
17.89
N


ATOM
2468
CA
LEU
A
331
26.221
0.626
58.766
1.00
18.11
C


ATOM
2469
CB
LEU
A
331
27.266
0.590
59.885
1.00
18.15
C


ATOM
2470
CG
LEU
A
331
28.644
1.179
59.568
1.00
18.84
C


ATOM
2471
CD1
LEU
A
331
29.422
1.432
60.849
1.00
19.51
C


ATOM
2472
CD2
LEU
A
331
29.428
0.257
58.639
1.00
18.77
C


ATOM
2473
C
LEU
A
331
25.100
−0.370
59.060
1.00
18.08
C


ATOM
2474
O
LEU
A
331
25.104
−1.491
58.543
1.00
18.15
O


ATOM
2475
N
ASP
A
332
24.144
0.049
59.888
1.00
18.23
N


ATOM
2476
CA
ASP
A
332
22.983
−0.778
60.221
1.00
18.36
C


ATOM
2477
CB
ASP
A
332
22.136
−0.109
61.307
1.00
18.62
C


ATOM
2478
CG
ASP
A
332
22.808
−0.123
62.670
1.00
19.73
C


ATOM
2479
OD1
ASP
A
332
23.821
−0.840
62.842
1.00
21.29
O


ATOM
2480
OD2
ASP
A
332
22.318
0.584
63.576
1.00
21.64
O


ATOM
2481
C
ASP
A
332
22.131
−1.068
58.992
1.00
18.13
C


ATOM
2482
O
ASP
A
332
21.719
−2.207
58.772
1.00
18.22
O


ATOM
2483
N
ASN
A
333
21.875
−0.034
58.191
1.00
18.07
N


ATOM
2484
CA
ASN
A
333
21.117
−0.187
56.950
1.00
18.06
C


ATOM
2485
CB
ASN
A
333
20.853
1.176
56.302
1.00
17.93
C


ATOM
2486
CG
ASN
A
333
19.598
1.853
56.836
1.00
18.32
C


ATOM
2487
OD1
ASN
A
333
19.377
3.038
56.592
1.00
19.16
O


ATOM
2488
ND2
ASN
A
333
18.766
1.101
57.549
1.00
17.36
N


ATOM
2489
C
ASN
A
333
21.811
−1.104
55.951
1.00
17.99
C


ATOM
2490
O
ASN
A
333
21.160
−1.894
55.270
1.00
18.27
O


ATOM
2491
N
LEU
A
334
23.135
−0.989
55.864
1.00
17.99
N


ATOM
2492
CA
LEU
A
334
23.922
−1.826
54.961
1.00
18.04
C


ATOM
2493
CB
LEU
A
334
25.395
−1.400
54.971
1.00
17.91
C


ATOM
2494
CG
LEU
A
334
26.366
−2.220
54.112
1.00
17.45
C


ATOM
2495
CD1
LEU
A
334
26.037
−2.092
52.631
1.00
18.05
C


ATOM
2496
CD2
LEU
A
334
27.801
−1.805
54.389
1.00
17.93
C


ATOM
2497
C
LEU
A
334
23.787
−3.305
55.320
1.00
18.45
C


ATOM
2498
O
LEU
A
334
23.619
−4.148
54.436
1.00
18.51
O


ATOM
2499
N
LYS
A
335
23.854
−3.608
56.617
1.00
18.96
N


ATOM
2500
CA
LYS
A
335
23.696
−4.981
57.098
1.00
19.62
C


ATOM
2501
CB
LYS
A
335
23.904
−5.056
58.615
1.00
19.51
C


ATOM
2502
CG
LYS
A
335
23.936
−6.478
59.166
1.00
20.07
C


ATOM
2503
CD
LYS
A
335
24.222
−6.492
60.659
1.00
20.67
C


ATOM
2504
CE
LYS
A
335
24.105
−7.901
61.234
1.00
22.00
C


ATOM
2505
NZ
LYS
A
335
22.687
−8.367
61.300
1.00
23.40
N


ATOM
2506
C
LYS
A
335
22.328
−5.545
56.713
1.00
19.76
C


ATOM
2507
O
LYS
A
3352
2.234
−6.662
56.204
1.00
20.11
O


ATOM
2508
N
ILE
A
336
21.275
−4.759
56.941
1.00
20.17
N


ATOM
2509
CA
ILE
A
336
19.912
−5.176
56.605
1.00
20.40
C


ATOM
2510
CB
ILE
A
336
18.852
−4.163
57.114
1.00
20.54
C


ATOM
2511
CG1
ILE
A
336
18.868
−4.102
58.645
1.00
20.57
C


ATOM
2512
CD1
ILE
A
336
18.142
−2.899
59.228
1.00
21.67
C


ATOM
2513
CG2
ILE
A
336
17.454
−4.540
56.609
1.00
20.44
C


ATOM
2514
C
ILE
A
336
19.750
−5.410
55.101
1.00
20.50
C


ATOM
2515
O
ILE
A
336
19.191
−6.425
54.685
1.00
20.70
O


ATOM
2516
N
LEU
A
337
20.259
−4.481
54.291
1.00
20.64
N


ATOM
2517
CA
LEU
A
337
20.169
−4.609
52.837
1.00
20.89
C


ATOM
2518
CB
LEU
A
337
20.764
−3.380
52.138
1.00
20.92
C


ATOM
2519
CG
LEU
A
337
19.896
−2.119
52.114
1.00
21.61
C


ATOM
2520
CD1
LEU
A
337
20.722
−0.928
51.680
1.00
22.45
C


ATOM
2521
CD2
LEU
A
337
18.680
−2.292
51.201
1.00
22.27
C


ATOM
2522
C
LEU
A
337
20.841
−5.885
52.338
1.00
20.93
C


ATOM
2523
O
LEU
A
337
20.287
−6.596
51.499
1.00
21.08
O


ATOM
2524
N
ARG
A
338
22.026
−6.176
52.875
1.00
21.06
N


ATOM
2525
CA
ARG
A
338
22.789
−7.369
52.498
1.00
21.19
C


ATOM
2526
CB
ARG
A
338
24.178
−7.334
53.132
1.00
20.97
C


ATOM
2527
CG
ARG
A
338
25.153
−6.431
52.402
1.00
20.33
C


ATOM
2528
CD
ARG
A
338
26.404
−6.179
53.220
1.00
19.44
C


ATOM
2529
NE
ARG
A
338
27.484
−5.639
52.395
1.00
18.52
N


ATOM
2530
CZ
ARG
A
338
28.638
−5.179
52.870
1.00
17.85
C


ATOM
2531
NH1
ARG
A
338
28.869
−5.173
54.179
1.00
18.83
N


ATOM
2532
NH2
ARG
A
338
29.562
−4.716
52.033
1.00
18.24
N


ATOM
2533
C
ARG
A
338
22.069
−8.663
52.868
1.00
21.66
C


ATOM
2534
O
ARG
A
338
22.253
−9.692
52.217
1.00
21.74
O


ATOM
2535
N
GLU
A
339
21.249
−8.600
53.912
1.00
22.15
N


ATOM
2536
CA
GLU
A
339
20.464
−9.750
54.352
1.00
22.84
C


ATOM
2537
CB
GLU
A
339
20.252
−9.699
55.868
1.00
22.87
C


ATOM
2538
CG
GLU
A
339
21.530
−9.890
56.681
1.00
23.77
C


ATOM
2539
CD
GLU
A
339
21.344
−9.598
58.163
1.00
24.29
C


ATOM
2540
OE1
GLU
A
339
20.214
−9.255
58.576
1.00
25.96
O


ATOM
2541
OE2
GLU
A
339
22.335
−9.711
58.916
1.00
26.34
O


ATOM
2542
C
GLU
A
339
19.121
−9.827
53.623
1.00
22.88
C


ATOM
2543
O
GLU
A
339
18.331
−10.747
53.853
1.00
22.86
O


ATOM
2544
N
ASN
A
340
18.874
−8.863
52.737
1.00
23.02
N


ATOM
2545
CA
ASN
A
340
17.625
−8.805
51.981
1.00
23.34
C


ATOM
2546
CB
ASN
A
340
16.726
−7.697
52.534
1.00
23.20
C


ATOM
2547
CG
ASN
A
340
16.119
−8.058
53.871
1.00
23.34
C


ATOM
2548
OD1
ASN
A
340
15.099
−8.743
53.937
1.00
23.26
O


ATOM
2549
ND2
ASN
A
340
16.740
−7.592
54.947
1.00
23.23
N


ATOM
2550
C
ASN
A
340
17.848
−8.609
50.476
1.00
23.61
C


ATOM
2551
O
ASN
A
340
17.505
−7.561
49.932
1.00
23.68
O


ATOM
2552
N
PRO
A
341
18.393
−9.638
49.793
1.00
23.96
N


ATOM
2553
CA
PRO
A
341
18.789
−9.499
48.385
1.00
24.26
C


ATOM
2554
CB
PRO
A
341
19.495
−10.831
48.079
1.00
24.37
C


ATOM
2555
CG
PRO
A
341
19.729
−11.481
49.405
1.00
24.14
C


ATOM
2556
CD
PRO
A
341
18.644
−11.000
50.293
1.00
24.07
C


ATOM
2557
C
PRO
A
341
17.606
−9.303
47.434
1.00
24.55
C


ATOM
2558
O
PRO
A
341
17.805
−8.904
46.285
1.00
24.53
O


ATOM
2559
N
GLN
A
342
16.391
−9.579
47.908
1.00
24.80
N


ATOM
2560
CA
GLN
A
342
15.183
−9.423
47.088
1.00
25.20
C


ATOM
2561
CB
GLN
A
342
13.965
−10.078
47.765
1.00
25.05
C


ATOM
2562
CG
GLN
A
342
13.384
−9.299
48.951
1.00
24.88
C


ATOM
2563
CD
GLN
A
342
14.148
−9.518
50.249
1.00
24.52
C


ATOM
2564
OE1
GLN
A
342
15.103
−10.293
50.303
1.00
24.25
O


ATOM
2565
NE2
GLN
A
342
13.721
−8.834
51.305
1.00
24.79
N


ATOM
2566
C
GLN
A
342
14.890
−7.956
46.744
1.00
25.48
C


ATOM
2567
O
GLN
A
342
14.076
−7.667
45.863
1.00
25.68
O


ATOM
2568
N
VAL
A
343
15.562
−7.041
47.443
1.00
25.92
N


ATOM
2569
CA
VAL
A
343
15.441
−5.609
47.168
1.00
26.34
C


ATOM
2570
CB
VAL
A
343
16.042
−4.745
48.326
1.00
26.42
C


ATOM
2571
CG1
VAL
A
343
17.565
−4.833
48.350
1.00
26.98
C


ATOM
2572
CG2
VAL
A
343
15.586
−3.295
48.215
1.00
27.06
C


ATOM
2573
C
VAL
A
343
16.067
−5.234
45.812
1.00
26.36
C


ATOM
2574
O
VAL
A
343
15.667
−4.247
45.190
1.00
26.27
O


ATOM
2575
N
ARG
A
344
17.033
−6.039
45.359
1.00
26.53
N


ATOM
2576
CA
ARG
A
344
17.685
−5.828
44.061
1.00
26.68
C


ATOM
2577
CB
ARG
A
344
18.747
−6.898
43.799
1.00
26.58
C


ATOM
2578
CG
ARG
A
344
19.907
−6.937
44.775
1.00
25.81
C


ATOM
2579
CD
ARG
A
344
20.955
−7.901
44.248
1.00
25.10
C


ATOM
2580
NE
ARG
A
344
22.003
−8.234
45.211
1.00
24.01
N


ATOM
2581
CZ
ARG
A
344
23.089
−7.498
45.430
1.00
23.61
C


ATOM
2582
NH1
ARG
A
344
23.266
−6.349
44.788
1.00
22.91
N


ATOM
2583
NH2
ARG
A
344
23.992
−7.903
46.309
1.00
23.37
N


ATOM
2584
C
ARG
A
344
16.669
−5.855
42.925
1.00
27.18
C


ATOM
2585
O
ARG
A
344
16.601
−4.925
42.124
1.00
27.16
O


ATOM
2586
N
GLU
A
345
15.885
−6.932
42.865
1.00
27.64
N


ATOM
2587
CA
GLU
A
345
14.881
−7.112
41.816
1.00
28.28
C


ATOM
2588
CB
GLU
A
345
14.278
−8.520
41.888
1.00
28.23
C


ATOM
2589
CG
GLU
A
345
13.704
−9.028
40.566
1.00
29.12
C


ATOM
2590
CD
GLU
A
345
13.217
−10.468
40.644
1.00
29.33
C


ATOM
2591
OE1
GLU
A
345
12.445
−10.795
41.572
1.00
30.44
O


ATOM
2592
OE2
GLU
A
345
13.597
−11.272
39.764
1.00
30.80
O


ATOM
2593
C
GLU
A
345
13.782
−6.053
41.912
1.00
28.27
C


ATOM
2594
O
GLU
A
345
13.224
−5.633
40.895
1.00
28.35
O


ATOM
2595
N
LYS
A
346
13.487
−5.625
43.139
1.00
28.49
N


ATOM
2596
CA
LYS
A
346
12.507
−4.567
43.389
1.00
28.78
C


ATOM
2597
CB
LYS
A
346
12.329
−4.339
44.889
1.00
28.82
C


ATOM
2598
CG
LYS
A
346
11.361
−5.282
45.567
1.00
29.10
C


ATOM
2599
CD
LYS
A
346
10.968
−4.726
46.923
1.00
29.38
C


ATOM
2600
CE
LYS
A
346
10.105
−5.689
47.705
1.00
29.35
C


ATOM
2601
NZ
LYS
A
346
9.740
−5.118
49.030
1.00
29.35
N


ATOM
2602
C
LYS
A
346
12.885
−3.248
42.714
1.00
28.92
C


ATOM
2603
O
LYS
A
346
12.077
−2.669
41.983
1.00
29.04
O


ATOM
2604
N
VAL
A
347
14.109
−2.777
42.963
1.00
29.06
N


ATOM
2605
CA
VAL
A
347
14.558
−1.482
42.429
1.00
29.09
C


ATOM
2606
CB
VAL
A
347
15.819
−0.919
43.164
1.00
29.02
C


ATOM
2607
CG1
VAL
A
347
15.500
−0.610
44.622
1.00
28.88
C


ATOM
2608
CG2
VAL
A
347
17.006
−1.876
43.051
1.00
28.85
C


ATOM
2609
C
VAL
A
347
14.777
−1.497
40.913
1.00
29.27
C


ATOM
2610
O
VAL
A
347
14.626
−0.468
40.254
1.00
29.25
O


ATOM
2611
N
VAL
A
348
15.125
−2.665
40.371
1.00
29.53
N


ATOM
2612
CA
VAL
A
348
15.235
−2.845
38.921
1.00
29.89
C


ATOM
2613
CB
VAL
A
348
15.838
−4.232
38.549
1.00
29.85
C


ATOM
2614
CG1
VAL
A
348
15.738
−4.489
37.046
1.00
29.65
C


ATOM
2615
CG2
VAL
A
348
17.282
−4.322
38.996
1.00
29.77
C


ATOM
2616
C
VAL
A
348
13.860
−2.688
38.277
1.00
30.26
C


ATOM
2617
O
VAL
A
348
13.722
−2.039
37.236
1.00
30.33
O


ATOM
2618
N
ALA
A
349
12.846
−3.266
38.921
1.00
30.72
N


ATOM
2619
CA
ALA
A
349
11.467
−3.192
38.442
1.00
31.16
C


ATOM
2620
CB
ALA
A
349
10.576
−4.123
39.247
1.00
31.09
C


ATOM
2621
C
ALA
A
349
10.915
−1.763
38.462
1.00
31.47
C


ATOM
2622
O
ALA
A
349
10.070
−1.413
37.637
1.00
31.59
O


ATOM
2623
N
ILE
A
350
11.398
−0.946
39.401
1.00
31.91
N


ATOM
2624
CA
ILE
A
350
11.031
0.475
39.466
1.00
32.31
C


ATOM
2625
CB
ILE
A
350
11.716
1.201
40.665
1.00
32.32
C


ATOM
2626
CG1
ILE
A
350
11.229
0.628
42.001
1.00
32.31
C


ATOM
2627
CD1
ILE
A
350
12.027
1.107
43.213
1.00
32.35
C


ATOM
2628
CG2
ILE
A
350
11.467
2.715
40.602
1.00
32.24
C


ATOM
2629
C
ILE
A
350
11.390
1.191
38.159
1.00
32.67
C


ATOM
2630
O
ILE
A
350
10.551
1.871
37.564
1.00
32.75
O


ATOM
2631
N
PHE
A
351
12.632
1.012
37.714
1.00
33.03
N


ATOM
2632
CA
PHE
A
351
13.145
1.701
36.531
1.00
33.41
C


ATOM
2633
CB
PHE
A
351
14.626
2.051
36.719
1.00
33.32
C


ATOM
2634
CG
PHE
A
351
14.895
2.945
37.899
1.00
33.07
C


ATOM
2635
CD1
PHE
A
351
15.278
2.406
39.124
1.00
32.93
C


ATOM
2636
CE1
PHE
A
351
15.528
3.228
40.220
1.00
32.82
C


ATOM
2637
CZ
PHE
A
351
15.400
4.608
40.095
1.00
32.92
C


ATOM
2638
CE2
PHE
A
351
15.020
5.159
38.875
1.00
32.86
C


ATOM
2639
CD2
PHE
A
351
14.771
4.328
37.785
1.00
32.98
C


ATOM
2640
C
PHE
A
351
12.950
0.893
35.243
1.00
33.83
C


ATOM
2641
O
PHE
A
351
13.425
1.293
34.174
1.00
33.89
O


ATOM
2642
N
ALA
A
352
12.246
−0.234
35.350
1.00
34.24
N


ATOM
2643
CA
ALA
A
352
12.010
−1.121
34.207
1.00
34.71
C


ATOM
2644
CB
ALA
A
352
11.557
−2.494
34.683
1.00
34.69
C


ATOM
2645
C
ALA
A
352
11.006
−0.542
33.210
1.00
35.05
C


ATOM
2646
O
ALA
A
352
11.147
−0.731
31.999
1.00
35.20
O


ATOM
2647
N
GLU
A
353
9.995
0.158
33.723
1.00
35.41
N


ATOM
2648
CA
GLU
A
353
8.970
0.771
32.874
1.00
35.75
C


ATOM
2649
CB
GLU
A
353
7.565
0.356
33.328
1.00
35.76
C


ATOM
2650
CG
GLU
A
353
7.194
0.809
34.737
1.00
36.09
C


ATOM
2651
CD
GLU
A
353
5.802
0.359
35.162
1.00
36.25
C


ATOM
2652
OE1
GLU
A
353
5.350
−0.716
34.706
1.00
36.77
O


ATOM
2653
OE2
GLU
A
353
5.162
1.081
35.962
1.00
36.88
O


ATOM
2654
C
GLU
A
353
9.094
2.295
32.836
1.00
35.78
C


ATOM
2655
O
GLU
A
353
9.601
2.914
33.774
1.00
35.89
O


ATOM
2656
N
SER
A
360
6.060
15.154
24.340
1.00
32.56
N


ATOM
2657
CA
SER
A
360
5.465
16.221
23.542
1.00
32.43
C


ATOM
2658
CB
SER
A
360
5.969
17.591
24.014
1.00
32.58
C


ATOM
2659
OG
SER
A
360
7.353
17.758
23.745
1.00
33.06
O


ATOM
2660
C
SER
A
360
5.759
16.028
22.054
1.00
32.11
C


ATOM
2661
O
SER
A
360
6.662
15.270
21.687
1.00
32.26
O


ATOM
2662
N
ASP
A
361
4.994
16.716
21.205
1.00
31.62
N


ATOM
2663
CA
ASP
A
361
5.202
16.656
19.754
1.00
31.02
C


ATOM
2664
CB
ASP
A
361
3.885
16.912
18.991
1.00
31.38
C


ATOM
2665
CG
ASP
A
361
3.271
18.285
19.292
1.00
32.23
C


ATOM
2666
OD1
ASP
A
361
3.942
19.142
19.908
1.00
33.51
O


ATOM
2667
OD2
ASP
A
361
2.104
18.504
18.900
1.00
33.69
O


ATOM
2668
C
ASP
A
361
6.313
17.603
19.279
1.00
30.18
C


ATOM
2669
O
ASP
A
361
6.628
17.658
18.087
1.00
30.33
O


ATOM
2670
N
ASN
A
362
6.897
18.341
20.222
1.00
28.99
N


ATOM
2671
CA
ASN
A
362
8.000
19.251
19.932
1.00
27.83
C


ATOM
2672
CB
ASN
A
362
8.117
20.313
21.037
1.00
27.87
C


ATOM
2673
CG
ASN
A
362
9.012
21.489
20.644
1.00
27.95
C


ATOM
2674
OD1
ASN
A
362
9.058
22.502
21.346
1.00
28.45
O


ATOM
2675
ND2
ASN
A
362
9.725
21.359
19.531
1.00
27.22
N


ATOM
2676
C
ASN
A
362
9.314
18.488
19.779
1.00
26.96
C


ATOM
2677
O
ASN
A
362
9.862
17.972
20.759
1.00
26.68
O


ATOM
2678
N
VAL
A
363
9.813
18.424
18.544
1.00
26.03
N


ATOM
2679
CA
VAL
A
363
11.051
17.701
18.236
1.00
25.16
C


ATOM
2680
CB
VAL
A
363
11.306
17.615
16.695
1.00
25.24
C


ATOM
2681
CG1
VAL
A
363
11.676
18.981
16.113
1.00
25.06
C


ATOM
2682
CG2
VAL
A
363
12.374
16.570
16.373
1.00
25.10
C


ATOM
2683
C
VAL
A
363
12.275
18.267
18.987
1.00
24.68
C


ATOM
2684
O
VAL
A
363
13.224
17.534
19.273
1.00
24.22
O


ATOM
2685
N
ASP
A
364
12.231
19.560
19.322
1.00
24.39
N


ATOM
2686
CA
ASP
A
364
13.261
20.185
20.171
1.00
24.11
C


ATOM
2687
CB
ASP
A
364
12.939
21.664
20.431
1.00
24.20
C


ATOM
2688
CG
ASP
A
364
13.269
22.568
19.244
1.00
24.94
C


ATOM
2689
OD1
ASP
A
364
13.819
22.081
18.234
1.00
25.45
O


ATOM
2690
OD2
ASP
A
364
12.974
23.781
19.334
1.00
26.26
O


ATOM
2691
C
ASP
A
364
13.417
19.465
21.515
1.00
23.85
C


ATOM
2692
O
ASP
A
364
14.499
19.465
22.103
1.00
23.56
O


ATOM
2693
N
ALA
A
365
12.330
18.860
21.994
1.00
23.43
N


ATOM
2694
CA
ALA
A
365
12.309
18.225
23.315
1.00
23.50
C


ATOM
2695
CB
ALA
A
365
10.956
18.461
23.987
1.00
23.51
C


ATOM
2696
C
ALA
A
365
12.628
16.726
23.266
1.00
23.38
C


ATOM
2697
O
ALA
A
365
12.537
16.032
24.285
1.00
23.47
O


ATOM
2698
N
GLN
A
366
13.032
16.240
22.096
1.00
23.35
N


ATOM
2699
CA
GLN
A
366
13.083
14.797
21.843
1.00
23.43
C


ATOM
2700
CB
GLN
A
366
12.219
14.445
20.627
1.00
23.36
C


ATOM
2701
CG
GLN
A
366
10.728
14.667
20.850
1.00
23.86
C


ATOM
2702
CD
GLN
A
366
9.879
14.294
19.645
1.00
24.06
C


ATOM
2703
OE1
GLN
A
366
10.393
13.879
18.606
1.00
25.85
O


ATOM
2704
NE2
GLN
A
366
8.569
14.444
19.783
1.00
25.43
N


ATOM
2705
C
GLN
A
366
14.491
14.206
21.688
1.00
23.42
C


ATOM
2706
O
GLN
A
366
14.654
13.128
21.113
1.00
23.21
O


ATOM
2707
N
LEU
A
367
15.498
14.895
22.222
1.00
23.58
N


ATOM
2708
CA
LEU
A
367
16.881
14.404
22.166
1.00
24.10
C


ATOM
2709
CB
LEU
A
367
17.829
15.346
22.931
1.00
23.96
C


ATOM
2710
CG
LEU
A
367
19.261
14.883
23.241
1.00
24.42
C


ATOM
2711
CD1
LEU
A
367
20.063
14.620
21.968
1.00
24.95
C


ATOM
2712
CD2
LEU
A
367
19.966
15.906
24.117
1.00
24.42
C


ATOM
2713
C
LEU
A
367
17.017
12.970
22.687
1.00
24.30
C


ATOM
2714
O
LEU
A
367
17.688
12.141
22.071
1.00
24.28
O


ATOM
2715
N
TYR
A
368
16.368
12.680
23.811
1.00
24.76
N


ATOM
2716
CA
TYR
A
368
16.534
11.386
24.473
1.00
25.35
C


ATOM
2717
CB
TYR
A
368
16.648
11.566
25.992
1.00
25.31
C


ATOM
2718
CG
TYR
A
368
17.858
12.381
26.399
1.00
25.37
C


ATOM
2719
CD1
TYR
A
368
19.149
11.891
26.200
1.00
25.28
C


ATOM
2720
CE1
TYR
A
368
20.265
12.635
26.558
1.00
25.61
C


ATOM
2721
CZ
TYR
A
368
20.101
13.885
27.122
1.00
25.52
C


ATOM
2722
OH
TYR
A
368
21.213
14.612
27.471
1.00
25.76
O


ATOM
2723
CE2
TYR
A
368
18.832
14.403
27.329
1.00
25.45
C


ATOM
2724
CD2
TYR
A
368
17.715
13.648
26.965
1.00
25.44
C


ATOM
2725
C
TYR
A
368
15.460
10.358
24.099
1.00
25.91
C


ATOM
2726
O
TYR
A
368
15.259
9.367
24.810
1.00
25.82
O


ATOM
2727
N
ASN
A
369
14.798
10.586
22.964
1.00
26.66
N


ATOM
2728
CA
ASN
A
369
13.861
9.611
22.401
1.00
27.46
C


ATOM
2729
CB
ASN
A
369
12.909
10.286
21.407
1.00
27.69
C


ATOM
2730
CG
ASN
A
369
11.733
10.963
22.086
1.00
28.32
C


ATOM
2731
OD1
ASN
A
369
11.880
11.608
23.126
1.00
29.94
O


ATOM
2732
ND2
ASN
A
369
10.553
10.826
21.491
1.00
29.53
N


ATOM
2733
C
ASN
A
369
14.573
8.433
21.731
1.00
27.79
C


ATOM
2734
O
ASN
A
369
13.940
7.614
21.058
1.00
28.22
O


ATOM
2735
N
GLY
A
370
15.889
8.356
21.918
1.00
28.11
N


ATOM
2736
CA
GLY
A
370
16.687
7.257
21.384
1.00
28.39
C


ATOM
2737
C
GLY
A
370
17.938
7.717
20.663
1.00
28.56
C


ATOM
2738
O
GLY
A
370
18.032
8.869
20.223
1.00
28.71
O


ATOM
2739
N
PHE
A
371
18.907
6.812
20.546
1.00
28.68
N


ATOM
2740
CA
PHE
A
371
20.119
7.072
19.777
1.00
28.78
C


ATOM
2741
CB
PHE
A
371
21.259
6.156
20.236
1.00
28.92
C


ATOM
2742
CG
PHE
A
371
21.633
6.323
21.683
1.00
29.24
C


ATOM
2743
CD1
PHE
A
371
22.419
7.398
22.095
1.00
29.38
C


ATOM
2744
CE1
PHE
A
371
22.773
7.552
23.437
1.00
29.62
C


ATOM
2745
CZ
PHE
A
371
22.344
6.621
24.380
1.00
29.79
C


ATOM
2746
CE2
PHE
A
371
21.563
5.540
23.979
1.00
29.99
C


ATOM
2747
CD2
PHE
A
371
21.214
5.395
22.634
1.00
29.62
C


ATOM
2748
C
PHE
A
371
19.860
6.860
18.292
1.00
28.64
C


ATOM
2749
O
PHE
A
371
19.043
6.018
17.907
1.00
28.78
O


ATOM
2750
N
PHE
A
372
20.557
7.628
17.460
1.00
28.49
N


ATOM
2751
CA
PHE
A
372
20.476
7.460
16.012
1.00
28.23
C


ATOM
2752
CB
PHE
A
372
20.894
8.745
15.292
1.00
28.15
C


ATOM
2753
CG
PHE
A
372
19.963
9.902
15.523
1.00
28.16
C


ATOM
2754
CD1
PHE
A
372
18.734
9.968
14.869
1.00
28.01
C


ATOM
2755
CE1
PHE
A
372
17.868
11.042
15.082
1.00
28.19
C


ATOM
2756
CZ
PHE
A
372
18.234
12.065
15.948
1.00
27.90
C


ATOM
2757
CE2
PHE
A
372
19.458
12.013
16.600
1.00
28.03
C


ATOM
2758
CD2
PHE
A
372
20.317
10.934
16.385
1.00
28.06
C


ATOM
2759
C
PHE
A
372
21.348
6.295
15.556
1.00
28.16
C


ATOM
2760
O
PHE
A
372
22.398
6.024
16.144
1.00
28.05
O


ATOM
2761
N
SER
A
373
20.905
5.608
14.506
1.00
28.17
N


ATOM
2762
CA
SER
A
373
21.667
4.503
13.928
1.00
28.13
C


ATOM
2763
CB
SER
A
373
20.780
3.672
12.995
1.00
28.09
C


ATOM
2764
OG
SER
A
373
20.357
4.433
11.876
1.00
28.16
O


ATOM
2765
C
SER
A
373
22.893
5.018
13.175
1.00
28.18
C


ATOM
2766
O
SER
A
373
23.011
6.218
12.908
1.00
28.07
O


ATOM
2767
N
ASP
A
374
23.804
4.105
12.841
1.00
28.21
N


ATOM
2768
CA
ASP
A
374
24.992
4.435
12.051
1.00
28.34
C


ATOM
2769
CB
ASP
A
374
25.867
3.192
11.847
1.00
28.51
C


ATOM
2770
CG
ASP
A
374
26.381
2.607
13.158
1.00
29.17
C


ATOM
2771
OD1
ASP
A
374
26.168
3.223
14.225
1.00
30.24
O


ATOM
2772
OD2
ASP
A
374
27.004
1.525
13.115
1.00
30.06
O


ATOM
2773
C
ASP
A
374
24.610
5.026
10.694
1.00
28.13
C


ATOM
2774
O
ASP
A
374
25.230
5.986
10.229
1.00
28.04
O


ATOM
2775
N
ALA
A
375
23.584
4.446
10.072
1.00
28.00
N


ATOM
2776
CA
ALA
A
375
23.096
4.903
8.771
1.00
27.78
C


ATOM
2777
CB
ALA
A
375
22.075
3.923
8.211
1.00
27.83
C


ATOM
2778
C
ALA
A
375
22.504
6.308
8.852
1.00
27.63
C


ATOM
2779
O
ALA
A
375
22.754
7.144
7.980
1.00
27.65
O


ATOM
2780
N
ASP
A
376
21.724
6.562
9.902
1.00
27.44
N


ATOM
2781
CA
ASP
A
376
21.133
7.883
10.122
1.00
27.26
C


ATOM
2782
CB
ASP
A
376
20.071
7.834
11.225
1.00
27.23
C


ATOM
2783
CG
ASP
A
376
18.683
7.504
10.691
1.00
27.44
C


ATOM
2784
OD1
ASP
A
376
18.487
7.517
9.454
1.00
27.54
O


ATOM
2785
OD2
ASP
A
376
17.781
7.242
11.512
1.00
27.38
O


ATOM
2786
C
ASP
A
376
22.182
8.946
10.436
1.00
27.06
C


ATOM
2787
O
ASP
A
376
22.063
10.086
9.989
1.00
26.87
O


ATOM
2788
N
ARG
A
377
23.205
8.567
11.202
1.00
26.93
N


ATOM
2789
CA
ARG
A
377
24.315
9.473
11.508
1.00
26.92
C


ATOM
2790
CB
ARG
A
377
25.228
8.878
12.592
1.00
27.11
C


ATOM
2791
CG
ARG
A
377
26.452
9.740
12.973
1.00
28.22
C


ATOM
2792
CD
ARG
A
377
26.082
11.190
13.314
1.00
29.90
C


ATOM
2793
NE
ARG
A
377
25.125
11.283
14.417
1.00
30.87
N


ATOM
2794
CZ
ARG
A
377
24.338
12.332
14.641
1.00
31.14
C


ATOM
2795
NH1
ARG
A
377
24.377
13.386
13.835
1.00
31.29
N


ATOM
2796
NH2
ARG
A
377
23.499
12.323
15.668
1.00
31.65
N


ATOM
2797
C
ARG
A
377
25.110
9.827
10.250
1.00
26.68
C


ATOM
2798
O
ARG
A
377
25.522
10.975
10.072
1.00
26.61
O


ATOM
2799
N
ALA
A
378
25.308
8.838
9.378
1.00
26.43
N


ATOM
2800
CA
ALA
A
378
25.990
9.052
8.103
1.00
26.33
C


ATOM
2801
CB
ALA
A
378
26.243
7.722
7.404
1.00
26.28
C


ATOM
2802
C
ALA
A
378
25.193
9.993
7.198
1.00
26.17
C


ATOM
2803
O
ALA
A
378
25.769
10.840
6.511
1.00
26.13
O


ATOM
2804
N
ALA
A
379
23.870
9.842
7.213
1.00
26.16
N


ATOM
2805
CA
ALA
A
379
22.975
10.688
6.422
1.00
26.13
C


ATOM
2806
CB
ALA
A
379
21.573
10.093
6.386
1.00
26.10
C


ATOM
2807
C
ALA
A
379
22.935
12.126
6.943
1.00
26.24
C


ATOM
2808
O
ALA
A
379
22.894
13.074
6.158
1.00
26.21
O


ATOM
2809
N
MET
A
380
22.945
12.280
8.267
1.00
26.32
N


ATOM
2810
CA
MET
A
380
22.957
13.608
8.888
1.00
26.67
C


ATOM
2811
CB
MET
A
380
22.642
13.516
10.389
1.00
26.57
C


ATOM
2812
CG
MET
A
380
21.196
13.107
10.693
1.00
26.96
C


ATOM
2813
SD
MET
A
380
20.810
13.016
12.455
1.00
28.29
S


ATOM
2814
CE
MET
A
380
19.994
14.578
12.728
1.00
29.37
C


ATOM
2815
C
MET
A
380
24.284
14.333
8.642
1.00
26.42
C


ATOM
2816
O
MET
A
380
24.323
15.562
8.570
1.00
26.41
O


ATOM
2817
N
LYS
A
381
25.362
13.561
8.498
1.00
26.41
N


ATOM
2818
CA
LYS
A
381
26.673
14.107
8.142
1.00
26.43
C


ATOM
2819
CB
LYS
A
381
27.755
13.027
8.263
1.00
26.44
C


ATOM
2820
CG
LYS
A
381
29.185
13.553
8.174
1.00
27.08
C


ATOM
2821
CD
LYS
A
381
30.198
12.449
8.439
1.00
27.35
C


ATOM
2822
CE
LYS
A
381
31.625
12.978
8.351
1.00
28.65
C


ATOM
2823
NZ
LYS
A
381
32.635
11.905
8.573
1.00
29.41
N


ATOM
2824
C
LYS
A
381
26.667
14.704
6.729
1.00
26.17
C


ATOM
2825
O
LYS
A
381
27.337
15.706
6.470
1.00
26.12
O


ATOM
2826
N
ILE
A
382
25.911
14.080
5.825
1.00
26.08
N


ATOM
2827
CA
ILE
A
382
25.738
14.606
4.468
1.00
26.02
C


ATOM
2828
CB
ILE
A
382
25.044
13.578
3.525
1.00
26.02
C


ATOM
2829
CG1
ILE
A
382
25.999
12.416
3.220
1.00
26.09
C


ATOM
2830
CD1
ILE
A
382
25.344
11.225
2.537
1.00
26.16
C


ATOM
2831
CG2
ILE
A
382
24.586
14.249
2.222
1.00
25.83
C


ATOM
2832
C
ILE
A
382
24.985
15.942
4.494
1.00
26.09
C


ATOM
2833
O
ILE
A
382
25.379
16.892
3.817
1.00
25.99
O


ATOM
2834
N
VAL
A
383
23.925
16.015
5.300
1.00
26.28
N


ATOM
2835
CA
VAL
A
383
23.202
17.275
5.526
1.00
26.60
C


ATOM
2836
CB
VAL
A
383
22.060
17.108
6.570
1.00
26.55
C


ATOM
2837
CG1
VAL
A
383
21.445
18.462
6.929
1.00
26.59
C


ATOM
2838
CG2
VAL
A
383
20.995
16.158
6.056
1.00
26.50
C


ATOM
2839
C
VAL
A
383
24.167
18.364
5.995
1.00
26.80
C


ATOM
2840
O
VAL
A
383
24.144
19.492
5.496
1.00
26.60
O


ATOM
2841
N
LEU
A
384
25.025
18.004
6.946
1.00
27.39
N


ATOM
2842
CA
LEU
A
384
25.989
18.927
7.528
1.00
28.05
C


ATOM
2843
CB
LEU
A
384
26.726
18.244
8.684
1.00
28.00
C


ATOM
2844
CG
LEU
A
384
27.578
19.102
9.615
1.00
28.19
C


ATOM
2845
CD1
LEU
A
384
26.710
20.077
10.398
1.00
28.31
C


ATOM
2846
CD2
LEU
A
384
28.363
18.202
10.553
1.00
28.11
C


ATOM
2847
C
LEU
A
384
26.993
19.447
6.496
1.00
28.58
C


ATOM
2848
O
LEU
A
384
27.352
20.628
6.509
1.00
28.62
O


ATOM
2849
N
GLU
A
385
27.434
18.564
5.601
1.00
29.30
N


ATOM
2850
CA
GLU
A
385
28.472
18.907
4.628
1.00
30.11
C


ATOM
2851
CB
GLU
A
385
29.430
17.726
4.424
1.00
30.16
C


ATOM
2852
CG
GLU
A
385
30.447
17.571
5.557
1.00
31.29
C


ATOM
2853
CD
GLU
A
385
31.052
16.177
5.644
1.00
32.28
C


ATOM
2854
OE1
GLU
A
385
31.035
15.441
4.636
1.00
33.18
O


ATOM
2855
OE2
GLU
A
385
31.554
15.820
6.728
1.00
33.47
O


ATOM
2856
C
GLU
A
385
27.913
19.419
3.291
1.00
30.40
C


ATOM
2857
O
GLU
A
385
28.671
19.840
2.415
1.00
30.53
O


ATOM
2858
N
THR
A
386
26.588
19.386
3.150
1.00
30.93
N


ATOM
2859
CA
THR
A
386
25.912
19.960
1.983
1.00
31.39
C


ATOM
2860
CB
THR
A
386
24.553
19.257
1.713
1.00
31.34
C


ATOM
2861
OG1
THR
A
386
24.767
17.853
1.523
1.00
30.95
O


ATOM
2862
CG2
THR
A
386
23.871
19.827
0.473
1.00
31.35
C


ATOM
2863
C
THR
A
386
25.686
21.461
2.183
1.00
31.90
C


ATOM
2864
O
THR
A
386
25.335
21.903
3.277
1.00
31.98
O


ATOM
2865
N
GLU
A
387
25.899
22.239
1.123
1.00
32.53
N


ATOM
2866
CA
GLU
A
387
25.625
23.676
1.154
1.00
33.12
C


ATOM
2867
CB
GLU
A
387
26.139
24.359
−0.122
1.00
33.31
C


ATOM
2868
CG
GLU
A
387
27.530
23.891
−0.565
1.00
34.06
C


ATOM
2869
CD
GLU
A
387
28.424
25.032
−1.013
1.00
35.29
C


ATOM
2870
OE1
GLU
A
387
28.701
25.933
−0.189
1.00
36.16
O


ATOM
2871
OE2
GLU
A
387
28.866
25.017
−2.181
1.00
35.88
O


ATOM
2872
C
GLU
A
387
24.121
23.918
1.333
1.00
33.40
C


ATOM
2873
O
GLU
A
387
23.308
23.226
0.720
1.00
33.41
O


ATOM
2874
N
PRO
A
388
23.749
24.890
2.197
1.00
33.68
N


ATOM
2875
CA
PRO
A
388
22.342
25.161
2.542
1.00
33.85
C


ATOM
2876
CB
PRO
A
388
22.424
26.474
3.325
1.00
33.91
C


ATOM
2877
CG
PRO
A
388
23.777
26.456
3.930
1.00
33.88
C


ATOM
2878
CD
PRO
A
388
24.668
25.791
2.920
1.00
33.73
C


ATOM
2879
C
PRO
A
388
21.412
25.318
1.333
1.00
34.05
C


ATOM
2880
O
PRO
A
388
20.248
24.918
1.399
1.00
34.14
O


ATOM
2881
N
ARG
A
389
21.926
25.890
0.243
1.00
34.14
N


ATOM
2882
CA
ARG
A
389
21.137
26.091
−0.979
1.00
34.28
C


ATOM
2883
CB
ARG
A
389
21.838
27.078
−1.926
1.00
34.29
C


ATOM
2884
CG
ARG
A
389
23.278
26.709
−2.278
1.00
34.69
C


ATOM
2885
CD
ARG
A
389
23.950
27.808
−3.086
1.00
35.21
C


ATOM
2886
NE
ARG
A
389
25.405
27.655
−3.111
1.00
36.56
N


ATOM
2887
CZ
ARG
A
389
26.075
26.948
−4.018
1.00
37.03
C


ATOM
2888
NH1
ARG
A
389
25.430
26.318
−4.994
1.00
37.57
N


ATOM
2889
NH2
ARG
A
389
27.398
26.873
−3.951
1.00
37.60
N


ATOM
2890
C
ARG
A
389
20.826
24.781
−1.712
1.00
34.05
C


ATOM
2891
O
ARG
A
389
19.870
24.711
−2.488
1.00
34.09
O


ATOM
2892
N
ASN
A
390
21.633
23.752
−1.458
1.00
33.80
N


ATOM
2893
CA
ASN
A
390
21.483
22.460
−2.133
1.00
33.57
C


ATOM
2894
CB
ASN
A
390
22.855
21.906
−2.541
1.00
33.55
C


ATOM
2895
CG
ASN
A
390
23.555
22.771
−3.582
1.00
33.68
C


ATOM
2896
OD1
ASN
A
390
22.913
23.505
−4.336
1.00
33.81
O


ATOM
2897
ND2
ASN
A
390
24.879
22.680
−3.630
1.00
33.82
N


ATOM
2898
C
ASN
A
390
20.704
21.420
−1.317
1.00
33.42
C


ATOM
2899
O
ASN
A
390
20.555
20.273
−1.743
1.00
33.34
O


ATOM
2900
N
LEU
A
391
20.200
21.831
−0.153
1.00
33.26
N


ATOM
2901
CA
LEU
A
391
19.431
20.936
0.719
1.00
33.09
C


ATOM
2902
CB
LEU
A
391
19.284
21.525
2.131
1.00
33.00
C


ATOM
2903
CG
LEU
A
391
20.515
21.489
3.045
1.00
32.79
C


ATOM
2904
CD1
LEU
A
391
20.262
22.291
4.313
1.00
32.24
C


ATOM
2905
CD2
LEU
A
391
20.921
20.054
3.387
1.00
32.47
C


ATOM
2906
C
LEU
A
391
18.056
20.514
0.160
1.00
33.13
C


ATOM
2907
O
LEU
A
391
17.671
19.353
0.308
1.00
33.18
O


ATOM
2908
N
PRO
A
392
17.311
21.450
−0.482
1.00
33.13
N


ATOM
2909
CA
PRO
A
392
15.982
21.081
−0.995
1.00
33.14
C


ATOM
2910
CB
PRO
A
392
15.471
22.386
−1.622
1.00
33.17
C


ATOM
2911
CG
PRO
A
392
16.277
23.460
−0.991
1.00
33.16
C


ATOM
2912
CD
PRO
A
392
17.620
22.865
−0.756
1.00
33.14
C


ATOM
2913
C
PRO
A
392
16.019
19.971
−2.050
1.00
33.14
C


ATOM
2914
O
PRO
A
392
15.075
19.185
−2.148
1.00
33.25
O


ATOM
2915
N
ALA
A
393
17.103
19.912
−2.824
1.00
33.05
N


ATOM
2916
CA
ALA
A
393
17.242
18.926
−3.897
1.00
33.01
C


ATOM
2917
CB
ALA
A
393
17.900
19.561
−5.117
1.00
33.04
C


ATOM
2918
C
ALA
A
393
18.017
17.679
−3.456
1.00
32.98
C


ATOM
2919
O
ALA
A
393
18.218
16.752
−4.247
1.00
33.01
O


ATOM
2920
N
LEU
A
394
18.439
17.658
−2.193
1.00
32.89
N


ATOM
2921
CA
LEU
A
394
19.246
16.561
−1.662
1.00
32.88
C


ATOM
2922
CB
LEU
A
394
19.795
16.922
−0.275
1.00
32.89
C


ATOM
2923
CG
LEU
A
394
20.937
16.084
0.309
1.00
32.90
C


ATOM
2924
CD1
LEU
A
394
22.191
16.156
−0.562
1.00
32.67
C


ATOM
2925
CD2
LEU
A
394
21.242
16.546
1.723
1.00
32.84
C


ATOM
2926
C
LEU
A
394
18.454
15.256
−1.607
1.00
32.91
C


ATOM
2927
O
LEU
A
394
17.362
15.200
−1.036
1.00
32.97
O


ATOM
2928
N
ASP
A
395
19.015
14.213
−2.213
1.00
32.90
N


ATOM
2929
CA
ASP
A
395
18.352
12.914
−2.305
1.00
32.91
C


ATOM
2930
CB
ASP
A
395
18.449
12.350
−3.736
1.00
33.07
C


ATOM
2931
CG
ASP
A
395
19.863
12.420
−4.311
1.00
33.85
C


ATOM
2932
OD1
ASP
A
395
20.491
13.503
−4.250
1.00
34.69
O


ATOM
2933
OD2
ASP
A
395
20.339
11.393
−4.844
1.00
34.84
O


ATOM
2934
C
ASP
A
395
18.890
11.914
−1.275
1.00
32.64
C


ATOM
2935
O
ASP
A
395
19.734
11.069
−1.588
1.00
32.73
O


ATOM
2936
N
ILE
A
396
18.402
12.031
−0.040
1.00
32.27
N


ATOM
2937
CA
ILE
A
396
18.761
11.101
1.039
1.00
31.92
C


ATOM
2938
CB
ILE
A
396
19.888
11.661
1.960
1.00
32.03
C


ATOM
2939
CG1
ILE
A
396
19.510
13.035
2.524
1.00
32.11
C


ATOM
2940
CD1
ILE
A
396
20.424
13.511
3.639
1.00
32.20
C


ATOM
2941
CG2
ILE
A
396
21.233
11.698
1.223
1.00
32.30
C


ATOM
2942
C
ILE
A
396
17.539
10.719
1.879
1.00
31.46
C


ATOM
2943
O
ILE
A
396
16.529
11.428
1.882
1.00
31.44
O


ATOM
2944
N
THR
A
397
17.641
9.595
2.586
1.00
30.85
N


ATOM
2945
CA
THR
A
397
16.527
9.057
3.365
1.00
30.33
C


ATOM
2946
CB
THR
A
397
16.032
7.708
2.771
1.00
30.35
C


ATOM
2947
OG1
THR
A
397
15.662
7.898
1.400
1.00
30.75
O


ATOM
2948
CG2
THR
A
397
14.826
7.170
3.541
1.00
30.65
C


ATOM
2949
C
THR
A
397
16.918
8.875
4.832
1.00
29.83
C


ATOM
2950
O
THR
A
397
18.070
8.559
5.144
1.00
29.69
O


ATOM
2951
N
PHE
A
398
15.953
9.093
5.724
1.00
29.24
N


ATOM
2952
CA
PHE
A
398
16.152
8.890
7.156
1.00
28.80
C


ATOM
2953
CB
PHE
A
398
15.952
10.202
7.920
1.00
28.77
C


ATOM
2954
CG
PHE
A
398
16.728
11.362
7.359
1.00
28.68
C


ATOM
2955
CD1
PHE
A
398
18.116
11.419
7.482
1.00
28.66
C


ATOM
2956
CE1
PHE
A
398
18.834
12.499
6.970
1.00
28.53
C


ATOM
2957
CZ
PHE
A
398
18.161
13.537
6.333
1.00
28.54
C


ATOM
2958
CE2
PHE
A
398
16.778
13.492
6.207
1.00
28.52
C


ATOM
2959
CD2
PHE
A
398
16.068
12.410
6.722
1.00
28.73
C


ATOM
2960
C
PHE
A
398
15.189
7.836
7.692
1.00
28.43
C


ATOM
2961
O
PHE
A
398
14.060
7.713
7.212
1.00
28.51
O


ATOM
2962
N
VAL
A
399
15.639
7.081
8.691
1.00
27.93
N


ATOM
2963
CA
VAL
A
399
14.789
6.095
9.356
1.00
27.51
C


ATOM
2964
CB
VAL
A
399
15.594
4.836
9.790
1.00
27.56
C


ATOM
2965
CG1
VAL
A
399
14.694
3.837
10.510
1.00
27.48
C


ATOM
2966
CG2
VAL
A
399
16.256
4.180
8.579
1.00
27.62
C


ATOM
2967
C
VAL
A
399
14.085
6.725
10.562
1.00
27.14
C


ATOM
2968
O
VAL
A
399
12.860
6.643
10.687
1.00
27.16
O


ATOM
2969
N
ASP
A
400
14.869
7.362
11.434
1.00
26.60
N


ATOM
2970
CA
ASP
A
400
14.344
8.027
12.627
1.00
26.12
C


ATOM
2971
CB
ASP
A
400
15.499
8.546
13.494
1.00
26.07
C


ATOM
2972
CG
ASP
A
400
15.071
8.866
14.916
1.00
25.68
C


ATOM
2973
OD1
ASP
A
400
14.322
9.844
15.111
1.00
24.98
O


ATOM
2974
OD2
ASP
A
400
15.504
8.150
15.845
1.00
25.50
O


ATOM
2975
C
ASP
A
400
13.403
9.173
12.249
1.00
25.99
C


ATOM
2976
O
ASP
A
400
13.758
10.043
11.449
1.00
25.75
O


ATOM
2977
N
LYS
A
401
12.209
9.166
12.842
1.00
25.84
N


ATOM
2978
CA
LYS
A
401
11.140
10.111
12.494
1.00
25.89
C


ATOM
2979
CB
LYS
A
401
9.806
9.650
13.094
1.00
26.10
C


ATOM
2980
CG
LYS
A
401
9.119
8.529
12.318
1.00
27.10
C


ATOM
2981
CD
LYS
A
401
8.119
9.070
11.296
1.00
28.84
C


ATOM
2982
CE
LYS
A
401
6.795
9.460
11.957
1.00
29.73
C


ATOM
2983
NZ
LYS
A
401
5.721
9.739
10.960
1.00
30.42
N


ATOM
2984
C
LYS
A
401
11.425
11.556
12.912
1.00
25.59
C


ATOM
2985
O
LYS
A
401
10.795
12.488
12.406
1.00
25.69
O


ATOM
2986
N
ARG
A
402
12.369
11.735
13.833
1.00
25.23
N


ATOM
2987
CA
ARG
A
402
12.731
13.070
14.322
1.00
24.90
C


ATOM
2988
CB
ARG
A
402
13.626
12.967
15.559
1.00
24.85
C


ATOM
2989
CG
ARG
A
402
12.933
12.426
16.804
1.00
24.34
C


ATOM
2990
CD
ARG
A
402
13.935
12.169
17.923
1.00
24.35
C


ATOM
2991
NE
ARG
A
402
14.868
11.091
17.593
1.00
23.14
N


ATOM
2992
CZ
ARG
A
402
15.897
10.724
18.355
1.00
23.18
C


ATOM
2993
NH1
ARG
A
402
16.144
11.350
19.500
1.00
22.48
N


ATOM
2994
NH2
ARG
A
402
16.686
9.732
17.968
1.00
23.20
N


ATOM
2995
C
ARG
A
402
13.434
13.914
13.261
1.00
25.03
C


ATOM
2996
O
ARG
A
402
13.277
15.138
13.233
1.00
25.02
O


ATOM
2997
N
ILE
A
403
14.202
13.257
12.392
1.00
25.12
N


ATOM
2998
CA
ILE
A
403
15.139
13.957
11.504
1.00
25.22
C


ATOM
2999
CB
ILE
A
403
16.121
12.984
10.796
1.00
25.16
C


ATOM
3000
CG1
ILE
A
403
16.822
12.092
11.829
1.00
25.47
C


ATOM
3001
CD1
ILE
A
403
17.636
10.951
11.234
1.00
25.14
C


ATOM
3002
CG2
ILE
A
403
17.151
13.773
9.983
1.00
25.08
C


ATOM
3003
C
ILE
A
403
14.448
14.878
10.487
1.00
25.43
C


ATOM
3004
O
ILE
A
403
14.899
16.003
10.262
1.00
25.44
O


ATOM
3005
N
GLU
A
404
13.358
14.400
9.889
1.00
25.70
N


ATOM
3006
CA
GLU
A
404
12.561
15.211
8.964
1.00
26.04
C


ATOM
3007
CB
GLU
A
404
11.339
14.430
8.465
1.00
26.36
C


ATOM
3008
CG
GLU
A
404
11.668
13.186
7.636
1.00
28.24
C


ATOM
3009
CD
GLU
A
404
11.785
11.916
8.472
1.00
30.17
C


ATOM
3010
OE1
GLU
A
404
11.889
12.014
9.716
1.00
31.41
O


ATOM
3011
OE2
GLU
A
404
11.766
10.812
7.879
1.00
31.34
O


ATOM
3012
C
GLU
A
404
12.114
16.519
9.623
1.00
25.73
C


ATOM
3013
O
GLU
A
404
12.182
17.587
9.012
1.00
25.68
O


ATOM
3014
N
LYS
A
405
11.667
16.418
10.874
1.00
25.31
N


ATOM
3015
CA
LYS
A
405
11.236
17.579
11.649
1.00
25.09
C


ATOM
3016
CB
LYS
A
405
10.519
17.138
12.927
1.00
25.34
C


ATOM
3017
CG
LYS
A
405
9.289
16.282
12.693
1.00
25.92
C


ATOM
3018
CD
LYS
A
405
8.734
15.764
14.007
1.00
26.97
C


ATOM
3019
CE
LYS
A
405
7.549
14.846
13.777
1.00
27.76
C


ATOM
3020
NZ
LYS
A
405
6.963
14.382
15.063
1.00
28.66
N


ATOM
3021
C
LYS
A
405
12.425
18.467
12.001
1.00
24.63
C


ATOM
3022
O
LYS
A
405
12.345
19.693
11.895
1.00
24.35
O


ATOM
3023
N
LEU
A
406
13.523
17.840
12.424
1.00
24.20
N


ATOM
3024
CA
LEU
A
406
14.759
18.561
12.725
1.00
23.99
C


ATOM
3025
CB
LEU
A
406
15.847
17.603
13.221
1.00
24.04
C


ATOM
3026
CG
LEU
A
406
15.716
17.022
14.633
1.00
24.13
C


ATOM
3027
CD1
LEU
A
406
16.721
15.897
14.837
1.00
24.41
C


ATOM
3028
CD2
LEU
A
406
15.891
18.097
15.701
1.00
24.39
C


ATOM
3029
C
LEU
A
406
15.265
19.323
11.508
1.00
23.82
C


ATOM
3030
O
LEU
A
406
15.735
20.452
11.631
1.00
23.88
O


ATOM
3031
N
LEU
A
407
15.151
18.702
10.334
1.00
23.66
N


ATOM
3032
CA
LEU
A
407
15.665
19.285
9.098
1.00
23.48
C


ATOM
3033
CB
LEU
A
407
15.693
18.244
7.970
1.00
23.48
C


ATOM
3034
CG
LEU
A
407
16.245
18.652
6.597
1.00
23.44
C


ATOM
3035
CD1
LEU
A
407
17.680
19.174
6.678
1.00
23.69
C


ATOM
3036
CD2
LEU
A
407
16.151
17.483
5.626
1.00
23.72
C


ATOM
3037
C
LEU
A
407
14.883
20.528
8.676
1.00
23.45
C


ATOM
3038
O
LEU
A
407
15.483
21.534
8.295
1.00
23.32
O


ATOM
3039
N
PHE
A
408
13.552
20.463
8.754
1.00
23.44
N


ATOM
3040
CA
PHE
A
408
12.722
21.625
8.428
1.00
23.61
C


ATOM
3041
CB
PHE
A
408
11.227
21.299
8.459
1.00
23.79
C


ATOM
3042
CG
PHE
A
408
10.351
22.500
8.213
1.00
24.34
C


ATOM
3043
CD1
PHE
A
408
10.211
23.024
6.926
1.00
24.69
C


ATOM
3044
CE1
PHE
A
408
9.421
24.146
6.695
1.00
25.46
C


ATOM
3045
CZ
PHE
A
408
8.768
24.764
7.755
1.00
25.45
C


ATOM
3046
CE2
PHE
A
408
8.904
24.259
9.042
1.00
25.49
C


ATOM
3047
CD2
PHE
A
408
9.698
23.133
9.267
1.00
24.99
C


ATOM
3048
C
PHE
A
408
13.015
22.808
9.348
1.00
23.50
C


ATOM
3049
O
PHE
A
408
13.247
23.921
8.873
1.00
23.58
O


ATOM
3050
N
ASN
A
409
12.996
22.561
10.659
1.00
23.47
N


ATOM
3051
CA
ASN
A
409
13.348
23.579
11.649
1.00
23.38
C


ATOM
3052
CB
ASN
A
409
13.283
23.000
13.065
1.00
23.45
C


ATOM
3053
CG
ASN
A
409
11.863
22.829
13.568
1.00
24.08
C


ATOM
3054
OD1
ASN
A
409
10.902
23.264
12.930
1.00
25.17
O


ATOM
3055
ND2
ASN
A
409
11.724
22.193
14.727
1.00
25.11
N


ATOM
3056
C
ASN
A
409
14.735
24.161
11.398
1.00
23.17
C


ATOM
3057
O
ASN
A
409
14.922
25.376
11.451
1.00
23.25
O


ATOM
3058
N
TYR
A
410
15.694
23.280
11.115
1.00
22.82
N


ATOM
3059
CA
TYR
A
410
17.077
23.666
10.825
1.00
22.69
C


ATOM
3060
CB
TYR
A
410
17.911
22.414
10.521
1.00
22.72
C


ATOM
3061
CG
TYR
A
410
19.363
22.658
10.155
1.00
22.89
C


ATOM
3062
CD1
TYR
A
410
20.302
23.008
11.129
1.00
22.39
C


ATOM
3063
CE1
TYR
A
410
21.641
23.214
10.798
1.00
22.91
C


ATOM
3064
CZ
TYR
A
410
22.057
23.053
9.485
1.00
22.99
C


ATOM
3065
OH
TYR
A
410
23.382
23.253
9.157
1.00
24.19
O


ATOM
3066
CE2
TYR
A
410
21.147
22.698
8.499
1.00
22.91
C


ATOM
3067
CD2
TYR
A
410
19.807
22.497
8.840
1.00
22.68
C


ATOM
3068
C
TYR
A
410
17.133
24.646
9.658
1.00
22.61
C


ATOM
3069
O
TYR
A
410
17.747
25.705
9.756
1.00
22.20
O


ATOM
3070
N
ARG
A
411
16.455
24.298
8.568
1.00
22.67
N


ATOM
3071
CA
ARG
A
411
16.416
25.144
7.381
1.00
22.90
C


ATOM
3072
CB
ARG
A
411
15.814
24.381
6.197
1.00
22.87
C


ATOM
3073
CG
ARG
A
411
16.669
23.217
5.711
1.00
23.06
C


ATOM
3074
CD
ARG
A
411
16.050
22.526
4.501
1.00
23.74
C


ATOM
3075
NE
ARG
A
411
15.922
23.438
3.365
1.00
25.83
N


ATOM
3076
CZ
ARG
A
411
14.769
23.784
2.797
1.00
27.04
C


ATOM
3077
NH1
ARG
A
411
13.621
23.281
3.234
1.00
27.76
N


ATOM
3078
NH2
ARG
A
411
14.766
24.631
1.779
1.00
27.44
N


ATOM
3079
C
ARG
A
411
15.650
26.445
7.623
1.00
22.98
C


ATOM
3080
O
ARG
A
411
16.107
27.516
7.236
1.00
23.23
O


ATOM
3081
N
ALA
A
412
14.493
26.344
8.274
1.00
23.00
N


ATOM
3082
CA
ALA
A
412
13.624
27.503
8.493
1.00
23.20
C


ATOM
3083
CB
ALA
A
412
12.244
27.056
8.938
1.00
23.26
C


ATOM
3084
C
ALA
A
412
14.206
28.520
9.481
1.00
23.39
C


ATOM
3085
O
ALA
A
412
14.024
29.725
9.312
1.00
23.34
O


ATOM
3086
N
ARG
A
413
14.901
28.027
10.506
1.00
23.67
N


ATOM
3087
CA
ARG
A
413
15.495
28.893
11.531
1.00
24.15
C


ATOM
3088
CB
ARG
A
413
15.727
28.111
12.826
1.00
23.96
C


ATOM
3089
CG
ARG
A
413
14.469
27.811
13.607
1.00
24.04
C


ATOM
3090
CD
ARG
A
413
14.776
26.932
14.804
1.00
23.45
C


ATOM
3091
NE
ARG
A
413
13.580
26.661
15.597
1.00
23.29
N


ATOM
3092
CZ
ARG
A
413
13.402
25.574
16.342
1.00
23.80
C


ATOM
3093
NH1
ARG
A
413
14.340
24.635
16.393
1.00
24.34
N


ATOM
3094
NH2
ARG
A
413
12.277
25.421
17.030
1.00
23.75
N


ATOM
3095
C
ARG
A
413
16.806
29.530
11.079
1.00
24.55
C


ATOM
3096
O
ARG
A
413
17.068
30.700
11.375
1.00
24.94
O


ATOM
3097
N
ASN
A
414
17.628
28.754
10.375
1.00
24.94
N


ATOM
3098
CA
ASN
A
414
18.976
29.187
10.003
1.00
25.44
C


ATOM
3099
CB
ASN
A
414
19.959
28.020
10.101
1.00
25.34
C


ATOM
3100
CG
ASN
A
414
20.127
27.520
11.518
1.00
25.48
C


ATOM
3101
OD1
ASN
A
414
19.707
26.415
11.851
1.00
26.75
O


ATOM
3102
ND2
ASN
A
414
20.735
28.335
12.363
1.00
24.95
N


ATOM
3103
C
ASN
A
414
19.060
29.806
8.617
1.00
25.77
C


ATOM
3104
O
ASN
A
414
19.779
30.787
8.414
1.00
25.93
O


ATOM
3105
N
PHE
A
415
18.334
29.223
7.664
1.00
26.20
N


ATOM
3106
CA
PHE
A
415
18.420
29.643
6.264
1.00
26.54
C


ATOM
3107
CB
PHE
A
415
19.195
28.600
5.444
1.00
26.66
C


ATOM
3108
CG
PHE
A
415
20.414
28.057
6.144
1.00
27.00
C


ATOM
3109
CD1
PHE
A
415
21.548
28.850
6.315
1.00
27.23
C


ATOM
3110
CE1
PHE
A
415
22.675
28.353
6.967
1.00
27.54
C


ATOM
3111
CZ
PHE
A
415
22.678
27.046
7.455
1.00
27.40
C


ATOM
3112
CE2
PHE
A
415
21.554
26.244
7.289
1.00
27.59
C


ATOM
3113
CD2
PHE
A
415
20.427
26.752
6.636
1.00
27.40
C


ATOM
3114
C
PHE
A
415
17.029
29.883
5.656
1.00
26.71
C


ATOM
3115
O
PHE
A
415
16.632
29.182
4.717
1.00
26.60
O


ATOM
3116
N
PRO
A
416
16.290
30.887
6.181
1.00
26.91
N


ATOM
3117
CA
PRO
A
416
14.900
31.119
5.761
1.00
26.95
C


ATOM
3118
CB
PRO
A
416
14.446
32.269
6.669
1.00
26.99
C


ATOM
3119
CG
PRO
A
416
15.701
32.954
7.068
1.00
27.10
C


ATOM
3120
CD
PRO
A
416
16.722
31.872
7.190
1.00
27.01
C


ATOM
3121
C
PRO
A
416
14.754
31.516
4.287
1.00
27.01
C


ATOM
3122
O
PRO
A
416
13.674
31.363
3.716
1.00
27.07
O


ATOM
3123
N
GLY
A
417
15.835
32.010
3.686
1.00
27.03
N


ATOM
3124
CA
GLY
A
417
15.832
32.404
2.275
1.00
26.99
C


ATOM
3125
C
GLY
A
417
15.814
31.232
1.307
1.00
26.96
C


ATOM
3126
O
GLY
A
417
15.642
31.419
0.097
1.00
27.15
O


ATOM
3127
N
THR
A
418
15.993
30.022
1.839
1.00
26.93
N


ATOM
3128
CA
THR
A
418
15.991
28.800
1.029
1.00
26.91
C


ATOM
3129
CB
THR
A
418
17.091
27.807
1.484
1.00
26.93
C


ATOM
3130
OG1
THR
A
418
16.789
27.320
2.797
1.00
26.88
O


ATOM
3131
CG2
THR
A
418
18.463
28.475
1.489
1.00
26.87
C


ATOM
3132
C
THR
A
418
14.631
28.089
1.046
1.00
26.81
C


ATOM
3133
O
THR
A
418
14.461
27.046
0.409
1.00
27.05
O


ATOM
3134
N
LEU
A
419
13.671
28.655
1.775
1.00
26.77
N


ATOM
3135
CA
LEU
A
419
12.323
28.090
1.856
1.00
26.69
C


ATOM
3136
CB
LEU
A
419
11.638
28.501
3.165
1.00
26.73
C


ATOM
3137
CG
LEU
A
419
12.333
28.262
4.510
1.00
26.68
C


ATOM
3138
CD1
LEU
A
419
11.499
28.866
5.626
1.00
27.10
C


ATOM
3139
CD2
LEU
A
419
12.585
26.779
4.767
1.00
26.83
C


ATOM
3140
C
LEU
A
419
11.463
28.543
0.682
1.00
26.67
C


ATOM
3141
O
LEU
A
419
11.508
29.712
0.289
1.00
26.75
O


ATOM
3142
N
ASP
A
420
10.675
27.621
0.129
1.00
26.66
N


ATOM
3143
CA
ASP
A
420
9.688
27.977
−0.897
1.00
26.64
C


ATOM
3144
CB
ASP
A
420
9.446
26.812
−1.880
1.00
26.99
C


ATOM
3145
CG
ASP
A
420
8.792
25.592
−1.226
1.00
27.60
C


ATOM
3146
OD1
ASP
A
420
8.213
25.714
−0.127
1.00
28.34
O


ATOM
3147
OD2
ASP
A
420
8.844
24.503
−1.838
1.00
29.00
O


ATOM
3148
C
ASP
A
420
8.386
28.468
−0.250
1.00
26.44
C


ATOM
3149
O
ASP
A
420
8.278
28.497
0.977
1.00
26.23
O


ATOM
3150
N
TYR
A
421
7.407
28.854
−1.069
1.00
26.26
N


ATOM
3151
CA
TYR
A
421
6.157
29.424
−0.552
1.00
26.15
C


ATOM
3152
CB
TYR
A
421
5.205
29.814
−1.690
1.00
26.02
C


ATOM
3153
CG
TYR
A
421
3.926
30.468
−1.203
1.00
26.01
C


ATOM
3154
CD1
TYR
A
421
3.890
31.828
−0.887
1.00
25.95
C


ATOM
3155
CE1
TYR
A
421
2.721
32.430
−0.429
1.00
25.88
C


ATOM
3156
CZ
TYR
A
421
1.571
31.668
−0.278
1.00
25.96
C


ATOM
3157
OH
TYR
A
421
0.410
32.256
0.173
1.00
26.24
O


ATOM
3158
CE2
TYR
A
421
1.581
30.316
−0.584
1.00
25.71
C


ATOM
3159
CD2
TYR
A
421
2.756
29.723
−1.041
1.00
25.85
C


ATOM
3160
C
TYR
A
421
5.448
28.501
0.441
1.00
26.30
C


ATOM
3161
O
TYR
A
421
5.021
28.944
1.511
1.00
26.11
O


ATOM
3162
N
ALA
A
422
5.328
27.223
0.081
1.00
26.38
N


ATOM
3163
CA
ALA
A
422
4.668
26.230
0.929
1.00
26.50
C


ATOM
3164
CB
ALA
A
422
4.560
24.895
0.204
1.00
26.50
C


ATOM
3165
C
ALA
A
422
5.387
26.060
2.268
1.00
26.59
C


ATOM
3166
O
ALA
A
422
4.743
25.950
3.313
1.00
26.66
O


ATOM
3167
N
GLU
A
423
6.720
26.047
2.225
1.00
26.74
N


ATOM
3168
CA
GLU
A
423
7.543
25.948
3.440
1.00
26.96
C


ATOM
3169
CB
GLU
A
423
9.001
25.635
3.086
1.00
27.01
C


ATOM
3170
CG
GLU
A
423
9.244
24.190
2.643
1.00
27.20
C


ATOM
3171
CD
GLU
A
423
10.597
23.988
1.970
1.00
27.41
C


ATOM
3172
OE1
GLU
A
423
11.132
24.955
1.388
1.00
27.82
O


ATOM
3173
OE2
GLU
A
423
11.118
22.853
2.012
1.00
27.85
O


ATOM
3174
C
GLU
A
423
7.462
27.219
4.286
1.00
27.00
C


ATOM
3175
O
GLU
A
423
7.503
27.156
5.520
1.00
26.93
O


ATOM
3176
N
GLN
A
424
7.346
28.367
3.618
1.00
27.08
N


ATOM
3177
CA
GLN
A
424
7.159
29.652
4.296
1.00
27.28
C


ATOM
3178
CB
GLN
A
424
7.221
30.808
3.291
1.00
27.26
C


ATOM
3179
CG
GLN
A
424
8.634
31.194
2.862
1.00
27.48
C


ATOM
3180
CD
GLN
A
424
8.654
32.162
1.686
1.00
28.08
C


ATOM
3181
OE1
GLN
A
424
7.618
32.692
1.279
1.00
28.92
O


ATOM
3182
NE2
GLN
A
424
9.839
32.390
1.131
1.00
29.26
N


ATOM
3183
C
GLN
A
424
5.839
29.696
5.066
1.00
27.30
C


ATOM
3184
O
GLN
A
424
5.775
30.247
6.166
1.00
27.24
O


ATOM
3185
N
GLN
A
425
4.793
29.114
4.481
1.00
27.36
N


ATOM
3186
CA
GLN
A
425
3.481
29.048
5.128
1.00
27.44
C


ATOM
3187
CB
GLN
A
425
2.389
28.685
4.116
1.00
27.51
C


ATOM
3188
CG
GLN
A
425
2.139
29.753
3.051
1.00
27.94
C


ATOM
3189
CD
GLN
A
425
1.797
31.113
3.642
1.00
28.66
C


ATOM
3190
OE1
GLN
A
425
2.521
32.087
3.442
1.00
29.19
O


ATOM
3191
NE2
GLN
A
425
0.692
31.181
4.379
1.00
29.28
N


ATOM
3192
C
GLN
A
425
3.475
28.067
6.298
1.00
27.51
C


ATOM
3193
O
GLN
A
425
2.792
28.293
7.299
1.00
27.41
O


ATOM
3194
N
ARG
A
426
4.239
26.983
6.164
1.00
27.53
N


ATOM
3195
CA
ARG
A
426
4.408
26.014
7.246
1.00
27.80
C


ATOM
3196
CB
ARG
A
426
5.198
24.790
6.763
1.00
27.86
C


ATOM
3197
CG
ARG
A
426
5.292
23.655
7.784
1.00
28.29
C


ATOM
3198
CD
ARG
A
426
6.118
22.486
7.259
1.00
28.56
C


ATOM
3199
NE
ARG
A
426
6.593
21.624
8.345
1.00
29.94
N


ATOM
3200
CZ
ARG
A
426
7.375
20.559
8.178
1.00
30.12
C


ATOM
3201
NH1
ARG
A
426
7.782
20.205
6.963
1.00
30.30
N


ATOM
3202
NH2
ARG
A
426
7.751
19.843
9.230
1.00
30.61
N


ATOM
3203
C
ARG
A
426
5.099
26.669
8.444
1.00
27.71
C


ATOM
3204
O
ARG
A
426
4.740
26.411
9.595
1.00
27.67
O


ATOM
3205
N
TRP
A
427
6.075
27.531
8.162
1.00
27.67
N


ATOM
3206
CA
TRP
A
427
6.793
28.248
9.213
1.00
27.78
C


ATOM
3207
CB
TRP
A
427
8.091
28.854
8.680
1.00
27.72
C


ATOM
3208
CG
TRP
A
427
8.970
29.396
9.767
1.00
27.64
C


ATOM
3209
CD1
TRP
A
427
9.319
30.700
9.965
1.00
27.83
C


ATOM
3210
NE1
TRP
A
427
10.131
30.811
11.070
1.00
27.75
N


ATOM
3211
CE2
TRP
A
427
10.313
29.568
11.615
1.00
27.64
C


ATOM
3212
CD2
TRP
A
427
9.591
28.649
10.821
1.00
27.94
C


ATOM
3213
CE3
TRP
A
427
9.610
27.291
11.169
1.00
27.75
C


ATOM
3214
CZ3
TRP
A
427
10.347
26.898
12.282
1.00
27.78
C


ATOM
3215
CH2
TRP
A
427
11.053
27.839
13.053
1.00
27.62
C


ATOM
3216
CZ2
TRP
A
427
11.050
29.173
12.735
1.00
27.48
C


ATOM
3217
C
TRP
A
427
5.936
29.325
9.875
1.00
28.06
C


ATOM
3218
O
TRP
A
427
6.022
29.531
11.086
1.00
27.94
O


ATOM
3219
N
LEU
A
428
5.117
30.011
9.078
1.00
28.34
N


ATOM
3220
CA
LEU
A
428
4.186
31.007
9.609
1.00
28.82
C


ATOM
3221
CB
LEU
A
428
3.427
31.708
8.477
1.00
28.88
C


ATOM
3222
CG
LEU
A
428
4.144
32.848
7.744
1.00
29.44
C


ATOM
3223
CD1
LEU
A
428
3.336
33.277
6.527
1.00
29.77
C


ATOM
3224
CD2
LEU
A
428
4.389
34.040
8.673
1.00
29.87
C


ATOM
3225
C
LEU
A
428
3.205
30.380
10.595
1.00
29.04
C


ATOM
3226
O
LEU
A
428
2.918
30.958
11.647
1.00
29.04
O


ATOM
3227
N
GLU
A
429
2.706
29.192
10.252
1.00
29.33
N


ATOM
3228
CA
GLU
A
429
1.798
28.447
11.123
1.00
29.77
C


ATOM
3229
CB
GLU
A
429
1.199
27.247
10.380
1.00
29.95
C


ATOM
3230
CG
GLU
A
429
0.032
26.575
11.106
1.00
31.05
C


ATOM
3231
CD
GLU
A
429
−1.092
27.545
11.440
1.00
32.27
C


ATOM
3232
OE1
GLU
A
429
−1.690
28.116
10.502
1.00
33.20
O


ATOM
3233
OE2
GLU
A
429
−1.377
27.732
12.642
1.00
33.24
O


ATOM
3234
C
GLU
A
429
2.505
27.987
12.399
1.00
29.75
C


ATOM
3235
O
GLU
A
429
1.921
28.020
13.484
1.00
29.78
O


ATOM
3236
N
HIS
A
430
3.760
27.562
12.255
1.00
29.80
N


ATOM
3237
CA
HIS
A
430
4.600
27.188
13.395
1.00
29.92
C


ATOM
3238
CB
HIS
A
430
5.984
26.734
12.910
1.00
29.82
C


ATOM
3239
CG
HIS
A
430
7.002
26.607
14.003
1.00
29.75
C


ATOM
3240
ND1
HIS
A
430
7.202
25.437
14.702
1.00
29.97
N


ATOM
3241
CE1
HIS
A
430
8.160
25.617
15.594
1.00
30.02
C


ATOM
3242
NE2
HIS
A
430
8.591
26.862
15.497
1.00
29.87
N


ATOM
3243
CD2
HIS
A
430
7.884
27.502
14.508
1.00
30.04
C


ATOM
3244
C
HIS
A
430
4.731
28.346
14.383
1.00
30.18
C


ATOM
3245
O
HIS
A
430
4.585
28.157
15.595
1.00
30.08
O


ATOM
3246
N
ARG
A
431
5.000
29.541
13.857
1.00
30.45
N


ATOM
3247
CA
ARG
A
431
5.151
30.740
14.685
1.00
30.84
C


ATOM
3248
CB
ARG
A
431
5.711
31.905
13.862
1.00
30.80
C


ATOM
3249
CG
ARG
A
431
7.134
31.681
13.364
1.00
31.07
C


ATOM
3250
CD
ARG
A
431
7.624
32.838
12.509
1.00
31.47
C


ATOM
3251
NE
ARG
A
431
8.098
33.960
13.317
1.00
32.66
N


ATOM
3252
CZ
ARG
A
431
7.475
35.132
13.427
1.00
33.11
C


ATOM
3253
NH1
ARG
A
431
6.340
35.357
12.774
1.00
33.51
N


ATOM
3254
NH2
ARG
A
431
7.994
36.085
14.188
1.00
33.18
N


ATOM
3255
C
ARG
A
431
3.838
31.139
15.355
1.00
30.98
C


ATOM
3256
O
ARG
A
431
3.833
31.576
16.505
1.00
30.90
O


ATOM
3257
N
ARG
A
432
2.729
30.976
14.631
1.00
31.21
N


ATOM
3258
CA
ARG
A
432
1.395
31.258
15.172
1.00
31.58
C


ATOM
3259
CB
ARG
A
432
0.334
31.187
14.067
1.00
31.56
C


ATOM
3260
CG
ARG
A
432
0.323
32.391
13.133
1.00
32.02
C


ATOM
3261
CD
ARG
A
432
−0.734
32.245
12.046
1.00
32.35
C


ATOM
3262
NE
ARG
A
432
−0.628
33.299
11.037
1.00
33.80
N


ATOM
3263
CZ
ARG
A
432
−1.452
33.439
10.001
1.00
34.49
C


ATOM
3264
NH1
ARG
A
432
−2.460
32.592
9.822
1.00
34.96
N


ATOM
3265
NH2
ARG
A
432
−1.270
34.431
9.139
1.00
35.02
N


ATOM
3266
C
ARG
A
432
1.025
30.315
16.321
1.00
31.58
C


ATOM
3267
O
ARG
A
432
0.307
30.705
17.244
1.00
31.53
O


ATOM
3268
N
GLN
A
433
1.520
29.079
16.256
1.00
31.63
N


ATOM
3269
CA
GLN
A
433
1.252
28.077
17.292
1.00
31.83
C


ATOM
3270
CB
GLN
A
433
1.495
26.663
16.752
1.00
31.81
C


ATOM
3271
CG
GLN
A
433
0.379
26.154
15.836
1.00
32.28
C


ATOM
3272
CD
GLN
A
433
0.749
24.880
15.085
1.00
32.55
C


ATOM
3273
OE1
GLN
A
433
1.763
24.240
15.373
1.00
33.88
O


ATOM
3274
NE2
GLN
A
433
−0.078
24.509
14.115
1.00
33.03
N


ATOM
3275
C
GLN
A
433
2.076
28.322
18.558
1.00
31.71
C


ATOM
3276
O
GLN
A
433
1.646
27.982
19.663
1.00
31.67
O


ATOM
3277
N
VAL
A
434
3.257
28.913
18.387
1.00
31.60
N


ATOM
3278
CA
VAL
A
434
4.078
29.346
19.519
1.00
31.59
C


ATOM
3279
CB
VAL
A
434
5.565
29.564
19.107
1.00
31.49
C


ATOM
3280
CG1
VAL
A
434
6.374
30.132
20.270
1.00
31.66
C


ATOM
3281
CG2
VAL
A
434
6.181
28.265
18.616
1.00
31.59
C


ATOM
3282
C
VAL
A
434
3.511
30.639
20.107
1.00
31.57
C


ATOM
3283
O
VAL
A
434
3.282
30.735
21.317
1.00
31.59
O


ATOM
3284
N
PHE
A
435
3.270
31.621
19.240
1.00
31.62
N


ATOM
3285
CA
PHE
A
435
2.837
32.944
19.674
1.00
31.68
C


ATOM
3286
CB
PHE
A
435
3.458
34.034
18.795
1.00
31.57
C


ATOM
3287
CG
PHE
A
435
4.960
33.977
18.730
1.00
31.44
C


ATOM
3288
CD1
PHE
A
435
5.718
33.801
19.890
1.00
31.49
C


ATOM
3289
CE1
PHE
A
435
7.109
33.748
19.832
1.00
31.29
C


ATOM
3290
CZ
PHE
A
435
7.755
33.882
18.609
1.00
31.33
C


ATOM
3291
CE2
PHE
A
435
7.012
34.061
17.447
1.00
31.39
C


ATOM
3292
CD2
PHE
A
435
5.621
34.110
17.513
1.00
31.62
C


ATOM
3293
C
PHE
A
435
1.317
33.075
19.723
1.00
31.86
C


ATOM
3294
O
PHE
A
435
0.689
33.627
18.810
1.00
31.90
O


ATOM
3295
N
THR
A
436
0.700
32.611
20.811
1.00
32.09
N


ATOM
3296
CA
THR
A
436
−0.744
32.538
20.995
1.00
32.28
C


ATOM
3297
CB
THR
A
436
−1.159
31.204
21.667
1.00
32.28
C


ATOM
3298
OG1
THR
A
436
−0.358
30.984
22.838
1.00
32.26
O


ATOM
3299
CG2
THR
A
436
−0.973
30.035
20.707
1.00
32.38
C


ATOM
3300
C
THR
A
436
−1.160
33.696
21.892
1.00
32.48
C


ATOM
3301
O
THR
A
436
−0.354
34.219
22.669
1.00
32.58
O


ATOM
3302
N
PRO
A
437
−2.343
34.199
21.692
1.00
32.62
N


ATOM
3303
CA
PRO
A
437
−2.854
35.312
22.499
1.00
32.65
C


ATOM
3304
CB
PRO
A
437
−4.369
35.295
22.216
1.00
32.69
C


ATOM
3305
CG
PRO
A
437
−4.623
34.009
21.452
1.00
32.68
C


ATOM
3306
CD
PRO
A
437
−3.353
33.708
20.741
1.00
32.65
C


ATOM
3307
C
PRO
A
437
−2.587
35.106
23.993
1.00
32.64
C


ATOM
3308
O
PRO
A
437
−2.222
36.053
24.690
1.00
32.71
O


ATOM
3309
N
GLU
A
438
−2.733
33.802
24.450
1.00
32.58
N


ATOM
3310
CA
GLU
A
438
−2.477
33.443
25.848
1.00
32.57
C


ATOM
3311
CB
GLU
A
438
−2.982
32.028
26.136
1.00
32.61
C


ATOM
3312
CG
GLU
A
438
−2.649
31.018
25.043
1.00
33.20
C


ATOM
3313
CD
GLU
A
438
−3.124
29.618
25.366
1.00
33.53
C


ATOM
3314
OE1
GLU
A
438
−3.471
29.361
26.543
1.00
34.34
O


ATOM
3315
OE2
GLU
A
438
−3.147
28.774
24.443
1.00
34.01
O


ATOM
3316
C
GLU
A
438
−1.000
33.554
26.226
1.00
32.24
C


ATOM
3317
O
GLU
A
438
−0.668
34.011
27.322
1.00
32.33
O


ATOM
3318
N
PHE
A
439
−0.109
33.131
25.363
1.00
31.85
N


ATOM
3319
CA
PHE
A
439
1.328
33.215
25.600
1.00
31.35
C


ATOM
3320
CB
PHE
A
439
2.105
32.373
24.581
1.00
31.40
C


ATOM
3321
CG
PHE
A
439
3.600
32.534
24.673
1.00
31.40
C


ATOM
3322
CD1
PHE
A
439
4.317
31.947
25.716
1.00
31.59
C


ATOM
3323
CE1
PHE
A
439
5.699
32.096
25.805
1.00
31.55
C


ATOM
3324
CZ
PHE
A
439
6.379
32.836
24.843
1.00
31.46
C


ATOM
3325
CE2
PHE
A
439
5.677
33.425
23.798
1.00
31.37
C


ATOM
3326
CD2
PHE
A
439
4.293
33.272
23.717
1.00
31.61
C


ATOM
3327
C
PHE
A
439
1.801
34.666
25.571
1.00
31.05
C


ATOM
3328
O
PHE
A
439
2.592
35.082
26.419
1.00
30.99
O


ATOM
3329
N
LEU
A
440
1.301
35.429
24.600
1.00
30.61
N


ATOM
3330
CA
LEU
A
440
1.692
36.828
24.435
1.00
30.26
C


ATOM
3331
CB
LEU
A
440
1.212
37.380
23.084
1.00
30.43
C


ATOM
3332
CG
LEU
A
440
1.605
36.629
21.804
1.00
30.59
C


ATOM
3333
CD1
LEU
A
440
1.288
37.462
20.571
1.00
31.06
C


ATOM
3334
CD2
LEU
A
440
3.069
36.214
21.810
1.00
31.06
C


ATOM
3335
C
LEU
A
440
1.179
37.697
25.580
1.00
29.92
C


ATOM
3336
O
LEU
A
440
1.871
38.614
26.028
1.00
29.84
O


ATOM
3337
N
GLN
A
441
−0.034
37.400
26.049
1.00
29.49
N


ATOM
3338
CA
GLN
A
441
−0.615
38.099
27.194
1.00
29.07
C


ATOM
3339
CB
GLN
A
441
−2.102
37.753
27.351
1.00
29.18
C


ATOM
3340
CG
GLN
A
441
−2.841
38.606
28.383
1.00
29.75
C


ATOM
3341
CD
GLN
A
441
−2.852
40.081
28.024
1.00
30.43
C


ATOM
3342
OE1
GLN
A
441
−3.384
40.476
26.986
1.00
31.08
O


ATOM
3343
NE2
GLN
A
441
−2.266
40.904
28.885
1.00
30.79
N


ATOM
3344
C
GLN
A
441
0.144
37.765
28.474
1.00
28.58
C


ATOM
3345
O
GLN
A
441
0.458
38.655
29.265
1.00
28.65
O


ATOM
3346
N
GLY
A
442
0.439
36.479
28.666
1.00
27.94
N


ATOM
3347
CA
GLY
A
442
1.241
36.022
29.800
1.00
27.15
C


ATOM
3348
C
GLY
A
442
2.633
36.628
29.795
1.00
26.49
C


ATOM
3349
O
GLY
A
442
3.180
36.958
30.849
1.00
26.50
O


ATOM
3350
N
TYR
A
443
3.200
36.781
28.599
1.00
25.80
N


ATOM
3351
CA
TYR
A
443
4.506
37.409
28.434
1.00
25.26
C


ATOM
3352
CB
TYR
A
443
5.005
37.245
26.994
1.00
24.62
C


ATOM
3353
CG
TYR
A
443
6.499
37.411
26.843
1.00
23.83
C


ATOM
3354
CD1
TYR
A
443
7.366
36.341
27.081
1.00
23.37
C


ATOM
3355
CE1
TYR
A
443
8.742
36.487
26.946
1.00
22.61
C


ATOM
3356
CZ
TYR
A
443
9.266
37.715
26.568
1.00
22.69
C


ATOM
3357
OH
TYR
A
443
10.626
37.863
26.431
1.00
22.52
O


ATOM
3358
CE2
TYR
A
443
8.428
38.792
26.325
1.00
22.51
C


ATOM
3359
CD2
TYR
A
443
7.051
38.635
26.465
1.00
22.79
C


ATOM
3360
C
TYR
A
443
4.459
38.888
28.819
1.00
25.28
C


ATOM
3361
O
TYR
A
443
5.304
39.363
29.580
1.00
25.21
O


ATOM
3362
N
ALA
A
444
3.462
39.604
28.297
1.00
25.48
N


ATOM
3363
CA
ALA
A
444
3.257
41.016
28.626
1.00
25.81
C


ATOM
3364
CB
ALA
A
444
2.107
41.593
27.806
1.00
25.81
C


ATOM
3365
C
ALA
A
444
3.001
41.213
30.120
1.00
26.01
C


ATOM
3366
O
ALA
A
444
3.508
42.162
30.724
1.00
26.04
O


ATOM
3367
N
ASP
A
445
2.220
40.307
30.708
1.00
26.34
N


ATOM
3368
CA
ASP
A
445
1.905
40.350
32.137
1.00
26.71
C


ATOM
3369
CB
ASP
A
445
0.853
39.293
32.497
1.00
26.87
C


ATOM
3370
CG
ASP
A
445
−0.544
39.660
32.012
1.00
27.59
C


ATOM
3371
OD1
ASP
A
445
−0.797
40.852
31.730
1.00
28.24
O


ATOM
3372
OD2
ASP
A
445
−1.395
38.749
31.919
1.00
28.77
O


ATOM
3373
C
ASP
A
445
3.144
40.169
33.010
1.00
26.77
C


ATOM
3374
O
ASP
A
445
3.273
40.815
34.050
1.00
26.68
O


ATOM
3375
N
GLU
A
446
4.047
39.285
32.587
1.00
26.79
N


ATOM
3376
CA
GLU
A
446
5.284
39.045
33.327
1.00
27.17
C


ATOM
3377
CB
GLU
A
446
6.018
37.808
32.799
1.00
27.24
C


ATOM
3378
CG
GLU
A
446
7.149
37.340
33.717
1.00
28.26
C


ATOM
3379
CD
GLU
A
446
7.944
36.169
33.159
1.00
28.85
C


ATOM
3380
OE1
GLU
A
446
7.471
35.503
32.211
1.00
31.26
O


ATOM
3381
OE2
GLU
A
446
9.050
35.912
33.682
1.00
30.75
O


ATOM
3382
C
GLU
A
446
6.202
40.265
33.290
1.00
26.78
C


ATOM
3383
O
GLU
A
446
6.779
40.644
34.310
1.00
26.64
O


ATOM
3384
N
LEU
A
447
6.325
40.876
32.112
1.00
26.64
N


ATOM
3385
CA
LEU
A
447
7.156
42.070
31.941
1.00
26.52
C


ATOM
3386
CB
LEU
A
447
7.206
42.491
30.468
1.00
26.40
C


ATOM
3387
CG
LEU
A
447
7.883
41.528
29.485
1.00
26.07
C


ATOM
3388
CD1
LEU
A
447
7.698
42.008
28.056
1.00
25.63
C


ATOM
3389
CD2
LEU
A
447
9.364
41.353
29.809
1.00
26.15
C


ATOM
3390
C
LEU
A
447
6.668
43.231
32.805
1.00
26.64
C


ATOM
3391
O
LEU
A
447
7.468
43.905
33.458
1.00
26.39
O


ATOM
3392
N
GLN
A
448
5.354
43.449
32.806
1.00
26.82
N


ATOM
3393
CA
GLN
A
448
4.740
44.508
33.607
1.00
27.29
C


ATOM
3394
CB
GLN
A
448
3.264
44.676
33.232
1.00
27.26
C


ATOM
3395
CG
GLN
A
448
3.053
45.288
31.847
1.00
28.22
C


ATOM
3396
CD
GLN
A
448
1.613
45.199
31.366
1.00
28.41
C


ATOM
3397
OE1
GLN
A
448
1.048
44.108
31.250
1.00
29.89
O


ATOM
3398
NE2
GLN
A
448
1.019
46.349
31.064
1.00
29.54
N


ATOM
3399
C
GLN
A
448
4.892
44.239
35.104
1.00
27.18
C


ATOM
3400
O
GLN
A
448
5.084
45.164
35.893
1.00
27.10
O


ATOM
3401
N
MET
A
449
4.820
42.965
35.482
1.00
27.21
N


ATOM
3402
CA
MET
A
449
5.036
42.551
36.864
1.00
27.66
C


ATOM
3403
CB
MET
A
449
4.669
41.077
37.034
1.00
27.54
C


ATOM
3404
CG
MET
A
449
4.509
40.630
38.473
1.00
28.84
C


ATOM
3405
SD
MET
A
449
4.974
38.903
38.692
1.00
30.54
S


ATOM
3406
CE
MET
A
449
6.764
39.033
38.635
1.00
29.99
C


ATOM
3407
C
MET
A
449
6.487
42.788
37.301
1.00
27.01
C


ATOM
3408
O
MET
A
449
6.740
43.274
38.404
1.00
27.03
O


ATOM
3409
N
LEU
A
450
7.431
42.447
36.426
1.00
26.53
N


ATOM
3410
CA
LEU
A
450
8.854
42.574
36.741
1.00
26.09
C


ATOM
3411
CB
LEU
A
450
9.703
41.746
35.769
1.00
25.90
C


ATOM
3412
CG
LEU
A
450
9.678
40.224
35.953
1.00
25.59
C


ATOM
3413
CD1
LEU
A
450
10.228
39.533
34.720
1.00
24.88
C


ATOM
3414
CD2
LEU
A
450
10.451
39.794
37.202
1.00
25.33
C


ATOM
3415
C
LEU
A
450
9.333
44.024
36.767
1.00
26.10
C


ATOM
3416
O
LEU
A
450
10.233
44.367
37.533
1.00
25.89
O


ATOM
3417
N
VAL
A
451
8.734
44.872
35.931
1.00
26.34
N


ATOM
3418
CA
VAL
A
451
9.092
46.294
35.903
1.00
26.66
C


ATOM
3419
CB
VAL
A
451
8.560
47.024
34.623
1.00
26.83
C


ATOM
3420
CG1
VAL
A
451
7.083
47.377
34.750
1.00
27.07
C


ATOM
3421
CG2
VAL
A
451
9.385
48.271
34.333
1.00
27.23
C


ATOM
3422
C
VAL
A
451
8.653
47.005
37.191
1.00
26.75
C


ATOM
3423
O
VAL
A
451
9.318
47.932
37.652
1.00
26.68
O


ATOM
3424
N
GLN
A
452
7.546
46.544
37.774
1.00
26.84
N


ATOM
3425
CA
GLN
A
452
7.090
47.040
39.071
1.00
27.12
C


ATOM
3426
CB
GLN
A
452
5.642
46.614
39.341
1.00
27.08
C


ATOM
3427
CG
GLN
A
452
4.604
47.333
38.478
1.00
27.73
C


ATOM
3428
CD
GLN
A
452
3.169
46.990
38.861
1.00
27.95
C


ATOM
3429
OE1
GLN
A
452
2.812
46.980
40.039
1.00
28.85
O


ATOM
3430
NE2
GLN
A
452
2.339
46.720
37.858
1.00
28.80
N


ATOM
3431
C
GLN
A
452
8.007
46.545
40.189
1.00
27.01
C


ATOM
3432
O
GLN
A
452
8.342
47.297
41.106
1.00
27.00
O


ATOM
3433
N
GLN
A
453
8.416
45.280
40.093
1.00
27.00
N


ATOM
3434
CA
GLN
A
453
9.306
44.660
41.077
1.00
27.00
C


ATOM
3435
CB
GLN
A
453
9.433
43.155
40.805
1.00
26.93
C


ATOM
3436
CG
GLN
A
453
10.280
42.392
41.825
1.00
27.10
C


ATOM
3437
CD
GLN
A
453
10.320
40.894
41.566
1.00
26.88
C


ATOM
3438
OE1
GLN
A
453
9.389
40.321
40.994
1.00
26.80
O


ATOM
3439
NE2
GLN
A
453
11.396
40.250
42.003
1.00
27.08
N


ATOM
3440
C
GLN
A
453
10.690
45.314
41.092
1.00
27.13
C


ATOM
3441
O
GLN
A
453
11.277
45.519
42.156
1.00
27.04
O


ATOM
3442
N
TYR
A
454
11.199
45.644
39.906
1.00
27.29
N


ATOM
3443
CA
TYR
A
454
12.549
46.189
39.767
1.00
27.53
C


ATOM
3444
CB
TYR
A
454
13.356
45.361
38.756
1.00
27.69
C


ATOM
3445
CG
TYR
A
454
13.641
43.947
39.214
1.00
28.08
C


ATOM
3446
CD1
TYR
A
454
14.590
43.694
40.207
1.00
28.54
C


ATOM
3447
CE1
TYR
A
454
14.858
42.397
40.635
1.00
28.98
C


ATOM
3448
CZ
TYR
A
454
14.172
41.334
40.071
1.00
28.56
C


ATOM
3449
OH
TYR
A
454
14.436
40.052
40.498
1.00
29.25
O


ATOM
3450
CE2
TYR
A
454
13.222
41.556
39.085
1.00
28.18
C


ATOM
3451
CD2
TYR
A
454
12.962
42.861
38.661
1.00
27.92
C


ATOM
3452
C
TYR
A
454
12.552
47.670
39.376
1.00
27.57
C


ATOM
3453
O
TYR
A
454
13.510
48.157
38.771
1.00
27.50
O


ATOM
3454
N
ALA
A
455
11.491
48.384
39.758
1.00
27.70
N


ATOM
3455
CA
ALA
A
455
11.306
49.795
39.386
1.00
27.84
C


ATOM
3456
CB
ALA
A
455
10.013
50.338
39.989
1.00
27.78
C


ATOM
3457
C
ALA
A
455
12.487
50.693
39.759
1.00
27.96
C


ATOM
3458
O
ALA
A
455
12.766
51.679
39.072
1.00
28.01
O


ATOM
3459
N
ASP
A
456
13.178
50.345
40.842
1.00
28.07
N


ATOM
3460
CA
ASP
A
456
14.289
51.152
41.341
1.00
28.26
C


ATOM
3461
CB
ASP
A
456
14.261
51.210
42.874
1.00
28.51
C


ATOM
3462
CG
ASP
A
456
13.053
51.974
43.408
1.00
29.33
C


ATOM
3463
OD1
ASP
A
456
12.679
53.008
42.807
1.00
30.45
O


ATOM
3464
OD2
ASP
A
456
12.480
51.544
44.432
1.00
30.63
O


ATOM
3465
C
ASP
A
456
15.659
50.689
40.823
1.00
28.05
C


ATOM
3466
O
ASP
A
456
16.692
51.271
41.167
1.00
28.26
O


ATOM
3467
N
ASP
A
457
15.657
49.649
39.990
1.00
27.64
N


ATOM
3468
CA
ASP
A
457
16.862
49.221
39.279
1.00
27.20
C


ATOM
3469
CB
ASP
A
457
17.069
47.706
39.413
1.00
27.37
C


ATOM
3470
CG
ASP
A
457
18.442
47.250
38.921
1.00
27.99
C


ATOM
3471
OD1
ASP
A
457
18.876
47.687
37.831
1.00
28.65
O


ATOM
3472
OD2
ASP
A
457
19.082
46.438
39.620
1.00
29.17
O


ATOM
3473
C
ASP
A
457
16.745
49.622
37.811
1.00
26.82
C


ATOM
3474
O
ASP
A
457
16.171
48.891
36.999
1.00
26.61
O


ATOM
3475
N
LYS
A
458
17.301
50.784
37.479
1.00
26.34
N


ATOM
3476
CA
LYS
A
458
17.100
51.393
36.162
1.00
26.00
C


ATOM
3477
CB
LYS
A
458
17.657
52.822
36.132
1.00
26.17
C


ATOM
3478
CG
LYS
A
458
17.052
53.764
37.189
1.00
26.56
C


ATOM
3479
CD
LYS
A
458
15.520
53.792
37.126
1.00
27.36
C


ATOM
3480
CE
LYS
A
458
14.930
54.831
38.072
1.00
27.51
C


ATOM
3481
NZ
LYS
A
458
15.049
54.436
39.504
1.00
28.15
N


ATOM
3482
C
LYS
A
458
17.673
50.558
35.013
1.00
25.67
C


ATOM
3483
O
LYS
A
458
17.127
50.564
33.908
1.00
25.29
O


ATOM
3484
N
GLU
A
459
18.764
49.841
35.282
1.00
25.32
N


ATOM
3485
CA
GLU
A
459
19.354
48.927
34.298
1.00
25.35
C


ATOM
3486
CB
GLU
A
459
20.676
48.358
34.809
1.00
25.44
C


ATOM
3487
CG
GLU
A
459
21.861
49.300
34.695
1.00
26.84
C


ATOM
3488
CD
GLU
A
459
23.128
48.722
35.309
1.00
27.47
C


ATOM
3489
OE1
GLU
A
459
23.124
47.527
35.692
1.00
30.55
O


ATOM
3490
OE2
GLU
A
459
24.130
49.463
35.411
1.00
30.02
O


ATOM
3491
C
GLU
A
459
18.403
47.784
33.962
1.00
24.66
C


ATOM
3492
O
GLU
A
459
18.244
47.422
32.796
1.00
24.46
O


ATOM
3493
N
LYS
A
460
17.779
47.213
34.991
1.00
24.09
N


ATOM
3494
CA
LYS
A
460
16.840
46.111
34.797
1.00
23.81
C


ATOM
3495
CB
LYS
A
460
16.492
45.445
36.130
1.00
23.95
C


ATOM
3496
CG
LYS
A
460
17.641
44.658
36.743
1.00
25.13
C


ATOM
3497
CD
LYS
A
460
17.149
43.729
37.839
1.00
27.43
C


ATOM
3498
CE
LYS
A
460
18.271
43.332
38.789
1.00
29.03
C


ATOM
3499
NZ
LYS
A
460
19.314
42.499
38.132
1.00
30.46
N


ATOM
3500
C
LYS
A
460
15.577
46.581
34.086
1.00
23.30
C


ATOM
3501
O
LYS
A
460
15.050
45.880
33.220
1.00
23.33
O


ATOM
3502
N
VAL
A
461
15.106
47.776
34.443
1.00
22.87
N


ATOM
3503
CA
VAL
A
461
13.964
48.386
33.761
1.00
22.45
C


ATOM
3504
CB
VAL
A
461
13.576
49.758
34.386
1.00
22.49
C


ATOM
3505
CG1
VAL
A
461
12.444
50.413
33.600
1.00
22.59
C


ATOM
3506
CG2
VAL
A
461
13.164
49.578
35.836
1.00
22.25
C


ATOM
3507
C
VAL
A
461
14.247
48.521
32.260
1.00
22.27
C


ATOM
3508
O
VAL
A
461
13.397
48.187
31.433
1.00
22.30
O


ATOM
3509
N
ALA
A
462
15.456
48.975
31.922
1.00
21.99
N


ATOM
3510
CA
ALA
A
462
15.887
49.092
30.524
1.00
21.82
C


ATOM
3511
CB
ALA
A
462
17.259
49.763
30.436
1.00
21.80
C


ATOM
3512
C
ALA
A
462
15.900
47.739
29.810
1.00
21.74
C


ATOM
3513
O
ALA
A
462
15.493
47.642
28.652
1.00
21.87
O


ATOM
3514
N
LEU
A
463
16.354
46.696
30.506
1.00
21.41
N


ATOM
3515
CA
LEU
A
463
16.355
45.344
29.938
1.00
21.23
C


ATOM
3516
CB
LEU
A
463
17.094
44.356
30.851
1.00
21.10
C


ATOM
3517
CG
LEU
A
463
18.619
44.467
30.963
1.00
20.92
C


ATOM
3518
CD1
LEU
A
463
19.140
43.560
32.069
1.00
20.25
C


ATOM
3519
CD2
LEU
A
463
19.305
44.144
29.639
1.00
21.03
C


ATOM
3520
C
LEU
A
463
14.934
44.856
29.668
1.00
21.23
C


ATOM
3521
O
LEU
A
463
14.666
44.253
28.630
1.00
21.26
O


ATOM
3522
N
LEU
A
464
14.022
45.136
30.600
1.00
21.24
N


ATOM
3523
CA
LEU
A
464
12.627
44.719
30.456
1.00
21.40
C


ATOM
3524
CB
LEU
A
464
11.875
44.873
31.781
1.00
21.24
C


ATOM
3525
CG
LEU
A
464
12.291
43.886
32.877
1.00
21.17
C


ATOM
3526
CD1
LEU
A
464
11.930
44.413
34.255
1.00
20.85
C


ATOM
3527
CD2
LEU
A
464
11.686
42.498
32.642
1.00
21.02
C


ATOM
3528
C
LEU
A
464
11.913
45.466
29.329
1.00
21.60
C


ATOM
3529
O
LEU
A
464
11.088
44.887
28.618
1.00
21.79
O


ATOM
3530
N
LYS
A
465
12.248
46.745
29.165
1.00
21.83
N


ATOM
3531
CA
LYS
A
465
11.737
47.548
28.050
1.00
22.23
C


ATOM
3532
CB
LYS
A
465
12.151
49.016
28.202
1.00
22.41
C


ATOM
3533
CG
LYS
A
465
11.571
49.718
29.424
1.00
24.11
C


ATOM
3534
CD
LYS
A
465
10.082
49.995
29.275
1.00
26.38
C


ATOM
3535
CE
LYS
A
465
9.534
50.732
30.492
1.00
27.88
C


ATOM
3536
NZ
LYS
A
465
10.156
52.079
30.662
1.00
28.79
N


ATOM
3537
C
LYS
A
465
12.216
47.005
26.705
1.00
22.14
C


ATOM
3538
O
LYS
A
465
11.464
47.001
25.727
1.00
22.11
O


ATOM
3539
N
ALA
A
466
13.468
46.548
26.668
1.00
22.09
N


ATOM
3540
CA
ALA
A
466
14.036
45.922
25.475
1.00
22.14
C


ATOM
3541
CB
ALA
A
466
15.519
45.646
25.673
1.00
22.15
C


ATOM
3542
C
ALA
A
466
13.290
44.635
25.119
1.00
22.22
C


ATOM
3543
O
ALA
A
466
13.030
44.364
23.948
1.00
22.19
O


ATOM
3544
N
LEU
A
467
12.934
43.855
26.138
1.00
22.40
N


ATOM
3545
CA
LEU
A
467
12.176
42.620
25.935
1.00
22.71
C


ATOM
3546
CB
LEU
A
467
12.093
41.818
27.235
1.00
22.59
C


ATOM
3547
CG
LEU
A
467
13.403
41.213
27.742
1.00
22.58
C


ATOM
3548
CD1
LEU
A
467
13.219
40.659
29.131
1.00
22.56
C


ATOM
3549
CD2
LEU
A
467
13.895
40.132
26.801
1.00
23.61
C


ATOM
3550
C
LEU
A
467
10.777
42.879
25.387
1.00
23.12
C


ATOM
3551
O
LEU
A
467
10.274
42.107
24.566
1.00
23.16
O


ATOM
3552
N
TRP
A
468
10.151
43.960
25.853
1.00
23.80
N


ATOM
3553
CA
TRP
A
468
8.846
44.383
25.346
1.00
24.42
C


ATOM
3554
CB
TRP
A
468
8.316
45.569
26.160
1.00
24.94
C


ATOM
3555
CG
TRP
A
468
6.899
45.965
25.820
1.00
25.60
C


ATOM
3556
CD1
TRP
A
468
6.488
46.704
24.745
1.00
26.31
C


ATOM
3557
NE1
TRP
A
468
5.124
46.863
24.772
1.00
26.64
N


ATOM
3558
CE2
TRP
A
468
4.623
46.228
25.878
1.00
26.57
C


ATOM
3559
CD2
TRP
A
468
5.715
45.651
26.566
1.00
26.41
C


ATOM
3560
CE3
TRP
A
468
5.469
44.935
27.748
1.00
26.50
C


ATOM
3561
CZ3
TRP
A
468
4.157
44.821
28.200
1.00
26.33
C


ATOM
3562
CH2
TRP
A
468
3.090
45.408
27.491
1.00
26.30
C


ATOM
3563
CZ2
TRP
A
468
3.303
46.113
26.332
1.00
26.49
C


ATOM
3564
C
TRP
A
468
8.946
44.757
23.869
1.00
24.63
C


ATOM
3565
O
TRP
A
468
8.140
44.310
23.052
1.00
24.46
O


ATOM
3566
N
GLN
A
469
9.954
45.562
23.540
1.00
24.89
N


ATOM
3567
CA
GLN
A
469
10.174
46.033
22.171
1.00
25.51
C


ATOM
3568
CB
GLN
A
469
11.314
47.053
22.137
1.00
25.53
C


ATOM
3569
CG
GLN
A
469
10.941
48.414
22.717
1.00
27.45
C


ATOM
3570
CD
GLN
A
469
12.153
49.242
23.113
1.00
29.02
C


ATOM
3571
OE1
GLN
A
469
13.108
49.379
22.347
1.00
30.62
O


ATOM
3572
NE2
GLN
A
469
12.113
49.807
24.316
1.00
30.06
N


ATOM
3573
C
GLN
A
469
10.457
44.884
21.205
1.00
25.42
C


ATOM
3574
O
GLN
A
469
9.975
44.887
20.070
1.00
25.46
O


ATOM
3575
N
TYR
A
470
11.234
43.903
21.662
1.00
25.53
N


ATOM
3576
CA
TYR
A
470
11.524
42.716
20.861
1.00
25.75
C


ATOM
3577
CB
TYR
A
470
12.596
41.853
21.533
1.00
25.15
C


ATOM
3578
CG
TYR
A
470
13.091
40.704
20.677
1.00
24.30
C


ATOM
3579
CD1
TYR
A
470
13.969
40.928
19.613
1.00
23.47
C


ATOM
3580
CE1
TYR
A
470
14.427
39.875
18.825
1.00
23.13
C


ATOM
3581
CZ
TYR
A
470
14.015
38.581
19.105
1.00
23.70
C


ATOM
3582
OH
TYR
A
470
14.467
37.537
18.333
1.00
23.91
O


ATOM
3583
CE2
TYR
A
470
13.148
38.333
20.161
1.00
23.33
C


ATOM
3584
CD2
TYR
A
470
12.694
39.392
20.939
1.00
23.86
C


ATOM
3585
C
TYR
A
470
10.257
41.903
20.612
1.00
26.49
C


ATOM
3586
O
TYR
A
470
10.011
41.463
19.490
1.00
26.47
O


ATOM
3587
N
ALA
A
471
9.455
41.721
21.663
1.00
27.50
N


ATOM
3588
CA
ALA
A
471
8.171
41.021
21.555
1.00
28.58
C


ATOM
3589
CB
ALA
A
471
7.530
40.861
22.930
1.00
28.43
C


ATOM
3590
C
ALA
A
471
7.215
41.731
20.593
1.00
29.45
C


ATOM
3591
O
ALA
A
471
6.536
41.083
19.799
1.00
29.58
O


ATOM
3592
N
ASP
A
472
7.181
43.062
20.662
1.00
30.53
N


ATOM
3593
CA
ASP
A
472
6.341
43.870
19.771
1.00
31.75
C


ATOM
3594
CB
ASP
A
472
6.453
45.358
20.127
1.00
31.91
C


ATOM
3595
CG
ASP
A
472
5.566
45.753
21.301
1.00
32.76
C


ATOM
3596
OD1
ASP
A
472
5.383
44.931
22.227
1.00
34.40
O


ATOM
3597
OD2
ASP
A
472
5.054
46.894
21.299
1.00
33.98
O


ATOM
3598
C
ASP
A
472
6.682
43.655
18.294
1.00
32.42
C


ATOM
3599
O
ASP
A
472
5.791
43.617
17.444
1.00
32.58
O


ATOM
3600
N
GLU
A
473
7.973
43.511
18.003
1.00
33.28
N


ATOM
3601
CA
GLU
A
473
8.454
43.315
16.636
1.00
34.24
C


ATOM
3602
CB
GLU
A
473
9.949
43.648
16.548
1.00
34.18
C


ATOM
3603
CG
GLU
A
473
10.546
43.519
15.144
1.00
34.99
C


ATOM
3604
CD
GLU
A
473
12.049
43.275
15.158
1.00
35.74
C


ATOM
3605
OE1
GLU
A
473
12.739
43.808
16.052
1.00
36.34
O


ATOM
3606
OE2
GLU
A
473
12.540
42.551
14.265
1.00
35.99
O


ATOM
3607
C
GLU
A
473
8.209
41.884
16.155
1.00
34.75
C


ATOM
3608
O
GLU
A
473
7.581
41.664
15.116
1.00
34.89
O


ATOM
3609
N
ILE
A
474
8.711
40.922
16.924
1.00
35.46
N


ATOM
3610
CA
ILE
A
474
8.707
39.513
16.535
1.00
36.13
C


ATOM
3611
CB
ILE
A
474
9.763
38.704
17.357
1.00
36.14
C


ATOM
3612
CG1
ILE
A
474
9.876
37.258
16.866
1.00
36.42
C


ATOM
3613
CD1
ILE
A
474
10.902
36.441
17.628
1.00
36.28
C


ATOM
3614
CG2
ILE
A
474
9.463
38.763
18.844
1.00
36.45
C


ATOM
3615
C
ILE
A
474
7.314
38.867
16.638
1.00
36.47
C


ATOM
3616
O
ILE
A
474
6.959
38.014
15.821
1.00
36.61
O


ATOM
3617
N
VAL
A
475
6.529
39.287
17.632
1.00
36.88
N


ATOM
3618
CA
VAL
A
475
5.220
38.674
17.889
1.00
37.23
C


ATOM
3619
CB
VAL
A
475
5.204
37.867
19.233
1.00
37.27
C


ATOM
3620
CG1
VAL
A
475
6.525
37.148
19.438
1.00
37.47
C


ATOM
3621
CG2
VAL
A
475
4.923
38.779
20.425
1.00
37.50
C


ATOM
3622
C
VAL
A
475
4.078
39.695
17.880
1.00
37.42
C


ATOM
3623
O
VAL
A
475
2.906
39.327
17.759
1.00
37.62
O


ATOM
3624
MG
MG
I
1
27.308
28.832
33.737
1.00
14.76
MG


ATOM
3625
CL1
YYY
B
1
28.094
2.115
55.180
1.00
22.85
CL


ATOM
3626
C4
YYY
B
1
29.678
2.529
55.906
1.00
23.32
C


ATOM
3627
C3
YYY
B
1
29.790
3.717
56.615
1.00
23.46
C


ATOM
3628
C2
YYY
B
1
31.000
4.068
57.200
1.00
23.50
C


ATOM
3629
C5
YYY
B
1
30.782
1.678
55.779
1.00
23.55
C


ATOM
3630
C6
YYY
B
1
32.000
2.034
56.372
1.00
23.45
C


ATOM
3631
S1
YYY
B
1
33.362
1.030
56.240
1.00
23.51
S


ATOM
3632
C7
YYY
B
1
32.103
3.231
57.079
1.00
23.62
C


ATOM
3633
N1
YYY
B
1
33.360
3.359
57.554
1.00
23.68
N


ATOM
3634
C1
YYY
B
1
34.103
2.293
57.193
1.00
23.69
C


ATOM
3635
N2
YYY
B
1
35.395
2.252
57.583
1.00
23.73
N


ATOM
3636
C8
YYY
B
1
36.295
1.293
57.331
1.00
23.94
C


ATOM
3637
O1
YYY
B
1
36.002
0.242
56.648
1.00
24.30
O


ATOM
3638
N3
YYY
B
1
35.995
3.280
58.357
1.00
23.88
N


ATOM
3639
C10
YYY
B
1
37.266
2.782
58.479
1.00
24.22
C


ATOM
3640
C9
YYY
B
1
37.674
1.458
57.871
1.00
24.01
C


ATOM
3641
C11
YYY
B
1
38.279
3.589
59.263
1.00
24.41
C


ATOM
3642
C12
YYY
B
1
38.106
3.275
60.744
1.00
25.86
C


ATOM
3643
C13
YYY
B
1
39.701
3.239
58.833
1.00
25.35
C


ATOM
3644
C14
YYY
B
1
38.042
5.078
59.026
1.00
25.63
C


ATOM
3645
OW0
HOH
Z
1
30.735
26.960
51.029
1.00
16.15
O


ATOM
3646
OW0
HOH
Z
2
44.217
16.660
49.450
1.00
14.33
O


ATOM
3647
OW0
HOH
Z
3
24.975
26.526
46.160
1.00
16.01
O


ATOM
3648
OW0
HOH
Z
4
29.478
19.724
49.693
1.00
15.11
O


ATOM
3649
OW0
HOH
Z
5
30.447
−0.495
45.382
1.00
19.69
O


ATOM
3650
OW0
HOH
Z
6
25.382
10.988
38.994
1.00
17.43
O


ATOM
3651
OW0
HOH
Z
7
44.837
23.107
52.651
1.00
20.53
O


ATOM
3652
OW0
HOH
Z
8
33.925
11.386
38.637
1.00
15.24
O


ATOM
3653
OW0
HOH
Z
9
38.427
5.626
46.633
1.00
16.61
O


ATOM
3654
OW0
HOH
Z
10
23.944
11.578
54.516
1.00
16.09
O


ATOM
3655
OW0
HOH
Z
11
28.525
13.633
42.165
1.00
17.08
O


ATOM
3656
OW0
HOH
Z
12
25.033
22.532
47.158
1.00
17.75
O


ATOM
3657
OW0
HOH
Z
13
27.496
29.414
40.232
1.00
20.32
O


ATOM
3658
OW0
HOH
Z
14
29.182
21.762
27.282
1.00
19.96
O


ATOM
3659
OW0
HOH
Z
15
32.302
10.304
34.313
1.00
17.52
O


ATOM
3660
OW0
HOH
Z
16
35.189
10.612
42.318
1.00
16.35
O


ATOM
3661
OW0
HOH
Z
17
35.725
12.468
40.290
1.00
15.12
O


ATOM
3662
OW0
HOH
Z
18
30.672
26.650
33.045
1.00
14.54
O


ATOM
3663
OW0
HOH
Z
19
24.951
22.872
11.339
1.00
22.33
O


ATOM
3664
OW0
HOH
Z
20
24.568
25.015
48.441
1.00
19.23
O


ATOM
3665
OW0
HOH
Z
21
19.932
32.297
20.323
1.00
19.71
O


ATOM
3666
OW0
HOH
Z
22
41.852
29.558
24.116
1.00
25.68
O


ATOM
3667
OW0
HOH
Z
23
18.984
43.268
16.674
1.00
17.99
O


ATOM
3668
OW0
HOH
Z
24
15.754
17.610
23.551
1.00
19.61
O


ATOM
3669
OW0
HOH
Z
25
19.703
30.937
14.675
1.00
21.60
O


ATOM
3670
OW0
HOH
Z
26
30.149
15.360
18.800
1.00
23.55
O


ATOM
3671
OW0
HOH
Z
27
16.476
31.681
55.796
1.00
21.45
O


ATOM
3672
OW0
HOH
Z
28
31.461
28.841
34.678
1.00
20.46
O


ATOM
3673
OW0
HOH
Z
29
26.682
19.963
37.147
1.00
18.83
O


ATOM
3674
OW0
HOH
Z
30
36.742
−0.870
35.859
1.00
19.22
O


ATOM
3675
OW0
HOH
Z
31
41.694
32.798
36.364
1.00
22.28
O


ATOM
3676
OW0
HOH
Z
32
13.964
35.164
19.055
1.00
23.29
O


ATOM
3677
OW0
HOH
Z
33
44.687
19.290
23.496
1.00
24.75
O


ATOM
3678
OW0
HOH
Z
34
11.439
39.520
24.163
1.00
20.33
O


ATOM
3679
OW0
HOH
Z
35
23.843
29.049
47.659
1.00
22.99
O


ATOM
3680
OW0
HOH
Z
36
22.474
12.245
56.697
1.00
19.77
O


ATOM
3681
OW0
HOH
Z
37
22.608
21.073
46.779
1.00
23.31
O


ATOM
3682
OW0
HOH
Z
38
22.463
10.731
58.957
1.00
22.59
O


ATOM
3683
OW0
HOH
Z
39
19.336
29.785
19.101
1.00
21.51
O


ATOM
3684
OW0
HOH
Z
41
14.440
21.298
15.751
1.00
20.75
O


ATOM
3685
OW0
HOH
Z
42
33.650
−3.329
39.080
1.00
24.45
O


ATOM
3686
OW0
HOH
Z
43
16.722
21.450
14.026
1.00
19.23
O


ATOM
3687
OW0
HOH
Z
44
39.081
3.110
40.982
1.00
24.16
O


ATOM
3688
OW0
HOH
Z
45
34.278
0.969
50.266
1.00
24.59
O


ATOM
3689
OW0
HOH
Z
46
14.349
14.267
25.329
1.00
25.77
O


ATOM
3690
OW0
HOH
Z
47
16.681
24.131
14.691
1.00
21.03
O


ATOM
3691
OW0
HOH
Z
48
46.024
29.060
46.493
1.00
26.02
O


ATOM
3692
OW0
HOH
Z
49
17.127
29.764
17.587
1.00
20.93
O


ATOM
3693
OW0
HOH
Z
50
43.551
11.011
34.180
1.00
24.73
O


ATOM
3694
OW0
HOH
Z
51
19.008
32.280
4.186
1.00
30.73
O


ATOM
3695
OW0
HOH
Z
52
34.412
6.047
58.495
1.00
22.05
O


ATOM
3696
OW0
HOH
Z
53
34.329
27.513
32.898
1.00
20.20
O


ATOM
3697
OW0
HOH
Z
54
19.084
25.572
14.852
1.00
20.40
O


ATOM
3698
OW0
HOH
Z
55
22.745
−0.549
33.308
1.00
26.43
O


ATOM
3699
OW0
HOH
Z
56
35.422
28.058
56.081
1.00
24.58
O


ATOM
3700
OW0
HOH
Z
57
22.195
43.452
25.965
1.00
27.10
O


ATOM
3701
OW0
HOH
Z
58
45.427
30.869
34.212
1.00
26.35
O


ATOM
3702
OW0
HOH
Z
59
21.828
24.908
48.645
1.00
24.91
O


ATOM
3703
OW0
HOH
Z
60
30.837
28.719
12.210
1.00
25.43
O


ATOM
3704
OW0
HOH
Z
61
17.828
17.925
50.430
1.00
27.79
O


ATOM
3705
OW0
HOH
Z
62
20.320
35.970
28.204
1.00
27.42
O


ATOM
3706
OW0
HOH
Z
63
35.174
15.298
40.368
1.00
20.63
O


ATOM
3707
OW0
HOH
Z
64
16.178
2.221
57.687
1.00
25.09
O


ATOM
3708
OW0
HOH
Z
65
19.078
25.252
23.832
1.00
21.17
O


ATOM
3709
OW0
HOH
Z
66
26.215
28.413
32.156
1.00
16.27
O


ATOM
3710
OW0
HOH
Z
67
25.853
16.573
41.891
1.00
23.07
O


ATOM
3711
OW0
HOH
Z
68
35.020
12.399
31.602
1.00
22.28
O


ATOM
3712
OW0
HOH
Z
69
21.269
22.265
48.825
1.00
24.30
O


ATOM
3713
OW0
HOH
Z
70
16.855
20.587
21.270
1.00
20.31
O


ATOM
3714
OW0
HOH
Z
71
29.288
15.327
14.200
1.00
30.70
O


ATOM
3715
OW0
HOH
Z
72
18.064
9.522
40.926
1.00
32.63
O


ATOM
3716
OW0
HOH
Z
73
18.792
32.399
12.581
1.00
24.74
O


ATOM
3717
OW0
HOH
Z
74
41.991
8.585
34.749
1.00
27.73
O


ATOM
3718
OW0
HOH
Z
75
19.048
27.076
27.917
1.00
24.01
O


ATOM
3719
OW0
HOH
Z
76
23.777
17.792
58.709
1.00
25.91
O


ATOM
3720
OW0
HOH
Z
77
29.374
36.692
17.816
1.00
24.49
O


ATOM
3721
OW0
HOH
Z
78
19.918
10.676
22.406
1.00
28.68
O


ATOM
3722
OW0
HOH
Z
79
27.313
−3.150
58.251
1.00
24.72
O


ATOM
3723
OW0
HOH
Z
80
42.835
30.604
42.664
1.00
26.43
O


ATOM
3724
OW0
HOH
Z
81
16.601
27.062
51.347
1.00
26.54
O


ATOM
3725
OW0
HOH
Z
82
36.122
14.693
20.290
1.00
24.81
O


ATOM
3726
OW0
HOH
Z
83
16.776
8.608
57.609
1.00
27.55
O


ATOM
3727
OW0
HOH
Z
84
49.363
21.380
43.879
1.00
26.69
O


ATOM
3728
OW0
HOH
Z
85
18.125
28.617
15.154
1.00
24.57
O


ATOM
3729
OW0
HOH
Z
86
23.381
9.809
18.221
1.00
24.73
O


ATOM
3730
OW0
HOH
Z
87
27.366
23.751
10.836
1.00
27.27
O


ATOM
3731
OW0
HOH
Z
88
18.276
5.937
13.820
1.00
31.75
O


ATOM
3732
OW0
HOH
Z
89
9.076
31.346
23.118
1.00
27.61
O


ATOM
3733
OW0
HOH
Z
90
12.198
18.017
6.329
1.00
24.92
O


ATOM
3734
OW0
HOH
Z
91
34.770
14.038
17.854
1.00
25.97
O


ATOM
3735
OW0
HOH
Z
92
20.353
45.797
23.808
1.00
24.47
O


ATOM
3736
OW0
HOH
Z
93
5.383
26.022
−2.819
1.00
37.33
O


ATOM
3737
OW0
HOH
Z
94
30.003
27.609
9.860
1.00
29.09
O


ATOM
3738
OW0
HOH
Z
95
22.149
32.114
31.499
1.00
30.63
O


ATOM
3739
OW0
HOH
Z
96
49.452
20.738
28.598
1.00
32.06
O


ATOM
3740
OW0
HOH
Z
97
24.888
33.333
10.620
1.00
26.86
O


ATOM
3741
OW0
HOH
Z
98
32.635
11.157
31.563
1.00
23.89
O


ATOM
3742
OW0
HOH
Z
99
47.392
31.855
32.606
1.00
28.44
O


ATOM
3743
OW0
HOH
Z
100
39.099
8.373
19.132
1.00
22.62
O


ATOM
3744
OW0
HOH
Z
101
29.416
18.809
39.094
1.00
28.00
O


ATOM
3745
OW0
HOH
Z
102
36.628
10.364
30.797
1.00
27.51
O


ATOM
3746
OW0
HOH
Z
103
33.009
16.670
38.915
1.00
29.71
O


ATOM
3747
OW0
HOH
Z
104
24.149
40.802
12.562
1.00
27.28
O


ATOM
3748
OW0
HOH
Z
105
30.877
9.387
62.920
1.00
28.76
O


ATOM
3749
OW0
HOH
Z
106
22.434
33.698
49.336
1.00
30.13
O


ATOM
3750
OW0
HOH
Z
107
42.970
15.955
28.432
1.00
29.47
O


ATOM
3751
OW0
HOH
Z
108
14.375
25.132
21.428
1.00
27.34
O


ATOM
3752
OW0
HOH
Z
109
11.291
34.633
33.574
1.00
30.36
O


ATOM
3753
OW0
HOH
Z
110
16.154
37.037
37.132
1.00
27.33
O


ATOM
3754
OW0
HOH
Z
111
50.368
22.690
46.917
1.00
30.48
O


ATOM
3755
OW0
HOH
Z
112
12.996
20.132
5.018
1.00
31.98
O


ATOM
3756
OW0
HOH
Z
113
45.519
11.333
44.780
1.00
25.99
O


ATOM
3757
OW0
HOH
Z
114
18.149
24.934
2.960
1.00
34.36
O


ATOM
3758
OW0
HOH
Z
115
34.566
0.240
61.652
1.00
34.36
O


ATOM
3759
OW0
HOH
Z
116
43.766
32.331
40.763
1.00
30.61
O


ATOM
3760
OW0
HOH
Z
117
13.521
46.083
19.695
1.00
29.81
O


ATOM
3761
OW0
HOH
Z
118
10.891
24.595
20.675
1.00
26.07
O


ATOM
3762
OW0
HOH
Z
119
24.216
−3.460
62.415
1.00
33.30
O


ATOM
3763
OW0
HOH
Z
120
14.526
7.764
53.236
1.00
27.09
O


ATOM
3764
OW0
HOH
Z
121
32.467
33.531
31.210
1.00
31.63
O


ATOM
3765
OW0
HOH
Z
122
43.690
32.022
37.913
1.00
33.60
O


ATOM
3766
OW0
HOH
Z
123
26.856
14.766
11.731
1.00
34.14
O


ATOM
3767
OW0
HOH
Z
124
22.483
15.624
15.244
1.00
36.61
O


ATOM
3768
OW0
HOH
Z
125
24.197
27.054
36.096
1.00
39.81
O


ATOM
3769
OW0
HOH
Z
126
35.806
27.449
16.681
1.00
29.95
O


ATOM
3770
OW0
HOH
Z
127
29.895
33.364
30.795
1.00
28.11
O


ATOM
3771
OW0
HOH
Z
128
35.259
8.012
30.913
1.00
27.34
O


ATOM
3772
OW0
HOH
Z
129
19.977
22.278
52.011
1.00
27.26
O


ATOM
3773
OW0
HOH
Z
130
21.679
−3.862
61.103
1.00
29.77
O


ATOM
3774
OW0
HOH
Z
131
38.336
35.245
38.625
1.00
31.39
O


ATOM
3775
OW0
HOH
Z
132
19.497
−4.560
35.579
1.00
36.99
O


ATOM
3776
OW0
HOH
Z
133
13.626
24.676
33.030
1.00
35.95
O


ATOM
3777
OW0
HOH
Z
134
29.966
0.914
30.456
1.00
28.42
O


ATOM
3778
OW0
HOH
Z
135
14.818
32.367
33.364
1.00
35.79
O


ATOM
3779
OW0
HOH
Z
136
43.100
32.469
34.116
1.00
30.84
O


ATOM
3780
OW0
HOH
Z
137
31.293
−11.499
43.457
1.00
32.64
O


ATOM
3781
OW0
HOH
Z
138
23.652
44.624
29.787
1.00
31.22
O


ATOM
3782
OW0
HOH
Z
139
34.426
23.668
57.286
1.00
36.73
O


ATOM
3783
OW0
HOH
Z
140
22.057
3.494
27.457
1.00
32.84
O


ATOM
3784
OW0
HOH
Z
141
13.333
10.323
5.028
1.00
39.48
O


ATOM
3785
OW0
HOH
Z
142
35.870
10.386
28.045
1.00
28.67
O


ATOM
3786
OW0
HOH
Z
143
25.342
28.817
9.171
1.00
31.20
O


ATOM
3787
OW0
HOH
Z
144
28.163
9.422
63.183
1.00
30.37
O


ATOM
3788
OW0
HOH
Z
145
15.391
17.073
26.164
1.00
32.48
O


ATOM
3789
OW0
HOH
Z
147
18.322
25.173
34.502
1.00
38.80
O


ATOM
3790
OW0
HOH
Z
148
35.921
14.923
15.423
1.00
33.55
O


ATOM
3791
OW0
HOH
Z
149
41.145
31.668
50.991
1.00
26.14
O


ATOM
3792
OW0
HOH
Z
150
34.974
38.563
43.958
1.00
35.93
O


ATOM
3793
OW0
HOH
Z
151
29.262
33.045
28.286
1.00
34.41
O


ATOM
3794
OW0
HOH
Z
152
32.969
0.998
63.374
1.00
29.95
O


ATOM
3795
OW0
HOH
Z
153
36.645
36.340
36.728
1.00
26.01
O


ATOM
3796
OW0
HOH
Z
154
14.570
19.845
2.779
1.00
37.35
O


ATOM
3797
OW0
HOH
Z
155
23.229
38.261
13.135
1.00
24.50
O


ATOM
3798
OW0
HOH
Z
156
11.740
26.762
21.998
1.00
26.79
O


ATOM
3799
OW0
HOH
Z
157
29.478
13.821
4.139
1.00
28.31
O


ATOM
3800
OW0
HOH
Z
158
40.787
26.421
56.755
1.00
32.84
O


ATOM
3801
OW0
HOH
Z
159
9.665
20.652
12.212
1.00
35.84
O


ATOM
3802
OW0
HOH
Z
160
39.205
9.838
31.145
1.00
36.76
O


ATOM
3803
OW0
HOH
Z
161
23.436
21.166
39.393
1.00
29.44
O


ATOM
3804
OW0
HOH
Z
162
21.335
23.224
37.167
1.00
34.57
O


ATOM
3805
OW0
HOH
Z
163
38.718
20.988
15.655
1.00
35.04
O


ATOM
3806
OW0
HOH
Z
164
41.044
1.755
39.757
1.00
33.08
O


ATOM
3807
OW0
HOH
Z
165
45.031
29.451
43.965
1.00
29.49
O


ATOM
3808
OW0
HOH
Z
166
38.081
25.941
56.123
1.00
32.80
O


ATOM
3809
OW0
HOH
Z
167
20.161
9.376
58.804
1.00
31.21
O


ATOM
3810
OW0
HOH
Z
168
47.018
18.000
42.384
1.00
37.13
O


ATOM
3811
OW0
HOH
Z
169
36.528
1.745
52.664
1.00
35.32
O


ATOM
3812
OW0
HOH
Z
170
18.928
8.125
24.229
1.00
26.06
O


ATOM
3813
OW0
HOH
Z
171
31.941
14.845
16.941
1.00
31.39
O


ATOM
3814
OW0
HOH
Z
172
22.944
15.985
32.916
1.00
29.55
O


ATOM
3815
OW0
HOH
Z
173
19.920
33.213
10.097
1.00
31.72
O


ATOM
3816
OW0
HOH
Z
174
18.293
10.153
53.111
1.00
36.29
O


ATOM
3817
OW0
HOH
Z
175
18.059
7.335
33.021
1.00
42.94
O


ATOM
3818
OW0
HOH
Z
176
28.432
−2.019
62.836
1.00
34.04
O


ATOM
3819
OW0
HOH
Z
177
30.260
16.127
38.651
1.00
29.47
O


ATOM
3820
OW0
HOH
Z
178
6.446
40.555
41.540
1.00
38.70
O


ATOM
3821
OW0
HOH
Z
179
26.333
18.199
39.290
1.00
32.47
O


ATOM
3822
OW0
HOH
Z
180
24.457
28.242
59.726
1.00
29.67
O


ATOM
3823
OW0
HOH
Z
181
27.364
28.017
37.544
1.00
31.95
O


ATOM
3824
OW0
HOH
Z
182
39.997
3.402
45.714
1.00
33.02
O


ATOM
3825
OW0
HOH
Z
183
49.996
23.378
42.174
1.00
39.39
O


ATOM
3826
OW0
HOH
Z
184
7.923
19.213
16.269
1.00
34.13
O


ATOM
3827
OW0
HOH
Z
185
27.164
−5.486
56.530
1.00
28.25
O


ATOM
3828
OW0
HOH
Z
186
16.652
−9.654
43.964
1.00
36.59
O


ATOM
3829
OW0
HOH
Z
187
43.634
17.615
30.496
1.00
33.30
O


ATOM
3830
OW0
HOH
Z
188
25.430
15.961
30.820
1.00
37.37
O


ATOM
3831
OW0
HOH
Z
189
26.820
13.382
38.133
1.00
33.66
O


ATOM
3832
OW0
HOH
Z
190
9.129
47.050
18.564
1.00
31.53
O


ATOM
3833
OW0
HOH
Z
191
25.669
−8.432
49.431
1.00
30.30
O


ATOM
3834
OW0
HOH
Z
192
45.776
16.987
31.896
1.00
35.42
O


ATOM
3835
OW0
HOH
Z
193
41.187
25.342
19.701
1.00
34.59
O


ATOM
3836
OW0
HOH
Z
194
27.200
7.055
64.435
1.00
29.95
O


ATOM
3837
OW0
HOH
Z
195
27.803
6.433
10.863
1.00
34.56
O


ATOM
3838
OW0
HOH
Z
196
49.509
18.917
42.454
1.00
43.82
O


ATOM
3839
OW0
HOH
Z
197
32.762
8.610
30.741
1.00
32.81
O


ATOM
3840
OW0
HOH
Z
198
31.505
21.855
11.049
1.00
36.84
O


ATOM
3841
OW0
HOH
Z
199
10.954
29.568
27.581
1.00
30.20
O


ATOM
3842
OW0
HOH
Z
200
39.303
8.355
22.166
1.00
44.80
O


ATOM
3843
OW0
HOH
Z
201
13.225
46.918
15.937
1.00
34.83
O


ATOM
3844
OW0
HOH
Z
202
22.374
−5.489
38.115
1.00
32.10
O


ATOM
3845
OW0
HOH
Z
203
42.406
39.234
47.357
1.00
31.98
O


ATOM
3846
OW0
HOH
Z
204
9.828
34.122
9.454
1.00
39.61
O


ATOM
3847
OW0
HOH
Z
205
21.143
18.937
42.697
1.00
39.50
O


ATOM
3848
OW0
HOH
Z
206
24.528
32.238
33.082
1.00
33.22
O


ATOM
3849
OW0
HOH
Z
207
7.747
21.062
4.366
1.00
41.57
O


ATOM
3850
OW0
HOH
Z
208
47.230
29.645
42.256
1.00
37.55
O


ATOM
3851
OW0
HOH
Z
209
22.547
1.506
10.647
1.00
45.42
O


ATOM
3852
OW0
HOH
Z
210
15.826
9.609
51.620
1.00
39.31
O


ATOM
3853
OW0
HOH
Z
211
2.253
24.652
3.430
1.00
35.99
O


ATOM
3854
OW0
HOH
Z
212
31.238
12.119
29.422
1.00
34.88
O


ATOM
3855
OW0
HOH
Z
213
23.361
28.226
0.607
1.00
45.18
O


ATOM
3856
OW0
HOH
Z
214
13.038
14.802
5.292
1.00
46.68
O


ATOM
3857
OW0
HOH
Z
215
49.714
15.276
45.776
1.00
43.87
O


ATOM
3858
OW0
HOH
Z
216
6.199
22.545
11.228
1.00
38.50
O


ATOM
3859
OW0
HOH
Z
217
19.024
19.372
46.664
1.00
40.03
O


ATOM
3860
OW0
HOH
Z
218
43.557
35.347
29.027
1.00
38.48
O


ATOM
3861
OW0
HOH
Z
219
20.983
42.950
35.348
1.00
43.44
O


ATOM
3862
OW0
HOH
Z
220
31.114
31.281
11.314
1.00
40.20
O


ATOM
3863
OW0
HOH
Z
221
36.177
0.796
48.006
1.00
42.56
O


ATOM
3864
OW0
HOH
Z
222
19.728
21.293
33.065
1.00
34.12
O


ATOM
3865
OW0
HOH
Z
223
16.075
49.403
26.726
1.00
29.77
O


ATOM
3866
OW0
HOH
Z
224
8.053
9.057
45.041
1.00
37.18
O


ATOM
3867
OW0
HOH
Z
225
7.350
33.889
9.389
1.00
43.38
O


ATOM
3868
OW0
HOH
Z
226
12.388
47.859
18.361
1.00
34.40
O


ATOM
3869
OW0
HOH
Z
227
28.994
39.741
14.691
1.00
39.78
O


ATOM
3870
OW0
HOH
Z
228
15.239
3.980
59.473
1.00
33.29
O


ATOM
3871
OW0
HOH
Z
229
35.649
33.806
53.865
1.00
35.34
O


ATOM
3872
OW0
HOH
Z
230
51.682
26.659
45.241
1.00
38.98
O


ATOM
3873
OW0
HOH
Z
231
38.537
9.458
25.717
1.00
32.29
O


ATOM
3874
OW0
HOH
Z
232
40.301
38.262
28.461
1.00
33.56
O


ATOM
3875
OW0
HOH
Z
233
24.403
19.220
40.931
1.00
31.65
O


ATOM
3876
OW0
HOH
Z
234
19.417
52.008
39.342
1.00
37.12
O


ATOM
3877
OW0
HOH
Z
235
23.456
−9.883
49.823
1.00
35.38
O


ATOM
3878
OW0
HOH
Z
236
44.033
34.971
33.166
1.00
47.26
O


ATOM
3879
OW0
HOH
Z
237
23.704
22.138
5.378
1.00
38.11
O


ATOM
3880
OW0
HOH
Z
238
21.182
46.392
26.444
1.00
32.01
O


ATOM
3881
OW0
HOH
Z
239
40.359
6.956
48.046
1.00
48.77
O


ATOM
3882
OW0
HOH
Z
240
11.410
26.740
29.056
1.00
40.03
O


ATOM
3883
OW0
HOH
Z
241
6.084
7.346
44.819
1.00
29.00
O


ATOM
3884
OW0
HOH
Z
242
38.607
15.896
56.596
1.00
37.31
O


ATOM
3885
OW0
HOH
Z
243
19.414
11.728
55.919
1.00
42.00
O


ATOM
3886
OW0
HOH
Z
244
26.826
−3.735
61.090
1.00
38.93
O


ATOM
3887
OW0
HOH
Z
245
10.003
37.534
40.258
1.00
43.01
O


ATOM
3888
OW0
HOH
Z
246
34.149
16.488
63.767
1.00
41.95
O


ATOM
3889
OW0
HOH
Z
247
9.400
12.826
16.332
1.00
37.21
O


ATOM
3890
OW0
HOH
Z
248
21.903
−6.746
41.205
1.00
38.57
O


ATOM
3891
OW0
HOH
Z
249
45.763
21.253
21.897
1.00
37.31
O


ATOM
3892
OW0
HOH
Z
250
33.096
22.047
13.280
1.00
47.97
O


ATOM
3893
OW0
HOH
Z
251
37.270
23.956
57.675
1.00
34.54
O


ATOM
3894
OW0
HOH
Z
252
18.185
14.737
49.781
1.00
32.85
O


ATOM
3895
OW0
HOH
Z
253
23.858
32.550
41.057
1.00
50.41
O


ATOM
3896
OW0
HOH
Z
254
18.544
10.488
49.874
1.00
44.44
O


ATOM
3897
OW0
HOH
Z
255
14.771
33.063
12.091
1.00
35.84
O


ATOM
3898
OW0
HOH
Z
256
20.711
11.123
40.135
1.00
43.08
O


ATOM
3899
OW0
HOH
Z
257
47.445
25.183
40.716
1.00
42.52
O


ATOM
3900
OW0
HOH
Z
258
49.714
23.073
26.775
1.00
46.07
O


ATOM
3901
OW0
HOH
Z
259
6.976
9.228
53.709
1.00
28.77
O


ATOM
3902
OW0
HOH
Z
260
16.396
5.631
15.703
1.00
45.74
O


ATOM
3903
OW0
HOH
Z
261
14.775
38.220
13.666
1.00
36.31
O


ATOM
3904
OW0
HOH
Z
262
7.503
22.471
23.700
1.00
43.06
O


ATOM
3905
OW0
HOH
Z
263
35.558
27.151
13.923
1.00
40.92
O


ATOM
3906
OW0
HOH
Z
264
40.908
35.213
37.942
1.00
38.55
O


ATOM
3907
OW0
HOH
Z
265
20.360
47.804
30.836
1.00
30.24
O


ATOM
3908
OW0
HOH
Z
266
5.399
33.984
2.079
1.00
45.30
O


ATOM
3909
OW0
HOH
Z
267
18.977
9.447
61.503
1.00
44.38
O


ATOM
3910
OW0
HOH
Z
268
34.863
16.985
56.795
1.00
37.59
O


ATOM
3911
OW0
HOH
Z
269
4.085
24.049
10.769
1.00
40.05
O


ATOM
3912
OW0
HOH
Z
270
12.703
−6.661
38.471
1.00
38.94
O


ATOM
3913
OW0
HOH
Z
271
22.387
46.165
31.578
1.00
38.09
O


ATOM
3914
OW0
HOH
Z
272
25.192
47.578
21.273
1.00
37.17
O


ATOM
3915
OW0
HOH
Z
273
30.912
35.165
49.928
1.00
49.31
O


ATOM
3916
OW0
HOH
Z
274
18.470
0.631
60.620
1.00
38.78
O


ATOM
3917
OW0
HOH
Z
275
21.139
32.446
6.639
1.00
37.32
O


ATOM
3918
OW0
HOH
Z
276
27.846
−9.129
51.274
1.00
37.62
O


ATOM
3919
OW0
HOH
Z
277
9.353
25.822
18.774
1.00
35.56
O


ATOM
3920
OW0
HOH
Z
278
26.313
21.017
−1.780
1.00
46.51
O


ATOM
3921
OW0
HOH
Z
279
18.304
17.977
27.500
1.00
39.04
O


ATOM
3922
OW0
HOH
Z
280
32.990
−5.269
40.752
1.00
34.10
O


ATOM
3923
OW0
HOH
Z
281
48.291
27.712
40.579
1.00
36.27
O


ATOM
3924
OW0
HOH
Z
282
22.238
31.903
47.422
1.00
48.17
O


ATOM
3925
OW0
HOH
Z
283
9.850
28.109
19.916
1.00
35.54
O


ATOM
3926
OW0
HOH
Z
284
18.199
24.982
51.065
1.00
36.70
O


ATOM
3927
OW0
HOH
Z
285
34.052
14.650
66.009
1.00
47.39
O


ATOM
3928
OW0
HOH
Z
286
3.668
28.719
23.076
1.00
41.76
O


ATOM
3929
OW0
HOH
Z
287
15.481
6.178
34.686
1.00
40.76
O


ATOM
3930
OW0
HOH
Z
288
30.307
43.454
21.426
1.00
41.96
O


ATOM
3931
OW0
HOH
Z
289
45.777
34.388
36.955
1.00
53.44
O


ATOM
3932
OW0
HOH
Z
290
38.322
26.570
16.277
1.00
40.13
O


ATOM
3933
OW0
HOH
Z
291
25.957
13.266
41.332
1.00
36.59
O


ATOM
3934
OW0
HOH
Z
292
9.867
31.765
26.398
1.00
38.30
O


ATOM
3935
OW0
HOH
Z
293
21.671
27.187
35.535
1.00
51.99
O


ATOM
3936
OW0
HOH
Z
294
33.306
26.920
12.585
1.00
48.74
O


ATOM
3937
OW0
HOH
Z
295
27.448
26.445
9.688
1.00
40.69
O


ATOM
3938
OW0
HOH
Z
296
4.820
25.564
17.188
1.00
41.40
O


ATOM
3939
OW0
HOH
Z
297
28.157
10.149
5.633
1.00
35.28
O


ATOM
3940
OW0
HOH
Z
298
27.680
14.319
25.632
1.00
39.39
O


ATOM
3941
OW0
HOH
Z
299
21.473
13.639
30.362
1.00
36.85
O


ATOM
3942
OW0
HOH
Z
300
24.994
25.325
57.875
1.00
33.41
O


ATOM
3943
OW0
HOH
Z
301
23.556
38.711
37.340
1.00
39.57
O


ATOM
3944
OW0
HOH
Z
302
44.768
34.965
26.428
1.00
42.42
O


ATOM
3945
OW0
HOH
Z
303
29.731
21.038
61.890
1.00
39.74
O


ATOM
3946
OW0
HOH
Z
304
2.707
35.429
33.045
1.00
42.38
O


ATOM
3947
OW0
HOH
Z
305
40.241
9.548
54.479
1.00
41.51
O


ATOM
3948
OW0
HOH
Z
306
48.716
29.622
46.334
1.00
37.26
O


ATOM
3949
OW0
HOH
Z
307
22.146
37.661
10.735
1.00
37.70
O


ATOM
3950
OW0
HOH
Z
308
29.721
33.796
53.597
1.00
34.03
O


ATOM
3951
OW0
HOH
Z
309
21.832
9.539
26.316
1.00
44.04
O


ATOM
3952
OW0
HOH
Z
310
18.625
11.738
44.175
1.00
49.66
O


ATOM
3953
OW0
HOH
Z
311
9.568
8.547
43.046
1.00
54.12
O


ATOM
3954
OW0
HOH
Z
312
9.559
17.734
6.257
1.00
40.96
O


ATOM
3955
OW0
HOH
Z
313
3.194
18.590
23.129
1.00
55.89
O


ATOM
3956
OW0
HOH
Z
314
4.647
38.489
41.572
1.00
38.75
O


ATOM
3957
OW0
HOH
Z
315
25.720
11.439
30.384
1.00
35.40
O


ATOM
3958
OW0
HOH
Z
316
20.644
−6.350
61.065
1.00
42.44
O


ATOM
3959
OW0
HOH
Z
317
19.281
29.040
49.588
1.00
42.23
O


ATOM
3960
OW0
HOH
Z
318
41.042
29.348
55.582
1.00
43.07
O


ATOM
3961
OW0
HOH
Z
319
39.711
24.510
17.303
1.00
40.26
O


ATOM
3962
OW0
HOH
Z
320
23.173
6.210
5.587
1.00
40.02
O


ATOM
3963
OW0
HOH
Z
321
36.405
35.222
20.283
1.00
42.88
O


ATOM
3964
OW0
HOH
Z
322
18.439
9.528
47.448
1.00
51.07
O


ATOM
3965
OW0
HOH
Z
323
10.573
7.258
58.154
1.00
45.42
O


ATOM
3966
OW0
HOH
Z
324
7.309
32.350
6.803
1.00
46.10
O


ATOM
3967
OW0
HOH
Z
325
8.176
23.236
12.922
1.00
43.35
O


ATOM
3968
OW0
HOH
Z
326
23.542
8.301
31.788
1.00
46.64
O


ATOM
3969
OW0
HOH
Z
327
11.408
26.036
31.693
1.00
46.43
O


ATOM
3970
OW0
HOH
Z
328
3.612
41.960
15.708
1.00
63.20
O


ATOM
3971
OW0
HOH
Z
329
22.848
17.153
41.528
1.00
36.33
O


ATOM
3972
OW0
HOH
Z
330
29.811
8.979
7.489
1.00
38.38
O


ATOM
3973
OW0
HOH
Z
331
26.967
6.984
14.844
1.00
44.87
O


ATOM
3974
OW0
HOH
Z
332
24.860
23.876
7.037
1.00
36.03
O


ATOM
3975
OW0
HOH
Z
333
39.537
16.594
15.749
1.00
42.23
O


ATOM
3976
OW0
HOH
Z
334
31.132
27.406
56.220
1.00
34.41
O


ATOM
3977
OW0
HOH
Z
335
13.304
7.877
17.789
1.00
42.52
O


ATOM
3978
OW0
HOH
Z
336
7.728
49.577
42.457
1.00
43.66
O


ATOM
3979
OW0
HOH
Z
337
51.361
20.241
45.329
1.00
40.12
O


ATOM
3980
OW0
HOH
Z
338
32.407
−4.809
50.652
1.00
39.95
O


ATOM
3981
OW0
HOH
Z
339
29.986
40.111
17.160
1.00
46.22
O


ATOM
3982
OW0
HOH
Z
340
29.950
10.535
14.992
1.00
52.45
O


ATOM
3983
OW0
HOH
Z
341
29.042
9.155
10.271
1.00
40.54
O


ATOM
3984
OW0
HOH
Z
342
9.599
33.188
31.757
1.00
46.01
O


ATOM
3985
OW0
HOH
Z
343
20.572
18.004
33.607
1.00
43.84
O


ATOM
3986
OW0
HOH
Z
344
16.649
17.660
2.196
1.00
47.16
O


ATOM
3987
OW0
HOH
Z
345
42.868
15.346
56.539
1.00
47.25
O


ATOM
3988
OW0
HOH
Z
346
20.132
31.342
50.528
1.00
42.58
O


ATOM
3989
OW0
HOH
Z
347
17.112
34.208
52.883
1.00
45.69
O


ATOM
3990
OW0
HOH
Z
348
9.715
22.663
17.042
1.00
36.52
O


ATOM
3991
OW0
HOH
Z
349
50.385
16.695
27.607
1.00
43.85
O


ATOM
3992
OW0
HOH
Z
350
12.167
−5.586
36.085
1.00
42.62
O


ATOM
3993
OW0
HOH
Z
351
25.445
35.375
34.031
1.00
50.62
O


ATOM
3994
OW0
HOH
Z
352
21.784
12.501
60.870
1.00
40.16
O


ATOM
3995
OW0
HOH
Z
353
31.839
19.501
29.680
1.00
41.28
O


ATOM
3996
OW0
HOH
Z
354
13.013
17.955
27.174
1.00
45.80
O


ATOM
3997
OW0
HOH
Z
355
48.602
5.061
19.549
1.00
45.60
O


ATOM
3998
OW0
HOH
Z
356
8.859
16.875
8.707
1.00
47.36
O


ATOM
3999
OW0
HOH
Z
357
46.442
32.338
41.142
1.00
38.09
O


ATOM
4000
OW0
HOH
Z
358
23.723
6.564
29.066
1.00
41.80
O


ATOM
4001
OW0
HOH
Z
359
33.801
10.610
66.323
1.00
47.53
O


ATOM
4002
OW0
HOH
Z
360
33.595
14.465
4.553
1.00
45.19
O


ATOM
4003
OW0
HOH
Z
361
33.437
11.589
28.090
1.00
45.12
O


ATOM
4004
OW0
HOH
Z
362
39.566
29.312
17.089
1.00
47.78
O


ATOM
4005
OW0
HOH
Z
363
26.913
−7.952
56.987
1.00
43.09
O


ATOM
4006
OW0
HOH
Z
364
22.795
14.326
58.303
1.00
38.53
O


ATOM
4007
OW0
HOH
Z
365
23.110
−10.449
47.395
1.00
40.34
O


ATOM
4008
OW0
HOH
Z
366
7.713
14.717
9.625
1.00
44.66
O


ATOM
4009
OW0
HOH
Z
367
50.975
28.269
28.930
1.00
55.08
O


ATOM
4010
OW0
HOH
Z
368
14.482
0.254
58.552
1.00
39.56
O


ATOM
4011
OW0
HOH
Z
369
18.764
10.405
37.621
1.00
40.03
O


ATOM
4012
OW0
HOH
Z
370
45.669
16.682
38.548
1.00
51.04
O


ATOM
4013
OW0
HOH
Z
371
36.035
30.009
17.161
1.00
45.79
O


ATOM
4014
OW0
HOH
Z
372
13.495
30.362
−2.110
1.00
52.87
O


ATOM
4015
OW0
HOH
Z
373
15.990
−7.871
57.592
1.00
41.45
O


ATOM
4016
OW0
HOH
Z
374
20.806
10.947
19.868
1.00
42.56
O


ATOM
4017
OW0
HOH
Z
375
11.600
6.596
14.566
1.00
47.69
O


ATOM
4018
OW0
HOH
Z
376
25.679
15.811
38.248
1.00
42.62
O


ATOM
4019
OW0
HOH
Z
377
41.484
8.318
52.350
1.00
49.22
O


ATOM
4020
OW0
HOH
Z
378
48.910
27.729
36.355
1.00
45.54
O


ATOM
4021
OW0
HOH
Z
379
18.457
22.556
−4.029
1.00
45.40
O


ATOM
4022
OW0
HOH
Z
380
15.923
13.477
48.926
1.00
53.94
O


ATOM
4023
OW0
HOH
Z
381
31.836
−4.021
53.522
1.00
45.73
O


ATOM
4024
OW0
HOH
Z
382
8.430
33.175
29.047
1.00
51.48
O


ATOM
4025
OW0
HOH
Z
383
26.954
23.450
61.270
1.00
40.29
O


ATOM
4026
OW0
HOH
Z
384
29.988
35.329
32.668
1.00
48.79
O


ATOM
4027
OW0
HOH
Z
385
5.483
42.993
40.757
1.00
32.49
O


ATOM
4028
OW0
HOH
Z
386
41.387
36.594
50.915
1.00
38.52
O


ATOM
4029
OW0
HOH
Z
387
36.465
6.256
29.053
1.00
39.44
O


ATOM
4030
OW0
HOH
Z
388
45.897
19.035
36.412
1.00
27.98
O


ATOM
4031
OW0
HOH
Z
389
48.052
31.929
38.993
1.00
49.72
O


ATOM
4032
OW0
HOH
Z
390
27.127
12.579
63.489
1.00
47.30
O


ATOM
4033
OW0
HOH
Z
391
26.324
9.487
19.115
1.00
46.32
O


ATOM
4034
OW0
HOH
Z
392
27.536
25.467
58.264
1.00
43.07
O


ATOM
4035
OW0
HOH
Z
393
29.603
3.246
65.779
1.00
43.20
O


ATOM
4036
OW0
HOH
Z
394
22.673
12.785
40.986
1.00
53.87
O


ATOM
4037
OW0
HOH
Z
395
40.519
3.822
43.160
1.00
45.29
O


ATOM
4038
OW0
HOH
Z
396
7.851
29.060
−3.909
1.00
34.56
O


ATOM
4039
OW0
HOH
Z
397
31.574
−2.074
55.542
1.00
39.25
O


ATOM
4040
OW0
HOH
Z
398
11.308
52.633
37.000
1.00
43.46
O


ATOM
4041
OW0
HOH
Z
399
14.385
44.274
17.999
1.00
43.00
O


ATOM
4042
OW0
HOH
Z
400
6.853
30.672
29.388
1.00
52.85
O


ATOM
4043
OW0
HOH
Z
401
44.730
9.323
46.401
1.00
43.46
O


ATOM
4044
OW0
HOH
Z
402
23.600
10.928
65.247
1.00
53.86
O


ATOM
4045
OW0
HOH
Z
403
27.612
36.694
33.323
1.00
47.16
O


ATOM
4046
OW0
HOH
Z
404
19.378
2.674
10.089
1.00
50.33
O


ATOM
4047
OW0
HOH
Z
405
36.151
−0.410
54.091
1.00
48.14
O


ATOM
4048
OW0
HOH
Z
406
17.502
−6.046
34.397
1.00
55.19
O


ATOM
4049
OW0
HOH
Z
407
14.682
36.620
15.814
1.00
36.83
O


ATOM
4050
OW0
HOH
Z
408
18.918
16.611
42.382
1.00
51.40
O


ATOM
4051
OW0
HOH
Z
409
21.073
50.082
37.594
1.00
47.32
O


ATOM
4052
OW0
HOH
Z
411
9.448
5.394
32.875
1.00
53.50
O


ATOM
4053
OW0
HOH
Z
413
2.663
−1.727
48.937
1.00
52.71
O


ATOM
4054
OW0
HOH
Z
414
21.233
25.587
45.932
1.00
44.02
O


ATOM
4055
OW0
HOH
Z
415
30.485
36.215
15.358
1.00
51.99
O


ATOM
4056
OW0
HOH
Z
416
51.843
21.922
40.072
1.00
56.29
O


ATOM
4057
OW0
HOH
Z
417
32.042
18.100
64.753
1.00
53.41
O


ATOM
4058
OW0
HOH
Z
418
30.544
21.851
3.348
1.00
49.80
O


ATOM
4059
OW0
HOH
Z
419
22.444
−4.502
33.538
1.00
43.58
O


ATOM
4060
OW0
HOH
Z
420
15.047
22.041
32.706
1.00
45.92
O


ATOM
4061
OW0
HOH
Z
421
29.257
25.725
56.322
1.00
40.75
O


ATOM
4062
OW0
HOH
Z
422
32.575
37.652
43.475
1.00
41.33
O


ATOM
4063
OW0
HOH
Z
423
37.131
38.600
50.665
1.00
44.87
O


ATOM
4064
OW0
HOH
Z
424
41.096
26.637
21.655
1.00
51.67
O


ATOM
4065
OW0
HOH
Z
425
26.571
38.214
31.343
1.00
46.55
O


ATOM
4066
OW0
HOH
Z
426
24.459
36.787
46.668
1.00
44.50
O


ATOM
4067
OW0
HOH
Z
427
25.441
−11.303
46.007
1.00
51.15
O


ATOM
4068
OW0
HOH
Z
428
46.170
14.110
31.720
1.00
39.70
O


ATOM
4069
OW0
HOH
Z
429
29.902
5.490
64.278
1.00
45.26
O


ATOM
4070
OW0
HOH
Z
430
12.331
32.728
34.937
1.00
52.97
O


ATOM
4071
OW0
HOH
Z
431
18.463
−9.869
42.087
1.00
44.05
O


ATOM
4072
OW0
HOH
Z
432
19.346
7.038
6.907
1.00
44.58
O


ATOM
4073
OW0
HOH
Z
433
9.947
32.080
6.486
1.00
48.15
O


ATOM
4074
OW0
HOH
Z
434
13.593
37.717
37.501
1.00
42.19
O


ATOM
4075
OW0
HOH
Z
435
−4.151
36.587
19.692
1.00
54.46
O


ATOM
4076
OW0
HOH
Z
436
46.660
11.419
22.542
1.00
54.74
O


ATOM
4077
OW0
HOH
Z
437
3.810
47.805
35.375
1.00
61.33
O


ATOM
4078
OW0
HOH
Z
438
37.872
−1.810
57.262
1.00
45.82
O


ATOM
4079
OW0
HOH
Z
439
36.643
16.851
59.689
1.00
52.24
O


ATOM
4080
OW0
HOH
Z
440
31.215
13.085
15.089
1.00
44.44
O


ATOM
4081
OW0
HOH
Z
441
31.115
16.489
12.583
1.00
46.55
O


ATOM
4082
OW0
HOH
Z
442
13.018
1.170
31.488
1.00
71.20
O


ATOM
4083
OW0
HOH
Z
443
28.936
33.840
39.024
1.00
57.61
O


ATOM
4084
OW0
HOH
Z
444
23.247
1.244
14.328
1.00
46.85
O


ATOM
4085
OW0
HOH
Z
445
13.213
32.167
10.184
1.00
42.76
O


ATOM
4086
OW0
HOH
Z
446
27.929
−6.168
61.609
1.00
45.29
O


ATOM
4087
OW0
HOH
Z
448
0.111
29.318
7.267
1.00
47.69
O


ATOM
4088
OW0
HOH
Z
449
33.521
26.325
56.999
1.00
44.66
O


ATOM
4089
OW0
HOH
Z
450
25.936
41.619
29.790
1.00
39.06
O


ATOM
4090
OW0
HOH
Z
451
43.840
1.243
37.210
1.00
49.42
O


ATOM
4091
OW0
HOH
Z
452
11.143
−7.541
50.997
1.00
43.90
O


ATOM
4092
OW0
HOH
Z
453
0.504
49.006
40.880
1.00
49.38
O


ATOM
4093
OW0
HOH
Z
454
49.382
22.778
22.490
1.00
50.62
O


ATOM
4094
OW0
HOH
Z
455
4.386
13.382
24.656
1.00
62.20
O


ATOM
4095
OW0
HOH
Z
456
22.642
16.253
62.524
1.00
40.21
O


ATOM
4096
OW0
HOH
Z
457
19.595
−2.565
63.161
1.00
54.59
O


ATOM
4097
OW0
HOH
Z
458
31.135
14.729
10.815
1.00
53.37
O


ATOM
4098
OW0
HOH
Z
459
15.020
−11.363
55.236
1.00
55.59
O


ATOM
4099
OW0
HOH
Z
460
11.933
28.886
34.221
1.00
49.32
O


ATOM
4100
OW0
HOH
Z
461
20.172
30.465
32.399
1.00
56.57
O


ATOM
4101
OW0
HOH
Z
462
11.248
32.686
4.270
1.00
45.49
O


ATOM
4102
OW0
HOH
Z
463
52.521
18.959
21.295
1.00
59.07
O


ATOM
4103
OW0
HOH
Z
464
5.334
34.592
30.241
1.00
63.41
O


ATOM
4104
OW0
HOH
Z
465
44.144
9.608
51.623
1.00
57.70
O


ATOM
4105
OW0
HOH
Z
466
37.097
21.260
13.439
1.00
52.51
O


ATOM
4106
OW0
HOH
Z
467
44.030
11.832
31.605
1.00
41.94
O


ATOM
4107
OW0
HOH
Z
468
34.117
35.918
18.044
1.00
44.68
O


ATOM
4108
OW0
HOH
Z
469
18.491
3.996
21.336
1.00
55.84
O


ATOM
4109
OW0
HOH
Z
471
29.303
8.886
20.237
1.00
53.15
O


ATOM
4110
OW0
HOH
Z
472
14.394
43.313
12.008
1.00
50.15
O


ATOM
4111
OW0
HOH
Z
473
23.952
51.031
33.322
1.00
54.98
O


ATOM
4112
OW0
HOH
Z
474
1.523
44.166
37.782
1.00
54.74
O


ATOM
4113
OW0
HOH
Z
475
24.759
18.478
−3.006
1.00
48.22
O


ATOM
4114
OW0
HOH
Z
476
12.952
37.928
39.944
1.00
39.92
O


ATOM
4115
OW0
HOH
Z
477
28.217
−2.061
20.941
1.00
50.36
O


ATOM
4116
OW0
HOH
Z
478
30.081
−3.165
57.599
1.00
44.63
O


ATOM
4117
OW0
HOH
Z
479
19.290
8.314
−1.363
1.00
55.01
O


ATOM
4118
OW0
HOH
Z
481
41.329
1.293
56.774
1.00
73.63
O


ATOM
4119
OW0
HOH
Z
482
44.221
6.919
35.599
1.00
52.10
O


ATOM
4120
OW0
HOH
Z
484
20.360
8.140
60.631
1.00
61.22
O


ATOM
4121
OW0
HOH
Z
485
11.293
41.055
12.455
1.00
51.10
O


ATOM
4122
OW0
HOH
Z
486
38.046
19.111
59.071
1.00
54.85
O


ATOM
4123
OW0
HOH
Z
487
31.249
33.416
15.195
1.00
53.18
O


ATOM
4124
OW0
HOH
Z
488
31.204
4.552
23.244
1.00
54.26
O


ATOM
4125
OW0
HOH
Z
489
30.921
−2.726
61.246
1.00
47.72
O


ATOM
4126
OW0
HOH
Z
490
14.235
−11.022
44.266
1.00
50.89
O


ATOM
4127
OW0
HOH
Z
491
4.881
23.737
15.186
1.00
53.86
O


ATOM
4128
OW0
HOH
Z
492
42.987
20.340
15.970
1.00
41.25
O


ATOM
4129
OW0
HOH
Z
493
6.931
24.571
18.740
1.00
46.69
O


ATOM
4130
OW0
HOH
Z
494
27.059
15.692
64.576
1.00
55.21
O


ATOM
4131
OW0
HOH
Z
496
−2.137
31.883
17.305
1.00
52.06
O


ATOM
4132
OW0
HOH
Z
497
16.583
10.141
−2.703
1.00
55.39
O


ATOM
4133
OW0
HOH
Z
498
29.765
11.212
3.701
1.00
45.51
O


ATOM
4134
OW0
HOH
Z
500
36.845
37.334
21.868
1.00
56.16
O


ATOM
4135
OW0
HOH
Z
501
32.478
9.326
7.561
1.00
51.65
O


ATOM
4136
OW0
HOH
Z
502
41.440
33.814
54.271
1.00
51.56
O


ATOM
4137
OW0
HOH
Z
503
15.629
19.817
31.255
1.00
46.43
O


ATOM
4138
OW0
HOH
Z
504
36.213
−4.072
40.780
1.00
52.48
O


ATOM
4139
OW0
HOH
Z
505
21.586
46.192
37.560
1.00
49.63
O


ATOM
4140
OW0
HOH
Z
506
20.992
20.522
38.327
1.00
49.64
O


ATOM
4141
OW0
HOH
Z
507
46.289
13.609
39.161
1.00
44.11
O


ATOM
4142
OW0
HOH
Z
508
46.618
15.202
18.151
1.00
55.74
O


ATOM
4143
OW0
HOH
Z
509
18.646
21.311
49.596
1.00
42.74
O


ATOM
4144
OW0
HOH
Z
510
33.117
5.574
24.893
1.00
58.41
O


ATOM
4145
OW0
HOH
Z
511
18.077
19.235
32.079
1.00
50.28
O


ATOM
4146
OW0
HOH
Z
512
13.592
51.634
46.901
1.00
53.90
O


ATOM
4147
OW0
HOH
Z
514
40.628
19.164
15.666
1.00
47.21
O


ATOM
4148
OW0
HOH
Z
515
26.567
32.671
35.413
1.00
53.85
O


ATOM
4149
OW0
HOH
Z
517
0.860
34.594
0.990
1.00
51.15
O


ATOM
4150
OW0
HOH
Z
518
21.869
18.466
−3.352
1.00
48.30
O


ATOM
4151
OW0
HOH
Z
519
14.655
4.120
14.381
1.00
59.21
O


ATOM
4152
OW0
HOH
Z
520
27.493
19.252
62.536
1.00
51.54
O


ATOM
4153
OW0
HOH
Z
521
26.107
29.405
−5.912
1.00
57.77
O


ATOM
4154
OW0
HOH
Z
523
24.095
33.282
7.056
1.00
56.77
O


ATOM
4155
OW0
HOH
Z
525
25.011
5.492
15.571
1.00
57.61
O


ATOM
4156
OW0
HOH
Z
526
46.978
36.267
24.404
1.00
62.44
O


ATOM
4157
OW0
HOH
Z
527
26.387
29.281
4.767
1.00
50.59
O


ATOM
4158
OW0
HOH
Z
528
29.687
38.296
31.604
1.00
60.44
O


ATOM
4159
OW0
HOH
Z
530
21.125
42.041
40.040
1.00
51.65
O


ATOM
4160
OW0
HOH
Z
531
26.717
20.913
56.908
1.00
18.75
O


ATOM
4161
OW0
HOH
Z
532
44.198
9.134
42.056
1.00
25.95
O


ATOM
4162
OW0
HOH
Z
534
40.793
7.373
60.743
1.00
50.90
O


ATOM
4163
OW0
HOH
Z
535
17.501
31.827
33.851
1.00
56.01
O


ATOM
4164
OW0
HOH
Z
536
6.030
22.869
3.287
1.00
54.63
O


ATOM
4165
OW0
HOH
Z
537
10.556
9.347
47.787
1.00
50.05
O


ATOM
4166
OW0
HOH
Z
538
15.353
16.546
−5.968
1.00
62.00
O


ATOM
4167
OW0
HOH
Z
539
19.481
22.979
35.392
1.00
46.36
O


ATOM
4168
OW0
HOH
Z
540
10.692
29.584
−4.152
1.00
51.33
O


ATOM
4169
OW0
HOH
Z
541
44.599
21.886
17.314
1.00
51.67
O


ATOM
4170
OW0
HOH
Z
542
22.147
25.599
−6.207
1.00
59.47
O


ATOM
4171
OW0
HOH
Z
543
3.884
2.935
39.688
1.00
59.44
O


ATOM
4172
OW0
HOH
Z
544
27.564
26.874
34.040
1.00
17.88
O


ATOM
4173
OW0
HOH
Z
545
4.793
5.591
43.427
1.00
66.19
O


ATOM
4174
OW0
HOH
Z
546
3.152
24.054
13.205
1.00
52.00
O


ATOM
4175
OW0
HOH
Z
547
15.692
46.446
42.589
1.00
51.31
O


ATOM
4176
OW0
HOH
Z
548
8.000
7.028
51.624
1.00
52.37
O


ATOM
4177
OW0
HOH
Z
549
35.215
−5.176
44.476
1.00
45.88
O


ATOM
4178
OW0
HOH
Z
550
16.928
4.221
30.356
1.00
66.82
O


ATOM
4179
OW0
HOH
Z
551
17.797
45.298
41.629
1.00
53.33
O


ATOM
4180
OW0
HOH
Z
552
25.483
41.413
33.816
1.00
53.83
O


ATOM
4181
OW0
HOH
Z
553
15.556
33.865
37.776
1.00
52.86
O


ATOM
4182
OW0
HOH
Z
554
27.337
−10.411
53.575
1.00
52.88
O


ATOM
4183
OW0
HOH
Z
555
45.968
11.887
34.801
1.00
49.96
O


ATOM
4184
OW0
HOH
Z
556
33.579
−0.659
59.497
1.00
61.78
O


ATOM
4185
OW0
HOH
Z
557
39.215
14.929
59.684
1.00
64.64
O


ATOM
4186
OW0
HOH
Z
559
4.022
23.837
29.725
1.00
58.44
O


ATOM
4187
OW0
HOH
Z
560
43.751
7.120
44.081
1.00
53.66
O


ATOM
4188
OW0
HOH
Z
561
26.890
30.995
33.381
1.00
19.60
O


ATOM
4189
OW0
HOH
Z
562
9.207
10.699
8.511
1.00
46.88
O


ATOM
4190
OW0
HOH
Z
563
20.032
15.557
15.518
1.00
51.24
O


ATOM
4191
OW0
HOH
Z
564
7.878
7.012
54.356
1.00
51.39
O


ATOM
4192
OW0
HOH
Z
566
10.276
20.805
3.467
1.00
51.83
O


ATOM
4193
OW0
HOH
Z
567
2.844
47.773
30.163
1.00
54.85
O


ATOM
4194
OW0
HOH
Z
568
24.328
−1.038
65.505
1.00
56.23
O


ATOM
4195
OW0
HOH
Z
569
5.510
14.287
26.944
1.00
64.54
O


ATOM
4196
OW0
HOH
Z
570
28.826
29.559
35.291
1.00
18.91
O


ATOM
4197
OW0
HOH
Z
571
30.590
7.060
30.452
1.00
37.05
O


ATOM
4198
OW0
HOH
Z
572
25.895
26.436
40.448
1.00
44.93
O


ATOM
4199
OW0
HOH
Z
573
7.981
47.102
29.714
1.00
42.60
O


ATOM
4200
OW0
HOH
Z
574
3.738
45.539
41.948
1.00
43.51
O


ATOM
4201
OW0
HOH
Z
575
15.872
52.569
32.650
1.00
43.50
O


ATOM
4202
OW0
HOH
Z
576
40.977
10.306
48.238
1.00
47.42
O


ATOM
4203
OW0
HOH
Z
577
31.615
12.687
4.974
1.00
54.35
O


ATOM
4204
OW0
HOH
Z
578
36.763
5.264
31.403
1.00
55.54
O


ATOM
4205
OW0
HOH
Z
579
20.058
27.099
25.492
1.00
52.07
O


ATOM
4206
OW0
HOH
Z
580
46.513
11.378
40.749
1.00
57.50
O


ATOM
4207
OW0
HOH
Z
581
24.468
−8.595
56.576
1.00
53.31
O


ATOM
4208
OW0
HOH
Z
582
42.920
13.084
49.055
1.00
69.61
O


ATOM
4209
OW0
HOH
Z
583
16.869
18.282
−7.940
1.00
61.38
O


ATOM
4210
OW0
HOH
Z
584
29.255
14.253
27.767
1.00
60.96
O


ATOM
4211
OW0
HOH
Z
586
42.338
2.629
60.950
1.00
55.14
O


ATOM
4212
OW0
HOH
Z
587
5.060
41.965
25.271
1.00
51.23
O


ATOM
4213
OW0
HOH
Z
588
22.095
10.890
12.872
1.00
62.83
O


ATOM
4214
OW0
HOH
Z
589
35.187
3.481
26.566
1.00
60.98
O


ATOM
4215
OW0
HOH
Z
590
21.325
45.254
34.133
1.00
58.44
O


ATOM
4216
OW0
HOH
Z
592
25.851
28.907
35.091
1.00
33.06
O


ATOM
4217
OW0
HOH
Z
593
30.294
32.534
55.904
1.00
52.54
O


ATOM
4218
OW0
HOH
Z
594
22.960
22.461
41.608
1.00
57.35
O


ATOM
4219
OW0
HOH
Z
595
35.665
31.696
55.608
1.00
62.87
O


ATOM
4220
OW0
HOH
Z
596
13.449
−11.478
53.120
1.00
61.95
O









Table 7 shows the coordinates of the crystal structure of E. coli ExoI bound to compound 10 that was identified in a screen according to the present invention. Compounds that bind prokaryotic exonucleases and that have crystal structures whose models substantially represent the atomic coordinates specified in Table 7, can be used for practicing the present invention.







TABLE 7





Coordinates of the crystal structure of E. coli Exol bound to compound 10
















REMARK
Written by O version 11.0.0


REMARK
Wed Apr  2 12:04:12 2008







CRYST1  52.671  91.939  103.081  90.00  90.00  90.00












ORIGX1
1.000000
0.000000
0.000000
0.00000



ORIGX2
0.000000
1.000000
0.000000
0.00000



ORIGX3
0.000000
0.000000
1.000000
0.00000



SCALE1
0.018986
0.000000
0.000000
0.00000



SCALE2
0.000000
0.010877
0.000000
0.00000



SCALE3
0.000000
0.000000
0.009701
0.00000



















ATOM
1
N
GLN
A
7
49.018
15.739
17.237
1.00
24.46
7


ATOM
2
CA
GLN
A
7
47.830
16.318
17.933
1.00
24.31
6


ATOM
3
CB
GLN
A
7
46.544
15.607
17.482
1.00
24.69
6


ATOM
4
CG
GLN
A
7
45.239
16.298
17.902
1.00
25.93
6


ATOM
5
CD
GLN
A
7
44.941
17.567
17.108
1.00
27.82
6


ATOM
6
OE1
GLN
A
7
45.555
17.830
16.069
1.00
28.38
8


ATOM
7
NE2
GLN
A
7
43.988
18.356
17.596
1.00
27.72
7


ATOM
8
C
GLN
A
7
47.998
16.229
19.449
1.00
23.82
6


ATOM
9
O
GLN
A
7
48.179
15.142
20.005
1.00
23.86
8


ATOM
10
N
GLN
A
8
47.955
17.383
20.109
1.00
23.00
7


ATOM
11
CA
GLN
A
8
48.120
17.451
21.554
1.00
22.42
6


ATOM
12
CB
GLN
A
8
48.937
18.696
21.947
1.00
22.71
6


ATOM
13
CG
GLN
A
8
48.107
19.966
22.161
1.00
23.51
6


ATOM
14
CD
GLN
A
8
48.940
21.241
22.139
1.00
23.89
6


ATOM
15
OE1
GLN
A
8
49.712
21.477
21.205
1.00
25.61
8


ATOM
16
NE2
GLN
A
8
48.767
22.082
23.158
1.00
23.84
7


ATOM
17
C
GLN
A
8
46.759
17.465
22.243
1.00
21.15
6


ATOM
18
O
GLN
A
8
45.751
17.855
21.642
1.00
21.30
8


ATOM
19
N
SER
A
9
46.736
17.043
23.504
1.00
19.81
7


ATOM
20
CA
SER
A
9
45.531
17.127
24.307
1.00
18.37
6


ATOM
21
CB
SER
A
9
45.670
16.289
25.574
1.00
18.76
6


ATOM
22
OG
SER
A
9
45.774
14.908
25.254
1.00
18.85
8


ATOM
23
C
SER
A
9
45.253
18.585
24.654
1.00
17.20
6


ATOM
24
O
SER
A
9
46.175
19.342
24.984
1.00
16.49
8


ATOM
25
N
THR
A
10
43.987
18.985
24.541
1.00
15.77
7


ATOM
26
CA
THR
A
10
43.577
20.347
24.902
1.00
14.81
6


ATOM
27
CB
THR
A
10
43.376
21.275
23.650
1.00
14.71
6


ATOM
28
OG1
THR
A
10
42.350
20.753
22.791
1.00
16.16
8


ATOM
29
CG2
THR
A
10
44.672
21.429
22.874
1.00
15.06
6


ATOM
30
C
THR
A
10
42.316
20.355
25.762
1.00
13.86
6


ATOM
31
O
THR
A
10
41.611
19.354
25.855
1.00
12.93
8


ATOM
32
N
PHE
A
11
42.072
21.491
26.412
1.00
12.98
7


ATOM
33
CA
PHE
A
11
40.811
21.757
27.082
1.00
12.52
6


ATOM
34
CB
PHE
A
11
41.059
22.241
28.513
1.00
12.52
6


ATOM
35
CG
PHE
A
11
41.543
21.175
29.438
1.00
12.02
6


ATOM
36
CD1
PHE
A
11
40.636
20.341
30.092
1.00
11.55
6


ATOM
37
CE1
PHE
A
11
41.078
19.360
30.962
1.00
14.18
6


ATOM
38
CZ
PHE
A
11
42.438
19.203
31.196
1.00
13.48
6


ATOM
39
CE2
PHE
A
11
43.355
20.032
30.557
1.00
13.73
6


ATOM
40
CD2
PHE
A
11
42.903
21.018
29.688
1.00
12.71
6


ATOM
41
C
PHE
A
11
40.093
22.847
26.321
1.00
12.33
6


ATOM
42
O
PHE
A
11
40.713
23.831
25.921
1.00
12.71
8


ATOM
43
N
LEU
A
12
38.795
22.665
26.096
1.00
11.52
7


ATOM
44
CA
LEU
A
12
37.965
23.748
25.588
1.00
11.19
6


ATOM
45
CB
LEU
A
12
37.265
23.363
24.276
1.00
11.40
6


ATOM
46
CG
LEU
A
12
36.596
24.520
23.514
1.00
12.89
6


ATOM
47
CD1
LEU
A
12
37.629
25.449
22.874
1.00
12.88
6


ATOM
48
CD2
LEU
A
12
35.657
23.989
22.468
1.00
14.11
6


ATOM
49
C
LEU
A
12
36.959
24.160
26.653
1.00
10.57
6


ATOM
50
O
LEU
A
12
35.951
23.485
26.876
1.00
10.17
8


ATOM
51
N
PHE
A
13
37.278
25.253
27.340
1.00
10.48
7


ATOM
52
CA
PHE
A
13
36.382
25.847
28.311
1.00
10.55
6


ATOM
53
CB
PHE
A
13
37.162
26.805
29.223
1.00
10.60
6


ATOM
54
CG
PHE
A
13
38.104
26.108
30.174
1.00
9.17
6


ATOM
55
CD1
PHE
A
13
37.705
25.808
31.480
1.00
9.71
6


ATOM
56
CE1
PHE
A
13
38.578
25.147
32.358
1.00
9.31
6


ATOM
57
CZ
PHE
A
13
39.852
24.775
31.937
1.00
9.96
6


ATOM
58
CE2
PHE
A
13
40.264
25.071
30.656
1.00
8.24
6


ATOM
59
CD2
PHE
A
13
39.380
25.733
29.768
1.00
8.18
6


ATOM
60
C
PHE
A
13
35.300
26.596
27.553
1.00
10.42
6


ATOM
61
O
PHE
A
13
35.594
27.305
26.584
1.00
11.02
8


ATOM
62
N
HIS
A
14
34.048
26.422
27.965
1.00
10.45
7


ATOM
63
CA
HIS
A
14
32.944
27.090
27.282
1.00
10.63
6


ATOM
64
CB
HIS
A
14
32.417
26.218
26.148
1.00
10.60
6


ATOM
65
CG
HIS
A
14
31.633
25.037
26.626
1.00
9.92
6


ATOM
66
ND1
HIS
A
14
30.254
24.986
26.578
1.00
12.95
7


ATOM
67
CE1
HIS
A
14
29.844
23.836
27.089
1.00
10.19
6


ATOM
68
NE2
HIS
A
14
30.903
23.145
27.467
1.00
10.83
7


ATOM
69
CD2
HIS
A
14
32.032
23.881
27.206
1.00
10.15
6


ATOM
70
C
HIS
A
14
31.797
27.434
28.210
1.00
10.83
6


ATOM
71
O
HIS
A
14
31.660
26.867
29.306
1.00
11.10
8


ATOM
72
N
ASP
A
15
30.955
28.351
27.745
1.00
11.37
7


ATOM
73
CA
ASP
A
15
29.776
28.773
28.486
1.00
11.71
6


ATOM
74
CB
ASP
A
15
30.161
29.825
29.524
1.00
12.27
6


ATOM
75
CG
ASP
A
15
29.045
30.118
30.500
1.00
13.18
6


ATOM
76
OD1
ASP
A
15
28.489
29.159
31.076
1.00
14.77
8


ATOM
77
OD2
ASP
A
15
28.728
31.316
30.698
1.00
15.12
8


ATOM
78
C
ASP
A
15
28.722
29.343
27.528
1.00
11.86
6


ATOM
79
O
ASP
A
15
29.061
30.065
26.575
1.00
11.63
8


ATOM
80
N
TYR
A
16
27.454
29.009
27.780
1.00
11.81
7


ATOM
81
CA
TYR
A
16
26.327
29.640
27.069
1.00
11.91
6


ATOM
82
CB
TYR
A
16
25.243
28.613
26.732
1.00
12.10
6


ATOM
83
CG
TYR
A
16
25.583
27.600
25.659
1.00
11.13
6


ATOM
84
CD1
TYR
A
16
25.346
27.873
24.308
1.00
11.76
6


ATOM
85
CE1
TYR
A
16
25.625
26.924
23.317
1.00
11.01
6


ATOM
86
CZ
TYR
A
16
26.139
25.682
23.688
1.00
11.35
6


ATOM
87
OH
TYR
A
16
26.427
24.734
22.728
1.00
11.33
8


ATOM
88
CE2
TYR
A
16
26.367
25.391
25.020
1.00
10.23
6


ATOM
89
CD2
TYR
A
16
26.085
26.344
25.998
1.00
11.77
6


ATOM
90
C
TYR
A
16
25.678
30.710
27.935
1.00
12.47
6


ATOM
91
O
TYR
A
16
25.557
30.544
29.146
1.00
12.24
8


ATOM
92
N
GLU
A
17
25.233
31.794
27.310
1.00
12.41
7


ATOM
93
CA
GLU
A
17
24.137
32.578
27.880
1.00
12.84
6


ATOM
94
CB
GLU
A
17
24.423
34.082
27.837
1.00
13.01
6


ATOM
95
CG
GLU
A
17
25.759
34.505
28.463
1.00
14.96
6


ATOM
96
CD
GLU
A
17
25.787
34.380
29.986
1.00
18.85
6


ATOM
97
OE1
GLU
A
17
24.713
34.341
30.620
1.00
19.07
8


ATOM
98
OE2
GLU
A
17
26.897
34.311
30.546
1.00
21.68
8


ATOM
99
C
GLU
A
17
22.911
32.243
27.049
1.00
12.28
6


ATOM
100
O
GLU
A
17
22.998
32.159
25.825
1.00
11.95
8


ATOM
101
N
THR
A
18
21.782
32.004
27.711
1.00
12.09
7


ATOM
102
CA
THR
A
18
20.561
31.608
27.010
1.00
11.78
6


ATOM
103
CB
THR
A
18
20.127
30.154
27.338
1.00
12.03
6


ATOM
104
OG1
THR
A
18
19.576
30.108
28.654
1.00
11.44
8


ATOM
105
CG2
THR
A
18
21.305
29.175
27.232
1.00
11.23
6


ATOM
106
C
THR
A
18
19.406
32.549
27.328
1.00
11.91
6


ATOM
107
O
THR
A
18
19.509
33.419
28.200
1.00
12.02
8


ATOM
108
N
PHE
A
19
18.300
32.361
26.620
1.00
11.86
7


ATOM
109
CA
PHE
A
19
17.111
33.173
26.828
1.00
12.22
6


ATOM
110
CB
PHE
A
19
16.438
33.464
25.485
1.00
12.24
6


ATOM
111
CG
PHE
A
19
17.136
34.516
24.692
1.00
12.23
6


ATOM
112
CD1
PHE
A
19
17.305
35.803
25.215
1.00
11.27
6


ATOM
113
CE1
PHE
A
19
17.969
36.799
24.481
1.00
12.54
6


ATOM
114
CZ
PHE
A
19
18.464
36.506
23.222
1.00
12.84
6


ATOM
115
CE2
PHE
A
19
18.300
35.230
22.687
1.00
13.20
6


ATOM
116
CD2
PHE
A
19
17.639
34.235
23.429
1.00
13.06
6


ATOM
117
C
PHE
A
19
16.136
32.557
27.836
1.00
12.67
6


ATOM
118
O
PHE
A
19
15.051
33.091
28.074
1.00
13.29
8


ATOM
119
N
GLY
A
20
16.544
31.457
28.461
1.00
13.25
7


ATOM
120
CA
GLY
A
20
15.726
30.830
29.500
1.00
14.08
6


ATOM
121
C
GLY
A
20
16.365
29.605
30.119
1.00
14.32
6


ATOM
122
O
GLY
A
20
17.464
29.197
29.727
1.00
14.46
8


ATOM
123
N
THR
A
21
15.654
28.993
31.062
1.00
14.83
7


ATOM
124
CA
THR
A
21
16.214
27.901
31.872
1.00
15.80
6


ATOM
125
CB
THR
A
21
15.575
27.827
33.293
1.00
15.79
6


ATOM
126
OG1
THR
A
21
14.147
27.766
33.190
1.00
17.19
8


ATOM
127
CG2
THR
A
21
15.992
29.022
34.165
1.00
17.19
6


ATOM
128
C
THR
A
21
16.084
26.523
31.227
1.00
15.42
6


ATOM
129
O
THR
A
21
16.817
25.606
31.584
1.00
15.27
8


ATOM
130
N
HIS
A
22
15.135
26.370
30.306
1.00
15.74
7


ATOM
131
CA
HIS
A
22
14.893
25.066
29.684
1.00
16.15
6


ATOM
132
CB
HIS
A
22
13.440
24.945
29.225
1.00
16.16
6


ATOM
133
CG
HIS
A
22
12.998
23.534
28.986
1.00
16.41
6


ATOM
134
ND1
HIS
A
22
11.971
22.945
29.694
1.00
17.55
7


ATOM
135
CE1
HIS
A
22
11.805
21.702
29.273
1.00
18.23
6


ATOM
136
NE2
HIS
A
22
12.695
21.460
28.326
1.00
17.96
7


ATOM
137
CD2
HIS
A
22
13.457
22.588
28.132
1.00
16.94
6


ATOM
138
C
HIS
A
22
15.859
24.827
28.519
1.00
16.60
6


ATOM
139
O
HIS
A
22
15.827
25.556
27.522
1.00
16.53
8


ATOM
140
N
PRO
A
23
16.727
23.796
28.644
1.00
17.14
7


ATOM
141
CA
PRO
A
23
17.791
23.552
27.661
1.00
17.15
6


ATOM
142
CB
PRO
A
23
18.491
22.297
28.199
1.00
17.23
6


ATOM
143
CG
PRO
A
23
18.096
22.196
29.625
1.00
17.52
6


ATOM
144
CD
PRO
A
23
16.733
22.794
29.722
1.00
17.32
6


ATOM
145
C
PRO
A
23
17.254
23.279
26.257
1.00
17.00
6


ATOM
146
O
PRO
A
23
17.957
23.518
25.271
1.00
17.62
8


ATOM
147
N
ALA
A
24
16.013
22.799
26.175
1.00
16.75
7


ATOM
148
CA
ALA
A
24
15.382
22.442
24.902
1.00
16.60
6


ATOM
149
CB
ALA
A
24
14.682
21.096
25.022
1.00
16.72
6


ATOM
150
C
ALA
A
24
14.405
23.497
24.374
1.00
16.34
6


ATOM
151
O
ALA
A
24
14.411
23.807
23.177
1.00
17.23
8


ATOM
152
N
LEU
A
25
13.571
24.039
25.264
1.00
15.74
7


ATOM
153
CA
LEU
A
25
12.443
24.894
24.863
1.00
14.72
6


ATOM
154
CB
LEU
A
25
11.207
24.588
25.715
1.00
15.02
6


ATOM
155
CG
LEU
A
25
10.619
23.178
25.556
1.00
16.37
6


ATOM
156
CD1
LEU
A
25
9.476
22.944
26.541
1.00
17.06
6


ATOM
157
CD2
LEU
A
25
10.164
22.927
24.121
1.00
17.74
6


ATOM
158
C
LEU
A
25
12.758
26.391
24.896
1.00
14.10
6


ATOM
159
O
LEU
A
25
11.990
27.211
24.380
1.00
13.80
8


ATOM
160
N
ASP
A
26
13.880
26.738
25.507
1.00
12.91
7


ATOM
161
CA
ASP
A
26
14.400
28.093
25.426
1.00
12.72
6


ATOM
162
CB
ASP
A
26
14.805
28.583
26.811
1.00
12.47
6


ATOM
163
CG
ASP
A
26
13.604
28.886
27.683
1.00
12.52
6


ATOM
164
OD1
ASP
A
26
12.746
29.681
27.242
1.00
13.57
8


ATOM
165
OD2
ASP
A
26
13.519
28.339
28.814
1.00
14.49
8


ATOM
166
C
ASP
A
26
15.583
28.102
24.479
1.00
12.67
6


ATOM
167
O
ASP
A
26
16.211
27.070
24.271
1.00
13.61
8


ATOM
168
N
ARG
A
27
15.864
29.260
23.886
1.00
12.50
7


ATOM
169
CA
ARG
A
27
16.893
29.364
22.854
1.00
12.20
6


ATOM
170
CB
ARG
A
27
16.396
30.204
21.662
1.00
12.54
6


ATOM
171
CG
ARG
A
27
14.996
29.860
21.135
1.00
12.35
6


ATOM
172
CD
ARG
A
27
14.897
28.450
20.545
1.00
12.86
6


ATOM
173
NE
ARG
A
27
13.506
28.000
20.484
1.00
13.60
7


ATOM
174
CZ
ARG
A
27
12.628
28.370
19.548
1.00
12.96
6


ATOM
175
NH1
ARG
A
27
12.988
29.206
18.581
1.00
12.94
7


ATOM
176
NH2
ARG
A
27
11.380
27.915
19.593
1.00
13.40
7


ATOM
177
C
ARG
A
27
18.176
29.972
23.423
1.00
12.27
6


ATOM
178
O
ARG
A
27
18.123
30.804
24.331
1.00
12.51
8


ATOM
179
N
PRO
A
28
19.337
29.573
22.874
1.00
11.85
7


ATOM
180
CA
PRO
A
28
20.615
30.147
23.299
1.00
11.63
6


ATOM
181
CB
PRO
A
28
21.641
29.264
22.582
1.00
11.77
6


ATOM
182
CG
PRO
A
28
20.919
28.789
21.356
1.00
11.13
6


ATOM
183
CD
PRO
A
28
19.511
28.573
21.803
1.00
11.90
6


ATOM
184
C
PRO
A
28
20.742
31.599
22.834
1.00
11.77
6


ATOM
185
O
PRO
A
28
20.088
31.989
21.864
1.00
12.13
8


ATOM
186
N
ALA
A
29
21.562
32.388
23.528
1.00
11.15
7


ATOM
187
CA
ALA
A
29
21.807
33.774
23.142
1.00
12.03
6


ATOM
188
CB
ALA
A
29
21.475
34.719
24.283
1.00
11.55
6


ATOM
189
C
ALA
A
29
23.246
33.980
22.694
1.00
11.81
6


ATOM
190
O
ALA
A
29
23.504
34.637
21.693
1.00
12.43
8


ATOM
191
N
GLN
A
30
24.183
33.421
23.455
1.00
12.09
7


ATOM
192
CA
GLN
A
30
25.595
33.668
23.240
1.00
12.07
6


ATOM
193
CB
GLN
A
30
26.028
34.870
24.083
1.00
12.59
6


ATOM
194
CG
GLN
A
30
27.437
35.367
23.838
1.00
13.47
6


ATOM
195
CD
GLN
A
30
27.927
36.215
24.984
1.00
14.83
6


ATOM
196
OE1
GLN
A
30
28.061
35.733
26.106
1.00
16.56
8


ATOM
197
NE2
GLN
A
30
28.184
37.484
24.716
1.00
15.99
7


ATOM
198
C
GLN
A
30
26.385
32.426
23.640
1.00
12.09
6


ATOM
199
O
GLN
A
30
26.045
31.753
24.613
1.00
11.17
8


ATOM
200
N
PHE
A
31
27.438
32.139
22.882
1.00
11.30
7


ATOM
201
CA
PHE
A
31
28.379
31.072
23.200
1.00
11.89
6


ATOM
202
CB
PHE
A
31
28.444
30.078
22.034
1.00
12.06
6


ATOM
203
CG
PHE
A
31
29.481
28.995
22.198
1.00
11.91
6


ATOM
204
CD1
PHE
A
31
29.169
27.804
22.851
1.00
12.42
6


ATOM
205
CE1
PHE
A
31
30.120
26.791
22.992
1.00
11.85
6


ATOM
206
CZ
PHE
A
31
31.397
26.951
22.450
1.00
12.35
6


ATOM
207
CE2
PHE
A
31
31.716
28.124
21.771
1.00
11.72
6


ATOM
208
CD2
PHE
A
31
30.758
29.142
21.648
1.00
11.50
6


ATOM
209
C
PHE
A
31
29.743
31.709
23.395
1.00
12.10
6


ATOM
210
O
PHE
A
31
30.140
32.560
22.605
1.00
11.84
8


ATOM
211
N
ALA
A
32
30.452
31.309
24.452
1.00
12.21
7


ATOM
212
CA
ALA
A
32
31.811
31.801
24.688
1.00
12.39
6


ATOM
213
CB
ALA
A
32
31.831
32.816
25.826
1.00
12.54
6


ATOM
214
C
ALA
A
32
32.728
30.634
24.996
1.00
12.38
6


ATOM
215
O
ALA
A
32
32.351
29.720
25.724
1.00
12.73
8


ATOM
216
N
ALA
A
33
33.928
30.654
24.422
1.00
12.31
7


ATOM
217
CA
ALA
A
33
34.885
29.565
24.637
1.00
11.94
6


ATOM
218
CB
ALA
A
33
34.574
28.405
23.715
1.00
12.28
6


ATOM
219
C
ALA
A
33
36.328
30.003
24.449
1.00
11.89
6


ATOM
220
O
ALA
A
33
36.606
31.015
23.807
1.00
12.03
8


ATOM
221
N
ILE
A
34
37.245
29.229
25.016
1.00
11.36
7


ATOM
222
CA
ILE
A
34
38.667
29.395
24.730
1.00
11.33
6


ATOM
223
CB
ILE
A
34
39.299
30.571
25.532
1.00
11.33
6


ATOM
224
CG1
ILE
A
34
40.464
31.201
24.749
1.00
10.79
6


ATOM
225
CD1
ILE
A
34
40.945
32.519
25.330
1.00
12.13
6


ATOM
226
CG2
ILE
A
34
39.748
30.123
26.903
1.00
12.48
6


ATOM
227
C
ILE
A
34
39.404
28.088
24.976
1.00
10.94
6


ATOM
228
O
ILE
A
34
39.032
27.316
25.854
1.00
10.90
8


ATOM
229
N
ARG
A
35
40.446
27.847
24.181
1.00
10.73
7


ATOM
230
CA
ARG
A
35
41.194
26.603
24.237
1.00
10.86
6


ATOM
231
CB
ARG
A
35
41.493
26.100
22.822
1.00
10.71
6


ATOM
232
CG
ARG
A
35
41.842
24.629
22.751
1.00
10.78
6


ATOM
233
CD
ARG
A
35
42.094
24.195
21.314
1.00
10.27
6


ATOM
234
NE
ARG
A
35
40.858
24.172
20.530
1.00
11.64
7


ATOM
235
CZ
ARG
A
35
39.989
23.166
20.525
1.00
11.78
6


ATOM
236
NH1
ARG
A
35
40.200
22.092
21.278
1.00
13.11
7


ATOM
237
NH2
ARG
A
35
38.899
23.238
19.773
1.00
13.03
7


ATOM
238
C
ARG
A
35
42.499
26.794
24.990
1.00
11.01
6


ATOM
239
O
ARG
A
35
43.199
27.785
24.792
1.00
10.81
8


ATOM
240
N
THR
A
36
42.821
25.835
25.851
1.00
11.74
7


ATOM
241
CA
THR
A
36
44.089
25.843
26.579
1.00
11.91
6


ATOM
242
CB
THR
A
36
43.896
25.976
28.114
1.00
12.23
6


ATOM
243
OG1
THR
A
36
43.503
24.715
28.658
1.00
11.98
8


ATOM
244
CG2
THR
A
36
42.868
27.059
28.480
1.00
10.73
6


ATOM
245
C
THR
A
36
44.825
24.536
26.330
1.00
12.22
6


ATOM
246
O
THR
A
36
44.229
23.551
25.899
1.00
12.29
8


ATOM
247
N
ASP
A
37
46.118
24.524
26.629
1.00
12.85
7


ATOM
248
CA
ASP
A
37
46.894
23.290
26.608
1.00
13.49
6


ATOM
249
CB
ASP
A
37
48.398
23.585
26.428
1.00
13.79
6


ATOM
250
CG
ASP
A
37
49.045
24.213
27.668
1.00
13.71
6


ATOM
251
OD1
ASP
A
37
48.405
24.279
28.736
1.00
15.96
8


ATOM
252
OD2
ASP
A
37
50.219
24.636
27.563
1.00
15.49
8


ATOM
253
C
ASP
A
37
46.618
22.449
27.864
1.00
14.23
6


ATOM
254
O
ASP
A
37
45.781
22.817
28.701
1.00
13.85
8


ATOM
255
N
SER
A
38
47.325
21.330
27.991
1.00
14.98
7


ATOM
256
CA
SER
A
38
47.087
20.382
29.083
1.00
15.89
6


ATOM
257
CB
SER
A
38
47.934
19.125
28.881
1.00
15.96
6


ATOM
258
OG
SER
A
38
49.310
19.460
28.885
1.00
17.21
8


ATOM
259
C
SER
A
38
47.362
20.988
30.464
1.00
16.06
6


ATOM
260
O
SER
A
38
46.896
20.465
31.480
1.00
16.84
8


ATOM
261
N
GLU
A
39
48.099
22.102
30.485
1.00
16.50
7


ATOM
262
CA
GLU
A
39
48.467
22.799
31.727
1.00
16.83
6


ATOM
263
CB
GLU
A
39
49.970
23.104
31.729
1.00
17.33
6


ATOM
264
CG
GLU
A
39
50.853
21.861
31.841
1.00
20.17
6


ATOM
265
CD
GLU
A
39
50.625
21.092
33.140
1.00
23.25
6


ATOM
266
OE1
GLU
A
39
50.540
21.734
34.213
1.00
25.80
8


ATOM
267
OE2
GLU
A
39
50.525
19.847
33.087
1.00
25.70
8


ATOM
268
C
GLU
A
39
47.658
24.091
31.951
1.00
16.45
6


ATOM
269
O
GLU
A
39
47.977
24.895
32.844
1.00
16.80
8


ATOM
270
N
PHE
A
40
46.605
24.267
31.152
1.00
15.76
7


ATOM
271
CA
PHE
A
40
45.692
25.426
31.253
1.00
15.42
6


ATOM
272
CB
PHE
A
40
45.114
25.575
32.668
1.00
15.00
6


ATOM
273
CG
PHE
A
40
44.362
24.362
33.153
1.00
15.57
6


ATOM
274
CD1
PHE
A
40
43.392
23.758
32.356
1.00
15.31
6


ATOM
275
CE1
PHE
A
40
42.692
22.639
32.805
1.00
15.59
6


ATOM
276
CZ
PHE
A
40
42.953
22.119
34.059
1.00
16.22
6


ATOM
277
CE2
PHE
A
40
43.921
22.714
34.869
1.00
16.87
6


ATOM
278
CD2
PHE
A
40
44.613
23.837
34.413
1.00
16.55
6


ATOM
279
C
PHE
A
40
46.282
26.756
30.764
1.00
15.13
6


ATOM
280
O
PHE
A
40
45.752
27.834
31.071
1.00
15.01
8


ATOM
281
N
ASN
A
41
47.356
26.674
29.983
1.00
14.93
7


ATOM
282
CA
ASN
A
41
47.868
27.839
29.260
1.00
14.96
6


ATOM
283
CB
ASN
A
41
49.299
27.592
28.772
1.00
14.97
6


ATOM
284
CG
ASN
A
41
50.260
27.284
29.900
1.00
15.95
6


ATOM
285
OD1
ASN
A
41
50.959
26.271
29.866
1.00
17.21
8


ATOM
286
ND2
ASN
A
41
50.298
28.152
30.909
1.00
15.72
7


ATOM
287
C
ASN
A
41
46.993
28.142
28.060
1.00
14.99
6


ATOM
288
O
ASN
A
41
46.815
27.290
27.191
1.00
14.78
8


ATOM
289
N
VAL
A
42
46.468
29.363
28.000
1.00
15.05
7


ATOM
290
CA
VAL
A
42
45.619
29.765
26.888
1.00
15.32
6


ATOM
291
CB
VAL
A
42
45.033
31.178
27.096
1.00
15.10
6


ATOM
292
CG1
VAL
A
42
44.346
31.669
25.825
1.00
15.35
6


ATOM
293
CG2
VAL
A
42
44.068
31.187
28.275
1.00
15.41
6


ATOM
294
C
VAL
A
42
46.408
29.697
25.581
1.00
15.38
6


ATOM
295
O
VAL
A
42
47.478
30.297
25.459
1.00
15.29
8


ATOM
296
N
ILE
A
43
45.896
28.926
24.625
1.00
15.85
7


ATOM
297
CA
ILE
A
43
46.567
28.776
23.325
1.00
16.32
6


ATOM
298
CB
ILE
A
43
47.081
27.321
23.091
1.00
16.48
6


ATOM
299
CG1
ILE
A
43
45.913
26.331
23.076
1.00
16.39
6


ATOM
300
CD1
ILE
A
43
46.284
24.925
22.619
1.00
16.03
6


ATOM
301
CG2
ILE
A
43
48.123
26.938
24.154
1.00
17.05
6


ATOM
302
C
ILE
A
43
45.705
29.225
22.140
1.00
16.88
6


ATOM
303
O
ILE
A
43
46.197
29.338
21.021
1.00
16.85
8


ATOM
304
N
GLY
A
44
44.421
29.475
22.391
1.00
17.13
7


ATOM
305
CA
GLY
A
44
43.516
29.927
21.337
1.00
17.42
6


ATOM
306
C
GLY
A
44
43.099
31.375
21.489
1.00
17.66
6


ATOM
307
O
GLY
A
44
43.445
32.033
22.475
1.00
18.18
8


ATOM
308
N
GLU
A
45
42.361
31.873
20.501
1.00
17.81
7


ATOM
309
CA
GLU
A
45
41.732
33.190
20.587
1.00
18.17
6


ATOM
310
CB
GLU
A
45
41.596
33.817
19.191
1.00
18.33
6


ATOM
311
CG
GLU
A
45
42.914
34.053
18.453
1.00
21.00
6


ATOM
312
CD
GLU
A
45
43.857
34.975
19.204
1.00
23.60
6


ATOM
313
OE1
GLU
A
45
43.477
36.137
19.471
1.00
25.01
8


ATOM
314
OE2
GLU
A
45
44.985
34.537
19.524
1.00
26.07
8


ATOM
315
C
GLU
A
45
40.351
33.025
21.202
1.00
17.41
6


ATOM
316
O
GLU
A
45
39.724
31.978
21.030
1.00
17.70
8


ATOM
317
N
PRO
A
46
39.867
34.051
21.930
1.00
17.19
7


ATOM
318
CA
PRO
A
46
38.490
33.992
22.437
1.00
16.54
6


ATOM
319
CB
PRO
A
46
38.288
35.385
23.042
1.00
17.03
6


ATOM
320
CG
PRO
A
46
39.663
35.797
23.461
1.00
17.48
6


ATOM
321
CD
PRO
A
46
40.552
35.286
22.356
1.00
16.95
6


ATOM
322
C
PRO
A
46
37.494
33.760
21.303
1.00
16.32
6


ATOM
323
O
PRO
A
46
37.587
34.413
20.257
1.00
15.63
8


ATOM
324
N
GLU
A
47
36.583
32.807
21.501
1.00
15.53
7


ATOM
325
CA
GLU
A
47
35.528
32.511
20.532
1.00
15.92
6


ATOM
326
CB
GLU
A
47
35.518
31.020
20.185
1.00
16.37
6


ATOM
327
CG
GLU
A
47
36.816
30.510
19.546
1.00
17.60
6


ATOM
328
CD
GLU
A
47
36.831
30.639
18.030
1.00
21.42
6


ATOM
329
OE1
GLU
A
47
35.890
31.228
17.459
1.00
21.52
8


ATOM
330
OE2
GLU
A
47
37.795
30.146
17.407
1.00
23.79
8


ATOM
331
C
GLU
A
47
34.182
32.916
21.111
1.00
15.64
6


ATOM
332
O
GLU
A
47
33.623
32.211
21.953
1.00
15.54
8


ATOM
333
N
VAL
A
48
33.668
34.056
20.662
1.00
15.23
7


ATOM
334
CA
VAL
A
48
32.434
34.625
21.217
1.00
15.21
6


ATOM
335
CB
VAL
A
48
32.702
35.928
22.024
1.00
15.39
6


ATOM
336
CG1
VAL
A
48
31.393
36.557
22.498
1.00
15.74
6


ATOM
337
CG2
VAL
A
48
33.632
35.660
23.213
1.00
15.26
6


ATOM
338
C
VAL
A
48
31.486
34.951
20.085
1.00
14.78
6


ATOM
339
O
VAL
A
48
31.820
35.729
19.202
1.00
14.93
8


ATOM
340
N
PHE
A
49
30.304
34.349
20.105
1.00
14.42
7


ATOM
341
CA
PHE
A
49
29.315
34.650
19.086
1.00
14.02
6


ATOM
342
CB
PHE
A
49
29.599
33.889
17.779
1.00
14.23
6


ATOM
343
CG
PHE
A
49
29.882
32.431
17.970
1.00
14.42
6


ATOM
344
CD1
PHE
A
49
28.873
31.496
17.838
1.00
14.89
6


ATOM
345
CE1
PHE
A
49
29.130
30.142
18.014
1.00
15.80
6


ATOM
346
CZ
PHE
A
49
30.420
29.715
18.311
1.00
14.95
6


ATOM
347
CE2
PHE
A
49
31.438
30.642
18.440
1.00
14.78
6


ATOM
348
CD2
PHE
A
49
31.171
31.990
18.268
1.00
14.37
6


ATOM
349
C
PHE
A
49
27.889
34.449
19.557
1.00
13.54
6


ATOM
350
O
PHE
A
49
27.637
33.841
20.611
1.00
12.57
8


ATOM
351
N
TYR
A
50
26.962
34.990
18.772
1.00
13.19
7


ATOM
352
CA
TYR
A
50
25.558
35.064
19.149
1.00
13.13
6


ATOM
353
CB
TYR
A
50
25.058
36.504
19.045
1.00
13.64
6


ATOM
354
CG
TYR
A
50
25.693
37.443
20.029
1.00
14.49
6


ATOM
355
CD1
TYR
A
50
25.050
37.765
21.219
1.00
15.09
6


ATOM
356
CE1
TYR
A
50
25.621
38.640
22.129
1.00
16.62
6


ATOM
357
CZ
TYR
A
50
26.851
39.198
21.857
1.00
16.15
6


ATOM
358
OH
TYR
A
50
27.417
40.065
22.761
1.00
17.68
8


ATOM
359
CE2
TYR
A
50
27.515
38.900
20.678
1.00
16.01
6


ATOM
360
CD2
TYR
A
50
26.932
38.024
19.769
1.00
15.85
6


ATOM
361
C
TYR
A
50
24.712
34.191
18.259
1.00
12.63
6


ATOM
362
O
TYR
A
50
25.107
33.857
17.126
1.00
12.64
8


ATOM
363
N
CYS
A
51
23.537
33.839
18.768
1.00
12.47
7


ATOM
364
CA
CYS
A
51
22.558
33.087
18.008
1.00
12.46
6


ATOM
365
CB
CYS
A
51
22.187
31.802
18.743
1.00
12.80
6


ATOM
366
SG
CYS
A
51
21.278
30.670
17.717
1.00
12.66
16


ATOM
367
C
CYS
A
51
21.308
33.922
17.794
1.00
12.59
6


ATOM
368
O
CYS
A
51
20.689
34.384
18.761
1.00
12.01
8


ATOM
369
N
LYS
A
52
20.948
34.121
16.527
1.00
12.54
7


ATOM
370
CA
LYS
A
52
19.672
34.742
16.164
1.00
12.82
6


ATOM
371
CB
LYS
A
52
19.562
34.883
14.650
1.00
12.80
6


ATOM
372
CG
LYS
A
52
20.423
35.954
14.034
1.00
14.17
6


ATOM
373
CD
LYS
A
52
20.272
35.944
12.518
1.00
17.60
6


ATOM
374
CE
LYS
A
52
18.818
35.924
12.105
1.00
18.27
6


ATOM
375
NZ
LYS
A
52
18.058
37.111
12.605
1.00
22.27
7


ATOM
376
C
LYS
A
52
18.502
33.883
16.629
1.00
12.59
6


ATOM
377
O
LYS
A
52
18.412
32.714
16.249
1.00
12.46
8


ATOM
378
N
PRO
A
53
17.586
34.462
17.433
1.00
12.78
7


ATOM
379
CA
PRO
A
53
16.369
33.712
17.761
1.00
12.96
6


ATOM
380
CB
PRO
A
53
15.841
34.413
19.019
1.00
12.61
6


ATOM
381
CG
PRO
A
53
16.375
35.826
18.940
1.00
13.03
6


ATOM
382
CD
PRO
A
53
17.623
35.796
18.062
1.00
12.66
6


ATOM
383
C
PRO
A
53
15.356
33.791
16.620
1.00
13.24
6


ATOM
384
O
PRO
A
53
15.181
34.860
16.022
1.00
13.74
8


ATOM
385
N
ALA
A
54
14.721
32.662
16.299
1.00
13.78
7


ATOM
386
CA
ALA
A
54
13.668
32.636
15.274
1.00
13.43
6


ATOM
387
CB
ALA
A
54
13.350
31.213
14.871
1.00
13.87
6


ATOM
388
C
ALA
A
54
12.413
33.343
15.780
1.00
13.62
6


ATOM
389
O
ALA
A
54
12.250
33.543
16.982
1.00
13.41
8


ATOM
390
N
ASP
A
55
11.526
33.720
14.862
1.00
13.35
7


ATOM
391
CA
ASP
A
55
10.387
34.570
15.221
1.00
13.69
6


ATOM
392
CB
ASP
A
55
9.940
35.426
14.027
1.00
14.38
6


ATOM
393
CG
ASP
A
55
9.390
34.595
12.872
1.00
15.75
6


ATOM
394
OD1
ASP
A
55
9.209
33.365
13.021
1.00
17.62
8


ATOM
395
OD2
ASP
A
55
9.142
35.186
11.801
1.00
19.79
8


ATOM
396
C
ASP
A
55
9.197
33.817
15.834
1.00
13.17
6


ATOM
397
O
ASP
A
55
8.082
34.349
15.896
1.00
12.92
8


ATOM
398
N
ASP
A
56
9.433
32.586
16.282
1.00
12.57
7


ATOM
399
CA
ASP
A
56
8.391
31.813
16.959
1.00
12.30
6


ATOM
400
CB
ASP
A
56
8.281
30.395
16.360
1.00
12.51
6


ATOM
401
CG
ASP
A
56
9.547
29.562
16.561
1.00
12.79
6


ATOM
402
OD1
ASP
A
56
10.628
30.142
16.802
1.00
15.49
8


ATOM
403
OD2
ASP
A
56
9.454
28.319
16.491
1.00
15.56
8


ATOM
404
C
ASP
A
56
8.639
31.749
18.469
1.00
12.36
6


ATOM
405
O
ASP
A
56
8.087
30.906
19.159
1.00
12.42
8


ATOM
406
N
TYR
A
57
9.456
32.666
18.977
1.00
12.11
7


ATOM
407
CA
TYR
A
57
9.928
32.561
20.350
1.00
12.08
6


ATOM
408
CB
TYR
A
57
11.270
31.823
20.370
1.00
11.87
6


ATOM
409
CG
TYR
A
57
11.913
31.708
21.732
1.00
11.72
6


ATOM
410
CD1
TYR
A
57
11.494
30.740
22.643
1.00
10.75
6


ATOM
411
CE1
TYR
A
57
12.091
30.633
23.892
1.00
9.98
6


ATOM
412
CZ
TYR
A
57
13.129
31.494
24.229
1.00
11.16
6


ATOM
413
OH
TYR
A
57
13.727
31.405
25.456
1.00
12.73
8


ATOM
414
CE2
TYR
A
57
13.566
32.457
23.335
1.00
11.39
6


ATOM
415
CD2
TYR
A
57
12.966
32.557
22.102
1.00
10.42
6


ATOM
416
C
TYR
A
57
10.053
33.915
21.034
1.00
12.15
6


ATOM
417
O
TYR
A
57
10.518
34.879
20.435
1.00
12.56
8


ATOM
418
N
LEU
A
58
9.626
33.978
22.296
1.00
12.41
7


ATOM
419
CA
LEU
A
58
9.932
35.124
23.157
1.00
12.34
6


ATOM
420
CB
LEU
A
58
8.657
35.801
23.663
1.00
12.56
6


ATOM
421
CG
LEU
A
58
7.849
36.615
22.648
1.00
13.12
6


ATOM
422
CD1
LEU
A
58
6.564
37.099
23.282
1.00
14.03
6


ATOM
423
CD2
LEU
A
58
8.656
37.789
22.112
1.00
13.18
6


ATOM
424
C
LEU
A
58
10.793
34.685
24.335
1.00
12.26
6


ATOM
425
O
LEU
A
58
10.521
33.660
24.952
1.00
11.94
8


ATOM
426
N
PRO
A
59
11.844
35.459
24.644
1.00
12.22
7


ATOM
427
CA
PRO
A
59
12.736
35.072
25.734
1.00
12.23
6


ATOM
428
CB
PRO
A
59
13.884
36.082
25.623
1.00
12.06
6


ATOM
429
CG
PRO
A
59
13.311
37.245
24.891
1.00
12.45
6


ATOM
430
CD
PRO
A
59
12.250
36.725
24.001
1.00
12.21
6


ATOM
431
C
PRO
A
59
12.057
35.174
27.099
1.00
12.77
6


ATOM
432
O
PRO
A
59
11.108
35.944
27.262
1.00
12.39
8


ATOM
433
N
GLN
A
60
12.523
34.379
28.061
1.00
12.95
7


ATOM
434
CA
GLN
A
60
12.093
34.545
29.445
1.00
14.10
6


ATOM
435
CB
GLN
A
60
12.576
33.378
30.318
1.00
14.10
6


ATOM
436
CG
GLN
A
60
11.984
32.027
29.929
1.00
15.57
6


ATOM
437
CD
GLN
A
60
12.275
30.909
30.930
1.00
17.12
6


ATOM
438
OE1
GLN
A
60
13.120
31.046
31.829
1.00
20.38
8


ATOM
439
NE2
GLN
A
60
11.582
29.783
30.765
1.00
20.41
7


ATOM
440
C
GLN
A
60
12.662
35.868
29.958
1.00
14.35
6


ATOM
441
O
GLN
A
60
13.874
36.065
29.920
1.00
13.24
8


ATOM
442
N
PRO
A
61
11.780
36.798
30.400
1.00
14.55
7


ATOM
443
CA
PRO
A
61
12.245
38.095
30.899
1.00
14.97
6


ATOM
444
CB
PRO
A
61
10.960
38.738
31.447
1.00
14.94
6


ATOM
445
CG
PRO
A
61
9.871
38.134
30.632
1.00
14.83
6


ATOM
446
CD
PRO
A
61
10.306
36.700
30.420
1.00
14.84
6


ATOM
447
C
PRO
A
61
13.303
37.976
32.007
1.00
15.13
6


ATOM
448
O
PRO
A
61
14.235
38.783
32.062
1.00
15.62
8


ATOM
449
N
GLY
A
62
13.162
36.971
32.868
1.00
15.59
7


ATOM
450
CA
GLY
A
62
14.108
36.748
33.949
1.00
16.07
6


ATOM
451
C
GLY
A
62
15.521
36.466
33.476
1.00
16.38
6


ATOM
452
O
GLY
A
62
16.493
36.860
34.132
1.00
17.16
8


ATOM
453
N
ALA
A
63
15.635
35.788
32.332
1.00
16.40
7


ATOM
454
CA
ALA
A
63
16.937
35.432
31.758
1.00
16.03
6


ATOM
455
CB
ALA
A
63
16.772
34.361
30.697
1.00
16.37
6


ATOM
456
C
ALA
A
63
17.659
36.647
31.183
1.00
16.03
6


ATOM
457
O
ALA
A
63
18.865
36.810
31.376
1.00
15.96
8


ATOM
458
N
VAL
A
64
16.915
37.495
30.474
1.00
15.90
7


ATOM
459
CA
VAL
A
64
17.464
38.731
29.925
1.00
15.95
6


ATOM
460
CB
VAL
A
64
16.443
39.451
29.007
1.00
15.64
6


ATOM
461
GG1
VAL
A
64
16.914
40.872
28.655
1.00
15.38
6


ATOM
462
CG2
VAL
A
64
16.214
38.633
27.749
1.00
15.05
6


ATOM
463
C
VAL
A
64
17.953
39.659
31.037
1.00
16.67
6


ATOM
464
O
VAL
A
64
18.984
40.303
30.893
1.00
17.04
8


ATOM
465
N
LEU
A
65
17.219
39.701
32.152
1.00
16.95
7


ATOM
466
CA
LEU
A
65
17.624
40.506
33.313
1.00
17.54
6


ATOM
467
CB
LEU
A
65
16.517
40.554
34.369
1.00
17.84
6


ATOM
468
CG
LEU
A
65
15.219
41.303
34.034
1.00
18.34
6


ATOM
469
CD1
LEU
A
65
14.344
41.430
35.272
1.00
19.45
6


ATOM
470
CD2
LEU
A
65
15.473
42.678
33.403
1.00
20.43
6


ATOM
471
C
LEU
A
65
18.938
40.032
33.948
1.00
17.82
6


ATOM
472
O
LEU
A
65
19.670
40.832
34.523
1.00
17.99
8


ATOM
473
N
ILE
A
66
19.224
38.734
33.843
1.00
17.97
7


ATOM
474
CA
ILE
A
66
20.485
38.170
34.350
1.00
18.30
6


ATOM
475
CB
ILE
A
66
20.354
36.654
34.643
1.00
18.40
6


ATOM
476
CG1
ILE
A
66
19.383
36.417
35.807
1.00
19.02
6


ATOM
477
CD1
ILE
A
66
18.964
34.950
35.984
1.00
19.25
6


ATOM
478
CG2
ILE
A
66
21.727
36.034
34.937
1.00
19.04
6


ATOM
479
C
ILE
A
66
21.649
38.399
33.376
1.00
18.39
6


ATOM
480
O
ILE
A
66
22.742
38.820
33.778
1.00
18.24
8


ATOM
481
N
THR
A
67
21.404
38.116
32.099
1.00
17.69
7


ATOM
482
CA
THR
A
67
22.457
38.151
31.074
1.00
17.85
6


ATOM
483
CB
THR
A
67
22.112
37.234
29.878
1.00
17.75
6


ATOM
484
OG1
THR
A
67
21.003
37.785
29.155
1.00
18.28
8


ATOM
485
CG2
THR
A
67
21.766
35.818
30.352
1.00
18.54
6


ATOM
486
C
THR
A
67
22.719
39.555
30.542
1.00
17.40
6


ATOM
487
O
THR
A
67
23.844
39.876
30.133
1.00
18.00
8


ATOM
488
N
GLY
A
68
21.682
40.385
30.526
1.00
16.56
7


ATOM
489
CA
GLY
A
68
21.777
41.710
29.939
1.00
16.28
6


ATOM
490
C
GLY
A
68
21.785
41.683
28.417
1.00
15.46
6


ATOM
491
O
GLY
A
68
22.046
42.711
27.772
1.00
15.84
8


ATOM
492
N
ILE
A
69
21.493
40.512
27.839
1.00
15.26
7


ATOM
493
CA
ILE
A
69
21.437
40.360
26.380
1.00
14.64
6


ATOM
494
CB
ILE
A
69
22.159
39.063
25.881
1.00
14.55
6


ATOM
495
CG1
ILE
A
69
23.608
39.011
26.376
1.00
14.87
6


ATOM
496
CD1
ILE
A
69
24.328
37.712
26.007
1.00
15.26
6


ATOM
497
CG2
ILE
A
69
22.120
38.974
24.348
1.00
15.35
6


ATOM
498
C
ILE
A
69
19.993
40.349
25.885
1.00
14.58
6


ATOM
499
O
ILE
A
69
19.233
39.424
26.189
1.00
14.60
8


ATOM
500
N
THR
A
70
19.630
41.377
25.117
1.00
14.27
7


ATOM
501
CA
THR
A
70
18.290
41.489
24.539
1.00
14.14
6


ATOM
502
CB
THR
A
70
17.955
42.959
24.127
1.00
13.96
6


ATOM
503
OG1
THR
A
70
18.867
43.401
23.111
1.00
14.89
8


ATOM
504
CG2
THR
A
70
18.036
43.885
25.318
1.00
15.10
6


ATOM
505
C
THR
A
70
18.168
40.595
23.311
1.00
13.62
6


ATOM
506
O
THR
A
70
19.179
40.280
22.668
1.00
13.66
8


ATOM
507
N
PRO
A
71
16.930
40.164
22.981
1.00
13.60
7


ATOM
508
CA
PRO
A
71
16.694
39.469
21.710
1.00
13.45
6


ATOM
509
CB
PRO
A
71
15.186
39.182
21.743
1.00
13.32
6


ATOM
510
CG
PRO
A
71
14.637
40.150
22.762
1.00
13.53
6


ATOM
511
CD
PRO
A
71
15.698
40.274
23.782
1.00
13.34
6


ATOM
512
C
PRO
A
71
17.062
40.325
20.486
1.00
13.67
6


ATOM
513
O
PRO
A
71
17.485
39.782
19.461
1.00
13.64
8


ATOM
514
N
GLN
A
72
16.908
41.647
20.598
1.00
13.97
7


ATOM
515
CA
GLN
A
72
17.346
42.565
19.534
1.00
14.07
6


ATOM
516
CB
GLN
A
72
17.014
44.024
19.886
1.00
14.43
6


ATOM
517
CG
GLN
A
72
15.531
44.374
19.828
1.00
14.67
6


ATOM
518
CD
GLN
A
72
14.863
44.331
21.185
1.00
14.98
6


ATOM
519
OE1
GLN
A
72
15.208
43.513
22.041
1.00
16.14
8


ATOM
520
NE2
GLN
A
72
13.894
45.212
21.389
1.00
15.04
7


ATOM
521
C
GLN
A
72
18.846
42.439
19.267
1.00
13.91
6


ATOM
522
O
GLN
A
72
19.282
42.416
18.108
1.00
14.07
8


ATOM
523
N
GLU
A
73
19.629
42.370
20.342
1.00
14.10
7


ATOM
524
CA
GLU
A
73
21.081
42.276
20.221
1.00
14.08
6


ATOM
525
CB
GLU
A
73
21.778
42.533
21.561
1.00
14.17
6


ATOM
526
CG
GLU
A
73
23.299
42.495
21.464
1.00
14.67
6


ATOM
527
CD
GLU
A
73
23.996
42.833
22.764
1.00
15.23
6


ATOM
528
OE1
GLU
A
73
23.460
42.499
23.841
1.00
18.79
8


ATOM
529
OE2
GLU
A
73
25.097
43.424
22.708
1.00
17.09
8


ATOM
530
C
GLU
A
73
21.524
40.943
19.625
1.00
13.82
6


ATOM
531
O
GLU
A
73
22.344
40.921
18.704
1.00
13.80
8


ATOM
532
N
ALA
A
74
20.986
39.836
20.142
1.00
13.17
7


ATOM
533
CA
ALA
A
74
21.284
38.503
19.575
1.00
12.70
6


ATOM
534
CB
ALA
A
74
20.645
37.399
20.411
1.00
12.95
6


ATOM
535
C
ALA
A
74
20.853
38.391
18.104
1.00
12.78
6


ATOM
536
O
ALA
A
74
21.575
37.816
17.275
1.00
12.37
8


ATOM
537
N
ARG
A
75
19.680
38.930
17.788
1.00
12.70
7


ATOM
538
CA
ARG
A
75
19.216
38.984
16.407
1.00
13.09
6


ATOM
539
CB
ARG
A
75
17.801
39.549
16.328
1.00
13.12
6


ATOM
540
CG
ARG
A
75
17.188
39.461
14.938
1.00
14.17
6


ATOM
541
CD
ARG
A
75
15.707
39.777
14.976
1.00
15.99
6


ATOM
542
NE
ARG
A
75
15.444
41.167
15.339
1.00
17.81
7


ATOM
543
CZ
ARG
A
75
14.242
41.732
15.316
1.00
18.68
6


ATOM
544
NH1
ARG
A
75
13.177
41.026
14.945
1.00
18.04
7


ATOM
545
NH2
ARG
A
75
14.101
43.006
15.662
1.00
18.75
7


ATOM
546
C
ARG
A
75
20.158
39.799
15.517
1.00
13.07
6


ATOM
547
O
ARG
A
75
20.479
39.383
14.413
1.00
13.04
8


ATOM
548
N
ALA
A
76
20.602
40.959
15.999
1.00
13.02
7


ATOM
549
CA
ALA
A
76
21.404
41.858
15.152
1.00
12.99
6


ATOM
550
CB
ALA
A
76
21.298
43.307
15.633
1.00
13.28
6


ATOM
551
C
ALA
A
76
22.869
41.426
15.038
1.00
13.53
6


ATOM
552
O
ALA
A
76
23.528
41.705
14.032
1.00
13.83
8


ATOM
553
N
LYS
A
77
23.381
40.749
16.070
1.00
13.38
7


ATOM
554
CA
LYS
A
77
24.792
40.333
16.086
1.00
13.73
6


ATOM
555
CB
LYS
A
77
25.426
40.628
17.451
1.00
13.72
6


ATOM
556
CG
LYS
A
77
25.422
42.107
17.818
1.00
15.21
6


ATOM
557
CD
LYS
A
77
26.171
42.370
19.095
1.00
15.59
6


ATOM
558
CE
LYS
A
77
26.307
43.858
19.339
1.00
16.23
6


ATOM
559
NZ
LYS
A
77
26.891
44.159
20.685
1.00
17.82
7


ATOM
560
C
LYS
A
77
24.966
38.858
15.746
1.00
13.84
6


ATOM
561
O
LYS
A
77
26.083
38.396
15.497
1.00
14.45
8


ATOM
562
N
GLY
A
78
23.862
38.123
15.718
1.00
13.79
7


ATOM
563
CA
GLY
A
78
23.924
36.666
15.634
1.00
14.22
6


ATOM
564
C
GLY
A
78
23.891
36.109
14.224
1.00
14.25
6


ATOM
565
O
GLY
A
78
23.579
36.817
13.265
1.00
14.82
8


ATOM
566
N
GLU
A
79
24.236
34.832
14.105
1.00
14.13
7


ATOM
567
CA
GLU
A
79
23.940
34.056
12.912
1.00
14.68
6


ATOM
568
CB
GLU
A
79
25.143
33.204
12.524
1.00
14.91
6


ATOM
569
CG
GLU
A
79
26.414
34.008
12.289
1.00
17.74
6


ATOM
570
CD
GLU
A
79
27.632
33.130
12.146
1.00
21.61
6


ATOM
571
OE1
GLU
A
79
27.869
32.288
13.040
1.00
22.92
8


ATOM
572
OE2
GLU
A
79
28.361
33.286
11.144
1.00
23.45
8


ATOM
573
C
GLU
A
79
22.765
33.156
13.245
1.00
14.11
6


ATOM
574
O
GLU
A
79
22.420
33.005
14.417
1.00
13.88
8


ATOM
575
N
ASN
A
80
22.141
32.555
12.231
1.00
13.72
7


ATOM
576
CA
ASN
A
80
21.043
31.632
12.513
1.00
13.40
6


ATOM
577
CB
ASN
A
80
20.285
31.221
11.246
1.00
13.79
6


ATOM
578
CG
ASN
A
80
21.159
30.486
10.223
1.00
14.18
6


ATOM
579
OD1
ASN
A
80
22.142
29.824
10.563
1.00
13.68
8


ATOM
580
ND2
ASN
A
80
20.768
30.578
8.963
1.00
15.88
7


ATOM
581
C
ASN
A
80
21.532
30.422
13.298
1.00
12.88
6


ATOM
582
O
ASN
A
80
22.733
30.177
13.382
1.00
12.27
8


ATOM
583
N
GLU
A
81
20.604
29.683
13.899
1.00
12.58
7


ATOM
584
CA
GLU
A
81
20.986
28.561
14.744
1.00
12.26
6


ATOM
585
CB
GLU
A
81
19.773
27.953
15.437
1.00
11.90
6


ATOM
586
CG
GLU
A
81
20.109
27.408
16.828
1.00
12.73
6


ATOM
587
CD
GLU
A
81
18.928
26.786
17.515
1.00
12.53
6


ATOM
588
OE1
GLU
A
81
18.349
25.840
16.946
1.00
12.98
8


ATOM
589
OE2
GLU
A
81
18.582
27.224
18.643
1.00
14.87
8


ATOM
590
C
GLU
A
81
21.782
27.492
13.988
1.00
12.21
6


ATOM
591
O
GLU
A
81
22.688
26.878
14.552
1.00
12.03
8


ATOM
592
N
ALA
A
82
21.472
27.298
12.705
1.00
12.78
7


ATOM
593
CA
ALA
A
82
22.242
26.363
11.877
1.00
12.90
6


ATOM
594
CB
ALA
A
82
21.707
26.334
10.438
1.00
13.31
6


ATOM
595
C
ALA
A
82
23.742
26.689
11.885
1.00
13.22
6


ATOM
596
O
ALA
A
82
24.574
25.807
12.101
1.00
13.38
8


ATOM
597
N
ALA
A
83
24.072
27.960
11.661
1.00
12.96
7


ATOM
598
CA
ALA
A
83
25.460
28.406
11.589
1.00
13.11
6


ATOM
599
CB
ALA
A
83
25.546
29.763
10.899
1.00
13.08
6


ATOM
600
C
ALA
A
83
26.094
28.464
12.981
1.00
13.06
6


ATOM
601
O
ALA
A
83
27.277
28.193
13.142
1.00
13.43
8


ATOM
602
N
PHE
A
84
25.282
28.816
13.977
1.00
12.44
7


ATOM
603
CA
PHE
A
84
25.683
28.820
15.388
1.00
12.44
6


ATOM
604
CB
PHE
A
84
24.476
29.257
16.231
1.00
12.30
6


ATOM
605
CG
PHE
A
84
24.784
29.527
17.683
1.00
12.81
6


ATOM
606
CD1
PHE
A
84
25.584
30.607
18.061
1.00
11.94
6


ATOM
607
CE1
PHE
A
84
25.836
30.871
19.405
1.00
12.19
6


ATOM
608
CZ
PHE
A
84
25.267
30.080
20.383
1.00
11.98
6


ATOM
609
CE2
PHE
A
84
24.448
29.011
20.021
1.00
12.37
6


ATOM
610
CD2
PHE
A
84
24.207
28.747
18.677
1.00
11.92
6


ATOM
611
C
PHE
A
84
26.150
27.418
15.799
1.00
12.49
6


ATOM
612
O
PHE
A
84
27.205
27.256
16.430
1.00
12.19
8


ATOM
613
N
ALA
A
85
25.359
26.418
15.409
1.00
12.22
7


ATOM
614
CA
ALA
A
85
25.661
25.009
15.644
1.00
12.13
6


ATOM
615
CB
ALA
A
85
24.494
24.146
15.176
1.00
11.23
6


ATOM
616
C
ALA
A
85
26.957
24.574
14.952
1.00
12.26
6


ATOM
617
O
ALA
A
85
27.790
23.880
15.555
1.00
12.18
8


ATOM
618
N
ALA
A
86
27.118
24.975
13.686
1.00
11.99
7


ATOM
619
CA
ALA
A
86
28.304
24.625
12.897
1.00
12.33
6


ATOM
620
CB
ALA
A
86
28.182
25.167
11.447
1.00
11.70
6


ATOM
621
C
ALA
A
86
29.593
25.104
13.540
1.00
12.55
6


ATOM
622
O
ALA
A
86
30.586
24.375
13.570
1.00
13.03
8


ATOM
623
N
ARG
A
87
29.567
26.327
14.069
1.00
13.24
7


ATOM
624
CA
ARG
A
87
30.720
26.904
14.754
1.00
13.60
6


ATOM
625
CB
ARG
A
87
30.455
28.374
15.096
1.00
13.81
6


ATOM
626
CG
ARG
A
87
30.556
29.336
13.925
1.00
15.20
6


ATOM
627
CD
ARG
A
87
30.584
30.781
14.414
1.00
17.78
6


ATOM
628
NE
ARG
A
87
30.344
31.745
13.338
1.00
21.20
7


ATOM
629
CZ
ARG
A
87
31.289
32.259
12.548
1.00
22.71
6


ATOM
630
NH1
ARG
A
87
32.561
31.908
12.696
1.00
23.42
7


ATOM
631
NH2
ARG
A
87
30.958
33.130
11.604
1.00
23.43
7


ATOM
632
C
ARG
A
87
31.071
26.121
16.031
1.00
13.48
6


ATOM
633
O
ARG
A
87
32.222
25.738
16.240
1.00
13.61
8


ATOM
634
N
ILE
A
88
30.068
25.886
16.873
1.00
13.61
7


ATOM
635
CA
ILE
A
88
30.251
25.109
18.093
1.00
13.81
6


ATOM
636
CB
ILE
A
88
28.946
25.071
18.930
1.00
13.72
6


ATOM
637
CG1
ILE
A
88
28.569
26.489
19.380
1.00
13.09
6


ATOM
638
CD1
ILE
A
88
27.163
26.616
19.913
1.00
13.63
6


ATOM
639
CG2
ILE
A
88
29.082
24.108
20.105
1.00
13.89
6


ATOM
640
C
ILE
A
88
30.739
23.683
17.793
1.00
14.15
6


ATOM
641
O
ILE
A
88
31.679
23.200
18.418
1.00
13.95
8


ATOM
642
N
HIS
A
89
30.104
23.033
16.818
1.00
14.67
7


ATOM
643
CA
HIS
A
89
30.462
21.669
16.422
1.00
14.87
6


ATOM
644
CB
HIS
A
89
29.488
21.141
15.368
1.00
15.06
6


ATOM
645
CG
HIS
A
89
29.723
19.710
14.990
1.00
15.19
6


ATOM
646
ND1
HIS
A
89
30.465
19.345
13.888
1.00
15.49
7


ATOM
647
CE1
HIS
A
89
30.497
18.027
13.798
1.00
14.66
6


ATOM
648
NE2
HIS
A
89
29.809
17.524
14.807
1.00
15.16
7


ATOM
649
CD2
HIS
A
89
29.316
18.555
15.569
1.00
15.52
6


ATOM
650
C
HIS
A
89
31.902
21.571
15.902
1.00
15.22
6


ATOM
651
O
HIS
A
89
32.596
20.595
16.166
1.00
15.06
8


ATOM
652
N
SER
A
90
32.342
22.596
15.176
1.00
15.51
7


ATOM
653
CA
SER
A
90
33.710
22.646
14.669
1.00
16.24
6


ATOM
654
CB
SER
A
90
33.891
23.827
13.709
1.00
16.26
6


ATOM
655
OG
SER
A
90
33.852
25.063
14.412
1.00
18.36
8


ATOM
656
C
SER
A
90
34.734
22.717
15.809
1.00
15.89
6


ATOM
657
O
SER
A
90
35.788
22.078
15.744
1.00
16.86
8


ATOM
658
N
LEU
A
91
34.410
23.481
16.853
1.00
15.75
7


ATOM
659
CA
LEU
A
91
35.275
23.607
18.030
1.00
14.94
6


ATOM
660
CB
LEU
A
91
34.820
24.779
18.907
1.00
14.86
6


ATOM
661
CG
LEU
A
91
35.010
26.197
18.359
1.00
15.05
6


ATOM
662
CD1
LEU
A
91
34.327
27.205
19.271
1.00
16.20
6


ATOM
663
CD2
LEU
A
91
36.490
26.525
18.209
1.00
16.84
6


ATOM
664
C
LEU
A
91
35.302
22.327
18.861
1.00
14.49
6


ATOM
665
O
LEU
A
91
36.363
21.909
19.342
1.00
14.78
8


ATOM
666
N
PHE
A
92
34.129
21.717
19.027
1.00
13.44
7


ATOM
667
CA
PHE
A
92
33.958
20.570
19.907
1.00
13.12
6


ATOM
668
CB
PHE
A
92
32.465
20.367
20.255
1.00
12.46
6


ATOM
669
CG
PHE
A
92
31.934
21.290
21.344
1.00
12.19
6


ATOM
670
CD1
PHE
A
92
32.612
22.448
21.714
1.00
11.10
6


ATOM
671
CE1
PHE
A
92
32.102
23.290
22.707
1.00
10.74
6


ATOM
672
CZ
PHE
A
92
30.905
22.980
23.338
1.00
11.11
6


ATOM
673
CE2
PHE
A
92
30.214
21.830
22.987
1.00
12.08
6


ATOM
674
CD2
PHE
A
92
30.729
20.987
21.985
1.00
11.63
6


ATOM
675
C
PHE
A
92
34.520
19.278
19.301
1.00
12.89
6


ATOM
676
O
PHE
A
92
34.759
18.319
20.021
1.00
13.28
8


ATOM
677
N
THR
A
93
34.709
19.240
17.980
1.00
12.89
7


ATOM
678
CA
THR
A
93
35.126
17.991
17.334
1.00
13.04
6


ATOM
679
CB
THR
A
93
34.237
17.618
16.135
1.00
13.01
6


ATOM
680
OG1
THR
A
93
34.195
18.714
15.216
1.00
12.12
8


ATOM
681
CG2
THR
A
93
32.821
17.271
16.609
1.00
14.51
6


ATOM
682
C
THR
A
93
36.599
17.948
16.931
1.00
13.18
6


ATOM
683
O
THR
A
93
37.034
17.014
16.259
1.00
13.01
8


ATOM
684
N
VAL
A
94
37.362
18.954
17.350
1.00
12.97
7


ATOM
685
CA
VAL
A
94
38.819
18.880
17.285
1.00
12.81
6


ATOM
686
CB
VAL
A
94
39.466
20.211
17.753
1.00
12.92
6


ATOM
687
CG1
VAL
A
94
40.983
20.077
17.873
1.00
12.48
6


ATOM
688
CG2
VAL
A
94
39.097
21.346
16.794
1.00
13.06
6


ATOM
689
C
VAL
A
94
39.271
17.705
18.172
1.00
12.77
6


ATOM
690
O
VAL
A
94
38.851
17.610
19.333
1.00
12.20
8


ATOM
691
N
PRO
A
95
40.079
16.777
17.609
1.00
13.06
7


ATOM
692
CA
PRO
A
95
40.550
15.592
18.345
1.00
13.26
6


ATOM
693
CB
PRO
A
95
41.524
14.938
17.361
1.00
13.42
6


ATOM
694
CG
PRO
A
95
41.037
15.356
16.025
1.00
13.24
6


ATOM
695
CD
PRO
A
95
40.561
16.771
16.213
1.00
13.23
6


ATOM
696
C
PRO
A
95
41.279
15.907
19.649
1.00
13.38
6


ATOM
697
O
PRO
A
95
41.921
16.951
19.765
1.00
14.01
8


ATOM
698
N
LYS
A
96
41.184
14.988
20.610
1.00
13.06
7


ATOM
699
CA
LYS
A
96
41.880
15.098
21.897
1.00
13.39
6


ATOM
700
CB
LYS
A
96
43.410
15.036
21.713
1.00
13.10
6


ATOM
701
CG
LYS
A
96
43.919
13.754
21.051
1.00
14.33
6


ATOM
702
CD
LYS
A
96
45.439
13.678
21.098
1.00
14.88
6


ATOM
703
CE
LYS
A
96
45.931
12.886
22.307
1.00
18.63
6


ATOM
704
NZ
LYS
A
96
45.840
11.412
22.079
1.00
19.29
7


ATOM
705
C
LYS
A
96
41.470
16.345
22.694
1.00
13.00
6


ATOM
706
O
LYS
A
96
42.276
16.912
23.443
1.00
13.26
8


ATOM
707
N
THR
A
97
40.216
16.761
22.525
1.00
12.75
7


ATOM
708
CA
THR
A
97
39.651
17.879
23.298
1.00
12.67
6


ATOM
709
CB
THR
A
97
38.711
18.754
22.430
1.00
12.99
6


ATOM
710
OG1
THR
A
97
39.433
19.270
21.313
1.00
13.19
8


ATOM
711
CG2
THR
A
97
38.154
19.924
23.244
1.00
13.21
6


ATOM
712
C
THR
A
97
38.855
17.387
24.493
1.00
12.55
6


ATOM
713
O
THR
A
97
37.980
16.526
24.350
1.00
12.80
8


ATOM
714
N
CYS
A
98
39.149
17.953
25.666
1.00
11.73
7


ATOM
715
CA
CYS
A
98
38.279
17.818
26.822
1.00
11.31
6


ATOM
716
CB
CYS
A
98
39.085
17.647
28.106
1.00
11.35
6


ATOM
717
SG
CYS
A
98
38.052
17.609
29.610
1.00
12.81
16


ATOM
718
C
CYS
A
98
37.395
19.056
26.911
1.00
10.55
6


ATOM
719
O
CYS
A
98
37.877
20.157
27.188
1.00
9.88
8


ATOM
720
N
ILE
A
99
36.109
18.869
26.636
1.00
10.46
7


ATOM
721
CA
ILE
A
99
35.147
19.967
26.622
1.00
10.53
6


ATOM
722
CB
ILE
A
99
33.979
19.686
25.626
1.00
10.72
6


ATOM
723
CG1
ILE
A
99
34.514
19.469
24.199
1.00
11.33
6


ATOM
724
CD1
ILE
A
99
34.577
18.015
23.786
1.00
13.60
6


ATOM
725
CG2
ILE
A
99
32.945
20.806
25.678
1.00
11.06
6


ATOM
726
C
ILE
A
99
34.579
20.117
28.009
1.00
10.69
6


ATOM
727
O
ILE
A
99
33.984
19.180
28.542
1.00
10.93
8


ATOM
728
N
LEU
A
100
34.770
21.288
28.615
1.00
10.45
7


ATOM
729
CA
LEU
A
100
34.360
21.464
30.009
1.00
10.47
6


ATOM
730
CB
LEU
A
100
35.500
21.089
30.980
1.00
10.45
6


ATOM
731
CG
LEU
A
100
36.689
22.043
31.181
1.00
11.09
6


ATOM
732
CD1
LEU
A
100
37.637
21.503
32.249
1.00
11.45
6


ATOM
733
CD2
LEU
A
100
37.447
22.275
29.889
1.00
11.97
6


ATOM
734
C
LEU
A
100
33.835
22.853
30.299
1.00
10.83
6


ATOM
735
O
LEU
A
100
34.066
23.790
29.543
1.00
11.82
8


ATOM
736
N
GLY
A
101
33.111
22.976
31.400
1.00
11.08
7


ATOM
737
CA
GLY
A
101
32.553
24.253
31.784
1.00
10.95
6


ATOM
738
C
GLY
A
101
32.315
24.278
33.270
1.00
10.91
6


ATOM
739
O
GLY
A
101
33.000
23.580
34.041
1.00
11.15
8


ATOM
740
N
TYR
A
102
31.340
25.079
33.673
1.00
11.01
7


ATOM
741
CA
TYR
A
102
30.942
25.144
35.064
1.00
11.18
6


ATOM
742
CB
TYR
A
102
31.344
26.479
35.692
1.00
11.65
6


ATOM
743
CG
TYR
A
102
31.350
26.407
37.190
1.00
11.24
6


ATOM
744
CD1
TYR
A
102
32.476
25.954
37.875
1.00
11.51
6


ATOM
745
CE1
TYR
A
102
32.475
25.853
39.262
1.00
12.12
6


ATOM
746
CZ
TYR
A
102
31.339
26.200
39.970
1.00
12.65
6


ATOM
747
OH
TYR
A
102
31.349
26.100
41.345
1.00
12.00
8


ATOM
748
CE2
TYR
A
102
30.200
26.640
39.303
1.00
12.68
6


ATOM
749
CD2
TYR
A
102
30.211
26.734
37.926
1.00
11.67
6


ATOM
750
C
TYR
A
102
29.436
24.945
35.139
1.00
11.33
6


ATOM
751
O
TYR
A
102
28.659
25.843
34.784
1.00
11.24
8


ATOM
752
N
ASN
A
103
29.041
23.760
35.602
1.00
12.10
7


ATOM
753
CA
ASN
A
103
27.656
23.275
35.527
1.00
12.63
6


ATOM
754
CB
ASN
A
103
26.650
24.281
36.121
1.00
12.54
6


ATOM
755
CG
ASN
A
103
25.297
23.641
36.434
1.00
13.23
6


ATOM
756
OD1
ASN
A
103
25.225
22.470
36.800
1.00
14.60
8


ATOM
757
ND2
ASN
A
103
24.221
24.410
36.272
1.00
16.03
7


ATOM
758
C
ASN
A
103
27.232
22.834
34.115
1.00
13.09
6


ATOM
759
O
ASN
A
103
26.034
22.764
33.802
1.00
13.38
8


ATOM
760
N
ASN
A
104
28.210
22.502
33.276
1.00
13.06
7


ATOM
761
CA
ASN
A
104
27.905
22.089
31.901
1.00
13.07
6


ATOM
762
CB
ASN
A
104
29.148
22.131
31.008
1.00
12.99
6


ATOM
763
CG
ASN
A
104
30.298
21.337
31.571
1.00
12.31
6


ATOM
764
OD1
ASN
A
104
30.783
21.629
32.662
1.00
12.01
8


ATOM
765
ND2
ASN
A
104
30.755
20.326
30.824
1.00
12.75
7


ATOM
766
C
ASN
A
104
27.208
20.736
31.793
1.00
13.48
6


ATOM
767
O
ASN
A
104
26.386
20.534
30.914
1.00
13.40
8


ATOM
768
N
VAL
A
105
27.522
19.814
32.697
1.00
14.08
7


ATOM
769
CA
VAL
A
105
26.940
18.473
32.619
1.00
14.71
6


ATOM
770
CB
VAL
A
105
27.525
17.526
33.685
1.00
14.68
6


ATOM
771
CG1
VAL
A
105
26.727
16.229
33.759
1.00
14.95
6


ATOM
772
CG2
VAL
A
105
28.970
17.220
33.364
1.00
14.65
6


ATOM
773
C
VAL
A
105
25.409
18.512
32.679
1.00
15.13
6


ATOM
774
O
VAL
A
105
24.733
17.824
31.898
1.00
16.46
8


ATOM
775
N
ARG
A
106
24.870
19.356
33.556
1.00
15.56
7


ATOM
776
CA
ARG
A
106
23.417
19.450
33.749
1.00
15.86
6


ATOM
777
CB
ARG
A
106
23.080
19.643
35.229
1.00
16.46
6


ATOM
778
CG
ARG
A
106
23.635
18.548
36.120
1.00
18.79
6


ATOM
779
CD
ARG
A
106
23.313
18.804
37.586
1.00
23.08
6


ATOM
780
NE
ARG
A
106
24.490
18.823
38.476
1.00
27.18
7


ATOM
781
CZ
ARG
A
106
25.685
18.278
38.218
1.00
27.90
6


ATOM
782
NH1
ARG
A
106
25.923
17.626
37.083
1.00
27.99
7


ATOM
783
NH2
ARG
A
106
26.654
18.391
39.111
1.00
28.51
7


ATOM
784
C
ARG
A
106
22.743
20.541
32.906
1.00
15.30
6


ATOM
785
O
ARG
A
106
21.532
20.480
32.665
1.00
15.59
8


ATOM
786
N
PHE
A
107
23.515
21.529
32.452
1.00
14.34
7


ATOM
787
CA
PHE
A
107
22.941
22.616
31.662
1.00
13.07
6


ATOM
788
CB
PHE
A
107
23.016
23.951
32.407
1.00
13.02
6


ATOM
789
CG
PHE
A
107
22.298
25.065
31.706
1.00
12.39
6


ATOM
790
CD1
PHE
A
107
20.911
25.019
31.536
1.00
13.22
6


ATOM
791
CE1
PHE
A
107
20.236
26.047
30.863
1.00
13.50
6


ATOM
792
CZ
PHE
A
107
20.946
27.129
30.373
1.00
12.88
6


ATOM
793
CE2
PHE
A
107
22.333
27.183
30.531
1.00
12.85
6


ATOM
794
CD2
PHE
A
107
23.000
26.151
31.188
1.00
12.71
6


ATOM
795
C
PHE
A
107
23.517
22.752
30.253
1.00
12.78
6


ATOM
796
O
PHE
A
107
22.840
22.441
29.276
1.00
12.53
8


ATOM
797
N
ASP
A
108
24.756
23.229
30.154
1.00
12.65
7


ATOM
798
CA
ASP
A
108
25.334
23.603
28.853
1.00
12.55
6


ATOM
799
CB
ASP
A
108
26.725
24.228
29.027
1.00
12.85
6


ATOM
800
CG
ASP
A
108
26.713
25.417
29.956
1.00
12.52
6


ATOM
801
OD1
ASP
A
108
26.824
26.561
29.454
1.00
12.38
8


ATOM
802
OD2
ASP
A
108
26.588
25.210
31.188
1.00
14.32
8


ATOM
803
C
ASP
A
108
25.390
22.441
27.862
1.00
12.78
6


ATOM
804
O
ASP
A
108
25.125
22.627
26.662
1.00
12.59
8


ATOM
805
N
ASP
A
109
25.728
21.248
28.355
1.00
12.76
7


ATOM
806
CA
ASP
A
109
25.757
20.050
27.510
1.00
13.49
6


ATOM
807
CB
ASP
A
109
26.316
18.855
28.283
1.00
13.76
6


ATOM
808
CG
ASP
A
109
27.803
18.985
28.571
1.00
15.55
6


ATOM
809
OD1
ASP
A
109
28.448
19.933
28.060
1.00
15.92
8


ATOM
810
OD2
ASP
A
109
28.335
18.124
29.311
1.00
17.53
8


ATOM
811
C
ASP
A
109
24.375
19.713
26.964
1.00
13.33
6


ATOM
812
O
ASP
A
109
24.236
19.255
25.824
1.00
13.67
8


ATOM
813
N
GLU
A
110
23.352
19.969
27.771
1.00
13.06
7


ATOM
814
CA
GLU
A
110
21.972
19.752
27.352
1.00
13.09
6


ATOM
815
CB
GLU
A
110
21.043
19.737
28.561
1.00
13.28
6


ATOM
816
CG
GLU
A
110
21.229
18.525
29.437
1.00
15.94
6


ATOM
817
CD
GLU
A
110
20.969
17.222
28.689
1.00
18.22
6


ATOM
818
OE1
GLU
A
110
19.877
17.086
28.094
1.00
20.07
8


ATOM
819
OE2
GLU
A
110
21.863
16.344
28.685
1.00
20.95
8


ATOM
820
C
GLU
A
110
21.515
20.780
26.318
1.00
12.47
6


ATOM
821
O
GLU
A
110
20.766
20.449
25.391
1.00
12.47
8


ATOM
822
N
VAL
A
111
21.973
22.023
26.464
1.00
11.80
7


ATOM
823
CA
VAL
A
111
21.793
23.022
25.399
1.00
11.50
6


ATOM
824
CB
VAL
A
111
22.323
24.421
25.809
1.00
11.38
6


ATOM
825
CG1
VAL
A
111
22.190
25.408
24.669
1.00
11.22
6


ATOM
826
CG2
VAL
A
111
21.582
24.937
27.037
1.00
11.05
6


ATOM
827
C
VAL
A
111
22.472
22.548
24.112
1.00
11.66
6


ATOM
828
O
VAL
A
111
21.860
22.546
23.045
1.00
12.10
8


ATOM
829
N
THR
A
112
23.732
22.131
24.227
1.00
11.70
7


ATOM
830
CA
THR
A
112
24.482
21.604
23.092
1.00
11.96
6


ATOM
831
CB
THR
A
112
25.878
21.132
23.525
1.00
11.97
6


ATOM
832
OG1
THR
A
112
26.601
22.243
24.073
1.00
12.20
8


ATOM
833
CG2
THR
A
112
26.650
20.558
22.339
1.00
11.65
6


ATOM
834
C
THR
A
112
23.731
20.465
22.400
1.00
12.19
6


ATOM
835
O
THR
A
112
23.548
20.483
21.180
1.00
11.83
8


ATOM
836
N
ARG
A
113
23.281
19.484
23.180
1.00
12.38
7


ATOM
837
CA
ARG
A
113
22.587
18.324
22.610
1.00
12.75
6


ATOM
838
CB
ARG
A
113
22.217
17.312
23.692
1.00
13.58
6


ATOM
839
CG
ARG
A
113
23.417
16.602
24.287
1.00
15.46
6


ATOM
840
CD
ARG
A
113
23.003
15.467
25.216
1.00
20.60
6


ATOM
841
NE
ARG
A
113
24.116
15.008
26.059
1.00
24.49
7


ATOM
842
CZ
ARG
A
113
25.241
14.450
25.600
1.00
27.34
6


ATOM
843
NH1
ARG
A
113
25.440
14.294
24.293
1.00
28.57
7


ATOM
844
NH2
ARG
A
113
26.182
14.056
26.449
1.00
28.87
7


ATOM
845
C
ARG
A
113
21.357
18.736
21.817
1.00
12.65
6


ATOM
846
O
ARG
A
113
21.089
18.188
20.747
1.00
12.92
8


ATOM
847
N
ASN
A
114
20.633
19.727
22.331
1.00
11.97
7


ATOM
848
CA
ASN
A
114
19.404
20.196
21.702
1.00
11.72
6


ATOM
849
CB
ASN
A
114
18.543
20.938
22.725
1.00
12.26
6


ATOM
850
CG
ASN
A
114
17.783
19.985
23.633
1.00
12.54
6


ATOM
851
OD1
ASN
A
114
18.139
19.791
24.806
1.00
15.86
8


ATOM
852
ND2
ASN
A
114
16.751
19.364
23.090
1.00
11.70
7


ATOM
853
C
ASN
A
114
19.631
21.031
20.440
1.00
11.53
6


ATOM
854
O
ASN
A
114
18.922
20.864
19.445
1.00
11.14
8


ATOM
855
N
ILE
A
115
20.631
21.909
20.472
1.00
11.38
7


ATOM
856
CA
ILE
A
115
21.030
22.669
19.281
1.00
12.11
6


ATOM
857
CB
ILE
A
115
22.187
23.643
19.596
1.00
12.40
6


ATOM
858
CG1
ILE
A
115
21.733
24.729
20.577
1.00
12.59
6


ATOM
859
CD1
ILE
A
115
22.890
25.485
21.210
1.00
12.12
6


ATOM
860
CG2
ILE
A
115
22.716
24.285
18.333
1.00
12.89
6


ATOM
861
C
ILE
A
115
21.463
21.729
18.144
1.00
12.20
6


ATOM
862
O
ILE
A
115
21.117
21.940
16.981
1.00
12.10
8


ATOM
863
N
PHE
A
116
22.225
20.693
18.501
1.00
12.63
7


ATOM
864
CA
PHE
A
116
22.696
19.697
17.541
1.00
12.35
6


ATOM
865
CB
PHE
A
116
23.721
18.770
18.210
1.00
12.67
6


ATOM
866
CG
PHE
A
116
25.100
19.391
18.389
1.00
11.93
6


ATOM
867
CD1
PHE
A
116
25.364
20.712
18.006
1.00
11.56
6


ATOM
868
CE1
PHE
A
116
26.639
21.264
18.180
1.00
11.52
6


ATOM
869
CZ
PHE
A
116
27.655
20.505
18.748
1.00
12.24
6


ATOM
870
CE2
PHE
A
116
27.411
19.194
19.121
1.00
11.81
6


ATOM
871
CD2
PHE
A
116
26.138
18.643
18.947
1.00
12.39
6


ATOM
872
C
PHE
A
116
21.515
18.892
16.994
1.00
12.80
6


ATOM
873
O
PHE
A
116
21.382
18.718
15.780
1.00
12.64
8


ATOM
874
N
TYR
A
117
20.653
18.438
17.906
1.00
13.04
7


ATOM
875
CA
TYR
A
117
19.387
17.763
17.571
1.00
13.50
6


ATOM
876
CB
TYR
A
117
18.622
17.426
18.869
1.00
13.97
6


ATOM
877
CG
TYR
A
117
17.168
17.010
18.714
1.00
14.55
6


ATOM
878
CD1
TYR
A
117
16.825
15.738
18.241
1.00
16.18
6


ATOM
879
CE1
TYR
A
117
15.487
15.344
18.124
1.00
15.17
6


ATOM
880
CZ
TYR
A
117
14.478
16.229
18.490
1.00
15.35
6


ATOM
881
OH
TYR
A
117
13.151
15.848
18.376
1.00
15.17
8


ATOM
882
CE2
TYR
A
117
14.797
17.493
18.978
1.00
14.92
6


ATOM
883
CD2
TYR
A
117
16.136
17.872
19.095
1.00
15.36
6


ATOM
884
C
TYR
A
117
18.514
18.569
16.599
1.00
13.52
6


ATOM
885
O
TYR
A
117
18.053
18.037
15.592
1.00
13.17
8


ATOM
886
N
ARG
A
118
18.305
19.854
16.889
1.00
13.25
7


ATOM
887
CA
ARG
A
118
17.463
20.692
16.028
1.00
13.20
6


ATOM
888
CB
ARG
A
118
17.145
22.027
16.701
1.00
13.03
6


ATOM
889
CG
ARG
A
118
16.295
21.903
17.954
1.00
12.95
6


ATOM
890
CD
ARG
A
118
15.677
23.240
18.331
1.00
13.09
6


ATOM
891
NE
ARG
A
118
16.644
24.190
18.887
1.00
12.69
7


ATOM
892
CZ
ARG
A
118
16.891
24.327
20.187
1.00
13.30
6


ATOM
893
NH1
ARG
A
118
16.265
23.553
21.071
1.00
13.22
7


ATOM
894
NH2
ARG
A
118
17.762
25.237
20.608
1.00
13.43
7


ATOM
895
C
ARG
A
118
18.071
20.939
14.645
1.00
13.42
6


ATOM
896
O
ARG
A
118
17.346
21.178
13.670
1.00
14.04
8


ATOM
897
N
ASN
A
119
19.398
20.880
14.564
1.00
13.34
7


ATOM
898
CA
ASN
A
119
20.111
21.326
13.377
1.00
13.62
6


ATOM
899
CB
ASN
A
119
20.995
22.520
13.730
1.00
13.54
6


ATOM
900
CG
ASN
A
119
20.172
23.723
14.176
1.00
12.59
6


ATOM
901
OD1
ASN
A
119
19.609
24.445
13.345
1.00
11.81
8


ATOM
902
ND2
ASN
A
119
20.055
23.915
15.491
1.00
13.00
7


ATOM
903
C
ASN
A
119
20.869
20.212
12.651
1.00
14.14
6


ATOM
904
O
ASN
A
119
21.810
20.468
11.876
1.00
14.12
8


ATOM
905
N
PHE
A
120
20.428
18.976
12.895
1.00
14.24
7


ATOM
906
CA
PHE
A
120
20.834
17.803
12.112
1.00
14.75
6


ATOM
907
CB
PHE
A
120
20.464
17.974
10.635
1.00
15.23
6


ATOM
908
CG
PHE
A
120
18.989
17.925
10.386
1.00
15.86
6


ATOM
909
CD1
PHE
A
120
18.381
16.740
9.990
1.00
16.57
6


ATOM
910
CE1
PHE
A
120
17.014
16.678
9.783
1.00
16.66
6


ATOM
911
CZ
PHE
A
120
16.234
17.808
9.977
1.00
16.99
6


ATOM
912
CE2
PHE
A
120
16.824
18.997
10.373
1.00
17.14
6


ATOM
913
CD2
PHE
A
120
18.199
19.050
10.586
1.00
16.48
6


ATOM
914
C
PHE
A
120
22.287
17.394
12.295
1.00
15.09
6


ATOM
915
O
PHE
A
120
22.906
16.828
11.386
1.00
14.87
8


ATOM
916
N
TYR
A
121
22.816
17.692
13.480
1.00
14.93
7


ATOM
917
CA
TYR
A
121
24.066
17.107
13.970
1.00
15.72
6


ATOM
918
CB
TYR
A
121
24.906
18.160
14.704
1.00
15.59
6


ATOM
919
CG
TYR
A
121
25.483
19.223
13.810
1.00
15.53
6


ATOM
920
CD1
TYR
A
121
26.726
19.048
13.201
1.00
15.17
6


ATOM
921
CE1
TYR
A
121
27.260
20.024
12.375
1.00
15.11
6


ATOM
922
CZ
TYR
A
121
26.549
21.188
12.150
1.00
15.67
6


ATOM
923
OH
TYR
A
121
27.073
22.147
11.322
1.00
17.50
8


ATOM
924
CE2
TYR
A
121
25.309
21.388
12.743
1.00
15.64
6


ATOM
925
CD2
TYR
A
121
24.784
20.409
13.564
1.00
14.74
6


ATOM
926
C
TYR
A
121
23.772
15.955
14.924
1.00
15.93
6


ATOM
927
O
TYR
A
121
22.711
15.915
15.556
1.00
16.24
8


ATOM
928
N
ASP
A
122
24.718
15.025
15.039
1.00
16.38
7


ATOM
929
CA
ASP
A
122
24.672
14.013
16.098
1.00
16.43
6


ATOM
930
CB
ASP
A
122
25.795
12.990
15.912
1.00
16.51
6


ATOM
931
CG
ASP
A
122
25.590
11.732
16.752
1.00
17.23
6


ATOM
932
OD1
ASP
A
122
25.727
11.794
17.993
1.00
18.13
8


ATOM
933
OD2
ASP
A
122
25.305
10.676
16.163
1.00
19.91
8


ATOM
934
C
ASP
A
122
24.795
14.695
17.466
1.00
16.67
6


ATOM
935
O
ASP
A
122
25.774
15.387
17.724
1.00
16.39
8


ATOM
936
N
PRO
A
123
23.790
14.501
18.343
1.00
16.80
7


ATOM
937
CA
PRO
A
123
23.777
15.146
19.658
1.00
17.07
6


ATOM
938
CB
PRO
A
123
22.364
14.840
20.188
1.00
17.05
6


ATOM
939
CG
PRO
A
123
21.578
14.389
18.985
1.00
16.74
6


ATOM
940
CD
PRO
A
123
22.579
13.694
18.127
1.00
16.70
6


ATOM
941
C
PRO
A
123
24.813
14.605
20.637
1.00
17.59
6


ATOM
942
O
PRO
A
123
25.054
15.231
21.671
1.00
17.72
8


ATOM
943
N
TYR
A
124
25.425
13.465
20.313
1.00
17.96
7


ATOM
944
CA
TYR
A
124
26.207
12.712
21.299
1.00
18.77
6


ATOM
945
CB
TYR
A
124
25.549
11.360
21.585
1.00
19.53
6


ATOM
946
CG
TYR
A
124
24.102
11.460
21.996
1.00
20.40
6


ATOM
947
CD1
TYR
A
124
23.753
11.839
23.291
1.00
21.05
6


ATOM
948
CE1
TYR
A
124
22.427
11.942
23.675
1.00
21.48
6


ATOM
949
CZ
TYR
A
124
21.428
11.660
22.762
1.00
21.42
6


ATOM
950
OH
TYR
A
124
20.116
11.762
23.149
1.00
22.21
8


ATOM
951
CE2
TYR
A
124
21.744
11.280
21.466
1.00
21.11
6


ATOM
952
CD2
TYR
A
124
23.079
11.182
21.090
1.00
20.18
6


ATOM
953
C
TYR
A
124
27.671
12.494
20.927
1.00
18.59
6


ATOM
954
O
TYR
A
124
28.542
12.529
21.800
1.00
18.82
8


ATOM
955
N
ALA
A
125
27.934
12.262
19.639
1.00
18.17
7


ATOM
956
CA
ALA
A
125
29.252
11.791
19.179
1.00
18.03
6


ATOM
957
CB
ALA
A
125
29.213
11.461
17.684
1.00
17.91
6


ATOM
958
C
ALA
A
125
30.405
12.751
19.485
1.00
17.64
6


ATOM
959
O
ALA
A
125
31.550
12.325
19.629
1.00
18.03
8


ATOM
960
N
TRP
A
126
30.094
14.043
19.579
1.00
17.14
7


ATOM
961
CA
TRP
A
126
31.102
15.086
19.774
1.00
16.85
6


ATOM
962
CB
TRP
A
126
30.440
16.468
19.824
1.00
16.86
6


ATOM
963
CG
TRP
A
126
29.392
16.596
20.903
1.00
16.99
6


ATOM
964
CD1
TRP
A
126
28.079
16.234
20.814
1.00
16.78
6


ATOM
965
NE1
TRP
A
126
27.432
16.499
21.995
1.00
17.08
7


ATOM
966
CE2
TRP
A
126
28.325
17.047
22.880
1.00
16.96
6


ATOM
967
CD2
TRP
A
126
29.575
17.121
22.226
1.00
16.61
6


ATOM
968
CE3
TRP
A
126
30.675
17.646
22.925
1.00
17.18
6


ATOM
969
CZ3
TRP
A
126
30.491
18.072
24.235
1.00
16.50
6


ATOM
970
CH2
TRP
A
126
29.230
17.989
24.858
1.00
16.04
6


ATOM
971
CZ2
TRP
A
126
28.141
17.475
24.201
1.00
16.55
6


ATOM
972
C
TRP
A
126
31.915
14.874
21.044
1.00
16.55
6


ATOM
973
O
TRP
A
126
33.080
15.260
21.109
1.00
16.76
8


ATOM
974
N
SER
A
127
31.293
14.242
22.039
1.00
15.96
7


ATOM
975
CA
SER
A
127
31.850
14.181
23.390
1.00
16.27
6


ATOM
976
CB
SER
A
127
30.724
14.164
24.429
1.00
15.79
6


ATOM
977
OG
SER
A
127
30.123
12.885
24.518
1.00
17.24
8


ATOM
978
C
SER
A
127
32.814
13.018
23.632
1.00
16.11
6


ATOM
979
O
SER
A
127
33.485
12.974
24.669
1.00
15.88
8


ATOM
980
N
TRP
A
128
32.881
12.077
22.691
1.00
16.51
7


ATOM
981
CA
TRP
A
128
33.727
10.894
22.874
1.00
16.47
6


ATOM
982
CB
TRP
A
128
32.901
9.680
23.323
1.00
16.28
6


ATOM
983
CG
TRP
A
128
31.877
9.210
22.328
1.00
16.51
6


ATOM
984
CD1
TRP
A
128
30.561
9.580
22.265
1.00
16.56
6


ATOM
985
NE1
TRP
A
128
29.933
8.922
21.232
1.00
16.33
7


ATOM
986
CE2
TRP
A
128
30.842
8.113
20.602
1.00
16.34
6


ATOM
987
CD2
TRP
A
128
32.078
8.261
21.273
1.00
16.30
6


ATOM
988
CE3
TRP
A
128
33.186
7.529
20.821
1.00
16.23
6


ATOM
989
CZ3
TRP
A
128
33.024
6.678
19.729
1.00
16.51
6


ATOM
990
CH2
TRP
A
128
31.776
6.552
19.084
1.00
16.57
6


ATOM
991
CZ2
TRP
A
128
30.680
7.260
19.503
1.00
15.83
6


ATOM
992
C
TRP
A
128
34.618
10.536
21.684
1.00
16.92
6


ATOM
993
O
TRP
A
128
35.686
9.957
21.875
1.00
16.97
8


ATOM
994
N
GLN
A
129
34.180
10.876
20.469
1.00
17.59
7


ATOM
995
CA
GLN
A
129
34.947
10.560
19.246
1.00
18.35
6


ATOM
996
CB
GLN
A
129
34.151
10.940
17.993
1.00
18.24
6


ATOM
997
CG
GLN
A
129
32.995
9.992
17.663
1.00
19.55
6


ATOM
998
CD
GLN
A
129
32.395
10.239
16.279
1.00
20.30
6


ATOM
999
OE1
GLN
A
129
32.560
11.315
15.698
1.00
22.16
8


ATOM
1000
NE2
GLN
A
129
31.704
9.231
15.741
1.00
21.07
7


ATOM
1001
C
GLN
A
129
36.302
11.273
19.228
1.00
18.43
6


ATOM
1002
O
GLN
A
129
36.453
12.326
19.834
1.00
18.58
8


ATOM
1003
N
HIS
A
130
37.276
10.689
18.526
1.00
19.05
7


ATOM
1004
CA
HIS
A
130
38.622
11.283
18.385
1.00
19.20
6


ATOM
1005
CB
HIS
A
130
38.577
12.608
17.599
1.00
19.81
6


ATOM
1006
CG
HIS
A
130
37.703
12.578
16.381
1.00
20.84
6


ATOM
1007
ND1
HIS
A
130
37.977
11.791
15.283
1.00
22.57
7


ATOM
1008
CE1
HIS
A
130
37.049
11.986
14.363
1.00
22.36
6


ATOM
1009
NE2
HIS
A
130
36.190
12.879
14.818
1.00
22.91
7


ATOM
1010
CD2
HIS
A
130
36.580
13.272
16.076
1.00
21.95
6


ATOM
1011
C
HIS
A
130
39.324
11.522
19.736
1.00
18.98
6


ATOM
1012
O
HIS
A
130
40.096
12.480
19.881
1.00
19.06
8


ATOM
1013
N
ASP
A
131
39.053
10.653
20.712
1.00
18.67
7


ATOM
1014
CA
ASP
A
131
39.667
10.729
22.048
1.00
18.57
6


ATOM
1015
CB
ASP
A
131
41.205
10.794
21.961
1.00
19.43
6


ATOM
1016
CG
ASP
A
131
41.827
9.483
21.524
1.00
21.89
6


ATOM
1017
OD1
ASP
A
131
41.223
8.409
21.765
1.00
24.99
8


ATOM
1018
OD2
ASP
A
131
42.940
9.526
20.948
1.00
24.98
8


ATOM
1019
C
ASP
A
131
39.151
11.896
22.893
1.00
17.54
6


ATOM
1020
O
ASP
A
131
39.745
12.229
23.924
1.00
17.28
8


ATOM
1021
N
ASN
A
132
38.045
12.505
22.469
1.00
16.25
7


ATOM
1022
CA
ASN
A
132
37.463
13.610
23.220
1.00
15.55
6


ATOM
1023
CB
ASN
A
132
36.412
14.353
22.389
1.00
15.22
6


ATOM
1024
CG
ASN
A
132
37.032
15.280
21.355
1.00
15.64
6


ATOM
1025
OD1
ASN
A
132
38.237
15.257
21.128
1.00
15.95
8


ATOM
1026
ND2
ASN
A
132
36.197
16.106
20.721
1.00
15.87
7


ATOM
1027
C
ASN
A
132
36.869
13.164
24.551
1.00
15.12
6


ATOM
1028
O
ASN
A
132
36.631
11.979
24.772
1.00
15.02
8


ATOM
1029
N
SER
A
133
36.645
14.125
25.439
1.00
14.92
7


ATOM
1030
CA
SER
A
133
36.028
13.847
26.725
1.00
14.40
6


ATOM
1031
CB
SER
A
133
37.088
13.418
27.745
1.00
14.47
6


ATOM
1032
OG
SER
A
133
37.968
14.493
28.064
1.00
13.85
8


ATOM
1033
C
SER
A
133
35.291
15.074
27.216
1.00
14.57
6


ATOM
1034
O
SER
A
133
35.308
16.122
26.563
1.00
14.41
8


ATOM
1035
N
ARG
A
134
34.629
14.937
28.356
1.00
14.55
7


ATOM
1036
CA
ARG
A
134
34.045
16.082
29.016
1.00
14.90
6


ATOM
1037
CB
ARG
A
134
32.540
16.203
28.744
1.00
15.97
6


ATOM
1038
CG
ARG
A
134
31.667
15.070
29.258
1.00
17.72
6


ATOM
1039
CD
ARG
A
134
30.207
15.397
28.947
1.00
22.47
6


ATOM
1040
NE
ARG
A
134
29.281
14.322
29.286
1.00
24.59
7


ATOM
1041
CZ
ARG
A
134
27.960
14.474
29.361
1.00
25.83
6


ATOM
1042
NH1
ARG
A
134
27.406
15.662
29.130
1.00
27.15
7


ATOM
1043
NH2
ARG
A
134
27.190
13.444
29.673
1.00
26.83
7


ATOM
1044
C
ARG
A
134
34.357
16.072
30.495
1.00
14.31
6


ATOM
1045
O
ARG
A
134
34.701
15.038
31.062
1.00
14.01
8


ATOM
1046
N
TRP
A
135
34.255
17.244
31.099
1.00
13.27
7


ATOM
1047
CA
TRP
A
135
34.474
17.420
32.516
1.00
12.49
6


ATOM
1048
CB
TRP
A
135
35.961
17.659
32.796
1.00
12.56
6


ATOM
1049
CG
TRP
A
135
36.408
17.280
34.188
1.00
11.49
6


ATOM
1050
CD1
TRP
A
135
35.770
16.432
35.062
1.00
11.76
6


ATOM
1051
NE1
TRP
A
135
36.497
16.317
36.225
1.00
10.56
7


ATOM
1052
CE2
TRP
A
135
37.628
17.085
36.123
1.00
11.76
6


ATOM
1053
CD2
TRP
A
135
37.613
17.697
34.847
1.00
12.04
6


ATOM
1054
CE3
TRP
A
135
38.679
18.541
34.488
1.00
12.85
6


ATOM
1055
CZ3
TRP
A
135
39.709
18.742
35.401
1.00
12.12
6


ATOM
1056
CH2
TRP
A
135
39.696
18.115
36.662
1.00
12.51
6


ATOM
1057
CZ2
TRP
A
135
38.670
17.292
37.042
1.00
11.64
6


ATOM
1058
C
TRP
A
135
33.636
18.618
32.930
1.00
12.61
6


ATOM
1059
O
TRP
A
135
33.064
19.309
32.081
1.00
12.34
8


ATOM
1060
N
ASP
A
136
33.529
18.847
34.230
1.00
12.04
7


ATOM
1061
CA
ASP
A
136
32.679
19.909
34.755
1.00
12.12
6


ATOM
1062
CB
ASP
A
136
31.253
19.383
34.960
1.00
12.12
6


ATOM
1063
CG
ASP
A
136
30.251
20.482
35.336
1.00
13.38
6


ATOM
1064
OD1
ASP
A
136
30.663
21.538
35.856
1.00
14.75
8


ATOM
1065
OD2
ASP
A
136
29.034
20.266
35.122
1.00
14.58
8


ATOM
1066
C
ASP
A
136
33.272
20.317
36.083
1.00
12.00
6


ATOM
1067
O
ASP
A
136
33.411
19.484
36.968
1.00
12.06
8


ATOM
1068
N
LEU
A
137
33.646
21.593
36.210
1.00
12.04
7


ATOM
1069
CA
LEU
A
137
34.324
22.074
37.420
1.00
12.35
6


ATOM
1070
CB
LEU
A
137
35.080
23.390
37.160
1.00
12.51
6


ATOM
1071
CG
LEU
A
137
36.546
23.321
36.699
1.00
14.36
6


ATOM
1072
CD1
LEU
A
137
37.426
22.512
37.646
1.00
16.05
6


ATOM
1073
CD2
LEU
A
137
36.661
22.802
35.268
1.00
13.72
6


ATOM
1074
C
LEU
A
137
33.405
22.220
38.625
1.00
12.12
6


ATOM
1075
O
LEU
A
137
33.879
22.289
39.763
1.00
12.23
8


ATOM
1076
N
LEU
A
138
32.095
22.257
38.390
1.00
11.86
7


ATOM
1077
CA
LEU
A
138
31.146
22.370
39.495
1.00
12.24
6


ATOM
1078
CB
LEU
A
138
29.699
22.480
38.989
1.00
12.09
6


ATOM
1079
CG
LEU
A
138
28.598
22.428
40.069
1.00
11.81
6


ATOM
1080
CD1
LEU
A
138
28.788
23.517
41.123
1.00
12.67
6


ATOM
1081
CD2
LEU
A
138
27.215
22.524
39.444
1.00
12.98
6


ATOM
1082
C
LEU
A
138
31.284
21.209
40.483
1.00
12.62
6


ATOM
1083
O
LEU
A
138
31.443
21.430
41.685
1.00
12.80
8


ATOM
1084
N
ASP
A
139
31.213
19.972
39.988
1.00
13.12
7


ATOM
1085
CA
ASP
A
139
31.338
18.826
40.884
1.00
13.51
6


ATOM
1086
CB
ASP
A
139
30.817
17.531
40.245
1.00
14.42
6


ATOM
1087
CG
ASP
A
139
29.290
17.425
40.285
1.00
16.19
6


ATOM
1088
OD1
ASP
A
139
28.627
18.220
41.000
1.00
18.88
8


ATOM
1089
OD2
ASP
A
139
28.748
16.530
39.603
1.00
20.15
8


ATOM
1090
C
ASP
A
139
32.760
18.660
41.420
1.00
12.95
6


ATOM
1091
O
ASP
A
139
32.950
18.092
42.483
1.00
13.00
8


ATOM
1092
N
VAL
A
140
33.746
19.205
40.708
1.00
12.48
7


ATOM
1093
CA
VAL
A
140
35.117
19.273
41.230
1.00
11.93
6


ATOM
1094
CB
VAL
A
140
36.128
19.770
40.153
1.00
11.93
6


ATOM
1095
CG1
VAL
A
140
37.510
20.050
40.779
1.00
11.40
6


ATOM
1096
CG2
VAL
A
140
36.247
18.750
39.015
1.00
11.91
6


ATOM
1097
C
VAL
A
140
35.183
20.156
42.489
1.00
11.81
6


ATOM
1098
O
VAL
A
140
35.746
19.749
43.512
1.00
11.72
8


ATOM
1099
N
MET
A
141
34.585
21.348
42.424
1.00
11.06
7


ATOM
1100
CA
MET
A
141
34.556
22.246
43.589
1.00
10.98
6


ATOM
1101
CB
MET
A
141
33.934
23.610
43.238
1.00
11.16
6


ATOM
1102
CG
MET
A
141
34.693
24.428
42.186
1.00
11.87
6


ATOM
1103
SD
MET
A
141
36.491
24.451
42.337
1.00
14.74
16


ATOM
1104
CE
MET
A
141
36.734
25.126
43.973
1.00
15.71
6


ATOM
1105
C
MET
A
141
33.802
21.601
44.750
1.00
10.49
6


ATOM
1106
O
MET
A
141
34.245
21.670
45.897
1.00
10.83
8


ATOM
1107
N
ARG
A
142
32.668
20.960
44.447
1.00
10.16
7


ATOM
1108
CA
ARG
A
142
31.880
20.264
45.469
1.00
10.59
6


ATOM
1109
CB
ARG
A
142
30.614
19.665
44.859
1.00
10.26
6


ATOM
1110
CG
ARG
A
142
29.550
20.695
44.532
1.00
10.62
6


ATOM
1111
CD
ARG
A
142
28.331
20.039
43.915
1.00
12.16
6


ATOM
1112
NE
ARG
A
142
27.202
20.963
43.822
1.00
14.23
7


ATOM
1113
CZ
ARG
A
142
26.296
20.940
42.845
1.00
14.32
6


ATOM
1114
NH1
ARG
A
142
26.387
20.039
41.863
1.00
15.14
7


ATOM
1115
NH2
ARG
A
142
25.302
21.817
42.847
1.00
15.34
7


ATOM
1116
C
ARG
A
142
32.691
19.166
46.146
1.00
10.62
6


ATOM
1117
O
ARG
A
142
32.651
19.016
47.365
1.00
11.76
8


ATOM
1118
N
ALA
A
143
33.415
18.398
45.335
1.00
11.35
7


ATOM
1119
CA
ALA
A
143
34.258
17.320
45.819
1.00
11.68
6


ATOM
1120
CB
ALA
A
143
34.841
16.521
44.638
1.00
11.74
6


ATOM
1121
C
ALA
A
143
35.372
17.847
46.727
1.00
12.02
6


ATOM
1122
O
ALA
A
143
35.670
17.240
47.747
1.00
12.10
8


ATOM
1123
N
CYS
A
144
35.975
18.979
46.359
1.00
12.27
7


ATOM
1124
CA
CYS
A
144
37.004
19.602
47.203
1.00
13.89
6


ATOM
1125
CB
CYS
A
144
37.589
20.847
46.543
1.00
13.89
6


ATOM
1126
SG
CYS
A
144
38.736
20.503
45.219
1.00
19.77
16


ATOM
1127
C
CYS
A
144
36.450
19.976
48.559
1.00
13.44
6


ATOM
1128
O
CYS
A
144
37.067
19.694
49.578
1.00
13.92
8


ATOM
1129
N
TYR
A
145
35.284
20.620
48.567
1.00
13.37
7


ATOM
1130
CA
TYR
A
145
34.666
21.061
49.810
1.00
13.40
6


ATOM
1131
CB
TYR
A
145
33.370
21.828
49.526
1.00
13.97
6


ATOM
1132
CG
TYR
A
145
32.588
22.149
50.779
1.00
13.99
6


ATOM
1133
CD1
TYR
A
145
32.935
23.246
51.581
1.00
17.07
6


ATOM
1134
CE1
TYR
A
145
32.232
23.534
52.741
1.00
15.19
6


ATOM
1135
CZ
TYR
A
145
31.172
22.723
53.121
1.00
14.57
6


ATOM
1136
OH
TYR
A
145
30.480
23.014
54.275
1.00
15.08
8


ATOM
1137
CE2
TYR
A
145
30.810
21.621
52.349
1.00
13.56
6


ATOM
1138
CD2
TYR
A
145
31.525
21.335
51.192
1.00
12.90
6


ATOM
1139
C
TYR
A
145
34.379
19.889
50.739
1.00
13.12
6


ATOM
1140
O
TYR
A
145
34.623
19.969
51.945
1.00
12.83
8


ATOM
1141
N
ALA
A
146
33.845
18.810
50.175
1.00
12.30
7


ATOM
1142
CA
ALA
A
146
33.457
17.654
50.966
1.00
12.79
6


ATOM
1143
CB
ALA
A
146
32.519
16.769
50.173
1.00
12.80
6


ATOM
1144
C
ALA
A
146
34.673
16.860
51.413
1.00
12.62
6


ATOM
1145
O
ALA
A
146
34.772
16.460
52.572
1.00
12.86
8


ATOM
1146
N
LEU
A
147
35.607
16.654
50.488
1.00
12.83
7


ATOM
1147
CA
LEU
A
147
36.637
15.641
50.669
1.00
12.59
6


ATOM
1148
CB
LEU
A
147
36.780
14.785
49.403
1.00
12.65
6


ATOM
1149
CG
LEU
A
147
35.555
14.040
48.868
1.00
12.45
6


ATOM
1150
CD1
LEU
A
147
35.883
13.423
47.531
1.00
11.07
6


ATOM
1151
CD2
LEU
A
147
35.053
12.971
49.835
1.00
11.34
6


ATOM
1152
C
LEU
A
147
37.998
16.183
51.072
1.00
12.61
6


ATOM
1153
O
LEU
A
147
38.724
15.534
51.821
1.00
13.21
8


ATOM
1154
N
ARG
A
148
38.349
17.360
50.556
1.00
12.50
7


ATOM
1155
CA
ARG
A
148
39.688
17.928
50.741
1.00
12.23
6


ATOM
1156
CB
ARG
A
148
40.611
17.529
49.574
1.00
12.30
6


ATOM
1157
CG
ARG
A
148
40.894
16.025
49.431
1.00
12.32
6


ATOM
1158
CD
ARG
A
148
41.714
15.480
50.600
1.00
13.52
6


ATOM
1159
NE
ARG
A
148
42.100
14.080
50.409
1.00
15.56
7


ATOM
1160
CZ
ARG
A
148
41.340
13.038
50.745
1.00
15.44
6


ATOM
1161
NH1
ARG
A
148
40.146
13.232
51.289
1.00
14.42
7


ATOM
1162
NH2
ARG
A
148
41.773
11.799
50.530
1.00
16.11
7


ATOM
1163
C
ARG
A
148
39.604
19.456
50.832
1.00
11.99
6


ATOM
1164
O
ARG
A
148
40.122
20.155
49.961
1.00
11.82
8


ATOM
1165
N
PRO
A
149
38.924
19.979
51.878
1.00
12.09
7


ATOM
1166
CA
PRO
A
149
38.625
21.426
51.933
1.00
12.04
6


ATOM
1167
CB
PRO
A
149
37.615
21.524
53.079
1.00
12.21
6


ATOM
1168
CG
PRO
A
149
37.973
20.382
53.978
1.00
11.98
6


ATOM
1169
CD
PRO
A
149
38.353
19.263
53.032
1.00
11.95
6


ATOM
1170
C
PRO
A
149
39.824
22.344
52.217
1.00
11.96
6


ATOM
1171
O
PRO
A
149
39.710
23.570
52.057
1.00
11.64
8


ATOM
1172
N
GLU
A
150
40.960
21.769
52.598
1.00
12.34
7


ATOM
1173
CA
GLU
A
150
42.139
22.575
52.983
1.00
13.08
6


ATOM
1174
CB
GLU
A
150
43.264
21.668
53.490
1.00
12.78
6


ATOM
1175
CG
GLU
A
150
44.601
22.384
53.677
1.00
13.74
6


ATOM
1176
CD
GLU
A
150
45.738
21.444
54.056
1.00
14.91
6


ATOM
1177
OE1
GLU
A
150
45.483
20.243
54.303
1.00
18.13
8


ATOM
1178
OE2
GLU
A
150
46.893
21.915
54.113
1.00
18.64
8


ATOM
1179
C
GLU
A
150
42.659
23.496
51.860
1.00
13.48
6


ATOM
1180
O
GLU
A
150
42.866
23.054
50.718
1.00
13.90
8


ATOM
1181
N
GLY
A
151
42.863
24.770
52.192
1.00
13.52
7


ATOM
1182
CA
GLY
A
151
43.538
25.705
51.285
1.00
13.84
6


ATOM
1183
C
GLY
A
151
42.630
26.597
50.456
1.00
14.13
6


ATOM
1184
O
GLY
A
151
43.085
27.570
49.851
1.00
14.44
8


ATOM
1185
N
ILE
A
152
41.344
26.276
50.433
1.00
14.41
7


ATOM
1186
CA
ILE
A
152
40.372
27.077
49.704
1.00
14.85
6


ATOM
1187
CB
ILE
A
152
39.660
26.223
48.617
1.00
14.98
6


ATOM
1188
CG1
ILE
A
152
40.684
25.742
47.587
1.00
15.34
6


ATOM
1189
CD1
ILE
A
152
40.199
24.605
46.716
1.00
16.38
6


ATOM
1190
CG2
ILE
A
152
38.543
27.006
47.936
1.00
16.02
6


ATOM
1191
C
ILE
A
152
39.358
27.713
50.651
1.00
14.69
6


ATOM
1192
O
ILE
A
152
38.902
27.078
51.588
1.00
14.63
8


ATOM
1193
N
ASN
A
153
39.023
28.977
50.403
1.00
14.67
7


ATOM
1194
CA
ASN
A
153
37.954
29.642
51.135
1.00
15.20
6


ATOM
1195
CB
ASN
A
153
38.106
31.167
51.063
1.00
15.27
6


ATOM
1196
CG
ASN
A
153
39.343
31.674
51.804
1.00
17.87
6


ATOM
1197
OD1
ASN
A
153
40.004
32.618
51.356
1.00
21.55
8


ATOM
1198
ND2
ASN
A
153
39.657
31.053
52.945
1.00
19.96
7


ATOM
1199
C
ASN
A
153
36.596
29.219
50.597
1.00
14.76
6


ATOM
1200
O
ASN
A
153
36.330
29.330
49.393
1.00
15.14
8


ATOM
1201
N
TRP
A
154
35.747
28.724
51.493
1.00
14.52
7


ATOM
1202
CA
TRP
A
154
34.435
28.212
51.118
1.00
14.46
6


ATOM
1203
CB
TRP
A
154
34.233
26.802
51.671
1.00
13.79
6


ATOM
1204
CG
TRP
A
154
35.263
25.856
51.161
1.00
12.68
6


ATOM
1205
CD1
TRP
A
154
36.330
25.352
51.850
1.00
12.25
6


ATOM
1206
NE1
TRP
A
154
37.071
24.524
51.037
1.00
12.34
7


ATOM
1207
CE2
TRP
A
154
36.500
24.499
49.791
1.00
11.74
6


ATOM
1208
CD2
TRP
A
154
35.355
25.330
49.833
1.00
11.94
6


ATOM
1209
CE3
TRP
A
154
34.577
25.473
48.676
1.00
11.13
6


ATOM
1210
CZ3
TRP
A
154
34.960
24.797
47.530
1.00
11.51
6


ATOM
1211
CH2
TRP
A
154
36.104
23.973
47.515
1.00
12.83
6


ATOM
1212
CZ2
TRP
A
154
36.885
23.811
48.635
1.00
11.80
6


ATOM
1213
C
TRP
A
154
33.327
29.154
51.580
1.00
15.21
6


ATOM
1214
O
TRP
A
154
32.987
29.190
52.764
1.00
15.69
8


ATOM
1215
N
PRO
A
155
32.757
29.918
50.637
1.00
15.87
7


ATOM
1216
CA
PRO
A
155
31.777
30.943
50.981
1.00
15.97
6


ATOM
1217
CB
PRO
A
155
31.670
31.761
49.691
1.00
15.86
6


ATOM
1218
CG
PRO
A
155
31.977
30.806
48.617
1.00
16.20
6


ATOM
1219
CD
PRO
A
155
33.003
29.857
49.180
1.00
15.99
6


ATOM
1220
C
PRO
A
155
30.417
30.347
51.343
1.00
16.18
6


ATOM
1221
O
PRO
A
155
30.048
29.291
50.835
1.00
15.97
8


ATOM
1222
N
GLU
A
156
29.700
31.025
52.236
1.00
16.45
7


ATOM
1223
CA
GLU
A
156
28.339
30.650
52.606
1.00
16.71
6


ATOM
1224
CB
GLU
A
156
28.135
30.795
54.101
1.00
17.19
6


ATOM
1225
CG
GLU
A
156
28.584
29.622
54.927
1.00
19.16
6


ATOM
1226
CD
GLU
A
156
28.212
29.791
56.388
1.00
22.32
6


ATOM
1227
OE1
GLU
A
156
27.408
30.699
56.699
1.00
24.65
8


ATOM
1228
OE2
GLU
A
156
28.727
29.024
57.223
1.00
23.32
8


ATOM
1229
C
GLU
A
156
27.367
31.578
51.923
1.00
16.31
6


ATOM
1230
O
GLU
A
156
27.601
32.791
51.868
1.00
16.58
8


ATOM
1231
N
ASN
A
157
26.255
31.029
51.439
1.00
15.73
7


ATOM
1232
CA
ASN
A
157
25.196
31.870
50.874
1.00
15.61
6


ATOM
1233
CB
ASN
A
157
24.352
31.096
49.852
1.00
15.40
6


ATOM
1234
CG
ASN
A
157
23.648
29.890
50.450
1.00
15.22
6


ATOM
1235
OD1
ASN
A
157
23.247
29.898
51.614
1.00
14.29
8


ATOM
1236
ND2
ASN
A
157
23.476
28.845
49.639
1.00
13.74
7


ATOM
1237
C
ASN
A
157
24.331
32.505
51.976
1.00
15.47
6


ATOM
1238
O
ASN
A
157
24.559
32.257
53.157
1.00
15.71
8


ATOM
1239
N
ASP
A
158
23.343
33.313
51.580
1.00
15.83
7


ATOM
1240
CA
ASP
A
158
22.492
34.047
52.541
1.00
15.56
6


ATOM
1241
CB
ASP
A
158
21.543
35.004
51.810
1.00
16.35
6


ATOM
1242
CG
ASP
A
158
22.263
36.185
51.175
1.00
18.10
6


ATOM
1243
OD1
ASP
A
158
23.376
36.535
51.626
1.00
19.35
8


ATOM
1244
OD2
ASP
A
158
21.703
36.770
50.220
1.00
20.70
8


ATOM
1245
C
ASP
A
158
21.671
33.131
53.449
1.00
14.72
6


ATOM
1246
O
ASP
A
158
21.087
33.585
54.441
1.00
14.75
8


ATOM
1247
N
ASP
A
159
21.633
31.845
53.110
1.00
13.87
7


ATOM
1248
CA
ASP
A
159
20.880
30.867
53.879
1.00
13.04
6


ATOM
1249
CB
ASP
A
159
20.162
29.885
52.942
1.00
13.41
6


ATOM
1250
CG
ASP
A
159
19.082
30.567
52.095
1.00
13.56
6


ATOM
1251
OD1
ASP
A
159
18.644
31.680
52.470
1.00
15.49
8


ATOM
1252
OD2
ASP
A
159
18.663
29.991
51.071
1.00
14.66
8


ATOM
1253
C
ASP
A
159
21.759
30.129
54.891
1.00
12.70
6


ATOM
1254
O
ASP
A
159
21.250
29.400
55.732
1.00
12.09
8


ATOM
1255
N
GLY
A
160
23.074
30.351
54.815
1.00
12.05
7


ATOM
1256
CA
GLY
A
160
24.028
29.751
55.758
1.00
12.10
6


ATOM
1257
C
GLY
A
160
24.553
28.401
55.312
1.00
11.86
6


ATOM
1258
O
GLY
A
160
25.075
27.625
56.122
1.00
11.81
8


ATOM
1259
N
LEU
A
161
24.432
28.134
54.015
1.00
11.86
7


ATOM
1260
CA
LEU
A
161
24.862
26.870
53.420
1.00
11.83
6


ATOM
1261
CB
LEU
A
161
23.715
26.245
52.611
1.00
12.11
6


ATOM
1262
CG
LEU
A
161
22.433
25.881
53.366
1.00
12.70
6


ATOM
1263
CD1
LEU
A
161
21.265
25.734
52.416
1.00
12.37
6


ATOM
1264
CD2
LEU
A
161
22.622
24.615
54.208
1.00
12.62
6


ATOM
1265
C
LEU
A
161
26.050
27.115
52.502
1.00
11.84
6


ATOM
1266
O
LEU
A
161
26.169
28.200
51.925
1.00
11.42
8


ATOM
1267
N
PRO
A
162
26.931
26.104
52.348
1.00
12.16
7


ATOM
1268
CA
PRO
A
162
28.066
26.304
51.451
1.00
12.38
6


ATOM
1269
CB
PRO
A
162
28.793
24.955
51.469
1.00
12.71
6


ATOM
1270
CG
PRO
A
162
27.841
23.982
52.074
1.00
12.59
6


ATOM
1271
CD
PRO
A
162
26.924
24.762
52.958
1.00
12.59
6


ATOM
1272
C
PRO
A
162
27.563
26.613
50.055
1.00
12.51
6


ATOM
1273
O
PRO
A
162
26.634
25.959
49.575
1.00
12.79
8


ATOM
1274
N
SER
A
163
28.161
27.619
49.428
1.00
13.08
7


ATOM
1275
CA
SER
A
163
27.755
28.063
48.099
1.00
13.05
6


ATOM
1276
CB
SER
A
163
27.612
29.582
48.065
1.00
13.35
6


ATOM
1277
OG
SER
A
163
27.218
30.022
46.775
1.00
14.58
8


ATOM
1278
C
SER
A
163
28.760
27.622
47.038
1.00
13.31
6


ATOM
1279
O
SER
A
163
29.970
27.653
47.266
1.00
13.16
8


ATOM
1280
N
PHE
A
164
28.250
27.231
45.877
1.00
13.51
7


ATOM
1281
CA
PHE
A
164
29.109
26.833
44.771
1.00
13.47
6


ATOM
1282
CB
PHE
A
164
29.028
25.323
44.549
1.00
13.49
6


ATOM
1283
CG
PHE
A
164
29.461
24.538
45.742
1.00
12.97
6


ATOM
1284
CD1
PHE
A
164
30.812
24.293
45.974
1.00
14.02
6


ATOM
1285
CE1
PHE
A
164
31.222
23.597
47.108
1.00
11.87
6


ATOM
1286
CZ
PHE
A
164
30.286
23.156
48.027
1.00
12.69
6


ATOM
1287
CE2
PHE
A
164
28.939
23.411
47.825
1.00
13.71
6


ATOM
1288
CD2
PHE
A
164
28.530
24.112
46.687
1.00
12.87
6


ATOM
1289
C
PHE
A
164
28.825
27.620
43.498
1.00
14.18
6


ATOM
1290
O
PHE
A
164
29.220
27.219
42.404
1.00
14.01
8


ATOM
1291
N
ARG
A
165
28.172
28.766
43.655
1.00
14.63
7


ATOM
1292
CA
ARG
A
165
28.023
29.702
42.557
1.00
15.46
6


ATOM
1293
CB
ARG
A
165
27.098
30.853
42.954
1.00
15.36
6


ATOM
1294
CG
ARG
A
165
25.681
30.390
43.284
1.00
17.75
6


ATOM
1295
CD
ARG
A
165
24.836
31.512
43.852
1.00
19.73
6


ATOM
1296
NE
ARG
A
165
24.649
32.605
42.900
1.00
22.69
7


ATOM
1297
CZ
ARG
A
165
23.933
33.701
43.146
1.00
24.60
6


ATOM
1298
NH1
ARG
A
165
23.326
33.862
44.321
1.00
25.88
7


ATOM
1299
NH2
ARG
A
165
23.824
34.642
42.217
1.00
26.54
7


ATOM
1300
C
ARG
A
165
29.404
30.217
42.169
1.00
15.30
6


ATOM
1301
O
ARG
A
165
30.214
30.568
43.029
1.00
14.95
8


ATOM
1302
N
LEU
A
166
29.680
30.222
40.870
1.00
15.78
7


ATOM
1303
CA
LEU
A
166
31.001
30.585
40.377
1.00
16.42
6


ATOM
1304
CB
LEU
A
166
31.007
30.595
38.841
1.00
16.03
6


ATOM
1305
CG
LEU
A
166
32.331
30.772
38.095
1.00
17.33
6


ATOM
1306
CD1
LEU
A
166
33.346
29.702
38.482
1.00
17.51
6


ATOM
1307
CD2
LEU
A
166
32.061
30.734
36.606
1.00
16.48
6


ATOM
1308
C
LEU
A
166
31.452
31.933
40.935
1.00
16.73
6


ATOM
1309
O
LEU
A
166
32.602
32.086
41.354
1.00
17.53
8


ATOM
1310
N
GLU
A
167
30.531
32.894
40.963
1.00
17.35
7


ATOM
1311
CA
GLU
A
167
30.828
34.251
41.414
1.00
17.88
6


ATOM
1312
CB
GLU
A
167
29.680
35.220
41.062
1.00
18.44
6


ATOM
1313
CG
GLU
A
167
28.287
34.794
41.560
1.00
20.26
6


ATOM
1314
CD
GLU
A
167
27.475
34.050
40.509
1.00
23.46
6


ATOM
1315
OE1
GLU
A
167
28.039
33.172
39.813
1.00
23.39
8


ATOM
1316
OE2
GLU
A
167
26.258
34.346
40.378
1.00
25.10
8


ATOM
1317
C
GLU
A
167
31.199
34.364
42.902
1.00
17.77
6


ATOM
1318
O
GLU
A
167
31.981
35.233
43.275
1.00
18.10
8


ATOM
1319
N
HIS
A
168
30.643
33.481
43.736
1.00
17.07
7


ATOM
1320
CA
HIS
A
168
30.955
33.464
45.170
1.00
16.85
6


ATOM
1321
CB
HIS
A
168
29.894
32.690
45.959
1.00
16.71
6


ATOM
1322
CG
HIS
A
168
28.561
33.366
46.007
1.00
16.61
6


ATOM
1323
ND1
HIS
A
168
27.399
32.694
46.318
1.00
17.09
7


ATOM
1324
CE1
HIS
A
168
26.384
33.540
46.296
1.00
17.64
6


ATOM
1325
NE2
HIS
A
168
26.844
34.733
45.963
1.00
17.96
7


ATOM
1326
CD2
HIS
A
168
28.202
34.652
45.780
1.00
16.80
6


ATOM
1327
C
HIS
A
168
32.322
32.860
45.425
1.00
16.62
6


ATOM
1328
O
HIS
A
168
33.074
33.339
46.282
1.00
16.69
8


ATOM
1329
N
LEU
A
169
32.636
31.803
44.680
1.00
16.15
7


ATOM
1330
CA
LEU
A
169
33.910
31.102
44.810
1.00
16.47
6


ATOM
1331
CB
LEU
A
169
33.852
29.744
44.101
1.00
16.52
6


ATOM
1332
CG
LEU
A
169
33.013
28.638
44.747
1.00
16.98
6


ATOM
1333
CD1
LEU
A
169
32.795
27.495
43.772
1.00
17.70
6


ATOM
1334
CD2
LEU
A
169
33.651
28.130
46.041
1.00
16.82
6


ATOM
1335
C
LEU
A
169
35.095
31.929
44.304
1.00
16.48
6


ATOM
1336
O
LEU
A
169
36.181
31.862
44.870
1.00
16.35
8


ATOM
1337
N
THR
A
170
34.888
32.713
43.243
1.00
16.89
7


ATOM
1338
CA
THR
A
170
35.937
33.633
42.776
1.00
17.53
6


ATOM
1339
CB
THR
A
170
35.633
34.242
41.390
1.00
17.67
6


ATOM
1340
OG1
THR
A
170
34.336
34.850
41.402
1.00
17.23
8


ATOM
1341
CG2
THR
A
170
35.682
33.173
40.312
1.00
17.43
6


ATOM
1342
C
THR
A
170
36.189
34.751
43.790
1.00
17.94
6


ATOM
1343
O
THR
A
170
37.324
34.955
44.217
1.00
18.14
8


ATOM
1344
N
LYS
A
171
35.122
35.449
44.189
1.00
18.32
7


ATOM
1345
CA
LYS
A
171
35.209
36.521
45.189
1.00
18.97
6


ATOM
1346
CB
LYS
A
171
33.816
37.109
45.467
1.00
18.97
6


ATOM
1347
CG
LYS
A
171
33.816
38.417
46.259
1.00
21.23
6


ATOM
1348
CD
LYS
A
171
34.155
39.612
45.371
1.00
24.05
6


ATOM
1349
CE
LYS
A
171
33.873
40.924
46.088
1.00
25.72
6


ATOM
1350
NZ
LYS
A
171
33.961
42.096
45.167
1.00
27.61
7


ATOM
1351
C
LYS
A
171
35.845
36.050
46.500
1.00
19.09
6


ATOM
1352
O
LYS
A
171
36.670
36.757
47.090
1.00
18.84
8


ATOM
1353
N
ALA
A
172
35.461
34.857
46.949
1.00
19.24
7


ATOM
1354
CA
ALA
A
172
35.952
34.309
48.215
1.00
19.56
6


ATOM
1355
CB
ALA
A
172
35.125
33.100
48.622
1.00
19.46
6


ATOM
1356
C
ALA
A
172
37.442
33.952
48.188
1.00
19.94
6


ATOM
1357
O
ALA
A
172
38.077
33.852
49.235
1.00
19.66
8


ATOM
1358
N
ASN
A
173
37.989
33.756
46.991
1.00
20.95
7


ATOM
1359
CA
ASN
A
173
39.381
33.325
46.853
1.00
21.67
6


ATOM
1360
CB
ASN
A
173
39.447
31.940
46.200
1.00
21.38
6


ATOM
1361
CG
ASN
A
173
38.875
30.855
47.090
1.00
20.21
6


ATOM
1362
OD1
ASN
A
173
37.723
30.445
46.933
1.00
19.52
8


ATOM
1363
ND2
ASN
A
173
39.669
30.403
48.051
1.00
17.17
7


ATOM
1364
C
ASN
A
173
40.269
34.337
46.124
1.00
22.78
6


ATOM
1365
O
ASN
A
173
41.377
34.005
45.688
1.00
22.90
8


ATOM
1366
N
GLY
A
174
39.778
35.571
46.011
1.00
23.91
7


ATOM
1367
CA
GLY
A
174
40.559
36.684
45.461
1.00
25.64
6


ATOM
1368
C
GLY
A
174
40.823
36.599
43.970
1.00
26.95
6


ATOM
1369
O
GLY
A
174
41.813
37.143
43.475
1.00
27.21
8


ATOM
1370
N
ILE
A
175
39.932
35.923
43.251
1.00
28.25
7


ATOM
1371
CA
ILE
A
175
40.046
35.781
41.803
1.00
29.65
6


ATOM
1372
CB
ILE
A
175
39.584
34.375
41.333
1.00
29.60
6


ATOM
1373
CG1
ILE
A
175
40.532
33.295
41.871
1.00
29.47
6


ATOM
1374
CD1
ILE
A
175
39.986
31.867
41.768
1.00
29.87
6


ATOM
1375
CG2
ILE
A
175
39.491
34.317
39.806
1.00
29.44
6


ATOM
1376
C
ILE
A
175
39.237
36.865
41.088
1.00
30.74
6


ATOM
1377
O
ILE
A
175
38.020
36.970
41.276
1.00
30.58
8


ATOM
1378
N
GLU
A
176
39.922
37.670
40.273
1.00
32.23
7


ATOM
1379
CA
GLU
A
176
39.269
38.732
39.498
1.00
33.84
6


ATOM
1380
CB
GLU
A
176
40.300
39.590
38.744
1.00
33.85
6


ATOM
1381
CG
GLU
A
176
41.406
38.801
38.025
1.00
34.65
6


ATOM
1382
CD
GLU
A
176
42.385
39.702
37.268
1.00
35.04
6


ATOM
1383
OE1
GLU
A
176
41.927
40.606
36.532
1.00
36.26
8


ATOM
1384
OE2
GLU
A
176
43.615
39.496
37.403
1.00
36.02
8


ATOM
1385
C
GLU
A
176
38.212
38.170
38.542
1.00
34.48
6


ATOM
1386
O
GLU
A
176
38.492
37.271
37.747
1.00
34.80
8


ATOM
1387
N
HIS
A
177
36.999
38.706
38.647
1.00
35.35
7


ATOM
1388
CA
HIS
A
177
35.841
38.199
37.920
1.00
36.08
6


ATOM
1389
CB
HIS
A
177
35.124
37.136
38.765
1.00
35.96
6


ATOM
1390
CG
HIS
A
177
34.106
36.334
38.013
1.00
35.77
6


ATOM
1391
ND1
HIS
A
177
33.159
35.557
38.647
1.00
35.39
7


ATOM
1392
CE1
HIS
A
177
32.402
34.962
37.743
1.00
35.38
6


ATOM
1393
NE2
HIS
A
177
32.820
35.328
36.544
1.00
35.21
7


ATOM
1394
CD2
HIS
A
177
33.885
36.186
36.685
1.00
35.24
6


ATOM
1395
C
HIS
A
177
34.900
39.360
37.597
1.00
36.63
6


ATOM
1396
O
HIS
A
177
34.486
40.102
38.496
1.00
36.97
8


ATOM
1397
N
SER
A
178
34.573
39.520
36.316
1.00
37.21
7


ATOM
1398
CA
SER
A
178
33.792
40.671
35.857
1.00
37.57
6


ATOM
1399
CB
SER
A
178
34.705
41.689
35.165
1.00
37.65
6


ATOM
1400
OG
SER
A
178
33.989
42.856
34.803
1.00
37.97
8


ATOM
1401
C
SER
A
178
32.646
40.259
34.929
1.00
37.78
6


ATOM
1402
O
SER
A
178
31.956
41.108
34.349
1.00
37.96
8


ATOM
1403
N
ASP
A
182
34.571
40.474
29.995
0.50
15.23
7


ATOM
1404
CA
ASP
A
182
33.167
40.814
29.783
0.50
15.04
6


ATOM
1405
CB
ASP
A
182
33.038
41.896
28.710
0.50
15.49
6


ATOM
1406
CG
ASP
A
182
31.872
42.839
28.965
0.50
16.16
6


ATOM
1407
OD1
ASP
A
182
30.738
42.354
29.165
0.50
18.07
8


ATOM
1408
OD2
ASP
A
182
32.094
44.073
28.957
0.50
18.37
8


ATOM
1409
C
ASP
A
182
32.376
39.570
29.384
0.50
14.62
6


ATOM
1410
O
ASP
A
182
31.899
38.827
30.239
0.50
14.80
8


ATOM
1411
N
ALA
A
183
32.247
39.337
28.082
0.50
13.88
7


ATOM
1412
CA
ALA
A
183
31.562
38.139
27.603
0.50
12.83
6


ATOM
1413
CB
ALA
A
183
31.299
38.233
26.114
0.50
13.22
6


ATOM
1414
C
ALA
A
183
32.373
36.880
27.930
0.50
12.32
6


ATOM
1415
O
ALA
A
183
31.833
35.781
27.991
0.50
11.94
8


ATOM
1416
N
MET
A
184
33.671
37.058
28.145
0.50
11.69
7


ATOM
1417
CA
MET
A
184
34.564
35.945
28.445
0.50
11.31
6


ATOM
1418
CB
MET
A
184
35.934
36.183
27.802
0.50
11.25
6


ATOM
1419
CG
MET
A
184
35.968
35.988
26.294
0.50
10.01
6


ATOM
1420
SD
MET
A
184
35.675
34.287
25.788
0.50
9.86
16


ATOM
1421
CE
MET
A
184
37.109
33.467
26.459
0.50
8.77
6


ATOM
1422
C
MET
A
184
34.725
35.737
29.953
0.50
11.29
6


ATOM
1423
O
MET
A
184
35.394
34.803
30.396
0.50
11.11
8


ATOM
1424
N
ALA
A
185
34.087
36.600
30.735
0.50
11.41
7


ATOM
1425
CA
ALA
A
185
34.241
36.587
32.189
0.50
11.95
6


ATOM
1426
CB
ALA
A
185
33.255
37.549
32.829
0.50
11.84
6


ATOM
1427
C
ALA
A
185
34.105
35.193
32.808
0.50
12.38
6


ATOM
1428
O
ALA
A
185
34.966
34.765
33.582
0.50
11.91
8


ATOM
1429
N
ASP
A
186
33.025
34.494
32.460
1.00
13.56
7


ATOM
1430
CA
ASP
A
186
32.702
33.191
33.053
1.00
14.47
6


ATOM
1431
CB
ASP
A
186
31.260
32.790
32.719
1.00
15.00
6


ATOM
1432
CG
ASP
A
186
30.229
33.666
33.423
1.00
17.39
6


ATOM
1433
OD1
ASP
A
186
29.039
33.592
33.055
1.00
21.39
8


ATOM
1434
OD2
ASP
A
186
30.607
34.414
34.348
1.00
19.82
8


ATOM
1435
C
ASP
A
186
33.671
32.089
32.622
1.00
14.62
6


ATOM
1436
O
ASP
A
186
34.022
31.208
33.417
1.00
15.17
8


ATOM
1437
N
VAL
A
187
34.104
32.146
31.364
1.00
14.28
7


ATOM
1438
CA
VAL
A
187
35.093
31.193
30.855
1.00
14.37
6


ATOM
1439
CB
VAL
A
187
35.263
31.294
29.312
1.00
14.35
6


ATOM
1440
CG1
VAL
A
187
36.449
30.461
28.833
1.00
13.97
6


ATOM
1441
CG2
VAL
A
187
33.974
30.865
28.593
1.00
15.55
6


ATOM
1442
C
VAL
A
187
36.443
31.348
31.566
1.00
14.34
6


ATOM
1443
O
VAL
A
187
37.038
30.360
31.995
1.00
14.59
8


ATOM
1444
N
TYR
A
188
36.915
32.592
31.709
1.00
14.01
7


ATOM
1445
CA
TYR
A
188
38.162
32.847
32.432
1.00
14.23
6


ATOM
1446
CB
TYR
A
188
38.592
34.308
32.287
1.00
14.43
6


ATOM
1447
CG
TYR
A
188
39.108
34.674
30.906
1.00
14.96
6


ATOM
1448
CD1
TYR
A
188
40.082
33.902
30.275
1.00
15.78
6


ATOM
1449
CE1
TYR
A
188
40.563
34.240
29.009
1.00
17.16
6


ATOM
1450
CZ
TYR
A
188
40.081
35.374
28.372
1.00
16.40
6


ATOM
1451
OH
TYR
A
188
40.561
35.721
27.126
1.00
17.69
8


ATOM
1452
CE2
TYR
A
188
39.130
36.166
28.984
1.00
16.08
6


ATOM
1453
CD2
TYR
A
188
38.650
35.820
30.246
1.00
15.95
6


ATOM
1454
C
TYR
A
188
38.055
32.460
33.914
1.00
14.23
6


ATOM
1455
O
TYR
A
188
38.994
31.894
34.479
1.00
13.98
8


ATOM
1456
N
ALA
A
189
36.909
32.754
34.530
1.00
14.31
7


ATOM
1457
CA
ALA
A
189
36.648
32.347
35.920
1.00
14.37
6


ATOM
1458
CB
ALA
A
189
35.278
32.854
36.384
1.00
14.64
6


ATOM
1459
C
ALA
A
189
36.753
30.826
36.100
1.00
14.54
6


ATOM
1460
O
ALA
A
189
37.296
30.339
37.108
1.00
14.81
8


ATOM
1461
N
THR
A
190
36.233
30.083
35.126
1.00
14.35
7


ATOM
1462
CA
THR
A
190
36.251
28.618
35.166
1.00
14.19
6


ATOM
1463
CB
THR
A
190
35.400
27.996
34.027
1.00
14.31
6


ATOM
1464
OG1
THR
A
190
34.077
28.549
34.044
1.00
14.06
8


ATOM
1465
CG2
THR
A
190
35.307
26.476
34.189
1.00
14.09
6


ATOM
1466
C
THR
A
190
37.684
28.087
35.092
1.00
14.10
6


ATOM
1467
O
THR
A
190
38.067
27.188
35.858
1.00
14.09
8


ATOM
1468
N
ILE
A
191
38.474
28.644
34.173
1.00
13.92
7


ATOM
1469
CA
ILE
A
191
39.903
28.311
34.075
1.00
13.91
6


ATOM
1470
CB
ILE
A
191
40.589
29.100
32.931
1.00
13.75
6


ATOM
1471
CG1
ILE
A
191
39.906
28.795
31.599
1.00
13.60
6


ATOM
1472
CD1
ILE
A
191
40.350
29.690
30.464
1.00
14.24
6


ATOM
1473
CG2
ILE
A
191
42.079
28.757
32.837
1.00
13.69
6


ATOM
1474
C
ILE
A
191
40.592
28.587
35.418
1.00
14.43
6


ATOM
1475
O
ILE
A
191
41.369
27.767
35.913
1.00
14.45
8


ATOM
1476
N
ALA
A
192
40.265
29.725
36.026
1.00
14.74
7


ATOM
1477
CA
ALA
A
192
40.862
30.101
37.309
1.00
15.21
6


ATOM
1478
CB
ALA
A
192
40.414
31.492
37.718
1.00
15.29
6


ATOM
1479
C
ALA
A
192
40.539
29.084
38.404
1.00
15.60
6


ATOM
1480
O
ALA
A
192
41.394
28.774
39.234
1.00
15.50
8


ATOM
1481
N
MET
A
193
39.318
28.549
38.390
1.00
16.15
7


ATOM
1482
CA
MET
A
193
38.909
27.535
39.373
1.00
17.25
6


ATOM
1483
CB
MET
A
193
37.407
27.247
39.268
1.00
18.07
6


ATOM
1484
CG
MET
A
193
36.511
28.441
39.570
1.00
21.14
6


ATOM
1485
SD
MET
A
193
36.789
29.173
41.204
1.00
28.40
16


ATOM
1486
CE
MET
A
193
36.177
27.877
42.237
1.00
28.37
6


ATOM
1487
C
MET
A
193
39.694
26.245
39.176
1.00
16.97
6


ATOM
1488
O
MET
A
193
40.109
25.605
40.146
1.00
16.53
8


ATOM
1489
N
ALA
A
194
39.899
25.878
37.910
1.00
16.44
7


ATOM
1490
CA
ALA
A
194
40.702
24.710
37.554
1.00
15.93
6


ATOM
1491
CB
ALA
A
194
40.710
24.510
36.049
1.00
16.22
6


ATOM
1492
C
ALA
A
194
42.127
24.838
38.091
1.00
15.72
6


ATOM
1493
O
ALA
A
194
42.649
23.908
38.710
1.00
15.37
8


ATOM
1494
N
LYS
A
195
42.744
25.997
37.870
1.00
15.57
7


ATOM
1495
CA
LYS
A
195
44.097
26.247
38.367
1.00
15.53
6


ATOM
1496
CB
LYS
A
195
44.615
27.600
37.876
1.00
15.59
6


ATOM
1497
CG
LYS
A
195
44.917
27.655
36.403
1.00
16.39
6


ATOM
1498
CD
LYS
A
195
45.420
29.035
36.008
1.00
18.30
6


ATOM
1499
CE
LYS
A
195
45.494
29.183
34.514
1.00
19.05
6


ATOM
1500
NZ
LYS
A
195
46.039
30.515
34.088
1.00
21.67
7


ATOM
1501
C
LYS
A
195
44.135
26.199
39.892
1.00
15.81
6


ATOM
1502
O
LYS
A
195
45.084
25.678
40.478
1.00
15.53
8


ATOM
1503
N
LEU
A
196
43.093
26.744
40.520
1.00
15.88
7


ATOM
1504
CA
LEU
A
196
42.978
26.784
41.979
1.00
16.34
6


ATOM
1505
CB
LEU
A
196
41.653
27.444
42.372
1.00
16.85
6


ATOM
1506
CG
LEU
A
196
41.417
27.747
43.850
1.00
17.42
6


ATOM
1507
CD1
LEU
A
196
42.162
28.986
44.241
1.00
19.30
6


ATOM
1508
CD2
LEU
A
196
39.928
27.926
44.116
1.00
19.06
6


ATOM
1509
C
LEU
A
196
43.059
25.383
42.584
1.00
16.42
6


ATOM
1510
O
LEU
A
196
43.872
25.123
43.475
1.00
16.57
8


ATOM
1511
N
VAL
A
197
42.222
24.482
42.084
1.00
16.10
7


ATOM
1512
CA
VAL
A
197
42.157
23.118
42.606
1.00
16.07
6


ATOM
1513
CB
VAL
A
197
40.907
22.383
42.075
1.00
16.21
6


ATOM
1514
CG1
VAL
A
197
40.839
20.962
42.628
1.00
16.46
6


ATOM
1515
CG2
VAL
A
197
39.659
23.152
42.442
1.00
15.68
6


ATOM
1516
C
VAL
A
197
43.433
22.330
42.279
1.00
15.93
6


ATOM
1517
O
VAL
A
197
43.972
21.621
43.131
1.00
16.31
8


ATOM
1518
N
LYS
A
198
43.912
22.466
41.044
1.00
15.56
7


ATOM
1519
CA
LYS
A
198
45.152
21.822
40.614
1.00
15.39
6


ATOM
1520
CB
LYS
A
198
45.470
22.189
39.162
1.00
15.41
6


ATOM
1521
CG
LYS
A
198
46.709
21.497
38.598
1.00
15.70
6


ATOM
1522
CD
LYS
A
198
46.937
21.867
37.133
1.00
16.82
6


ATOM
1523
CE
LYS
A
198
48.200
21.220
36.581
1.00
17.97
6


ATOM
1524
NZ
LYS
A
198
48.014
19.765
36.301
1.00
20.73
7


ATOM
1525
C
LYS
A
198
46.327
22.195
41.511
1.00
14.85
6


ATOM
1526
O
LYS
A
198
47.167
21.348
41.822
1.00
14.91
8


ATOM
1527
N
THR
A
199
46.384
23.463
41.919
1.00
14.63
7


ATOM
1528
CA
THR
A
199
47.488
23.954
42.754
1.00
14.66
6


ATOM
1529
CB
THR
A
199
47.669
25.497
42.619
1.00
14.98
6


ATOM
1530
OG1
THR
A
199
47.981
25.821
41.259
1.00
15.83
8


ATOM
1531
CG2
THR
A
199
48.799
25.997
43.514
1.00
15.86
6


ATOM
1532
C
THR
A
199
47.309
23.579
44.221
1.00
14.17
6


ATOM
1533
O
THR
A
199
48.271
23.201
44.893
1.00
13.93
8


ATOM
1534
N
ARG
A
200
46.078
23.668
44.714
1.00
13.57
7


ATOM
1535
CA
ARG
A
200
45.836
23.530
46.151
1.00
13.08
6


ATOM
1536
CB
ARG
A
200
44.846
24.596
46.652
1.00
13.41
6


ATOM
1537
CG
ARG
A
200
45.253
26.024
46.252
1.00
13.52
6


ATOM
1538
CD
ARG
A
200
44.457
27.091
46.961
1.00
13.50
6


ATOM
1539
NE
ARG
A
200
44.756
28.425
46.430
1.00
13.22
7


ATOM
1540
CZ
ARG
A
200
44.169
29.546
46.843
1.00
13.91
6


ATOM
1541
NH1
ARG
A
200
43.246
29.509
47.798
1.00
14.65
7


ATOM
1542
NH2
ARG
A
200
44.497
30.709
46.290
1.00
15.99
7


ATOM
1543
C
ARG
A
200
45.439
22.118
46.578
1.00
12.61
6


ATOM
1544
O
ARG
A
200
45.646
21.741
47.730
1.00
11.64
8


ATOM
1545
N
GLN
A
201
44.908
21.329
45.640
1.00
11.66
7


ATOM
1546
CA
GLN
A
201
44.626
19.908
45.894
1.00
11.35
6


ATOM
1547
CB
GLN
A
201
43.140
19.696
46.224
1.00
11.05
6


ATOM
1548
CG
GLN
A
201
42.729
20.218
47.590
1.00
9.96
6


ATOM
1549
CD
GLN
A
201
43.431
19.495
48.744
1.00
9.52
6


ATOM
1550
OE1
GLN
A
201
43.895
18.349
48.600
1.00
9.28
8


ATOM
1551
NE2
GLN
A
201
43.505
20.159
49.896
1.00
11.21
7


ATOM
1552
C
GLN
A
201
45.059
19.018
44.715
1.00
11.22
6


ATOM
1553
O
GLN
A
201
44.220
18.449
44.019
1.00
11.30
8


ATOM
1554
N
PRO
A
202
46.380
18.889
44.510
1.00
11.61
7


ATOM
1555
CA
PRO
A
202
46.983
18.277
43.317
1.00
12.06
6


ATOM
1556
CB
PRO
A
202
48.486
18.348
43.617
1.00
11.93
6


ATOM
1557
CG
PRO
A
202
48.621
19.431
44.610
1.00
11.58
6


ATOM
1558
CD
PRO
A
202
47.415
19.346
45.457
1.00
11.92
6


ATOM
1559
C
PRO
A
202
46.571
16.822
43.062
1.00
12.45
6


ATOM
1560
O
PRO
A
202
46.242
16.463
41.917
1.00
12.38
8


ATOM
1561
N
ARG
A
203
46.617
15.991
44.105
1.00
12.80
7


ATOM
1562
CA
ARG
A
203
46.281
14.572
43.969
1.00
13.00
6


ATOM
1563
CB
ARG
A
203
46.701
13.780
45.214
1.00
13.35
6


ATOM
1564
CG
ARG
A
203
48.176
13.895
45.543
1.00
14.48
6


ATOM
1565
CD
ARG
A
203
49.012
12.746
45.003
1.00
18.79
6


ATOM
1566
NE
ARG
A
203
50.383
12.819
45.517
1.00
21.14
7


ATOM
1567
CZ
ARG
A
203
50.828
12.173
46.597
1.00
21.94
6


ATOM
1568
NH1
ARG
A
203
50.018
11.383
47.295
1.00
24.20
7


ATOM
1569
NH2
ARG
A
203
52.089
12.319
46.981
1.00
22.21
7


ATOM
1570
C
ARG
A
203
44.795
14.366
43.682
1.00
13.11
6


ATOM
1571
O
ARG
A
203
44.432
13.538
42.845
1.00
13.70
8


ATOM
1572
N
LEU
A
204
43.942
15.119
44.379
1.00
13.22
7


ATOM
1573
CA
LEU
A
204
42.499
15.048
44.138
1.00
13.24
6


ATOM
1574
CB
LEU
A
204
41.704
15.853
45.178
1.00
13.22
6


ATOM
1575
CG
LEU
A
204
40.171
15.725
45.111
1.00
13.20
6


ATOM
1576
CD1
LEU
A
204
39.714
14.294
45.397
1.00
13.81
6


ATOM
1577
CD2
LEU
A
204
39.501
16.693
46.059
1.00
13.54
6


ATOM
1578
C
LEU
A
204
42.162
15.507
42.727
1.00
13.65
6


ATOM
1579
O
LEU
A
204
41.359
14.875
42.041
1.00
13.87
8


ATOM
1580
N
PHE
A
205
42.794
16.594
42.287
1.00
13.49
7


ATOM
1581
CA
PHE
A
205
42.587
17.102
40.929
1.00
13.52
6


ATOM
1582
CB
PHE
A
205
43.441
18.345
40.679
1.00
13.70
6


ATOM
1583
CG
PHE
A
205
43.052
19.097
39.439
1.00
14.74
6


ATOM
1584
CD1
PHE
A
205
41.975
19.975
39.454
1.00
15.30
6


ATOM
1585
CE1
PHE
A
205
41.607
20.670
38.305
1.00
16.10
6


ATOM
1586
CZ
PHE
A
205
42.324
20.489
37.131
1.00
15.73
6


ATOM
1587
CE2
PHE
A
205
43.394
19.615
37.102
1.00
15.12
6


ATOM
1588
CD2
PHE
A
205
43.758
18.923
38.253
1.00
16.09
6


ATOM
1589
C
PHE
A
205
42.901
16.029
39.878
1.00
13.54
6


ATOM
1590
O
PHE
A
205
42.082
15.743
39.014
1.00
13.05
8


ATOM
1591
N
ASP
A
206
44.090
15.438
39.989
1.00
13.80
7


ATOM
1592
CA
ASP
A
206
44.535
14.361
39.108
1.00
14.29
6


ATOM
1593
CB
ASP
A
206
45.939
13.903
39.523
1.00
14.93
6


ATOM
1594
CG
ASP
A
206
46.608
13.010
38.486
1.00
18.25
6


ATOM
1595
OD1
ASP
A
206
46.012
11.983
38.086
1.00
23.29
8


ATOM
1596
OD2
ASP
A
206
47.752
13.320
38.088
1.00
23.48
8


ATOM
1597
C
ASP
A
206
43.563
13.185
39.152
1.00
13.70
6


ATOM
1598
O
ASP
A
206
43.215
12.616
38.109
1.00
13.46
8


ATOM
1599
N
TYR
A
207
43.118
12.829
40.358
1.00
13.43
7


ATOM
1600
CA
TYR
A
207
42.202
11.703
40.525
1.00
12.98
6


ATOM
1601
CB
TYR
A
207
41.912
11.431
42.010
1.00
13.61
6


ATOM
1602
CG
TYR
A
207
40.850
10.374
42.191
1.00
13.23
6


ATOM
1603
CD1
TYR
A
207
41.189
9.029
42.237
1.00
13.68
6


ATOM
1604
CE1
TYR
A
207
40.209
8.043
42.366
1.00
15.29
6


ATOM
1605
CZ
TYR
A
207
38.874
8.408
42.446
1.00
13.86
6


ATOM
1606
OH
TYR
A
207
37.915
7.437
42.567
1.00
14.70
8


ATOM
1607
CE2
TYR
A
207
38.502
9.742
42.397
1.00
13.03
6


ATOM
1608
CD2
TYR
A
207
39.489
10.720
42.259
1.00
14.11
6


ATOM
1609
C
TYR
A
207
40.886
11.956
39.797
1.00
13.25
6


ATOM
1610
O
TYR
A
207
40.377
11.089
39.084
1.00
13.56
8


ATOM
1611
N
LEU
A
208
40.328
13.142
40.014
1.00
13.12
7


ATOM
1612
CA
LEU
A
208
39.043
13.499
39.437
1.00
12.88
6


ATOM
1613
CB
LEU
A
208
38.513
14.799
40.042
1.00
12.52
6


ATOM
1614
CG
LEU
A
208
38.132
14.703
41.528
1.00
13.07
6


ATOM
1615
CD1
LEU
A
208
37.920
16.080
42.126
1.00
12.35
6


ATOM
1616
CD2
LEU
A
208
36.894
13.836
41.725
1.00
11.77
6


ATOM
1617
C
LEU
A
208
39.107
13.590
37.916
1.00
12.66
6


ATOM
1618
O
LEU
A
208
38.183
13.157
37.244
1.00
13.36
8


ATOM
1619
N
PHE
A
209
40.202
14.156
37.389
1.00
12.62
7


ATOM
1620
CA
PHE
A
209
40.420
14.250
35.944
1.00
12.65
6


ATOM
1621
CB
PHE
A
209
41.685
15.066
35.631
1.00
12.13
6


ATOM
1622
CG
PHE
A
209
42.012
15.161
34.153
1.00
13.29
6


ATOM
1623
CD1
PHE
A
209
41.216
15.921
33.290
1.00
11.93
6


ATOM
1624
CE1
PHE
A
209
41.521
16.012
31.923
1.00
12.87
6


ATOM
1625
CZ
PHE
A
209
42.638
15.350
31.412
1.00
12.61
6


ATOM
1626
CE2
PHE
A
209
43.443
14.594
32.265
1.00
14.03
6


ATOM
1627
CD2
PHE
A
209
43.130
14.507
33.629
1.00
13.02
6


ATOM
1628
C
PHE
A
209
40.512
12.868
35.304
1.00
13.00
6


ATOM
1629
O
PHE
A
209
39.867
12.599
34.289
1.00
13.00
8


ATOM
1630
N
THR
A
210
41.314
11.994
35.904
1.00
13.10
7


ATOM
1631
CA
THR
A
210
41.469
10.629
35.404
1.00
13.88
6


ATOM
1632
CB
THR
A
210
42.510
9.853
36.228
1.00
13.82
6


ATOM
1633
OG1
THR
A
210
43.775
10.517
36.141
1.00
15.00
8


ATOM
1634
CG2
THR
A
210
42.663
8.431
35.719
1.00
14.67
6


ATOM
1635
C
THR
A
210
40.124
9.883
35.412
1.00
13.91
6


ATOM
1636
O
THR
A
210
39.784
9.174
34.455
1.00
14.05
8


ATOM
1637
N
HIS
A
211
39.349
10.078
36.472
1.00
14.13
7


ATOM
1638
CA
HIS
A
211
38.096
9.353
36.637
1.00
14.28
6


ATOM
1639
CB
HIS
A
211
37.856
9.028
38.109
1.00
14.55
6


ATOM
1640
CG
HIS
A
211
38.848
8.053
38.656
1.00
15.29
6


ATOM
1641
ND1
HIS
A
211
38.523
6.746
38.952
1.00
17.69
7


ATOM
1642
CE1
HIS
A
211
39.604
6.113
39.372
1.00
15.87
6


ATOM
1643
NE2
HIS
A
211
40.624
6.948
39.320
1.00
17.19
7


ATOM
1644
CD2
HIS
A
211
40.181
8.164
38.859
1.00
14.71
6


ATOM
1645
C
HIS
A
211
36.893
10.025
35.982
1.00
14.06
6


ATOM
1646
O
HIS
A
211
35.754
9.672
36.264
1.00
14.58
8


ATOM
1647
N
ARG
A
212
37.155
10.958
35.067
1.00
14.17
7


ATOM
1648
CA
ARG
A
212
36.103
11.484
34.205
1.00
14.39
6


ATOM
1649
CB
ARG
A
212
36.552
12.787
33.538
1.00
14.33
6


ATOM
1650
CG
ARG
A
212
37.300
12.576
32.216
1.00
13.41
6


ATOM
1651
CD
ARG
A
212
38.074
13.823
31.806
1.00
13.05
6


ATOM
1652
NE
ARG
A
212
38.890
13.621
30.605
1.00
13.41
7


ATOM
1653
CZ
ARG
A
212
40.056
12.972
30.575
1.00
13.67
6


ATOM
1654
NH1
ARG
A
212
40.559
12.414
31.677
1.00
12.39
7


ATOM
1655
NH2
ARG
A
212
40.713
12.859
29.432
1.00
12.54
7


ATOM
1656
C
ARG
A
212
35.746
10.438
33.133
1.00
15.04
6


ATOM
1657
O
ARG
A
212
34.706
10.532
32.485
1.00
15.58
8


ATOM
1658
N
ASN
A
213
36.634
9.459
32.954
1.00
15.64
7


ATOM
1659
CA
ASN
A
213
36.465
8.383
31.973
1.00
16.37
6


ATOM
1660
CB
ASN
A
213
37.850
7.850
31.558
1.00
16.74
6


ATOM
1661
CG
ASN
A
213
37.779
6.589
30.721
1.00
17.30
6


ATOM
1662
OD1
ASN
A
213
37.680
5.481
31.252
1.00
19.16
8


ATOM
1663
ND2
ASN
A
213
37.880
6.746
29.403
1.00
19.82
7


ATOM
1664
C
ASN
A
213
35.582
7.265
32.534
1.00
16.38
6


ATOM
1665
O
ASN
A
213
35.796
6.805
33.653
1.00
16.27
8


ATOM
1666
N
LYS
A
214
34.581
6.842
31.760
1.00
16.55
7


ATOM
1667
CA
LYS
A
214
33.581
5.892
32.268
1.00
16.84
6


ATOM
1668
CB
LYS
A
214
32.412
5.723
31.290
1.00
17.04
6


ATOM
1669
CG
LYS
A
214
32.765
5.049
29.982
1.00
17.62
6


ATOM
1670
CD
LYS
A
214
31.534
4.876
29.101
1.00
17.60
6


ATOM
1671
CE
LYS
A
214
31.911
4.269
27.761
1.00
19.76
6


ATOM
1672
NZ
LYS
A
214
30.726
4.105
26.865
1.00
20.59
7


ATOM
1673
C
LYS
A
214
34.179
4.539
32.648
1.00
16.84
6


ATOM
1674
O
LYS
A
214
33.710
3.895
33.588
1.00
16.84
8


ATOM
1675
N
HIS
A
215
35.225
4.125
31.936
1.00
16.78
7


ATOM
1676
CA
HIS
A
215
35.832
2.813
32.165
1.00
17.28
6


ATOM
1677
CB
HIS
A
215
36.702
2.389
30.974
1.00
17.65
6


ATOM
1678
CG
HIS
A
215
35.937
2.236
29.694
1.00
18.04
6


ATOM
1679
ND1
HIS
A
215
34.976
1.265
29.515
1.00
19.00
7


ATOM
1680
CE1
HIS
A
215
34.463
1.372
28.301
1.00
18.51
6


ATOM
1681
NE2
HIS
A
215
35.056
2.379
27.688
1.00
19.90
7


ATOM
1682
CD2
HIS
A
215
35.982
2.937
28.536
1.00
19.66
6


ATOM
1683
C
HIS
A
215
36.610
2.758
33.485
1.00
17.13
6


ATOM
1684
O
HIS
A
215
36.643
1.717
34.147
1.00
17.51
8


ATOM
1685
N
LYS
A
216
37.209
3.885
33.870
1.00
17.20
7


ATOM
1686
CA
LYS
A
216
37.843
4.028
35.190
1.00
17.24
6


ATOM
1687
CB
LYS
A
216
38.688
5.306
35.261
1.00
17.58
6


ATOM
1688
CG
LYS
A
216
39.921
5.305
34.356
1.00
18.27
6


ATOM
1689
CD
LYS
A
216
40.997
4.329
34.847
1.00
20.51
6


ATOM
1690
CE
LYS
A
216
41.804
4.912
35.995
1.00
21.67
6


ATOM
1691
NZ
LYS
A
216
43.031
4.117
36.284
1.00
23.96
7


ATOM
1692
C
LYS
A
216
36.811
4.044
36.313
1.00
17.13
6


ATOM
1693
O
LYS
A
216
37.056
3.514
37.395
1.00
17.48
8


ATOM
1694
N
LEU
A
217
35.669
4.685
36.062
1.00
17.16
7


ATOM
1695
CA
LEU
A
217
34.566
4.676
37.014
1.00
16.82
6


ATOM
1696
CB
LEU
A
217
33.449
5.632
36.574
1.00
16.58
6


ATOM
1697
CG
LEU
A
217
33.743
7.131
36.686
1.00
15.75
6


ATOM
1698
CD1
LEU
A
217
32.686
7.925
35.959
1.00
16.55
6


ATOM
1699
CD2
LEU
A
217
33.846
7.574
38.160
1.00
15.59
6


ATOM
1700
C
LEU
A
217
34.028
3.259
37.205
1.00
16.77
6


ATOM
1701
O
LEU
A
217
33.735
2.845
38.332
1.00
16.81
8


ATOM
1702
N
MET
A
218
33.929
2.516
36.103
1.00
16.90
7


ATOM
1703
CA
MET
A
218
33.451
1.129
36.131
1.00
17.24
6


ATOM
1704
CB
MET
A
218
33.481
0.515
34.722
1.00
16.98
6


ATOM
1705
CG
MET
A
218
32.299
0.887
33.819
1.00
17.78
6


ATOM
1706
SD
MET
A
218
32.371
−0.006
32.241
1.00
20.08
16


ATOM
1707
CE
MET
A
218
30.702
0.179
31.616
1.00
18.58
6


ATOM
1708
C
MET
A
218
34.260
0.258
37.101
1.00
16.57
6


ATOM
1709
O
MET
A
218
33.705
−0.631
37.748
1.00
16.75
8


ATOM
1710
N
ALA
A
219
35.564
0.532
37.203
1.00
16.30
7


ATOM
1711
CA
ALA
A
219
36.478
−0.245
38.062
1.00
16.23
6


ATOM
1712
CB
ALA
A
219
37.924
0.142
37.789
1.00
15.99
6


ATOM
1713
C
ALA
A
219
36.170
−0.121
39.557
1.00
16.23
6


ATOM
1714
O
ALA
A
219
36.572
−0.979
40.359
1.00
15.84
8


ATOM
1715
N
LEU
A
220
35.474
0.950
39.927
1.00
16.33
7


ATOM
1716
CA
LEU
A
220
35.114
1.195
41.327
1.00
16.78
6


ATOM
1717
CB
LEU
A
220
34.886
2.691
41.567
1.00
16.95
6


ATOM
1718
CG
LEU
A
220
36.003
3.684
41.221
1.00
17.43
6


ATOM
1719
CD1
LEU
A
220
35.459
5.106
41.202
1.00
18.75
6


ATOM
1720
CD2
LEU
A
220
37.181
3.573
42.180
1.00
17.78
6


ATOM
1721
C
LEU
A
220
33.862
0.427
41.725
1.00
16.95
6


ATOM
1722
O
LEU
A
220
33.561
0.285
42.917
1.00
16.90
8


ATOM
1723
N
ILE
A
221
33.137
−0.070
40.727
1.00
17.36
7


ATOM
1724
CA
ILE
A
221
31.809
−0.639
40.939
1.00
17.60
6


ATOM
1725
CB
ILE
A
221
30.835
−0.239
39.785
1.00
17.59
6


ATOM
1726
CG1
ILE
A
221
30.583
1.279
39.814
1.00
17.89
6


ATOM
1727
CD1
ILE
A
221
30.253
1.886
38.462
1.00
20.35
6


ATOM
1728
CG2
ILE
A
221
29.520
−1.018
39.877
1.00
17.41
6


ATOM
1729
C
ILE
A
221
31.842
−2.158
41.134
1.00
18.01
6


ATOM
1730
O
ILE
A
221
32.277
−2.900
40.251
1.00
17.44
8


ATOM
1731
N
ASP
A
222
31.397
−2.602
42.311
1.00
18.37
7


ATOM
1732
CA
ASP
A
222
31.273
−4.028
42.622
1.00
19.05
6


ATOM
1733
CB
ASP
A
222
32.328
−4.437
43.665
1.00
19.17
6


ATOM
1734
CG
ASP
A
222
32.518
−5.947
43.765
1.00
20.60
6


ATOM
1735
OD1
ASP
A
222
31.595
−6.709
43.414
1.00
20.94
8


ATOM
1736
OD2
ASP
A
222
33.602
−6.369
44.224
1.00
22.12
8


ATOM
1737
C
ASP
A
222
29.853
−4.312
43.126
1.00
19.09
6


ATOM
1738
O
ASP
A
222
29.551
−4.138
44.313
1.00
19.36
8


ATOM
1739
N
VAL
A
223
28.986
−4.744
42.210
1.00
19.41
7


ATOM
1740
CA
VAL
A
223
27.581
−5.014
42.525
1.00
19.75
6


ATOM
1741
CB
VAL
A
223
26.710
−5.150
41.235
1.00
19.86
6


ATOM
1742
CG1
VAL
A
223
25.277
−5.552
41.578
1.00
20.05
6


ATOM
1743
CG2
VAL
A
223
26.723
−3.857
40.450
1.00
20.09
6


ATOM
1744
C
VAL
A
223
27.387
−6.230
43.461
1.00
19.78
6


ATOM
1745
O
VAL
A
223
26.704
−6.109
44.477
1.00
19.65
8


ATOM
1746
N
PRO
A
224
27.987
−7.400
43.124
1.00
19.92
7


ATOM
1747
CA
PRO
A
224
27.799
−8.572
43.992
1.00
20.19
6


ATOM
1748
CB
PRO
A
224
28.699
−9.631
43.349
1.00
20.26
6


ATOM
1749
CG
PRO
A
224
28.788
−9.224
41.922
1.00
20.12
6


ATOM
1750
CD
PRO
A
224
28.831
−7.729
41.957
1.00
20.08
6


ATOM
1751
C
PRO
A
224
28.220
−8.340
45.443
1.00
20.36
6


ATOM
1752
O
PRO
A
224
27.578
−8.859
46.356
1.00
20.24
8


ATOM
1753
N
GLN
A
225
29.289
−7.573
45.643
1.00
20.74
7


ATOM
1754
CA
GLN
A
225
29.795
−7.284
46.988
1.00
21.15
6


ATOM
1755
CB
GLN
A
225
31.304
−7.020
46.954
1.00
21.14
6


ATOM
1756
CG
GLN
A
225
32.167
−8.272
47.020
1.00
22.23
6


ATOM
1757
CD
GLN
A
225
33.641
−7.966
47.287
1.00
22.85
6


ATOM
1758
OE1
GLN
A
225
34.097
−6.818
47.153
1.00
24.66
8


ATOM
1759
NE2
GLN
A
225
34.398
−8.999
47.658
1.00
24.30
7


ATOM
1760
C
GLN
A
225
29.079
−6.100
47.638
1.00
20.88
6


ATOM
1761
O
GLN
A
225
29.185
−5.898
48.851
1.00
20.82
8


ATOM
1762
N
MET
A
226
28.340
−5.337
46.829
1.00
20.77
7


ATOM
1763
CA
MET
A
226
27.776
−4.040
47.237
1.00
20.93
6


ATOM
1764
CB
MET
A
226
26.588
−4.213
48.202
1.00
21.17
6


ATOM
1765
CG
MET
A
226
25.362
−4.889
47.595
1.00
21.57
6


ATOM
1766
SD
MET
A
226
23.964
−4.878
48.740
1.00
22.39
16


ATOM
1767
CE
MET
A
226
22.884
−6.114
48.014
1.00
23.45
6


ATOM
1768
C
MET
A
226
28.846
−3.140
47.857
1.00
20.67
6


ATOM
1769
O
MET
A
226
28.631
−2.538
48.909
1.00
20.39
8


ATOM
1770
N
LYS
A
227
29.996
−3.049
47.189
1.00
20.10
7


ATOM
1771
CA
LYS
A
227
31.130
−2.291
47.705
1.00
19.62
6


ATOM
1772
CB
LYS
A
227
32.331
−2.426
46.763
1.00
19.99
6


ATOM
1773
CG
LYS
A
227
33.577
−1.693
47.230
1.00
22.00
6


ATOM
1774
CD
LYS
A
227
34.838
−2.383
46.738
1.00
24.37
6


ATOM
1775
CE
LYS
A
227
36.083
−1.744
47.332
1.00
26.67
6


ATOM
1776
NZ
LYS
A
227
37.278
−2.634
47.179
1.00
28.20
7


ATOM
1777
C
LYS
A
227
30.757
−0.814
47.899
1.00
18.73
6


ATOM
1778
O
LYS
A
227
30.327
−0.161
46.955
1.00
18.60
8


ATOM
1779
N
PRO
A
228
30.908
−0.297
49.132
1.00
18.10
7


ATOM
1780
CA
PRO
A
228
30.583
1.109
49.398
1.00
17.36
6


ATOM
1781
CB
PRO
A
228
30.681
1.213
50.925
1.00
17.56
6


ATOM
1782
CG
PRO
A
228
31.580
0.128
51.327
1.00
18.03
6


ATOM
1783
CD
PRO
A
228
31.375
−0.994
50.345
1.00
17.90
6


ATOM
1784
C
PRO
A
228
31.542
2.098
48.727
1.00
16.76
6


ATOM
1785
O
PRO
A
228
32.745
1.846
48.651
1.00
16.20
8


ATOM
1786
N
LEU
A
229
30.987
3.205
48.228
1.00
15.78
7


ATOM
1787
CA
LEU
A
229
31.768
4.299
47.651
1.00
15.53
6


ATOM
1788
CB
LEU
A
229
31.582
4.351
46.122
1.00
15.75
6


ATOM
1789
CG
LEU
A
229
31.890
3.099
45.300
1.00
15.95
6


ATOM
1790
CD1
LEU
A
229
31.273
3.216
43.905
1.00
17.34
6


ATOM
1791
CD2
LEU
A
229
33.393
2.842
45.223
1.00
16.41
6


ATOM
1792
C
LEU
A
229
31.302
5.620
48.243
1.00
15.35
6


ATOM
1793
O
LEU
A
229
30.161
5.735
48.695
1.00
15.10
8


ATOM
1794
N
VAL
A
230
32.177
6.622
48.246
1.00
14.74
7


ATOM
1795
CA
VAL
A
230
31.712
7.979
48.485
1.00
15.19
6


ATOM
1796
CB
VAL
A
230
32.782
8.871
49.197
1.00
15.47
6


ATOM
1797
CG1
VAL
A
230
34.080
8.920
48.413
1.00
16.18
6


ATOM
1798
CG2
VAL
A
230
32.238
10.276
49.461
1.00
17.25
6


ATOM
1799
C
VAL
A
230
31.247
8.562
47.151
1.00
14.57
6


ATOM
1800
O
VAL
A
230
31.851
8.317
46.110
1.00
14.85
8


ATOM
1801
N
HIS
A
231
30.141
9.287
47.187
1.00
14.53
7


ATOM
1802
CA
HIS
A
231
29.582
9.880
45.991
1.00
13.71
6


ATOM
1803
CB
HIS
A
231
28.322
9.114
45.576
1.00
13.94
6


ATOM
1804
CG
HIS
A
231
27.632
9.663
44.363
1.00
12.94
6


ATOM
1805
ND1
HIS
A
231
28.308
10.033
43.219
1.00
13.82
7


ATOM
1806
CE1
HIS
A
231
27.439
10.449
42.312
1.00
12.18
6


ATOM
1807
NE2
HIS
A
231
26.225
10.346
42.821
1.00
13.09
7


ATOM
1808
CD2
HIS
A
231
26.317
9.853
44.100
1.00
13.14
6


ATOM
1809
C
HIS
A
231
29.268
11.333
46.308
1.00
14.30
6


ATOM
1810
O
HIS
A
231
28.628
11.623
47.317
1.00
14.18
8


ATOM
1811
N
VAL
A
232
29.772
12.235
45.472
1.00
14.51
7


ATOM
1812
CA
VAL
A
232
29.472
13.659
45.598
1.00
14.51
6


ATOM
1813
CB
VAL
A
232
30.762
14.532
45.594
1.00
14.88
6


ATOM
1814
CG1
VAL
A
232
30.414
16.020
45.791
1.00
14.32
6


ATOM
1815
CG2
VAL
A
232
31.740
14.052
46.682
1.00
14.13
6


ATOM
1816
C
VAL
A
232
28.524
14.081
44.487
1.00
15.20
6


ATOM
1817
O
VAL
A
232
28.839
13.947
43.295
1.00
15.23
8


ATOM
1818
N
SER
A
233
27.354
14.575
44.883
1.00
15.31
7


ATOM
1819
CA
SER
A
233
26.292
14.900
43.953
1.00
15.75
6


ATOM
1820
CB
SER
A
233
25.382
13.692
43.742
1.00
15.55
6


ATOM
1821
OG
SER
A
233
24.330
14.015
42.850
1.00
17.12
8


ATOM
1822
C
SER
A
233
25.464
16.058
44.493
1.00
15.65
6


ATOM
1823
O
SER
A
233
25.147
16.100
45.684
1.00
15.67
8


ATOM
1824
N
GLY
A
234
25.107
16.987
43.613
1.00
15.99
7


ATOM
1825
CA
GLY
A
234
24.217
18.096
43.984
1.00
16.27
6


ATOM
1826
C
GLY
A
234
22.866
17.624
44.513
1.00
16.69
6


ATOM
1827
O
GLY
A
234
22.194
18.347
45.260
1.00
17.48
8


ATOM
1828
N
MET
A
235
22.473
16.408
44.131
1.00
16.74
7


ATOM
1829
CA
MET
A
235
21.201
15.821
44.564
1.00
17.05
6


ATOM
1830
CB
MET
A
235
20.904
14.531
43.784
1.00
17.78
6


ATOM
1831
CG
MET
A
235
20.673
14.732
42.283
1.00
21.45
6


ATOM
1832
SD
MET
A
235
19.162
15.639
41.872
1.00
29.38
16


ATOM
1833
CE
MET
A
235
19.794
17.287
41.562
1.00
28.47
6


ATOM
1834
C
MET
A
235
21.181
15.538
46.065
1.00
16.24
6


ATOM
1835
O
MET
A
235
20.112
15.483
46.682
1.00
16.70
8


ATOM
1836
N
PHE
A
236
22.363
15.364
46.654
1.00
15.55
7


ATOM
1837
CA
PHE
A
236
22.464
15.115
48.093
1.00
14.98
6


ATOM
1838
CB
PHE
A
236
23.822
14.501
48.439
1.00
14.62
6


ATOM
1839
CG
PHE
A
236
23.971
13.056
48.009
1.00
14.77
6


ATOM
1840
CD1
PHE
A
236
22.881
12.182
48.041
1.00
14.91
6


ATOM
1841
CE1
PHE
A
236
23.022
10.836
47.658
1.00
15.23
6


ATOM
1842
CZ
PHE
A
236
24.261
10.362
47.251
1.00
13.93
6


ATOM
1843
CE2
PHE
A
236
25.359
11.225
47.227
1.00
14.40
6


ATOM
1844
CD2
PHE
A
236
25.207
12.564
47.607
1.00
14.85
6


ATOM
1845
C
PHE
A
236
22.215
16.380
48.929
1.00
14.67
6


ATOM
1846
O
PHE
A
236
21.808
16.297
50.095
1.00
14.95
8


ATOM
1847
N
GLY
A
237
22.474
17.547
48.348
1.00
14.01
7


ATOM
1848
CA
GLY
A
237
22.184
18.813
49.038
1.00
13.81
6


ATOM
1849
C
GLY
A
237
23.361
19.369
49.824
1.00
13.87
6


ATOM
1850
O
GLY
A
237
24.117
18.616
50.464
1.00
13.27
8


ATOM
1851
N
ALA
A
238
23.510
20.692
49.774
1.00
13.61
7


ATOM
1852
CA
ALA
A
238
24.639
21.389
50.399
1.00
13.96
6


ATOM
1853
CB
ALA
A
238
24.641
22.845
49.987
1.00
14.18
6


ATOM
1854
C
ALA
A
238
24.658
21.271
51.924
1.00
13.87
6


ATOM
1855
O
ALA
A
238
25.709
21.469
52.558
1.00
13.19
8


ATOM
1856
N
TRP
A
239
23.502
20.955
52.513
1.00
14.04
7


ATOM
1857
CA
TRP
A
239
23.391
20.823
53.970
1.00
14.13
6


ATOM
1858
CB
TRP
A
239
21.929
20.617
54.403
1.00
14.31
6


ATOM
1859
CG
TRP
A
239
21.299
19.359
53.865
1.00
14.66
6


ATOM
1860
CD1
TRP
A
239
20.614
19.221
52.694
1.00
15.69
6


ATOM
1861
NE1
TRP
A
239
20.184
17.925
52.543
1.00
15.17
7


ATOM
1862
CE2
TRP
A
239
20.590
17.196
53.630
1.00
15.91
6


ATOM
1863
CD2
TRP
A
239
21.291
18.070
54.488
1.00
14.80
6


ATOM
1864
CE3
TRP
A
239
21.808
17.570
55.693
1.00
16.09
6


ATOM
1865
CZ3
TRP
A
239
21.621
16.223
55.989
1.00
15.31
6


ATOM
1866
CH2
TRP
A
239
20.920
15.380
55.111
1.00
15.67
6


ATOM
1867
CZ2
TRP
A
239
20.397
15.845
53.932
1.00
15.63
6


ATOM
1868
C
TRP
A
239
24.268
19.684
54.492
1.00
14.03
6


ATOM
1869
O
TRP
A
239
24.673
19.688
55.651
1.00
13.54
8


ATOM
1870
N
ARG
A
240
24.540
18.705
53.635
1.00
13.47
7


ATOM
1871
CA
ARG
A
240
25.468
17.628
53.979
1.00
13.54
6


ATOM
1872
CB
ARG
A
240
24.762
16.271
53.974
1.00
13.59
6


ATOM
1873
CG
ARG
A
240
23.952
15.979
52.719
1.00
13.69
6


ATOM
1874
CD
ARG
A
240
23.549
14.520
52.693
1.00
13.99
6


ATOM
1875
NE
ARG
A
240
22.384
14.272
51.858
1.00
14.86
7


ATOM
1876
CZ
ARG
A
240
21.912
13.056
51.577
1.00
13.53
6


ATOM
1877
NH1
ARG
A
240
22.517
11.977
52.058
1.00
15.69
7


ATOM
1878
NH2
ARG
A
240
20.835
12.919
50.814
1.00
15.33
7


ATOM
1879
C
ARG
A
240
26.668
17.622
53.034
1.00
13.66
6


ATOM
1880
O
ARG
A
240
27.235
16.571
52.746
1.00
14.06
8


ATOM
1881
N
GLY
A
241
27.039
18.810
52.549
1.00
13.86
7


ATOM
1882
CA
GLY
A
241
28.174
18.951
51.638
1.00
13.42
6


ATOM
1883
C
GLY
A
241
28.058
18.112
50.379
1.00
13.72
6


ATOM
1884
O
GLY
A
241
29.071
17.675
49.829
1.00
13.79
8


ATOM
1885
N
ASN
A
242
26.821
17.894
49.917
1.00
13.27
7


ATOM
1886
CA
ASN
A
242
26.551
17.150
48.667
1.00
13.18
6


ATOM
1887
CB
ASN
A
242
27.039
17.942
47.453
1.00
13.15
6


ATOM
1888
CG
ASN
A
242
26.381
19.280
47.341
1.00
13.61
6


ATOM
1889
OD1
ASN
A
242
25.162
19.372
47.189
1.00
14.76
8


ATOM
1890
ND2
ASN
A
242
27.178
20.339
47.406
1.00
15.97
7


ATOM
1891
C
ASN
A
242
27.134
15.736
48.614
1.00
13.01
6


ATOM
1892
O
ASN
A
242
27.378
15.200
47.524
1.00
12.74
8


ATOM
1893
N
THR
A
243
27.293
15.120
49.778
1.00
12.81
7


ATOM
1894
CA
THR
A
243
28.096
13.910
49.901
1.00
13.09
6


ATOM
1895
CB
THR
A
243
29.461
14.251
50.545
1.00
13.52
6


ATOM
1896
OG1
THR
A
243
30.143
15.188
49.706
1.00
13.64
8


ATOM
1897
CG2
THR
A
243
30.329
13.017
50.717
1.00
13.34
6


ATOM
1898
C
THR
A
243
27.377
12.835
50.706
1.00
13.15
6


ATOM
1899
O
THR
A
243
26.699
13.130
51.691
1.00
13.24
8


ATOM
1900
N
SER
A
244
27.510
11.588
50.261
1.00
13.25
7


ATOM
1901
CA
SER
A
244
27.110
10.448
51.073
1.00
13.21
6


ATOM
1902
CB
SER
A
244
25.629
10.127
50.891
1.00
13.30
6


ATOM
1903
OG
SER
A
244
25.160
9.331
51.974
1.00
13.88
8


ATOM
1904
C
SER
A
244
27.949
9.230
50.737
1.00
13.09
6


ATOM
1905
O
SER
A
244
28.767
9.265
49.816
1.00
13.10
8


ATOM
1906
N
TRP
A
245
27.763
8.169
51.517
1.00
13.47
7


ATOM
1907
CA
TRP
A
245
28.262
6.845
51.165
1.00
13.66
6


ATOM
1908
CB
TRP
A
245
28.744
6.093
52.410
1.00
14.15
6


ATOM
1909
CG
TRP
A
245
30.148
6.463
52.832
1.00
13.65
6


ATOM
1910
CD1
TRP
A
245
31.282
6.388
52.069
1.00
14.03
6


ATOM
1911
NE1
TRP
A
245
32.372
6.802
52.796
1.00
14.33
7


ATOM
1912
CE2
TRP
A
245
31.955
7.154
54.054
1.00
14.70
6


ATOM
1913
CD2
TRP
A
245
30.557
6.950
54.111
1.00
14.81
6


ATOM
1914
CE3
TRP
A
245
29.877
7.240
55.304
1.00
13.42
6


ATOM
1915
CZ3
TRP
A
245
30.603
7.716
56.386
1.00
13.91
6


ATOM
1916
CH2
TRP
A
245
31.992
7.910
56.298
1.00
14.30
6


ATOM
1917
CZ2
TRP
A
245
32.683
7.642
55.137
1.00
13.87
6


ATOM
1918
C
TRP
A
245
27.154
6.069
50.472
1.00
14.09
6


ATOM
1919
O
TRP
A
245
26.019
6.032
50.953
1.00
14.21
8


ATOM
1920
N
VAL
A
246
27.487
5.463
49.337
1.00
14.32
7


ATOM
1921
CA
VAL
A
246
26.506
4.743
48.521
1.00
14.39
6


ATOM
1922
CB
VAL
A
246
26.226
5.472
47.183
1.00
14.57
6


ATOM
1923
CG1
VAL
A
246
25.711
6.880
47.443
1.00
13.84
6


ATOM
1924
CG2
VAL
A
246
27.485
5.512
46.304
1.00
14.53
6


ATOM
1925
C
VAL
A
246
26.958
3.320
48.245
1.00
15.10
6


ATOM
1926
O
VAL
A
246
28.137
2.996
48.390
1.00
15.41
8


ATOM
1927
N
ALA
A
247
26.010
2.473
47.852
1.00
15.43
7


ATOM
1928
CA
ALA
A
247
26.316
1.105
47.444
1.00
16.07
6


ATOM
1929
CB
ALA
A
247
25.913
0.131
48.523
1.00
16.42
6


ATOM
1930
C
ALA
A
247
25.578
0.795
46.151
1.00
16.26
6


ATOM
1931
O
ALA
A
247
24.402
1.131
46.022
1.00
16.24
8


ATOM
1932
N
PRO
A
248
26.264
0.156
45.183
1.00
16.78
7


ATOM
1933
CA
PRO
A
248
25.573
−0.252
43.964
1.00
17.28
6


ATOM
1934
CB
PRO
A
248
26.717
−0.513
42.977
1.00
17.46
6


ATOM
1935
CG
PRO
A
248
27.887
−0.844
43.810
1.00
17.27
6


ATOM
1936
CD
PRO
A
248
27.698
−0.196
45.161
1.00
16.54
6


ATOM
1937
C
PRO
A
248
24.740
−1.518
44.170
1.00
17.69
6


ATOM
1938
O
PRO
A
248
25.243
−2.516
44.694
1.00
17.84
8


ATOM
1939
N
LEU
A
249
23.476
−1.471
43.754
1.00
18.15
7


ATOM
1940
CA
LEU
A
249
22.572
−2.615
43.920
1.00
18.51
6


ATOM
1941
CB
LEU
A
249
21.204
−2.152
44.420
1.00
19.03
6


ATOM
1942
CG
LEU
A
249
21.062
−1.575
45.829
1.00
20.20
6


ATOM
1943
CD1
LEU
A
249
19.592
−1.352
46.121
1.00
21.74
6


ATOM
1944
CD2
LEU
A
249
21.685
−2.476
46.892
1.00
22.27
6


ATOM
1945
C
LEU
A
249
22.396
−3.409
42.632
1.00
18.48
6


ATOM
1946
O
LEU
A
249
22.305
−4.643
42.649
1.00
18.65
8


ATOM
1947
N
ALA
A
250
22.299
−2.688
41.523
1.00
18.26
7


ATOM
1948
CA
ALA
A
250
22.127
−3.293
40.212
1.00
18.04
6


ATOM
1949
CB
ALA
A
250
20.732
−3.874
40.077
1.00
17.83
6


ATOM
1950
C
ALA
A
250
22.362
−2.246
39.147
1.00
17.93
6


ATOM
1951
O
ALA
A
250
22.480
−1.049
39.448
1.00
18.06
8


ATOM
1952
N
TRP
A
251
22.437
−2.697
37.903
1.00
17.94
7


ATOM
1953
CA
TRP
A
251
22.515
−1.806
36.772
1.00
18.27
6


ATOM
1954
CB
TRP
A
251
23.480
−2.355
35.726
1.00
18.21
6


ATOM
1955
CG
TRP
A
251
24.904
−2.207
36.134
1.00
17.39
6


ATOM
1956
CD1
TRP
A
251
25.621
−3.053
36.931
1.00
16.61
6


ATOM
1957
NE1
TRP
A
251
26.900
−2.576
37.097
1.00
16.75
7


ATOM
1958
CE2
TRP
A
251
27.027
−1.395
36.412
1.00
16.95
6


ATOM
1959
CD2
TRP
A
251
25.784
−1.130
35.794
1.00
16.91
6


ATOM
1960
CE3
TRP
A
251
25.644
0.036
35.025
1.00
17.57
6


ATOM
1961
CZ3
TRP
A
251
26.742
0.892
34.900
1.00
17.56
6


ATOM
1962
CH2
TRP
A
251
27.965
0.596
35.522
1.00
17.80
6


ATOM
1963
CZ2
TRP
A
251
28.129
−0.542
36.279
1.00
17.98
6


ATOM
1964
C
TRP
A
251
21.131
−1.597
36.179
1.00
19.04
6


ATOM
1965
O
TRP
A
251
20.283
−2.499
36.216
1.00
18.74
8


ATOM
1966
N
HIS
A
252
20.900
−0.397
35.658
1.00
19.75
7


ATOM
1967
CA
HIS
A
252
19.625
−0.055
35.050
1.00
20.70
6


ATOM
1968
CB
HIS
A
252
19.674
1.369
34.505
1.00
20.60
6


ATOM
1969
CG
HIS
A
252
18.329
1.957
34.224
1.00
20.81
6


ATOM
1970
ND1
HIS
A
252
17.600
1.642
33.097
1.00
20.57
7


ATOM
1971
CE1
HIS
A
252
16.463
2.314
33.110
1.00
20.70
6


ATOM
1972
NE2
HIS
A
252
16.432
3.060
34.200
1.00
21.32
7


ATOM
1973
CD2
HIS
A
252
17.587
2.854
34.914
1.00
20.42
6


ATOM
1974
C
HIS
A
252
19.302
−1.063
33.936
1.00
21.37
6


ATOM
1975
O
HIS
A
252
20.156
−1.360
33.096
1.00
21.57
8


ATOM
1976
N
PRO
A
253
18.077
−1.621
33.951
1.00
22.27
7


ATOM
1977
CA
PRO
A
253
17.707
−2.669
32.993
1.00
22.77
6


ATOM
1978
CB
PRO
A
253
16.342
−3.140
33.503
1.00
22.79
6


ATOM
1979
CG
PRO
A
253
15.801
−1.984
34.252
1.00
22.68
6


ATOM
1980
CD
PRO
A
253
16.978
−1.319
34.887
1.00
22.15
6


ATOM
1981
C
PRO
A
253
17.597
−2.188
31.540
1.00
23.44
6


ATOM
1982
O
PRO
A
253
17.578
−3.012
30.626
1.00
23.61
8


ATOM
1983
N
GLU
A
254
17.535
−0.873
31.335
1.00
23.97
7


ATOM
1984
CA
GLU
A
254
17.409
−0.303
29.989
1.00
24.25
6


ATOM
1985
CB
GLU
A
254
16.075
0.444
29.835
1.00
24.50
6


ATOM
1986
CG
GLU
A
254
14.827
−0.395
30.139
1.00
25.98
6


ATOM
1987
CD
GLU
A
254
14.722
−1.657
29.282
1.00
27.85
6


ATOM
1988
OE1
GLU
A
254
15.258
−1.668
28.150
1.00
28.69
8


ATOM
1989
OE2
GLU
A
254
14.091
−2.638
29.743
1.00
28.74
8


ATOM
1990
C
GLU
A
254
18.574
0.619
29.619
1.00
24.10
6


ATOM
1991
O
GLU
A
254
19.053
0.602
28.482
1.00
24.16
8


ATOM
1992
N
ASN
A
255
19.019
1.425
30.580
1.00
23.78
7


ATOM
1993
CA
ASN
A
255
20.098
2.381
30.354
1.00
23.59
6


ATOM
1994
CB
ASN
A
255
19.918
3.607
31.258
1.00
23.74
6


ATOM
1995
CG
ASN
A
255
20.753
4.809
30.809
1.00
24.62
6


ATOM
1996
OD1
ASN
A
255
21.780
4.666
30.140
1.00
25.73
8


ATOM
1997
ND2
ASN
A
255
20.313
6.002
31.194
1.00
25.16
7


ATOM
1998
C
ASN
A
255
21.464
1.742
30.586
1.00
23.14
6


ATOM
1999
O
ASN
A
255
21.818
1.412
31.717
1.00
22.76
8


ATOM
2000
N
ARG
A
256
22.225
1.582
29.504
1.00
22.74
7


ATOM
2001
CA
ARG
A
256
23.532
0.915
29.543
1.00
22.32
6


ATOM
2002
CB
ARG
A
256
24.107
0.812
28.124
1.00
22.70
6


ATOM
2003
CG
ARG
A
256
25.121
−0.303
27.929
1.00
23.54
6


ATOM
2004
CD
ARG
A
256
25.415
−0.527
26.456
1.00
24.61
6


ATOM
2005
NE
ARG
A
256
26.269
−1.697
26.244
1.00
25.65
7


ATOM
2006
CZ
ARG
A
256
26.583
−2.196
25.051
1.00
25.61
6


ATOM
2007
NH1
ARG
A
256
26.113
−1.635
23.941
1.00
25.69
7


ATOM
2008
NH2
ARG
A
256
27.368
−3.264
24.967
1.00
26.14
7


ATOM
2009
C
ARG
A
256
24.537
1.613
30.475
1.00
21.82
6


ATOM
2010
O
ARG
A
256
25.368
0.954
31.101
1.00
21.80
8


ATOM
2011
N
ASN
A
257
24.441
2.940
30.566
1.00
21.11
7


ATOM
2012
CA
ASN
A
257
25.393
3.750
31.338
1.00
20.82
6


ATOM
2013
CB
ASN
A
257
25.724
5.041
30.590
1.00
21.21
6


ATOM
2014
CG
ASN
A
257
26.349
4.788
29.241
1.00
22.48
6


ATOM
2015
OD1
ASN
A
257
25.856
5.268
28.219
1.00
24.94
8


ATOM
2016
ND2
ASN
A
257
27.439
4.028
29.223
1.00
23.25
7


ATOM
2017
C
ASN
A
257
24.936
4.099
32.752
1.00
19.99
6


ATOM
2018
O
ASN
A
257
25.632
4.815
33.468
1.00
19.95
8


ATOM
2019
N
ALA
A
258
23.767
3.609
33.149
1.00
19.28
7


ATOM
2020
CA
ALA
A
258
23.229
3.942
34.465
1.00
18.46
6


ATOM
2021
CB
ALA
A
258
21.802
4.463
34.348
1.00
18.55
6


ATOM
2022
C
ALA
A
258
23.301
2.777
35.438
1.00
18.25
6


ATOM
2023
O
ALA
A
258
22.886
1.653
35.116
1.00
17.66
8


ATOM
2024
N
VAL
A
259
23.844
3.055
36.627
1.00
17.53
7


ATOM
2025
CA
VAL
A
259
23.877
2.099
37.728
1.00
17.46
6


ATOM
2026
CB
VAL
A
259
25.333
1.885
38.268
1.00
17.84
6


ATOM
2027
CG1
VAL
A
259
25.928
3.190
38.802
1.00
17.61
6


ATOM
2028
CG2
VAL
A
259
25.373
0.786
39.324
1.00
17.59
6


ATOM
2029
C
VAL
A
259
22.952
2.593
38.838
1.00
17.01
6


ATOM
2030
O
VAL
A
259
22.828
3.803
39.066
1.00
16.30
8


ATOM
2031
N
ILE
A
260
22.291
1.653
39.509
1.00
17.04
7


ATOM
2032
CA
ILE
A
260
21.334
1.978
40.562
1.00
17.28
6


ATOM
2033
CB
ILE
A
260
20.098
1.027
40.537
1.00
17.31
6


ATOM
2034
CG1
ILE
A
260
19.441
1.023
39.150
1.00
17.29
6


ATOM
2035
CD1
ILE
A
260
18.563
−0.202
38.868
1.00
17.13
6


ATOM
2036
CG2
ILE
A
260
19.092
1.442
41.598
1.00
16.90
6


ATOM
2037
C
ILE
A
260
22.016
1.911
41.925
1.00
17.69
6


ATOM
2038
O
ILE
A
260
22.482
0.850
42.347
1.00
17.67
8


ATOM
2039
N
MET
A
261
22.078
3.058
42.598
1.00
17.90
7


ATOM
2040
CA
MET
A
261
22.766
3.185
43.882
1.00
18.30
6


ATOM
2041
CB
MET
A
261
23.692
4.402
43.859
1.00
18.67
6


ATOM
2042
CG
MET
A
261
24.843
4.294
42.885
1.00
19.51
6


ATOM
2043
SD
MET
A
261
26.176
3.276
43.530
1.00
22.87
16


ATOM
2044
CE
MET
A
261
27.533
3.810
42.490
1.00
19.74
6


ATOM
2045
C
MET
A
261
21.768
3.362
45.007
1.00
18.17
6


ATOM
2046
O
MET
A
261
20.721
3.983
44.813
1.00
17.92
8


ATOM
2047
N
VAL
A
262
22.094
2.826
46.187
1.00
17.88
7


ATOM
2048
CA
VAL
A
262
21.383
3.195
47.410
1.00
17.88
6


ATOM
2049
CB
VAL
A
262
20.984
1.964
48.276
1.00
18.06
6


ATOM
2050
CG1
VAL
A
262
20.640
2.382
49.723
1.00
19.13
6


ATOM
2051
CG2
VAL
A
262
19.806
1.277
47.672
1.00
19.52
6


ATOM
2052
C
VAL
A
262
22.235
4.150
48.227
1.00
17.60
6


ATOM
2053
O
VAL
A
262
23.436
3.951
48.374
1.00
17.13
8


ATOM
2054
N
ASP
A
263
21.603
5.203
48.724
1.00
16.99
7


ATOM
2055
CA
ASP
A
263
22.233
6.115
49.658
1.00
17.03
6


ATOM
2056
CB
ASP
A
263
21.476
7.445
49.658
1.00
16.56
6


ATOM
2057
CG
ASP
A
263
22.015
8.438
50.673
1.00
16.33
6


ATOM
2058
OD1
ASP
A
263
22.997
8.128
51.381
1.00
16.88
8


ATOM
2059
OD2
ASP
A
263
21.442
9.540
50.756
1.00
17.38
8


ATOM
2060
C
ASP
A
263
22.189
5.453
51.031
1.00
17.03
6


ATOM
2061
O
ASP
A
263
21.107
5.247
51.593
1.00
17.19
8


ATOM
2062
N
LEU
A
264
23.362
5.103
51.561
1.00
17.34
7


ATOM
2063
CA
LEU
A
264
23.440
4.357
52.826
1.00
17.57
6


ATOM
2064
CB
LEU
A
264
24.825
3.720
53.005
1.00
17.59
6


ATOM
2065
CG
LEU
A
264
25.254
2.605
52.045
1.00
17.00
6


ATOM
2066
CD1
LEU
A
264
26.732
2.302
52.210
1.00
16.09
6


ATOM
2067
CD2
LEU
A
264
24.421
1.330
52.226
1.00
16.43
6


ATOM
2068
C
LEU
A
264
23.073
5.199
54.056
1.00
18.25
6


ATOM
2069
O
LEU
A
264
22.771
4.658
55.123
1.00
18.17
8


ATOM
2070
N
ALA
A
265
23.088
6.520
53.898
1.00
18.46
7


ATOM
2071
CA
ALA
A
265
22.668
7.426
54.964
1.00
18.74
6


ATOM
2072
CB
ALA
A
265
23.297
8.790
54.773
1.00
18.88
6


ATOM
2073
C
ALA
A
265
21.148
7.546
55.040
1.00
19.01
6


ATOM
2074
O
ALA
A
265
20.605
8.049
56.027
1.00
19.41
8


ATOM
2075
N
GLY
A
266
20.464
7.087
53.995
1.00
18.99
7


ATOM
2076
CA
GLY
A
266
19.006
7.181
53.929
1.00
19.57
6


ATOM
2077
C
GLY
A
266
18.303
6.171
54.818
1.00
19.83
6


ATOM
2078
O
GLY
A
266
18.943
5.444
55.580
1.00
19.94
8


ATOM
2079
N
ASP
A
267
16.976
6.141
54.719
1.00
20.35
7


ATOM
2080
CA
ASP
A
267
16.150
5.153
55.402
1.00
21.00
6


ATOM
2081
CB
ASP
A
267
14.879
5.823
55.951
1.00
21.02
6


ATOM
2082
CG
ASP
A
267
13.842
4.820
56.462
1.00
22.22
6


ATOM
2083
OD1
ASP
A
267
14.226
3.720
56.928
1.00
23.40
8


ATOM
2084
OD2
ASP
A
267
12.634
5.149
56.406
1.00
22.86
8


ATOM
2085
C
ASP
A
267
15.792
4.053
54.413
1.00
21.20
6


ATOM
2086
O
ASP
A
267
15.074
4.296
53.438
1.00
21.21
8


ATOM
2087
N
ILE
A
268
16.295
2.845
54.659
1.00
21.65
7


ATOM
2088
CA
ILE
A
268
16.088
1.735
53.724
1.00
22.09
6


ATOM
2089
CB
ILE
A
268
17.322
0.781
53.636
1.00
22.05
6


ATOM
2090
CG1
ILE
A
268
17.655
0.187
55.007
1.00
21.91
6


ATOM
2091
CD1
ILE
A
268
18.443
−1.110
54.936
1.00
22.50
6


ATOM
2092
CG2
ILE
A
268
18.525
1.507
53.012
1.00
21.71
6


ATOM
2093
C
ILE
A
268
14.810
0.931
53.992
1.00
22.52
6


ATOM
2094
O
ILE
A
268
14.504
−0.007
53.253
1.00
22.71
8


ATOM
2095
N
SER
A
269
14.061
1.316
55.029
1.00
23.11
7


ATOM
2096
CA
SER
A
269
12.784
0.654
55.373
1.00
23.57
6


ATOM
2097
CB
SER
A
269
12.032
1.423
56.469
1.00
23.63
6


ATOM
2098
OG
SER
A
269
12.653
1.259
57.733
1.00
23.20
8


ATOM
2099
C
SER
A
269
11.860
0.407
54.166
1.00
24.17
6


ATOM
2100
O
SER
A
269
11.387
−0.714
53.987
1.00
23.84
8


ATOM
2101
N
PRO
A
270
11.607
1.452
53.334
1.00
24.71
7


ATOM
2102
CA
PRO
A
270
10.720
1.275
52.172
1.00
25.34
6


ATOM
2103
CB
PRO
A
270
10.725
2.657
51.508
1.00
25.44
6


ATOM
2104
CG
PRO
A
270
11.151
3.598
52.574
1.00
25.14
6


ATOM
2105
CD
PRO
A
270
12.104
2.839
53.425
1.00
24.80
6


ATOM
2106
C
PRO
A
270
11.226
0.225
51.184
1.00
25.96
6


ATOM
2107
O
PRO
A
270
10.425
−0.459
50.552
1.00
25.83
8


ATOM
2108
N
LEU
A
271
12.546
0.108
51.054
1.00
26.77
7


ATOM
2109
CA
LEU
A
271
13.150
−0.908
50.190
1.00
27.62
6


ATOM
2110
CB
LEU
A
271
14.648
−0.659
50.030
1.00
27.56
6


ATOM
2111
CG
LEU
A
271
15.100
0.596
49.292
1.00
27.99
6


ATOM
2112
CD1
LEU
A
271
16.612
0.675
49.335
1.00
27.52
6


ATOM
2113
CD2
LEU
A
271
14.599
0.593
47.851
1.00
27.69
6


ATOM
2114
C
LEU
A
271
12.935
−2.316
50.729
1.00
28.33
6


ATOM
2115
O
LEU
A
271
12.900
−3.279
49.966
1.00
28.38
8


ATOM
2116
N
LEU
A
272
12.806
−2.426
52.047
1.00
29.24
7


ATOM
2117
CA
LEU
A
272
12.671
−3.721
52.703
1.00
30.15
6


ATOM
2118
CB
LEU
A
272
13.278
−3.681
54.112
1.00
30.10
6


ATOM
2119
CG
LEU
A
272
14.717
−3.177
54.294
1.00
30.15
6


ATOM
2120
CD1
LEU
A
272
15.129
−3.294
55.750
1.00
30.47
6


ATOM
2121
CD2
LEU
A
272
15.712
−3.907
53.388
1.00
30.28
6


ATOM
2122
C
LEU
A
272
11.220
−4.194
52.773
1.00
30.81
6


ATOM
2123
O
LEU
A
272
10.924
−5.345
52.454
1.00
30.93
8


ATOM
2124
N
GLU
A
273
10.321
−3.301
53.183
1.00
31.65
7


ATOM
2125
CA
GLU
A
273
8.949
−3.694
53.527
1.00
32.45
6


ATOM
2126
CB
GLU
A
273
8.588
−3.206
54.941
1.00
32.44
6


ATOM
2127
CG
GLU
A
273
8.545
−1.691
55.107
1.00
32.58
6


ATOM
2128
CD
GLU
A
273
8.584
−1.255
56.565
1.00
32.88
6


ATOM
2129
OE1
GLU
A
273
7.635
−0.568
57.006
1.00
33.17
8


ATOM
2130
OE2
GLU
A
273
9.561
−1.596
57.270
1.00
32.64
8


ATOM
2131
C
GLU
A
273
7.883
−3.258
52.508
1.00
32.95
6


ATOM
2132
O
GLU
A
273
6.682
−3.434
52.745
1.00
33.07
8


ATOM
2133
N
LEU
A
274
8.323
−2.720
51.374
1.00
33.45
7


ATOM
2134
CA
LEU
A
274
7.402
−2.208
50.360
1.00
34.04
6


ATOM
2135
CB
LEU
A
274
7.506
−0.683
50.283
1.00
33.97
6


ATOM
2136
CG
LEU
A
274
6.236
0.150
50.124
1.00
34.16
6


ATOM
2137
CD1
LEU
A
274
5.282
−0.062
51.301
1.00
34.18
6


ATOM
2138
CD2
LEU
A
274
6.603
1.620
49.992
1.00
34.16
6


ATOM
2139
C
LEU
A
274
7.687
−2.829
48.994
1.00
34.44
6


ATOM
2140
O
LEU
A
274
8.845
−3.032
48.630
1.00
34.54
8


ATOM
2141
N
ASP
A
275
6.626
−3.125
48.242
1.00
35.01
7


ATOM
2142
CA
ASP
A
275
6.755
−3.782
46.933
1.00
35.42
6


ATOM
2143
CB
ASP
A
275
5.427
−4.430
46.514
1.00
35.48
6


ATOM
2144
CG
ASP
A
275
4.312
−3.418
46.337
1.00
35.85
6


ATOM
2145
OD1
ASP
A
275
3.510
−3.246
47.280
1.00
36.48
8


ATOM
2146
OD2
ASP
A
275
4.240
−2.790
45.259
1.00
36.29
8


ATOM
2147
C
ASP
A
275
7.269
−2.832
45.844
1.00
35.72
6


ATOM
2148
O
ASP
A
275
7.333
−1.616
46.047
1.00
35.80
8


ATOM
2149
N
SER
A
276
7.624
−3.397
44.691
1.00
35.93
7


ATOM
2150
CA
SER
A
276
8.289
−2.647
43.619
1.00
36.22
6


ATOM
2151
CB
SER
A
276
8.898
−3.605
42.592
1.00
36.27
6


ATOM
2152
OG
SER
A
276
7.902
−4.407
41.984
1.00
36.57
8


ATOM
2153
C
SER
A
276
7.387
−1.620
42.921
1.00
36.32
6


ATOM
2154
O
SER
A
276
7.873
−0.618
42.391
1.00
36.34
8


ATOM
2155
N
ASP
A
277
6.081
−1.876
42.919
1.00
36.42
7


ATOM
2156
CA
ASP
A
277
5.116
−0.956
42.315
1.00
36.57
6


ATOM
2157
CB
ASP
A
277
3.773
−1.656
42.080
1.00
36.60
6


ATOM
2158
CG
ASP
A
277
3.790
−2.565
40.862
1.00
36.84
6


ATOM
2159
OD1
ASP
A
277
4.314
−2.145
39.806
1.00
37.07
8


ATOM
2160
OD2
ASP
A
277
3.264
−3.695
40.958
1.00
36.61
8


ATOM
2161
C
ASP
A
277
4.919
0.301
43.162
1.00
36.56
6


ATOM
2162
O
ASP
A
277
4.825
1.411
42.629
1.00
36.46
8


ATOM
2163
N
THR
A
278
4.861
0.116
44.481
1.00
36.62
7


ATOM
2164
CA
THR
A
278
4.682
1.223
45.419
1.00
36.66
6


ATOM
2165
CB
THR
A
278
4.329
0.712
46.833
1.00
36.65
6


ATOM
2166
OG1
THR
A
278
3.410
−0.382
46.733
1.00
36.38
8


ATOM
2167
CG2
THR
A
278
3.697
1.822
47.667
1.00
36.69
6


ATOM
2168
C
THR
A
278
5.938
2.096
45.482
1.00
36.82
6


ATOM
2169
O
THR
A
278
5.849
3.315
45.656
1.00
36.84
8


ATOM
2170
N
LEU
A
279
7.100
1.463
45.332
1.00
36.94
7


ATOM
2171
CA
LEU
A
279
8.377
2.173
45.279
1.00
37.06
6


ATOM
2172
CB
LEU
A
279
9.548
1.193
45.414
1.00
37.03
6


ATOM
2173
CG
LEU
A
279
9.747
0.495
46.767
1.00
36.91
6


ATOM
2174
CD1
LEU
A
279
10.610
−0.749
46.612
1.00
36.89
6


ATOM
2175
CD2
LEU
A
279
10.338
1.440
47.807
1.00
36.58
6


ATOM
2176
C
LEU
A
279
8.510
2.990
43.995
1.00
37.17
6


ATOM
2177
O
LEU
A
279
9.136
4.052
43.989
1.00
37.26
8


ATOM
2178
N
ARG
A
280
7.913
2.493
42.912
1.00
37.40
7


ATOM
2179
CA
ARG
A
280
7.874
3.225
41.647
1.00
37.69
6


ATOM
2180
CB
ARG
A
280
7.628
2.272
40.474
1.00
37.74
6


ATOM
2181
CG
ARG
A
280
8.019
2.854
39.114
1.00
38.23
6


ATOM
2182
CD
ARG
A
280
7.385
2.101
37.947
1.00
38.72
6


ATOM
2183
NE
ARG
A
280
7.840
0.714
37.859
1.00
39.36
7


ATOM
2184
CZ
ARG
A
280
7.064
−0.347
38.066
1.00
39.83
6


ATOM
2185
NH1
ARG
A
280
5.778
−0.192
38.365
1.00
40.20
7


ATOM
2186
NH2
ARG
A
280
7.570
−1.568
37.965
1.00
39.89
7


ATOM
2187
C
ARG
A
280
6.795
4.308
41.675
1.00
37.76
6


ATOM
2188
O
ARG
A
280
6.858
5.246
42.472
1.00
37.89
8


ATOM
2189
N
ALA
A
295
10.621
8.192
52.084
1.00
25.34
7


ATOM
2190
CA
ALA
A
295
11.604
8.462
51.036
1.00
25.42
6


ATOM
2191
CB
ALA
A
295
12.610
9.502
51.506
1.00
25.37
6


ATOM
2192
C
ALA
A
295
12.318
7.186
50.604
1.00
25.41
6


ATOM
2193
O
ALA
A
295
12.677
6.354
51.437
1.00
26.03
8


ATOM
2194
N
VAL
A
296
12.514
7.037
49.298
1.00
25.14
7


ATOM
2195
CA
VAL
A
296
13.261
5.906
48.751
1.00
24.60
6


ATOM
2196
CB
VAL
A
296
12.630
5.376
47.439
1.00
24.64
6


ATOM
2197
CG1
VAL
A
296
13.259
4.053
47.038
1.00
24.60
6


ATOM
2198
CG2
VAL
A
296
11.119
5.217
47.596
1.00
24.23
6


ATOM
2199
C
VAL
A
296
14.706
6.344
48.501
1.00
24.40
6


ATOM
2200
O
VAL
A
296
14.959
7.187
47.638
1.00
24.50
8


ATOM
2201
N
PRO
A
297
15.660
5.781
49.269
1.00
24.02
7


ATOM
2202
CA
PRO
A
297
17.061
6.208
49.187
1.00
23.76
6


ATOM
2203
CB
PRO
A
297
17.651
5.700
50.505
1.00
23.78
6


ATOM
2204
CG
PRO
A
297
16.855
4.480
50.819
1.00
23.88
6


ATOM
2205
CD
PRO
A
297
15.466
4.705
50.261
1.00
24.07
6


ATOM
2206
C
PRO
A
297
17.790
5.595
47.985
1.00
23.58
6


ATOM
2207
O
PRO
A
297
18.804
4.913
48.148
1.00
23.52
8


ATOM
2208
N
VAL
A
298
17.275
5.860
46.790
1.00
23.17
7


ATOM
2209
CA
VAL
A
298
17.780
5.255
45.564
1.00
23.25
6


ATOM
2210
CB
VAL
A
298
16.784
4.185
45.029
1.00
23.01
6


ATOM
2211
CG1
VAL
A
298
17.071
3.829
43.573
1.00
23.88
6


ATOM
2212
CG2
VAL
A
298
16.800
2.940
45.915
1.00
23.31
6


ATOM
2213
C
VAL
A
298
18.001
6.334
44.504
1.00
23.14
6


ATOM
2214
O
VAL
A
298
17.177
7.236
44.350
1.00
23.07
8


ATOM
2215
N
LYS
A
299
19.116
6.244
43.785
1.00
23.13
7


ATOM
2216
CA
LYS
A
299
19.380
7.168
42.681
1.00
23.24
6


ATOM
2217
CB
LYS
A
299
20.072
8.447
43.178
1.00
23.39
6


ATOM
2218
CG
LYS
A
299
21.537
8.285
43.573
1.00
23.24
6


ATOM
2219
CD
LYS
A
299
22.274
9.626
43.577
1.00
23.83
6


ATOM
2220
CE
LYS
A
299
22.384
10.200
42.173
1.00
24.10
6


ATOM
2221
NZ
LYS
A
299
23.620
10.991
41.958
1.00
23.51
7


ATOM
2222
C
LYS
A
299
20.182
6.519
41.560
1.00
22.98
6


ATOM
2223
O
LYS
A
299
20.913
5.550
41.786
1.00
23.45
8


ATOM
2224
N
LEU
A
300
20.023
7.048
40.350
1.00
22.51
7


ATOM
2225
CA
LEU
A
300
20.823
6.613
39.207
1.00
22.13
6


ATOM
2226
CB
LEU
A
300
20.053
6.799
37.895
1.00
22.32
6


ATOM
2227
CG
LEU
A
300
18.733
6.053
37.692
1.00
22.01
6


ATOM
2228
CD1
LEU
A
300
18.184
6.340
36.301
1.00
22.82
6


ATOM
2229
CD2
LEU
A
300
18.897
4.546
37.912
1.00
22.32
6


ATOM
2230
C
LEU
A
300
22.118
7.399
39.145
1.00
21.88
6


ATOM
2231
O
LEU
A
300
22.117
8.625
39.275
1.00
22.04
8


ATOM
2232
N
VAL
A
301
23.222
6.687
38.944
1.00
21.12
7


ATOM
2233
CA
VAL
A
301
24.500
7.316
38.641
1.00
20.46
6


ATOM
2234
CB
VAL
A
301
25.616
6.802
39.580
1.00
20.35
6


ATOM
2235
CG1
VAL
A
301
26.979
7.334
39.150
1.00
20.43
6


ATOM
2236
CG2
VAL
A
301
25.310
7.181
41.033
1.00
19.99
6


ATOM
2237
C
VAL
A
301
24.852
7.031
37.179
1.00
20.21
6


ATOM
2238
O
VAL
A
301
24.966
5.870
36.779
1.00
20.01
8


ATOM
2239
N
HIS
A
302
24.991
8.091
36.386
1.00
19.71
7


ATOM
2240
CA
HIS
A
302
25.262
7.962
34.949
1.00
19.59
6


ATOM
2241
CB
HIS
A
302
24.476
9.006
34.151
1.00
20.12
6


ATOM
2242
CG
HIS
A
302
22.992
8.896
34.315
1.00
21.05
6


ATOM
2243
ND1
HIS
A
302
22.315
9.478
35.365
1.00
22.18
7


ATOM
2244
CE1
HIS
A
302
21.026
9.206
35.259
1.00
22.11
6


ATOM
2245
NE2
HIS
A
302
20.846
8.455
34.189
1.00
21.70
7


ATOM
2246
CD2
HIS
A
302
22.060
8.244
33.581
1.00
21.43
6


ATOM
2247
C
HIS
A
302
26.753
8.098
34.688
1.00
19.07
6


ATOM
2248
O
HIS
A
302
27.319
9.179
34.830
1.00
18.57
8


ATOM
2249
N
ILE
A
303
27.385
6.992
34.301
1.00
18.30
7


ATOM
2250
CA
ILE
A
303
28.846
6.925
34.258
1.00
18.00
6


ATOM
2251
CB
ILE
A
303
29.364
5.465
34.226
1.00
18.13
6


ATOM
2252
CG1
ILE
A
303
28.809
4.724
32.998
1.00
18.15
6


ATOM
2253
CD1
ILE
A
303
29.434
3.372
32.751
1.00
18.23
6


ATOM
2254
CG2
ILE
A
303
29.027
4.756
35.543
1.00
19.14
6


ATOM
2255
C
ILE
A
303
29.476
7.733
33.123
1.00
17.56
6


ATOM
2256
O
ILE
A
303
30.679
7.985
33.144
1.00
17.17
8


ATOM
2257
N
ASN
A
304
28.659
8.136
32.147
1.00
17.49
7


ATOM
2258
CA
ASN
A
304
29.105
9.024
31.068
1.00
17.68
6


ATOM
2259
CB
ASN
A
304
28.415
8.648
29.750
1.00
17.81
6


ATOM
2260
CG
ASN
A
304
26.929
8.968
29.757
1.00
18.29
6


ATOM
2261
OD1
ASN
A
304
26.189
8.545
30.649
1.00
17.64
8


ATOM
2262
ND2
ASN
A
304
26.481
9.711
28.746
1.00
20.26
7


ATOM
2263
C
ASN
A
304
28.863
10.509
31.373
1.00
17.93
6


ATOM
2264
O
ASN
A
304
29.026
11.368
30.495
1.00
18.09
8


ATOM
2265
N
LYS
A
305
28.482
10.805
32.616
1.00
17.72
7


ATOM
2266
CA
LYS
A
305
28.155
12.174
33.016
1.00
17.83
6


ATOM
2267
CB
LYS
A
305
26.675
12.276
33.401
1.00
18.11
6


ATOM
2268
CG
LYS
A
305
25.737
12.191
32.202
1.00
19.13
6


ATOM
2269
CD
LYS
A
305
24.292
12.462
32.578
1.00
21.75
6


ATOM
2270
CE
LYS
A
305
23.470
12.752
31.330
1.00
22.85
6


ATOM
2271
NZ
LYS
A
305
22.020
12.892
31.633
1.00
24.04
7


ATOM
2272
C
LYS
A
305
29.069
12.695
34.142
1.00
17.68
6


ATOM
2273
O
LYS
A
305
28.645
13.490
34.992
1.00
17.81
8


ATOM
2274
N
CYS
A
306
30.323
12.239
34.124
1.00
17.47
7


ATOM
2275
CA
CYS
A
306
31.351
12.656
35.096
1.00
17.66
6


ATOM
2276
CB
CYS
A
306
31.885
14.050
34.765
1.00
18.21
6


ATOM
2277
SG
CYS
A
306
32.338
14.276
33.080
1.00
22.01
16


ATOM
2278
C
CYS
A
306
30.885
12.653
36.549
1.00
16.80
6


ATOM
2279
O
CYS
A
306
31.097
13.640
37.258
1.00
17.11
8


ATOM
2280
N
PRO
A
307
30.273
11.550
37.014
1.00
16.12
7


ATOM
2281
CA
PRO
A
307
29.924
11.554
38.438
1.00
15.54
6


ATOM
2282
CB
PRO
A
307
29.065
10.305
38.589
1.00
15.62
6


ATOM
2283
CG
PRO
A
307
29.548
9.385
37.502
1.00
15.98
6


ATOM
2284
CD
PRO
A
307
29.892
10.290
36.351
1.00
16.06
6


ATOM
2285
C
PRO
A
307
31.163
11.436
39.306
1.00
15.17
6


ATOM
2286
O
PRO
A
307
32.145
10.807
38.903
1.00
14.80
8


ATOM
2287
N
VAL
A
308
31.119
12.048
40.487
1.00
14.15
7


ATOM
2288
CA
VAL
A
308
32.218
11.941
41.424
1.00
13.90
6


ATOM
2289
CB
VAL
A
308
32.378
13.217
42.271
1.00
13.72
6


ATOM
2290
CG1
VAL
A
308
33.415
13.010
43.364
1.00
13.75
6


ATOM
2291
CG2
VAL
A
308
32.769
14.389
41.369
1.00
13.17
6


ATOM
2292
C
VAL
A
308
32.036
10.700
42.290
1.00
14.08
6


ATOM
2293
O
VAL
A
308
31.091
10.612
43.077
1.00
13.79
8


ATOM
2294
N
LEU
A
309
32.919
9.724
42.078
1.00
14.49
7


ATOM
2295
CA
LEU
A
309
32.931
8.472
42.838
1.00
14.34
6


ATOM
2296
CB
LEU
A
309
32.390
7.311
41.993
1.00
14.97
6


ATOM
2297
CG
LEU
A
309
30.912
7.300
41.603
1.00
15.28
6


ATOM
2298
CD1
LEU
A
309
30.660
6.290
40.474
1.00
14.92
6


ATOM
2299
CD2
LEU
A
309
30.028
6.990
42.811
1.00
15.39
6


ATOM
2300
C
LEU
A
309
34.351
8.149
43.264
1.00
14.48
6


ATOM
2301
O
LEU
A
309
35.300
8.378
42.512
1.00
13.62
8


ATOM
2302
N
ALA
A
310
34.489
7.597
44.469
1.00
14.21
7


ATOM
2303
CA
ALA
A
310
35.784
7.154
44.977
1.00
14.57
6


ATOM
2304
CB
ALA
A
310
36.562
8.335
45.566
1.00
14.47
6


ATOM
2305
C
ALA
A
310
35.592
6.078
46.023
1.00
14.97
6


ATOM
2306
O
ALA
A
310
34.503
5.937
46.580
1.00
14.05
8


ATOM
2307
N
GLN
A
311
36.650
5.317
46.299
1.00
15.60
7


ATOM
2308
CA
GLN
A
311
36.594
4.316
47.358
1.00
17.03
6


ATOM
2309
CB
GLN
A
311
37.934
3.578
47.517
1.00
16.88
6


ATOM
2310
CG
GLN
A
311
39.117
4.464
47.874
1.00
18.50
6


ATOM
2311
CD
GLN
A
311
40.389
3.670
48.141
1.00
19.48
6


ATOM
2312
OE1
GLN
A
311
40.435
2.818
49.035
1.00
22.53
8


ATOM
2313
NE2
GLN
A
311
41.429
3.950
47.369
1.00
21.87
7


ATOM
2314
C
GLN
A
311
36.161
4.965
48.670
1.00
16.84
6


ATOM
2315
O
GLN
A
311
36.436
6.148
48.919
1.00
17.36
8


ATOM
2316
N
ALA
A
312
35.471
4.188
49.493
1.00
16.84
7


ATOM
2317
CA
ALA
A
312
34.773
4.715
50.658
1.00
16.78
6


ATOM
2318
CB
ALA
A
312
34.020
3.599
51.362
1.00
16.66
6


ATOM
2319
C
ALA
A
312
35.658
5.499
51.649
1.00
16.67
6


ATOM
2320
O
ALA
A
312
35.201
6.468
52.236
1.00
16.21
8


ATOM
2321
N
ASN
A
313
36.919
5.089
51.808
1.00
16.92
7


ATOM
2322
CA
ASN
A
313
37.821
5.737
52.780
1.00
17.32
6


ATOM
2323
CB
ASN
A
313
38.939
4.775
53.237
1.00
17.92
6


ATOM
2324
CG
ASN
A
313
40.068
4.638
52.221
1.00
19.28
6


ATOM
2325
OD1
ASN
A
313
39.994
5.154
51.106
1.00
20.50
8


ATOM
2326
ND2
ASN
A
313
41.126
3.931
52.615
1.00
21.31
7


ATOM
2327
C
ASN
A
313
38.382
7.093
52.321
1.00
17.34
6


ATOM
2328
O
ASN
A
313
39.155
7.729
53.037
1.00
17.22
8


ATOM
2329
N
THR
A
314
37.983
7.520
51.124
1.00
17.12
7


ATOM
2330
CA
THR
A
314
38.349
8.839
50.605
1.00
17.09
6


ATOM
2331
CB
THR
A
314
37.974
8.976
49.118
1.00
17.16
6


ATOM
2332
OG1
THR
A
314
38.580
7.907
48.386
1.00
17.59
8


ATOM
2333
CG2
THR
A
314
38.455
10.314
48.544
1.00
16.81
6


ATOM
2334
C
THR
A
314
37.687
9.948
51.417
1.00
16.74
6


ATOM
2335
O
THR
A
314
38.215
11.063
51.505
1.00
17.26
8


ATOM
2336
N
LEU
A
315
36.529
9.644
52.006
1.00
16.36
7


ATOM
2337
CA
LEU
A
315
35.912
10.543
52.977
1.00
16.48
6


ATOM
2338
CB
LEU
A
315
34.379
10.427
52.954
1.00
16.42
6


ATOM
2339
CG
LEU
A
315
33.582
11.274
53.963
1.00
16.43
6


ATOM
2340
CD1
LEU
A
315
33.759
12.776
53.706
1.00
16.50
6


ATOM
2341
CD2
LEU
A
315
32.089
10.886
53.972
1.00
16.53
6


ATOM
2342
C
LEU
A
315
36.468
10.246
54.366
1.00
16.28
6


ATOM
2343
O
LEU
A
315
36.164
9.206
54.952
1.00
15.88
8


ATOM
2344
N
ARG
A
316
37.296
11.163
54.873
1.00
16.21
7


ATOM
2345
CA
ARG
A
316
37.976
10.993
56.153
1.00
16.48
6


ATOM
2346
CB
ARG
A
316
39.172
11.957
56.258
1.00
16.38
6


ATOM
2347
CG
ARG
A
316
40.324
11.589
55.340
1.00
15.89
6


ATOM
2348
CD
ARG
A
316
41.289
12.745
55.119
1.00
16.12
6


ATOM
2349
NE
ARG
A
316
42.392
12.340
54.246
1.00
16.37
7


ATOM
2350
CZ
ARG
A
316
43.106
13.169
53.484
1.00
17.30
6


ATOM
2351
NH1
ARG
A
316
42.838
14.474
53.467
1.00
16.55
7


ATOM
2352
NH2
ARG
A
316
44.088
12.690
52.728
1.00
17.52
7


ATOM
2353
C
ARG
A
316
37.010
11.201
57.325
1.00
16.65
6


ATOM
2354
O
ARG
A
316
36.056
11.971
57.211
1.00
16.26
8


ATOM
2355
N
PRO
A
317
37.237
10.485
58.450
1.00
17.32
7


ATOM
2356
CA
PRO
A
317
36.368
10.624
59.618
1.00
17.54
6


ATOM
2357
CB
PRO
A
317
37.172
9.939
60.731
1.00
17.52
6


ATOM
2358
CG
PRO
A
317
37.951
8.895
60.021
1.00
17.53
6


ATOM
2359
CD
PRO
A
317
38.290
9.472
58.669
1.00
17.36
6


ATOM
2360
C
PRO
A
317
36.080
12.078
59.989
1.00
17.91
6


ATOM
2361
O
PRO
A
317
34.917
12.440
60.180
1.00
17.77
8


ATOM
2362
N
GLU
A
318
37.129
12.897
60.086
1.00
18.53
7


ATOM
2363
CA
GLU
A
318
36.983
14.303
60.471
1.00
19.05
6


ATOM
2364
CB
GLU
A
318
38.351
14.998
60.588
1.00
19.27
6


ATOM
2365
CG
GLU
A
318
39.206
14.992
59.311
1.00
20.97
6


ATOM
2366
CD
GLU
A
318
40.249
13.874
59.283
1.00
24.08
6


ATOM
2367
OE1
GLU
A
318
41.394
14.155
58.864
1.00
25.28
8


ATOM
2368
OE2
GLU
A
318
39.933
12.721
59.668
1.00
24.58
8


ATOM
2369
C
GLU
A
318
36.054
15.074
59.520
1.00
18.89
6


ATOM
2370
O
GLU
A
318
35.327
15.971
59.941
1.00
19.64
8


ATOM
2371
N
ASP
A
319
36.076
14.709
58.244
1.00
18.93
7


ATOM
2372
CA
ASP
A
319
35.214
15.347
57.258
1.00
18.62
6


ATOM
2373
CB
ASP
A
319
35.816
15.235
55.860
1.00
18.66
6


ATOM
2374
CG
ASP
A
319
37.060
16.088
55.705
1.00
18.52
6


ATOM
2375
OD1
ASP
A
319
36.959
17.327
55.882
1.00
18.49
8


ATOM
2376
OD2
ASP
A
319
38.137
15.520
55.432
1.00
18.14
8


ATOM
2377
C
ASP
A
319
33.796
14.804
57.295
1.00
18.72
6


ATOM
2378
O
ASP
A
319
32.840
15.565
57.165
1.00
18.32
8


ATOM
2379
N
ALA
A
320
33.661
13.490
57.485
1.00
18.88
7


ATOM
2380
CA
ALA
A
320
32.348
12.877
57.692
1.00
19.13
6


ATOM
2381
CB
ALA
A
320
32.489
11.370
57.911
1.00
19.62
6


ATOM
2382
C
ALA
A
320
31.671
13.538
58.892
1.00
19.42
6


ATOM
2383
O
ALA
A
320
30.489
13.884
58.843
1.00
19.04
8


ATOM
2384
N
ASP
A
321
32.448
13.745
59.953
1.00
19.43
7


ATOM
2385
CA
ASP
A
321
31.993
14.476
61.133
1.00
20.01
6


ATOM
2386
CB
ASP
A
321
33.114
14.527
62.175
1.00
20.71
6


ATOM
2387
CG
ASP
A
321
32.687
15.195
63.468
1.00
22.52
6


ATOM
2388
OD1
ASP
A
321
31.819
14.637
64.177
1.00
26.24
8


ATOM
2389
OD2
ASP
A
321
33.238
16.273
63.786
1.00
25.69
8


ATOM
2390
C
ASP
A
321
31.543
15.894
60.769
1.00
19.66
6


ATOM
2391
O
ASP
A
321
30.442
16.320
61.134
1.00
19.86
8


ATOM
2392
N
ARG
A
322
32.396
16.608
60.036
1.00
19.12
7


ATOM
2393
CA
ARG
A
322
32.110
17.974
59.599
1.00
18.88
6


ATOM
2394
CB
ARG
A
322
33.274
18.502
58.740
1.00
18.93
6


ATOM
2395
CG
ARG
A
322
33.138
19.955
58.276
1.00
18.80
6


ATOM
2396
CD
ARG
A
322
34.418
20.446
57.581
1.00
18.83
6


ATOM
2397
NE
ARG
A
322
34.861
19.514
56.543
1.00
19.15
7


ATOM
2398
CZ
ARG
A
322
34.529
19.605
55.257
1.00
18.83
6


ATOM
2399
NH1
ARG
A
322
33.769
20.603
54.830
1.00
19.04
7


ATOM
2400
NH2
ARG
A
322
34.967
18.702
54.398
1.00
18.79
7


ATOM
2401
C
ARG
A
322
30.782
18.058
58.827
1.00
18.51
6


ATOM
2402
O
ARG
A
322
30.002
18.988
59.026
1.00
18.47
8


ATOM
2403
N
LEU
A
323
30.532
17.070
57.967
1.00
18.43
7


ATOM
2404
CA
LEU
A
323
29.343
17.065
57.103
1.00
18.00
6


ATOM
2405
CB
LEU
A
323
29.642
16.348
55.777
1.00
18.10
6


ATOM
2406
CG
LEU
A
323
30.782
16.916
54.918
1.00
17.20
6


ATOM
2407
CD1
LEU
A
323
31.002
16.091
53.661
1.00
17.72
6


ATOM
2408
CD2
LEU
A
323
30.552
18.390
54.562
1.00
16.29
6


ATOM
2409
C
LEU
A
323
28.109
16.455
57.780
1.00
18.26
6


ATOM
2410
O
LEU
A
323
27.017
16.471
57.218
1.00
18.25
8


ATOM
2411
N
GLY
A
324
28.297
15.905
58.979
1.00
18.16
7


ATOM
2412
CA
GLY
A
324
27.198
15.332
59.759
1.00
18.68
6


ATOM
2413
C
GLY
A
324
26.771
13.942
59.317
1.00
18.99
6


ATOM
2414
O
GLY
A
324
25.688
13.481
59.669
1.00
19.21
8


ATOM
2415
N
ILE
A
325
27.630
13.267
58.557
1.00
19.24
7


ATOM
2416
CA
ILE
A
325
27.320
11.937
58.028
1.00
19.72
6


ATOM
2417
CB
ILE
A
325
28.128
11.640
56.733
1.00
19.37
6


ATOM
2418
CG1
ILE
A
325
27.786
12.671
55.654
1.00
19.77
6


ATOM
2419
CD1
ILE
A
325
28.832
12.806
54.570
1.00
20.67
6


ATOM
2420
CG2
ILE
A
325
27.865
10.201
56.240
1.00
19.89
6


ATOM
2421
C
ILE
A
325
27.577
10.856
59.079
1.00
20.15
6


ATOM
2422
O
ILE
A
325
28.688
10.727
59.589
1.00
20.85
8


ATOM
2423
N
ASN
A
326
26.537
10.087
59.398
1.00
20.42
7


ATOM
2424
CA
ASN
A
326
26.619
9.057
60.433
1.00
20.40
6


ATOM
2425
CB
ASN
A
326
25.254
8.881
61.116
1.00
20.48
6


ATOM
2426
CG
ASN
A
326
25.278
7.836
62.222
1.00
20.98
6


ATOM
2427
OD1
ASN
A
326
26.157
6.973
62.268
1.00
21.02
8


ATOM
2428
ND2
ASN
A
326
24.294
7.900
63.111
1.00
22.87
7


ATOM
2429
C
ASN
A
326
27.149
7.717
59.898
1.00
20.44
6


ATOM
2430
O
ASN
A
326
26.425
6.967
59.243
1.00
20.31
8


ATOM
2431
N
ARG
A
327
28.408
7.424
60.215
1.00
20.35
7


ATOM
2432
CA
ARG
A
327
29.114
6.251
59.685
1.00
20.35
6


ATOM
2433
CB
ARG
A
327
30.563
6.257
60.171
1.00
20.35
6


ATOM
2434
CG
ARG
A
327
31.451
5.230
59.509
1.00
21.65
6


ATOM
2435
CD
ARG
A
327
32.799
5.165
60.190
1.00
22.69
6


ATOM
2436
NE
ARG
A
327
33.723
4.300
59.465
1.00
25.02
7


ATOM
2437
CZ
ARG
A
327
34.576
4.715
58.530
1.00
25.86
6


ATOM
2438
NH1
ARG
A
327
34.639
6.000
58.192
1.00
26.09
7


ATOM
2439
NH2
ARG
A
327
35.374
3.838
57.935
1.00
26.78
7


ATOM
2440
C
ARG
A
327
28.442
4.938
60.080
1.00
20.50
6


ATOM
2441
O
ARG
A
327
28.260
4.042
59.242
1.00
20.53
8


ATOM
2442
N
GLN
A
328
28.068
4.835
61.353
1.00
20.30
7


ATOM
2443
CA
GLN
A
328
27.468
3.610
61.886
1.00
20.64
6


ATOM
2444
CB
GLN
A
328
27.358
3.672
63.411
1.00
20.92
6


ATOM
2445
CG
GLN
A
328
27.081
2.311
64.081
1.00
21.67
6


ATOM
2446
CD
GLN
A
328
28.031
1.209
63.613
1.00
23.09
6


ATOM
2447
OE1
GLN
A
328
29.255
1.372
63.620
1.00
23.75
8


ATOM
2448
NE2
GLN
A
328
27.466
0.083
63.205
1.00
23.92
7


ATOM
2449
C
GLN
A
328
26.111
3.302
61.249
1.00
20.45
6


ATOM
2450
O
GLN
A
328
25.795
2.145
60.990
1.00
20.50
8


ATOM
2451
N
HIS
A
329
25.324
4.345
60.990
1.00
20.24
7


ATOM
2452
CA
HIS
A
329
24.057
4.203
60.270
1.00
20.11
6


ATOM
2453
CB
HIS
A
329
23.359
5.565
60.138
1.00
20.60
6


ATOM
2454
CG
HIS
A
329
22.046
5.506
59.419
1.00
21.78
6


ATOM
2455
ND1
HIS
A
329
20.857
5.235
60.061
1.00
23.34
7


ATOM
2456
CE1
HIS
A
329
19.872
5.245
59.181
1.00
24.18
6


ATOM
2457
NE2
HIS
A
329
20.379
5.511
57.991
1.00
23.80
7


ATOM
2458
CD2
HIS
A
329
21.737
5.678
58.111
1.00
23.01
6


ATOM
2459
C
HIS
A
329
24.284
3.597
58.886
1.00
19.67
6


ATOM
2460
O
HIS
A
329
23.585
2.661
58.479
1.00
18.85
8


ATOM
2461
N
CYS
A
330
25.264
4.142
58.168
1.00
19.17
7


ATOM
2462
CA
CYS
A
330
25.615
3.647
56.845
1.00
19.01
6


ATOM
2463
CB
CYS
A
330
26.662
4.547
56.200
1.00
18.89
6


ATOM
2464
SG
CYS
A
330
26.065
6.222
55.830
1.00
18.67
16


ATOM
2465
C
CYS
A
330
26.096
2.199
56.900
1.00
19.15
6


ATOM
2466
O
CYS
A
330
25.693
1.389
56.077
1.00
19.29
8


ATOM
2467
N
LEU
A
331
26.947
1.883
57.880
1.00
19.22
7


ATOM
2468
CA
LEU
A
331
27.420
0.503
58.097
1.00
19.91
6


ATOM
2469
CB
LEU
A
331
28.437
0.437
59.243
1.00
19.96
6


ATOM
2470
CG
LEU
A
331
29.908
0.307
58.845
1.00
21.65
6


ATOM
2471
CD1
LEU
A
331
30.670
1.547
59.234
1.00
22.54
6


ATOM
2472
CD2
LEU
A
331
30.524
−0.914
59.524
1.00
22.49
6


ATOM
2473
C
LEU
A
331
26.281
−0.467
58.376
1.00
19.81
6


ATOM
2474
O
LEU
A
331
26.235
−1.564
57.805
1.00
19.80
8


ATOM
2475
N
ASP
A
332
25.366
−0.062
59.257
1.00
19.78
7


ATOM
2476
CA
ASP
A
332
24.220
−0.897
59.619
1.00
20.10
6


ATOM
2477
CB
ASP
A
332
23.408
−0.256
60.753
1.00
20.33
6


ATOM
2478
CG
ASP
A
332
24.145
−0.261
62.087
1.00
21.59
6


ATOM
2479
OD1
ASP
A
332
25.191
−0.942
62.210
1.00
22.98
8


ATOM
2480
OD2
ASP
A
332
23.670
0.422
63.022
1.00
23.86
8


ATOM
2481
C
ASP
A
332
23.323
−1.165
58.413
1.00
19.89
6


ATOM
2482
O
ASP
A
332
22.888
−2.297
58.198
1.00
19.92
8


ATOM
2483
N
ASN
A
333
23.061
−0.119
57.627
1.00
19.48
7


ATOM
2484
CA
ASN
A
333
22.299
−0.250
56.391
1.00
19.35
6


ATOM
2485
CB
ASN
A
333
22.053
1.127
55.752
1.00
19.04
6


ATOM
2486
CG
ASN
A
333
20.868
1.864
56.366
1.00
19.49
6


ATOM
2487
OD1
ASN
A
333
20.703
3.076
56.165
1.00
18.93
8


ATOM
2488
ND2
ASN
A
333
20.033
1.143
57.099
1.00
18.69
7


ATOM
2489
C
ASN
A
333
22.995
−1.174
55.392
1.00
19.44
6


ATOM
2490
O
ASN
A
333
22.347
−2.005
54.754
1.00
19.71
8


ATOM
2491
N
LEU
A
334
24.316
−1.028
55.268
1.00
19.53
7


ATOM
2492
CA
LEU
A
334
25.092
−1.849
54.336
1.00
19.61
6


ATOM
2493
CB
LEU
A
334
26.560
−1.416
54.302
1.00
19.82
6


ATOM
2494
CG
LEU
A
334
27.477
−2.115
53.286
1.00
19.61
6


ATOM
2495
CD1
LEU
A
334
26.985
−1.939
51.843
1.00
20.01
6


ATOM
2496
CD2
LEU
A
334
28.905
−1.620
53.440
1.00
19.55
6


ATOM
2497
C
LEU
A
334
24.981
−3.336
54.670
1.00
19.79
6


ATOM
2498
O
LEU
A
334
24.756
−4.154
53.777
1.00
19.48
8


ATOM
2499
N
LYS
A
335
25.138
−3.672
55.952
1.00
20.08
7


ATOM
2500
CA
LYS
A
335
25.012
−5.060
56.416
1.00
21.16
6


ATOM
2501
CB
LYS
A
335
25.289
−5.159
57.921
1.00
21.01
6


ATOM
2502
CG
LYS
A
335
25.374
−6.589
58.443
1.00
22.32
6


ATOM
2503
CD
LYS
A
335
25.769
−6.626
59.910
1.00
22.83
6


ATOM
2504
CE
LYS
A
335
25.499
−7.998
60.521
1.00
24.73
6


ATOM
2505
NZ
LYS
A
335
24.038
−8.271
60.634
1.00
25.63
7


ATOM
2506
C
LYS
A
335
23.637
−5.637
56.091
1.00
21.23
6


ATOM
2507
O
LYS
A
335
23.533
−6.759
55.590
1.00
21.44
8


ATOM
2508
N
ILE
A
336
22.589
−4.860
56.363
1.00
21.44
7


ATOM
2509
CA
ILE
A
336
21.210
−5.288
56.096
1.00
21.69
6


ATOM
2510
CB
ILE
A
336
20.172
−4.259
56.624
1.00
21.75
6


ATOM
2511
CG1
ILE
A
336
20.167
−4.249
58.158
1.00
22.07
6


ATOM
2512
CD1
ILE
A
336
19.544
−2.998
58.778
1.00
22.69
6


ATOM
2513
CG2
ILE
A
336
18.770
−4.576
56.091
1.00
21.66
6


ATOM
2514
C
ILE
A
336
20.988
−5.560
54.605
1.00
21.92
6


ATOM
2515
O
ILE
A
336
20.445
−6.603
54.236
1.00
21.84
8


ATOM
2516
N
LEU
A
337
21.432
−4.633
53.754
1.00
21.98
7


ATOM
2517
CA
LEU
A
337
21.277
−4.785
52.305
1.00
22.50
6


ATOM
2518
CB
LEU
A
337
21.762
−3.537
51.566
1.00
22.09
6


ATOM
2519
CG
LEU
A
337
20.932
−2.256
51.713
1.00
22.02
6


ATOM
2520
CD1
LEU
A
337
21.780
−1.042
51.385
1.00
21.70
6


ATOM
2521
CD2
LEU
A
337
19.669
−2.292
50.846
1.00
22.24
6


ATOM
2522
C
LEU
A
337
22.000
−6.026
51.781
1.00
22.99
6


ATOM
2523
O
LEU
A
337
21.483
−6.731
50.910
1.00
23.37
8


ATOM
2524
N
ARG
A
338
23.188
−6.289
52.322
1.00
23.58
7


ATOM
2525
CA
ARG
A
338
23.975
−7.467
51.937
1.00
24.38
6


ATOM
2526
CB
ARG
A
338
25.383
−7.391
52.531
1.00
24.30
6


ATOM
2527
CG
ARG
A
338
26.323
−6.492
51.754
1.00
23.96
6


ATOM
2528
CD
ARG
A
338
27.632
−6.265
52.495
1.00
23.56
6


ATOM
2529
NE
ARG
A
338
28.613
−5.594
51.646
1.00
22.34
7


ATOM
2530
CZ
ARG
A
338
29.794
−5.140
52.060
1.00
22.32
6


ATOM
2531
NH1
ARG
A
338
30.160
−5.270
53.331
1.00
22.83
7


ATOM
2532
NH2
ARG
A
338
30.609
−4.548
51.200
1.00
22.28
7


ATOM
2533
C
ARG
A
338
23.303
−8.780
52.338
1.00
25.05
6


ATOM
2534
O
ARG
A
338
23.446
−9.792
51.646
1.00
24.77
8


ATOM
2535
N
GLU
A
339
22.567
−8.753
53.449
1.00
25.86
7


ATOM
2536
CA
GLU
A
339
21.854
−9.937
53.948
1.00
27.24
6


ATOM
2537
CB
GLU
A
339
21.703
−9.872
55.470
1.00
27.32
6


ATOM
2538
CG
GLU
A
339
23.019
−9.983
56.233
1.00
28.40
6


ATOM
2539
CD
GLU
A
339
22.908
−9.502
57.670
1.00
29.57
6


ATOM
2540
OE1
GLU
A
339
22.146
−8.540
57.925
1.00
30.40
8


ATOM
2541
OE2
GLU
A
339
23.590
−10.079
58.544
1.00
30.29
8


ATOM
2542
C
GLU
A
339
20.481
−10.103
53.288
1.00
27.73
6


ATOM
2543
O
GLU
A
339
19.803
−11.116
53.489
1.00
27.75
8


ATOM
2544
N
ASN
A
340
20.083
−9.106
52.500
1.00
28.43
7


ATOM
2545
CA
ASN
A
340
18.814
−9.143
51.777
1.00
29.16
6


ATOM
2546
CB
ASN
A
340
17.826
−8.148
52.392
1.00
29.16
6


ATOM
2547
CG
ASN
A
340
17.479
−8.487
53.825
1.00
29.55
6


ATOM
2548
OD1
ASN
A
340
16.859
−9.516
54.099
1.00
29.43
8


ATOM
2549
ND2
ASN
A
340
17.871
−7.621
54.749
1.00
29.85
7


ATOM
2550
C
ASN
A
340
18.985
−8.871
50.275
1.00
29.59
6


ATOM
2551
O
ASN
A
340
18.555
−7.827
49.779
1.00
29.62
8


ATOM
2552
N
PRO
A
341
19.588
−9.829
49.539
1.00
30.24
7


ATOM
2553
CA
PRO
A
341
19.910
−9.628
48.121
1.00
30.66
6


ATOM
2554
CB
PRO
A
341
20.760
−10.862
47.768
1.00
30.66
6


ATOM
2555
CG
PRO
A
341
21.111
−11.502
49.088
1.00
30.55
6


ATOM
2556
CD
PRO
A
341
19.988
−11.170
49.998
1.00
30.37
6


ATOM
2557
C
PRO
A
341
18.676
−9.553
47.210
1.00
31.08
6


ATOM
2558
O
PRO
A
341
18.807
−9.236
46.026
1.00
31.16
8


ATOM
2559
N
GLN
A
342
17.496
−9.839
47.758
1.00
31.68
7


ATOM
2560
CA
GLN
A
342
16.242
−9.722
47.004
1.00
32.33
6


ATOM
2561
CB
GLN
A
342
15.077
−10.381
47.756
1.00
32.34
6


ATOM
2562
CG
GLN
A
342
14.705
−9.715
49.085
1.00
32.97
6


ATOM
2563
CD
GLN
A
342
15.417
−10.331
50.284
1.00
33.61
6


ATOM
2564
OE1
GLN
A
342
16.330
−11.146
50.135
1.00
33.60
8


ATOM
2565
NE2
GLN
A
342
14.994
−9.943
51.484
1.00
34.10
7


ATOM
2566
C
GLN
A
342
15.907
−8.265
46.675
1.00
32.67
6


ATOM
2567
O
GLN
A
342
15.036
−7.990
45.844
1.00
32.86
8


ATOM
2568
N
VAL
A
343
16.603
−7.339
47.333
1.00
33.09
7


ATOM
2569
CA
VAL
A
343
16.420
−5.911
47.090
1.00
33.29
6


ATOM
2570
CB
VAL
A
343
17.059
−5.050
48.225
1.00
33.39
6


ATOM
2571
CG1
VAL
A
343
18.577
−4.920
48.041
1.00
33.38
6


ATOM
2572
CG2
VAL
A
343
16.400
−3.684
48.298
1.00
33.43
6


ATOM
2573
C
VAL
A
343
16.948
−5.495
45.707
1.00
33.47
6


ATOM
2574
O
VAL
A
343
16.491
−4.500
45.137
1.00
33.44
8


ATOM
2575
N
ARG
A
344
17.900
−6.267
45.177
1.00
33.65
7


ATOM
2576
CA
ARG
A
344
18.460
−6.028
43.844
1.00
34.02
6


ATOM
2577
CB
ARG
A
344
19.572
−7.031
43.530
1.00
34.01
6


ATOM
2578
CG
ARG
A
344
20.754
−7.037
44.475
1.00
33.95
6


ATOM
2579
CD
ARG
A
344
21.813
−7.993
43.936
1.00
34.05
6


ATOM
2580
NE
ARG
A
344
22.876
−8.292
44.893
1.00
33.29
7


ATOM
2581
CZ
ARG
A
344
23.918
−7.500
45.129
1.00
33.06
6


ATOM
2582
NH1
ARG
A
344
24.031
−6.334
44.504
1.00
32.76
7


ATOM
2583
NH2
ARG
A
344
24.842
−7.867
46.008
1.00
32.74
7


ATOM
2584
C
ARG
A
344
17.384
−6.156
42.775
1.00
34.29
6


ATOM
2585
O
ARG
A
344
17.299
−5.333
41.865
1.00
34.31
8


ATOM
2586
N
GLU
A
345
16.575
−7.208
42.889
1.00
34.65
7


ATOM
2587
CA
GLU
A
345
15.495
−7.473
41.946
1.00
35.00
6


ATOM
2588
CB
GLU
A
345
14.923
−8.866
42.192
1.00
34.98
6


ATOM
2589
CG
GLU
A
345
14.387
−9.552
40.954
1.00
35.52
6


ATOM
2590
CD
GLU
A
345
13.661
−10.839
41.285
1.00
35.71
6


ATOM
2591
OE1
GLU
A
345
12.439
−10.782
41.546
1.00
35.80
8


ATOM
2592
OE2
GLU
A
345
14.314
−11.904
41.288
1.00
35.68
8


ATOM
2593
C
GLU
A
345
14.394
−6.423
42.079
1.00
35.09
6


ATOM
2594
O
GLU
A
345
13.767
−6.038
41.092
1.00
35.27
8


ATOM
2595
N
LYS
A
346
14.182
−5.962
43.309
1.00
35.32
7


ATOM
2596
CA
LYS
A
346
13.179
−4.952
43.619
1.00
35.52
6


ATOM
2597
CB
LYS
A
346
13.117
−4.729
45.128
1.00
35.51
6


ATOM
2598
CG
LYS
A
346
11.720
−4.700
45.701
1.00
35.58
6


ATOM
2599
CD
LYS
A
346
11.774
−4.667
47.215
1.00
35.76
6


ATOM
2600
CE
LYS
A
346
10.646
−5.469
47.830
1.00
36.00
6


ATOM
2601
NZ
LYS
A
346
10.636
−5.347
49.314
1.00
35.94
7


ATOM
2602
C
LYS
A
346
13.460
−3.625
42.909
1.00
35.67
6


ATOM
2603
O
LYS
A
346
12.565
−3.049
42.292
1.00
35.78
8


ATOM
2604
N
VAL
A
347
14.704
−3.150
42.996
1.00
35.88
7


ATOM
2605
CA
VAL
A
347
15.076
−1.857
42.401
1.00
36.07
6


ATOM
2606
CB
VAL
A
347
16.398
−1.269
42.992
1.00
36.04
6


ATOM
2607
CG1
VAL
A
347
16.185
−0.808
44.429
1.00
36.01
6


ATOM
2608
CG2
VAL
A
347
17.550
−2.272
42.898
1.00
35.88
6


ATOM
2609
C
VAL
A
347
15.140
−1.890
40.870
1.00
36.33
6


ATOM
2610
O
VAL
A
347
14.891
−0.874
40.215
1.00
36.41
8


ATOM
2611
N
VAL
A
348
15.472
−3.052
40.307
1.00
36.52
7


ATOM
2612
CA
VAL
A
348
15.461
−3.233
38.854
1.00
36.81
6


ATOM
2613
CB
VAL
A
348
16.093
−4.590
38.428
1.00
36.85
6


ATOM
2614
CG1
VAL
A
348
15.800
−4.894
36.958
1.00
36.84
6


ATOM
2615
CG2
VAL
A
348
17.587
−4.578
38.667
1.00
36.61
6


ATOM
2616
C
VAL
A
348
14.027
−3.129
38.331
1.00
37.13
6


ATOM
2617
O
VAL
A
348
13.776
−2.488
37.305
1.00
37.13
8


ATOM
2618
N
ALA
A
349
13.094
−3.740
39.063
1.00
37.45
7


ATOM
2619
CA
ALA
A
349
11.675
−3.731
38.701
1.00
37.83
6


ATOM
2620
CB
ALA
A
349
10.880
−4.597
39.660
1.00
37.72
6


ATOM
2621
C
ALA
A
349
11.096
−2.316
38.648
1.00
38.08
6


ATOM
2622
O
ALA
A
349
10.208
−2.035
37.843
1.00
38.12
8


ATOM
2623
N
ILE
A
350
11.609
−1.435
39.507
1.00
38.41
7


ATOM
2624
CA
ILE
A
350
11.217
−0.023
39.509
1.00
38.79
6


ATOM
2625
CB
ILE
A
350
11.884
0.754
40.677
1.00
38.76
6


ATOM
2626
CG1
ILE
A
350
11.542
0.109
42.024
1.00
38.80
6


ATOM
2627
CD1
ILE
A
350
12.390
0.607
43.182
1.00
38.67
6


ATOM
2628
CG2
ILE
A
350
11.469
2.233
40.658
1.00
38.85
6


ATOM
2629
C
ILE
A
350
11.577
0.652
38.184
1.00
39.08
6


ATOM
2630
O
ILE
A
350
10.773
1.394
37.616
1.00
39.19
8


ATOM
2631
N
PHE
A
351
12.785
0.378
37.695
1.00
39.46
7


ATOM
2632
CA
PHE
A
351
13.306
1.025
36.490
1.00
39.78
6


ATOM
2633
CB
PHE
A
351
14.798
1.340
36.658
1.00
39.67
6


ATOM
2634
CG
PHE
A
351
15.094
2.312
37.767
1.00
39.46
6


ATOM
2635
CD1
PHE
A
351
15.440
1.857
39.038
1.00
39.40
6


ATOM
2636
CE1
PHE
A
351
15.715
2.752
40.069
1.00
39.18
6


ATOM
2637
CZ
PHE
A
351
15.647
4.120
39.834
1.00
39.41
6


ATOM
2638
CE2
PHE
A
351
15.304
4.590
38.569
1.00
39.12
6


ATOM
2639
CD2
PHE
A
351
15.030
3.685
37.543
1.00
39.35
6


ATOM
2640
C
PHE
A
351
13.072
0.199
35.220
1.00
40.14
6


ATOM
2641
O
PHE
A
351
13.471
0.608
34.123
1.00
40.10
8


ATOM
2642
N
ALA
A
352
12.420
−0.955
35.375
1.00
40.59
7


ATOM
2643
CA
ALA
A
352
12.122
−1.847
34.248
1.00
41.09
6


ATOM
2644
CB
ALA
A
352
11.628
−3.201
34.751
1.00
41.04
6


ATOM
2645
C
ALA
A
352
11.113
−1.235
33.271
1.00
41.44
6


ATOM
2646
O
ALA
A
352
11.161
−1.508
32.067
1.00
41.51
8


ATOM
2647
N
GLU
A
353
10.202
−0.418
33.798
1.00
41.79
7


ATOM
2648
CA
GLU
A
353
9.239
0.306
32.970
1.00
42.19
6


ATOM
2649
CB
GLU
A
353
7.818
0.137
33.515
1.00
42.19
6


ATOM
2650
CG
GLU
A
353
6.732
0.761
32.632
1.00
42.62
6


ATOM
2651
CD
GLU
A
353
5.417
0.987
33.368
1.00
42.93
6


ATOM
2652
OE1
GLU
A
353
5.393
0.879
34.616
1.00
43.76
8


ATOM
2653
OE2
GLU
A
353
4.405
1.282
32.695
1.00
43.62
8


ATOM
2654
C
GLU
A
353
9.602
1.788
32.889
1.00
42.15
6


ATOM
2655
O
GLU
A
353
9.853
2.432
33.908
1.00
42.24
8


ATOM
2656
N
SER
A
360
5.006
15.462
24.991
1.00
33.60
7


ATOM
2657
CA
SER
A
360
4.227
16.498
24.316
1.00
33.33
6


ATOM
2658
CB
SER
A
360
4.624
17.890
24.826
1.00
33.56
6


ATOM
2659
OG
SER
A
360
5.972
18.190
24.507
1.00
34.29
8


ATOM
2660
C
SER
A
360
4.386
16.417
22.798
1.00
32.91
6


ATOM
2661
O
SEP
A
360
5.261
15.706
22.292
1.00
32.93
8


ATOM
2662
N
ASP
A
361
3.536
17.149
22.078
1.00
32.32
7


ATOM
2663
CA
ASP
A
361
3.544
17.133
20.613
1.00
31.78
6


ATOM
2664
CB
ASP
A
361
2.160
17.514
20.061
1.00
32.17
6


ATOM
2665
CG
ASP
A
361
1.741
18.933
20.441
1.00
33.38
6


ATOM
2666
OD1
ASP
A
361
2.355
19.524
21.362
1.00
34.59
8


ATOM
2667
OD2
ASP
A
361
0.788
19.455
19.818
1.00
34.63
8


ATOM
2668
C
ASP
A
361
4.624
18.041
20.018
1.00
30.91
6


ATOM
2669
O
ASP
A
361
4.754
18.144
18.793
1.00
31.02
8


ATOM
2670
N
ASN
A
362
5.388
18.698
20.892
1.00
29.69
7


ATOM
2671
CA
ASN
A
362
6.452
19.606
20.475
1.00
28.43
6


ATOM
2672
CB
ASN
A
362
6.709
20.655
21.566
1.00
28.33
6


ATOM
2673
CG
ASN
A
362
7.528
21.849
21.072
1.00
28.33
6


ATOM
2674
OD1
ASN
A
362
7.667
22.847
21.779
1.00
28.67
8


ATOM
2675
ND2
ASN
A
362
8.072
21.749
19.867
1.00
28.47
7


ATOM
2676
C
ASN
A
362
7.729
18.837
20.158
1.00
27.58
6


ATOM
2677
O
ASN
A
362
8.379
18.295
21.059
1.00
27.24
8


ATOM
2678
N
VAL
A
363
8.078
18.792
18.871
1.00
26.42
7


ATOM
2679
CA
VAL
A
363
9.273
18.081
18.399
1.00
25.51
6


ATOM
2680
CB
VAL
A
363
9.370
18.085
16.837
1.00
25.64
6


ATOM
2681
CG1
VAL
A
363
9.858
19.438
16.309
1.00
25.68
6


ATOM
2682
CG2
VAL
A
363
10.260
16.947
16.337
1.00
25.67
6


ATOM
2683
C
VAL
A
363
10.575
18.605
19.043
1.00
24.70
6


ATOM
2684
O
VAL
A
363
11.533
17.853
19.200
1.00
24.39
8


ATOM
2685
N
ASP
A
364
10.585
19.885
19.427
1.00
23.77
7


ATOM
2686
CA
ASP
A
364
11.713
20.488
20.159
1.00
22.98
6


ATOM
2687
CB
ASP
A
364
11.452
21.975
20.424
1.00
22.81
6


ATOM
2688
CG
ASP
A
364
11.733
22.855
19.213
1.00
22.40
6


ATOM
2689
OD1
ASP
A
364
12.408
22.402
18.269
1.00
22.47
8


ATOM
2690
OD2
ASP
A
364
11.278
24.017
19.213
1.00
22.46
8


ATOM
2691
C
ASP
A
364
11.987
19.792
21.496
1.00
22.98
6


ATOM
2692
O
ASP
A
364
13.103
19.848
22.017
1.00
22.61
8


ATOM
2693
N
ALA
A
365
10.960
19.147
22.045
1.00
22.74
7


ATOM
2694
CA
ALA
A
365
11.042
18.546
23.371
1.00
22.77
6


ATOM
2695
CB
ALA
A
365
9.782
18.881
24.175
1.00
22.69
6


ATOM
2696
C
ALA
A
365
11.256
17.032
23.315
1.00
22.89
6


ATOM
2697
O
ALA
A
365
11.188
16.354
24.344
1.00
22.67
8


ATOM
2698
N
GLN
A
366
11.551
16.515
22.123
1.00
22.86
7


ATOM
2699
CA
GLN
A
366
11.510
15.069
21.875
1.00
23.42
6


ATOM
2700
CB
GLN
A
366
10.559
14.761
20.713
1.00
23.34
6


ATOM
2701
CG
GLN
A
366
9.085
14.743
21.110
1.00
23.19
6


ATOM
2702
CD
GLN
A
366
8.141
14.648
19.915
1.00
23.54
6


ATOM
2703
OE1
GLN
A
366
8.548
14.312
18.805
1.00
24.15
8


ATOM
2704
NE2
GLN
A
366
6.872
14.952
20.145
1.00
23.82
7


ATOM
2705
C
GLN
A
366
12.869
14.390
21.638
1.00
23.76
6


ATOM
2706
O
GLN
A
366
12.915
13.258
21.150
1.00
23.61
8


ATOM
2707
N
LEU
A
367
13.961
15.060
22.010
1.00
24.33
7


ATOM
2708
CA
LEU
A
367
15.310
14.488
21.860
1.00
24.97
6


ATOM
2709
CB
LEU
A
367
16.363
15.382
22.541
1.00
24.97
6


ATOM
2710
CG
LEU
A
367
17.811
14.873
22.685
1.00
24.94
6


ATOM
2711
CD1
LEU
A
367
18.431
14.477
21.343
1.00
24.94
6


ATOM
2712
CD2
LEU
A
367
18.672
15.907
23.386
1.00
24.99
6


ATOM
2713
C
LEU
A
367
15.416
13.047
22.381
1.00
25.45
6


ATOM
2714
O
LEU
A
367
15.978
12.173
21.707
1.00
25.48
8


ATOM
2715
N
TYR
A
368
14.861
12.803
23.567
1.00
26.04
7


ATOM
2716
CA
TYR
A
368
15.042
11.518
24.250
1.00
26.75
6


ATOM
2717
CB
TYR
A
368
15.254
11.731
25.751
1.00
26.76
6


ATOM
2718
CG
TYR
A
368
16.489
12.544
26.073
1.00
27.28
6


ATOM
2719
CD1
TYR
A
368
17.758
12.082
25.726
1.00
27.42
6


ATOM
2720
CE1
TYR
A
368
18.896
12.825
26.008
1.00
27.53
6


ATOM
2721
CZ
TYR
A
368
18.775
14.044
26.648
1.00
27.37
6


ATOM
2722
OH
TYR
A
368
19.908
14.772
26.926
1.00
27.63
8


ATOM
2723
CE2
TYR
A
368
17.528
14.530
27.007
1.00
27.01
6


ATOM
2724
CD2
TYR
A
368
16.390
13.779
26.715
1.00
27.03
6


ATOM
2725
C
TYR
A
368
13.912
10.521
23.997
1.00
27.12
6


ATOM
2726
O
TYR
A
368
13.786
9.525
24.708
1.00
27.07
8


ATOM
2727
N
ASN
A
369
13.105
10.784
22.970
1.00
27.74
7


ATOM
2728
CA
ASN
A
369
12.064
9.842
22.549
1.00
28.40
6


ATOM
2729
CB
ASN
A
369
11.006
10.545
21.698
1.00
28.44
6


ATOM
2730
CG
ASN
A
369
9.994
11.311
22.532
1.00
29.10
6


ATOM
2731
OD1
ASN
A
369
10.304
11.803
23.621
1.00
29.89
8


ATOM
2732
ND2
ASN
A
369
8.773
11.423
22.019
1.00
29.54
7


ATOM
2733
C
ASN
A
369
12.628
8.622
21.811
1.00
28.68
6


ATOM
2734
O
ASN
A
369
11.880
7.834
21.233
1.00
29.02
8


ATOM
2735
N
GLY
A
370
13.950
8.471
21.847
1.00
29.10
7


ATOM
2736
CA
GLY
A
370
14.612
7.307
21.268
1.00
29.41
6


ATOM
2737
C
GLY
A
370
15.756
7.670
20.345
1.00
29.60
6


ATOM
2738
O
GLY
A
370
15.851
8.808
19.867
1.00
29.84
8


ATOM
2739
N
PHE
A
371
16.636
6.701
20.103
1.00
29.62
7


ATOM
2740
CA
PHE
A
371
17.723
6.874
19.151
1.00
29.63
6


ATOM
2741
CB
PHE
A
371
18.865
5.896
19.442
1.00
29.99
6


ATOM
2742
CG
PHE
A
371
19.574
6.155
20.745
1.00
30.35
6


ATOM
2743
CD1
PHE
A
371
20.516
7.177
20.851
1.00
30.97
6


ATOM
2744
CE1
PHE
A
371
21.179
7.416
22.057
1.00
30.97
6


ATOM
2745
CZ
PHE
A
371
20.904
6.620
23.170
1.00
31.41
6


ATOM
2746
CE2
PHE
A
371
19.969
5.595
23.074
1.00
30.97
6


ATOM
2747
CD2
PHE
A
371
19.312
5.364
21.864
1.00
30.71
6


ATOM
2748
C
PHE
A
371
17.205
6.668
17.733
1.00
29.29
6


ATOM
2749
O
PHE
A
371
16.379
5.788
17.487
1.00
29.33
8


ATOM
2750
N
PHE
A
372
17.681
7.496
16.808
1.00
29.08
7


ATOM
2751
CA
PHE
A
372
17.369
7.324
15.393
1.00
28.88
6


ATOM
2752
CB
PHE
A
372
17.803
8.556
14.594
1.00
28.77
6


ATOM
2753
CG
PHE
A
372
17.118
9.831
15.013
1.00
28.94
6


ATOM
2754
CD1
PHE
A
372
15.859
10.160
14.514
1.00
29.09
6


ATOM
2755
CE1
PHE
A
372
15.225
11.344
14.894
1.00
29.05
6


ATOM
2756
CZ
PHE
A
372
15.855
12.213
15.776
1.00
29.07
6


ATOM
2757
CE2
PHE
A
372
17.112
11.898
16.277
1.00
29.09
6


ATOM
2758
CD2
PHE
A
372
17.739
10.713
15.892
1.00
28.80
6


ATOM
2759
C
PHE
A
372
18.090
6.089
14.868
1.00
28.71
6


ATOM
2760
O
PHE
A
372
19.146
5.720
15.381
1.00
28.76
8


ATOM
2761
N
SER
A
373
17.517
5.451
13.850
1.00
28.68
7


ATOM
2762
CA
SER
A
373
18.163
4.308
13.206
1.00
28.51
6


ATOM
2763
CB
SER
A
373
17.193
3.605
12.251
1.00
28.57
6


ATOM
2764
OG
SER
A
373
16.772
4.476
11.216
1.00
28.59
8


ATOM
2765
C
SER
A
373
19.420
4.755
12.460
1.00
28.51
6


ATOM
2766
O
SER
A
373
19.623
5.953
12.227
1.00
28.35
8


ATOM
2767
N
ASP
A
374
20.265
3.794
12.101
1.00
28.35
7


ATOM
2768
CA
ASP
A
374
21.471
4.077
11.325
1.00
28.40
6


ATOM
2769
CB
ASP
A
374
22.252
2.788
11.048
1.00
28.57
6


ATOM
2770
CG
ASP
A
374
23.128
2.362
12.219
1.00
28.94
6


ATOM
2771
OD1
ASP
A
374
23.078
3.008
13.291
1.00
29.85
8


ATOM
2772
OD2
ASP
A
374
23.874
1.373
12.062
1.00
29.40
8


ATOM
2773
C
ASP
A
374
21.132
4.779
10.009
1.00
28.18
6


ATOM
2774
O
ASP
A
374
21.797
5.741
9.624
1.00
28.04
8


ATOM
2775
N
ALA
A
375
20.088
4.293
9.334
1.00
28.00
7


ATOM
2776
CA
ALA
A
375
19.644
4.859
8.058
1.00
27.81
6


ATOM
2777
CB
ALA
A
375
18.574
3.976
7.427
1.00
27.84
6


ATOM
2778
C
ALA
A
375
19.133
6.293
8.217
1.00
27.59
6


ATOM
2779
O
ALA
A
375
19.440
7.161
7.399
1.00
27.70
8


ATOM
2780
N
ASP
A
376
18.362
6.535
9.277
1.00
27.48
7


ATOM
2781
CA
ASP
A
376
17.840
7.875
9.567
1.00
27.20
6


ATOM
2782
CB
ASP
A
376
16.904
7.848
10.780
1.00
27.40
6


ATOM
2783
CG
ASP
A
376
15.481
7.445
10.415
1.00
27.81
6


ATOM
2784
OD1
ASP
A
376
15.093
7.582
9.235
1.00
27.89
8


ATOM
2785
OD2
ASP
A
376
14.746
6.996
11.317
1.00
29.32
8


ATOM
2786
C
ASP
A
376
18.952
8.909
9.766
1.00
26.85
6


ATOM
2787
O
ASP
A
376
18.857
10.027
9.261
1.00
26.80
8


ATOM
2788
N
ARG
A
377
20.004
8.521
10.487
1.00
26.44
7


ATOM
2789
CA
ARG
A
377
21.169
9.388
10.708
1.00
26.42
6


ATOM
2790
CB
ARG
A
377
22.107
8.781
11.766
1.00
26.71
6


ATOM
2791
CG
ARG
A
377
23.458
9.518
11.965
1.00
28.22
6


ATOM
2792
CD
ARG
A
377
23.281
10.986
12.387
1.00
30.39
6


ATOM
2793
NE
ARG
A
377
22.424
11.120
13.564
1.00
31.49
7


ATOM
2794
CZ
ARG
A
377
21.860
12.257
13.961
1.00
31.86
6


ATOM
2795
NH1
ARG
A
377
22.055
13.378
13.277
1.00
32.25
7


ATOM
2796
NH2
ARG
A
377
21.093
12.271
15.043
1.00
31.79
7


ATOM
2797
C
ARG
A
377
21.924
9.671
9.407
1.00
25.85
6


ATOM
2798
O
ARG
A
377
22.355
10.802
9.166
1.00
25.70
8


ATOM
2799
N
ALA
A
378
22.076
8.641
8.574
1.00
25.25
7


ATOM
2800
CA
ALA
A
378
22.675
8.801
7.250
1.00
24.71
6


ATOM
2801
CB
ALA
A
378
22.779
7.450
6.541
1.00
24.87
6


ATOM
2802
C
ALA
A
378
21.869
9.795
6.410
1.00
24.39
6


ATOM
2803
O
ALA
A
378
22.442
10.626
5.699
1.00
24.49
8


ATOM
2804
N
ALA
A
379
20.542
9.706
6.512
1.00
23.71
7


ATOM
2805
CA
ALA
A
379
19.635
10.619
5.816
1.00
23.08
6


ATOM
2806
CB
ALA
A
379
18.191
10.109
5.912
1.00
23.21
6


ATOM
2807
C
ALA
A
379
19.739
12.045
6.363
1.00
22.67
6


ATOM
2808
O
ALA
A
379
19.781
13.009
5.599
1.00
21.90
8


ATOM
2809
N
MET
A
380
19.794
12.168
7.690
1.00
22.16
7


ATOM
2810
CA
MET
A
380
19.915
13.475
8.343
1.00
22.18
6


ATOM
2811
CB
MET
A
380
19.674
13.346
9.852
1.00
22.10
6


ATOM
2812
CG
MET
A
380
18.234
12.968
10.214
1.00
22.50
6


ATOM
2813
SD
MET
A
380
17.978
12.667
11.988
1.00
24.18
16


ATOM
2814
CE
MET
A
380
17.743
14.328
12.597
1.00
24.12
6


ATOM
2815
C
MET
A
380
21.275
14.129
8.062
1.00
21.74
6


ATOM
2816
O
MET
A
380
21.386
15.355
8.022
1.00
21.39
8


ATOM
2817
N
LYS
A
381
22.297
13.297
7.857
1.00
21.31
7


ATOM
2818
CA
LYS
A
381
23.625
13.768
7.458
1.00
21.13
6


ATOM
2819
CB
LYS
A
381
24.644
12.623
7.534
1.00
20.93
6


ATOM
2820
CG
LYS
A
381
26.078
13.025
7.195
1.00
21.65
6


ATOM
2821
CD
LYS
A
381
27.047
11.864
7.401
1.00
21.67
6


ATOM
2822
CE
LYS
A
381
28.488
12.305
7.191
1.00
22.46
6


ATOM
2823
NZ
LYS
A
381
29.396
11.150
6.934
1.00
22.12
7


ATOM
2824
C
LYS
A
381
23.606
14.379
6.049
1.00
20.78
6


ATOM
2825
O
LYS
A
381
24.323
15.345
5.773
1.00
20.57
8


ATOM
2826
N
ILE
A
382
22.790
13.810
5.164
1.00
20.48
7


ATOM
2827
CA
ILE
A
382
22.581
14.394
3.836
1.00
20.43
6


ATOM
2828
CB
ILE
A
382
21.766
13.455
2.901
1.00
20.56
6


ATOM
2829
CG1
ILE
A
382
22.596
12.212
2.545
1.00
20.26
6


ATOM
2830
CD1
ILE
A
382
21.828
11.133
1.794
1.00
20.99
6


ATOM
2831
CG2
ILE
A
382
21.327
14.196
1.635
1.00
19.44
6


ATOM
2832
C
ILE
A
382
21.924
15.780
3.947
1.00
20.55
6


ATOM
2833
O
ILE
A
382
22.313
16.716
3.244
1.00
20.65
8


ATOM
2834
N
VAL
A
383
20.952
15.914
4.849
1.00
20.73
7


ATOM
2835
CA
VAL
A
383
20.307
17.211
5.083
1.00
20.72
6


ATOM
2836
CB
VAL
A
383
19.166
17.118
6.137
1.00
20.92
6


ATOM
2837
CG1
VAL
A
383
18.723
18.510
6.571
1.00
20.94
6


ATOM
2838
CG2
VAL
A
383
17.988
16.330
5.582
1.00
20.80
6


ATOM
2839
C
VAL
A
383
21.336
18.246
5.525
1.00
20.80
6


ATOM
2840
O
VAL
A
383
21.402
19.347
4.979
1.00
20.54
8


ATOM
2841
N
LEU
A
384
22.147
17.871
6.509
1.00
21.06
7


ATOM
2842
CA
LEU
A
384
23.175
18.742
7.050
1.00
21.36
6


ATOM
2843
CB
LEU
A
384
23.929
18.009
8.166
1.00
21.22
6


ATOM
2844
CG
LEU
A
384
25.140
18.682
8.804
1.00
21.34
6


ATOM
2845
CD1
LEU
A
384
24.724
19.968
9.490
1.00
20.96
6


ATOM
2846
CD2
LEU
A
384
25.800
17.728
9.785
1.00
20.69
6


ATOM
2847
C
LEU
A
384
24.154
19.222
5.972
1.00
21.96
6


ATOM
2848
O
LEU
A
384
24.540
20.394
5.945
1.00
21.43
8


ATOM
2849
N
GLU
A
385
24.533
18.318
5.075
1.00
22.80
7


ATOM
2850
CA
GLU
A
385
25.612
18.590
4.139
1.00
24.07
6


ATOM
2851
CB
GLU
A
385
26.560
17.385
4.052
1.00
23.85
6


ATOM
2852
CG
GLU
A
385
27.179
17.028
5.418
1.00
24.42
6


ATOM
2853
CD
GLU
A
385
28.210
15.910
5.358
1.00
25.16
6


ATOM
2854
OE1
GLU
A
385
28.292
15.205
4.328
1.00
26.14
8


ATOM
2855
OE2
GLU
A
385
28.935
15.732
6.361
1.00
26.19
8


ATOM
2856
C
GLU
A
385
25.116
19.044
2.764
1.00
24.64
6


ATOM
2857
O
GLU
A
385
25.911
19.297
1.865
1.00
24.84
8


ATOM
2858
N
THR
A
386
23.798
19.160
2.620
1.00
25.75
7


ATOM
2859
CA
THR
A
386
23.194
19.748
1.424
1.00
26.53
6


ATOM
2860
CB
THR
A
386
21.802
19.114
1.111
1.00
26.26
6


ATOM
2861
OG1
THR
A
386
21.964
17.718
0.831
1.00
25.28
8


ATOM
2862
CG2
THR
A
386
21.144
19.786
−0.090
1.00
26.38
6


ATOM
2863
C
THR
A
386
23.064
21.265
1.585
1.00
27.66
6


ATOM
2864
O
THR
A
386
22.743
21.764
2.668
1.00
27.98
8


ATOM
2865
N
GLU
A
387
23.334
21.991
0.503
1.00
29.12
7


ATOM
2866
CA
GLU
A
387
23.162
23.445
0.473
1.00
30.48
6


ATOM
2867
CB
GLU
A
387
23.592
24.009
−0.887
1.00
30.60
6


ATOM
2868
CG
GLU
A
387
24.936
23.485
−1.374
1.00
31.46
6


ATOM
2869
CD
GLU
A
387
25.792
24.560
−2.009
1.00
33.21
6


ATOM
2870
OE1
GLU
A
387
25.768
25.713
−1.519
1.00
34.12
8


ATOM
2871
OE2
GLU
A
387
26.507
24.247
−2.985
1.00
33.67
8


ATOM
2872
C
GLU
A
387
21.712
23.831
0.767
1.00
31.33
6


ATOM
2873
O
GLU
A
387
20.785
23.220
0.228
1.00
31.57
8


ATOM
2874
N
PRO
A
388
21.512
24.849
1.628
1.00
32.04
7


ATOM
2875
CA
PRO
A
388
20.176
25.261
2.074
1.00
32.56
6


ATOM
2876
CB
PRO
A
388
20.451
26.558
2.834
1.00
32.54
6


ATOM
2877
CG
PRO
A
388
21.848
26.410
3.319
1.00
32.35
6


ATOM
2878
CD
PRO
A
388
22.571
25.678
2.237
1.00
32.36
6


ATOM
2879
C
PRO
A
388
19.217
25.517
0.910
1.00
32.99
6


ATOM
2880
O
PRO
A
388
18.030
25.181
0.996
1.00
33.09
8


ATOM
2881
N
ARG
A
389
19.741
26.090
−0.172
1.00
33.52
7


ATOM
2882
CA
ARG
A
389
18.949
26.379
−1.369
1.00
34.09
6


ATOM
2883
CB
ARG
A
389
19.723
27.302
−2.322
1.00
34.15
6


ATOM
2884
CG
ARG
A
389
21.085
26.770
−2.763
1.00
34.53
6


ATOM
2885
CD
ARG
A
389
21.702
27.661
−3.831
1.00
34.96
6


ATOM
2886
NE
ARG
A
389
23.133
27.407
−4.015
1.00
36.37
7


ATOM
2887
CZ
ARG
A
389
23.642
26.430
−4.766
1.00
36.73
6


ATOM
2888
NH1
ARG
A
389
22.844
25.585
−5.410
1.00
36.62
7


ATOM
2889
NH2
ARG
A
389
24.958
26.295
−4.869
1.00
37.32
7


ATOM
2890
C
ARG
A
389
18.499
25.112
−2.107
1.00
34.18
6


ATOM
2891
O
ARG
A
389
17.590
25.162
−2.938
1.00
34.13
8


ATOM
2892
N
ASN
A
390
19.133
23.982
−1.789
1.00
34.27
7


ATOM
2893
CA
ASN
A
390
18.845
22.708
−2.452
1.00
34.26
6


ATOM
2894
CB
ASN
A
390
20.147
22.026
−2.878
1.00
34.43
6


ATOM
2895
CG
ASN
A
390
20.818
22.720
−4.048
1.00
34.48
6


ATOM
2896
OD1
ASN
A
390
20.181
23.453
−4.805
1.00
35.38
8


ATOM
2897
ND2
ASN
A
390
22.114
22.482
−4.206
1.00
34.81
7


ATOM
2898
C
ASN
A
390
18.005
21.740
−1.617
1.00
34.15
6


ATOM
2899
O
ASN
A
390
17.795
20.593
−2.017
1.00
34.10
8


ATOM
2900
N
LEU
A
391
17.526
22.204
−0.463
1.00
34.05
7


ATOM
2901
CA
LEU
A
391
16.720
21.365
0.436
1.00
33.90
6


ATOM
2902
CB
LEU
A
391
16.736
21.908
1.874
1.00
33.73
6


ATOM
2903
CG
LEU
A
391
17.985
21.612
2.712
1.00
32.85
6


ATOM
2904
CD1
LEU
A
391
17.889
22.297
4.073
1.00
32.38
6


ATOM
2905
CD2
LEU
A
391
18.201
20.109
2.880
1.00
31.92
6


ATOM
2906
C
LEU
A
391
15.275
21.116
−0.035
1.00
34.07
6


ATOM
2907
O
LEU
A
391
14.740
20.031
0.197
1.00
34.10
8


ATOM
2908
N
PRO
A
392
14.634
22.122
−0.679
1.00
34.29
7


ATOM
2909
CA
PRO
A
392
13.293
21.895
−1.235
1.00
34.54
6


ATOM
2910
CB
PRO
A
392
12.980
23.219
−1.942
1.00
34.58
6


ATOM
2911
CG
PRO
A
392
13.819
24.222
−1.250
1.00
34.49
6


ATOM
2912
CD
PRO
A
392
15.082
23.511
−0.899
1.00
34.40
6


ATOM
2913
C
PRO
A
392
13.248
20.739
−2.240
1.00
34.86
6


ATOM
2914
O
PRO
A
392
12.278
19.979
−2.262
1.00
34.92
8


ATOM
2915
N
ALA
A
393
14.299
20.607
−3.049
1.00
35.12
7


ATOM
2916
CA
ALA
A
393
14.345
19.599
−4.111
1.00
35.33
6


ATOM
2917
CB
ALA
A
393
15.112
20.136
−5.318
1.00
35.30
6


ATOM
2918
C
ALA
A
393
14.927
18.255
−3.659
1.00
35.50
6


ATOM
2919
O
ALA
A
393
14.965
17.300
−4.438
1.00
35.59
8


ATOM
2920
N
LEU
A
394
15.370
18.181
−2.404
1.00
35.73
7


ATOM
2921
CA
LEU
A
394
15.972
16.953
−1.867
1.00
35.99
6


ATOM
2922
CB
LEU
A
394
16.553
17.197
−0.467
1.00
35.98
6


ATOM
2923
CG
LEU
A
394
17.430
16.108
0.171
1.00
35.86
6


ATOM
2924
CD1
LEU
A
394
18.642
15.763
−0.696
1.00
35.75
6


ATOM
2925
CD2
LEU
A
394
17.873
16.533
1.563
1.00
35.96
6


ATOM
2926
C
LEU
A
394
14.970
15.795
−1.852
1.00
36.28
6


ATOM
2927
O
LEU
A
394
13.812
15.967
−1.466
1.00
36.29
8


ATOM
2928
N
ASP
A
395
15.433
14.619
−2.274
1.00
36.61
7


ATOM
2929
CA
ASP
A
395
14.552
13.483
−2.555
1.00
36.96
6


ATOM
2930
CB
ASP
A
395
14.614
13.124
−4.052
1.00
37.19
6


ATOM
2931
CG
ASP
A
395
16.049
12.907
−4.553
1.00
37.77
6


ATOM
2932
OD1
ASP
A
395
17.012
13.263
−3.829
1.00
38.34
8


ATOM
2933
OD2
ASP
A
395
16.210
12.383
−5.679
1.00
38.22
8


ATOM
2934
C
ASP
A
395
14.858
12.247
−1.698
1.00
36.85
6


ATOM
2935
O
ASP
A
395
14.892
11.120
−2.207
1.00
36.99
8


ATOM
2936
N
ILE
A
396
15.053
12.458
−0.398
1.00
36.67
7


ATOM
2937
CA
ILE
A
396
15.412
11.362
0.513
1.00
36.40
6


ATOM
2938
CB
ILE
A
396
16.673
11.688
1.359
1.00
36.50
6


ATOM
2939
CG1
ILE
A
396
16.477
12.981
2.158
1.00
36.43
6


ATOM
2940
CD1
ILE
A
396
17.479
13.165
3.279
1.00
36.78
6


ATOM
2941
CG2
ILE
A
396
17.917
11.758
0.460
1.00
36.55
6


ATOM
2942
C
ILE
A
396
14.257
10.913
1.419
1.00
36.12
6


ATOM
2943
O
ILE
A
396
13.197
11.545
1.454
1.00
36.03
8


ATOM
2944
N
THR
A
397
14.482
9.824
2.154
1.00
35.81
7


ATOM
2945
CA
THR
A
397
13.424
9.159
2.913
1.00
35.49
6


ATOM
2946
CB
THR
A
397
13.129
7.752
2.333
1.00
35.54
6


ATOM
2947
OG1
THR
A
397
12.949
7.841
0.913
1.00
36.23
8


ATOM
2948
CG2
THR
A
397
11.879
7.159
2.957
1.00
35.57
6


ATOM
2949
C
THR
A
397
13.769
9.030
4.399
1.00
35.06
6


ATOM
2950
O
THR
A
397
14.891
8.660
4.756
1.00
35.10
8


ATOM
2951
N
PHE
A
398
12.796
9.340
5.255
1.00
34.49
7


ATOM
2952
CA
PHE
A
398
12.927
9.145
6.702
1.00
33.98
6


ATOM
2953
CB
PHE
A
398
12.780
10.475
7.455
1.00
34.19
6


ATOM
2954
CG
PHE
A
398
13.592
11.599
6.881
1.00
34.43
6


ATOM
2955
CD1
PHE
A
398
14.972
11.660
7.086
1.00
34.71
6


ATOM
2956
CE1
PHE
A
398
15.725
12.708
6.557
1.00
34.76
6


ATOM
2957
CZ
PHE
A
398
15.097
13.710
5.820
1.00
34.92
6


ATOM
2958
CE2
PHE
A
398
13.720
13.660
5.613
1.00
34.74
6


ATOM
2959
CD2
PHE
A
398
12.976
12.610
6.146
1.00
34.51
6


ATOM
2960
C
PHE
A
398
11.863
8.176
7.204
1.00
33.50
6


ATOM
2961
O
PHE
A
398
10.778
8.079
6.622
1.00
33.42
8


ATOM
2962
N
VAL
A
399
12.169
7.473
8.292
1.00
32.78
7


ATOM
2963
CA
VAL
A
399
11.183
6.622
8.952
1.00
32.26
6


ATOM
2964
CB
VAL
A
399
11.723
5.187
9.219
1.00
32.22
6


ATOM
2965
CG1
VAL
A
399
10.639
4.312
9.848
1.00
32.33
6


ATOM
2966
CG2
VAL
A
399
12.227
4.553
7.923
1.00
32.59
6


ATOM
2967
C
VAL
A
399
10.707
7.268
10.253
1.00
31.72
6


ATOM
2968
O
VAL
A
399
9.505
7.380
10.490
1.00
31.85
8


ATOM
2969
N
ASP
A
400
11.659
7.707
11.078
1.00
31.03
7


ATOM
2970
CA
ASP
A
400
11.350
8.326
12.367
1.00
30.39
6


ATOM
2971
CB
ASP
A
400
12.633
8.762
13.080
1.00
30.47
6


ATOM
2972
CG
ASP
A
400
12.404
9.105
14.539
1.00
30.50
6


ATOM
2973
OD1
ASP
A
400
11.746
10.131
14.819
1.00
29.80
8


ATOM
2974
OD2
ASP
A
400
12.889
8.352
15.408
1.00
31.06
8


ATOM
2975
C
ASP
A
400
10.406
9.511
12.195
1.00
29.85
6


ATOM
2976
O
ASP
A
400
10.649
10.397
11.375
1.00
29.84
8


ATOM
2977
N
LYS
A
401
9.332
9.513
12.981
1.00
29.15
7


ATOM
2978
CA
LYS
A
401
8.240
10.477
12.829
1.00
28.50
6


ATOM
2979
CB
LYS
A
401
7.026
10.042
13.662
1.00
28.69
6


ATOM
2980
CG
LYS
A
401
6.427
8.690
13.246
1.00
29.56
6


ATOM
2981
CD
LYS
A
401
5.299
8.849
12.222
1.00
31.12
6


ATOM
2982
CE
LYS
A
401
3.947
9.071
12.908
1.00
31.76
6


ATOM
2983
NZ
LYS
A
401
2.831
9.216
11.932
1.00
32.57
7


ATOM
2984
C
LYS
A
401
8.646
11.908
13.187
1.00
27.77
6


ATOM
2985
O
LYS
A
401
8.044
12.867
12.701
1.00
27.88
8


ATOM
2986
N
ARG
A
402
9.673
12.045
14.027
1.00
26.67
7


ATOM
2987
CA
ARG
A
402
10.144
13.360
14.470
1.00
25.83
6


ATOM
2988
CB
ARG
A
402
11.170
13.215
15.595
1.00
25.44
6


ATOM
2989
CG
ARG
A
402
10.636
12.604
16.876
1.00
24.77
6


ATOM
2990
CD
ARG
A
402
11.769
12.361
17.865
1.00
22.45
6


ATOM
2991
NE
ARG
A
402
12.590
11.208
17.496
1.00
20.66
7


ATOM
2992
CZ
ARG
A
402
13.667
10.809
18.167
1.00
19.71
6


ATOM
2993
NH1
ARG
A
402
14.073
11.475
19.242
1.00
18.90
7


ATOM
2994
NH2
ARG
A
402
14.340
9.742
17.763
1.00
19.13
7


ATOM
2995
C
ARG
A
402
10.769
14.169
13.333
1.00
25.37
6


ATOM
2996
O
ARG
A
402
10.671
15.399
13.315
1.00
25.39
8


ATOM
2997
N
ILE
A
403
11.411
13.476
12.395
1.00
24.74
7


ATOM
2998
CA
ILE
A
403
12.288
14.129
11.411
1.00
24.21
6


ATOM
2999
CB
ILE
A
403
13.160
13.113
10.620
1.00
24.36
6


ATOM
3000
CG1
ILE
A
403
13.896
12.177
11.586
1.00
24.46
6


ATOM
3001
CD1
ILE
A
403
14.659
11.041
10.908
1.00
23.96
6


ATOM
3002
CG2
ILE
A
403
14.170
13.854
9.730
1.00
24.51
6


ATOM
3003
C
ILE
A
403
11.565
15.102
10.458
1.00
23.96
6


ATOM
3004
O
ILE
A
403
12.099
16.171
10.148
1.00
23.88
8


ATOM
3005
N
GLU
A
404
10.360
14.737
10.013
1.00
23.47
7


ATOM
3006
CA
GLU
A
404
9.563
15.613
9.138
1.00
22.96
6


ATOM
3007
CB
GLU
A
404
8.213
14.966
8.788
1.00
23.13
6


ATOM
3008
CG
GLU
A
404
7.498
15.584
7.560
1.00
24.03
6


ATOM
3009
CD
GLU
A
404
6.828
16.938
7.853
1.00
25.31
6


ATOM
3010
OE1
GLU
A
404
6.226
17.101
8.942
1.00
26.78
8


ATOM
3011
OE2
GLU
A
404
6.912
17.842
6.991
1.00
24.96
8


ATOM
3012
C
GLU
A
404
9.342
16.980
9.784
1.00
22.57
6


ATOM
3013
O
GLU
A
404
9.489
18.018
9.131
1.00
21.94
8


ATOM
3014
N
LYS
A
405
8.991
16.966
11.069
1.00
22.05
7


ATOM
3015
CA
LYS
A
405
8.772
18.189
11.833
1.00
21.97
6


ATOM
3016
CB
LYS
A
405
8.099
17.866
13.175
1.00
22.00
6


ATOM
3017
CG
LYS
A
405
6.824
17.030
13.051
1.00
22.65
6


ATOM
3018
CD
LYS
A
405
6.321
16.543
14.417
1.00
23.92
6


ATOM
3019
CE
LYS
A
405
5.144
15.581
14.255
1.00
26.28
6


ATOM
3020
NZ
LYS
A
405
4.636
15.069
15.564
1.00
26.95
7


ATOM
3021
C
LYS
A
405
10.092
18.923
12.069
1.00
21.21
6


ATOM
3022
O
LYS
A
405
10.158
20.153
11.963
1.00
21.26
8


ATOM
3023
N
LEU
A
406
11.144
18.166
12.373
1.00
20.28
7


ATOM
3024
CA
LEU
A
406
12.463
18.758
12.575
1.00
19.71
6


ATOM
3025
CB
LEU
A
406
13.491
17.703
13.001
1.00
20.01
6


ATOM
3026
CG
LEU
A
406
13.441
17.215
14.454
1.00
19.85
6


ATOM
3027
CD1
LEU
A
406
14.268
15.952
14.615
1.00
19.87
6


ATOM
3028
CD2
LEU
A
406
13.897
18.293
15.446
1.00
20.53
6


ATOM
3029
C
LEU
A
406
12.925
19.462
11.313
1.00
19.32
6


ATOM
3030
O
LEU
A
406
13.421
20.589
11.370
1.00
19.21
8


ATOM
3031
N
LEU
A
407
12.742
18.805
10.172
1.00
18.83
7


ATOM
3032
CA
LEU
A
407
13.170
19.370
8.902
1.00
18.57
6


ATOM
3033
CB
LEU
A
407
13.028
18.348
7.768
1.00
18.53
6


ATOM
3034
CG
LEU
A
407
13.509
18.842
6.397
1.00
18.48
6


ATOM
3035
CD1
LEU
A
407
14.974
19.258
6.440
1.00
19.88
6


ATOM
3036
CD2
LEU
A
407
13.270
17.799
5.307
1.00
18.90
6


ATOM
3037
C
LEU
A
407
12.405
20.648
8.571
1.00
18.84
6


ATOM
3038
O
LEU
A
407
12.995
21.618
8.089
1.00
18.90
8


ATOM
3039
N
PHE
A
408
11.095
20.647
8.819
1.00
18.64
7


ATOM
3040
CA
PHE
A
408
10.287
21.827
8.534
1.00
19.04
6


ATOM
3041
CB
PHE
A
408
8.797
21.578
8.735
1.00
19.21
6


ATOM
3042
CG
PHE
A
408
7.962
22.812
8.531
1.00
19.93
6


ATOM
3043
CD1
PHE
A
408
7.833
23.374
7.257
1.00
20.23
6


ATOM
3044
CE1
PHE
A
408
7.092
24.536
7.059
1.00
20.75
6


ATOM
3045
CZ
PHE
A
408
6.477
25.158
8.138
1.00
19.52
6


ATOM
3046
CE2
PHE
A
408
6.609
24.617
9.422
1.00
19.66
6


ATOM
3047
CD2
PHE
A
408
7.358
23.451
9.611
1.00
19.92
6


ATOM
3048
C
PHE
A
408
10.712
23.013
9.385
1.00
18.98
6


ATOM
3049
O
PHE
A
408
10.918
24.108
8.861
1.00
18.89
8


ATOM
3050
N
ASN
A
409
10.812
22.785
10.700
1.00
18.64
7


ATOM
3051
CA
ASN
A
409
11.253
23.812
11.654
1.00
18.84
6


ATOM
3052
CB
ASN
A
409
11.259
23.252
13.075
1.00
19.12
6


ATOM
3053
CG
ASN
A
409
9.876
23.187
13.688
1.00
19.32
6


ATOM
3054
OD1
ASN
A
409
8.886
23.611
13.089
1.00
20.07
8


ATOM
3055
ND2
ASN
A
409
9.805
22.668
14.908
1.00
19.67
7


ATOM
3056
C
ASN
A
409
12.634
24.348
11.318
1.00
18.74
6


ATOM
3057
O
ASN
A
409
12.894
25.548
11.433
1.00
18.69
8


ATOM
3058
N
TYR
A
410
13.508
23.444
10.885
1.00
18.82
7


ATOM
3059
CA
TYR
A
410
14.873
23.781
10.511
1.00
18.34
6


ATOM
3060
CB
TYR
A
410
15.638
22.487
10.222
1.00
18.67
6


ATOM
3061
CG
TYR
A
410
17.043
22.648
9.702
1.00
18.88
6


ATOM
3062
CD1
TYR
A
410
18.090
23.044
10.545
1.00
19.44
6


ATOM
3063
CE1
TYR
A
410
19.389
23.173
10.063
1.00
18.92
6


ATOM
3064
CZ
TYR
A
410
19.652
22.882
8.727
1.00
18.31
6


ATOM
3065
OH
TYR
A
410
20.931
22.991
8.232
1.00
19.44
8


ATOM
3066
CE2
TYR
A
410
18.632
22.473
7.883
1.00
19.61
6


ATOM
3067
CD2
TYR
A
410
17.340
22.352
8.374
1.00
18.93
6


ATOM
3068
C
TYR
A
410
14.898
24.744
9.315
1.00
18.15
6


ATOM
3069
O
TYR
A
410
15.539
25.796
9.365
1.00
18.32
8


ATOM
3070
N
ARG
A
411
14.160
24.405
8.263
1.00
17.91
7


ATOM
3071
CA
ARG
A
411
14.062
25.278
7.093
1.00
17.70
6


ATOM
3072
CB
ARG
A
411
13.369
24.553
5.928
1.00
17.55
6


ATOM
3073
CG
ARG
A
411
14.069
23.272
5.485
1.00
17.37
6


ATOM
3074
CD
ARG
A
411
13.507
22.730
4.162
1.00
18.08
6


ATOM
3075
NE
ARG
A
411
13.321
23.806
3.195
1.00
19.85
7


ATOM
3076
CZ
ARG
A
411
12.218
24.013
2.478
1.00
20.73
6


ATOM
3077
NH1
ARG
A
411
11.185
23.184
2.559
1.00
20.45
7


ATOM
3078
NH2
ARG
A
411
12.166
25.046
1.653
1.00
20.58
7


ATOM
3079
C
ARG
A
411
13.343
26.595
7.424
1.00
17.61
6


ATOM
3080
O
ARG
A
411
13.824
27.670
7.082
1.00
18.08
8


ATOM
3081
N
ALA
A
412
12.188
26.501
8.079
1.00
17.49
7


ATOM
3082
CA
ALA
A
412
11.402
27.685
8.447
1.00
17.63
6


ATOM
3083
CB
ALA
A
412
10.116
27.268
9.124
1.00
17.68
6


ATOM
3084
C
ALA
A
412
12.171
28.665
9.334
1.00
17.94
6


ATOM
3085
O
ALA
A
412
12.152
29.873
9.095
1.00
18.32
8


ATOM
3086
N
ARG
A
413
12.856
28.140
10.347
1.00
18.19
7


ATOM
3087
CA
ARG
A
413
13.562
28.993
11.309
1.00
17.94
6


ATOM
3088
CB
ARG
A
413
13.883
28.226
12.585
1.00
18.37
6


ATOM
3089
CG
ARG
A
413
12.677
27.928
13.429
1.00
17.52
6


ATOM
3090
CD
ARG
A
413
13.075
27.092
14.622
1.00
18.65
6


ATOM
3091
NE
ARG
A
413
11.943
26.813
15.494
1.00
19.98
7


ATOM
3092
CZ
ARG
A
413
11.836
25.720
16.235
1.00
20.14
6


ATOM
3093
NH1
ARG
A
413
12.784
24.787
16.185
1.00
20.05
7


ATOM
3094
NH2
ARG
A
413
10.776
25.552
17.016
1.00
20.78
7


ATOM
3095
C
ARG
A
413
14.832
29.598
10.745
1.00
18.29
6


ATOM
3096
O
ARG
A
413
15.133
30.762
11.006
1.00
18.74
8


ATOM
3097
N
ASN
A
414
15.576
28.811
9.968
1.00
18.54
7


ATOM
3098
CA
ASN
A
414
16.899
29.227
9.522
1.00
19.31
6


ATOM
3099
CB
ASN
A
414
17.873
28.050
9.558
1.00
19.40
6


ATOM
3100
CG
ASN
A
414
18.164
27.577
10.965
1.00
21.04
6


ATOM
3101
OD1
ASN
A
414
17.837
26.450
11.329
1.00
23.62
8


ATOM
3102
ND2
ASN
A
414
18.768
28.442
11.773
1.00
21.00
7


ATOM
3103
C
ASN
A
414
16.897
29.864
8.142
1.00
19.66
6


ATOM
3104
O
ASN
A
414
17.654
30.807
7.885
1.00
19.89
8


ATOM
3105
N
PHE
A
415
16.037
29.348
7.262
1.00
19.68
7


ATOM
3106
CA
PHE
A
415
16.052
29.712
5.842
1.00
20.51
6


ATOM
3107
CB
PHE
A
415
16.673
28.567
5.027
1.00
20.04
6


ATOM
3108
CG
PHE
A
415
17.913
27.971
5.654
1.00
20.86
6


ATOM
3109
CD1
PHE
A
415
19.077
28.729
5.795
1.00
20.73
6


ATOM
3110
CE1
PHE
A
415
20.223
28.181
6.379
1.00
20.29
6


ATOM
3111
CZ
PHE
A
415
20.213
26.861
6.826
1.00
19.99
6


ATOM
3112
CE2
PHE
A
415
19.069
26.096
6.688
1.00
21.34
6


ATOM
3113
CD2
PHE
A
415
17.922
26.649
6.100
1.00
20.91
6


ATOM
3114
C
PHE
A
415
14.641
30.052
5.313
1.00
21.15
6


ATOM
3115
O
PHE
A
415
14.144
29.397
4.388
1.00
21.43
8


ATOM
3116
N
PRO
A
416
13.996
31.086
5.896
1.00
22.16
7


ATOM
3117
CA
PRO
A
416
12.593
31.376
5.550
1.00
22.37
6


ATOM
3118
CB
PRO
A
416
12.203
32.507
6.514
1.00
22.54
6


ATOM
3119
CG
PRO
A
416
13.488
33.086
7.002
1.00
22.48
6


ATOM
3120
CD
PRO
A
416
14.540
32.029
6.895
1.00
21.91
6


ATOM
3121
C
PRO
A
416
12.376
31.793
4.084
1.00
22.77
6


ATOM
3122
O
PRO
A
416
11.300
31.563
3.547
1.00
22.99
8


ATOM
3123
N
GLY
A
417
13.402
32.367
3.451
1.00
23.02
7


ATOM
3124
CA
GLY
A
417
13.334
32.769
2.037
1.00
23.31
6


ATOM
3125
C
GLY
A
417
13.267
31.608
1.052
1.00
23.43
6


ATOM
3126
O
GLY
A
417
13.128
31.816
−0.161
1.00
23.99
8


ATOM
3127
N
THR
A
418
13.367
30.386
1.576
1.00
23.63
7


ATOM
3128
CA
THR
A
418
13.331
29.168
0.759
1.00
23.57
6


ATOM
3129
CB
THR
A
418
14.425
28.154
1.190
1.00
23.50
6


ATOM
3130
OG1
THR
A
418
14.070
27.560
2.443
1.00
23.59
8


ATOM
3131
CG2
THR
A
418
15.786
28.831
1.310
1.00
23.19
6


ATOM
3132
C
THR
A
418
11.966
28.475
0.824
1.00
23.55
6


ATOM
3133
O
THR
A
418
11.746
27.461
0.160
1.00
23.89
8


ATOM
3134
N
LEU
A
419
11.061
29.019
1.638
1.00
23.34
7


ATOM
3135
CA
LEU
A
419
9.722
28.450
1.799
1.00
22.71
6


ATOM
3136
CB
LEU
A
419
9.135
28.813
3.166
1.00
22.30
6


ATOM
3137
CG
LEU
A
419
9.888
28.432
4.447
1.00
21.68
6


ATOM
3138
CD1
LEU
A
419
9.022
28.766
5.653
1.00
21.75
6


ATOM
3139
CD2
LEU
A
419
10.271
26.955
4.450
1.00
19.91
6


ATOM
3140
C
LEU
A
419
8.773
28.922
0.708
1.00
22.56
6


ATOM
3141
O
LEU
A
419
8.732
30.112
0.382
1.00
22.76
8


ATOM
3142
N
ASP
A
420
8.001
27.991
0.154
1.00
22.56
7


ATOM
3143
CA
ASP
A
420
6.935
28.350
−0.783
1.00
22.05
6


ATOM
3144
CB
ASP
A
420
6.623
27.199
−1.758
1.00
22.46
6


ATOM
3145
CG
ASP
A
420
6.020
25.979
−1.072
1.00
22.60
6


ATOM
3146
OD1
ASP
A
420
5.596
26.075
0.103
1.00
23.08
8


ATOM
3147
OD2
ASP
A
420
5.965
24.918
−1.721
1.00
23.60
8


ATOM
3148
C
ASP
A
420
5.688
28.811
−0.019
1.00
21.92
6


ATOM
3149
O
ASP
A
420
5.678
28.805
1.215
1.00
21.76
8


ATOM
3150
N
TYR
A
421
4.648
29.214
−0.749
1.00
21.37
7


ATOM
3151
CA
TYR
A
421
3.454
29.789
−0.127
1.00
21.07
6


ATOM
3152
CB
TYR
A
421
2.402
30.151
−1.179
1.00
20.95
6


ATOM
3153
CG
TYR
A
421
1.164
30.799
−0.597
1.00
21.02
6


ATOM
3154
CD1
TYR
A
421
1.121
32.172
−0.362
1.00
21.22
6


ATOM
3155
CE1
TYR
A
421
−0.013
32.774
0.172
1.00
21.77
6


ATOM
3156
CZ
TYR
A
421
−1.120
32.001
0.484
1.00
21.08
6


ATOM
3157
OH
TYR
A
421
−2.238
32.601
1.016
1.00
21.11
8


ATOM
3158
CE2
TYR
A
421
−1.104
30.633
0.262
1.00
20.96
6


ATOM
3159
CD2
TYR
A
421
0.034
30.039
−0.281
1.00
20.97
6


ATOM
3160
C
TYR
A
421
2.842
28.882
0.942
1.00
21.18
6


ATOM
3161
O
TYR
A
421
2.588
29.324
2.066
1.00
20.82
8


ATOM
3162
N
ALA
A
422
2.608
27.620
0.583
1.00
21.26
7


ATOM
3163
CA
ALA
A
422
2.016
26.649
1.499
1.00
21.65
6


ATOM
3164
CB
ALA
A
422
1.841
25.303
0.814
1.00
21.74
6


ATOM
3165
C
ALA
A
422
2.853
26.502
2.767
1.00
22.07
6


ATOM
3166
O
ALA
A
422
2.311
26.408
3.865
1.00
22.27
8


ATOM
3167
N
GLU
A
423
4.176
26.497
2.606
1.00
22.51
7


ATOM
3168
CA
GLU
A
423
5.094
26.386
3.741
1.00
23.04
6


ATOM
3169
CB
GLU
A
423
6.519
26.106
3.258
1.00
23.15
6


ATOM
3170
CG
GLU
A
423
6.761
24.658
2.867
1.00
23.80
6


ATOM
3171
CD
GLU
A
423
8.049
24.455
2.086
1.00
24.72
6


ATOM
3172
OE1
GLU
A
423
8.510
25.404
1.418
1.00
26.01
8


ATOM
3173
OE2
GLU
A
423
8.598
23.334
2.133
1.00
25.39
8


ATOM
3174
C
GLU
A
423
5.056
27.626
4.638
1.00
23.24
6


ATOM
3175
O
GLU
A
423
5.173
27.517
5.859
1.00
23.72
8


ATOM
3176
N
GLN
A
424
4.882
28.796
4.026
1.00
23.33
7


ATOM
3177
CA
GLN
A
424
4.737
30.051
4.773
1.00
23.64
6


ATOM
3178
CB
GLN
A
424
4.725
31.247
3.819
1.00
23.81
6


ATOM
3179
CG
GLN
A
424
6.064
31.540
3.152
1.00
24.01
6


ATOM
3180
CD
GLN
A
424
5.937
32.505
1.979
1.00
24.45
6


ATOM
3181
OE1
GLN
A
424
4.842
32.949
1.636
1.00
25.87
8


ATOM
3182
NE2
GLN
A
424
7.065
32.834
1.363
1.00
25.39
7


ATOM
3183
C
GLN
A
424
3.466
30.052
5.625
1.00
23.40
6


ATOM
3184
O
GLN
A
424
3.464
30.548
6.748
1.00
23.59
8


ATOM
3185
N
GLN
A
425
2.388
29.501
5.071
1.00
23.22
7


ATOM
3186
CA
GLN
A
425
1.113
29.407
5.779
1.00
23.02
6


ATOM
3187
CB
GLN
A
425
−0.008
29.014
4.811
1.00
23.05
6


ATOM
3188
CG
GLN
A
425
−0.342
30.106
3.805
1.00
23.06
6


ATOM
3189
CD
GLN
A
425
−0.763
31.408
4.476
1.00
23.69
6


ATOM
3190
OE1
GLN
A
425
−0.058
32.417
4.399
1.00
24.45
8


ATOM
3191
NE2
GLN
A
425
−1.903
31.382
5.156
1.00
24.12
7


ATOM
3192
C
GLN
A
425
1.185
28.434
6.955
1.00
22.88
6


ATOM
3193
O
GLN
A
425
0.577
28.671
8.005
1.00
23.24
8


ATOM
3194
N
ARG
A
426
1.949
27.358
6.779
1.00
22.56
7


ATOM
3195
CA
ARG
A
426
2.153
26.371
7.830
1.00
22.54
6


ATOM
3196
CB
ARG
A
426
2.895
25.142
7.290
1.00
22.35
6


ATOM
3197
CG
ARG
A
426
3.003
24.000
8.294
1.00
22.51
6


ATOM
3198
CD
ARG
A
426
3.884
22.869
7.796
1.00
22.62
6


ATOM
3199
NE
ARG
A
426
4.286
21.983
8.891
1.00
21.79
7


ATOM
3200
CZ
ARG
A
426
4.929
20.829
8.730
1.00
22.00
6


ATOM
3201
NH1
ARG
A
426
5.258
20.407
7.511
1.00
20.70
7


ATOM
3202
NH2
ARG
A
426
5.245
20.095
9.791
1.00
20.99
7


ATOM
3203
C
ARG
A
426
2.923
26.999
8.993
1.00
22.53
6


ATOM
3204
O
ARG
A
426
2.602
26.758
10.160
1.00
22.93
8


ATOM
3205
N
TRP
A
427
3.918
27.821
8.663
1.00
22.67
7


ATOM
3206
CA
TRP
A
427
4.717
28.532
9.671
1.00
22.89
6


ATOM
3207
CB
TRP
A
427
5.958
29.159
9.026
1.00
23.11
6


ATOM
3208
CG
TRP
A
427
6.907
29.791
10.005
1.00
23.53
6


ATOM
3209
CD1
TRP
A
427
7.222
31.114
10.102
1.00
23.91
6


ATOM
3210
NE1
TRP
A
427
8.119
31.316
11.118
1.00
23.46
7


ATOM
3211
CE2
TRP
A
427
8.403
30.111
11.707
1.00
24.42
6


ATOM
3212
CD2
TRP
A
427
7.654
29.125
11.031
1.00
24.10
6


ATOM
3213
CE3
TRP
A
427
7.761
27.789
11.445
1.00
24.38
6


ATOM
3214
CZ3
TRP
A
427
8.613
27.486
12.503
1.00
23.53
6


ATOM
3215
CH2
TRP
A
427
9.341
28.495
13.160
1.00
23.89
6


ATOM
3216
CZ2
TRP
A
427
9.255
29.808
12.770
1.00
24.49
6


ATOM
3217
C
TRP
A
427
3.900
29.596
10.406
1.00
23.13
6


ATOM
3218
O
TRP
A
427
4.038
29.765
11.625
1.00
23.22
8


ATOM
3219
N
LEU
A
428
3.052
30.312
9.668
1.00
23.41
7


ATOM
3220
CA
LEU
A
428
2.164
31.304
10.278
1.00
23.78
6


ATOM
3221
CB
LEU
A
428
1.357
32.068
9.217
1.00
23.93
6


ATOM
3222
CG
LEU
A
428
2.116
33.127
8.403
1.00
25.03
6


ATOM
3223
CD1
LEU
A
428
1.188
33.838
7.424
1.00
25.26
6


ATOM
3224
CD2
LEU
A
428
2.819
34.138
9.306
1.00
25.54
6


ATOM
3225
C
LEU
A
428
1.242
30.663
11.312
1.00
23.87
6


ATOM
3226
O
LEU
A
428
1.048
31.215
12.395
1.00
23.81
8


ATOM
3227
N
GLU
A
429
0.704
29.486
10.981
1.00
23.88
7


ATOM
3228
CA
GLU
A
429
−0.114
28.714
11.919
1.00
23.99
6


ATOM
3229
CB
GLU
A
429
−0.745
27.504
11.231
1.00
24.08
6


ATOM
3230
CG
GLU
A
429
−1.851
26.828
12.052
1.00
25.69
6


ATOM
3231
CD
GLU
A
429
−2.977
27.792
12.447
1.00
28.08
6


ATOM
3232
OE1
GLU
A
429
−3.300
28.707
11.653
1.00
29.53
8


ATOM
3233
OE2
GLU
A
429
−3.539
27.630
13.553
1.00
29.02
8


ATOM
3234
C
GLU
A
429
0.693
28.267
13.141
1.00
23.68
6


ATOM
3235
O
GLU
A
429
0.221
28.367
14.276
1.00
23.61
8


ATOM
3236
N
HIS
A
430
1.905
27.777
12.894
1.00
23.62
7


ATOM
3237
CA
HIS
A
430
2.829
27.400
13.958
1.00
23.67
6


ATOM
3238
CB
HIS
A
430
4.187
27.003
13.366
1.00
23.58
6


ATOM
3239
CG
HIS
A
430
5.289
26.917
14.377
1.00
23.49
6


ATOM
3240
ND1
HIS
A
430
5.461
25.824
15.199
1.00
23.55
7


ATOM
3241
CE1
HIS
A
430
6.508
26.025
15.980
1.00
23.00
6


ATOM
3242
NE2
HIS
A
430
7.019
27.208
15.696
1.00
22.62
7


ATOM
3243
CD2
HIS
A
430
6.277
27.786
14.696
1.00
23.79
6


ATOM
3244
C
HIS
A
430
2.999
28.529
14.975
1.00
23.90
6


ATOM
3245
O
HIS
A
430
2.923
28.299
16.188
1.00
24.00
8


ATOM
3246
N
ARG
A
431
3.228
29.744
14.479
1.00
24.05
7


ATOM
3247
CA
ARG
A
431
3.474
30.896
15.351
1.00
24.65
6


ATOM
3248
CB
ARG
A
431
4.016
32.080
14.552
1.00
24.67
6


ATOM
3249
CG
ARG
A
431
5.363
31.811
13.895
1.00
25.11
6


ATOM
3250
CD
ARG
A
431
5.835
32.995
13.068
1.00
25.85
6


ATOM
3251
NE
ARG
A
431
6.238
34.130
13.895
1.00
25.71
7


ATOM
3252
CZ
ARG
A
431
5.668
35.332
13.850
1.00
27.06
6


ATOM
3253
NH1
ARG
A
431
4.674
35.568
13.001
1.00
27.51
7


ATOM
3254
NH2
ARG
A
431
6.103
36.305
14.640
1.00
26.77
7


ATOM
3255
C
ARG
A
431
2.230
31.309
16.136
1.00
24.89
6


ATOM
3256
O
ARG
A
431
2.334
31.778
17.275
1.00
24.94
8


ATOM
3257
N
ARG
A
432
1.060
31.131
15.525
1.00
25.45
7


ATOM
3258
CA
ARG
A
432
−0.215
31.423
16.191
1.00
25.97
6


ATOM
3259
CB
ARG
A
432
−1.370
31.410
15.187
1.00
26.24
6


ATOM
3260
CG
ARG
A
432
−1.419
32.632
14.289
1.00
27.84
6


ATOM
3261
CD
ARG
A
432
−2.578
32.558
13.308
1.00
30.85
6


ATOM
3262
NE
ARG
A
432
−2.375
33.459
12.175
1.00
32.77
7


ATOM
3263
CZ
ARG
A
432
−3.129
33.478
11.077
1.00
33.96
6


ATOM
3264
NH1
ARG
A
432
−4.158
32.648
10.949
1.00
34.46
7


ATOM
3265
NH2
ARG
A
432
−2.854
34.335
10.103
1.00
34.72
7


ATOM
3266
C
ARG
A
432
−0.507
30.456
17.336
1.00
25.97
6


ATOM
3267
O
ARG
A
432
−1.142
30.830
18.324
1.00
25.98
8


ATOM
3268
N
GLN
A
433
−0.044
29.216
17.200
1.00
25.92
7


ATOM
3269
CA
GLN
A
433
−0.272
28.195
18.222
1.00
26.14
6


ATOM
3270
CB
GLN
A
433
−0.145
26.793
17.627
1.00
26.15
6


ATOM
3271
CG
GLN
A
433
−1.275
26.422
16.676
1.00
27.27
6


ATOM
3272
CD
GLN
A
433
−1.112
25.035
16.081
1.00
28.02
6


ATOM
3273
OE1
GLN
A
433
−0.274
24.244
16.528
1.00
30.66
8


ATOM
3274
NE2
GLN
A
433
−1.914
24.730
15.066
1.00
29.12
7


ATOM
3275
C
GLN
A
433
0.673
28.359
19.408
1.00
25.65
6


ATOM
3276
O
GLN
A
433
0.375
27.903
20.513
1.00
25.91
8


ATOM
3277
N
VAL
A
434
1.816
29.002
19.169
1.00
25.30
7


ATOM
3278
CA
VAL
A
434
2.733
29.370
20.249
1.00
24.78
6


ATOM
3279
CB
VAL
A
434
4.155
29.668
19.719
1.00
24.94
6


ATOM
3280
CG1
VAL
A
434
5.073
30.116
20.858
1.00
24.75
6


ATOM
3281
CG2
VAL
A
434
4.730
28.448
19.007
1.00
25.19
6


ATOM
3282
C
VAL
A
434
2.209
30.605
20.971
1.00
24.51
6


ATOM
3283
O
VAL
A
434
2.075
30.614
22.200
1.00
24.62
8


ATOM
3284
N
PHE
A
435
1.911
31.644
20.200
1.00
24.08
7


ATOM
3285
CA
PHE
A
435
1.487
32.918
20.751
1.00
24.09
6


ATOM
3286
CB
PHE
A
435
1.928
34.070
19.834
1.00
23.80
6


ATOM
3287
CG
PHE
A
435
3.424
34.098
19.564
1.00
24.00
6


ATOM
3288
CD1
PHE
A
435
4.343
33.950
20.610
1.00
23.54
6


ATOM
3289
CE1
PHE
A
435
5.721
33.978
20.363
1.00
22.80
6


ATOM
3290
CZ
PHE
A
435
6.189
34.160
19.061
1.00
23.69
6


ATOM
3291
CE2
PHE
A
435
5.284
34.315
18.017
1.00
23.32
6


ATOM
3292
CD2
PHE
A
435
3.909
34.286
18.273
1.00
23.76
6


ATOM
3293
C
PHE
A
435
−0.026
32.933
21.023
1.00
24.14
6


ATOM
3294
O
PHE
A
435
−0.774
33.721
20.441
1.00
24.23
8


ATOM
3295
N
THR
A
436
−0.452
32.042
21.917
1.00
24.33
7


ATOM
3296
CA
THR
A
436
−1.854
31.937
22.342
1.00
24.39
6


ATOM
3297
CB
THR
A
436
−2.076
30.703
23.258
1.00
24.49
6


ATOM
3298
OG1
THR
A
436
−1.265
30.820
24.437
1.00
25.08
8


ATOM
3299
CG2
THR
A
436
−1.736
29.417
22.531
1.00
24.96
6


ATOM
3300
C
THR
A
436
−2.295
33.184
23.109
1.00
24.29
6


ATOM
3301
O
THR
A
436
−1.452
33.977
23.537
1.00
24.55
8


ATOM
3302
N
PRO
A
437
−3.624
33.362
23.287
1.00
24.19
7


ATOM
3303
CA
PRO
A
437
−4.166
34.436
24.131
1.00
24.01
6


ATOM
3304
CB
PRO
A
437
−5.668
34.135
24.150
1.00
24.02
6


ATOM
3305
CG
PRO
A
437
−5.915
33.385
22.890
1.00
23.90
6


ATOM
3306
CD
PRO
A
437
−4.698
32.557
22.671
1.00
24.00
6


ATOM
3307
C
PRO
A
437
−3.607
34.413
25.558
1.00
23.91
6


ATOM
3308
O
PRO
A
437
−3.292
35.469
26.112
1.00
23.67
8


ATOM
3309
N
GLU
A
438
−3.483
33.215
26.138
1.00
23.83
7


ATOM
3310
CA
GLU
A
438
−2.983
33.055
27.507
1.00
23.91
6


ATOM
3311
CB
GLU
A
438
−3.169
31.610
27.989
1.00
24.06
6


ATOM
3312
CG
GLU
A
438
−3.118
31.433
29.509
1.00
23.80
6


ATOM
3313
CD
GLU
A
438
−4.375
31.932
30.208
1.00
23.67
6


ATOM
3314
OE1
GLU
A
438
−5.493
31.658
29.715
1.00
22.83
8


ATOM
3315
OE2
GLU
A
438
−4.243
32.595
31.261
1.00
24.20
8


ATOM
3316
C
GLU
A
438
−1.516
33.459
27.605
1.00
23.96
6


ATOM
3317
O
GLU
A
438
−1.119
34.168
28.535
1.00
23.84
8


ATOM
3318
N
PHE
A
439
−0.725
33.019
26.626
1.00
23.86
7


ATOM
3319
CA
PHE
A
439
0.700
33.338
26.562
1.00
23.64
6


ATOM
3320
CB
PHE
A
439
1.351
32.632
25.369
1.00
23.93
6


ATOM
3321
CG
PHE
A
439
2.821
32.891
25.248
1.00
24.27
6


ATOM
3322
CD1
PHE
A
439
3.729
32.162
26.005
1.00
25.20
6


ATOM
3323
CE1
PHE
A
439
5.094
32.405
25.909
1.00
26.17
6


ATOM
3324
CZ
PHE
A
439
5.560
33.390
25.050
1.00
25.59
6


ATOM
3325
CE2
PHE
A
439
4.663
34.133
24.295
1.00
25.83
6


ATOM
3326
CD2
PHE
A
439
3.298
33.884
24.396
1.00
25.12
6


ATOM
3327
C
PHE
A
439
0.966
34.843
26.483
1.00
23.38
6


ATOM
3328
O
PHE
A
439
1.742
35.382
27.273
1.00
23.11
8


ATOM
3329
N
LEU
A
440
0.332
35.507
25.521
1.00
23.00
7


ATOM
3330
CA
LEU
A
440
0.542
36.937
25.291
1.00
23.12
6


ATOM
3331
CB
LEU
A
440
−0.229
37.408
24.051
1.00
23.50
6


ATOM
3332
CG
LEU
A
440
0.087
36.722
22.716
1.00
24.05
6


ATOM
3333
CD1
LEU
A
440
−0.761
37.307
21.594
1.00
25.69
6


ATOM
3334
CD2
LEU
A
440
1.564
36.829
22.388
1.00
25.16
6


ATOM
3335
C
LEU
A
440
0.151
37.778
26.504
1.00
22.94
6


ATOM
3336
O
LEU
A
440
0.883
38.687
26.905
1.00
22.98
8


ATOM
3337
N
GLN
A
441
−1.000
37.467
27.092
1.00
22.46
7


ATOM
3338
CA
GLN
A
441
−1.467
38.202
28.256
1.00
22.12
6


ATOM
3339
CB
GLN
A
441
−2.877
37.763
28.659
1.00
22.48
6


ATOM
3340
CG
GLN
A
441
−3.569
38.745
29.592
1.00
22.58
6


ATOM
3341
CD
GLN
A
441
−3.574
40.165
29.040
1.00
23.12
6


ATOM
3342
OE1
GLN
A
441
−4.206
40.444
28.020
1.00
24.29
8


ATOM
3343
NE2
GLN
A
441
−2.863
41.065
29.710
1.00
23.68
7


ATOM
3344
C
GLN
A
441
−0.497
38.019
29.414
1.00
21.78
6


ATOM
3345
O
GLN
A
441
−0.095
38.991
30.054
1.00
22.11
8


ATOM
3346
N
GLY
A
442
−0.103
36.772
29.655
1.00
21.20
7


ATOM
3347
CA
GLY
A
442
0.842
36.448
30.719
1.00
20.66
6


ATOM
3348
C
GLY
A
442
2.172
37.161
30.546
1.00
20.25
6


ATOM
3349
O
GLY
A
442
2.773
37.619
31.520
1.00
20.34
8


ATOM
3350
N
TYR
A
443
2.628
37.262
29.301
1.00
19.78
7


ATOM
3351
CA
TYR
A
443
3.902
37.914
29.004
1.00
19.42
6


ATOM
3352
CB
TYR
A
443
4.300
37.673
27.550
1.00
19.04
6


ATOM
3353
CG
TYR
A
443
5.784
37.827
27.293
1.00
18.78
6


ATOM
3354
CD1
TYR
A
443
6.646
36.746
27.437
1.00
18.27
6


ATOM
3355
CE1
TYR
A
443
8.011
36.879
27.205
1.00
18.70
6


ATOM
3356
CZ
TYR
A
443
8.521
38.103
26.817
1.00
18.74
6


ATOM
3357
OH
TYR
A
443
9.870
38.232
26.585
1.00
18.29
8


ATOM
3358
CE2
TYR
A
443
7.681
39.201
26.669
1.00
18.28
6


ATOM
3359
CD2
TYR
A
443
6.323
39.057
26.909
1.00
18.09
6


ATOM
3360
C
TYR
A
443
3.825
39.414
29.283
1.00
19.44
6


ATOM
3361
O
TYR
A
443
4.714
39.983
29.918
1.00
19.42
8


ATOM
3362
N
ALA
A
444
2.758
40.047
28.795
1.00
19.73
7


ATOM
3363
CA
ALA
A
444
2.507
41.459
29.064
1.00
20.07
6


ATOM
3364
CB
ALA
A
444
1.228
41.906
28.374
1.00
20.31
6


ATOM
3365
C
ALA
A
444
2.431
41.722
30.571
1.00
20.42
6


ATOM
3366
O
ALA
A
444
3.015
42.687
31.072
1.00
20.26
8


ATOM
3367
N
ASP
A
445
1.731
40.841
31.288
1.00
20.66
7


ATOM
3368
CA
ASP
A
445
1.575
40.962
32.744
1.00
21.16
6


ATOM
3369
CB
ASP
A
445
0.588
39.920
33.274
1.00
21.25
6


ATOM
3370
CG
ASP
A
445
−0.843
40.198
32.854
1.00
22.08
6


ATOM
3371
OD1
ASP
A
445
−1.124
41.306
32.333
1.00
23.14
8


ATOM
3372
OD2
ASP
A
445
−1.695
39.304
33.053
1.00
23.52
8


ATOM
3373
C
ASP
A
445
2.901
40.846
33.494
1.00
21.07
6


ATOM
3374
O
ASP
A
445
3.149
41.603
34.436
1.00
21.11
8


ATOM
3375
N
GLU
A
446
3.746
39.898
33.077
1.00
21.09
7


ATOM
3376
CA
GLU
A
446
5.042
39.683
33.731
1.00
21.14
6


ATOM
3377
CB
GLU
A
446
5.730
38.406
33.219
1.00
20.98
6


ATOM
3378
CG
GLU
A
446
6.973
38.013
34.044
1.00
21.95
6


ATOM
3379
CD
GLU
A
446
7.739
36.816
33.490
1.00
22.88
6


ATOM
3380
OE1
GLU
A
446
7.189
36.067
32.648
1.00
25.21
8


ATOM
3381
OE2
GLU
A
446
8.905
36.626
33.909
1.00
24.54
8


ATOM
3382
C
GLU
A
446
5.962
40.889
33.549
1.00
20.73
6


ATOM
3383
O
GLU
A
446
6.628
41.317
34.492
1.00
20.06
8


ATOM
3384
N
LEU
A
447
5.993
41.430
32.334
1.00
20.30
7


ATOM
3385
CA
LEU
A
447
6.818
42.599
32.036
1.00
20.56
6


ATOM
3386
CB
LEU
A
447
6.743
42.943
30.551
1.00
20.01
6


ATOM
3387
CG
LEU
A
447
7.458
42.024
29.560
1.00
19.89
6


ATOM
3388
CD1
LEU
A
447
7.258
42.554
28.158
1.00
19.01
6


ATOM
3389
CD2
LEU
A
447
8.948
41.907
29.879
1.00
19.15
6


ATOM
3390
C
LEU
A
447
6.394
43.807
32.866
1.00
20.96
6


ATOM
3391
O
LEU
A
447
7.237
44.503
33.446
1.00
21.08
8


ATOM
3392
N
GLN
A
448
5.082
44.041
32.929
1.00
21.54
7


ATOM
3393
CA
GLN
A
448
4.522
45.144
33.715
1.00
22.06
6


ATOM
3394
CB
GLN
A
448
3.022
45.308
33.429
1.00
22.25
6


ATOM
3395
CG
GLN
A
448
2.700
45.943
32.066
1.00
22.77
6


ATOM
3396
CD
GLN
A
448
1.223
45.818
31.684
1.00
23.39
6


ATOM
3397
OE1
GLN
A
448
0.771
44.764
31.221
1.00
24.95
8


ATOM
3398
NE2
GLN
A
448
0.471
46.901
31.865
1.00
23.35
7


ATOM
3399
C
GLN
A
448
4.770
44.944
35.212
1.00
22.26
6


ATOM
3400
O
GLN
A
448
5.030
45.901
35.941
1.00
21.92
8


ATOM
3401
N
MET
A
449
4.702
43.694
35.658
1.00
22.38
7


ATOM
3402
CA
MET
A
449
5.014
43.362
37.042
1.00
23.27
6


ATOM
3403
CB
MET
A
449
4.647
41.915
37.339
1.00
23.26
6


ATOM
3404
CG
MET
A
449
4.629
41.583
38.812
1.00
24.06
6


ATOM
3405
SD
MET
A
449
5.150
39.896
39.132
1.00
27.08
16


ATOM
3406
CE
MET
A
449
6.874
40.005
38.673
1.00
27.87
6


ATOM
3407
C
MET
A
449
6.492
43.604
37.354
1.00
22.38
6


ATOM
3408
O
MET
A
449
6.825
44.222
38.367
1.00
22.47
8


ATOM
3409
N
LEU
A
450
7.368
43.135
36.465
1.00
21.90
7


ATOM
3410
CA
LEU
A
450
8.810
43.242
36.677
1.00
21.35
6


ATOM
3411
CB
LEU
A
450
9.590
42.378
35.672
1.00
20.75
6


ATOM
3412
CG
LEU
A
450
9.503
40.847
35.842
1.00
19.52
6


ATOM
3413
CD1
LEU
A
450
10.124
40.136
34.662
1.00
17.72
6


ATOM
3414
CD2
LEU
A
450
10.146
40.363
37.157
1.00
16.51
6


ATOM
3415
C
LEU
A
450
9.299
44.689
36.644
1.00
21.44
6


ATOM
3416
O
LEU
A
450
10.203
45.055
37.395
1.00
21.74
8


ATOM
3417
N
VAL
A
451
8.685
45.516
35.797
1.00
21.64
7


ATOM
3418
CA
VAL
A
451
9.071
46.930
35.704
1.00
21.97
6


ATOM
3419
CB
VAL
A
451
8.458
47.626
34.445
1.00
22.18
6


ATOM
3420
CG1
VAL
A
451
7.007
48.035
34.687
1.00
22.69
6


ATOM
3421
CG2
VAL
A
451
9.299
48.823
34.030
1.00
22.54
6


ATOM
3422
C
VAL
A
451
8.750
47.702
36.999
1.00
22.09
6


ATOM
3423
O
VAL
A
451
9.425
48.677
37.337
1.00
22.08
8


ATOM
3424
N
GLN
A
452
7.725
47.246
37.716
1.00
22.24
7


ATOM
3425
CA
GLN
A
452
7.392
47.772
39.039
1.00
22.88
6


ATOM
3426
CB
GLN
A
452
5.929
47.478
39.382
1.00
22.95
6


ATOM
3427
CG
GLN
A
452
4.921
48.254
38.554
1.00
23.68
6


ATOM
3428
CD
GLN
A
452
3.485
47.946
38.935
1.00
23.99
6


ATOM
3429
OE1
GLN
A
452
3.173
47.727
40.105
1.00
25.35
8


ATOM
3430
NE2
GLN
A
452
2.598
47.943
37.944
1.00
25.72
7


ATOM
3431
C
GLN
A
452
8.299
47.162
40.105
1.00
22.83
6


ATOM
3432
O
GLN
A
452
8.748
47.856
41.021
1.00
22.95
8


ATOM
3433
N
GLN
A
453
8.561
45.860
39.981
1.00
22.86
7


ATOM
3434
CA
GLN
A
453
9.429
45.147
40.919
1.00
23.22
6


ATOM
3435
CB
GLN
A
453
9.505
43.660
40.559
1.00
23.09
6


ATOM
3436
CG
GLN
A
453
10.409
42.841
41.473
1.00
23.75
6


ATOM
3437
CD
GLN
A
453
10.227
41.346
41.299
1.00
24.12
6


ATOM
3438
OE1
GLN
A
453
9.308
40.891
40.613
1.00
26.13
8


ATOM
3439
NE2
GLN
A
453
11.108
40.570
41.920
1.00
25.32
7


ATOM
3440
C
GLN
A
453
10.830
45.753
40.954
1.00
23.23
6


ATOM
3441
O
GLN
A
453
11.395
45.975
42.036
1.00
22.72
8


ATOM
3442
N
TYR
A
454
11.374
46.027
39.769
1.00
23.30
7


ATOM
3443
CA
TYR
A
454
12.735
46.545
39.631
1.00
23.90
6


ATOM
3444
CB
TYR
A
454
13.531
45.686
38.648
1.00
24.07
6


ATOM
3445
CG
TYR
A
454
13.745
44.278
39.142
1.00
24.27
6


ATOM
3446
CD1
TYR
A
454
14.619
44.017
40.198
1.00
24.54
6


ATOM
3447
CE1
TYR
A
454
14.814
42.730
40.664
1.00
24.49
6


ATOM
3448
CZ
TYR
A
454
14.129
41.684
40.078
1.00
24.69
6


ATOM
3449
OH
TYR
A
454
14.323
40.406
40.540
1.00
25.29
8


ATOM
3450
CE2
TYR
A
454
13.251
41.915
39.031
1.00
24.39
6


ATOM
3451
CD2
TYR
A
454
13.061
43.208
38.574
1.00
24.13
6


ATOM
3452
C
TYR
A
454
12.757
48.012
39.217
1.00
24.19
6


ATOM
3453
O
TYR
A
454
13.678
48.463
38.520
1.00
24.02
8


ATOM
3454
N
ALA
A
455
11.749
48.754
39.676
1.00
24.70
7


ATOM
3455
CA
ALA
A
455
11.597
50.178
39.366
1.00
25.24
6


ATOM
3456
CB
ALA
A
455
10.389
50.753
40.107
1.00
24.90
6


ATOM
3457
C
ALA
A
455
12.850
50.992
39.687
1.00
25.55
6


ATOM
3458
O
ALA
A
455
13.196
51.922
38.957
1.00
26.17
8


ATOM
3459
N
ASP
A
456
13.525
50.636
40.777
1.00
26.19
7


ATOM
3460
CA
ASP
A
456
14.702
51.376
41.227
1.00
26.41
6


ATOM
3461
CB
ASP
A
456
14.826
51.315
42.754
1.00
26.75
6


ATOM
3462
CG
ASP
A
456
13.680
52.025
43.458
1.00
27.82
6


ATOM
3463
OD1
ASP
A
456
13.581
53.269
43.341
1.00
28.98
8


ATOM
3464
OD2
ASP
A
456
12.876
51.339
44.130
1.00
29.60
8


ATOM
3465
C
ASP
A
456
16.001
50.929
40.544
1.00
26.25
6


ATOM
3466
O
ASP
A
456
17.055
51.545
40.733
1.00
26.14
8


ATOM
3467
N
ASP
A
457
15.917
49.871
39.740
1.00
25.98
7


ATOM
3468
CA
ASP
A
457
17.060
49.404
38.965
1.00
25.84
6


ATOM
3469
CB
ASP
A
457
17.166
47.876
39.027
1.00
26.05
6


ATOM
3470
CG
ASP
A
457
18.527
47.357
38.573
1.00
27.14
6


ATOM
3471
OD1
ASP
A
457
19.009
47.759
37.485
1.00
26.99
8


ATOM
3472
OD2
ASP
A
457
19.109
46.521
39.300
1.00
28.05
8


ATOM
3473
C
ASP
A
457
16.926
49.881
37.518
1.00
25.36
6


ATOM
3474
O
ASP
A
457
16.162
49.319
36.735
1.00
25.31
8


ATOM
3475
N
LYS
A
458
17.674
50.927
37.177
1.00
24.98
7


ATOM
3476
CA
LYS
A
458
17.531
51.600
35.881
1.00
24.54
6


ATOM
3477
CB
LYS
A
458
18.289
52.932
35.881
1.00
24.70
6


ATOM
3478
CG
LYS
A
458
17.809
53.912
36.944
1.00
25.23
6


ATOM
3479
CD
LYS
A
458
16.310
54.183
36.810
1.00
26.62
6


ATOM
3480
CE
LYS
A
458
15.741
54.837
38.067
1.00
27.52
6


ATOM
3481
NZ
LYS
A
458
15.771
53.929
39.240
1.00
29.10
7


ATOM
3482
C
LYS
A
458
17.953
50.740
34.689
1.00
24.45
6


ATOM
3483
O
LYS
A
458
17.380
50.857
33.603
1.00
23.97
8


ATOM
3484
N
GLU
A
459
18.944
49.875
34.899
1.00
24.33
7


ATOM
3485
CA
GLU
A
459
19.410
48.960
33.851
1.00
24.57
6


ATOM
3486
CB
GLU
A
459
20.708
48.271
34.273
1.00
24.62
6


ATOM
3487
CG
GLU
A
459
21.930
49.172
34.239
1.00
26.21
6


ATOM
3488
CD
GLU
A
459
23.172
48.502
34.802
1.00
27.01
6


ATOM
3489
OE1
GLU
A
459
23.326
47.269
34.629
1.00
29.74
8


ATOM
3490
OE2
GLU
A
459
23.998
49.214
35.416
1.00
29.82
8


ATOM
3491
C
GLU
A
459
18.358
47.913
33.492
1.00
23.75
6


ATOM
3492
O
GLU
A
459
18.090
47.672
32.315
1.00
23.90
8


ATOM
3493
N
LYS
A
460
17.775
47.289
34.515
1.00
23.14
7


ATOM
3494
CA
LYS
A
460
16.705
46.308
34.320
1.00
22.28
6


ATOM
3495
CB
LYS
A
460
16.317
45.652
35.656
1.00
22.25
6


ATOM
3496
CG
LYS
A
460
17.458
44.923
36.364
1.00
22.79
6


ATOM
3497
CD
LYS
A
460
16.929
44.006
37.465
1.00
23.87
6


ATOM
3498
CE
LYS
A
460
18.037
43.542
38.403
1.00
25.80
6


ATOM
3499
NZ
LYS
A
460
18.924
42.520
37.785
1.00
26.75
7


ATOM
3500
C
LYS
A
460
15.474
46.948
33.660
1.00
21.70
6


ATOM
3501
O
LYS
A
460
14.875
46.364
32.750
1.00
20.70
8


ATOM
3502
N
VAL
A
461
15.108
48.149
34.113
1.00
20.71
7


ATOM
3503
CA
VAL
A
461
13.976
48.879
33.518
1.00
20.36
6


ATOM
3504
CB
VAL
A
461
13.731
50.253
34.207
1.00
20.51
6


ATOM
3505
CG1
VAL
A
461
12.753
51.103
33.399
1.00
20.47
6


ATOM
3506
CG2
VAL
A
461
13.200
50.045
35.621
1.00
20.69
6


ATOM
3507
C
VAL
A
461
14.170
49.050
32.005
1.00
20.06
6


ATOM
3508
O
VAL
A
461
13.252
48.788
31.224
1.00
19.80
8


ATOM
3509
N
ALA
A
462
15.373
49.455
31.601
1.00
19.89
7


ATOM
3510
CA
ALA
A
462
15.692
49.622
30.175
1.00
19.77
6


ATOM
3511
CB
ALA
A
462
17.050
50.298
30.000
1.00
19.84
6


ATOM
3512
C
ALA
A
462
15.646
48.299
29.413
1.00
20.08
6


ATOM
3513
O
ALA
A
462
15.192
48.254
28.266
1.00
20.07
8


ATOM
3514
N
LEU
A
463
16.104
47.224
30.057
1.00
19.97
7


ATOM
3515
CA
LEU
A
463
16.035
45.887
29.469
1.00
20.08
6


ATOM
3516
CB
LEU
A
463
16.808
44.870
30.315
1.00
20.26
6


ATOM
3517
CG
LEU
A
463
18.344
44.897
30.255
1.00
20.34
6


ATOM
3518
CD1
LEU
A
463
18.921
43.995
31.322
1.00
19.89
6


ATOM
3519
CD2
LEU
A
463
18.871
44.505
28.875
1.00
20.59
6


ATOM
3520
C
LEU
A
463
14.584
45.432
29.293
1.00
19.87
6


ATOM
3521
O
LEU
A
463
14.236
44.839
28.281
1.00
20.39
8


ATOM
3522
N
LEU
A
464
13.742
45.748
30.271
1.00
19.79
7


ATOM
3523
CA
LEU
A
464
12.333
45.364
30.231
1.00
19.47
6


ATOM
3524
CB
LEU
A
464
11.681
45.549
31.605
1.00
19.53
6


ATOM
3525
CG
LEU
A
464
12.159
44.519
32.643
1.00
18.88
6


ATOM
3526
CD1
LEU
A
464
11.937
45.000
34.074
1.00
19.80
6


ATOM
3527
CD2
LEU
A
464
11.510
43.149
32.413
1.00
17.25
6


ATOM
3528
C
LEU
A
464
11.547
46.097
29.139
1.00
19.49
6


ATOM
3529
O
LEU
A
464
10.701
45.497
28.468
1.00
19.63
8


ATOM
3530
N
LYS
A
465
11.836
47.384
28.952
1.00
19.77
7


ATOM
3531
CA
LYS
A
465
11.227
48.150
27.857
1.00
20.15
6


ATOM
3532
CB
LYS
A
465
11.588
49.641
27.952
1.00
20.63
6


ATOM
3533
CG
LYS
A
465
11.212
50.318
29.285
1.00
22.22
6


ATOM
3534
CD
LYS
A
465
9.700
50.442
29.473
1.00
23.96
6


ATOM
3535
CE
LYS
A
465
9.346
51.051
30.830
1.00
23.54
6


ATOM
3536
NZ
LYS
A
465
9.485
52.540
30.838
1.00
25.59
7


ATOM
3537
C
LYS
A
465
11.649
47.573
26.500
1.00
20.03
6


ATOM
3538
O
LYS
A
465
10.858
47.550
25.548
1.00
19.79
8


ATOM
3539
N
ALA
A
466
12.892
47.092
26.433
1.00
20.19
7


ATOM
3540
CA
ALA
A
466
13.414
46.404
25.246
1.00
20.37
6


ATOM
3541
CB
ALA
A
466
14.896
46.098
25.425
1.00
20.51
6


ATOM
3542
C
ALA
A
466
12.634
45.114
24.952
1.00
20.34
6


ATOM
3543
O
ALA
A
466
12.311
44.816
23.792
1.00
20.41
8


ATOM
3544
N
LEU
A
467
12.331
44.361
26.007
1.00
20.46
7


ATOM
3545
CA
LEU
A
467
11.548
43.133
25.882
1.00
20.44
6


ATOM
3546
CB
LEU
A
467
11.554
42.345
27.189
1.00
20.75
6


ATOM
3547
CG
LEU
A
467
12.911
41.784
27.607
1.00
20.77
6


ATOM
3548
CD1
LEU
A
467
12.872
41.353
29.061
1.00
20.29
6


ATOM
3549
CD2
LEU
A
467
13.311
40.630
26.702
1.00
22.45
6


ATOM
3550
C
LEU
A
467
10.121
43.416
25.435
1.00
20.78
6


ATOM
3551
O
LEU
A
467
9.573
42.685
24.610
1.00
20.48
8


ATOM
3552
N
TRP
A
468
9.526
44.484
25.968
1.00
20.99
7


ATOM
3553
CA
TRP
A
468
8.208
44.918
25.508
1.00
21.63
6


ATOM
3554
CB
TRP
A
468
7.714
46.127
26.302
1.00
22.17
6


ATOM
3555
CG
TRP
A
468
6.287
46.499
25.973
1.00
22.71
6


ATOM
3556
CD1
TRP
A
468
5.849
47.222
24.890
1.00
23.71
6


ATOM
3557
NE1
TRP
A
468
4.481
47.343
24.923
1.00
23.94
7


ATOM
3558
CE2
TRP
A
468
4.003
46.701
26.038
1.00
23.95
6


ATOM
3559
CD2
TRP
A
468
5.114
46.151
26.722
1.00
23.90
6


ATOM
3560
CE3
TRP
A
468
4.892
45.431
27.907
1.00
23.41
6


ATOM
3561
CZ3
TRP
A
468
3.582
45.283
28.367
1.00
23.80
6


ATOM
3562
CH2
TRP
A
468
2.495
45.842
27.662
1.00
23.71
6


ATOM
3563
CZ2
TRP
A
468
2.685
46.552
26.501
1.00
23.80
6


ATOM
3564
C
TRP
A
468
8.217
45.246
24.013
1.00
21.67
6


ATOM
3565
O
TRP
A
468
7.337
44.807
23.270
1.00
21.85
8


ATOM
3566
N
GLN
A
469
9.210
46.023
23.585
1.00
21.78
7


ATOM
3567
CA
GLN
A
469
9.334
46.424
22.183
1.00
22.07
6


ATOM
3568
CB
GLN
A
469
10.508
47.388
22.001
1.00
22.69
6


ATOM
3569
CG
GLN
A
469
10.198
48.841
22.349
1.00
24.91
6


ATOM
3570
CD
GLN
A
469
11.391
49.564
22.970
1.00
27.79
6


ATOM
3571
OE1
GLN
A
469
12.547
49.188
22.755
1.00
28.89
8


ATOM
3572
NE2
GLN
A
469
11.110
50.603
23.755
1.00
28.75
7


ATOM
3573
C
GLN
A
469
9.499
45.223
21.253
1.00
21.80
6


ATOM
3574
O
GLN
A
469
8.918
45.188
20.172
1.00
21.45
8


ATOM
3575
N
TYR
A
470
10.286
44.235
21.685
1.00
21.34
7


ATOM
3576
CA
TYR
A
470
10.520
43.040
20.871
1.00
21.34
6


ATOM
3577
CB
TYR
A
470
11.647
42.194
21.454
1.00
20.73
6


ATOM
3578
CG
TYR
A
470
12.023
41.005
20.592
1.00
20.38
6


ATOM
3579
CD1
TYR
A
470
12.753
41.179
19.417
1.00
20.34
6


ATOM
3580
CE1
TYR
A
470
13.114
40.092
18.623
1.00
19.64
6


ATOM
3581
CZ
TYR
A
470
12.743
38.814
18.998
1.00
19.36
6


ATOM
3582
OH
TYR
A
470
13.108
37.746
18.207
1.00
19.18
8


ATOM
3583
CE2
TYR
A
470
12.017
38.606
20.169
1.00
20.34
6


ATOM
3584
CD2
TYR
A
470
11.664
39.705
20.961
1.00
19.79
6


ATOM
3585
C
TYR
A
470
9.255
42.202
20.719
1.00
21.88
6


ATOM
3586
O
TYR
A
470
8.938
41.733
19.621
1.00
21.16
8


ATOM
3587
N
ALA
A
471
8.537
42.023
21.825
1.00
22.90
7


ATOM
3588
CA
ALA
A
471
7.269
41.307
21.811
1.00
24.35
6


ATOM
3589
CB
ALA
A
471
6.738
41.119
23.232
1.00
24.27
6


ATOM
3590
C
ALA
A
471
6.245
42.034
20.944
1.00
25.46
6


ATOM
3591
O
ALA
A
471
5.509
41.400
20.194
1.00
25.50
8


ATOM
3592
N
ASP
A
472
6.215
43.365
21.036
1.00
26.95
7


ATOM
3593
CA
ASP
A
472
5.311
44.173
20.212
1.00
28.53
6


ATOM
3594
CB
ASP
A
472
5.456
45.668
20.527
1.00
28.64
6


ATOM
3595
CG
ASP
A
472
4.520
46.131
21.640
1.00
30.11
6


ATOM
3596
OD1
ASP
A
472
4.284
45.356
22.596
1.00
32.36
8


ATOM
3597
OD2
ASP
A
472
4.023
47.282
21.562
1.00
32.11
8


ATOM
3598
C
ASP
A
472
5.537
43.910
18.721
1.00
29.26
6


ATOM
3599
O
ASP
A
472
4.578
43.751
17.965
1.00
29.51
8


ATOM
3600
N
GLU
A
473
6.806
43.839
18.314
1.00
30.31
7


ATOM
3601
CA
GLU
A
473
7.164
43.542
16.923
1.00
31.47
6


ATOM
3602
CB
GLU
A
473
8.662
43.793
16.681
1.00
31.31
6


ATOM
3603
CG
GLU
A
473
9.119
43.550
15.228
1.00
31.98
6


ATOM
3604
CD
GLU
A
473
10.629
43.342
15.084
1.00
32.05
6


ATOM
3605
OE1
GLU
A
473
11.400
43.875
15.912
1.00
32.71
8


ATOM
3606
OE2
GLU
A
473
11.044
42.648
14.127
1.00
32.42
8


ATOM
3607
C
GLU
A
473
6.805
42.101
16.540
1.00
32.31
6


ATOM
3608
O
GLU
A
473
6.126
41.867
15.537
1.00
32.39
8


ATOM
3609
N
ILE
A
474
7.264
41.149
17.351
1.00
33.34
7


ATOM
3610
CA
ILE
A
474
7.190
39.725
17.016
1.00
34.42
6


ATOM
3611
CB
ILE
A
474
8.296
38.902
17.780
1.00
34.32
6


ATOM
3612
CG1
ILE
A
474
9.700
39.344
17.342
1.00
34.34
6


ATOM
3613
CD1
ILE
A
474
10.074
38.977
15.901
1.00
34.40
6


ATOM
3614
CG2
ILE
A
474
8.119
37.383
17.592
1.00
34.61
6


ATOM
3615
C
ILE
A
474
5.799
39.132
17.253
1.00
35.23
6


ATOM
3616
O
ILE
A
474
5.382
38.222
16.533
1.00
35.39
8


ATOM
3617
N
VAL
A
475
5.080
39.659
18.245
1.00
36.28
7


ATOM
3618
CA
VAL
A
475
3.804
39.061
18.675
1.00
37.41
6


ATOM
3619
CB
VAL
A
475
3.989
38.175
19.949
1.00
37.31
6


ATOM
3620
CG1
VAL
A
475
5.244
37.354
19.846
1.00
37.72
6


ATOM
3621
CG2
VAL
A
475
4.037
39.025
21.222
1.00
37.83
6


ATOM
3622
C
VAL
A
475
2.663
40.069
18.917
1.00
37.93
6


ATOM
3623
O
VAL
A
475
1.500
39.772
18.628
1.00
38.21
8


ATOM
3624
N
GLU
A
476
3.017
41.257
19.420
1.00
38.57
7


ATOM
3625
CA
GLU
A
476
2.078
42.200
20.072
1.00
39.02
6


ATOM
3626
CB
GLU
A
476
0.719
42.274
19.363
1.00
39.13
6


ATOM
3627
CG
GLU
A
476
−0.230
43.320
19.974
1.00
40.06
6


ATOM
3628
CD
GLU
A
476
−1.711
42.991
19.790
1.00
41.26
6


ATOM
3629
OE1
GLU
A
476
−2.038
41.853
19.381
1.00
41.94
8


ATOM
3630
OE2
GLU
A
476
−2.551
43.875
20.071
1.00
41.62
8


ATOM
3631
C
GLU
A
476
1.884
41.853
21.549
1.00
38.98
6


ATOM
3632
O
GLU
A
476
2.722
42.182
22.392
1.00
39.17
8


ATOM
3633
O3
XXX
B
1
36.620
0.299
53.346
1.00
31.59
8


ATOM
3634
C16
XXX
B
1
36.394
−0.943
53.264
1.00
30.79
6


ATOM
3635
O2
XXX
B
1
37.256
−1.724
52.792
1.00
32.22
8


ATOM
3636
C6
XXX
B
1
35.034
−1.437
53.555
1.00
29.59
6


ATOM
3637
C5
XXX
B
1
34.807
−2.745
53.216
1.00
29.56
6


ATOM
3638
C4
XXX
B
1
33.540
−3.262
53.396
1.00
29.83
6


ATOM
3639
O1
XXX
B
1
33.336
−4.577
53.106
1.00
30.11
8


ATOM
3640
C2
XXX
B
1
33.810
−5.534
54.078
1.00
30.31
6


ATOM
3641
C3
XXX
B
1
32.508
−2.454
53.901
1.00
29.73
6


ATOM
3642
C8
XXX
B
1
32.754
−1.115
54.228
1.00
29.61
6


ATOM
3643
C7
XXX
B
1
34.038
−0.587
54.034
1.00
29.31
6


ATOM
3644
N1
XXX
B
1
34.363
0.697
54.335
1.00
34.18
7


ATOM
3645
C9
XXX
B
1
33.570
1.759
54.668
1.00
34.35
6


ATOM
3646
C10
XXX
B
1
34.206
2.952
54.992
1.00
34.37
6


ATOM
3647
CL1
XXX
B
1
35.990
3.017
54.990
1.00
35.08
17


ATOM
3648
C11
XXX
B
1
33.491
4.090
55.340
1.00
34.31
6


ATOM
3649
C12
XXX
B
1
32.105
4.031
55.375
1.00
34.37
6


ATOM
3650
C15
XXX
B
1
32.179
1.702
54.697
1.00
34.22
6


ATOM
3651
C13
XXX
B
1
31.458
2.834
55.071
1.00
34.29
6


ATOM
3652
C14
XXX
B
1
29.980
2.811
55.031
1.00
34.34
6


ATOM
3653
F2
XXX
B
1
29.542
1.620
54.665
1.00
34.23
9


ATOM
3654
F1
XXX
B
1
29.423
3.256
56.133
1.00
34.40
9


ATOM
3655
F3
XXX
B
1
29.667
3.628
54.034
1.00
33.85
9


ATOM
3656
OW0
HOH
Z
1
37.822
13.622
53.680
1.00
15.33
8


ATOM
3657
OW0
HOH
Z
2
18.685
32.491
19.622
1.00
13.60
8


ATOM
3658
OW0
HOH
Z
3
38.854
5.704
44.654
1.00
15.09
8


ATOM
3659
OW0
HOH
Z
4
27.903
21.019
56.001
1.00
19.13
8


ATOM
3660
OW0
HOH
Z
5
18.488
29.463
56.125
1.00
12.99
8


ATOM
3661
OW0
HOH
Z
6
25.385
26.563
45.292
1.00
19.53
8


ATOM
3662
OW0
HOH
Z
7
25.083
10.850
37.888
1.00
17.27
8


ATOM
3663
OW0
HOH
Z
8
18.171
25.457
23.312
1.00
13.96
8


ATOM
3664
OW0
HOH
Z
9
34.748
0.785
58.071
1.00
25.49
8


ATOM
3665
OW0
HOH
Z
10
15.402
20.878
20.971
1.00
18.20
8


ATOM
3666
OW0
HOH
Z
11
33.766
11.435
36.799
1.00
14.84
8


ATOM
3667
OW0
HOH
Z
12
31.486
26.934
49.667
1.00
15.39
8


ATOM
3668
OW0
HOH
Z
13
26.745
31.060
32.322
1.00
17.29
8


ATOM
3669
OW0
HOH
Z
14
36.010
−0.330
50.274
1.00
35.76
8


ATOM
3670
OW0
HOH
Z
15
21.934
32.232
30.615
1.00
26.33
8


ATOM
3671
OW0
HOH
Z
16
41.814
32.600
33.985
1.00
19.62
8


ATOM
3672
OW0
HOH
Z
17
30.209
26.754
31.566
1.00
17.55
8


ATOM
3673
OW0
HOH
Z
18
28.352
15.062
17.636
1.00
21.36
8


ATOM
3674
OW0
HOH
Z
19
14.792
24.142
14.382
1.00
20.89
8


ATOM
3675
OW0
HOH
Z
20
31.192
−0.541
44.151
1.00
17.74
8


ATOM
3676
OW0
HOH
Z
21
37.963
2.333
50.889
1.00
28.89
8


ATOM
3677
OW0
HOH
Z
22
28.011
36.495
16.475
1.00
18.28
8


ATOM
3678
OW0
HOH
Z
23
13.139
25.476
21.409
1.00
22.29
8


ATOM
3679
OW0
HOH
Z
24
43.167
10.915
31.847
1.00
19.40
8


ATOM
3680
OW0
HOH
Z
25
12.632
21.429
15.684
1.00
23.33
8


ATOM
3681
OW0
HOH
Z
26
28.232
21.780
25.905
1.00
15.83
8


ATOM
3682
OW0
HOH
Z
27
41.619
18.732
53.427
1.00
18.13
8


ATOM
3683
OW0
HOH
Z
28
28.934
28.618
10.813
1.00
22.82
8


ATOM
3684
OW0
HOH
Z
29
25.750
28.578
31.056
1.00
16.06
8


ATOM
3685
OW0
HOH
Z
30
14.431
17.847
23.211
1.00
23.94
8


ATOM
3686
OW0
HOH
Z
31
28.500
29.572
34.250
1.00
16.88
8


ATOM
3687
OW0
HOH
Z
32
26.444
20.176
36.005
1.00
19.45
8


ATOM
3688
OW0
HOH
Z
33
45.495
23.199
49.991
1.00
17.53
8


ATOM
3689
OW0
HOH
Z
34
31.253
29.028
33.200
1.00
19.70
8


ATOM
3690
OW0
HOH
Z
35
25.130
11.609
53.672
1.00
15.27
8


ATOM
3691
OW0
HOH
Z
36
14.722
21.507
13.868
1.00
15.75
8


ATOM
3692
OW0
HOH
Z
37
22.718
22.669
10.485
1.00
21.08
8


ATOM
3693
OW0
HOH
Z
38
43.259
18.983
21.022
1.00
28.09
8


ATOM
3694
OW0
HOH
Z
39
17.542
43.226
16.007
1.00
21.00
8


ATOM
3695
OW0
HOH
Z
40
17.230
25.687
14.371
1.00
18.65
8


ATOM
3696
OW0
HOH
Z
41
47.216
23.783
52.019
1.00
18.04
8


ATOM
3697
OW0
HOH
Z
42
18.267
27.408
27.308
1.00
19.35
8


ATOM
3698
OW0
HOH
Z
43
18.176
9.114
40.214
1.00
28.57
8


ATOM
3699
OW0
HOH
Z
44
39.197
3.317
39.068
1.00
28.47
8


ATOM
3700
OW0
HOH
Z
45
17.803
30.035
18.612
1.00
16.42
8


ATOM
3701
OW0
HOH
Z
46
24.483
29.548
46.805
1.00
28.93
8


ATOM
3702
OW0
HOH
Z
47
18.064
30.991
14.064
1.00
18.70
8


ATOM
3703
OW0
HOH
Z
48
35.800
12.559
38.381
1.00
14.71
8


ATOM
3704
OW0
HOH
Z
49
16.166
37.300
36.944
1.00
22.52
8


ATOM
3705
OW0
HOH
Z
50
27.074
15.074
12.960
1.00
22.10
8


ATOM
3706
OW0
HOH
Z
51
35.244
15.402
38.632
1.00
20.62
8


ATOM
3707
OW0
HOH
Z
52
29.144
19.248
2.533
1.00
32.02
8


ATOM
3708
OW0
HOH
Z
53
30.023
19.663
48.274
1.00
20.38
8


ATOM
3709
OW0
HOH
Z
54
16.485
32.550
4.015
1.00
22.22
8


ATOM
3710
OW0
HOH
Z
55
34.237
−3.231
38.221
1.00
22.14
8


ATOM
3711
OW0
HOH
Z
56
32.859
13.776
16.407
1.00
33.97
8


ATOM
3712
OW0
HOH
Z
57
16.387
28.781
14.798
1.00
20.46
8


ATOM
3713
OW0
HOH
Z
58
23.463
21.736
38.714
1.00
20.50
8


ATOM
3714
OW0
HOH
Z
59
28.599
13.684
40.844
1.00
22.55
8


ATOM
3715
OW0
HOH
Z
60
25.509
22.712
46.019
1.00
18.42
8


ATOM
3716
OW0
HOH
Z
61
15.655
29.984
17.139
1.00
15.72
8


ATOM
3717
OW0
HOH
Z
62
19.467
31.603
31.434
1.00
36.87
8


ATOM
3718
OW0
HOH
Z
63
40.126
14.067
26.325
1.00
18.04
8


ATOM
3719
OW0
HOH
Z
64
36.413
28.366
54.314
1.00
27.75
8


ATOM
3720
OW0
HOH
Z
65
30.152
16.353
37.179
1.00
25.23
8


ATOM
3721
OW0
HOH
Z
66
15.155
50.449
26.574
1.00
23.49
8


ATOM
3722
OW0
HOH
Z
67
24.302
14.378
11.006
1.00
35.27
8


ATOM
3723
OW0
HOH
Z
68
40.627
16.095
54.612
1.00
20.22
8


ATOM
3724
OW0
HOH
Z
69
24.088
20.337
−2.432
1.00
26.18
8


ATOM
3725
OW0
HOH
Z
70
48.658
20.278
25.536
1.00
28.46
8


ATOM
3726
OW0
HOH
Z
71
32.047
10.197
32.662
1.00
20.68
8


ATOM
3727
OW0
HOH
Z
72
19.918
36.104
27.470
1.00
22.48
8


ATOM
3728
OW0
HOH
Z
73
22.987
21.121
45.859
1.00
19.68
8


ATOM
3729
OW0
HOH
Z
74
18.380
34.430
53.619
1.00
25.04
8


ATOM
3730
OW0
HOH
Z
75
28.549
32.967
26.882
1.00
22.48
8


ATOM
3731
OW0
HOH
Z
76
41.296
9.330
52.172
1.00
22.60
8


ATOM
3732
OW0
HOH
Z
77
10.988
35.127
33.410
1.00
18.15
8


ATOM
3733
OW0
HOH
Z
78
35.295
10.622
40.452
1.00
15.95
8


ATOM
3734
OW0
HOH
Z
79
17.949
27.440
50.589
1.00
19.93
8


ATOM
3735
OW0
HOH
Z
80
10.767
39.966
24.397
1.00
23.87
8


ATOM
3736
OW0
HOH
Z
81
45.901
11.280
42.434
1.00
19.40
8


ATOM
3737
OW0
HOH
Z
82
7.978
31.749
23.537
1.00
21.58
8


ATOM
3738
OW0
HOH
Z
83
24.952
25.325
47.596
1.00
20.04
8


ATOM
3739
OW0
HOH
Z
84
25.229
23.737
10.203
1.00
13.90
8


ATOM
3740
OW0
HOH
Z
85
10.484
27.190
22.207
1.00
23.26
8


ATOM
3741
OW0
HOH
Z
86
10.102
29.856
27.603
1.00
29.94
8


ATOM
3742
OW0
HOH
Z
87
8.946
32.409
26.777
1.00
36.89
8


ATOM
3743
OW0
HOH
Z
88
35.821
10.369
29.087
1.00
31.98
8


ATOM
3744
OW0
HOH
Z
89
8.443
28.533
19.890
1.00
28.09
8


ATOM
3745
OW0
HOH
Z
90
45.395
30.512
31.462
1.00
19.93
8


ATOM
3746
OW0
HOH
Z
91
7.807
22.983
17.578
1.00
33.34
8


ATOM
3747
OW0
HOH
Z
92
32.197
33.701
29.608
1.00
33.95
8


ATOM
3748
OW0
HOH
Z
93
33.089
16.643
36.962
1.00
29.54
8


ATOM
3749
OW0
HOH
Z
94
31.422
22.669
11.824
1.00
31.11
8


ATOM
3750
OW0
HOH
Z
95
9.295
11.972
9.825
1.00
31.39
8


ATOM
3751
OW0
HOH
Z
96
27.520
29.277
38.934
1.00
17.79
8


ATOM
3752
OW0
HOH
Z
97
22.829
−0.768
32.759
1.00
30.73
8


ATOM
3753
OW0
HOH
Z
98
13.120
14.386
25.369
1.00
29.64
8


ATOM
3754
OW0
HOH
Z
99
12.752
33.382
12.039
1.00
46.98
8


ATOM
3755
OW0
HOH
Z
100
39.623
25.028
17.741
1.00
37.05
8


ATOM
3756
OW0
HOH
Z
101
44.001
32.051
35.403
1.00
28.33
8


ATOM
3757
OW0
HOH
Z
102
34.319
12.395
29.727
1.00
26.70
8


ATOM
3758
OW0
HOH
Z
103
40.241
29.254
21.534
1.00
19.18
8


ATOM
3759
OW0
HOH
Z
104
34.506
14.424
18.601
1.00
31.18
8


ATOM
3760
OW0
HOH
Z
105
43.862
13.985
47.722
1.00
20.99
8


ATOM
3761
OW0
HOH
Z
106
22.975
17.226
40.496
1.00
30.41
8


ATOM
3762
OW0
HOH
Z
107
38.656
10.110
28.761
1.00
31.21
8


ATOM
3763
OW0
HOH
Z
108
25.585
29.128
33.955
1.00
16.75
8


ATOM
3764
OW0
HOH
Z
109
2.167
36.413
33.710
1.00
28.37
8


ATOM
3765
OW0
HOH
Z
110
17.638
2.594
57.322
1.00
26.05
8


ATOM
3766
OW0
HOH
Z
111
11.751
19.947
2.718
1.00
27.71
8


ATOM
3767
OW0
HOH
Z
112
16.958
32.577
12.152
1.00
14.35
8


ATOM
3768
OW0
HOH
Z
113
21.418
43.736
24.993
1.00
31.71
8


ATOM
3769
OW0
HOH
Z
114
42.968
11.107
45.905
1.00
27.38
8


ATOM
3770
OW0
HOH
Z
115
10.369
20.726
5.200
1.00
22.98
8


ATOM
3771
OW0
HOH
Z
116
12.841
38.505
13.745
1.00
29.31
8


ATOM
3772
OW0
HOH
Z
117
23.993
27.166
34.757
1.00
37.52
8


ATOM
3773
OW0
HOH
Z
118
4.067
22.772
11.599
1.00
33.53
8


ATOM
3774
OW0
HOH
Z
119
36.685
36.532
34.585
1.00
28.02
8


ATOM
3775
OW0
HOH
Z
120
13.334
5.898
18.696
1.00
37.68
8


ATOM
3776
OW0
HOH
Z
121
12.697
35.375
18.933
1.00
17.13
8


ATOM
3777
OW0
HOH
Z
122
8.129
28.979
22.405
1.00
28.71
8


ATOM
3778
OW0
HOH
Z
123
24.067
10.544
58.129
1.00
23.85
8


ATOM
3779
OW0
HOH
Z
124
12.618
46.765
19.149
1.00
35.48
8


ATOM
3780
OW0
HOH
Z
125
34.377
27.461
14.842
1.00
30.14
8


ATOM
3781
OW0
HOH
Z
126
39.812
7.571
55.629
1.00
27.98
8


ATOM
3782
OW0
HOH
Z
127
23.824
12.244
55.913
1.00
20.56
8


ATOM
3783
OW0
HOH
Z
128
24.421
14.594
57.356
1.00
30.28
8


ATOM
3784
OW0
HOH
Z
129
13.103
25.051
32.881
1.00
32.37
8


ATOM
3785
OW0
HOH
Z
130
41.353
8.304
32.306
1.00
24.37
8


ATOM
3786
OW0
HOH
Z
131
24.902
18.010
57.781
1.00
24.38
8


ATOM
3787
OW0
HOH
Z
132
43.169
32.138
31.595
1.00
25.80
8


ATOM
3788
OW0
HOH
Z
133
13.080
36.914
15.756
1.00
26.12
8


ATOM
3789
OW0
HOH
Z
134
32.686
32.912
15.360
1.00
44.56
8


ATOM
3790
OW0
HOH
Z
135
30.118
−5.020
39.780
1.00
43.54
8


ATOM
3791
OW0
HOH
Z
136
46.349
28.908
43.950
1.00
25.34
8


ATOM
3792
OW0
HOH
Z
137
15.834
53.176
32.767
1.00
24.36
8


ATOM
3793
OW0
HOH
Z
138
15.758
45.060
16.791
1.00
29.03
8


ATOM
3794
OW0
HOH
Z
139
35.319
1.432
48.753
1.00
21.30
8


ATOM
3795
OW0
HOH
Z
140
9.445
25.069
20.886
1.00
20.28
8


ATOM
3796
OW0
HOH
Z
141
21.792
9.271
58.485
1.00
32.74
8


ATOM
3797
OW0
HOH
Z
142
42.205
25.913
54.888
1.00
27.36
8


ATOM
3798
OW0
HOH
Z
143
26.020
16.812
41.060
1.00
25.66
8


ATOM
3799
OW0
HOH
Z
144
9.426
18.328
6.516
1.00
26.81
8


ATOM
3800
OW0
HOH
Z
145
29.345
18.825
37.732
1.00
32.18
8


ATOM
3801
OW0
HOH
Z
146
27.286
8.358
20.729
1.00
34.20
8


ATOM
3802
OW0
HOH
Z
147
5.192
29.609
−3.540
1.00
29.15
8


ATOM
3803
OW0
HOH
Z
148
43.225
30.320
40.375
1.00
26.17
8


ATOM
3804
OW0
HOH
Z
149
23.005
33.152
9.707
1.00
20.56
8


ATOM
3805
OW0
HOH
Z
150
1.301
24.310
14.139
1.00
27.77
8


ATOM
3806
OW0
HOH
Z
151
14.773
22.679
33.210
1.00
47.52
8


ATOM
3807
OW0
HOH
Z
152
14.441
16.781
25.645
1.00
29.72
8


ATOM
3808
OW0
HOH
Z
153
15.832
25.353
2.636
1.00
32.00
8


ATOM
3809
OW0
HOH
Z
154
33.917
27.535
31.100
1.00
24.90
8


ATOM
3810
OW0
HOH
Z
155
16.573
18.337
26.993
1.00
30.65
8


ATOM
3811
OW0
HOH
Z
156
49.083
24.041
35.174
1.00
50.65
8


ATOM
3812
OW0
HOH
Z
157
25.656
28.124
58.668
1.00
25.06
8


ATOM
3813
OW0
HOH
Z
158
29.025
35.725
30.500
1.00
29.89
8


ATOM
3814
OW0
HOH
Z
159
29.404
33.380
29.383
1.00
27.48
8


ATOM
3815
OW0
HOH
Z
160
3.036
33.894
29.099
1.00
34.64
8


ATOM
3816
OW0
HOH
Z
161
36.806
20.478
13.785
1.00
31.35
8


ATOM
3817
OW0
HOH
Z
162
22.710
28.005
−0.360
1.00
40.32
8


ATOM
3818
OW0
HOH
Z
163
49.395
29.484
44.215
1.00
27.87
8


ATOM
3819
OW0
HOH
Z
164
38.195
7.496
21.008
1.00
35.78
8


ATOM
3820
OW0
HOH
Z
165
27.362
27.286
32.830
1.00
24.87
8


ATOM
3821
OW0
HOH
Z
166
35.178
20.590
11.628
1.00
41.69
8


ATOM
3822
OW0
HOH
Z
167
1.900
24.512
11.600
1.00
27.52
8


ATOM
3823
OW0
HOH
Z
168
17.133
32.107
33.189
1.00
51.63
8


ATOM
3824
OW0
HOH
Z
169
23.236
28.962
8.047
1.00
22.58
8


ATOM
3825
OW0
HOH
Z
170
48.158
23.950
55.109
1.00
25.58
8


ATOM
3826
OW0
HOH
Z
171
3.245
43.682
24.450
1.00
52.57
8


ATOM
3827
OW0
HOH
Z
172
48.636
28.997
19.770
1.00
31.29
8


ATOM
3828
OW0
HOH
Z
173
29.325
21.740
10.162
1.00
38.25
8


ATOM
3829
OW0
HOH
Z
174
43.154
38.981
44.762
1.00
31.59
8


ATOM
3830
OW0
HOH
Z
175
40.336
27.024
19.307
1.00
40.82
8


ATOM
3831
OW0
HOH
Z
176
22.845
32.080
46.844
1.00
29.32
8


ATOM
3832
OW0
HOH
Z
177
18.470
17.527
50.146
1.00
26.02
8


ATOM
3833
OW0
HOH
Z
178
35.329
23.084
10.710
1.00
57.72
8


ATOM
3834
OW0
HOH
Z
179
16.593
37.497
10.415
1.00
51.98
8


ATOM
3835
OW0
HOH
Z
180
14.291
50.563
24.073
1.00
47.83
8


ATOM
3836
OW0
HOH
Z
181
27.396
3.187
67.249
1.00
33.61
8


ATOM
3837
OW0
HOH
Z
182
27.769
27.390
8.617
1.00
26.03
8


ATOM
3838
OW0
HOH
Z
183
7.562
9.332
53.022
1.00
32.97
8


ATOM
3839
OW0
HOH
Z
184
22.829
34.060
48.715
1.00
35.59
8


ATOM
3840
OW0
HOH
Z
185
50.459
15.517
43.604
1.00
35.09
8


ATOM
3841
OW0
HOH
Z
186
33.695
8.260
29.443
1.00
32.85
8


ATOM
3842
OW0
HOH
Z
187
14.359
48.227
42.474
1.00
45.87
8


ATOM
3843
OW0
HOH
Z
188
24.143
19.814
40.471
1.00
35.57
8


ATOM
3844
OW0
HOH
Z
189
38.593
8.163
17.010
1.00
39.72
8


ATOM
3845
OW0
HOH
Z
190
7.857
26.087
19.027
1.00
36.57
8


ATOM
3846
OW0
HOH
Z
191
9.017
7.035
14.732
1.00
44.76
8


ATOM
3847
OW0
HOH
Z
192
19.795
51.849
39.250
1.00
33.06
8


ATOM
3848
OW0
HOH
Z
193
45.205
9.722
39.677
1.00
36.05
8


ATOM
3849
OW0
HOH
Z
194
24.718
9.870
4.590
1.00
28.64
8


ATOM
3850
OW0
HOH
Z
195
37.810
24.483
15.049
1.00
40.21
8


ATOM
3851
OW0
HOH
Z
196
38.824
18.936
57.170
1.00
27.46
8


ATOM
3852
OW0
HOH
Z
197
40.110
3.376
43.825
1.00
31.70
8


ATOM
3853
OW0
HOH
Z
198
28.698
16.252
10.769
1.00
38.76
8


ATOM
3854
OW0
HOH
Z
199
9.187
32.983
4.147
1.00
38.86
8


ATOM
3855
OW0
HOH
Z
200
51.813
20.350
42.847
1.00
29.38
8


ATOM
3856
OW0
HOH
Z
201
28.748
15.079
63.026
1.00
35.69
8


ATOM
3857
OW0
HOH
Z
202
20.468
37.756
10.039
1.00
48.67
8


ATOM
3858
OW0
HOH
Z
203
17.990
8.848
56.759
1.00
35.68
8


ATOM
3859
OW0
HOH
Z
204
5.145
25.229
19.650
1.00
34.82
8


ATOM
3860
OW0
HOH
Z
205
31.863
11.213
29.933
1.00
39.80
8


ATOM
3861
OW0
HOH
Z
206
22.608
−5.570
37.559
1.00
36.84
8


ATOM
3862
OW0
HOH
Z
207
48.062
25.072
37.444
1.00
44.17
8


ATOM
3863
OW0
HOH
Z
208
13.541
20.150
31.969
1.00
57.25
8


ATOM
3864
OW0
HOH
Z
209
31.863
0.830
25.886
1.00
39.37
8


ATOM
3865
OW0
HOH
Z
210
35.449
17.282
62.211
1.00
38.11
8


ATOM
3866
OW0
HOH
Z
211
19.296
9.780
18.915
1.00
74.89
8


ATOM
3867
OW0
HOH
Z
212
9.113
8.119
43.855
1.00
42.78
8


ATOM
3868
OW0
HOH
Z
213
25.316
26.074
8.860
1.00
30.16
8


ATOM
3869
OW0
HOH
Z
214
20.140
29.894
48.350
1.00
43.12
8


ATOM
3870
OW0
HOH
Z
215
29.660
14.503
15.123
1.00
48.14
8


ATOM
3871
OW0
HOH
Z
216
41.481
8.331
18.292
1.00
39.82
8


ATOM
3872
OW0
HOH
Z
217
−3.523
31.903
18.867
1.00
35.80
8


ATOM
3873
OW0
HOH
Z
218
51.266
25.888
25.263
1.00
23.86
8


ATOM
3874
OW0
HOH
Z
219
36.513
7.196
56.549
1.00
27.66
8


ATOM
3875
OW0
HOH
Z
220
12.213
18.423
27.309
1.00
37.25
8


ATOM
3876
OW0
HOH
Z
221
32.240
1.474
62.119
1.00
53.64
8


ATOM
3877
OW0
HOH
Z
222
33.674
8.526
60.220
1.00
37.38
8


ATOM
3878
OW0
HOH
Z
223
21.183
22.012
5.098
1.00
47.51
8


ATOM
3879
OW0
HOH
Z
224
17.780
33.381
9.563
1.00
33.21
8


ATOM
3880
OW0
HOH
Z
225
32.481
11.769
63.015
1.00
53.06
8


ATOM
3881
OW0
HOH
Z
226
21.211
10.090
17.270
1.00
48.88
8


ATOM
3882
OW0
HOH
Z
227
3.413
13.486
25.700
1.00
57.93
8


ATOM
3883
OW0
HOH
Z
228
41.372
7.528
49.259
1.00
57.18
8


ATOM
3884
OW0
HOH
Z
229
44.091
13.172
15.975
1.00
48.72
8


ATOM
3885
OW0
HOH
Z
230
22.649
45.181
28.556
1.00
38.14
8


ATOM
3886
OW0
HOH
Z
231
32.314
27.093
54.668
1.00
34.77
8


ATOM
3887
OW0
HOH
Z
232
−2.290
26.794
20.664
1.00
42.85
8


ATOM
3888
OW0
HOH
Z
233
37.329
−3.664
39.804
1.00
35.89
8


ATOM
3889
OW0
HOH
Z
234
5.340
32.703
7.314
1.00
45.25
8


ATOM
3890
OW0
HOH
Z
235
2.333
33.544
2.954
1.00
35.13
8


ATOM
3891
OW0
HOH
Z
236
25.900
13.080
40.172
1.00
43.16
8


ATOM
3892
OW0
HOH
Z
237
19.138
14.576
49.299
1.00
42.79
8


ATOM
3893
OW0
HOH
Z
238
25.567
26.472
40.031
1.00
39.97
8


ATOM
3894
OW0
HOH
Z
239
17.546
−9.985
43.762
1.00
58.18
8


ATOM
3895
OW0
HOH
Z
240
−1.672
29.072
26.286
1.00
52.04
8


ATOM
3896
OW0
HOH
Z
241
6.097
34.431
9.544
1.00
38.91
8


ATOM
3897
OW0
HOH
Z
242
50.812
22.728
44.664
1.00
36.96
8


ATOM
3898
OW0
HOH
Z
243
45.963
17.701
32.633
1.00
34.09
8


ATOM
3899
OW0
HOH
Z
244
22.571
15.881
32.301
1.00
39.52
8


ATOM
3900
OW0
HOH
Z
245
29.466
34.586
49.675
1.00
30.29
8


ATOM
3901
OW0
HOH
Z
246
−0.096
25.184
4.188
1.00
30.65
8


ATOM
3902
OW0
HOH
Z
247
18.238
39.484
37.998
1.00
39.98
8


ATOM
3903
OW0
HOH
Z
248
23.712
15.984
61.484
1.00
44.49
8


ATOM
3904
OW0
HOH
Z
249
42.851
17.446
27.926
1.00
29.01
8


ATOM
3905
OW0
HOH
Z
250
21.804
38.564
12.235
1.00
49.41
8


ATOM
3906
OW0
HOH
Z
251
36.403
39.596
28.126
1.00
44.13
8


END









Table 8 illustrates the number and identity of known protein interactions with bacterial SSBs.







TABLE 8







Protein interactions with bacterial SSBs










SSB-Ct



SSB-interacting protein
required?
References





Chi (DNA
Yes
Butland et al., 2005, Nature 433:


polymerase III)

531-537


DNA polymerase II
Yes
Molineux and Gefter, 1974, Proc.




Natl. Acad. Sci. USA 71:




3858-3862


DNA polymerase V
Yes
Arad et al., 2008, J. Biol. Chem.




283: 8274-8282


Exonuclease I
Yes
Butland et al., 2005, Nature 433:




531-537


Exonuclease IX
Unknown
Hodskinson et al., 2007, Nucl.




Acids Res. 35: 4094-4102


PriA
Yes
Butland et al., 2005, Nature 433:




531-537


PriB
Unknown
Low et al., 1982, J. Biol. 257:




6242-6250


Primase
Yes
Yuzhakov et al., 1999, Cell 96:




153-163


RecG
Unknown
Butland et al., 2005, Nature 433:




531-537


RecJ
Unknown
Butland et al., 2005, Nature 433:




531-537


RecO
Unknown
Umezu et al., 1993, Proc. Natl.




Acad. Sci. 90: 3875-3879


RecQ
Yes
Butland et al., 2005, Nature 433:




531-537


Topoisomerase III
Unknown
Butland et al., 2005, Nature 433:




531-537


Uracil DNA glycosylase
Yes
Purnapatre et al., 1999, Nucl.




Acids Res. 27: 3487-3492









Table 9 illustrates the crystallographic data collection and structure refinement statistics.







TABLE 9





Crystallographic data collection and structure refinement statistics

















Space group
P212121
P212121


Unit cell parameters
52, 63, 92.08, 102.79
67.15, 92.19, 91.28


(a, b, c (Å)) (α, β, γ (°))
90, 90, 90
90, 90, 90


Resolution range
  20-1.7 (1.77-1.70)
  20-2.7 (2.77-2.70)


(High resolution) (Å)




Rsym (%)*
 6.1 (47.9)
 7.9 (38.3)


Completeness (%)
92.5 (91.5)
98.0 (88.2)


Redundancy
4.0 (4.0)
3.7 (3.8)


<I/σ>
37.7 (4.0) 
25.9 (4.0) 


Refinement




Resolution (Å)
 20-1.7
 20-2.7


Rwork/Rfree (%)**
18.0/21.3
19.8/25.2


Residues
446
465


Protein atoms***
3740
3782


Solvent atoms
436
42


<B factor> protein
23.9
52.5


<B factor> peptide A
Not applicable
50.4


<B factor> peptide B
Not applicable
80.4


<B factor> solvent
37.0
43.1


RMSD bond lengths
0.013
0.013


(Å)




RMSD bond angles (°)
1.10
1.05


Ramachandran statistics,
92.7
90.4


% core




% allowed
7.3
9.6


% generously allowed
0
0


% disallowed
0
0





*Rsym = ΣΣj|Ij − <I>|/ΣIj, where Ij is the intensity measurement for reflection j and <I> is the mean intensity for multiply recorded reflections.


**Rwork, free = Σ||Fobs| − |Fcalc||/|Fobs|, where the working and free R factors are calculated using the working and free reflection sets, respectively. The free R reflections (5% of the total) were held aside throughout refinement.


***Note that for the apo-Exol structure, several side-chains and one loop sequence were modeled in multiple rotamers/conformations; in cases where atoms have been modeled in multiple conformations, each modeled position is counted in the number of protein atoms (i.e. if a given atom is modeled in two positions it is counted as two protein atoms rather than one in the SI Table 9).






Table 10 shows Kd, app values for F-SSB-Ct binding by ExoI and variants.







TABLE 10







Kd, app values for F-SSB-Ct binding by Exol and variants












Role of mutated residue




Protein
in Exol
Kd, app (nM)






Exol
—
136 +/− 11



Arg148Ala
peptide A binding
>>1000



Tyr207Ala
peptide A binding
>1000



Gln311Ala
peptide A binding
304 +/− 14



Arg316Ala
flanks peptide A
>1000



Arg327Ala
peptide B binding
270 +/− 22



Leu331Ala
peptide B binding
193 +/− 3 



Lys227Ala
basic ridge
~1000



Arg338Ala
basic ridge
398 +/− 15



Glu150Ala
Mg2+ binding
72 +/− 1



Glu318Ala
Mg2+ binding
80 +/− 6



Asp319Ala
Mg2+ binding
299 +/− 8 



Gln448Ala
helical domain
181 +/− 25



Gln452Ala
helical domain
212 +/− 6 









Topoisomerase III Peptide Binding

Topoisomerase III binding assays were conducted (FIG. 24) to determine if the candidate compounds can inhibit the binding of the C-terminal tail of E. coli SSB to other proteins that are known SSB binding partners. One such binding partner is Topoisomerase III (TopoIII), one of a number of proteins that interact with the C-terminal tail of SSB (Shereda, Bernstein, and Keck, unpublished observation). TopoIII was titrated into 10 nM fluorescent peptide, as described above for the ExoI binding assays. The buffer conditions for this binding assay were: 300 mM NaCl, 20 mM Tris pH 8.0, 10% Glycerol, 1 mM BME (Beta-Mercaptoethanol), and 1% DMSO. Concentrations of TopoIII used are given on the graph in FIG. 24. Changes in anisotropy upon binding were read using PanVera Beacon 2000 FP.
The data indicate that peptide binding is much weaker in the case of TopoIII/peptide, making it difficult to accurately determine a binding constant (Kd). In order to determine if the compounds had an effect on peptide binding to TopoIII, a similar set of experiments as stated above was set up, except for the omission of DMSO from the buffer solution. Either unlabeled peptide or various compounds were then added to a final concentration of 100 μM. These compounds and unlabeled peptide were dissolved in DMSO and their addition brought the final concentration of DMSO to 1%.
Some of the candidate compounds were able to inhibit binding of the peptide to TopoIII, lowering the observed anisotropy value. As shown in FIG. 24, even addition of 100 μM unlabeled peptide did not bring the anisotropy values down to the baseline (the values that would be expected with no binding of fluorescently labeled peptide). This is due to the very high concentrations of TopoIII that need to be used in order to observe binding. Thus, some of the compounds such as 10 can not only inhibit binding of the fluorescent peptide to ExoI but also to other known binding partners, such TopoIII. Therefore, at least some of the identified inhibitors can actually inhibit binding of the C-terminal tail of SSB to more than one of its binding partners, and not just ExoI.
Mammalian Cell Toxicity
The toxicity of the identified antimicrobial candidate compounds was tested using human colorectal adenocarcinoma cells in vitro. The tested compounds are significantly less toxic to HT-29 (human colorectal adenocarcinoma) than to Gram-positive bacterial cells or the cell wall compromised E. coli cells. The mammalian cells were tested using a CellTiter-Glo cell viability assay (Promega, Madison, Wis.).
According to the data obtained with this assay compound 3 had an IC50>100 μM, compound 8 had an IC50>100 μM, compound 9 had an IC50=38 μM, compound 10 had an IC50=60 μM, compounds 28, 29, 32, and 37 all had an IC50>100 μM, compound 42 had an IC50=51 μM, and compound 46 had an IC50=55 μM. Comparing these data to the IC50 from the bacterial growth curves, the conclusion is that the compounds are much more effective at killing bacteria than mammalian cells.
Hemolysis
In vitro hemolysis experiments were carried out to determine if the identified drug candidates merely inhibited bacterial growth by causing cell lysis. The identified small molecules were incubated with red blood cells to see what percentage of cells would lyse after 1 hour. The results from these experiments are shown in Table 11. Estimated hemolysis data are due to problem with reading absorbance, when the compound absorbs at the same wavelength as heme or if the compound precipitates. In such instances it is difficult to quantitate the absorbance readings; however, visual determination of how many cells have lysed can then be performed, which provides an estimate of cell lysis.







TABLE 11







Results from hemolysis experiments












% hemolysis at
% hemolysis at



Inhibitor
given concentration
given concentration















3
20% 100
μM




8
estimated 0% 200
μM
estimated 90% 400 uM



9
0% >800
μM




10
0% 400
μM
85% at 800 μM



32
0% >800
μM




37
estimated 0% 800
μM




28
0% >800
μM




29
0% >800
μM




31
0% >800
μM




46
0% >800
μM




42
0% >800
μM









It is to be understood that this invention is not limited to the particular devices, methodology, protocols, subjects, or reagents described, and as such may vary. It is also to be understood that 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 limited only by the claims. Other suitable modifications and adaptations of a variety of conditions and parameters, obvious to those skilled in the art of biochemistry and pharmaceutical chemistry, are within the scope of this invention. All publications, patents, and patent applications cited herein are incorporated by reference in their entirety for all purposes.

## Claims

1. A method of inhibiting the growth of a bacterium, the method comprising:
contacting the bacterium with a compound of the formula




wherein Y represents NH, R1 represents Cl, R2 represents CF3, R3 represents CO2H, R4 represents H, and R3 represents OCH3.

2. A method of inhibiting the growth of a microorganism, the method comprising:
contacting the microorganism with a compound of the formula




wherein Y is selected from the group consisting of CH2, O, and NH,
R1 is selected from the group consisting of H, F, Cl, Br, and I,
R2 is selected from the group consisting of H and CF3,
R3 is selected from the group consisting of H and CO2H,
R4 is selected from the group consisting of H and OH,
R5 is selected from the group consisting of H, alkoxy, and NO2,
at least one of R1, R2, R3, R4, and R5 is a group other than H, and
when R4 is OH, at least one of R1, R2, R3, and R5 is a group other than H,
the microorganism comprising at least one of Bacillus anthracis, Clostridium difficile, Francisella tularensis, Shigella dysenteriae, Salmonella typhimurium, Listeria monocytogenes, Campylobacter jejuni, Yersinia enterocolitica, Mycobacterium tuberculosis, Brucella abortus, Coxiella burnetii, Burkholderia mallei, Clostridium perfringens, Rickettsia prowazekii, Staphylococcus aureus, Streptococcus pneumoniae, Streptococcus pyogenes, Streptococcus sanguinis, Streptococcus thermophilus, Streptococcus agalactiae, Streptococcus mutans, Streptococcus suis, and Enterococcus faecalis.

3. A method of treating a subject having a bacterial infection, the method comprising:
administering a therapeutically effective amount of an antibacterial pharmaceutical composition to a subject experiencing a bacterial infection from bacteria comprising at least one of Bacillus anthracis, Clostridium difficile, Francisella tularensis, Shigella dysenteriae, Salmonella typhimurium, Listeria monocytogenes, Campylobacter jejuni, Yersinia enterocolitica, Mycobacterium tuberculosis, Brucella abortus, Coxiella burnetii, Burkholderia mallei, Clostridium perfringens, Rickettsia prowazekii, Staphylococcus aureus, Streptococcus pneumoniae, Streptococcus pyogenes, Streptococcus sanguinis, Streptococcus thermophilus, Streptococcus agalactiae, Streptococcus mutans, Streptococcus suis, and Enterococcus faecalis, 
the antibacterial pharmaceutical composition comprising, as an active agent, a compound having the formula




wherein Y is selected from the group consisting of CH2, O, and NH,
R1 is selected from the group consisting of H, F, Cl, Br, and I,
R2 is selected from the group consisting of H and CF3,
R3 is selected from the group consisting of H and CO2H,
R4 is selected from the group consisting of H and OH,
R5 is selected from the group consisting of H, alkoxy, and NO2, and
at least one of R1, R2, R3, R4, and R5 is a group other than H,
the compound being present in the composition in an amount sufficient to inhibit the growth of a bacterium.

4. The method of claim 3, wherein Y represents NH, R1 represents Cl, R2 represents CF3, R3 represents CO2H, R4 represents H, and R5 represents OCH3.

5. The method of claim 3, wherein R1 is F, Cl or Br.

6. A method of inhibiting the growth of a microorganism, the method comprising: contacting the microorganism with a compound of the formula



wherein Y is selected from the group consisting of CH2, O, and NH,
R1 is selected from the group consisting of H, F, Cl, Br, and I,
R2 is selected from the group consisting of H and CF3,
R3 is selected from the group consisting of H and CO2H,
R4 is selected from the group consisting of H and OH,
R5 is selected from the group consisting of H, alkoxy, and NO2, and
at least one of R1, R2, R3, R4, and R3 is a group other than H
the microorganism comprising at least one of Bacillus anthracia, Clostridium difficile, Francisella tularensis, Shigella dysenteriae, Salmonella typhimurium, Listeria monocytogenes, Campylobacter jejuni, Yersinia enterocolitica, Mycobacterium tuberculosis, Brucella abortus, Coxiella burnetii, Burkholderia mallei, Clostridium perfringens, Rickettsia prowazekii, Staphylococcus aureus, Streptococcus pneumoniae, Streptococcus pyogenes, Streptococcus sanguinis, Streptococcus thermophilus, Streptococcus agalactiae, Streptococcus mutans, Streptococcus suis, and Enterococcus faecalis.

7. The method of claim 6, wherein contacting the microorganism with the compound inhibits binding of a prokaryotic single-stranded DNA binding protein to a polypeptide that binds to the prokaryotic single-stranded DNA binding protein of the microorganism.

8. The method according to claim 6, wherein Y represents NH, R1 represents Cl, R2 represents CF3, R3 represents CO2H, R4 represents H, and R5 represents OCH3.

9. An antimicrobial pharmaceutical composition comprising:
as an active agent a compound of the formula




wherein Y is NH, R1 is F, Cl or Br, R2 is CF3, R3 is CO2H, R4 is H, and R5 is OCH3.

10. The antibacterial pharmaceutical composition of claim 9, wherein the compound is present in an amount sufficient to inhibit the rate of growth of a population of bacteria.

11. The antimicrobial pharmaceutical composition of claim 9, wherein R1 is Cl.

12. A method of inhibiting the growth of a microorganism, the method comprising:
administering a composition to a subject, the composition comprising a compound; and
contacting a microorganism comprising at least one of Bacillus anthracis, Clostridium difficile, Francisella tularensis, Shigella dysenteriae, Salmonella typhimurium, Listeria monocytogenes, Campylobacter jejuni, Yersinia enterocolitica, Mycobacterium tuberculosis, Brucella abortus, Coxiella burnetii, Burkholderia mallei, Clostridium perfringens, Rickettsia prowazekii, Staphylococcus aureus, Streptococcus pneumoniae, Streptococcus pyogenes, Streptococcus sanguinis, Streptococcus thermophilus, Streptococcus agalactiae, Streptococcus mutans, Streptococcus suis, and Enterococcus faecalis with the compound,
the compound having the formula




wherein Y is NH, R1 is Cl, R2 is CF3, R3 is CO2H, R4 is H, and R15 is OCH3.

13. An antimicrobial pharmaceutical composition comprising:
as an active agent a compound of the formula




wherein Y is NH, R1 is Cl, R2 is CF3, R3 is CO2H, R4 is H, and R15 is OCH3; and
at least one of a pharmaceutically acceptable carrier and a pharmaceutically acceptable excipient,
the composition being in a dosage form selected from the group consisting of an orally administered dosage form and a parenterally administered dosage form, and
the compound being present in the composition in an amount sufficient to inhibit the growth of a microbe comprising at least one of Bacillus anthracis, Clostridium difficile, Francisella tularensis, Shigella dysenteriae, Salmonella typhimurium, Listeria monocytogenes, Campylobacter jejuni, Yersinia enterocolitica, Mycobacterium tuberculosis, Brucella abortus, Coxiella burnetii, Burkholderia mallei, Clostridium perfringens, Rickettsia prowazekii, Staphylococcus aureus, Streptococcus pneumoniae, Streptococcus pyogenes, Streptococcus sanguinis, Streptococcus thermophilus, Streptococcus agalactiae, Streptococcus mutans, Streptococcus suis, and Enterococcus faecalis.

14. An antimicrobial pharmaceutical composition comprising:
as an active agent a compound of the formula




wherein Y is NH, R1 is Cl, R2 is CF3, R3 is CO2H, R4 is H, and R15 is OCH3; and
at least one of a pharmaceutically acceptable carrier and a pharmaceutically acceptable excipient,
the compound being present in the composition in an amount sufficient to inhibit the rate of growth of a population of bacteria, the bacteria comprising at least one of Bacillus anthracis, Clostridium difficile, Francisella tularensis, Shigella dysenteriae, Salmonella typhimurium, Listeria monocytogenes, Campylobacter jejuni, Yersinia enterocolitica, Mycobacterium tuberculosis, Brucella abortus, Coxiella burnetii, Burkholderia mallei, Clostridium perfringens, Rickettsia prowazekii, Staphylococcus aureus, Streptococcus pneumoniae, Streptococcus pyogenes, Streptococcus sanguinis, Streptococcus thermophilus, Streptococcus agalactiae, Streptococcus mutans, Streptococcus suis, and Enterococcus faecalis.

15. A method of treating a subject having a microbial infection, the method comprising:
administering a therapeutically effective amount of a pharmaceutical composition to a subject experiencing a microbial infection from bacteria comprising at least one of Bacillus anthracis, Clostridium difficile, Francisella tularensis, Shigella dysenteriae, Salmonella typhimurium, Listeria monocytogenes, Campylobacter jejuni, Yersinia enterocolitica, Mycobacterium tuberculosis, Brucella abortus, Coxiella burnetii, Burkholderia mallei, Clostridium perfringens, Rickettsia prowazekii, Staphylococcus aureus, Streptococcus pneumoniae, Streptococcus pyogenes, Streptococcus sanguinis, Streptococcus thermophilus, Streptococcus agalactiae, Streptococcus mutans, Streptococcus suis, and Enterococcus faecalis, 
the pharmaceutical composition comprising, as an active agent, a compound of the formula




wherein Y is selected from the group consisting of CH2, O, and NH,
R1 is selected from the group consisting of H, F, Cl, Br, and I,
R2 is selected from the group consisting of H and CF3,
R3 is selected from the group consisting of H and CO2H,
R4 is selected from the group consisting of H and OH,
R5 is selected from the group consisting of H, alkoxy, and NO2, and
at least one of R1, R2, R3, R4, and R5 is a group other than H; and
at least one of a pharmaceutically acceptable carrier and a pharmaceutically acceptable excipient,
the compound being present in the composition in an amount sufficient to inhibit the rate of growth of a population of bacteria, the bacteria comprising at least one of Bacillus anthracis, Clostridium difficile, Francisella tularensis, Shigella dysenteriae, Salmonella typhimurium, Listeria monocytogenes, Campylobacter jejuni, Yersinia enterocolitica, Mycobacterium tuberculosis, Brucella abortus, Coxiella burnetii, Burkholderia mallei, Clostridium perfringens, Rickettsia prowazekii, Staphylococcus aureus, Streptococcus pneumoniae, Streptococcus pyogenes, Streptococcus sanguinis, Streptococcus thermophilus, Streptococcus agalactiae, Streptococcus mutans, Streptococcus suis, and Enterococcus faecalis.