CNRS Nantes University UFIP UFIP
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***  TRANSFERASE 12-JAN-11 3QAW  ***

elNémo ID: 22100401185723686

Job options:

ID        	=	 22100401185723686
JOBID     	=	 TRANSFERASE 12-JAN-11 3QAW
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 10
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    TRANSFERASE                             12-JAN-11   3QAW              
TITLE     CRYSTAL STRUCTURE OF A GLUTATHIONE-S-TRANSFERASE FROM ANTARCTIC CLAM  
TITLE    2 LATERNULA ELLIPTICA IN A COMPLEX WITH GLUTATHIONE                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RHO-CLASS GLUTATHIONE S-TRANSFERASE;                       
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 2.5.1.18;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: LATERNULA ELLIPTICA;                            
SOURCE   3 ORGANISM_TAXID: 228457;                                              
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    CYTOSOL, TRANSFERASE                                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.K.PARK,J.H.MOON,Y.M.CHI                                             
REVDAT   3   08-NOV-17 3QAW    1       REMARK                                   
REVDAT   2   13-FEB-13 3QAW    1       JRNL                                     
REVDAT   1   01-FEB-12 3QAW    0                                                
JRNL        AUTH   A.K.PARK,J.H.MOON,E.H.JANG,H.PARK,I.Y.AHN,K.S.LEE,Y.M.CHI    
JRNL        TITL   THE STRUCTURE OF A SHELLFISH SPECIFIC GST CLASS GLUTATHIONE  
JRNL        TITL 2 S-TRANSFERASE FROM ANTARCTIC BIVALVE LATERNULA ELLIPTICA     
JRNL        TITL 3 REVEALS NOVEL ACTIVE SITE ARCHITECTURE.                      
JRNL        REF    PROTEINS                      V.  81   531 2013              
JRNL        REFN                   ISSN 0887-3585                               
JRNL        PMID   23152139                                                     
JRNL        DOI    10.1002/PROT.24208                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 95.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 11476                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.181                           
REMARK   3   FREE R VALUE                     : 0.215                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.600                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 592                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1783                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 20                                      
REMARK   3   SOLVENT ATOMS            : 130                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.81                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.69700                                              
REMARK   3    B22 (A**2) : 3.38300                                              
REMARK   3    B33 (A**2) : -6.08000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -1.45700                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 2.657 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 3.359 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 4.106 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 5.566 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 67.75                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : GSH.PARAM                                      
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3QAW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 27-JAN-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000063413.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-JUN-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 77                                 
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PAL/PLS                            
REMARK 200  BEAMLINE                       : 4A                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00000                            
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, HKL-2000                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 11476                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.860                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: 3QAV                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.10                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.16                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 7% TACSIMATE PH 8.0, 24% (W/V)           
REMARK 280  POLYETHYLENE GLYCOL 3350, VAPOR DIFFUSION, SITTING DROP,            
REMARK 280  TEMPERATURE 295K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       45.19650            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       28.80550            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       45.19650            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       28.80550            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2350 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20210 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000       28.63661            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       92.11142            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -19                                                      
REMARK 465     GLY A   -18                                                      
REMARK 465     SER A   -17                                                      
REMARK 465     SER A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     HIS A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     SER A    -8                                                      
REMARK 465     GLY A    -7                                                      
REMARK 465     LEU A    -6                                                      
REMARK 465     VAL A    -5                                                      
REMARK 465     PRO A    -4                                                      
REMARK 465     ARG A    -3                                                      
REMARK 465     GLY A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     THR A     3                                                      
REMARK 465     THR A     4                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  63       76.01   -163.62                                   
REMARK 500    VAL A 112      -68.12    -91.82                                   
REMARK 500    MET A 113       -9.59    -56.83                                   
REMARK 500    LYS A 121      -89.40    -57.51                                   
REMARK 500    ASN A 122       43.06    -73.13                                   
REMARK 500    ASP A 124      -17.25     66.17                                   
REMARK 500    SER A 125       50.14   -112.09                                   
REMARK 500    ASN A 218        1.47    -62.96                                   
REMARK 500    LEU A 222      -69.08    -28.67                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GSH A 300                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3QAV   RELATED DB: PDB                                   
DBREF  3QAW A    1   223  UNP    B9VX79   B9VX79_9BIVA     1    223             
SEQADV 3QAW MET A  -19  UNP  B9VX79              EXPRESSION TAG                 
SEQADV 3QAW GLY A  -18  UNP  B9VX79              EXPRESSION TAG                 
SEQADV 3QAW SER A  -17  UNP  B9VX79              EXPRESSION TAG                 
SEQADV 3QAW SER A  -16  UNP  B9VX79              EXPRESSION TAG                 
SEQADV 3QAW HIS A  -15  UNP  B9VX79              EXPRESSION TAG                 
SEQADV 3QAW HIS A  -14  UNP  B9VX79              EXPRESSION TAG                 
SEQADV 3QAW HIS A  -13  UNP  B9VX79              EXPRESSION TAG                 
SEQADV 3QAW HIS A  -12  UNP  B9VX79              EXPRESSION TAG                 
SEQADV 3QAW HIS A  -11  UNP  B9VX79              EXPRESSION TAG                 
SEQADV 3QAW HIS A  -10  UNP  B9VX79              EXPRESSION TAG                 
SEQADV 3QAW SER A   -9  UNP  B9VX79              EXPRESSION TAG                 
SEQADV 3QAW SER A   -8  UNP  B9VX79              EXPRESSION TAG                 
SEQADV 3QAW GLY A   -7  UNP  B9VX79              EXPRESSION TAG                 
SEQADV 3QAW LEU A   -6  UNP  B9VX79              EXPRESSION TAG                 
SEQADV 3QAW VAL A   -5  UNP  B9VX79              EXPRESSION TAG                 
SEQADV 3QAW PRO A   -4  UNP  B9VX79              EXPRESSION TAG                 
SEQADV 3QAW ARG A   -3  UNP  B9VX79              EXPRESSION TAG                 
SEQADV 3QAW GLY A   -2  UNP  B9VX79              EXPRESSION TAG                 
SEQADV 3QAW SER A   -1  UNP  B9VX79              EXPRESSION TAG                 
SEQADV 3QAW HIS A    0  UNP  B9VX79              EXPRESSION TAG                 
SEQRES   1 A  243  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  243  LEU VAL PRO ARG GLY SER HIS MET ALA THR THR SER LYS          
SEQRES   3 A  243  PRO PHE VAL TYR TRP GLY SER GLY SER PRO PRO CYS TRP          
SEQRES   4 A  243  LYS VAL LEU LEU VAL LEU GLN GLU LYS LYS ILE ASP TYR          
SEQRES   5 A  243  ASP GLU LYS ILE ILE SER PHE SER LYS LYS GLU HIS LYS          
SEQRES   6 A  243  SER GLU GLU ILE LEU GLU LEU ASN PRO ARG GLY GLN VAL          
SEQRES   7 A  243  PRO THR PHE THR ASP GLY ASP VAL VAL VAL ASN GLU SER          
SEQRES   8 A  243  THR ALA ILE CYS MET TYR LEU GLU GLU LYS TYR PRO LYS          
SEQRES   9 A  243  VAL PRO LEU PHE PRO SER ASP THR THR ILE ARG ALA LYS          
SEQRES  10 A  243  VAL TYR GLN ARG MET PHE GLU THR SER ASN ILE SER THR          
SEQRES  11 A  243  ASN VAL MET GLU PHE VAL GLN TYR LYS MET LYS ASN LYS          
SEQRES  12 A  243  ASP SER ILE ASP GLN VAL LEU LEU LYS GLU LYS LYS ASP          
SEQRES  13 A  243  LYS ALA HIS VAL GLU LEU GLY HIS TRP GLU ASN TYR LEU          
SEQRES  14 A  243  LYS GLN THR GLY GLY PHE VAL ALA THR LYS GLU PHE THR          
SEQRES  15 A  243  MET ALA ASP VAL PHE PHE PHE PRO MET VAL ALA LEU ILE          
SEQRES  16 A  243  VAL ARG GLN GLY ALA ASN LEU LYS ASP SER TYR PRO ASN          
SEQRES  17 A  243  ILE PHE LYS TYR TYR ASN MET MET MET ASP ARG PRO THR          
SEQRES  18 A  243  ILE VAL LYS THR MET PRO PRO HIS TRP ALA GLU SER ASP          
SEQRES  19 A  243  SER PRO GLY ASN LEU LEU ASP LEU CYS                          
HET    GSH  A 300      20                                                       
HETNAM     GSH GLUTATHIONE                                                      
FORMUL   2  GSH    C10 H17 N3 O6 S                                              
FORMUL   3  HOH   *130(H2 O)                                                    
HELIX    1   1 SER A   15  LYS A   28  1                                  14    
HELIX    2   2 LYS A   42  LYS A   45  5                                   4    
HELIX    3   3 SER A   46  ASN A   53  1                                   8    
HELIX    4   4 GLU A   70  TYR A   82  1                                  13    
HELIX    5   5 ASP A   91  THR A  105  1                                  15    
HELIX    6   6 THR A  105  VAL A  112  1                                   8    
HELIX    7   7 VAL A  112  LYS A  121  1                                  10    
HELIX    8   8 ASP A  127  GLY A  153  1                                  27    
HELIX    9   9 THR A  162  GLN A  178  1                                  17    
HELIX   10  10 ASN A  181  TYR A  186  1                                   6    
HELIX   11  11 TYR A  186  ASP A  198  1                                  13    
HELIX   12  12 ARG A  199  THR A  205  1                                   7    
SHEET    1   A 4 ASP A  33  ILE A  36  0                                        
SHEET    2   A 4 PHE A   8  TRP A  11  1  N  VAL A   9   O  ASP A  33           
SHEET    3   A 4 THR A  60  ASP A  63 -1  O  THR A  60   N  TYR A  10           
SHEET    4   A 4 VAL A  66  VAL A  68 -1  O  VAL A  68   N  PHE A  61           
CISPEP   1 VAL A   58    PRO A   59          0         0.44                     
SITE     1 AC1 12 SER A  15  PRO A  17  HIS A  44  LYS A  45                    
SITE     2 AC1 12 GLY A  56  GLN A  57  VAL A  58  GLU A  70                    
SITE     3 AC1 12 SER A  71  HOH A 225  HOH A 228  HOH A 269                    
CRYST1   90.393   57.611   55.449  90.00 123.84  90.00 C 1 2 1       4          
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      0.011063  0.000000  0.007417        0.00000                         
SCALE2      0.000000  0.017358  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.021713        0.00000                         
ATOM      1  N   SER A   5      34.628  70.250  38.023  1.00 45.07           N  
ATOM      2  CA  SER A   5      34.276  68.842  38.370  1.00 43.26           C  
ATOM      3  C   SER A   5      33.562  68.114  37.237  1.00 42.15           C  
ATOM      4  O   SER A   5      32.568  68.604  36.694  1.00 42.93           O  
ATOM      5  CB  SER A   5      33.387  68.807  39.608  1.00 44.64           C  
ATOM      6  OG  SER A   5      32.891  67.497  39.821  1.00 45.08           O  
ATOM      7  N   LYS A   6      34.069  66.934  36.899  1.00 38.52           N  
ATOM      8  CA  LYS A   6      33.497  66.125  35.838  1.00 34.67           C  
ATOM      9  C   LYS A   6      33.215  64.724  36.382  1.00 33.69           C  
ATOM     10  O   LYS A   6      34.107  64.063  36.919  1.00 32.14           O  
ATOM     11  CB  LYS A   6      34.473  66.071  34.662  1.00 34.36           C  
ATOM     12  CG  LYS A   6      33.967  65.346  33.431  1.00 34.13           C  
ATOM     13  CD  LYS A   6      34.935  65.529  32.269  1.00 34.51           C  
ATOM     14  CE  LYS A   6      34.525  64.702  31.060  1.00 35.28           C  
ATOM     15  NZ  LYS A   6      35.372  64.988  29.870  1.00 35.74           N  
ATOM     16  N   PRO A   7      31.956  64.263  36.269  1.00 31.73           N  
ATOM     17  CA  PRO A   7      31.524  62.940  36.742  1.00 29.47           C  
ATOM     18  C   PRO A   7      32.268  61.778  36.092  1.00 27.43           C  
ATOM     19  O   PRO A   7      32.692  61.868  34.942  1.00 27.62           O  
ATOM     20  CB  PRO A   7      30.036  62.918  36.394  1.00 29.40           C  
ATOM     21  CG  PRO A   7      29.645  64.352  36.522  1.00 30.59           C  
ATOM     22  CD  PRO A   7      30.797  65.063  35.837  1.00 30.97           C  
ATOM     23  N   PHE A   8      32.433  60.695  36.845  1.00 25.71           N  
ATOM     24  CA  PHE A   8      33.084  59.492  36.346  1.00 24.31           C  
ATOM     25  C   PHE A   8      32.214  58.319  36.769  1.00 23.70           C  
ATOM     26  O   PHE A   8      31.830  58.205  37.933  1.00 22.97           O  
ATOM     27  CB  PHE A   8      34.495  59.334  36.921  1.00 24.45           C  
ATOM     28  CG  PHE A   8      35.259  58.173  36.331  1.00 22.94           C  
ATOM     29  CD1 PHE A   8      34.904  56.863  36.628  1.00 23.10           C  
ATOM     30  CD2 PHE A   8      36.322  58.396  35.467  1.00 24.22           C  
ATOM     31  CE1 PHE A   8      35.596  55.790  36.073  1.00 26.89           C  
ATOM     32  CE2 PHE A   8      37.023  57.331  34.905  1.00 26.08           C  
ATOM     33  CZ  PHE A   8      36.660  56.024  35.210  1.00 26.19           C  
ATOM     34  N   VAL A   9      31.908  57.441  35.822  1.00 23.42           N  
ATOM     35  CA  VAL A   9      31.050  56.302  36.107  1.00 22.65           C  
ATOM     36  C   VAL A   9      31.588  54.968  35.589  1.00 21.56           C  
ATOM     37  O   VAL A   9      31.876  54.835  34.399  1.00 21.74           O  
ATOM     38  CB  VAL A   9      29.629  56.558  35.519  1.00 22.38           C  
ATOM     39  CG1 VAL A   9      29.751  57.162  34.135  1.00 24.38           C  
ATOM     40  CG2 VAL A   9      28.832  55.263  35.450  1.00 22.52           C  
ATOM     41  N   TYR A  10      31.738  54.000  36.495  1.00 19.32           N  
ATOM     42  CA  TYR A  10      32.189  52.654  36.136  1.00 18.91           C  
ATOM     43  C   TYR A  10      30.900  51.883  35.931  1.00 19.06           C  
ATOM     44  O   TYR A  10      30.039  51.888  36.808  1.00 18.02           O  
ATOM     45  CB  TYR A  10      32.945  51.954  37.274  1.00 20.78           C  
ATOM     46  CG  TYR A  10      34.228  52.599  37.739  1.00 23.76           C  
ATOM     47  CD1 TYR A  10      34.208  53.673  38.630  1.00 23.31           C  
ATOM     48  CD2 TYR A  10      35.469  52.119  37.304  1.00 24.02           C  
ATOM     49  CE1 TYR A  10      35.385  54.249  39.077  1.00 25.99           C  
ATOM     50  CE2 TYR A  10      36.655  52.690  37.744  1.00 24.96           C  
ATOM     51  CZ  TYR A  10      36.606  53.755  38.629  1.00 25.24           C  
ATOM     52  OH  TYR A  10      37.769  54.336  39.062  1.00 27.02           O  
ATOM     53  N   TRP A  11      30.764  51.207  34.798  1.00 19.15           N  
ATOM     54  CA  TRP A  11      29.546  50.454  34.533  1.00 17.47           C  
ATOM     55  C   TRP A  11      29.787  49.274  33.609  1.00 17.30           C  
ATOM     56  O   TRP A  11      30.811  49.192  32.941  1.00 16.39           O  
ATOM     57  CB  TRP A  11      28.484  51.368  33.926  1.00 17.41           C  
ATOM     58  CG  TRP A  11      28.893  52.006  32.642  1.00 16.22           C  
ATOM     59  CD1 TRP A  11      29.660  53.124  32.486  1.00 17.32           C  
ATOM     60  CD2 TRP A  11      28.526  51.583  31.323  1.00 18.14           C  
ATOM     61  NE1 TRP A  11      29.787  53.431  31.146  1.00 19.01           N  
ATOM     62  CE2 TRP A  11      29.102  52.500  30.411  1.00 18.12           C  
ATOM     63  CE3 TRP A  11      27.764  50.518  30.820  1.00 18.23           C  
ATOM     64  CZ2 TRP A  11      28.940  52.385  29.026  1.00 17.45           C  
ATOM     65  CZ3 TRP A  11      27.600  50.404  29.436  1.00 17.34           C  
ATOM     66  CH2 TRP A  11      28.187  51.333  28.559  1.00 17.47           C  
ATOM     67  N   GLY A  12      28.819  48.368  33.567  1.00 18.70           N  
ATOM     68  CA  GLY A  12      28.945  47.192  32.730  1.00 19.48           C  
ATOM     69  C   GLY A  12      27.800  47.091  31.753  1.00 21.21           C  
ATOM     70  O   GLY A  12      26.812  47.817  31.864  1.00 21.67           O  
ATOM     71  N   SER A  13      27.935  46.171  30.804  1.00 20.05           N  
ATOM     72  CA  SER A  13      26.939  45.959  29.771  1.00 19.86           C  
ATOM     73  C   SER A  13      25.743  45.116  30.205  1.00 20.19           C  
ATOM     74  O   SER A  13      25.902  44.061  30.812  1.00 20.40           O  
ATOM     75  CB  SER A  13      27.610  45.305  28.555  1.00 18.28           C  
ATOM     76  OG  SER A  13      26.708  45.174  27.475  1.00 17.22           O  
ATOM     77  N   GLY A  14      24.543  45.595  29.886  1.00 21.87           N  
ATOM     78  CA  GLY A  14      23.331  44.855  30.199  1.00 20.41           C  
ATOM     79  C   GLY A  14      22.785  44.985  31.604  1.00 21.07           C  
ATOM     80  O   GLY A  14      21.892  44.230  31.991  1.00 20.24           O  
ATOM     81  N   SER A  15      23.307  45.954  32.352  1.00 19.82           N  
ATOM     82  CA  SER A  15      22.896  46.203  33.730  1.00 16.71           C  
ATOM     83  C   SER A  15      21.928  47.373  33.883  1.00 15.84           C  
ATOM     84  O   SER A  15      22.303  48.521  33.650  1.00 15.59           O  
ATOM     85  CB  SER A  15      24.136  46.480  34.584  1.00 15.97           C  
ATOM     86  OG  SER A  15      23.789  47.164  35.773  1.00 17.19           O  
ATOM     87  N   PRO A  16      20.677  47.102  34.299  1.00 14.88           N  
ATOM     88  CA  PRO A  16      19.679  48.168  34.480  1.00 14.86           C  
ATOM     89  C   PRO A  16      20.134  49.263  35.464  1.00 15.30           C  
ATOM     90  O   PRO A  16      19.865  50.461  35.255  1.00 15.61           O  
ATOM     91  CB  PRO A  16      18.446  47.409  34.963  1.00 15.78           C  
ATOM     92  CG  PRO A  16      18.587  46.063  34.257  1.00 13.38           C  
ATOM     93  CD  PRO A  16      20.064  45.770  34.469  1.00 14.59           C  
ATOM     94  N   PRO A  17      20.810  48.878  36.559  1.00 13.40           N  
ATOM     95  CA  PRO A  17      21.250  49.932  37.483  1.00 13.89           C  
ATOM     96  C   PRO A  17      22.198  50.930  36.783  1.00 13.43           C  
ATOM     97  O   PRO A  17      22.120  52.139  37.010  1.00 13.93           O  
ATOM     98  CB  PRO A  17      21.943  49.150  38.592  1.00 11.46           C  
ATOM     99  CG  PRO A  17      21.138  47.885  38.641  1.00 12.51           C  
ATOM    100  CD  PRO A  17      20.950  47.546  37.176  1.00 14.61           C  
ATOM    101  N   CYS A  18      23.075  50.414  35.923  1.00 12.07           N  
ATOM    102  CA  CYS A  18      24.020  51.245  35.194  1.00 12.76           C  
ATOM    103  C   CYS A  18      23.316  52.070  34.118  1.00 14.55           C  
ATOM    104  O   CYS A  18      23.633  53.243  33.912  1.00 14.12           O  
ATOM    105  CB  CYS A  18      25.107  50.375  34.550  1.00 12.04           C  
ATOM    106  SG  CYS A  18      26.216  49.515  35.723  1.00 13.94           S  
ATOM    107  N   TRP A  19      22.359  51.447  33.436  1.00 14.88           N  
ATOM    108  CA  TRP A  19      21.603  52.106  32.376  1.00 15.72           C  
ATOM    109  C   TRP A  19      20.885  53.328  32.944  1.00 14.23           C  
ATOM    110  O   TRP A  19      20.904  54.397  32.336  1.00 16.22           O  
ATOM    111  CB  TRP A  19      20.588  51.125  31.771  1.00 15.58           C  
ATOM    112  CG  TRP A  19      20.216  51.411  30.336  1.00 16.69           C  
ATOM    113  CD1 TRP A  19      20.218  52.630  29.710  1.00 16.84           C  
ATOM    114  CD2 TRP A  19      19.698  50.472  29.380  1.00 15.43           C  
ATOM    115  NE1 TRP A  19      19.726  52.506  28.435  1.00 17.61           N  
ATOM    116  CE2 TRP A  19      19.400  51.195  28.204  1.00 17.34           C  
ATOM    117  CE3 TRP A  19      19.455  49.092  29.406  1.00 15.15           C  
ATOM    118  CZ2 TRP A  19      18.870  50.584  27.057  1.00 16.66           C  
ATOM    119  CZ3 TRP A  19      18.928  48.480  28.264  1.00 16.98           C  
ATOM    120  CH2 TRP A  19      18.641  49.233  27.104  1.00 16.72           C  
ATOM    121  N   LYS A  20      20.260  53.174  34.109  1.00 13.21           N  
ATOM    122  CA  LYS A  20      19.559  54.292  34.756  1.00 13.61           C  
ATOM    123  C   LYS A  20      20.472  55.503  34.833  1.00 12.48           C  
ATOM    124  O   LYS A  20      20.094  56.612  34.471  1.00 13.86           O  
ATOM    125  CB  LYS A  20      19.132  53.927  36.190  1.00 14.33           C  
ATOM    126  CG  LYS A  20      17.974  52.948  36.301  1.00  9.56           C  
ATOM    127  CD  LYS A  20      17.919  52.300  37.687  1.00 14.41           C  
ATOM    128  CE  LYS A  20      17.644  53.305  38.799  1.00 15.75           C  
ATOM    129  NZ  LYS A  20      17.622  52.656  40.155  1.00 17.86           N  
ATOM    130  N   VAL A  21      21.683  55.275  35.320  1.00 14.74           N  
ATOM    131  CA  VAL A  21      22.672  56.334  35.474  1.00 12.47           C  
ATOM    132  C   VAL A  21      23.091  56.954  34.143  1.00 14.31           C  
ATOM    133  O   VAL A  21      23.234  58.175  34.044  1.00 13.43           O  
ATOM    134  CB  VAL A  21      23.922  55.796  36.186  1.00 13.01           C  
ATOM    135  CG1 VAL A  21      24.956  56.901  36.339  1.00 12.14           C  
ATOM    136  CG2 VAL A  21      23.521  55.218  37.545  1.00 11.32           C  
ATOM    137  N   LEU A  22      23.288  56.113  33.125  1.00 14.32           N  
ATOM    138  CA  LEU A  22      23.695  56.608  31.817  1.00 17.59           C  
ATOM    139  C   LEU A  22      22.596  57.444  31.186  1.00 17.36           C  
ATOM    140  O   LEU A  22      22.875  58.491  30.604  1.00 19.76           O  
ATOM    141  CB  LEU A  22      24.084  55.451  30.896  1.00 16.72           C  
ATOM    142  CG  LEU A  22      25.364  54.711  31.322  1.00 18.01           C  
ATOM    143  CD1 LEU A  22      25.673  53.602  30.322  1.00 14.57           C  
ATOM    144  CD2 LEU A  22      26.535  55.690  31.413  1.00 16.80           C  
ATOM    145  N   LEU A  23      21.350  56.996  31.318  1.00 16.51           N  
ATOM    146  CA  LEU A  23      20.225  57.735  30.761  1.00 16.60           C  
ATOM    147  C   LEU A  23      20.152  59.117  31.396  1.00 16.19           C  
ATOM    148  O   LEU A  23      20.066  60.129  30.701  1.00 15.04           O  
ATOM    149  CB  LEU A  23      18.911  56.994  30.999  1.00 16.93           C  
ATOM    150  CG  LEU A  23      18.597  55.806  30.099  1.00 20.34           C  
ATOM    151  CD1 LEU A  23      17.244  55.239  30.498  1.00 19.68           C  
ATOM    152  CD2 LEU A  23      18.580  56.248  28.629  1.00 20.52           C  
ATOM    153  N   VAL A  24      20.189  59.158  32.722  1.00 17.16           N  
ATOM    154  CA  VAL A  24      20.129  60.434  33.435  1.00 16.61           C  
ATOM    155  C   VAL A  24      21.211  61.374  32.921  1.00 18.53           C  
ATOM    156  O   VAL A  24      20.934  62.531  32.597  1.00 19.33           O  
ATOM    157  CB  VAL A  24      20.322  60.237  34.947  1.00 16.07           C  
ATOM    158  CG1 VAL A  24      20.459  61.587  35.639  1.00 14.40           C  
ATOM    159  CG2 VAL A  24      19.153  59.445  35.513  1.00 12.10           C  
ATOM    160  N   LEU A  25      22.443  60.867  32.849  1.00 18.67           N  
ATOM    161  CA  LEU A  25      23.586  61.648  32.367  1.00 16.62           C  
ATOM    162  C   LEU A  25      23.391  62.198  30.960  1.00 16.09           C  
ATOM    163  O   LEU A  25      23.662  63.368  30.705  1.00 14.04           O  
ATOM    164  CB  LEU A  25      24.854  60.797  32.403  1.00 15.12           C  
ATOM    165  CG  LEU A  25      25.466  60.624  33.791  1.00 16.51           C  
ATOM    166  CD1 LEU A  25      26.535  59.536  33.742  1.00 17.37           C  
ATOM    167  CD2 LEU A  25      26.051  61.959  34.268  1.00 12.83           C  
ATOM    168  N   GLN A  26      22.932  61.340  30.054  1.00 17.70           N  
ATOM    169  CA  GLN A  26      22.684  61.711  28.660  1.00 20.11           C  
ATOM    170  C   GLN A  26      21.509  62.683  28.524  1.00 20.97           C  
ATOM    171  O   GLN A  26      21.614  63.717  27.872  1.00 21.13           O  
ATOM    172  CB  GLN A  26      22.381  60.458  27.844  1.00 22.02           C  
ATOM    173  CG  GLN A  26      23.495  59.433  27.844  1.00 26.88           C  
ATOM    174  CD  GLN A  26      24.556  59.741  26.820  1.00 27.87           C  
ATOM    175  OE1 GLN A  26      25.665  59.217  26.886  1.00 31.18           O  
ATOM    176  NE2 GLN A  26      24.217  60.584  25.854  1.00 27.75           N  
ATOM    177  N   GLU A  27      20.388  62.330  29.141  1.00 22.02           N  
ATOM    178  CA  GLU A  27      19.186  63.148  29.100  1.00 24.21           C  
ATOM    179  C   GLU A  27      19.426  64.561  29.603  1.00 25.38           C  
ATOM    180  O   GLU A  27      18.839  65.516  29.096  1.00 28.23           O  
ATOM    181  CB  GLU A  27      18.082  62.481  29.920  1.00 23.17           C  
ATOM    182  CG  GLU A  27      17.555  61.200  29.286  1.00 24.98           C  
ATOM    183  CD  GLU A  27      16.582  61.470  28.154  1.00 24.92           C  
ATOM    184  OE1 GLU A  27      16.149  60.506  27.481  1.00 23.10           O  
ATOM    185  OE2 GLU A  27      16.239  62.651  27.948  1.00 25.97           O  
ATOM    186  N   LYS A  28      20.284  64.701  30.604  1.00 24.49           N  
ATOM    187  CA  LYS A  28      20.575  66.019  31.135  1.00 24.06           C  
ATOM    188  C   LYS A  28      21.779  66.585  30.396  1.00 24.73           C  
ATOM    189  O   LYS A  28      22.210  67.702  30.659  1.00 26.29           O  
ATOM    190  CB  LYS A  28      20.822  65.929  32.642  1.00 23.87           C  
ATOM    191  CG  LYS A  28      19.645  65.283  33.380  1.00 24.75           C  
ATOM    192  CD  LYS A  28      19.893  65.112  34.870  1.00 24.32           C  
ATOM    193  CE  LYS A  28      19.934  66.446  35.585  1.00 24.28           C  
ATOM    194  NZ  LYS A  28      18.637  67.189  35.581  1.00 21.29           N  
ATOM    195  N   LYS A  29      22.309  65.797  29.463  1.00 24.40           N  
ATOM    196  CA  LYS A  29      23.448  66.199  28.640  1.00 26.16           C  
ATOM    197  C   LYS A  29      24.689  66.612  29.425  1.00 26.17           C  
ATOM    198  O   LYS A  29      25.361  67.584  29.085  1.00 26.53           O  
ATOM    199  CB  LYS A  29      23.027  67.332  27.691  1.00 28.32           C  
ATOM    200  CG  LYS A  29      22.026  66.899  26.617  1.00 30.79           C  
ATOM    201  CD  LYS A  29      21.570  68.059  25.737  1.00 34.76           C  
ATOM    202  CE  LYS A  29      20.563  68.952  26.460  1.00 37.15           C  
ATOM    203  NZ  LYS A  29      19.267  68.251  26.708  1.00 37.66           N  
ATOM    204  N   ILE A  30      24.994  65.855  30.472  1.00 27.21           N  
ATOM    205  CA  ILE A  30      26.161  66.115  31.307  1.00 26.42           C  
ATOM    206  C   ILE A  30      27.339  65.347  30.721  1.00 27.40           C  
ATOM    207  O   ILE A  30      27.235  64.148  30.462  1.00 28.70           O  
ATOM    208  CB  ILE A  30      25.928  65.617  32.738  1.00 25.53           C  
ATOM    209  CG1 ILE A  30      24.694  66.299  33.332  1.00 23.88           C  
ATOM    210  CG2 ILE A  30      27.155  65.886  33.584  1.00 24.50           C  
ATOM    211  CD1 ILE A  30      24.030  65.489  34.424  1.00 23.09           C  
ATOM    212  N   ASP A  31      28.454  66.037  30.511  1.00 27.43           N  
ATOM    213  CA  ASP A  31      29.655  65.415  29.957  1.00 27.78           C  
ATOM    214  C   ASP A  31      30.327  64.631  31.081  1.00 27.57           C  
ATOM    215  O   ASP A  31      30.669  65.200  32.123  1.00 27.27           O  
ATOM    216  CB  ASP A  31      30.602  66.501  29.435  1.00 30.09           C  
ATOM    217  CG  ASP A  31      31.801  65.940  28.670  1.00 33.27           C  
ATOM    218  OD1 ASP A  31      32.773  66.703  28.495  1.00 35.86           O  
ATOM    219  OD2 ASP A  31      31.788  64.764  28.225  1.00 35.09           O  
ATOM    220  N   TYR A  32      30.519  63.332  30.873  1.00 25.04           N  
ATOM    221  CA  TYR A  32      31.141  62.489  31.893  1.00 25.00           C  
ATOM    222  C   TYR A  32      32.234  61.566  31.374  1.00 24.68           C  
ATOM    223  O   TYR A  32      32.335  61.320  30.173  1.00 25.16           O  
ATOM    224  CB  TYR A  32      30.080  61.627  32.575  1.00 21.86           C  
ATOM    225  CG  TYR A  32      29.319  60.743  31.613  1.00 21.17           C  
ATOM    226  CD1 TYR A  32      28.267  61.249  30.851  1.00 18.39           C  
ATOM    227  CD2 TYR A  32      29.644  59.395  31.475  1.00 19.52           C  
ATOM    228  CE1 TYR A  32      27.556  60.434  29.984  1.00 18.53           C  
ATOM    229  CE2 TYR A  32      28.940  58.570  30.608  1.00 19.33           C  
ATOM    230  CZ  TYR A  32      27.894  59.093  29.868  1.00 19.42           C  
ATOM    231  OH  TYR A  32      27.177  58.263  29.028  1.00 17.70           O  
ATOM    232  N   ASP A  33      33.046  61.065  32.302  1.00 25.04           N  
ATOM    233  CA  ASP A  33      34.122  60.129  31.997  1.00 24.72           C  
ATOM    234  C   ASP A  33      33.598  58.758  32.399  1.00 24.80           C  
ATOM    235  O   ASP A  33      32.766  58.645  33.298  1.00 21.90           O  
ATOM    236  CB  ASP A  33      35.387  60.432  32.809  1.00 25.06           C  
ATOM    237  CG  ASP A  33      36.118  61.670  32.329  1.00 28.63           C  
ATOM    238  OD1 ASP A  33      36.220  61.878  31.100  1.00 29.61           O  
ATOM    239  OD2 ASP A  33      36.614  62.431  33.183  1.00 30.61           O  
ATOM    240  N   GLU A  34      34.099  57.712  31.758  1.00 24.89           N  
ATOM    241  CA  GLU A  34      33.617  56.387  32.075  1.00 24.74           C  
ATOM    242  C   GLU A  34      34.670  55.305  31.944  1.00 25.06           C  
ATOM    243  O   GLU A  34      35.715  55.488  31.317  1.00 27.13           O  
ATOM    244  CB  GLU A  34      32.455  56.034  31.146  1.00 25.07           C  
ATOM    245  CG  GLU A  34      32.936  55.607  29.756  1.00 24.42           C  
ATOM    246  CD  GLU A  34      31.815  55.392  28.764  1.00 22.28           C  
ATOM    247  OE1 GLU A  34      30.670  55.158  29.197  1.00 23.46           O  
ATOM    248  OE2 GLU A  34      32.087  55.446  27.549  1.00 22.85           O  
ATOM    249  N   LYS A  35      34.359  54.167  32.545  1.00 25.62           N  
ATOM    250  CA  LYS A  35      35.191  52.987  32.484  1.00 25.80           C  
ATOM    251  C   LYS A  35      34.201  51.842  32.259  1.00 25.08           C  
ATOM    252  O   LYS A  35      33.414  51.514  33.145  1.00 23.85           O  
ATOM    253  CB  LYS A  35      35.952  52.795  33.792  1.00 27.43           C  
ATOM    254  CG  LYS A  35      37.010  51.701  33.734  1.00 30.85           C  
ATOM    255  CD  LYS A  35      37.952  51.915  32.559  1.00 33.69           C  
ATOM    256  CE  LYS A  35      39.242  51.108  32.711  1.00 36.91           C  
ATOM    257  NZ  LYS A  35      40.098  51.635  33.813  1.00 35.60           N  
ATOM    258  N   ILE A  36      34.208  51.273  31.056  1.00 23.86           N  
ATOM    259  CA  ILE A  36      33.311  50.170  30.744  1.00 24.24           C  
ATOM    260  C   ILE A  36      34.038  48.916  31.175  1.00 24.79           C  
ATOM    261  O   ILE A  36      35.020  48.495  30.546  1.00 26.51           O  
ATOM    262  CB  ILE A  36      32.985  50.085  29.237  1.00 24.29           C  
ATOM    263  CG1 ILE A  36      32.432  51.430  28.742  1.00 26.22           C  
ATOM    264  CG2 ILE A  36      31.940  48.999  29.002  1.00 25.73           C  
ATOM    265  CD1 ILE A  36      32.062  51.461  27.251  1.00 24.75           C  
ATOM    266  N   ILE A  37      33.560  48.326  32.265  1.00 23.37           N  
ATOM    267  CA  ILE A  37      34.190  47.144  32.817  1.00 19.93           C  
ATOM    268  C   ILE A  37      33.631  45.857  32.254  1.00 19.30           C  
ATOM    269  O   ILE A  37      32.525  45.823  31.718  1.00 18.92           O  
ATOM    270  CB  ILE A  37      34.085  47.153  34.365  1.00 19.44           C  
ATOM    271  CG1 ILE A  37      32.623  47.032  34.822  1.00 18.99           C  
ATOM    272  CG2 ILE A  37      34.665  48.457  34.903  1.00 18.11           C  
ATOM    273  CD1 ILE A  37      32.067  45.614  34.833  1.00 14.73           C  
ATOM    274  N   SER A  38      34.420  44.797  32.364  1.00 19.28           N  
ATOM    275  CA  SER A  38      34.006  43.491  31.896  1.00 21.76           C  
ATOM    276  C   SER A  38      33.568  42.632  33.078  1.00 22.92           C  
ATOM    277  O   SER A  38      34.357  42.371  33.984  1.00 24.87           O  
ATOM    278  CB  SER A  38      35.162  42.800  31.167  1.00 23.10           C  
ATOM    279  OG  SER A  38      34.863  41.436  30.913  1.00 25.31           O  
ATOM    280  N   PHE A  39      32.307  42.208  33.070  1.00 22.97           N  
ATOM    281  CA  PHE A  39      31.777  41.351  34.118  1.00 22.22           C  
ATOM    282  C   PHE A  39      32.398  39.968  33.996  1.00 24.69           C  
ATOM    283  O   PHE A  39      32.832  39.384  34.992  1.00 27.24           O  
ATOM    284  CB  PHE A  39      30.264  41.199  33.985  1.00 21.08           C  
ATOM    285  CG  PHE A  39      29.481  42.383  34.462  1.00 21.95           C  
ATOM    286  CD1 PHE A  39      29.519  42.768  35.800  1.00 19.89           C  
ATOM    287  CD2 PHE A  39      28.675  43.097  33.579  1.00 22.02           C  
ATOM    288  CE1 PHE A  39      28.766  43.843  36.252  1.00 19.56           C  
ATOM    289  CE2 PHE A  39      27.915  44.174  34.023  1.00 23.15           C  
ATOM    290  CZ  PHE A  39      27.962  44.547  35.364  1.00 22.25           C  
ATOM    291  N   SER A  40      32.430  39.438  32.773  1.00 25.47           N  
ATOM    292  CA  SER A  40      32.980  38.104  32.544  1.00 27.58           C  
ATOM    293  C   SER A  40      34.420  37.993  33.033  1.00 27.67           C  
ATOM    294  O   SER A  40      34.865  36.919  33.446  1.00 28.95           O  
ATOM    295  CB  SER A  40      32.893  37.726  31.060  1.00 28.21           C  
ATOM    296  OG  SER A  40      33.734  38.536  30.263  1.00 33.21           O  
ATOM    297  N   LYS A  41      35.144  39.107  32.984  1.00 27.12           N  
ATOM    298  CA  LYS A  41      36.523  39.145  33.442  1.00 25.94           C  
ATOM    299  C   LYS A  41      36.572  39.687  34.877  1.00 25.68           C  
ATOM    300  O   LYS A  41      37.644  40.022  35.399  1.00 24.83           O  
ATOM    301  CB  LYS A  41      37.365  40.006  32.493  1.00 28.00           C  
ATOM    302  CG  LYS A  41      37.476  39.408  31.089  1.00 29.80           C  
ATOM    303  CD  LYS A  41      37.878  40.434  30.029  1.00 31.09           C  
ATOM    304  CE  LYS A  41      37.660  39.863  28.630  1.00 31.82           C  
ATOM    305  NZ  LYS A  41      37.841  40.861  27.532  1.00 31.36           N  
ATOM    306  N   LYS A  42      35.394  39.770  35.497  1.00 24.06           N  
ATOM    307  CA  LYS A  42      35.243  40.226  36.879  1.00 24.96           C  
ATOM    308  C   LYS A  42      35.866  41.574  37.202  1.00 23.82           C  
ATOM    309  O   LYS A  42      36.414  41.751  38.284  1.00 23.36           O  
ATOM    310  CB  LYS A  42      35.834  39.188  37.839  1.00 26.82           C  
ATOM    311  CG  LYS A  42      35.097  37.862  37.888  1.00 29.78           C  
ATOM    312  CD  LYS A  42      35.824  36.870  38.800  1.00 30.65           C  
ATOM    313  CE  LYS A  42      35.866  37.339  40.260  1.00 35.50           C  
ATOM    314  NZ  LYS A  42      34.517  37.386  40.926  1.00 36.38           N  
ATOM    315  N   GLU A  43      35.771  42.530  36.290  1.00 23.74           N  
ATOM    316  CA  GLU A  43      36.365  43.843  36.527  1.00 23.69           C  
ATOM    317  C   GLU A  43      35.601  44.712  37.513  1.00 24.22           C  
ATOM    318  O   GLU A  43      36.096  45.750  37.941  1.00 27.09           O  
ATOM    319  CB  GLU A  43      36.561  44.577  35.196  1.00 24.14           C  
ATOM    320  CG  GLU A  43      37.820  44.124  34.464  1.00 25.11           C  
ATOM    321  CD  GLU A  43      37.846  44.520  33.000  1.00 27.29           C  
ATOM    322  OE1 GLU A  43      37.471  45.666  32.668  1.00 28.39           O  
ATOM    323  OE2 GLU A  43      38.260  43.676  32.180  1.00 28.47           O  
ATOM    324  N   HIS A  44      34.397  44.292  37.879  1.00 24.72           N  
ATOM    325  CA  HIS A  44      33.602  45.035  38.851  1.00 25.31           C  
ATOM    326  C   HIS A  44      34.148  44.766  40.256  1.00 25.34           C  
ATOM    327  O   HIS A  44      33.740  45.404  41.224  1.00 25.23           O  
ATOM    328  CB  HIS A  44      32.133  44.621  38.772  1.00 24.58           C  
ATOM    329  CG  HIS A  44      31.927  43.141  38.721  1.00 24.49           C  
ATOM    330  ND1 HIS A  44      31.139  42.468  39.629  1.00 23.86           N  
ATOM    331  CD2 HIS A  44      32.391  42.206  37.858  1.00 25.47           C  
ATOM    332  CE1 HIS A  44      31.126  41.182  39.327  1.00 24.51           C  
ATOM    333  NE2 HIS A  44      31.877  40.996  38.257  1.00 25.35           N  
ATOM    334  N   LYS A  45      35.077  43.817  40.353  1.00 26.35           N  
ATOM    335  CA  LYS A  45      35.706  43.467  41.628  1.00 25.95           C  
ATOM    336  C   LYS A  45      37.149  43.955  41.688  1.00 25.83           C  
ATOM    337  O   LYS A  45      37.917  43.501  42.532  1.00 26.47           O  
ATOM    338  CB  LYS A  45      35.701  41.948  41.852  1.00 23.85           C  
ATOM    339  CG  LYS A  45      34.316  41.307  41.912  1.00 24.50           C  
ATOM    340  CD  LYS A  45      33.456  41.900  43.017  1.00 22.24           C  
ATOM    341  CE  LYS A  45      32.088  41.239  43.048  1.00 23.63           C  
ATOM    342  NZ  LYS A  45      31.212  41.807  44.109  1.00 21.13           N  
ATOM    343  N   SER A  46      37.532  44.871  40.804  1.00 24.94           N  
ATOM    344  CA  SER A  46      38.907  45.354  40.835  1.00 27.18           C  
ATOM    345  C   SER A  46      39.138  46.122  42.130  1.00 27.86           C  
ATOM    346  O   SER A  46      38.186  46.501  42.816  1.00 28.21           O  
ATOM    347  CB  SER A  46      39.218  46.243  39.618  1.00 26.09           C  
ATOM    348  OG  SER A  46      38.623  47.527  39.720  1.00 28.52           O  
ATOM    349  N   GLU A  47      40.404  46.330  42.473  1.00 28.33           N  
ATOM    350  CA  GLU A  47      40.758  47.051  43.688  1.00 30.25           C  
ATOM    351  C   GLU A  47      40.339  48.507  43.569  1.00 29.24           C  
ATOM    352  O   GLU A  47      39.907  49.134  44.539  1.00 27.92           O  
ATOM    353  CB  GLU A  47      42.268  46.967  43.917  1.00 34.18           C  
ATOM    354  CG  GLU A  47      42.761  45.590  44.311  1.00 38.40           C  
ATOM    355  CD  GLU A  47      42.394  45.231  45.740  1.00 42.97           C  
ATOM    356  OE1 GLU A  47      41.185  45.175  46.059  1.00 43.03           O  
ATOM    357  OE2 GLU A  47      43.321  45.008  46.548  1.00 47.39           O  
ATOM    358  N   GLU A  48      40.489  49.040  42.365  1.00 28.96           N  
ATOM    359  CA  GLU A  48      40.128  50.418  42.073  1.00 28.59           C  
ATOM    360  C   GLU A  48      38.642  50.627  42.365  1.00 26.62           C  
ATOM    361  O   GLU A  48      38.247  51.662  42.905  1.00 25.95           O  
ATOM    362  CB  GLU A  48      40.439  50.712  40.603  1.00 30.30           C  
ATOM    363  CG  GLU A  48      39.981  52.061  40.108  1.00 32.83           C  
ATOM    364  CD  GLU A  48      40.418  52.315  38.681  1.00 33.87           C  
ATOM    365  OE1 GLU A  48      40.135  51.472  37.803  1.00 33.02           O  
ATOM    366  OE2 GLU A  48      41.049  53.363  38.438  1.00 37.96           O  
ATOM    367  N   ILE A  49      37.829  49.634  42.010  1.00 24.06           N  
ATOM    368  CA  ILE A  49      36.385  49.685  42.245  1.00 23.94           C  
ATOM    369  C   ILE A  49      36.058  49.486  43.730  1.00 22.41           C  
ATOM    370  O   ILE A  49      35.181  50.159  44.282  1.00 21.79           O  
ATOM    371  CB  ILE A  49      35.641  48.572  41.473  1.00 24.38           C  
ATOM    372  CG1 ILE A  49      35.810  48.759  39.964  1.00 25.78           C  
ATOM    373  CG2 ILE A  49      34.157  48.571  41.866  1.00 23.20           C  
ATOM    374  CD1 ILE A  49      34.866  49.764  39.364  1.00 23.99           C  
ATOM    375  N   LEU A  50      36.753  48.545  44.363  1.00 19.98           N  
ATOM    376  CA  LEU A  50      36.516  48.254  45.766  1.00 20.62           C  
ATOM    377  C   LEU A  50      36.843  49.410  46.700  1.00 20.43           C  
ATOM    378  O   LEU A  50      36.178  49.585  47.707  1.00 20.88           O  
ATOM    379  CB  LEU A  50      37.275  46.997  46.190  1.00 23.17           C  
ATOM    380  CG  LEU A  50      36.676  45.691  45.654  1.00 26.59           C  
ATOM    381  CD1 LEU A  50      37.516  44.503  46.095  1.00 27.54           C  
ATOM    382  CD2 LEU A  50      35.252  45.543  46.158  1.00 26.47           C  
ATOM    383  N   GLU A  51      37.844  50.218  46.378  1.00 21.55           N  
ATOM    384  CA  GLU A  51      38.154  51.332  47.261  1.00 25.52           C  
ATOM    385  C   GLU A  51      36.969  52.281  47.346  1.00 26.02           C  
ATOM    386  O   GLU A  51      36.663  52.798  48.418  1.00 26.73           O  
ATOM    387  CB  GLU A  51      39.381  52.100  46.778  1.00 28.51           C  
ATOM    388  CG  GLU A  51      40.683  51.384  47.032  1.00 36.46           C  
ATOM    389  CD  GLU A  51      41.882  52.296  46.859  1.00 42.06           C  
ATOM    390  OE1 GLU A  51      43.027  51.801  46.975  1.00 44.09           O  
ATOM    391  OE2 GLU A  51      41.676  53.509  46.613  1.00 43.75           O  
ATOM    392  N   LEU A  52      36.307  52.492  46.209  1.00 25.43           N  
ATOM    393  CA  LEU A  52      35.151  53.380  46.120  1.00 23.87           C  
ATOM    394  C   LEU A  52      33.852  52.705  46.521  1.00 23.13           C  
ATOM    395  O   LEU A  52      32.967  53.335  47.092  1.00 22.43           O  
ATOM    396  CB  LEU A  52      35.001  53.904  44.688  1.00 23.98           C  
ATOM    397  CG  LEU A  52      36.112  54.816  44.152  1.00 25.51           C  
ATOM    398  CD1 LEU A  52      35.854  55.152  42.697  1.00 24.61           C  
ATOM    399  CD2 LEU A  52      36.175  56.085  44.980  1.00 22.52           C  
ATOM    400  N   ASN A  53      33.739  51.418  46.215  1.00 23.62           N  
ATOM    401  CA  ASN A  53      32.525  50.667  46.508  1.00 21.91           C  
ATOM    402  C   ASN A  53      32.859  49.343  47.186  1.00 20.89           C  
ATOM    403  O   ASN A  53      33.226  48.367  46.533  1.00 20.82           O  
ATOM    404  CB  ASN A  53      31.763  50.427  45.194  1.00 20.93           C  
ATOM    405  CG  ASN A  53      30.377  49.837  45.407  1.00 24.15           C  
ATOM    406  OD1 ASN A  53      29.541  49.858  44.494  1.00 24.68           O  
ATOM    407  ND2 ASN A  53      30.125  49.299  46.598  1.00 20.47           N  
ATOM    408  N   PRO A  54      32.744  49.297  48.519  1.00 21.97           N  
ATOM    409  CA  PRO A  54      33.041  48.070  49.263  1.00 20.53           C  
ATOM    410  C   PRO A  54      32.255  46.833  48.810  1.00 20.66           C  
ATOM    411  O   PRO A  54      32.639  45.708  49.122  1.00 23.24           O  
ATOM    412  CB  PRO A  54      32.736  48.467  50.703  1.00 20.91           C  
ATOM    413  CG  PRO A  54      33.129  49.918  50.726  1.00 21.12           C  
ATOM    414  CD  PRO A  54      32.534  50.433  49.438  1.00 19.84           C  
ATOM    415  N   ARG A  55      31.160  47.018  48.083  1.00 18.14           N  
ATOM    416  CA  ARG A  55      30.392  45.858  47.636  1.00 19.22           C  
ATOM    417  C   ARG A  55      30.879  45.299  46.302  1.00 18.92           C  
ATOM    418  O   ARG A  55      30.420  44.247  45.871  1.00 20.62           O  
ATOM    419  CB  ARG A  55      28.903  46.202  47.527  1.00 20.09           C  
ATOM    420  CG  ARG A  55      28.250  46.556  48.855  1.00 20.37           C  
ATOM    421  CD  ARG A  55      26.873  47.174  48.651  1.00 20.85           C  
ATOM    422  NE  ARG A  55      26.244  47.479  49.931  1.00 18.93           N  
ATOM    423  CZ  ARG A  55      25.610  46.591  50.691  1.00 20.07           C  
ATOM    424  NH1 ARG A  55      25.083  46.965  51.848  1.00 17.21           N  
ATOM    425  NH2 ARG A  55      25.475  45.341  50.283  1.00 18.79           N  
ATOM    426  N   GLY A  56      31.800  46.003  45.651  1.00 18.41           N  
ATOM    427  CA  GLY A  56      32.305  45.543  44.371  1.00 18.05           C  
ATOM    428  C   GLY A  56      31.194  45.412  43.346  1.00 19.07           C  
ATOM    429  O   GLY A  56      30.968  44.336  42.785  1.00 18.66           O  
ATOM    430  N   GLN A  57      30.489  46.510  43.103  1.00 16.81           N  
ATOM    431  CA  GLN A  57      29.399  46.499  42.141  1.00 18.39           C  
ATOM    432  C   GLN A  57      29.444  47.730  41.266  1.00 18.31           C  
ATOM    433  O   GLN A  57      30.170  48.688  41.548  1.00 18.23           O  
ATOM    434  CB  GLN A  57      28.034  46.484  42.847  1.00 18.27           C  
ATOM    435  CG  GLN A  57      27.812  45.337  43.815  1.00 21.53           C  
ATOM    436  CD  GLN A  57      26.450  45.405  44.489  1.00 24.75           C  
ATOM    437  OE1 GLN A  57      26.086  46.431  45.076  1.00 24.80           O  
ATOM    438  NE2 GLN A  57      25.692  44.314  44.408  1.00 23.47           N  
ATOM    439  N   VAL A  58      28.667  47.681  40.192  1.00 17.18           N  
ATOM    440  CA  VAL A  58      28.528  48.811  39.290  1.00 17.48           C  
ATOM    441  C   VAL A  58      27.027  49.055  39.230  1.00 17.00           C  
ATOM    442  O   VAL A  58      26.231  48.121  39.329  1.00 19.86           O  
ATOM    443  CB  VAL A  58      29.097  48.532  37.867  1.00 15.68           C  
ATOM    444  CG1 VAL A  58      30.617  48.522  37.924  1.00 15.94           C  
ATOM    445  CG2 VAL A  58      28.575  47.213  37.327  1.00 15.13           C  
ATOM    446  N   PRO A  59      26.621  50.311  39.061  1.00 17.17           N  
ATOM    447  CA  PRO A  59      27.522  51.455  38.922  1.00 18.32           C  
ATOM    448  C   PRO A  59      28.259  51.895  40.192  1.00 18.18           C  
ATOM    449  O   PRO A  59      27.799  51.673  41.312  1.00 17.43           O  
ATOM    450  CB  PRO A  59      26.591  52.540  38.408  1.00 17.68           C  
ATOM    451  CG  PRO A  59      25.346  52.258  39.214  1.00 18.44           C  
ATOM    452  CD  PRO A  59      25.214  50.753  39.061  1.00 16.10           C  
ATOM    453  N   THR A  60      29.425  52.492  39.976  1.00 17.64           N  
ATOM    454  CA  THR A  60      30.258  53.069  41.022  1.00 18.06           C  
ATOM    455  C   THR A  60      30.459  54.447  40.413  1.00 17.27           C  
ATOM    456  O   THR A  60      30.704  54.566  39.216  1.00 17.87           O  
ATOM    457  CB  THR A  60      31.588  52.332  41.190  1.00 19.57           C  
ATOM    458  OG1 THR A  60      31.335  51.027  41.726  1.00 17.91           O  
ATOM    459  CG2 THR A  60      32.490  53.093  42.149  1.00 20.59           C  
ATOM    460  N   PHE A  61      30.357  55.490  41.220  1.00 17.73           N  
ATOM    461  CA  PHE A  61      30.409  56.816  40.649  1.00 17.51           C  
ATOM    462  C   PHE A  61      31.014  57.915  41.521  1.00 17.77           C  
ATOM    463  O   PHE A  61      30.854  57.909  42.740  1.00 18.14           O  
ATOM    464  CB  PHE A  61      28.960  57.134  40.238  1.00 14.38           C  
ATOM    465  CG  PHE A  61      28.662  58.584  40.012  1.00 14.44           C  
ATOM    466  CD1 PHE A  61      28.365  59.047  38.732  1.00 16.67           C  
ATOM    467  CD2 PHE A  61      28.593  59.473  41.075  1.00 14.37           C  
ATOM    468  CE1 PHE A  61      27.999  60.375  38.522  1.00 15.79           C  
ATOM    469  CE2 PHE A  61      28.230  60.799  40.877  1.00 17.26           C  
ATOM    470  CZ  PHE A  61      27.932  61.253  39.600  1.00 17.15           C  
ATOM    471  N   THR A  62      31.713  58.851  40.876  1.00 18.53           N  
ATOM    472  CA  THR A  62      32.320  59.997  41.554  1.00 19.42           C  
ATOM    473  C   THR A  62      32.009  61.294  40.793  1.00 21.12           C  
ATOM    474  O   THR A  62      31.598  61.272  39.631  1.00 19.41           O  
ATOM    475  CB  THR A  62      33.862  59.876  41.665  1.00 18.83           C  
ATOM    476  OG1 THR A  62      34.451  59.991  40.364  1.00 19.61           O  
ATOM    477  CG2 THR A  62      34.256  58.551  42.279  1.00 17.66           C  
ATOM    478  N   ASP A  63      32.187  62.419  41.476  1.00 23.09           N  
ATOM    479  CA  ASP A  63      31.975  63.745  40.903  1.00 25.07           C  
ATOM    480  C   ASP A  63      32.678  64.692  41.865  1.00 27.69           C  
ATOM    481  O   ASP A  63      32.038  65.376  42.671  1.00 25.97           O  
ATOM    482  CB  ASP A  63      30.484  64.089  40.817  1.00 25.63           C  
ATOM    483  CG  ASP A  63      30.220  65.335  39.973  1.00 25.10           C  
ATOM    484  OD1 ASP A  63      29.075  65.854  39.985  1.00 20.80           O  
ATOM    485  OD2 ASP A  63      31.165  65.788  39.292  1.00 24.76           O  
ATOM    486  N   GLY A  64      34.005  64.709  41.772  1.00 29.90           N  
ATOM    487  CA  GLY A  64      34.812  65.524  42.656  1.00 32.56           C  
ATOM    488  C   GLY A  64      35.092  64.685  43.891  1.00 35.46           C  
ATOM    489  O   GLY A  64      35.716  63.621  43.803  1.00 35.24           O  
ATOM    490  N   ASP A  65      34.621  65.154  45.042  1.00 37.25           N  
ATOM    491  CA  ASP A  65      34.805  64.435  46.298  1.00 38.93           C  
ATOM    492  C   ASP A  65      33.551  63.609  46.529  1.00 38.37           C  
ATOM    493  O   ASP A  65      33.497  62.753  47.413  1.00 39.19           O  
ATOM    494  CB  ASP A  65      34.979  65.417  47.461  1.00 42.64           C  
ATOM    495  CG  ASP A  65      35.942  66.541  47.136  1.00 46.01           C  
ATOM    496  OD1 ASP A  65      37.035  66.254  46.603  1.00 47.82           O  
ATOM    497  OD2 ASP A  65      35.607  67.711  47.421  1.00 48.80           O  
ATOM    498  N   VAL A  66      32.536  63.886  45.723  1.00 36.34           N  
ATOM    499  CA  VAL A  66      31.268  63.188  45.818  1.00 34.33           C  
ATOM    500  C   VAL A  66      31.388  61.755  45.294  1.00 33.54           C  
ATOM    501  O   VAL A  66      31.739  61.529  44.136  1.00 34.39           O  
ATOM    502  CB  VAL A  66      30.189  63.947  45.021  1.00 33.79           C  
ATOM    503  CG1 VAL A  66      28.808  63.337  45.269  1.00 32.05           C  
ATOM    504  CG2 VAL A  66      30.215  65.429  45.418  1.00 33.89           C  
ATOM    505  N   VAL A  67      31.124  60.789  46.165  1.00 31.99           N  
ATOM    506  CA  VAL A  67      31.169  59.381  45.785  1.00 30.70           C  
ATOM    507  C   VAL A  67      29.800  58.800  46.119  1.00 28.24           C  
ATOM    508  O   VAL A  67      29.319  58.951  47.246  1.00 28.88           O  
ATOM    509  CB  VAL A  67      32.242  58.586  46.569  1.00 30.88           C  
ATOM    510  CG1 VAL A  67      32.422  57.198  45.933  1.00 29.26           C  
ATOM    511  CG2 VAL A  67      33.563  59.347  46.578  1.00 32.05           C  
ATOM    512  N   VAL A  68      29.174  58.154  45.138  1.00 24.95           N  
ATOM    513  CA  VAL A  68      27.842  57.556  45.313  1.00 22.19           C  
ATOM    514  C   VAL A  68      27.753  56.299  44.449  1.00 19.90           C  
ATOM    515  O   VAL A  68      28.217  56.290  43.310  1.00 18.27           O  
ATOM    516  CB  VAL A  68      26.730  58.531  44.864  1.00 21.97           C  
ATOM    517  CG1 VAL A  68      25.386  58.078  45.410  1.00 22.89           C  
ATOM    518  CG2 VAL A  68      27.056  59.939  45.311  1.00 22.54           C  
ATOM    519  N   ASN A  69      27.140  55.246  44.972  1.00 19.78           N  
ATOM    520  CA  ASN A  69      27.045  54.016  44.205  1.00 20.15           C  
ATOM    521  C   ASN A  69      25.632  53.506  43.895  1.00 18.86           C  
ATOM    522  O   ASN A  69      25.369  53.106  42.761  1.00 20.28           O  
ATOM    523  CB  ASN A  69      27.862  52.914  44.891  1.00 19.61           C  
ATOM    524  CG  ASN A  69      29.308  53.319  45.113  1.00 21.73           C  
ATOM    525  OD1 ASN A  69      29.972  53.836  44.206  1.00 19.95           O  
ATOM    526  ND2 ASN A  69      29.805  53.087  46.320  1.00 22.17           N  
ATOM    527  N   GLU A  70      24.730  53.484  44.873  1.00 14.94           N  
ATOM    528  CA  GLU A  70      23.380  53.004  44.577  1.00 13.65           C  
ATOM    529  C   GLU A  70      22.880  53.785  43.354  1.00 14.72           C  
ATOM    530  O   GLU A  70      22.844  55.019  43.363  1.00 14.06           O  
ATOM    531  CB  GLU A  70      22.442  53.218  45.774  1.00 16.21           C  
ATOM    532  CG  GLU A  70      22.628  52.209  46.937  1.00 15.35           C  
ATOM    533  CD  GLU A  70      22.366  50.759  46.509  1.00 20.14           C  
ATOM    534  OE1 GLU A  70      21.334  50.510  45.843  1.00 18.54           O  
ATOM    535  OE2 GLU A  70      23.181  49.869  46.841  1.00 16.41           O  
ATOM    536  N   SER A  71      22.515  53.068  42.295  1.00 12.38           N  
ATOM    537  CA  SER A  71      22.051  53.721  41.083  1.00 13.45           C  
ATOM    538  C   SER A  71      20.980  54.768  41.357  1.00 12.91           C  
ATOM    539  O   SER A  71      20.992  55.848  40.754  1.00 12.91           O  
ATOM    540  CB  SER A  71      21.536  52.688  40.074  1.00 13.82           C  
ATOM    541  OG  SER A  71      20.438  51.964  40.577  1.00 15.02           O  
ATOM    542  N   THR A  72      20.062  54.468  42.272  1.00 12.06           N  
ATOM    543  CA  THR A  72      19.005  55.427  42.586  1.00 12.77           C  
ATOM    544  C   THR A  72      19.534  56.666  43.309  1.00 12.93           C  
ATOM    545  O   THR A  72      19.011  57.764  43.121  1.00 13.24           O  
ATOM    546  CB  THR A  72      17.899  54.779  43.415  1.00 12.55           C  
ATOM    547  OG1 THR A  72      17.316  53.717  42.655  1.00 15.97           O  
ATOM    548  CG2 THR A  72      16.817  55.798  43.768  1.00 13.17           C  
ATOM    549  N   ALA A  73      20.578  56.502  44.116  1.00 12.36           N  
ATOM    550  CA  ALA A  73      21.147  57.648  44.823  1.00 12.72           C  
ATOM    551  C   ALA A  73      21.875  58.539  43.823  1.00 14.47           C  
ATOM    552  O   ALA A  73      21.810  59.766  43.912  1.00 13.83           O  
ATOM    553  CB  ALA A  73      22.106  57.193  45.888  1.00 12.96           C  
ATOM    554  N   ILE A  74      22.562  57.912  42.870  1.00 13.34           N  
ATOM    555  CA  ILE A  74      23.300  58.645  41.853  1.00 13.97           C  
ATOM    556  C   ILE A  74      22.320  59.510  41.048  1.00 15.27           C  
ATOM    557  O   ILE A  74      22.549  60.713  40.875  1.00 17.08           O  
ATOM    558  CB  ILE A  74      24.061  57.667  40.904  1.00 13.89           C  
ATOM    559  CG1 ILE A  74      25.122  56.897  41.683  1.00 11.52           C  
ATOM    560  CG2 ILE A  74      24.738  58.430  39.779  1.00 13.97           C  
ATOM    561  CD1 ILE A  74      25.597  55.656  40.968  1.00 10.46           C  
ATOM    562  N   CYS A  75      21.227  58.903  40.577  1.00 14.59           N  
ATOM    563  CA  CYS A  75      20.213  59.635  39.805  1.00 13.31           C  
ATOM    564  C   CYS A  75      19.648  60.797  40.602  1.00 13.45           C  
ATOM    565  O   CYS A  75      19.476  61.890  40.070  1.00 13.43           O  
ATOM    566  CB  CYS A  75      19.056  58.716  39.384  1.00 14.04           C  
ATOM    567  SG  CYS A  75      19.506  57.396  38.240  1.00 15.47           S  
ATOM    568  N   MET A  76      19.346  60.570  41.878  1.00 14.91           N  
ATOM    569  CA  MET A  76      18.811  61.654  42.704  1.00 14.62           C  
ATOM    570  C   MET A  76      19.842  62.747  42.873  1.00 15.29           C  
ATOM    571  O   MET A  76      19.511  63.927  42.836  1.00 18.11           O  
ATOM    572  CB  MET A  76      18.381  61.151  44.084  1.00 12.62           C  
ATOM    573  CG  MET A  76      17.125  60.301  44.084  1.00 15.13           C  
ATOM    574  SD  MET A  76      15.755  61.090  43.209  1.00 20.55           S  
ATOM    575  CE  MET A  76      15.454  62.520  44.215  1.00 19.15           C  
ATOM    576  N   TYR A  77      21.101  62.365  43.054  1.00 15.93           N  
ATOM    577  CA  TYR A  77      22.148  63.369  43.225  1.00 17.27           C  
ATOM    578  C   TYR A  77      22.306  64.221  41.966  1.00 16.96           C  
ATOM    579  O   TYR A  77      22.450  65.441  42.056  1.00 16.80           O  
ATOM    580  CB  TYR A  77      23.483  62.709  43.565  1.00 16.97           C  
ATOM    581  CG  TYR A  77      24.683  63.579  43.245  1.00 17.25           C  
ATOM    582  CD1 TYR A  77      25.061  64.628  44.081  1.00 18.17           C  
ATOM    583  CD2 TYR A  77      25.420  63.366  42.085  1.00 16.05           C  
ATOM    584  CE1 TYR A  77      26.153  65.447  43.765  1.00 16.59           C  
ATOM    585  CE2 TYR A  77      26.499  64.170  41.757  1.00 17.13           C  
ATOM    586  CZ  TYR A  77      26.866  65.209  42.598  1.00 19.83           C  
ATOM    587  OH  TYR A  77      27.943  66.000  42.255  1.00 17.62           O  
ATOM    588  N   LEU A  78      22.274  63.567  40.802  1.00 17.10           N  
ATOM    589  CA  LEU A  78      22.424  64.239  39.502  1.00 16.59           C  
ATOM    590  C   LEU A  78      21.285  65.211  39.234  1.00 17.64           C  
ATOM    591  O   LEU A  78      21.476  66.266  38.623  1.00 17.13           O  
ATOM    592  CB  LEU A  78      22.470  63.209  38.369  1.00 12.46           C  
ATOM    593  CG  LEU A  78      23.691  62.297  38.323  1.00 15.04           C  
ATOM    594  CD1 LEU A  78      23.530  61.290  37.186  1.00 11.21           C  
ATOM    595  CD2 LEU A  78      24.971  63.141  38.147  1.00  8.73           C  
ATOM    596  N   GLU A  79      20.094  64.830  39.681  1.00 17.92           N  
ATOM    597  CA  GLU A  79      18.905  65.655  39.514  1.00 20.58           C  
ATOM    598  C   GLU A  79      19.085  66.919  40.349  1.00 21.01           C  
ATOM    599  O   GLU A  79      18.756  68.014  39.904  1.00 21.68           O  
ATOM    600  CB  GLU A  79      17.664  64.882  39.985  1.00 18.82           C  
ATOM    601  CG  GLU A  79      16.342  65.659  39.928  1.00 20.70           C  
ATOM    602  CD  GLU A  79      15.979  66.140  38.523  1.00 20.58           C  
ATOM    603  OE1 GLU A  79      16.472  65.561  37.537  1.00 20.56           O  
ATOM    604  OE2 GLU A  79      15.179  67.089  38.406  1.00 23.72           O  
ATOM    605  N   GLU A  80      19.628  66.751  41.552  1.00 20.44           N  
ATOM    606  CA  GLU A  80      19.852  67.863  42.468  1.00 22.26           C  
ATOM    607  C   GLU A  80      21.094  68.702  42.167  1.00 22.57           C  
ATOM    608  O   GLU A  80      21.097  69.909  42.415  1.00 23.41           O  
ATOM    609  CB  GLU A  80      19.921  67.353  43.917  1.00 20.91           C  
ATOM    610  CG  GLU A  80      18.561  67.033  44.526  1.00 22.66           C  
ATOM    611  CD  GLU A  80      18.649  66.464  45.942  1.00 22.71           C  
ATOM    612  OE1 GLU A  80      19.666  66.693  46.630  1.00 20.57           O  
ATOM    613  OE2 GLU A  80      17.685  65.795  46.371  1.00 22.65           O  
ATOM    614  N   LYS A  81      22.141  68.078  41.638  1.00 22.08           N  
ATOM    615  CA  LYS A  81      23.370  68.811  41.333  1.00 22.40           C  
ATOM    616  C   LYS A  81      23.282  69.568  40.004  1.00 22.37           C  
ATOM    617  O   LYS A  81      23.746  70.696  39.908  1.00 21.15           O  
ATOM    618  CB  LYS A  81      24.572  67.857  41.308  1.00 21.93           C  
ATOM    619  CG  LYS A  81      25.937  68.555  41.346  1.00 21.63           C  
ATOM    620  CD  LYS A  81      26.047  69.468  42.566  1.00 23.57           C  
ATOM    621  CE  LYS A  81      27.411  70.160  42.675  1.00 23.05           C  
ATOM    622  NZ  LYS A  81      28.469  69.290  43.256  1.00 21.79           N  
ATOM    623  N   TYR A  82      22.683  68.943  38.992  1.00 22.44           N  
ATOM    624  CA  TYR A  82      22.530  69.557  37.671  1.00 23.24           C  
ATOM    625  C   TYR A  82      21.034  69.716  37.373  1.00 24.83           C  
ATOM    626  O   TYR A  82      20.427  68.887  36.697  1.00 23.16           O  
ATOM    627  CB  TYR A  82      23.203  68.684  36.601  1.00 22.38           C  
ATOM    628  CG  TYR A  82      24.630  68.331  36.944  1.00 23.80           C  
ATOM    629  CD1 TYR A  82      24.924  67.209  37.717  1.00 23.36           C  
ATOM    630  CD2 TYR A  82      25.686  69.160  36.559  1.00 25.36           C  
ATOM    631  CE1 TYR A  82      26.236  66.920  38.105  1.00 23.86           C  
ATOM    632  CE2 TYR A  82      27.002  68.883  36.945  1.00 25.35           C  
ATOM    633  CZ  TYR A  82      27.265  67.765  37.718  1.00 24.98           C  
ATOM    634  OH  TYR A  82      28.553  67.506  38.123  1.00 25.08           O  
ATOM    635  N   PRO A  83      20.431  70.805  37.869  1.00 26.12           N  
ATOM    636  CA  PRO A  83      19.010  71.127  37.707  1.00 29.16           C  
ATOM    637  C   PRO A  83      18.530  71.721  36.382  1.00 31.50           C  
ATOM    638  O   PRO A  83      17.320  71.820  36.161  1.00 31.23           O  
ATOM    639  CB  PRO A  83      18.757  72.074  38.872  1.00 28.27           C  
ATOM    640  CG  PRO A  83      20.029  72.875  38.889  1.00 27.85           C  
ATOM    641  CD  PRO A  83      21.106  71.816  38.707  1.00 26.27           C  
ATOM    642  N   LYS A  84      19.451  72.107  35.502  1.00 33.86           N  
ATOM    643  CA  LYS A  84      19.056  72.720  34.231  1.00 36.34           C  
ATOM    644  C   LYS A  84      18.039  71.932  33.401  1.00 36.22           C  
ATOM    645  O   LYS A  84      17.112  72.524  32.841  1.00 38.98           O  
ATOM    646  CB  LYS A  84      20.290  73.034  33.377  1.00 38.63           C  
ATOM    647  CG  LYS A  84      21.350  73.844  34.114  1.00 42.62           C  
ATOM    648  CD  LYS A  84      20.726  74.910  35.016  1.00 46.15           C  
ATOM    649  CE  LYS A  84      21.774  75.568  35.910  1.00 48.25           C  
ATOM    650  NZ  LYS A  84      21.161  76.489  36.913  1.00 48.23           N  
ATOM    651  N   VAL A  85      18.201  70.613  33.311  1.00 33.20           N  
ATOM    652  CA  VAL A  85      17.261  69.789  32.550  1.00 30.35           C  
ATOM    653  C   VAL A  85      16.507  68.848  33.502  1.00 29.73           C  
ATOM    654  O   VAL A  85      16.860  67.674  33.650  1.00 29.67           O  
ATOM    655  CB  VAL A  85      18.001  68.962  31.468  1.00 29.55           C  
ATOM    656  CG1 VAL A  85      17.008  68.110  30.684  1.00 27.10           C  
ATOM    657  CG2 VAL A  85      18.753  69.900  30.524  1.00 28.72           C  
ATOM    658  N   PRO A  86      15.456  69.361  34.165  1.00 28.97           N  
ATOM    659  CA  PRO A  86      14.631  68.601  35.117  1.00 27.24           C  
ATOM    660  C   PRO A  86      14.034  67.303  34.586  1.00 25.43           C  
ATOM    661  O   PRO A  86      13.436  67.277  33.516  1.00 24.98           O  
ATOM    662  CB  PRO A  86      13.528  69.590  35.494  1.00 26.32           C  
ATOM    663  CG  PRO A  86      14.164  70.917  35.308  1.00 28.06           C  
ATOM    664  CD  PRO A  86      14.940  70.735  34.021  1.00 28.59           C  
ATOM    665  N   LEU A  87      14.194  66.227  35.352  1.00 25.28           N  
ATOM    666  CA  LEU A  87      13.625  64.941  34.987  1.00 23.32           C  
ATOM    667  C   LEU A  87      12.371  64.765  35.839  1.00 22.71           C  
ATOM    668  O   LEU A  87      11.683  63.744  35.775  1.00 23.91           O  
ATOM    669  CB  LEU A  87      14.642  63.806  35.204  1.00 24.09           C  
ATOM    670  CG  LEU A  87      15.784  63.837  34.169  1.00 25.57           C  
ATOM    671  CD1 LEU A  87      16.659  62.583  34.257  1.00 25.15           C  
ATOM    672  CD2 LEU A  87      15.182  63.945  32.763  1.00 26.65           C  
ATOM    673  N   PHE A  88      12.078  65.795  36.625  1.00 21.55           N  
ATOM    674  CA  PHE A  88      10.886  65.835  37.468  1.00 22.21           C  
ATOM    675  C   PHE A  88      10.116  67.121  37.171  1.00 22.86           C  
ATOM    676  O   PHE A  88      10.721  68.168  36.938  1.00 22.30           O  
ATOM    677  CB  PHE A  88      11.234  65.875  38.955  1.00 18.91           C  
ATOM    678  CG  PHE A  88      11.623  64.560  39.541  1.00 17.90           C  
ATOM    679  CD1 PHE A  88      12.951  64.156  39.553  1.00 17.61           C  
ATOM    680  CD2 PHE A  88      10.672  63.755  40.148  1.00 15.71           C  
ATOM    681  CE1 PHE A  88      13.326  62.977  40.171  1.00 18.93           C  
ATOM    682  CE2 PHE A  88      11.038  62.577  40.765  1.00 16.91           C  
ATOM    683  CZ  PHE A  88      12.369  62.186  40.780  1.00 16.99           C  
ATOM    684  N   PRO A  89       8.773  67.059  37.169  1.00 24.05           N  
ATOM    685  CA  PRO A  89       8.005  68.282  36.908  1.00 24.56           C  
ATOM    686  C   PRO A  89       8.101  69.111  38.181  1.00 26.23           C  
ATOM    687  O   PRO A  89       8.688  68.658  39.165  1.00 28.14           O  
ATOM    688  CB  PRO A  89       6.595  67.758  36.643  1.00 23.82           C  
ATOM    689  CG  PRO A  89       6.534  66.515  37.488  1.00 25.31           C  
ATOM    690  CD  PRO A  89       7.886  65.881  37.216  1.00 23.86           C  
ATOM    691  N   SER A  90       7.546  70.317  38.186  1.00 27.50           N  
ATOM    692  CA  SER A  90       7.628  71.154  39.381  1.00 27.92           C  
ATOM    693  C   SER A  90       6.457  70.942  40.332  1.00 27.18           C  
ATOM    694  O   SER A  90       6.557  71.199  41.529  1.00 28.30           O  
ATOM    695  CB  SER A  90       7.720  72.631  38.984  1.00 28.65           C  
ATOM    696  OG  SER A  90       6.708  72.970  38.054  1.00 30.92           O  
ATOM    697  N   ASP A  91       5.342  70.470  39.801  1.00 26.70           N  
ATOM    698  CA  ASP A  91       4.180  70.243  40.633  1.00 26.93           C  
ATOM    699  C   ASP A  91       4.467  69.134  41.643  1.00 26.51           C  
ATOM    700  O   ASP A  91       4.731  67.994  41.266  1.00 26.83           O  
ATOM    701  CB  ASP A  91       2.990  69.850  39.773  1.00 28.85           C  
ATOM    702  CG  ASP A  91       1.684  70.063  40.484  1.00 30.33           C  
ATOM    703  OD1 ASP A  91       1.226  71.220  40.502  1.00 32.79           O  
ATOM    704  OD2 ASP A  91       1.133  69.090  41.041  1.00 28.69           O  
ATOM    705  N   THR A  92       4.397  69.468  42.925  1.00 25.25           N  
ATOM    706  CA  THR A  92       4.669  68.497  43.974  1.00 25.12           C  
ATOM    707  C   THR A  92       3.761  67.280  43.906  1.00 24.78           C  
ATOM    708  O   THR A  92       4.204  66.152  44.136  1.00 24.36           O  
ATOM    709  CB  THR A  92       4.555  69.142  45.373  1.00 24.68           C  
ATOM    710  OG1 THR A  92       5.520  70.194  45.482  1.00 26.32           O  
ATOM    711  CG2 THR A  92       4.842  68.120  46.460  1.00 25.68           C  
ATOM    712  N   THR A  93       2.492  67.514  43.592  1.00 24.95           N  
ATOM    713  CA  THR A  93       1.506  66.442  43.483  1.00 24.34           C  
ATOM    714  C   THR A  93       1.823  65.506  42.318  1.00 23.43           C  
ATOM    715  O   THR A  93       1.672  64.292  42.428  1.00 25.24           O  
ATOM    716  CB  THR A  93       0.097  67.024  43.282  1.00 24.73           C  
ATOM    717  OG1 THR A  93      -0.290  67.738  44.464  1.00 25.82           O  
ATOM    718  CG2 THR A  93      -0.906  65.922  42.983  1.00 23.42           C  
ATOM    719  N   ILE A  94       2.259  66.078  41.201  1.00 22.08           N  
ATOM    720  CA  ILE A  94       2.593  65.287  40.031  1.00 21.73           C  
ATOM    721  C   ILE A  94       3.931  64.576  40.233  1.00 21.58           C  
ATOM    722  O   ILE A  94       4.127  63.478  39.718  1.00 21.40           O  
ATOM    723  CB  ILE A  94       2.659  66.160  38.753  1.00 22.07           C  
ATOM    724  CG1 ILE A  94       1.374  66.990  38.622  1.00 21.88           C  
ATOM    725  CG2 ILE A  94       2.823  65.269  37.526  1.00 18.09           C  
ATOM    726  CD1 ILE A  94       1.360  67.936  37.442  1.00 22.74           C  
ATOM    727  N   ARG A  95       4.843  65.194  40.985  1.00 20.77           N  
ATOM    728  CA  ARG A  95       6.145  64.582  41.253  1.00 20.27           C  
ATOM    729  C   ARG A  95       5.906  63.309  42.059  1.00 19.66           C  
ATOM    730  O   ARG A  95       6.605  62.303  41.893  1.00 18.22           O  
ATOM    731  CB  ARG A  95       7.043  65.533  42.053  1.00 21.09           C  
ATOM    732  CG  ARG A  95       7.442  66.801  41.316  1.00 23.93           C  
ATOM    733  CD  ARG A  95       7.938  67.873  42.288  1.00 25.03           C  
ATOM    734  NE  ARG A  95       9.198  67.516  42.928  1.00 27.17           N  
ATOM    735  CZ  ARG A  95      10.406  67.761  42.419  1.00 27.66           C  
ATOM    736  NH1 ARG A  95      11.490  67.387  43.083  1.00 26.40           N  
ATOM    737  NH2 ARG A  95      10.538  68.393  41.260  1.00 26.49           N  
ATOM    738  N   ALA A  96       4.897  63.359  42.922  1.00 18.40           N  
ATOM    739  CA  ALA A  96       4.545  62.219  43.755  1.00 18.09           C  
ATOM    740  C   ALA A  96       4.256  61.006  42.871  1.00 19.23           C  
ATOM    741  O   ALA A  96       4.624  59.880  43.202  1.00 18.95           O  
ATOM    742  CB  ALA A  96       3.320  62.556  44.607  1.00 17.81           C  
ATOM    743  N   LYS A  97       3.598  61.238  41.743  1.00 18.22           N  
ATOM    744  CA  LYS A  97       3.275  60.148  40.828  1.00 20.51           C  
ATOM    745  C   LYS A  97       4.540  59.613  40.168  1.00 18.73           C  
ATOM    746  O   LYS A  97       4.661  58.410  39.923  1.00 20.03           O  
ATOM    747  CB  LYS A  97       2.295  60.626  39.756  1.00 22.31           C  
ATOM    748  CG  LYS A  97       2.165  59.669  38.583  1.00 30.07           C  
ATOM    749  CD  LYS A  97       1.316  58.456  38.921  1.00 33.24           C  
ATOM    750  CE  LYS A  97      -0.146  58.858  39.123  1.00 37.39           C  
ATOM    751  NZ  LYS A  97      -0.671  59.671  37.978  1.00 38.29           N  
ATOM    752  N   VAL A  98       5.474  60.513  39.874  1.00 16.24           N  
ATOM    753  CA  VAL A  98       6.738  60.130  39.253  1.00 15.47           C  
ATOM    754  C   VAL A  98       7.524  59.251  40.227  1.00 16.11           C  
ATOM    755  O   VAL A  98       8.096  58.233  39.832  1.00 17.31           O  
ATOM    756  CB  VAL A  98       7.568  61.384  38.873  1.00 17.18           C  
ATOM    757  CG1 VAL A  98       8.984  60.982  38.458  1.00 15.94           C  
ATOM    758  CG2 VAL A  98       6.867  62.142  37.739  1.00 14.08           C  
ATOM    759  N   TYR A  99       7.539  59.644  41.499  1.00 14.06           N  
ATOM    760  CA  TYR A  99       8.226  58.881  42.536  1.00 14.58           C  
ATOM    761  C   TYR A  99       7.557  57.525  42.705  1.00 14.16           C  
ATOM    762  O   TYR A  99       8.232  56.518  42.860  1.00 12.27           O  
ATOM    763  CB  TYR A  99       8.187  59.632  43.870  1.00 15.10           C  
ATOM    764  CG  TYR A  99       9.204  60.744  44.012  1.00 15.07           C  
ATOM    765  CD1 TYR A  99       8.819  62.010  44.447  1.00 14.17           C  
ATOM    766  CD2 TYR A  99      10.565  60.511  43.784  1.00 16.58           C  
ATOM    767  CE1 TYR A  99       9.759  63.017  44.659  1.00 16.18           C  
ATOM    768  CE2 TYR A  99      11.518  61.517  43.999  1.00 17.78           C  
ATOM    769  CZ  TYR A  99      11.104  62.765  44.437  1.00 18.29           C  
ATOM    770  OH  TYR A  99      12.035  63.763  44.660  1.00 19.85           O  
ATOM    771  N   GLN A 100       6.225  57.511  42.684  1.00 15.19           N  
ATOM    772  CA  GLN A 100       5.459  56.271  42.822  1.00 14.69           C  
ATOM    773  C   GLN A 100       5.867  55.257  41.763  1.00 15.66           C  
ATOM    774  O   GLN A 100       6.148  54.099  42.074  1.00 13.91           O  
ATOM    775  CB  GLN A 100       3.949  56.547  42.695  1.00 14.05           C  
ATOM    776  CG  GLN A 100       3.093  55.298  42.448  1.00 14.32           C  
ATOM    777  CD  GLN A 100       3.065  54.322  43.633  1.00 19.25           C  
ATOM    778  OE1 GLN A 100       2.839  53.107  43.462  1.00 15.80           O  
ATOM    779  NE2 GLN A 100       3.275  54.848  44.837  1.00 14.55           N  
ATOM    780  N   ARG A 101       5.893  55.701  40.507  1.00 16.53           N  
ATOM    781  CA  ARG A 101       6.247  54.824  39.395  1.00 15.82           C  
ATOM    782  C   ARG A 101       7.703  54.400  39.463  1.00 14.53           C  
ATOM    783  O   ARG A 101       8.014  53.245  39.214  1.00 14.40           O  
ATOM    784  CB  ARG A 101       5.960  55.518  38.068  1.00 16.97           C  
ATOM    785  CG  ARG A 101       4.496  55.825  37.830  1.00 20.35           C  
ATOM    786  CD  ARG A 101       3.714  54.575  37.420  1.00 21.69           C  
ATOM    787  NE  ARG A 101       3.026  53.934  38.531  1.00 22.15           N  
ATOM    788  CZ  ARG A 101       1.793  54.237  38.937  1.00 23.55           C  
ATOM    789  NH1 ARG A 101       1.260  53.586  39.968  1.00 20.60           N  
ATOM    790  NH2 ARG A 101       1.089  55.175  38.313  1.00 22.67           N  
ATOM    791  N   MET A 102       8.587  55.335  39.802  1.00 13.28           N  
ATOM    792  CA  MET A 102      10.017  55.045  39.924  1.00 14.31           C  
ATOM    793  C   MET A 102      10.305  53.857  40.833  1.00 14.33           C  
ATOM    794  O   MET A 102      10.943  52.886  40.432  1.00 13.91           O  
ATOM    795  CB  MET A 102      10.769  56.238  40.521  1.00 15.30           C  
ATOM    796  CG  MET A 102      11.151  57.353  39.584  1.00 13.14           C  
ATOM    797  SD  MET A 102      11.737  58.760  40.574  1.00 19.47           S  
ATOM    798  CE  MET A 102      13.033  58.022  41.559  1.00  9.55           C  
ATOM    799  N   PHE A 103       9.849  53.967  42.076  1.00 14.84           N  
ATOM    800  CA  PHE A 103      10.080  52.948  43.092  1.00 14.78           C  
ATOM    801  C   PHE A 103       9.249  51.690  42.928  1.00 15.71           C  
ATOM    802  O   PHE A 103       9.673  50.608  43.327  1.00 15.19           O  
ATOM    803  CB  PHE A 103       9.884  53.574  44.476  1.00 15.23           C  
ATOM    804  CG  PHE A 103      10.841  54.720  44.745  1.00 17.10           C  
ATOM    805  CD1 PHE A 103      10.370  56.018  44.943  1.00 15.56           C  
ATOM    806  CD2 PHE A 103      12.222  54.513  44.687  1.00 13.65           C  
ATOM    807  CE1 PHE A 103      11.263  57.091  45.067  1.00 14.25           C  
ATOM    808  CE2 PHE A 103      13.115  55.575  44.809  1.00 10.74           C  
ATOM    809  CZ  PHE A 103      12.636  56.865  44.996  1.00 13.22           C  
ATOM    810  N   GLU A 104       8.077  51.827  42.320  1.00 16.11           N  
ATOM    811  CA  GLU A 104       7.213  50.681  42.093  1.00 17.17           C  
ATOM    812  C   GLU A 104       7.843  49.746  41.056  1.00 17.85           C  
ATOM    813  O   GLU A 104       7.498  48.566  40.992  1.00 20.30           O  
ATOM    814  CB  GLU A 104       5.827  51.146  41.618  1.00 14.80           C  
ATOM    815  CG  GLU A 104       4.888  50.029  41.201  1.00 13.54           C  
ATOM    816  CD  GLU A 104       3.500  50.533  40.813  1.00 14.70           C  
ATOM    817  OE1 GLU A 104       3.313  51.755  40.664  1.00 14.97           O  
ATOM    818  OE2 GLU A 104       2.593  49.701  40.641  1.00 17.25           O  
ATOM    819  N   THR A 105       8.771  50.260  40.255  1.00 17.10           N  
ATOM    820  CA  THR A 105       9.405  49.423  39.239  1.00 19.49           C  
ATOM    821  C   THR A 105      10.235  48.288  39.828  1.00 20.42           C  
ATOM    822  O   THR A 105      10.652  47.400  39.099  1.00 20.92           O  
ATOM    823  CB  THR A 105      10.325  50.222  38.294  1.00 19.04           C  
ATOM    824  OG1 THR A 105      11.438  50.743  39.033  1.00 19.08           O  
ATOM    825  CG2 THR A 105       9.563  51.352  37.633  1.00 17.84           C  
ATOM    826  N   SER A 106      10.480  48.312  41.136  1.00 20.60           N  
ATOM    827  CA  SER A 106      11.257  47.243  41.761  1.00 22.47           C  
ATOM    828  C   SER A 106      10.457  45.949  41.726  1.00 23.49           C  
ATOM    829  O   SER A 106      11.007  44.863  41.895  1.00 23.07           O  
ATOM    830  CB  SER A 106      11.590  47.584  43.210  1.00 21.49           C  
ATOM    831  OG  SER A 106      10.411  47.652  43.993  1.00 25.66           O  
ATOM    832  N   ASN A 107       9.150  46.082  41.516  1.00 23.62           N  
ATOM    833  CA  ASN A 107       8.247  44.943  41.441  1.00 25.05           C  
ATOM    834  C   ASN A 107       8.451  44.156  40.152  1.00 26.20           C  
ATOM    835  O   ASN A 107       8.323  42.939  40.140  1.00 27.22           O  
ATOM    836  CB  ASN A 107       6.800  45.423  41.514  1.00 26.55           C  
ATOM    837  CG  ASN A 107       6.439  45.976  42.875  1.00 28.46           C  
ATOM    838  OD1 ASN A 107       6.327  45.228  43.850  1.00 27.93           O  
ATOM    839  ND2 ASN A 107       6.260  47.294  42.952  1.00 27.20           N  
ATOM    840  N   ILE A 108       8.749  44.852  39.061  1.00 27.08           N  
ATOM    841  CA  ILE A 108       8.969  44.177  37.790  1.00 27.56           C  
ATOM    842  C   ILE A 108      10.081  43.164  37.995  1.00 30.07           C  
ATOM    843  O   ILE A 108       9.960  42.000  37.632  1.00 29.91           O  
ATOM    844  CB  ILE A 108       9.396  45.163  36.687  1.00 25.40           C  
ATOM    845  CG1 ILE A 108       8.275  46.170  36.425  1.00 21.54           C  
ATOM    846  CG2 ILE A 108       9.741  44.393  35.410  1.00 24.82           C  
ATOM    847  CD1 ILE A 108       8.641  47.257  35.442  1.00 17.69           C  
ATOM    848  N   SER A 109      11.162  43.629  38.602  1.00 33.23           N  
ATOM    849  CA  SER A 109      12.314  42.794  38.877  1.00 36.98           C  
ATOM    850  C   SER A 109      11.932  41.498  39.592  1.00 38.63           C  
ATOM    851  O   SER A 109      12.336  40.411  39.182  1.00 40.08           O  
ATOM    852  CB  SER A 109      13.313  43.584  39.726  1.00 38.01           C  
ATOM    853  OG  SER A 109      14.406  42.772  40.111  1.00 40.24           O  
ATOM    854  N   THR A 110      11.141  41.616  40.651  1.00 40.06           N  
ATOM    855  CA  THR A 110      10.727  40.458  41.436  1.00 41.27           C  
ATOM    856  C   THR A 110       9.646  39.570  40.817  1.00 41.49           C  
ATOM    857  O   THR A 110       9.801  38.350  40.759  1.00 42.43           O  
ATOM    858  CB  THR A 110      10.243  40.896  42.826  1.00 41.83           C  
ATOM    859  OG1 THR A 110       9.221  41.889  42.679  1.00 43.99           O  
ATOM    860  CG2 THR A 110      11.399  41.479  43.636  1.00 40.31           C  
ATOM    861  N   ASN A 111       8.552  40.168  40.359  1.00 40.46           N  
ATOM    862  CA  ASN A 111       7.472  39.384  39.776  1.00 39.55           C  
ATOM    863  C   ASN A 111       7.707  38.958  38.328  1.00 40.57           C  
ATOM    864  O   ASN A 111       7.189  37.929  37.886  1.00 40.91           O  
ATOM    865  CB  ASN A 111       6.158  40.152  39.896  1.00 37.78           C  
ATOM    866  CG  ASN A 111       5.870  40.568  41.319  1.00 36.06           C  
ATOM    867  OD1 ASN A 111       6.178  39.839  42.261  1.00 34.21           O  
ATOM    868  ND2 ASN A 111       5.272  41.738  41.485  1.00 34.95           N  
ATOM    869  N   VAL A 112       8.488  39.739  37.591  1.00 41.01           N  
ATOM    870  CA  VAL A 112       8.775  39.405  36.208  1.00 42.47           C  
ATOM    871  C   VAL A 112      10.043  38.572  36.086  1.00 45.05           C  
ATOM    872  O   VAL A 112       9.988  37.392  35.742  1.00 46.00           O  
ATOM    873  CB  VAL A 112       8.960  40.657  35.342  1.00 41.10           C  
ATOM    874  CG1 VAL A 112       9.125  40.250  33.887  1.00 40.02           C  
ATOM    875  CG2 VAL A 112       7.783  41.590  35.512  1.00 41.26           C  
ATOM    876  N   MET A 113      11.184  39.187  36.380  1.00 47.68           N  
ATOM    877  CA  MET A 113      12.468  38.504  36.263  1.00 50.91           C  
ATOM    878  C   MET A 113      12.612  37.221  37.064  1.00 51.51           C  
ATOM    879  O   MET A 113      13.585  36.494  36.890  1.00 51.31           O  
ATOM    880  CB  MET A 113      13.614  39.461  36.601  1.00 52.52           C  
ATOM    881  CG  MET A 113      13.665  40.667  35.678  1.00 53.86           C  
ATOM    882  SD  MET A 113      13.275  40.217  33.972  1.00 56.11           S  
ATOM    883  CE  MET A 113      14.946  40.029  33.259  1.00 54.51           C  
ATOM    884  N   GLU A 114      11.656  36.935  37.940  1.00 53.30           N  
ATOM    885  CA  GLU A 114      11.714  35.700  38.712  1.00 55.40           C  
ATOM    886  C   GLU A 114      11.434  34.584  37.704  1.00 57.18           C  
ATOM    887  O   GLU A 114      12.060  33.524  37.731  1.00 57.00           O  
ATOM    888  CB  GLU A 114      10.641  35.696  39.801  1.00 55.27           C  
ATOM    889  CG  GLU A 114      11.112  35.226  41.179  1.00 55.94           C  
ATOM    890  CD  GLU A 114      11.514  33.757  41.227  1.00 57.10           C  
ATOM    891  OE1 GLU A 114      11.659  33.221  42.349  1.00 57.11           O  
ATOM    892  OE2 GLU A 114      11.694  33.138  40.156  1.00 56.04           O  
ATOM    893  N   PHE A 115      10.495  34.850  36.801  1.00 59.32           N  
ATOM    894  CA  PHE A 115      10.114  33.891  35.768  1.00 61.15           C  
ATOM    895  C   PHE A 115      11.357  33.402  35.023  1.00 62.11           C  
ATOM    896  O   PHE A 115      11.496  32.210  34.746  1.00 62.29           O  
ATOM    897  CB  PHE A 115       9.142  34.546  34.778  1.00 61.72           C  
ATOM    898  CG  PHE A 115       8.535  33.587  33.790  1.00 61.93           C  
ATOM    899  CD1 PHE A 115       8.330  33.971  32.467  1.00 62.15           C  
ATOM    900  CD2 PHE A 115       8.158  32.304  34.181  1.00 61.54           C  
ATOM    901  CE1 PHE A 115       7.759  33.091  31.545  1.00 62.32           C  
ATOM    902  CE2 PHE A 115       7.586  31.418  33.271  1.00 61.04           C  
ATOM    903  CZ  PHE A 115       7.387  31.812  31.950  1.00 61.61           C  
ATOM    904  N   VAL A 116      12.256  34.331  34.707  1.00 62.98           N  
ATOM    905  CA  VAL A 116      13.490  34.002  33.998  1.00 64.82           C  
ATOM    906  C   VAL A 116      14.483  33.296  34.921  1.00 66.54           C  
ATOM    907  O   VAL A 116      15.117  32.317  34.525  1.00 66.99           O  
ATOM    908  CB  VAL A 116      14.162  35.272  33.422  1.00 64.39           C  
ATOM    909  CG1 VAL A 116      15.447  34.903  32.687  1.00 63.70           C  
ATOM    910  CG2 VAL A 116      13.205  35.978  32.483  1.00 63.98           C  
ATOM    911  N   GLN A 117      14.611  33.799  36.148  1.00 68.11           N  
ATOM    912  CA  GLN A 117      15.520  33.222  37.140  1.00 69.31           C  
ATOM    913  C   GLN A 117      15.254  31.731  37.302  1.00 69.82           C  
ATOM    914  O   GLN A 117      16.138  30.902  37.096  1.00 69.89           O  
ATOM    915  CB  GLN A 117      15.331  33.897  38.506  1.00 69.00           C  
ATOM    916  CG  GLN A 117      15.617  35.392  38.552  1.00 70.35           C  
ATOM    917  CD  GLN A 117      17.060  35.733  38.226  1.00 71.38           C  
ATOM    918  OE1 GLN A 117      17.487  35.645  37.074  1.00 71.72           O  
ATOM    919  NE2 GLN A 117      17.822  36.120  39.245  1.00 72.22           N  
ATOM    920  N   TYR A 118      14.020  31.415  37.679  1.00 70.58           N  
ATOM    921  CA  TYR A 118      13.576  30.046  37.904  1.00 71.90           C  
ATOM    922  C   TYR A 118      13.988  29.083  36.793  1.00 72.35           C  
ATOM    923  O   TYR A 118      14.593  28.044  37.056  1.00 72.27           O  
ATOM    924  CB  TYR A 118      12.054  30.040  38.078  1.00 72.07           C  
ATOM    925  CG  TYR A 118      11.474  28.726  38.543  1.00 72.93           C  
ATOM    926  CD1 TYR A 118      11.193  27.704  37.637  1.00 73.55           C  
ATOM    927  CD2 TYR A 118      11.203  28.506  39.893  1.00 73.16           C  
ATOM    928  CE1 TYR A 118      10.650  26.492  38.065  1.00 74.35           C  
ATOM    929  CE2 TYR A 118      10.662  27.299  40.332  1.00 74.13           C  
ATOM    930  CZ  TYR A 118      10.387  26.296  39.414  1.00 74.12           C  
ATOM    931  OH  TYR A 118       9.848  25.104  39.842  1.00 73.63           O  
ATOM    932  N   LYS A 119      13.661  29.433  35.553  1.00 73.32           N  
ATOM    933  CA  LYS A 119      13.991  28.594  34.407  1.00 74.38           C  
ATOM    934  C   LYS A 119      15.495  28.381  34.262  1.00 75.62           C  
ATOM    935  O   LYS A 119      15.932  27.388  33.682  1.00 76.10           O  
ATOM    936  CB  LYS A 119      13.423  29.214  33.126  1.00 73.71           C  
ATOM    937  CG  LYS A 119      11.913  29.392  33.164  1.00 72.94           C  
ATOM    938  CD  LYS A 119      11.393  30.184  31.975  1.00 72.64           C  
ATOM    939  CE  LYS A 119      11.457  29.385  30.689  1.00 72.72           C  
ATOM    940  NZ  LYS A 119      10.770  30.102  29.581  1.00 72.10           N  
ATOM    941  N   MET A 120      16.284  29.310  34.792  1.00 77.19           N  
ATOM    942  CA  MET A 120      17.740  29.209  34.721  1.00 79.00           C  
ATOM    943  C   MET A 120      18.312  28.473  35.931  1.00 80.13           C  
ATOM    944  O   MET A 120      19.098  27.535  35.787  1.00 80.52           O  
ATOM    945  CB  MET A 120      18.369  30.601  34.642  1.00 79.16           C  
ATOM    946  CG  MET A 120      18.083  31.355  33.358  1.00 79.63           C  
ATOM    947  SD  MET A 120      18.868  32.982  33.369  1.00 81.01           S  
ATOM    948  CE  MET A 120      20.524  32.576  32.761  1.00 80.70           C  
ATOM    949  N   LYS A 121      17.914  28.912  37.121  1.00 81.56           N  
ATOM    950  CA  LYS A 121      18.379  28.317  38.369  1.00 82.85           C  
ATOM    951  C   LYS A 121      18.067  26.827  38.436  1.00 83.67           C  
ATOM    952  O   LYS A 121      18.873  25.993  38.025  1.00 83.50           O  
ATOM    953  CB  LYS A 121      17.729  29.027  39.562  1.00 83.05           C  
ATOM    954  CG  LYS A 121      18.007  30.522  39.628  1.00 83.36           C  
ATOM    955  CD  LYS A 121      17.249  31.178  40.772  1.00 83.16           C  
ATOM    956  CE  LYS A 121      17.499  32.677  40.810  1.00 83.29           C  
ATOM    957  NZ  LYS A 121      16.689  33.350  41.863  1.00 82.85           N  
ATOM    958  N   ASN A 122      16.889  26.505  38.959  1.00 84.48           N  
ATOM    959  CA  ASN A 122      16.452  25.123  39.099  1.00 85.02           C  
ATOM    960  C   ASN A 122      16.068  24.489  37.763  1.00 86.03           C  
ATOM    961  O   ASN A 122      15.056  23.794  37.667  1.00 86.36           O  
ATOM    962  CB  ASN A 122      15.265  25.054  40.060  1.00 84.60           C  
ATOM    963  CG  ASN A 122      14.113  25.937  39.622  1.00 84.64           C  
ATOM    964  OD1 ASN A 122      13.561  25.761  38.536  1.00 83.94           O  
ATOM    965  ND2 ASN A 122      13.745  26.897  40.465  1.00 84.36           N  
ATOM    966  N   LYS A 123      16.877  24.734  36.734  1.00 86.84           N  
ATOM    967  CA  LYS A 123      16.627  24.168  35.412  1.00 87.64           C  
ATOM    968  C   LYS A 123      16.663  22.643  35.495  1.00 88.51           C  
ATOM    969  O   LYS A 123      17.070  22.083  36.517  1.00 88.54           O  
ATOM    970  CB  LYS A 123      17.676  24.678  34.417  1.00 87.46           C  
ATOM    971  CG  LYS A 123      19.116  24.605  34.920  1.00 88.00           C  
ATOM    972  CD  LYS A 123      19.700  23.205  34.809  1.00 87.85           C  
ATOM    973  CE  LYS A 123      19.951  22.830  33.356  1.00 87.97           C  
ATOM    974  NZ  LYS A 123      20.933  23.742  32.704  1.00 87.77           N  
ATOM    975  N   ASP A 124      16.237  21.974  34.426  1.00 89.04           N  
ATOM    976  CA  ASP A 124      16.202  20.510  34.393  1.00 89.13           C  
ATOM    977  C   ASP A 124      15.173  20.002  35.401  1.00 88.91           C  
ATOM    978  O   ASP A 124      14.736  18.850  35.337  1.00 88.90           O  
ATOM    979  CB  ASP A 124      17.588  19.925  34.714  1.00 89.21           C  
ATOM    980  CG  ASP A 124      18.567  20.056  33.552  1.00 89.47           C  
ATOM    981  OD1 ASP A 124      19.773  19.793  33.750  1.00 89.19           O  
ATOM    982  OD2 ASP A 124      18.134  20.415  32.436  1.00 89.82           O  
ATOM    983  N   SER A 125      14.793  20.879  36.327  1.00 88.67           N  
ATOM    984  CA  SER A 125      13.812  20.567  37.363  1.00 88.37           C  
ATOM    985  C   SER A 125      12.560  21.398  37.088  1.00 88.13           C  
ATOM    986  O   SER A 125      12.035  22.071  37.979  1.00 88.05           O  
ATOM    987  CB  SER A 125      14.371  20.920  38.745  1.00 88.05           C  
ATOM    988  OG  SER A 125      15.619  20.288  38.970  1.00 87.34           O  
ATOM    989  N   ILE A 126      12.093  21.338  35.844  1.00 87.79           N  
ATOM    990  CA  ILE A 126      10.921  22.090  35.410  1.00 87.26           C  
ATOM    991  C   ILE A 126       9.594  21.541  35.932  1.00 86.33           C  
ATOM    992  O   ILE A 126       9.160  20.453  35.552  1.00 86.00           O  
ATOM    993  CB  ILE A 126      10.863  22.163  33.861  1.00 87.57           C  
ATOM    994  CG1 ILE A 126       9.638  22.965  33.421  1.00 88.00           C  
ATOM    995  CG2 ILE A 126      10.839  20.762  33.267  1.00 88.14           C  
ATOM    996  CD1 ILE A 126       9.652  24.406  33.893  1.00 88.34           C  
ATOM    997  N   ASP A 127       8.956  22.315  36.806  1.00 85.54           N  
ATOM    998  CA  ASP A 127       7.672  21.942  37.392  1.00 84.59           C  
ATOM    999  C   ASP A 127       6.590  22.882  36.873  1.00 83.68           C  
ATOM   1000  O   ASP A 127       6.357  23.948  37.444  1.00 83.92           O  
ATOM   1001  CB  ASP A 127       7.746  22.030  38.917  1.00 84.94           C  
ATOM   1002  CG  ASP A 127       6.393  21.849  39.578  1.00 85.45           C  
ATOM   1003  OD1 ASP A 127       5.723  20.829  39.304  1.00 85.52           O  
ATOM   1004  OD2 ASP A 127       6.000  22.728  40.374  1.00 85.37           O  
ATOM   1005  N   GLN A 128       5.927  22.478  35.794  1.00 82.52           N  
ATOM   1006  CA  GLN A 128       4.890  23.301  35.184  1.00 80.93           C  
ATOM   1007  C   GLN A 128       3.680  23.609  36.061  1.00 80.09           C  
ATOM   1008  O   GLN A 128       2.835  24.421  35.681  1.00 79.74           O  
ATOM   1009  CB  GLN A 128       4.436  22.675  33.860  1.00 80.71           C  
ATOM   1010  CG  GLN A 128       5.505  22.730  32.772  1.00 79.74           C  
ATOM   1011  CD  GLN A 128       4.967  22.398  31.393  1.00 79.39           C  
ATOM   1012  OE1 GLN A 128       4.588  21.258  31.116  1.00 79.60           O  
ATOM   1013  NE2 GLN A 128       4.928  23.399  30.518  1.00 78.55           N  
ATOM   1014  N   VAL A 129       3.585  22.974  37.227  1.00 79.11           N  
ATOM   1015  CA  VAL A 129       2.464  23.246  38.124  1.00 77.97           C  
ATOM   1016  C   VAL A 129       2.812  24.511  38.903  1.00 77.49           C  
ATOM   1017  O   VAL A 129       1.937  25.207  39.421  1.00 77.28           O  
ATOM   1018  CB  VAL A 129       2.216  22.084  39.120  1.00 78.04           C  
ATOM   1019  CG1 VAL A 129       3.245  22.115  40.244  1.00 76.90           C  
ATOM   1020  CG2 VAL A 129       0.802  22.177  39.679  1.00 77.28           C  
ATOM   1021  N   LEU A 130       4.110  24.791  38.973  1.00 76.75           N  
ATOM   1022  CA  LEU A 130       4.631  25.969  39.653  1.00 75.56           C  
ATOM   1023  C   LEU A 130       5.041  26.992  38.599  1.00 74.97           C  
ATOM   1024  O   LEU A 130       4.955  28.200  38.816  1.00 74.96           O  
ATOM   1025  CB  LEU A 130       5.840  25.591  40.508  1.00 75.18           C  
ATOM   1026  CG  LEU A 130       6.780  26.716  40.947  1.00 74.32           C  
ATOM   1027  CD1 LEU A 130       6.006  27.817  41.649  1.00 74.24           C  
ATOM   1028  CD2 LEU A 130       7.842  26.137  41.861  1.00 74.55           C  
ATOM   1029  N   LEU A 131       5.489  26.490  37.455  1.00 74.16           N  
ATOM   1030  CA  LEU A 131       5.910  27.337  36.347  1.00 73.37           C  
ATOM   1031  C   LEU A 131       4.754  28.240  35.920  1.00 72.70           C  
ATOM   1032  O   LEU A 131       4.942  29.425  35.638  1.00 72.67           O  
ATOM   1033  CB  LEU A 131       6.341  26.465  35.166  1.00 73.00           C  
ATOM   1034  CG  LEU A 131       6.925  27.178  33.947  1.00 73.03           C  
ATOM   1035  CD1 LEU A 131       8.310  27.714  34.288  1.00 72.72           C  
ATOM   1036  CD2 LEU A 131       7.003  26.208  32.778  1.00 72.66           C  
ATOM   1037  N   LYS A 132       3.556  27.670  35.873  1.00 71.47           N  
ATOM   1038  CA  LYS A 132       2.375  28.423  35.483  1.00 70.11           C  
ATOM   1039  C   LYS A 132       1.957  29.380  36.597  1.00 69.02           C  
ATOM   1040  O   LYS A 132       1.080  30.222  36.404  1.00 69.49           O  
ATOM   1041  CB  LYS A 132       1.224  27.466  35.153  1.00 70.41           C  
ATOM   1042  CG  LYS A 132      -0.004  28.146  34.555  1.00 70.73           C  
ATOM   1043  CD  LYS A 132       0.339  28.868  33.256  1.00 70.89           C  
ATOM   1044  CE  LYS A 132      -0.866  29.606  32.686  1.00 70.54           C  
ATOM   1045  NZ  LYS A 132      -0.502  30.420  31.491  1.00 70.20           N  
ATOM   1046  N   GLU A 133       2.585  29.251  37.763  1.00 66.95           N  
ATOM   1047  CA  GLU A 133       2.262  30.117  38.891  1.00 65.81           C  
ATOM   1048  C   GLU A 133       2.927  31.474  38.687  1.00 63.97           C  
ATOM   1049  O   GLU A 133       2.262  32.508  38.618  1.00 63.54           O  
ATOM   1050  CB  GLU A 133       2.764  29.513  40.209  1.00 67.65           C  
ATOM   1051  CG  GLU A 133       2.437  28.037  40.433  1.00 70.50           C  
ATOM   1052  CD  GLU A 133       0.948  27.736  40.483  1.00 71.87           C  
ATOM   1053  OE1 GLU A 133       0.271  27.894  39.444  1.00 72.36           O  
ATOM   1054  OE2 GLU A 133       0.459  27.334  41.564  1.00 71.56           O  
ATOM   1055  N   LYS A 134       4.251  31.452  38.592  1.00 61.55           N  
ATOM   1056  CA  LYS A 134       5.038  32.660  38.405  1.00 58.48           C  
ATOM   1057  C   LYS A 134       4.784  33.295  37.046  1.00 56.97           C  
ATOM   1058  O   LYS A 134       4.937  34.505  36.885  1.00 57.15           O  
ATOM   1059  CB  LYS A 134       6.522  32.336  38.558  1.00 57.95           C  
ATOM   1060  CG  LYS A 134       6.866  31.727  39.903  1.00 57.13           C  
ATOM   1061  CD  LYS A 134       8.352  31.468  40.032  1.00 56.68           C  
ATOM   1062  CE  LYS A 134       8.710  31.127  41.464  1.00 56.24           C  
ATOM   1063  NZ  LYS A 134       8.296  32.227  42.379  1.00 56.33           N  
ATOM   1064  N   LYS A 135       4.403  32.481  36.066  1.00 54.90           N  
ATOM   1065  CA  LYS A 135       4.124  33.008  34.736  1.00 52.58           C  
ATOM   1066  C   LYS A 135       2.931  33.955  34.837  1.00 51.34           C  
ATOM   1067  O   LYS A 135       2.918  35.022  34.218  1.00 51.35           O  
ATOM   1068  CB  LYS A 135       3.817  31.875  33.751  1.00 51.72           C  
ATOM   1069  CG  LYS A 135       3.751  32.346  32.303  1.00 51.34           C  
ATOM   1070  CD  LYS A 135       3.799  31.198  31.308  1.00 50.40           C  
ATOM   1071  CE  LYS A 135       3.932  31.728  29.882  1.00 49.57           C  
ATOM   1072  NZ  LYS A 135       4.136  30.646  28.872  1.00 48.19           N  
ATOM   1073  N   ASP A 136       1.937  33.559  35.627  1.00 49.67           N  
ATOM   1074  CA  ASP A 136       0.744  34.376  35.837  1.00 48.89           C  
ATOM   1075  C   ASP A 136       1.086  35.639  36.637  1.00 47.54           C  
ATOM   1076  O   ASP A 136       0.453  36.681  36.464  1.00 46.36           O  
ATOM   1077  CB  ASP A 136      -0.332  33.564  36.568  1.00 49.60           C  
ATOM   1078  CG  ASP A 136      -0.975  32.508  35.681  1.00 50.46           C  
ATOM   1079  OD1 ASP A 136      -1.747  31.677  36.208  1.00 51.31           O  
ATOM   1080  OD2 ASP A 136      -0.716  32.511  34.459  1.00 49.66           O  
ATOM   1081  N   LYS A 137       2.086  35.539  37.512  1.00 45.75           N  
ATOM   1082  CA  LYS A 137       2.516  36.682  38.313  1.00 44.43           C  
ATOM   1083  C   LYS A 137       3.204  37.707  37.421  1.00 43.51           C  
ATOM   1084  O   LYS A 137       3.087  38.913  37.640  1.00 43.48           O  
ATOM   1085  CB  LYS A 137       3.495  36.250  39.404  1.00 44.34           C  
ATOM   1086  CG  LYS A 137       2.899  35.359  40.466  1.00 45.38           C  
ATOM   1087  CD  LYS A 137       3.885  35.142  41.603  1.00 47.39           C  
ATOM   1088  CE  LYS A 137       3.300  34.214  42.653  1.00 49.79           C  
ATOM   1089  NZ  LYS A 137       1.993  34.715  43.172  1.00 50.84           N  
ATOM   1090  N   ALA A 138       3.933  37.219  36.421  1.00 40.96           N  
ATOM   1091  CA  ALA A 138       4.633  38.097  35.499  1.00 38.95           C  
ATOM   1092  C   ALA A 138       3.601  38.900  34.722  1.00 37.75           C  
ATOM   1093  O   ALA A 138       3.740  40.114  34.552  1.00 36.77           O  
ATOM   1094  CB  ALA A 138       5.504  37.278  34.541  1.00 37.77           C  
ATOM   1095  N   HIS A 139       2.559  38.214  34.261  1.00 36.83           N  
ATOM   1096  CA  HIS A 139       1.501  38.867  33.505  1.00 35.53           C  
ATOM   1097  C   HIS A 139       0.711  39.838  34.377  1.00 33.24           C  
ATOM   1098  O   HIS A 139       0.318  40.914  33.910  1.00 31.41           O  
ATOM   1099  CB  HIS A 139       0.570  37.823  32.879  1.00 37.26           C  
ATOM   1100  CG  HIS A 139       1.154  37.141  31.679  1.00 40.72           C  
ATOM   1101  ND1 HIS A 139       0.472  36.184  30.959  1.00 41.89           N  
ATOM   1102  CD2 HIS A 139       2.352  37.290  31.064  1.00 42.16           C  
ATOM   1103  CE1 HIS A 139       1.223  35.774  29.951  1.00 42.42           C  
ATOM   1104  NE2 HIS A 139       2.369  36.429  29.993  1.00 42.35           N  
ATOM   1105  N   VAL A 140       0.476  39.461  35.633  1.00 31.30           N  
ATOM   1106  CA  VAL A 140      -0.248  40.334  36.559  1.00 30.53           C  
ATOM   1107  C   VAL A 140       0.566  41.612  36.721  1.00 28.05           C  
ATOM   1108  O   VAL A 140       0.031  42.717  36.639  1.00 29.51           O  
ATOM   1109  CB  VAL A 140      -0.442  39.677  37.954  1.00 29.74           C  
ATOM   1110  CG1 VAL A 140      -0.852  40.725  38.974  1.00 30.58           C  
ATOM   1111  CG2 VAL A 140      -1.515  38.610  37.878  1.00 29.90           C  
ATOM   1112  N   GLU A 141       1.868  41.445  36.929  1.00 27.03           N  
ATOM   1113  CA  GLU A 141       2.781  42.571  37.087  1.00 24.79           C  
ATOM   1114  C   GLU A 141       2.776  43.477  35.856  1.00 24.78           C  
ATOM   1115  O   GLU A 141       2.594  44.684  35.971  1.00 25.52           O  
ATOM   1116  CB  GLU A 141       4.197  42.055  37.337  1.00 24.62           C  
ATOM   1117  CG  GLU A 141       5.249  43.141  37.525  1.00 23.66           C  
ATOM   1118  CD  GLU A 141       4.954  44.035  38.719  1.00 22.54           C  
ATOM   1119  OE1 GLU A 141       4.574  43.496  39.774  1.00 20.23           O  
ATOM   1120  OE2 GLU A 141       5.109  45.270  38.601  1.00 20.51           O  
ATOM   1121  N   LEU A 142       2.975  42.891  34.678  1.00 23.79           N  
ATOM   1122  CA  LEU A 142       3.003  43.657  33.441  1.00 23.37           C  
ATOM   1123  C   LEU A 142       1.671  44.357  33.186  1.00 24.64           C  
ATOM   1124  O   LEU A 142       1.627  45.435  32.586  1.00 23.77           O  
ATOM   1125  CB  LEU A 142       3.334  42.740  32.254  1.00 25.95           C  
ATOM   1126  CG  LEU A 142       4.664  41.974  32.214  1.00 25.89           C  
ATOM   1127  CD1 LEU A 142       4.639  41.006  31.045  1.00 27.49           C  
ATOM   1128  CD2 LEU A 142       5.839  42.930  32.068  1.00 24.45           C  
ATOM   1129  N   GLY A 143       0.585  43.737  33.639  1.00 25.54           N  
ATOM   1130  CA  GLY A 143      -0.733  44.323  33.452  1.00 24.52           C  
ATOM   1131  C   GLY A 143      -0.826  45.696  34.089  1.00 23.65           C  
ATOM   1132  O   GLY A 143      -1.407  46.616  33.514  1.00 22.42           O  
ATOM   1133  N   HIS A 144      -0.248  45.836  35.281  1.00 22.77           N  
ATOM   1134  CA  HIS A 144      -0.258  47.109  35.990  1.00 20.23           C  
ATOM   1135  C   HIS A 144       0.369  48.183  35.115  1.00 20.33           C  
ATOM   1136  O   HIS A 144      -0.213  49.248  34.902  1.00 21.63           O  
ATOM   1137  CB  HIS A 144       0.528  46.994  37.302  1.00 20.34           C  
ATOM   1138  CG  HIS A 144      -0.128  46.126  38.332  1.00 21.13           C  
ATOM   1139  ND1 HIS A 144       0.537  45.106  38.982  1.00 19.48           N  
ATOM   1140  CD2 HIS A 144      -1.383  46.139  38.839  1.00 19.45           C  
ATOM   1141  CE1 HIS A 144      -0.280  44.530  39.844  1.00 17.29           C  
ATOM   1142  NE2 HIS A 144      -1.450  45.138  39.778  1.00 19.20           N  
ATOM   1143  N   TRP A 145       1.558  47.895  34.597  1.00 20.99           N  
ATOM   1144  CA  TRP A 145       2.265  48.847  33.750  1.00 21.87           C  
ATOM   1145  C   TRP A 145       1.525  49.079  32.443  1.00 22.45           C  
ATOM   1146  O   TRP A 145       1.482  50.200  31.942  1.00 22.31           O  
ATOM   1147  CB  TRP A 145       3.697  48.366  33.499  1.00 19.62           C  
ATOM   1148  CG  TRP A 145       4.402  48.103  34.772  1.00 17.37           C  
ATOM   1149  CD1 TRP A 145       4.504  46.909  35.413  1.00 19.32           C  
ATOM   1150  CD2 TRP A 145       4.978  49.082  35.650  1.00 17.24           C  
ATOM   1151  NE1 TRP A 145       5.101  47.077  36.642  1.00 18.72           N  
ATOM   1152  CE2 TRP A 145       5.401  48.403  36.812  1.00 18.02           C  
ATOM   1153  CE3 TRP A 145       5.172  50.467  35.570  1.00 15.35           C  
ATOM   1154  CZ2 TRP A 145       6.005  49.063  37.890  1.00 17.39           C  
ATOM   1155  CZ3 TRP A 145       5.774  51.123  36.643  1.00 15.11           C  
ATOM   1156  CH2 TRP A 145       6.182  50.418  37.786  1.00 17.41           C  
ATOM   1157  N   GLU A 146       0.936  48.021  31.895  1.00 23.96           N  
ATOM   1158  CA  GLU A 146       0.160  48.143  30.662  1.00 26.53           C  
ATOM   1159  C   GLU A 146      -0.962  49.166  30.888  1.00 27.04           C  
ATOM   1160  O   GLU A 146      -1.172  50.076  30.072  1.00 25.75           O  
ATOM   1161  CB  GLU A 146      -0.439  46.784  30.284  1.00 28.46           C  
ATOM   1162  CG  GLU A 146      -1.465  46.819  29.152  1.00 30.75           C  
ATOM   1163  CD  GLU A 146      -0.880  47.272  27.829  1.00 33.98           C  
ATOM   1164  OE1 GLU A 146       0.240  46.822  27.499  1.00 34.78           O  
ATOM   1165  OE2 GLU A 146      -1.547  48.061  27.114  1.00 32.96           O  
ATOM   1166  N   ASN A 147      -1.668  49.016  32.009  1.00 26.67           N  
ATOM   1167  CA  ASN A 147      -2.761  49.915  32.364  1.00 26.78           C  
ATOM   1168  C   ASN A 147      -2.256  51.342  32.544  1.00 26.59           C  
ATOM   1169  O   ASN A 147      -2.923  52.292  32.154  1.00 26.24           O  
ATOM   1170  CB  ASN A 147      -3.437  49.447  33.655  1.00 30.40           C  
ATOM   1171  CG  ASN A 147      -4.085  48.075  33.523  1.00 33.68           C  
ATOM   1172  OD1 ASN A 147      -4.519  47.493  34.518  1.00 36.43           O  
ATOM   1173  ND2 ASN A 147      -4.162  47.556  32.297  1.00 35.59           N  
ATOM   1174  N   TYR A 148      -1.076  51.484  33.144  1.00 26.58           N  
ATOM   1175  CA  TYR A 148      -0.468  52.798  33.362  1.00 26.08           C  
ATOM   1176  C   TYR A 148      -0.241  53.517  32.034  1.00 26.49           C  
ATOM   1177  O   TYR A 148      -0.655  54.663  31.858  1.00 27.08           O  
ATOM   1178  CB  TYR A 148       0.876  52.646  34.082  1.00 25.42           C  
ATOM   1179  CG  TYR A 148       0.790  52.077  35.482  1.00 22.42           C  
ATOM   1180  CD1 TYR A 148       1.858  51.364  36.021  1.00 21.51           C  
ATOM   1181  CD2 TYR A 148      -0.341  52.278  36.283  1.00 23.21           C  
ATOM   1182  CE1 TYR A 148       1.808  50.863  37.316  1.00 19.43           C  
ATOM   1183  CE2 TYR A 148      -0.399  51.782  37.590  1.00 18.52           C  
ATOM   1184  CZ  TYR A 148       0.681  51.076  38.091  1.00 18.97           C  
ATOM   1185  OH  TYR A 148       0.647  50.562  39.357  1.00 20.66           O  
ATOM   1186  N   LEU A 149       0.440  52.851  31.107  1.00 27.46           N  
ATOM   1187  CA  LEU A 149       0.701  53.433  29.793  1.00 27.86           C  
ATOM   1188  C   LEU A 149      -0.649  53.728  29.134  1.00 31.07           C  
ATOM   1189  O   LEU A 149      -0.825  54.752  28.466  1.00 30.94           O  
ATOM   1190  CB  LEU A 149       1.546  52.465  28.958  1.00 23.95           C  
ATOM   1191  CG  LEU A 149       2.969  52.356  29.527  1.00 22.28           C  
ATOM   1192  CD1 LEU A 149       3.727  51.186  28.947  1.00 20.63           C  
ATOM   1193  CD2 LEU A 149       3.696  53.655  29.248  1.00 22.79           C  
ATOM   1194  N   LYS A 150      -1.610  52.834  29.353  1.00 33.88           N  
ATOM   1195  CA  LYS A 150      -2.953  53.017  28.822  1.00 37.08           C  
ATOM   1196  C   LYS A 150      -3.536  54.295  29.427  1.00 37.72           C  
ATOM   1197  O   LYS A 150      -4.090  55.132  28.719  1.00 38.95           O  
ATOM   1198  CB  LYS A 150      -3.845  51.822  29.186  1.00 38.01           C  
ATOM   1199  CG  LYS A 150      -5.228  51.859  28.524  1.00 41.30           C  
ATOM   1200  CD  LYS A 150      -6.020  50.585  28.787  1.00 43.33           C  
ATOM   1201  CE  LYS A 150      -5.379  49.381  28.110  1.00 45.14           C  
ATOM   1202  NZ  LYS A 150      -5.981  48.090  28.559  1.00 46.70           N  
ATOM   1203  N   GLN A 151      -3.382  54.448  30.738  1.00 38.70           N  
ATOM   1204  CA  GLN A 151      -3.899  55.616  31.447  1.00 40.85           C  
ATOM   1205  C   GLN A 151      -3.278  56.953  31.032  1.00 41.05           C  
ATOM   1206  O   GLN A 151      -3.959  57.978  31.043  1.00 41.98           O  
ATOM   1207  CB  GLN A 151      -3.737  55.429  32.960  1.00 41.64           C  
ATOM   1208  CG  GLN A 151      -4.576  54.300  33.540  1.00 45.54           C  
ATOM   1209  CD  GLN A 151      -4.287  54.036  35.015  1.00 49.02           C  
ATOM   1210  OE1 GLN A 151      -4.914  53.172  35.636  1.00 51.20           O  
ATOM   1211  NE2 GLN A 151      -3.334  54.776  35.581  1.00 49.15           N  
ATOM   1212  N   THR A 152      -1.996  56.960  30.673  1.00 40.08           N  
ATOM   1213  CA  THR A 152      -1.356  58.216  30.276  1.00 39.09           C  
ATOM   1214  C   THR A 152      -1.378  58.414  28.766  1.00 37.64           C  
ATOM   1215  O   THR A 152      -1.541  59.533  28.284  1.00 38.23           O  
ATOM   1216  CB  THR A 152       0.121  58.302  30.754  1.00 38.80           C  
ATOM   1217  OG1 THR A 152       0.922  57.351  30.037  1.00 37.25           O  
ATOM   1218  CG2 THR A 152       0.215  58.021  32.251  1.00 38.49           C  
ATOM   1219  N   GLY A 153      -1.215  57.323  28.025  1.00 35.96           N  
ATOM   1220  CA  GLY A 153      -1.209  57.412  26.578  1.00 35.10           C  
ATOM   1221  C   GLY A 153       0.166  57.780  26.053  1.00 35.19           C  
ATOM   1222  O   GLY A 153       0.383  57.830  24.835  1.00 34.28           O  
ATOM   1223  N   GLY A 154       1.095  58.029  26.977  1.00 33.53           N  
ATOM   1224  CA  GLY A 154       2.454  58.390  26.606  1.00 31.80           C  
ATOM   1225  C   GLY A 154       3.554  57.686  27.395  1.00 29.79           C  
ATOM   1226  O   GLY A 154       3.850  56.511  27.159  1.00 28.75           O  
ATOM   1227  N   PHE A 155       4.163  58.406  28.336  1.00 27.84           N  
ATOM   1228  CA  PHE A 155       5.239  57.852  29.152  1.00 25.48           C  
ATOM   1229  C   PHE A 155       4.689  57.158  30.403  1.00 24.79           C  
ATOM   1230  O   PHE A 155       3.544  57.392  30.792  1.00 26.79           O  
ATOM   1231  CB  PHE A 155       6.227  58.964  29.499  1.00 24.88           C  
ATOM   1232  CG  PHE A 155       6.950  59.520  28.293  1.00 25.62           C  
ATOM   1233  CD1 PHE A 155       8.133  58.937  27.840  1.00 22.39           C  
ATOM   1234  CD2 PHE A 155       6.412  60.590  27.572  1.00 26.89           C  
ATOM   1235  CE1 PHE A 155       8.768  59.407  26.688  1.00 23.98           C  
ATOM   1236  CE2 PHE A 155       7.038  61.066  26.416  1.00 25.67           C  
ATOM   1237  CZ  PHE A 155       8.219  60.472  25.974  1.00 23.70           C  
ATOM   1238  N   VAL A 156       5.505  56.305  31.023  1.00 22.12           N  
ATOM   1239  CA  VAL A 156       5.083  55.533  32.200  1.00 18.96           C  
ATOM   1240  C   VAL A 156       4.429  56.294  33.356  1.00 17.84           C  
ATOM   1241  O   VAL A 156       3.591  55.729  34.056  1.00 19.06           O  
ATOM   1242  CB  VAL A 156       6.256  54.695  32.786  1.00 17.35           C  
ATOM   1243  CG1 VAL A 156       7.121  55.554  33.712  1.00 15.25           C  
ATOM   1244  CG2 VAL A 156       5.705  53.486  33.531  1.00 15.37           C  
ATOM   1245  N   ALA A 157       4.790  57.559  33.552  1.00 17.16           N  
ATOM   1246  CA  ALA A 157       4.232  58.341  34.659  1.00 18.91           C  
ATOM   1247  C   ALA A 157       3.352  59.538  34.261  1.00 19.82           C  
ATOM   1248  O   ALA A 157       2.373  59.849  34.947  1.00 20.12           O  
ATOM   1249  CB  ALA A 157       5.366  58.814  35.572  1.00 19.00           C  
ATOM   1250  N   THR A 158       3.712  60.210  33.171  1.00 21.38           N  
ATOM   1251  CA  THR A 158       2.962  61.363  32.680  1.00 23.16           C  
ATOM   1252  C   THR A 158       3.062  61.398  31.154  1.00 24.61           C  
ATOM   1253  O   THR A 158       3.446  60.410  30.534  1.00 23.11           O  
ATOM   1254  CB  THR A 158       3.529  62.686  33.233  1.00 23.77           C  
ATOM   1255  OG1 THR A 158       4.796  62.949  32.620  1.00 26.80           O  
ATOM   1256  CG2 THR A 158       3.714  62.611  34.755  1.00 21.45           C  
ATOM   1257  N   LYS A 159       2.720  62.533  30.548  1.00 27.38           N  
ATOM   1258  CA  LYS A 159       2.791  62.659  29.092  1.00 29.91           C  
ATOM   1259  C   LYS A 159       4.151  63.187  28.626  1.00 30.32           C  
ATOM   1260  O   LYS A 159       4.317  63.592  27.473  1.00 30.42           O  
ATOM   1261  CB  LYS A 159       1.672  63.567  28.578  1.00 31.36           C  
ATOM   1262  CG  LYS A 159       0.282  62.979  28.759  1.00 33.76           C  
ATOM   1263  CD  LYS A 159      -0.797  63.919  28.235  1.00 35.93           C  
ATOM   1264  CE  LYS A 159      -2.189  63.380  28.545  1.00 36.55           C  
ATOM   1265  NZ  LYS A 159      -2.335  61.962  28.122  1.00 37.11           N  
ATOM   1266  N   GLU A 160       5.115  63.179  29.541  1.00 30.26           N  
ATOM   1267  CA  GLU A 160       6.471  63.622  29.249  1.00 30.31           C  
ATOM   1268  C   GLU A 160       7.446  62.613  29.827  1.00 29.40           C  
ATOM   1269  O   GLU A 160       7.082  61.781  30.671  1.00 29.00           O  
ATOM   1270  CB  GLU A 160       6.762  64.981  29.884  1.00 32.51           C  
ATOM   1271  CG  GLU A 160       5.799  66.082  29.509  1.00 36.80           C  
ATOM   1272  CD  GLU A 160       6.256  67.421  30.039  1.00 39.54           C  
ATOM   1273  OE1 GLU A 160       6.696  67.474  31.205  1.00 39.96           O  
ATOM   1274  OE2 GLU A 160       6.176  68.419  29.293  1.00 43.39           O  
ATOM   1275  N   PHE A 161       8.689  62.699  29.365  1.00 26.75           N  
ATOM   1276  CA  PHE A 161       9.748  61.830  29.834  1.00 22.89           C  
ATOM   1277  C   PHE A 161      10.128  62.326  31.225  1.00 22.10           C  
ATOM   1278  O   PHE A 161      10.356  63.526  31.411  1.00 22.23           O  
ATOM   1279  CB  PHE A 161      10.956  61.947  28.907  1.00 22.54           C  
ATOM   1280  CG  PHE A 161      12.133  61.113  29.331  1.00 20.40           C  
ATOM   1281  CD1 PHE A 161      12.264  59.796  28.895  1.00 20.05           C  
ATOM   1282  CD2 PHE A 161      13.112  61.647  30.162  1.00 19.07           C  
ATOM   1283  CE1 PHE A 161      13.360  59.018  29.277  1.00 19.17           C  
ATOM   1284  CE2 PHE A 161      14.215  60.881  30.555  1.00 20.77           C  
ATOM   1285  CZ  PHE A 161      14.338  59.560  30.108  1.00 20.45           C  
ATOM   1286  N   THR A 162      10.176  61.418  32.200  1.00 18.97           N  
ATOM   1287  CA  THR A 162      10.558  61.790  33.564  1.00 18.39           C  
ATOM   1288  C   THR A 162      11.513  60.745  34.134  1.00 17.52           C  
ATOM   1289  O   THR A 162      11.844  59.766  33.464  1.00 16.70           O  
ATOM   1290  CB  THR A 162       9.323  61.905  34.513  1.00 16.83           C  
ATOM   1291  OG1 THR A 162       8.735  60.615  34.705  1.00 15.13           O  
ATOM   1292  CG2 THR A 162       8.285  62.844  33.937  1.00 14.71           C  
ATOM   1293  N   MET A 163      11.948  60.957  35.371  1.00 17.19           N  
ATOM   1294  CA  MET A 163      12.850  60.025  36.039  1.00 16.57           C  
ATOM   1295  C   MET A 163      12.239  58.624  36.100  1.00 15.81           C  
ATOM   1296  O   MET A 163      12.961  57.631  36.146  1.00 17.85           O  
ATOM   1297  CB  MET A 163      13.159  60.504  37.459  1.00 13.70           C  
ATOM   1298  CG  MET A 163      14.222  59.664  38.169  1.00 10.76           C  
ATOM   1299  SD  MET A 163      15.896  59.872  37.494  1.00 12.83           S  
ATOM   1300  CE  MET A 163      16.517  61.249  38.427  1.00  8.98           C  
ATOM   1301  N   ALA A 164      10.911  58.545  36.096  1.00 16.49           N  
ATOM   1302  CA  ALA A 164      10.226  57.250  36.146  1.00 15.33           C  
ATOM   1303  C   ALA A 164      10.527  56.374  34.930  1.00 15.94           C  
ATOM   1304  O   ALA A 164      10.635  55.151  35.063  1.00 15.36           O  
ATOM   1305  CB  ALA A 164       8.717  57.451  36.273  1.00 15.80           C  
ATOM   1306  N   ASP A 165      10.646  56.991  33.750  1.00 14.10           N  
ATOM   1307  CA  ASP A 165      10.938  56.248  32.531  1.00 12.72           C  
ATOM   1308  C   ASP A 165      12.392  55.775  32.551  1.00 13.15           C  
ATOM   1309  O   ASP A 165      12.742  54.779  31.918  1.00 10.17           O  
ATOM   1310  CB  ASP A 165      10.683  57.114  31.291  1.00 12.46           C  
ATOM   1311  CG  ASP A 165       9.242  57.602  31.205  1.00 15.19           C  
ATOM   1312  OD1 ASP A 165       8.978  58.783  31.522  1.00 15.70           O  
ATOM   1313  OD2 ASP A 165       8.369  56.799  30.836  1.00 14.15           O  
ATOM   1314  N   VAL A 166      13.233  56.508  33.281  1.00 12.54           N  
ATOM   1315  CA  VAL A 166      14.646  56.170  33.422  1.00 11.62           C  
ATOM   1316  C   VAL A 166      14.755  54.830  34.142  1.00 11.42           C  
ATOM   1317  O   VAL A 166      15.633  54.026  33.849  1.00 11.34           O  
ATOM   1318  CB  VAL A 166      15.392  57.242  34.255  1.00 12.83           C  
ATOM   1319  CG1 VAL A 166      16.718  56.688  34.770  1.00 12.19           C  
ATOM   1320  CG2 VAL A 166      15.623  58.488  33.406  1.00 11.70           C  
ATOM   1321  N   PHE A 167      13.844  54.605  35.082  1.00 11.21           N  
ATOM   1322  CA  PHE A 167      13.807  53.377  35.877  1.00 11.81           C  
ATOM   1323  C   PHE A 167      13.096  52.239  35.164  1.00 11.50           C  
ATOM   1324  O   PHE A 167      13.564  51.112  35.148  1.00 11.32           O  
ATOM   1325  CB  PHE A 167      13.074  53.629  37.203  1.00 12.79           C  
ATOM   1326  CG  PHE A 167      13.880  54.376  38.224  1.00 14.50           C  
ATOM   1327  CD1 PHE A 167      14.402  55.635  37.942  1.00 13.65           C  
ATOM   1328  CD2 PHE A 167      14.094  53.824  39.489  1.00 13.83           C  
ATOM   1329  CE1 PHE A 167      15.130  56.345  38.906  1.00 14.57           C  
ATOM   1330  CE2 PHE A 167      14.821  54.522  40.466  1.00 17.75           C  
ATOM   1331  CZ  PHE A 167      15.341  55.788  40.171  1.00 17.16           C  
ATOM   1332  N   PHE A 168      11.949  52.558  34.581  1.00 13.39           N  
ATOM   1333  CA  PHE A 168      11.106  51.587  33.889  1.00 14.48           C  
ATOM   1334  C   PHE A 168      11.637  51.022  32.572  1.00 15.61           C  
ATOM   1335  O   PHE A 168      11.698  49.814  32.396  1.00 18.28           O  
ATOM   1336  CB  PHE A 168       9.731  52.227  33.658  1.00 15.23           C  
ATOM   1337  CG  PHE A 168       8.724  51.326  33.001  1.00 15.49           C  
ATOM   1338  CD1 PHE A 168       8.405  50.095  33.552  1.00 14.51           C  
ATOM   1339  CD2 PHE A 168       8.050  51.743  31.852  1.00 15.40           C  
ATOM   1340  CE1 PHE A 168       7.421  49.288  32.969  1.00 16.66           C  
ATOM   1341  CE2 PHE A 168       7.071  50.949  31.264  1.00 13.64           C  
ATOM   1342  CZ  PHE A 168       6.754  49.723  31.820  1.00 14.89           C  
ATOM   1343  N   PHE A 169      12.027  51.888  31.648  1.00 16.43           N  
ATOM   1344  CA  PHE A 169      12.486  51.418  30.347  1.00 16.90           C  
ATOM   1345  C   PHE A 169      13.576  50.353  30.335  1.00 16.36           C  
ATOM   1346  O   PHE A 169      13.458  49.369  29.622  1.00 17.36           O  
ATOM   1347  CB  PHE A 169      12.936  52.579  29.461  1.00 15.84           C  
ATOM   1348  CG  PHE A 169      13.475  52.125  28.136  1.00 19.54           C  
ATOM   1349  CD1 PHE A 169      12.614  51.655  27.147  1.00 19.42           C  
ATOM   1350  CD2 PHE A 169      14.851  52.090  27.904  1.00 16.34           C  
ATOM   1351  CE1 PHE A 169      13.116  51.153  25.944  1.00 19.26           C  
ATOM   1352  CE2 PHE A 169      15.359  51.594  26.719  1.00 17.94           C  
ATOM   1353  CZ  PHE A 169      14.491  51.122  25.732  1.00 20.08           C  
ATOM   1354  N   PRO A 170      14.662  50.543  31.101  1.00 17.40           N  
ATOM   1355  CA  PRO A 170      15.706  49.517  31.084  1.00 17.34           C  
ATOM   1356  C   PRO A 170      15.157  48.126  31.376  1.00 19.19           C  
ATOM   1357  O   PRO A 170      15.628  47.126  30.821  1.00 16.64           O  
ATOM   1358  CB  PRO A 170      16.672  50.005  32.153  1.00 16.73           C  
ATOM   1359  CG  PRO A 170      16.589  51.493  31.985  1.00 15.41           C  
ATOM   1360  CD  PRO A 170      15.100  51.722  31.872  1.00 15.37           C  
ATOM   1361  N   MET A 171      14.161  48.070  32.253  1.00 19.93           N  
ATOM   1362  CA  MET A 171      13.554  46.801  32.616  1.00 22.44           C  
ATOM   1363  C   MET A 171      12.745  46.254  31.447  1.00 21.50           C  
ATOM   1364  O   MET A 171      12.788  45.054  31.161  1.00 18.67           O  
ATOM   1365  CB  MET A 171      12.681  46.984  33.859  1.00 25.25           C  
ATOM   1366  CG  MET A 171      13.500  47.435  35.071  1.00 27.58           C  
ATOM   1367  SD  MET A 171      12.566  47.410  36.600  1.00 34.40           S  
ATOM   1368  CE  MET A 171      13.346  48.828  37.469  1.00 35.21           C  
ATOM   1369  N   VAL A 172      12.024  47.147  30.769  1.00 21.31           N  
ATOM   1370  CA  VAL A 172      11.227  46.771  29.610  1.00 21.05           C  
ATOM   1371  C   VAL A 172      12.166  46.213  28.532  1.00 22.99           C  
ATOM   1372  O   VAL A 172      11.892  45.164  27.939  1.00 22.37           O  
ATOM   1373  CB  VAL A 172      10.445  47.989  29.048  1.00 21.24           C  
ATOM   1374  CG1 VAL A 172       9.744  47.616  27.744  1.00 19.45           C  
ATOM   1375  CG2 VAL A 172       9.411  48.459  30.069  1.00 19.41           C  
ATOM   1376  N   ALA A 173      13.282  46.903  28.303  1.00 23.03           N  
ATOM   1377  CA  ALA A 173      14.256  46.478  27.293  1.00 24.51           C  
ATOM   1378  C   ALA A 173      14.808  45.101  27.623  1.00 25.11           C  
ATOM   1379  O   ALA A 173      14.841  44.216  26.772  1.00 26.31           O  
ATOM   1380  CB  ALA A 173      15.393  47.484  27.193  1.00 23.27           C  
ATOM   1381  N   LEU A 174      15.243  44.919  28.862  1.00 26.23           N  
ATOM   1382  CA  LEU A 174      15.777  43.634  29.286  1.00 27.56           C  
ATOM   1383  C   LEU A 174      14.753  42.527  29.021  1.00 28.07           C  
ATOM   1384  O   LEU A 174      15.115  41.434  28.597  1.00 27.41           O  
ATOM   1385  CB  LEU A 174      16.133  43.688  30.771  1.00 28.83           C  
ATOM   1386  CG  LEU A 174      16.953  42.545  31.376  1.00 30.79           C  
ATOM   1387  CD1 LEU A 174      18.249  42.339  30.603  1.00 32.17           C  
ATOM   1388  CD2 LEU A 174      17.260  42.887  32.828  1.00 32.18           C  
ATOM   1389  N   ILE A 175      13.476  42.818  29.268  1.00 28.82           N  
ATOM   1390  CA  ILE A 175      12.402  41.848  29.041  1.00 28.93           C  
ATOM   1391  C   ILE A 175      12.342  41.452  27.572  1.00 27.61           C  
ATOM   1392  O   ILE A 175      12.270  40.272  27.235  1.00 27.19           O  
ATOM   1393  CB  ILE A 175      11.020  42.413  29.476  1.00 28.58           C  
ATOM   1394  CG1 ILE A 175      10.954  42.484  31.003  1.00 28.40           C  
ATOM   1395  CG2 ILE A 175       9.897  41.519  28.965  1.00 28.86           C  
ATOM   1396  CD1 ILE A 175       9.705  43.131  31.546  1.00 29.99           C  
ATOM   1397  N   VAL A 176      12.378  42.450  26.702  1.00 27.18           N  
ATOM   1398  CA  VAL A 176      12.345  42.214  25.273  1.00 26.78           C  
ATOM   1399  C   VAL A 176      13.620  41.499  24.816  1.00 28.65           C  
ATOM   1400  O   VAL A 176      13.586  40.696  23.882  1.00 29.42           O  
ATOM   1401  CB  VAL A 176      12.211  43.531  24.514  1.00 25.82           C  
ATOM   1402  CG1 VAL A 176      12.389  43.291  23.026  1.00 26.44           C  
ATOM   1403  CG2 VAL A 176      10.859  44.148  24.798  1.00 23.37           C  
ATOM   1404  N   ARG A 177      14.740  41.803  25.471  1.00 28.30           N  
ATOM   1405  CA  ARG A 177      16.018  41.180  25.143  1.00 27.92           C  
ATOM   1406  C   ARG A 177      15.907  39.689  25.412  1.00 29.29           C  
ATOM   1407  O   ARG A 177      16.628  38.891  24.822  1.00 29.70           O  
ATOM   1408  CB  ARG A 177      17.142  41.786  25.989  1.00 25.87           C  
ATOM   1409  CG  ARG A 177      18.391  40.916  26.127  1.00 25.68           C  
ATOM   1410  CD  ARG A 177      19.269  40.871  24.870  1.00 26.03           C  
ATOM   1411  NE  ARG A 177      20.498  40.107  25.114  1.00 24.94           N  
ATOM   1412  CZ  ARG A 177      21.475  39.925  24.224  1.00 25.34           C  
ATOM   1413  NH1 ARG A 177      22.546  39.214  24.554  1.00 23.36           N  
ATOM   1414  NH2 ARG A 177      21.391  40.455  23.008  1.00 23.08           N  
ATOM   1415  N   GLN A 178      15.003  39.324  26.316  1.00 30.73           N  
ATOM   1416  CA  GLN A 178      14.776  37.923  26.651  1.00 33.07           C  
ATOM   1417  C   GLN A 178      13.776  37.327  25.650  1.00 34.50           C  
ATOM   1418  O   GLN A 178      13.409  36.158  25.754  1.00 34.20           O  
ATOM   1419  CB  GLN A 178      14.231  37.791  28.076  1.00 33.23           C  
ATOM   1420  CG  GLN A 178      15.204  38.184  29.177  1.00 32.95           C  
ATOM   1421  CD  GLN A 178      16.413  37.277  29.241  1.00 35.27           C  
ATOM   1422  OE1 GLN A 178      16.477  36.260  28.547  1.00 36.13           O  
ATOM   1423  NE2 GLN A 178      17.379  37.634  30.084  1.00 32.73           N  
ATOM   1424  N   GLY A 179      13.325  38.154  24.705  1.00 36.70           N  
ATOM   1425  CA  GLY A 179      12.404  37.704  23.669  1.00 40.03           C  
ATOM   1426  C   GLY A 179      10.899  37.717  23.904  1.00 42.27           C  
ATOM   1427  O   GLY A 179      10.221  36.730  23.602  1.00 43.17           O  
ATOM   1428  N   ALA A 180      10.360  38.823  24.413  1.00 42.68           N  
ATOM   1429  CA  ALA A 180       8.920  38.921  24.662  1.00 43.43           C  
ATOM   1430  C   ALA A 180       8.153  39.550  23.498  1.00 44.54           C  
ATOM   1431  O   ALA A 180       8.396  40.702  23.142  1.00 45.91           O  
ATOM   1432  CB  ALA A 180       8.667  39.729  25.929  1.00 42.94           C  
ATOM   1433  N   ASN A 181       7.227  38.801  22.908  1.00 44.45           N  
ATOM   1434  CA  ASN A 181       6.430  39.336  21.807  1.00 45.48           C  
ATOM   1435  C   ASN A 181       5.231  40.075  22.413  1.00 44.92           C  
ATOM   1436  O   ASN A 181       4.115  39.551  22.462  1.00 45.76           O  
ATOM   1437  CB  ASN A 181       5.953  38.205  20.884  1.00 46.80           C  
ATOM   1438  CG  ASN A 181       5.215  38.723  19.650  1.00 48.35           C  
ATOM   1439  OD1 ASN A 181       4.791  37.944  18.790  1.00 48.59           O  
ATOM   1440  ND2 ASN A 181       5.060  40.043  19.561  1.00 48.02           N  
ATOM   1441  N   LEU A 182       5.482  41.298  22.866  1.00 42.39           N  
ATOM   1442  CA  LEU A 182       4.467  42.128  23.503  1.00 41.73           C  
ATOM   1443  C   LEU A 182       3.580  42.892  22.512  1.00 42.81           C  
ATOM   1444  O   LEU A 182       2.624  43.567  22.917  1.00 42.06           O  
ATOM   1445  CB  LEU A 182       5.153  43.139  24.421  1.00 41.13           C  
ATOM   1446  CG  LEU A 182       6.269  42.675  25.357  1.00 38.26           C  
ATOM   1447  CD1 LEU A 182       6.944  43.889  25.971  1.00 36.36           C  
ATOM   1448  CD2 LEU A 182       5.705  41.767  26.426  1.00 37.92           C  
ATOM   1449  N   LYS A 183       3.902  42.791  21.224  1.00 43.17           N  
ATOM   1450  CA  LYS A 183       3.155  43.490  20.176  1.00 41.80           C  
ATOM   1451  C   LYS A 183       1.642  43.448  20.332  1.00 40.48           C  
ATOM   1452  O   LYS A 183       0.990  44.489  20.332  1.00 38.97           O  
ATOM   1453  CB  LYS A 183       3.524  42.939  18.795  1.00 43.14           C  
ATOM   1454  CG  LYS A 183       2.732  43.578  17.647  1.00 45.19           C  
ATOM   1455  CD  LYS A 183       3.024  42.905  16.308  1.00 44.66           C  
ATOM   1456  CE  LYS A 183       2.050  43.380  15.232  1.00 45.45           C  
ATOM   1457  NZ  LYS A 183       0.617  43.101  15.586  1.00 44.89           N  
ATOM   1458  N   ASP A 184       1.085  42.250  20.466  1.00 40.84           N  
ATOM   1459  CA  ASP A 184      -0.364  42.105  20.594  1.00 41.10           C  
ATOM   1460  C   ASP A 184      -0.868  41.919  22.019  1.00 40.30           C  
ATOM   1461  O   ASP A 184      -1.980  42.331  22.338  1.00 39.75           O  
ATOM   1462  CB  ASP A 184      -0.856  40.944  19.719  1.00 43.06           C  
ATOM   1463  CG  ASP A 184      -0.711  41.232  18.232  1.00 44.59           C  
ATOM   1464  OD1 ASP A 184      -1.387  42.158  17.733  1.00 44.72           O  
ATOM   1465  OD2 ASP A 184       0.087  40.538  17.562  1.00 46.75           O  
ATOM   1466  N   SER A 185      -0.057  41.304  22.875  1.00 39.87           N  
ATOM   1467  CA  SER A 185      -0.456  41.079  24.263  1.00 39.66           C  
ATOM   1468  C   SER A 185      -0.418  42.368  25.108  1.00 38.90           C  
ATOM   1469  O   SER A 185      -1.314  42.623  25.907  1.00 38.73           O  
ATOM   1470  CB  SER A 185       0.440  40.002  24.889  1.00 41.24           C  
ATOM   1471  OG  SER A 185       0.434  38.821  24.098  1.00 40.79           O  
ATOM   1472  N   TYR A 186       0.610  43.185  24.915  1.00 37.73           N  
ATOM   1473  CA  TYR A 186       0.752  44.432  25.658  1.00 36.19           C  
ATOM   1474  C   TYR A 186       1.025  45.574  24.681  1.00 36.59           C  
ATOM   1475  O   TYR A 186       2.087  46.192  24.700  1.00 37.33           O  
ATOM   1476  CB  TYR A 186       1.893  44.292  26.666  1.00 34.01           C  
ATOM   1477  CG  TYR A 186       1.603  43.265  27.741  1.00 34.19           C  
ATOM   1478  CD1 TYR A 186       0.674  43.527  28.751  1.00 34.76           C  
ATOM   1479  CD2 TYR A 186       2.231  42.023  27.735  1.00 32.39           C  
ATOM   1480  CE1 TYR A 186       0.379  42.569  29.730  1.00 32.45           C  
ATOM   1481  CE2 TYR A 186       1.943  41.063  28.707  1.00 32.23           C  
ATOM   1482  CZ  TYR A 186       1.017  41.344  29.699  1.00 31.64           C  
ATOM   1483  OH  TYR A 186       0.728  40.400  30.652  1.00 31.15           O  
ATOM   1484  N   PRO A 187       0.047  45.882  23.822  1.00 37.67           N  
ATOM   1485  CA  PRO A 187       0.194  46.953  22.830  1.00 37.26           C  
ATOM   1486  C   PRO A 187       0.728  48.275  23.374  1.00 36.84           C  
ATOM   1487  O   PRO A 187       1.467  48.982  22.682  1.00 37.40           O  
ATOM   1488  CB  PRO A 187      -1.216  47.088  22.253  1.00 36.84           C  
ATOM   1489  CG  PRO A 187      -2.091  46.702  23.416  1.00 38.44           C  
ATOM   1490  CD  PRO A 187      -1.366  45.475  23.944  1.00 37.74           C  
ATOM   1491  N   ASN A 188       0.358  48.623  24.601  1.00 35.72           N  
ATOM   1492  CA  ASN A 188       0.839  49.876  25.164  1.00 34.43           C  
ATOM   1493  C   ASN A 188       2.294  49.810  25.603  1.00 32.57           C  
ATOM   1494  O   ASN A 188       3.041  50.759  25.388  1.00 30.62           O  
ATOM   1495  CB  ASN A 188      -0.037  50.328  26.326  1.00 35.30           C  
ATOM   1496  CG  ASN A 188      -1.281  51.036  25.860  1.00 36.04           C  
ATOM   1497  OD1 ASN A 188      -2.275  50.404  25.502  1.00 35.97           O  
ATOM   1498  ND2 ASN A 188      -1.228  52.364  25.839  1.00 37.17           N  
ATOM   1499  N   ILE A 189       2.703  48.706  26.217  1.00 30.17           N  
ATOM   1500  CA  ILE A 189       4.092  48.595  26.629  1.00 30.78           C  
ATOM   1501  C   ILE A 189       4.953  48.530  25.362  1.00 32.84           C  
ATOM   1502  O   ILE A 189       5.969  49.220  25.259  1.00 32.62           O  
ATOM   1503  CB  ILE A 189       4.339  47.336  27.498  1.00 29.45           C  
ATOM   1504  CG1 ILE A 189       3.564  47.446  28.821  1.00 25.56           C  
ATOM   1505  CG2 ILE A 189       5.844  47.180  27.765  1.00 31.03           C  
ATOM   1506  CD1 ILE A 189       3.766  46.276  29.766  1.00 17.97           C  
ATOM   1507  N   PHE A 190       4.527  47.718  24.393  1.00 34.39           N  
ATOM   1508  CA  PHE A 190       5.245  47.568  23.132  1.00 34.78           C  
ATOM   1509  C   PHE A 190       5.333  48.913  22.424  1.00 35.98           C  
ATOM   1510  O   PHE A 190       6.386  49.280  21.896  1.00 36.62           O  
ATOM   1511  CB  PHE A 190       4.530  46.559  22.231  1.00 37.84           C  
ATOM   1512  CG  PHE A 190       5.146  46.412  20.862  1.00 38.63           C  
ATOM   1513  CD1 PHE A 190       4.455  46.827  19.724  1.00 38.00           C  
ATOM   1514  CD2 PHE A 190       6.410  45.837  20.708  1.00 39.70           C  
ATOM   1515  CE1 PHE A 190       5.009  46.667  18.447  1.00 37.24           C  
ATOM   1516  CE2 PHE A 190       6.975  45.673  19.436  1.00 38.91           C  
ATOM   1517  CZ  PHE A 190       6.271  46.088  18.304  1.00 37.71           C  
ATOM   1518  N   LYS A 191       4.227  49.649  22.412  1.00 34.39           N  
ATOM   1519  CA  LYS A 191       4.223  50.956  21.774  1.00 35.50           C  
ATOM   1520  C   LYS A 191       5.219  51.850  22.505  1.00 34.69           C  
ATOM   1521  O   LYS A 191       5.909  52.668  21.888  1.00 36.96           O  
ATOM   1522  CB  LYS A 191       2.828  51.585  21.826  1.00 36.37           C  
ATOM   1523  CG  LYS A 191       2.798  53.006  21.266  1.00 40.45           C  
ATOM   1524  CD  LYS A 191       1.411  53.646  21.294  1.00 39.81           C  
ATOM   1525  CE  LYS A 191       1.488  55.064  20.729  1.00 41.77           C  
ATOM   1526  NZ  LYS A 191       0.172  55.762  20.641  1.00 42.91           N  
ATOM   1527  N   TYR A 192       5.279  51.684  23.825  1.00 32.26           N  
ATOM   1528  CA  TYR A 192       6.177  52.446  24.693  1.00 27.72           C  
ATOM   1529  C   TYR A 192       7.621  52.071  24.396  1.00 26.03           C  
ATOM   1530  O   TYR A 192       8.491  52.925  24.340  1.00 24.40           O  
ATOM   1531  CB  TYR A 192       5.864  52.139  26.164  1.00 25.96           C  
ATOM   1532  CG  TYR A 192       6.814  52.768  27.173  1.00 24.52           C  
ATOM   1533  CD1 TYR A 192       6.728  54.121  27.499  1.00 22.63           C  
ATOM   1534  CD2 TYR A 192       7.799  52.002  27.804  1.00 22.50           C  
ATOM   1535  CE1 TYR A 192       7.601  54.700  28.435  1.00 22.08           C  
ATOM   1536  CE2 TYR A 192       8.669  52.568  28.734  1.00 22.59           C  
ATOM   1537  CZ  TYR A 192       8.565  53.914  29.046  1.00 21.48           C  
ATOM   1538  OH  TYR A 192       9.421  54.466  29.974  1.00 21.36           O  
ATOM   1539  N   TYR A 193       7.862  50.780  24.215  1.00 27.56           N  
ATOM   1540  CA  TYR A 193       9.197  50.264  23.926  1.00 29.65           C  
ATOM   1541  C   TYR A 193       9.757  50.823  22.619  1.00 30.97           C  
ATOM   1542  O   TYR A 193      10.824  51.446  22.612  1.00 30.30           O  
ATOM   1543  CB  TYR A 193       9.146  48.740  23.857  1.00 28.10           C  
ATOM   1544  CG  TYR A 193      10.460  48.080  23.541  1.00 29.94           C  
ATOM   1545  CD1 TYR A 193      11.522  48.132  24.439  1.00 30.36           C  
ATOM   1546  CD2 TYR A 193      10.633  47.364  22.356  1.00 31.54           C  
ATOM   1547  CE1 TYR A 193      12.723  47.483  24.172  1.00 31.94           C  
ATOM   1548  CE2 TYR A 193      11.831  46.712  22.075  1.00 31.75           C  
ATOM   1549  CZ  TYR A 193      12.870  46.772  22.988  1.00 32.79           C  
ATOM   1550  OH  TYR A 193      14.040  46.097  22.736  1.00 29.29           O  
ATOM   1551  N   ASN A 194       9.031  50.604  21.522  1.00 32.61           N  
ATOM   1552  CA  ASN A 194       9.447  51.075  20.199  1.00 34.80           C  
ATOM   1553  C   ASN A 194       9.630  52.584  20.194  1.00 35.06           C  
ATOM   1554  O   ASN A 194      10.516  53.121  19.524  1.00 35.71           O  
ATOM   1555  CB  ASN A 194       8.399  50.699  19.153  1.00 37.42           C  
ATOM   1556  CG  ASN A 194       8.135  49.212  19.105  1.00 39.55           C  
ATOM   1557  OD1 ASN A 194       7.163  48.768  18.500  1.00 41.13           O  
ATOM   1558  ND2 ASN A 194       9.004  48.430  19.742  1.00 38.02           N  
ATOM   1559  N   MET A 195       8.774  53.267  20.940  1.00 34.73           N  
ATOM   1560  CA  MET A 195       8.845  54.715  21.031  1.00 34.34           C  
ATOM   1561  C   MET A 195      10.161  55.078  21.722  1.00 33.56           C  
ATOM   1562  O   MET A 195      10.962  55.860  21.201  1.00 34.06           O  
ATOM   1563  CB  MET A 195       7.651  55.233  21.837  1.00 36.34           C  
ATOM   1564  CG  MET A 195       7.433  56.734  21.774  1.00 38.57           C  
ATOM   1565  SD  MET A 195       8.012  57.611  23.231  1.00 42.08           S  
ATOM   1566  CE  MET A 195       6.987  56.844  24.511  1.00 40.43           C  
ATOM   1567  N   MET A 196      10.385  54.488  22.891  1.00 29.93           N  
ATOM   1568  CA  MET A 196      11.598  54.747  23.664  1.00 27.53           C  
ATOM   1569  C   MET A 196      12.872  54.347  22.907  1.00 24.30           C  
ATOM   1570  O   MET A 196      13.830  55.115  22.849  1.00 21.52           O  
ATOM   1571  CB  MET A 196      11.519  54.009  25.008  1.00 25.33           C  
ATOM   1572  CG  MET A 196      10.469  54.579  25.959  1.00 24.68           C  
ATOM   1573  SD  MET A 196      10.859  56.260  26.484  1.00 25.05           S  
ATOM   1574  CE  MET A 196      11.772  55.913  27.952  1.00 26.95           C  
ATOM   1575  N   MET A 197      12.868  53.149  22.331  1.00 22.58           N  
ATOM   1576  CA  MET A 197      14.007  52.639  21.574  1.00 24.04           C  
ATOM   1577  C   MET A 197      14.460  53.605  20.492  1.00 25.80           C  
ATOM   1578  O   MET A 197      15.585  53.522  20.010  1.00 26.45           O  
ATOM   1579  CB  MET A 197      13.644  51.306  20.924  1.00 22.83           C  
ATOM   1580  CG  MET A 197      13.763  50.119  21.852  1.00 22.63           C  
ATOM   1581  SD  MET A 197      15.474  49.847  22.325  1.00 20.71           S  
ATOM   1582  CE  MET A 197      16.025  48.911  20.863  1.00 21.27           C  
ATOM   1583  N   ASP A 198      13.570  54.522  20.130  1.00 27.34           N  
ATOM   1584  CA  ASP A 198      13.811  55.512  19.097  1.00 29.16           C  
ATOM   1585  C   ASP A 198      14.394  56.808  19.644  1.00 29.27           C  
ATOM   1586  O   ASP A 198      14.899  57.639  18.888  1.00 30.72           O  
ATOM   1587  CB  ASP A 198      12.491  55.809  18.394  1.00 35.80           C  
ATOM   1588  CG  ASP A 198      12.680  56.229  16.963  1.00 41.38           C  
ATOM   1589  OD1 ASP A 198      13.064  57.399  16.722  1.00 43.68           O  
ATOM   1590  OD2 ASP A 198      12.451  55.369  16.082  1.00 43.70           O  
ATOM   1591  N   ARG A 199      14.308  56.994  20.955  1.00 26.38           N  
ATOM   1592  CA  ARG A 199      14.836  58.199  21.587  1.00 24.29           C  
ATOM   1593  C   ARG A 199      16.372  58.175  21.495  1.00 23.31           C  
ATOM   1594  O   ARG A 199      17.014  57.209  21.908  1.00 22.84           O  
ATOM   1595  CB  ARG A 199      14.368  58.232  23.050  1.00 23.08           C  
ATOM   1596  CG  ARG A 199      14.460  59.573  23.741  1.00 21.12           C  
ATOM   1597  CD  ARG A 199      14.042  59.430  25.207  1.00 22.06           C  
ATOM   1598  NE  ARG A 199      14.175  60.686  25.936  1.00 21.28           N  
ATOM   1599  CZ  ARG A 199      13.272  61.658  25.909  1.00 20.73           C  
ATOM   1600  NH1 ARG A 199      13.476  62.774  26.599  1.00 15.11           N  
ATOM   1601  NH2 ARG A 199      12.156  61.500  25.200  1.00 21.94           N  
ATOM   1602  N   PRO A 200      16.981  59.243  20.959  1.00 24.11           N  
ATOM   1603  CA  PRO A 200      18.442  59.331  20.811  1.00 23.73           C  
ATOM   1604  C   PRO A 200      19.244  58.818  22.015  1.00 23.72           C  
ATOM   1605  O   PRO A 200      20.122  57.964  21.876  1.00 23.70           O  
ATOM   1606  CB  PRO A 200      18.673  60.818  20.559  1.00 22.53           C  
ATOM   1607  CG  PRO A 200      17.439  61.224  19.828  1.00 24.31           C  
ATOM   1608  CD  PRO A 200      16.346  60.528  20.615  1.00 24.38           C  
ATOM   1609  N   THR A 201      18.932  59.354  23.189  1.00 22.67           N  
ATOM   1610  CA  THR A 201      19.598  58.989  24.437  1.00 23.89           C  
ATOM   1611  C   THR A 201      19.602  57.484  24.724  1.00 21.98           C  
ATOM   1612  O   THR A 201      20.557  56.947  25.278  1.00 20.34           O  
ATOM   1613  CB  THR A 201      18.931  59.724  25.623  1.00 24.38           C  
ATOM   1614  OG1 THR A 201      19.163  61.133  25.496  1.00 24.72           O  
ATOM   1615  CG2 THR A 201      19.505  59.246  26.943  1.00 30.95           C  
ATOM   1616  N   ILE A 202      18.528  56.810  24.341  1.00 21.98           N  
ATOM   1617  CA  ILE A 202      18.411  55.380  24.561  1.00 21.22           C  
ATOM   1618  C   ILE A 202      19.198  54.599  23.515  1.00 21.80           C  
ATOM   1619  O   ILE A 202      19.816  53.585  23.831  1.00 19.51           O  
ATOM   1620  CB  ILE A 202      16.927  54.951  24.550  1.00 22.35           C  
ATOM   1621  CG1 ILE A 202      16.254  55.450  25.833  1.00 20.96           C  
ATOM   1622  CG2 ILE A 202      16.807  53.436  24.409  1.00 21.21           C  
ATOM   1623  CD1 ILE A 202      14.826  55.024  25.979  1.00 22.90           C  
ATOM   1624  N   VAL A 203      19.179  55.068  22.271  1.00 21.34           N  
ATOM   1625  CA  VAL A 203      19.929  54.384  21.225  1.00 22.16           C  
ATOM   1626  C   VAL A 203      21.394  54.406  21.629  1.00 22.49           C  
ATOM   1627  O   VAL A 203      22.095  53.412  21.488  1.00 22.72           O  
ATOM   1628  CB  VAL A 203      19.785  55.081  19.848  1.00 21.56           C  
ATOM   1629  CG1 VAL A 203      20.774  54.474  18.842  1.00 21.89           C  
ATOM   1630  CG2 VAL A 203      18.366  54.927  19.336  1.00 21.61           C  
ATOM   1631  N   LYS A 204      21.838  55.549  22.146  1.00 23.48           N  
ATOM   1632  CA  LYS A 204      23.221  55.741  22.573  1.00 23.20           C  
ATOM   1633  C   LYS A 204      23.665  54.917  23.784  1.00 22.32           C  
ATOM   1634  O   LYS A 204      24.858  54.661  23.963  1.00 21.82           O  
ATOM   1635  CB  LYS A 204      23.474  57.229  22.843  1.00 24.95           C  
ATOM   1636  CG  LYS A 204      23.502  58.066  21.569  1.00 31.56           C  
ATOM   1637  CD  LYS A 204      24.626  57.592  20.630  1.00 35.09           C  
ATOM   1638  CE  LYS A 204      24.384  58.010  19.175  1.00 36.25           C  
ATOM   1639  NZ  LYS A 204      23.169  57.368  18.592  1.00 36.01           N  
ATOM   1640  N   THR A 205      22.718  54.490  24.609  1.00 21.47           N  
ATOM   1641  CA  THR A 205      23.082  53.711  25.783  1.00 20.38           C  
ATOM   1642  C   THR A 205      22.664  52.242  25.761  1.00 20.16           C  
ATOM   1643  O   THR A 205      22.599  51.613  26.815  1.00 18.80           O  
ATOM   1644  CB  THR A 205      22.532  54.352  27.068  1.00 19.28           C  
ATOM   1645  OG1 THR A 205      21.105  54.424  26.990  1.00 18.23           O  
ATOM   1646  CG2 THR A 205      23.103  55.754  27.253  1.00 19.42           C  
ATOM   1647  N   MET A 206      22.376  51.691  24.581  1.00 18.02           N  
ATOM   1648  CA  MET A 206      22.003  50.280  24.506  1.00 19.03           C  
ATOM   1649  C   MET A 206      23.186  49.470  25.018  1.00 16.91           C  
ATOM   1650  O   MET A 206      24.324  49.807  24.731  1.00 20.68           O  
ATOM   1651  CB  MET A 206      21.705  49.857  23.060  1.00 21.18           C  
ATOM   1652  CG  MET A 206      20.446  50.465  22.454  1.00 24.13           C  
ATOM   1653  SD  MET A 206      18.952  49.976  23.326  1.00 24.46           S  
ATOM   1654  CE  MET A 206      18.825  48.257  22.810  1.00 25.07           C  
ATOM   1655  N   PRO A 207      22.935  48.400  25.791  1.00 16.50           N  
ATOM   1656  CA  PRO A 207      23.999  47.545  26.334  1.00 17.00           C  
ATOM   1657  C   PRO A 207      24.950  47.089  25.229  1.00 18.13           C  
ATOM   1658  O   PRO A 207      24.559  46.336  24.337  1.00 18.72           O  
ATOM   1659  CB  PRO A 207      23.228  46.374  26.927  1.00 16.12           C  
ATOM   1660  CG  PRO A 207      21.967  47.010  27.381  1.00 17.21           C  
ATOM   1661  CD  PRO A 207      21.614  47.925  26.233  1.00 16.82           C  
ATOM   1662  N   PRO A 208      26.217  47.518  25.293  1.00 18.69           N  
ATOM   1663  CA  PRO A 208      27.246  47.176  24.307  1.00 18.75           C  
ATOM   1664  C   PRO A 208      27.354  45.741  23.793  1.00 19.32           C  
ATOM   1665  O   PRO A 208      27.557  45.535  22.592  1.00 16.54           O  
ATOM   1666  CB  PRO A 208      28.532  47.633  24.987  1.00 17.35           C  
ATOM   1667  CG  PRO A 208      28.071  48.863  25.737  1.00 17.97           C  
ATOM   1668  CD  PRO A 208      26.776  48.381  26.353  1.00 19.55           C  
ATOM   1669  N   HIS A 209      27.222  44.754  24.681  1.00 18.79           N  
ATOM   1670  CA  HIS A 209      27.375  43.360  24.265  1.00 18.13           C  
ATOM   1671  C   HIS A 209      26.175  42.726  23.586  1.00 17.62           C  
ATOM   1672  O   HIS A 209      26.275  41.612  23.085  1.00 16.58           O  
ATOM   1673  CB  HIS A 209      27.792  42.474  25.449  1.00 17.93           C  
ATOM   1674  CG  HIS A 209      26.652  42.018  26.311  1.00 20.25           C  
ATOM   1675  ND1 HIS A 209      26.125  42.790  27.325  1.00 20.43           N  
ATOM   1676  CD2 HIS A 209      25.969  40.849  26.336  1.00 21.06           C  
ATOM   1677  CE1 HIS A 209      25.172  42.113  27.943  1.00 21.27           C  
ATOM   1678  NE2 HIS A 209      25.058  40.932  27.362  1.00 21.99           N  
ATOM   1679  N   TRP A 210      25.054  43.432  23.550  1.00 18.40           N  
ATOM   1680  CA  TRP A 210      23.840  42.890  22.948  1.00 20.17           C  
ATOM   1681  C   TRP A 210      23.890  42.688  21.434  1.00 20.86           C  
ATOM   1682  O   TRP A 210      23.427  41.668  20.927  1.00 22.36           O  
ATOM   1683  CB  TRP A 210      22.642  43.776  23.315  1.00 21.18           C  
ATOM   1684  CG  TRP A 210      22.128  43.590  24.741  1.00 21.63           C  
ATOM   1685  CD1 TRP A 210      22.664  42.792  25.724  1.00 19.84           C  
ATOM   1686  CD2 TRP A 210      20.963  44.201  25.315  1.00 19.87           C  
ATOM   1687  NE1 TRP A 210      21.901  42.870  26.867  1.00 20.00           N  
ATOM   1688  CE2 TRP A 210      20.851  43.727  26.643  1.00 21.01           C  
ATOM   1689  CE3 TRP A 210      20.000  45.100  24.833  1.00 21.05           C  
ATOM   1690  CZ2 TRP A 210      19.813  44.123  27.496  1.00 21.23           C  
ATOM   1691  CZ3 TRP A 210      18.963  45.496  25.683  1.00 22.11           C  
ATOM   1692  CH2 TRP A 210      18.881  45.004  27.000  1.00 22.18           C  
ATOM   1693  N   ALA A 211      24.461  43.645  20.713  1.00 21.38           N  
ATOM   1694  CA  ALA A 211      24.534  43.555  19.257  1.00 21.62           C  
ATOM   1695  C   ALA A 211      25.154  42.267  18.703  1.00 22.48           C  
ATOM   1696  O   ALA A 211      24.588  41.647  17.807  1.00 22.40           O  
ATOM   1697  CB  ALA A 211      25.277  44.763  18.702  1.00 21.11           C  
ATOM   1698  N   GLU A 212      26.307  41.859  19.230  1.00 23.56           N  
ATOM   1699  CA  GLU A 212      26.978  40.656  18.730  1.00 25.19           C  
ATOM   1700  C   GLU A 212      26.764  39.385  19.551  1.00 27.18           C  
ATOM   1701  O   GLU A 212      27.583  38.470  19.510  1.00 26.55           O  
ATOM   1702  CB  GLU A 212      28.482  40.913  18.589  1.00 23.52           C  
ATOM   1703  CG  GLU A 212      28.860  42.001  17.584  1.00 21.21           C  
ATOM   1704  CD  GLU A 212      28.393  41.688  16.177  1.00 21.61           C  
ATOM   1705  OE1 GLU A 212      27.897  40.565  15.949  1.00 20.44           O  
ATOM   1706  OE2 GLU A 212      28.522  42.567  15.298  1.00 21.57           O  
ATOM   1707  N   SER A 213      25.674  39.327  20.304  1.00 30.69           N  
ATOM   1708  CA  SER A 213      25.379  38.144  21.102  1.00 33.83           C  
ATOM   1709  C   SER A 213      23.907  37.793  20.971  1.00 36.80           C  
ATOM   1710  O   SER A 213      23.068  38.656  20.690  1.00 37.41           O  
ATOM   1711  CB  SER A 213      25.751  38.375  22.571  1.00 34.23           C  
ATOM   1712  OG  SER A 213      25.111  39.521  23.094  1.00 34.11           O  
ATOM   1713  N   ASP A 214      23.593  36.519  21.162  1.00 40.07           N  
ATOM   1714  CA  ASP A 214      22.217  36.061  21.046  1.00 44.32           C  
ATOM   1715  C   ASP A 214      21.390  36.256  22.313  1.00 45.77           C  
ATOM   1716  O   ASP A 214      21.894  36.157  23.433  1.00 45.00           O  
ATOM   1717  CB  ASP A 214      22.188  34.584  20.627  1.00 45.29           C  
ATOM   1718  CG  ASP A 214      22.141  34.404  19.114  1.00 46.87           C  
ATOM   1719  OD1 ASP A 214      22.853  35.140  18.397  1.00 48.72           O  
ATOM   1720  OD2 ASP A 214      21.393  33.520  18.643  1.00 47.31           O  
ATOM   1721  N   SER A 215      20.110  36.546  22.107  1.00 47.03           N  
ATOM   1722  CA  SER A 215      19.157  36.743  23.187  1.00 49.00           C  
ATOM   1723  C   SER A 215      19.096  35.487  24.063  1.00 49.12           C  
ATOM   1724  O   SER A 215      19.087  34.366  23.552  1.00 49.93           O  
ATOM   1725  CB  SER A 215      17.773  37.033  22.583  1.00 49.48           C  
ATOM   1726  OG  SER A 215      16.735  36.890  23.539  1.00 52.05           O  
ATOM   1727  N   PRO A 216      19.070  35.654  25.395  1.00 49.19           N  
ATOM   1728  CA  PRO A 216      19.005  34.467  26.261  1.00 48.49           C  
ATOM   1729  C   PRO A 216      17.695  33.714  25.990  1.00 47.17           C  
ATOM   1730  O   PRO A 216      17.586  32.508  26.225  1.00 45.46           O  
ATOM   1731  CB  PRO A 216      19.062  35.060  27.669  1.00 49.16           C  
ATOM   1732  CG  PRO A 216      19.853  36.339  27.469  1.00 49.42           C  
ATOM   1733  CD  PRO A 216      19.258  36.882  26.187  1.00 48.80           C  
ATOM   1734  N   GLY A 217      16.708  34.454  25.490  1.00 46.92           N  
ATOM   1735  CA  GLY A 217      15.411  33.887  25.149  1.00 47.03           C  
ATOM   1736  C   GLY A 217      14.583  33.256  26.256  1.00 46.51           C  
ATOM   1737  O   GLY A 217      13.592  32.580  25.970  1.00 46.80           O  
ATOM   1738  N   ASN A 218      14.966  33.471  27.510  1.00 46.10           N  
ATOM   1739  CA  ASN A 218      14.226  32.898  28.634  1.00 46.69           C  
ATOM   1740  C   ASN A 218      12.786  33.398  28.754  1.00 45.65           C  
ATOM   1741  O   ASN A 218      12.069  33.007  29.669  1.00 46.47           O  
ATOM   1742  CB  ASN A 218      14.956  33.169  29.951  1.00 46.70           C  
ATOM   1743  CG  ASN A 218      16.288  32.461  30.033  1.00 47.26           C  
ATOM   1744  OD1 ASN A 218      16.374  31.251  29.837  1.00 48.68           O  
ATOM   1745  ND2 ASN A 218      17.339  33.213  30.332  1.00 49.19           N  
ATOM   1746  N   LEU A 219      12.359  34.254  27.832  1.00 45.09           N  
ATOM   1747  CA  LEU A 219      11.000  34.780  27.870  1.00 45.17           C  
ATOM   1748  C   LEU A 219      10.224  34.598  26.559  1.00 45.35           C  
ATOM   1749  O   LEU A 219       9.065  35.001  26.462  1.00 45.22           O  
ATOM   1750  CB  LEU A 219      11.029  36.263  28.264  1.00 45.58           C  
ATOM   1751  CG  LEU A 219      11.421  36.586  29.710  1.00 44.94           C  
ATOM   1752  CD1 LEU A 219      11.278  38.077  29.964  1.00 45.20           C  
ATOM   1753  CD2 LEU A 219      10.526  35.809  30.664  1.00 45.50           C  
ATOM   1754  N   LEU A 220      10.859  33.981  25.564  1.00 44.43           N  
ATOM   1755  CA  LEU A 220      10.232  33.739  24.262  1.00 44.53           C  
ATOM   1756  C   LEU A 220       8.808  33.193  24.338  1.00 44.02           C  
ATOM   1757  O   LEU A 220       8.019  33.369  23.409  1.00 42.45           O  
ATOM   1758  CB  LEU A 220      11.084  32.769  23.438  1.00 45.92           C  
ATOM   1759  CG  LEU A 220      11.970  33.377  22.353  1.00 47.35           C  
ATOM   1760  CD1 LEU A 220      12.747  32.270  21.647  1.00 48.78           C  
ATOM   1761  CD2 LEU A 220      11.096  34.149  21.359  1.00 47.20           C  
ATOM   1762  N   ASP A 221       8.488  32.530  25.445  1.00 43.66           N  
ATOM   1763  CA  ASP A 221       7.169  31.942  25.651  1.00 44.86           C  
ATOM   1764  C   ASP A 221       6.196  32.850  26.413  1.00 45.12           C  
ATOM   1765  O   ASP A 221       4.982  32.640  26.378  1.00 44.75           O  
ATOM   1766  CB  ASP A 221       7.322  30.626  26.415  1.00 44.56           C  
ATOM   1767  CG  ASP A 221       8.165  30.779  27.668  1.00 44.52           C  
ATOM   1768  OD1 ASP A 221       9.390  30.982  27.542  1.00 44.14           O  
ATOM   1769  OD2 ASP A 221       7.601  30.711  28.779  1.00 46.16           O  
ATOM   1770  N   LEU A 222       6.733  33.854  27.098  1.00 45.87           N  
ATOM   1771  CA  LEU A 222       5.931  34.772  27.900  1.00 46.41           C  
ATOM   1772  C   LEU A 222       4.507  34.976  27.417  1.00 47.45           C  
ATOM   1773  O   LEU A 222       3.556  34.554  28.072  1.00 47.49           O  
ATOM   1774  CB  LEU A 222       6.603  36.138  27.981  1.00 45.42           C  
ATOM   1775  CG  LEU A 222       5.840  37.124  28.863  1.00 43.46           C  
ATOM   1776  CD1 LEU A 222       6.021  36.723  30.320  1.00 43.92           C  
ATOM   1777  CD2 LEU A 222       6.349  38.533  28.632  1.00 44.89           C  
ATOM   1778  N   CYS A 223       4.377  35.638  26.270  1.00 48.78           N  
ATOM   1779  CA  CYS A 223       3.077  35.948  25.683  1.00 49.76           C  
ATOM   1780  C   CYS A 223       3.173  36.047  24.162  1.00 49.25           C  
ATOM   1781  O   CYS A 223       3.240  35.036  23.465  1.00 48.99           O  
ATOM   1782  CB  CYS A 223       2.566  37.277  26.247  1.00 50.95           C  
ATOM   1783  SG  CYS A 223       3.775  38.630  26.082  1.00 51.65           S  
TER    1784      CYS A 223                                                      
HETATM 1785  N1  GSH A 300      21.281  48.410  44.280  1.00 27.04           N  
HETATM 1786  CA1 GSH A 300      22.353  48.587  43.381  1.00 27.98           C  
HETATM 1787  C1  GSH A 300      21.947  49.648  42.404  1.00 27.70           C  
HETATM 1788  O11 GSH A 300      22.866  50.326  42.109  1.00 28.17           O  
HETATM 1789  O12 GSH A 300      20.872  49.738  42.018  1.00 25.76           O  
HETATM 1790  CB1 GSH A 300      22.677  47.238  42.728  1.00 30.74           C  
HETATM 1791  CG1 GSH A 300      23.815  47.142  41.689  1.00 33.46           C  
HETATM 1792  CD1 GSH A 300      24.080  45.779  41.101  1.00 35.57           C  
HETATM 1793  OE1 GSH A 300      23.397  44.882  41.486  1.00 34.77           O  
HETATM 1794  N2  GSH A 300      25.037  45.684  40.221  1.00 37.37           N  
HETATM 1795  CA2 GSH A 300      25.441  44.503  39.565  1.00 39.10           C  
HETATM 1796  C2  GSH A 300      26.854  44.264  39.994  1.00 39.60           C  
HETATM 1797  O2  GSH A 300      27.783  44.957  39.850  1.00 36.06           O  
HETATM 1798  CB2 GSH A 300      25.384  44.582  38.019  1.00 39.52           C  
HETATM 1799  SG2 GSH A 300      23.742  44.864  37.378  1.00 40.58           S  
HETATM 1800  N3  GSH A 300      26.863  43.193  40.534  1.00 40.49           N  
HETATM 1801  CA3 GSH A 300      27.977  42.609  41.071  1.00 44.34           C  
HETATM 1802  C3  GSH A 300      27.962  41.930  42.346  1.00 45.86           C  
HETATM 1803  O31 GSH A 300      29.031  41.525  42.573  1.00 47.60           O  
HETATM 1804  O32 GSH A 300      27.030  41.760  43.128  1.00 48.21           O  
HETATM 1805  O   HOH A 224       6.613  59.925  32.825  1.00 18.99           O  
HETATM 1806  O   HOH A 225      23.453  47.526  46.281  1.00 16.64           O  
HETATM 1807  O   HOH A 226      28.906  44.929  15.990  1.00 14.28           O  
HETATM 1808  O   HOH A 227      25.547  50.450  47.260  1.00 12.78           O  
HETATM 1809  O   HOH A 228      25.642  50.200  42.585  1.00 25.75           O  
HETATM 1810  O   HOH A 229      26.639  48.996  45.009  1.00 14.72           O  
HETATM 1811  O   HOH A 230       1.474  55.915  35.840  1.00 19.86           O  
HETATM 1812  O   HOH A 231      19.820  52.205  43.811  1.00 16.09           O  
HETATM 1813  O   HOH A 232       4.194  54.538  24.649  1.00 40.21           O  
HETATM 1814  O   HOH A 233      28.369  56.151  27.748  1.00 19.64           O  
HETATM 1815  O   HOH A 234       1.531  48.680  20.105  1.00 29.02           O  
HETATM 1816  O   HOH A 235      -2.593  43.576  36.489  1.00 29.10           O  
HETATM 1817  O   HOH A 236       6.250  36.289  24.268  1.00 27.98           O  
HETATM 1818  O   HOH A 237      16.183  51.707  44.168  1.00 23.65           O  
HETATM 1819  O   HOH A 238       2.055  53.099  25.028  1.00 30.42           O  
HETATM 1820  O   HOH A 239      27.952  43.354  20.721  1.00 13.98           O  
HETATM 1821  O   HOH A 240      28.246  50.486  48.353  1.00 25.04           O  
HETATM 1822  O   HOH A 241      15.367  45.013  24.405  1.00 24.14           O  
HETATM 1823  O   HOH A 242      34.663  62.520  39.194  1.00 32.55           O  
HETATM 1824  O   HOH A 243      -3.841  45.868  26.834  1.00 33.24           O  
HETATM 1825  O   HOH A 244      24.568  48.539  30.452  1.00 22.48           O  
HETATM 1826  O   HOH A 245      23.934  50.640  29.052  1.00 28.61           O  
HETATM 1827  O   HOH A 246      26.345  43.550  48.424  1.00 23.16           O  
HETATM 1828  O   HOH A 247      10.699  40.698  22.251  1.00 36.21           O  
HETATM 1829  O   HOH A 248      10.912  65.473  29.682  1.00 30.80           O  
HETATM 1830  O   HOH A 249      22.870  38.348  29.035  1.00 35.34           O  
HETATM 1831  O   HOH A 250      24.415  46.607  21.477  1.00 16.54           O  
HETATM 1832  O   HOH A 251      19.458  34.754  30.956  1.00 31.30           O  
HETATM 1833  O   HOH A 252      35.950  52.333  28.862  1.00 15.48           O  
HETATM 1834  O   HOH A 253      27.358  47.359  20.692  1.00 28.99           O  
HETATM 1835  O   HOH A 254       5.690  53.261  19.193  1.00 41.76           O  
HETATM 1836  O   HOH A 255       6.502  25.579  28.444  1.00 29.61           O  
HETATM 1837  O   HOH A 256       6.002  65.269  33.939  1.00 22.27           O  
HETATM 1838  O   HOH A 257      36.020  62.406  35.459  1.00 32.69           O  
HETATM 1839  O   HOH A 258      -0.459  51.897  41.726  1.00 17.74           O  
HETATM 1840  O   HOH A 259      30.133  68.566  35.986  1.00 41.89           O  
HETATM 1841  O   HOH A 260       8.699  64.128  26.970  1.00 41.44           O  
HETATM 1842  O   HOH A 261      28.422  42.903  46.574  1.00 27.19           O  
HETATM 1843  O   HOH A 262       2.988  35.572  20.408  1.00 33.63           O  
HETATM 1844  O   HOH A 263      11.652  58.896  20.691  1.00 25.88           O  
HETATM 1845  O   HOH A 264       9.784  49.382  45.880  1.00 21.24           O  
HETATM 1846  O   HOH A 265      28.606  40.775  22.260  1.00 24.84           O  
HETATM 1847  O   HOH A 266      36.214  58.367  29.890  1.00 33.04           O  
HETATM 1848  O   HOH A 267      13.462  69.410  31.665  1.00 28.58           O  
HETATM 1849  O   HOH A 268      15.143  66.332  45.138  1.00 23.47           O  
HETATM 1850  O   HOH A 269      17.892  49.945  42.817  1.00 50.10           O  
HETATM 1851  O   HOH A 270      30.345  54.518  25.772  1.00 25.49           O  
HETATM 1852  O   HOH A 271      41.693  47.957  46.853  1.00 52.28           O  
HETATM 1853  O   HOH A 272       0.059  61.426  35.243  1.00 31.23           O  
HETATM 1854  O   HOH A 273      26.907  52.449  24.940  1.00 25.12           O  
HETATM 1855  O   HOH A 274      28.261  68.946  32.229  1.00 34.46           O  
HETATM 1856  O   HOH A 275      10.985  70.411  38.085  1.00 27.29           O  
HETATM 1857  O   HOH A 276       4.761  71.104  37.146  1.00 38.92           O  
HETATM 1858  O   HOH A 277      38.183  56.975  38.790  1.00 36.34           O  
HETATM 1859  O   HOH A 278       0.538  64.289  31.915  1.00 27.44           O  
HETATM 1860  O   HOH A 279      15.000  35.349  21.374  1.00 54.86           O  
HETATM 1861  O   HOH A 280      25.543  50.949  22.107  1.00 23.32           O  
HETATM 1862  O   HOH A 281      14.661  43.882  19.786  1.00 35.99           O  
HETATM 1863  O   HOH A 282      -2.724  43.810  27.754  1.00 34.92           O  
HETATM 1864  O   HOH A 283       4.256  42.159  43.775  1.00 34.33           O  
HETATM 1865  O   HOH A 284      35.446  61.063  28.748  1.00 29.38           O  
HETATM 1866  O   HOH A 285      42.281  48.408  40.599  1.00 45.56           O  
HETATM 1867  O   HOH A 286       6.661  45.586  46.602  1.00 34.96           O  
HETATM 1868  O   HOH A 287      15.657  53.065  17.511  1.00 37.83           O  
HETATM 1869  O   HOH A 288      27.576  53.943  22.052  1.00 36.00           O  
HETATM 1870  O   HOH A 289      17.098  63.644  25.534  1.00 23.80           O  
HETATM 1871  O   HOH A 290      -0.271  61.793  31.927  1.00 58.63           O  
HETATM 1872  O   HOH A 291      21.011  39.462  28.079  1.00 31.37           O  
HETATM 1873  O   HOH A 292      16.930  62.483  23.318  1.00 24.83           O  
HETATM 1874  O   HOH A 293       8.105  66.533  33.486  1.00 30.42           O  
HETATM 1875  O   HOH A 294      35.929  65.987  38.458  1.00 52.32           O  
HETATM 1876  O   HOH A 295      11.932  52.496  17.319  1.00 40.94           O  
HETATM 1877  O   HOH A 296      38.868  55.785  40.790  1.00 39.40           O  
HETATM 1878  O   HOH A 297      29.225  52.087  24.962  1.00 30.92           O  
HETATM 1879  O   HOH A 298      14.591  37.776  20.649  1.00 36.05           O  
HETATM 1880  O   HOH A 299       5.111  28.250  28.178  1.00 38.45           O  
HETATM 1881  O   HOH A 301      37.076  45.392  29.599  1.00 35.27           O  
HETATM 1882  O   HOH A 302      26.834  54.464  26.764  1.00 18.13           O  
HETATM 1883  O   HOH A 303       6.502  42.423  19.286  1.00 46.33           O  
HETATM 1884  O   HOH A 304      40.084  50.655  27.281  1.00 25.69           O  
HETATM 1885  O   HOH A 305      28.660  45.600  18.745  1.00 17.60           O  
HETATM 1886  O   HOH A 306      24.908  48.859  20.125  1.00 24.76           O  
HETATM 1887  O   HOH A 307      28.097  49.878  21.933  1.00 18.55           O  
HETATM 1888  O   HOH A 308       6.288  65.230  45.713  1.00 23.56           O  
HETATM 1889  O   HOH A 309      17.167  43.705  22.586  1.00 23.84           O  
HETATM 1890  O   HOH A 310       4.884  50.853  18.694  1.00 46.48           O  
HETATM 1891  O   HOH A 311      11.902  50.921  45.061  1.00 28.19           O  
HETATM 1892  O   HOH A 312      13.249  60.709  16.967  1.00 46.58           O  
HETATM 1893  O   HOH A 313      15.782  41.987  20.992  1.00 38.73           O  
HETATM 1894  O   HOH A 314      37.519  50.365  26.738  1.00 35.42           O  
HETATM 1895  O   HOH A 315      45.697  45.975  46.345  1.00 54.02           O  
HETATM 1896  O   HOH A 316      23.576  40.061  31.701  1.00 39.99           O  
HETATM 1897  O   HOH A 317      36.704  48.811  50.017  1.00 27.49           O  
HETATM 1898  O   HOH A 318      17.114  57.501  16.973  1.00 36.39           O  
HETATM 1899  O   HOH A 319       4.396  45.581  25.420  1.00 46.25           O  
HETATM 1900  O   HOH A 320      30.300  67.600  33.252  1.00 34.26           O  
HETATM 1901  O   HOH A 321       9.027  37.251  26.709  1.00 57.70           O  
HETATM 1902  O   HOH A 322       7.071  18.455  38.792  1.00 37.63           O  
HETATM 1903  O   HOH A 323      22.599  41.198  29.696  1.00 30.27           O  
HETATM 1904  O   HOH A 324       2.835  73.949  42.470  1.00 39.21           O  
HETATM 1905  O   HOH A 325      39.778  53.879  43.149  1.00 26.15           O  
HETATM 1906  O   HOH A 326      34.574  54.558  27.020  1.00 24.24           O  
HETATM 1907  O   HOH A 327       1.753  34.324  32.247  1.00 48.92           O  
HETATM 1908  O   HOH A 328       8.267  69.402  45.275  1.00 40.69           O  
HETATM 1909  O   HOH A 329      42.634  53.061  42.918  1.00 26.74           O  
HETATM 1910  O   HOH A 330       3.903  72.010  43.774  1.00 31.55           O  
HETATM 1911  O   HOH A 331      28.728  61.682  48.953  1.00 46.57           O  
HETATM 1912  O   HOH A 332      36.743  63.978  39.750  1.00 40.34           O  
HETATM 1913  O   HOH A 333      15.544  64.942  28.855  1.00 26.43           O  
HETATM 1914  O   HOH A 334      33.223  37.524  43.370  1.00 47.50           O  
HETATM 1915  O   HOH A 335      19.258  58.364  17.548  1.00 43.08           O  
HETATM 1916  O   HOH A 336      41.219  46.856  33.811  1.00 36.38           O  
HETATM 1917  O   HOH A 337      42.443  44.275  34.289  1.00 37.07           O  
HETATM 1918  O   HOH A 338      18.623  36.904  19.140  1.00 41.77           O  
HETATM 1919  O   HOH A 339      -5.127  60.295  28.354  1.00 58.91           O  
HETATM 1920  O   HOH A 340      20.584  68.746  33.771  1.00 29.33           O  
HETATM 1921  O   HOH A 341      17.742  52.035  20.859  1.00 23.05           O  
HETATM 1922  O   HOH A 342       7.737  22.907  30.493  1.00 45.29           O  
HETATM 1923  O   HOH A 343      35.158  70.208  46.892  1.00 33.38           O  
HETATM 1924  O   HOH A 344      -5.378  31.299  36.057  1.00 48.13           O  
HETATM 1925  O   HOH A 345       7.035  71.644  35.515  1.00 35.99           O  
HETATM 1926  O   HOH A 346       8.506  22.797  41.624  1.00 65.66           O  
HETATM 1927  O   HOH A 347      15.243  50.257  40.229  1.00 30.89           O  
HETATM 1928  O   HOH A 348      36.552  52.826  51.277  1.00 56.52           O  
HETATM 1929  O   HOH A 349       9.149  71.346  43.722  1.00 41.62           O  
HETATM 1930  O   HOH A 350      37.162  56.199  48.348  1.00 31.48           O  
HETATM 1931  O   HOH A 351      12.515  73.545  36.730  1.00 43.26           O  
HETATM 1932  O   HOH A 352      32.676  68.847  45.468  1.00 35.07           O  
HETATM 1933  O   HOH A 353      -3.607  43.622  18.444  1.00 35.32           O  
HETATM 1934  O   HOH A 354      15.785  50.317  16.413  1.00 31.75           O  
CONECT 1785 1786                                                                
CONECT 1786 1785 1787 1790                                                      
CONECT 1787 1786 1788 1789                                                      
CONECT 1788 1787                                                                
CONECT 1789 1787                                                                
CONECT 1790 1786 1791                                                           
CONECT 1791 1790 1792                                                           
CONECT 1792 1791 1793 1794                                                      
CONECT 1793 1792                                                                
CONECT 1794 1792 1795                                                           
CONECT 1795 1794 1796 1798                                                      
CONECT 1796 1795 1797 1800                                                      
CONECT 1797 1796                                                                
CONECT 1798 1795 1799                                                           
CONECT 1799 1798                                                                
CONECT 1800 1796 1801                                                           
CONECT 1801 1800 1802                                                           
CONECT 1802 1801 1803 1804                                                      
CONECT 1803 1802                                                                
CONECT 1804 1802                                                                
MASTER      290    0    1   12    4    0    3    6 1933    1   20   19          
END                                                                             



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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: October 18th, 2018.