CNRS Nantes University UFIP UFIP
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***  adktest  ***

elNémo ID: 220616091311124970

Job options:

ID        	=	 220616091311124970
JOBID     	=	 adktest
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 5
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER adktest

HEADER    TRANSFERASE                             13-OCT-98   1BX4              
TITLE     STRUCTURE OF HUMAN ADENOSINE KINASE AT 1.50 ANGSTROMS                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN (ADENOSINE KINASE);                                
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 2.7.1.20;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21[DE3], B834[DE3];                      
SOURCE   8 OTHER_DETAILS: NATIVE PROTEIN WAS EXPRESSED IN BL21[DE3] CELLS       
SOURCE   9 SELENO METHIONINE PROTEIN IN B834[DE3] CELLS                         
KEYWDS    HUMAN ADENOSINE KINASE, TRANSFERASE                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    I.I.MATHEWS,M.D.ERION,S.E.EALICK                                      
REVDAT   3   04-OCT-17 1BX4    1       REMARK                                   
REVDAT   2   24-FEB-09 1BX4    1       VERSN                                    
REVDAT   1   13-OCT-99 1BX4    0                                                
JRNL        AUTH   I.I.MATHEWS,M.D.ERION,S.E.EALICK                             
JRNL        TITL   STRUCTURE OF HUMAN ADENOSINE KINASE AT 1.5 A RESOLUTION.     
JRNL        REF    BIOCHEMISTRY                  V.  37 15607 1998              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   9843365                                                      
JRNL        DOI    10.1021/BI9815445                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.8                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1000000.000                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0010                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 95.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 55983                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.192                           
REMARK   3   FREE R VALUE                     : 0.226                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2438                            
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           : 8                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.57                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 81.50                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 5289                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2470                       
REMARK   3   BIN FREE R VALUE                    : 0.2670                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.00                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 281                          
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            : 2696                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 43                                      
REMARK   3   SOLVENT ATOMS            : 354                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 16.90                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.17                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.20                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.014                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.360                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.10                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.400                           
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) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
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  : PARHCSDX.PRO                                   
REMARK   3  PARAMETER FILE  2  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: TOPOLOGY AND PARAMETER FILES FOR          
REMARK   3  ADENOSINE WERE GENERATED.                                           
REMARK   4                                                                      
REMARK   4 1BX4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-JUL-99.                  
REMARK 100 THE DEPOSITION ID IS D_1000007027.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-AUG-97                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CHESS                              
REMARK 200  BEAMLINE                       : F1                                 
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.929                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 57595                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.3                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.04800                            
REMARK 200  R SYM                      (I) : 0.04800                            
REMARK 200   FOR THE DATA SET  : 6.3000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.58                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.18500                            
REMARK 200  R SYM FOR SHELL            (I) : 0.18500                            
REMARK 200   FOR SHELL         : 3.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SNB, SOLVE                                            
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: MLPHARE WAS USED FOR THE REFINEMENT                          
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20%PEG 4K, 0.16M MGCL2, 0.1M TRIS, PH    
REMARK 280  7.5                                                                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
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       32.65000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       55.54000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       32.65000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       55.54000            
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: MONOMERIC                         
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 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     1                                                      
REMARK 465     THR A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     HIS A 345    CG   ND1  CD2  CE1  NE2                             
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    GLN A  78      -57.64     67.47                                   
REMARK 500    ILE A  92       79.09   -102.71                                   
REMARK 500    ALA A 139     -118.09     45.62                                   
REMARK 500    HIS A 149      -70.24   -141.24                                   
REMARK 500    SER A 198      -51.49     68.34                                   
REMARK 500    GLN A 204      -68.20    -94.82                                   
REMARK 500    ASP A 343       66.71   -114.28                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG A 163         0.24    SIDE CHAIN                              
REMARK 500    TYR A 216         0.07    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 360  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 748   O                                                      
REMARK 620 2 HOH A 749   O    88.2                                              
REMARK 620 3 HOH A 750   O    89.8  86.0                                        
REMARK 620 4 HOH A 747   O    88.6  87.2 173.1                                  
REMARK 620 5 HOH A 751   O   178.3  91.6  91.9  89.7                            
REMARK 620 6 HOH A 746   O    94.0 177.0  92.0  94.8  86.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 365  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 755   O                                                      
REMARK 620 2 HOH A 754   O   178.1                                              
REMARK 620 3 HOH A 752   O    90.8  88.8                                        
REMARK 620 4 HOH A 753   O    90.9  87.3  93.2                                  
REMARK 620 5 ASN A 131   OD1  91.3  89.3 175.9  90.3                            
REMARK 620 6 ASP A 130   OD1  87.5  94.3  84.3 177.0  92.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 375  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 758   O                                                      
REMARK 620 2 HOH A 402   O    90.3                                              
REMARK 620 3 HOH A 759   O    86.9 166.4                                        
REMARK 620 4 HOH A 757   O    86.3  95.0  71.6                                  
REMARK 620 5 HOH A 756   O   167.0 102.4  80.2  89.9                            
REMARK 620 6 SER A  32   OG   87.3  87.3 105.8 173.3  95.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: ADA                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: ADN 350 BINDS IN THE SUBSTRATE BINDING SITE.       
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: ADB                                                 
REMARK 800 EVIDENCE_CODE: AUTHOR                                                
REMARK 800 SITE_DESCRIPTION: ADN 355 BINDS IN THE ATP BINDING SITE.             
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 380                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 385                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 360                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 365                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 375                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADN A 350                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADN A 355                 
DBREF  1BX4 A    1   345  UNP    P55263   ADK_HUMAN        1    345             
SEQRES   1 A  345  MET THR SER VAL ARG GLU ASN ILE LEU PHE GLY MET GLY          
SEQRES   2 A  345  ASN PRO LEU LEU ASP ILE SER ALA VAL VAL ASP LYS ASP          
SEQRES   3 A  345  PHE LEU ASP LYS TYR SER LEU LYS PRO ASN ASP GLN ILE          
SEQRES   4 A  345  LEU ALA GLU ASP LYS HIS LYS GLU LEU PHE ASP GLU LEU          
SEQRES   5 A  345  VAL LYS LYS PHE LYS VAL GLU TYR HIS ALA GLY GLY SER          
SEQRES   6 A  345  THR GLN ASN SER ILE LYS VAL ALA GLN TRP MET ILE GLN          
SEQRES   7 A  345  GLN PRO HIS LYS ALA ALA THR PHE PHE GLY CYS ILE GLY          
SEQRES   8 A  345  ILE ASP LYS PHE GLY GLU ILE LEU LYS ARG LYS ALA ALA          
SEQRES   9 A  345  GLU ALA HIS VAL ASP ALA HIS TYR TYR GLU GLN ASN GLU          
SEQRES  10 A  345  GLN PRO THR GLY THR CYS ALA ALA CYS ILE THR GLY ASP          
SEQRES  11 A  345  ASN ARG SER LEU ILE ALA ASN LEU ALA ALA ALA ASN CYS          
SEQRES  12 A  345  TYR LYS LYS GLU LYS HIS LEU ASP LEU GLU LYS ASN TRP          
SEQRES  13 A  345  MET LEU VAL GLU LYS ALA ARG VAL CYS TYR ILE ALA GLY          
SEQRES  14 A  345  PHE PHE LEU THR VAL SER PRO GLU SER VAL LEU LYS VAL          
SEQRES  15 A  345  ALA HIS HIS ALA SER GLU ASN ASN ARG ILE PHE THR LEU          
SEQRES  16 A  345  ASN LEU SER ALA PRO PHE ILE SER GLN PHE TYR LYS GLU          
SEQRES  17 A  345  SER LEU MET LYS VAL MET PRO TYR VAL ASP ILE LEU PHE          
SEQRES  18 A  345  GLY ASN GLU THR GLU ALA ALA THR PHE ALA ARG GLU GLN          
SEQRES  19 A  345  GLY PHE GLU THR LYS ASP ILE LYS GLU ILE ALA LYS LYS          
SEQRES  20 A  345  THR GLN ALA LEU PRO LYS MET ASN SER LYS ARG GLN ARG          
SEQRES  21 A  345  ILE VAL ILE PHE THR GLN GLY ARG ASP ASP THR ILE MET          
SEQRES  22 A  345  ALA THR GLU SER GLU VAL THR ALA PHE ALA VAL LEU ASP          
SEQRES  23 A  345  GLN ASP GLN LYS GLU ILE ILE ASP THR ASN GLY ALA GLY          
SEQRES  24 A  345  ASP ALA PHE VAL GLY GLY PHE LEU SER GLN LEU VAL SER          
SEQRES  25 A  345  ASP LYS PRO LEU THR GLU CYS ILE ARG ALA GLY HIS TYR          
SEQRES  26 A  345  ALA ALA SER ILE ILE ILE ARG ARG THR GLY CYS THR PHE          
SEQRES  27 A  345  PRO GLU LYS PRO ASP PHE HIS                                  
HET     CL  A 380       1                                                       
HET     CL  A 385       1                                                       
HET     MG  A 360       1                                                       
HET     MG  A 365       1                                                       
HET     MG  A 375       1                                                       
HET    ADN  A 350      19                                                       
HET    ADN  A 355      19                                                       
HETNAM      CL CHLORIDE ION                                                     
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     ADN ADENOSINE                                                        
FORMUL   2   CL    2(CL 1-)                                                     
FORMUL   4   MG    3(MG 2+)                                                     
FORMUL   7  ADN    2(C10 H13 N5 O4)                                             
FORMUL   9  HOH   *354(H2 O)                                                    
HELIX    1   1 LYS A   25  LYS A   30  1                                   6    
HELIX    2   2 ASP A   43  LYS A   55  5                                  13    
HELIX    3   3 SER A   65  ILE A   77  1                                  13    
HELIX    4   4 LYS A   94  GLU A  105  1                                  12    
HELIX    5   5 ALA A  139  CYS A  143  5                                   5    
HELIX    6   6 LYS A  146  LYS A  148  5                                   3    
HELIX    7   7 GLU A  153  LYS A  161  1                                   9    
HELIX    8   8 GLY A  169  THR A  173  5                                   5    
HELIX    9   9 PRO A  176  GLU A  188  1                                  13    
HELIX   10  10 PRO A  200  PHE A  205  1                                   6    
HELIX   11  11 LYS A  207  TYR A  216  1                                  10    
HELIX   12  12 GLU A  224  GLU A  233  1                                  10    
HELIX   13  13 ILE A  241  GLN A  249  1                                   9    
HELIX   14  14 THR A  295  LEU A  310  1                                  16    
HELIX   15  15 LEU A  316  ARG A  332  1                                  17    
SHEET    1   A 9 VAL A 279  PHE A 282  0                                        
SHEET    2   A 9 THR A 271  ALA A 274 -1  N  MET A 273   O  THR A 280           
SHEET    3   A 9 ILE A 261  THR A 265 -1  N  PHE A 264   O  ILE A 272           
SHEET    4   A 9 ILE A 219  ASN A 223  1  N  LEU A 220   O  ILE A 261           
SHEET    5   A 9 ILE A 192  ASN A 196  1  N  LEU A 195   O  ILE A 219           
SHEET    6   A 9 VAL A 164  ALA A 168  1  N  CYS A 165   O  ILE A 192           
SHEET    7   A 9 LEU A   9  MET A  12  1  N  PHE A  10   O  VAL A 164           
SHEET    8   A 9 ALA A  84  GLY A  91  1  N  THR A  85   O  LEU A   9           
SHEET    9   A 9 ASP A 109  GLN A 115  1  N  ASP A 109   O  PHE A  86           
SHEET    1   B 5 GLU A  59  GLY A  63  0                                        
SHEET    2   B 5 LEU A  16  VAL A  22 -1  N  SER A  20   O  GLU A  59           
SHEET    3   B 5 THR A 122  THR A 128  1  N  CYS A 123   O  LEU A  17           
SHEET    4   B 5 ASN A 131  ASN A 137 -1  N  ASN A 137   O  THR A 122           
SHEET    5   B 5 ASP A  37  LEU A  40  1  N  ASP A  37   O  LEU A 134           
LINK        MG    MG A 360                 O   HOH A 748     1555   1555  2.20  
LINK        MG    MG A 360                 O   HOH A 749     1555   1555  2.22  
LINK        MG    MG A 360                 O   HOH A 750     1555   1555  2.18  
LINK        MG    MG A 360                 O   HOH A 747     1555   1555  2.15  
LINK        MG    MG A 360                 O   HOH A 751     1555   1555  2.17  
LINK        MG    MG A 360                 O   HOH A 746     1555   1555  2.17  
LINK        MG    MG A 365                 O   HOH A 755     1555   1555  2.17  
LINK        MG    MG A 365                 O   HOH A 754     1555   1555  2.19  
LINK        MG    MG A 365                 O   HOH A 752     1555   1555  2.30  
LINK        MG    MG A 365                 O   HOH A 753     1555   1555  2.20  
LINK        MG    MG A 375                 O   HOH A 758     1555   1555  2.27  
LINK        MG    MG A 375                 O   HOH A 402     1555   1555  2.44  
LINK        MG    MG A 375                 O   HOH A 759     1555   1555  2.20  
LINK        MG    MG A 375                 O   HOH A 757     1555   1555  2.31  
LINK        MG    MG A 375                 O   HOH A 756     1555   1555  2.37  
LINK        MG    MG A 365                 OD1 ASN A 131     1555   1555  2.12  
LINK        MG    MG A 365                 OD1 ASP A 130     1555   1555  2.18  
LINK        MG    MG A 375                 OG  SER A  32     1555   1555  2.17  
CISPEP   1 GLN A   79    PRO A   80          0         0.09                     
SITE     1 ADA  1 ADN A 350                                                     
SITE     1 ADB  1 ADN A 355                                                     
SITE     1 AC1  3 ASN A  14  THR A  66  ADN A 350                               
SITE     1 AC2  3 THR A 265  HOH A 556  HOH A 746                               
SITE     1 AC3  6 HOH A 746  HOH A 747  HOH A 748  HOH A 749                    
SITE     2 AC3  6 HOH A 750  HOH A 751                                          
SITE     1 AC4  6 ASP A 130  ASN A 131  HOH A 752  HOH A 753                    
SITE     2 AC4  6 HOH A 754  HOH A 755                                          
SITE     1 AC5  6 SER A  32  HOH A 402  HOH A 756  HOH A 757                    
SITE     2 AC5  6 HOH A 758  HOH A 759                                          
SITE     1 AC6 14 ASN A  14  ASP A  18  LEU A  40  GLY A  64                    
SITE     2 AC6 14 SER A  65  ASN A  68  PHE A 170  ASN A 296                    
SITE     3 AC6 14 GLY A 297  ASP A 300   CL A 380  HOH A 415                    
SITE     4 AC6 14 HOH A 416  HOH A 430                                          
SITE     1 AC7 19 THR A 265  GLY A 267  ARG A 268  THR A 271                    
SITE     2 AC7 19 ASP A 286  GLN A 289  ILE A 292  ALA A 298                    
SITE     3 AC7 19 GLY A 299  HIS A 324  ALA A 327  ILE A 331                    
SITE     4 AC7 19 HOH A 408  HOH A 410  HOH A 420  HOH A 425                    
SITE     5 AC7 19 HOH A 577  HOH A 597  HOH A 637                               
CRYST1   65.300  111.080   49.690  90.00  90.00  90.00 P 21 21 2     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      0.015314  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009003  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.020125        0.00000                         
ATOM      1  N   VAL A   4      63.268  27.861  32.229  1.00 28.45           N  
ATOM      2  CA  VAL A   4      64.499  28.180  31.457  1.00 30.39           C  
ATOM      3  C   VAL A   4      64.296  28.154  29.946  1.00 30.18           C  
ATOM      4  O   VAL A   4      64.311  29.210  29.315  1.00 32.72           O  
ATOM      5  CB  VAL A   4      65.652  27.271  31.836  1.00 32.23           C  
ATOM      6  CG1 VAL A   4      66.951  27.814  31.235  1.00 33.45           C  
ATOM      7  CG2 VAL A   4      65.753  27.179  33.354  1.00 33.40           C  
ATOM      8  N   ARG A   5      64.179  26.979  29.330  1.00 28.26           N  
ATOM      9  CA  ARG A   5      63.928  26.953  27.883  1.00 26.22           C  
ATOM     10  C   ARG A   5      62.708  26.107  27.507  1.00 24.35           C  
ATOM     11  O   ARG A   5      62.026  25.552  28.381  1.00 22.93           O  
ATOM     12  CB  ARG A   5      65.174  26.555  27.066  1.00 29.09           C  
ATOM     13  CG  ARG A   5      65.442  25.056  26.922  1.00 33.07           C  
ATOM     14  CD  ARG A   5      66.083  24.437  28.158  1.00 35.61           C  
ATOM     15  NE  ARG A   5      67.499  24.786  28.280  1.00 38.82           N  
ATOM     16  CZ  ARG A   5      68.386  24.114  29.016  1.00 39.62           C  
ATOM     17  NH1 ARG A   5      68.029  23.029  29.719  1.00 38.75           N  
ATOM     18  NH2 ARG A   5      69.646  24.543  29.058  1.00 41.99           N  
ATOM     19  N   GLU A   6      62.399  26.065  26.216  1.00 21.94           N  
ATOM     20  CA  GLU A   6      61.257  25.312  25.724  1.00 21.94           C  
ATOM     21  C   GLU A   6      61.337  23.837  26.030  1.00 20.15           C  
ATOM     22  O   GLU A   6      62.434  23.259  26.026  1.00 19.95           O  
ATOM     23  CB  GLU A   6      61.109  25.500  24.225  1.00 24.67           C  
ATOM     24  CG  GLU A   6      60.639  26.879  23.867  1.00 30.70           C  
ATOM     25  CD  GLU A   6      60.963  27.247  22.437  1.00 35.13           C  
ATOM     26  OE1 GLU A   6      60.895  26.329  21.572  1.00 36.12           O  
ATOM     27  OE2 GLU A   6      61.294  28.452  22.191  1.00 36.38           O  
ATOM     28  N   ASN A   7      60.176  23.249  26.349  1.00 17.23           N  
ATOM     29  CA  ASN A   7      60.070  21.820  26.645  1.00 15.36           C  
ATOM     30  C   ASN A   7      60.910  21.321  27.824  1.00 12.89           C  
ATOM     31  O   ASN A   7      61.273  20.153  27.878  1.00 13.70           O  
ATOM     32  CB  ASN A   7      60.401  21.030  25.375  1.00 15.07           C  
ATOM     33  CG  ASN A   7      59.576  21.486  24.186  1.00 15.65           C  
ATOM     34  OD1 ASN A   7      58.350  21.384  24.197  1.00 18.13           O  
ATOM     35  ND2 ASN A   7      60.232  22.022  23.170  1.00 15.07           N  
ATOM     36  N   ILE A   8      61.237  22.213  28.751  1.00 12.20           N  
ATOM     37  CA  ILE A   8      62.023  21.876  29.937  1.00 11.92           C  
ATOM     38  C   ILE A   8      61.185  21.054  30.945  1.00 11.20           C  
ATOM     39  O   ILE A   8      61.738  20.310  31.770  1.00 11.21           O  
ATOM     40  CB  ILE A   8      62.617  23.187  30.612  1.00 14.17           C  
ATOM     41  CG1 ILE A   8      63.654  22.855  31.688  1.00 14.04           C  
ATOM     42  CG2 ILE A   8      61.502  24.051  31.248  1.00 13.50           C  
ATOM     43  CD1 ILE A   8      64.955  22.356  31.130  1.00 17.37           C  
ATOM     44  N   LEU A   9      59.858  21.205  30.879  1.00 10.90           N  
ATOM     45  CA  LEU A   9      58.936  20.466  31.767  1.00 10.84           C  
ATOM     46  C   LEU A   9      57.986  19.605  30.922  1.00  9.70           C  
ATOM     47  O   LEU A   9      57.409  20.093  29.953  1.00 10.15           O  
ATOM     48  CB  LEU A   9      58.128  21.435  32.656  1.00 11.55           C  
ATOM     49  CG  LEU A   9      57.003  20.874  33.556  1.00 11.60           C  
ATOM     50  CD1 LEU A   9      57.542  19.956  34.618  1.00 10.36           C  
ATOM     51  CD2 LEU A   9      56.214  22.051  34.205  1.00 12.31           C  
ATOM     52  N   PHE A  10      57.889  18.315  31.250  1.00  9.87           N  
ATOM     53  CA  PHE A  10      57.025  17.386  30.520  1.00 10.00           C  
ATOM     54  C   PHE A  10      55.932  16.766  31.385  1.00  9.30           C  
ATOM     55  O   PHE A  10      56.210  16.294  32.486  1.00 11.05           O  
ATOM     56  CB  PHE A  10      57.851  16.234  29.901  1.00  9.38           C  
ATOM     57  CG  PHE A  10      56.995  15.157  29.224  1.00 10.04           C  
ATOM     58  CD1 PHE A  10      56.518  15.340  27.920  1.00  8.69           C  
ATOM     59  CD2 PHE A  10      56.620  13.981  29.920  1.00 10.23           C  
ATOM     60  CE1 PHE A  10      55.681  14.385  27.324  1.00  8.98           C  
ATOM     61  CE2 PHE A  10      55.778  13.019  29.317  1.00  9.25           C  
ATOM     62  CZ  PHE A  10      55.312  13.229  28.022  1.00  7.91           C  
ATOM     63  N   GLY A  11      54.705  16.742  30.865  1.00  9.14           N  
ATOM     64  CA  GLY A  11      53.600  16.099  31.571  1.00  8.67           C  
ATOM     65  C   GLY A  11      52.737  15.291  30.597  1.00  9.69           C  
ATOM     66  O   GLY A  11      52.763  15.546  29.383  1.00  9.80           O  
ATOM     67  N   MET A  12      52.058  14.250  31.094  1.00  8.85           N  
ATOM     68  CA  MET A  12      51.122  13.475  30.267  1.00  9.24           C  
ATOM     69  C   MET A  12      49.997  12.950  31.163  1.00  8.28           C  
ATOM     70  O   MET A  12      50.195  12.790  32.370  1.00  8.67           O  
ATOM     71  CB  MET A  12      51.805  12.357  29.463  1.00 11.04           C  
ATOM     72  CG  MET A  12      52.138  11.081  30.228  1.00 12.27           C  
ATOM     73  SD  MET A  12      53.221   9.874  29.296  1.00 13.45           S  
ATOM     74  CE  MET A  12      52.336   9.637  27.787  1.00 10.29           C  
ATOM     75  N   GLY A  13      48.797  12.798  30.597  1.00  8.77           N  
ATOM     76  CA  GLY A  13      47.663  12.317  31.387  1.00  7.48           C  
ATOM     77  C   GLY A  13      46.349  12.230  30.621  1.00  9.17           C  
ATOM     78  O   GLY A  13      46.327  12.027  29.407  1.00  8.59           O  
ATOM     79  N   ASN A  14      45.242  12.401  31.352  1.00  8.57           N  
ATOM     80  CA  ASN A  14      43.904  12.344  30.790  1.00  8.83           C  
ATOM     81  C   ASN A  14      43.294  13.743  30.478  1.00  9.73           C  
ATOM     82  O   ASN A  14      42.955  14.486  31.392  1.00  8.87           O  
ATOM     83  CB  ASN A  14      42.979  11.618  31.790  1.00  8.09           C  
ATOM     84  CG  ASN A  14      43.403  10.174  32.049  1.00  8.65           C  
ATOM     85  OD1 ASN A  14      43.955   9.511  31.159  1.00 11.20           O  
ATOM     86  ND2 ASN A  14      43.173   9.690  33.268  1.00  8.63           N  
ATOM     87  N   PRO A  15      43.158  14.112  29.185  1.00 10.79           N  
ATOM     88  CA  PRO A  15      42.566  15.419  28.839  1.00 10.92           C  
ATOM     89  C   PRO A  15      41.046  15.247  28.992  1.00 11.81           C  
ATOM     90  O   PRO A  15      40.460  14.378  28.323  1.00 12.57           O  
ATOM     91  CB  PRO A  15      42.925  15.589  27.356  1.00 11.72           C  
ATOM     92  CG  PRO A  15      43.989  14.529  27.081  1.00 10.97           C  
ATOM     93  CD  PRO A  15      43.625  13.395  27.985  1.00 10.97           C  
ATOM     94  N   LEU A  16      40.419  16.044  29.862  1.00  8.84           N  
ATOM     95  CA  LEU A  16      38.974  15.933  30.108  1.00  9.83           C  
ATOM     96  C   LEU A  16      38.217  17.281  30.091  1.00  9.93           C  
ATOM     97  O   LEU A  16      38.763  18.295  30.513  1.00  9.84           O  
ATOM     98  CB  LEU A  16      38.720  15.286  31.484  1.00  9.22           C  
ATOM     99  CG  LEU A  16      39.356  13.930  31.827  1.00 10.03           C  
ATOM    100  CD1 LEU A  16      39.058  13.577  33.282  1.00  8.86           C  
ATOM    101  CD2 LEU A  16      38.829  12.826  30.888  1.00 10.89           C  
ATOM    102  N   LEU A  17      36.976  17.280  29.589  1.00  9.27           N  
ATOM    103  CA  LEU A  17      36.151  18.485  29.592  1.00 10.53           C  
ATOM    104  C   LEU A  17      35.261  18.378  30.832  1.00 10.92           C  
ATOM    105  O   LEU A  17      34.459  17.438  30.968  1.00  9.31           O  
ATOM    106  CB  LEU A  17      35.288  18.592  28.322  1.00 11.19           C  
ATOM    107  CG  LEU A  17      34.492  19.912  28.207  1.00 12.95           C  
ATOM    108  CD1 LEU A  17      35.427  21.087  27.956  1.00 14.28           C  
ATOM    109  CD2 LEU A  17      33.456  19.826  27.110  1.00 13.81           C  
ATOM    110  N   ASP A  18      35.433  19.319  31.761  1.00 10.69           N  
ATOM    111  CA  ASP A  18      34.646  19.329  32.999  1.00 11.03           C  
ATOM    112  C   ASP A  18      33.226  19.880  32.787  1.00 11.88           C  
ATOM    113  O   ASP A  18      33.064  20.943  32.152  1.00 12.81           O  
ATOM    114  CB  ASP A  18      35.341  20.186  34.068  1.00 12.27           C  
ATOM    115  CG  ASP A  18      36.651  19.589  34.546  1.00 14.23           C  
ATOM    116  OD1 ASP A  18      36.783  18.337  34.635  1.00 14.27           O  
ATOM    117  OD2 ASP A  18      37.547  20.380  34.874  1.00 16.33           O  
ATOM    118  N   ILE A  19      32.230  19.175  33.346  1.00 10.19           N  
ATOM    119  CA  ILE A  19      30.827  19.590  33.276  1.00 11.36           C  
ATOM    120  C   ILE A  19      30.327  19.718  34.713  1.00 11.75           C  
ATOM    121  O   ILE A  19      30.126  18.721  35.396  1.00 13.01           O  
ATOM    122  CB  ILE A  19      29.951  18.589  32.494  1.00 12.81           C  
ATOM    123  CG1 ILE A  19      30.568  18.314  31.112  1.00 12.06           C  
ATOM    124  CG2 ILE A  19      28.542  19.192  32.284  1.00 12.34           C  
ATOM    125  CD1 ILE A  19      29.880  17.215  30.342  1.00 12.98           C  
ATOM    126  N   SER A  20      30.145  20.954  35.182  1.00 12.32           N  
ATOM    127  CA  SER A  20      29.717  21.162  36.566  1.00 12.34           C  
ATOM    128  C   SER A  20      28.368  21.836  36.733  1.00 11.48           C  
ATOM    129  O   SER A  20      27.961  22.625  35.884  1.00 12.26           O  
ATOM    130  CB  SER A  20      30.788  21.958  37.345  1.00 15.03           C  
ATOM    131  OG  SER A  20      31.059  23.237  36.774  1.00 19.43           O  
ATOM    132  N   ALA A  21      27.729  21.561  37.867  1.00 10.41           N  
ATOM    133  CA  ALA A  21      26.438  22.143  38.207  1.00 10.33           C  
ATOM    134  C   ALA A  21      26.149  21.912  39.673  1.00 10.75           C  
ATOM    135  O   ALA A  21      26.680  20.961  40.268  1.00  9.73           O  
ATOM    136  CB  ALA A  21      25.331  21.511  37.383  1.00 12.38           C  
ATOM    137  N   VAL A  22      25.363  22.823  40.266  1.00  9.03           N  
ATOM    138  CA  VAL A  22      24.951  22.669  41.653  1.00  9.65           C  
ATOM    139  C   VAL A  22      23.699  21.767  41.589  1.00 10.33           C  
ATOM    140  O   VAL A  22      22.718  22.073  40.885  1.00 10.62           O  
ATOM    141  CB  VAL A  22      24.610  24.021  42.360  1.00  9.73           C  
ATOM    142  CG1 VAL A  22      24.058  23.750  43.764  1.00 11.18           C  
ATOM    143  CG2 VAL A  22      25.845  24.892  42.455  1.00  9.99           C  
ATOM    144  N   VAL A  23      23.756  20.642  42.285  1.00  9.38           N  
ATOM    145  CA  VAL A  23      22.646  19.679  42.297  1.00  9.79           C  
ATOM    146  C   VAL A  23      22.007  19.580  43.689  1.00 11.70           C  
ATOM    147  O   VAL A  23      22.387  20.322  44.614  1.00 11.87           O  
ATOM    148  CB  VAL A  23      23.142  18.267  41.847  1.00  9.65           C  
ATOM    149  CG1 VAL A  23      23.803  18.354  40.446  1.00  7.73           C  
ATOM    150  CG2 VAL A  23      24.116  17.676  42.896  1.00  8.25           C  
ATOM    151  N   ASP A  24      21.016  18.699  43.832  1.00 11.55           N  
ATOM    152  CA  ASP A  24      20.354  18.501  45.123  1.00 13.14           C  
ATOM    153  C   ASP A  24      20.591  17.103  45.726  1.00 12.91           C  
ATOM    154  O   ASP A  24      21.175  16.216  45.080  1.00 12.01           O  
ATOM    155  CB  ASP A  24      18.843  18.803  45.028  1.00 15.31           C  
ATOM    156  CG  ASP A  24      18.137  18.023  43.926  1.00 18.98           C  
ATOM    157  OD1 ASP A  24      16.951  18.318  43.660  1.00 21.36           O  
ATOM    158  OD2 ASP A  24      18.737  17.113  43.324  1.00 19.40           O  
ATOM    159  N   LYS A  25      20.165  16.933  46.980  1.00 13.69           N  
ATOM    160  CA  LYS A  25      20.309  15.667  47.708  1.00 15.33           C  
ATOM    161  C   LYS A  25      19.666  14.501  46.953  1.00 15.32           C  
ATOM    162  O   LYS A  25      20.241  13.417  46.898  1.00 15.42           O  
ATOM    163  CB  LYS A  25      19.695  15.805  49.088  1.00 16.35           C  
ATOM    164  CG  LYS A  25      19.816  14.597  49.975  1.00 20.95           C  
ATOM    165  CD  LYS A  25      18.776  14.700  51.108  1.00 25.30           C  
ATOM    166  CE  LYS A  25      18.851  13.530  52.063  1.00 28.61           C  
ATOM    167  NZ  LYS A  25      20.130  13.577  52.836  1.00 30.97           N  
ATOM    168  N   ASP A  26      18.503  14.720  46.338  1.00 15.65           N  
ATOM    169  CA  ASP A  26      17.839  13.656  45.572  1.00 16.42           C  
ATOM    170  C   ASP A  26      18.765  13.129  44.455  1.00 15.10           C  
ATOM    171  O   ASP A  26      18.824  11.923  44.239  1.00 15.78           O  
ATOM    172  CB  ASP A  26      16.516  14.145  44.933  1.00 20.55           C  
ATOM    173  CG  ASP A  26      15.330  14.199  45.926  1.00 25.03           C  
ATOM    174  OD1 ASP A  26      15.440  13.682  47.065  1.00 25.54           O  
ATOM    175  OD2 ASP A  26      14.266  14.757  45.548  1.00 27.54           O  
ATOM    176  N   PHE A  27      19.485  14.022  43.766  1.00 12.32           N  
ATOM    177  CA  PHE A  27      20.378  13.644  42.665  1.00 11.24           C  
ATOM    178  C   PHE A  27      21.578  12.826  43.167  1.00 12.54           C  
ATOM    179  O   PHE A  27      21.953  11.816  42.547  1.00 13.08           O  
ATOM    180  CB  PHE A  27      20.855  14.895  41.922  1.00 12.44           C  
ATOM    181  CG  PHE A  27      21.657  14.607  40.702  1.00 13.78           C  
ATOM    182  CD1 PHE A  27      21.049  14.538  39.452  1.00 16.21           C  
ATOM    183  CD2 PHE A  27      23.023  14.408  40.785  1.00 13.70           C  
ATOM    184  CE1 PHE A  27      21.804  14.273  38.299  1.00 16.58           C  
ATOM    185  CE2 PHE A  27      23.769  14.144  39.654  1.00 14.22           C  
ATOM    186  CZ  PHE A  27      23.166  14.076  38.412  1.00 14.76           C  
ATOM    187  N   LEU A  28      22.191  13.244  44.277  1.00 11.93           N  
ATOM    188  CA  LEU A  28      23.319  12.479  44.834  1.00 12.34           C  
ATOM    189  C   LEU A  28      22.846  11.071  45.256  1.00 13.49           C  
ATOM    190  O   LEU A  28      23.523  10.083  44.973  1.00 13.24           O  
ATOM    191  CB  LEU A  28      23.956  13.205  46.031  1.00 11.51           C  
ATOM    192  CG  LEU A  28      24.622  14.579  45.780  1.00 13.00           C  
ATOM    193  CD1 LEU A  28      25.245  15.081  47.109  1.00 12.14           C  
ATOM    194  CD2 LEU A  28      25.706  14.494  44.675  1.00 10.79           C  
ATOM    195  N   ASP A  29      21.678  10.991  45.901  1.00 14.17           N  
ATOM    196  CA  ASP A  29      21.091   9.704  46.341  1.00 16.02           C  
ATOM    197  C   ASP A  29      20.745   8.797  45.170  1.00 15.87           C  
ATOM    198  O   ASP A  29      20.956   7.585  45.242  1.00 15.26           O  
ATOM    199  CB  ASP A  29      19.828   9.914  47.188  1.00 18.11           C  
ATOM    200  CG  ASP A  29      20.135  10.483  48.550  1.00 22.44           C  
ATOM    201  OD1 ASP A  29      21.328  10.679  48.862  1.00 27.64           O  
ATOM    202  OD2 ASP A  29      19.189  10.769  49.318  1.00 27.31           O  
ATOM    203  N   LYS A  30      20.227   9.384  44.093  1.00 15.41           N  
ATOM    204  CA  LYS A  30      19.864   8.624  42.906  1.00 16.56           C  
ATOM    205  C   LYS A  30      21.038   7.859  42.299  1.00 17.11           C  
ATOM    206  O   LYS A  30      20.847   6.756  41.773  1.00 18.31           O  
ATOM    207  CB  LYS A  30      19.248   9.525  41.841  1.00 15.48           C  
ATOM    208  CG  LYS A  30      18.869   8.790  40.575  1.00 17.60           C  
ATOM    209  CD  LYS A  30      18.029   9.666  39.681  1.00 20.55           C  
ATOM    210  CE  LYS A  30      17.585   8.899  38.447  1.00 22.46           C  
ATOM    211  NZ  LYS A  30      16.904   9.771  37.455  1.00 23.63           N  
ATOM    212  N   TYR A  31      22.238   8.438  42.364  1.00 15.15           N  
ATOM    213  CA  TYR A  31      23.423   7.803  41.791  1.00 13.82           C  
ATOM    214  C   TYR A  31      24.413   7.298  42.827  1.00 12.94           C  
ATOM    215  O   TYR A  31      25.571   6.962  42.501  1.00 12.69           O  
ATOM    216  CB  TYR A  31      24.080   8.745  40.798  1.00 14.56           C  
ATOM    217  CG  TYR A  31      23.202   8.971  39.603  1.00 15.69           C  
ATOM    218  CD1 TYR A  31      22.375  10.085  39.526  1.00 17.24           C  
ATOM    219  CD2 TYR A  31      23.153   8.047  38.564  1.00 17.08           C  
ATOM    220  CE1 TYR A  31      21.512  10.272  38.440  1.00 18.53           C  
ATOM    221  CE2 TYR A  31      22.291   8.224  37.473  1.00 18.81           C  
ATOM    222  CZ  TYR A  31      21.483   9.334  37.419  1.00 17.28           C  
ATOM    223  OH  TYR A  31      20.674   9.527  36.336  1.00 20.93           O  
ATOM    224  N   SER A  32      23.947   7.249  44.070  1.00 11.17           N  
ATOM    225  CA  SER A  32      24.724   6.763  45.200  1.00 12.12           C  
ATOM    226  C   SER A  32      26.094   7.444  45.325  1.00 13.93           C  
ATOM    227  O   SER A  32      27.131   6.791  45.572  1.00 12.05           O  
ATOM    228  CB  SER A  32      24.875   5.235  45.103  1.00 13.74           C  
ATOM    229  OG  SER A  32      23.596   4.613  45.182  1.00 13.58           O  
ATOM    230  N   LEU A  33      26.070   8.771  45.182  1.00 12.72           N  
ATOM    231  CA  LEU A  33      27.280   9.602  45.242  1.00 12.79           C  
ATOM    232  C   LEU A  33      27.618  10.142  46.634  1.00 12.41           C  
ATOM    233  O   LEU A  33      26.725  10.558  47.372  1.00 13.75           O  
ATOM    234  CB  LEU A  33      27.129  10.777  44.270  1.00 11.21           C  
ATOM    235  CG  LEU A  33      26.841  10.415  42.813  1.00  9.23           C  
ATOM    236  CD1 LEU A  33      26.585  11.671  41.978  1.00  9.56           C  
ATOM    237  CD2 LEU A  33      28.002   9.595  42.259  1.00 11.01           C  
ATOM    238  N   LYS A  34      28.901  10.101  46.996  1.00 11.31           N  
ATOM    239  CA  LYS A  34      29.373  10.638  48.267  1.00 12.83           C  
ATOM    240  C   LYS A  34      29.548  12.176  48.004  1.00 12.95           C  
ATOM    241  O   LYS A  34      29.976  12.575  46.914  1.00 12.21           O  
ATOM    242  CB  LYS A  34      30.688   9.931  48.625  1.00 14.82           C  
ATOM    243  CG  LYS A  34      31.272  10.322  49.981  1.00 22.82           C  
ATOM    244  CD  LYS A  34      32.424   9.394  50.429  1.00 27.21           C  
ATOM    245  CE  LYS A  34      33.207  10.002  51.626  1.00 28.25           C  
ATOM    246  NZ  LYS A  34      34.099  11.159  51.233  1.00 29.32           N  
ATOM    247  N   PRO A  35      29.186  13.047  48.976  1.00 12.84           N  
ATOM    248  CA  PRO A  35      29.317  14.509  48.763  1.00 12.97           C  
ATOM    249  C   PRO A  35      30.684  15.009  48.272  1.00 11.24           C  
ATOM    250  O   PRO A  35      30.765  15.865  47.393  1.00 10.09           O  
ATOM    251  CB  PRO A  35      28.921  15.102  50.114  1.00 13.17           C  
ATOM    252  CG  PRO A  35      27.969  14.083  50.652  1.00 16.23           C  
ATOM    253  CD  PRO A  35      28.597  12.755  50.297  1.00 13.92           C  
ATOM    254  N   ASN A  36      31.754  14.464  48.836  1.00 11.80           N  
ATOM    255  CA  ASN A  36      33.116  14.806  48.414  1.00 11.66           C  
ATOM    256  C   ASN A  36      33.755  13.479  48.013  1.00 13.09           C  
ATOM    257  O   ASN A  36      33.991  12.636  48.883  1.00 14.35           O  
ATOM    258  CB  ASN A  36      33.911  15.414  49.572  1.00 12.27           C  
ATOM    259  CG  ASN A  36      33.441  16.812  49.929  1.00 11.74           C  
ATOM    260  OD1 ASN A  36      32.831  17.026  50.995  1.00 16.28           O  
ATOM    261  ND2 ASN A  36      33.660  17.754  49.019  1.00  9.67           N  
ATOM    262  N   ASP A  37      34.011  13.288  46.720  1.00 10.85           N  
ATOM    263  CA  ASP A  37      34.592  12.029  46.229  1.00 11.49           C  
ATOM    264  C   ASP A  37      35.088  12.204  44.811  1.00  8.94           C  
ATOM    265  O   ASP A  37      34.785  13.209  44.173  1.00  9.32           O  
ATOM    266  CB  ASP A  37      33.502  10.944  46.238  1.00 12.40           C  
ATOM    267  CG  ASP A  37      34.060   9.532  46.368  1.00 16.85           C  
ATOM    268  OD1 ASP A  37      35.287   9.357  46.497  1.00 17.02           O  
ATOM    269  OD2 ASP A  37      33.264   8.565  46.356  1.00 18.41           O  
ATOM    270  N   GLN A  38      35.942  11.280  44.361  1.00  7.46           N  
ATOM    271  CA  GLN A  38      36.441  11.265  42.980  1.00  7.86           C  
ATOM    272  C   GLN A  38      36.442   9.796  42.584  1.00  9.08           C  
ATOM    273  O   GLN A  38      37.109   8.984  43.243  1.00 10.91           O  
ATOM    274  CB  GLN A  38      37.871  11.811  42.844  1.00  8.62           C  
ATOM    275  CG  GLN A  38      38.041  13.254  43.264  1.00 11.36           C  
ATOM    276  CD  GLN A  38      39.452  13.736  43.057  1.00 12.47           C  
ATOM    277  OE1 GLN A  38      40.334  13.556  43.933  1.00 14.15           O  
ATOM    278  NE2 GLN A  38      39.701  14.298  41.882  1.00 11.30           N  
ATOM    279  N   ILE A  39      35.687   9.451  41.540  1.00  8.45           N  
ATOM    280  CA  ILE A  39      35.587   8.062  41.063  1.00  9.22           C  
ATOM    281  C   ILE A  39      35.568   8.006  39.517  1.00 10.10           C  
ATOM    282  O   ILE A  39      35.468   9.038  38.841  1.00  8.50           O  
ATOM    283  CB  ILE A  39      34.269   7.350  41.595  1.00  9.78           C  
ATOM    284  CG1 ILE A  39      33.043   7.881  40.842  1.00  9.96           C  
ATOM    285  CG2 ILE A  39      34.118   7.540  43.118  1.00  9.98           C  
ATOM    286  CD1 ILE A  39      31.698   7.245  41.256  1.00 13.03           C  
ATOM    287  N   LEU A  40      35.719   6.796  38.968  1.00  9.93           N  
ATOM    288  CA  LEU A  40      35.652   6.572  37.515  1.00 10.77           C  
ATOM    289  C   LEU A  40      34.190   6.195  37.161  1.00 12.06           C  
ATOM    290  O   LEU A  40      33.520   5.494  37.934  1.00 13.02           O  
ATOM    291  CB  LEU A  40      36.587   5.417  37.095  1.00 11.29           C  
ATOM    292  CG  LEU A  40      38.088   5.616  37.290  1.00 11.16           C  
ATOM    293  CD1 LEU A  40      38.809   4.357  36.835  1.00 11.42           C  
ATOM    294  CD2 LEU A  40      38.558   6.837  36.485  1.00 11.35           C  
ATOM    295  N   ALA A  41      33.721   6.643  35.999  1.00 14.91           N  
ATOM    296  CA  ALA A  41      32.356   6.347  35.549  1.00 19.05           C  
ATOM    297  C   ALA A  41      32.220   4.935  34.986  1.00 23.35           C  
ATOM    298  O   ALA A  41      33.000   4.502  34.100  1.00 23.64           O  
ATOM    299  CB  ALA A  41      31.914   7.345  34.498  1.00 19.56           C  
ATOM    300  N   GLU A  42      31.254   4.217  35.543  1.00 25.33           N  
ATOM    301  CA  GLU A  42      30.915   2.866  35.110  1.00 28.73           C  
ATOM    302  C   GLU A  42      29.731   2.933  34.093  1.00 30.04           C  
ATOM    303  O   GLU A  42      29.268   4.027  33.709  1.00 29.00           O  
ATOM    304  CB  GLU A  42      30.530   2.041  36.335  1.00 29.02           C  
ATOM    305  CG  GLU A  42      31.670   1.862  37.333  1.00 32.36           C  
ATOM    306  CD  GLU A  42      31.158   1.570  38.734  1.00 35.71           C  
ATOM    307  OE1 GLU A  42      30.459   2.448  39.294  1.00 38.67           O  
ATOM    308  OE2 GLU A  42      31.430   0.471  39.285  1.00 38.16           O  
ATOM    309  N   ASP A  43      29.271   1.776  33.620  1.00 30.06           N  
ATOM    310  CA  ASP A  43      28.166   1.745  32.662  1.00 29.83           C  
ATOM    311  C   ASP A  43      26.864   2.257  33.321  1.00 27.94           C  
ATOM    312  O   ASP A  43      26.032   2.907  32.661  1.00 26.76           O  
ATOM    313  CB  ASP A  43      27.982   0.321  32.122  1.00 32.76           C  
ATOM    314  CG  ASP A  43      27.029   0.270  30.963  1.00 35.82           C  
ATOM    315  OD1 ASP A  43      25.929  -0.311  31.125  1.00 36.85           O  
ATOM    316  OD2 ASP A  43      27.373   0.847  29.901  1.00 39.80           O  
ATOM    317  N   LYS A  44      26.707   1.967  34.621  1.00 25.33           N  
ATOM    318  CA  LYS A  44      25.550   2.408  35.397  1.00 23.00           C  
ATOM    319  C   LYS A  44      25.407   3.956  35.511  1.00 24.57           C  
ATOM    320  O   LYS A  44      24.372   4.444  35.956  1.00 25.90           O  
ATOM    321  CB  LYS A  44      25.651   1.834  36.811  1.00 21.94           C  
ATOM    322  CG  LYS A  44      27.018   1.974  37.404  1.00 23.52           C  
ATOM    323  CD  LYS A  44      27.096   1.503  38.841  1.00 26.05           C  
ATOM    324  CE  LYS A  44      26.466   2.513  39.769  1.00 27.47           C  
ATOM    325  NZ  LYS A  44      27.023   2.377  41.151  1.00 30.36           N  
ATOM    326  N   HIS A  45      26.442   4.713  35.139  1.00 22.91           N  
ATOM    327  CA  HIS A  45      26.433   6.175  35.236  1.00 21.29           C  
ATOM    328  C   HIS A  45      26.106   6.864  33.912  1.00 23.02           C  
ATOM    329  O   HIS A  45      26.249   8.079  33.820  1.00 23.64           O  
ATOM    330  CB  HIS A  45      27.807   6.707  35.724  1.00 17.86           C  
ATOM    331  CG  HIS A  45      28.203   6.277  37.110  1.00 14.92           C  
ATOM    332  ND1 HIS A  45      29.320   5.505  37.360  1.00 15.33           N  
ATOM    333  CD2 HIS A  45      27.669   6.558  38.323  1.00 13.99           C  
ATOM    334  CE1 HIS A  45      29.454   5.330  38.662  1.00 12.43           C  
ATOM    335  NE2 HIS A  45      28.465   5.960  39.271  1.00 16.00           N  
ATOM    336  N   LYS A  46      25.699   6.128  32.871  1.00 25.73           N  
ATOM    337  CA  LYS A  46      25.385   6.801  31.589  1.00 27.71           C  
ATOM    338  C   LYS A  46      24.183   7.711  31.756  1.00 26.98           C  
ATOM    339  O   LYS A  46      24.090   8.772  31.101  1.00 29.80           O  
ATOM    340  CB  LYS A  46      25.130   5.808  30.440  1.00 30.60           C  
ATOM    341  CG  LYS A  46      26.322   5.550  29.511  1.00 32.74           C  
ATOM    342  CD  LYS A  46      27.342   4.594  30.165  1.00 35.27           C  
ATOM    343  CE  LYS A  46      28.471   4.190  29.205  1.00 36.49           C  
ATOM    344  NZ  LYS A  46      27.945   3.532  27.944  1.00 37.53           N  
ATOM    345  N   GLU A  47      23.277   7.334  32.659  1.00 25.66           N  
ATOM    346  CA  GLU A  47      22.100   8.169  32.902  1.00 24.77           C  
ATOM    347  C   GLU A  47      22.466   9.488  33.584  1.00 22.76           C  
ATOM    348  O   GLU A  47      21.866  10.526  33.294  1.00 22.31           O  
ATOM    349  CB  GLU A  47      21.076   7.431  33.757  1.00 27.62           C  
ATOM    350  CG  GLU A  47      20.546   6.175  33.120  1.00 34.49           C  
ATOM    351  CD  GLU A  47      19.904   6.433  31.770  1.00 39.42           C  
ATOM    352  OE1 GLU A  47      20.645   6.639  30.761  1.00 43.04           O  
ATOM    353  OE2 GLU A  47      18.646   6.425  31.718  1.00 43.50           O  
ATOM    354  N   LEU A  48      23.481   9.441  34.451  1.00 19.62           N  
ATOM    355  CA  LEU A  48      23.964  10.598  35.215  1.00 17.74           C  
ATOM    356  C   LEU A  48      24.318  11.805  34.358  1.00 16.90           C  
ATOM    357  O   LEU A  48      23.808  12.892  34.588  1.00 16.85           O  
ATOM    358  CB  LEU A  48      25.161  10.192  36.085  1.00 15.54           C  
ATOM    359  CG  LEU A  48      25.674  11.143  37.172  1.00 14.08           C  
ATOM    360  CD1 LEU A  48      26.581  10.375  38.108  1.00 13.74           C  
ATOM    361  CD2 LEU A  48      26.418  12.297  36.540  1.00 12.89           C  
ATOM    362  N   PHE A  49      25.193  11.619  33.381  1.00 16.59           N  
ATOM    363  CA  PHE A  49      25.598  12.696  32.494  1.00 17.64           C  
ATOM    364  C   PHE A  49      24.437  13.356  31.706  1.00 20.58           C  
ATOM    365  O   PHE A  49      24.418  14.595  31.522  1.00 21.08           O  
ATOM    366  CB  PHE A  49      26.704  12.199  31.554  1.00 18.25           C  
ATOM    367  CG  PHE A  49      28.036  11.973  32.248  1.00 18.90           C  
ATOM    368  CD1 PHE A  49      28.296  10.778  32.927  1.00 19.60           C  
ATOM    369  CD2 PHE A  49      29.006  12.977  32.262  1.00 19.86           C  
ATOM    370  CE1 PHE A  49      29.496  10.587  33.621  1.00 20.46           C  
ATOM    371  CE2 PHE A  49      30.218  12.801  32.950  1.00 19.49           C  
ATOM    372  CZ  PHE A  49      30.459  11.610  33.632  1.00 21.55           C  
ATOM    373  N   ASP A  50      23.462  12.562  31.256  1.00 20.93           N  
ATOM    374  CA  ASP A  50      22.333  13.148  30.523  1.00 22.85           C  
ATOM    375  C   ASP A  50      21.387  13.907  31.445  1.00 20.86           C  
ATOM    376  O   ASP A  50      20.881  14.970  31.085  1.00 20.73           O  
ATOM    377  CB  ASP A  50      21.547  12.094  29.726  1.00 26.38           C  
ATOM    378  CG  ASP A  50      22.256  11.678  28.435  1.00 32.21           C  
ATOM    379  OD1 ASP A  50      22.351  10.454  28.190  1.00 35.89           O  
ATOM    380  OD2 ASP A  50      22.706  12.560  27.654  1.00 35.47           O  
ATOM    381  N   GLU A  51      21.153  13.366  32.634  1.00 19.77           N  
ATOM    382  CA  GLU A  51      20.254  14.013  33.573  1.00 19.26           C  
ATOM    383  C   GLU A  51      20.837  15.335  34.086  1.00 19.51           C  
ATOM    384  O   GLU A  51      20.117  16.318  34.208  1.00 19.48           O  
ATOM    385  CB  GLU A  51      19.901  13.075  34.723  1.00 19.92           C  
ATOM    386  CG  GLU A  51      18.720  13.594  35.548  1.00 25.00           C  
ATOM    387  CD  GLU A  51      18.322  12.713  36.717  1.00 26.50           C  
ATOM    388  OE1 GLU A  51      17.499  13.172  37.547  1.00 29.84           O  
ATOM    389  OE2 GLU A  51      18.810  11.566  36.807  1.00 28.66           O  
ATOM    390  N   LEU A  52      22.147  15.376  34.323  1.00 17.99           N  
ATOM    391  CA  LEU A  52      22.823  16.589  34.800  1.00 19.22           C  
ATOM    392  C   LEU A  52      22.621  17.776  33.832  1.00 19.38           C  
ATOM    393  O   LEU A  52      22.206  18.856  34.243  1.00 19.00           O  
ATOM    394  CB  LEU A  52      24.334  16.312  34.980  1.00 19.13           C  
ATOM    395  CG  LEU A  52      25.246  17.373  35.620  1.00 18.88           C  
ATOM    396  CD1 LEU A  52      24.938  17.530  37.101  1.00 16.84           C  
ATOM    397  CD2 LEU A  52      26.695  16.922  35.459  1.00 20.78           C  
ATOM    398  N   VAL A  53      22.889  17.539  32.552  1.00 19.11           N  
ATOM    399  CA  VAL A  53      22.760  18.545  31.497  1.00 20.96           C  
ATOM    400  C   VAL A  53      21.317  18.929  31.176  1.00 22.78           C  
ATOM    401  O   VAL A  53      21.071  20.004  30.618  1.00 26.03           O  
ATOM    402  CB  VAL A  53      23.416  18.055  30.205  1.00 19.21           C  
ATOM    403  CG1 VAL A  53      23.164  19.008  29.077  1.00 20.19           C  
ATOM    404  CG2 VAL A  53      24.903  17.843  30.429  1.00 18.65           C  
ATOM    405  N   LYS A  54      20.373  18.060  31.527  1.00 23.23           N  
ATOM    406  CA  LYS A  54      18.965  18.307  31.261  1.00 24.41           C  
ATOM    407  C   LYS A  54      18.205  18.928  32.437  1.00 24.08           C  
ATOM    408  O   LYS A  54      17.334  19.768  32.207  1.00 26.56           O  
ATOM    409  CB  LYS A  54      18.280  17.013  30.773  1.00 26.25           C  
ATOM    410  CG  LYS A  54      16.795  17.147  30.474  1.00 30.18           C  
ATOM    411  CD  LYS A  54      16.290  15.979  29.628  1.00 33.41           C  
ATOM    412  CE  LYS A  54      14.737  15.927  29.534  1.00 34.98           C  
ATOM    413  NZ  LYS A  54      14.094  15.180  30.685  1.00 36.09           N  
ATOM    414  N   LYS A  55      18.564  18.593  33.679  1.00 21.61           N  
ATOM    415  CA  LYS A  55      17.864  19.116  34.858  1.00 20.65           C  
ATOM    416  C   LYS A  55      18.485  20.328  35.567  1.00 19.91           C  
ATOM    417  O   LYS A  55      17.830  20.941  36.429  1.00 18.17           O  
ATOM    418  CB  LYS A  55      17.692  18.030  35.933  1.00 22.54           C  
ATOM    419  CG  LYS A  55      17.074  16.719  35.479  1.00 26.58           C  
ATOM    420  CD  LYS A  55      15.698  16.903  34.872  1.00 30.04           C  
ATOM    421  CE  LYS A  55      15.072  15.550  34.534  1.00 32.85           C  
ATOM    422  NZ  LYS A  55      13.701  15.688  33.942  1.00 35.25           N  
ATOM    423  N   PHE A  56      19.748  20.636  35.266  1.00 17.44           N  
ATOM    424  CA  PHE A  56      20.433  21.739  35.934  1.00 16.28           C  
ATOM    425  C   PHE A  56      21.196  22.667  34.991  1.00 17.03           C  
ATOM    426  O   PHE A  56      21.447  22.324  33.826  1.00 16.72           O  
ATOM    427  CB  PHE A  56      21.420  21.171  36.963  1.00 16.56           C  
ATOM    428  CG  PHE A  56      20.801  20.203  37.945  1.00 14.88           C  
ATOM    429  CD1 PHE A  56      20.867  18.831  37.728  1.00 14.18           C  
ATOM    430  CD2 PHE A  56      20.167  20.667  39.096  1.00 14.79           C  
ATOM    431  CE1 PHE A  56      20.312  17.943  38.649  1.00 15.76           C  
ATOM    432  CE2 PHE A  56      19.610  19.784  40.023  1.00 16.14           C  
ATOM    433  CZ  PHE A  56      19.686  18.410  39.799  1.00 15.74           C  
ATOM    434  N   LYS A  57      21.549  23.854  35.495  1.00 16.16           N  
ATOM    435  CA  LYS A  57      22.339  24.797  34.712  1.00 16.53           C  
ATOM    436  C   LYS A  57      23.828  24.379  34.804  1.00 15.86           C  
ATOM    437  O   LYS A  57      24.426  24.442  35.877  1.00 15.34           O  
ATOM    438  CB  LYS A  57      22.166  26.226  35.233  1.00 18.38           C  
ATOM    439  CG  LYS A  57      22.975  27.242  34.448  1.00 21.72           C  
ATOM    440  CD  LYS A  57      22.802  28.617  35.044  1.00 27.11           C  
ATOM    441  CE  LYS A  57      23.947  29.544  34.654  1.00 30.72           C  
ATOM    442  NZ  LYS A  57      24.127  29.585  33.170  1.00 34.85           N  
ATOM    443  N   VAL A  58      24.416  23.983  33.680  1.00 15.17           N  
ATOM    444  CA  VAL A  58      25.804  23.531  33.666  1.00 15.17           C  
ATOM    445  C   VAL A  58      26.765  24.506  33.007  1.00 15.51           C  
ATOM    446  O   VAL A  58      26.345  25.364  32.240  1.00 16.36           O  
ATOM    447  CB  VAL A  58      25.956  22.174  32.912  1.00 15.24           C  
ATOM    448  CG1 VAL A  58      25.301  21.050  33.673  1.00 16.50           C  
ATOM    449  CG2 VAL A  58      25.364  22.279  31.507  1.00 16.89           C  
ATOM    450  N   GLU A  59      28.046  24.397  33.369  1.00 15.07           N  
ATOM    451  CA  GLU A  59      29.130  25.185  32.780  1.00 16.10           C  
ATOM    452  C   GLU A  59      30.158  24.150  32.273  1.00 15.18           C  
ATOM    453  O   GLU A  59      30.315  23.082  32.885  1.00 14.49           O  
ATOM    454  CB  GLU A  59      29.834  26.069  33.813  1.00 19.92           C  
ATOM    455  CG  GLU A  59      28.984  27.157  34.439  1.00 26.05           C  
ATOM    456  CD  GLU A  59      29.795  28.167  35.296  1.00 31.55           C  
ATOM    457  OE1 GLU A  59      29.208  29.217  35.672  1.00 34.96           O  
ATOM    458  OE2 GLU A  59      30.998  27.933  35.600  1.00 31.76           O  
ATOM    459  N   TYR A  60      30.909  24.519  31.234  1.00 13.81           N  
ATOM    460  CA  TYR A  60      31.930  23.658  30.638  1.00 13.44           C  
ATOM    461  C   TYR A  60      33.276  24.356  30.700  1.00 14.85           C  
ATOM    462  O   TYR A  60      33.392  25.524  30.299  1.00 14.79           O  
ATOM    463  CB  TYR A  60      31.613  23.384  29.167  1.00 14.40           C  
ATOM    464  CG  TYR A  60      30.325  22.632  28.942  1.00 16.18           C  
ATOM    465  CD1 TYR A  60      29.099  23.297  28.872  1.00 16.51           C  
ATOM    466  CD2 TYR A  60      30.324  21.250  28.806  1.00 17.05           C  
ATOM    467  CE1 TYR A  60      27.910  22.594  28.674  1.00 17.33           C  
ATOM    468  CE2 TYR A  60      29.137  20.545  28.605  1.00 17.70           C  
ATOM    469  CZ  TYR A  60      27.940  21.221  28.542  1.00 17.59           C  
ATOM    470  OH  TYR A  60      26.781  20.514  28.370  1.00 18.98           O  
ATOM    471  N   HIS A  61      34.286  23.637  31.200  1.00 14.08           N  
ATOM    472  CA  HIS A  61      35.662  24.144  31.315  1.00 13.34           C  
ATOM    473  C   HIS A  61      36.688  23.053  30.985  1.00 13.57           C  
ATOM    474  O   HIS A  61      36.570  21.925  31.466  1.00 13.47           O  
ATOM    475  CB  HIS A  61      35.961  24.583  32.753  1.00 14.98           C  
ATOM    476  CG  HIS A  61      35.226  25.811  33.191  1.00 17.80           C  
ATOM    477  ND1 HIS A  61      34.058  25.758  33.924  1.00 18.56           N  
ATOM    478  CD2 HIS A  61      35.515  27.125  33.025  1.00 18.19           C  
ATOM    479  CE1 HIS A  61      33.662  26.990  34.195  1.00 19.62           C  
ATOM    480  NE2 HIS A  61      34.529  27.836  33.661  1.00 18.94           N  
ATOM    481  N   ALA A  62      37.714  23.400  30.214  1.00 12.49           N  
ATOM    482  CA  ALA A  62      38.795  22.453  29.893  1.00 11.88           C  
ATOM    483  C   ALA A  62      39.461  22.024  31.213  1.00 12.36           C  
ATOM    484  O   ALA A  62      39.743  22.857  32.098  1.00 13.14           O  
ATOM    485  CB  ALA A  62      39.823  23.107  28.964  1.00 11.34           C  
ATOM    486  N   GLY A  63      39.667  20.714  31.353  1.00 11.40           N  
ATOM    487  CA  GLY A  63      40.244  20.151  32.565  1.00 10.93           C  
ATOM    488  C   GLY A  63      41.190  18.969  32.418  1.00 10.08           C  
ATOM    489  O   GLY A  63      41.810  18.789  31.362  1.00 10.64           O  
ATOM    490  N   GLY A  64      41.189  18.095  33.432  1.00  9.52           N  
ATOM    491  CA  GLY A  64      42.127  16.973  33.468  1.00  9.39           C  
ATOM    492  C   GLY A  64      43.197  17.399  34.481  1.00  8.88           C  
ATOM    493  O   GLY A  64      43.793  18.474  34.314  1.00  9.94           O  
ATOM    494  N   SER A  65      43.484  16.574  35.493  1.00  6.89           N  
ATOM    495  CA  SER A  65      44.449  16.941  36.534  1.00  6.87           C  
ATOM    496  C   SER A  65      45.855  17.357  36.079  1.00  6.87           C  
ATOM    497  O   SER A  65      46.330  18.447  36.425  1.00  7.22           O  
ATOM    498  CB  SER A  65      44.526  15.862  37.609  1.00  6.97           C  
ATOM    499  OG  SER A  65      45.328  16.298  38.704  1.00  8.87           O  
ATOM    500  N   THR A  66      46.534  16.494  35.336  1.00  7.71           N  
ATOM    501  CA  THR A  66      47.880  16.818  34.852  1.00  8.28           C  
ATOM    502  C   THR A  66      47.847  18.056  33.935  1.00  8.86           C  
ATOM    503  O   THR A  66      48.723  18.931  34.033  1.00  7.79           O  
ATOM    504  CB  THR A  66      48.520  15.626  34.105  1.00  8.99           C  
ATOM    505  OG1 THR A  66      48.598  14.487  34.983  1.00  9.52           O  
ATOM    506  CG2 THR A  66      49.950  15.980  33.660  1.00  8.82           C  
ATOM    507  N   GLN A  67      46.832  18.139  33.069  1.00  9.12           N  
ATOM    508  CA  GLN A  67      46.695  19.281  32.143  1.00  9.51           C  
ATOM    509  C   GLN A  67      46.572  20.601  32.930  1.00  8.34           C  
ATOM    510  O   GLN A  67      47.222  21.576  32.580  1.00  9.30           O  
ATOM    511  CB  GLN A  67      45.489  19.088  31.198  1.00 12.02           C  
ATOM    512  CG  GLN A  67      45.492  20.064  29.995  1.00 16.68           C  
ATOM    513  CD  GLN A  67      44.658  19.576  28.808  1.00 19.94           C  
ATOM    514  OE1 GLN A  67      45.198  19.321  27.742  1.00 22.33           O  
ATOM    515  NE2 GLN A  67      43.332  19.470  28.987  1.00 22.48           N  
ATOM    516  N   ASN A  68      45.786  20.595  34.014  1.00  7.75           N  
ATOM    517  CA  ASN A  68      45.602  21.769  34.875  1.00  9.02           C  
ATOM    518  C   ASN A  68      46.964  22.192  35.455  1.00  9.37           C  
ATOM    519  O   ASN A  68      47.332  23.372  35.393  1.00  8.99           O  
ATOM    520  CB  ASN A  68      44.645  21.451  36.058  1.00  8.81           C  
ATOM    521  CG  ASN A  68      43.174  21.395  35.654  1.00 10.09           C  
ATOM    522  OD1 ASN A  68      42.791  21.814  34.564  1.00 11.67           O  
ATOM    523  ND2 ASN A  68      42.347  20.867  36.540  1.00  9.70           N  
ATOM    524  N   SER A  69      47.691  21.238  36.043  1.00  7.68           N  
ATOM    525  CA  SER A  69      49.009  21.528  36.636  1.00  7.47           C  
ATOM    526  C   SER A  69      50.024  22.089  35.625  1.00  7.08           C  
ATOM    527  O   SER A  69      50.782  23.012  35.945  1.00  7.80           O  
ATOM    528  CB  SER A  69      49.580  20.275  37.334  1.00  7.43           C  
ATOM    529  OG  SER A  69      48.771  19.885  38.431  1.00  7.20           O  
ATOM    530  N   ILE A  70      50.025  21.550  34.411  1.00  7.03           N  
ATOM    531  CA  ILE A  70      50.947  22.015  33.361  1.00  8.06           C  
ATOM    532  C   ILE A  70      50.589  23.462  32.911  1.00  8.89           C  
ATOM    533  O   ILE A  70      51.494  24.289  32.685  1.00  8.96           O  
ATOM    534  CB  ILE A  70      50.947  21.027  32.161  1.00  8.63           C  
ATOM    535  CG1 ILE A  70      51.646  19.703  32.555  1.00 11.68           C  
ATOM    536  CG2 ILE A  70      51.572  21.632  30.935  1.00  9.06           C  
ATOM    537  CD1 ILE A  70      53.127  19.790  32.920  1.00 11.25           C  
ATOM    538  N   LYS A  71      49.292  23.779  32.814  1.00  8.71           N  
ATOM    539  CA  LYS A  71      48.845  25.146  32.433  1.00  9.26           C  
ATOM    540  C   LYS A  71      49.263  26.149  33.507  1.00  9.67           C  
ATOM    541  O   LYS A  71      49.732  27.252  33.192  1.00  9.95           O  
ATOM    542  CB  LYS A  71      47.330  25.216  32.270  1.00 11.73           C  
ATOM    543  CG  LYS A  71      46.835  24.522  31.014  1.00 17.13           C  
ATOM    544  CD  LYS A  71      45.307  24.611  30.851  1.00 19.82           C  
ATOM    545  CE  LYS A  71      44.852  23.910  29.556  1.00 18.53           C  
ATOM    546  NZ  LYS A  71      43.385  23.694  29.574  1.00 17.35           N  
ATOM    547  N   VAL A  72      49.119  25.754  34.769  1.00  8.17           N  
ATOM    548  CA  VAL A  72      49.509  26.622  35.883  1.00  8.33           C  
ATOM    549  C   VAL A  72      51.038  26.819  35.942  1.00  8.70           C  
ATOM    550  O   VAL A  72      51.507  27.924  36.211  1.00  8.89           O  
ATOM    551  CB  VAL A  72      48.950  26.100  37.242  1.00  8.56           C  
ATOM    552  CG1 VAL A  72      49.554  26.870  38.412  1.00  8.74           C  
ATOM    553  CG2 VAL A  72      47.420  26.224  37.252  1.00  8.75           C  
ATOM    554  N   ALA A  73      51.813  25.759  35.686  1.00  8.23           N  
ATOM    555  CA  ALA A  73      53.272  25.876  35.701  1.00  8.33           C  
ATOM    556  C   ALA A  73      53.687  26.857  34.609  1.00  9.13           C  
ATOM    557  O   ALA A  73      54.494  27.753  34.863  1.00  9.59           O  
ATOM    558  CB  ALA A  73      53.931  24.509  35.478  1.00  8.32           C  
ATOM    559  N   GLN A  74      53.136  26.688  33.405  1.00  8.38           N  
ATOM    560  CA  GLN A  74      53.442  27.570  32.280  1.00  9.92           C  
ATOM    561  C   GLN A  74      53.095  29.034  32.636  1.00 11.33           C  
ATOM    562  O   GLN A  74      53.868  29.956  32.325  1.00 12.01           O  
ATOM    563  CB  GLN A  74      52.646  27.135  31.052  1.00  9.79           C  
ATOM    564  CG  GLN A  74      52.890  27.988  29.802  1.00 13.33           C  
ATOM    565  CD  GLN A  74      54.358  28.047  29.349  1.00 14.17           C  
ATOM    566  OE1 GLN A  74      55.036  27.023  29.251  1.00 14.32           O  
ATOM    567  NE2 GLN A  74      54.843  29.262  29.053  1.00 15.86           N  
ATOM    568  N   TRP A  75      51.954  29.245  33.299  1.00  9.35           N  
ATOM    569  CA  TRP A  75      51.532  30.591  33.688  1.00 10.41           C  
ATOM    570  C   TRP A  75      52.568  31.256  34.599  1.00 11.20           C  
ATOM    571  O   TRP A  75      52.908  32.419  34.402  1.00 11.92           O  
ATOM    572  CB  TRP A  75      50.181  30.544  34.415  1.00 10.60           C  
ATOM    573  CG  TRP A  75      49.665  31.889  34.902  1.00 11.70           C  
ATOM    574  CD1 TRP A  75      49.339  32.982  34.127  1.00 13.43           C  
ATOM    575  CD2 TRP A  75      49.356  32.263  36.260  1.00 12.35           C  
ATOM    576  NE1 TRP A  75      48.844  33.999  34.917  1.00 13.52           N  
ATOM    577  CE2 TRP A  75      48.841  33.591  36.225  1.00 13.39           C  
ATOM    578  CE3 TRP A  75      49.452  31.606  37.496  1.00 13.23           C  
ATOM    579  CZ2 TRP A  75      48.427  34.269  37.378  1.00 13.83           C  
ATOM    580  CZ3 TRP A  75      49.034  32.286  38.653  1.00 13.84           C  
ATOM    581  CH2 TRP A  75      48.530  33.602  38.577  1.00 13.75           C  
ATOM    582  N   MET A  76      53.061  30.519  35.594  1.00 10.54           N  
ATOM    583  CA  MET A  76      54.024  31.050  36.550  1.00 10.33           C  
ATOM    584  C   MET A  76      55.394  31.265  35.920  1.00 12.36           C  
ATOM    585  O   MET A  76      56.119  32.170  36.327  1.00 13.63           O  
ATOM    586  CB  MET A  76      54.140  30.109  37.750  1.00 12.50           C  
ATOM    587  CG  MET A  76      52.890  30.000  38.639  1.00 12.61           C  
ATOM    588  SD  MET A  76      52.732  31.341  39.827  1.00 16.26           S  
ATOM    589  CE  MET A  76      54.101  31.044  40.929  1.00 15.48           C  
ATOM    590  N   ILE A  77      55.755  30.436  34.944  1.00 11.45           N  
ATOM    591  CA  ILE A  77      57.049  30.551  34.268  1.00 12.76           C  
ATOM    592  C   ILE A  77      57.054  31.831  33.395  1.00 14.13           C  
ATOM    593  O   ILE A  77      58.067  32.551  33.347  1.00 15.02           O  
ATOM    594  CB  ILE A  77      57.324  29.263  33.414  1.00 12.69           C  
ATOM    595  CG1 ILE A  77      57.640  28.077  34.339  1.00 12.03           C  
ATOM    596  CG2 ILE A  77      58.435  29.495  32.374  1.00 15.02           C  
ATOM    597  CD1 ILE A  77      57.722  26.707  33.649  1.00 11.29           C  
ATOM    598  N   GLN A  78      55.904  32.117  32.768  1.00 14.56           N  
ATOM    599  CA  GLN A  78      55.639  33.271  31.884  1.00 17.60           C  
ATOM    600  C   GLN A  78      56.391  33.272  30.561  1.00 17.71           C  
ATOM    601  O   GLN A  78      55.773  33.326  29.490  1.00 17.43           O  
ATOM    602  CB  GLN A  78      55.856  34.612  32.595  1.00 19.46           C  
ATOM    603  CG  GLN A  78      54.688  35.075  33.434  1.00 23.85           C  
ATOM    604  CD  GLN A  78      53.443  35.394  32.593  1.00 28.90           C  
ATOM    605  OE1 GLN A  78      53.348  36.483  31.994  1.00 31.59           O  
ATOM    606  NE2 GLN A  78      52.477  34.451  32.545  1.00 25.91           N  
ATOM    607  N   GLN A  79      57.721  33.224  30.646  1.00 17.31           N  
ATOM    608  CA  GLN A  79      58.577  33.217  29.467  1.00 18.20           C  
ATOM    609  C   GLN A  79      59.640  32.127  29.614  1.00 17.84           C  
ATOM    610  O   GLN A  79      60.233  31.974  30.681  1.00 18.81           O  
ATOM    611  CB  GLN A  79      59.250  34.586  29.303  1.00 20.28           C  
ATOM    612  CG  GLN A  79      58.277  35.727  28.972  1.00 25.04           C  
ATOM    613  CD  GLN A  79      57.552  35.537  27.617  1.00 28.04           C  
ATOM    614  OE1 GLN A  79      56.339  35.819  27.487  1.00 29.91           O  
ATOM    615  NE2 GLN A  79      58.289  35.056  26.616  1.00 27.03           N  
ATOM    616  N   PRO A  80      59.906  31.360  28.538  1.00 17.13           N  
ATOM    617  CA  PRO A  80      59.281  31.454  27.214  1.00 16.95           C  
ATOM    618  C   PRO A  80      57.948  30.694  27.081  1.00 16.97           C  
ATOM    619  O   PRO A  80      57.542  29.942  27.985  1.00 17.19           O  
ATOM    620  CB  PRO A  80      60.337  30.810  26.312  1.00 17.89           C  
ATOM    621  CG  PRO A  80      60.843  29.686  27.170  1.00 18.09           C  
ATOM    622  CD  PRO A  80      60.923  30.287  28.570  1.00 17.07           C  
ATOM    623  N   HIS A  81      57.256  30.920  25.968  1.00 16.85           N  
ATOM    624  CA  HIS A  81      56.031  30.181  25.695  1.00 18.06           C  
ATOM    625  C   HIS A  81      56.535  28.782  25.391  1.00 16.97           C  
ATOM    626  O   HIS A  81      57.691  28.607  24.986  1.00 16.93           O  
ATOM    627  CB  HIS A  81      55.302  30.722  24.459  1.00 19.01           C  
ATOM    628  CG  HIS A  81      54.627  32.035  24.684  1.00 19.35           C  
ATOM    629  ND1 HIS A  81      54.168  32.818  23.651  1.00 19.56           N  
ATOM    630  CD2 HIS A  81      54.333  32.703  25.825  1.00 21.01           C  
ATOM    631  CE1 HIS A  81      53.618  33.913  24.144  1.00 19.17           C  
ATOM    632  NE2 HIS A  81      53.705  33.868  25.460  1.00 20.90           N  
ATOM    633  N   LYS A  82      55.698  27.782  25.642  1.00 17.64           N  
ATOM    634  CA  LYS A  82      56.070  26.393  25.370  1.00 17.67           C  
ATOM    635  C   LYS A  82      57.232  25.806  26.219  1.00 16.14           C  
ATOM    636  O   LYS A  82      57.965  24.924  25.756  1.00 16.95           O  
ATOM    637  CB  LYS A  82      56.290  26.177  23.849  1.00 18.96           C  
ATOM    638  CG  LYS A  82      55.032  26.452  23.000  1.00 21.92           C  
ATOM    639  CD  LYS A  82      55.171  26.102  21.513  1.00 25.75           C  
ATOM    640  CE  LYS A  82      55.932  27.184  20.731  1.00 30.44           C  
ATOM    641  NZ  LYS A  82      56.114  26.869  19.243  1.00 32.34           N  
ATOM    642  N   ALA A  83      57.394  26.308  27.451  1.00 13.89           N  
ATOM    643  CA  ALA A  83      58.386  25.797  28.392  1.00 12.40           C  
ATOM    644  C   ALA A  83      57.872  24.420  28.863  1.00 13.32           C  
ATOM    645  O   ALA A  83      58.671  23.547  29.220  1.00 13.15           O  
ATOM    646  CB  ALA A  83      58.531  26.723  29.604  1.00 10.81           C  
ATOM    647  N   ALA A  84      56.538  24.259  28.903  1.00 13.90           N  
ATOM    648  CA  ALA A  84      55.890  22.997  29.328  1.00 13.33           C  
ATOM    649  C   ALA A  84      55.178  22.238  28.192  1.00 13.36           C  
ATOM    650  O   ALA A  84      54.463  22.839  27.383  1.00 13.23           O  
ATOM    651  CB  ALA A  84      54.931  23.247  30.525  1.00 13.02           C  
ATOM    652  N   THR A  85      55.410  20.916  28.150  1.00 13.61           N  
ATOM    653  CA  THR A  85      54.866  19.984  27.147  1.00 12.78           C  
ATOM    654  C   THR A  85      53.735  19.113  27.753  1.00 12.31           C  
ATOM    655  O   THR A  85      53.788  18.768  28.937  1.00 12.54           O  
ATOM    656  CB  THR A  85      55.979  18.965  26.682  1.00 13.32           C  
ATOM    657  OG1 THR A  85      57.203  19.655  26.402  1.00 13.26           O  
ATOM    658  CG2 THR A  85      55.531  18.183  25.419  1.00 14.33           C  
ATOM    659  N   PHE A  86      52.733  18.754  26.954  1.00 10.91           N  
ATOM    660  CA  PHE A  86      51.670  17.868  27.446  1.00 10.80           C  
ATOM    661  C   PHE A  86      51.209  16.880  26.365  1.00 11.78           C  
ATOM    662  O   PHE A  86      50.913  17.320  25.241  1.00 10.25           O  
ATOM    663  CB  PHE A  86      50.436  18.662  27.912  1.00 11.75           C  
ATOM    664  CG  PHE A  86      49.315  17.788  28.423  1.00 10.87           C  
ATOM    665  CD1 PHE A  86      49.345  17.283  29.718  1.00 10.73           C  
ATOM    666  CD2 PHE A  86      48.259  17.419  27.584  1.00 10.89           C  
ATOM    667  CE1 PHE A  86      48.342  16.414  30.174  1.00 10.06           C  
ATOM    668  CE2 PHE A  86      47.258  16.551  28.029  1.00 10.49           C  
ATOM    669  CZ  PHE A  86      47.306  16.049  29.334  1.00 10.93           C  
ATOM    670  N   PHE A  87      51.108  15.584  26.728  1.00 10.40           N  
ATOM    671  CA  PHE A  87      50.620  14.505  25.835  1.00 10.37           C  
ATOM    672  C   PHE A  87      49.350  13.829  26.455  1.00 10.79           C  
ATOM    673  O   PHE A  87      49.299  13.572  27.659  1.00 10.55           O  
ATOM    674  CB  PHE A  87      51.644  13.351  25.682  1.00 11.84           C  
ATOM    675  CG  PHE A  87      52.905  13.671  24.876  1.00 10.93           C  
ATOM    676  CD1 PHE A  87      53.156  14.931  24.336  1.00 12.12           C  
ATOM    677  CD2 PHE A  87      53.862  12.673  24.699  1.00 10.56           C  
ATOM    678  CE1 PHE A  87      54.354  15.181  23.632  1.00 12.31           C  
ATOM    679  CE2 PHE A  87      55.050  12.904  24.009  1.00 10.60           C  
ATOM    680  CZ  PHE A  87      55.301  14.163  23.471  1.00 11.65           C  
ATOM    681  N   GLY A  88      48.388  13.466  25.604  1.00 12.05           N  
ATOM    682  CA  GLY A  88      47.159  12.791  26.029  1.00 10.30           C  
ATOM    683  C   GLY A  88      46.328  12.375  24.807  1.00 11.14           C  
ATOM    684  O   GLY A  88      46.676  12.748  23.678  1.00 10.18           O  
ATOM    685  N   CYS A  89      45.215  11.663  25.016  1.00  9.95           N  
ATOM    686  CA  CYS A  89      44.372  11.220  23.903  1.00 10.53           C  
ATOM    687  C   CYS A  89      43.010  11.881  23.930  1.00 11.56           C  
ATOM    688  O   CYS A  89      42.419  12.022  25.005  1.00 10.79           O  
ATOM    689  CB  CYS A  89      44.183   9.701  23.965  1.00 10.81           C  
ATOM    690  SG  CYS A  89      43.163   8.977  22.633  1.00 12.81           S  
ATOM    691  N   ILE A  90      42.505  12.265  22.748  1.00 11.29           N  
ATOM    692  CA  ILE A  90      41.181  12.898  22.622  1.00 11.55           C  
ATOM    693  C   ILE A  90      40.426  12.327  21.407  1.00 12.94           C  
ATOM    694  O   ILE A  90      40.993  11.553  20.622  1.00 12.15           O  
ATOM    695  CB  ILE A  90      41.264  14.441  22.412  1.00 11.76           C  
ATOM    696  CG1 ILE A  90      42.067  14.750  21.143  1.00 11.74           C  
ATOM    697  CG2 ILE A  90      41.796  15.152  23.680  1.00 11.49           C  
ATOM    698  CD1 ILE A  90      42.093  16.221  20.767  1.00 13.69           C  
ATOM    699  N   GLY A  91      39.150  12.705  21.290  1.00 13.49           N  
ATOM    700  CA  GLY A  91      38.329  12.286  20.169  1.00 14.20           C  
ATOM    701  C   GLY A  91      38.370  13.359  19.095  1.00 16.05           C  
ATOM    702  O   GLY A  91      38.954  14.424  19.284  1.00 15.20           O  
ATOM    703  N   ILE A  92      37.774  13.078  17.948  1.00 17.29           N  
ATOM    704  CA  ILE A  92      37.720  14.056  16.851  1.00 19.70           C  
ATOM    705  C   ILE A  92      36.308  14.652  16.852  1.00 20.24           C  
ATOM    706  O   ILE A  92      35.445  14.233  16.076  1.00 21.48           O  
ATOM    707  CB  ILE A  92      38.060  13.382  15.513  1.00 19.88           C  
ATOM    708  CG1 ILE A  92      39.524  12.914  15.569  1.00 19.90           C  
ATOM    709  CG2 ILE A  92      37.863  14.362  14.364  1.00 21.63           C  
ATOM    710  CD1 ILE A  92      39.948  11.924  14.491  1.00 22.24           C  
ATOM    711  N   ASP A  93      36.075  15.594  17.767  1.00 18.58           N  
ATOM    712  CA  ASP A  93      34.760  16.203  17.957  1.00 18.95           C  
ATOM    713  C   ASP A  93      34.833  17.628  18.495  1.00 17.39           C  
ATOM    714  O   ASP A  93      35.920  18.160  18.667  1.00 18.04           O  
ATOM    715  CB  ASP A  93      33.936  15.333  18.925  1.00 19.76           C  
ATOM    716  CG  ASP A  93      34.739  14.895  20.173  1.00 22.10           C  
ATOM    717  OD1 ASP A  93      34.426  13.804  20.713  1.00 23.51           O  
ATOM    718  OD2 ASP A  93      35.668  15.620  20.614  1.00 20.35           O  
ATOM    719  N   LYS A  94      33.676  18.225  18.788  1.00 17.17           N  
ATOM    720  CA  LYS A  94      33.625  19.590  19.304  1.00 17.40           C  
ATOM    721  C   LYS A  94      34.308  19.708  20.668  1.00 17.49           C  
ATOM    722  O   LYS A  94      35.046  20.669  20.911  1.00 16.76           O  
ATOM    723  CB  LYS A  94      32.189  20.102  19.373  1.00 17.67           C  
ATOM    724  CG  LYS A  94      31.652  20.529  18.015  1.00 20.20           C  
ATOM    725  CD  LYS A  94      30.234  21.104  18.106  1.00 22.46           C  
ATOM    726  CE  LYS A  94      29.595  21.208  16.706  1.00 25.63           C  
ATOM    727  NZ  LYS A  94      28.287  21.958  16.694  1.00 26.41           N  
ATOM    728  N   PHE A  95      34.075  18.734  21.552  1.00 16.56           N  
ATOM    729  CA  PHE A  95      34.717  18.764  22.870  1.00 17.25           C  
ATOM    730  C   PHE A  95      36.243  18.755  22.739  1.00 17.43           C  
ATOM    731  O   PHE A  95      36.942  19.472  23.457  1.00 17.26           O  
ATOM    732  CB  PHE A  95      34.254  17.592  23.731  1.00 16.55           C  
ATOM    733  CG  PHE A  95      32.891  17.779  24.330  1.00 17.53           C  
ATOM    734  CD1 PHE A  95      32.169  18.950  24.118  1.00 16.42           C  
ATOM    735  CD2 PHE A  95      32.325  16.784  25.101  1.00 17.95           C  
ATOM    736  CE1 PHE A  95      30.912  19.127  24.665  1.00 16.91           C  
ATOM    737  CE2 PHE A  95      31.045  16.954  25.661  1.00 20.11           C  
ATOM    738  CZ  PHE A  95      30.344  18.134  25.437  1.00 18.82           C  
ATOM    739  N   GLY A  96      36.742  17.941  21.808  1.00 17.59           N  
ATOM    740  CA  GLY A  96      38.171  17.844  21.562  1.00 18.83           C  
ATOM    741  C   GLY A  96      38.769  19.138  21.050  1.00 19.02           C  
ATOM    742  O   GLY A  96      39.902  19.478  21.397  1.00 19.46           O  
ATOM    743  N   GLU A  97      38.012  19.874  20.237  1.00 19.01           N  
ATOM    744  CA  GLU A  97      38.494  21.155  19.708  1.00 19.99           C  
ATOM    745  C   GLU A  97      38.611  22.191  20.835  1.00 19.53           C  
ATOM    746  O   GLU A  97      39.523  23.022  20.831  1.00 19.40           O  
ATOM    747  CB  GLU A  97      37.573  21.661  18.595  1.00 22.11           C  
ATOM    748  CG  GLU A  97      37.728  20.906  17.258  1.00 26.61           C  
ATOM    749  CD  GLU A  97      39.095  21.131  16.578  1.00 30.68           C  
ATOM    750  OE1 GLU A  97      39.603  20.192  15.910  1.00 31.81           O  
ATOM    751  OE2 GLU A  97      39.672  22.246  16.699  1.00 33.34           O  
ATOM    752  N   ILE A  98      37.701  22.121  21.810  1.00 18.97           N  
ATOM    753  CA  ILE A  98      37.728  23.017  22.967  1.00 17.74           C  
ATOM    754  C   ILE A  98      39.036  22.818  23.748  1.00 18.25           C  
ATOM    755  O   ILE A  98      39.718  23.793  24.077  1.00 19.41           O  
ATOM    756  CB  ILE A  98      36.531  22.751  23.922  1.00 17.52           C  
ATOM    757  CG1 ILE A  98      35.203  23.107  23.246  1.00 17.24           C  
ATOM    758  CG2 ILE A  98      36.662  23.563  25.198  1.00 16.68           C  
ATOM    759  CD1 ILE A  98      34.000  22.833  24.131  1.00 18.95           C  
ATOM    760  N   LEU A  99      39.400  21.557  24.011  1.00 17.86           N  
ATOM    761  CA  LEU A  99      40.623  21.230  24.767  1.00 16.29           C  
ATOM    762  C   LEU A  99      41.906  21.698  24.062  1.00 16.93           C  
ATOM    763  O   LEU A  99      42.823  22.211  24.723  1.00 16.69           O  
ATOM    764  CB  LEU A  99      40.690  19.721  25.106  1.00 13.73           C  
ATOM    765  CG  LEU A  99      39.570  19.113  25.983  1.00 14.24           C  
ATOM    766  CD1 LEU A  99      39.881  17.686  26.333  1.00 12.96           C  
ATOM    767  CD2 LEU A  99      39.346  19.915  27.274  1.00 13.61           C  
ATOM    768  N   LYS A 100      41.965  21.531  22.736  1.00 17.22           N  
ATOM    769  CA  LYS A 100      43.131  21.956  21.952  1.00 19.19           C  
ATOM    770  C   LYS A 100      43.248  23.489  21.920  1.00 20.15           C  
ATOM    771  O   LYS A 100      44.347  24.062  22.039  1.00 20.73           O  
ATOM    772  CB  LYS A 100      43.039  21.448  20.518  1.00 19.95           C  
ATOM    773  CG  LYS A 100      43.264  19.979  20.361  1.00 23.76           C  
ATOM    774  CD  LYS A 100      43.725  19.666  18.945  1.00 26.91           C  
ATOM    775  CE  LYS A 100      42.744  20.150  17.915  1.00 27.62           C  
ATOM    776  NZ  LYS A 100      41.483  19.408  18.035  1.00 30.49           N  
ATOM    777  N   ARG A 101      42.116  24.145  21.707  1.00 19.07           N  
ATOM    778  CA  ARG A 101      42.077  25.597  21.683  1.00 20.29           C  
ATOM    779  C   ARG A 101      42.561  26.152  23.037  1.00 19.22           C  
ATOM    780  O   ARG A 101      43.384  27.041  23.070  1.00 19.02           O  
ATOM    781  CB  ARG A 101      40.650  26.053  21.385  1.00 22.77           C  
ATOM    782  CG  ARG A 101      40.471  27.556  21.163  1.00 29.11           C  
ATOM    783  CD  ARG A 101      38.977  27.931  21.020  1.00 32.08           C  
ATOM    784  NE  ARG A 101      38.291  28.012  22.318  1.00 35.64           N  
ATOM    785  CZ  ARG A 101      37.198  27.326  22.649  1.00 35.18           C  
ATOM    786  NH1 ARG A 101      36.637  26.489  21.781  1.00 38.24           N  
ATOM    787  NH2 ARG A 101      36.652  27.494  23.845  1.00 36.28           N  
ATOM    788  N   LYS A 102      42.086  25.606  24.155  1.00 18.05           N  
ATOM    789  CA  LYS A 102      42.523  26.108  25.462  1.00 18.37           C  
ATOM    790  C   LYS A 102      43.976  25.793  25.816  1.00 17.54           C  
ATOM    791  O   LYS A 102      44.610  26.560  26.541  1.00 17.18           O  
ATOM    792  CB  LYS A 102      41.597  25.640  26.583  1.00 18.44           C  
ATOM    793  CG  LYS A 102      40.219  26.245  26.474  1.00 21.88           C  
ATOM    794  CD  LYS A 102      40.293  27.749  26.745  1.00 26.10           C  
ATOM    795  CE  LYS A 102      39.001  28.456  26.344  1.00 30.58           C  
ATOM    796  NZ  LYS A 102      39.072  29.965  26.454  1.00 32.46           N  
ATOM    797  N   ALA A 103      44.515  24.687  25.312  1.00 15.99           N  
ATOM    798  CA  ALA A 103      45.908  24.356  25.609  1.00 15.27           C  
ATOM    799  C   ALA A 103      46.822  25.354  24.881  1.00 16.34           C  
ATOM    800  O   ALA A 103      47.840  25.792  25.425  1.00 15.02           O  
ATOM    801  CB  ALA A 103      46.219  22.942  25.192  1.00 15.29           C  
ATOM    802  N   ALA A 104      46.420  25.734  23.663  1.00 16.97           N  
ATOM    803  CA  ALA A 104      47.174  26.696  22.851  1.00 17.22           C  
ATOM    804  C   ALA A 104      47.137  28.107  23.472  1.00 17.99           C  
ATOM    805  O   ALA A 104      48.169  28.782  23.566  1.00 17.53           O  
ATOM    806  CB  ALA A 104      46.635  26.710  21.402  1.00 17.79           C  
ATOM    807  N   GLU A 105      45.956  28.542  23.906  1.00 18.13           N  
ATOM    808  CA  GLU A 105      45.818  29.844  24.530  1.00 19.20           C  
ATOM    809  C   GLU A 105      46.636  29.916  25.830  1.00 19.13           C  
ATOM    810  O   GLU A 105      46.999  31.007  26.279  1.00 18.35           O  
ATOM    811  CB  GLU A 105      44.348  30.137  24.828  1.00 23.19           C  
ATOM    812  CG  GLU A 105      43.439  30.215  23.592  1.00 28.52           C  
ATOM    813  CD  GLU A 105      41.966  30.492  23.945  1.00 32.12           C  
ATOM    814  OE1 GLU A 105      41.113  30.536  23.019  1.00 34.64           O  
ATOM    815  OE2 GLU A 105      41.661  30.667  25.151  1.00 34.13           O  
ATOM    816  N   ALA A 106      46.907  28.757  26.440  1.00 17.22           N  
ATOM    817  CA  ALA A 106      47.676  28.678  27.683  1.00 15.84           C  
ATOM    818  C   ALA A 106      49.181  28.673  27.407  1.00 14.95           C  
ATOM    819  O   ALA A 106      49.999  28.658  28.340  1.00 15.34           O  
ATOM    820  CB  ALA A 106      47.277  27.418  28.479  1.00 15.77           C  
ATOM    821  N   HIS A 107      49.549  28.692  26.128  1.00 14.78           N  
ATOM    822  CA  HIS A 107      50.956  28.700  25.710  1.00 15.48           C  
ATOM    823  C   HIS A 107      51.699  27.392  26.057  1.00 15.62           C  
ATOM    824  O   HIS A 107      52.916  27.388  26.257  1.00 16.21           O  
ATOM    825  CB  HIS A 107      51.694  29.941  26.293  1.00 17.38           C  
ATOM    826  CG  HIS A 107      50.999  31.242  26.015  1.00 17.96           C  
ATOM    827  ND1 HIS A 107      50.679  31.661  24.736  1.00 20.00           N  
ATOM    828  CD2 HIS A 107      50.496  32.182  26.852  1.00 19.97           C  
ATOM    829  CE1 HIS A 107      50.001  32.796  24.796  1.00 18.33           C  
ATOM    830  NE2 HIS A 107      49.875  33.135  26.068  1.00 21.36           N  
ATOM    831  N   VAL A 108      50.954  26.289  26.138  1.00 15.23           N  
ATOM    832  CA  VAL A 108      51.529  24.967  26.429  1.00 13.50           C  
ATOM    833  C   VAL A 108      51.786  24.233  25.095  1.00 14.24           C  
ATOM    834  O   VAL A 108      51.005  24.389  24.150  1.00 15.36           O  
ATOM    835  CB  VAL A 108      50.540  24.136  27.338  1.00 14.43           C  
ATOM    836  CG1 VAL A 108      50.936  22.629  27.415  1.00 12.66           C  
ATOM    837  CG2 VAL A 108      50.489  24.743  28.751  1.00 13.57           C  
ATOM    838  N   ASP A 109      52.891  23.478  25.004  1.00 14.91           N  
ATOM    839  CA  ASP A 109      53.208  22.692  23.795  1.00 15.64           C  
ATOM    840  C   ASP A 109      52.483  21.325  23.889  1.00 14.83           C  
ATOM    841  O   ASP A 109      53.064  20.321  24.320  1.00 14.14           O  
ATOM    842  CB  ASP A 109      54.725  22.494  23.645  1.00 16.55           C  
ATOM    843  CG  ASP A 109      55.144  22.060  22.219  1.00 19.08           C  
ATOM    844  OD1 ASP A 109      54.310  22.099  21.281  1.00 21.03           O  
ATOM    845  OD2 ASP A 109      56.330  21.700  22.039  1.00 21.58           O  
ATOM    846  N   ALA A 110      51.221  21.309  23.456  1.00 15.49           N  
ATOM    847  CA  ALA A 110      50.387  20.111  23.523  1.00 15.16           C  
ATOM    848  C   ALA A 110      50.328  19.310  22.236  1.00 15.32           C  
ATOM    849  O   ALA A 110      50.047  19.852  21.157  1.00 14.92           O  
ATOM    850  CB  ALA A 110      48.999  20.475  23.959  1.00 16.26           C  
ATOM    851  N   HIS A 111      50.582  18.009  22.377  1.00 14.63           N  
ATOM    852  CA  HIS A 111      50.556  17.074  21.262  1.00 16.39           C  
ATOM    853  C   HIS A 111      49.626  15.930  21.668  1.00 16.13           C  
ATOM    854  O   HIS A 111      49.927  15.158  22.588  1.00 16.30           O  
ATOM    855  CB  HIS A 111      51.981  16.570  20.934  1.00 17.12           C  
ATOM    856  CG  HIS A 111      52.925  17.656  20.505  1.00 19.42           C  
ATOM    857  ND1 HIS A 111      53.114  18.005  19.183  1.00 22.23           N  
ATOM    858  CD2 HIS A 111      53.692  18.508  21.229  1.00 19.85           C  
ATOM    859  CE1 HIS A 111      53.948  19.029  19.113  1.00 21.48           C  
ATOM    860  NE2 HIS A 111      54.312  19.354  20.341  1.00 20.49           N  
ATOM    861  N   TYR A 112      48.476  15.860  20.998  1.00 15.60           N  
ATOM    862  CA  TYR A 112      47.445  14.855  21.276  1.00 15.49           C  
ATOM    863  C   TYR A 112      47.384  13.643  20.348  1.00 16.44           C  
ATOM    864  O   TYR A 112      47.761  13.718  19.172  1.00 17.87           O  
ATOM    865  CB  TYR A 112      46.060  15.524  21.268  1.00 15.04           C  
ATOM    866  CG  TYR A 112      45.885  16.601  22.309  1.00 15.40           C  
ATOM    867  CD1 TYR A 112      45.982  17.947  21.972  1.00 15.25           C  
ATOM    868  CD2 TYR A 112      45.650  16.272  23.643  1.00 15.65           C  
ATOM    869  CE1 TYR A 112      45.855  18.938  22.935  1.00 16.66           C  
ATOM    870  CE2 TYR A 112      45.515  17.267  24.622  1.00 18.07           C  
ATOM    871  CZ  TYR A 112      45.620  18.590  24.257  1.00 16.89           C  
ATOM    872  OH  TYR A 112      45.483  19.560  25.201  1.00 18.20           O  
ATOM    873  N   TYR A 113      46.970  12.513  20.908  1.00 15.69           N  
ATOM    874  CA  TYR A 113      46.756  11.307  20.124  1.00 17.42           C  
ATOM    875  C   TYR A 113      45.258  11.416  19.821  1.00 17.23           C  
ATOM    876  O   TYR A 113      44.429  11.407  20.733  1.00 15.37           O  
ATOM    877  CB  TYR A 113      47.093  10.039  20.933  1.00 18.34           C  
ATOM    878  CG  TYR A 113      46.712   8.714  20.276  1.00 20.27           C  
ATOM    879  CD1 TYR A 113      46.790   8.528  18.885  1.00 20.84           C  
ATOM    880  CD2 TYR A 113      46.218   7.660  21.051  1.00 20.25           C  
ATOM    881  CE1 TYR A 113      46.367   7.326  18.294  1.00 21.00           C  
ATOM    882  CE2 TYR A 113      45.807   6.466  20.479  1.00 20.36           C  
ATOM    883  CZ  TYR A 113      45.876   6.299  19.104  1.00 22.75           C  
ATOM    884  OH  TYR A 113      45.428   5.100  18.562  1.00 24.42           O  
ATOM    885  N   GLU A 114      44.939  11.674  18.556  1.00 18.12           N  
ATOM    886  CA  GLU A 114      43.555  11.819  18.132  1.00 20.52           C  
ATOM    887  C   GLU A 114      43.063  10.558  17.483  1.00 22.05           C  
ATOM    888  O   GLU A 114      43.730  10.049  16.575  1.00 23.19           O  
ATOM    889  CB  GLU A 114      43.422  12.934  17.108  1.00 21.99           C  
ATOM    890  CG  GLU A 114      43.708  14.338  17.625  1.00 26.87           C  
ATOM    891  CD  GLU A 114      43.383  15.411  16.582  1.00 29.98           C  
ATOM    892  OE1 GLU A 114      42.358  16.127  16.725  1.00 31.62           O  
ATOM    893  OE2 GLU A 114      44.161  15.531  15.611  1.00 34.22           O  
ATOM    894  N   GLN A 115      41.887  10.085  17.905  1.00 21.98           N  
ATOM    895  CA  GLN A 115      41.282   8.875  17.335  1.00 22.87           C  
ATOM    896  C   GLN A 115      39.775   9.039  17.228  1.00 24.06           C  
ATOM    897  O   GLN A 115      39.222   9.994  17.778  1.00 23.73           O  
ATOM    898  CB  GLN A 115      41.641   7.635  18.164  1.00 21.92           C  
ATOM    899  CG  GLN A 115      41.401   7.738  19.675  1.00 19.42           C  
ATOM    900  CD  GLN A 115      39.943   7.728  20.045  1.00 17.46           C  
ATOM    901  OE1 GLN A 115      39.225   6.787  19.737  1.00 17.68           O  
ATOM    902  NE2 GLN A 115      39.490   8.791  20.699  1.00 15.74           N  
ATOM    903  N   ASN A 116      39.096   8.136  16.520  1.00 25.08           N  
ATOM    904  CA  ASN A 116      37.635   8.279  16.408  1.00 27.88           C  
ATOM    905  C   ASN A 116      36.698   7.133  16.813  1.00 27.03           C  
ATOM    906  O   ASN A 116      35.540   7.123  16.424  1.00 29.13           O  
ATOM    907  CB  ASN A 116      37.233   8.851  15.044  1.00 29.27           C  
ATOM    908  CG  ASN A 116      37.897   8.149  13.904  1.00 31.57           C  
ATOM    909  OD1 ASN A 116      38.089   6.924  13.939  1.00 33.35           O  
ATOM    910  ND2 ASN A 116      38.274   8.915  12.878  1.00 32.31           N  
ATOM    911  N   GLU A 117      37.190   6.199  17.617  1.00 27.03           N  
ATOM    912  CA  GLU A 117      36.379   5.097  18.103  1.00 26.40           C  
ATOM    913  C   GLU A 117      35.667   5.555  19.360  1.00 25.31           C  
ATOM    914  O   GLU A 117      34.557   5.109  19.644  1.00 26.37           O  
ATOM    915  CB  GLU A 117      37.244   3.879  18.428  1.00 29.04           C  
ATOM    916  CG  GLU A 117      37.617   3.034  17.198  1.00 34.18           C  
ATOM    917  CD  GLU A 117      38.823   3.567  16.408  1.00 37.33           C  
ATOM    918  OE1 GLU A 117      39.182   2.935  15.387  1.00 38.32           O  
ATOM    919  OE2 GLU A 117      39.440   4.584  16.817  1.00 39.08           O  
ATOM    920  N   GLN A 118      36.299   6.454  20.110  1.00 21.98           N  
ATOM    921  CA  GLN A 118      35.711   6.967  21.347  1.00 19.78           C  
ATOM    922  C   GLN A 118      35.663   8.505  21.393  1.00 17.96           C  
ATOM    923  O   GLN A 118      36.562   9.180  20.892  1.00 17.34           O  
ATOM    924  CB  GLN A 118      36.512   6.484  22.556  1.00 20.54           C  
ATOM    925  CG  GLN A 118      36.352   5.037  22.927  1.00 24.19           C  
ATOM    926  CD  GLN A 118      35.012   4.737  23.587  1.00 27.96           C  
ATOM    927  OE1 GLN A 118      34.608   5.382  24.570  1.00 31.17           O  
ATOM    928  NE2 GLN A 118      34.316   3.748  23.054  1.00 29.16           N  
ATOM    929  N   PRO A 119      34.608   9.073  21.999  1.00 16.58           N  
ATOM    930  CA  PRO A 119      34.462  10.531  22.115  1.00 15.87           C  
ATOM    931  C   PRO A 119      35.436  11.080  23.174  1.00 14.88           C  
ATOM    932  O   PRO A 119      35.912  10.320  24.022  1.00 14.46           O  
ATOM    933  CB  PRO A 119      33.011  10.683  22.597  1.00 17.47           C  
ATOM    934  CG  PRO A 119      32.789   9.423  23.421  1.00 16.67           C  
ATOM    935  CD  PRO A 119      33.426   8.370  22.538  1.00 16.65           C  
ATOM    936  N   THR A 120      35.726  12.385  23.121  1.00 14.19           N  
ATOM    937  CA  THR A 120      36.620  13.033  24.094  1.00 12.82           C  
ATOM    938  C   THR A 120      36.092  12.804  25.531  1.00 12.16           C  
ATOM    939  O   THR A 120      34.889  12.887  25.770  1.00 13.35           O  
ATOM    940  CB  THR A 120      36.736  14.567  23.798  1.00 13.03           C  
ATOM    941  OG1 THR A 120      37.383  14.769  22.531  1.00 13.01           O  
ATOM    942  CG2 THR A 120      37.530  15.283  24.888  1.00 10.91           C  
ATOM    943  N   GLY A 121      36.976  12.470  26.468  1.00 10.41           N  
ATOM    944  CA  GLY A 121      36.541  12.221  27.842  1.00 11.33           C  
ATOM    945  C   GLY A 121      35.958  13.427  28.567  1.00 10.48           C  
ATOM    946  O   GLY A 121      36.308  14.552  28.241  1.00 10.93           O  
ATOM    947  N   THR A 122      35.065  13.198  29.529  1.00 10.34           N  
ATOM    948  CA  THR A 122      34.433  14.284  30.296  1.00 10.77           C  
ATOM    949  C   THR A 122      34.450  13.916  31.782  1.00 11.46           C  
ATOM    950  O   THR A 122      34.694  12.752  32.133  1.00 11.90           O  
ATOM    951  CB  THR A 122      32.946  14.515  29.849  1.00 12.34           C  
ATOM    952  OG1 THR A 122      32.234  13.274  29.917  1.00 14.10           O  
ATOM    953  CG2 THR A 122      32.864  15.034  28.402  1.00 11.96           C  
ATOM    954  N   CYS A 123      34.244  14.899  32.660  1.00 10.92           N  
ATOM    955  CA  CYS A 123      34.217  14.662  34.112  1.00 10.10           C  
ATOM    956  C   CYS A 123      33.095  15.481  34.744  1.00 10.19           C  
ATOM    957  O   CYS A 123      33.108  16.705  34.646  1.00 11.95           O  
ATOM    958  CB  CYS A 123      35.554  15.065  34.778  1.00 10.00           C  
ATOM    959  SG  CYS A 123      35.691  14.622  36.552  1.00 12.88           S  
ATOM    960  N   ALA A 124      32.116  14.824  35.361  1.00  9.79           N  
ATOM    961  CA  ALA A 124      31.026  15.550  36.011  1.00  9.98           C  
ATOM    962  C   ALA A 124      31.411  16.014  37.422  1.00 10.40           C  
ATOM    963  O   ALA A 124      31.981  15.248  38.197  1.00  9.94           O  
ATOM    964  CB  ALA A 124      29.747  14.670  36.072  1.00 11.24           C  
ATOM    965  N   ALA A 125      31.144  17.289  37.721  1.00 10.79           N  
ATOM    966  CA  ALA A 125      31.391  17.859  39.052  1.00 10.02           C  
ATOM    967  C   ALA A 125      30.002  18.234  39.571  1.00 10.51           C  
ATOM    968  O   ALA A 125      29.366  19.160  39.045  1.00 11.69           O  
ATOM    969  CB  ALA A 125      32.279  19.081  38.965  1.00  9.99           C  
ATOM    970  N   CYS A 126      29.512  17.441  40.527  1.00  9.05           N  
ATOM    971  CA  CYS A 126      28.191  17.589  41.133  1.00  8.47           C  
ATOM    972  C   CYS A 126      28.407  18.317  42.443  1.00  7.77           C  
ATOM    973  O   CYS A 126      28.860  17.728  43.433  1.00  8.40           O  
ATOM    974  CB  CYS A 126      27.564  16.197  41.334  1.00 10.50           C  
ATOM    975  SG  CYS A 126      27.479  15.234  39.768  1.00 12.26           S  
ATOM    976  N   ILE A 127      28.086  19.612  42.425  1.00  8.11           N  
ATOM    977  CA  ILE A 127      28.318  20.501  43.572  1.00  9.00           C  
ATOM    978  C   ILE A 127      27.169  20.653  44.562  1.00  9.43           C  
ATOM    979  O   ILE A 127      26.015  20.766  44.156  1.00  9.78           O  
ATOM    980  CB  ILE A 127      28.674  21.948  43.054  1.00 10.24           C  
ATOM    981  CG1 ILE A 127      29.877  21.891  42.104  1.00 11.81           C  
ATOM    982  CG2 ILE A 127      28.937  22.903  44.224  1.00 10.16           C  
ATOM    983  CD1 ILE A 127      30.039  23.128  41.262  1.00 13.42           C  
ATOM    984  N   THR A 128      27.482  20.607  45.854  1.00  8.08           N  
ATOM    985  CA  THR A 128      26.481  20.860  46.889  1.00  8.60           C  
ATOM    986  C   THR A 128      27.160  21.751  47.927  1.00  9.09           C  
ATOM    987  O   THR A 128      27.975  21.292  48.702  1.00  9.49           O  
ATOM    988  CB  THR A 128      25.852  19.581  47.547  1.00  9.74           C  
ATOM    989  OG1 THR A 128      26.865  18.709  48.085  1.00 11.44           O  
ATOM    990  CG2 THR A 128      24.992  18.811  46.526  1.00  9.80           C  
ATOM    991  N   GLY A 129      26.843  23.047  47.911  1.00  9.05           N  
ATOM    992  CA  GLY A 129      27.465  23.962  48.866  1.00  9.51           C  
ATOM    993  C   GLY A 129      28.967  23.995  48.643  1.00  7.93           C  
ATOM    994  O   GLY A 129      29.407  24.247  47.514  1.00  9.15           O  
ATOM    995  N   ASP A 130      29.734  23.697  49.696  1.00  8.55           N  
ATOM    996  CA  ASP A 130      31.196  23.658  49.612  1.00  8.94           C  
ATOM    997  C   ASP A 130      31.759  22.271  49.236  1.00 10.50           C  
ATOM    998  O   ASP A 130      32.985  22.055  49.253  1.00 11.15           O  
ATOM    999  CB  ASP A 130      31.859  24.193  50.906  1.00 10.28           C  
ATOM   1000  CG  ASP A 130      31.572  23.341  52.165  1.00 12.17           C  
ATOM   1001  OD1 ASP A 130      30.962  22.258  52.071  1.00 11.29           O  
ATOM   1002  OD2 ASP A 130      31.990  23.762  53.287  1.00 14.32           O  
ATOM   1003  N   ASN A 131      30.861  21.346  48.883  1.00  9.05           N  
ATOM   1004  CA  ASN A 131      31.219  19.966  48.512  1.00  9.85           C  
ATOM   1005  C   ASN A 131      31.239  19.756  46.991  1.00  9.66           C  
ATOM   1006  O   ASN A 131      30.490  20.418  46.257  1.00 10.76           O  
ATOM   1007  CB  ASN A 131      30.194  19.002  49.124  1.00  8.33           C  
ATOM   1008  CG  ASN A 131      29.936  19.272  50.586  1.00  9.58           C  
ATOM   1009  OD1 ASN A 131      30.854  19.234  51.402  1.00  8.78           O  
ATOM   1010  ND2 ASN A 131      28.672  19.520  50.937  1.00  9.59           N  
ATOM   1011  N   ARG A 132      32.077  18.823  46.523  1.00  9.61           N  
ATOM   1012  CA  ARG A 132      32.164  18.486  45.086  1.00 10.54           C  
ATOM   1013  C   ARG A 132      32.339  16.959  44.892  1.00 10.44           C  
ATOM   1014  O   ARG A 132      33.282  16.374  45.431  1.00 10.28           O  
ATOM   1015  CB  ARG A 132      33.344  19.208  44.402  1.00 11.60           C  
ATOM   1016  CG  ARG A 132      33.326  20.728  44.607  1.00 17.43           C  
ATOM   1017  CD  ARG A 132      34.492  21.434  43.921  1.00 18.18           C  
ATOM   1018  NE  ARG A 132      34.369  21.404  42.468  1.00 20.73           N  
ATOM   1019  CZ  ARG A 132      33.904  22.411  41.742  1.00 20.58           C  
ATOM   1020  NH1 ARG A 132      33.510  23.544  42.347  1.00 22.23           N  
ATOM   1021  NH2 ARG A 132      33.851  22.290  40.415  1.00 22.18           N  
ATOM   1022  N   SER A 133      31.398  16.324  44.183  1.00  9.17           N  
ATOM   1023  CA  SER A 133      31.462  14.885  43.884  1.00  9.17           C  
ATOM   1024  C   SER A 133      31.807  14.743  42.388  1.00  9.17           C  
ATOM   1025  O   SER A 133      31.024  15.128  41.510  1.00  8.98           O  
ATOM   1026  CB  SER A 133      30.119  14.206  44.189  1.00  8.55           C  
ATOM   1027  OG  SER A 133      30.263  12.801  44.262  1.00  8.30           O  
ATOM   1028  N   LEU A 134      32.979  14.176  42.105  1.00  9.18           N  
ATOM   1029  CA  LEU A 134      33.457  14.036  40.725  1.00  9.26           C  
ATOM   1030  C   LEU A 134      33.341  12.617  40.150  1.00  9.18           C  
ATOM   1031  O   LEU A 134      33.626  11.657  40.857  1.00  9.03           O  
ATOM   1032  CB  LEU A 134      34.920  14.518  40.620  1.00 10.32           C  
ATOM   1033  CG  LEU A 134      35.209  16.010  40.355  1.00 13.25           C  
ATOM   1034  CD1 LEU A 134      34.523  16.906  41.347  1.00 12.85           C  
ATOM   1035  CD2 LEU A 134      36.723  16.233  40.364  1.00 13.28           C  
ATOM   1036  N   ILE A 135      32.897  12.519  38.887  1.00  8.11           N  
ATOM   1037  CA  ILE A 135      32.744  11.236  38.189  1.00  9.33           C  
ATOM   1038  C   ILE A 135      33.384  11.358  36.809  1.00  9.43           C  
ATOM   1039  O   ILE A 135      32.869  12.077  35.937  1.00  9.94           O  
ATOM   1040  CB  ILE A 135      31.261  10.813  38.035  1.00  8.75           C  
ATOM   1041  CG1 ILE A 135      30.555  10.799  39.390  1.00  9.69           C  
ATOM   1042  CG2 ILE A 135      31.186   9.434  37.395  1.00 10.43           C  
ATOM   1043  CD1 ILE A 135      29.838  12.106  39.726  1.00  9.94           C  
ATOM   1044  N   ALA A 136      34.510  10.655  36.607  1.00  9.19           N  
ATOM   1045  CA  ALA A 136      35.245  10.720  35.353  1.00  8.16           C  
ATOM   1046  C   ALA A 136      34.906   9.660  34.311  1.00 10.52           C  
ATOM   1047  O   ALA A 136      35.158   8.466  34.509  1.00 11.46           O  
ATOM   1048  CB  ALA A 136      36.759  10.698  35.636  1.00  8.12           C  
ATOM   1049  N   ASN A 137      34.358  10.103  33.192  1.00 10.47           N  
ATOM   1050  CA  ASN A 137      34.042   9.196  32.084  1.00 11.61           C  
ATOM   1051  C   ASN A 137      35.234   9.369  31.115  1.00 11.66           C  
ATOM   1052  O   ASN A 137      35.205  10.219  30.218  1.00 12.50           O  
ATOM   1053  CB  ASN A 137      32.717   9.609  31.432  1.00 13.76           C  
ATOM   1054  CG  ASN A 137      32.299   8.660  30.332  1.00 17.02           C  
ATOM   1055  OD1 ASN A 137      32.299   9.017  29.159  1.00 19.49           O  
ATOM   1056  ND2 ASN A 137      31.963   7.437  30.708  1.00 18.38           N  
ATOM   1057  N   LEU A 138      36.284   8.572  31.302  1.00 11.05           N  
ATOM   1058  CA  LEU A 138      37.494   8.722  30.495  1.00  9.92           C  
ATOM   1059  C   LEU A 138      37.347   8.643  28.983  1.00 10.84           C  
ATOM   1060  O   LEU A 138      37.946   9.456  28.276  1.00 11.24           O  
ATOM   1061  CB  LEU A 138      38.629   7.820  31.014  1.00  9.21           C  
ATOM   1062  CG  LEU A 138      39.052   7.979  32.494  1.00  9.57           C  
ATOM   1063  CD1 LEU A 138      40.233   7.095  32.814  1.00  9.68           C  
ATOM   1064  CD2 LEU A 138      39.404   9.434  32.814  1.00 10.11           C  
ATOM   1065  N   ALA A 139      36.557   7.690  28.482  1.00 11.46           N  
ATOM   1066  CA  ALA A 139      36.323   7.535  27.026  1.00 11.05           C  
ATOM   1067  C   ALA A 139      37.622   7.620  26.209  1.00 11.55           C  
ATOM   1068  O   ALA A 139      38.529   6.819  26.446  1.00 12.38           O  
ATOM   1069  CB  ALA A 139      35.267   8.544  26.534  1.00  8.97           C  
ATOM   1070  N   ALA A 140      37.766   8.598  25.311  1.00 10.92           N  
ATOM   1071  CA  ALA A 140      39.001   8.695  24.508  1.00 10.91           C  
ATOM   1072  C   ALA A 140      40.292   8.734  25.335  1.00 10.52           C  
ATOM   1073  O   ALA A 140      41.304   8.153  24.934  1.00 10.57           O  
ATOM   1074  CB  ALA A 140      38.943   9.879  23.580  1.00 11.38           C  
ATOM   1075  N   ALA A 141      40.257   9.379  26.503  1.00  9.84           N  
ATOM   1076  CA  ALA A 141      41.455   9.465  27.359  1.00 10.70           C  
ATOM   1077  C   ALA A 141      42.025   8.083  27.717  1.00 11.13           C  
ATOM   1078  O   ALA A 141      43.232   7.927  27.853  1.00 12.82           O  
ATOM   1079  CB  ALA A 141      41.156  10.250  28.637  1.00  9.62           C  
ATOM   1080  N   ASN A 142      41.148   7.090  27.864  1.00 11.07           N  
ATOM   1081  CA  ASN A 142      41.545   5.718  28.220  1.00 12.88           C  
ATOM   1082  C   ASN A 142      42.062   4.921  26.996  1.00 12.94           C  
ATOM   1083  O   ASN A 142      42.380   3.738  27.120  1.00 14.28           O  
ATOM   1084  CB  ASN A 142      40.340   5.026  28.903  1.00 12.50           C  
ATOM   1085  CG  ASN A 142      40.670   3.671  29.512  1.00 15.37           C  
ATOM   1086  OD1 ASN A 142      41.607   3.511  30.281  1.00 14.77           O  
ATOM   1087  ND2 ASN A 142      39.857   2.674  29.169  1.00 18.76           N  
ATOM   1088  N   CYS A 143      42.148   5.572  25.830  1.00 12.42           N  
ATOM   1089  CA  CYS A 143      42.644   4.936  24.589  1.00 13.54           C  
ATOM   1090  C   CYS A 143      44.113   5.269  24.260  1.00 13.60           C  
ATOM   1091  O   CYS A 143      44.625   4.894  23.187  1.00 13.79           O  
ATOM   1092  CB  CYS A 143      41.778   5.329  23.377  1.00 13.56           C  
ATOM   1093  SG  CYS A 143      40.076   4.679  23.426  1.00 19.06           S  
ATOM   1094  N   TYR A 144      44.796   5.962  25.164  1.00 12.60           N  
ATOM   1095  CA  TYR A 144      46.189   6.322  24.917  1.00 13.09           C  
ATOM   1096  C   TYR A 144      47.054   5.070  24.802  1.00 14.35           C  
ATOM   1097  O   TYR A 144      47.011   4.181  25.664  1.00 14.31           O  
ATOM   1098  CB  TYR A 144      46.741   7.237  26.020  1.00 11.45           C  
ATOM   1099  CG  TYR A 144      48.076   7.845  25.637  1.00 12.03           C  
ATOM   1100  CD1 TYR A 144      48.141   9.013  24.861  1.00 11.58           C  
ATOM   1101  CD2 TYR A 144      49.281   7.217  25.985  1.00 10.65           C  
ATOM   1102  CE1 TYR A 144      49.371   9.540  24.436  1.00 10.65           C  
ATOM   1103  CE2 TYR A 144      50.513   7.732  25.568  1.00 10.63           C  
ATOM   1104  CZ  TYR A 144      50.547   8.898  24.790  1.00 10.70           C  
ATOM   1105  OH  TYR A 144      51.762   9.407  24.377  1.00 12.29           O  
ATOM   1106  N   LYS A 145      47.813   4.995  23.710  1.00 15.88           N  
ATOM   1107  CA  LYS A 145      48.709   3.864  23.469  1.00 17.25           C  
ATOM   1108  C   LYS A 145      50.132   4.350  23.222  1.00 15.03           C  
ATOM   1109  O   LYS A 145      50.372   5.095  22.278  1.00 14.25           O  
ATOM   1110  CB  LYS A 145      48.249   3.067  22.250  1.00 19.27           C  
ATOM   1111  CG  LYS A 145      46.908   2.380  22.412  1.00 22.54           C  
ATOM   1112  CD  LYS A 145      46.226   2.302  21.049  1.00 25.64           C  
ATOM   1113  CE  LYS A 145      44.878   1.606  21.140  1.00 28.36           C  
ATOM   1114  NZ  LYS A 145      43.932   2.287  22.071  1.00 27.12           N  
ATOM   1115  N   LYS A 146      51.087   3.881  24.023  1.00 16.19           N  
ATOM   1116  CA  LYS A 146      52.463   4.325  23.811  1.00 16.06           C  
ATOM   1117  C   LYS A 146      53.011   3.997  22.431  1.00 15.51           C  
ATOM   1118  O   LYS A 146      53.682   4.820  21.837  1.00 14.98           O  
ATOM   1119  CB  LYS A 146      53.421   3.866  24.915  1.00 17.68           C  
ATOM   1120  CG  LYS A 146      53.664   2.409  25.024  1.00 20.68           C  
ATOM   1121  CD  LYS A 146      54.651   2.116  26.149  1.00 22.15           C  
ATOM   1122  CE  LYS A 146      56.069   2.395  25.733  1.00 25.23           C  
ATOM   1123  NZ  LYS A 146      56.574   1.418  24.692  1.00 25.02           N  
ATOM   1124  N   GLU A 147      52.672   2.832  21.886  1.00 15.73           N  
ATOM   1125  CA  GLU A 147      53.170   2.447  20.552  1.00 17.67           C  
ATOM   1126  C   GLU A 147      52.669   3.370  19.451  1.00 17.61           C  
ATOM   1127  O   GLU A 147      53.331   3.527  18.419  1.00 19.61           O  
ATOM   1128  CB  GLU A 147      52.770   1.004  20.226  1.00 20.60           C  
ATOM   1129  CG  GLU A 147      53.277  -0.031  21.241  1.00 26.95           C  
ATOM   1130  CD  GLU A 147      52.380  -0.228  22.517  1.00 30.61           C  
ATOM   1131  OE1 GLU A 147      52.711  -1.179  23.287  1.00 31.76           O  
ATOM   1132  OE2 GLU A 147      51.365   0.510  22.748  1.00 28.80           O  
ATOM   1133  N   LYS A 148      51.490   3.958  19.664  1.00 16.27           N  
ATOM   1134  CA  LYS A 148      50.867   4.867  18.704  1.00 15.70           C  
ATOM   1135  C   LYS A 148      51.224   6.363  18.870  1.00 15.58           C  
ATOM   1136  O   LYS A 148      50.993   7.146  17.941  1.00 15.34           O  
ATOM   1137  CB  LYS A 148      49.334   4.731  18.768  1.00 17.37           C  
ATOM   1138  CG  LYS A 148      48.769   3.353  18.482  1.00 19.52           C  
ATOM   1139  CD  LYS A 148      49.005   2.920  17.036  1.00 21.27           C  
ATOM   1140  CE  LYS A 148      48.266   1.594  16.726  1.00 23.84           C  
ATOM   1141  NZ  LYS A 148      48.685   0.933  15.446  1.00 23.34           N  
ATOM   1142  N   HIS A 149      51.809   6.766  20.004  1.00 13.90           N  
ATOM   1143  CA  HIS A 149      52.111   8.189  20.222  1.00 14.40           C  
ATOM   1144  C   HIS A 149      53.451   8.434  20.926  1.00 14.19           C  
ATOM   1145  O   HIS A 149      54.411   8.909  20.305  1.00 14.29           O  
ATOM   1146  CB  HIS A 149      50.940   8.852  21.000  1.00 14.04           C  
ATOM   1147  CG  HIS A 149      50.970  10.360  21.010  1.00 14.00           C  
ATOM   1148  ND1 HIS A 149      51.455  11.087  22.075  1.00 13.68           N  
ATOM   1149  CD2 HIS A 149      50.588  11.273  20.081  1.00 14.09           C  
ATOM   1150  CE1 HIS A 149      51.381  12.380  21.798  1.00 12.96           C  
ATOM   1151  NE2 HIS A 149      50.857  12.519  20.596  1.00 12.54           N  
ATOM   1152  N   LEU A 150      53.527   8.091  22.210  1.00 13.44           N  
ATOM   1153  CA  LEU A 150      54.751   8.279  22.993  1.00 13.39           C  
ATOM   1154  C   LEU A 150      56.008   7.760  22.305  1.00 14.91           C  
ATOM   1155  O   LEU A 150      57.037   8.433  22.349  1.00 15.59           O  
ATOM   1156  CB  LEU A 150      54.630   7.625  24.370  1.00 11.81           C  
ATOM   1157  CG  LEU A 150      55.810   7.813  25.338  1.00 10.96           C  
ATOM   1158  CD1 LEU A 150      55.860   9.277  25.747  1.00 11.37           C  
ATOM   1159  CD2 LEU A 150      55.707   6.909  26.568  1.00 10.04           C  
ATOM   1160  N   ASP A 151      55.905   6.622  21.606  1.00 15.15           N  
ATOM   1161  CA  ASP A 151      57.060   6.010  20.947  1.00 16.07           C  
ATOM   1162  C   ASP A 151      57.461   6.570  19.593  1.00 16.63           C  
ATOM   1163  O   ASP A 151      58.525   6.204  19.093  1.00 18.90           O  
ATOM   1164  CB  ASP A 151      56.881   4.492  20.825  1.00 18.19           C  
ATOM   1165  CG  ASP A 151      56.801   3.786  22.181  1.00 21.53           C  
ATOM   1166  OD1 ASP A 151      57.218   4.377  23.197  1.00 22.51           O  
ATOM   1167  OD2 ASP A 151      56.319   2.627  22.241  1.00 22.05           O  
ATOM   1168  N   LEU A 152      56.635   7.409  18.969  1.00 15.85           N  
ATOM   1169  CA  LEU A 152      57.002   7.975  17.665  1.00 17.61           C  
ATOM   1170  C   LEU A 152      58.230   8.863  17.890  1.00 20.10           C  
ATOM   1171  O   LEU A 152      58.337   9.527  18.926  1.00 18.74           O  
ATOM   1172  CB  LEU A 152      55.851   8.769  17.039  1.00 16.83           C  
ATOM   1173  CG  LEU A 152      54.560   7.983  16.805  1.00 17.69           C  
ATOM   1174  CD1 LEU A 152      53.609   8.769  15.927  1.00 18.83           C  
ATOM   1175  CD2 LEU A 152      54.861   6.636  16.168  1.00 18.45           C  
ATOM   1176  N   GLU A 153      59.171   8.843  16.946  1.00 21.45           N  
ATOM   1177  CA  GLU A 153      60.415   9.613  17.080  1.00 23.97           C  
ATOM   1178  C   GLU A 153      60.293  11.069  17.498  1.00 22.58           C  
ATOM   1179  O   GLU A 153      60.963  11.511  18.440  1.00 21.90           O  
ATOM   1180  CB  GLU A 153      61.223   9.554  15.787  1.00 28.41           C  
ATOM   1181  CG  GLU A 153      62.701   9.352  16.031  1.00 34.50           C  
ATOM   1182  CD  GLU A 153      63.016   7.945  16.547  1.00 38.17           C  
ATOM   1183  OE1 GLU A 153      62.682   7.637  17.731  1.00 40.86           O  
ATOM   1184  OE2 GLU A 153      63.612   7.151  15.765  1.00 40.01           O  
ATOM   1185  N   LYS A 154      59.474  11.800  16.749  1.00 21.78           N  
ATOM   1186  CA  LYS A 154      59.198  13.221  16.949  1.00 21.69           C  
ATOM   1187  C   LYS A 154      58.645  13.548  18.343  1.00 21.04           C  
ATOM   1188  O   LYS A 154      58.955  14.591  18.907  1.00 21.84           O  
ATOM   1189  CB  LYS A 154      58.210  13.686  15.885  1.00 23.52           C  
ATOM   1190  CG  LYS A 154      58.433  15.106  15.411  1.00 26.66           C  
ATOM   1191  CD  LYS A 154      57.880  15.292  13.999  1.00 27.42           C  
ATOM   1192  CE  LYS A 154      58.382  16.593  13.387  1.00 27.61           C  
ATOM   1193  NZ  LYS A 154      59.857  16.561  13.210  1.00 27.96           N  
ATOM   1194  N   ASN A 155      57.805  12.674  18.883  1.00 18.48           N  
ATOM   1195  CA  ASN A 155      57.253  12.880  20.221  1.00 16.51           C  
ATOM   1196  C   ASN A 155      58.254  12.526  21.319  1.00 16.44           C  
ATOM   1197  O   ASN A 155      58.358  13.246  22.318  1.00 16.24           O  
ATOM   1198  CB  ASN A 155      55.985  12.047  20.399  1.00 15.83           C  
ATOM   1199  CG  ASN A 155      54.905  12.440  19.433  1.00 16.15           C  
ATOM   1200  OD1 ASN A 155      54.091  11.606  18.997  1.00 18.72           O  
ATOM   1201  ND2 ASN A 155      54.884  13.716  19.075  1.00 17.18           N  
ATOM   1202  N   TRP A 156      58.969  11.409  21.165  1.00 15.85           N  
ATOM   1203  CA  TRP A 156      59.942  10.998  22.178  1.00 17.42           C  
ATOM   1204  C   TRP A 156      61.055  12.038  22.339  1.00 18.02           C  
ATOM   1205  O   TRP A 156      61.550  12.252  23.455  1.00 17.55           O  
ATOM   1206  CB  TRP A 156      60.534   9.601  21.885  1.00 17.33           C  
ATOM   1207  CG  TRP A 156      61.415   9.087  23.005  1.00 16.89           C  
ATOM   1208  CD1 TRP A 156      62.784   8.910  22.971  1.00 16.64           C  
ATOM   1209  CD2 TRP A 156      61.004   8.759  24.346  1.00 16.15           C  
ATOM   1210  NE1 TRP A 156      63.238   8.506  24.208  1.00 17.75           N  
ATOM   1211  CE2 TRP A 156      62.170   8.408  25.068  1.00 17.26           C  
ATOM   1212  CE3 TRP A 156      59.765   8.738  25.007  1.00 15.21           C  
ATOM   1213  CZ2 TRP A 156      62.131   8.040  26.427  1.00 16.97           C  
ATOM   1214  CZ3 TRP A 156      59.730   8.372  26.361  1.00 15.42           C  
ATOM   1215  CH2 TRP A 156      60.902   8.030  27.053  1.00 16.40           C  
ATOM   1216  N   MET A 157      61.446  12.680  21.233  1.00 20.02           N  
ATOM   1217  CA  MET A 157      62.486  13.725  21.297  1.00 22.15           C  
ATOM   1218  C   MET A 157      62.083  14.848  22.294  1.00 20.42           C  
ATOM   1219  O   MET A 157      62.929  15.411  23.013  1.00 19.49           O  
ATOM   1220  CB  MET A 157      62.754  14.319  19.903  1.00 25.04           C  
ATOM   1221  CG  MET A 157      63.273  13.296  18.902  1.00 30.41           C  
ATOM   1222  SD  MET A 157      63.895  13.955  17.296  1.00 39.37           S  
ATOM   1223  CE  MET A 157      62.392  14.714  16.495  1.00 33.28           C  
ATOM   1224  N   LEU A 158      60.793  15.163  22.335  1.00 18.45           N  
ATOM   1225  CA  LEU A 158      60.305  16.180  23.255  1.00 17.80           C  
ATOM   1226  C   LEU A 158      60.494  15.734  24.695  1.00 15.95           C  
ATOM   1227  O   LEU A 158      60.825  16.546  25.547  1.00 16.41           O  
ATOM   1228  CB  LEU A 158      58.844  16.522  22.968  1.00 17.92           C  
ATOM   1229  CG  LEU A 158      58.614  17.185  21.602  1.00 19.46           C  
ATOM   1230  CD1 LEU A 158      57.137  17.438  21.375  1.00 21.11           C  
ATOM   1231  CD2 LEU A 158      59.403  18.490  21.529  1.00 19.88           C  
ATOM   1232  N   VAL A 159      60.277  14.459  24.981  1.00 14.52           N  
ATOM   1233  CA  VAL A 159      60.488  13.992  26.347  1.00 15.19           C  
ATOM   1234  C   VAL A 159      61.983  14.078  26.726  1.00 16.70           C  
ATOM   1235  O   VAL A 159      62.314  14.370  27.877  1.00 15.69           O  
ATOM   1236  CB  VAL A 159      59.997  12.522  26.550  1.00 14.57           C  
ATOM   1237  CG1 VAL A 159      60.219  12.093  27.988  1.00 14.47           C  
ATOM   1238  CG2 VAL A 159      58.515  12.392  26.184  1.00 14.77           C  
ATOM   1239  N   GLU A 160      62.880  13.817  25.767  1.00 17.41           N  
ATOM   1240  CA  GLU A 160      64.320  13.880  26.047  1.00 19.53           C  
ATOM   1241  C   GLU A 160      64.846  15.298  26.342  1.00 18.43           C  
ATOM   1242  O   GLU A 160      65.903  15.437  26.969  1.00 19.57           O  
ATOM   1243  CB  GLU A 160      65.147  13.186  24.948  1.00 23.25           C  
ATOM   1244  CG  GLU A 160      65.099  11.647  25.030  1.00 28.99           C  
ATOM   1245  CD  GLU A 160      65.843  10.934  23.884  1.00 33.48           C  
ATOM   1246  OE1 GLU A 160      66.502   9.894  24.165  1.00 34.81           O  
ATOM   1247  OE2 GLU A 160      65.744  11.388  22.703  1.00 35.17           O  
ATOM   1248  N   LYS A 161      64.102  16.331  25.927  1.00 17.18           N  
ATOM   1249  CA  LYS A 161      64.450  17.730  26.207  1.00 16.33           C  
ATOM   1250  C   LYS A 161      64.115  18.121  27.660  1.00 16.10           C  
ATOM   1251  O   LYS A 161      64.653  19.094  28.181  1.00 15.61           O  
ATOM   1252  CB  LYS A 161      63.690  18.684  25.295  1.00 16.19           C  
ATOM   1253  CG  LYS A 161      64.044  18.561  23.825  1.00 18.26           C  
ATOM   1254  CD  LYS A 161      63.225  19.518  22.981  1.00 19.21           C  
ATOM   1255  CE  LYS A 161      63.660  20.964  23.190  1.00 21.36           C  
ATOM   1256  NZ  LYS A 161      62.837  21.897  22.379  1.00 21.42           N  
ATOM   1257  N   ALA A 162      63.252  17.357  28.325  1.00 14.25           N  
ATOM   1258  CA  ALA A 162      62.864  17.699  29.683  1.00 13.48           C  
ATOM   1259  C   ALA A 162      63.877  17.456  30.788  1.00 14.16           C  
ATOM   1260  O   ALA A 162      64.663  16.516  30.723  1.00 15.81           O  
ATOM   1261  CB  ALA A 162      61.554  17.000  30.024  1.00 14.35           C  
ATOM   1262  N   ARG A 163      63.844  18.299  31.816  1.00 14.42           N  
ATOM   1263  CA  ARG A 163      64.705  18.145  32.987  1.00 15.87           C  
ATOM   1264  C   ARG A 163      63.825  17.720  34.172  1.00 14.00           C  
ATOM   1265  O   ARG A 163      64.320  17.211  35.179  1.00 14.42           O  
ATOM   1266  CB  ARG A 163      65.421  19.451  33.339  1.00 20.68           C  
ATOM   1267  CG  ARG A 163      66.945  19.452  33.122  1.00 27.37           C  
ATOM   1268  CD  ARG A 163      67.353  19.503  31.633  1.00 30.92           C  
ATOM   1269  NE  ARG A 163      68.087  18.320  31.157  1.00 33.89           N  
ATOM   1270  CZ  ARG A 163      67.897  17.763  29.955  1.00 34.79           C  
ATOM   1271  NH1 ARG A 163      67.850  18.532  28.867  1.00 36.19           N  
ATOM   1272  NH2 ARG A 163      67.626  16.467  29.848  1.00 32.32           N  
ATOM   1273  N   VAL A 164      62.527  18.008  34.075  1.00 13.57           N  
ATOM   1274  CA  VAL A 164      61.564  17.618  35.120  1.00 12.37           C  
ATOM   1275  C   VAL A 164      60.345  16.994  34.423  1.00 11.21           C  
ATOM   1276  O   VAL A 164      59.862  17.522  33.418  1.00 10.17           O  
ATOM   1277  CB  VAL A 164      61.073  18.836  35.977  1.00 12.65           C  
ATOM   1278  CG1 VAL A 164      60.003  18.390  36.969  1.00 12.44           C  
ATOM   1279  CG2 VAL A 164      62.210  19.440  36.767  1.00 13.30           C  
ATOM   1280  N   CYS A 165      59.894  15.839  34.918  1.00 11.41           N  
ATOM   1281  CA  CYS A 165      58.699  15.169  34.365  1.00 12.36           C  
ATOM   1282  C   CYS A 165      57.665  15.036  35.492  1.00 11.92           C  
ATOM   1283  O   CYS A 165      58.033  14.824  36.664  1.00 12.33           O  
ATOM   1284  CB  CYS A 165      59.043  13.763  33.829  1.00 11.75           C  
ATOM   1285  SG  CYS A 165      60.067  13.726  32.327  1.00 15.63           S  
ATOM   1286  N   TYR A 166      56.389  15.190  35.140  1.00 10.14           N  
ATOM   1287  CA  TYR A 166      55.278  15.063  36.100  1.00  9.24           C  
ATOM   1288  C   TYR A 166      54.069  14.338  35.484  1.00  8.62           C  
ATOM   1289  O   TYR A 166      53.623  14.682  34.374  1.00  7.66           O  
ATOM   1290  CB  TYR A 166      54.804  16.437  36.587  1.00  9.19           C  
ATOM   1291  CG  TYR A 166      53.537  16.361  37.423  1.00  6.81           C  
ATOM   1292  CD1 TYR A 166      53.563  15.818  38.713  1.00  7.28           C  
ATOM   1293  CD2 TYR A 166      52.316  16.792  36.916  1.00  7.23           C  
ATOM   1294  CE1 TYR A 166      52.405  15.700  39.475  1.00  7.34           C  
ATOM   1295  CE2 TYR A 166      51.129  16.680  37.679  1.00  7.67           C  
ATOM   1296  CZ  TYR A 166      51.189  16.131  38.953  1.00  6.66           C  
ATOM   1297  OH  TYR A 166      50.047  16.009  39.710  1.00  8.93           O  
ATOM   1298  N   ILE A 167      53.579  13.311  36.197  1.00  8.73           N  
ATOM   1299  CA  ILE A 167      52.395  12.545  35.750  1.00  8.47           C  
ATOM   1300  C   ILE A 167      51.502  12.262  36.957  1.00  7.83           C  
ATOM   1301  O   ILE A 167      51.982  11.783  37.995  1.00  7.35           O  
ATOM   1302  CB  ILE A 167      52.754  11.161  35.100  1.00  8.48           C  
ATOM   1303  CG1 ILE A 167      53.622  11.358  33.846  1.00  8.21           C  
ATOM   1304  CG2 ILE A 167      51.450  10.405  34.745  1.00  7.83           C  
ATOM   1305  CD1 ILE A 167      54.201  10.051  33.237  1.00  9.64           C  
ATOM   1306  N   ALA A 168      50.214  12.592  36.839  1.00  6.74           N  
ATOM   1307  CA  ALA A 168      49.280  12.303  37.925  1.00  7.14           C  
ATOM   1308  C   ALA A 168      49.041  10.787  37.999  1.00  7.08           C  
ATOM   1309  O   ALA A 168      48.992  10.104  36.962  1.00  7.93           O  
ATOM   1310  CB  ALA A 168      47.937  13.011  37.697  1.00  7.42           C  
ATOM   1311  N   GLY A 169      48.911  10.279  39.231  1.00  7.09           N  
ATOM   1312  CA  GLY A 169      48.622   8.866  39.462  1.00  6.72           C  
ATOM   1313  C   GLY A 169      47.396   8.391  38.690  1.00  7.75           C  
ATOM   1314  O   GLY A 169      47.282   7.190  38.389  1.00  8.61           O  
ATOM   1315  N   PHE A 170      46.476   9.314  38.367  1.00  7.46           N  
ATOM   1316  CA  PHE A 170      45.286   8.978  37.575  1.00  7.01           C  
ATOM   1317  C   PHE A 170      45.641   8.229  36.281  1.00  6.61           C  
ATOM   1318  O   PHE A 170      44.898   7.354  35.853  1.00  7.79           O  
ATOM   1319  CB  PHE A 170      44.527  10.241  37.166  1.00  5.75           C  
ATOM   1320  CG  PHE A 170      43.715  10.899  38.282  1.00  6.32           C  
ATOM   1321  CD1 PHE A 170      43.860  12.269  38.552  1.00  6.84           C  
ATOM   1322  CD2 PHE A 170      42.722  10.187  38.987  1.00  5.38           C  
ATOM   1323  CE1 PHE A 170      43.023  12.918  39.493  1.00  6.53           C  
ATOM   1324  CE2 PHE A 170      41.885  10.834  39.925  1.00  5.49           C  
ATOM   1325  CZ  PHE A 170      42.036  12.205  40.174  1.00  5.52           C  
ATOM   1326  N   PHE A 171      46.748   8.599  35.632  1.00  7.88           N  
ATOM   1327  CA  PHE A 171      47.144   7.960  34.360  1.00  6.75           C  
ATOM   1328  C   PHE A 171      47.526   6.466  34.476  1.00  8.49           C  
ATOM   1329  O   PHE A 171      47.585   5.764  33.469  1.00  8.47           O  
ATOM   1330  CB  PHE A 171      48.270   8.744  33.691  1.00  7.06           C  
ATOM   1331  CG  PHE A 171      48.392   8.492  32.206  1.00  6.91           C  
ATOM   1332  CD1 PHE A 171      47.288   8.637  31.365  1.00  7.83           C  
ATOM   1333  CD2 PHE A 171      49.625   8.214  31.632  1.00  8.01           C  
ATOM   1334  CE1 PHE A 171      47.409   8.524  29.979  1.00  8.66           C  
ATOM   1335  CE2 PHE A 171      49.756   8.101  30.242  1.00  7.69           C  
ATOM   1336  CZ  PHE A 171      48.647   8.259  29.417  1.00  8.57           C  
ATOM   1337  N   LEU A 172      47.763   5.987  35.699  1.00  7.99           N  
ATOM   1338  CA  LEU A 172      48.085   4.570  35.951  1.00  8.49           C  
ATOM   1339  C   LEU A 172      46.920   3.619  35.576  1.00 10.27           C  
ATOM   1340  O   LEU A 172      47.145   2.422  35.374  1.00 10.68           O  
ATOM   1341  CB  LEU A 172      48.466   4.349  37.425  1.00  8.79           C  
ATOM   1342  CG  LEU A 172      49.780   4.961  37.914  1.00  7.55           C  
ATOM   1343  CD1 LEU A 172      49.889   4.895  39.445  1.00  8.75           C  
ATOM   1344  CD2 LEU A 172      50.982   4.274  37.223  1.00 10.25           C  
ATOM   1345  N   THR A 173      45.689   4.136  35.493  1.00  8.86           N  
ATOM   1346  CA  THR A 173      44.538   3.297  35.121  1.00  9.33           C  
ATOM   1347  C   THR A 173      44.451   3.153  33.583  1.00  9.87           C  
ATOM   1348  O   THR A 173      43.685   2.321  33.079  1.00 10.94           O  
ATOM   1349  CB  THR A 173      43.163   3.888  35.636  1.00  9.48           C  
ATOM   1350  OG1 THR A 173      42.679   4.910  34.737  1.00  8.65           O  
ATOM   1351  CG2 THR A 173      43.292   4.462  37.061  1.00  9.32           C  
ATOM   1352  N   VAL A 174      45.251   3.943  32.853  1.00  8.53           N  
ATOM   1353  CA  VAL A 174      45.234   3.954  31.390  1.00  9.30           C  
ATOM   1354  C   VAL A 174      46.468   3.357  30.729  1.00 10.29           C  
ATOM   1355  O   VAL A 174      46.350   2.469  29.866  1.00 11.54           O  
ATOM   1356  CB  VAL A 174      45.061   5.401  30.857  1.00  9.99           C  
ATOM   1357  CG1 VAL A 174      45.151   5.454  29.305  1.00  9.17           C  
ATOM   1358  CG2 VAL A 174      43.738   5.996  31.378  1.00 10.15           C  
ATOM   1359  N   SER A 175      47.640   3.883  31.065  1.00  9.92           N  
ATOM   1360  CA  SER A 175      48.857   3.372  30.464  1.00 10.88           C  
ATOM   1361  C   SER A 175      50.046   3.267  31.411  1.00 10.78           C  
ATOM   1362  O   SER A 175      50.979   4.070  31.332  1.00 10.51           O  
ATOM   1363  CB  SER A 175      49.227   4.192  29.227  1.00 12.35           C  
ATOM   1364  OG  SER A 175      50.365   3.648  28.558  1.00 13.88           O  
ATOM   1365  N   PRO A 176      50.024   2.279  32.339  1.00 11.47           N  
ATOM   1366  CA  PRO A 176      51.151   2.109  33.271  1.00 11.49           C  
ATOM   1367  C   PRO A 176      52.457   1.876  32.495  1.00 12.42           C  
ATOM   1368  O   PRO A 176      53.522   2.277  32.955  1.00 12.67           O  
ATOM   1369  CB  PRO A 176      50.740   0.900  34.143  1.00 11.40           C  
ATOM   1370  CG  PRO A 176      49.693   0.201  33.341  1.00 12.10           C  
ATOM   1371  CD  PRO A 176      48.947   1.312  32.626  1.00 11.14           C  
ATOM   1372  N   GLU A 177      52.374   1.303  31.292  1.00 12.04           N  
ATOM   1373  CA  GLU A 177      53.585   1.094  30.472  1.00 13.93           C  
ATOM   1374  C   GLU A 177      54.202   2.458  30.042  1.00 13.26           C  
ATOM   1375  O   GLU A 177      55.425   2.597  29.994  1.00 13.42           O  
ATOM   1376  CB  GLU A 177      53.299   0.220  29.243  1.00 16.65           C  
ATOM   1377  CG  GLU A 177      52.627  -1.142  29.550  1.00 23.08           C  
ATOM   1378  CD  GLU A 177      51.100  -1.050  29.892  1.00 27.12           C  
ATOM   1379  OE1 GLU A 177      50.579  -2.078  30.413  1.00 31.30           O  
ATOM   1380  OE2 GLU A 177      50.425   0.009  29.641  1.00 24.35           O  
ATOM   1381  N   SER A 178      53.367   3.450  29.732  1.00 10.57           N  
ATOM   1382  CA  SER A 178      53.876   4.769  29.366  1.00 10.29           C  
ATOM   1383  C   SER A 178      54.540   5.426  30.594  1.00 11.39           C  
ATOM   1384  O   SER A 178      55.636   6.013  30.490  1.00 11.41           O  
ATOM   1385  CB  SER A 178      52.749   5.673  28.870  1.00  9.97           C  
ATOM   1386  OG  SER A 178      52.277   5.301  27.575  1.00 10.89           O  
ATOM   1387  N   VAL A 179      53.865   5.364  31.745  1.00 10.78           N  
ATOM   1388  CA  VAL A 179      54.411   5.956  32.967  1.00 11.33           C  
ATOM   1389  C   VAL A 179      55.768   5.348  33.266  1.00 12.92           C  
ATOM   1390  O   VAL A 179      56.708   6.079  33.601  1.00 13.09           O  
ATOM   1391  CB  VAL A 179      53.490   5.743  34.193  1.00 12.23           C  
ATOM   1392  CG1 VAL A 179      54.124   6.393  35.471  1.00 12.53           C  
ATOM   1393  CG2 VAL A 179      52.081   6.320  33.918  1.00 10.21           C  
ATOM   1394  N   LEU A 180      55.884   4.018  33.133  1.00 12.84           N  
ATOM   1395  CA  LEU A 180      57.166   3.341  33.397  1.00 14.14           C  
ATOM   1396  C   LEU A 180      58.258   3.704  32.403  1.00 13.23           C  
ATOM   1397  O   LEU A 180      59.407   3.853  32.799  1.00 15.46           O  
ATOM   1398  CB  LEU A 180      57.012   1.814  33.481  1.00 15.98           C  
ATOM   1399  CG  LEU A 180      56.571   1.280  34.842  1.00 17.26           C  
ATOM   1400  CD1 LEU A 180      56.055  -0.136  34.680  1.00 20.07           C  
ATOM   1401  CD2 LEU A 180      57.720   1.340  35.833  1.00 16.91           C  
ATOM   1402  N   LYS A 181      57.920   3.881  31.133  1.00 11.96           N  
ATOM   1403  CA  LYS A 181      58.951   4.240  30.155  1.00 13.53           C  
ATOM   1404  C   LYS A 181      59.566   5.610  30.485  1.00 13.72           C  
ATOM   1405  O   LYS A 181      60.796   5.773  30.477  1.00 14.57           O  
ATOM   1406  CB  LYS A 181      58.382   4.258  28.734  1.00 14.40           C  
ATOM   1407  CG  LYS A 181      59.472   4.409  27.673  1.00 16.90           C  
ATOM   1408  CD  LYS A 181      58.891   4.563  26.290  1.00 17.82           C  
ATOM   1409  CE  LYS A 181      60.016   4.719  25.301  1.00 21.08           C  
ATOM   1410  NZ  LYS A 181      59.511   5.104  23.969  1.00 24.56           N  
ATOM   1411  N   VAL A 182      58.702   6.576  30.806  1.00 12.06           N  
ATOM   1412  CA  VAL A 182      59.121   7.940  31.165  1.00 11.29           C  
ATOM   1413  C   VAL A 182      59.907   7.939  32.481  1.00 11.23           C  
ATOM   1414  O   VAL A 182      60.946   8.591  32.570  1.00 11.42           O  
ATOM   1415  CB  VAL A 182      57.882   8.886  31.286  1.00 10.73           C  
ATOM   1416  CG1 VAL A 182      58.280  10.258  31.817  1.00 12.67           C  
ATOM   1417  CG2 VAL A 182      57.199   9.041  29.923  1.00 11.34           C  
ATOM   1418  N   ALA A 183      59.430   7.208  33.491  1.00 10.98           N  
ATOM   1419  CA  ALA A 183      60.115   7.133  34.793  1.00 12.18           C  
ATOM   1420  C   ALA A 183      61.503   6.476  34.708  1.00 14.34           C  
ATOM   1421  O   ALA A 183      62.446   6.921  35.366  1.00 13.65           O  
ATOM   1422  CB  ALA A 183      59.257   6.412  35.827  1.00 12.10           C  
ATOM   1423  N   HIS A 184      61.633   5.425  33.899  1.00 15.87           N  
ATOM   1424  CA  HIS A 184      62.930   4.751  33.750  1.00 17.82           C  
ATOM   1425  C   HIS A 184      63.940   5.682  33.058  1.00 17.60           C  
ATOM   1426  O   HIS A 184      65.086   5.760  33.481  1.00 17.40           O  
ATOM   1427  CB  HIS A 184      62.771   3.435  32.963  1.00 20.25           C  
ATOM   1428  CG  HIS A 184      64.066   2.715  32.709  1.00 24.80           C  
ATOM   1429  ND1 HIS A 184      64.759   2.046  33.701  1.00 27.43           N  
ATOM   1430  CD2 HIS A 184      64.801   2.573  31.575  1.00 26.49           C  
ATOM   1431  CE1 HIS A 184      65.866   1.527  33.189  1.00 28.39           C  
ATOM   1432  NE2 HIS A 184      65.916   1.834  31.903  1.00 27.41           N  
ATOM   1433  N   HIS A 185      63.494   6.409  32.028  1.00 16.95           N  
ATOM   1434  CA  HIS A 185      64.342   7.350  31.282  1.00 18.17           C  
ATOM   1435  C   HIS A 185      64.927   8.443  32.171  1.00 18.94           C  
ATOM   1436  O   HIS A 185      66.069   8.862  31.975  1.00 19.16           O  
ATOM   1437  CB  HIS A 185      63.552   8.004  30.170  1.00 19.33           C  
ATOM   1438  CG  HIS A 185      64.362   8.926  29.326  1.00 24.00           C  
ATOM   1439  ND1 HIS A 185      65.197   8.476  28.324  1.00 27.19           N  
ATOM   1440  CD2 HIS A 185      64.443  10.276  29.306  1.00 26.89           C  
ATOM   1441  CE1 HIS A 185      65.751   9.511  27.718  1.00 27.67           C  
ATOM   1442  NE2 HIS A 185      65.310  10.616  28.294  1.00 28.26           N  
ATOM   1443  N   ALA A 186      64.110   8.939  33.102  1.00 17.19           N  
ATOM   1444  CA  ALA A 186      64.516   9.966  34.049  1.00 15.27           C  
ATOM   1445  C   ALA A 186      65.575   9.375  34.992  1.00 17.05           C  
ATOM   1446  O   ALA A 186      66.598   9.996  35.261  1.00 16.34           O  
ATOM   1447  CB  ALA A 186      63.305  10.444  34.834  1.00 15.05           C  
ATOM   1448  N   SER A 187      65.334   8.155  35.462  1.00 16.64           N  
ATOM   1449  CA  SER A 187      66.251   7.470  36.361  1.00 18.96           C  
ATOM   1450  C   SER A 187      67.608   7.185  35.701  1.00 19.70           C  
ATOM   1451  O   SER A 187      68.658   7.345  36.329  1.00 20.91           O  
ATOM   1452  CB  SER A 187      65.634   6.158  36.819  1.00 19.07           C  
ATOM   1453  OG  SER A 187      66.384   5.626  37.898  1.00 23.32           O  
ATOM   1454  N   GLU A 188      67.579   6.773  34.440  1.00 20.32           N  
ATOM   1455  CA  GLU A 188      68.798   6.480  33.709  1.00 22.32           C  
ATOM   1456  C   GLU A 188      69.619   7.723  33.413  1.00 22.39           C  
ATOM   1457  O   GLU A 188      70.846   7.669  33.394  1.00 23.59           O  
ATOM   1458  CB  GLU A 188      68.489   5.780  32.385  1.00 24.50           C  
ATOM   1459  CG  GLU A 188      68.278   4.298  32.528  1.00 31.92           C  
ATOM   1460  CD  GLU A 188      69.342   3.650  33.426  1.00 36.97           C  
ATOM   1461  OE1 GLU A 188      70.483   3.432  32.936  1.00 40.48           O  
ATOM   1462  OE2 GLU A 188      69.042   3.369  34.621  1.00 39.30           O  
ATOM   1463  N   ASN A 189      68.940   8.833  33.170  1.00 21.86           N  
ATOM   1464  CA  ASN A 189      69.602  10.082  32.839  1.00 22.45           C  
ATOM   1465  C   ASN A 189      69.663  11.097  33.996  1.00 21.98           C  
ATOM   1466  O   ASN A 189      69.873  12.280  33.769  1.00 23.09           O  
ATOM   1467  CB  ASN A 189      68.932  10.689  31.604  1.00 22.34           C  
ATOM   1468  CG  ASN A 189      69.122   9.839  30.350  1.00 24.40           C  
ATOM   1469  OD1 ASN A 189      70.002  10.107  29.548  1.00 25.58           O  
ATOM   1470  ND2 ASN A 189      68.281   8.826  30.169  1.00 23.96           N  
ATOM   1471  N   ASN A 190      69.549  10.605  35.225  1.00 22.30           N  
ATOM   1472  CA  ASN A 190      69.568  11.427  36.447  1.00 24.12           C  
ATOM   1473  C   ASN A 190      68.743  12.719  36.375  1.00 23.97           C  
ATOM   1474  O   ASN A 190      69.199  13.802  36.783  1.00 23.51           O  
ATOM   1475  CB  ASN A 190      71.008  11.727  36.934  1.00 26.86           C  
ATOM   1476  CG  ASN A 190      71.048  12.227  38.383  1.00 28.52           C  
ATOM   1477  OD1 ASN A 190      70.221  11.835  39.225  1.00 29.96           O  
ATOM   1478  ND2 ASN A 190      72.006  13.102  38.676  1.00 28.66           N  
ATOM   1479  N   ARG A 191      67.530  12.597  35.827  1.00 22.50           N  
ATOM   1480  CA  ARG A 191      66.598  13.719  35.722  1.00 20.51           C  
ATOM   1481  C   ARG A 191      65.516  13.522  36.798  1.00 19.41           C  
ATOM   1482  O   ARG A 191      65.448  12.469  37.441  1.00 19.65           O  
ATOM   1483  CB  ARG A 191      66.035  13.797  34.308  1.00 20.16           C  
ATOM   1484  CG  ARG A 191      67.183  14.053  33.336  1.00 22.87           C  
ATOM   1485  CD  ARG A 191      66.818  14.164  31.880  1.00 24.49           C  
ATOM   1486  NE  ARG A 191      68.049  14.228  31.080  1.00 25.73           N  
ATOM   1487  CZ  ARG A 191      68.159  13.855  29.801  1.00 28.50           C  
ATOM   1488  NH1 ARG A 191      67.113  13.383  29.118  1.00 27.98           N  
ATOM   1489  NH2 ARG A 191      69.343  13.924  29.200  1.00 29.96           N  
ATOM   1490  N   ILE A 192      64.718  14.559  37.046  1.00 18.17           N  
ATOM   1491  CA  ILE A 192      63.680  14.492  38.079  1.00 16.03           C  
ATOM   1492  C   ILE A 192      62.324  13.931  37.600  1.00 14.57           C  
ATOM   1493  O   ILE A 192      61.778  14.390  36.596  1.00 14.77           O  
ATOM   1494  CB  ILE A 192      63.495  15.895  38.736  1.00 15.96           C  
ATOM   1495  CG1 ILE A 192      64.811  16.314  39.388  1.00 17.30           C  
ATOM   1496  CG2 ILE A 192      62.401  15.870  39.795  1.00 17.16           C  
ATOM   1497  CD1 ILE A 192      64.753  17.636  40.104  1.00 18.91           C  
ATOM   1498  N   PHE A 193      61.829  12.899  38.290  1.00 12.95           N  
ATOM   1499  CA  PHE A 193      60.524  12.306  37.978  1.00 10.80           C  
ATOM   1500  C   PHE A 193      59.612  12.521  39.198  1.00  9.68           C  
ATOM   1501  O   PHE A 193      59.966  12.157  40.324  1.00  9.15           O  
ATOM   1502  CB  PHE A 193      60.632  10.797  37.673  1.00 11.10           C  
ATOM   1503  CG  PHE A 193      59.301  10.173  37.326  1.00 12.73           C  
ATOM   1504  CD1 PHE A 193      58.758  10.337  36.041  1.00 12.75           C  
ATOM   1505  CD2 PHE A 193      58.534   9.533  38.315  1.00 13.25           C  
ATOM   1506  CE1 PHE A 193      57.459   9.885  35.733  1.00 13.20           C  
ATOM   1507  CE2 PHE A 193      57.228   9.073  38.028  1.00 13.75           C  
ATOM   1508  CZ  PHE A 193      56.690   9.254  36.729  1.00 13.75           C  
ATOM   1509  N   THR A 194      58.429  13.089  38.952  1.00  9.93           N  
ATOM   1510  CA  THR A 194      57.450  13.400  40.014  1.00  8.68           C  
ATOM   1511  C   THR A 194      56.059  12.786  39.698  1.00  7.71           C  
ATOM   1512  O   THR A 194      55.678  12.637  38.526  1.00  7.18           O  
ATOM   1513  CB  THR A 194      57.337  14.964  40.214  1.00 10.09           C  
ATOM   1514  OG1 THR A 194      56.865  15.584  39.001  1.00 10.78           O  
ATOM   1515  CG2 THR A 194      58.701  15.555  40.557  1.00 10.74           C  
ATOM   1516  N   LEU A 195      55.313  12.448  40.756  1.00  7.03           N  
ATOM   1517  CA  LEU A 195      54.008  11.787  40.601  1.00  7.81           C  
ATOM   1518  C   LEU A 195      53.018  12.218  41.701  1.00  7.92           C  
ATOM   1519  O   LEU A 195      53.421  12.586  42.827  1.00  7.60           O  
ATOM   1520  CB  LEU A 195      54.228  10.252  40.679  1.00  8.84           C  
ATOM   1521  CG  LEU A 195      53.088   9.228  40.461  1.00  9.47           C  
ATOM   1522  CD1 LEU A 195      52.976   8.839  38.990  1.00  9.73           C  
ATOM   1523  CD2 LEU A 195      53.377   7.982  41.293  1.00 13.11           C  
ATOM   1524  N   ASN A 196      51.726  12.132  41.380  1.00  6.90           N  
ATOM   1525  CA  ASN A 196      50.662  12.455  42.348  1.00  7.21           C  
ATOM   1526  C   ASN A 196      49.886  11.183  42.778  1.00  6.62           C  
ATOM   1527  O   ASN A 196      49.629  10.318  41.931  1.00  7.87           O  
ATOM   1528  CB  ASN A 196      49.655  13.433  41.707  1.00  6.76           C  
ATOM   1529  CG  ASN A 196      48.982  14.333  42.731  1.00  8.01           C  
ATOM   1530  OD1 ASN A 196      48.266  13.869  43.644  1.00  8.39           O  
ATOM   1531  ND2 ASN A 196      49.212  15.648  42.593  1.00  8.56           N  
ATOM   1532  N   LEU A 197      49.534  11.068  44.069  1.00  5.62           N  
ATOM   1533  CA  LEU A 197      48.704   9.935  44.564  1.00  7.36           C  
ATOM   1534  C   LEU A 197      47.273  10.045  43.924  1.00  7.93           C  
ATOM   1535  O   LEU A 197      46.563   9.038  43.787  1.00  7.58           O  
ATOM   1536  CB  LEU A 197      48.625   9.920  46.100  1.00  6.79           C  
ATOM   1537  CG  LEU A 197      49.871   9.452  46.862  1.00  6.09           C  
ATOM   1538  CD1 LEU A 197      49.653   9.555  48.355  1.00  7.57           C  
ATOM   1539  CD2 LEU A 197      50.223   8.017  46.464  1.00  8.12           C  
ATOM   1540  N   SER A 198      46.876  11.290  43.592  1.00  7.88           N  
ATOM   1541  CA  SER A 198      45.628  11.640  42.874  1.00  6.92           C  
ATOM   1542  C   SER A 198      44.266  11.457  43.528  1.00  7.94           C  
ATOM   1543  O   SER A 198      43.440  12.366  43.483  1.00  7.07           O  
ATOM   1544  CB  SER A 198      45.596  10.984  41.485  1.00  6.96           C  
ATOM   1545  OG  SER A 198      46.506  11.606  40.578  1.00  8.46           O  
ATOM   1546  N   ALA A 199      44.003  10.266  44.059  1.00  8.56           N  
ATOM   1547  CA  ALA A 199      42.704   9.959  44.694  1.00  8.01           C  
ATOM   1548  C   ALA A 199      42.822   8.639  45.467  1.00  8.50           C  
ATOM   1549  O   ALA A 199      43.651   7.783  45.127  1.00  8.20           O  
ATOM   1550  CB  ALA A 199      41.594   9.816  43.608  1.00  6.61           C  
ATOM   1551  N   PRO A 200      41.983   8.447  46.508  1.00 10.20           N  
ATOM   1552  CA  PRO A 200      42.062   7.178  47.268  1.00 10.32           C  
ATOM   1553  C   PRO A 200      41.979   5.889  46.391  1.00  9.69           C  
ATOM   1554  O   PRO A 200      42.698   4.909  46.666  1.00  9.78           O  
ATOM   1555  CB  PRO A 200      40.870   7.290  48.238  1.00 10.93           C  
ATOM   1556  CG  PRO A 200      40.789   8.806  48.508  1.00 10.52           C  
ATOM   1557  CD  PRO A 200      41.027   9.402  47.122  1.00 10.36           C  
ATOM   1558  N   PHE A 201      41.202   5.906  45.302  1.00  9.24           N  
ATOM   1559  CA  PHE A 201      41.070   4.690  44.477  1.00  9.53           C  
ATOM   1560  C   PHE A 201      42.359   4.199  43.818  1.00 10.21           C  
ATOM   1561  O   PHE A 201      42.483   2.994  43.507  1.00 11.25           O  
ATOM   1562  CB  PHE A 201      39.884   4.748  43.480  1.00  9.99           C  
ATOM   1563  CG  PHE A 201      40.079   5.655  42.270  1.00 10.66           C  
ATOM   1564  CD1 PHE A 201      40.784   5.213  41.146  1.00 10.96           C  
ATOM   1565  CD2 PHE A 201      39.467   6.935  42.217  1.00 10.82           C  
ATOM   1566  CE1 PHE A 201      40.876   6.023  39.990  1.00 10.58           C  
ATOM   1567  CE2 PHE A 201      39.551   7.744  41.070  1.00  7.59           C  
ATOM   1568  CZ  PHE A 201      40.252   7.293  39.960  1.00  9.51           C  
ATOM   1569  N   ILE A 202      43.334   5.104  43.644  1.00  9.68           N  
ATOM   1570  CA  ILE A 202      44.627   4.752  43.029  1.00  8.91           C  
ATOM   1571  C   ILE A 202      45.439   3.881  43.994  1.00  9.78           C  
ATOM   1572  O   ILE A 202      46.031   2.887  43.567  1.00 11.32           O  
ATOM   1573  CB  ILE A 202      45.433   6.022  42.589  1.00  9.32           C  
ATOM   1574  CG1 ILE A 202      44.710   6.731  41.433  1.00  8.64           C  
ATOM   1575  CG2 ILE A 202      46.868   5.638  42.169  1.00 10.15           C  
ATOM   1576  CD1 ILE A 202      44.616   5.913  40.142  1.00 10.19           C  
ATOM   1577  N   SER A 203      45.420   4.226  45.289  1.00 10.01           N  
ATOM   1578  CA  SER A 203      46.111   3.449  46.338  1.00 11.45           C  
ATOM   1579  C   SER A 203      45.357   2.153  46.749  1.00 13.36           C  
ATOM   1580  O   SER A 203      45.899   1.322  47.492  1.00 15.92           O  
ATOM   1581  CB  SER A 203      46.282   4.294  47.605  1.00 11.10           C  
ATOM   1582  OG  SER A 203      47.320   5.232  47.445  1.00 13.73           O  
ATOM   1583  N   GLN A 204      44.084   2.048  46.374  1.00 12.17           N  
ATOM   1584  CA  GLN A 204      43.282   0.875  46.716  1.00 14.05           C  
ATOM   1585  C   GLN A 204      43.298  -0.133  45.590  1.00 15.13           C  
ATOM   1586  O   GLN A 204      43.985  -1.137  45.667  1.00 18.39           O  
ATOM   1587  CB  GLN A 204      41.838   1.272  47.034  1.00 15.27           C  
ATOM   1588  CG  GLN A 204      41.702   2.077  48.318  1.00 16.97           C  
ATOM   1589  CD  GLN A 204      40.361   2.796  48.466  1.00 19.26           C  
ATOM   1590  OE1 GLN A 204      39.722   3.196  47.494  1.00 21.86           O  
ATOM   1591  NE2 GLN A 204      39.964   3.007  49.703  1.00 22.88           N  
ATOM   1592  N   PHE A 205      42.682   0.209  44.477  1.00 12.90           N  
ATOM   1593  CA  PHE A 205      42.585  -0.730  43.369  1.00 14.85           C  
ATOM   1594  C   PHE A 205      43.734  -0.827  42.358  1.00 14.90           C  
ATOM   1595  O   PHE A 205      43.920  -1.876  41.734  1.00 19.00           O  
ATOM   1596  CB  PHE A 205      41.220  -0.511  42.708  1.00 14.71           C  
ATOM   1597  CG  PHE A 205      40.109  -0.339  43.737  1.00 18.64           C  
ATOM   1598  CD1 PHE A 205      39.826  -1.386  44.649  1.00 18.90           C  
ATOM   1599  CD2 PHE A 205      39.452   0.895  43.897  1.00 16.21           C  
ATOM   1600  CE1 PHE A 205      38.937  -1.201  45.681  1.00 19.30           C  
ATOM   1601  CE2 PHE A 205      38.565   1.097  44.922  1.00 18.28           C  
ATOM   1602  CZ  PHE A 205      38.292   0.058  45.831  1.00 20.28           C  
ATOM   1603  N   TYR A 206      44.577   0.200  42.277  1.00 11.92           N  
ATOM   1604  CA  TYR A 206      45.677   0.199  41.312  1.00 11.51           C  
ATOM   1605  C   TYR A 206      47.033   0.239  42.020  1.00 12.16           C  
ATOM   1606  O   TYR A 206      48.038   0.631  41.408  1.00 11.95           O  
ATOM   1607  CB  TYR A 206      45.534   1.420  40.380  1.00 10.52           C  
ATOM   1608  CG  TYR A 206      44.227   1.432  39.590  1.00  9.24           C  
ATOM   1609  CD1 TYR A 206      43.043   1.921  40.154  1.00  7.82           C  
ATOM   1610  CD2 TYR A 206      44.167   0.902  38.296  1.00  9.12           C  
ATOM   1611  CE1 TYR A 206      41.833   1.878  39.453  1.00  8.44           C  
ATOM   1612  CE2 TYR A 206      42.956   0.855  37.588  1.00 10.18           C  
ATOM   1613  CZ  TYR A 206      41.793   1.354  38.176  1.00  9.06           C  
ATOM   1614  OH  TYR A 206      40.608   1.375  37.457  1.00 11.62           O  
ATOM   1615  N   LYS A 207      47.074  -0.237  43.273  1.00 13.79           N  
ATOM   1616  CA  LYS A 207      48.311  -0.170  44.062  1.00 15.44           C  
ATOM   1617  C   LYS A 207      49.473  -0.948  43.512  1.00 17.28           C  
ATOM   1618  O   LYS A 207      50.624  -0.627  43.812  1.00 18.03           O  
ATOM   1619  CB  LYS A 207      48.088  -0.505  45.532  1.00 16.03           C  
ATOM   1620  CG  LYS A 207      47.643  -1.938  45.824  1.00 18.85           C  
ATOM   1621  CD  LYS A 207      47.475  -2.100  47.338  1.00 21.19           C  
ATOM   1622  CE  LYS A 207      46.996  -3.470  47.713  1.00 22.01           C  
ATOM   1623  NZ  LYS A 207      46.858  -3.549  49.184  1.00 23.67           N  
ATOM   1624  N   GLU A 208      49.192  -1.950  42.686  1.00 18.42           N  
ATOM   1625  CA  GLU A 208      50.274  -2.717  42.097  1.00 19.77           C  
ATOM   1626  C   GLU A 208      51.043  -1.886  41.060  1.00 17.68           C  
ATOM   1627  O   GLU A 208      52.268  -1.967  41.002  1.00 16.51           O  
ATOM   1628  CB  GLU A 208      49.779  -4.023  41.477  1.00 23.85           C  
ATOM   1629  CG  GLU A 208      50.935  -4.826  40.866  1.00 31.21           C  
ATOM   1630  CD  GLU A 208      50.477  -6.028  40.083  1.00 34.93           C  
ATOM   1631  OE1 GLU A 208      50.428  -5.944  38.819  1.00 36.06           O  
ATOM   1632  OE2 GLU A 208      50.163  -7.052  40.744  1.00 37.28           O  
ATOM   1633  N   SER A 209      50.342  -1.121  40.228  1.00 15.39           N  
ATOM   1634  CA  SER A 209      51.011  -0.271  39.242  1.00 14.77           C  
ATOM   1635  C   SER A 209      51.726   0.863  39.985  1.00 13.49           C  
ATOM   1636  O   SER A 209      52.840   1.235  39.637  1.00 12.74           O  
ATOM   1637  CB  SER A 209      50.007   0.335  38.287  1.00 16.26           C  
ATOM   1638  OG  SER A 209      49.392  -0.681  37.543  1.00 22.30           O  
ATOM   1639  N   LEU A 210      51.074   1.376  41.027  1.00 12.83           N  
ATOM   1640  CA  LEU A 210      51.615   2.463  41.840  1.00 13.05           C  
ATOM   1641  C   LEU A 210      52.948   2.053  42.463  1.00 13.44           C  
ATOM   1642  O   LEU A 210      53.935   2.789  42.372  1.00 13.15           O  
ATOM   1643  CB  LEU A 210      50.618   2.855  42.951  1.00 12.03           C  
ATOM   1644  CG  LEU A 210      51.084   3.941  43.936  1.00 11.77           C  
ATOM   1645  CD1 LEU A 210      51.386   5.237  43.175  1.00 11.24           C  
ATOM   1646  CD2 LEU A 210      50.027   4.177  45.010  1.00 11.59           C  
ATOM   1647  N   MET A 211      52.990   0.855  43.050  1.00 14.25           N  
ATOM   1648  CA  MET A 211      54.210   0.389  43.695  1.00 13.78           C  
ATOM   1649  C   MET A 211      55.275  -0.045  42.705  1.00 14.35           C  
ATOM   1650  O   MET A 211      56.452  -0.073  43.054  1.00 14.67           O  
ATOM   1651  CB  MET A 211      53.928  -0.663  44.763  1.00 13.62           C  
ATOM   1652  CG  MET A 211      53.196  -0.099  45.962  1.00 15.24           C  
ATOM   1653  SD  MET A 211      54.071   1.219  46.838  1.00 19.87           S  
ATOM   1654  CE  MET A 211      55.423   0.277  47.657  1.00 19.25           C  
ATOM   1655  N   LYS A 212      54.891  -0.307  41.458  1.00 14.58           N  
ATOM   1656  CA  LYS A 212      55.873  -0.663  40.429  1.00 15.59           C  
ATOM   1657  C   LYS A 212      56.680   0.597  40.033  1.00 16.02           C  
ATOM   1658  O   LYS A 212      57.899   0.547  39.801  1.00 16.18           O  
ATOM   1659  CB  LYS A 212      55.163  -1.241  39.204  1.00 18.09           C  
ATOM   1660  CG  LYS A 212      56.071  -1.863  38.178  1.00 21.85           C  
ATOM   1661  CD  LYS A 212      55.292  -2.905  37.360  1.00 27.30           C  
ATOM   1662  CE  LYS A 212      56.095  -3.459  36.163  1.00 28.88           C  
ATOM   1663  NZ  LYS A 212      57.256  -4.318  36.537  1.00 31.77           N  
ATOM   1664  N   VAL A 213      55.989   1.732  39.986  1.00 13.37           N  
ATOM   1665  CA  VAL A 213      56.601   3.017  39.633  1.00 13.32           C  
ATOM   1666  C   VAL A 213      57.330   3.712  40.808  1.00 11.66           C  
ATOM   1667  O   VAL A 213      58.303   4.458  40.587  1.00 11.67           O  
ATOM   1668  CB  VAL A 213      55.512   3.991  39.031  1.00 13.13           C  
ATOM   1669  CG1 VAL A 213      56.069   5.401  38.809  1.00 15.92           C  
ATOM   1670  CG2 VAL A 213      54.998   3.449  37.689  1.00 14.09           C  
ATOM   1671  N   MET A 214      56.869   3.471  42.040  1.00 10.19           N  
ATOM   1672  CA  MET A 214      57.438   4.132  43.220  1.00 10.87           C  
ATOM   1673  C   MET A 214      58.974   4.198  43.341  1.00 11.26           C  
ATOM   1674  O   MET A 214      59.509   5.240  43.753  1.00 11.51           O  
ATOM   1675  CB  MET A 214      56.820   3.589  44.514  1.00 10.76           C  
ATOM   1676  CG  MET A 214      57.010   4.468  45.753  1.00 12.41           C  
ATOM   1677  SD  MET A 214      56.183   6.144  45.702  1.00 14.18           S  
ATOM   1678  CE  MET A 214      54.358   5.679  45.689  1.00 12.89           C  
ATOM   1679  N   PRO A 215      59.708   3.104  42.982  1.00 11.70           N  
ATOM   1680  CA  PRO A 215      61.176   3.182  43.102  1.00 11.73           C  
ATOM   1681  C   PRO A 215      61.818   4.286  42.243  1.00 11.87           C  
ATOM   1682  O   PRO A 215      62.970   4.668  42.490  1.00 12.37           O  
ATOM   1683  CB  PRO A 215      61.638   1.767  42.662  1.00 10.96           C  
ATOM   1684  CG  PRO A 215      60.506   0.902  43.090  1.00 11.29           C  
ATOM   1685  CD  PRO A 215      59.296   1.720  42.646  1.00 11.80           C  
ATOM   1686  N   TYR A 216      61.105   4.745  41.213  1.00 10.58           N  
ATOM   1687  CA  TYR A 216      61.589   5.798  40.324  1.00 11.22           C  
ATOM   1688  C   TYR A 216      61.121   7.222  40.703  1.00 11.12           C  
ATOM   1689  O   TYR A 216      61.535   8.192  40.071  1.00 12.52           O  
ATOM   1690  CB  TYR A 216      61.118   5.542  38.898  1.00 12.66           C  
ATOM   1691  CG  TYR A 216      61.618   4.273  38.256  1.00 18.30           C  
ATOM   1692  CD1 TYR A 216      60.714   3.357  37.687  1.00 18.67           C  
ATOM   1693  CD2 TYR A 216      62.993   4.048  38.076  1.00 18.73           C  
ATOM   1694  CE1 TYR A 216      61.168   2.269  36.932  1.00 21.53           C  
ATOM   1695  CE2 TYR A 216      63.455   2.954  37.330  1.00 21.58           C  
ATOM   1696  CZ  TYR A 216      62.537   2.079  36.753  1.00 23.03           C  
ATOM   1697  OH  TYR A 216      62.990   1.060  35.943  1.00 25.65           O  
ATOM   1698  N   VAL A 217      60.249   7.345  41.703  1.00 10.46           N  
ATOM   1699  CA  VAL A 217      59.698   8.649  42.099  1.00 10.23           C  
ATOM   1700  C   VAL A 217      60.592   9.486  42.992  1.00  9.76           C  
ATOM   1701  O   VAL A 217      60.818   9.128  44.150  1.00 10.30           O  
ATOM   1702  CB  VAL A 217      58.331   8.455  42.783  1.00 10.54           C  
ATOM   1703  CG1 VAL A 217      57.772   9.767  43.256  1.00 10.19           C  
ATOM   1704  CG2 VAL A 217      57.349   7.800  41.780  1.00 10.29           C  
ATOM   1705  N   ASP A 218      61.064  10.608  42.437  1.00 10.12           N  
ATOM   1706  CA  ASP A 218      61.930  11.583  43.118  1.00 10.57           C  
ATOM   1707  C   ASP A 218      61.136  12.511  44.046  1.00  9.77           C  
ATOM   1708  O   ASP A 218      61.620  12.887  45.115  1.00 10.74           O  
ATOM   1709  CB  ASP A 218      62.717  12.402  42.096  1.00 11.28           C  
ATOM   1710  CG  ASP A 218      63.711  11.551  41.308  1.00 14.42           C  
ATOM   1711  OD1 ASP A 218      64.505  10.816  41.946  1.00 17.28           O  
ATOM   1712  OD2 ASP A 218      63.699  11.609  40.054  1.00 16.18           O  
ATOM   1713  N   ILE A 219      59.943  12.918  43.609  1.00  9.18           N  
ATOM   1714  CA  ILE A 219      59.070  13.747  44.439  1.00  9.61           C  
ATOM   1715  C   ILE A 219      57.631  13.229  44.319  1.00  7.48           C  
ATOM   1716  O   ILE A 219      57.100  13.088  43.205  1.00  7.78           O  
ATOM   1717  CB  ILE A 219      59.102  15.256  44.036  1.00 10.68           C  
ATOM   1718  CG1 ILE A 219      60.546  15.775  44.046  1.00 10.46           C  
ATOM   1719  CG2 ILE A 219      58.220  16.093  45.029  1.00  9.69           C  
ATOM   1720  CD1 ILE A 219      60.663  17.230  43.624  1.00 12.66           C  
ATOM   1721  N   LEU A 220      57.039  12.905  45.466  1.00  8.28           N  
ATOM   1722  CA  LEU A 220      55.650  12.431  45.510  1.00  8.11           C  
ATOM   1723  C   LEU A 220      54.748  13.505  46.140  1.00  7.53           C  
ATOM   1724  O   LEU A 220      55.041  14.018  47.233  1.00  8.51           O  
ATOM   1725  CB  LEU A 220      55.523  11.153  46.357  1.00  8.63           C  
ATOM   1726  CG  LEU A 220      54.108  10.524  46.444  1.00  7.56           C  
ATOM   1727  CD1 LEU A 220      53.738   9.869  45.084  1.00  8.43           C  
ATOM   1728  CD2 LEU A 220      54.049   9.516  47.598  1.00  9.05           C  
ATOM   1729  N   PHE A 221      53.626  13.779  45.463  1.00  7.71           N  
ATOM   1730  CA  PHE A 221      52.619  14.749  45.921  1.00  7.91           C  
ATOM   1731  C   PHE A 221      51.297  14.014  46.273  1.00  9.01           C  
ATOM   1732  O   PHE A 221      50.955  12.993  45.649  1.00  8.40           O  
ATOM   1733  CB  PHE A 221      52.262  15.763  44.812  1.00  7.34           C  
ATOM   1734  CG  PHE A 221      53.412  16.605  44.325  1.00  7.21           C  
ATOM   1735  CD1 PHE A 221      54.003  16.342  43.091  1.00  9.28           C  
ATOM   1736  CD2 PHE A 221      53.857  17.708  45.054  1.00  8.89           C  
ATOM   1737  CE1 PHE A 221      55.018  17.166  42.576  1.00 10.29           C  
ATOM   1738  CE2 PHE A 221      54.882  18.548  44.544  1.00  8.87           C  
ATOM   1739  CZ  PHE A 221      55.455  18.276  43.311  1.00 11.19           C  
ATOM   1740  N   GLY A 222      50.545  14.573  47.229  1.00  8.02           N  
ATOM   1741  CA  GLY A 222      49.249  14.018  47.581  1.00  7.47           C  
ATOM   1742  C   GLY A 222      48.610  14.839  48.678  1.00  8.95           C  
ATOM   1743  O   GLY A 222      49.303  15.683  49.259  1.00  9.04           O  
ATOM   1744  N   ASN A 223      47.300  14.672  48.920  1.00  8.54           N  
ATOM   1745  CA  ASN A 223      46.639  15.387  50.036  1.00  9.81           C  
ATOM   1746  C   ASN A 223      46.527  14.457  51.278  1.00 10.16           C  
ATOM   1747  O   ASN A 223      46.979  13.295  51.238  1.00 10.03           O  
ATOM   1748  CB  ASN A 223      45.271  16.001  49.632  1.00  9.86           C  
ATOM   1749  CG  ASN A 223      44.194  14.952  49.322  1.00 11.01           C  
ATOM   1750  OD1 ASN A 223      44.363  13.754  49.603  1.00 12.01           O  
ATOM   1751  ND2 ASN A 223      43.060  15.410  48.775  1.00 11.23           N  
ATOM   1752  N   GLU A 224      45.874  14.921  52.346  1.00 10.64           N  
ATOM   1753  CA  GLU A 224      45.816  14.104  53.562  1.00 12.37           C  
ATOM   1754  C   GLU A 224      44.942  12.842  53.515  1.00 11.53           C  
ATOM   1755  O   GLU A 224      45.252  11.875  54.217  1.00 11.13           O  
ATOM   1756  CB  GLU A 224      45.530  14.941  54.807  1.00 16.24           C  
ATOM   1757  CG  GLU A 224      44.103  15.100  55.144  1.00 22.70           C  
ATOM   1758  CD  GLU A 224      43.511  16.333  54.533  1.00 29.71           C  
ATOM   1759  OE1 GLU A 224      43.675  16.524  53.300  1.00 30.28           O  
ATOM   1760  OE2 GLU A 224      42.884  17.126  55.299  1.00 34.16           O  
ATOM   1761  N   THR A 225      43.899  12.821  52.679  1.00 10.81           N  
ATOM   1762  CA  THR A 225      43.094  11.611  52.590  1.00 11.71           C  
ATOM   1763  C   THR A 225      43.794  10.552  51.734  1.00 10.89           C  
ATOM   1764  O   THR A 225      43.696   9.357  52.038  1.00  9.85           O  
ATOM   1765  CB  THR A 225      41.650  11.850  52.115  1.00 14.24           C  
ATOM   1766  OG1 THR A 225      41.643  12.612  50.913  1.00 17.45           O  
ATOM   1767  CG2 THR A 225      40.872  12.574  53.195  1.00 17.12           C  
ATOM   1768  N   GLU A 226      44.518  10.986  50.698  1.00  8.50           N  
ATOM   1769  CA  GLU A 226      45.264  10.046  49.860  1.00  9.28           C  
ATOM   1770  C   GLU A 226      46.423   9.425  50.680  1.00  9.11           C  
ATOM   1771  O   GLU A 226      46.731   8.249  50.544  1.00  9.63           O  
ATOM   1772  CB  GLU A 226      45.798  10.757  48.605  1.00  8.68           C  
ATOM   1773  CG  GLU A 226      44.734  11.036  47.553  1.00 10.83           C  
ATOM   1774  CD  GLU A 226      44.773  12.452  46.940  1.00 12.95           C  
ATOM   1775  OE1 GLU A 226      45.859  13.108  46.884  1.00 11.07           O  
ATOM   1776  OE2 GLU A 226      43.688  12.899  46.506  1.00 12.03           O  
ATOM   1777  N   ALA A 227      47.086  10.228  51.514  1.00  9.18           N  
ATOM   1778  CA  ALA A 227      48.169   9.732  52.364  1.00  8.31           C  
ATOM   1779  C   ALA A 227      47.636   8.670  53.337  1.00  9.52           C  
ATOM   1780  O   ALA A 227      48.291   7.654  53.555  1.00 10.58           O  
ATOM   1781  CB  ALA A 227      48.823  10.896  53.156  1.00  7.47           C  
ATOM   1782  N   ALA A 228      46.461   8.905  53.929  1.00  8.88           N  
ATOM   1783  CA  ALA A 228      45.878   7.959  54.885  1.00  8.66           C  
ATOM   1784  C   ALA A 228      45.515   6.618  54.223  1.00 10.18           C  
ATOM   1785  O   ALA A 228      45.730   5.537  54.797  1.00 11.00           O  
ATOM   1786  CB  ALA A 228      44.659   8.576  55.556  1.00 10.35           C  
ATOM   1787  N   THR A 229      44.968   6.697  53.013  1.00 10.61           N  
ATOM   1788  CA  THR A 229      44.583   5.509  52.253  1.00 11.04           C  
ATOM   1789  C   THR A 229      45.846   4.717  51.872  1.00 10.79           C  
ATOM   1790  O   THR A 229      45.913   3.505  52.058  1.00 10.14           O  
ATOM   1791  CB  THR A 229      43.802   5.901  50.980  1.00 11.93           C  
ATOM   1792  OG1 THR A 229      42.642   6.661  51.343  1.00 12.87           O  
ATOM   1793  CG2 THR A 229      43.366   4.655  50.198  1.00 13.41           C  
ATOM   1794  N   PHE A 230      46.847   5.410  51.346  1.00  9.58           N  
ATOM   1795  CA  PHE A 230      48.107   4.787  50.983  1.00  9.60           C  
ATOM   1796  C   PHE A 230      48.734   4.063  52.181  1.00 10.52           C  
ATOM   1797  O   PHE A 230      49.223   2.946  52.030  1.00 10.75           O  
ATOM   1798  CB  PHE A 230      49.071   5.863  50.475  1.00 10.19           C  
ATOM   1799  CG  PHE A 230      50.409   5.335  50.034  1.00 10.76           C  
ATOM   1800  CD1 PHE A 230      50.529   4.637  48.817  1.00  9.85           C  
ATOM   1801  CD2 PHE A 230      51.546   5.531  50.834  1.00 10.83           C  
ATOM   1802  CE1 PHE A 230      51.757   4.134  48.400  1.00 11.45           C  
ATOM   1803  CE2 PHE A 230      52.790   5.038  50.433  1.00 11.47           C  
ATOM   1804  CZ  PHE A 230      52.899   4.334  49.208  1.00 13.18           C  
ATOM   1805  N   ALA A 231      48.735   4.697  53.359  1.00 10.89           N  
ATOM   1806  CA  ALA A 231      49.310   4.096  54.559  1.00 11.60           C  
ATOM   1807  C   ALA A 231      48.568   2.818  54.955  1.00 13.28           C  
ATOM   1808  O   ALA A 231      49.186   1.799  55.264  1.00 14.21           O  
ATOM   1809  CB  ALA A 231      49.297   5.087  55.723  1.00 12.14           C  
ATOM   1810  N   ARG A 232      47.240   2.869  54.935  1.00 13.82           N  
ATOM   1811  CA  ARG A 232      46.407   1.715  55.283  1.00 15.91           C  
ATOM   1812  C   ARG A 232      46.729   0.541  54.348  1.00 16.28           C  
ATOM   1813  O   ARG A 232      47.110  -0.543  54.798  1.00 17.89           O  
ATOM   1814  CB  ARG A 232      44.933   2.111  55.110  1.00 18.59           C  
ATOM   1815  CG  ARG A 232      43.879   1.137  55.615  1.00 23.12           C  
ATOM   1816  CD  ARG A 232      42.491   1.634  55.182  1.00 26.24           C  
ATOM   1817  NE  ARG A 232      42.321   3.037  55.567  1.00 28.79           N  
ATOM   1818  CZ  ARG A 232      41.843   4.018  54.792  1.00 28.95           C  
ATOM   1819  NH1 ARG A 232      41.440   3.789  53.547  1.00 27.16           N  
ATOM   1820  NH2 ARG A 232      41.856   5.271  55.245  1.00 29.21           N  
ATOM   1821  N   GLU A 233      46.651   0.798  53.044  1.00 15.09           N  
ATOM   1822  CA  GLU A 233      46.870  -0.218  52.010  1.00 14.74           C  
ATOM   1823  C   GLU A 233      48.267  -0.806  51.971  1.00 15.46           C  
ATOM   1824  O   GLU A 233      48.433  -1.962  51.548  1.00 15.82           O  
ATOM   1825  CB  GLU A 233      46.469   0.312  50.626  1.00 15.05           C  
ATOM   1826  CG  GLU A 233      44.999   0.718  50.490  1.00 16.80           C  
ATOM   1827  CD  GLU A 233      44.027  -0.474  50.435  1.00 21.08           C  
ATOM   1828  OE1 GLU A 233      42.867  -0.337  50.903  1.00 22.09           O  
ATOM   1829  OE2 GLU A 233      44.409  -1.541  49.905  1.00 21.02           O  
ATOM   1830  N   GLN A 234      49.264  -0.034  52.411  1.00 15.02           N  
ATOM   1831  CA  GLN A 234      50.648  -0.514  52.451  1.00 15.47           C  
ATOM   1832  C   GLN A 234      51.014  -1.122  53.805  1.00 15.45           C  
ATOM   1833  O   GLN A 234      52.139  -1.559  54.005  1.00 17.80           O  
ATOM   1834  CB  GLN A 234      51.641   0.584  52.063  1.00 15.34           C  
ATOM   1835  CG  GLN A 234      51.503   1.026  50.634  1.00 15.43           C  
ATOM   1836  CD  GLN A 234      51.819  -0.084  49.678  1.00 18.24           C  
ATOM   1837  OE1 GLN A 234      52.849  -0.748  49.827  1.00 19.01           O  
ATOM   1838  NE2 GLN A 234      50.938  -0.317  48.695  1.00 16.44           N  
ATOM   1839  N   GLY A 235      50.053  -1.168  54.720  1.00 16.22           N  
ATOM   1840  CA  GLY A 235      50.278  -1.765  56.028  1.00 16.04           C  
ATOM   1841  C   GLY A 235      51.190  -1.003  56.974  1.00 17.91           C  
ATOM   1842  O   GLY A 235      51.797  -1.625  57.868  1.00 18.15           O  
ATOM   1843  N   PHE A 236      51.271   0.322  56.809  1.00 16.60           N  
ATOM   1844  CA  PHE A 236      52.108   1.187  57.653  1.00 16.86           C  
ATOM   1845  C   PHE A 236      51.749   1.177  59.147  1.00 18.35           C  
ATOM   1846  O   PHE A 236      52.594   1.506  59.991  1.00 18.30           O  
ATOM   1847  CB  PHE A 236      52.053   2.644  57.172  1.00 16.59           C  
ATOM   1848  CG  PHE A 236      52.902   2.946  55.958  1.00 16.57           C  
ATOM   1849  CD1 PHE A 236      52.957   4.255  55.451  1.00 15.73           C  
ATOM   1850  CD2 PHE A 236      53.648   1.950  55.317  1.00 16.04           C  
ATOM   1851  CE1 PHE A 236      53.744   4.570  54.315  1.00 14.71           C  
ATOM   1852  CE2 PHE A 236      54.443   2.256  54.178  1.00 15.83           C  
ATOM   1853  CZ  PHE A 236      54.489   3.565  53.678  1.00 14.44           C  
ATOM   1854  N   GLU A 237      50.487   0.882  59.469  1.00 19.55           N  
ATOM   1855  CA  GLU A 237      49.999   0.835  60.862  1.00 22.71           C  
ATOM   1856  C   GLU A 237      50.049   2.137  61.671  1.00 22.82           C  
ATOM   1857  O   GLU A 237      50.213   2.131  62.885  1.00 23.94           O  
ATOM   1858  CB  GLU A 237      50.675  -0.290  61.642  1.00 25.54           C  
ATOM   1859  CG  GLU A 237      50.497  -1.654  60.992  1.00 30.83           C  
ATOM   1860  CD  GLU A 237      50.599  -2.790  61.983  1.00 34.33           C  
ATOM   1861  OE1 GLU A 237      51.724  -3.128  62.417  1.00 36.58           O  
ATOM   1862  OE2 GLU A 237      49.534  -3.341  62.339  1.00 37.59           O  
ATOM   1863  N   THR A 238      49.928   3.256  60.975  1.00 22.37           N  
ATOM   1864  CA  THR A 238      49.902   4.574  61.595  1.00 20.49           C  
ATOM   1865  C   THR A 238      48.955   5.440  60.766  1.00 19.41           C  
ATOM   1866  O   THR A 238      48.752   5.211  59.564  1.00 19.46           O  
ATOM   1867  CB  THR A 238      51.322   5.252  61.659  1.00 21.31           C  
ATOM   1868  OG1 THR A 238      51.201   6.581  62.198  1.00 19.66           O  
ATOM   1869  CG2 THR A 238      51.970   5.352  60.268  1.00 21.72           C  
ATOM   1870  N   LYS A 239      48.353   6.418  61.425  1.00 18.68           N  
ATOM   1871  CA  LYS A 239      47.459   7.345  60.755  1.00 18.66           C  
ATOM   1872  C   LYS A 239      47.979   8.789  60.877  1.00 18.45           C  
ATOM   1873  O   LYS A 239      47.337   9.712  60.387  1.00 19.16           O  
ATOM   1874  CB  LYS A 239      46.047   7.229  61.329  1.00 19.24           C  
ATOM   1875  CG  LYS A 239      45.465   5.830  61.292  1.00 19.53           C  
ATOM   1876  CD  LYS A 239      44.033   5.884  61.782  1.00 24.32           C  
ATOM   1877  CE  LYS A 239      43.368   4.516  61.792  1.00 26.94           C  
ATOM   1878  NZ  LYS A 239      41.933   4.647  62.179  1.00 29.30           N  
ATOM   1879  N   ASP A 240      49.121   8.974  61.546  1.00 17.55           N  
ATOM   1880  CA  ASP A 240      49.767  10.296  61.738  1.00 17.22           C  
ATOM   1881  C   ASP A 240      50.445  10.752  60.435  1.00 15.36           C  
ATOM   1882  O   ASP A 240      51.360  10.086  59.947  1.00 14.63           O  
ATOM   1883  CB  ASP A 240      50.816  10.221  62.859  1.00 19.79           C  
ATOM   1884  CG  ASP A 240      51.556  11.551  63.070  1.00 23.80           C  
ATOM   1885  OD1 ASP A 240      51.036  12.399  63.828  1.00 25.60           O  
ATOM   1886  OD2 ASP A 240      52.652  11.747  62.486  1.00 24.01           O  
ATOM   1887  N   ILE A 241      50.037  11.913  59.920  1.00 14.62           N  
ATOM   1888  CA  ILE A 241      50.550  12.419  58.637  1.00 14.40           C  
ATOM   1889  C   ILE A 241      52.063  12.571  58.527  1.00 13.06           C  
ATOM   1890  O   ILE A 241      52.651  12.256  57.489  1.00 11.82           O  
ATOM   1891  CB  ILE A 241      49.831  13.728  58.214  1.00 15.91           C  
ATOM   1892  CG1 ILE A 241      50.185  14.097  56.785  1.00 15.59           C  
ATOM   1893  CG2 ILE A 241      50.230  14.889  59.118  1.00 18.87           C  
ATOM   1894  CD1 ILE A 241      49.430  13.321  55.789  1.00 20.71           C  
ATOM   1895  N   LYS A 242      52.699  13.018  59.610  1.00 14.23           N  
ATOM   1896  CA  LYS A 242      54.161  13.195  59.631  1.00 15.21           C  
ATOM   1897  C   LYS A 242      54.911  11.850  59.620  1.00 15.22           C  
ATOM   1898  O   LYS A 242      55.946  11.715  58.970  1.00 15.02           O  
ATOM   1899  CB  LYS A 242      54.576  14.046  60.838  1.00 15.88           C  
ATOM   1900  CG  LYS A 242      54.055  15.468  60.756  1.00 16.92           C  
ATOM   1901  CD  LYS A 242      54.624  16.291  61.881  1.00 21.06           C  
ATOM   1902  CE  LYS A 242      54.307  17.749  61.689  1.00 24.08           C  
ATOM   1903  NZ  LYS A 242      55.146  18.568  62.611  1.00 29.39           N  
ATOM   1904  N   GLU A 243      54.340  10.846  60.286  1.00 14.43           N  
ATOM   1905  CA  GLU A 243      54.938   9.520  60.327  1.00 14.14           C  
ATOM   1906  C   GLU A 243      54.754   8.839  58.964  1.00 12.09           C  
ATOM   1907  O   GLU A 243      55.644   8.139  58.492  1.00 12.57           O  
ATOM   1908  CB  GLU A 243      54.309   8.703  61.454  1.00 16.77           C  
ATOM   1909  CG  GLU A 243      54.969   7.370  61.723  1.00 20.58           C  
ATOM   1910  CD  GLU A 243      56.335   7.490  62.403  1.00 23.99           C  
ATOM   1911  OE1 GLU A 243      56.668   8.575  62.947  1.00 24.58           O  
ATOM   1912  OE2 GLU A 243      57.074   6.478  62.408  1.00 26.17           O  
ATOM   1913  N   ILE A 244      53.590   9.023  58.343  1.00 11.37           N  
ATOM   1914  CA  ILE A 244      53.337   8.443  57.022  1.00  9.64           C  
ATOM   1915  C   ILE A 244      54.317   9.077  56.007  1.00 10.82           C  
ATOM   1916  O   ILE A 244      54.878   8.379  55.154  1.00 11.07           O  
ATOM   1917  CB  ILE A 244      51.878   8.660  56.565  1.00  9.23           C  
ATOM   1918  CG1 ILE A 244      50.924   7.994  57.575  1.00 10.79           C  
ATOM   1919  CG2 ILE A 244      51.688   8.189  55.093  1.00  9.17           C  
ATOM   1920  CD1 ILE A 244      49.422   8.365  57.410  1.00 11.68           C  
ATOM   1921  N   ALA A 245      54.513  10.399  56.075  1.00 10.58           N  
ATOM   1922  CA  ALA A 245      55.455  11.079  55.156  1.00 10.05           C  
ATOM   1923  C   ALA A 245      56.883  10.510  55.344  1.00  9.90           C  
ATOM   1924  O   ALA A 245      57.612  10.305  54.380  1.00 10.01           O  
ATOM   1925  CB  ALA A 245      55.450  12.605  55.410  1.00 10.31           C  
ATOM   1926  N   LYS A 246      57.250  10.246  56.600  1.00 10.59           N  
ATOM   1927  CA  LYS A 246      58.569   9.679  56.936  1.00 12.90           C  
ATOM   1928  C   LYS A 246      58.725   8.274  56.322  1.00 12.34           C  
ATOM   1929  O   LYS A 246      59.696   8.018  55.615  1.00 13.13           O  
ATOM   1930  CB  LYS A 246      58.731   9.621  58.462  1.00 13.21           C  
ATOM   1931  CG  LYS A 246      60.070   9.145  58.966  1.00 17.20           C  
ATOM   1932  CD  LYS A 246      60.034   9.022  60.477  1.00 18.94           C  
ATOM   1933  CE  LYS A 246      61.287   8.356  60.990  1.00 22.42           C  
ATOM   1934  NZ  LYS A 246      61.115   7.974  62.421  1.00 24.80           N  
ATOM   1935  N   LYS A 247      57.749   7.387  56.552  1.00 12.89           N  
ATOM   1936  CA  LYS A 247      57.806   6.016  56.014  1.00 13.28           C  
ATOM   1937  C   LYS A 247      57.771   5.966  54.492  1.00 12.41           C  
ATOM   1938  O   LYS A 247      58.463   5.151  53.876  1.00 12.48           O  
ATOM   1939  CB  LYS A 247      56.670   5.166  56.585  1.00 14.19           C  
ATOM   1940  CG  LYS A 247      56.799   4.833  58.072  1.00 16.35           C  
ATOM   1941  CD  LYS A 247      55.495   4.255  58.564  1.00 20.39           C  
ATOM   1942  CE  LYS A 247      55.608   3.752  59.961  1.00 23.12           C  
ATOM   1943  NZ  LYS A 247      56.535   2.606  59.925  1.00 27.63           N  
ATOM   1944  N   THR A 248      56.970   6.847  53.883  1.00 11.28           N  
ATOM   1945  CA  THR A 248      56.863   6.907  52.428  1.00 10.78           C  
ATOM   1946  C   THR A 248      58.203   7.378  51.842  1.00 11.37           C  
ATOM   1947  O   THR A 248      58.661   6.865  50.821  1.00 10.69           O  
ATOM   1948  CB  THR A 248      55.730   7.895  51.985  1.00 11.88           C  
ATOM   1949  OG1 THR A 248      54.474   7.489  52.569  1.00 11.72           O  
ATOM   1950  CG2 THR A 248      55.607   7.906  50.453  1.00 10.92           C  
ATOM   1951  N   GLN A 249      58.828   8.358  52.496  1.00 10.61           N  
ATOM   1952  CA  GLN A 249      60.105   8.867  52.012  1.00 12.10           C  
ATOM   1953  C   GLN A 249      61.153   7.746  51.993  1.00 12.04           C  
ATOM   1954  O   GLN A 249      61.972   7.678  51.076  1.00 12.71           O  
ATOM   1955  CB  GLN A 249      60.591  10.032  52.901  1.00 11.09           C  
ATOM   1956  CG  GLN A 249      61.785  10.841  52.343  1.00 11.40           C  
ATOM   1957  CD  GLN A 249      63.157  10.152  52.492  1.00 12.46           C  
ATOM   1958  OE1 GLN A 249      63.382   9.382  53.425  1.00 14.06           O  
ATOM   1959  NE2 GLN A 249      64.081  10.471  51.590  1.00 11.89           N  
ATOM   1960  N   ALA A 250      61.095   6.872  52.995  1.00 13.35           N  
ATOM   1961  CA  ALA A 250      62.043   5.761  53.154  1.00 14.09           C  
ATOM   1962  C   ALA A 250      61.849   4.536  52.269  1.00 15.34           C  
ATOM   1963  O   ALA A 250      62.700   3.652  52.291  1.00 17.02           O  
ATOM   1964  CB  ALA A 250      62.095   5.330  54.607  1.00 13.71           C  
ATOM   1965  N   LEU A 251      60.772   4.477  51.483  1.00 14.38           N  
ATOM   1966  CA  LEU A 251      60.511   3.331  50.595  1.00 13.93           C  
ATOM   1967  C   LEU A 251      61.664   3.076  49.636  1.00 15.14           C  
ATOM   1968  O   LEU A 251      62.397   3.990  49.296  1.00 15.10           O  
ATOM   1969  CB  LEU A 251      59.233   3.532  49.786  1.00 12.88           C  
ATOM   1970  CG  LEU A 251      57.948   3.432  50.602  1.00 12.85           C  
ATOM   1971  CD1 LEU A 251      56.756   3.756  49.730  1.00 13.35           C  
ATOM   1972  CD2 LEU A 251      57.821   2.029  51.184  1.00 13.79           C  
ATOM   1973  N   PRO A 252      61.846   1.816  49.189  1.00 16.45           N  
ATOM   1974  CA  PRO A 252      62.941   1.485  48.264  1.00 16.82           C  
ATOM   1975  C   PRO A 252      63.049   2.434  47.062  1.00 17.47           C  
ATOM   1976  O   PRO A 252      62.045   2.736  46.386  1.00 17.67           O  
ATOM   1977  CB  PRO A 252      62.593   0.068  47.815  1.00 17.93           C  
ATOM   1978  CG  PRO A 252      61.905  -0.512  49.040  1.00 18.56           C  
ATOM   1979  CD  PRO A 252      61.023   0.627  49.498  1.00 16.76           C  
ATOM   1980  N   LYS A 253      64.273   2.879  46.781  1.00 16.65           N  
ATOM   1981  CA  LYS A 253      64.542   3.800  45.680  1.00 16.88           C  
ATOM   1982  C   LYS A 253      65.679   3.292  44.788  1.00 18.79           C  
ATOM   1983  O   LYS A 253      66.708   2.814  45.300  1.00 18.25           O  
ATOM   1984  CB  LYS A 253      64.855   5.210  46.227  1.00 15.58           C  
ATOM   1985  CG  LYS A 253      64.932   6.263  45.145  1.00 15.34           C  
ATOM   1986  CD  LYS A 253      64.730   7.636  45.685  1.00 15.06           C  
ATOM   1987  CE  LYS A 253      64.351   8.594  44.556  1.00 14.63           C  
ATOM   1988  NZ  LYS A 253      65.417   8.761  43.547  1.00 14.15           N  
ATOM   1989  N   MET A 254      65.483   3.412  43.469  1.00 18.38           N  
ATOM   1990  CA  MET A 254      66.440   2.945  42.465  1.00 20.47           C  
ATOM   1991  C   MET A 254      67.688   3.800  42.323  1.00 21.92           C  
ATOM   1992  O   MET A 254      68.814   3.294  42.445  1.00 21.79           O  
ATOM   1993  CB  MET A 254      65.752   2.814  41.112  1.00 21.36           C  
ATOM   1994  CG  MET A 254      66.676   2.374  39.974  1.00 26.07           C  
ATOM   1995  SD  MET A 254      67.393   0.693  40.210  1.00 31.89           S  
ATOM   1996  CE  MET A 254      68.386   0.557  38.714  1.00 30.70           C  
ATOM   1997  N   ASN A 255      67.474   5.085  42.031  1.00 22.80           N  
ATOM   1998  CA  ASN A 255      68.531   6.090  41.850  1.00 24.13           C  
ATOM   1999  C   ASN A 255      69.074   6.620  43.198  1.00 24.61           C  
ATOM   2000  O   ASN A 255      68.442   7.427  43.884  1.00 24.61           O  
ATOM   2001  CB  ASN A 255      67.964   7.226  40.993  1.00 25.01           C  
ATOM   2002  CG  ASN A 255      68.998   8.257  40.600  1.00 27.34           C  
ATOM   2003  OD1 ASN A 255      68.680   9.223  39.874  1.00 28.11           O  
ATOM   2004  ND2 ASN A 255      70.241   8.073  41.067  1.00 26.34           N  
ATOM   2005  N   SER A 256      70.252   6.141  43.576  1.00 24.86           N  
ATOM   2006  CA  SER A 256      70.912   6.535  44.826  1.00 25.83           C  
ATOM   2007  C   SER A 256      71.419   7.997  44.820  1.00 24.49           C  
ATOM   2008  O   SER A 256      71.787   8.535  45.871  1.00 24.22           O  
ATOM   2009  CB  SER A 256      72.110   5.613  45.063  1.00 25.74           C  
ATOM   2010  OG  SER A 256      72.970   5.681  43.931  1.00 25.90           O  
ATOM   2011  N   LYS A 257      71.478   8.606  43.635  1.00 23.68           N  
ATOM   2012  CA  LYS A 257      71.953   9.985  43.492  1.00 24.44           C  
ATOM   2013  C   LYS A 257      70.958  11.083  43.945  1.00 22.94           C  
ATOM   2014  O   LYS A 257      71.325  12.258  44.021  1.00 23.33           O  
ATOM   2015  CB  LYS A 257      72.369  10.257  42.043  1.00 25.55           C  
ATOM   2016  CG  LYS A 257      73.686   9.622  41.591  1.00 28.11           C  
ATOM   2017  CD  LYS A 257      73.915   9.958  40.097  1.00 29.33           C  
ATOM   2018  CE  LYS A 257      75.359   9.730  39.659  1.00 32.17           C  
ATOM   2019  NZ  LYS A 257      76.347  10.563  40.447  1.00 33.65           N  
ATOM   2020  N   ARG A 258      69.699  10.710  44.179  1.00 20.98           N  
ATOM   2021  CA  ARG A 258      68.657  11.654  44.619  1.00 19.01           C  
ATOM   2022  C   ARG A 258      67.785  10.984  45.668  1.00 18.65           C  
ATOM   2023  O   ARG A 258      67.245   9.904  45.424  1.00 19.09           O  
ATOM   2024  CB  ARG A 258      67.722  12.060  43.470  1.00 19.13           C  
ATOM   2025  CG  ARG A 258      68.373  12.714  42.286  1.00 21.35           C  
ATOM   2026  CD  ARG A 258      67.316  13.225  41.309  1.00 21.42           C  
ATOM   2027  NE  ARG A 258      67.944  13.887  40.169  1.00 23.22           N  
ATOM   2028  CZ  ARG A 258      68.238  15.185  40.123  1.00 23.93           C  
ATOM   2029  NH1 ARG A 258      67.954  15.973  41.156  1.00 24.49           N  
ATOM   2030  NH2 ARG A 258      68.812  15.701  39.043  1.00 22.24           N  
ATOM   2031  N   GLN A 259      67.654  11.626  46.825  1.00 17.45           N  
ATOM   2032  CA  GLN A 259      66.822  11.133  47.917  1.00 18.15           C  
ATOM   2033  C   GLN A 259      65.404  11.564  47.583  1.00 16.38           C  
ATOM   2034  O   GLN A 259      65.211  12.632  46.992  1.00 17.16           O  
ATOM   2035  CB  GLN A 259      67.228  11.817  49.219  1.00 21.62           C  
ATOM   2036  CG  GLN A 259      68.722  11.806  49.447  1.00 29.35           C  
ATOM   2037  CD  GLN A 259      69.189  10.432  49.805  1.00 33.11           C  
ATOM   2038  OE1 GLN A 259      68.903   9.957  50.905  1.00 37.72           O  
ATOM   2039  NE2 GLN A 259      69.875   9.748  48.871  1.00 35.46           N  
ATOM   2040  N   ARG A 260      64.419  10.765  47.978  1.00 14.44           N  
ATOM   2041  CA  ARG A 260      63.025  11.106  47.709  1.00 12.34           C  
ATOM   2042  C   ARG A 260      62.562  12.258  48.613  1.00 11.27           C  
ATOM   2043  O   ARG A 260      63.054  12.412  49.745  1.00 10.80           O  
ATOM   2044  CB  ARG A 260      62.109   9.895  47.951  1.00 12.11           C  
ATOM   2045  CG  ARG A 260      60.658  10.096  47.475  1.00 10.60           C  
ATOM   2046  CD  ARG A 260      59.833   8.846  47.637  1.00 10.85           C  
ATOM   2047  NE  ARG A 260      60.248   7.779  46.727  1.00 11.30           N  
ATOM   2048  CZ  ARG A 260      60.870   6.665  47.102  1.00 10.33           C  
ATOM   2049  NH1 ARG A 260      61.179   6.470  48.379  1.00 10.23           N  
ATOM   2050  NH2 ARG A 260      61.101   5.713  46.200  1.00 10.75           N  
ATOM   2051  N   ILE A 261      61.647  13.076  48.075  1.00 10.88           N  
ATOM   2052  CA  ILE A 261      61.016  14.202  48.796  1.00  9.70           C  
ATOM   2053  C   ILE A 261      59.521  13.915  48.716  1.00  9.12           C  
ATOM   2054  O   ILE A 261      59.019  13.572  47.643  1.00  8.98           O  
ATOM   2055  CB  ILE A 261      61.305  15.563  48.120  1.00  9.36           C  
ATOM   2056  CG1 ILE A 261      62.806  15.871  48.140  1.00  8.59           C  
ATOM   2057  CG2 ILE A 261      60.558  16.705  48.838  1.00 10.26           C  
ATOM   2058  CD1 ILE A 261      63.200  16.942  47.122  1.00 11.49           C  
ATOM   2059  N   VAL A 262      58.846  13.956  49.862  1.00  9.00           N  
ATOM   2060  CA  VAL A 262      57.396  13.708  49.934  1.00  9.82           C  
ATOM   2061  C   VAL A 262      56.673  14.979  50.442  1.00 11.05           C  
ATOM   2062  O   VAL A 262      57.053  15.559  51.476  1.00 10.79           O  
ATOM   2063  CB  VAL A 262      57.077  12.508  50.850  1.00  9.00           C  
ATOM   2064  CG1 VAL A 262      55.580  12.213  50.855  1.00  8.14           C  
ATOM   2065  CG2 VAL A 262      57.817  11.292  50.361  1.00  8.42           C  
ATOM   2066  N   ILE A 263      55.623  15.388  49.726  1.00  9.07           N  
ATOM   2067  CA  ILE A 263      54.867  16.587  50.078  1.00  9.46           C  
ATOM   2068  C   ILE A 263      53.360  16.295  50.188  1.00  8.72           C  
ATOM   2069  O   ILE A 263      52.703  15.987  49.179  1.00  9.02           O  
ATOM   2070  CB  ILE A 263      55.096  17.671  49.019  1.00 11.24           C  
ATOM   2071  CG1 ILE A 263      56.557  18.112  49.079  1.00 13.75           C  
ATOM   2072  CG2 ILE A 263      54.187  18.877  49.277  1.00 10.70           C  
ATOM   2073  CD1 ILE A 263      56.996  18.785  47.886  1.00 17.45           C  
ATOM   2074  N   PHE A 264      52.833  16.413  51.405  1.00  8.81           N  
ATOM   2075  CA  PHE A 264      51.417  16.149  51.669  1.00 10.02           C  
ATOM   2076  C   PHE A 264      50.699  17.425  52.140  1.00 10.18           C  
ATOM   2077  O   PHE A 264      51.022  17.976  53.197  1.00 10.64           O  
ATOM   2078  CB  PHE A 264      51.229  15.065  52.763  1.00  9.92           C  
ATOM   2079  CG  PHE A 264      51.630  13.652  52.351  1.00  9.72           C  
ATOM   2080  CD1 PHE A 264      52.133  12.769  53.318  1.00 10.39           C  
ATOM   2081  CD2 PHE A 264      51.501  13.201  51.032  1.00  9.66           C  
ATOM   2082  CE1 PHE A 264      52.506  11.458  52.976  1.00 11.20           C  
ATOM   2083  CE2 PHE A 264      51.866  11.890  50.670  1.00  8.57           C  
ATOM   2084  CZ  PHE A 264      52.369  11.021  51.648  1.00 10.64           C  
ATOM   2085  N   THR A 265      49.722  17.882  51.358  1.00  9.81           N  
ATOM   2086  CA  THR A 265      48.950  19.070  51.731  1.00  9.75           C  
ATOM   2087  C   THR A 265      47.815  18.653  52.689  1.00 10.55           C  
ATOM   2088  O   THR A 265      47.411  17.471  52.735  1.00 10.36           O  
ATOM   2089  CB  THR A 265      48.353  19.762  50.495  1.00  9.22           C  
ATOM   2090  OG1 THR A 265      47.506  18.836  49.808  1.00 10.94           O  
ATOM   2091  CG2 THR A 265      49.454  20.266  49.539  1.00  8.61           C  
ATOM   2092  N   GLN A 266      47.325  19.605  53.475  1.00  8.81           N  
ATOM   2093  CA  GLN A 266      46.269  19.329  54.440  1.00  8.62           C  
ATOM   2094  C   GLN A 266      45.147  20.391  54.424  1.00  8.99           C  
ATOM   2095  O   GLN A 266      44.600  20.743  55.486  1.00  9.55           O  
ATOM   2096  CB  GLN A 266      46.849  19.223  55.854  1.00  9.17           C  
ATOM   2097  CG  GLN A 266      47.882  18.135  56.098  1.00 10.18           C  
ATOM   2098  CD  GLN A 266      48.219  18.014  57.593  1.00 12.61           C  
ATOM   2099  OE1 GLN A 266      48.942  18.854  58.167  1.00 13.18           O  
ATOM   2100  NE2 GLN A 266      47.642  17.015  58.242  1.00 11.31           N  
ATOM   2101  N   GLY A 267      44.776  20.847  53.228  1.00  8.90           N  
ATOM   2102  CA  GLY A 267      43.719  21.851  53.101  1.00  9.70           C  
ATOM   2103  C   GLY A 267      44.131  23.194  53.687  1.00 10.07           C  
ATOM   2104  O   GLY A 267      45.096  23.799  53.216  1.00 10.79           O  
ATOM   2105  N   ARG A 268      43.379  23.684  54.679  1.00 10.42           N  
ATOM   2106  CA  ARG A 268      43.746  24.943  55.348  1.00 10.78           C  
ATOM   2107  C   ARG A 268      44.837  24.682  56.412  1.00 11.02           C  
ATOM   2108  O   ARG A 268      45.398  25.631  56.957  1.00  9.98           O  
ATOM   2109  CB  ARG A 268      42.536  25.615  55.995  1.00 11.49           C  
ATOM   2110  CG  ARG A 268      42.039  24.908  57.238  1.00 14.51           C  
ATOM   2111  CD  ARG A 268      40.728  25.567  57.778  1.00 15.80           C  
ATOM   2112  NE  ARG A 268      40.924  26.994  58.042  1.00 16.90           N  
ATOM   2113  CZ  ARG A 268      39.994  27.821  58.505  1.00 17.38           C  
ATOM   2114  NH1 ARG A 268      38.772  27.367  58.759  1.00 17.23           N  
ATOM   2115  NH2 ARG A 268      40.298  29.095  58.730  1.00 17.39           N  
ATOM   2116  N   ASP A 269      45.109  23.406  56.741  1.00 11.10           N  
ATOM   2117  CA  ASP A 269      46.172  23.069  57.699  1.00 11.51           C  
ATOM   2118  C   ASP A 269      47.552  22.984  57.001  1.00 10.99           C  
ATOM   2119  O   ASP A 269      47.634  22.988  55.756  1.00  9.92           O  
ATOM   2120  CB  ASP A 269      45.852  21.793  58.478  1.00 16.18           C  
ATOM   2121  CG  ASP A 269      44.712  21.988  59.467  1.00 24.06           C  
ATOM   2122  OD1 ASP A 269      44.907  22.676  60.496  1.00 28.96           O  
ATOM   2123  OD2 ASP A 269      43.607  21.463  59.216  1.00 29.04           O  
ATOM   2124  N   ASP A 270      48.619  22.901  57.805  1.00 10.42           N  
ATOM   2125  CA  ASP A 270      49.992  22.905  57.293  1.00 10.43           C  
ATOM   2126  C   ASP A 270      50.382  21.887  56.223  1.00 10.60           C  
ATOM   2127  O   ASP A 270      49.982  20.714  56.293  1.00 10.65           O  
ATOM   2128  CB  ASP A 270      50.992  22.748  58.444  1.00 11.14           C  
ATOM   2129  CG  ASP A 270      50.927  23.891  59.466  1.00 14.67           C  
ATOM   2130  OD1 ASP A 270      50.104  24.827  59.330  1.00 14.67           O  
ATOM   2131  OD2 ASP A 270      51.699  23.834  60.446  1.00 15.73           O  
ATOM   2132  N   THR A 271      51.143  22.346  55.223  1.00  9.57           N  
ATOM   2133  CA  THR A 271      51.690  21.460  54.185  1.00  9.25           C  
ATOM   2134  C   THR A 271      52.921  20.757  54.832  1.00 10.40           C  
ATOM   2135  O   THR A 271      53.755  21.417  55.471  1.00 10.40           O  
ATOM   2136  CB  THR A 271      52.106  22.256  52.955  1.00  9.66           C  
ATOM   2137  OG1 THR A 271      50.940  22.833  52.360  1.00  8.74           O  
ATOM   2138  CG2 THR A 271      52.802  21.361  51.916  1.00  9.15           C  
ATOM   2139  N   ILE A 272      52.982  19.422  54.723  1.00  9.92           N  
ATOM   2140  CA  ILE A 272      54.057  18.603  55.308  1.00  9.71           C  
ATOM   2141  C   ILE A 272      55.097  18.165  54.276  1.00 10.80           C  
ATOM   2142  O   ILE A 272      54.736  17.644  53.218  1.00 11.24           O  
ATOM   2143  CB  ILE A 272      53.453  17.324  55.988  1.00  9.75           C  
ATOM   2144  CG1 ILE A 272      52.382  17.714  57.031  1.00 10.55           C  
ATOM   2145  CG2 ILE A 272      54.550  16.454  56.593  1.00 12.03           C  
ATOM   2146  CD1 ILE A 272      52.885  18.600  58.166  1.00 11.76           C  
ATOM   2147  N   MET A 273      56.389  18.369  54.580  1.00 10.19           N  
ATOM   2148  CA  MET A 273      57.465  17.946  53.680  1.00 11.10           C  
ATOM   2149  C   MET A 273      58.469  17.019  54.374  1.00 11.64           C  
ATOM   2150  O   MET A 273      59.040  17.371  55.412  1.00 12.72           O  
ATOM   2151  CB  MET A 273      58.232  19.143  53.080  1.00 11.34           C  
ATOM   2152  CG  MET A 273      59.338  18.714  52.138  1.00 13.12           C  
ATOM   2153  SD  MET A 273      60.232  20.042  51.252  1.00 16.70           S  
ATOM   2154  CE  MET A 273      61.172  20.806  52.661  1.00 15.11           C  
ATOM   2155  N   ALA A 274      58.662  15.835  53.801  1.00 10.95           N  
ATOM   2156  CA  ALA A 274      59.624  14.871  54.316  1.00 11.25           C  
ATOM   2157  C   ALA A 274      60.803  14.744  53.374  1.00 11.26           C  
ATOM   2158  O   ALA A 274      60.638  14.599  52.153  1.00 10.88           O  
ATOM   2159  CB  ALA A 274      58.971  13.483  54.489  1.00 11.57           C  
ATOM   2160  N   THR A 275      62.000  14.850  53.944  1.00 13.79           N  
ATOM   2161  CA  THR A 275      63.233  14.665  53.182  1.00 15.99           C  
ATOM   2162  C   THR A 275      64.021  13.525  53.881  1.00 17.87           C  
ATOM   2163  O   THR A 275      63.535  12.908  54.835  1.00 16.18           O  
ATOM   2164  CB  THR A 275      64.099  15.971  53.106  1.00 15.88           C  
ATOM   2165  OG1 THR A 275      64.475  16.375  54.431  1.00 16.91           O  
ATOM   2166  CG2 THR A 275      63.330  17.103  52.386  1.00 14.17           C  
ATOM   2167  N   GLU A 276      65.214  13.232  53.378  1.00 19.52           N  
ATOM   2168  CA  GLU A 276      66.038  12.186  53.939  1.00 22.91           C  
ATOM   2169  C   GLU A 276      66.316  12.400  55.423  1.00 23.43           C  
ATOM   2170  O   GLU A 276      66.220  11.466  56.206  1.00 23.47           O  
ATOM   2171  CB  GLU A 276      67.348  12.136  53.155  1.00 25.74           C  
ATOM   2172  CG  GLU A 276      68.445  11.313  53.785  1.00 31.61           C  
ATOM   2173  CD  GLU A 276      69.800  11.563  53.114  1.00 37.24           C  
ATOM   2174  OE1 GLU A 276      70.685  10.675  53.245  1.00 40.95           O  
ATOM   2175  OE2 GLU A 276      69.975  12.623  52.435  1.00 38.62           O  
ATOM   2176  N   SER A 277      66.532  13.656  55.813  1.00 24.69           N  
ATOM   2177  CA  SER A 277      66.880  14.009  57.197  1.00 26.38           C  
ATOM   2178  C   SER A 277      65.811  14.400  58.218  1.00 24.89           C  
ATOM   2179  O   SER A 277      66.028  14.222  59.425  1.00 24.19           O  
ATOM   2180  CB  SER A 277      67.975  15.097  57.185  1.00 28.90           C  
ATOM   2181  OG  SER A 277      67.544  16.269  56.488  1.00 33.00           O  
ATOM   2182  N   GLU A 278      64.678  14.936  57.756  1.00 23.00           N  
ATOM   2183  CA  GLU A 278      63.608  15.373  58.663  1.00 21.11           C  
ATOM   2184  C   GLU A 278      62.264  15.600  57.973  1.00 18.78           C  
ATOM   2185  O   GLU A 278      62.136  15.503  56.759  1.00 17.21           O  
ATOM   2186  CB  GLU A 278      63.996  16.707  59.283  1.00 24.55           C  
ATOM   2187  CG  GLU A 278      64.086  17.769  58.218  1.00 29.16           C  
ATOM   2188  CD  GLU A 278      64.805  19.012  58.659  1.00 34.81           C  
ATOM   2189  OE1 GLU A 278      64.677  19.424  59.850  1.00 36.28           O  
ATOM   2190  OE2 GLU A 278      65.504  19.580  57.783  1.00 36.61           O  
ATOM   2191  N   VAL A 279      61.273  15.913  58.795  1.00 17.06           N  
ATOM   2192  CA  VAL A 279      59.933  16.226  58.338  1.00 16.54           C  
ATOM   2193  C   VAL A 279      59.639  17.629  58.893  1.00 17.22           C  
ATOM   2194  O   VAL A 279      59.735  17.854  60.111  1.00 18.60           O  
ATOM   2195  CB  VAL A 279      58.920  15.240  58.892  1.00 13.56           C  
ATOM   2196  CG1 VAL A 279      57.487  15.652  58.489  1.00 13.84           C  
ATOM   2197  CG2 VAL A 279      59.245  13.846  58.379  1.00 15.16           C  
ATOM   2198  N   THR A 280      59.318  18.565  58.004  1.00 17.32           N  
ATOM   2199  CA  THR A 280      59.023  19.949  58.396  1.00 18.20           C  
ATOM   2200  C   THR A 280      57.605  20.389  57.944  1.00 16.89           C  
ATOM   2201  O   THR A 280      57.015  19.779  57.051  1.00 16.66           O  
ATOM   2202  CB  THR A 280      60.118  20.925  57.850  1.00 19.71           C  
ATOM   2203  OG1 THR A 280      60.162  20.862  56.424  1.00 23.22           O  
ATOM   2204  CG2 THR A 280      61.509  20.543  58.371  1.00 21.64           C  
ATOM   2205  N   ALA A 281      57.060  21.437  58.579  1.00 14.97           N  
ATOM   2206  CA  ALA A 281      55.701  21.948  58.280  1.00 12.85           C  
ATOM   2207  C   ALA A 281      55.691  23.383  57.774  1.00 12.32           C  
ATOM   2208  O   ALA A 281      56.477  24.208  58.245  1.00 12.84           O  
ATOM   2209  CB  ALA A 281      54.844  21.843  59.518  1.00 13.46           C  
ATOM   2210  N   PHE A 282      54.821  23.679  56.803  1.00 11.13           N  
ATOM   2211  CA  PHE A 282      54.689  25.030  56.204  1.00  9.66           C  
ATOM   2212  C   PHE A 282      53.236  25.524  56.330  1.00 10.46           C  
ATOM   2213  O   PHE A 282      52.313  24.954  55.714  1.00  9.49           O  
ATOM   2214  CB  PHE A 282      55.086  25.040  54.714  1.00  9.57           C  
ATOM   2215  CG  PHE A 282      56.549  24.768  54.466  1.00 13.27           C  
ATOM   2216  CD1 PHE A 282      57.048  23.465  54.511  1.00 14.19           C  
ATOM   2217  CD2 PHE A 282      57.434  25.820  54.202  1.00 14.56           C  
ATOM   2218  CE1 PHE A 282      58.416  23.203  54.297  1.00 15.62           C  
ATOM   2219  CE2 PHE A 282      58.799  25.580  53.987  1.00 16.84           C  
ATOM   2220  CZ  PHE A 282      59.292  24.265  54.035  1.00 15.48           C  
ATOM   2221  N   ALA A 283      53.037  26.593  57.095  1.00  9.39           N  
ATOM   2222  CA  ALA A 283      51.704  27.147  57.270  1.00  9.24           C  
ATOM   2223  C   ALA A 283      51.057  27.684  55.997  1.00  9.53           C  
ATOM   2224  O   ALA A 283      51.726  28.200  55.096  1.00  9.37           O  
ATOM   2225  CB  ALA A 283      51.734  28.245  58.318  1.00  8.82           C  
ATOM   2226  N   VAL A 284      49.737  27.506  55.893  1.00 10.13           N  
ATOM   2227  CA  VAL A 284      48.974  28.070  54.770  1.00 10.09           C  
ATOM   2228  C   VAL A 284      48.561  29.431  55.375  1.00 10.50           C  
ATOM   2229  O   VAL A 284      47.738  29.492  56.283  1.00 10.06           O  
ATOM   2230  CB  VAL A 284      47.721  27.205  54.414  1.00  9.63           C  
ATOM   2231  CG1 VAL A 284      46.869  27.919  53.353  1.00  9.25           C  
ATOM   2232  CG2 VAL A 284      48.180  25.823  53.857  1.00  9.29           C  
ATOM   2233  N   LEU A 285      49.192  30.507  54.916  1.00 10.69           N  
ATOM   2234  CA  LEU A 285      48.910  31.843  55.454  1.00 11.75           C  
ATOM   2235  C   LEU A 285      47.616  32.530  54.967  1.00 13.06           C  
ATOM   2236  O   LEU A 285      47.110  33.442  55.622  1.00 12.99           O  
ATOM   2237  CB  LEU A 285      50.164  32.732  55.298  1.00 11.91           C  
ATOM   2238  CG  LEU A 285      51.412  32.171  56.023  1.00 12.42           C  
ATOM   2239  CD1 LEU A 285      52.625  32.995  55.694  1.00 12.54           C  
ATOM   2240  CD2 LEU A 285      51.216  32.107  57.528  1.00  9.87           C  
ATOM   2241  N   ASP A 286      47.068  32.053  53.849  1.00 13.86           N  
ATOM   2242  CA  ASP A 286      45.819  32.555  53.269  1.00 14.90           C  
ATOM   2243  C   ASP A 286      44.663  31.791  53.930  1.00 14.75           C  
ATOM   2244  O   ASP A 286      44.186  30.791  53.384  1.00 14.77           O  
ATOM   2245  CB  ASP A 286      45.822  32.284  51.755  1.00 18.65           C  
ATOM   2246  CG  ASP A 286      44.463  32.529  51.101  1.00 23.46           C  
ATOM   2247  OD1 ASP A 286      43.727  33.433  51.582  1.00 25.71           O  
ATOM   2248  OD2 ASP A 286      44.135  31.823  50.104  1.00 24.00           O  
ATOM   2249  N   GLN A 287      44.190  32.293  55.068  1.00 13.32           N  
ATOM   2250  CA  GLN A 287      43.127  31.633  55.829  1.00 13.78           C  
ATOM   2251  C   GLN A 287      41.652  32.052  55.628  1.00 15.14           C  
ATOM   2252  O   GLN A 287      40.753  31.475  56.238  1.00 15.05           O  
ATOM   2253  CB  GLN A 287      43.472  31.704  57.300  1.00 12.11           C  
ATOM   2254  CG  GLN A 287      44.663  30.828  57.682  1.00 13.25           C  
ATOM   2255  CD  GLN A 287      44.366  29.328  57.554  1.00 14.20           C  
ATOM   2256  OE1 GLN A 287      45.194  28.556  57.048  1.00 13.85           O  
ATOM   2257  NE2 GLN A 287      43.191  28.913  58.025  1.00 12.12           N  
ATOM   2258  N   ASP A 288      41.410  33.027  54.764  1.00 17.56           N  
ATOM   2259  CA  ASP A 288      40.056  33.526  54.491  1.00 20.67           C  
ATOM   2260  C   ASP A 288      39.248  32.459  53.735  1.00 19.10           C  
ATOM   2261  O   ASP A 288      39.566  32.179  52.586  1.00 20.83           O  
ATOM   2262  CB  ASP A 288      40.157  34.780  53.617  1.00 25.51           C  
ATOM   2263  CG  ASP A 288      41.403  35.623  53.921  1.00 33.82           C  
ATOM   2264  OD1 ASP A 288      41.232  36.706  54.562  1.00 37.90           O  
ATOM   2265  OD2 ASP A 288      42.544  35.216  53.505  1.00 34.69           O  
ATOM   2266  N   GLN A 289      38.188  31.911  54.344  1.00 16.88           N  
ATOM   2267  CA  GLN A 289      37.354  30.843  53.710  1.00 14.70           C  
ATOM   2268  C   GLN A 289      36.191  31.331  52.847  1.00 13.89           C  
ATOM   2269  O   GLN A 289      35.679  30.588  51.998  1.00 12.38           O  
ATOM   2270  CB  GLN A 289      36.729  29.933  54.780  1.00 12.75           C  
ATOM   2271  CG  GLN A 289      37.710  29.325  55.778  1.00 13.51           C  
ATOM   2272  CD  GLN A 289      38.703  28.389  55.102  1.00 14.98           C  
ATOM   2273  OE1 GLN A 289      38.340  27.308  54.634  1.00 13.28           O  
ATOM   2274  NE2 GLN A 289      39.959  28.826  55.012  1.00 12.80           N  
ATOM   2275  N   LYS A 290      35.792  32.585  53.043  1.00 13.77           N  
ATOM   2276  CA  LYS A 290      34.636  33.121  52.343  1.00 14.09           C  
ATOM   2277  C   LYS A 290      34.504  32.947  50.847  1.00 13.05           C  
ATOM   2278  O   LYS A 290      33.463  32.486  50.382  1.00 11.67           O  
ATOM   2279  CB  LYS A 290      34.360  34.557  52.797  1.00 17.51           C  
ATOM   2280  CG  LYS A 290      33.779  34.572  54.221  1.00 20.06           C  
ATOM   2281  CD  LYS A 290      33.511  35.972  54.745  1.00 22.77           C  
ATOM   2282  CE  LYS A 290      32.877  35.935  56.152  1.00 24.25           C  
ATOM   2283  NZ  LYS A 290      33.677  35.203  57.192  1.00 25.90           N  
ATOM   2284  N   GLU A 291      35.573  33.189  50.097  1.00 12.69           N  
ATOM   2285  CA  GLU A 291      35.517  33.078  48.648  1.00 13.33           C  
ATOM   2286  C   GLU A 291      35.970  31.751  48.021  1.00 12.27           C  
ATOM   2287  O   GLU A 291      36.109  31.661  46.793  1.00 11.50           O  
ATOM   2288  CB  GLU A 291      36.297  34.223  48.013  1.00 18.18           C  
ATOM   2289  CG  GLU A 291      35.766  35.615  48.346  1.00 25.10           C  
ATOM   2290  CD  GLU A 291      36.602  36.708  47.695  1.00 30.59           C  
ATOM   2291  OE1 GLU A 291      37.770  36.908  48.132  1.00 32.57           O  
ATOM   2292  OE2 GLU A 291      36.098  37.340  46.727  1.00 34.27           O  
ATOM   2293  N   ILE A 292      36.139  30.713  48.839  1.00 11.31           N  
ATOM   2294  CA  ILE A 292      36.566  29.412  48.319  1.00 10.98           C  
ATOM   2295  C   ILE A 292      35.516  28.789  47.366  1.00 11.00           C  
ATOM   2296  O   ILE A 292      34.322  28.706  47.691  1.00 11.30           O  
ATOM   2297  CB  ILE A 292      36.879  28.435  49.492  1.00 10.04           C  
ATOM   2298  CG1 ILE A 292      38.096  28.915  50.284  1.00  9.30           C  
ATOM   2299  CG2 ILE A 292      37.151  27.033  48.970  1.00  9.22           C  
ATOM   2300  CD1 ILE A 292      38.410  28.021  51.449  1.00 10.95           C  
ATOM   2301  N   ILE A 293      35.992  28.337  46.209  1.00 11.52           N  
ATOM   2302  CA  ILE A 293      35.168  27.699  45.171  1.00 12.61           C  
ATOM   2303  C   ILE A 293      35.541  26.245  44.777  1.00 13.92           C  
ATOM   2304  O   ILE A 293      34.673  25.381  44.747  1.00 14.63           O  
ATOM   2305  CB  ILE A 293      35.208  28.526  43.867  1.00 13.14           C  
ATOM   2306  CG1 ILE A 293      34.620  29.910  44.090  1.00 13.12           C  
ATOM   2307  CG2 ILE A 293      34.482  27.792  42.760  1.00 15.16           C  
ATOM   2308  CD1 ILE A 293      33.168  29.905  44.457  1.00 15.11           C  
ATOM   2309  N   ASP A 294      36.825  25.976  44.494  1.00 13.69           N  
ATOM   2310  CA  ASP A 294      37.278  24.657  43.995  1.00 13.06           C  
ATOM   2311  C   ASP A 294      38.567  24.127  44.637  1.00 13.31           C  
ATOM   2312  O   ASP A 294      39.682  24.415  44.156  1.00 11.96           O  
ATOM   2313  CB  ASP A 294      37.489  24.801  42.478  1.00 15.29           C  
ATOM   2314  CG  ASP A 294      37.885  23.491  41.770  1.00 17.92           C  
ATOM   2315  OD1 ASP A 294      37.858  22.401  42.379  1.00 16.93           O  
ATOM   2316  OD2 ASP A 294      38.199  23.572  40.551  1.00 20.35           O  
ATOM   2317  N   THR A 295      38.422  23.300  45.671  1.00 12.68           N  
ATOM   2318  CA  THR A 295      39.598  22.748  46.338  1.00 13.94           C  
ATOM   2319  C   THR A 295      40.343  21.673  45.549  1.00 13.07           C  
ATOM   2320  O   THR A 295      41.554  21.498  45.747  1.00 11.75           O  
ATOM   2321  CB  THR A 295      39.297  22.253  47.754  1.00 15.63           C  
ATOM   2322  OG1 THR A 295      38.345  21.201  47.686  1.00 20.82           O  
ATOM   2323  CG2 THR A 295      38.723  23.377  48.600  1.00 19.57           C  
ATOM   2324  N   ASN A 296      39.658  20.974  44.640  1.00 11.89           N  
ATOM   2325  CA  ASN A 296      40.338  19.952  43.830  1.00 11.84           C  
ATOM   2326  C   ASN A 296      41.329  20.643  42.889  1.00 11.03           C  
ATOM   2327  O   ASN A 296      42.479  20.249  42.804  1.00 10.49           O  
ATOM   2328  CB  ASN A 296      39.346  19.116  43.000  1.00 13.20           C  
ATOM   2329  CG  ASN A 296      38.478  18.230  43.853  1.00 16.77           C  
ATOM   2330  OD1 ASN A 296      38.971  17.390  44.607  1.00 18.76           O  
ATOM   2331  ND2 ASN A 296      37.175  18.411  43.741  1.00 17.96           N  
ATOM   2332  N   GLY A 297      40.860  21.674  42.188  1.00 10.87           N  
ATOM   2333  CA  GLY A 297      41.705  22.446  41.284  1.00  9.38           C  
ATOM   2334  C   GLY A 297      42.814  23.151  42.062  1.00  9.49           C  
ATOM   2335  O   GLY A 297      43.911  23.322  41.535  1.00  9.30           O  
ATOM   2336  N   ALA A 298      42.560  23.528  43.317  1.00  7.86           N  
ATOM   2337  CA  ALA A 298      43.608  24.153  44.133  1.00  8.21           C  
ATOM   2338  C   ALA A 298      44.813  23.177  44.295  1.00  8.00           C  
ATOM   2339  O   ALA A 298      45.968  23.613  44.313  1.00  8.51           O  
ATOM   2340  CB  ALA A 298      43.043  24.559  45.532  1.00  8.25           C  
ATOM   2341  N   GLY A 299      44.535  21.872  44.438  1.00  7.38           N  
ATOM   2342  CA  GLY A 299      45.589  20.872  44.572  1.00  6.01           C  
ATOM   2343  C   GLY A 299      46.390  20.781  43.272  1.00  7.18           C  
ATOM   2344  O   GLY A 299      47.619  20.648  43.301  1.00  7.86           O  
ATOM   2345  N   ASP A 300      45.717  20.836  42.122  1.00  6.09           N  
ATOM   2346  CA  ASP A 300      46.446  20.808  40.836  1.00  6.75           C  
ATOM   2347  C   ASP A 300      47.317  22.081  40.692  1.00  7.65           C  
ATOM   2348  O   ASP A 300      48.453  22.018  40.198  1.00  8.16           O  
ATOM   2349  CB  ASP A 300      45.487  20.710  39.647  1.00  6.74           C  
ATOM   2350  CG  ASP A 300      44.646  19.432  39.673  1.00  8.82           C  
ATOM   2351  OD1 ASP A 300      45.037  18.407  40.308  1.00  9.91           O  
ATOM   2352  OD2 ASP A 300      43.589  19.445  39.014  1.00 10.88           O  
ATOM   2353  N   ALA A 301      46.779  23.228  41.116  1.00  7.06           N  
ATOM   2354  CA  ALA A 301      47.507  24.502  41.048  1.00  7.47           C  
ATOM   2355  C   ALA A 301      48.716  24.515  42.014  1.00  7.66           C  
ATOM   2356  O   ALA A 301      49.735  25.135  41.706  1.00  8.43           O  
ATOM   2357  CB  ALA A 301      46.549  25.676  41.347  1.00  7.10           C  
ATOM   2358  N   PHE A 302      48.601  23.863  43.172  1.00  6.67           N  
ATOM   2359  CA  PHE A 302      49.719  23.792  44.115  1.00  6.34           C  
ATOM   2360  C   PHE A 302      50.900  23.101  43.420  1.00  7.00           C  
ATOM   2361  O   PHE A 302      52.039  23.560  43.496  1.00  7.42           O  
ATOM   2362  CB  PHE A 302      49.341  23.021  45.383  1.00  6.73           C  
ATOM   2363  CG  PHE A 302      50.512  22.792  46.314  1.00  7.98           C  
ATOM   2364  CD1 PHE A 302      50.883  23.757  47.243  1.00  7.66           C  
ATOM   2365  CD2 PHE A 302      51.288  21.636  46.201  1.00 10.44           C  
ATOM   2366  CE1 PHE A 302      52.030  23.587  48.058  1.00  7.40           C  
ATOM   2367  CE2 PHE A 302      52.433  21.436  47.005  1.00  9.81           C  
ATOM   2368  CZ  PHE A 302      52.809  22.410  47.934  1.00  8.54           C  
ATOM   2369  N   VAL A 303      50.627  21.989  42.747  1.00  7.58           N  
ATOM   2370  CA  VAL A 303      51.683  21.277  42.033  1.00  8.09           C  
ATOM   2371  C   VAL A 303      52.250  22.127  40.890  1.00  7.22           C  
ATOM   2372  O   VAL A 303      53.457  22.185  40.732  1.00  8.63           O  
ATOM   2373  CB  VAL A 303      51.194  19.895  41.521  1.00  8.98           C  
ATOM   2374  CG1 VAL A 303      52.275  19.241  40.628  1.00 10.29           C  
ATOM   2375  CG2 VAL A 303      50.890  18.996  42.724  1.00  9.44           C  
ATOM   2376  N   GLY A 304      51.398  22.815  40.133  1.00  7.04           N  
ATOM   2377  CA  GLY A 304      51.876  23.657  39.041  1.00  8.07           C  
ATOM   2378  C   GLY A 304      52.836  24.761  39.547  1.00  7.72           C  
ATOM   2379  O   GLY A 304      53.886  25.040  38.937  1.00  9.20           O  
ATOM   2380  N   GLY A 305      52.490  25.387  40.669  1.00  8.29           N  
ATOM   2381  CA  GLY A 305      53.353  26.420  41.236  1.00  8.38           C  
ATOM   2382  C   GLY A 305      54.682  25.839  41.695  1.00  9.25           C  
ATOM   2383  O   GLY A 305      55.745  26.399  41.412  1.00  9.47           O  
ATOM   2384  N   PHE A 306      54.633  24.711  42.399  1.00  8.61           N  
ATOM   2385  CA  PHE A 306      55.842  24.041  42.880  1.00  7.60           C  
ATOM   2386  C   PHE A 306      56.767  23.704  41.691  1.00  9.50           C  
ATOM   2387  O   PHE A 306      57.958  24.052  41.708  1.00  9.78           O  
ATOM   2388  CB  PHE A 306      55.444  22.772  43.639  1.00  7.12           C  
ATOM   2389  CG  PHE A 306      56.557  22.139  44.391  1.00  6.66           C  
ATOM   2390  CD1 PHE A 306      56.616  22.240  45.779  1.00  7.18           C  
ATOM   2391  CD2 PHE A 306      57.542  21.390  43.723  1.00  8.49           C  
ATOM   2392  CE1 PHE A 306      57.650  21.593  46.503  1.00  8.90           C  
ATOM   2393  CE2 PHE A 306      58.568  20.746  44.443  1.00  8.43           C  
ATOM   2394  CZ  PHE A 306      58.620  20.849  45.821  1.00  7.87           C  
ATOM   2395  N   LEU A 307      56.223  23.056  40.653  1.00  8.61           N  
ATOM   2396  CA  LEU A 307      57.003  22.702  39.449  1.00 10.16           C  
ATOM   2397  C   LEU A 307      57.656  23.922  38.716  1.00 10.46           C  
ATOM   2398  O   LEU A 307      58.751  23.787  38.145  1.00 10.92           O  
ATOM   2399  CB  LEU A 307      56.121  21.939  38.448  1.00 10.42           C  
ATOM   2400  CG  LEU A 307      55.556  20.562  38.855  1.00 11.71           C  
ATOM   2401  CD1 LEU A 307      54.589  20.086  37.764  1.00 11.94           C  
ATOM   2402  CD2 LEU A 307      56.662  19.534  39.103  1.00 11.54           C  
ATOM   2403  N   SER A 308      56.978  25.081  38.705  1.00  9.88           N  
ATOM   2404  CA  SER A 308      57.499  26.275  38.028  1.00 10.37           C  
ATOM   2405  C   SER A 308      58.814  26.750  38.636  1.00 10.36           C  
ATOM   2406  O   SER A 308      59.639  27.330  37.925  1.00 11.81           O  
ATOM   2407  CB  SER A 308      56.472  27.430  38.010  1.00 10.94           C  
ATOM   2408  OG  SER A 308      56.324  28.053  39.280  1.00 11.01           O  
ATOM   2409  N   GLN A 309      59.005  26.488  39.928  1.00  9.11           N  
ATOM   2410  CA  GLN A 309      60.229  26.883  40.623  1.00 10.90           C  
ATOM   2411  C   GLN A 309      61.325  25.782  40.603  1.00 13.10           C  
ATOM   2412  O   GLN A 309      62.544  26.074  40.642  1.00 12.72           O  
ATOM   2413  CB  GLN A 309      59.917  27.349  42.049  1.00 10.01           C  
ATOM   2414  CG  GLN A 309      58.901  28.509  42.135  1.00 12.60           C  
ATOM   2415  CD  GLN A 309      59.202  29.674  41.189  1.00 13.59           C  
ATOM   2416  OE1 GLN A 309      58.406  30.021  40.302  1.00 15.13           O  
ATOM   2417  NE2 GLN A 309      60.359  30.280  41.371  1.00 13.39           N  
ATOM   2418  N   LEU A 310      60.901  24.519  40.541  1.00 13.37           N  
ATOM   2419  CA  LEU A 310      61.825  23.389  40.455  1.00 15.23           C  
ATOM   2420  C   LEU A 310      62.605  23.497  39.118  1.00 15.74           C  
ATOM   2421  O   LEU A 310      63.826  23.279  39.086  1.00 15.59           O  
ATOM   2422  CB  LEU A 310      61.021  22.078  40.515  1.00 16.88           C  
ATOM   2423  CG  LEU A 310      61.623  20.757  40.978  1.00 18.92           C  
ATOM   2424  CD1 LEU A 310      62.221  20.877  42.377  1.00 17.63           C  
ATOM   2425  CD2 LEU A 310      60.483  19.745  40.980  1.00 20.38           C  
ATOM   2426  N   VAL A 311      61.947  23.903  38.029  1.00 15.41           N  
ATOM   2427  CA  VAL A 311      62.686  24.021  36.770  1.00 17.24           C  
ATOM   2428  C   VAL A 311      63.582  25.252  36.694  1.00 19.39           C  
ATOM   2429  O   VAL A 311      64.435  25.333  35.810  1.00 20.83           O  
ATOM   2430  CB  VAL A 311      61.802  23.946  35.506  1.00 16.55           C  
ATOM   2431  CG1 VAL A 311      61.175  22.577  35.389  1.00 18.15           C  
ATOM   2432  CG2 VAL A 311      60.779  25.037  35.496  1.00 15.03           C  
ATOM   2433  N   SER A 312      63.381  26.204  37.609  1.00 19.67           N  
ATOM   2434  CA  SER A 312      64.175  27.443  37.663  1.00 21.09           C  
ATOM   2435  C   SER A 312      65.321  27.238  38.636  1.00 20.89           C  
ATOM   2436  O   SER A 312      66.045  28.180  38.956  1.00 22.64           O  
ATOM   2437  CB  SER A 312      63.336  28.631  38.170  1.00 21.32           C  
ATOM   2438  OG  SER A 312      62.103  28.751  37.468  1.00 26.34           O  
ATOM   2439  N   ASP A 313      65.394  26.034  39.192  1.00 19.80           N  
ATOM   2440  CA  ASP A 313      66.432  25.645  40.138  1.00 19.38           C  
ATOM   2441  C   ASP A 313      66.399  26.418  41.449  1.00 17.01           C  
ATOM   2442  O   ASP A 313      67.433  26.894  41.919  1.00 18.24           O  
ATOM   2443  CB  ASP A 313      67.810  25.786  39.480  1.00 22.66           C  
ATOM   2444  CG  ASP A 313      68.898  25.082  40.261  1.00 27.26           C  
ATOM   2445  OD1 ASP A 313      68.566  24.197  41.101  1.00 29.06           O  
ATOM   2446  OD2 ASP A 313      70.085  25.423  40.032  1.00 29.03           O  
ATOM   2447  N   LYS A 314      65.226  26.517  42.060  1.00 12.94           N  
ATOM   2448  CA  LYS A 314      65.090  27.264  43.302  1.00 11.34           C  
ATOM   2449  C   LYS A 314      65.040  26.373  44.531  1.00 10.19           C  
ATOM   2450  O   LYS A 314      64.821  25.165  44.409  1.00 11.33           O  
ATOM   2451  CB  LYS A 314      63.819  28.135  43.250  1.00 11.90           C  
ATOM   2452  CG  LYS A 314      63.809  29.193  42.157  1.00 14.59           C  
ATOM   2453  CD  LYS A 314      64.883  30.235  42.404  1.00 16.07           C  
ATOM   2454  CE  LYS A 314      64.822  31.364  41.394  1.00 19.19           C  
ATOM   2455  NZ  LYS A 314      65.217  30.882  40.060  1.00 20.34           N  
ATOM   2456  N   PRO A 315      65.326  26.936  45.730  1.00  9.71           N  
ATOM   2457  CA  PRO A 315      65.276  26.123  46.948  1.00  9.25           C  
ATOM   2458  C   PRO A 315      63.848  25.582  47.168  1.00  8.68           C  
ATOM   2459  O   PRO A 315      62.864  26.159  46.648  1.00  8.38           O  
ATOM   2460  CB  PRO A 315      65.678  27.122  48.055  1.00  8.90           C  
ATOM   2461  CG  PRO A 315      66.576  28.073  47.352  1.00  8.76           C  
ATOM   2462  CD  PRO A 315      65.879  28.282  46.022  1.00  9.14           C  
ATOM   2463  N   LEU A 316      63.727  24.493  47.929  1.00  7.67           N  
ATOM   2464  CA  LEU A 316      62.406  23.916  48.206  1.00  8.16           C  
ATOM   2465  C   LEU A 316      61.451  24.907  48.913  1.00  8.29           C  
ATOM   2466  O   LEU A 316      60.243  24.870  48.690  1.00  7.79           O  
ATOM   2467  CB  LEU A 316      62.537  22.605  48.997  1.00  9.49           C  
ATOM   2468  CG  LEU A 316      63.169  21.426  48.220  1.00 10.56           C  
ATOM   2469  CD1 LEU A 316      63.550  20.337  49.222  1.00 10.53           C  
ATOM   2470  CD2 LEU A 316      62.228  20.881  47.106  1.00  9.31           C  
ATOM   2471  N   THR A 317      61.989  25.770  49.779  1.00  7.90           N  
ATOM   2472  CA  THR A 317      61.186  26.791  50.486  1.00  8.72           C  
ATOM   2473  C   THR A 317      60.426  27.668  49.459  1.00  8.97           C  
ATOM   2474  O   THR A 317      59.255  28.021  49.664  1.00  8.55           O  
ATOM   2475  CB  THR A 317      62.108  27.732  51.332  1.00  9.82           C  
ATOM   2476  OG1 THR A 317      63.146  28.257  50.489  1.00  9.68           O  
ATOM   2477  CG2 THR A 317      62.738  26.976  52.516  1.00 11.08           C  
ATOM   2478  N   GLU A 318      61.109  28.030  48.373  1.00  8.38           N  
ATOM   2479  CA  GLU A 318      60.525  28.849  47.316  1.00  9.60           C  
ATOM   2480  C   GLU A 318      59.516  28.049  46.481  1.00  9.80           C  
ATOM   2481  O   GLU A 318      58.519  28.611  46.017  1.00  9.61           O  
ATOM   2482  CB  GLU A 318      61.626  29.455  46.421  1.00  9.58           C  
ATOM   2483  CG  GLU A 318      61.143  30.508  45.397  1.00 10.45           C  
ATOM   2484  CD  GLU A 318      60.711  31.871  45.992  1.00 11.50           C  
ATOM   2485  OE1 GLU A 318      60.527  32.003  47.224  1.00 12.63           O  
ATOM   2486  OE2 GLU A 318      60.509  32.819  45.200  1.00 12.35           O  
ATOM   2487  N   CYS A 319      59.779  26.752  46.272  1.00  8.85           N  
ATOM   2488  CA  CYS A 319      58.848  25.898  45.531  1.00  8.25           C  
ATOM   2489  C   CYS A 319      57.512  25.825  46.316  1.00  8.02           C  
ATOM   2490  O   CYS A 319      56.415  25.912  45.728  1.00  8.44           O  
ATOM   2491  CB  CYS A 319      59.442  24.491  45.366  1.00  9.35           C  
ATOM   2492  SG  CYS A 319      60.925  24.428  44.287  1.00 11.88           S  
ATOM   2493  N   ILE A 320      57.612  25.683  47.643  1.00  7.72           N  
ATOM   2494  CA  ILE A 320      56.422  25.636  48.503  1.00  7.94           C  
ATOM   2495  C   ILE A 320      55.696  27.002  48.502  1.00  7.86           C  
ATOM   2496  O   ILE A 320      54.468  27.043  48.405  1.00  8.74           O  
ATOM   2497  CB  ILE A 320      56.791  25.178  49.935  1.00  9.65           C  
ATOM   2498  CG1 ILE A 320      57.238  23.708  49.896  1.00 11.40           C  
ATOM   2499  CG2 ILE A 320      55.610  25.347  50.890  1.00 10.27           C  
ATOM   2500  CD1 ILE A 320      57.851  23.220  51.141  1.00 15.69           C  
ATOM   2501  N   ARG A 321      56.431  28.119  48.565  1.00  7.47           N  
ATOM   2502  CA  ARG A 321      55.762  29.430  48.520  1.00  6.58           C  
ATOM   2503  C   ARG A 321      55.003  29.608  47.188  1.00  6.64           C  
ATOM   2504  O   ARG A 321      53.873  30.136  47.175  1.00  6.94           O  
ATOM   2505  CB  ARG A 321      56.769  30.588  48.714  1.00  8.83           C  
ATOM   2506  CG  ARG A 321      56.117  32.018  48.801  1.00  8.97           C  
ATOM   2507  CD  ARG A 321      57.123  33.158  49.059  1.00 10.02           C  
ATOM   2508  NE  ARG A 321      57.932  33.507  47.888  1.00 12.31           N  
ATOM   2509  CZ  ARG A 321      57.699  34.535  47.064  1.00 13.61           C  
ATOM   2510  NH1 ARG A 321      56.651  35.333  47.261  1.00 15.58           N  
ATOM   2511  NH2 ARG A 321      58.547  34.807  46.070  1.00 12.49           N  
ATOM   2512  N   ALA A 322      55.612  29.189  46.070  1.00  5.90           N  
ATOM   2513  CA  ALA A 322      54.964  29.295  44.759  1.00  6.26           C  
ATOM   2514  C   ALA A 322      53.707  28.411  44.690  1.00  7.63           C  
ATOM   2515  O   ALA A 322      52.697  28.803  44.103  1.00  7.95           O  
ATOM   2516  CB  ALA A 322      55.937  28.935  43.650  1.00  6.81           C  
ATOM   2517  N   GLY A 323      53.770  27.222  45.299  1.00  7.21           N  
ATOM   2518  CA  GLY A 323      52.625  26.325  45.329  1.00  6.81           C  
ATOM   2519  C   GLY A 323      51.482  26.941  46.132  1.00  6.37           C  
ATOM   2520  O   GLY A 323      50.329  26.904  45.693  1.00  7.40           O  
ATOM   2521  N   HIS A 324      51.782  27.489  47.305  1.00  7.00           N  
ATOM   2522  CA  HIS A 324      50.738  28.129  48.117  1.00  6.72           C  
ATOM   2523  C   HIS A 324      50.151  29.359  47.371  1.00  7.55           C  
ATOM   2524  O   HIS A 324      48.933  29.599  47.410  1.00  7.70           O  
ATOM   2525  CB  HIS A 324      51.282  28.537  49.495  1.00  8.05           C  
ATOM   2526  CG  HIS A 324      51.409  27.400  50.466  1.00  8.24           C  
ATOM   2527  ND1 HIS A 324      52.106  27.508  51.652  1.00 12.55           N  
ATOM   2528  CD2 HIS A 324      50.928  26.134  50.429  1.00  9.95           C  
ATOM   2529  CE1 HIS A 324      52.053  26.356  52.300  1.00 13.34           C  
ATOM   2530  NE2 HIS A 324      51.346  25.504  51.577  1.00 11.75           N  
ATOM   2531  N   TYR A 325      50.999  30.095  46.640  1.00  7.25           N  
ATOM   2532  CA  TYR A 325      50.527  31.273  45.906  1.00  7.35           C  
ATOM   2533  C   TYR A 325      49.548  30.868  44.795  1.00  6.77           C  
ATOM   2534  O   TYR A 325      48.426  31.388  44.713  1.00  8.17           O  
ATOM   2535  CB  TYR A 325      51.709  32.093  45.327  1.00  8.33           C  
ATOM   2536  CG  TYR A 325      51.259  33.220  44.392  1.00  9.11           C  
ATOM   2537  CD1 TYR A 325      50.754  34.426  44.892  1.00 10.60           C  
ATOM   2538  CD2 TYR A 325      51.273  33.045  42.997  1.00 10.05           C  
ATOM   2539  CE1 TYR A 325      50.276  35.426  44.022  1.00 11.33           C  
ATOM   2540  CE2 TYR A 325      50.794  34.025  42.132  1.00 11.51           C  
ATOM   2541  CZ  TYR A 325      50.300  35.211  42.650  1.00 12.31           C  
ATOM   2542  OH  TYR A 325      49.832  36.160  41.760  1.00 18.41           O  
ATOM   2543  N   ALA A 326      49.948  29.925  43.950  1.00  7.60           N  
ATOM   2544  CA  ALA A 326      49.071  29.493  42.849  1.00  7.46           C  
ATOM   2545  C   ALA A 326      47.773  28.865  43.369  1.00  7.44           C  
ATOM   2546  O   ALA A 326      46.706  29.113  42.809  1.00  8.65           O  
ATOM   2547  CB  ALA A 326      49.800  28.548  41.931  1.00  8.80           C  
ATOM   2548  N   ALA A 327      47.860  28.100  44.451  1.00  7.10           N  
ATOM   2549  CA  ALA A 327      46.655  27.498  45.039  1.00  8.26           C  
ATOM   2550  C   ALA A 327      45.698  28.606  45.550  1.00  8.21           C  
ATOM   2551  O   ALA A 327      44.483  28.525  45.358  1.00  9.31           O  
ATOM   2552  CB  ALA A 327      47.017  26.526  46.176  1.00  7.98           C  
ATOM   2553  N   SER A 328      46.238  29.673  46.129  1.00  7.97           N  
ATOM   2554  CA  SER A 328      45.397  30.765  46.639  1.00  9.12           C  
ATOM   2555  C   SER A 328      44.633  31.525  45.537  1.00  9.49           C  
ATOM   2556  O   SER A 328      43.559  32.084  45.787  1.00 10.43           O  
ATOM   2557  CB  SER A 328      46.218  31.757  47.484  1.00 10.00           C  
ATOM   2558  OG  SER A 328      46.951  32.637  46.630  1.00 15.16           O  
ATOM   2559  N   ILE A 329      45.188  31.557  44.333  1.00  9.17           N  
ATOM   2560  CA  ILE A 329      44.544  32.228  43.205  1.00 10.42           C  
ATOM   2561  C   ILE A 329      43.436  31.323  42.633  1.00 11.40           C  
ATOM   2562  O   ILE A 329      42.268  31.723  42.528  1.00 10.87           O  
ATOM   2563  CB  ILE A 329      45.578  32.570  42.065  1.00 11.74           C  
ATOM   2564  CG1 ILE A 329      46.684  33.495  42.598  1.00 12.82           C  
ATOM   2565  CG2 ILE A 329      44.883  33.190  40.850  1.00 11.58           C  
ATOM   2566  CD1 ILE A 329      46.177  34.825  43.090  1.00 16.20           C  
ATOM   2567  N   ILE A 330      43.804  30.089  42.302  1.00  9.94           N  
ATOM   2568  CA  ILE A 330      42.856  29.142  41.712  1.00 10.07           C  
ATOM   2569  C   ILE A 330      41.686  28.714  42.614  1.00  8.95           C  
ATOM   2570  O   ILE A 330      40.567  28.535  42.116  1.00 10.98           O  
ATOM   2571  CB  ILE A 330      43.631  27.897  41.121  1.00 11.12           C  
ATOM   2572  CG1 ILE A 330      44.208  28.243  39.736  1.00 12.17           C  
ATOM   2573  CG2 ILE A 330      42.713  26.636  41.016  1.00  9.31           C  
ATOM   2574  CD1 ILE A 330      45.278  29.335  39.737  1.00 13.85           C  
ATOM   2575  N   ILE A 331      41.919  28.581  43.919  1.00  8.70           N  
ATOM   2576  CA  ILE A 331      40.881  28.147  44.858  1.00  8.93           C  
ATOM   2577  C   ILE A 331      39.645  29.059  44.902  1.00 10.36           C  
ATOM   2578  O   ILE A 331      38.547  28.606  45.230  1.00 10.80           O  
ATOM   2579  CB  ILE A 331      41.465  27.908  46.292  1.00  9.34           C  
ATOM   2580  CG1 ILE A 331      40.536  27.005  47.113  1.00 10.63           C  
ATOM   2581  CG2 ILE A 331      41.684  29.204  47.013  1.00 10.05           C  
ATOM   2582  CD1 ILE A 331      41.108  26.526  48.455  1.00  9.93           C  
ATOM   2583  N   ARG A 332      39.805  30.322  44.523  1.00 10.60           N  
ATOM   2584  CA  ARG A 332      38.684  31.267  44.521  1.00 12.61           C  
ATOM   2585  C   ARG A 332      38.062  31.471  43.147  1.00 13.75           C  
ATOM   2586  O   ARG A 332      37.320  32.439  42.966  1.00 15.54           O  
ATOM   2587  CB  ARG A 332      39.145  32.640  45.005  1.00 16.36           C  
ATOM   2588  CG  ARG A 332      39.620  32.669  46.408  1.00 19.77           C  
ATOM   2589  CD  ARG A 332      40.296  34.005  46.683  1.00 25.77           C  
ATOM   2590  NE  ARG A 332      40.508  34.173  48.116  1.00 28.79           N  
ATOM   2591  CZ  ARG A 332      41.458  33.562  48.820  1.00 31.96           C  
ATOM   2592  NH1 ARG A 332      42.328  32.733  48.237  1.00 30.27           N  
ATOM   2593  NH2 ARG A 332      41.508  33.751  50.132  1.00 32.99           N  
ATOM   2594  N   ARG A 333      38.366  30.610  42.175  1.00 13.38           N  
ATOM   2595  CA  ARG A 333      37.844  30.767  40.807  1.00 15.39           C  
ATOM   2596  C   ARG A 333      37.369  29.434  40.259  1.00 16.36           C  
ATOM   2597  O   ARG A 333      37.583  28.399  40.901  1.00 16.29           O  
ATOM   2598  CB  ARG A 333      38.943  31.299  39.874  1.00 16.28           C  
ATOM   2599  CG  ARG A 333      39.545  32.613  40.320  1.00 19.92           C  
ATOM   2600  CD  ARG A 333      40.672  33.060  39.418  1.00 22.47           C  
ATOM   2601  NE  ARG A 333      40.262  33.229  38.021  1.00 24.32           N  
ATOM   2602  CZ  ARG A 333      40.419  34.352  37.315  1.00 25.63           C  
ATOM   2603  NH1 ARG A 333      40.962  35.436  37.878  1.00 25.73           N  
ATOM   2604  NH2 ARG A 333      40.133  34.363  36.012  1.00 24.98           N  
ATOM   2605  N   THR A 334      36.721  29.455  39.089  1.00 17.68           N  
ATOM   2606  CA  THR A 334      36.261  28.210  38.449  1.00 20.18           C  
ATOM   2607  C   THR A 334      37.125  27.894  37.223  1.00 21.18           C  
ATOM   2608  O   THR A 334      37.646  28.813  36.580  1.00 22.86           O  
ATOM   2609  CB  THR A 334      34.774  28.273  37.972  1.00 20.67           C  
ATOM   2610  OG1 THR A 334      34.672  29.175  36.871  1.00 23.27           O  
ATOM   2611  CG2 THR A 334      33.852  28.729  39.083  1.00 20.47           C  
ATOM   2612  N   GLY A 335      37.320  26.599  36.959  1.00 21.28           N  
ATOM   2613  CA  GLY A 335      38.073  26.128  35.804  1.00 23.26           C  
ATOM   2614  C   GLY A 335      39.580  26.301  35.795  1.00 24.93           C  
ATOM   2615  O   GLY A 335      40.185  26.337  34.714  1.00 25.08           O  
ATOM   2616  N   CYS A 336      40.204  26.334  36.978  1.00 25.94           N  
ATOM   2617  CA  CYS A 336      41.657  26.549  37.075  1.00 27.20           C  
ATOM   2618  C   CYS A 336      42.073  27.782  36.267  1.00 26.95           C  
ATOM   2619  O   CYS A 336      43.035  27.720  35.479  1.00 28.56           O  
ATOM   2620  CB  CYS A 336      42.461  25.330  36.584  1.00 28.54           C  
ATOM   2621  SG  CYS A 336      43.042  24.282  37.915  1.00 34.86           S  
ATOM   2622  N   THR A 337      41.293  28.861  36.371  1.00 25.28           N  
ATOM   2623  CA  THR A 337      41.633  30.096  35.651  1.00 24.02           C  
ATOM   2624  C   THR A 337      42.439  31.019  36.573  1.00 24.23           C  
ATOM   2625  O   THR A 337      42.479  30.829  37.803  1.00 23.37           O  
ATOM   2626  CB  THR A 337      40.391  30.850  35.100  1.00 22.90           C  
ATOM   2627  OG1 THR A 337      39.479  31.107  36.169  1.00 22.69           O  
ATOM   2628  CG2 THR A 337      39.703  30.040  34.002  1.00 23.60           C  
ATOM   2629  N   PHE A 338      43.057  32.035  35.984  1.00 23.62           N  
ATOM   2630  CA  PHE A 338      43.889  32.948  36.761  1.00 23.84           C  
ATOM   2631  C   PHE A 338      44.013  34.297  36.025  1.00 24.43           C  
ATOM   2632  O   PHE A 338      43.679  34.386  34.822  1.00 23.13           O  
ATOM   2633  CB  PHE A 338      45.255  32.278  36.942  1.00 23.12           C  
ATOM   2634  CG  PHE A 338      45.721  31.523  35.721  1.00 22.53           C  
ATOM   2635  CD1 PHE A 338      46.113  32.197  34.576  1.00 22.37           C  
ATOM   2636  CD2 PHE A 338      45.727  30.136  35.707  1.00 22.29           C  
ATOM   2637  CE1 PHE A 338      46.497  31.504  33.440  1.00 21.97           C  
ATOM   2638  CE2 PHE A 338      46.112  29.434  34.573  1.00 21.94           C  
ATOM   2639  CZ  PHE A 338      46.496  30.119  33.438  1.00 23.34           C  
ATOM   2640  N   PRO A 339      44.469  35.363  36.732  1.00 24.51           N  
ATOM   2641  CA  PRO A 339      44.624  36.696  36.113  1.00 25.72           C  
ATOM   2642  C   PRO A 339      45.663  36.699  34.980  1.00 26.80           C  
ATOM   2643  O   PRO A 339      46.468  35.764  34.830  1.00 26.63           O  
ATOM   2644  CB  PRO A 339      45.047  37.577  37.287  1.00 25.59           C  
ATOM   2645  CG  PRO A 339      45.751  36.614  38.209  1.00 26.37           C  
ATOM   2646  CD  PRO A 339      44.863  35.396  38.151  1.00 25.17           C  
ATOM   2647  N   GLU A 340      45.638  37.731  34.155  1.00 27.20           N  
ATOM   2648  CA  GLU A 340      46.573  37.787  33.040  1.00 28.25           C  
ATOM   2649  C   GLU A 340      48.047  37.499  33.370  1.00 26.90           C  
ATOM   2650  O   GLU A 340      48.722  36.798  32.604  1.00 28.18           O  
ATOM   2651  CB  GLU A 340      46.424  39.117  32.295  1.00 31.67           C  
ATOM   2652  CG  GLU A 340      45.633  38.995  31.000  1.00 36.55           C  
ATOM   2653  CD  GLU A 340      46.420  38.237  29.928  1.00 40.07           C  
ATOM   2654  OE1 GLU A 340      47.609  38.607  29.694  1.00 41.22           O  
ATOM   2655  OE2 GLU A 340      45.856  37.271  29.340  1.00 41.83           O  
ATOM   2656  N   LYS A 341      48.529  37.988  34.510  1.00 24.03           N  
ATOM   2657  CA  LYS A 341      49.921  37.792  34.893  1.00 22.64           C  
ATOM   2658  C   LYS A 341      50.083  37.514  36.384  1.00 21.03           C  
ATOM   2659  O   LYS A 341      49.351  38.064  37.209  1.00 19.14           O  
ATOM   2660  CB  LYS A 341      50.727  39.036  34.530  1.00 26.62           C  
ATOM   2661  CG  LYS A 341      50.511  39.520  33.096  1.00 29.53           C  
ATOM   2662  CD  LYS A 341      51.604  40.480  32.682  1.00 32.64           C  
ATOM   2663  CE  LYS A 341      51.972  40.278  31.217  1.00 33.87           C  
ATOM   2664  NZ  LYS A 341      53.264  40.964  30.887  1.00 35.40           N  
ATOM   2665  N   PRO A 342      51.034  36.629  36.755  1.00 20.61           N  
ATOM   2666  CA  PRO A 342      51.245  36.317  38.174  1.00 19.38           C  
ATOM   2667  C   PRO A 342      51.953  37.454  38.886  1.00 19.98           C  
ATOM   2668  O   PRO A 342      52.667  38.230  38.252  1.00 22.20           O  
ATOM   2669  CB  PRO A 342      52.112  35.051  38.123  1.00 18.53           C  
ATOM   2670  CG  PRO A 342      52.891  35.220  36.846  1.00 19.60           C  
ATOM   2671  CD  PRO A 342      51.854  35.757  35.886  1.00 19.61           C  
ATOM   2672  N   ASP A 343      51.675  37.601  40.174  1.00 21.25           N  
ATOM   2673  CA  ASP A 343      52.306  38.628  41.001  1.00 24.43           C  
ATOM   2674  C   ASP A 343      53.170  37.899  42.046  1.00 24.72           C  
ATOM   2675  O   ASP A 343      52.908  37.901  43.257  1.00 26.04           O  
ATOM   2676  CB  ASP A 343      51.256  39.529  41.664  1.00 27.65           C  
ATOM   2677  CG  ASP A 343      51.888  40.642  42.515  1.00 31.43           C  
ATOM   2678  OD1 ASP A 343      52.982  41.148  42.146  1.00 32.54           O  
ATOM   2679  OD2 ASP A 343      51.288  40.999  43.556  1.00 32.61           O  
ATOM   2680  N   PHE A 344      54.203  37.252  41.535  1.00 24.68           N  
ATOM   2681  CA  PHE A 344      55.126  36.472  42.338  1.00 24.24           C  
ATOM   2682  C   PHE A 344      56.529  36.816  41.791  1.00 26.11           C  
ATOM   2683  O   PHE A 344      56.797  36.650  40.582  1.00 27.99           O  
ATOM   2684  CB  PHE A 344      54.792  34.980  42.103  1.00 19.06           C  
ATOM   2685  CG  PHE A 344      55.585  34.023  42.953  1.00 15.46           C  
ATOM   2686  CD1 PHE A 344      55.146  33.680  44.231  1.00 13.16           C  
ATOM   2687  CD2 PHE A 344      56.775  33.475  42.483  1.00 13.50           C  
ATOM   2688  CE1 PHE A 344      55.873  32.818  45.022  1.00 13.34           C  
ATOM   2689  CE2 PHE A 344      57.514  32.611  43.270  1.00 13.81           C  
ATOM   2690  CZ  PHE A 344      57.066  32.280  44.542  1.00 13.81           C  
ATOM   2691  N   HIS A 345      57.406  37.334  42.647  1.00 26.70           N  
ATOM   2692  CA  HIS A 345      58.767  37.658  42.208  1.00 28.39           C  
ATOM   2693  C   HIS A 345      59.855  36.935  43.071  1.00 29.73           C  
ATOM   2694  O   HIS A 345      59.576  36.618  44.247  1.00 30.48           O  
ATOM   2695  CB  HIS A 345      58.964  39.193  42.208  1.00 28.30           C  
ATOM   2696  OXT HIS A 345      60.986  36.666  42.588  1.00 30.35           O  
TER    2697      HIS A 345                                                      
HETATM 2698 CL    CL A 380      45.762  13.289  34.477  1.00  6.86          CL  
HETATM 2699 CL    CL A 385      47.488  18.157  46.948  1.00 19.68          CL  
HETATM 2700 MG    MG A 360      44.403  16.299  44.144  1.00 11.04          MG  
HETATM 2701 MG    MG A 365      31.268  20.381  53.134  1.00 15.62          MG  
HETATM 2702 MG    MG A 375      22.677   4.493  47.143  1.00 28.44          MG  
HETATM 2703  O5' ADN A 350      41.304  18.534  40.336  1.00 11.59           O  
HETATM 2704  C5' ADN A 350      40.267  18.968  39.461  1.00 10.73           C  
HETATM 2705  C4' ADN A 350      40.492  18.124  38.214  1.00 11.38           C  
HETATM 2706  O4' ADN A 350      40.463  16.696  38.532  1.00 10.65           O  
HETATM 2707  C3' ADN A 350      39.323  18.273  37.235  1.00 10.91           C  
HETATM 2708  O3' ADN A 350      39.772  19.164  36.205  1.00 12.64           O  
HETATM 2709  C2' ADN A 350      39.068  16.862  36.663  1.00 10.47           C  
HETATM 2710  O2' ADN A 350      38.967  16.826  35.235  1.00  9.19           O  
HETATM 2711  C1' ADN A 350      40.233  16.066  37.280  1.00  9.28           C  
HETATM 2712  N9  ADN A 350      40.065  14.598  37.304  1.00  8.71           N  
HETATM 2713  C8  ADN A 350      39.114  13.871  38.035  1.00  7.96           C  
HETATM 2714  N7  ADN A 350      39.167  12.571  37.855  1.00  7.72           N  
HETATM 2715  C5  ADN A 350      40.222  12.408  36.942  1.00  8.05           C  
HETATM 2716  C6  ADN A 350      40.806  11.250  36.309  1.00  8.15           C  
HETATM 2717  N6  ADN A 350      40.384  10.000  36.521  1.00  7.39           N  
HETATM 2718  N1  ADN A 350      41.834  11.467  35.456  1.00  7.03           N  
HETATM 2719  C2  ADN A 350      42.267  12.717  35.240  1.00  8.08           C  
HETATM 2720  N3  ADN A 350      41.808  13.867  35.762  1.00  7.59           N  
HETATM 2721  C4  ADN A 350      40.782  13.641  36.606  1.00  7.59           C  
HETATM 2722  O5' ADN A 355      44.800  21.862  48.755  1.00 14.24           O  
HETATM 2723  C5' ADN A 355      45.929  22.293  47.965  1.00 13.05           C  
HETATM 2724  C4' ADN A 355      46.313  23.741  48.587  1.00 10.61           C  
HETATM 2725  O4' ADN A 355      45.164  24.610  48.418  1.00 11.59           O  
HETATM 2726  C3' ADN A 355      46.562  23.784  50.146  1.00 11.65           C  
HETATM 2727  O3' ADN A 355      47.855  23.319  50.629  1.00 12.48           O  
HETATM 2728  C2' ADN A 355      46.313  25.244  50.415  1.00 11.82           C  
HETATM 2729  O2' ADN A 355      47.483  25.992  49.997  1.00 10.60           O  
HETATM 2730  C1' ADN A 355      45.092  25.568  49.514  1.00 11.56           C  
HETATM 2731  N9  ADN A 355      43.849  25.286  50.268  1.00 11.65           N  
HETATM 2732  C8  ADN A 355      43.061  24.131  50.208  1.00 12.61           C  
HETATM 2733  N7  ADN A 355      42.013  24.151  51.010  1.00 12.34           N  
HETATM 2734  C5  ADN A 355      42.103  25.400  51.645  1.00 11.83           C  
HETATM 2735  C6  ADN A 355      41.296  26.048  52.617  1.00 11.61           C  
HETATM 2736  N6  ADN A 355      40.194  25.505  53.138  1.00 11.04           N  
HETATM 2737  N1  ADN A 355      41.682  27.279  53.025  1.00 10.37           N  
HETATM 2738  C2  ADN A 355      42.788  27.844  52.509  1.00  9.73           C  
HETATM 2739  N3  ADN A 355      43.630  27.341  51.590  1.00 10.69           N  
HETATM 2740  C4  ADN A 355      43.223  26.102  51.197  1.00 11.67           C  
HETATM 2741  O   HOH A 402      23.677   2.274  47.348  1.00 25.42           O  
HETATM 2742  O   HOH A 406      45.014  10.278  27.607  1.00 10.67           O  
HETATM 2743  O   HOH A 407      48.696  30.566  51.623  1.00 10.59           O  
HETATM 2744  O   HOH A 408      47.507  28.740  49.771  1.00  9.53           O  
HETATM 2745  O   HOH A 409      47.924  17.123  38.585  1.00  9.88           O  
HETATM 2746  O   HOH A 410      48.391  22.365  53.219  1.00  8.51           O  
HETATM 2747  O   HOH A 411      32.339  30.677  48.382  1.00  9.76           O  
HETATM 2748  O   HOH A 412      45.282  15.724  32.511  1.00  8.68           O  
HETATM 2749  O   HOH A 413      28.480  17.298  46.318  1.00 10.25           O  
HETATM 2750  O   HOH A 414      46.275  14.328  40.654  1.00  9.31           O  
HETATM 2751  O   HOH A 415      38.223  10.134  38.983  1.00  7.89           O  
HETATM 2752  O   HOH A 416      42.126   7.545  35.922  1.00 10.85           O  
HETATM 2753  O   HOH A 417      52.613  31.953  48.877  1.00 10.69           O  
HETATM 2754  O   HOH A 418      40.878   3.676  32.990  1.00 13.67           O  
HETATM 2755  O   HOH A 419      51.195  30.086  52.861  1.00 11.33           O  
HETATM 2756  O   HOH A 420      45.120  19.828  50.524  1.00 10.99           O  
HETATM 2757  O   HOH A 421      30.875   9.017  44.887  1.00 10.79           O  
HETATM 2758  O   HOH A 422      39.805  12.823  26.136  1.00 11.55           O  
HETATM 2759  O   HOH A 423      50.127   1.619  26.498  1.00 13.18           O  
HETATM 2760  O   HOH A 424      48.149  26.147  57.978  1.00  9.50           O  
HETATM 2761  O   HOH A 425      44.788  29.300  49.822  1.00 11.22           O  
HETATM 2762  O   HOH A 426      39.103  12.381  46.383  1.00 16.10           O  
HETATM 2763  O   HOH A 427      46.191   7.319  46.109  1.00 10.99           O  
HETATM 2764  O   HOH A 428      24.339  24.902  38.521  1.00 14.24           O  
HETATM 2765  O   HOH A 429      36.688   4.581  40.741  1.00 16.68           O  
HETATM 2766  O   HOH A 430      41.753  15.955  41.181  1.00 12.54           O  
HETATM 2767  O   HOH A 431      55.057  29.121  52.067  1.00 11.17           O  
HETATM 2768  O   HOH A 432      59.232  18.215  27.279  1.00 13.73           O  
HETATM 2769  O   HOH A 433      61.903  11.824  56.712  1.00 14.76           O  
HETATM 2770  O   HOH A 434      33.030  23.049  34.586  1.00 17.03           O  
HETATM 2771  O   HOH A 435      34.712  24.240  48.815  1.00 14.82           O  
HETATM 2772  O   HOH A 436      32.970  26.396  47.803  1.00 12.95           O  
HETATM 2773  O   HOH A 437      31.823  10.811  42.966  1.00 11.73           O  
HETATM 2774  O   HOH A 438      34.727  24.160  53.678  1.00 16.61           O  
HETATM 2775  O   HOH A 439      59.299   2.752  54.789  1.00 19.08           O  
HETATM 2776  O   HOH A 440      35.881   6.032  32.871  1.00 15.28           O  
HETATM 2777  O   HOH A 441      62.277   9.039  55.910  1.00 14.05           O  
HETATM 2778  O   HOH A 442      16.638  16.675  47.056  1.00 22.17           O  
HETATM 2779  O   HOH A 443      54.610  28.529  55.030  1.00 13.19           O  
HETATM 2780  O   HOH A 444      59.283   1.833  46.398  1.00 17.85           O  
HETATM 2781  O   HOH A 445      47.565  -1.830  38.933  1.00 20.41           O  
HETATM 2782  O   HOH A 446      64.952   6.543  41.801  1.00 17.48           O  
HETATM 2783  O   HOH A 447      48.005   6.343  64.294  1.00 15.63           O  
HETATM 2784  O   HOH A 448      36.031  26.090  55.344  1.00 15.01           O  
HETATM 2785  O   HOH A 449      41.612  34.433  42.629  1.00 18.85           O  
HETATM 2786  O   HOH A 451      27.641  25.838  45.650  1.00 14.65           O  
HETATM 2787  O   HOH A 452      49.980   9.826  17.302  1.00 17.30           O  
HETATM 2788  O   HOH A 453      58.023  28.683  52.175  1.00 15.81           O  
HETATM 2789  O   HOH A 454      61.228  32.647  42.434  1.00 19.33           O  
HETATM 2790  O   HOH A 455      21.783  24.506  40.009  1.00 13.52           O  
HETATM 2791  O   HOH A 456      22.236  19.613  49.140  1.00  9.14           O  
HETATM 2792  O   HOH A 457      50.962  17.809  47.446  1.00 16.20           O  
HETATM 2793  O   HOH A 458      22.145   4.483  43.014  1.00 18.00           O  
HETATM 2794  O   HOH A 459      64.360  13.999  44.836  1.00 21.94           O  
HETATM 2795  O   HOH A 460      39.308  26.206  39.612  1.00 20.29           O  
HETATM 2796  O   HOH A 461      50.752   6.051  15.373  1.00 16.67           O  
HETATM 2797  O   HOH A 462      38.785   7.820  45.374  1.00 12.21           O  
HETATM 2798  O   HOH A 463      42.890  21.915  27.435  1.00 14.12           O  
HETATM 2799  O   HOH A 464      40.286   1.133  34.595  1.00 17.31           O  
HETATM 2800  O   HOH A 465      45.955   5.304  57.498  1.00 21.48           O  
HETATM 2801  O   HOH A 466      35.971  24.349  38.720  1.00 22.69           O  
HETATM 2802  O   HOH A 467      24.165  23.720  47.072  1.00 17.83           O  
HETATM 2803  O   HOH A 468      31.648  17.011  21.095  1.00 20.48           O  
HETATM 2804  O   HOH A 469      61.748  18.557  55.443  1.00 20.22           O  
HETATM 2805  O   HOH A 470      35.029  17.865  36.938  1.00 20.28           O  
HETATM 2806  O   HOH A 471      35.021  33.512  44.883  1.00 18.47           O  
HETATM 2807  O   HOH A 472      19.878  24.618  38.012  1.00 16.93           O  
HETATM 2808  O   HOH A 473      31.014  16.900  17.905  1.00 19.30           O  
HETATM 2809  O   HOH A 474      40.581  -1.253  49.445  1.00 27.38           O  
HETATM 2810  O   HOH A 475      50.355  14.323  18.428  1.00 16.55           O  
HETATM 2811  O   HOH A 476      65.631   8.014  54.218  1.00 26.14           O  
HETATM 2812  O   HOH A 477      29.795  26.994  30.012  1.00 17.27           O  
HETATM 2813  O   HOH A 478      41.578  12.737  48.199  1.00 15.91           O  
HETATM 2814  O   HOH A 479      65.480  15.969  21.951  1.00 26.14           O  
HETATM 2815  O   HOH A 480      55.243  28.449  57.869  1.00 13.67           O  
HETATM 2816  O   HOH A 481      42.150  26.098  29.973  1.00 22.55           O  
HETATM 2817  O   HOH A 482      42.015  35.788  40.234  1.00 31.31           O  
HETATM 2818  O   HOH A 483      59.722  38.594  46.533  1.00 19.15           O  
HETATM 2819  O   HOH A 484      23.029  17.044  49.904  1.00 20.78           O  
HETATM 2820  O   HOH A 485      66.787   9.143  51.689  1.00 20.58           O  
HETATM 2821  O   HOH A 486      17.668  12.963  40.786  1.00 24.94           O  
HETATM 2822  O   HOH A 487      47.472  33.708  58.092  1.00 19.07           O  
HETATM 2823  O   HOH A 488      19.277   5.126  44.673  1.00 16.58           O  
HETATM 2824  O   HOH A 489      47.593  17.641  18.698  1.00 25.71           O  
HETATM 2825  O   HOH A 490      44.445  34.391  32.315  1.00 24.36           O  
HETATM 2826  O   HOH A 491      24.185   4.129  38.409  1.00 28.31           O  
HETATM 2827  O   HOH A 492      43.632  28.328  28.080  1.00 24.30           O  
HETATM 2828  O   HOH A 493      41.638  31.241  50.752  1.00 29.05           O  
HETATM 2829  O   HOH A 494      35.953  10.514  18.386  1.00 30.62           O  
HETATM 2830  O   HOH A 495      59.436  24.698  57.827  1.00 29.67           O  
HETATM 2831  O   HOH A 496      53.728  -3.757  42.482  1.00 18.53           O  
HETATM 2832  O   HOH A 497      59.178   7.201  14.744  1.00 26.18           O  
HETATM 2833  O   HOH A 498      52.020  29.560  22.448  1.00 31.94           O  
HETATM 2834  O   HOH A 499      50.048  19.125  61.148  1.00 19.92           O  
HETATM 2835  O   HOH A 500      39.931  16.746  18.074  1.00 23.53           O  
HETATM 2836  O   HOH A 501      47.824  13.234  61.138  1.00 21.30           O  
HETATM 2837  O   HOH A 502      58.607  31.891  38.041  1.00 25.07           O  
HETATM 2838  O   HOH A 503      62.695   4.095  29.477  1.00 22.09           O  
HETATM 2839  O   HOH A 504      35.221  20.585  47.442  1.00 26.01           O  
HETATM 2840  O   HOH A 505      31.932  23.776  45.773  1.00 33.97           O  
HETATM 2841  O   HOH A 506      54.756  12.366  64.218  1.00 27.15           O  
HETATM 2842  O   HOH A 507      65.802  10.286  38.941  1.00 23.70           O  
HETATM 2843  O   HOH A 508      66.546   3.100  48.579  1.00 27.41           O  
HETATM 2844  O   HOH A 509      56.982   0.958  19.763  1.00 29.57           O  
HETATM 2845  O   HOH A 510      53.356  25.719  61.339  1.00 18.48           O  
HETATM 2846  O   HOH A 511      61.912  15.395  61.541  1.00 19.46           O  
HETATM 2847  O   HOH A 512      33.094  11.711  27.615  1.00 24.35           O  
HETATM 2848  O   HOH A 513      48.079  28.909  59.280  1.00 20.78           O  
HETATM 2849  O   HOH A 514      57.184   0.422  29.654  1.00 22.22           O  
HETATM 2850  O   HOH A 515      40.781  16.383  46.374  1.00 17.19           O  
HETATM 2851  O   HOH A 516      35.494  22.982  46.419  1.00 22.20           O  
HETATM 2852  O   HOH A 517      34.710   5.856  29.579  1.00 25.90           O  
HETATM 2853  O   HOH A 518      17.578  23.388  37.679  1.00 20.09           O  
HETATM 2854  O   HOH A 519      49.234  29.001  30.941  1.00 19.95           O  
HETATM 2855  O   HOH A 520      46.605  -3.537  42.288  1.00 24.53           O  
HETATM 2856  O   HOH A 521      69.764  22.539  42.813  1.00 27.45           O  
HETATM 2857  O   HOH A 522      59.071   5.251  61.032  1.00 28.12           O  
HETATM 2858  O   HOH A 523      46.610  22.690  21.659  1.00 26.38           O  
HETATM 2859  O   HOH A 524      64.187   7.916  39.152  1.00 25.12           O  
HETATM 2860  O   HOH A 525      48.059  37.989  42.743  1.00 26.77           O  
HETATM 2861  O   HOH A 526      43.059  22.685  32.176  1.00 27.71           O  
HETATM 2862  O   HOH A 527      48.766   1.748  48.227  1.00 19.12           O  
HETATM 2863  O   HOH A 528      53.311  32.028  29.129  1.00 23.43           O  
HETATM 2864  O   HOH A 529      37.731  10.167  47.339  1.00 24.15           O  
HETATM 2865  O   HOH A 530      55.097  -0.505  51.105  1.00 24.20           O  
HETATM 2866  O   HOH A 531      51.836  12.037  66.781  1.00 20.19           O  
HETATM 2867  O   HOH A 532      72.304   7.702  38.903  1.00 41.18           O  
HETATM 2868  O   HOH A 533      48.524  34.429  48.306  1.00 21.06           O  
HETATM 2869  O   HOH A 534      37.594   4.185  26.829  1.00 26.42           O  
HETATM 2870  O   HOH A 535      64.247   5.741  49.883  1.00 31.06           O  
HETATM 2871  O   HOH A 536      34.212  23.098  19.639  1.00 29.34           O  
HETATM 2872  O   HOH A 537      36.041  16.199  45.499  1.00 20.32           O  
HETATM 2873  O   HOH A 538      41.171  15.269  51.478  1.00 31.00           O  
HETATM 2874  O   HOH A 539      40.951  22.179  55.509  1.00 17.54           O  
HETATM 2875  O   HOH A 540      68.970  14.454  46.544  1.00 32.83           O  
HETATM 2876  O   HOH A 541      61.692  31.222  39.198  1.00 31.82           O  
HETATM 2877  O   HOH A 542      58.904  30.066  22.839  1.00 28.49           O  
HETATM 2878  O   HOH A 543      33.346   3.983  40.084  1.00 29.23           O  
HETATM 2879  O   HOH A 544      17.097  15.825  41.435  1.00 30.17           O  
HETATM 2880  O   HOH A 545      52.338   3.730  15.329  1.00 30.38           O  
HETATM 2881  O   HOH A 546      48.194  22.702  60.801  1.00 30.69           O  
HETATM 2882  O   HOH A 547      20.992  15.497  28.366  1.00 33.73           O  
HETATM 2883  O   HOH A 548      39.452  25.928  32.394  1.00 23.44           O  
HETATM 2884  O   HOH A 549      51.597  21.825  19.999  1.00 31.16           O  
HETATM 2885  O   HOH A 550      23.592   3.470  32.228  1.00 38.31           O  
HETATM 2886  O   HOH A 551      48.227  -0.291  58.421  1.00 25.59           O  
HETATM 2887  O   HOH A 552      65.563  14.019  50.748  1.00 27.85           O  
HETATM 2888  O   HOH A 553      56.080  25.775  60.462  1.00 25.11           O  
HETATM 2889  O   HOH A 554      45.156   2.559  26.707  1.00 25.93           O  
HETATM 2890  O   HOH A 555      52.380  21.062  61.742  1.00 27.63           O  
HETATM 2891  O   HOH A 556      48.052  17.942  44.086  1.00 11.75           O  
HETATM 2892  O   HOH A 557      37.308  26.100  28.757  1.00 16.20           O  
HETATM 2893  O   HOH A 558      53.560  34.584  47.806  1.00 13.90           O  
HETATM 2894  O   HOH A 559      51.922  28.083  62.088  1.00 16.48           O  
HETATM 2895  O   HOH A 560      60.501  12.694  61.602  1.00 18.35           O  
HETATM 2896  O   HOH A 561      36.087  23.891  51.276  1.00 18.74           O  
HETATM 2897  O   HOH A 562      19.048  18.937  48.552  1.00 17.29           O  
HETATM 2898  O   HOH A 563      53.236  31.613  51.572  1.00 14.88           O  
HETATM 2899  O   HOH A 564      62.605  12.273  59.375  1.00 21.43           O  
HETATM 2900  O   HOH A 565      35.935  20.130  38.424  1.00 24.33           O  
HETATM 2901  O   HOH A 566      60.686   5.307  58.466  1.00 22.13           O  
HETATM 2902  O   HOH A 567      31.398  32.456  46.579  1.00 18.01           O  
HETATM 2903  O   HOH A 568      29.329  18.916  21.685  1.00 17.48           O  
HETATM 2904  O   HOH A 569      61.781  25.665  56.157  1.00 19.85           O  
HETATM 2905  O   HOH A 570      37.691   0.715  35.136  1.00 19.48           O  
HETATM 2906  O   HOH A 571      36.790  20.172  41.228  1.00 23.66           O  
HETATM 2907  O   HOH A 572      49.994  32.309  49.669  1.00 17.97           O  
HETATM 2908  O   HOH A 573      57.745  12.305  61.430  1.00 24.33           O  
HETATM 2909  O   HOH A 574      41.717   1.128  23.180  1.00 39.13           O  
HETATM 2910  O   HOH A 575      60.318   2.840  57.243  1.00 25.13           O  
HETATM 2911  O   HOH A 576      41.107   8.388  53.728  1.00 26.88           O  
HETATM 2912  O   HOH A 577      38.863  23.187  52.465  1.00 29.67           O  
HETATM 2913  O   HOH A 578      28.459  27.132  43.528  1.00 22.32           O  
HETATM 2914  O   HOH A 579      38.430  22.838  34.842  1.00 32.88           O  
HETATM 2915  O   HOH A 580      58.658  32.688  24.021  1.00 24.73           O  
HETATM 2916  O   HOH A 581      62.091  11.006  31.252  1.00 28.44           O  
HETATM 2917  O   HOH A 582      24.350  21.632  27.516  1.00 21.62           O  
HETATM 2918  O   HOH A 583      58.474  22.020  61.199  1.00 24.01           O  
HETATM 2919  O   HOH A 584      37.917   4.159  32.508  1.00 23.22           O  
HETATM 2920  O   HOH A 585      56.423  36.105  24.206  1.00 27.70           O  
HETATM 2921  O   HOH A 586      47.607   9.065  64.398  1.00 24.52           O  
HETATM 2922  O   HOH A 587      59.550  34.761  40.432  1.00 28.32           O  
HETATM 2923  O   HOH A 588      49.705  27.104  60.992  1.00 22.40           O  
HETATM 2924  O   HOH A 589      62.319  39.179  45.952  1.00 26.35           O  
HETATM 2925  O   HOH A 590      15.315  23.712  39.501  1.00 30.88           O  
HETATM 2926  O   HOH A 591      16.910  10.007  44.746  1.00 28.20           O  
HETATM 2927  O   HOH A 592      17.378   6.948  46.126  1.00 28.86           O  
HETATM 2928  O   HOH A 593      59.048  -1.008  45.944  1.00 27.34           O  
HETATM 2929  O   HOH A 594      26.572  25.961  36.436  1.00 27.86           O  
HETATM 2930  O   HOH A 595      35.234  26.167  58.229  1.00 31.93           O  
HETATM 2931  O   HOH A 596      64.266  13.730  29.971  1.00 32.56           O  
HETATM 2932  O   HOH A 597      42.963  19.978  47.331  1.00 31.93           O  
HETATM 2933  O   HOH A 598      57.623  19.183  61.532  1.00 30.38           O  
HETATM 2934  O   HOH A 599      35.458  32.393  38.715  1.00 32.73           O  
HETATM 2935  O   HOH A 600      50.895  36.642  48.071  1.00 26.49           O  
HETATM 2936  O   HOH A 601      38.577  17.825  16.095  1.00 27.92           O  
HETATM 2937  O   HOH A 602      49.358  23.842  22.169  1.00 26.54           O  
HETATM 2938  O   HOH A 603      65.525   8.151  49.072  1.00 26.39           O  
HETATM 2939  O   HOH A 604      55.376   2.088  17.699  1.00 26.66           O  
HETATM 2940  O   HOH A 605      38.411   1.828  40.928  1.00 25.46           O  
HETATM 2941  O   HOH A 606      57.371  28.035  59.584  1.00 26.05           O  
HETATM 2942  O   HOH A 607      37.456  14.358  47.075  1.00 28.50           O  
HETATM 2943  O   HOH A 608      51.307  16.907  17.663  1.00 28.98           O  
HETATM 2944  O   HOH A 609      34.448  20.035  50.297  1.00 30.64           O  
HETATM 2945  O   HOH A 610      62.804  14.690  33.870  1.00 31.66           O  
HETATM 2946  O   HOH A 611      31.728  14.377  22.032  1.00 30.04           O  
HETATM 2947  O   HOH A 612      63.928   8.208  58.308  1.00 31.06           O  
HETATM 2948  O   HOH A 613      43.059  19.172  57.626  1.00 30.61           O  
HETATM 2949  O   HOH A 614      58.084  -1.933  43.575  1.00 33.56           O  
HETATM 2950  O   HOH A 615      63.127  34.636  42.113  1.00 32.59           O  
HETATM 2951  O   HOH A 616      64.917  21.905  27.189  1.00 29.86           O  
HETATM 2952  O   HOH A 617      74.425   3.721  43.970  1.00 30.99           O  
HETATM 2953  O   HOH A 618      60.496  16.601  18.060  1.00 28.27           O  
HETATM 2954  O   HOH A 619      42.839  31.648  33.148  1.00 27.43           O  
HETATM 2955  O   HOH A 620      60.373  34.390  25.299  1.00 28.08           O  
HETATM 2956  O   HOH A 621      66.687  15.645  43.445  1.00 30.71           O  
HETATM 2957  O   HOH A 622      32.998  11.754  18.984  1.00 31.47           O  
HETATM 2958  O   HOH A 623      47.107   2.711  13.572  1.00 35.97           O  
HETATM 2959  O   HOH A 624      31.685  14.029  52.144  1.00 13.12           O  
HETATM 2960  O   HOH A 625      52.519  -4.355  38.052  1.00 38.34           O  
HETATM 2961  O   HOH A 626      30.985  -0.544  33.121  1.00 31.84           O  
HETATM 2962  O   HOH A 627      32.972  34.812  46.579  1.00 33.75           O  
HETATM 2963  O   HOH A 628      53.365  -3.148  48.588  1.00 31.77           O  
HETATM 2964  O   HOH A 629      29.422  12.977  29.139  1.00 33.41           O  
HETATM 2965  O   HOH A 630      16.836  24.684  35.023  1.00 34.60           O  
HETATM 2966  O   HOH A 631      39.105  22.239  38.341  1.00 28.43           O  
HETATM 2967  O   HOH A 632      36.336   4.428  44.088  1.00 30.14           O  
HETATM 2968  O   HOH A 633      44.066  35.229  56.061  1.00 29.06           O  
HETATM 2969  O   HOH A 634      52.825  36.736  45.954  1.00 32.60           O  
HETATM 2970  O   HOH A 635      55.694  -1.608  23.775  1.00 28.71           O  
HETATM 2971  O   HOH A 636      39.284  32.157  58.498  1.00 29.01           O  
HETATM 2972  O   HOH A 637      40.648  21.791  51.090  1.00 30.03           O  
HETATM 2973  O   HOH A 638      42.964  18.122  51.492  1.00 24.97           O  
HETATM 2974  O   HOH A 639      56.087   0.622  58.385  1.00 31.04           O  
HETATM 2975  O   HOH A 640      37.310   5.362  46.739  1.00 35.80           O  
HETATM 2976  O   HOH A 641      47.360  -0.368  28.995  1.00 36.21           O  
HETATM 2977  O   HOH A 642      46.826  12.160  16.238  1.00 32.07           O  
HETATM 2978  O   HOH A 643      44.871  15.960  58.186  1.00 29.44           O  
HETATM 2979  O   HOH A 644      65.891  23.204  42.814  1.00 28.28           O  
HETATM 2980  O   HOH A 645      43.330   3.903  19.863  1.00 36.26           O  
HETATM 2981  O   HOH A 646      15.086  11.714  42.050  1.00 34.91           O  
HETATM 2982  O   HOH A 647      59.664  27.458  58.008  1.00 34.40           O  
HETATM 2983  O   HOH A 648      48.611  40.422  38.780  1.00 37.45           O  
HETATM 2984  O   HOH A 649      31.143   8.174  26.392  1.00 30.38           O  
HETATM 2985  O   HOH A 650      66.647  17.076  36.594  1.00 30.40           O  
HETATM 2986  O   HOH A 651      46.356  -1.023  32.107  1.00 36.36           O  
HETATM 2987  O   HOH A 652      29.500   6.379  31.565  1.00 32.82           O  
HETATM 2988  O   HOH A 653      50.887  -2.836  47.079  1.00 29.64           O  
HETATM 2989  O   HOH A 654      57.269  20.957  19.658  1.00 32.02           O  
HETATM 2990  O   HOH A 655      38.089  23.277  55.600  1.00 27.42           O  
HETATM 2991  O   HOH A 656      28.346  23.980  14.481  1.00 30.34           O  
HETATM 2992  O   HOH A 657      42.618  -0.011  34.070  1.00 26.72           O  
HETATM 2993  O   HOH A 658      35.881  22.623  36.238  1.00 38.61           O  
HETATM 2994  O   HOH A 659      57.207  34.957  35.901  1.00 35.43           O  
HETATM 2995  O   HOH A 660      71.517  15.132  36.109  1.00 31.17           O  
HETATM 2996  O   HOH A 661      14.368  16.461  43.360  1.00 34.05           O  
HETATM 2997  O   HOH A 662      61.591   5.705  22.302  1.00 29.31           O  
HETATM 2998  O   HOH A 663      45.357   9.249  58.677  1.00 34.73           O  
HETATM 2999  O   HOH A 664      44.736  30.076  29.702  1.00 29.38           O  
HETATM 3000  O   HOH A 665      27.059  17.937  27.146  1.00 35.37           O  
HETATM 3001  O   HOH A 666      68.408   7.310  47.093  1.00 33.41           O  
HETATM 3002  O   HOH A 667      55.063  37.978  36.604  1.00 36.26           O  
HETATM 3003  O   HOH A 668      30.271  21.732  22.443  1.00 17.58           O  
HETATM 3004  O   HOH A 669      17.925  21.229  47.368  1.00 21.82           O  
HETATM 3005  O   HOH A 670      41.493   1.709  52.084  1.00 23.53           O  
HETATM 3006  O   HOH A 671      26.742  19.374  17.238  1.00 28.05           O  
HETATM 3007  O   HOH A 672      30.129  32.282  44.301  1.00 24.96           O  
HETATM 3008  O   HOH A 673      62.668  33.028  24.194  1.00 27.78           O  
HETATM 3009  O   HOH A 674      54.964  38.399  46.267  1.00 30.80           O  
HETATM 3010  O   HOH A 675      41.455  10.127  56.155  1.00 28.74           O  
HETATM 3011  O   HOH A 676      62.265  10.915  62.989  1.00 33.77           O  
HETATM 3012  O   HOH A 677      50.364  31.447  30.349  1.00 25.92           O  
HETATM 3013  O   HOH A 678      59.864   0.954  24.594  1.00 30.60           O  
HETATM 3014  O   HOH A 679      28.750  17.764  19.043  1.00 31.01           O  
HETATM 3015  O   HOH A 680      28.393  10.344  29.007  1.00 31.02           O  
HETATM 3016  O   HOH A 681      18.486  27.707  34.420  1.00 26.77           O  
HETATM 3017  O   HOH A 682      36.975  25.778  19.425  1.00 27.66           O  
HETATM 3018  O   HOH A 683      56.245  -0.930  53.464  1.00 29.07           O  
HETATM 3019  O   HOH A 684      34.402  23.115  16.904  1.00 30.70           O  
HETATM 3020  O   HOH A 685      25.186  14.903  28.604  1.00 31.14           O  
HETATM 3021  O   HOH A 686      48.688  36.078  58.132  1.00 33.31           O  
HETATM 3022  O   HOH A 687      74.826   3.565  46.696  1.00 30.22           O  
HETATM 3023  O   HOH A 688      62.751  18.048  19.116  1.00 31.09           O  
HETATM 3024  O   HOH A 689      63.250   5.561  58.857  1.00 32.16           O  
HETATM 3025  O   HOH A 690      19.174   9.836  32.639  1.00 34.63           O  
HETATM 3026  O   HOH A 691      53.933  19.190  65.398  1.00 33.06           O  
HETATM 3027  O   HOH A 692      46.992  36.059  50.550  1.00 36.17           O  
HETATM 3028  O   HOH A 693      72.297  10.992  30.050  1.00 33.24           O  
HETATM 3029  O   HOH A 694      38.026   2.219  24.990  1.00 36.08           O  
HETATM 3030  O   HOH A 695      69.464  -0.151  34.362  1.00 36.19           O  
HETATM 3031  O   HOH A 696      39.694  15.469  49.007  1.00 32.84           O  
HETATM 3032  O   HOH A 697      47.541  20.547  19.735  1.00 32.00           O  
HETATM 3033  O   HOH A 698      46.081  -1.800  56.729  1.00 37.70           O  
HETATM 3034  O   HOH A 699      54.217  -2.009  55.734  1.00 31.27           O  
HETATM 3035  O   HOH A 700      54.151   0.981  62.235  1.00 31.91           O  
HETATM 3036  O   HOH A 701      58.305  40.864  46.155  1.00 34.50           O  
HETATM 3037  O   HOH A 702      65.263  20.980  39.748  1.00 32.42           O  
HETATM 3038  O   HOH A 703      33.579   5.816  15.012  1.00 35.15           O  
HETATM 3039  O   HOH A 704      35.873  34.132  41.157  1.00 37.09           O  
HETATM 3040  O   HOH A 705      19.764   6.756  49.555  1.00 33.39           O  
HETATM 3041  O   HOH A 706      34.946  26.929  25.690  1.00 35.10           O  
HETATM 3042  O   HOH A 707      22.342  21.545  46.969  1.00 16.91           O  
HETATM 3043  O   HOH A 708      28.075   5.755  42.054  1.00 17.48           O  
HETATM 3044  O   HOH A 709      29.703   6.501  44.181  1.00 16.36           O  
HETATM 3045  O   HOH A 710      26.028  17.371  50.267  1.00 21.89           O  
HETATM 3046  O   HOH A 711      38.314  33.625  50.713  1.00 18.65           O  
HETATM 3047  O   HOH A 712      58.707  10.237  14.430  1.00 26.89           O  
HETATM 3048  O   HOH A 713      37.521  35.308  53.935  1.00 24.54           O  
HETATM 3049  O   HOH A 714      16.982  13.026  32.550  1.00 32.90           O  
HETATM 3050  O   HOH A 715      36.448  37.251  52.376  1.00 33.99           O  
HETATM 3051  O   HOH A 716      47.751  22.079  29.970  1.00 35.03           O  
HETATM 3052  O   HOH A 717      68.397  13.271  26.177  1.00 32.74           O  
HETATM 3053  O   HOH A 718      63.373  30.299  23.696  1.00 33.23           O  
HETATM 3054  O   HOH A 719      22.939  25.401  31.233  1.00 35.02           O  
HETATM 3055  O   HOH A 720      41.832  -2.025  40.278  1.00 36.30           O  
HETATM 3056  O   HOH A 721      47.586   3.013  58.268  1.00 33.53           O  
HETATM 3057  O   HOH A 722      56.380  41.257  49.005  1.00 33.01           O  
HETATM 3058  O   HOH A 723      40.493   6.161  14.989  1.00 33.46           O  
HETATM 3059  O   HOH A 724      43.121   5.676  58.267  1.00 31.17           O  
HETATM 3060  O   HOH A 725      43.347  18.225  62.472  1.00 34.87           O  
HETATM 3061  O   HOH A 726      56.717   4.292  63.877  1.00 34.34           O  
HETATM 3062  O   HOH A 727      57.613   0.622  55.401  1.00 35.77           O  
HETATM 3063  O   HOH A 728      59.264  -1.390  37.938  1.00 32.87           O  
HETATM 3064  O   HOH A 729      22.807  22.720  29.402  1.00 33.51           O  
HETATM 3065  O   HOH A 730      42.686  36.033  44.545  1.00 34.03           O  
HETATM 3066  O   HOH A 731      37.695  24.478  58.937  1.00 36.10           O  
HETATM 3067  O   HOH A 732      64.545  19.005  55.262  1.00 31.07           O  
HETATM 3068  O   HOH A 733      29.024  25.199  37.592  1.00 34.69           O  
HETATM 3069  O   HOH A 734      39.768   5.062  51.358  1.00 36.82           O  
HETATM 3070  O   HOH A 735      65.087   5.373  28.545  1.00 35.71           O  
HETATM 3071  O   HOH A 736      43.560  16.283  60.600  1.00 34.74           O  
HETATM 3072  O   HOH A 737      46.078   0.004  35.648  1.00 38.98           O  
HETATM 3073  O   HOH A 738      32.506  30.494  35.995  1.00 36.59           O  
HETATM 3074  O   HOH A 739      66.768   7.567  25.275  1.00 42.24           O  
HETATM 3075  O   HOH A 740      58.684  23.340  21.217  1.00 36.02           O  
HETATM 3076  O   HOH A 741      37.841   1.474  22.194  1.00 32.94           O  
HETATM 3077  O   HOH A 742      43.574   1.495  28.798  1.00 25.98           O  
HETATM 3078  O   HOH A 743      26.127  11.725  27.589  1.00 38.09           O  
HETATM 3079  O   HOH A 744      38.738  10.983  57.050  1.00 36.42           O  
HETATM 3080  O   HOH A 745      17.039  12.642  49.003  1.00 35.10           O  
HETATM 3081  O   HOH A 746      44.869  17.651  45.778  1.00 10.43           O  
HETATM 3082  O   HOH A 747      42.964  15.151  45.263  1.00 11.36           O  
HETATM 3083  O   HOH A 748      42.752  17.536  43.390  1.00 10.79           O  
HETATM 3084  O   HOH A 749      44.040  14.906  42.454  1.00  9.35           O  
HETATM 3085  O   HOH A 750      45.780  17.329  42.798  1.00 12.62           O  
HETATM 3086  O   HOH A 751      45.990  15.041  44.919  1.00 11.24           O  
HETATM 3087  O   HOH A 752      31.780  21.741  54.916  1.00 16.09           O  
HETATM 3088  O   HOH A 753      31.541  18.535  54.304  1.00 16.30           O  
HETATM 3089  O   HOH A 754      33.403  20.273  52.663  1.00 16.38           O  
HETATM 3090  O   HOH A 755      29.158  20.442  53.656  1.00 12.95           O  
HETATM 3091  O   HOH A 756      24.264   5.870  48.236  1.00 30.33           O  
HETATM 3092  O   HOH A 757      21.462   4.347  49.101  1.00 34.23           O  
HETATM 3093  O   HOH A 758      20.865   3.595  46.122  1.00 23.00           O  
HETATM 3094  O   HOH A 759      21.490   6.333  47.364  1.00 19.68           O  
CONECT  229 2702                                                                
CONECT 1001 2701                                                                
CONECT 1009 2701                                                                
CONECT 2700 3081 3082 3083 3084                                                 
CONECT 2700 3085 3086                                                           
CONECT 2701 1001 1009 3087 3088                                                 
CONECT 2701 3089 3090                                                           
CONECT 2702  229 2741 3091 3092                                                 
CONECT 2702 3093 3094                                                           
CONECT 2703 2704                                                                
CONECT 2704 2703 2705                                                           
CONECT 2705 2704 2706 2707                                                      
CONECT 2706 2705 2711                                                           
CONECT 2707 2705 2708 2709                                                      
CONECT 2708 2707                                                                
CONECT 2709 2707 2710 2711                                                      
CONECT 2710 2709                                                                
CONECT 2711 2706 2709 2712                                                      
CONECT 2712 2711 2713 2721                                                      
CONECT 2713 2712 2714                                                           
CONECT 2714 2713 2715                                                           
CONECT 2715 2714 2716 2721                                                      
CONECT 2716 2715 2717 2718                                                      
CONECT 2717 2716                                                                
CONECT 2718 2716 2719                                                           
CONECT 2719 2718 2720                                                           
CONECT 2720 2719 2721                                                           
CONECT 2721 2712 2715 2720                                                      
CONECT 2722 2723                                                                
CONECT 2723 2722 2724                                                           
CONECT 2724 2723 2725 2726                                                      
CONECT 2725 2724 2730                                                           
CONECT 2726 2724 2727 2728                                                      
CONECT 2727 2726                                                                
CONECT 2728 2726 2729 2730                                                      
CONECT 2729 2728                                                                
CONECT 2730 2725 2728 2731                                                      
CONECT 2731 2730 2732 2740                                                      
CONECT 2732 2731 2733                                                           
CONECT 2733 2732 2734                                                           
CONECT 2734 2733 2735 2740                                                      
CONECT 2735 2734 2736 2737                                                      
CONECT 2736 2735                                                                
CONECT 2737 2735 2738                                                           
CONECT 2738 2737 2739                                                           
CONECT 2739 2738 2740                                                           
CONECT 2740 2731 2734 2739                                                      
CONECT 2741 2702                                                                
CONECT 3081 2700                                                                
CONECT 3082 2700                                                                
CONECT 3083 2700                                                                
CONECT 3084 2700                                                                
CONECT 3085 2700                                                                
CONECT 3086 2700                                                                
CONECT 3087 2701                                                                
CONECT 3088 2701                                                                
CONECT 3089 2701                                                                
CONECT 3090 2701                                                                
CONECT 3091 2702                                                                
CONECT 3092 2702                                                                
CONECT 3093 2702                                                                
CONECT 3094 2702                                                                
MASTER      334    0    7   15   14    0   19    6 3093    1   62   27          
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.