HEADER    HYDROLASE                               21-APR-98   1BA1              
TITLE     HEAT-SHOCK COGNATE 70KD PROTEIN 44KD ATPASE N-TERMINAL MUTANT WITH CYS
TITLE    2 17 REPLACED BY LYS                                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HEAT-SHOCK COGNATE 70KD PROTEIN;                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: 44KD ATPASE N-TERMINAL FRAGMENT;                           
COMPND   5 EC: 3.6.1.3;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE   3 ORGANISM_COMMON: CATTLE;                                             
SOURCE   4 ORGANISM_TAXID: 9913;                                                
SOURCE   5 CELL_LINE: BL21 (DE3);                                               
SOURCE   6 ORGAN: BRAIN;                                                        
SOURCE   7 CELLULAR_LOCATION: CYTOSOL;                                          
SOURCE   8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   9 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  10 EXPRESSION_SYSTEM_CELL_LINE: BL21 (DE3);                             
SOURCE  11 EXPRESSION_SYSTEM_VECTOR: PET21;                                     
SOURCE  12 EXPRESSION_SYSTEM_PLASMID: BL21                                      
KEYWDS    HYDROLASE, ACTING ON ACID ANHYDRIDES, ATP-BINDING, HEAT SHOCK         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.M.WILBANKS,D.B.MCKAY                                                
REVDAT   5   02-AUG-23 1BA1    1       REMARK                                   
REVDAT   4   03-NOV-21 1BA1    1       REMARK SEQADV                            
REVDAT   3   24-FEB-09 1BA1    1       VERSN                                    
REVDAT   2   01-APR-03 1BA1    1       JRNL                                     
REVDAT   1   15-JUL-98 1BA1    0                                                
JRNL        AUTH   S.M.WILBANKS,D.B.MCKAY                                       
JRNL        TITL   STRUCTURAL REPLACEMENT OF ACTIVE SITE MONOVALENT CATIONS BY  
JRNL        TITL 2 THE EPSILON-AMINO GROUP OF LYSINE IN THE ATPASE FRAGMENT OF  
JRNL        TITL 3 BOVINE HSC70.                                                
JRNL        REF    BIOCHEMISTRY                  V.  37  7456 1998              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   9585559                                                      
JRNL        DOI    10.1021/BI973046M                                            
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   K.M.FLAHERTY,S.M.WILBANKS,C.DELUCA-FLAHERTY,D.B.MCKAY        
REMARK   1  TITL   STRUCTURAL BASIS OF THE 70-KILODALTON HEAT SHOCK COGNATE     
REMARK   1  TITL 2 PROTEIN ATP HYDROLYTIC ACTIVITY. II. STRUCTURE OF THE ACTIVE 
REMARK   1  TITL 3 SITE WITH ADP OR ATP BOUND TO WILD TYPE AND MUTANT ATPASE    
REMARK   1  TITL 4 FRAGMENT                                                     
REMARK   1  REF    J.BIOL.CHEM.                  V. 269 12899 1994              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   K.M.FLAHERTY,C.DELUCA-FLAHERTY,D.B.MCKAY                     
REMARK   1  TITL   THREE-DIMENSIONAL STRUCTURE OF THE ATPASE FRAGMENT OF A 70K  
REMARK   1  TITL 2 HEAT-SHOCK COGNATE PROTEIN                                   
REMARK   1  REF    NATURE                        V. 346   623 1990              
REMARK   1  REFN                   ISSN 0028-0836                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR                                               
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 6.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 100000.000                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.1000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 94.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 45230                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.202                           
REMARK   3   FREE R VALUE                     : 0.244                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.100                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 4454                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.600                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.76                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 0.75                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 5000                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3500                       
REMARK   3   BIN FREE R VALUE                    : 0.3800                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.00                        
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 500                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.600                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2907                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 31                                      
REMARK   3   SOLVENT ATOMS            : 442                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
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) : 0.30                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 40.0                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.300                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 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  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: SCALE                                     
REMARK   3  ORTHORHOMBIC, LONGEST AXIS FIRST                                    
REMARK   4                                                                      
REMARK   4 1BA1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 100 THE DEPOSITION ID IS D_1000171510.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : OCT-95                             
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 9.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RUH2R                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : GRAPHITE(002)                      
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS                       
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 34106                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 3.200                              
REMARK 200  R MERGE                    (I) : 1.00000                            
REMARK 200  R SYM                      (I) : 0.05600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.97                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 69.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.00000                            
REMARK 200  R SYM FOR SHELL            (I) : 0.13300                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 12.00                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1HPM                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.73                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG-8000 1.0M NACL 50MM CHES, PH 9   
REMARK 280  1MM MGATP, PH 9.0                                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       71.90000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       23.05000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       32.05000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       23.05000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       71.90000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       32.05000            
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     SER A     2                                                      
REMARK 465     LYS A     3                                                      
REMARK 465     GLY A   382                                                      
REMARK 465     ASP A   383                                                      
REMARK 465     LYS A   384                                                      
REMARK 465     SER A   385                                                      
REMARK 465     GLU A   386                                                      
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     ARG A  77    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 100    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 188    CG   CD   CE   NZ                                   
REMARK 470     LYS A 248    CG   CD   CE   NZ                                   
REMARK 470     LYS A 250    CG   CD   CE   NZ                                   
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    THR A 140      -54.28   -122.72                                   
REMARK 500    LYS A 361       23.93   -141.61                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 615                                                                      
REMARK 615 ZERO OCCUPANCY ATOM                                                  
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 615   M RES C  SSEQI                                                     
REMARK 615     HOH A   564                                                      
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 487  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ADP A 486   O1B                                                    
REMARK 620 2 HOH A 560   O    96.9                                              
REMARK 620 3 HOH A 561   O   173.4  89.4                                        
REMARK 620 4 HOH A 562   O    89.8 173.3  83.8                                  
REMARK 620 5 HOH A 563   O    90.5  86.6  88.3  93.0                            
REMARK 620 6 HOH A 564   O    98.9  85.0  83.1  94.4 168.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 487                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 491                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 451                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 455                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 486                 
DBREF  1BA1 A    1   386  UNP    P19120   HSP7C_BOVIN      1    386             
SEQADV 1BA1 LYS A   17  UNP  P19120    CYS    17 ENGINEERED MUTATION            
SEQRES   1 A  386  MET SER LYS GLY PRO ALA VAL GLY ILE ASP LEU GLY THR          
SEQRES   2 A  386  THR TYR SER LYS VAL GLY VAL PHE GLN HIS GLY LYS VAL          
SEQRES   3 A  386  GLU ILE ILE ALA ASN ASP GLN GLY ASN ARG THR THR PRO          
SEQRES   4 A  386  SER TYR VAL ALA PHE THR ASP THR GLU ARG LEU ILE GLY          
SEQRES   5 A  386  ASP ALA ALA LYS ASN GLN VAL ALA MET ASN PRO THR ASN          
SEQRES   6 A  386  THR VAL PHE ASP ALA LYS ARG LEU ILE GLY ARG ARG PHE          
SEQRES   7 A  386  ASP ASP ALA VAL VAL GLN SER ASP MET LYS HIS TRP PRO          
SEQRES   8 A  386  PHE MET VAL VAL ASN ASP ALA GLY ARG PRO LYS VAL GLN          
SEQRES   9 A  386  VAL GLU TYR LYS GLY GLU THR LYS SER PHE TYR PRO GLU          
SEQRES  10 A  386  GLU VAL SER SER MET VAL LEU THR LYS MET LYS GLU ILE          
SEQRES  11 A  386  ALA GLU ALA TYR LEU GLY LYS THR VAL THR ASN ALA VAL          
SEQRES  12 A  386  VAL THR VAL PRO ALA TYR PHE ASN ASP SER GLN ARG GLN          
SEQRES  13 A  386  ALA THR LYS ASP ALA GLY THR ILE ALA GLY LEU ASN VAL          
SEQRES  14 A  386  LEU ARG ILE ILE ASN GLU PRO THR ALA ALA ALA ILE ALA          
SEQRES  15 A  386  TYR GLY LEU ASP LYS LYS VAL GLY ALA GLU ARG ASN VAL          
SEQRES  16 A  386  LEU ILE PHE ASP LEU GLY GLY GLY THR PHE ASP VAL SER          
SEQRES  17 A  386  ILE LEU THR ILE GLU ASP GLY ILE PHE GLU VAL LYS SER          
SEQRES  18 A  386  THR ALA GLY ASP THR HIS LEU GLY GLY GLU ASP PHE ASP          
SEQRES  19 A  386  ASN ARG MET VAL ASN HIS PHE ILE ALA GLU PHE LYS ARG          
SEQRES  20 A  386  LYS HIS LYS LYS ASP ILE SER GLU ASN LYS ARG ALA VAL          
SEQRES  21 A  386  ARG ARG LEU ARG THR ALA CYS GLU ARG ALA LYS ARG THR          
SEQRES  22 A  386  LEU SER SER SER THR GLN ALA SER ILE GLU ILE ASP SER          
SEQRES  23 A  386  LEU TYR GLU GLY ILE ASP PHE TYR THR SER ILE THR ARG          
SEQRES  24 A  386  ALA ARG PHE GLU GLU LEU ASN ALA ASP LEU PHE ARG GLY          
SEQRES  25 A  386  THR LEU ASP PRO VAL GLU LYS ALA LEU ARG ASP ALA LYS          
SEQRES  26 A  386  LEU ASP LYS SER GLN ILE HIS ASP ILE VAL LEU VAL GLY          
SEQRES  27 A  386  GLY SER THR ARG ILE PRO LYS ILE GLN LYS LEU LEU GLN          
SEQRES  28 A  386  ASP PHE PHE ASN GLY LYS GLU LEU ASN LYS SER ILE ASN          
SEQRES  29 A  386  PRO ASP GLU ALA VAL ALA TYR GLY ALA ALA VAL GLN ALA          
SEQRES  30 A  386  ALA ILE LEU SER GLY ASP LYS SER GLU                          
HET     MG  A 487       1                                                       
HET     NA  A 491       1                                                       
HET     CL  A 451       1                                                       
HET     CL  A 455       1                                                       
HET    ADP  A 486      27                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM      NA SODIUM ION                                                       
HETNAM      CL CHLORIDE ION                                                     
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
FORMUL   2   MG    MG 2+                                                        
FORMUL   3   NA    NA 1+                                                        
FORMUL   4   CL    2(CL 1-)                                                     
FORMUL   6  ADP    C10 H15 N5 O10 P2                                            
FORMUL   7  HOH   *442(H2 O)                                                    
HELIX    1   1 ASP A   53  GLN A   58  1                                   6    
HELIX    2   2 PRO A   63  ASN A   65  5                                   3    
HELIX    3   3 ALA A   70  ARG A   72  5                                   3    
HELIX    4   4 ALA A   81  HIS A   89  1                                   9    
HELIX    5   5 PRO A  116  LEU A  135  1                                  20    
HELIX    6   6 ASP A  152  ILE A  164  1                                  13    
HELIX    7   7 GLU A  175  TYR A  183  1                                   9    
HELIX    8   8 GLY A  230  HIS A  249  1                                  20    
HELIX    9   9 LYS A  257  SER A  275  1                                  19    
HELIX   10  10 ARG A  299  ALA A  324  1                                  26    
HELIX   11  11 LYS A  328  GLN A  330  5                                   3    
HELIX   12  12 GLY A  339  ARG A  342  5                                   4    
HELIX   13  13 PRO A  344  PHE A  353  1                                  10    
HELIX   14  14 ALA A  368  ILE A  379  1                                  12    
SHEET    1   A 5 ASN A 168  ASN A 174  0                                        
SHEET    2   A 5 ASN A 141  VAL A 146  1  N  ALA A 142   O  ASN A 168           
SHEET    3   A 5 VAL A   7  ASP A  10  1  N  VAL A   7   O  VAL A 143           
SHEET    4   A 5 LYS A  17  GLN A  22 -1  N  GLY A  19   O  GLY A   8           
SHEET    5   A 5 LYS A  25  ILE A  28 -1  N  GLU A  27   O  VAL A  20           
SHEET    1   B 2 VAL A  42  PHE A  44  0                                        
SHEET    2   B 2 ARG A  49  ILE A  51 -1  N  LEU A  50   O  ALA A  43           
SHEET    1   C 3 MET A  93  ASP A  97  0                                        
SHEET    2   C 3 ARG A 100  TYR A 107 -1  N  GLN A 104   O  MET A  93           
SHEET    3   C 3 GLU A 110  TYR A 115 -1  N  PHE A 114   O  VAL A 103           
SHEET    1   D 4 ASP A 333  VAL A 337  0                                        
SHEET    2   D 4 ARG A 193  LEU A 200  1  N  LEU A 196   O  ASP A 333           
SHEET    3   D 4 PHE A 205  GLU A 213 -1  N  ILE A 212   O  ARG A 193           
SHEET    4   D 4 ILE A 216  ASP A 225 -1  N  ASP A 225   O  PHE A 205           
SHEET    1   E 2 GLN A 279  ILE A 284  0                                        
SHEET    2   E 2 PHE A 293  THR A 298 -1  N  ILE A 297   O  ALA A 280           
LINK         O1B ADP A 486                MG    MG A 487     1555   1555  2.17  
LINK        MG    MG A 487                 O   HOH A 560     1555   1555  2.09  
LINK        MG    MG A 487                 O   HOH A 561     1555   1555  2.21  
LINK        MG    MG A 487                 O   HOH A 562     1555   1555  2.11  
LINK        MG    MG A 487                 O   HOH A 563     1555   1555  2.12  
LINK        MG    MG A 487                 O   HOH A 564     1555   1555  1.91  
LINK        NA    NA A 491                 O   HOH A 564     1555   1555  2.92  
CISPEP   1 GLY A    4    PRO A    5          0        -0.63                     
SITE     1 AC1  5 ADP A 486  HOH A 560  HOH A 561  HOH A 562                    
SITE     2 AC1  5 HOH A 563                                                     
SITE     1 AC2  3 ASP A 199  THR A 204  ASP A 206                               
SITE     1 AC3  4 TYR A 183  LYS A 345  LYS A 348  HOH A 537                    
SITE     1 AC4  4 ASN A  31  ASP A  32  GLN A  33  LYS A 126                    
SITE     1 AC5 25 GLY A  12  THR A  13  THR A  14  TYR A  15                    
SITE     2 AC5 25 LYS A  17  GLY A 201  GLY A 202  GLY A 230                    
SITE     3 AC5 25 GLU A 268  LYS A 271  ARG A 272  SER A 275                    
SITE     4 AC5 25 GLY A 338  GLY A 339  SER A 340  ARG A 342                    
SITE     5 AC5 25  MG A 487  HOH A 547  HOH A 560  HOH A 562                    
SITE     6 AC5 25 HOH A 563  HOH A 587  HOH A 819  HOH A1053                    
SITE     7 AC5 25 HOH A1054                                                     
CRYST1  143.800   64.100   46.100  90.00  90.00  90.00 P 21 21 21    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      0.006954  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015601  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.021692        0.00000                         
ATOM      1  N   GLY A   4      17.148  16.139  -6.958  1.00 36.14           N  
ATOM      2  CA  GLY A   4      16.014  17.101  -6.858  1.00 35.80           C  
ATOM      3  C   GLY A   4      16.272  18.451  -7.507  1.00 35.24           C  
ATOM      4  O   GLY A   4      15.594  18.799  -8.473  1.00 38.85           O  
ATOM      5  N   PRO A   5      17.281  19.217  -7.047  1.00 33.10           N  
ATOM      6  CA  PRO A   5      18.179  18.873  -5.936  1.00 30.40           C  
ATOM      7  C   PRO A   5      17.451  18.750  -4.601  1.00 26.22           C  
ATOM      8  O   PRO A   5      16.306  19.193  -4.464  1.00 25.97           O  
ATOM      9  CB  PRO A   5      19.179  20.034  -5.941  1.00 30.96           C  
ATOM     10  CG  PRO A   5      18.348  21.188  -6.414  1.00 32.58           C  
ATOM     11  CD  PRO A   5      17.559  20.574  -7.547  1.00 34.12           C  
ATOM     12  N   ALA A   6      18.065  18.022  -3.675  1.00 21.26           N  
ATOM     13  CA  ALA A   6      17.492  17.849  -2.349  1.00 16.83           C  
ATOM     14  C   ALA A   6      17.985  19.064  -1.574  1.00 15.44           C  
ATOM     15  O   ALA A   6      19.015  19.640  -1.925  1.00 14.97           O  
ATOM     16  CB  ALA A   6      17.996  16.572  -1.719  1.00 13.15           C  
ATOM     17  N   VAL A   7      17.245  19.483  -0.556  1.00 12.33           N  
ATOM     18  CA  VAL A   7      17.652  20.645   0.223  1.00 10.29           C  
ATOM     19  C   VAL A   7      17.896  20.277   1.674  1.00  8.68           C  
ATOM     20  O   VAL A   7      17.518  19.193   2.124  1.00  7.51           O  
ATOM     21  CB  VAL A   7      16.596  21.776   0.165  1.00 11.96           C  
ATOM     22  CG1 VAL A   7      16.376  22.230  -1.287  1.00 12.05           C  
ATOM     23  CG2 VAL A   7      15.283  21.315   0.805  1.00 11.78           C  
ATOM     24  N   GLY A   8      18.579  21.164   2.381  1.00  8.69           N  
ATOM     25  CA  GLY A   8      18.854  20.955   3.787  1.00  6.76           C  
ATOM     26  C   GLY A   8      18.080  22.012   4.544  1.00  6.41           C  
ATOM     27  O   GLY A   8      18.138  23.198   4.200  1.00  6.27           O  
ATOM     28  N   ILE A   9      17.330  21.597   5.558  1.00  7.24           N  
ATOM     29  CA  ILE A   9      16.544  22.541   6.329  1.00  7.99           C  
ATOM     30  C   ILE A   9      16.827  22.462   7.820  1.00  7.93           C  
ATOM     31  O   ILE A   9      16.773  21.387   8.430  1.00  7.70           O  
ATOM     32  CB  ILE A   9      15.028  22.336   6.109  1.00  8.27           C  
ATOM     33  CG1 ILE A   9      14.696  22.401   4.612  1.00  8.13           C  
ATOM     34  CG2 ILE A   9      14.239  23.407   6.869  1.00 10.20           C  
ATOM     35  CD1 ILE A   9      13.257  22.046   4.276  1.00  5.40           C  
ATOM     36  N   ASP A  10      17.143  23.618   8.386  1.00  7.93           N  
ATOM     37  CA  ASP A  10      17.395  23.767   9.809  1.00  7.67           C  
ATOM     38  C   ASP A  10      16.084  24.329  10.374  1.00  6.80           C  
ATOM     39  O   ASP A  10      15.757  25.503  10.166  1.00  6.86           O  
ATOM     40  CB  ASP A  10      18.549  24.754  10.024  1.00  8.20           C  
ATOM     41  CG  ASP A  10      18.734  25.161  11.482  1.00  9.53           C  
ATOM     42  OD1 ASP A  10      18.072  24.621  12.396  1.00  8.05           O  
ATOM     43  OD2 ASP A  10      19.572  26.044  11.721  1.00  8.81           O  
ATOM     44  N   LEU A  11      15.318  23.472  11.042  1.00  4.94           N  
ATOM     45  CA  LEU A  11      14.049  23.871  11.637  1.00  6.61           C  
ATOM     46  C   LEU A  11      14.379  24.354  13.047  1.00  6.35           C  
ATOM     47  O   LEU A  11      14.350  23.579  13.995  1.00  7.64           O  
ATOM     48  CB  LEU A  11      13.094  22.665  11.670  1.00  5.79           C  
ATOM     49  CG  LEU A  11      11.713  22.810  12.323  1.00  5.82           C  
ATOM     50  CD1 LEU A  11      10.953  23.985  11.720  1.00  8.60           C  
ATOM     51  CD2 LEU A  11      10.929  21.511  12.153  1.00  6.39           C  
ATOM     52  N   GLY A  12      14.723  25.635  13.173  1.00  5.62           N  
ATOM     53  CA  GLY A  12      15.096  26.173  14.468  1.00  7.49           C  
ATOM     54  C   GLY A  12      13.957  26.501  15.414  1.00  6.62           C  
ATOM     55  O   GLY A  12      12.802  26.625  15.006  1.00  7.85           O  
ATOM     56  N   THR A  13      14.276  26.613  16.698  1.00  6.93           N  
ATOM     57  CA  THR A  13      13.266  26.957  17.687  1.00  6.01           C  
ATOM     58  C   THR A  13      12.716  28.352  17.379  1.00  6.33           C  
ATOM     59  O   THR A  13      11.507  28.585  17.452  1.00  8.58           O  
ATOM     60  CB  THR A  13      13.853  26.958  19.111  1.00  7.56           C  
ATOM     61  OG1 THR A  13      14.322  25.645  19.434  1.00  8.63           O  
ATOM     62  CG2 THR A  13      12.804  27.398  20.131  1.00  6.13           C  
ATOM     63  N   THR A  14      13.600  29.265  16.999  1.00  6.59           N  
ATOM     64  CA  THR A  14      13.199  30.630  16.705  1.00  7.38           C  
ATOM     65  C   THR A  14      13.278  31.026  15.225  1.00  7.64           C  
ATOM     66  O   THR A  14      12.422  31.771  14.738  1.00  8.04           O  
ATOM     67  CB  THR A  14      13.998  31.614  17.577  1.00  9.14           C  
ATOM     68  OG1 THR A  14      15.391  31.530  17.251  1.00 13.11           O  
ATOM     69  CG2 THR A  14      13.830  31.245  19.048  1.00 10.95           C  
ATOM     70  N   TYR A  15      14.304  30.558  14.521  1.00  7.04           N  
ATOM     71  CA  TYR A  15      14.464  30.859  13.098  1.00  7.61           C  
ATOM     72  C   TYR A  15      14.836  29.601  12.337  1.00  8.20           C  
ATOM     73  O   TYR A  15      15.610  28.771  12.828  1.00  7.15           O  
ATOM     74  CB  TYR A  15      15.572  31.893  12.846  1.00  8.45           C  
ATOM     75  CG  TYR A  15      15.278  33.308  13.290  1.00  8.36           C  
ATOM     76  CD1 TYR A  15      14.668  34.224  12.430  1.00  7.41           C  
ATOM     77  CD2 TYR A  15      15.649  33.744  14.561  1.00 10.77           C  
ATOM     78  CE1 TYR A  15      14.447  35.546  12.827  1.00  8.03           C  
ATOM     79  CE2 TYR A  15      15.433  35.055  14.965  1.00 11.66           C  
ATOM     80  CZ  TYR A  15      14.834  35.951  14.098  1.00 11.97           C  
ATOM     81  OH  TYR A  15      14.659  37.255  14.507  1.00 15.08           O  
ATOM     82  N   SER A  16      14.315  29.492  11.122  1.00  6.23           N  
ATOM     83  CA  SER A  16      14.592  28.361  10.249  1.00  7.55           C  
ATOM     84  C   SER A  16      15.382  28.833   9.030  1.00  5.59           C  
ATOM     85  O   SER A  16      15.324  30.008   8.653  1.00  6.14           O  
ATOM     86  CB  SER A  16      13.294  27.679   9.822  1.00  7.40           C  
ATOM     87  OG  SER A  16      12.683  27.055  10.937  1.00  7.22           O  
ATOM     88  N   LYS A  17      16.155  27.922   8.448  1.00  7.05           N  
ATOM     89  CA  LYS A  17      16.988  28.235   7.290  1.00  7.49           C  
ATOM     90  C   LYS A  17      16.967  27.070   6.316  1.00  7.97           C  
ATOM     91  O   LYS A  17      16.770  25.921   6.715  1.00  7.89           O  
ATOM     92  CB  LYS A  17      18.444  28.498   7.714  1.00  6.01           C  
ATOM     93  CG  LYS A  17      18.638  29.520   8.829  1.00  6.02           C  
ATOM     94  CD  LYS A  17      18.472  28.905  10.214  1.00  7.52           C  
ATOM     95  CE  LYS A  17      18.585  29.969  11.298  1.00  7.73           C  
ATOM     96  NZ  LYS A  17      18.490  29.391  12.666  1.00  5.79           N  
ATOM     97  N   VAL A  18      17.169  27.370   5.038  1.00  8.40           N  
ATOM     98  CA  VAL A  18      17.186  26.342   4.015  1.00  6.70           C  
ATOM     99  C   VAL A  18      18.356  26.574   3.066  1.00  7.23           C  
ATOM    100  O   VAL A  18      18.640  27.708   2.674  1.00  8.20           O  
ATOM    101  CB  VAL A  18      15.833  26.268   3.245  1.00  6.41           C  
ATOM    102  CG1 VAL A  18      15.530  27.575   2.527  1.00  6.97           C  
ATOM    103  CG2 VAL A  18      15.834  25.080   2.282  1.00  8.34           C  
ATOM    104  N   GLY A  19      19.074  25.502   2.767  1.00  9.21           N  
ATOM    105  CA  GLY A  19      20.210  25.593   1.873  1.00  8.99           C  
ATOM    106  C   GLY A  19      20.165  24.512   0.818  1.00  9.04           C  
ATOM    107  O   GLY A  19      19.473  23.496   0.974  1.00  8.66           O  
ATOM    108  N   VAL A  20      20.900  24.727  -0.266  1.00  8.81           N  
ATOM    109  CA  VAL A  20      20.952  23.756  -1.351  1.00 11.19           C  
ATOM    110  C   VAL A  20      22.370  23.697  -1.892  1.00 11.02           C  
ATOM    111  O   VAL A  20      23.019  24.734  -2.073  1.00  9.58           O  
ATOM    112  CB  VAL A  20      19.934  24.089  -2.498  1.00 11.11           C  
ATOM    113  CG1 VAL A  20      20.274  25.415  -3.181  1.00  9.44           C  
ATOM    114  CG2 VAL A  20      19.888  22.944  -3.504  1.00 10.94           C  
ATOM    115  N   PHE A  21      22.871  22.479  -2.067  1.00 12.04           N  
ATOM    116  CA  PHE A  21      24.214  22.262  -2.580  1.00 13.79           C  
ATOM    117  C   PHE A  21      24.133  22.122  -4.103  1.00 16.54           C  
ATOM    118  O   PHE A  21      23.413  21.262  -4.631  1.00 16.86           O  
ATOM    119  CB  PHE A  21      24.816  21.004  -1.944  1.00 14.32           C  
ATOM    120  CG  PHE A  21      26.244  20.742  -2.327  1.00 16.07           C  
ATOM    121  CD1 PHE A  21      27.285  21.284  -1.590  1.00 17.88           C  
ATOM    122  CD2 PHE A  21      26.549  19.903  -3.396  1.00 19.67           C  
ATOM    123  CE1 PHE A  21      28.609  20.995  -1.905  1.00 19.12           C  
ATOM    124  CE2 PHE A  21      27.872  19.609  -3.721  1.00 21.16           C  
ATOM    125  CZ  PHE A  21      28.902  20.157  -2.967  1.00 19.23           C  
ATOM    126  N   GLN A  22      24.816  23.023  -4.800  1.00 16.86           N  
ATOM    127  CA  GLN A  22      24.851  23.023  -6.255  1.00 19.72           C  
ATOM    128  C   GLN A  22      26.246  23.419  -6.716  1.00 19.89           C  
ATOM    129  O   GLN A  22      26.886  24.286  -6.115  1.00 17.07           O  
ATOM    130  CB  GLN A  22      23.830  24.006  -6.833  1.00 22.03           C  
ATOM    131  CG  GLN A  22      22.372  23.613  -6.633  1.00 25.54           C  
ATOM    132  CD  GLN A  22      21.420  24.485  -7.436  1.00 26.94           C  
ATOM    133  OE1 GLN A  22      21.401  25.709  -7.288  1.00 28.36           O  
ATOM    134  NE2 GLN A  22      20.626  23.858  -8.296  1.00 29.39           N  
ATOM    135  N   HIS A  23      26.727  22.729  -7.747  1.00 20.58           N  
ATOM    136  CA  HIS A  23      28.041  22.978  -8.331  1.00 21.33           C  
ATOM    137  C   HIS A  23      29.164  23.056  -7.302  1.00 21.47           C  
ATOM    138  O   HIS A  23      30.008  23.954  -7.342  1.00 21.79           O  
ATOM    139  CB  HIS A  23      27.994  24.233  -9.205  1.00 22.06           C  
ATOM    140  CG  HIS A  23      27.163  24.069 -10.446  1.00 25.11           C  
ATOM    141  ND1 HIS A  23      26.044  24.826 -10.698  1.00 25.25           N  
ATOM    142  CD2 HIS A  23      27.300  23.225 -11.500  1.00 24.33           C  
ATOM    143  CE1 HIS A  23      25.520  24.461 -11.861  1.00 25.03           C  
ATOM    144  NE2 HIS A  23      26.262  23.495 -12.362  1.00 24.25           N  
ATOM    145  N   GLY A  24      29.173  22.086  -6.393  1.00 21.68           N  
ATOM    146  CA  GLY A  24      30.188  22.034  -5.358  1.00 21.67           C  
ATOM    147  C   GLY A  24      30.119  23.114  -4.292  1.00 22.60           C  
ATOM    148  O   GLY A  24      31.040  23.229  -3.478  1.00 23.58           O  
ATOM    149  N   LYS A  25      29.036  23.890  -4.261  1.00 20.98           N  
ATOM    150  CA  LYS A  25      28.901  24.956  -3.274  1.00 18.40           C  
ATOM    151  C   LYS A  25      27.519  24.937  -2.655  1.00 17.36           C  
ATOM    152  O   LYS A  25      26.546  24.543  -3.299  1.00 15.13           O  
ATOM    153  CB  LYS A  25      29.110  26.330  -3.919  1.00 20.83           C  
ATOM    154  CG  LYS A  25      30.312  26.436  -4.837  1.00 25.82           C  
ATOM    155  CD  LYS A  25      30.468  27.853  -5.362  1.00 28.56           C  
ATOM    156  CE  LYS A  25      29.187  28.379  -5.993  1.00 31.77           C  
ATOM    157  NZ  LYS A  25      28.943  27.879  -7.377  1.00 32.25           N  
ATOM    158  N   VAL A  26      27.439  25.382  -1.410  1.00 15.53           N  
ATOM    159  CA  VAL A  26      26.169  25.445  -0.716  1.00 14.12           C  
ATOM    160  C   VAL A  26      25.636  26.862  -0.799  1.00 14.41           C  
ATOM    161  O   VAL A  26      26.375  27.826  -0.605  1.00 13.63           O  
ATOM    162  CB  VAL A  26      26.296  25.076   0.782  1.00 12.50           C  
ATOM    163  CG1 VAL A  26      24.944  25.277   1.485  1.00  9.49           C  
ATOM    164  CG2 VAL A  26      26.752  23.640   0.905  1.00 10.42           C  
ATOM    165  N   GLU A  27      24.359  26.970  -1.126  1.00 14.44           N  
ATOM    166  CA  GLU A  27      23.686  28.242  -1.203  1.00 15.18           C  
ATOM    167  C   GLU A  27      22.595  28.319  -0.109  1.00 12.61           C  
ATOM    168  O   GLU A  27      21.708  27.466  -0.077  1.00 11.39           O  
ATOM    169  CB  GLU A  27      23.158  28.395  -2.623  1.00 19.01           C  
ATOM    170  CG  GLU A  27      21.762  28.941  -2.781  1.00 28.12           C  
ATOM    171  CD  GLU A  27      21.669  30.456  -2.616  1.00 34.44           C  
ATOM    172  OE1 GLU A  27      22.681  31.237  -2.889  1.00 33.99           O  
ATOM    173  OE2 GLU A  27      20.576  30.903  -2.178  1.00 41.49           O  
ATOM    174  N   ILE A  28      22.721  29.292   0.802  1.00 10.68           N  
ATOM    175  CA  ILE A  28      21.773  29.506   1.892  1.00 10.40           C  
ATOM    176  C   ILE A  28      20.765  30.456   1.251  1.00 10.84           C  
ATOM    177  O   ILE A  28      21.080  31.622   0.946  1.00 11.77           O  
ATOM    178  CB  ILE A  28      22.453  30.104   3.147  1.00 10.81           C  
ATOM    179  CG1 ILE A  28      23.507  29.123   3.671  1.00  8.57           C  
ATOM    180  CG2 ILE A  28      21.403  30.386   4.185  1.00 11.74           C  
ATOM    181  CD1 ILE A  28      22.976  27.722   4.023  1.00  8.86           C  
ATOM    182  N   ILE A  29      19.568  29.931   0.995  1.00 11.45           N  
ATOM    183  CA  ILE A  29      18.516  30.680   0.315  1.00 10.14           C  
ATOM    184  C   ILE A  29      17.767  31.785   1.074  1.00  9.95           C  
ATOM    185  O   ILE A  29      17.248  31.558   2.164  1.00 10.47           O  
ATOM    186  CB  ILE A  29      17.505  29.675  -0.246  1.00  8.84           C  
ATOM    187  CG1 ILE A  29      18.255  28.534  -0.955  1.00  9.02           C  
ATOM    188  CG2 ILE A  29      16.541  30.378  -1.211  1.00  7.69           C  
ATOM    189  CD1 ILE A  29      17.411  27.361  -1.359  1.00  8.15           C  
ATOM    190  N   ALA A  30      17.711  32.966   0.457  1.00  9.27           N  
ATOM    191  CA  ALA A  30      17.015  34.127   1.042  1.00 10.55           C  
ATOM    192  C   ALA A  30      15.531  34.028   0.694  1.00 10.85           C  
ATOM    193  O   ALA A  30      15.171  33.553  -0.396  1.00  9.54           O  
ATOM    194  CB  ALA A  30      17.603  35.420   0.490  1.00 13.12           C  
ATOM    195  N   ASN A  31      14.677  34.456   1.620  1.00  9.83           N  
ATOM    196  CA  ASN A  31      13.228  34.422   1.406  1.00 10.87           C  
ATOM    197  C   ASN A  31      12.723  35.637   0.629  1.00 12.05           C  
ATOM    198  O   ASN A  31      13.513  36.467   0.178  1.00 11.42           O  
ATOM    199  CB  ASN A  31      12.478  34.237   2.742  1.00  9.59           C  
ATOM    200  CG  ASN A  31      12.635  35.412   3.704  1.00  6.61           C  
ATOM    201  OD1 ASN A  31      12.888  36.544   3.298  1.00  8.88           O  
ATOM    202  ND2 ASN A  31      12.431  35.146   4.992  1.00  5.09           N  
ATOM    203  N   ASP A  32      11.405  35.731   0.475  1.00 14.71           N  
ATOM    204  CA  ASP A  32      10.777  36.839  -0.255  1.00 15.70           C  
ATOM    205  C   ASP A  32      11.196  38.216   0.232  1.00 16.59           C  
ATOM    206  O   ASP A  32      11.137  39.182  -0.526  1.00 15.15           O  
ATOM    207  CB  ASP A  32       9.247  36.759  -0.179  1.00 18.59           C  
ATOM    208  CG  ASP A  32       8.671  35.565  -0.922  1.00 24.04           C  
ATOM    209  OD1 ASP A  32       9.438  34.770  -1.508  1.00 27.48           O  
ATOM    210  OD2 ASP A  32       7.430  35.425  -0.920  1.00 26.21           O  
ATOM    211  N   GLN A  33      11.573  38.312   1.505  1.00 15.62           N  
ATOM    212  CA  GLN A  33      11.989  39.582   2.089  1.00 14.48           C  
ATOM    213  C   GLN A  33      13.504  39.778   2.031  1.00 13.97           C  
ATOM    214  O   GLN A  33      14.019  40.770   2.544  1.00 16.41           O  
ATOM    215  CB  GLN A  33      11.504  39.688   3.541  1.00 14.99           C  
ATOM    216  CG  GLN A  33       9.982  39.736   3.713  1.00 14.22           C  
ATOM    217  CD  GLN A  33       9.290  38.444   3.319  1.00 15.68           C  
ATOM    218  OE1 GLN A  33       8.434  38.429   2.435  1.00 16.26           O  
ATOM    219  NE2 GLN A  33       9.662  37.350   3.968  1.00 11.90           N  
ATOM    220  N   GLY A  34      14.208  38.845   1.392  1.00 12.35           N  
ATOM    221  CA  GLY A  34      15.658  38.929   1.292  1.00 10.27           C  
ATOM    222  C   GLY A  34      16.375  38.435   2.540  1.00 10.19           C  
ATOM    223  O   GLY A  34      17.587  38.611   2.684  1.00 11.05           O  
ATOM    224  N   ASN A  35      15.643  37.763   3.424  1.00  9.03           N  
ATOM    225  CA  ASN A  35      16.221  37.258   4.664  1.00  7.91           C  
ATOM    226  C   ASN A  35      16.690  35.818   4.564  1.00  8.07           C  
ATOM    227  O   ASN A  35      15.938  34.943   4.126  1.00  8.00           O  
ATOM    228  CB  ASN A  35      15.217  37.408   5.799  1.00  8.51           C  
ATOM    229  CG  ASN A  35      14.813  38.841   6.013  1.00 10.26           C  
ATOM    230  OD1 ASN A  35      15.647  39.742   5.958  1.00 11.05           O  
ATOM    231  ND2 ASN A  35      13.532  39.070   6.236  1.00  8.45           N  
ATOM    232  N   ARG A  36      17.933  35.578   4.976  1.00  7.89           N  
ATOM    233  CA  ARG A  36      18.536  34.245   4.940  1.00  7.99           C  
ATOM    234  C   ARG A  36      18.040  33.319   6.060  1.00  8.30           C  
ATOM    235  O   ARG A  36      18.410  32.139   6.108  1.00  9.02           O  
ATOM    236  CB  ARG A  36      20.065  34.352   4.933  1.00  8.56           C  
ATOM    237  CG  ARG A  36      20.612  34.949   3.633  1.00 13.54           C  
ATOM    238  CD  ARG A  36      22.041  35.468   3.778  1.00 15.34           C  
ATOM    239  NE  ARG A  36      23.041  34.404   3.846  1.00 15.40           N  
ATOM    240  CZ  ARG A  36      23.720  33.941   2.798  1.00 15.33           C  
ATOM    241  NH1 ARG A  36      23.495  34.423   1.583  1.00 17.36           N  
ATOM    242  NH2 ARG A  36      24.614  32.976   2.960  1.00 12.40           N  
ATOM    243  N   THR A  37      17.264  33.877   6.992  1.00  8.40           N  
ATOM    244  CA  THR A  37      16.657  33.098   8.073  1.00  7.80           C  
ATOM    245  C   THR A  37      15.178  33.497   8.066  1.00  7.71           C  
ATOM    246  O   THR A  37      14.832  34.609   7.648  1.00  7.36           O  
ATOM    247  CB  THR A  37      17.263  33.398   9.475  1.00  8.49           C  
ATOM    248  OG1 THR A  37      16.923  34.731   9.882  1.00 10.38           O  
ATOM    249  CG2 THR A  37      18.778  33.217   9.476  1.00  7.18           C  
ATOM    250  N   THR A  38      14.315  32.601   8.528  1.00  8.06           N  
ATOM    251  CA  THR A  38      12.880  32.843   8.558  1.00  7.34           C  
ATOM    252  C   THR A  38      12.303  32.464   9.921  1.00  8.02           C  
ATOM    253  O   THR A  38      12.484  31.340  10.379  1.00  7.60           O  
ATOM    254  CB  THR A  38      12.186  32.016   7.451  1.00  8.27           C  
ATOM    255  OG1 THR A  38      12.622  32.485   6.171  1.00  9.95           O  
ATOM    256  CG2 THR A  38      10.667  32.130   7.538  1.00  8.99           C  
ATOM    257  N   PRO A  39      11.604  33.405  10.589  1.00  8.78           N  
ATOM    258  CA  PRO A  39      11.010  33.130  11.906  1.00  9.35           C  
ATOM    259  C   PRO A  39      10.133  31.879  11.905  1.00  8.35           C  
ATOM    260  O   PRO A  39       9.324  31.681  10.996  1.00  8.62           O  
ATOM    261  CB  PRO A  39      10.173  34.384  12.167  1.00  7.67           C  
ATOM    262  CG  PRO A  39      10.973  35.458  11.504  1.00  7.52           C  
ATOM    263  CD  PRO A  39      11.356  34.804  10.191  1.00  8.21           C  
ATOM    264  N   SER A  40      10.325  31.022  12.905  1.00  7.82           N  
ATOM    265  CA  SER A  40       9.530  29.801  13.032  1.00  8.59           C  
ATOM    266  C   SER A  40       8.220  30.205  13.726  1.00  9.46           C  
ATOM    267  O   SER A  40       7.919  29.757  14.840  1.00  9.04           O  
ATOM    268  CB  SER A  40      10.301  28.752  13.850  1.00  8.48           C  
ATOM    269  OG  SER A  40      11.565  28.461  13.260  1.00  6.05           O  
ATOM    270  N   TYR A  41       7.479  31.099  13.070  1.00  8.48           N  
ATOM    271  CA  TYR A  41       6.214  31.637  13.578  1.00  8.38           C  
ATOM    272  C   TYR A  41       5.071  31.392  12.600  1.00  9.25           C  
ATOM    273  O   TYR A  41       5.271  31.413  11.384  1.00  8.38           O  
ATOM    274  CB  TYR A  41       6.321  33.157  13.757  1.00  7.95           C  
ATOM    275  CG  TYR A  41       6.981  33.624  15.033  1.00 11.49           C  
ATOM    276  CD1 TYR A  41       8.277  33.227  15.364  1.00 13.52           C  
ATOM    277  CD2 TYR A  41       6.297  34.456  15.920  1.00 13.02           C  
ATOM    278  CE1 TYR A  41       8.880  33.654  16.541  1.00 15.59           C  
ATOM    279  CE2 TYR A  41       6.887  34.890  17.104  1.00 14.53           C  
ATOM    280  CZ  TYR A  41       8.176  34.480  17.412  1.00 17.45           C  
ATOM    281  OH  TYR A  41       8.761  34.889  18.591  1.00 19.28           O  
ATOM    282  N   VAL A  42       3.870  31.211  13.142  1.00 10.20           N  
ATOM    283  CA  VAL A  42       2.657  31.019  12.343  1.00  9.88           C  
ATOM    284  C   VAL A  42       1.557  31.790  13.084  1.00 11.20           C  
ATOM    285  O   VAL A  42       1.390  31.629  14.292  1.00 11.06           O  
ATOM    286  CB  VAL A  42       2.247  29.520  12.210  1.00 10.56           C  
ATOM    287  CG1 VAL A  42       0.997  29.396  11.336  1.00 12.17           C  
ATOM    288  CG2 VAL A  42       3.362  28.712  11.588  1.00  7.78           C  
ATOM    289  N   ALA A  43       0.840  32.656  12.375  1.00  9.52           N  
ATOM    290  CA  ALA A  43      -0.224  33.449  12.989  1.00 10.84           C  
ATOM    291  C   ALA A  43      -1.557  33.188  12.312  1.00  9.98           C  
ATOM    292  O   ALA A  43      -1.611  32.884  11.120  1.00 10.90           O  
ATOM    293  CB  ALA A  43       0.106  34.933  12.927  1.00  8.29           C  
ATOM    294  N   PHE A  44      -2.629  33.300  13.085  1.00 10.09           N  
ATOM    295  CA  PHE A  44      -3.977  33.081  12.577  1.00  9.05           C  
ATOM    296  C   PHE A  44      -4.812  34.320  12.897  1.00 10.20           C  
ATOM    297  O   PHE A  44      -4.749  34.848  14.011  1.00 10.26           O  
ATOM    298  CB  PHE A  44      -4.578  31.840  13.231  1.00  9.63           C  
ATOM    299  CG  PHE A  44      -3.758  30.593  13.031  1.00  9.91           C  
ATOM    300  CD1 PHE A  44      -2.699  30.293  13.888  1.00  9.23           C  
ATOM    301  CD2 PHE A  44      -4.034  29.726  11.977  1.00 11.91           C  
ATOM    302  CE1 PHE A  44      -1.925  29.147  13.700  1.00  9.27           C  
ATOM    303  CE2 PHE A  44      -3.263  28.571  11.777  1.00 11.04           C  
ATOM    304  CZ  PHE A  44      -2.206  28.284  12.644  1.00 10.67           C  
ATOM    305  N   THR A  45      -5.558  34.811  11.911  1.00  9.51           N  
ATOM    306  CA  THR A  45      -6.379  36.000  12.102  1.00  9.57           C  
ATOM    307  C   THR A  45      -7.810  35.721  11.660  1.00  9.92           C  
ATOM    308  O   THR A  45      -8.171  34.575  11.386  1.00  9.70           O  
ATOM    309  CB  THR A  45      -5.820  37.199  11.280  1.00  9.59           C  
ATOM    310  OG1 THR A  45      -6.052  36.985   9.880  1.00 10.97           O  
ATOM    311  CG2 THR A  45      -4.322  37.356  11.506  1.00 11.68           C  
ATOM    312  N   ASP A  46      -8.628  36.768  11.624  1.00  9.81           N  
ATOM    313  CA  ASP A  46     -10.008  36.643  11.182  1.00 11.87           C  
ATOM    314  C   ASP A  46     -10.067  36.271   9.713  1.00 10.53           C  
ATOM    315  O   ASP A  46     -11.080  35.748   9.251  1.00 11.00           O  
ATOM    316  CB  ASP A  46     -10.758  37.967  11.341  1.00 11.89           C  
ATOM    317  CG  ASP A  46     -11.212  38.226  12.755  1.00 12.24           C  
ATOM    318  OD1 ASP A  46     -11.208  37.290  13.582  1.00 13.50           O  
ATOM    319  OD2 ASP A  46     -11.590  39.383  13.040  1.00 16.47           O  
ATOM    320  N   THR A  47      -8.990  36.535   8.979  1.00 10.84           N  
ATOM    321  CA  THR A  47      -8.982  36.265   7.547  1.00 11.04           C  
ATOM    322  C   THR A  47      -7.809  35.509   6.935  1.00 11.14           C  
ATOM    323  O   THR A  47      -7.895  35.098   5.787  1.00 12.78           O  
ATOM    324  CB  THR A  47      -9.137  37.580   6.749  1.00 11.34           C  
ATOM    325  OG1 THR A  47      -8.084  38.481   7.108  1.00 11.22           O  
ATOM    326  CG2 THR A  47     -10.474  38.243   7.043  1.00 10.50           C  
ATOM    327  N   GLU A  48      -6.692  35.365   7.639  1.00 11.78           N  
ATOM    328  CA  GLU A  48      -5.567  34.659   7.029  1.00 12.27           C  
ATOM    329  C   GLU A  48      -4.673  33.913   7.992  1.00 10.74           C  
ATOM    330  O   GLU A  48      -4.772  34.073   9.204  1.00 11.20           O  
ATOM    331  CB  GLU A  48      -4.679  35.614   6.209  1.00 17.38           C  
ATOM    332  CG  GLU A  48      -5.134  37.063   6.138  1.00 18.75           C  
ATOM    333  CD  GLU A  48      -4.057  37.990   5.626  1.00 20.21           C  
ATOM    334  OE1 GLU A  48      -3.574  37.798   4.489  1.00 23.16           O  
ATOM    335  OE2 GLU A  48      -3.685  38.915   6.371  1.00 18.59           O  
ATOM    336  N   ARG A  49      -3.822  33.070   7.422  1.00  9.66           N  
ATOM    337  CA  ARG A  49      -2.841  32.311   8.175  1.00 10.82           C  
ATOM    338  C   ARG A  49      -1.540  32.887   7.642  1.00 11.54           C  
ATOM    339  O   ARG A  49      -1.305  32.873   6.426  1.00 12.80           O  
ATOM    340  CB  ARG A  49      -2.920  30.827   7.839  1.00 13.17           C  
ATOM    341  CG  ARG A  49      -1.791  30.005   8.440  1.00 14.50           C  
ATOM    342  CD  ARG A  49      -1.807  28.586   7.915  1.00 16.91           C  
ATOM    343  NE  ARG A  49      -3.004  27.867   8.342  1.00 21.52           N  
ATOM    344  CZ  ARG A  49      -3.201  26.563   8.166  1.00 24.73           C  
ATOM    345  NH1 ARG A  49      -2.274  25.815   7.571  1.00 26.04           N  
ATOM    346  NH2 ARG A  49      -4.325  26.003   8.593  1.00 23.78           N  
ATOM    347  N   LEU A  50      -0.725  33.438   8.532  1.00 10.44           N  
ATOM    348  CA  LEU A  50       0.543  34.048   8.144  1.00 11.03           C  
ATOM    349  C   LEU A  50       1.689  33.172   8.647  1.00 10.62           C  
ATOM    350  O   LEU A  50       1.565  32.550   9.696  1.00 10.53           O  
ATOM    351  CB  LEU A  50       0.631  35.465   8.732  1.00 10.62           C  
ATOM    352  CG  LEU A  50      -0.562  36.399   8.450  1.00 12.82           C  
ATOM    353  CD1 LEU A  50      -0.499  37.628   9.337  1.00 11.03           C  
ATOM    354  CD2 LEU A  50      -0.617  36.798   6.985  1.00 11.44           C  
ATOM    355  N   ILE A  51       2.777  33.083   7.886  1.00 11.00           N  
ATOM    356  CA  ILE A  51       3.926  32.261   8.280  1.00 10.24           C  
ATOM    357  C   ILE A  51       5.245  33.023   8.098  1.00 10.42           C  
ATOM    358  O   ILE A  51       5.364  33.872   7.212  1.00 11.44           O  
ATOM    359  CB  ILE A  51       3.990  30.918   7.466  1.00 11.49           C  
ATOM    360  CG1 ILE A  51       2.744  30.057   7.716  1.00 11.74           C  
ATOM    361  CG2 ILE A  51       5.210  30.092   7.867  1.00  8.37           C  
ATOM    362  CD1 ILE A  51       1.687  30.188   6.662  1.00 16.95           C  
ATOM    363  N   GLY A  52       6.202  32.760   8.988  1.00  9.13           N  
ATOM    364  CA  GLY A  52       7.507  33.391   8.908  1.00  7.87           C  
ATOM    365  C   GLY A  52       7.520  34.869   9.243  1.00  8.84           C  
ATOM    366  O   GLY A  52       6.935  35.289  10.242  1.00 10.75           O  
ATOM    367  N   ASP A  53       8.187  35.657   8.399  1.00  7.90           N  
ATOM    368  CA  ASP A  53       8.292  37.106   8.589  1.00  8.89           C  
ATOM    369  C   ASP A  53       6.932  37.758   8.785  1.00  8.62           C  
ATOM    370  O   ASP A  53       6.752  38.546   9.708  1.00  9.57           O  
ATOM    371  CB  ASP A  53       9.023  37.766   7.405  1.00  9.67           C  
ATOM    372  CG  ASP A  53      10.527  37.504   7.418  1.00 11.67           C  
ATOM    373  OD1 ASP A  53      11.124  37.432   8.511  1.00 11.53           O  
ATOM    374  OD2 ASP A  53      11.125  37.372   6.337  1.00 13.51           O  
ATOM    375  N   ALA A  54       5.976  37.405   7.932  1.00  8.85           N  
ATOM    376  CA  ALA A  54       4.625  37.951   8.012  1.00  9.96           C  
ATOM    377  C   ALA A  54       3.964  37.716   9.377  1.00 10.45           C  
ATOM    378  O   ALA A  54       3.223  38.563   9.878  1.00 10.17           O  
ATOM    379  CB  ALA A  54       3.773  37.359   6.911  1.00 10.12           C  
ATOM    380  N   ALA A  55       4.237  36.563   9.979  1.00 10.23           N  
ATOM    381  CA  ALA A  55       3.676  36.227  11.281  1.00  9.89           C  
ATOM    382  C   ALA A  55       4.405  36.943  12.415  1.00 12.65           C  
ATOM    383  O   ALA A  55       3.771  37.504  13.313  1.00 15.14           O  
ATOM    384  CB  ALA A  55       3.703  34.718  11.501  1.00  8.11           C  
ATOM    385  N   LYS A  56       5.733  36.952  12.379  1.00 11.99           N  
ATOM    386  CA  LYS A  56       6.472  37.614  13.445  1.00 14.34           C  
ATOM    387  C   LYS A  56       6.253  39.120  13.424  1.00 13.81           C  
ATOM    388  O   LYS A  56       6.185  39.748  14.477  1.00 14.95           O  
ATOM    389  CB  LYS A  56       7.971  37.291  13.395  1.00 17.65           C  
ATOM    390  CG  LYS A  56       8.712  37.774  14.645  1.00 20.09           C  
ATOM    391  CD  LYS A  56      10.144  37.288  14.722  1.00 25.65           C  
ATOM    392  CE  LYS A  56      10.750  37.668  16.071  1.00 28.87           C  
ATOM    393  NZ  LYS A  56      12.096  37.065  16.308  1.00 31.53           N  
ATOM    394  N   ASN A  57       6.074  39.688  12.236  1.00 14.79           N  
ATOM    395  CA  ASN A  57       5.863  41.130  12.113  1.00 17.62           C  
ATOM    396  C   ASN A  57       4.550  41.635  12.724  1.00 20.78           C  
ATOM    397  O   ASN A  57       4.340  42.844  12.829  1.00 24.07           O  
ATOM    398  CB  ASN A  57       5.966  41.578  10.654  1.00 20.68           C  
ATOM    399  CG  ASN A  57       7.366  41.418  10.085  1.00 21.28           C  
ATOM    400  OD1 ASN A  57       8.335  41.203  10.819  1.00 22.45           O  
ATOM    401  ND2 ASN A  57       7.476  41.518   8.766  1.00 24.01           N  
ATOM    402  N   GLN A  58       3.662  40.723  13.113  1.00 19.81           N  
ATOM    403  CA  GLN A  58       2.398  41.124  13.727  1.00 19.92           C  
ATOM    404  C   GLN A  58       2.163  40.464  15.097  1.00 21.68           C  
ATOM    405  O   GLN A  58       1.076  40.575  15.677  1.00 21.42           O  
ATOM    406  CB  GLN A  58       1.214  40.880  12.768  1.00 16.39           C  
ATOM    407  CG  GLN A  58       0.996  39.443  12.295  1.00 14.68           C  
ATOM    408  CD  GLN A  58       0.318  38.572  13.335  1.00 14.12           C  
ATOM    409  OE1 GLN A  58      -0.910  38.570  13.465  1.00 13.58           O  
ATOM    410  NE2 GLN A  58       1.113  37.827  14.082  1.00 12.25           N  
ATOM    411  N   VAL A  59       3.203  39.837  15.641  1.00 22.16           N  
ATOM    412  CA  VAL A  59       3.105  39.162  16.934  1.00 22.34           C  
ATOM    413  C   VAL A  59       2.661  40.113  18.055  1.00 24.67           C  
ATOM    414  O   VAL A  59       1.839  39.750  18.909  1.00 24.13           O  
ATOM    415  CB  VAL A  59       4.456  38.471  17.311  1.00 22.70           C  
ATOM    416  CG1 VAL A  59       5.575  39.498  17.491  1.00 21.12           C  
ATOM    417  CG2 VAL A  59       4.297  37.632  18.563  1.00 19.62           C  
ATOM    418  N   ALA A  60       3.159  41.350  17.998  1.00 25.78           N  
ATOM    419  CA  ALA A  60       2.870  42.392  18.986  1.00 24.70           C  
ATOM    420  C   ALA A  60       1.397  42.770  19.111  1.00 23.09           C  
ATOM    421  O   ALA A  60       0.951  43.198  20.173  1.00 22.94           O  
ATOM    422  CB  ALA A  60       3.692  43.631  18.676  1.00 26.66           C  
ATOM    423  N   MET A  61       0.654  42.619  18.022  1.00 21.72           N  
ATOM    424  CA  MET A  61      -0.754  42.964  18.020  1.00 19.47           C  
ATOM    425  C   MET A  61      -1.679  41.754  18.064  1.00 19.02           C  
ATOM    426  O   MET A  61      -2.877  41.905  18.280  1.00 21.71           O  
ATOM    427  CB  MET A  61      -1.077  43.822  16.797  1.00 18.53           C  
ATOM    428  CG  MET A  61      -0.916  43.098  15.480  1.00 15.75           C  
ATOM    429  SD  MET A  61      -1.406  44.142  14.105  1.00 24.18           S  
ATOM    430  CE  MET A  61      -3.189  44.089  14.274  1.00 18.72           C  
ATOM    431  N   ASN A  62      -1.130  40.558  17.865  1.00 18.44           N  
ATOM    432  CA  ASN A  62      -1.921  39.326  17.882  1.00 16.89           C  
ATOM    433  C   ASN A  62      -1.188  38.237  18.682  1.00 18.68           C  
ATOM    434  O   ASN A  62      -1.029  37.112  18.209  1.00 18.59           O  
ATOM    435  CB  ASN A  62      -2.153  38.860  16.439  1.00 16.72           C  
ATOM    436  CG  ASN A  62      -3.080  37.662  16.337  1.00 16.31           C  
ATOM    437  OD1 ASN A  62      -3.844  37.356  17.258  1.00 17.37           O  
ATOM    438  ND2 ASN A  62      -3.031  36.981  15.200  1.00 12.67           N  
ATOM    439  N   PRO A  63      -0.839  38.526  19.949  1.00 19.21           N  
ATOM    440  CA  PRO A  63      -0.123  37.556  20.786  1.00 17.92           C  
ATOM    441  C   PRO A  63      -0.845  36.245  21.084  1.00 17.01           C  
ATOM    442  O   PRO A  63      -0.209  35.199  21.195  1.00 18.37           O  
ATOM    443  CB  PRO A  63       0.147  38.351  22.064  1.00 17.86           C  
ATOM    444  CG  PRO A  63      -1.061  39.214  22.170  1.00 20.26           C  
ATOM    445  CD  PRO A  63      -1.224  39.707  20.747  1.00 18.93           C  
ATOM    446  N   THR A  64      -2.163  36.277  21.179  1.00 16.96           N  
ATOM    447  CA  THR A  64      -2.886  35.061  21.503  1.00 17.10           C  
ATOM    448  C   THR A  64      -3.000  34.059  20.347  1.00 17.42           C  
ATOM    449  O   THR A  64      -3.088  32.847  20.570  1.00 17.28           O  
ATOM    450  CB  THR A  64      -4.277  35.382  22.119  1.00 20.55           C  
ATOM    451  OG1 THR A  64      -4.633  34.358  23.055  1.00 25.25           O  
ATOM    452  CG2 THR A  64      -5.348  35.456  21.051  1.00 21.24           C  
ATOM    453  N   ASN A  65      -2.950  34.549  19.112  1.00 14.30           N  
ATOM    454  CA  ASN A  65      -3.082  33.654  17.969  1.00 13.76           C  
ATOM    455  C   ASN A  65      -1.821  33.535  17.135  1.00 13.66           C  
ATOM    456  O   ASN A  65      -1.866  33.093  15.986  1.00 14.50           O  
ATOM    457  CB  ASN A  65      -4.277  34.058  17.102  1.00 14.41           C  
ATOM    458  CG  ASN A  65      -5.585  33.976  17.856  1.00 15.16           C  
ATOM    459  OD1 ASN A  65      -5.953  32.915  18.370  1.00 14.68           O  
ATOM    460  ND2 ASN A  65      -6.275  35.102  17.968  1.00 14.76           N  
ATOM    461  N   THR A  66      -0.704  33.970  17.702  1.00 13.29           N  
ATOM    462  CA  THR A  66       0.577  33.878  17.018  1.00 13.05           C  
ATOM    463  C   THR A  66       1.371  32.793  17.743  1.00 12.12           C  
ATOM    464  O   THR A  66       1.720  32.937  18.916  1.00 13.64           O  
ATOM    465  CB  THR A  66       1.314  35.229  17.020  1.00 13.05           C  
ATOM    466  OG1 THR A  66       0.496  36.205  16.356  1.00 13.73           O  
ATOM    467  CG2 THR A  66       2.644  35.116  16.280  1.00 11.25           C  
ATOM    468  N   VAL A  67       1.576  31.677  17.055  1.00 10.19           N  
ATOM    469  CA  VAL A  67       2.280  30.529  17.610  1.00  9.09           C  
ATOM    470  C   VAL A  67       3.765  30.521  17.267  1.00  7.65           C  
ATOM    471  O   VAL A  67       4.163  30.843  16.150  1.00  7.68           O  
ATOM    472  CB  VAL A  67       1.626  29.211  17.115  1.00  8.77           C  
ATOM    473  CG1 VAL A  67       2.288  27.990  17.760  1.00  8.34           C  
ATOM    474  CG2 VAL A  67       0.127  29.233  17.409  1.00  9.29           C  
ATOM    475  N   PHE A  68       4.569  30.149  18.255  1.00  7.56           N  
ATOM    476  CA  PHE A  68       6.018  30.049  18.124  1.00  8.83           C  
ATOM    477  C   PHE A  68       6.424  28.982  19.144  1.00  8.60           C  
ATOM    478  O   PHE A  68       5.574  28.486  19.886  1.00  8.49           O  
ATOM    479  CB  PHE A  68       6.702  31.394  18.426  1.00  8.99           C  
ATOM    480  CG  PHE A  68       6.409  31.943  19.800  1.00 11.03           C  
ATOM    481  CD1 PHE A  68       5.298  32.754  20.017  1.00  9.89           C  
ATOM    482  CD2 PHE A  68       7.231  31.631  20.881  1.00  9.56           C  
ATOM    483  CE1 PHE A  68       5.010  33.243  21.285  1.00 11.07           C  
ATOM    484  CE2 PHE A  68       6.951  32.116  22.157  1.00 10.40           C  
ATOM    485  CZ  PHE A  68       5.837  32.922  22.360  1.00  9.46           C  
ATOM    486  N   ASP A  69       7.700  28.607  19.168  1.00  8.52           N  
ATOM    487  CA  ASP A  69       8.177  27.595  20.111  1.00  7.00           C  
ATOM    488  C   ASP A  69       7.558  26.207  19.937  1.00  7.82           C  
ATOM    489  O   ASP A  69       7.561  25.405  20.876  1.00  7.30           O  
ATOM    490  CB  ASP A  69       7.951  28.057  21.555  1.00  8.18           C  
ATOM    491  CG  ASP A  69       9.111  28.855  22.110  1.00 11.35           C  
ATOM    492  OD1 ASP A  69      10.059  29.164  21.360  1.00 12.27           O  
ATOM    493  OD2 ASP A  69       9.080  29.169  23.317  1.00 10.88           O  
ATOM    494  N   ALA A  70       7.053  25.903  18.741  1.00  8.20           N  
ATOM    495  CA  ALA A  70       6.457  24.588  18.487  1.00  7.55           C  
ATOM    496  C   ALA A  70       7.496  23.479  18.701  1.00  7.47           C  
ATOM    497  O   ALA A  70       7.149  22.355  19.082  1.00  7.34           O  
ATOM    498  CB  ALA A  70       5.887  24.520  17.069  1.00  6.38           C  
ATOM    499  N   LYS A  71       8.770  23.810  18.494  1.00  6.87           N  
ATOM    500  CA  LYS A  71       9.859  22.844  18.663  1.00  7.43           C  
ATOM    501  C   LYS A  71       9.987  22.375  20.114  1.00  7.61           C  
ATOM    502  O   LYS A  71      10.520  21.298  20.377  1.00  6.39           O  
ATOM    503  CB  LYS A  71      11.184  23.444  18.180  1.00  7.26           C  
ATOM    504  CG  LYS A  71      12.335  22.450  18.103  1.00  5.62           C  
ATOM    505  CD  LYS A  71      13.499  23.076  17.366  1.00  5.48           C  
ATOM    506  CE  LYS A  71      14.661  22.123  17.233  1.00  6.27           C  
ATOM    507  NZ  LYS A  71      15.776  22.799  16.516  1.00  6.51           N  
ATOM    508  N   ARG A  72       9.483  23.182  21.046  1.00  7.20           N  
ATOM    509  CA  ARG A  72       9.528  22.844  22.468  1.00  8.44           C  
ATOM    510  C   ARG A  72       8.448  21.825  22.834  1.00  8.65           C  
ATOM    511  O   ARG A  72       8.532  21.173  23.879  1.00 10.13           O  
ATOM    512  CB  ARG A  72       9.356  24.098  23.335  1.00  6.56           C  
ATOM    513  CG  ARG A  72      10.504  25.093  23.263  1.00  4.88           C  
ATOM    514  CD  ARG A  72      10.319  26.209  24.282  1.00  7.06           C  
ATOM    515  NE  ARG A  72      11.380  27.212  24.203  1.00  8.52           N  
ATOM    516  CZ  ARG A  72      12.600  27.061  24.721  1.00  6.79           C  
ATOM    517  NH1 ARG A  72      12.927  25.951  25.373  1.00  7.71           N  
ATOM    518  NH2 ARG A  72      13.499  28.026  24.592  1.00  7.41           N  
ATOM    519  N   LEU A  73       7.436  21.701  21.976  1.00  8.50           N  
ATOM    520  CA  LEU A  73       6.327  20.771  22.195  1.00  8.45           C  
ATOM    521  C   LEU A  73       6.392  19.524  21.330  1.00  7.04           C  
ATOM    522  O   LEU A  73       5.846  18.478  21.682  1.00  7.75           O  
ATOM    523  CB  LEU A  73       5.001  21.460  21.871  1.00  7.02           C  
ATOM    524  CG  LEU A  73       4.519  22.581  22.774  1.00  7.62           C  
ATOM    525  CD1 LEU A  73       3.307  23.233  22.135  1.00  9.43           C  
ATOM    526  CD2 LEU A  73       4.190  22.019  24.155  1.00  8.92           C  
ATOM    527  N   ILE A  74       7.027  19.651  20.176  1.00  7.60           N  
ATOM    528  CA  ILE A  74       7.096  18.562  19.220  1.00  8.20           C  
ATOM    529  C   ILE A  74       7.596  17.215  19.766  1.00  7.25           C  
ATOM    530  O   ILE A  74       8.658  17.119  20.385  1.00  8.27           O  
ATOM    531  CB  ILE A  74       7.830  19.020  17.918  1.00  6.94           C  
ATOM    532  CG1 ILE A  74       7.392  18.160  16.728  1.00  6.49           C  
ATOM    533  CG2 ILE A  74       9.346  19.020  18.114  1.00  7.06           C  
ATOM    534  CD1 ILE A  74       7.738  18.772  15.369  1.00  6.45           C  
ATOM    535  N   GLY A  75       6.760  16.194  19.603  1.00  8.45           N  
ATOM    536  CA  GLY A  75       7.108  14.865  20.058  1.00  7.56           C  
ATOM    537  C   GLY A  75       6.954  14.620  21.546  1.00  8.16           C  
ATOM    538  O   GLY A  75       7.280  13.530  22.018  1.00  9.83           O  
ATOM    539  N   ARG A  76       6.466  15.611  22.289  1.00  9.78           N  
ATOM    540  CA  ARG A  76       6.285  15.463  23.733  1.00  9.58           C  
ATOM    541  C   ARG A  76       4.844  15.157  24.138  1.00 12.29           C  
ATOM    542  O   ARG A  76       3.920  15.262  23.329  1.00 11.91           O  
ATOM    543  CB  ARG A  76       6.766  16.713  24.471  1.00  8.88           C  
ATOM    544  CG  ARG A  76       8.257  16.968  24.381  1.00  9.82           C  
ATOM    545  CD  ARG A  76       8.638  18.113  25.311  1.00 14.88           C  
ATOM    546  NE  ARG A  76       9.902  18.749  24.946  1.00 19.15           N  
ATOM    547  CZ  ARG A  76      11.097  18.366  25.389  1.00 21.89           C  
ATOM    548  NH1 ARG A  76      11.208  17.324  26.210  1.00 21.53           N  
ATOM    549  NH2 ARG A  76      12.188  19.017  24.994  1.00 21.70           N  
ATOM    550  N   ARG A  77       4.668  14.734  25.388  1.00 12.26           N  
ATOM    551  CA  ARG A  77       3.342  14.424  25.923  1.00 11.33           C  
ATOM    552  C   ARG A  77       2.866  15.637  26.713  1.00 11.65           C  
ATOM    553  O   ARG A  77       3.679  16.387  27.267  1.00 11.77           O  
ATOM    554  CB  ARG A  77       3.403  13.192  26.830  1.00 13.78           C  
ATOM    555  N   PHE A  78       1.556  15.828  26.770  1.00 11.30           N  
ATOM    556  CA  PHE A  78       0.980  16.961  27.479  1.00 10.23           C  
ATOM    557  C   PHE A  78       1.418  16.999  28.944  1.00 12.26           C  
ATOM    558  O   PHE A  78       1.749  18.059  29.472  1.00 13.00           O  
ATOM    559  CB  PHE A  78      -0.553  16.915  27.390  1.00 11.95           C  
ATOM    560  CG  PHE A  78      -1.235  18.100  28.014  1.00 11.01           C  
ATOM    561  CD1 PHE A  78      -1.390  19.284  27.299  1.00 10.52           C  
ATOM    562  CD2 PHE A  78      -1.709  18.040  29.322  1.00 12.18           C  
ATOM    563  CE1 PHE A  78      -2.003  20.388  27.873  1.00  8.02           C  
ATOM    564  CE2 PHE A  78      -2.327  19.146  29.906  1.00 11.76           C  
ATOM    565  CZ  PHE A  78      -2.473  20.320  29.181  1.00 10.29           C  
ATOM    566  N   ASP A  79       1.432  15.842  29.595  1.00 12.98           N  
ATOM    567  CA  ASP A  79       1.803  15.762  31.004  1.00 15.00           C  
ATOM    568  C   ASP A  79       3.281  15.926  31.324  1.00 14.37           C  
ATOM    569  O   ASP A  79       3.653  15.866  32.490  1.00 16.29           O  
ATOM    570  CB  ASP A  79       1.284  14.462  31.631  1.00 18.74           C  
ATOM    571  CG  ASP A  79      -0.241  14.360  31.617  1.00 26.38           C  
ATOM    572  OD1 ASP A  79      -0.932  15.378  31.382  1.00 28.61           O  
ATOM    573  OD2 ASP A  79      -0.757  13.243  31.840  1.00 33.35           O  
ATOM    574  N   ASP A  80       4.122  16.115  30.311  1.00 12.60           N  
ATOM    575  CA  ASP A  80       5.553  16.294  30.547  1.00 11.16           C  
ATOM    576  C   ASP A  80       5.772  17.532  31.383  1.00 10.69           C  
ATOM    577  O   ASP A  80       5.185  18.581  31.118  1.00  9.52           O  
ATOM    578  CB  ASP A  80       6.322  16.488  29.239  1.00 14.85           C  
ATOM    579  CG  ASP A  80       6.494  15.208  28.449  1.00 20.16           C  
ATOM    580  OD1 ASP A  80       6.242  14.103  28.982  1.00 24.39           O  
ATOM    581  OD2 ASP A  80       6.905  15.313  27.277  1.00 23.49           O  
ATOM    582  N   ALA A  81       6.676  17.429  32.346  1.00 10.79           N  
ATOM    583  CA  ALA A  81       6.988  18.551  33.217  1.00 11.60           C  
ATOM    584  C   ALA A  81       7.386  19.799  32.430  1.00 11.82           C  
ATOM    585  O   ALA A  81       6.887  20.894  32.709  1.00 12.94           O  
ATOM    586  CB  ALA A  81       8.093  18.169  34.186  1.00 13.70           C  
ATOM    587  N   VAL A  82       8.257  19.641  31.433  1.00 12.14           N  
ATOM    588  CA  VAL A  82       8.708  20.792  30.646  1.00 11.99           C  
ATOM    589  C   VAL A  82       7.572  21.448  29.872  1.00 10.77           C  
ATOM    590  O   VAL A  82       7.540  22.671  29.746  1.00 12.46           O  
ATOM    591  CB  VAL A  82       9.879  20.457  29.680  1.00 13.24           C  
ATOM    592  CG1 VAL A  82      11.078  19.938  30.460  1.00 13.52           C  
ATOM    593  CG2 VAL A  82       9.444  19.457  28.634  1.00 16.44           C  
ATOM    594  N   VAL A  83       6.639  20.642  29.371  1.00 10.51           N  
ATOM    595  CA  VAL A  83       5.495  21.164  28.626  1.00  9.91           C  
ATOM    596  C   VAL A  83       4.669  22.003  29.591  1.00 10.06           C  
ATOM    597  O   VAL A  83       4.360  23.169  29.320  1.00 10.80           O  
ATOM    598  CB  VAL A  83       4.633  20.016  28.038  1.00 10.23           C  
ATOM    599  CG1 VAL A  83       3.332  20.560  27.458  1.00  9.89           C  
ATOM    600  CG2 VAL A  83       5.419  19.273  26.957  1.00 10.18           C  
ATOM    601  N   GLN A  84       4.393  21.430  30.758  1.00 11.15           N  
ATOM    602  CA  GLN A  84       3.614  22.118  31.776  1.00 10.95           C  
ATOM    603  C   GLN A  84       4.285  23.417  32.229  1.00 10.21           C  
ATOM    604  O   GLN A  84       3.609  24.420  32.451  1.00  9.96           O  
ATOM    605  CB  GLN A  84       3.338  21.173  32.945  1.00 12.18           C  
ATOM    606  CG  GLN A  84       2.386  20.023  32.581  1.00 12.02           C  
ATOM    607  CD  GLN A  84       1.030  20.530  32.105  1.00 14.56           C  
ATOM    608  OE1 GLN A  84       0.408  21.373  32.755  1.00 17.32           O  
ATOM    609  NE2 GLN A  84       0.579  20.038  30.965  1.00 12.62           N  
ATOM    610  N   SER A  85       5.616  23.415  32.295  1.00 11.48           N  
ATOM    611  CA  SER A  85       6.356  24.609  32.694  1.00 11.85           C  
ATOM    612  C   SER A  85       6.300  25.661  31.591  1.00 10.94           C  
ATOM    613  O   SER A  85       6.002  26.831  31.843  1.00 12.43           O  
ATOM    614  CB  SER A  85       7.825  24.279  32.989  1.00 14.63           C  
ATOM    615  OG  SER A  85       7.957  23.366  34.061  1.00 23.68           O  
ATOM    616  N   ASP A  86       6.582  25.237  30.363  1.00 10.35           N  
ATOM    617  CA  ASP A  86       6.580  26.148  29.221  1.00 10.13           C  
ATOM    618  C   ASP A  86       5.258  26.851  29.006  1.00 10.47           C  
ATOM    619  O   ASP A  86       5.230  28.039  28.692  1.00 11.47           O  
ATOM    620  CB  ASP A  86       6.962  25.415  27.941  1.00 11.05           C  
ATOM    621  CG  ASP A  86       8.446  25.179  27.827  1.00 12.43           C  
ATOM    622  OD1 ASP A  86       9.222  25.956  28.410  1.00 17.04           O  
ATOM    623  OD2 ASP A  86       8.841  24.215  27.153  1.00 12.55           O  
ATOM    624  N   MET A  87       4.168  26.115  29.181  1.00 11.78           N  
ATOM    625  CA  MET A  87       2.832  26.657  28.997  1.00 13.41           C  
ATOM    626  C   MET A  87       2.587  27.933  29.791  1.00 15.54           C  
ATOM    627  O   MET A  87       1.890  28.835  29.323  1.00 16.16           O  
ATOM    628  CB  MET A  87       1.783  25.608  29.358  1.00 15.42           C  
ATOM    629  CG  MET A  87       1.538  24.578  28.270  1.00 16.85           C  
ATOM    630  SD  MET A  87       0.602  23.175  28.898  1.00 18.10           S  
ATOM    631  CE  MET A  87      -1.011  23.955  29.188  1.00 18.80           C  
ATOM    632  N   LYS A  88       3.187  28.022  30.975  1.00 14.63           N  
ATOM    633  CA  LYS A  88       3.021  29.191  31.830  1.00 17.45           C  
ATOM    634  C   LYS A  88       3.653  30.465  31.267  1.00 19.15           C  
ATOM    635  O   LYS A  88       3.453  31.551  31.811  1.00 21.52           O  
ATOM    636  CB  LYS A  88       3.616  28.917  33.207  1.00 19.12           C  
ATOM    637  CG  LYS A  88       3.002  27.736  33.928  1.00 22.73           C  
ATOM    638  CD  LYS A  88       3.768  27.439  35.208  1.00 26.03           C  
ATOM    639  CE  LYS A  88       3.267  26.166  35.869  1.00 28.15           C  
ATOM    640  NZ  LYS A  88       4.160  25.741  36.983  1.00 31.10           N  
ATOM    641  N   HIS A  89       4.435  30.342  30.201  1.00 18.33           N  
ATOM    642  CA  HIS A  89       5.095  31.510  29.623  1.00 19.50           C  
ATOM    643  C   HIS A  89       4.611  31.866  28.219  1.00 17.57           C  
ATOM    644  O   HIS A  89       4.940  32.933  27.705  1.00 20.12           O  
ATOM    645  CB  HIS A  89       6.617  31.314  29.631  1.00 22.75           C  
ATOM    646  CG  HIS A  89       7.165  30.919  30.969  1.00 30.86           C  
ATOM    647  ND1 HIS A  89       7.060  31.725  32.084  1.00 34.06           N  
ATOM    648  CD2 HIS A  89       7.777  29.787  31.384  1.00 33.02           C  
ATOM    649  CE1 HIS A  89       7.582  31.108  33.127  1.00 34.67           C  
ATOM    650  NE2 HIS A  89       8.026  29.921  32.727  1.00 36.27           N  
ATOM    651  N   TRP A  90       3.805  30.999  27.617  1.00 14.52           N  
ATOM    652  CA  TRP A  90       3.288  31.250  26.273  1.00 13.40           C  
ATOM    653  C   TRP A  90       1.964  32.000  26.295  1.00 14.16           C  
ATOM    654  O   TRP A  90       1.102  31.719  27.127  1.00 13.78           O  
ATOM    655  CB  TRP A  90       3.093  29.935  25.525  1.00 11.45           C  
ATOM    656  CG  TRP A  90       4.365  29.240  25.185  1.00  9.51           C  
ATOM    657  CD1 TRP A  90       5.544  29.824  24.822  1.00  9.85           C  
ATOM    658  CD2 TRP A  90       4.571  27.829  25.147  1.00  8.79           C  
ATOM    659  NE1 TRP A  90       6.477  28.850  24.546  1.00  9.18           N  
ATOM    660  CE2 TRP A  90       5.917  27.624  24.724  1.00  7.97           C  
ATOM    661  CE3 TRP A  90       3.766  26.710  25.395  1.00  8.11           C  
ATOM    662  CZ2 TRP A  90       6.457  26.342  24.574  1.00  8.18           C  
ATOM    663  CZ3 TRP A  90       4.306  25.438  25.244  1.00  6.60           C  
ATOM    664  CH2 TRP A  90       5.640  25.266  24.826  1.00  9.38           C  
ATOM    665  N   PRO A  91       1.788  32.974  25.382  1.00 14.81           N  
ATOM    666  CA  PRO A  91       0.551  33.763  25.297  1.00 15.48           C  
ATOM    667  C   PRO A  91      -0.562  33.014  24.554  1.00 15.05           C  
ATOM    668  O   PRO A  91      -1.716  33.435  24.559  1.00 16.33           O  
ATOM    669  CB  PRO A  91       0.999  35.008  24.544  1.00 13.73           C  
ATOM    670  CG  PRO A  91       2.048  34.479  23.629  1.00 15.70           C  
ATOM    671  CD  PRO A  91       2.835  33.545  24.514  1.00 14.93           C  
ATOM    672  N   PHE A  92      -0.199  31.919  23.890  1.00 14.28           N  
ATOM    673  CA  PHE A  92      -1.171  31.106  23.167  1.00 13.00           C  
ATOM    674  C   PHE A  92      -1.564  29.914  24.039  1.00 13.33           C  
ATOM    675  O   PHE A  92      -0.815  29.517  24.942  1.00 13.22           O  
ATOM    676  CB  PHE A  92      -0.608  30.650  21.814  1.00 11.87           C  
ATOM    677  CG  PHE A  92       0.741  29.984  21.902  1.00 12.48           C  
ATOM    678  CD1 PHE A  92       0.847  28.629  22.201  1.00 11.02           C  
ATOM    679  CD2 PHE A  92       1.905  30.709  21.654  1.00 10.76           C  
ATOM    680  CE1 PHE A  92       2.090  28.006  22.249  1.00 12.01           C  
ATOM    681  CE2 PHE A  92       3.151  30.097  21.699  1.00  9.23           C  
ATOM    682  CZ  PHE A  92       3.246  28.742  21.996  1.00 10.18           C  
ATOM    683  N   MET A  93      -2.730  29.341  23.769  1.00 12.98           N  
ATOM    684  CA  MET A  93      -3.226  28.216  24.547  1.00 14.02           C  
ATOM    685  C   MET A  93      -2.724  26.855  24.072  1.00 13.40           C  
ATOM    686  O   MET A  93      -2.592  26.613  22.872  1.00 11.69           O  
ATOM    687  CB  MET A  93      -4.758  28.213  24.539  1.00 19.13           C  
ATOM    688  CG  MET A  93      -5.381  27.326  25.603  1.00 26.90           C  
ATOM    689  SD  MET A  93      -7.174  27.185  25.453  1.00 39.35           S  
ATOM    690  CE  MET A  93      -7.635  28.882  24.967  1.00 32.94           C  
ATOM    691  N   VAL A  94      -2.431  25.976  25.026  1.00 13.04           N  
ATOM    692  CA  VAL A  94      -1.995  24.622  24.724  1.00 11.69           C  
ATOM    693  C   VAL A  94      -2.982  23.717  25.447  1.00 12.87           C  
ATOM    694  O   VAL A  94      -3.199  23.861  26.656  1.00 11.92           O  
ATOM    695  CB  VAL A  94      -0.561  24.337  25.212  1.00 11.62           C  
ATOM    696  CG1 VAL A  94      -0.194  22.891  24.933  1.00  8.95           C  
ATOM    697  CG2 VAL A  94       0.416  25.261  24.514  1.00  9.93           C  
ATOM    698  N   VAL A  95      -3.625  22.837  24.687  1.00 12.23           N  
ATOM    699  CA  VAL A  95      -4.627  21.924  25.224  1.00 11.99           C  
ATOM    700  C   VAL A  95      -4.201  20.463  25.160  1.00 11.81           C  
ATOM    701  O   VAL A  95      -3.225  20.113  24.488  1.00 11.51           O  
ATOM    702  CB  VAL A  95      -5.999  22.106  24.507  1.00 10.79           C  
ATOM    703  CG1 VAL A  95      -6.502  23.534  24.689  1.00 11.15           C  
ATOM    704  CG2 VAL A  95      -5.888  21.759  23.023  1.00 10.07           C  
ATOM    705  N   ASN A  96      -4.939  19.615  25.869  1.00 11.56           N  
ATOM    706  CA  ASN A  96      -4.641  18.195  25.916  1.00 12.92           C  
ATOM    707  C   ASN A  96      -5.578  17.353  25.061  1.00 14.91           C  
ATOM    708  O   ASN A  96      -6.782  17.280  25.320  1.00 17.38           O  
ATOM    709  CB  ASN A  96      -4.701  17.699  27.361  1.00 12.62           C  
ATOM    710  CG  ASN A  96      -4.275  16.254  27.503  1.00 12.44           C  
ATOM    711  OD1 ASN A  96      -3.846  15.618  26.541  1.00 13.61           O  
ATOM    712  ND2 ASN A  96      -4.367  15.732  28.717  1.00 17.50           N  
ATOM    713  N   ASP A  97      -5.020  16.705  24.051  1.00 13.65           N  
ATOM    714  CA  ASP A  97      -5.809  15.838  23.204  1.00 14.71           C  
ATOM    715  C   ASP A  97      -5.313  14.409  23.386  1.00 14.64           C  
ATOM    716  O   ASP A  97      -4.351  13.987  22.744  1.00 13.82           O  
ATOM    717  CB  ASP A  97      -5.712  16.255  21.738  1.00 17.76           C  
ATOM    718  CG  ASP A  97      -6.813  15.641  20.891  1.00 21.16           C  
ATOM    719  OD1 ASP A  97      -6.923  14.396  20.857  1.00 21.01           O  
ATOM    720  OD2 ASP A  97      -7.589  16.405  20.278  1.00 24.23           O  
ATOM    721  N   ALA A  98      -5.962  13.677  24.286  1.00 15.61           N  
ATOM    722  CA  ALA A  98      -5.615  12.284  24.567  1.00 17.53           C  
ATOM    723  C   ALA A  98      -4.155  12.098  24.990  1.00 17.39           C  
ATOM    724  O   ALA A  98      -3.506  11.115  24.622  1.00 16.81           O  
ATOM    725  CB  ALA A  98      -5.939  11.405  23.350  1.00 19.96           C  
ATOM    726  N   GLY A  99      -3.648  13.052  25.763  1.00 15.74           N  
ATOM    727  CA  GLY A  99      -2.281  12.972  26.228  1.00 14.57           C  
ATOM    728  C   GLY A  99      -1.303  13.690  25.327  1.00 14.72           C  
ATOM    729  O   GLY A  99      -0.146  13.845  25.690  1.00 16.46           O  
ATOM    730  N   ARG A 100      -1.762  14.129  24.159  1.00 15.43           N  
ATOM    731  CA  ARG A 100      -0.907  14.830  23.204  1.00 14.16           C  
ATOM    732  C   ARG A 100      -1.230  16.317  23.227  1.00 14.16           C  
ATOM    733  O   ARG A 100      -2.395  16.699  23.245  1.00 14.22           O  
ATOM    734  CB  ARG A 100      -1.110  14.263  21.799  1.00 12.86           C  
ATOM    735  N   PRO A 101      -0.192  17.178  23.284  1.00 14.13           N  
ATOM    736  CA  PRO A 101      -0.423  18.626  23.308  1.00 12.36           C  
ATOM    737  C   PRO A 101      -0.815  19.176  21.938  1.00 11.50           C  
ATOM    738  O   PRO A 101      -0.370  18.673  20.905  1.00 12.50           O  
ATOM    739  CB  PRO A 101       0.941  19.173  23.748  1.00 10.80           C  
ATOM    740  CG  PRO A 101       1.894  18.214  23.126  1.00 11.22           C  
ATOM    741  CD  PRO A 101       1.244  16.872  23.395  1.00 11.98           C  
ATOM    742  N   LYS A 102      -1.665  20.193  21.937  1.00  9.81           N  
ATOM    743  CA  LYS A 102      -2.088  20.842  20.702  1.00  9.07           C  
ATOM    744  C   LYS A 102      -2.213  22.325  21.014  1.00  9.84           C  
ATOM    745  O   LYS A 102      -2.596  22.696  22.125  1.00 12.07           O  
ATOM    746  CB  LYS A 102      -3.451  20.322  20.225  1.00  9.35           C  
ATOM    747  CG  LYS A 102      -3.501  18.844  19.877  1.00  9.35           C  
ATOM    748  CD  LYS A 102      -4.768  18.500  19.110  1.00  9.16           C  
ATOM    749  CE  LYS A 102      -4.707  19.028  17.681  1.00  9.98           C  
ATOM    750  NZ  LYS A 102      -5.956  18.762  16.910  1.00  7.96           N  
ATOM    751  N   VAL A 103      -1.816  23.175  20.078  1.00  9.51           N  
ATOM    752  CA  VAL A 103      -1.959  24.606  20.296  1.00  9.83           C  
ATOM    753  C   VAL A 103      -3.360  24.965  19.797  1.00 10.59           C  
ATOM    754  O   VAL A 103      -3.803  24.471  18.756  1.00 10.45           O  
ATOM    755  CB  VAL A 103      -0.870  25.431  19.564  1.00 12.15           C  
ATOM    756  CG1 VAL A 103       0.509  24.955  19.997  1.00 11.60           C  
ATOM    757  CG2 VAL A 103      -1.023  25.331  18.052  1.00 15.96           C  
ATOM    758  N   GLN A 104      -4.086  25.752  20.583  1.00 12.02           N  
ATOM    759  CA  GLN A 104      -5.436  26.149  20.218  1.00 12.45           C  
ATOM    760  C   GLN A 104      -5.462  27.630  19.888  1.00 11.60           C  
ATOM    761  O   GLN A 104      -4.963  28.449  20.656  1.00 12.72           O  
ATOM    762  CB  GLN A 104      -6.402  25.847  21.357  1.00 14.74           C  
ATOM    763  CG  GLN A 104      -7.850  26.078  20.996  1.00 17.19           C  
ATOM    764  CD  GLN A 104      -8.772  25.875  22.181  1.00 20.86           C  
ATOM    765  OE1 GLN A 104      -9.169  26.833  22.842  1.00 24.69           O  
ATOM    766  NE2 GLN A 104      -9.131  24.629  22.446  1.00 20.90           N  
ATOM    767  N   VAL A 105      -6.026  27.966  18.731  1.00 13.47           N  
ATOM    768  CA  VAL A 105      -6.111  29.349  18.279  1.00 13.15           C  
ATOM    769  C   VAL A 105      -7.457  29.634  17.621  1.00 14.78           C  
ATOM    770  O   VAL A 105      -8.275  28.737  17.422  1.00 13.00           O  
ATOM    771  CB  VAL A 105      -5.032  29.663  17.208  1.00 13.10           C  
ATOM    772  CG1 VAL A 105      -3.638  29.539  17.789  1.00 13.22           C  
ATOM    773  CG2 VAL A 105      -5.208  28.744  16.006  1.00 13.50           C  
ATOM    774  N   GLU A 106      -7.669  30.904  17.296  1.00 15.00           N  
ATOM    775  CA  GLU A 106      -8.864  31.345  16.603  1.00 15.65           C  
ATOM    776  C   GLU A 106      -8.405  31.632  15.180  1.00 14.55           C  
ATOM    777  O   GLU A 106      -7.360  32.251  14.967  1.00 12.72           O  
ATOM    778  CB  GLU A 106      -9.418  32.635  17.213  1.00 17.18           C  
ATOM    779  CG  GLU A 106      -9.941  32.498  18.628  1.00 22.25           C  
ATOM    780  CD  GLU A 106     -10.982  31.410  18.758  1.00 25.07           C  
ATOM    781  OE1 GLU A 106     -12.010  31.476  18.053  1.00 29.98           O  
ATOM    782  OE2 GLU A 106     -10.766  30.480  19.558  1.00 27.31           O  
ATOM    783  N   TYR A 107      -9.164  31.146  14.213  1.00 14.56           N  
ATOM    784  CA  TYR A 107      -8.860  31.375  12.812  1.00 14.62           C  
ATOM    785  C   TYR A 107     -10.204  31.549  12.126  1.00 14.01           C  
ATOM    786  O   TYR A 107     -11.062  30.670  12.199  1.00 13.92           O  
ATOM    787  CB  TYR A 107      -8.115  30.184  12.207  1.00 14.86           C  
ATOM    788  CG  TYR A 107      -7.853  30.349  10.727  1.00 17.88           C  
ATOM    789  CD1 TYR A 107      -7.172  31.468  10.244  1.00 17.27           C  
ATOM    790  CD2 TYR A 107      -8.293  29.396   9.805  1.00 20.72           C  
ATOM    791  CE1 TYR A 107      -6.942  31.641   8.891  1.00 16.90           C  
ATOM    792  CE2 TYR A 107      -8.065  29.560   8.437  1.00 22.80           C  
ATOM    793  CZ  TYR A 107      -7.385  30.686   7.991  1.00 23.96           C  
ATOM    794  OH  TYR A 107      -7.138  30.857   6.649  1.00 26.01           O  
ATOM    795  N   LYS A 108     -10.393  32.696  11.488  1.00 14.63           N  
ATOM    796  CA  LYS A 108     -11.642  32.995  10.797  1.00 17.59           C  
ATOM    797  C   LYS A 108     -12.854  32.835  11.714  1.00 17.75           C  
ATOM    798  O   LYS A 108     -13.859  32.222  11.344  1.00 18.64           O  
ATOM    799  CB  LYS A 108     -11.791  32.125   9.550  1.00 17.46           C  
ATOM    800  CG  LYS A 108     -10.876  32.532   8.418  1.00 21.95           C  
ATOM    801  CD  LYS A 108     -11.259  31.813   7.141  1.00 26.51           C  
ATOM    802  CE  LYS A 108     -10.649  32.494   5.929  1.00 30.20           C  
ATOM    803  NZ  LYS A 108      -9.166  32.491   5.992  1.00 35.60           N  
ATOM    804  N   GLY A 109     -12.722  33.350  12.930  1.00 19.28           N  
ATOM    805  CA  GLY A 109     -13.804  33.289  13.896  1.00 20.33           C  
ATOM    806  C   GLY A 109     -14.107  31.937  14.515  1.00 20.27           C  
ATOM    807  O   GLY A 109     -15.046  31.825  15.303  1.00 20.82           O  
ATOM    808  N   GLU A 110     -13.334  30.911  14.177  1.00 19.54           N  
ATOM    809  CA  GLU A 110     -13.570  29.587  14.742  1.00 19.78           C  
ATOM    810  C   GLU A 110     -12.352  29.089  15.511  1.00 18.09           C  
ATOM    811  O   GLU A 110     -11.217  29.393  15.153  1.00 17.72           O  
ATOM    812  CB  GLU A 110     -13.952  28.580  13.648  1.00 23.08           C  
ATOM    813  CG  GLU A 110     -15.224  28.926  12.853  1.00 28.91           C  
ATOM    814  CD  GLU A 110     -16.473  29.107  13.724  1.00 33.26           C  
ATOM    815  OE1 GLU A 110     -16.658  28.347  14.702  1.00 34.50           O  
ATOM    816  OE2 GLU A 110     -17.281  30.014  13.419  1.00 34.07           O  
ATOM    817  N   THR A 111     -12.605  28.379  16.606  1.00 17.42           N  
ATOM    818  CA  THR A 111     -11.544  27.818  17.435  1.00 17.73           C  
ATOM    819  C   THR A 111     -10.990  26.570  16.752  1.00 17.09           C  
ATOM    820  O   THR A 111     -11.749  25.703  16.324  1.00 17.48           O  
ATOM    821  CB  THR A 111     -12.069  27.420  18.833  1.00 18.38           C  
ATOM    822  OG1 THR A 111     -12.751  28.530  19.427  1.00 20.15           O  
ATOM    823  CG2 THR A 111     -10.925  27.008  19.738  1.00 19.18           C  
ATOM    824  N   LYS A 112      -9.669  26.477  16.664  1.00 17.05           N  
ATOM    825  CA  LYS A 112      -9.008  25.340  16.036  1.00 16.84           C  
ATOM    826  C   LYS A 112      -7.766  24.950  16.822  1.00 15.17           C  
ATOM    827  O   LYS A 112      -7.211  25.762  17.560  1.00 14.93           O  
ATOM    828  CB  LYS A 112      -8.615  25.688  14.599  1.00 18.33           C  
ATOM    829  CG  LYS A 112      -9.809  25.928  13.697  1.00 24.70           C  
ATOM    830  CD  LYS A 112      -9.410  26.570  12.392  1.00 27.86           C  
ATOM    831  CE  LYS A 112     -10.632  27.027  11.602  1.00 30.52           C  
ATOM    832  NZ  LYS A 112     -11.495  25.896  11.159  1.00 31.31           N  
ATOM    833  N   SER A 113      -7.347  23.699  16.676  1.00 15.10           N  
ATOM    834  CA  SER A 113      -6.156  23.207  17.355  1.00 13.36           C  
ATOM    835  C   SER A 113      -5.260  22.476  16.360  1.00 13.24           C  
ATOM    836  O   SER A 113      -5.740  21.871  15.392  1.00 11.72           O  
ATOM    837  CB  SER A 113      -6.516  22.303  18.543  1.00 13.78           C  
ATOM    838  OG  SER A 113      -7.307  21.199  18.153  1.00 14.57           O  
ATOM    839  N   PHE A 114      -3.955  22.573  16.581  1.00 11.24           N  
ATOM    840  CA  PHE A 114      -2.973  21.943  15.710  1.00 10.79           C  
ATOM    841  C   PHE A 114      -1.920  21.207  16.524  1.00 10.03           C  
ATOM    842  O   PHE A 114      -1.518  21.669  17.597  1.00  9.88           O  
ATOM    843  CB  PHE A 114      -2.270  23.009  14.854  1.00 11.25           C  
ATOM    844  CG  PHE A 114      -3.202  23.809  13.982  1.00 10.14           C  
ATOM    845  CD1 PHE A 114      -3.541  23.359  12.711  1.00 11.56           C  
ATOM    846  CD2 PHE A 114      -3.745  25.008  14.436  1.00 10.20           C  
ATOM    847  CE1 PHE A 114      -4.411  24.092  11.903  1.00 12.61           C  
ATOM    848  CE2 PHE A 114      -4.614  25.746  13.636  1.00 12.77           C  
ATOM    849  CZ  PHE A 114      -4.949  25.285  12.366  1.00 10.06           C  
ATOM    850  N   TYR A 115      -1.500  20.047  16.036  1.00  7.97           N  
ATOM    851  CA  TYR A 115      -0.443  19.300  16.705  1.00  8.57           C  
ATOM    852  C   TYR A 115       0.840  20.078  16.420  1.00  8.34           C  
ATOM    853  O   TYR A 115       0.915  20.803  15.421  1.00  8.00           O  
ATOM    854  CB  TYR A 115      -0.328  17.898  16.120  1.00  9.53           C  
ATOM    855  CG  TYR A 115      -1.471  17.008  16.513  1.00 11.48           C  
ATOM    856  CD1 TYR A 115      -1.558  16.493  17.807  1.00 11.61           C  
ATOM    857  CD2 TYR A 115      -2.492  16.712  15.608  1.00 13.13           C  
ATOM    858  CE1 TYR A 115      -2.624  15.695  18.188  1.00 15.51           C  
ATOM    859  CE2 TYR A 115      -3.571  15.913  15.980  1.00 13.55           C  
ATOM    860  CZ  TYR A 115      -3.632  15.416  17.274  1.00 14.75           C  
ATOM    861  OH  TYR A 115      -4.683  14.618  17.656  1.00 17.54           O  
ATOM    862  N   PRO A 116       1.852  19.976  17.291  1.00  9.16           N  
ATOM    863  CA  PRO A 116       3.111  20.699  17.071  1.00  8.70           C  
ATOM    864  C   PRO A 116       3.701  20.445  15.675  1.00  6.99           C  
ATOM    865  O   PRO A 116       4.184  21.372  15.029  1.00  8.67           O  
ATOM    866  CB  PRO A 116       4.013  20.164  18.182  1.00  9.59           C  
ATOM    867  CG  PRO A 116       3.034  19.945  19.311  1.00  9.89           C  
ATOM    868  CD  PRO A 116       1.855  19.295  18.608  1.00  8.65           C  
ATOM    869  N   GLU A 117       3.611  19.201  15.206  1.00  8.16           N  
ATOM    870  CA  GLU A 117       4.122  18.836  13.888  1.00  8.76           C  
ATOM    871  C   GLU A 117       3.342  19.523  12.768  1.00  7.67           C  
ATOM    872  O   GLU A 117       3.881  19.752  11.687  1.00  5.93           O  
ATOM    873  CB  GLU A 117       4.186  17.309  13.680  1.00  9.77           C  
ATOM    874  CG  GLU A 117       2.889  16.529  13.888  1.00 10.55           C  
ATOM    875  CD  GLU A 117       2.739  15.976  15.302  1.00 13.43           C  
ATOM    876  OE1 GLU A 117       2.872  16.746  16.272  1.00 12.85           O  
ATOM    877  OE2 GLU A 117       2.469  14.768  15.446  1.00 14.43           O  
ATOM    878  N   GLU A 118       2.087  19.883  13.034  1.00  8.72           N  
ATOM    879  CA  GLU A 118       1.295  20.587  12.028  1.00 10.72           C  
ATOM    880  C   GLU A 118       1.786  22.032  11.945  1.00  8.97           C  
ATOM    881  O   GLU A 118       1.969  22.582  10.857  1.00  9.20           O  
ATOM    882  CB  GLU A 118      -0.190  20.517  12.357  1.00 12.17           C  
ATOM    883  CG  GLU A 118      -0.818  19.260  11.804  1.00 17.33           C  
ATOM    884  CD  GLU A 118      -2.291  19.145  12.119  1.00 22.20           C  
ATOM    885  OE1 GLU A 118      -2.659  18.912  13.294  1.00 20.36           O  
ATOM    886  OE2 GLU A 118      -3.086  19.257  11.162  1.00 28.98           O  
ATOM    887  N   VAL A 119       2.035  22.639  13.100  1.00  8.24           N  
ATOM    888  CA  VAL A 119       2.554  23.998  13.117  1.00  8.77           C  
ATOM    889  C   VAL A 119       3.923  24.003  12.422  1.00  8.69           C  
ATOM    890  O   VAL A 119       4.196  24.851  11.566  1.00  8.15           O  
ATOM    891  CB  VAL A 119       2.695  24.530  14.551  1.00  9.24           C  
ATOM    892  CG1 VAL A 119       3.422  25.869  14.543  1.00  8.02           C  
ATOM    893  CG2 VAL A 119       1.313  24.678  15.183  1.00  6.82           C  
ATOM    894  N   SER A 120       4.769  23.036  12.767  1.00  6.68           N  
ATOM    895  CA  SER A 120       6.087  22.950  12.157  1.00  6.75           C  
ATOM    896  C   SER A 120       6.023  22.632  10.659  1.00  6.59           C  
ATOM    897  O   SER A 120       6.875  23.086   9.896  1.00  6.79           O  
ATOM    898  CB  SER A 120       6.964  21.953  12.911  1.00  6.82           C  
ATOM    899  OG  SER A 120       7.201  22.427  14.228  1.00  6.59           O  
ATOM    900  N   SER A 121       4.999  21.896  10.223  1.00  6.87           N  
ATOM    901  CA  SER A 121       4.860  21.579   8.799  1.00  6.00           C  
ATOM    902  C   SER A 121       4.603  22.879   8.035  1.00  6.94           C  
ATOM    903  O   SER A 121       5.013  23.027   6.890  1.00  7.38           O  
ATOM    904  CB  SER A 121       3.712  20.593   8.558  1.00  5.89           C  
ATOM    905  OG  SER A 121       2.444  21.223   8.663  1.00  7.72           O  
ATOM    906  N   MET A 122       3.907  23.814   8.675  1.00  6.26           N  
ATOM    907  CA  MET A 122       3.614  25.106   8.068  1.00  7.92           C  
ATOM    908  C   MET A 122       4.919  25.864   7.839  1.00  8.62           C  
ATOM    909  O   MET A 122       5.118  26.488   6.790  1.00  8.35           O  
ATOM    910  CB  MET A 122       2.679  25.914   8.974  1.00  6.55           C  
ATOM    911  CG  MET A 122       1.253  25.357   9.028  1.00  8.78           C  
ATOM    912  SD  MET A 122       0.232  26.145  10.287  1.00 12.53           S  
ATOM    913  CE  MET A 122      -0.861  24.800  10.737  1.00 13.90           C  
ATOM    914  N   VAL A 123       5.813  25.804   8.822  1.00  8.51           N  
ATOM    915  CA  VAL A 123       7.102  26.473   8.709  1.00  8.53           C  
ATOM    916  C   VAL A 123       7.926  25.785   7.624  1.00  9.10           C  
ATOM    917  O   VAL A 123       8.544  26.456   6.791  1.00 10.39           O  
ATOM    918  CB  VAL A 123       7.867  26.478  10.057  1.00  9.05           C  
ATOM    919  CG1 VAL A 123       9.263  27.080   9.879  1.00  7.64           C  
ATOM    920  CG2 VAL A 123       7.083  27.280  11.095  1.00  5.97           C  
ATOM    921  N   LEU A 124       7.897  24.452   7.600  1.00  7.19           N  
ATOM    922  CA  LEU A 124       8.641  23.700   6.589  1.00  7.38           C  
ATOM    923  C   LEU A 124       8.102  23.960   5.182  1.00  7.61           C  
ATOM    924  O   LEU A 124       8.872  23.996   4.222  1.00  8.70           O  
ATOM    925  CB  LEU A 124       8.656  22.202   6.906  1.00  5.33           C  
ATOM    926  CG  LEU A 124       9.473  21.798   8.139  1.00  6.92           C  
ATOM    927  CD1 LEU A 124       9.347  20.314   8.393  1.00  6.89           C  
ATOM    928  CD2 LEU A 124      10.930  22.177   7.950  1.00  8.73           C  
ATOM    929  N   THR A 125       6.787  24.128   5.058  1.00  6.37           N  
ATOM    930  CA  THR A 125       6.182  24.432   3.764  1.00  6.84           C  
ATOM    931  C   THR A 125       6.765  25.757   3.266  1.00  9.00           C  
ATOM    932  O   THR A 125       7.126  25.885   2.088  1.00  8.30           O  
ATOM    933  CB  THR A 125       4.644  24.551   3.865  1.00  8.93           C  
ATOM    934  OG1 THR A 125       4.084  23.263   4.157  1.00 10.06           O  
ATOM    935  CG2 THR A 125       4.055  25.076   2.554  1.00  8.23           C  
ATOM    936  N   LYS A 126       6.865  26.734   4.167  1.00  6.94           N  
ATOM    937  CA  LYS A 126       7.432  28.036   3.835  1.00  8.38           C  
ATOM    938  C   LYS A 126       8.885  27.864   3.368  1.00  8.32           C  
ATOM    939  O   LYS A 126       9.285  28.442   2.355  1.00  6.19           O  
ATOM    940  CB  LYS A 126       7.344  28.976   5.050  1.00  7.34           C  
ATOM    941  CG  LYS A 126       8.174  30.264   4.961  1.00  9.62           C  
ATOM    942  CD  LYS A 126       7.748  31.188   3.828  1.00 11.71           C  
ATOM    943  CE  LYS A 126       6.456  31.928   4.144  1.00 13.73           C  
ATOM    944  NZ  LYS A 126       6.130  32.927   3.084  1.00 13.07           N  
ATOM    945  N   MET A 127       9.660  27.045   4.077  1.00  7.60           N  
ATOM    946  CA  MET A 127      11.055  26.821   3.693  1.00  7.51           C  
ATOM    947  C   MET A 127      11.142  26.134   2.327  1.00  8.24           C  
ATOM    948  O   MET A 127      12.020  26.442   1.518  1.00  8.94           O  
ATOM    949  CB  MET A 127      11.797  25.997   4.753  1.00  6.86           C  
ATOM    950  CG  MET A 127      11.800  26.618   6.156  1.00  5.96           C  
ATOM    951  SD  MET A 127      12.024  28.428   6.212  1.00 10.53           S  
ATOM    952  CE  MET A 127      13.748  28.622   5.639  1.00  7.99           C  
ATOM    953  N   LYS A 128      10.214  25.216   2.071  1.00  8.90           N  
ATOM    954  CA  LYS A 128      10.152  24.482   0.806  1.00  9.82           C  
ATOM    955  C   LYS A 128       9.868  25.466  -0.334  1.00 10.28           C  
ATOM    956  O   LYS A 128      10.527  25.426  -1.380  1.00 11.48           O  
ATOM    957  CB  LYS A 128       9.044  23.430   0.898  1.00  8.45           C  
ATOM    958  CG  LYS A 128       8.853  22.509  -0.294  1.00  9.85           C  
ATOM    959  CD  LYS A 128       7.571  21.700  -0.065  1.00 12.78           C  
ATOM    960  CE  LYS A 128       7.348  20.587  -1.085  1.00 16.79           C  
ATOM    961  NZ  LYS A 128       7.086  21.102  -2.462  1.00 19.54           N  
ATOM    962  N   GLU A 129       8.921  26.376  -0.111  1.00 10.02           N  
ATOM    963  CA  GLU A 129       8.551  27.381  -1.107  1.00  8.87           C  
ATOM    964  C   GLU A 129       9.673  28.368  -1.370  1.00  9.91           C  
ATOM    965  O   GLU A 129       9.864  28.818  -2.503  1.00  9.48           O  
ATOM    966  CB  GLU A 129       7.281  28.110  -0.674  1.00  8.19           C  
ATOM    967  CG  GLU A 129       6.057  27.213  -0.748  1.00 11.24           C  
ATOM    968  CD  GLU A 129       4.824  27.807  -0.096  1.00 14.08           C  
ATOM    969  OE1 GLU A 129       4.921  28.869   0.556  1.00 16.71           O  
ATOM    970  OE2 GLU A 129       3.744  27.194  -0.233  1.00 17.68           O  
ATOM    971  N   ILE A 130      10.415  28.699  -0.320  1.00  9.95           N  
ATOM    972  CA  ILE A 130      11.549  29.612  -0.433  1.00  9.29           C  
ATOM    973  C   ILE A 130      12.581  28.977  -1.366  1.00  8.77           C  
ATOM    974  O   ILE A 130      13.064  29.627  -2.293  1.00 11.79           O  
ATOM    975  CB  ILE A 130      12.166  29.907   0.962  1.00  9.74           C  
ATOM    976  CG1 ILE A 130      11.221  30.813   1.760  1.00  9.98           C  
ATOM    977  CG2 ILE A 130      13.541  30.560   0.826  1.00  9.68           C  
ATOM    978  CD1 ILE A 130      11.616  30.985   3.214  1.00  8.35           C  
ATOM    979  N   ALA A 131      12.877  27.694  -1.155  1.00  8.25           N  
ATOM    980  CA  ALA A 131      13.830  26.981  -2.001  1.00  7.82           C  
ATOM    981  C   ALA A 131      13.306  26.881  -3.439  1.00 10.53           C  
ATOM    982  O   ALA A 131      14.058  27.093  -4.394  1.00  9.13           O  
ATOM    983  CB  ALA A 131      14.106  25.597  -1.443  1.00  6.56           C  
ATOM    984  N   GLU A 132      12.015  26.587  -3.590  1.00  8.62           N  
ATOM    985  CA  GLU A 132      11.408  26.470  -4.913  1.00 10.27           C  
ATOM    986  C   GLU A 132      11.431  27.769  -5.705  1.00 10.40           C  
ATOM    987  O   GLU A 132      11.663  27.756  -6.913  1.00 11.58           O  
ATOM    988  CB  GLU A 132       9.986  25.938  -4.803  1.00 10.10           C  
ATOM    989  CG  GLU A 132       9.950  24.489  -4.377  1.00 10.28           C  
ATOM    990  CD  GLU A 132       8.553  23.921  -4.275  1.00 14.05           C  
ATOM    991  OE1 GLU A 132       7.592  24.694  -4.116  1.00 14.96           O  
ATOM    992  OE2 GLU A 132       8.414  22.685  -4.340  1.00 13.08           O  
ATOM    993  N   ALA A 133      11.198  28.887  -5.027  1.00 10.89           N  
ATOM    994  CA  ALA A 133      11.220  30.193  -5.679  1.00 12.47           C  
ATOM    995  C   ALA A 133      12.630  30.462  -6.203  1.00 13.43           C  
ATOM    996  O   ALA A 133      12.801  31.006  -7.289  1.00 13.35           O  
ATOM    997  CB  ALA A 133      10.803  31.285  -4.705  1.00 11.40           C  
ATOM    998  N   TYR A 134      13.633  30.056  -5.429  1.00 11.75           N  
ATOM    999  CA  TYR A 134      15.031  30.238  -5.802  1.00 12.67           C  
ATOM   1000  C   TYR A 134      15.465  29.321  -6.947  1.00 13.27           C  
ATOM   1001  O   TYR A 134      16.052  29.768  -7.932  1.00 12.80           O  
ATOM   1002  CB  TYR A 134      15.926  29.986  -4.584  1.00 12.91           C  
ATOM   1003  CG  TYR A 134      17.398  29.906  -4.905  1.00 13.49           C  
ATOM   1004  CD1 TYR A 134      18.137  31.058  -5.166  1.00 17.00           C  
ATOM   1005  CD2 TYR A 134      18.044  28.675  -4.984  1.00 15.14           C  
ATOM   1006  CE1 TYR A 134      19.481  30.984  -5.491  1.00 17.46           C  
ATOM   1007  CE2 TYR A 134      19.384  28.589  -5.311  1.00 16.66           C  
ATOM   1008  CZ  TYR A 134      20.097  29.746  -5.567  1.00 18.60           C  
ATOM   1009  OH  TYR A 134      21.437  29.667  -5.874  1.00 24.29           O  
ATOM   1010  N   LEU A 135      15.180  28.033  -6.798  1.00 12.79           N  
ATOM   1011  CA  LEU A 135      15.561  27.025  -7.780  1.00 12.48           C  
ATOM   1012  C   LEU A 135      14.724  27.003  -9.053  1.00 13.47           C  
ATOM   1013  O   LEU A 135      15.187  26.522 -10.091  1.00 14.66           O  
ATOM   1014  CB  LEU A 135      15.515  25.642  -7.134  1.00 11.42           C  
ATOM   1015  CG  LEU A 135      16.454  25.398  -5.954  1.00 11.43           C  
ATOM   1016  CD1 LEU A 135      16.093  24.089  -5.278  1.00 12.08           C  
ATOM   1017  CD2 LEU A 135      17.898  25.384  -6.423  1.00 12.85           C  
ATOM   1018  N   GLY A 136      13.497  27.505  -8.977  1.00 12.08           N  
ATOM   1019  CA  GLY A 136      12.628  27.483 -10.138  1.00 12.70           C  
ATOM   1020  C   GLY A 136      12.241  26.047 -10.472  1.00 15.10           C  
ATOM   1021  O   GLY A 136      11.907  25.734 -11.624  1.00 14.18           O  
ATOM   1022  N   LYS A 137      12.274  25.181  -9.457  1.00 13.73           N  
ATOM   1023  CA  LYS A 137      11.944  23.764  -9.593  1.00 14.67           C  
ATOM   1024  C   LYS A 137      11.239  23.290  -8.337  1.00 15.09           C  
ATOM   1025  O   LYS A 137      11.422  23.859  -7.255  1.00 13.39           O  
ATOM   1026  CB  LYS A 137      13.212  22.915  -9.727  1.00 14.68           C  
ATOM   1027  CG  LYS A 137      14.122  23.252 -10.882  1.00 22.00           C  
ATOM   1028  CD  LYS A 137      15.389  22.437 -10.778  1.00 24.33           C  
ATOM   1029  CE  LYS A 137      16.385  22.806 -11.858  1.00 29.37           C  
ATOM   1030  NZ  LYS A 137      17.643  22.021 -11.692  1.00 32.15           N  
ATOM   1031  N   THR A 138      10.451  22.232  -8.482  1.00 14.75           N  
ATOM   1032  CA  THR A 138       9.751  21.643  -7.349  1.00 13.68           C  
ATOM   1033  C   THR A 138      10.783  20.958  -6.449  1.00 11.47           C  
ATOM   1034  O   THR A 138      11.689  20.286  -6.936  1.00 11.55           O  
ATOM   1035  CB  THR A 138       8.700  20.606  -7.827  1.00 15.90           C  
ATOM   1036  OG1 THR A 138       7.625  21.291  -8.481  1.00 17.92           O  
ATOM   1037  CG2 THR A 138       8.148  19.798  -6.659  1.00 15.98           C  
ATOM   1038  N   VAL A 139      10.666  21.186  -5.145  1.00 10.77           N  
ATOM   1039  CA  VAL A 139      11.556  20.598  -4.149  1.00 10.66           C  
ATOM   1040  C   VAL A 139      10.779  19.551  -3.358  1.00 10.86           C  
ATOM   1041  O   VAL A 139       9.729  19.858  -2.803  1.00 12.70           O  
ATOM   1042  CB  VAL A 139      12.071  21.672  -3.162  1.00  9.96           C  
ATOM   1043  CG1 VAL A 139      12.824  21.019  -2.000  1.00 12.04           C  
ATOM   1044  CG2 VAL A 139      12.967  22.651  -3.891  1.00  9.93           C  
ATOM   1045  N   THR A 140      11.299  18.329  -3.307  1.00 10.79           N  
ATOM   1046  CA  THR A 140      10.647  17.249  -2.578  1.00 13.50           C  
ATOM   1047  C   THR A 140      11.550  16.635  -1.505  1.00 13.22           C  
ATOM   1048  O   THR A 140      11.185  16.587  -0.333  1.00 16.25           O  
ATOM   1049  CB  THR A 140      10.178  16.141  -3.536  1.00 17.94           C  
ATOM   1050  OG1 THR A 140       9.219  16.684  -4.455  1.00 21.29           O  
ATOM   1051  CG2 THR A 140       9.529  14.992  -2.758  1.00 19.23           C  
ATOM   1052  N   ASN A 141      12.741  16.200  -1.900  1.00 11.87           N  
ATOM   1053  CA  ASN A 141      13.680  15.574  -0.973  1.00 10.58           C  
ATOM   1054  C   ASN A 141      14.378  16.576  -0.069  1.00  9.70           C  
ATOM   1055  O   ASN A 141      14.830  17.633  -0.528  1.00  7.75           O  
ATOM   1056  CB  ASN A 141      14.724  14.779  -1.747  1.00 14.63           C  
ATOM   1057  CG  ASN A 141      14.104  13.773  -2.682  1.00 18.13           C  
ATOM   1058  OD1 ASN A 141      13.141  13.093  -2.329  1.00 17.60           O  
ATOM   1059  ND2 ASN A 141      14.642  13.680  -3.889  1.00 21.53           N  
ATOM   1060  N   ALA A 142      14.496  16.226   1.208  1.00  8.73           N  
ATOM   1061  CA  ALA A 142      15.148  17.100   2.173  1.00  8.33           C  
ATOM   1062  C   ALA A 142      15.726  16.351   3.351  1.00  8.32           C  
ATOM   1063  O   ALA A 142      15.348  15.215   3.635  1.00  7.54           O  
ATOM   1064  CB  ALA A 142      14.165  18.151   2.685  1.00  6.80           C  
ATOM   1065  N   VAL A 143      16.718  16.974   3.973  1.00  8.92           N  
ATOM   1066  CA  VAL A 143      17.337  16.457   5.186  1.00  8.99           C  
ATOM   1067  C   VAL A 143      16.922  17.528   6.190  1.00  9.08           C  
ATOM   1068  O   VAL A 143      17.065  18.722   5.915  1.00  8.18           O  
ATOM   1069  CB  VAL A 143      18.888  16.393   5.096  1.00  9.09           C  
ATOM   1070  CG1 VAL A 143      19.508  16.341   6.502  1.00  8.90           C  
ATOM   1071  CG2 VAL A 143      19.308  15.155   4.323  1.00  9.05           C  
ATOM   1072  N   VAL A 144      16.319  17.110   7.298  1.00  8.71           N  
ATOM   1073  CA  VAL A 144      15.878  18.044   8.329  1.00  7.73           C  
ATOM   1074  C   VAL A 144      16.685  17.732   9.590  1.00  8.94           C  
ATOM   1075  O   VAL A 144      16.884  16.564   9.937  1.00  9.07           O  
ATOM   1076  CB  VAL A 144      14.346  17.918   8.596  1.00  7.40           C  
ATOM   1077  CG1 VAL A 144      13.895  18.933   9.651  1.00  7.17           C  
ATOM   1078  CG2 VAL A 144      13.567  18.127   7.297  1.00  7.19           C  
ATOM   1079  N   THR A 145      17.195  18.771  10.243  1.00  8.10           N  
ATOM   1080  CA  THR A 145      18.011  18.588  11.438  1.00  7.57           C  
ATOM   1081  C   THR A 145      17.243  18.713  12.766  1.00  7.40           C  
ATOM   1082  O   THR A 145      16.174  19.329  12.819  1.00  5.85           O  
ATOM   1083  CB  THR A 145      19.213  19.580  11.419  1.00  7.33           C  
ATOM   1084  OG1 THR A 145      18.735  20.920  11.248  1.00  5.72           O  
ATOM   1085  CG2 THR A 145      20.170  19.256  10.279  1.00  6.46           C  
ATOM   1086  N   VAL A 146      17.789  18.103  13.822  1.00  6.58           N  
ATOM   1087  CA  VAL A 146      17.209  18.151  15.172  1.00  7.47           C  
ATOM   1088  C   VAL A 146      18.337  18.211  16.222  1.00  8.14           C  
ATOM   1089  O   VAL A 146      19.487  17.863  15.926  1.00  7.06           O  
ATOM   1090  CB  VAL A 146      16.333  16.902  15.488  1.00  7.65           C  
ATOM   1091  CG1 VAL A 146      15.114  16.848  14.577  1.00  9.01           C  
ATOM   1092  CG2 VAL A 146      17.154  15.626  15.383  1.00  6.83           C  
ATOM   1093  N   PRO A 147      18.043  18.737  17.427  1.00  8.10           N  
ATOM   1094  CA  PRO A 147      19.085  18.801  18.459  1.00  8.78           C  
ATOM   1095  C   PRO A 147      19.509  17.373  18.791  1.00  8.66           C  
ATOM   1096  O   PRO A 147      18.687  16.454  18.776  1.00  7.98           O  
ATOM   1097  CB  PRO A 147      18.361  19.451  19.641  1.00  8.17           C  
ATOM   1098  CG  PRO A 147      17.340  20.326  18.976  1.00  7.69           C  
ATOM   1099  CD  PRO A 147      16.814  19.410  17.883  1.00  6.92           C  
ATOM   1100  N   ALA A 148      20.780  17.202  19.133  1.00  8.48           N  
ATOM   1101  CA  ALA A 148      21.339  15.890  19.447  1.00  9.45           C  
ATOM   1102  C   ALA A 148      20.606  15.136  20.542  1.00 10.44           C  
ATOM   1103  O   ALA A 148      20.618  13.901  20.557  1.00 13.50           O  
ATOM   1104  CB  ALA A 148      22.809  16.023  19.811  1.00  8.98           C  
ATOM   1105  N   TYR A 149      19.987  15.868  21.466  1.00 10.02           N  
ATOM   1106  CA  TYR A 149      19.264  15.243  22.568  1.00  9.22           C  
ATOM   1107  C   TYR A 149      17.827  14.815  22.258  1.00  8.36           C  
ATOM   1108  O   TYR A 149      17.145  14.275  23.132  1.00  9.30           O  
ATOM   1109  CB  TYR A 149      19.279  16.150  23.802  1.00  9.50           C  
ATOM   1110  CG  TYR A 149      18.677  17.509  23.565  1.00 11.00           C  
ATOM   1111  CD1 TYR A 149      17.288  17.694  23.586  1.00 10.60           C  
ATOM   1112  CD2 TYR A 149      19.491  18.615  23.303  1.00 12.67           C  
ATOM   1113  CE1 TYR A 149      16.726  18.938  23.338  1.00 10.42           C  
ATOM   1114  CE2 TYR A 149      18.937  19.867  23.054  1.00 12.22           C  
ATOM   1115  CZ  TYR A 149      17.557  20.022  23.076  1.00 12.95           C  
ATOM   1116  OH  TYR A 149      17.016  21.257  22.809  1.00 17.45           O  
ATOM   1117  N   PHE A 150      17.344  15.095  21.051  1.00  8.82           N  
ATOM   1118  CA  PHE A 150      15.979  14.709  20.699  1.00  8.28           C  
ATOM   1119  C   PHE A 150      15.837  13.194  20.731  1.00  9.36           C  
ATOM   1120  O   PHE A 150      16.737  12.473  20.296  1.00 10.20           O  
ATOM   1121  CB  PHE A 150      15.584  15.244  19.316  1.00  6.97           C  
ATOM   1122  CG  PHE A 150      14.828  16.548  19.358  1.00  6.68           C  
ATOM   1123  CD1 PHE A 150      14.988  17.438  20.420  1.00  6.53           C  
ATOM   1124  CD2 PHE A 150      13.946  16.886  18.336  1.00  8.50           C  
ATOM   1125  CE1 PHE A 150      14.279  18.639  20.466  1.00  7.02           C  
ATOM   1126  CE2 PHE A 150      13.229  18.087  18.374  1.00  7.13           C  
ATOM   1127  CZ  PHE A 150      13.400  18.963  19.443  1.00  6.85           C  
ATOM   1128  N   ASN A 151      14.727  12.718  21.288  1.00  9.10           N  
ATOM   1129  CA  ASN A 151      14.467  11.282  21.368  1.00  9.38           C  
ATOM   1130  C   ASN A 151      13.749  10.772  20.108  1.00  9.81           C  
ATOM   1131  O   ASN A 151      13.474  11.541  19.182  1.00  8.50           O  
ATOM   1132  CB  ASN A 151      13.668  10.939  22.636  1.00  9.85           C  
ATOM   1133  CG  ASN A 151      12.301  11.612  22.688  1.00  9.66           C  
ATOM   1134  OD1 ASN A 151      11.670  11.850  21.665  1.00  8.10           O  
ATOM   1135  ND2 ASN A 151      11.836  11.908  23.896  1.00 10.16           N  
ATOM   1136  N   ASP A 152      13.435   9.479  20.086  1.00 10.67           N  
ATOM   1137  CA  ASP A 152      12.762   8.869  18.944  1.00  9.11           C  
ATOM   1138  C   ASP A 152      11.445   9.545  18.593  1.00 10.38           C  
ATOM   1139  O   ASP A 152      11.149   9.756  17.419  1.00 10.46           O  
ATOM   1140  CB  ASP A 152      12.521   7.377  19.193  1.00 11.46           C  
ATOM   1141  CG  ASP A 152      13.806   6.544  19.122  1.00 16.87           C  
ATOM   1142  OD1 ASP A 152      14.858   7.066  18.696  1.00 14.91           O  
ATOM   1143  OD2 ASP A 152      13.756   5.347  19.480  1.00 18.52           O  
ATOM   1144  N   SER A 153      10.659   9.883  19.607  1.00  8.77           N  
ATOM   1145  CA  SER A 153       9.372  10.531  19.391  1.00  9.80           C  
ATOM   1146  C   SER A 153       9.522  11.940  18.799  1.00  8.56           C  
ATOM   1147  O   SER A 153       8.791  12.319  17.878  1.00  8.00           O  
ATOM   1148  CB  SER A 153       8.583  10.574  20.706  1.00 10.91           C  
ATOM   1149  OG  SER A 153       7.327  11.216  20.535  1.00 15.22           O  
ATOM   1150  N   GLN A 154      10.475  12.707  19.318  1.00  7.54           N  
ATOM   1151  CA  GLN A 154      10.721  14.061  18.837  1.00  6.86           C  
ATOM   1152  C   GLN A 154      11.249  14.027  17.403  1.00  7.88           C  
ATOM   1153  O   GLN A 154      10.916  14.896  16.592  1.00  8.12           O  
ATOM   1154  CB  GLN A 154      11.706  14.773  19.758  1.00  7.10           C  
ATOM   1155  CG  GLN A 154      11.151  15.058  21.140  1.00  6.48           C  
ATOM   1156  CD  GLN A 154      12.215  15.546  22.095  1.00  5.85           C  
ATOM   1157  OE1 GLN A 154      13.149  14.815  22.412  1.00  8.75           O  
ATOM   1158  NE2 GLN A 154      12.099  16.792  22.538  1.00  6.86           N  
ATOM   1159  N   ARG A 155      12.060  13.017  17.095  1.00  7.26           N  
ATOM   1160  CA  ARG A 155      12.609  12.847  15.752  1.00  7.42           C  
ATOM   1161  C   ARG A 155      11.493  12.440  14.786  1.00  8.06           C  
ATOM   1162  O   ARG A 155      11.385  12.978  13.677  1.00  7.39           O  
ATOM   1163  CB  ARG A 155      13.727  11.796  15.760  1.00  9.05           C  
ATOM   1164  CG  ARG A 155      14.966  12.278  16.494  1.00  7.72           C  
ATOM   1165  CD  ARG A 155      16.063  11.227  16.628  1.00  8.23           C  
ATOM   1166  NE  ARG A 155      17.073  11.716  17.566  1.00  9.48           N  
ATOM   1167  CZ  ARG A 155      18.152  12.415  17.214  1.00  9.24           C  
ATOM   1168  NH1 ARG A 155      18.450  12.610  15.932  1.00 10.14           N  
ATOM   1169  NH2 ARG A 155      18.985  12.851  18.147  1.00  9.93           N  
ATOM   1170  N   GLN A 156      10.634  11.535  15.244  1.00  6.95           N  
ATOM   1171  CA  GLN A 156       9.512  11.061  14.445  1.00  8.24           C  
ATOM   1172  C   GLN A 156       8.578  12.216  14.115  1.00  7.76           C  
ATOM   1173  O   GLN A 156       8.211  12.403  12.952  1.00  9.91           O  
ATOM   1174  CB  GLN A 156       8.739   9.974  15.195  1.00  8.29           C  
ATOM   1175  CG  GLN A 156       7.543   9.418  14.432  1.00  9.86           C  
ATOM   1176  CD  GLN A 156       7.948   8.602  13.225  1.00  9.34           C  
ATOM   1177  OE1 GLN A 156       8.440   7.481  13.355  1.00  9.85           O  
ATOM   1178  NE2 GLN A 156       7.721   9.150  12.039  1.00 10.46           N  
ATOM   1179  N   ALA A 157       8.205  12.991  15.131  1.00  7.15           N  
ATOM   1180  CA  ALA A 157       7.297  14.131  14.956  1.00  8.57           C  
ATOM   1181  C   ALA A 157       7.873  15.197  14.019  1.00  8.58           C  
ATOM   1182  O   ALA A 157       7.131  15.868  13.287  1.00  7.56           O  
ATOM   1183  CB  ALA A 157       6.946  14.746  16.317  1.00  8.28           C  
ATOM   1184  N   THR A 158       9.194  15.348  14.049  1.00  8.35           N  
ATOM   1185  CA  THR A 158       9.873  16.313  13.192  1.00  8.40           C  
ATOM   1186  C   THR A 158       9.819  15.810  11.749  1.00  8.97           C  
ATOM   1187  O   THR A 158       9.520  16.580  10.828  1.00  7.30           O  
ATOM   1188  CB  THR A 158      11.336  16.535  13.645  1.00  7.82           C  
ATOM   1189  OG1 THR A 158      11.339  17.109  14.959  1.00  7.92           O  
ATOM   1190  CG2 THR A 158      12.062  17.479  12.698  1.00  8.55           C  
ATOM   1191  N   LYS A 159      10.077  14.516  11.562  1.00  7.19           N  
ATOM   1192  CA  LYS A 159      10.024  13.924  10.230  1.00  7.75           C  
ATOM   1193  C   LYS A 159       8.599  14.067   9.692  1.00  8.50           C  
ATOM   1194  O   LYS A 159       8.400  14.434   8.532  1.00  6.66           O  
ATOM   1195  CB  LYS A 159      10.415  12.453  10.259  1.00  7.48           C  
ATOM   1196  CG  LYS A 159      10.357  11.821   8.882  1.00 11.61           C  
ATOM   1197  CD  LYS A 159      10.434  10.319   8.944  1.00 16.07           C  
ATOM   1198  CE  LYS A 159      10.187   9.726   7.570  1.00 19.36           C  
ATOM   1199  NZ  LYS A 159      10.156   8.244   7.615  1.00 22.28           N  
ATOM   1200  N   ASP A 160       7.616  13.813  10.558  1.00  7.41           N  
ATOM   1201  CA  ASP A 160       6.207  13.934  10.190  1.00  7.37           C  
ATOM   1202  C   ASP A 160       5.865  15.341   9.705  1.00  6.80           C  
ATOM   1203  O   ASP A 160       5.104  15.500   8.752  1.00  5.32           O  
ATOM   1204  CB  ASP A 160       5.294  13.552  11.361  1.00  6.81           C  
ATOM   1205  CG  ASP A 160       5.378  12.080  11.718  1.00  9.30           C  
ATOM   1206  OD1 ASP A 160       5.941  11.287  10.934  1.00  8.36           O  
ATOM   1207  OD2 ASP A 160       4.881  11.715  12.804  1.00 11.01           O  
ATOM   1208  N   ALA A 161       6.415  16.356  10.369  1.00  6.12           N  
ATOM   1209  CA  ALA A 161       6.182  17.742   9.980  1.00  5.90           C  
ATOM   1210  C   ALA A 161       6.641  17.925   8.529  1.00  6.92           C  
ATOM   1211  O   ALA A 161       5.971  18.585   7.728  1.00  6.29           O  
ATOM   1212  CB  ALA A 161       6.948  18.677  10.899  1.00  5.54           C  
ATOM   1213  N   GLY A 162       7.779  17.315   8.199  1.00  6.00           N  
ATOM   1214  CA  GLY A 162       8.307  17.385   6.847  1.00  7.14           C  
ATOM   1215  C   GLY A 162       7.376  16.695   5.868  1.00  7.04           C  
ATOM   1216  O   GLY A 162       7.021  17.248   4.826  1.00  7.48           O  
ATOM   1217  N   THR A 163       6.951  15.491   6.221  1.00  7.67           N  
ATOM   1218  CA  THR A 163       6.046  14.716   5.382  1.00  9.63           C  
ATOM   1219  C   THR A 163       4.762  15.494   5.095  1.00  9.87           C  
ATOM   1220  O   THR A 163       4.314  15.567   3.948  1.00 10.49           O  
ATOM   1221  CB  THR A 163       5.704  13.382   6.057  1.00 10.00           C  
ATOM   1222  OG1 THR A 163       6.921  12.668   6.319  1.00 13.19           O  
ATOM   1223  CG2 THR A 163       4.802  12.541   5.171  1.00 11.93           C  
ATOM   1224  N   ILE A 164       4.199  16.106   6.133  1.00  9.80           N  
ATOM   1225  CA  ILE A 164       2.966  16.883   6.004  1.00 10.08           C  
ATOM   1226  C   ILE A 164       3.167  18.061   5.053  1.00 11.84           C  
ATOM   1227  O   ILE A 164       2.258  18.411   4.277  1.00 11.31           O  
ATOM   1228  CB  ILE A 164       2.470  17.356   7.391  1.00 10.28           C  
ATOM   1229  CG1 ILE A 164       2.011  16.137   8.197  1.00 11.11           C  
ATOM   1230  CG2 ILE A 164       1.338  18.389   7.258  1.00  9.74           C  
ATOM   1231  CD1 ILE A 164       1.686  16.434   9.640  1.00 11.43           C  
ATOM   1232  N   ALA A 165       4.372  18.629   5.081  1.00  9.70           N  
ATOM   1233  CA  ALA A 165       4.729  19.756   4.219  1.00 10.21           C  
ATOM   1234  C   ALA A 165       4.970  19.321   2.768  1.00  9.68           C  
ATOM   1235  O   ALA A 165       5.203  20.158   1.895  1.00 10.73           O  
ATOM   1236  CB  ALA A 165       5.962  20.481   4.770  1.00 10.55           C  
ATOM   1237  N   GLY A 166       4.919  18.017   2.519  1.00  8.65           N  
ATOM   1238  CA  GLY A 166       5.112  17.508   1.173  1.00 10.88           C  
ATOM   1239  C   GLY A 166       6.551  17.164   0.864  1.00 11.50           C  
ATOM   1240  O   GLY A 166       6.928  16.965  -0.293  1.00 12.13           O  
ATOM   1241  N   LEU A 167       7.359  17.062   1.906  1.00 11.00           N  
ATOM   1242  CA  LEU A 167       8.758  16.736   1.731  1.00 10.56           C  
ATOM   1243  C   LEU A 167       9.015  15.266   2.006  1.00 11.39           C  
ATOM   1244  O   LEU A 167       8.341  14.647   2.833  1.00 12.64           O  
ATOM   1245  CB  LEU A 167       9.616  17.569   2.684  1.00 10.42           C  
ATOM   1246  CG  LEU A 167       9.611  19.088   2.500  1.00 11.94           C  
ATOM   1247  CD1 LEU A 167      10.167  19.752   3.748  1.00 13.76           C  
ATOM   1248  CD2 LEU A 167      10.412  19.483   1.261  1.00 11.48           C  
ATOM   1249  N   ASN A 168       9.944  14.692   1.256  1.00 11.43           N  
ATOM   1250  CA  ASN A 168      10.350  13.316   1.471  1.00 11.01           C  
ATOM   1251  C   ASN A 168      11.615  13.503   2.301  1.00 11.08           C  
ATOM   1252  O   ASN A 168      12.658  13.917   1.779  1.00  8.55           O  
ATOM   1253  CB  ASN A 168      10.688  12.612   0.156  1.00 11.87           C  
ATOM   1254  CG  ASN A 168      11.334  11.259   0.379  1.00 16.78           C  
ATOM   1255  OD1 ASN A 168      10.828  10.440   1.147  1.00 19.65           O  
ATOM   1256  ND2 ASN A 168      12.465  11.022  -0.273  1.00 18.67           N  
ATOM   1257  N   VAL A 169      11.480  13.335   3.612  1.00 10.29           N  
ATOM   1258  CA  VAL A 169      12.607  13.496   4.514  1.00 10.93           C  
ATOM   1259  C   VAL A 169      13.566  12.323   4.354  1.00 11.62           C  
ATOM   1260  O   VAL A 169      13.307  11.217   4.834  1.00 11.02           O  
ATOM   1261  CB  VAL A 169      12.150  13.618   5.984  1.00 10.09           C  
ATOM   1262  CG1 VAL A 169      13.368  13.770   6.901  1.00  7.11           C  
ATOM   1263  CG2 VAL A 169      11.211  14.812   6.141  1.00  8.10           C  
ATOM   1264  N   LEU A 170      14.663  12.582   3.650  1.00 10.95           N  
ATOM   1265  CA  LEU A 170      15.691  11.584   3.390  1.00 11.84           C  
ATOM   1266  C   LEU A 170      16.289  11.060   4.691  1.00 11.48           C  
ATOM   1267  O   LEU A 170      16.535   9.859   4.842  1.00 10.29           O  
ATOM   1268  CB  LEU A 170      16.794  12.199   2.522  1.00 12.01           C  
ATOM   1269  CG  LEU A 170      16.430  12.576   1.085  1.00 11.17           C  
ATOM   1270  CD1 LEU A 170      17.568  13.369   0.451  1.00 13.94           C  
ATOM   1271  CD2 LEU A 170      16.130  11.317   0.283  1.00 11.64           C  
ATOM   1272  N   ARG A 171      16.498  11.966   5.638  1.00 11.00           N  
ATOM   1273  CA  ARG A 171      17.070  11.600   6.920  1.00 12.59           C  
ATOM   1274  C   ARG A 171      16.967  12.753   7.897  1.00 11.77           C  
ATOM   1275  O   ARG A 171      16.889  13.918   7.491  1.00 11.49           O  
ATOM   1276  CB  ARG A 171      18.546  11.229   6.750  1.00 16.29           C  
ATOM   1277  CG  ARG A 171      19.195  10.683   8.011  1.00 21.51           C  
ATOM   1278  CD  ARG A 171      20.653  10.327   7.781  1.00 27.40           C  
ATOM   1279  NE  ARG A 171      20.804   9.200   6.867  1.00 30.92           N  
ATOM   1280  CZ  ARG A 171      21.964   8.814   6.338  1.00 31.38           C  
ATOM   1281  NH1 ARG A 171      23.085   9.467   6.630  1.00 30.08           N  
ATOM   1282  NH2 ARG A 171      22.002   7.767   5.520  1.00 30.54           N  
ATOM   1283  N   ILE A 172      16.888  12.407   9.178  1.00 11.40           N  
ATOM   1284  CA  ILE A 172      16.856  13.384  10.259  1.00  9.76           C  
ATOM   1285  C   ILE A 172      18.259  13.261  10.856  1.00  8.79           C  
ATOM   1286  O   ILE A 172      18.679  12.158  11.217  1.00  8.41           O  
ATOM   1287  CB  ILE A 172      15.819  13.010  11.359  1.00  9.59           C  
ATOM   1288  CG1 ILE A 172      14.384  13.152  10.833  1.00  9.82           C  
ATOM   1289  CG2 ILE A 172      16.026  13.887  12.597  1.00  9.57           C  
ATOM   1290  CD1 ILE A 172      13.960  14.584  10.563  1.00 11.40           C  
ATOM   1291  N   ILE A 173      19.012  14.355  10.883  1.00  8.53           N  
ATOM   1292  CA  ILE A 173      20.361  14.312  11.449  1.00  9.33           C  
ATOM   1293  C   ILE A 173      20.518  15.344  12.562  1.00  8.46           C  
ATOM   1294  O   ILE A 173      19.734  16.299  12.665  1.00  7.32           O  
ATOM   1295  CB  ILE A 173      21.496  14.512  10.377  1.00 11.51           C  
ATOM   1296  CG1 ILE A 173      21.489  15.935   9.818  1.00 13.69           C  
ATOM   1297  CG2 ILE A 173      21.357  13.507   9.243  1.00 13.67           C  
ATOM   1298  CD1 ILE A 173      22.657  16.229   8.884  1.00 13.96           C  
ATOM   1299  N   ASN A 174      21.539  15.146  13.387  1.00  8.22           N  
ATOM   1300  CA  ASN A 174      21.812  16.039  14.504  1.00  7.81           C  
ATOM   1301  C   ASN A 174      22.386  17.363  14.045  1.00  6.58           C  
ATOM   1302  O   ASN A 174      23.270  17.407  13.196  1.00  6.09           O  
ATOM   1303  CB  ASN A 174      22.772  15.375  15.495  1.00  7.90           C  
ATOM   1304  CG  ASN A 174      22.142  14.196  16.211  1.00 10.10           C  
ATOM   1305  OD1 ASN A 174      20.930  14.160  16.408  1.00 11.20           O  
ATOM   1306  ND2 ASN A 174      22.955  13.219  16.584  1.00 10.92           N  
ATOM   1307  N   GLU A 175      21.898  18.437  14.650  1.00  6.85           N  
ATOM   1308  CA  GLU A 175      22.343  19.785  14.343  1.00  6.88           C  
ATOM   1309  C   GLU A 175      23.853  19.972  14.513  1.00  7.89           C  
ATOM   1310  O   GLU A 175      24.507  20.509  13.617  1.00  7.10           O  
ATOM   1311  CB  GLU A 175      21.553  20.801  15.172  1.00  8.41           C  
ATOM   1312  CG  GLU A 175      20.097  20.885  14.734  1.00  7.93           C  
ATOM   1313  CD  GLU A 175      19.205  21.661  15.683  1.00 12.35           C  
ATOM   1314  OE1 GLU A 175      19.713  22.376  16.573  1.00 14.08           O  
ATOM   1315  OE2 GLU A 175      17.970  21.544  15.534  1.00  8.23           O  
ATOM   1316  N   PRO A 176      24.435  19.503  15.640  1.00  8.22           N  
ATOM   1317  CA  PRO A 176      25.888  19.681  15.804  1.00  8.93           C  
ATOM   1318  C   PRO A 176      26.690  18.937  14.733  1.00  9.30           C  
ATOM   1319  O   PRO A 176      27.709  19.434  14.249  1.00  9.80           O  
ATOM   1320  CB  PRO A 176      26.146  19.148  17.220  1.00  8.55           C  
ATOM   1321  CG  PRO A 176      25.021  18.174  17.446  1.00  7.78           C  
ATOM   1322  CD  PRO A 176      23.845  18.894  16.846  1.00  7.64           C  
ATOM   1323  N   THR A 177      26.190  17.774  14.330  1.00  7.88           N  
ATOM   1324  CA  THR A 177      26.822  16.961  13.296  1.00  9.06           C  
ATOM   1325  C   THR A 177      26.742  17.706  11.959  1.00  8.51           C  
ATOM   1326  O   THR A 177      27.713  17.735  11.198  1.00  8.14           O  
ATOM   1327  CB  THR A 177      26.112  15.593  13.183  1.00 11.94           C  
ATOM   1328  OG1 THR A 177      26.210  14.907  14.440  1.00 13.55           O  
ATOM   1329  CG2 THR A 177      26.735  14.738  12.085  1.00 11.81           C  
ATOM   1330  N   ALA A 178      25.586  18.309  11.680  1.00  7.63           N  
ATOM   1331  CA  ALA A 178      25.388  19.073  10.449  1.00  6.35           C  
ATOM   1332  C   ALA A 178      26.397  20.223  10.408  1.00  5.97           C  
ATOM   1333  O   ALA A 178      27.029  20.471   9.377  1.00  6.20           O  
ATOM   1334  CB  ALA A 178      23.955  19.609  10.375  1.00  6.64           C  
ATOM   1335  N   ALA A 179      26.593  20.878  11.551  1.00  5.92           N  
ATOM   1336  CA  ALA A 179      27.546  21.987  11.644  1.00  7.89           C  
ATOM   1337  C   ALA A 179      28.969  21.505  11.332  1.00  7.82           C  
ATOM   1338  O   ALA A 179      29.712  22.169  10.599  1.00  9.46           O  
ATOM   1339  CB  ALA A 179      27.483  22.631  13.023  1.00  5.74           C  
ATOM   1340  N   ALA A 180      29.328  20.336  11.862  1.00  7.18           N  
ATOM   1341  CA  ALA A 180      30.645  19.748  11.628  1.00  7.46           C  
ATOM   1342  C   ALA A 180      30.827  19.412  10.147  1.00  9.20           C  
ATOM   1343  O   ALA A 180      31.909  19.611   9.583  1.00  8.42           O  
ATOM   1344  CB  ALA A 180      30.820  18.502  12.468  1.00  7.40           C  
ATOM   1345  N   ILE A 181      29.773  18.893   9.521  1.00  8.58           N  
ATOM   1346  CA  ILE A 181      29.818  18.543   8.105  1.00  8.69           C  
ATOM   1347  C   ILE A 181      30.034  19.785   7.238  1.00  8.70           C  
ATOM   1348  O   ILE A 181      30.767  19.735   6.247  1.00  8.95           O  
ATOM   1349  CB  ILE A 181      28.537  17.785   7.672  1.00  8.25           C  
ATOM   1350  CG1 ILE A 181      28.541  16.384   8.288  1.00  7.30           C  
ATOM   1351  CG2 ILE A 181      28.452  17.686   6.147  1.00  7.80           C  
ATOM   1352  CD1 ILE A 181      27.230  15.640   8.139  1.00  8.74           C  
ATOM   1353  N   ALA A 182      29.448  20.907   7.644  1.00  7.91           N  
ATOM   1354  CA  ALA A 182      29.595  22.160   6.901  1.00  7.61           C  
ATOM   1355  C   ALA A 182      31.072  22.555   6.782  1.00  7.97           C  
ATOM   1356  O   ALA A 182      31.503  23.068   5.748  1.00  7.04           O  
ATOM   1357  CB  ALA A 182      28.785  23.282   7.568  1.00  7.03           C  
ATOM   1358  N   TYR A 183      31.849  22.273   7.824  1.00  7.62           N  
ATOM   1359  CA  TYR A 183      33.276  22.596   7.829  1.00  8.99           C  
ATOM   1360  C   TYR A 183      34.164  21.460   7.318  1.00 10.66           C  
ATOM   1361  O   TYR A 183      35.383  21.493   7.492  1.00 12.47           O  
ATOM   1362  CB  TYR A 183      33.717  23.016   9.236  1.00  7.22           C  
ATOM   1363  CG  TYR A 183      33.347  24.439   9.571  1.00  8.59           C  
ATOM   1364  CD1 TYR A 183      34.156  25.498   9.163  1.00  7.81           C  
ATOM   1365  CD2 TYR A 183      32.186  24.734  10.291  1.00  9.57           C  
ATOM   1366  CE1 TYR A 183      33.833  26.809   9.459  1.00  7.43           C  
ATOM   1367  CE2 TYR A 183      31.847  26.059  10.598  1.00  8.55           C  
ATOM   1368  CZ  TYR A 183      32.683  27.088  10.179  1.00  7.89           C  
ATOM   1369  OH  TYR A 183      32.395  28.390  10.496  1.00  7.54           O  
ATOM   1370  N   GLY A 184      33.545  20.438   6.738  1.00  8.80           N  
ATOM   1371  CA  GLY A 184      34.294  19.304   6.220  1.00 10.92           C  
ATOM   1372  C   GLY A 184      34.982  18.467   7.288  1.00 12.22           C  
ATOM   1373  O   GLY A 184      35.862  17.666   6.977  1.00 12.19           O  
ATOM   1374  N   LEU A 185      34.533  18.588   8.534  1.00 12.30           N  
ATOM   1375  CA  LEU A 185      35.131  17.844   9.639  1.00 13.71           C  
ATOM   1376  C   LEU A 185      34.787  16.353   9.625  1.00 15.93           C  
ATOM   1377  O   LEU A 185      35.220  15.590  10.488  1.00 16.10           O  
ATOM   1378  CB  LEU A 185      34.756  18.490  10.977  1.00 12.68           C  
ATOM   1379  CG  LEU A 185      35.287  19.923  11.130  1.00 14.79           C  
ATOM   1380  CD1 LEU A 185      34.755  20.572  12.398  1.00 13.81           C  
ATOM   1381  CD2 LEU A 185      36.809  19.911  11.135  1.00 15.42           C  
ATOM   1382  N   ASP A 186      34.005  15.941   8.637  1.00 15.27           N  
ATOM   1383  CA  ASP A 186      33.635  14.538   8.503  1.00 18.94           C  
ATOM   1384  C   ASP A 186      34.592  13.772   7.577  1.00 19.19           C  
ATOM   1385  O   ASP A 186      34.513  12.545   7.473  1.00 19.12           O  
ATOM   1386  CB  ASP A 186      32.189  14.406   8.009  1.00 19.58           C  
ATOM   1387  CG  ASP A 186      31.950  15.108   6.690  1.00 20.89           C  
ATOM   1388  OD1 ASP A 186      32.458  16.231   6.487  1.00 18.69           O  
ATOM   1389  OD2 ASP A 186      31.235  14.534   5.852  1.00 24.77           O  
ATOM   1390  N   LYS A 187      35.478  14.494   6.892  1.00 18.73           N  
ATOM   1391  CA  LYS A 187      36.443  13.862   5.990  1.00 20.50           C  
ATOM   1392  C   LYS A 187      37.430  13.010   6.789  1.00 21.81           C  
ATOM   1393  O   LYS A 187      37.799  13.362   7.909  1.00 20.87           O  
ATOM   1394  CB  LYS A 187      37.227  14.909   5.189  1.00 21.41           C  
ATOM   1395  CG  LYS A 187      36.413  15.748   4.225  1.00 21.78           C  
ATOM   1396  CD  LYS A 187      37.341  16.705   3.499  1.00 24.49           C  
ATOM   1397  CE  LYS A 187      36.592  17.656   2.598  1.00 25.28           C  
ATOM   1398  NZ  LYS A 187      37.564  18.477   1.836  1.00 25.52           N  
ATOM   1399  N   LYS A 188      37.875  11.907   6.198  1.00 25.24           N  
ATOM   1400  CA  LYS A 188      38.816  11.011   6.859  1.00 28.21           C  
ATOM   1401  C   LYS A 188      40.245  11.549   6.778  1.00 30.55           C  
ATOM   1402  O   LYS A 188      40.736  11.871   5.689  1.00 30.05           O  
ATOM   1403  CB  LYS A 188      38.739   9.622   6.238  1.00 27.40           C  
ATOM   1404  N   VAL A 189      40.895  11.671   7.934  1.00 32.37           N  
ATOM   1405  CA  VAL A 189      42.277  12.154   8.008  1.00 33.76           C  
ATOM   1406  C   VAL A 189      43.163  11.117   8.697  1.00 35.13           C  
ATOM   1407  O   VAL A 189      44.358  11.347   8.905  1.00 37.42           O  
ATOM   1408  CB  VAL A 189      42.392  13.487   8.788  1.00 32.11           C  
ATOM   1409  CG1 VAL A 189      41.678  14.606   8.043  1.00 31.48           C  
ATOM   1410  CG2 VAL A 189      41.839  13.323  10.195  1.00 29.91           C  
ATOM   1411  N   GLY A 190      42.569   9.983   9.052  1.00 35.00           N  
ATOM   1412  CA  GLY A 190      43.314   8.934   9.719  1.00 35.79           C  
ATOM   1413  C   GLY A 190      42.730   8.627  11.082  1.00 36.16           C  
ATOM   1414  O   GLY A 190      41.786   7.840  11.194  1.00 38.82           O  
ATOM   1415  N   ALA A 191      43.254   9.286  12.111  1.00 34.74           N  
ATOM   1416  CA  ALA A 191      42.794   9.078  13.479  1.00 30.76           C  
ATOM   1417  C   ALA A 191      41.528   9.864  13.809  1.00 28.92           C  
ATOM   1418  O   ALA A 191      41.093  10.723  13.037  1.00 27.58           O  
ATOM   1419  CB  ALA A 191      43.902   9.435  14.455  1.00 32.35           C  
ATOM   1420  N   GLU A 192      40.948   9.561  14.965  1.00 25.94           N  
ATOM   1421  CA  GLU A 192      39.736  10.228  15.421  1.00 24.58           C  
ATOM   1422  C   GLU A 192      40.026  11.671  15.811  1.00 22.24           C  
ATOM   1423  O   GLU A 192      41.153  12.015  16.183  1.00 21.92           O  
ATOM   1424  CB  GLU A 192      39.136   9.499  16.624  1.00 25.17           C  
ATOM   1425  CG  GLU A 192      40.039   9.499  17.849  1.00 28.64           C  
ATOM   1426  CD  GLU A 192      39.374   8.923  19.088  1.00 28.73           C  
ATOM   1427  OE1 GLU A 192      38.483   8.056  18.948  1.00 28.56           O  
ATOM   1428  OE2 GLU A 192      39.757   9.334  20.205  1.00 28.73           O  
ATOM   1429  N   ARG A 193      38.990  12.499  15.759  1.00 20.10           N  
ATOM   1430  CA  ARG A 193      39.095  13.907  16.111  1.00 19.19           C  
ATOM   1431  C   ARG A 193      37.926  14.295  17.017  1.00 18.73           C  
ATOM   1432  O   ARG A 193      36.803  13.829  16.830  1.00 17.26           O  
ATOM   1433  CB  ARG A 193      39.079  14.781  14.850  1.00 21.57           C  
ATOM   1434  CG  ARG A 193      40.242  14.546  13.877  1.00 24.16           C  
ATOM   1435  CD  ARG A 193      41.584  14.983  14.454  1.00 25.35           C  
ATOM   1436  NE  ARG A 193      42.694  14.662  13.559  1.00 28.64           N  
ATOM   1437  CZ  ARG A 193      43.599  13.708  13.781  1.00 31.72           C  
ATOM   1438  NH1 ARG A 193      43.545  12.967  14.880  1.00 32.82           N  
ATOM   1439  NH2 ARG A 193      44.569  13.503  12.899  1.00 32.15           N  
ATOM   1440  N   ASN A 194      38.216  15.097  18.036  1.00 15.53           N  
ATOM   1441  CA  ASN A 194      37.195  15.567  18.966  1.00 15.38           C  
ATOM   1442  C   ASN A 194      36.861  16.997  18.574  1.00 14.60           C  
ATOM   1443  O   ASN A 194      37.746  17.845  18.476  1.00 14.30           O  
ATOM   1444  CB  ASN A 194      37.713  15.532  20.403  1.00 15.05           C  
ATOM   1445  CG  ASN A 194      38.186  14.159  20.814  1.00 16.11           C  
ATOM   1446  OD1 ASN A 194      37.483  13.170  20.627  1.00 18.41           O  
ATOM   1447  ND2 ASN A 194      39.389  14.086  21.364  1.00 16.03           N  
ATOM   1448  N   VAL A 195      35.588  17.258  18.329  1.00 13.01           N  
ATOM   1449  CA  VAL A 195      35.137  18.581  17.922  1.00 12.39           C  
ATOM   1450  C   VAL A 195      34.090  19.082  18.917  1.00 11.83           C  
ATOM   1451  O   VAL A 195      33.257  18.301  19.387  1.00 11.91           O  
ATOM   1452  CB  VAL A 195      34.514  18.513  16.494  1.00 13.85           C  
ATOM   1453  CG1 VAL A 195      33.923  19.865  16.091  1.00 16.08           C  
ATOM   1454  CG2 VAL A 195      35.569  18.054  15.476  1.00 13.22           C  
ATOM   1455  N   LEU A 196      34.171  20.358  19.285  1.00 10.18           N  
ATOM   1456  CA  LEU A 196      33.199  20.941  20.207  1.00  9.23           C  
ATOM   1457  C   LEU A 196      32.315  21.930  19.453  1.00  8.98           C  
ATOM   1458  O   LEU A 196      32.814  22.824  18.757  1.00  7.54           O  
ATOM   1459  CB  LEU A 196      33.887  21.636  21.395  1.00  8.67           C  
ATOM   1460  CG  LEU A 196      32.957  22.252  22.453  1.00  8.28           C  
ATOM   1461  CD1 LEU A 196      33.545  22.121  23.859  1.00  7.90           C  
ATOM   1462  CD2 LEU A 196      32.657  23.708  22.122  1.00  9.27           C  
ATOM   1463  N   ILE A 197      31.003  21.727  19.552  1.00  8.13           N  
ATOM   1464  CA  ILE A 197      30.028  22.598  18.912  1.00  8.54           C  
ATOM   1465  C   ILE A 197      29.442  23.497  19.996  1.00  8.33           C  
ATOM   1466  O   ILE A 197      28.888  23.012  20.984  1.00  8.69           O  
ATOM   1467  CB  ILE A 197      28.880  21.795  18.258  1.00 10.14           C  
ATOM   1468  CG1 ILE A 197      29.439  20.703  17.335  1.00 10.77           C  
ATOM   1469  CG2 ILE A 197      27.949  22.738  17.498  1.00  9.76           C  
ATOM   1470  CD1 ILE A 197      30.204  21.225  16.137  1.00 10.62           C  
ATOM   1471  N   PHE A 198      29.604  24.802  19.820  1.00  7.52           N  
ATOM   1472  CA  PHE A 198      29.108  25.797  20.765  1.00  7.84           C  
ATOM   1473  C   PHE A 198      27.969  26.498  20.039  1.00  7.70           C  
ATOM   1474  O   PHE A 198      28.194  27.367  19.193  1.00  5.49           O  
ATOM   1475  CB  PHE A 198      30.229  26.783  21.110  1.00  8.18           C  
ATOM   1476  CG  PHE A 198      29.852  27.800  22.146  1.00  7.49           C  
ATOM   1477  CD1 PHE A 198      29.180  28.966  21.786  1.00  7.02           C  
ATOM   1478  CD2 PHE A 198      30.211  27.616  23.479  1.00  8.43           C  
ATOM   1479  CE1 PHE A 198      28.872  29.934  22.734  1.00  8.46           C  
ATOM   1480  CE2 PHE A 198      29.910  28.579  24.434  1.00  7.27           C  
ATOM   1481  CZ  PHE A 198      29.241  29.742  24.061  1.00  8.10           C  
ATOM   1482  N   ASP A 199      26.747  26.114  20.380  1.00  7.35           N  
ATOM   1483  CA  ASP A 199      25.559  26.644  19.726  1.00  6.17           C  
ATOM   1484  C   ASP A 199      24.670  27.506  20.622  1.00  5.06           C  
ATOM   1485  O   ASP A 199      23.907  26.987  21.427  1.00  7.20           O  
ATOM   1486  CB  ASP A 199      24.754  25.460  19.176  1.00  7.17           C  
ATOM   1487  CG  ASP A 199      23.691  25.868  18.171  1.00  9.01           C  
ATOM   1488  OD1 ASP A 199      23.237  27.033  18.171  1.00  7.87           O  
ATOM   1489  OD2 ASP A 199      23.298  24.992  17.371  1.00  9.94           O  
ATOM   1490  N   LEU A 200      24.711  28.816  20.407  1.00  5.75           N  
ATOM   1491  CA  LEU A 200      23.897  29.751  21.172  1.00  6.46           C  
ATOM   1492  C   LEU A 200      22.877  30.385  20.224  1.00  8.00           C  
ATOM   1493  O   LEU A 200      23.212  31.280  19.441  1.00  8.07           O  
ATOM   1494  CB  LEU A 200      24.785  30.820  21.813  1.00  6.75           C  
ATOM   1495  CG  LEU A 200      24.144  31.755  22.838  1.00  6.65           C  
ATOM   1496  CD1 LEU A 200      23.477  30.952  23.949  1.00  7.93           C  
ATOM   1497  CD2 LEU A 200      25.203  32.689  23.400  1.00  7.77           C  
ATOM   1498  N   GLY A 201      21.646  29.884  20.274  1.00  8.05           N  
ATOM   1499  CA  GLY A 201      20.592  30.377  19.406  1.00  8.12           C  
ATOM   1500  C   GLY A 201      19.717  31.493  19.947  1.00  9.84           C  
ATOM   1501  O   GLY A 201      20.186  32.399  20.635  1.00  9.41           O  
ATOM   1502  N   GLY A 202      18.433  31.431  19.613  1.00  9.73           N  
ATOM   1503  CA  GLY A 202      17.492  32.444  20.053  1.00 10.22           C  
ATOM   1504  C   GLY A 202      16.905  32.179  21.425  1.00 10.57           C  
ATOM   1505  O   GLY A 202      16.652  33.113  22.183  1.00 11.10           O  
ATOM   1506  N   GLY A 203      16.663  30.910  21.739  1.00 10.89           N  
ATOM   1507  CA  GLY A 203      16.105  30.564  23.035  1.00 10.98           C  
ATOM   1508  C   GLY A 203      16.805  29.409  23.726  1.00 10.33           C  
ATOM   1509  O   GLY A 203      16.525  29.129  24.888  1.00 11.88           O  
ATOM   1510  N   THR A 204      17.750  28.771  23.042  1.00  9.68           N  
ATOM   1511  CA  THR A 204      18.458  27.629  23.609  1.00 10.10           C  
ATOM   1512  C   THR A 204      19.971  27.708  23.437  1.00 10.08           C  
ATOM   1513  O   THR A 204      20.472  28.349  22.510  1.00 10.42           O  
ATOM   1514  CB  THR A 204      17.972  26.307  22.966  1.00 11.63           C  
ATOM   1515  OG1 THR A 204      18.239  26.331  21.554  1.00 13.60           O  
ATOM   1516  CG2 THR A 204      16.467  26.120  23.188  1.00 10.51           C  
ATOM   1517  N   PHE A 205      20.684  27.013  24.315  1.00  9.15           N  
ATOM   1518  CA  PHE A 205      22.139  26.963  24.288  1.00  8.88           C  
ATOM   1519  C   PHE A 205      22.524  25.485  24.311  1.00  8.89           C  
ATOM   1520  O   PHE A 205      22.158  24.766  25.240  1.00  8.69           O  
ATOM   1521  CB  PHE A 205      22.700  27.684  25.521  1.00  8.01           C  
ATOM   1522  CG  PHE A 205      24.188  27.565  25.675  1.00  8.55           C  
ATOM   1523  CD1 PHE A 205      25.032  27.639  24.565  1.00  9.46           C  
ATOM   1524  CD2 PHE A 205      24.750  27.380  26.934  1.00  8.94           C  
ATOM   1525  CE1 PHE A 205      26.417  27.532  24.707  1.00  9.09           C  
ATOM   1526  CE2 PHE A 205      26.128  27.272  27.089  1.00  9.95           C  
ATOM   1527  CZ  PHE A 205      26.966  27.350  25.970  1.00  9.75           C  
ATOM   1528  N   ASP A 206      23.236  25.026  23.284  1.00  8.24           N  
ATOM   1529  CA  ASP A 206      23.655  23.629  23.191  1.00  9.26           C  
ATOM   1530  C   ASP A 206      25.150  23.490  22.969  1.00 10.63           C  
ATOM   1531  O   ASP A 206      25.696  24.063  22.029  1.00 10.75           O  
ATOM   1532  CB  ASP A 206      22.978  22.928  22.008  1.00 12.60           C  
ATOM   1533  CG  ASP A 206      21.485  22.820  22.162  1.00 17.22           C  
ATOM   1534  OD1 ASP A 206      21.034  22.146  23.108  1.00 17.88           O  
ATOM   1535  OD2 ASP A 206      20.762  23.397  21.324  1.00 18.03           O  
ATOM   1536  N   VAL A 207      25.796  22.697  23.808  1.00  9.19           N  
ATOM   1537  CA  VAL A 207      27.218  22.421  23.668  1.00  9.22           C  
ATOM   1538  C   VAL A 207      27.261  20.922  23.383  1.00  8.66           C  
ATOM   1539  O   VAL A 207      26.593  20.147  24.065  1.00  9.45           O  
ATOM   1540  CB  VAL A 207      28.005  22.716  24.971  1.00  9.63           C  
ATOM   1541  CG1 VAL A 207      29.464  22.283  24.811  1.00 10.87           C  
ATOM   1542  CG2 VAL A 207      27.936  24.191  25.311  1.00  8.33           C  
ATOM   1543  N   SER A 208      27.983  20.516  22.347  1.00  8.10           N  
ATOM   1544  CA  SER A 208      28.077  19.100  22.010  1.00 10.02           C  
ATOM   1545  C   SER A 208      29.512  18.744  21.687  1.00 10.27           C  
ATOM   1546  O   SER A 208      30.222  19.528  21.057  1.00 10.40           O  
ATOM   1547  CB  SER A 208      27.208  18.769  20.784  1.00 11.08           C  
ATOM   1548  OG  SER A 208      25.885  19.273  20.910  1.00 10.21           O  
ATOM   1549  N   ILE A 209      29.961  17.592  22.165  1.00 10.97           N  
ATOM   1550  CA  ILE A 209      31.311  17.141  21.856  1.00 11.50           C  
ATOM   1551  C   ILE A 209      31.155  15.886  21.019  1.00 11.09           C  
ATOM   1552  O   ILE A 209      30.529  14.914  21.449  1.00 12.93           O  
ATOM   1553  CB  ILE A 209      32.164  16.862  23.114  1.00 13.02           C  
ATOM   1554  CG1 ILE A 209      32.462  18.185  23.836  1.00 14.05           C  
ATOM   1555  CG2 ILE A 209      33.470  16.148  22.716  1.00 11.16           C  
ATOM   1556  CD1 ILE A 209      33.389  18.066  25.022  1.00 12.15           C  
ATOM   1557  N   LEU A 210      31.672  15.945  19.799  1.00 11.55           N  
ATOM   1558  CA  LEU A 210      31.584  14.840  18.860  1.00 10.15           C  
ATOM   1559  C   LEU A 210      32.958  14.249  18.634  1.00 12.13           C  
ATOM   1560  O   LEU A 210      33.964  14.957  18.705  1.00 11.85           O  
ATOM   1561  CB  LEU A 210      31.068  15.342  17.508  1.00 11.77           C  
ATOM   1562  CG  LEU A 210      29.898  16.336  17.459  1.00 13.21           C  
ATOM   1563  CD1 LEU A 210      29.683  16.808  16.022  1.00 13.24           C  
ATOM   1564  CD2 LEU A 210      28.632  15.700  18.033  1.00 12.09           C  
ATOM   1565  N   THR A 211      32.997  12.940  18.419  1.00 13.28           N  
ATOM   1566  CA  THR A 211      34.239  12.245  18.106  1.00 13.86           C  
ATOM   1567  C   THR A 211      33.977  11.656  16.729  1.00 13.23           C  
ATOM   1568  O   THR A 211      33.000  10.927  16.525  1.00 14.47           O  
ATOM   1569  CB  THR A 211      34.595  11.156  19.132  1.00 15.29           C  
ATOM   1570  OG1 THR A 211      34.772  11.771  20.411  1.00 17.92           O  
ATOM   1571  CG2 THR A 211      35.906  10.466  18.750  1.00 12.36           C  
ATOM   1572  N   ILE A 212      34.788  12.071  15.767  1.00 12.88           N  
ATOM   1573  CA  ILE A 212      34.633  11.632  14.394  1.00 14.18           C  
ATOM   1574  C   ILE A 212      35.828  10.795  13.953  1.00 15.17           C  
ATOM   1575  O   ILE A 212      36.981  11.144  14.233  1.00 13.54           O  
ATOM   1576  CB  ILE A 212      34.508  12.855  13.441  1.00 13.55           C  
ATOM   1577  CG1 ILE A 212      33.552  13.895  14.037  1.00 13.07           C  
ATOM   1578  CG2 ILE A 212      34.014  12.409  12.066  1.00 12.40           C  
ATOM   1579  CD1 ILE A 212      33.735  15.294  13.493  1.00 12.54           C  
ATOM   1580  N   GLU A 213      35.545   9.678  13.292  1.00 17.10           N  
ATOM   1581  CA  GLU A 213      36.583   8.798  12.766  1.00 20.51           C  
ATOM   1582  C   GLU A 213      35.984   8.018  11.601  1.00 21.03           C  
ATOM   1583  O   GLU A 213      34.871   7.496  11.704  1.00 17.66           O  
ATOM   1584  CB  GLU A 213      37.103   7.842  13.840  1.00 22.95           C  
ATOM   1585  CG  GLU A 213      38.312   7.030  13.381  1.00 29.33           C  
ATOM   1586  CD  GLU A 213      38.865   6.108  14.456  1.00 33.55           C  
ATOM   1587  OE1 GLU A 213      38.112   5.746  15.388  1.00 35.61           O  
ATOM   1588  OE2 GLU A 213      40.057   5.739  14.362  1.00 36.96           O  
ATOM   1589  N   ASP A 214      36.706   7.981  10.483  1.00 23.42           N  
ATOM   1590  CA  ASP A 214      36.245   7.279   9.282  1.00 26.88           C  
ATOM   1591  C   ASP A 214      34.875   7.789   8.819  1.00 25.29           C  
ATOM   1592  O   ASP A 214      34.054   7.018   8.313  1.00 25.61           O  
ATOM   1593  CB  ASP A 214      36.186   5.762   9.530  1.00 33.29           C  
ATOM   1594  CG  ASP A 214      37.454   5.043   9.090  1.00 41.19           C  
ATOM   1595  OD1 ASP A 214      38.435   5.011   9.869  1.00 43.44           O  
ATOM   1596  OD2 ASP A 214      37.460   4.501   7.961  1.00 44.62           O  
ATOM   1597  N   GLY A 215      34.633   9.086   9.009  1.00 22.61           N  
ATOM   1598  CA  GLY A 215      33.367   9.680   8.612  1.00 20.64           C  
ATOM   1599  C   GLY A 215      32.202   9.333   9.525  1.00 18.41           C  
ATOM   1600  O   GLY A 215      31.063   9.701   9.248  1.00 19.04           O  
ATOM   1601  N   ILE A 216      32.486   8.626  10.612  1.00 18.04           N  
ATOM   1602  CA  ILE A 216      31.465   8.222  11.575  1.00 17.99           C  
ATOM   1603  C   ILE A 216      31.473   9.142  12.799  1.00 16.35           C  
ATOM   1604  O   ILE A 216      32.521   9.359  13.420  1.00 14.66           O  
ATOM   1605  CB  ILE A 216      31.692   6.767  12.037  1.00 19.03           C  
ATOM   1606  CG1 ILE A 216      31.650   5.826  10.829  1.00 19.86           C  
ATOM   1607  CG2 ILE A 216      30.647   6.369  13.071  1.00 20.04           C  
ATOM   1608  CD1 ILE A 216      31.919   4.375  11.171  1.00 25.36           C  
ATOM   1609  N   PHE A 217      30.298   9.659  13.147  1.00 15.26           N  
ATOM   1610  CA  PHE A 217      30.148  10.564  14.283  1.00 14.10           C  
ATOM   1611  C   PHE A 217      29.644   9.863  15.530  1.00 15.68           C  
ATOM   1612  O   PHE A 217      28.767   8.998  15.458  1.00 17.55           O  
ATOM   1613  CB  PHE A 217      29.153  11.683  13.961  1.00 13.73           C  
ATOM   1614  CG  PHE A 217      29.659  12.695  12.974  1.00 13.40           C  
ATOM   1615  CD1 PHE A 217      29.634  12.432  11.607  1.00 13.48           C  
ATOM   1616  CD2 PHE A 217      30.123  13.930  13.409  1.00 12.14           C  
ATOM   1617  CE1 PHE A 217      30.064  13.390  10.693  1.00 12.06           C  
ATOM   1618  CE2 PHE A 217      30.554  14.890  12.502  1.00 12.66           C  
ATOM   1619  CZ  PHE A 217      30.524  14.622  11.145  1.00 11.48           C  
ATOM   1620  N   GLU A 218      30.187  10.258  16.672  1.00 14.62           N  
ATOM   1621  CA  GLU A 218      29.755   9.730  17.955  1.00 15.74           C  
ATOM   1622  C   GLU A 218      29.552  10.945  18.843  1.00 15.30           C  
ATOM   1623  O   GLU A 218      30.441  11.793  18.939  1.00 14.86           O  
ATOM   1624  CB  GLU A 218      30.812   8.834  18.592  1.00 18.00           C  
ATOM   1625  CG  GLU A 218      30.399   8.338  19.983  1.00 26.35           C  
ATOM   1626  CD  GLU A 218      31.558   7.853  20.842  1.00 30.16           C  
ATOM   1627  OE1 GLU A 218      32.608   7.461  20.293  1.00 33.03           O  
ATOM   1628  OE2 GLU A 218      31.414   7.865  22.083  1.00 34.17           O  
ATOM   1629  N   VAL A 219      28.374  11.060  19.443  1.00 14.61           N  
ATOM   1630  CA  VAL A 219      28.085  12.175  20.336  1.00 15.20           C  
ATOM   1631  C   VAL A 219      28.608  11.771  21.712  1.00 15.38           C  
ATOM   1632  O   VAL A 219      28.013  10.929  22.385  1.00 15.90           O  
ATOM   1633  CB  VAL A 219      26.561  12.473  20.415  1.00 16.48           C  
ATOM   1634  CG1 VAL A 219      26.292  13.623  21.381  1.00 16.54           C  
ATOM   1635  CG2 VAL A 219      26.016  12.819  19.035  1.00 14.80           C  
ATOM   1636  N   LYS A 220      29.758  12.320  22.089  1.00 14.90           N  
ATOM   1637  CA  LYS A 220      30.370  12.017  23.376  1.00 17.04           C  
ATOM   1638  C   LYS A 220      29.614  12.602  24.561  1.00 17.16           C  
ATOM   1639  O   LYS A 220      29.454  11.940  25.592  1.00 15.79           O  
ATOM   1640  CB  LYS A 220      31.811  12.508  23.409  1.00 19.27           C  
ATOM   1641  CG  LYS A 220      32.786  11.560  22.771  1.00 24.64           C  
ATOM   1642  CD  LYS A 220      34.146  11.732  23.417  1.00 29.48           C  
ATOM   1643  CE  LYS A 220      34.703  10.398  23.878  1.00 32.93           C  
ATOM   1644  NZ  LYS A 220      35.249   9.624  22.739  1.00 33.96           N  
ATOM   1645  N   SER A 221      29.212  13.864  24.436  1.00 15.73           N  
ATOM   1646  CA  SER A 221      28.466  14.539  25.489  1.00 14.98           C  
ATOM   1647  C   SER A 221      27.710  15.744  24.952  1.00 13.23           C  
ATOM   1648  O   SER A 221      28.025  16.274  23.879  1.00 11.71           O  
ATOM   1649  CB  SER A 221      29.394  14.985  26.624  1.00 13.67           C  
ATOM   1650  OG  SER A 221      30.310  15.983  26.200  1.00 14.85           O  
ATOM   1651  N   THR A 222      26.690  16.146  25.701  1.00 13.63           N  
ATOM   1652  CA  THR A 222      25.870  17.299  25.363  1.00 13.92           C  
ATOM   1653  C   THR A 222      25.606  18.029  26.671  1.00 14.10           C  
ATOM   1654  O   THR A 222      25.485  17.397  27.726  1.00 15.14           O  
ATOM   1655  CB  THR A 222      24.503  16.904  24.712  1.00 14.68           C  
ATOM   1656  OG1 THR A 222      23.746  16.073  25.606  1.00 13.41           O  
ATOM   1657  CG2 THR A 222      24.720  16.165  23.390  1.00 13.97           C  
ATOM   1658  N   ALA A 223      25.541  19.350  26.608  1.00 11.70           N  
ATOM   1659  CA  ALA A 223      25.284  20.171  27.779  1.00 10.73           C  
ATOM   1660  C   ALA A 223      24.623  21.437  27.271  1.00 11.32           C  
ATOM   1661  O   ALA A 223      24.454  21.611  26.060  1.00 12.43           O  
ATOM   1662  CB  ALA A 223      26.589  20.500  28.490  1.00 12.69           C  
ATOM   1663  N   GLY A 224      24.225  22.313  28.182  1.00  9.53           N  
ATOM   1664  CA  GLY A 224      23.600  23.546  27.758  1.00 11.49           C  
ATOM   1665  C   GLY A 224      22.455  23.995  28.636  1.00 12.98           C  
ATOM   1666  O   GLY A 224      22.363  23.615  29.809  1.00 14.23           O  
ATOM   1667  N   ASP A 225      21.575  24.802  28.055  1.00 12.65           N  
ATOM   1668  CA  ASP A 225      20.429  25.350  28.759  1.00 11.44           C  
ATOM   1669  C   ASP A 225      19.348  25.557  27.707  1.00 10.41           C  
ATOM   1670  O   ASP A 225      19.510  26.365  26.795  1.00 10.06           O  
ATOM   1671  CB  ASP A 225      20.814  26.695  29.393  1.00 12.87           C  
ATOM   1672  CG  ASP A 225      19.785  27.200  30.393  1.00 15.24           C  
ATOM   1673  OD1 ASP A 225      18.579  26.939  30.225  1.00 12.76           O  
ATOM   1674  OD2 ASP A 225      20.192  27.874  31.362  1.00 18.06           O  
ATOM   1675  N   THR A 226      18.245  24.831  27.842  1.00 11.59           N  
ATOM   1676  CA  THR A 226      17.134  24.926  26.896  1.00 11.69           C  
ATOM   1677  C   THR A 226      16.383  26.242  27.032  1.00 11.87           C  
ATOM   1678  O   THR A 226      15.468  26.527  26.258  1.00 11.02           O  
ATOM   1679  CB  THR A 226      16.138  23.763  27.081  1.00 12.95           C  
ATOM   1680  OG1 THR A 226      15.632  23.769  28.423  1.00 13.95           O  
ATOM   1681  CG2 THR A 226      16.816  22.434  26.803  1.00 14.18           C  
ATOM   1682  N   HIS A 227      16.759  27.035  28.028  1.00  9.40           N  
ATOM   1683  CA  HIS A 227      16.112  28.319  28.246  1.00 12.80           C  
ATOM   1684  C   HIS A 227      17.103  29.485  28.356  1.00 12.42           C  
ATOM   1685  O   HIS A 227      16.981  30.348  29.228  1.00 14.06           O  
ATOM   1686  CB  HIS A 227      15.188  28.254  29.470  1.00 13.49           C  
ATOM   1687  CG  HIS A 227      14.010  27.351  29.286  1.00 14.53           C  
ATOM   1688  ND1 HIS A 227      12.855  27.743  28.638  1.00 15.59           N  
ATOM   1689  CD2 HIS A 227      13.806  26.060  29.657  1.00 13.34           C  
ATOM   1690  CE1 HIS A 227      12.002  26.739  28.617  1.00 10.33           C  
ATOM   1691  NE2 HIS A 227      12.547  25.711  29.226  1.00 14.78           N  
ATOM   1692  N   LEU A 228      18.105  29.480  27.485  1.00 11.59           N  
ATOM   1693  CA  LEU A 228      19.102  30.546  27.444  1.00 11.24           C  
ATOM   1694  C   LEU A 228      19.403  30.795  25.982  1.00  9.92           C  
ATOM   1695  O   LEU A 228      19.769  29.871  25.265  1.00 10.58           O  
ATOM   1696  CB  LEU A 228      20.408  30.162  28.157  1.00 13.10           C  
ATOM   1697  CG  LEU A 228      21.545  31.191  27.996  1.00 13.18           C  
ATOM   1698  CD1 LEU A 228      21.201  32.488  28.719  1.00 14.74           C  
ATOM   1699  CD2 LEU A 228      22.857  30.635  28.507  1.00 15.40           C  
ATOM   1700  N   GLY A 229      19.264  32.041  25.553  1.00  8.73           N  
ATOM   1701  CA  GLY A 229      19.535  32.373  24.170  1.00  9.64           C  
ATOM   1702  C   GLY A 229      19.456  33.866  23.987  1.00  9.91           C  
ATOM   1703  O   GLY A 229      19.297  34.603  24.967  1.00  9.89           O  
ATOM   1704  N   GLY A 230      19.516  34.302  22.730  1.00  9.30           N  
ATOM   1705  CA  GLY A 230      19.457  35.715  22.402  1.00  7.92           C  
ATOM   1706  C   GLY A 230      18.281  36.472  22.990  1.00  8.22           C  
ATOM   1707  O   GLY A 230      18.416  37.649  23.315  1.00  8.91           O  
ATOM   1708  N   GLU A 231      17.134  35.812  23.134  1.00  8.72           N  
ATOM   1709  CA  GLU A 231      15.950  36.459  23.703  1.00 13.74           C  
ATOM   1710  C   GLU A 231      16.242  37.006  25.088  1.00 12.33           C  
ATOM   1711  O   GLU A 231      15.760  38.074  25.466  1.00 13.37           O  
ATOM   1712  CB  GLU A 231      14.781  35.483  23.807  1.00 17.76           C  
ATOM   1713  CG  GLU A 231      14.175  35.094  22.490  1.00 27.28           C  
ATOM   1714  CD  GLU A 231      12.873  34.319  22.652  1.00 33.70           C  
ATOM   1715  OE1 GLU A 231      12.912  33.166  23.139  1.00 37.09           O  
ATOM   1716  OE2 GLU A 231      11.817  34.877  22.293  1.00 38.53           O  
ATOM   1717  N   ASP A 232      17.039  36.264  25.844  1.00 11.14           N  
ATOM   1718  CA  ASP A 232      17.388  36.673  27.192  1.00 12.30           C  
ATOM   1719  C   ASP A 232      18.215  37.949  27.186  1.00 10.84           C  
ATOM   1720  O   ASP A 232      18.084  38.781  28.087  1.00 11.91           O  
ATOM   1721  CB  ASP A 232      18.107  35.535  27.907  1.00 13.16           C  
ATOM   1722  CG  ASP A 232      17.248  34.294  28.001  1.00 15.77           C  
ATOM   1723  OD1 ASP A 232      16.301  34.300  28.806  1.00 20.08           O  
ATOM   1724  OD2 ASP A 232      17.480  33.332  27.247  1.00 14.73           O  
ATOM   1725  N   PHE A 233      19.030  38.130  26.153  1.00  8.52           N  
ATOM   1726  CA  PHE A 233      19.846  39.332  26.052  1.00  8.81           C  
ATOM   1727  C   PHE A 233      18.927  40.501  25.716  1.00  9.57           C  
ATOM   1728  O   PHE A 233      19.082  41.600  26.252  1.00 10.44           O  
ATOM   1729  CB  PHE A 233      20.951  39.164  25.000  1.00  7.32           C  
ATOM   1730  CG  PHE A 233      21.751  37.897  25.167  1.00 10.25           C  
ATOM   1731  CD1 PHE A 233      21.965  37.350  26.439  1.00  9.11           C  
ATOM   1732  CD2 PHE A 233      22.267  37.234  24.056  1.00  8.26           C  
ATOM   1733  CE1 PHE A 233      22.650  36.153  26.599  1.00  9.34           C  
ATOM   1734  CE2 PHE A 233      22.955  36.034  24.201  1.00  9.77           C  
ATOM   1735  CZ  PHE A 233      23.157  35.495  25.475  1.00 10.56           C  
ATOM   1736  N   ASP A 234      17.937  40.246  24.864  1.00 10.34           N  
ATOM   1737  CA  ASP A 234      16.966  41.271  24.484  1.00 10.14           C  
ATOM   1738  C   ASP A 234      16.209  41.692  25.736  1.00 10.17           C  
ATOM   1739  O   ASP A 234      15.947  42.873  25.933  1.00 11.22           O  
ATOM   1740  CB  ASP A 234      15.954  40.728  23.469  1.00 10.77           C  
ATOM   1741  CG  ASP A 234      16.600  40.235  22.190  1.00 11.21           C  
ATOM   1742  OD1 ASP A 234      17.767  40.574  21.920  1.00  9.30           O  
ATOM   1743  OD2 ASP A 234      15.915  39.507  21.445  1.00 11.41           O  
ATOM   1744  N   ASN A 235      15.853  40.717  26.575  1.00 11.00           N  
ATOM   1745  CA  ASN A 235      15.132  40.987  27.823  1.00 12.03           C  
ATOM   1746  C   ASN A 235      15.896  41.970  28.703  1.00 12.10           C  
ATOM   1747  O   ASN A 235      15.314  42.908  29.255  1.00  9.67           O  
ATOM   1748  CB  ASN A 235      14.924  39.702  28.630  1.00 15.23           C  
ATOM   1749  CG  ASN A 235      13.877  38.787  28.038  1.00 19.70           C  
ATOM   1750  OD1 ASN A 235      13.851  37.591  28.339  1.00 26.58           O  
ATOM   1751  ND2 ASN A 235      12.999  39.330  27.218  1.00 21.00           N  
ATOM   1752  N   ARG A 236      17.200  41.740  28.853  1.00 11.30           N  
ATOM   1753  CA  ARG A 236      18.035  42.613  29.674  1.00 12.27           C  
ATOM   1754  C   ARG A 236      18.023  44.041  29.132  1.00 12.12           C  
ATOM   1755  O   ARG A 236      17.953  45.012  29.898  1.00 11.14           O  
ATOM   1756  CB  ARG A 236      19.469  42.074  29.752  1.00  9.99           C  
ATOM   1757  CG  ARG A 236      19.604  40.770  30.530  1.00 11.50           C  
ATOM   1758  CD  ARG A 236      19.330  40.972  32.016  1.00 12.23           C  
ATOM   1759  NE  ARG A 236      19.460  39.729  32.781  1.00 11.12           N  
ATOM   1760  CZ  ARG A 236      20.612  39.248  33.254  1.00 14.07           C  
ATOM   1761  NH1 ARG A 236      21.760  39.891  33.045  1.00 12.10           N  
ATOM   1762  NH2 ARG A 236      20.628  38.112  33.942  1.00 13.54           N  
ATOM   1763  N   MET A 237      18.049  44.160  27.808  1.00  9.61           N  
ATOM   1764  CA  MET A 237      18.031  45.462  27.152  1.00 10.17           C  
ATOM   1765  C   MET A 237      16.676  46.140  27.343  1.00  9.05           C  
ATOM   1766  O   MET A 237      16.608  47.336  27.629  1.00  8.78           O  
ATOM   1767  CB  MET A 237      18.315  45.307  25.659  1.00 11.59           C  
ATOM   1768  CG  MET A 237      19.668  44.711  25.334  1.00 13.44           C  
ATOM   1769  SD  MET A 237      19.853  44.519  23.548  1.00 18.25           S  
ATOM   1770  CE  MET A 237      20.054  46.270  23.058  1.00 13.36           C  
ATOM   1771  N   VAL A 238      15.603  45.368  27.193  1.00 10.20           N  
ATOM   1772  CA  VAL A 238      14.253  45.896  27.354  1.00 10.00           C  
ATOM   1773  C   VAL A 238      14.070  46.502  28.748  1.00 10.12           C  
ATOM   1774  O   VAL A 238      13.647  47.651  28.877  1.00 11.75           O  
ATOM   1775  CB  VAL A 238      13.187  44.801  27.100  1.00  9.26           C  
ATOM   1776  CG1 VAL A 238      11.797  45.303  27.473  1.00 10.14           C  
ATOM   1777  CG2 VAL A 238      13.206  44.391  25.636  1.00  9.68           C  
ATOM   1778  N   ASN A 239      14.443  45.754  29.781  1.00  9.76           N  
ATOM   1779  CA  ASN A 239      14.319  46.239  31.154  1.00 11.57           C  
ATOM   1780  C   ASN A 239      15.130  47.512  31.364  1.00 11.33           C  
ATOM   1781  O   ASN A 239      14.666  48.467  31.993  1.00 11.83           O  
ATOM   1782  CB  ASN A 239      14.731  45.153  32.149  1.00 13.70           C  
ATOM   1783  CG  ASN A 239      13.751  43.989  32.179  1.00 12.41           C  
ATOM   1784  OD1 ASN A 239      14.126  42.855  32.467  1.00 17.42           O  
ATOM   1785  ND2 ASN A 239      12.489  44.269  31.894  1.00 14.48           N  
ATOM   1786  N   HIS A 240      16.320  47.539  30.778  1.00 10.79           N  
ATOM   1787  CA  HIS A 240      17.210  48.693  30.858  1.00 12.36           C  
ATOM   1788  C   HIS A 240      16.533  49.938  30.273  1.00 12.11           C  
ATOM   1789  O   HIS A 240      16.550  51.015  30.873  1.00  9.77           O  
ATOM   1790  CB  HIS A 240      18.509  48.375  30.099  1.00 13.39           C  
ATOM   1791  CG  HIS A 240      19.436  49.542  29.942  1.00 12.38           C  
ATOM   1792  ND1 HIS A 240      20.142  50.075  30.996  1.00 13.15           N  
ATOM   1793  CD2 HIS A 240      19.794  50.253  28.851  1.00 13.82           C  
ATOM   1794  CE1 HIS A 240      20.900  51.067  30.562  1.00 14.31           C  
ATOM   1795  NE2 HIS A 240      20.705  51.195  29.258  1.00 14.16           N  
ATOM   1796  N   PHE A 241      15.920  49.782  29.105  1.00 12.62           N  
ATOM   1797  CA  PHE A 241      15.260  50.903  28.454  1.00 12.52           C  
ATOM   1798  C   PHE A 241      13.924  51.281  29.069  1.00 11.22           C  
ATOM   1799  O   PHE A 241      13.525  52.444  29.006  1.00 11.81           O  
ATOM   1800  CB  PHE A 241      15.183  50.689  26.942  1.00 12.11           C  
ATOM   1801  CG  PHE A 241      16.510  50.866  26.257  1.00 13.00           C  
ATOM   1802  CD1 PHE A 241      17.233  52.047  26.417  1.00 14.90           C  
ATOM   1803  CD2 PHE A 241      17.066  49.844  25.501  1.00 13.34           C  
ATOM   1804  CE1 PHE A 241      18.486  52.204  25.838  1.00 15.34           C  
ATOM   1805  CE2 PHE A 241      18.321  49.995  24.919  1.00 15.79           C  
ATOM   1806  CZ  PHE A 241      19.030  51.178  25.089  1.00 15.55           C  
ATOM   1807  N   ILE A 242      13.241  50.322  29.684  1.00 11.43           N  
ATOM   1808  CA  ILE A 242      11.982  50.640  30.357  1.00 11.83           C  
ATOM   1809  C   ILE A 242      12.357  51.580  31.521  1.00 12.59           C  
ATOM   1810  O   ILE A 242      11.717  52.613  31.727  1.00 11.86           O  
ATOM   1811  CB  ILE A 242      11.269  49.369  30.889  1.00 12.39           C  
ATOM   1812  CG1 ILE A 242      10.670  48.585  29.718  1.00  9.86           C  
ATOM   1813  CG2 ILE A 242      10.176  49.747  31.907  1.00 13.56           C  
ATOM   1814  CD1 ILE A 242      10.041  47.263  30.106  1.00 11.58           C  
ATOM   1815  N   ALA A 243      13.444  51.251  32.224  1.00 13.42           N  
ATOM   1816  CA  ALA A 243      13.940  52.063  33.341  1.00 14.02           C  
ATOM   1817  C   ALA A 243      14.316  53.456  32.841  1.00 14.79           C  
ATOM   1818  O   ALA A 243      13.984  54.472  33.462  1.00 15.29           O  
ATOM   1819  CB  ALA A 243      15.156  51.392  33.978  1.00 12.24           C  
ATOM   1820  N   GLU A 244      14.997  53.495  31.702  1.00 13.82           N  
ATOM   1821  CA  GLU A 244      15.409  54.753  31.106  1.00 14.71           C  
ATOM   1822  C   GLU A 244      14.214  55.642  30.737  1.00 14.20           C  
ATOM   1823  O   GLU A 244      14.201  56.835  31.053  1.00 14.68           O  
ATOM   1824  CB  GLU A 244      16.260  54.490  29.872  1.00 13.72           C  
ATOM   1825  CG  GLU A 244      16.742  55.753  29.219  1.00 15.78           C  
ATOM   1826  CD  GLU A 244      17.644  55.491  28.050  1.00 17.02           C  
ATOM   1827  OE1 GLU A 244      18.547  54.633  28.169  1.00 17.23           O  
ATOM   1828  OE2 GLU A 244      17.451  56.150  27.011  1.00 18.80           O  
ATOM   1829  N   PHE A 245      13.222  55.062  30.065  1.00 13.56           N  
ATOM   1830  CA  PHE A 245      12.022  55.792  29.663  1.00 15.22           C  
ATOM   1831  C   PHE A 245      11.283  56.322  30.889  1.00 15.60           C  
ATOM   1832  O   PHE A 245      10.802  57.460  30.893  1.00 16.35           O  
ATOM   1833  CB  PHE A 245      11.089  54.890  28.846  1.00 17.20           C  
ATOM   1834  CG  PHE A 245       9.947  55.628  28.185  1.00 19.17           C  
ATOM   1835  CD1 PHE A 245       8.737  55.815  28.852  1.00 19.42           C  
ATOM   1836  CD2 PHE A 245      10.086  56.139  26.894  1.00 19.16           C  
ATOM   1837  CE1 PHE A 245       7.682  56.503  28.243  1.00 19.89           C  
ATOM   1838  CE2 PHE A 245       9.041  56.826  26.277  1.00 19.84           C  
ATOM   1839  CZ  PHE A 245       7.838  57.008  26.951  1.00 20.28           C  
ATOM   1840  N   LYS A 246      11.208  55.498  31.930  1.00 16.07           N  
ATOM   1841  CA  LYS A 246      10.534  55.878  33.167  1.00 18.98           C  
ATOM   1842  C   LYS A 246      11.238  57.067  33.804  1.00 18.81           C  
ATOM   1843  O   LYS A 246      10.599  57.994  34.297  1.00 19.90           O  
ATOM   1844  CB  LYS A 246      10.522  54.709  34.152  1.00 19.91           C  
ATOM   1845  CG  LYS A 246       9.634  54.941  35.359  1.00 24.39           C  
ATOM   1846  CD  LYS A 246       9.890  53.908  36.443  1.00 28.07           C  
ATOM   1847  CE  LYS A 246       8.863  54.022  37.558  1.00 32.09           C  
ATOM   1848  NZ  LYS A 246       8.698  55.428  38.026  1.00 32.91           N  
ATOM   1849  N   ARG A 247      12.562  57.043  33.761  1.00 17.93           N  
ATOM   1850  CA  ARG A 247      13.376  58.101  34.332  1.00 21.66           C  
ATOM   1851  C   ARG A 247      13.190  59.423  33.581  1.00 22.33           C  
ATOM   1852  O   ARG A 247      12.980  60.472  34.192  1.00 22.16           O  
ATOM   1853  CB  ARG A 247      14.837  57.665  34.288  1.00 22.66           C  
ATOM   1854  CG  ARG A 247      15.645  58.031  35.502  1.00 27.04           C  
ATOM   1855  CD  ARG A 247      16.942  57.248  35.501  1.00 28.88           C  
ATOM   1856  NE  ARG A 247      17.606  57.332  34.200  1.00 30.81           N  
ATOM   1857  CZ  ARG A 247      17.972  56.273  33.478  1.00 30.54           C  
ATOM   1858  NH1 ARG A 247      17.745  55.040  33.923  1.00 25.00           N  
ATOM   1859  NH2 ARG A 247      18.574  56.447  32.309  1.00 30.36           N  
ATOM   1860  N   LYS A 248      13.206  59.349  32.254  1.00 22.83           N  
ATOM   1861  CA  LYS A 248      13.067  60.521  31.399  1.00 25.55           C  
ATOM   1862  C   LYS A 248      11.646  61.052  31.215  1.00 26.69           C  
ATOM   1863  O   LYS A 248      11.459  62.224  30.884  1.00 29.69           O  
ATOM   1864  CB  LYS A 248      13.698  60.236  30.022  1.00 25.73           C  
ATOM   1865  N   HIS A 249      10.641  60.203  31.399  1.00 27.00           N  
ATOM   1866  CA  HIS A 249       9.263  60.641  31.188  1.00 27.46           C  
ATOM   1867  C   HIS A 249       8.312  60.401  32.342  1.00 27.29           C  
ATOM   1868  O   HIS A 249       7.121  60.707  32.236  1.00 27.69           O  
ATOM   1869  CB  HIS A 249       8.703  59.978  29.931  1.00 28.44           C  
ATOM   1870  CG  HIS A 249       9.511  60.249  28.703  1.00 29.06           C  
ATOM   1871  ND1 HIS A 249       9.637  61.510  28.162  1.00 30.47           N  
ATOM   1872  CD2 HIS A 249      10.263  59.431  27.932  1.00 29.70           C  
ATOM   1873  CE1 HIS A 249      10.432  61.455  27.108  1.00 30.60           C  
ATOM   1874  NE2 HIS A 249      10.824  60.207  26.949  1.00 30.94           N  
ATOM   1875  N   LYS A 250       8.830  59.845  33.433  1.00 26.00           N  
ATOM   1876  CA  LYS A 250       8.023  59.547  34.608  1.00 26.04           C  
ATOM   1877  C   LYS A 250       6.795  58.703  34.244  1.00 24.66           C  
ATOM   1878  O   LYS A 250       5.720  58.868  34.826  1.00 25.12           O  
ATOM   1879  CB  LYS A 250       7.611  60.846  35.307  1.00 28.01           C  
ATOM   1880  N   LYS A 251       6.975  57.798  33.282  1.00 22.80           N  
ATOM   1881  CA  LYS A 251       5.915  56.907  32.820  1.00 21.67           C  
ATOM   1882  C   LYS A 251       6.458  55.501  32.649  1.00 20.31           C  
ATOM   1883  O   LYS A 251       7.529  55.314  32.078  1.00 21.21           O  
ATOM   1884  CB  LYS A 251       5.345  57.382  31.480  1.00 23.82           C  
ATOM   1885  CG  LYS A 251       4.526  58.654  31.567  1.00 27.65           C  
ATOM   1886  CD  LYS A 251       3.965  59.054  30.221  1.00 30.73           C  
ATOM   1887  CE  LYS A 251       3.243  60.389  30.313  1.00 34.33           C  
ATOM   1888  NZ  LYS A 251       2.073  60.339  31.241  1.00 37.68           N  
ATOM   1889  N   ASP A 252       5.711  54.520  33.135  1.00 19.00           N  
ATOM   1890  CA  ASP A 252       6.097  53.120  33.034  1.00 19.63           C  
ATOM   1891  C   ASP A 252       5.290  52.452  31.920  1.00 18.83           C  
ATOM   1892  O   ASP A 252       4.066  52.377  31.999  1.00 19.33           O  
ATOM   1893  CB  ASP A 252       5.832  52.409  34.364  1.00 23.10           C  
ATOM   1894  CG  ASP A 252       6.599  51.104  34.496  1.00 25.28           C  
ATOM   1895  OD1 ASP A 252       6.637  50.332  33.528  1.00 24.43           O  
ATOM   1896  OD2 ASP A 252       7.185  50.854  35.569  1.00 31.77           O  
ATOM   1897  N   ILE A 253       5.982  51.938  30.906  1.00 17.80           N  
ATOM   1898  CA  ILE A 253       5.336  51.282  29.770  1.00 16.37           C  
ATOM   1899  C   ILE A 253       5.159  49.773  29.947  1.00 17.42           C  
ATOM   1900  O   ILE A 253       4.533  49.123  29.108  1.00 18.80           O  
ATOM   1901  CB  ILE A 253       6.143  51.494  28.454  1.00 16.12           C  
ATOM   1902  CG1 ILE A 253       7.418  50.632  28.462  1.00 16.11           C  
ATOM   1903  CG2 ILE A 253       6.509  52.965  28.287  1.00 13.06           C  
ATOM   1904  CD1 ILE A 253       8.186  50.617  27.135  1.00 14.24           C  
ATOM   1905  N   SER A 254       5.712  49.223  31.026  1.00 16.60           N  
ATOM   1906  CA  SER A 254       5.677  47.784  31.297  1.00 17.86           C  
ATOM   1907  C   SER A 254       4.374  47.033  31.076  1.00 19.12           C  
ATOM   1908  O   SER A 254       4.389  45.869  30.671  1.00 19.59           O  
ATOM   1909  CB  SER A 254       6.171  47.499  32.718  1.00 18.43           C  
ATOM   1910  OG  SER A 254       7.512  47.922  32.883  1.00 25.22           O  
ATOM   1911  N   GLU A 255       3.253  47.674  31.373  1.00 20.64           N  
ATOM   1912  CA  GLU A 255       1.970  47.009  31.219  1.00 22.69           C  
ATOM   1913  C   GLU A 255       1.359  47.095  29.830  1.00 22.94           C  
ATOM   1914  O   GLU A 255       0.400  46.385  29.534  1.00 24.54           O  
ATOM   1915  CB  GLU A 255       0.988  47.485  32.287  1.00 24.04           C  
ATOM   1916  CG  GLU A 255       1.399  47.094  33.703  1.00 26.50           C  
ATOM   1917  CD  GLU A 255       1.612  45.596  33.860  1.00 29.72           C  
ATOM   1918  OE1 GLU A 255       0.702  44.814  33.511  1.00 33.28           O  
ATOM   1919  OE2 GLU A 255       2.695  45.198  34.331  1.00 32.57           O  
ATOM   1920  N   ASN A 256       1.924  47.943  28.975  1.00 23.67           N  
ATOM   1921  CA  ASN A 256       1.437  48.090  27.608  1.00 23.69           C  
ATOM   1922  C   ASN A 256       2.179  47.073  26.752  1.00 25.12           C  
ATOM   1923  O   ASN A 256       3.311  47.316  26.322  1.00 25.32           O  
ATOM   1924  CB  ASN A 256       1.686  49.508  27.093  1.00 23.97           C  
ATOM   1925  CG  ASN A 256       1.068  49.747  25.731  1.00 26.26           C  
ATOM   1926  OD1 ASN A 256       1.314  49.004  24.781  1.00 26.29           O  
ATOM   1927  ND2 ASN A 256       0.250  50.780  25.631  1.00 26.75           N  
ATOM   1928  N   LYS A 257       1.537  45.935  26.514  1.00 25.73           N  
ATOM   1929  CA  LYS A 257       2.124  44.846  25.736  1.00 27.47           C  
ATOM   1930  C   LYS A 257       2.750  45.262  24.410  1.00 27.59           C  
ATOM   1931  O   LYS A 257       3.864  44.831  24.092  1.00 27.43           O  
ATOM   1932  CB  LYS A 257       1.099  43.739  25.508  1.00 28.28           C  
ATOM   1933  CG  LYS A 257       0.759  42.974  26.771  1.00 30.40           C  
ATOM   1934  CD  LYS A 257      -0.229  41.856  26.490  1.00 32.76           C  
ATOM   1935  CE  LYS A 257      -0.369  40.926  27.688  1.00 35.30           C  
ATOM   1936  NZ  LYS A 257      -1.070  41.531  28.860  1.00 36.29           N  
ATOM   1937  N   ARG A 258       2.042  46.085  23.640  1.00 28.69           N  
ATOM   1938  CA  ARG A 258       2.537  46.553  22.353  1.00 28.68           C  
ATOM   1939  C   ARG A 258       3.837  47.325  22.499  1.00 28.54           C  
ATOM   1940  O   ARG A 258       4.836  46.998  21.852  1.00 30.09           O  
ATOM   1941  CB  ARG A 258       1.503  47.445  21.667  1.00 29.05           C  
ATOM   1942  CG  ARG A 258       2.015  48.043  20.365  1.00 29.48           C  
ATOM   1943  CD  ARG A 258       1.002  48.978  19.741  1.00 31.95           C  
ATOM   1944  NE  ARG A 258       1.576  49.755  18.650  1.00 30.29           N  
ATOM   1945  CZ  ARG A 258       1.708  49.296  17.402  1.00 30.33           C  
ATOM   1946  NH1 ARG A 258       1.332  48.043  17.074  1.00 31.88           N  
ATOM   1947  NH2 ARG A 258       2.154  50.107  16.443  1.00 31.54           N  
ATOM   1948  N   ALA A 259       3.801  48.351  23.345  1.00 24.38           N  
ATOM   1949  CA  ALA A 259       4.948  49.209  23.599  1.00 20.99           C  
ATOM   1950  C   ALA A 259       6.175  48.376  23.955  1.00 19.71           C  
ATOM   1951  O   ALA A 259       7.274  48.633  23.455  1.00 19.42           O  
ATOM   1952  CB  ALA A 259       4.628  50.194  24.722  1.00 19.42           C  
ATOM   1953  N   VAL A 260       5.974  47.367  24.800  1.00 17.41           N  
ATOM   1954  CA  VAL A 260       7.056  46.484  25.221  1.00 17.62           C  
ATOM   1955  C   VAL A 260       7.598  45.675  24.040  1.00 19.48           C  
ATOM   1956  O   VAL A 260       8.813  45.603  23.843  1.00 17.51           O  
ATOM   1957  CB  VAL A 260       6.603  45.544  26.367  1.00 15.33           C  
ATOM   1958  CG1 VAL A 260       7.669  44.503  26.665  1.00 15.16           C  
ATOM   1959  CG2 VAL A 260       6.313  46.362  27.628  1.00 13.66           C  
ATOM   1960  N   ARG A 261       6.703  45.106  23.235  1.00 20.75           N  
ATOM   1961  CA  ARG A 261       7.129  44.319  22.079  1.00 22.47           C  
ATOM   1962  C   ARG A 261       7.863  45.183  21.058  1.00 21.14           C  
ATOM   1963  O   ARG A 261       8.842  44.740  20.463  1.00 24.36           O  
ATOM   1964  CB  ARG A 261       5.949  43.590  21.425  1.00 24.96           C  
ATOM   1965  CG  ARG A 261       6.379  42.408  20.541  1.00 27.72           C  
ATOM   1966  CD  ARG A 261       7.120  41.353  21.355  1.00 31.29           C  
ATOM   1967  NE  ARG A 261       7.624  40.233  20.560  1.00 36.77           N  
ATOM   1968  CZ  ARG A 261       8.775  40.237  19.885  1.00 39.16           C  
ATOM   1969  NH1 ARG A 261       9.563  41.311  19.885  1.00 38.47           N  
ATOM   1970  NH2 ARG A 261       9.167  39.144  19.236  1.00 39.68           N  
ATOM   1971  N   ARG A 262       7.416  46.424  20.885  1.00 19.68           N  
ATOM   1972  CA  ARG A 262       8.058  47.346  19.952  1.00 19.46           C  
ATOM   1973  C   ARG A 262       9.472  47.676  20.437  1.00 19.26           C  
ATOM   1974  O   ARG A 262      10.406  47.775  19.635  1.00 17.95           O  
ATOM   1975  CB  ARG A 262       7.231  48.628  19.781  1.00 22.64           C  
ATOM   1976  CG  ARG A 262       5.857  48.380  19.154  1.00 24.33           C  
ATOM   1977  CD  ARG A 262       5.541  49.384  18.051  1.00 23.44           C  
ATOM   1978  NE  ARG A 262       5.342  50.732  18.573  1.00 25.47           N  
ATOM   1979  CZ  ARG A 262       5.772  51.839  17.973  1.00 26.84           C  
ATOM   1980  NH1 ARG A 262       6.429  51.772  16.826  1.00 25.97           N  
ATOM   1981  NH2 ARG A 262       5.562  53.022  18.530  1.00 28.92           N  
ATOM   1982  N   LEU A 263       9.622  47.846  21.750  1.00 17.08           N  
ATOM   1983  CA  LEU A 263      10.924  48.129  22.350  1.00 15.62           C  
ATOM   1984  C   LEU A 263      11.815  46.896  22.187  1.00 14.49           C  
ATOM   1985  O   LEU A 263      12.987  47.011  21.834  1.00 14.02           O  
ATOM   1986  CB  LEU A 263      10.770  48.485  23.835  1.00 13.28           C  
ATOM   1987  CG  LEU A 263      12.045  48.720  24.658  1.00 11.48           C  
ATOM   1988  CD1 LEU A 263      12.942  49.750  23.998  1.00  9.19           C  
ATOM   1989  CD2 LEU A 263      11.682  49.151  26.070  1.00  9.18           C  
ATOM   1990  N   ARG A 264      11.235  45.718  22.400  1.00 13.64           N  
ATOM   1991  CA  ARG A 264      11.952  44.451  22.275  1.00 16.13           C  
ATOM   1992  C   ARG A 264      12.520  44.250  20.866  1.00 15.97           C  
ATOM   1993  O   ARG A 264      13.683  43.866  20.700  1.00 13.61           O  
ATOM   1994  CB  ARG A 264      11.026  43.296  22.634  1.00 15.98           C  
ATOM   1995  CG  ARG A 264      11.633  41.931  22.422  1.00 21.96           C  
ATOM   1996  CD  ARG A 264      10.660  40.847  22.849  1.00 28.30           C  
ATOM   1997  NE  ARG A 264      10.350  40.945  24.270  1.00 33.85           N  
ATOM   1998  CZ  ARG A 264      11.245  40.738  25.231  1.00 38.87           C  
ATOM   1999  NH1 ARG A 264      12.495  40.402  24.915  1.00 38.92           N  
ATOM   2000  NH2 ARG A 264      10.892  40.850  26.505  1.00 38.55           N  
ATOM   2001  N   THR A 265      11.693  44.511  19.860  1.00 15.63           N  
ATOM   2002  CA  THR A 265      12.104  44.385  18.469  1.00 15.39           C  
ATOM   2003  C   THR A 265      13.250  45.360  18.206  1.00 12.62           C  
ATOM   2004  O   THR A 265      14.259  45.002  17.597  1.00 12.78           O  
ATOM   2005  CB  THR A 265      10.921  44.687  17.519  1.00 16.96           C  
ATOM   2006  OG1 THR A 265       9.902  43.695  17.703  1.00 18.03           O  
ATOM   2007  CG2 THR A 265      11.376  44.691  16.067  1.00 17.54           C  
ATOM   2008  N   ALA A 266      13.112  46.579  18.718  1.00 12.16           N  
ATOM   2009  CA  ALA A 266      14.140  47.595  18.551  1.00 12.88           C  
ATOM   2010  C   ALA A 266      15.425  47.135  19.238  1.00 12.94           C  
ATOM   2011  O   ALA A 266      16.515  47.322  18.704  1.00 12.63           O  
ATOM   2012  CB  ALA A 266      13.672  48.931  19.128  1.00 12.93           C  
ATOM   2013  N   CYS A 267      15.294  46.518  20.409  1.00 11.52           N  
ATOM   2014  CA  CYS A 267      16.458  46.033  21.149  1.00 12.73           C  
ATOM   2015  C   CYS A 267      17.193  44.921  20.416  1.00 12.15           C  
ATOM   2016  O   CYS A 267      18.413  44.963  20.270  1.00 11.37           O  
ATOM   2017  CB  CYS A 267      16.058  45.566  22.550  1.00 11.28           C  
ATOM   2018  SG  CYS A 267      15.734  46.941  23.665  1.00 11.67           S  
ATOM   2019  N   GLU A 268      16.438  43.952  19.914  1.00 11.54           N  
ATOM   2020  CA  GLU A 268      17.004  42.826  19.187  1.00  9.56           C  
ATOM   2021  C   GLU A 268      17.793  43.346  17.982  1.00 10.39           C  
ATOM   2022  O   GLU A 268      18.879  42.852  17.679  1.00  8.97           O  
ATOM   2023  CB  GLU A 268      15.871  41.894  18.755  1.00 11.83           C  
ATOM   2024  CG  GLU A 268      16.305  40.539  18.230  1.00 13.34           C  
ATOM   2025  CD  GLU A 268      16.755  40.559  16.783  1.00 15.46           C  
ATOM   2026  OE1 GLU A 268      16.455  41.523  16.040  1.00 14.75           O  
ATOM   2027  OE2 GLU A 268      17.406  39.582  16.380  1.00 14.80           O  
ATOM   2028  N   ARG A 269      17.243  44.347  17.301  1.00 11.62           N  
ATOM   2029  CA  ARG A 269      17.903  44.943  16.146  1.00 12.85           C  
ATOM   2030  C   ARG A 269      19.167  45.693  16.548  1.00 10.78           C  
ATOM   2031  O   ARG A 269      20.197  45.588  15.877  1.00 11.26           O  
ATOM   2032  CB  ARG A 269      16.954  45.888  15.425  1.00 16.95           C  
ATOM   2033  CG  ARG A 269      15.845  45.197  14.633  1.00 27.30           C  
ATOM   2034  CD  ARG A 269      15.096  46.223  13.807  1.00 35.44           C  
ATOM   2035  NE  ARG A 269      16.037  47.071  13.047  1.00 43.71           N  
ATOM   2036  CZ  ARG A 269      16.402  48.304  13.405  1.00 46.77           C  
ATOM   2037  NH1 ARG A 269      15.907  48.859  14.508  1.00 47.65           N  
ATOM   2038  NH2 ARG A 269      17.307  48.955  12.699  1.00 50.50           N  
ATOM   2039  N   ALA A 270      19.086  46.446  17.639  1.00  9.40           N  
ATOM   2040  CA  ALA A 270      20.240  47.185  18.137  1.00  9.49           C  
ATOM   2041  C   ALA A 270      21.331  46.187  18.508  1.00  8.92           C  
ATOM   2042  O   ALA A 270      22.514  46.412  18.237  1.00  9.20           O  
ATOM   2043  CB  ALA A 270      19.852  48.014  19.340  1.00 10.00           C  
ATOM   2044  N   LYS A 271      20.916  45.065  19.089  1.00  7.96           N  
ATOM   2045  CA  LYS A 271      21.825  43.994  19.489  1.00  7.59           C  
ATOM   2046  C   LYS A 271      22.647  43.491  18.297  1.00  8.34           C  
ATOM   2047  O   LYS A 271      23.868  43.351  18.386  1.00  8.18           O  
ATOM   2048  CB  LYS A 271      21.034  42.833  20.087  1.00  7.69           C  
ATOM   2049  CG  LYS A 271      21.890  41.673  20.561  1.00  6.96           C  
ATOM   2050  CD  LYS A 271      21.044  40.504  21.027  1.00  7.38           C  
ATOM   2051  CE  LYS A 271      20.221  39.918  19.887  1.00  6.08           C  
ATOM   2052  NZ  LYS A 271      19.351  38.792  20.349  1.00  5.98           N  
ATOM   2053  N   ARG A 272      21.978  43.206  17.185  1.00  8.80           N  
ATOM   2054  CA  ARG A 272      22.677  42.731  15.998  1.00  9.40           C  
ATOM   2055  C   ARG A 272      23.712  43.753  15.547  1.00  9.68           C  
ATOM   2056  O   ARG A 272      24.862  43.403  15.263  1.00 10.60           O  
ATOM   2057  CB  ARG A 272      21.694  42.437  14.874  1.00  8.12           C  
ATOM   2058  CG  ARG A 272      20.760  41.299  15.173  1.00  9.91           C  
ATOM   2059  CD  ARG A 272      20.110  40.814  13.898  1.00 11.60           C  
ATOM   2060  NE  ARG A 272      19.019  39.891  14.186  1.00 13.71           N  
ATOM   2061  CZ  ARG A 272      18.794  38.753  13.533  1.00 13.70           C  
ATOM   2062  NH1 ARG A 272      19.585  38.384  12.535  1.00 14.27           N  
ATOM   2063  NH2 ARG A 272      17.772  37.979  13.883  1.00 12.53           N  
ATOM   2064  N   THR A 273      23.321  45.021  15.529  1.00  7.94           N  
ATOM   2065  CA  THR A 273      24.226  46.093  15.138  1.00 10.44           C  
ATOM   2066  C   THR A 273      25.470  46.139  16.038  1.00 10.33           C  
ATOM   2067  O   THR A 273      26.585  46.334  15.554  1.00  9.80           O  
ATOM   2068  CB  THR A 273      23.496  47.450  15.159  1.00 10.80           C  
ATOM   2069  OG1 THR A 273      22.461  47.434  14.171  1.00 11.29           O  
ATOM   2070  CG2 THR A 273      24.460  48.597  14.863  1.00 13.15           C  
ATOM   2071  N   LEU A 274      25.280  45.883  17.329  1.00  8.85           N  
ATOM   2072  CA  LEU A 274      26.380  45.901  18.283  1.00  9.33           C  
ATOM   2073  C   LEU A 274      27.423  44.810  18.052  1.00  9.33           C  
ATOM   2074  O   LEU A 274      28.492  44.846  18.648  1.00 10.66           O  
ATOM   2075  CB  LEU A 274      25.851  45.844  19.720  1.00  8.65           C  
ATOM   2076  CG  LEU A 274      25.144  47.117  20.183  1.00  7.58           C  
ATOM   2077  CD1 LEU A 274      24.546  46.908  21.555  1.00  7.88           C  
ATOM   2078  CD2 LEU A 274      26.117  48.285  20.187  1.00  8.86           C  
ATOM   2079  N   SER A 275      27.106  43.828  17.213  1.00  8.91           N  
ATOM   2080  CA  SER A 275      28.056  42.765  16.911  1.00  9.42           C  
ATOM   2081  C   SER A 275      29.073  43.250  15.884  1.00 11.40           C  
ATOM   2082  O   SER A 275      30.141  42.653  15.726  1.00  9.94           O  
ATOM   2083  CB  SER A 275      27.336  41.525  16.372  1.00 10.64           C  
ATOM   2084  OG  SER A 275      26.621  40.860  17.401  1.00 11.54           O  
ATOM   2085  N   SER A 276      28.727  44.332  15.191  1.00 13.17           N  
ATOM   2086  CA  SER A 276      29.576  44.913  14.156  1.00 16.45           C  
ATOM   2087  C   SER A 276      30.085  46.302  14.529  1.00 16.74           C  
ATOM   2088  O   SER A 276      31.153  46.724  14.080  1.00 19.95           O  
ATOM   2089  CB  SER A 276      28.800  45.019  12.836  1.00 16.36           C  
ATOM   2090  OG  SER A 276      28.440  43.743  12.342  1.00 23.15           O  
ATOM   2091  N   SER A 277      29.290  47.028  15.302  1.00 15.98           N  
ATOM   2092  CA  SER A 277      29.643  48.374  15.709  1.00 15.65           C  
ATOM   2093  C   SER A 277      29.687  48.426  17.222  1.00 14.20           C  
ATOM   2094  O   SER A 277      29.153  47.542  17.887  1.00 13.14           O  
ATOM   2095  CB  SER A 277      28.593  49.355  15.189  1.00 18.11           C  
ATOM   2096  OG  SER A 277      28.345  49.153  13.805  1.00 25.28           O  
ATOM   2097  N   THR A 278      30.284  49.483  17.760  1.00 14.34           N  
ATOM   2098  CA  THR A 278      30.401  49.643  19.204  1.00 15.60           C  
ATOM   2099  C   THR A 278      29.270  50.469  19.813  1.00 16.12           C  
ATOM   2100  O   THR A 278      29.274  50.735  21.015  1.00 16.34           O  
ATOM   2101  CB  THR A 278      31.761  50.265  19.588  1.00 17.14           C  
ATOM   2102  OG1 THR A 278      31.986  51.446  18.807  1.00 17.66           O  
ATOM   2103  CG2 THR A 278      32.898  49.276  19.332  1.00 17.99           C  
ATOM   2104  N   GLN A 279      28.326  50.900  18.980  1.00 18.26           N  
ATOM   2105  CA  GLN A 279      27.181  51.682  19.440  1.00 18.61           C  
ATOM   2106  C   GLN A 279      26.017  51.472  18.479  1.00 16.91           C  
ATOM   2107  O   GLN A 279      26.224  51.163  17.302  1.00 14.57           O  
ATOM   2108  CB  GLN A 279      27.531  53.174  19.544  1.00 22.44           C  
ATOM   2109  CG  GLN A 279      26.401  54.020  20.131  1.00 33.43           C  
ATOM   2110  CD  GLN A 279      26.873  55.142  21.055  1.00 39.97           C  
ATOM   2111  OE1 GLN A 279      26.057  55.915  21.566  1.00 41.74           O  
ATOM   2112  NE2 GLN A 279      28.181  55.217  21.299  1.00 44.00           N  
ATOM   2113  N   ALA A 280      24.797  51.616  18.987  1.00 15.31           N  
ATOM   2114  CA  ALA A 280      23.596  51.438  18.180  1.00 15.03           C  
ATOM   2115  C   ALA A 280      22.545  52.442  18.615  1.00 15.95           C  
ATOM   2116  O   ALA A 280      22.445  52.770  19.794  1.00 14.30           O  
ATOM   2117  CB  ALA A 280      23.060  50.012  18.333  1.00 14.65           C  
ATOM   2118  N   SER A 281      21.779  52.946  17.656  1.00 18.62           N  
ATOM   2119  CA  SER A 281      20.733  53.912  17.946  1.00 22.27           C  
ATOM   2120  C   SER A 281      19.362  53.256  17.908  1.00 22.16           C  
ATOM   2121  O   SER A 281      19.074  52.453  17.023  1.00 23.78           O  
ATOM   2122  CB  SER A 281      20.773  55.059  16.936  1.00 23.09           C  
ATOM   2123  OG  SER A 281      22.027  55.720  16.968  1.00 31.52           O  
ATOM   2124  N   ILE A 282      18.539  53.572  18.900  1.00 22.58           N  
ATOM   2125  CA  ILE A 282      17.178  53.056  18.987  1.00 22.44           C  
ATOM   2126  C   ILE A 282      16.274  54.276  18.819  1.00 22.23           C  
ATOM   2127  O   ILE A 282      16.419  55.262  19.536  1.00 21.96           O  
ATOM   2128  CB  ILE A 282      16.927  52.354  20.350  1.00 23.43           C  
ATOM   2129  CG1 ILE A 282      17.583  50.970  20.339  1.00 22.22           C  
ATOM   2130  CG2 ILE A 282      15.434  52.261  20.657  1.00 21.62           C  
ATOM   2131  CD1 ILE A 282      17.370  50.183  21.597  1.00 24.83           C  
ATOM   2132  N   GLU A 283      15.410  54.247  17.813  1.00 22.41           N  
ATOM   2133  CA  GLU A 283      14.515  55.369  17.564  1.00 23.81           C  
ATOM   2134  C   GLU A 283      13.114  54.854  17.314  1.00 23.42           C  
ATOM   2135  O   GLU A 283      12.812  54.312  16.250  1.00 24.55           O  
ATOM   2136  CB  GLU A 283      15.008  56.197  16.376  1.00 27.01           C  
ATOM   2137  CG  GLU A 283      16.431  56.713  16.548  1.00 32.64           C  
ATOM   2138  CD  GLU A 283      16.834  57.731  15.498  1.00 37.01           C  
ATOM   2139  OE1 GLU A 283      16.276  57.697  14.379  1.00 39.77           O  
ATOM   2140  OE2 GLU A 283      17.709  58.573  15.800  1.00 39.21           O  
ATOM   2141  N   ILE A 284      12.259  55.023  18.312  1.00 20.73           N  
ATOM   2142  CA  ILE A 284      10.889  54.555  18.230  1.00 20.36           C  
ATOM   2143  C   ILE A 284       9.921  55.737  18.243  1.00 21.25           C  
ATOM   2144  O   ILE A 284       9.962  56.574  19.141  1.00 21.12           O  
ATOM   2145  CB  ILE A 284      10.575  53.597  19.408  1.00 16.95           C  
ATOM   2146  CG1 ILE A 284      11.700  52.566  19.563  1.00 16.19           C  
ATOM   2147  CG2 ILE A 284       9.279  52.856  19.151  1.00 16.89           C  
ATOM   2148  CD1 ILE A 284      11.511  51.614  20.715  1.00 14.45           C  
ATOM   2149  N   ASP A 285       9.082  55.829  17.218  1.00 22.95           N  
ATOM   2150  CA  ASP A 285       8.104  56.907  17.129  1.00 22.83           C  
ATOM   2151  C   ASP A 285       6.901  56.555  17.978  1.00 21.33           C  
ATOM   2152  O   ASP A 285       6.377  55.450  17.872  1.00 19.78           O  
ATOM   2153  CB  ASP A 285       7.645  57.119  15.683  1.00 23.09           C  
ATOM   2154  CG  ASP A 285       8.734  57.689  14.793  1.00 23.48           C  
ATOM   2155  OD1 ASP A 285       9.765  58.164  15.314  1.00 24.29           O  
ATOM   2156  OD2 ASP A 285       8.548  57.667  13.562  1.00 23.64           O  
ATOM   2157  N   SER A 286       6.508  57.487  18.843  1.00 22.09           N  
ATOM   2158  CA  SER A 286       5.356  57.329  19.725  1.00 22.57           C  
ATOM   2159  C   SER A 286       5.272  55.951  20.381  1.00 22.22           C  
ATOM   2160  O   SER A 286       4.314  55.201  20.174  1.00 22.55           O  
ATOM   2161  CB  SER A 286       4.064  57.657  18.966  1.00 25.02           C  
ATOM   2162  OG  SER A 286       4.070  59.007  18.512  1.00 27.64           O  
ATOM   2163  N   LEU A 287       6.279  55.641  21.189  1.00 21.63           N  
ATOM   2164  CA  LEU A 287       6.351  54.361  21.886  1.00 19.55           C  
ATOM   2165  C   LEU A 287       5.234  54.198  22.915  1.00 19.12           C  
ATOM   2166  O   LEU A 287       4.679  53.110  23.081  1.00 17.17           O  
ATOM   2167  CB  LEU A 287       7.705  54.232  22.591  1.00 19.19           C  
ATOM   2168  CG  LEU A 287       7.917  53.013  23.499  1.00 19.72           C  
ATOM   2169  CD1 LEU A 287       7.862  51.711  22.701  1.00 17.85           C  
ATOM   2170  CD2 LEU A 287       9.257  53.153  24.212  1.00 19.13           C  
ATOM   2171  N   TYR A 288       4.914  55.283  23.609  1.00 19.89           N  
ATOM   2172  CA  TYR A 288       3.892  55.238  24.642  1.00 20.49           C  
ATOM   2173  C   TYR A 288       3.241  56.602  24.792  1.00 19.74           C  
ATOM   2174  O   TYR A 288       3.928  57.608  24.969  1.00 18.40           O  
ATOM   2175  CB  TYR A 288       4.541  54.815  25.960  1.00 19.54           C  
ATOM   2176  CG  TYR A 288       3.584  54.547  27.101  1.00 19.58           C  
ATOM   2177  CD1 TYR A 288       2.824  53.378  27.138  1.00 19.26           C  
ATOM   2178  CD2 TYR A 288       3.492  55.431  28.180  1.00 20.33           C  
ATOM   2179  CE1 TYR A 288       1.995  53.094  28.218  1.00 22.17           C  
ATOM   2180  CE2 TYR A 288       2.664  55.158  29.265  1.00 20.68           C  
ATOM   2181  CZ  TYR A 288       1.924  53.985  29.284  1.00 22.65           C  
ATOM   2182  OH  TYR A 288       1.127  53.690  30.369  1.00 23.86           O  
ATOM   2183  N   GLU A 289       1.915  56.623  24.673  1.00 22.56           N  
ATOM   2184  CA  GLU A 289       1.117  57.839  24.784  1.00 23.23           C  
ATOM   2185  C   GLU A 289       1.628  58.958  23.879  1.00 24.21           C  
ATOM   2186  O   GLU A 289       1.654  60.126  24.265  1.00 26.34           O  
ATOM   2187  CB  GLU A 289       1.043  58.291  26.245  1.00 22.81           C  
ATOM   2188  CG  GLU A 289       0.358  57.266  27.147  1.00 24.50           C  
ATOM   2189  CD  GLU A 289       0.185  57.729  28.592  1.00 26.25           C  
ATOM   2190  OE1 GLU A 289       0.641  58.839  28.942  1.00 26.10           O  
ATOM   2191  OE2 GLU A 289      -0.419  56.971  29.381  1.00 26.81           O  
ATOM   2192  N   GLY A 290       2.041  58.583  22.670  1.00 24.54           N  
ATOM   2193  CA  GLY A 290       2.544  59.549  21.710  1.00 24.64           C  
ATOM   2194  C   GLY A 290       3.959  60.035  21.962  1.00 25.87           C  
ATOM   2195  O   GLY A 290       4.429  60.969  21.300  1.00 27.53           O  
ATOM   2196  N   ILE A 291       4.655  59.407  22.903  1.00 24.96           N  
ATOM   2197  CA  ILE A 291       6.016  59.810  23.219  1.00 26.31           C  
ATOM   2198  C   ILE A 291       7.053  59.014  22.427  1.00 25.76           C  
ATOM   2199  O   ILE A 291       7.073  57.780  22.480  1.00 24.28           O  
ATOM   2200  CB  ILE A 291       6.320  59.658  24.729  1.00 26.05           C  
ATOM   2201  CG1 ILE A 291       5.269  60.387  25.566  1.00 25.58           C  
ATOM   2202  CG2 ILE A 291       7.683  60.254  25.042  1.00 28.87           C  
ATOM   2203  CD1 ILE A 291       5.484  60.256  27.065  1.00 25.48           C  
ATOM   2204  N   ASP A 292       7.871  59.724  21.651  1.00 27.82           N  
ATOM   2205  CA  ASP A 292       8.932  59.096  20.860  1.00 27.47           C  
ATOM   2206  C   ASP A 292      10.029  58.670  21.836  1.00 25.72           C  
ATOM   2207  O   ASP A 292      10.213  59.300  22.883  1.00 24.74           O  
ATOM   2208  CB  ASP A 292       9.576  60.094  19.880  1.00 28.43           C  
ATOM   2209  CG  ASP A 292       8.629  60.596  18.794  1.00 28.81           C  
ATOM   2210  OD1 ASP A 292       7.596  59.963  18.500  1.00 27.06           O  
ATOM   2211  OD2 ASP A 292       8.957  61.647  18.206  1.00 31.21           O  
ATOM   2212  N   PHE A 293      10.771  57.628  21.484  1.00 23.36           N  
ATOM   2213  CA  PHE A 293      11.871  57.168  22.316  1.00 21.45           C  
ATOM   2214  C   PHE A 293      13.098  57.046  21.425  1.00 19.72           C  
ATOM   2215  O   PHE A 293      13.234  56.096  20.663  1.00 19.82           O  
ATOM   2216  CB  PHE A 293      11.549  55.828  22.975  1.00 20.63           C  
ATOM   2217  CG  PHE A 293      12.536  55.419  24.034  1.00 19.61           C  
ATOM   2218  CD1 PHE A 293      13.109  56.370  24.878  1.00 20.27           C  
ATOM   2219  CD2 PHE A 293      12.876  54.083  24.204  1.00 20.71           C  
ATOM   2220  CE1 PHE A 293      13.997  55.992  25.881  1.00 18.32           C  
ATOM   2221  CE2 PHE A 293      13.762  53.694  25.203  1.00 19.14           C  
ATOM   2222  CZ  PHE A 293      14.325  54.651  26.042  1.00 18.50           C  
ATOM   2223  N   TYR A 294      13.932  58.075  21.453  1.00 20.49           N  
ATOM   2224  CA  TYR A 294      15.152  58.105  20.663  1.00 21.95           C  
ATOM   2225  C   TYR A 294      16.314  58.050  21.640  1.00 22.01           C  
ATOM   2226  O   TYR A 294      16.464  58.931  22.493  1.00 22.28           O  
ATOM   2227  CB  TYR A 294      15.236  59.398  19.862  1.00 24.07           C  
ATOM   2228  CG  TYR A 294      14.293  59.496  18.684  1.00 27.37           C  
ATOM   2229  CD1 TYR A 294      13.021  58.918  18.708  1.00 26.32           C  
ATOM   2230  CD2 TYR A 294      14.679  60.183  17.541  1.00 29.74           C  
ATOM   2231  CE1 TYR A 294      12.159  59.043  17.622  1.00 29.35           C  
ATOM   2232  CE2 TYR A 294      13.831  60.312  16.458  1.00 31.34           C  
ATOM   2233  CZ  TYR A 294      12.578  59.738  16.499  1.00 30.98           C  
ATOM   2234  OH  TYR A 294      11.758  59.898  15.409  1.00 34.97           O  
ATOM   2235  N   THR A 295      17.136  57.017  21.521  1.00 20.84           N  
ATOM   2236  CA  THR A 295      18.269  56.845  22.413  1.00 19.43           C  
ATOM   2237  C   THR A 295      19.299  55.934  21.740  1.00 18.39           C  
ATOM   2238  O   THR A 295      19.209  55.663  20.542  1.00 17.27           O  
ATOM   2239  CB  THR A 295      17.792  56.255  23.775  1.00 19.32           C  
ATOM   2240  OG1 THR A 295      18.869  56.268  24.724  1.00 19.93           O  
ATOM   2241  CG2 THR A 295      17.254  54.833  23.595  1.00 17.35           C  
ATOM   2242  N   SER A 296      20.279  55.476  22.508  1.00 17.78           N  
ATOM   2243  CA  SER A 296      21.321  54.606  21.982  1.00 17.12           C  
ATOM   2244  C   SER A 296      21.889  53.737  23.088  1.00 15.90           C  
ATOM   2245  O   SER A 296      21.522  53.874  24.257  1.00 16.07           O  
ATOM   2246  CB  SER A 296      22.446  55.430  21.337  1.00 17.01           C  
ATOM   2247  OG  SER A 296      23.021  56.344  22.254  1.00 17.34           O  
ATOM   2248  N   ILE A 297      22.762  52.820  22.705  1.00 14.44           N  
ATOM   2249  CA  ILE A 297      23.395  51.930  23.652  1.00 13.39           C  
ATOM   2250  C   ILE A 297      24.745  51.527  23.072  1.00 13.31           C  
ATOM   2251  O   ILE A 297      24.896  51.370  21.857  1.00 14.57           O  
ATOM   2252  CB  ILE A 297      22.510  50.685  23.943  1.00 13.53           C  
ATOM   2253  CG1 ILE A 297      23.134  49.843  25.059  1.00 13.26           C  
ATOM   2254  CG2 ILE A 297      22.284  49.869  22.676  1.00 12.43           C  
ATOM   2255  CD1 ILE A 297      22.239  48.770  25.588  1.00 14.83           C  
ATOM   2256  N   THR A 298      25.746  51.450  23.933  1.00 12.78           N  
ATOM   2257  CA  THR A 298      27.081  51.075  23.507  1.00 13.03           C  
ATOM   2258  C   THR A 298      27.256  49.569  23.653  1.00 12.50           C  
ATOM   2259  O   THR A 298      26.500  48.913  24.374  1.00 12.29           O  
ATOM   2260  CB  THR A 298      28.145  51.764  24.381  1.00 13.73           C  
ATOM   2261  OG1 THR A 298      27.949  51.380  25.748  1.00 12.48           O  
ATOM   2262  CG2 THR A 298      28.047  53.286  24.258  1.00 13.53           C  
ATOM   2263  N   ARG A 299      28.257  49.023  22.971  1.00 11.17           N  
ATOM   2264  CA  ARG A 299      28.549  47.601  23.070  1.00 11.31           C  
ATOM   2265  C   ARG A 299      28.965  47.310  24.513  1.00 11.47           C  
ATOM   2266  O   ARG A 299      28.560  46.300  25.091  1.00 10.19           O  
ATOM   2267  CB  ARG A 299      29.679  47.224  22.115  1.00 11.19           C  
ATOM   2268  CG  ARG A 299      30.172  45.801  22.272  1.00 10.35           C  
ATOM   2269  CD  ARG A 299      31.331  45.528  21.334  1.00 10.66           C  
ATOM   2270  NE  ARG A 299      30.920  45.586  19.937  1.00 11.82           N  
ATOM   2271  CZ  ARG A 299      31.740  45.404  18.907  1.00 12.78           C  
ATOM   2272  NH1 ARG A 299      33.028  45.167  19.117  1.00 12.35           N  
ATOM   2273  NH2 ARG A 299      31.275  45.468  17.664  1.00 10.13           N  
ATOM   2274  N   ALA A 300      29.742  48.223  25.101  1.00 11.53           N  
ATOM   2275  CA  ALA A 300      30.207  48.073  26.480  1.00 11.33           C  
ATOM   2276  C   ALA A 300      29.030  47.941  27.442  1.00 10.92           C  
ATOM   2277  O   ALA A 300      29.027  47.063  28.302  1.00 11.12           O  
ATOM   2278  CB  ALA A 300      31.086  49.245  26.878  1.00 10.73           C  
ATOM   2279  N   ARG A 301      28.022  48.796  27.280  1.00 11.49           N  
ATOM   2280  CA  ARG A 301      26.844  48.753  28.136  1.00 12.42           C  
ATOM   2281  C   ARG A 301      26.076  47.441  27.930  1.00 10.90           C  
ATOM   2282  O   ARG A 301      25.647  46.806  28.895  1.00 12.37           O  
ATOM   2283  CB  ARG A 301      25.932  49.947  27.853  1.00 14.00           C  
ATOM   2284  CG  ARG A 301      24.878  50.168  28.922  1.00 17.97           C  
ATOM   2285  CD  ARG A 301      25.538  50.407  30.273  1.00 22.72           C  
ATOM   2286  NE  ARG A 301      24.580  50.809  31.296  1.00 28.63           N  
ATOM   2287  CZ  ARG A 301      24.155  50.013  32.273  1.00 32.19           C  
ATOM   2288  NH1 ARG A 301      24.598  48.763  32.367  1.00 34.86           N  
ATOM   2289  NH2 ARG A 301      23.265  50.461  33.150  1.00 33.06           N  
ATOM   2290  N   PHE A 302      25.907  47.049  26.671  1.00  8.99           N  
ATOM   2291  CA  PHE A 302      25.213  45.813  26.322  1.00  8.22           C  
ATOM   2292  C   PHE A 302      25.926  44.615  26.965  1.00  8.27           C  
ATOM   2293  O   PHE A 302      25.283  43.697  27.479  1.00  8.90           O  
ATOM   2294  CB  PHE A 302      25.152  45.673  24.790  1.00  7.14           C  
ATOM   2295  CG  PHE A 302      24.700  44.317  24.311  1.00  7.94           C  
ATOM   2296  CD1 PHE A 302      23.366  43.927  24.423  1.00  6.83           C  
ATOM   2297  CD2 PHE A 302      25.616  43.422  23.755  1.00  9.07           C  
ATOM   2298  CE1 PHE A 302      22.954  42.666  23.995  1.00  6.74           C  
ATOM   2299  CE2 PHE A 302      25.213  42.159  23.323  1.00  8.44           C  
ATOM   2300  CZ  PHE A 302      23.877  41.781  23.445  1.00  9.46           C  
ATOM   2301  N   GLU A 303      27.256  44.637  26.961  1.00  8.59           N  
ATOM   2302  CA  GLU A 303      28.026  43.548  27.561  1.00  9.40           C  
ATOM   2303  C   GLU A 303      27.812  43.518  29.067  1.00 10.96           C  
ATOM   2304  O   GLU A 303      27.637  42.445  29.650  1.00 11.57           O  
ATOM   2305  CB  GLU A 303      29.512  43.681  27.227  1.00  7.51           C  
ATOM   2306  CG  GLU A 303      29.801  43.434  25.757  1.00 10.46           C  
ATOM   2307  CD  GLU A 303      31.219  43.780  25.351  1.00 13.22           C  
ATOM   2308  OE1 GLU A 303      31.929  44.463  26.122  1.00 14.57           O  
ATOM   2309  OE2 GLU A 303      31.620  43.379  24.241  1.00 10.60           O  
ATOM   2310  N   GLU A 304      27.789  44.695  29.689  1.00 10.06           N  
ATOM   2311  CA  GLU A 304      27.576  44.761  31.126  1.00 11.78           C  
ATOM   2312  C   GLU A 304      26.201  44.232  31.513  1.00 10.14           C  
ATOM   2313  O   GLU A 304      26.084  43.418  32.428  1.00  9.05           O  
ATOM   2314  CB  GLU A 304      27.753  46.175  31.672  1.00 16.26           C  
ATOM   2315  CG  GLU A 304      27.539  46.205  33.185  1.00 20.98           C  
ATOM   2316  CD  GLU A 304      27.880  47.527  33.821  1.00 25.85           C  
ATOM   2317  OE1 GLU A 304      27.007  48.422  33.847  1.00 27.51           O  
ATOM   2318  OE2 GLU A 304      29.018  47.659  34.319  1.00 26.46           O  
ATOM   2319  N   LEU A 305      25.165  44.675  30.804  1.00  9.80           N  
ATOM   2320  CA  LEU A 305      23.801  44.228  31.082  1.00  8.50           C  
ATOM   2321  C   LEU A 305      23.662  42.709  31.019  1.00  8.78           C  
ATOM   2322  O   LEU A 305      22.813  42.133  31.700  1.00  9.74           O  
ATOM   2323  CB  LEU A 305      22.814  44.853  30.089  1.00  9.49           C  
ATOM   2324  CG  LEU A 305      22.503  46.350  30.175  1.00 11.07           C  
ATOM   2325  CD1 LEU A 305      21.730  46.789  28.936  1.00 12.07           C  
ATOM   2326  CD2 LEU A 305      21.715  46.648  31.439  1.00 10.12           C  
ATOM   2327  N   ASN A 306      24.511  42.065  30.222  1.00  8.30           N  
ATOM   2328  CA  ASN A 306      24.461  40.612  30.041  1.00  8.77           C  
ATOM   2329  C   ASN A 306      25.684  39.830  30.527  1.00  7.31           C  
ATOM   2330  O   ASN A 306      25.763  38.617  30.309  1.00  7.59           O  
ATOM   2331  CB  ASN A 306      24.235  40.290  28.553  1.00  7.09           C  
ATOM   2332  CG  ASN A 306      22.907  40.803  28.036  1.00  7.76           C  
ATOM   2333  OD1 ASN A 306      22.846  41.805  27.331  1.00 10.78           O  
ATOM   2334  ND2 ASN A 306      21.836  40.116  28.390  1.00  6.29           N  
ATOM   2335  N   ALA A 307      26.597  40.499  31.222  1.00  9.42           N  
ATOM   2336  CA  ALA A 307      27.836  39.875  31.707  1.00  9.63           C  
ATOM   2337  C   ALA A 307      27.699  38.481  32.318  1.00 10.07           C  
ATOM   2338  O   ALA A 307      28.411  37.555  31.925  1.00 10.88           O  
ATOM   2339  CB  ALA A 307      28.542  40.801  32.685  1.00  9.64           C  
ATOM   2340  N   ASP A 308      26.785  38.336  33.274  1.00 10.28           N  
ATOM   2341  CA  ASP A 308      26.560  37.060  33.948  1.00  9.31           C  
ATOM   2342  C   ASP A 308      26.089  35.958  33.001  1.00  7.35           C  
ATOM   2343  O   ASP A 308      26.570  34.825  33.065  1.00  6.76           O  
ATOM   2344  CB  ASP A 308      25.570  37.234  35.114  1.00 12.49           C  
ATOM   2345  CG  ASP A 308      24.210  37.744  34.665  1.00 12.68           C  
ATOM   2346  OD1 ASP A 308      24.161  38.787  33.987  1.00 14.02           O  
ATOM   2347  OD2 ASP A 308      23.191  37.102  34.995  1.00 16.44           O  
ATOM   2348  N   LEU A 309      25.163  36.298  32.112  1.00  7.23           N  
ATOM   2349  CA  LEU A 309      24.633  35.333  31.155  1.00  7.80           C  
ATOM   2350  C   LEU A 309      25.723  34.873  30.177  1.00  6.59           C  
ATOM   2351  O   LEU A 309      25.854  33.682  29.893  1.00  7.53           O  
ATOM   2352  CB  LEU A 309      23.447  35.941  30.398  1.00  7.52           C  
ATOM   2353  CG  LEU A 309      22.287  36.411  31.276  1.00  6.92           C  
ATOM   2354  CD1 LEU A 309      21.195  37.026  30.416  1.00  8.10           C  
ATOM   2355  CD2 LEU A 309      21.747  35.239  32.073  1.00  8.72           C  
ATOM   2356  N   PHE A 310      26.518  35.822  29.697  1.00  8.67           N  
ATOM   2357  CA  PHE A 310      27.603  35.527  28.765  1.00  8.81           C  
ATOM   2358  C   PHE A 310      28.611  34.603  29.444  1.00  9.75           C  
ATOM   2359  O   PHE A 310      28.968  33.551  28.917  1.00 10.78           O  
ATOM   2360  CB  PHE A 310      28.316  36.819  28.341  1.00  8.81           C  
ATOM   2361  CG  PHE A 310      27.517  37.710  27.416  1.00  8.45           C  
ATOM   2362  CD1 PHE A 310      26.293  37.305  26.898  1.00  7.72           C  
ATOM   2363  CD2 PHE A 310      28.009  38.968  27.059  1.00  9.49           C  
ATOM   2364  CE1 PHE A 310      25.573  38.138  26.030  1.00  8.23           C  
ATOM   2365  CE2 PHE A 310      27.297  39.806  26.193  1.00  8.90           C  
ATOM   2366  CZ  PHE A 310      26.077  39.391  25.681  1.00  7.27           C  
ATOM   2367  N   ARG A 311      29.062  35.006  30.626  1.00 10.14           N  
ATOM   2368  CA  ARG A 311      30.041  34.244  31.392  1.00 10.36           C  
ATOM   2369  C   ARG A 311      29.528  32.833  31.708  1.00  9.99           C  
ATOM   2370  O   ARG A 311      30.289  31.858  31.701  1.00  9.96           O  
ATOM   2371  CB  ARG A 311      30.343  34.996  32.691  1.00 10.29           C  
ATOM   2372  CG  ARG A 311      31.613  34.587  33.407  1.00 14.14           C  
ATOM   2373  CD  ARG A 311      31.640  35.186  34.818  1.00 20.67           C  
ATOM   2374  NE  ARG A 311      31.328  36.619  34.837  1.00 25.36           N  
ATOM   2375  CZ  ARG A 311      30.301  37.163  35.501  1.00 28.13           C  
ATOM   2376  NH1 ARG A 311      29.465  36.409  36.215  1.00 24.71           N  
ATOM   2377  NH2 ARG A 311      30.104  38.475  35.451  1.00 27.61           N  
ATOM   2378  N   GLY A 312      28.226  32.732  31.955  1.00  9.91           N  
ATOM   2379  CA  GLY A 312      27.614  31.457  32.287  1.00  8.87           C  
ATOM   2380  C   GLY A 312      27.649  30.387  31.216  1.00  8.22           C  
ATOM   2381  O   GLY A 312      27.462  29.207  31.527  1.00  8.04           O  
ATOM   2382  N   THR A 313      27.887  30.779  29.964  1.00  8.49           N  
ATOM   2383  CA  THR A 313      27.937  29.819  28.863  1.00  8.91           C  
ATOM   2384  C   THR A 313      29.138  28.885  29.001  1.00  9.26           C  
ATOM   2385  O   THR A 313      29.136  27.777  28.465  1.00 11.63           O  
ATOM   2386  CB  THR A 313      27.984  30.517  27.474  1.00  7.97           C  
ATOM   2387  OG1 THR A 313      29.189  31.282  27.351  1.00  7.50           O  
ATOM   2388  CG2 THR A 313      26.778  31.426  27.284  1.00  6.35           C  
ATOM   2389  N   LEU A 314      30.140  29.309  29.764  1.00  7.62           N  
ATOM   2390  CA  LEU A 314      31.332  28.492  29.954  1.00  9.79           C  
ATOM   2391  C   LEU A 314      31.122  27.297  30.888  1.00  9.70           C  
ATOM   2392  O   LEU A 314      31.842  26.303  30.794  1.00 11.08           O  
ATOM   2393  CB  LEU A 314      32.518  29.354  30.411  1.00  8.19           C  
ATOM   2394  CG  LEU A 314      32.965  30.450  29.427  1.00  6.21           C  
ATOM   2395  CD1 LEU A 314      34.105  31.249  30.028  1.00  7.57           C  
ATOM   2396  CD2 LEU A 314      33.389  29.842  28.097  1.00  7.57           C  
ATOM   2397  N   ASP A 315      30.124  27.369  31.768  1.00  9.26           N  
ATOM   2398  CA  ASP A 315      29.860  26.255  32.677  1.00 11.00           C  
ATOM   2399  C   ASP A 315      29.494  24.985  31.903  1.00 10.47           C  
ATOM   2400  O   ASP A 315      30.063  23.920  32.159  1.00 10.69           O  
ATOM   2401  CB  ASP A 315      28.784  26.610  33.712  1.00 13.77           C  
ATOM   2402  CG  ASP A 315      29.331  27.432  34.873  1.00 19.00           C  
ATOM   2403  OD1 ASP A 315      30.564  27.418  35.103  1.00 21.47           O  
ATOM   2404  OD2 ASP A 315      28.523  28.085  35.566  1.00 21.04           O  
ATOM   2405  N   PRO A 316      28.538  25.073  30.952  1.00 10.97           N  
ATOM   2406  CA  PRO A 316      28.173  23.875  30.186  1.00 10.51           C  
ATOM   2407  C   PRO A 316      29.356  23.357  29.361  1.00 10.16           C  
ATOM   2408  O   PRO A 316      29.447  22.163  29.076  1.00 10.00           O  
ATOM   2409  CB  PRO A 316      27.044  24.379  29.293  1.00 11.11           C  
ATOM   2410  CG  PRO A 316      26.385  25.406  30.148  1.00 12.89           C  
ATOM   2411  CD  PRO A 316      27.576  26.160  30.688  1.00 11.78           C  
ATOM   2412  N   VAL A 317      30.256  24.257  28.969  1.00  9.26           N  
ATOM   2413  CA  VAL A 317      31.434  23.858  28.203  1.00  9.70           C  
ATOM   2414  C   VAL A 317      32.332  22.978  29.074  1.00  9.55           C  
ATOM   2415  O   VAL A 317      32.800  21.926  28.633  1.00 10.19           O  
ATOM   2416  CB  VAL A 317      32.224  25.078  27.684  1.00  9.23           C  
ATOM   2417  CG1 VAL A 317      33.524  24.614  27.005  1.00 10.26           C  
ATOM   2418  CG2 VAL A 317      31.364  25.871  26.696  1.00  8.32           C  
ATOM   2419  N   GLU A 318      32.561  23.403  30.313  1.00  9.47           N  
ATOM   2420  CA  GLU A 318      33.379  22.618  31.229  1.00 11.35           C  
ATOM   2421  C   GLU A 318      32.678  21.301  31.534  1.00 10.03           C  
ATOM   2422  O   GLU A 318      33.313  20.253  31.606  1.00 10.40           O  
ATOM   2423  CB  GLU A 318      33.609  23.371  32.532  1.00 13.10           C  
ATOM   2424  CG  GLU A 318      34.263  24.712  32.359  1.00 17.13           C  
ATOM   2425  CD  GLU A 318      34.539  25.385  33.684  1.00 23.22           C  
ATOM   2426  OE1 GLU A 318      33.595  25.936  34.288  1.00 27.07           O  
ATOM   2427  OE2 GLU A 318      35.700  25.347  34.137  1.00 24.28           O  
ATOM   2428  N   LYS A 319      31.359  21.349  31.695  1.00 11.34           N  
ATOM   2429  CA  LYS A 319      30.623  20.130  31.988  1.00 12.79           C  
ATOM   2430  C   LYS A 319      30.694  19.118  30.851  1.00 12.76           C  
ATOM   2431  O   LYS A 319      30.917  17.930  31.091  1.00 14.58           O  
ATOM   2432  CB  LYS A 319      29.167  20.411  32.340  1.00 14.29           C  
ATOM   2433  CG  LYS A 319      28.444  19.138  32.732  1.00 16.10           C  
ATOM   2434  CD  LYS A 319      27.196  19.405  33.536  1.00 24.48           C  
ATOM   2435  CE  LYS A 319      26.736  18.132  34.240  1.00 26.07           C  
ATOM   2436  NZ  LYS A 319      26.571  17.011  33.278  1.00 27.78           N  
ATOM   2437  N   ALA A 320      30.506  19.586  29.619  1.00 11.30           N  
ATOM   2438  CA  ALA A 320      30.556  18.707  28.455  1.00 10.58           C  
ATOM   2439  C   ALA A 320      31.925  18.048  28.380  1.00 11.34           C  
ATOM   2440  O   ALA A 320      32.036  16.850  28.110  1.00 11.28           O  
ATOM   2441  CB  ALA A 320      30.271  19.488  27.180  1.00  9.38           C  
ATOM   2442  N   LEU A 321      32.968  18.833  28.636  1.00 11.47           N  
ATOM   2443  CA  LEU A 321      34.328  18.316  28.612  1.00 12.38           C  
ATOM   2444  C   LEU A 321      34.512  17.198  29.641  1.00 14.66           C  
ATOM   2445  O   LEU A 321      35.033  16.129  29.311  1.00 16.86           O  
ATOM   2446  CB  LEU A 321      35.339  19.447  28.846  1.00 12.78           C  
ATOM   2447  CG  LEU A 321      35.636  20.366  27.657  1.00  9.87           C  
ATOM   2448  CD1 LEU A 321      36.384  21.591  28.126  1.00  9.99           C  
ATOM   2449  CD2 LEU A 321      36.445  19.609  26.614  1.00  8.81           C  
ATOM   2450  N   ARG A 322      34.061  17.424  30.873  1.00 15.82           N  
ATOM   2451  CA  ARG A 322      34.190  16.406  31.913  1.00 16.92           C  
ATOM   2452  C   ARG A 322      33.407  15.154  31.557  1.00 17.73           C  
ATOM   2453  O   ARG A 322      33.919  14.043  31.689  1.00 18.90           O  
ATOM   2454  CB  ARG A 322      33.727  16.927  33.266  1.00 18.68           C  
ATOM   2455  CG  ARG A 322      34.571  18.063  33.809  1.00 25.07           C  
ATOM   2456  CD  ARG A 322      34.234  18.322  35.264  1.00 28.74           C  
ATOM   2457  NE  ARG A 322      32.791  18.239  35.467  1.00 32.88           N  
ATOM   2458  CZ  ARG A 322      31.975  19.289  35.524  1.00 34.18           C  
ATOM   2459  NH1 ARG A 322      32.452  20.526  35.435  1.00 34.95           N  
ATOM   2460  NH2 ARG A 322      30.678  19.105  35.705  1.00 37.07           N  
ATOM   2461  N   ASP A 323      32.173  15.327  31.089  1.00 17.60           N  
ATOM   2462  CA  ASP A 323      31.346  14.184  30.706  1.00 16.99           C  
ATOM   2463  C   ASP A 323      31.982  13.406  29.559  1.00 15.97           C  
ATOM   2464  O   ASP A 323      31.865  12.186  29.489  1.00 16.72           O  
ATOM   2465  CB  ASP A 323      29.933  14.632  30.314  1.00 18.23           C  
ATOM   2466  CG  ASP A 323      29.114  15.108  31.502  1.00 20.23           C  
ATOM   2467  OD1 ASP A 323      29.560  14.941  32.658  1.00 21.59           O  
ATOM   2468  OD2 ASP A 323      28.012  15.652  31.277  1.00 22.40           O  
ATOM   2469  N   ALA A 324      32.662  14.117  28.668  1.00 15.54           N  
ATOM   2470  CA  ALA A 324      33.322  13.486  27.537  1.00 16.26           C  
ATOM   2471  C   ALA A 324      34.679  12.914  27.941  1.00 17.56           C  
ATOM   2472  O   ALA A 324      35.340  12.247  27.142  1.00 18.11           O  
ATOM   2473  CB  ALA A 324      33.488  14.486  26.410  1.00 15.49           C  
ATOM   2474  N   LYS A 325      35.085  13.181  29.183  1.00 19.30           N  
ATOM   2475  CA  LYS A 325      36.368  12.725  29.721  1.00 20.95           C  
ATOM   2476  C   LYS A 325      37.524  13.286  28.899  1.00 19.22           C  
ATOM   2477  O   LYS A 325      38.489  12.578  28.595  1.00 18.77           O  
ATOM   2478  CB  LYS A 325      36.430  11.195  29.765  1.00 23.78           C  
ATOM   2479  CG  LYS A 325      35.524  10.563  30.815  1.00 28.54           C  
ATOM   2480  CD  LYS A 325      35.426   9.063  30.602  1.00 35.30           C  
ATOM   2481  CE  LYS A 325      36.803   8.400  30.627  1.00 39.10           C  
ATOM   2482  NZ  LYS A 325      36.833   7.146  29.813  1.00 43.85           N  
ATOM   2483  N   LEU A 326      37.428  14.574  28.577  1.00 17.48           N  
ATOM   2484  CA  LEU A 326      38.439  15.258  27.781  1.00 15.80           C  
ATOM   2485  C   LEU A 326      38.865  16.574  28.405  1.00 16.20           C  
ATOM   2486  O   LEU A 326      38.081  17.230  29.084  1.00 15.42           O  
ATOM   2487  CB  LEU A 326      37.897  15.555  26.381  1.00 16.23           C  
ATOM   2488  CG  LEU A 326      37.514  14.392  25.472  1.00 16.22           C  
ATOM   2489  CD1 LEU A 326      36.861  14.935  24.214  1.00 16.39           C  
ATOM   2490  CD2 LEU A 326      38.745  13.580  25.131  1.00 16.73           C  
ATOM   2491  N   ASP A 327      40.119  16.940  28.155  1.00 17.47           N  
ATOM   2492  CA  ASP A 327      40.728  18.187  28.614  1.00 19.07           C  
ATOM   2493  C   ASP A 327      40.554  19.177  27.450  1.00 16.93           C  
ATOM   2494  O   ASP A 327      40.380  18.756  26.308  1.00 14.87           O  
ATOM   2495  CB  ASP A 327      42.228  17.950  28.894  1.00 23.01           C  
ATOM   2496  CG  ASP A 327      42.947  19.199  29.418  1.00 29.86           C  
ATOM   2497  OD1 ASP A 327      43.381  20.043  28.598  1.00 32.83           O  
ATOM   2498  OD2 ASP A 327      43.091  19.335  30.655  1.00 34.67           O  
ATOM   2499  N   LYS A 328      40.593  20.478  27.738  1.00 17.27           N  
ATOM   2500  CA  LYS A 328      40.462  21.523  26.711  1.00 18.32           C  
ATOM   2501  C   LYS A 328      41.321  21.219  25.492  1.00 18.09           C  
ATOM   2502  O   LYS A 328      40.863  21.290  24.350  1.00 16.62           O  
ATOM   2503  CB  LYS A 328      40.947  22.875  27.244  1.00 18.54           C  
ATOM   2504  CG  LYS A 328      40.202  23.451  28.406  1.00 20.84           C  
ATOM   2505  CD  LYS A 328      40.844  24.782  28.791  1.00 18.60           C  
ATOM   2506  CE  LYS A 328      40.168  25.402  29.994  1.00 15.42           C  
ATOM   2507  NZ  LYS A 328      40.743  26.730  30.324  1.00 14.06           N  
ATOM   2508  N   SER A 329      42.590  20.928  25.764  1.00 18.34           N  
ATOM   2509  CA  SER A 329      43.596  20.640  24.745  1.00 19.68           C  
ATOM   2510  C   SER A 329      43.294  19.482  23.806  1.00 17.45           C  
ATOM   2511  O   SER A 329      43.916  19.360  22.751  1.00 19.79           O  
ATOM   2512  CB  SER A 329      44.955  20.405  25.415  1.00 21.65           C  
ATOM   2513  OG  SER A 329      44.882  19.333  26.348  1.00 23.29           O  
ATOM   2514  N   GLN A 330      42.366  18.619  24.198  1.00 16.26           N  
ATOM   2515  CA  GLN A 330      42.017  17.482  23.362  1.00 15.69           C  
ATOM   2516  C   GLN A 330      40.975  17.809  22.292  1.00 14.77           C  
ATOM   2517  O   GLN A 330      40.656  16.962  21.448  1.00 15.04           O  
ATOM   2518  CB  GLN A 330      41.577  16.307  24.227  1.00 15.75           C  
ATOM   2519  CG  GLN A 330      42.711  15.738  25.076  1.00 17.50           C  
ATOM   2520  CD  GLN A 330      42.249  14.634  26.006  1.00 17.78           C  
ATOM   2521  OE1 GLN A 330      41.667  14.897  27.055  1.00 16.19           O  
ATOM   2522  NE2 GLN A 330      42.488  13.388  25.615  1.00 20.80           N  
ATOM   2523  N   ILE A 331      40.439  19.026  22.333  1.00 14.32           N  
ATOM   2524  CA  ILE A 331      39.451  19.466  21.350  1.00 13.07           C  
ATOM   2525  C   ILE A 331      40.234  19.955  20.137  1.00 13.49           C  
ATOM   2526  O   ILE A 331      41.025  20.891  20.242  1.00 15.06           O  
ATOM   2527  CB  ILE A 331      38.564  20.628  21.898  1.00 11.73           C  
ATOM   2528  CG1 ILE A 331      37.756  20.158  23.110  1.00 11.73           C  
ATOM   2529  CG2 ILE A 331      37.629  21.148  20.816  1.00  9.10           C  
ATOM   2530  CD1 ILE A 331      36.866  18.964  22.837  1.00 12.88           C  
ATOM   2531  N   HIS A 332      40.027  19.308  18.996  1.00 13.80           N  
ATOM   2532  CA  HIS A 332      40.731  19.673  17.765  1.00 13.56           C  
ATOM   2533  C   HIS A 332      40.106  20.857  17.038  1.00 11.62           C  
ATOM   2534  O   HIS A 332      40.796  21.599  16.337  1.00 10.87           O  
ATOM   2535  CB  HIS A 332      40.807  18.471  16.820  1.00 16.87           C  
ATOM   2536  CG  HIS A 332      41.477  17.275  17.419  1.00 24.62           C  
ATOM   2537  ND1 HIS A 332      40.832  16.446  18.323  1.00 25.43           N  
ATOM   2538  CD2 HIS A 332      42.717  16.769  17.266  1.00 27.71           C  
ATOM   2539  CE1 HIS A 332      41.666  15.479  18.693  1.00 25.70           C  
ATOM   2540  NE2 HIS A 332      42.808  15.658  18.063  1.00 28.79           N  
ATOM   2541  N   ASP A 333      38.792  21.006  17.152  1.00 10.33           N  
ATOM   2542  CA  ASP A 333      38.105  22.106  16.490  1.00 11.12           C  
ATOM   2543  C   ASP A 333      36.960  22.621  17.339  1.00  9.67           C  
ATOM   2544  O   ASP A 333      36.276  21.842  17.998  1.00 10.11           O  
ATOM   2545  CB  ASP A 333      37.544  21.659  15.132  1.00 10.86           C  
ATOM   2546  CG  ASP A 333      38.624  21.145  14.186  1.00 14.44           C  
ATOM   2547  OD1 ASP A 333      38.969  19.944  14.272  1.00 14.94           O  
ATOM   2548  OD2 ASP A 333      39.127  21.940  13.363  1.00 15.62           O  
ATOM   2549  N   ILE A 334      36.770  23.936  17.315  1.00  9.69           N  
ATOM   2550  CA  ILE A 334      35.680  24.597  18.035  1.00 10.13           C  
ATOM   2551  C   ILE A 334      34.826  25.258  16.956  1.00 10.74           C  
ATOM   2552  O   ILE A 334      35.312  26.108  16.209  1.00 10.19           O  
ATOM   2553  CB  ILE A 334      36.177  25.709  18.977  1.00  9.12           C  
ATOM   2554  CG1 ILE A 334      37.129  25.148  20.026  1.00  9.60           C  
ATOM   2555  CG2 ILE A 334      34.987  26.378  19.663  1.00 10.64           C  
ATOM   2556  CD1 ILE A 334      37.882  26.236  20.751  1.00 10.21           C  
ATOM   2557  N   VAL A 335      33.558  24.878  16.885  1.00 10.02           N  
ATOM   2558  CA  VAL A 335      32.661  25.420  15.877  1.00  9.96           C  
ATOM   2559  C   VAL A 335      31.564  26.298  16.482  1.00  9.04           C  
ATOM   2560  O   VAL A 335      30.825  25.861  17.363  1.00  7.61           O  
ATOM   2561  CB  VAL A 335      32.013  24.268  15.054  1.00  9.00           C  
ATOM   2562  CG1 VAL A 335      31.087  24.826  13.987  1.00  9.70           C  
ATOM   2563  CG2 VAL A 335      33.093  23.399  14.414  1.00  9.75           C  
ATOM   2564  N   LEU A 336      31.486  27.541  16.025  1.00  8.66           N  
ATOM   2565  CA  LEU A 336      30.465  28.463  16.501  1.00  8.80           C  
ATOM   2566  C   LEU A 336      29.188  28.266  15.699  1.00  9.54           C  
ATOM   2567  O   LEU A 336      29.206  28.284  14.465  1.00  9.94           O  
ATOM   2568  CB  LEU A 336      30.911  29.917  16.348  1.00 10.39           C  
ATOM   2569  CG  LEU A 336      32.004  30.473  17.257  1.00 10.87           C  
ATOM   2570  CD1 LEU A 336      32.059  31.979  17.071  1.00  9.90           C  
ATOM   2571  CD2 LEU A 336      31.704  30.142  18.710  1.00 12.44           C  
ATOM   2572  N   VAL A 337      28.074  28.085  16.396  1.00  7.82           N  
ATOM   2573  CA  VAL A 337      26.790  27.904  15.734  1.00  7.58           C  
ATOM   2574  C   VAL A 337      25.771  28.768  16.472  1.00  7.79           C  
ATOM   2575  O   VAL A 337      25.892  28.988  17.679  1.00  6.74           O  
ATOM   2576  CB  VAL A 337      26.325  26.421  15.784  1.00  8.24           C  
ATOM   2577  CG1 VAL A 337      25.039  26.234  14.974  1.00  6.99           C  
ATOM   2578  CG2 VAL A 337      27.427  25.489  15.272  1.00  9.16           C  
ATOM   2579  N   GLY A 338      24.772  29.260  15.747  1.00  8.89           N  
ATOM   2580  CA  GLY A 338      23.749  30.076  16.367  1.00  8.09           C  
ATOM   2581  C   GLY A 338      24.018  31.554  16.200  1.00  8.63           C  
ATOM   2582  O   GLY A 338      25.157  31.997  16.337  1.00  8.37           O  
ATOM   2583  N   GLY A 339      22.960  32.319  15.945  1.00  9.13           N  
ATOM   2584  CA  GLY A 339      23.094  33.751  15.746  1.00  8.07           C  
ATOM   2585  C   GLY A 339      23.755  34.493  16.895  1.00  8.04           C  
ATOM   2586  O   GLY A 339      24.463  35.475  16.680  1.00  8.97           O  
ATOM   2587  N   SER A 340      23.540  34.021  18.115  1.00  7.90           N  
ATOM   2588  CA  SER A 340      24.125  34.673  19.282  1.00  9.32           C  
ATOM   2589  C   SER A 340      25.652  34.570  19.369  1.00  8.46           C  
ATOM   2590  O   SER A 340      26.287  35.366  20.053  1.00  8.28           O  
ATOM   2591  CB  SER A 340      23.482  34.153  20.571  1.00  9.17           C  
ATOM   2592  OG  SER A 340      22.100  34.466  20.616  1.00  8.63           O  
ATOM   2593  N   THR A 341      26.257  33.623  18.660  1.00  9.23           N  
ATOM   2594  CA  THR A 341      27.708  33.499  18.715  1.00  9.29           C  
ATOM   2595  C   THR A 341      28.427  34.598  17.916  1.00 10.36           C  
ATOM   2596  O   THR A 341      29.655  34.646  17.885  1.00  9.23           O  
ATOM   2597  CB  THR A 341      28.197  32.088  18.299  1.00  8.07           C  
ATOM   2598  OG1 THR A 341      27.827  31.816  16.943  1.00 10.26           O  
ATOM   2599  CG2 THR A 341      27.605  31.025  19.214  1.00  6.27           C  
ATOM   2600  N   ARG A 342      27.661  35.465  17.250  1.00 10.06           N  
ATOM   2601  CA  ARG A 342      28.248  36.575  16.508  1.00  9.55           C  
ATOM   2602  C   ARG A 342      28.634  37.681  17.492  1.00  8.91           C  
ATOM   2603  O   ARG A 342      29.360  38.606  17.138  1.00  8.45           O  
ATOM   2604  CB  ARG A 342      27.288  37.127  15.445  1.00 11.50           C  
ATOM   2605  CG  ARG A 342      27.127  36.234  14.221  1.00 15.83           C  
ATOM   2606  CD  ARG A 342      26.755  37.040  12.968  1.00 20.48           C  
ATOM   2607  NE  ARG A 342      27.864  37.875  12.496  1.00 25.30           N  
ATOM   2608  CZ  ARG A 342      28.844  37.449  11.690  1.00 30.59           C  
ATOM   2609  NH1 ARG A 342      28.861  36.195  11.238  1.00 27.96           N  
ATOM   2610  NH2 ARG A 342      29.814  38.282  11.320  1.00 30.16           N  
ATOM   2611  N   ILE A 343      28.142  37.581  18.727  1.00  8.19           N  
ATOM   2612  CA  ILE A 343      28.462  38.569  19.760  1.00  8.56           C  
ATOM   2613  C   ILE A 343      29.957  38.469  20.100  1.00  8.95           C  
ATOM   2614  O   ILE A 343      30.444  37.422  20.558  1.00  8.87           O  
ATOM   2615  CB  ILE A 343      27.622  38.354  21.052  1.00  7.80           C  
ATOM   2616  CG1 ILE A 343      26.124  38.467  20.736  1.00  7.97           C  
ATOM   2617  CG2 ILE A 343      28.020  39.380  22.119  1.00  6.23           C  
ATOM   2618  CD1 ILE A 343      25.215  38.072  21.895  1.00  8.40           C  
ATOM   2619  N   PRO A 344      30.709  39.558  19.871  1.00  9.73           N  
ATOM   2620  CA  PRO A 344      32.147  39.610  20.142  1.00  9.41           C  
ATOM   2621  C   PRO A 344      32.552  39.132  21.537  1.00  8.18           C  
ATOM   2622  O   PRO A 344      33.531  38.397  21.678  1.00  8.48           O  
ATOM   2623  CB  PRO A 344      32.472  41.089  19.925  1.00 12.01           C  
ATOM   2624  CG  PRO A 344      31.535  41.457  18.799  1.00 11.50           C  
ATOM   2625  CD  PRO A 344      30.243  40.829  19.281  1.00  8.94           C  
ATOM   2626  N   LYS A 345      31.800  39.523  22.561  1.00  7.14           N  
ATOM   2627  CA  LYS A 345      32.129  39.115  23.928  1.00  7.51           C  
ATOM   2628  C   LYS A 345      32.045  37.608  24.127  1.00  7.22           C  
ATOM   2629  O   LYS A 345      32.853  37.035  24.858  1.00  8.35           O  
ATOM   2630  CB  LYS A 345      31.226  39.808  24.944  1.00  8.92           C  
ATOM   2631  CG  LYS A 345      31.720  39.689  26.385  1.00 10.01           C  
ATOM   2632  CD  LYS A 345      33.073  40.377  26.554  1.00 11.78           C  
ATOM   2633  CE  LYS A 345      33.345  40.726  28.006  1.00 13.64           C  
ATOM   2634  NZ  LYS A 345      34.521  41.632  28.138  1.00 16.24           N  
ATOM   2635  N   ILE A 346      31.058  36.970  23.497  1.00  6.38           N  
ATOM   2636  CA  ILE A 346      30.889  35.526  23.609  1.00  6.15           C  
ATOM   2637  C   ILE A 346      32.096  34.844  22.966  1.00  7.00           C  
ATOM   2638  O   ILE A 346      32.662  33.897  23.521  1.00  6.62           O  
ATOM   2639  CB  ILE A 346      29.585  35.051  22.913  1.00  8.68           C  
ATOM   2640  CG1 ILE A 346      28.356  35.522  23.699  1.00  9.66           C  
ATOM   2641  CG2 ILE A 346      29.564  33.536  22.778  1.00  8.22           C  
ATOM   2642  CD1 ILE A 346      28.144  34.795  25.009  1.00 11.71           C  
ATOM   2643  N   GLN A 347      32.493  35.339  21.799  1.00  6.07           N  
ATOM   2644  CA  GLN A 347      33.641  34.777  21.104  1.00  6.27           C  
ATOM   2645  C   GLN A 347      34.906  34.931  21.944  1.00  7.05           C  
ATOM   2646  O   GLN A 347      35.724  34.011  22.012  1.00  7.88           O  
ATOM   2647  CB  GLN A 347      33.817  35.430  19.736  1.00  7.45           C  
ATOM   2648  CG  GLN A 347      32.685  35.118  18.774  1.00  7.72           C  
ATOM   2649  CD  GLN A 347      32.916  35.694  17.391  1.00 10.09           C  
ATOM   2650  OE1 GLN A 347      33.989  36.228  17.095  1.00  8.65           O  
ATOM   2651  NE2 GLN A 347      31.916  35.585  16.534  1.00 10.39           N  
ATOM   2652  N   LYS A 348      35.044  36.079  22.603  1.00  6.51           N  
ATOM   2653  CA  LYS A 348      36.198  36.337  23.458  1.00  7.75           C  
ATOM   2654  C   LYS A 348      36.227  35.347  24.623  1.00  8.00           C  
ATOM   2655  O   LYS A 348      37.257  34.727  24.896  1.00  9.03           O  
ATOM   2656  CB  LYS A 348      36.161  37.762  24.012  1.00  7.45           C  
ATOM   2657  CG  LYS A 348      37.373  38.108  24.865  1.00 10.58           C  
ATOM   2658  CD  LYS A 348      37.301  39.537  25.382  1.00 12.26           C  
ATOM   2659  CE  LYS A 348      38.620  39.967  26.020  1.00 14.41           C  
ATOM   2660  NZ  LYS A 348      39.003  39.090  27.155  1.00 11.07           N  
ATOM   2661  N   LEU A 349      35.098  35.216  25.312  1.00  6.54           N  
ATOM   2662  CA  LEU A 349      34.981  34.305  26.452  1.00  7.78           C  
ATOM   2663  C   LEU A 349      35.364  32.875  26.097  1.00  8.34           C  
ATOM   2664  O   LEU A 349      36.147  32.237  26.805  1.00  7.90           O  
ATOM   2665  CB  LEU A 349      33.554  34.331  27.002  1.00  6.57           C  
ATOM   2666  CG  LEU A 349      33.182  35.530  27.880  1.00  7.85           C  
ATOM   2667  CD1 LEU A 349      31.665  35.683  27.957  1.00  7.22           C  
ATOM   2668  CD2 LEU A 349      33.785  35.344  29.269  1.00  9.14           C  
ATOM   2669  N   LEU A 350      34.815  32.379  24.992  1.00  8.79           N  
ATOM   2670  CA  LEU A 350      35.091  31.019  24.546  1.00  8.62           C  
ATOM   2671  C   LEU A 350      36.551  30.829  24.128  1.00  7.30           C  
ATOM   2672  O   LEU A 350      37.185  29.843  24.498  1.00  8.14           O  
ATOM   2673  CB  LEU A 350      34.157  30.640  23.391  1.00  8.01           C  
ATOM   2674  CG  LEU A 350      34.217  29.185  22.909  1.00  9.83           C  
ATOM   2675  CD1 LEU A 350      33.855  28.211  24.039  1.00  7.41           C  
ATOM   2676  CD2 LEU A 350      33.274  29.017  21.732  1.00  9.19           C  
ATOM   2677  N   GLN A 351      37.090  31.776  23.367  1.00  8.45           N  
ATOM   2678  CA  GLN A 351      38.469  31.668  22.921  1.00  8.90           C  
ATOM   2679  C   GLN A 351      39.421  31.721  24.111  1.00  8.16           C  
ATOM   2680  O   GLN A 351      40.362  30.927  24.198  1.00  7.54           O  
ATOM   2681  CB  GLN A 351      38.786  32.762  21.916  1.00 11.46           C  
ATOM   2682  CG  GLN A 351      40.087  32.548  21.194  1.00 16.00           C  
ATOM   2683  CD  GLN A 351      40.149  33.349  19.917  1.00 19.19           C  
ATOM   2684  OE1 GLN A 351      40.105  34.578  19.936  1.00 23.84           O  
ATOM   2685  NE2 GLN A 351      40.234  32.658  18.799  1.00 20.26           N  
ATOM   2686  N   ASP A 352      39.171  32.658  25.021  1.00  7.55           N  
ATOM   2687  CA  ASP A 352      39.975  32.799  26.234  1.00  6.66           C  
ATOM   2688  C   ASP A 352      39.937  31.482  27.001  1.00  6.09           C  
ATOM   2689  O   ASP A 352      40.971  30.979  27.433  1.00  7.21           O  
ATOM   2690  CB  ASP A 352      39.431  33.928  27.119  1.00  6.01           C  
ATOM   2691  CG  ASP A 352      39.785  35.313  26.599  1.00  3.50           C  
ATOM   2692  OD1 ASP A 352      40.516  35.424  25.599  1.00  8.80           O  
ATOM   2693  OD2 ASP A 352      39.344  36.307  27.204  1.00  6.43           O  
ATOM   2694  N   PHE A 353      38.743  30.916  27.151  1.00  5.57           N  
ATOM   2695  CA  PHE A 353      38.594  29.649  27.849  1.00  6.79           C  
ATOM   2696  C   PHE A 353      39.462  28.578  27.192  1.00  8.25           C  
ATOM   2697  O   PHE A 353      40.042  27.738  27.871  1.00  8.34           O  
ATOM   2698  CB  PHE A 353      37.130  29.193  27.856  1.00  7.63           C  
ATOM   2699  CG  PHE A 353      36.912  27.887  28.573  1.00  8.47           C  
ATOM   2700  CD1 PHE A 353      36.863  27.840  29.965  1.00 10.74           C  
ATOM   2701  CD2 PHE A 353      36.804  26.700  27.859  1.00  9.37           C  
ATOM   2702  CE1 PHE A 353      36.711  26.625  30.635  1.00 10.72           C  
ATOM   2703  CE2 PHE A 353      36.650  25.479  28.518  1.00  9.95           C  
ATOM   2704  CZ  PHE A 353      36.605  25.440  29.906  1.00 10.82           C  
ATOM   2705  N   PHE A 354      39.538  28.599  25.866  1.00  7.50           N  
ATOM   2706  CA  PHE A 354      40.352  27.623  25.156  1.00  7.77           C  
ATOM   2707  C   PHE A 354      41.772  28.115  24.902  1.00  8.52           C  
ATOM   2708  O   PHE A 354      42.439  27.690  23.954  1.00  9.71           O  
ATOM   2709  CB  PHE A 354      39.669  27.183  23.866  1.00  8.04           C  
ATOM   2710  CG  PHE A 354      38.668  26.077  24.068  1.00  9.67           C  
ATOM   2711  CD1 PHE A 354      39.090  24.750  24.175  1.00  8.81           C  
ATOM   2712  CD2 PHE A 354      37.307  26.359  24.180  1.00  8.48           C  
ATOM   2713  CE1 PHE A 354      38.169  23.719  24.394  1.00 11.70           C  
ATOM   2714  CE2 PHE A 354      36.378  25.333  24.400  1.00  8.54           C  
ATOM   2715  CZ  PHE A 354      36.814  24.012  24.507  1.00  9.73           C  
ATOM   2716  N   ASN A 355      42.214  29.032  25.754  1.00  8.81           N  
ATOM   2717  CA  ASN A 355      43.558  29.593  25.701  1.00 10.67           C  
ATOM   2718  C   ASN A 355      44.049  30.086  24.344  1.00 10.50           C  
ATOM   2719  O   ASN A 355      45.160  29.761  23.917  1.00 10.76           O  
ATOM   2720  CB  ASN A 355      44.549  28.599  26.309  1.00 12.91           C  
ATOM   2721  CG  ASN A 355      44.205  28.252  27.748  1.00 15.43           C  
ATOM   2722  OD1 ASN A 355      43.938  29.141  28.563  1.00 16.12           O  
ATOM   2723  ND2 ASN A 355      44.206  26.963  28.068  1.00 15.88           N  
ATOM   2724  N   GLY A 356      43.211  30.869  23.669  1.00  9.16           N  
ATOM   2725  CA  GLY A 356      43.585  31.430  22.383  1.00 10.05           C  
ATOM   2726  C   GLY A 356      43.344  30.595  21.140  1.00 10.63           C  
ATOM   2727  O   GLY A 356      43.659  31.042  20.038  1.00  9.98           O  
ATOM   2728  N   LYS A 357      42.790  29.395  21.298  1.00 10.23           N  
ATOM   2729  CA  LYS A 357      42.525  28.534  20.153  1.00  9.20           C  
ATOM   2730  C   LYS A 357      41.546  29.195  19.182  1.00 10.26           C  
ATOM   2731  O   LYS A 357      40.572  29.829  19.594  1.00 11.57           O  
ATOM   2732  CB  LYS A 357      41.979  27.179  20.602  1.00  9.99           C  
ATOM   2733  CG  LYS A 357      41.668  26.243  19.437  1.00 12.88           C  
ATOM   2734  CD  LYS A 357      41.312  24.838  19.884  1.00 16.57           C  
ATOM   2735  CE  LYS A 357      40.931  23.980  18.685  1.00 19.16           C  
ATOM   2736  NZ  LYS A 357      41.999  23.925  17.647  1.00 20.92           N  
ATOM   2737  N   GLU A 358      41.818  29.052  17.891  1.00 11.28           N  
ATOM   2738  CA  GLU A 358      40.964  29.629  16.867  1.00 13.74           C  
ATOM   2739  C   GLU A 358      39.589  28.987  16.804  1.00 11.51           C  
ATOM   2740  O   GLU A 358      39.437  27.785  17.040  1.00 10.30           O  
ATOM   2741  CB  GLU A 358      41.642  29.552  15.506  1.00 19.01           C  
ATOM   2742  CG  GLU A 358      42.686  30.628  15.317  1.00 27.44           C  
ATOM   2743  CD  GLU A 358      42.155  32.030  15.581  1.00 33.76           C  
ATOM   2744  OE1 GLU A 358      41.133  32.452  14.969  1.00 37.85           O  
ATOM   2745  OE2 GLU A 358      42.778  32.742  16.406  1.00 35.31           O  
ATOM   2746  N   LEU A 359      38.590  29.808  16.503  1.00 10.32           N  
ATOM   2747  CA  LEU A 359      37.212  29.355  16.398  1.00 10.42           C  
ATOM   2748  C   LEU A 359      36.838  29.232  14.926  1.00 11.47           C  
ATOM   2749  O   LEU A 359      37.294  30.026  14.099  1.00 11.28           O  
ATOM   2750  CB  LEU A 359      36.277  30.365  17.073  1.00 10.07           C  
ATOM   2751  CG  LEU A 359      36.634  30.812  18.497  1.00 10.62           C  
ATOM   2752  CD1 LEU A 359      35.642  31.867  18.980  1.00 10.96           C  
ATOM   2753  CD2 LEU A 359      36.663  29.618  19.440  1.00 10.45           C  
ATOM   2754  N   ASN A 360      36.062  28.204  14.594  1.00  9.92           N  
ATOM   2755  CA  ASN A 360      35.596  28.005  13.224  1.00 10.04           C  
ATOM   2756  C   ASN A 360      34.362  28.883  13.135  1.00  9.29           C  
ATOM   2757  O   ASN A 360      33.327  28.541  13.714  1.00  9.70           O  
ATOM   2758  CB  ASN A 360      35.196  26.551  12.994  1.00 10.20           C  
ATOM   2759  CG  ASN A 360      36.379  25.660  12.717  1.00 14.14           C  
ATOM   2760  OD1 ASN A 360      36.355  24.862  11.779  1.00 18.25           O  
ATOM   2761  ND2 ASN A 360      37.411  25.765  13.539  1.00 14.49           N  
ATOM   2762  N   LYS A 361      34.489  30.034  12.483  1.00  7.62           N  
ATOM   2763  CA  LYS A 361      33.374  30.972  12.366  1.00  7.28           C  
ATOM   2764  C   LYS A 361      33.286  31.662  11.007  1.00  8.46           C  
ATOM   2765  O   LYS A 361      32.723  32.750  10.903  1.00 10.58           O  
ATOM   2766  CB  LYS A 361      33.455  32.023  13.479  1.00  7.60           C  
ATOM   2767  CG  LYS A 361      34.800  32.739  13.550  1.00  7.72           C  
ATOM   2768  CD  LYS A 361      34.817  33.807  14.629  1.00 11.28           C  
ATOM   2769  CE  LYS A 361      36.210  34.403  14.806  1.00 12.92           C  
ATOM   2770  NZ  LYS A 361      36.745  34.977  13.546  1.00 13.67           N  
ATOM   2771  N   SER A 362      33.845  31.040   9.972  1.00  7.78           N  
ATOM   2772  CA  SER A 362      33.805  31.607   8.624  1.00  8.20           C  
ATOM   2773  C   SER A 362      32.418  31.468   7.992  1.00  7.84           C  
ATOM   2774  O   SER A 362      32.046  32.256   7.126  1.00  8.84           O  
ATOM   2775  CB  SER A 362      34.856  30.944   7.740  1.00  7.52           C  
ATOM   2776  OG  SER A 362      34.814  29.542   7.894  1.00  8.17           O  
ATOM   2777  N   ILE A 363      31.676  30.441   8.394  1.00  7.73           N  
ATOM   2778  CA  ILE A 363      30.318  30.228   7.894  1.00  7.88           C  
ATOM   2779  C   ILE A 363      29.416  30.909   8.918  1.00  9.66           C  
ATOM   2780  O   ILE A 363      29.584  30.693  10.124  1.00  9.02           O  
ATOM   2781  CB  ILE A 363      29.949  28.716   7.846  1.00  6.24           C  
ATOM   2782  CG1 ILE A 363      30.876  27.969   6.882  1.00  6.35           C  
ATOM   2783  CG2 ILE A 363      28.491  28.535   7.439  1.00  7.33           C  
ATOM   2784  CD1 ILE A 363      30.713  26.468   6.893  1.00  5.64           C  
ATOM   2785  N   ASN A 364      28.512  31.771   8.454  1.00  8.11           N  
ATOM   2786  CA  ASN A 364      27.576  32.469   9.342  1.00  9.21           C  
ATOM   2787  C   ASN A 364      27.077  31.455  10.357  1.00  8.14           C  
ATOM   2788  O   ASN A 364      26.449  30.466   9.980  1.00  8.41           O  
ATOM   2789  CB  ASN A 364      26.396  32.999   8.539  1.00 13.31           C  
ATOM   2790  CG  ASN A 364      26.235  34.489   8.653  1.00 20.61           C  
ATOM   2791  OD1 ASN A 364      27.085  35.183   9.214  1.00 26.73           O  
ATOM   2792  ND2 ASN A 364      25.129  35.001   8.132  1.00 22.46           N  
ATOM   2793  N   PRO A 365      27.327  31.684  11.658  1.00  7.66           N  
ATOM   2794  CA  PRO A 365      26.891  30.740  12.678  1.00  7.16           C  
ATOM   2795  C   PRO A 365      25.443  30.264  12.598  1.00  8.04           C  
ATOM   2796  O   PRO A 365      25.176  29.073  12.762  1.00  8.52           O  
ATOM   2797  CB  PRO A 365      27.201  31.474  13.978  1.00  8.03           C  
ATOM   2798  CG  PRO A 365      28.436  32.250  13.616  1.00  7.96           C  
ATOM   2799  CD  PRO A 365      28.031  32.826  12.281  1.00  6.56           C  
ATOM   2800  N   ASP A 366      24.514  31.168  12.320  1.00  8.09           N  
ATOM   2801  CA  ASP A 366      23.112  30.765  12.239  1.00  8.60           C  
ATOM   2802  C   ASP A 366      22.763  30.021  10.945  1.00  8.45           C  
ATOM   2803  O   ASP A 366      21.623  29.627  10.735  1.00  9.10           O  
ATOM   2804  CB  ASP A 366      22.182  31.966  12.462  1.00  9.84           C  
ATOM   2805  CG  ASP A 366      22.349  33.062  11.415  1.00 12.59           C  
ATOM   2806  OD1 ASP A 366      23.148  32.913  10.463  1.00 18.13           O  
ATOM   2807  OD2 ASP A 366      21.664  34.094  11.551  1.00 10.72           O  
ATOM   2808  N   GLU A 367      23.754  29.833  10.080  1.00  7.23           N  
ATOM   2809  CA  GLU A 367      23.544  29.137   8.814  1.00  6.86           C  
ATOM   2810  C   GLU A 367      24.290  27.804   8.721  1.00  7.75           C  
ATOM   2811  O   GLU A 367      24.002  26.992   7.837  1.00  7.38           O  
ATOM   2812  CB  GLU A 367      23.965  30.037   7.645  1.00  7.52           C  
ATOM   2813  CG  GLU A 367      23.139  31.305   7.491  1.00  6.03           C  
ATOM   2814  CD  GLU A 367      23.701  32.259   6.448  1.00 10.70           C  
ATOM   2815  OE1 GLU A 367      24.505  31.838   5.591  1.00 11.25           O  
ATOM   2816  OE2 GLU A 367      23.339  33.446   6.487  1.00 14.25           O  
ATOM   2817  N   ALA A 368      25.233  27.584   9.638  1.00  7.44           N  
ATOM   2818  CA  ALA A 368      26.062  26.372   9.659  1.00  7.82           C  
ATOM   2819  C   ALA A 368      25.303  25.039   9.623  1.00  7.76           C  
ATOM   2820  O   ALA A 368      25.685  24.121   8.889  1.00  7.02           O  
ATOM   2821  CB  ALA A 368      27.015  26.412  10.850  1.00  7.13           C  
ATOM   2822  N   VAL A 369      24.228  24.937  10.402  1.00  6.27           N  
ATOM   2823  CA  VAL A 369      23.419  23.717  10.444  1.00  6.97           C  
ATOM   2824  C   VAL A 369      22.753  23.445   9.085  1.00  7.17           C  
ATOM   2825  O   VAL A 369      22.821  22.328   8.567  1.00  8.29           O  
ATOM   2826  CB  VAL A 369      22.345  23.790  11.567  1.00  6.61           C  
ATOM   2827  CG1 VAL A 369      21.397  22.604  11.480  1.00  7.02           C  
ATOM   2828  CG2 VAL A 369      23.020  23.801  12.937  1.00  7.20           C  
ATOM   2829  N   ALA A 370      22.119  24.462   8.507  1.00  6.26           N  
ATOM   2830  CA  ALA A 370      21.466  24.304   7.208  1.00  6.69           C  
ATOM   2831  C   ALA A 370      22.507  23.970   6.136  1.00  7.37           C  
ATOM   2832  O   ALA A 370      22.269  23.142   5.250  1.00  7.81           O  
ATOM   2833  CB  ALA A 370      20.708  25.576   6.837  1.00  8.10           C  
ATOM   2834  N   TYR A 371      23.670  24.609   6.248  1.00  8.62           N  
ATOM   2835  CA  TYR A 371      24.793  24.422   5.332  1.00  7.23           C  
ATOM   2836  C   TYR A 371      25.173  22.945   5.300  1.00  5.02           C  
ATOM   2837  O   TYR A 371      25.199  22.328   4.235  1.00  6.92           O  
ATOM   2838  CB  TYR A 371      25.971  25.272   5.819  1.00  8.20           C  
ATOM   2839  CG  TYR A 371      27.103  25.469   4.833  1.00  6.77           C  
ATOM   2840  CD1 TYR A 371      27.881  24.393   4.398  1.00  8.48           C  
ATOM   2841  CD2 TYR A 371      27.432  26.746   4.379  1.00  7.52           C  
ATOM   2842  CE1 TYR A 371      28.968  24.588   3.545  1.00  9.11           C  
ATOM   2843  CE2 TYR A 371      28.519  26.954   3.530  1.00  9.96           C  
ATOM   2844  CZ  TYR A 371      29.284  25.870   3.117  1.00  9.57           C  
ATOM   2845  OH  TYR A 371      30.381  26.081   2.302  1.00 10.21           O  
ATOM   2846  N   GLY A 372      25.430  22.371   6.472  1.00  6.28           N  
ATOM   2847  CA  GLY A 372      25.788  20.966   6.550  1.00  5.74           C  
ATOM   2848  C   GLY A 372      24.662  20.051   6.097  1.00  8.20           C  
ATOM   2849  O   GLY A 372      24.903  19.022   5.449  1.00  7.77           O  
ATOM   2850  N   ALA A 373      23.430  20.416   6.450  1.00  8.08           N  
ATOM   2851  CA  ALA A 373      22.253  19.641   6.072  1.00  8.21           C  
ATOM   2852  C   ALA A 373      22.121  19.575   4.547  1.00  8.01           C  
ATOM   2853  O   ALA A 373      21.775  18.529   4.001  1.00  7.77           O  
ATOM   2854  CB  ALA A 373      20.998  20.243   6.700  1.00  7.31           C  
ATOM   2855  N   ALA A 374      22.422  20.684   3.870  1.00  7.21           N  
ATOM   2856  CA  ALA A 374      22.354  20.756   2.409  1.00  9.47           C  
ATOM   2857  C   ALA A 374      23.409  19.836   1.792  1.00 10.17           C  
ATOM   2858  O   ALA A 374      23.144  19.129   0.814  1.00 10.13           O  
ATOM   2859  CB  ALA A 374      22.561  22.182   1.946  1.00  8.90           C  
ATOM   2860  N   VAL A 375      24.604  19.836   2.371  1.00 11.94           N  
ATOM   2861  CA  VAL A 375      25.684  18.972   1.887  1.00 12.83           C  
ATOM   2862  C   VAL A 375      25.260  17.505   2.005  1.00 11.66           C  
ATOM   2863  O   VAL A 375      25.322  16.747   1.035  1.00 12.10           O  
ATOM   2864  CB  VAL A 375      26.996  19.198   2.683  1.00 11.00           C  
ATOM   2865  CG1 VAL A 375      28.042  18.153   2.297  1.00 12.91           C  
ATOM   2866  CG2 VAL A 375      27.526  20.600   2.422  1.00 11.04           C  
ATOM   2867  N   GLN A 376      24.777  17.127   3.182  1.00 11.05           N  
ATOM   2868  CA  GLN A 376      24.341  15.758   3.426  1.00 13.35           C  
ATOM   2869  C   GLN A 376      23.175  15.377   2.515  1.00 13.17           C  
ATOM   2870  O   GLN A 376      23.101  14.246   2.030  1.00 14.55           O  
ATOM   2871  CB  GLN A 376      23.957  15.583   4.901  1.00 14.63           C  
ATOM   2872  CG  GLN A 376      23.924  14.136   5.370  1.00 17.93           C  
ATOM   2873  CD  GLN A 376      25.235  13.397   5.130  1.00 19.64           C  
ATOM   2874  OE1 GLN A 376      25.242  12.183   4.942  1.00 25.73           O  
ATOM   2875  NE2 GLN A 376      26.346  14.125   5.127  1.00 16.79           N  
ATOM   2876  N   ALA A 377      22.284  16.332   2.261  1.00 12.06           N  
ATOM   2877  CA  ALA A 377      21.129  16.104   1.397  1.00 11.77           C  
ATOM   2878  C   ALA A 377      21.602  15.754  -0.008  1.00 13.32           C  
ATOM   2879  O   ALA A 377      21.090  14.822  -0.628  1.00 13.53           O  
ATOM   2880  CB  ALA A 377      20.246  17.337   1.357  1.00 10.95           C  
ATOM   2881  N   ALA A 378      22.598  16.487  -0.496  1.00 15.16           N  
ATOM   2882  CA  ALA A 378      23.147  16.247  -1.829  1.00 16.08           C  
ATOM   2883  C   ALA A 378      23.819  14.881  -1.888  1.00 16.99           C  
ATOM   2884  O   ALA A 378      23.735  14.191  -2.897  1.00 19.56           O  
ATOM   2885  CB  ALA A 378      24.137  17.340  -2.196  1.00 16.08           C  
ATOM   2886  N   ILE A 379      24.482  14.499  -0.802  1.00 17.37           N  
ATOM   2887  CA  ILE A 379      25.154  13.206  -0.726  1.00 19.87           C  
ATOM   2888  C   ILE A 379      24.140  12.063  -0.761  1.00 21.77           C  
ATOM   2889  O   ILE A 379      24.374  11.027  -1.387  1.00 22.14           O  
ATOM   2890  CB  ILE A 379      25.996  13.093   0.560  1.00 19.47           C  
ATOM   2891  CG1 ILE A 379      27.163  14.080   0.501  1.00 20.39           C  
ATOM   2892  CG2 ILE A 379      26.505  11.665   0.746  1.00 21.46           C  
ATOM   2893  CD1 ILE A 379      28.004  14.119   1.752  1.00 18.80           C  
ATOM   2894  N   LEU A 380      23.024  12.246  -0.064  1.00 21.64           N  
ATOM   2895  CA  LEU A 380      21.984  11.229  -0.019  1.00 23.17           C  
ATOM   2896  C   LEU A 380      21.112  11.211  -1.273  1.00 27.70           C  
ATOM   2897  O   LEU A 380      20.268  10.322  -1.427  1.00 30.56           O  
ATOM   2898  CB  LEU A 380      21.102  11.427   1.213  1.00 20.46           C  
ATOM   2899  CG  LEU A 380      21.759  11.389   2.592  1.00 17.31           C  
ATOM   2900  CD1 LEU A 380      20.708  11.671   3.652  1.00 16.51           C  
ATOM   2901  CD2 LEU A 380      22.420  10.044   2.832  1.00 17.04           C  
ATOM   2902  N   SER A 381      21.280  12.210  -2.136  1.00 31.08           N  
ATOM   2903  CA  SER A 381      20.510  12.304  -3.376  1.00 34.47           C  
ATOM   2904  C   SER A 381      21.107  11.449  -4.492  1.00 36.28           C  
ATOM   2905  O   SER A 381      20.309  10.841  -5.242  1.00 38.60           O  
ATOM   2906  CB  SER A 381      20.426  13.755  -3.846  1.00 35.05           C  
ATOM   2907  OG  SER A 381      19.519  14.499  -3.053  1.00 39.37           O  
TER    2908      SER A 381                                                      
HETATM 2909 MG    MG A 487      19.809  26.562  15.776  1.00 16.94          MG  
HETATM 2910 NA    NA A 491      20.923  26.211  20.073  1.00 31.27          NA  
HETATM 2911 CL    CL A 451      35.707  25.282   5.886  1.00 14.96          CL  
HETATM 2912 CL    CL A 455       9.087  34.347   2.482  1.00 12.82          CL  
HETATM 2913  PB  ADP A 486      17.674  28.914  16.448  1.00 11.56           P  
HETATM 2914  O1B ADP A 486      18.372  28.141  15.409  1.00 10.66           O  
HETATM 2915  O2B ADP A 486      16.263  29.210  16.123  1.00 11.50           O  
HETATM 2916  O3B ADP A 486      17.921  28.442  17.835  1.00 14.18           O  
HETATM 2917  PA  ADP A 486      19.449  31.115  15.695  1.00  8.49           P  
HETATM 2918  O1A ADP A 486      20.718  30.355  15.825  1.00  6.96           O  
HETATM 2919  O2A ADP A 486      18.989  31.580  14.377  1.00 11.30           O  
HETATM 2920  O3A ADP A 486      18.300  30.368  16.504  1.00 10.01           O  
HETATM 2921  O5' ADP A 486      19.665  32.460  16.527  1.00  9.45           O  
HETATM 2922  C5' ADP A 486      18.658  33.468  16.706  1.00  6.78           C  
HETATM 2923  C4' ADP A 486      19.199  34.457  17.704  1.00  8.81           C  
HETATM 2924  O4' ADP A 486      20.427  34.991  17.188  1.00  8.48           O  
HETATM 2925  C3' ADP A 486      18.250  35.613  17.973  1.00  6.88           C  
HETATM 2926  O3' ADP A 486      18.229  35.772  19.374  1.00  8.41           O  
HETATM 2927  C2' ADP A 486      18.963  36.729  17.262  1.00  7.78           C  
HETATM 2928  O2' ADP A 486      18.712  37.988  17.852  1.00  6.25           O  
HETATM 2929  C1' ADP A 486      20.419  36.394  17.433  1.00  7.46           C  
HETATM 2930  N9  ADP A 486      21.289  37.029  16.426  1.00  9.71           N  
HETATM 2931  C8  ADP A 486      21.284  36.917  15.045  1.00  9.38           C  
HETATM 2932  N7  ADP A 486      22.217  37.613  14.444  1.00  8.55           N  
HETATM 2933  C5  ADP A 486      22.885  38.228  15.490  1.00  9.11           C  
HETATM 2934  C6  ADP A 486      23.975  39.098  15.519  1.00 10.85           C  
HETATM 2935  N6  ADP A 486      24.541  39.604  14.416  1.00 11.33           N  
HETATM 2936  N1  ADP A 486      24.391  39.499  16.725  1.00  9.70           N  
HETATM 2937  C2  ADP A 486      23.773  39.089  17.814  1.00 10.21           C  
HETATM 2938  N3  ADP A 486      22.735  38.286  17.930  1.00  8.54           N  
HETATM 2939  C4  ADP A 486      22.335  37.883  16.701  1.00 10.59           C  
HETATM 2940  O   HOH A 504       9.707  26.417  17.173  1.00  4.97           O  
HETATM 2941  O   HOH A 506      13.854  36.884   9.009  1.00 11.28           O  
HETATM 2942  O   HOH A 507      10.192  30.446  19.025  1.00 12.68           O  
HETATM 2943  O   HOH A 508      25.010  30.832   0.385  1.00 15.20           O  
HETATM 2944  O   HOH A 509      18.080  23.405  21.139  1.00 18.99           O  
HETATM 2945  O   HOH A 510      35.561  21.372  35.359  1.00 38.91           O  
HETATM 2946  O   HOH A 511      30.159  22.776  35.139  1.00 23.33           O  
HETATM 2947  O   HOH A 512      -8.566  34.940  20.034  1.00 69.16           O  
HETATM 2948  O   HOH A 513      14.397  20.618  14.347  1.00  6.63           O  
HETATM 2949  O   HOH A 514      17.172  22.218  13.045  1.00  7.87           O  
HETATM 2950  O   HOH A 515      10.298  18.906  21.756  1.00  9.36           O  
HETATM 2951  O   HOH A 517      -2.674  13.543  29.909  1.00 28.60           O  
HETATM 2952  O   HOH A 518      -5.268  18.820  14.200  1.00 11.11           O  
HETATM 2953  O   HOH A 520      13.791  17.364  -4.361  1.00 18.90           O  
HETATM 2954  O   HOH A 521      15.985   9.480   9.713  1.00 10.16           O  
HETATM 2955  O   HOH A 522      23.246  12.581  12.830  1.00  6.89           O  
HETATM 2956  O   HOH A 524      35.847  21.133   3.141  1.00 16.55           O  
HETATM 2957  O   HOH A 525      10.524  24.928  14.922  1.00  8.42           O  
HETATM 2958  O   HOH A 526      42.993  11.077   4.675  1.00 15.86           O  
HETATM 2959  O   HOH A 527      24.510  28.525  31.079  1.00 50.10           O  
HETATM 2960  O   HOH A 529      12.428  40.180  18.391  1.00 27.37           O  
HETATM 2961  O   HOH A 530       1.709  52.630  18.171  1.00 47.53           O  
HETATM 2962  O   HOH A 532      30.158  41.913  22.443  1.00 10.10           O  
HETATM 2963  O   HOH A 533      40.195  21.039  30.633  1.00 17.69           O  
HETATM 2964  O   HOH A 534      24.801  52.934  26.639  1.00 11.47           O  
HETATM 2965  O   HOH A 535      38.716  25.573  16.036  1.00 14.02           O  
HETATM 2966  O   HOH A 536      30.125  28.727  11.905  1.00  9.70           O  
HETATM 2967  O   HOH A 537      37.246  35.921  28.836  1.00  8.32           O  
HETATM 2968  O   HOH A 538      38.854  32.692  16.558  1.00 29.18           O  
HETATM 2969  O   HOH A 539      37.517  35.667  18.209  1.00 47.27           O  
HETATM 2970  O   HOH A 540      41.623  29.437  30.333  1.00  9.98           O  
HETATM 2971  O   HOH A 541      46.703  26.749  23.344  1.00 39.86           O  
HETATM 2972  O   HOH A 544      25.840  41.986  19.920  1.00  9.48           O  
HETATM 2973  O   HOH A 546      23.882  22.313  18.070  1.00  9.14           O  
HETATM 2974  O   HOH A 547      21.821  37.233  20.536  1.00  6.71           O  
HETATM 2975  O   HOH A 548       0.362  27.947  27.015  1.00 15.37           O  
HETATM 2976  O   HOH A 549      16.853  49.481  16.911  1.00 17.98           O  
HETATM 2977  O   HOH A 550      25.830  21.882  19.982  1.00  8.37           O  
HETATM 2978  O   HOH A 551      21.202  21.904  18.832  1.00 14.14           O  
HETATM 2979  O   HOH A 552      32.410  24.717  -1.455  1.00 41.07           O  
HETATM 2980  O   HOH A 553      12.423  30.233  22.768  1.00 12.86           O  
HETATM 2981  O   HOH A 554      33.216  44.495  28.613  1.00 24.78           O  
HETATM 2982  O   HOH A 555       9.778  22.092  15.313  1.00  5.45           O  
HETATM 2983  O   HOH A 556       7.337  27.313  16.077  1.00  5.73           O  
HETATM 2984  O   HOH A 558      21.466  26.863  10.008  1.00  6.12           O  
HETATM 2985  O   HOH A 559      13.180  39.120  21.607  1.00 24.19           O  
HETATM 2986  O   HOH A 560      21.315  27.770  16.563  1.00 11.04           O  
HETATM 2987  O   HOH A 561      21.129  24.805  16.005  1.00 10.13           O  
HETATM 2988  O   HOH A 562      18.446  25.153  15.002  1.00  8.40           O  
HETATM 2989  O   HOH A 563      20.701  26.906  13.879  1.00 12.00           O  
HETATM 2990  O   HOH A 564      19.385  26.193  17.597  0.00 38.99           O  
HETATM 2991  O   HOH A 565      22.192  19.444  19.710  1.00 12.75           O  
HETATM 2992  O   HOH A 566      22.719  20.133  24.407  1.00 10.94           O  
HETATM 2993  O   HOH A 567      23.361  19.160  22.012  1.00 11.71           O  
HETATM 2994  O   HOH A 568      21.461  20.263  -1.027  1.00 13.56           O  
HETATM 2995  O   HOH A 569      11.789  20.024  15.334  1.00  7.40           O  
HETATM 2996  O   HOH A 570       7.920  25.265  14.081  1.00  6.81           O  
HETATM 2997  O   HOH A 571      29.583  30.102   0.966  1.00  9.41           O  
HETATM 2998  O   HOH A 572      17.105  30.227   4.518  1.00  5.54           O  
HETATM 2999  O   HOH A 573      23.126  27.203  12.299  1.00  6.33           O  
HETATM 3000  O   HOH A 574       2.096  34.999   5.395  1.00 21.54           O  
HETATM 3001  O   HOH A 575      -5.037  39.201   8.715  1.00 10.04           O  
HETATM 3002  O   HOH A 576       2.420  35.088  20.364  1.00 14.98           O  
HETATM 3003  O   HOH A 577      -4.431  30.727  21.787  1.00 12.15           O  
HETATM 3004  O   HOH A 578      -4.208  38.101  20.025  1.00 19.50           O  
HETATM 3005  O   HOH A 579      16.875  25.306  17.844  1.00 25.72           O  
HETATM 3006  O   HOH A 580      19.835  23.227  25.280  1.00 23.41           O  
HETATM 3007  O   HOH A 581      15.322  31.351  26.289  1.00 25.65           O  
HETATM 3008  O   HOH A 582       3.735  51.786  20.868  1.00 35.79           O  
HETATM 3009  O   HOH A 583      28.393  37.784   7.882  1.00 20.22           O  
HETATM 3010  O   HOH A 584      30.664  34.383   9.942  1.00 15.95           O  
HETATM 3011  O   HOH A 585      43.298  31.892  28.606  1.00  8.66           O  
HETATM 3012  O   HOH A 586      10.492  32.961  19.552  1.00 17.10           O  
HETATM 3013  O   HOH A 587      16.122  37.337  19.918  1.00 11.92           O  
HETATM 3014  O   HOH A 590      21.908  34.439   8.400  1.00 14.09           O  
HETATM 3015  O   HOH A 591      25.377  29.745  -4.000  1.00 40.11           O  
HETATM 3016  O   HOH A 592      13.553  32.470  -2.449  1.00 13.62           O  
HETATM 3017  O   HOH A 593      -2.525  40.616  12.680  1.00 16.77           O  
HETATM 3018  O   HOH A 594      17.997  10.851  13.640  1.00 11.27           O  
HETATM 3019  O   HOH A 596      20.327  21.063  27.275  1.00 25.65           O  
HETATM 3020  O   HOH A 597      17.907  18.988  27.092  1.00 54.25           O  
HETATM 3021  O   HOH A 598      14.603  14.685  24.633  1.00 22.05           O  
HETATM 3022  O   HOH A 599      12.099  34.417  15.578  1.00 21.36           O  
HETATM 3023  O   HOH A 602      10.773  39.084  10.779  1.00 28.36           O  
HETATM 3024  O   HOH A 606      31.456  20.868   3.235  1.00 32.31           O  
HETATM 3025  O   HOH A 609      26.813  30.179   4.670  1.00 12.72           O  
HETATM 3026  O   HOH A 611      19.196  33.258  -2.149  1.00 17.89           O  
HETATM 3027  O   HOH A 612       8.863  34.442   5.823  1.00 12.35           O  
HETATM 3028  O   HOH A 614      24.195  38.219   3.454  1.00 40.46           O  
HETATM 3029  O   HOH A 615      19.564  37.770   5.641  1.00 13.53           O  
HETATM 3030  O   HOH A 617      15.705  38.711   9.903  1.00 20.70           O  
HETATM 3031  O   HOH A 618      17.741  36.844   8.234  1.00 14.76           O  
HETATM 3032  O   HOH A 620       7.197  36.264  20.750  1.00 33.91           O  
HETATM 3033  O   HOH A 625       7.179  47.954   5.685  1.00 30.71           O  
HETATM 3034  O   HOH A 627       8.104  46.425  16.167  1.00 28.34           O  
HETATM 3035  O   HOH A 632       7.861  40.636   1.112  1.00 32.89           O  
HETATM 3036  O   HOH A 633       4.678  42.075   7.154  1.00 14.22           O  
HETATM 3037  O   HOH A 635      -1.554  42.757  22.818  1.00 24.94           O  
HETATM 3038  O   HOH A 636       2.335  49.435  13.700  1.00 28.84           O  
HETATM 3039  O   HOH A 638      -6.700  42.846  14.744  1.00 13.81           O  
HETATM 3040  O   HOH A 645      -8.587  19.469  15.102  1.00 34.17           O  
HETATM 3041  O   HOH A 651      14.138   7.638  22.226  1.00 17.26           O  
HETATM 3042  O   HOH A 653      10.817   8.475  22.417  1.00 13.01           O  
HETATM 3043  O   HOH A 654      25.291  12.381  14.870  1.00 14.04           O  
HETATM 3044  O   HOH A 655      36.980  18.955  -1.823  1.00 31.22           O  
HETATM 3045  O   HOH A 656      31.912  17.976   4.322  1.00 44.22           O  
HETATM 3046  O   HOH A 658      40.015  17.634  10.460  1.00 21.39           O  
HETATM 3047  O   HOH A 659      40.557  21.178   7.477  1.00 20.52           O  
HETATM 3048  O   HOH A 663      45.595  10.592   6.289  1.00 19.72           O  
HETATM 3049  O   HOH A 664      37.863  20.832   0.305  1.00 27.47           O  
HETATM 3050  O   HOH A 665      38.690  15.880   0.123  1.00  7.36           O  
HETATM 3051  O   HOH A 669      24.580  31.743  31.327  1.00 12.31           O  
HETATM 3052  O   HOH A 672      17.915  23.046  30.063  1.00 19.57           O  
HETATM 3053  O   HOH A 673      25.085  20.933  36.355  1.00 29.69           O  
HETATM 3054  O   HOH A 678      18.717  44.618  32.558  1.00 11.70           O  
HETATM 3055  O   HOH A 679      21.199  43.575  33.621  1.00 18.93           O  
HETATM 3056  O   HOH A 680      23.040  45.659  34.776  1.00 21.38           O  
HETATM 3057  O   HOH A 681      20.007  48.950  33.547  1.00 19.37           O  
HETATM 3058  O   HOH A 686      -1.624  50.201  23.089  1.00 32.32           O  
HETATM 3059  O   HOH A 694       9.357  53.925  15.065  1.00 23.55           O  
HETATM 3060  O   HOH A 696      22.505  52.171  14.763  1.00 14.36           O  
HETATM 3061  O   HOH A 697      27.195  40.850  13.039  1.00 11.16           O  
HETATM 3062  O   HOH A 698      28.024  43.170  21.128  1.00  7.79           O  
HETATM 3063  O   HOH A 699      30.738  39.004  14.844  1.00 22.21           O  
HETATM 3064  O   HOH A 700      35.175  43.370  17.283  1.00 62.25           O  
HETATM 3065  O   HOH A 702      31.427  50.446  23.780  1.00 11.07           O  
HETATM 3066  O   HOH A 703      24.844  33.989  12.472  1.00 23.31           O  
HETATM 3067  O   HOH A 705       6.417  40.588   5.151  1.00 35.98           O  
HETATM 3068  O   HOH A 706       1.745  55.896  21.683  1.00 28.71           O  
HETATM 3069  O   HOH A 708      30.745  38.553  30.377  1.00 16.14           O  
HETATM 3070  O   HOH A 712      31.975  36.474  13.810  1.00 22.25           O  
HETATM 3071  O   HOH A 713      39.063  39.725  16.558  1.00 67.21           O  
HETATM 3072  O   HOH A 715      38.425  35.461  10.726  1.00 22.22           O  
HETATM 3073  O   HOH A 717       2.108  40.738   8.454  1.00 19.99           O  
HETATM 3074  O   HOH A 721      10.288  48.621  17.041  1.00 28.55           O  
HETATM 3075  O   HOH A 723      15.110  51.501  16.522  1.00 14.65           O  
HETATM 3076  O   HOH A 724       2.363  50.361  31.734  1.00 24.26           O  
HETATM 3077  O   HOH A 725       8.863  52.883  31.117  1.00 15.81           O  
HETATM 3078  O   HOH A 727      40.340  35.878  22.714  1.00 26.75           O  
HETATM 3079  O   HOH A 728      43.756  21.306  15.257  1.00 29.61           O  
HETATM 3080  O   HOH A 729      44.738  24.494  26.374  1.00 23.31           O  
HETATM 3081  O   HOH A 730      16.921  43.002  33.878  1.00 20.76           O  
HETATM 3082  O   HOH A 731      18.132  47.001  33.801  1.00 18.95           O  
HETATM 3083  O   HOH A 732      13.090  48.074  34.206  1.00 19.93           O  
HETATM 3084  O   HOH A 733      18.269  52.636  32.246  1.00 14.38           O  
HETATM 3085  O   HOH A 734      13.934  54.407  36.220  1.00 15.76           O  
HETATM 3086  O   HOH A 735      15.133  36.228  30.306  1.00 30.38           O  
HETATM 3087  O   HOH A 737      29.972  40.967  29.276  1.00 11.41           O  
HETATM 3088  O   HOH A 738      31.043  52.884  22.241  1.00 31.60           O  
HETATM 3089  O   HOH A 739      19.588  49.918  16.633  1.00 22.99           O  
HETATM 3090  O   HOH A 740      25.604  52.004  14.725  1.00 31.20           O  
HETATM 3091  O   HOH A 741       9.060  12.154   4.540  1.00 13.58           O  
HETATM 3092  O   HOH A 742       4.273  16.350  18.356  1.00 13.82           O  
HETATM 3093  O   HOH A 743      -8.036  34.911  14.754  1.00 12.51           O  
HETATM 3094  O   HOH A 744     -10.539  34.537  14.225  1.00 22.26           O  
HETATM 3095  O   HOH A 745      -7.820  39.107  13.711  1.00  6.91           O  
HETATM 3096  O   HOH A 746      -7.331  39.951   4.907  1.00 14.97           O  
HETATM 3097  O   HOH A 748      -7.362  22.763  12.916  1.00 40.94           O  
HETATM 3098  O   HOH A 750      -6.597  20.879  27.996  1.00 18.18           O  
HETATM 3099  O   HOH A 751       7.255  22.235  26.133  1.00 13.63           O  
HETATM 3100  O   HOH A 752      10.323  24.322  30.235  1.00 23.59           O  
HETATM 3101  O   HOH A 753      10.007  21.455  34.570  1.00  4.22           O  
HETATM 3102  O   HOH A 754      11.527  23.741  26.544  1.00  9.05           O  
HETATM 3103  O   HOH A 755      10.298  31.487  24.239  1.00 20.27           O  
HETATM 3104  O   HOH A 756       0.392  31.600  29.971  1.00 52.78           O  
HETATM 3105  O   HOH A 757       8.004  28.931  28.011  1.00 29.87           O  
HETATM 3106  O   HOH A 758      -2.138  27.071  27.828  1.00 18.37           O  
HETATM 3107  O   HOH A 759      -8.411  19.220  21.000  1.00 30.73           O  
HETATM 3108  O   HOH A 760      -5.070  42.494   5.519  1.00 43.11           O  
HETATM 3109  O   HOH A 761      27.792   8.984  11.696  1.00 23.15           O  
HETATM 3110  O   HOH A 764      19.364  10.746  21.521  1.00 42.86           O  
HETATM 3111  O   HOH A 765      26.215   8.970  19.062  1.00 20.38           O  
HETATM 3112  O   HOH A 767      29.102  28.733  -1.275  1.00 28.64           O  
HETATM 3113  O   HOH A 769      17.939  35.654  12.318  1.00 15.52           O  
HETATM 3114  O   HOH A 770       7.793  29.149  -4.286  1.00 14.22           O  
HETATM 3115  O   HOH A 771       6.489  31.549   0.189  1.00 25.27           O  
HETATM 3116  O   HOH A 772       3.363  33.005   5.031  1.00 67.95           O  
HETATM 3117  O   HOH A 773       3.975  29.327   3.121  1.00 18.11           O  
HETATM 3118  O   HOH A 774       6.448  35.972   5.448  1.00 10.87           O  
HETATM 3119  O   HOH A 775      13.157  34.089  19.670  1.00 70.11           O  
HETATM 3120  O   HOH A 777      37.163  26.781  36.008  1.00 34.33           O  
HETATM 3121  O   HOH A 778      38.155  24.085  33.257  1.00 17.75           O  
HETATM 3122  O   HOH A 779      37.667  22.242  31.395  1.00 15.69           O  
HETATM 3123  O   HOH A 781       7.106  32.743  25.392  1.00 38.78           O  
HETATM 3124  O   HOH A 782      -6.797  37.125  15.660  1.00 23.30           O  
HETATM 3125  O   HOH A 783      -5.161  40.578  13.073  1.00 26.45           O  
HETATM 3126  O   HOH A 785      25.060  21.878 -14.753  1.00  7.73           O  
HETATM 3127  O   HOH A 786       1.098  55.791  32.215  1.00 39.86           O  
HETATM 3128  O   HOH A 787       8.716  25.422  -9.281  1.00 27.87           O  
HETATM 3129  O   HOH A 788       6.172  21.339 -10.864  1.00 15.95           O  
HETATM 3130  O   HOH A 789       3.157  27.534   5.070  1.00 22.01           O  
HETATM 3131  O   HOH A 790      36.146  20.223  32.193  1.00 14.41           O  
HETATM 3132  O   HOH A 791      37.695  17.979  31.628  1.00 26.05           O  
HETATM 3133  O   HOH A 792      21.717  18.661  26.568  1.00 28.87           O  
HETATM 3134  O   HOH A 793      34.921  32.626  34.074  1.00 14.37           O  
HETATM 3135  O   HOH A 794      33.140  31.734  36.068  1.00 27.13           O  
HETATM 3136  O   HOH A 795      41.446  10.951  26.979  1.00 37.27           O  
HETATM 3137  O   HOH A 796      42.028  22.737  22.384  1.00 25.81           O  
HETATM 3138  O   HOH A 797      44.560  27.936  17.438  1.00 32.02           O  
HETATM 3139  O   HOH A 798      24.288  37.803   6.629  1.00 36.15           O  
HETATM 3140  O   HOH A 799      22.985  40.052  11.604  1.00 19.84           O  
HETATM 3141  O   HOH A 800      33.858  38.444  15.284  1.00 44.60           O  
HETATM 3142  O   HOH A 801      35.860  39.162  20.211  1.00 22.51           O  
HETATM 3143  O   HOH A 802      35.155  34.993  32.962  1.00 13.51           O  
HETATM 3144  O   HOH A 803      29.488  31.314  35.545  1.00 32.81           O  
HETATM 3145  O   HOH A 804      31.412  30.448  34.074  1.00 22.28           O  
HETATM 3146  O   HOH A 805      25.723  28.195  34.114  1.00 37.29           O  
HETATM 3147  O   HOH A 806      39.291  26.523  32.923  1.00 18.89           O  
HETATM 3148  O   HOH A 810      -1.125  28.225   4.359  1.00 26.69           O  
HETATM 3149  O   HOH A 812      31.311  46.093  30.060  1.00 30.60           O  
HETATM 3150  O   HOH A 813       0.247  54.361  24.701  1.00 51.75           O  
HETATM 3151  O   HOH A 814      -1.270  59.167  22.149  1.00 29.62           O  
HETATM 3152  O   HOH A 815       0.996  51.143  22.593  1.00 41.03           O  
HETATM 3153  O   HOH A 816      -3.849  51.096  24.946  1.00 54.68           O  
HETATM 3154  O   HOH A 818      -7.685  12.080  19.344  1.00 49.60           O  
HETATM 3155  O   HOH A 819      16.720  28.725  19.955  1.00 19.85           O  
HETATM 3156  O   HOH A 820       9.635  16.721  30.864  1.00 17.12           O  
HETATM 3157  O   HOH A 821      29.981  25.551  -0.205  1.00 26.57           O  
HETATM 3158  O   HOH A 822      36.164  22.208  -0.780  1.00 42.94           O  
HETATM 3159  O   HOH A 823      27.059  30.512   2.044  1.00 29.59           O  
HETATM 3160  O   HOH A 824      25.049  32.340  -1.701  1.00 31.52           O  
HETATM 3161  O   HOH A 826      17.578  34.388  -3.822  1.00 41.29           O  
HETATM 3162  O   HOH A 827      16.193  38.207  -1.939  1.00 42.21           O  
HETATM 3163  O   HOH A 829      11.252  32.926  -1.314  1.00 53.43           O  
HETATM 3164  O   HOH A 830       5.413  35.362   0.990  1.00 45.98           O  
HETATM 3165  O   HOH A 831       5.868  37.298   3.142  1.00 34.56           O  
HETATM 3166  O   HOH A 832       7.258  32.901  -2.365  1.00 49.70           O  
HETATM 3167  O   HOH A 833       9.675  41.621   6.772  1.00 18.78           O  
HETATM 3168  O   HOH A 834      21.347  36.737   7.484  1.00 33.32           O  
HETATM 3169  O   HOH A 835       4.321  36.957  21.606  1.00 22.03           O  
HETATM 3170  O   HOH A 836       3.709  39.648  21.363  1.00 31.60           O  
HETATM 3171  O   HOH A 837       4.853  42.475  25.122  1.00 27.20           O  
HETATM 3172  O   HOH A 838       7.272  41.792  24.343  1.00 16.95           O  
HETATM 3173  O   HOH A 839       2.888  40.508  23.979  1.00 21.81           O  
HETATM 3174  O   HOH A 840       1.150  42.360  22.608  1.00 20.04           O  
HETATM 3175  O   HOH A 841       1.534  38.640  25.686  1.00 30.74           O  
HETATM 3176  O   HOH A 842      -1.272  38.097  25.758  1.00 24.25           O  
HETATM 3177  O   HOH A 843      -5.491  40.717  17.695  1.00 37.45           O  
HETATM 3178  O   HOH A 844       1.010  39.821   5.999  1.00 20.92           O  
HETATM 3179  O   HOH A 845     -13.810  40.784   8.705  1.00 36.03           O  
HETATM 3180  O   HOH A 846     -12.249  41.181  10.595  1.00 20.11           O  
HETATM 3181  O   HOH A 847      -7.191  33.142   3.746  1.00 37.46           O  
HETATM 3182  O   HOH A 848      13.692  42.540  16.131  1.00 45.32           O  
HETATM 3183  O   HOH A 849       8.138  42.201  14.767  1.00 80.08           O  
HETATM 3184  O   HOH A 850      -3.842  41.036  10.189  1.00 18.82           O  
HETATM 3185  O   HOH A 853      -7.344  32.387  21.051  1.00 41.51           O  
HETATM 3186  O   HOH A 856       8.662   9.600  23.892  1.00 41.19           O  
HETATM 3187  O   HOH A 857       8.930  12.583  24.049  1.00  9.31           O  
HETATM 3188  O   HOH A 859       0.194  13.365  28.599  1.00 13.97           O  
HETATM 3189  O   HOH A 860       7.627  12.849  26.438  1.00 24.65           O  
HETATM 3190  O   HOH A 861       1.676  16.522  34.891  1.00 28.59           O  
HETATM 3191  O   HOH A 862      -0.384  17.253  33.279  1.00 31.56           O  
HETATM 3192  O   HOH A 863      -3.717  15.253  32.310  1.00 64.49           O  
HETATM 3193  O   HOH A 864       9.591  26.898  31.143  1.00 14.14           O  
HETATM 3194  O   HOH A 865      11.145  23.350  32.682  1.00 20.31           O  
HETATM 3195  O   HOH A 866      12.752  34.660  26.600  1.00 32.36           O  
HETATM 3196  O   HOH A 867      14.735  31.927  28.997  1.00 94.99           O  
HETATM 3197  O   HOH A 868      16.920  38.207  30.626  1.00 31.22           O  
HETATM 3198  O   HOH A 869      11.451  42.410  34.168  1.00100.00           O  
HETATM 3199  O   HOH A 873       0.944  16.449  19.879  1.00 36.47           O  
HETATM 3200  O   HOH A 875      -9.492  21.896  14.466  1.00 29.53           O  
HETATM 3201  O   HOH A 876       1.625  22.591   6.231  1.00 16.72           O  
HETATM 3202  O   HOH A 877      14.976  33.519  -4.850  1.00 30.51           O  
HETATM 3203  O   HOH A 878      17.936  26.034 -10.487  1.00 38.11           O  
HETATM 3204  O   HOH A 880      12.960  16.086  -6.759  1.00 38.19           O  
HETATM 3205  O   HOH A 881       0.890  19.564  -5.041  1.00 99.73           O  
HETATM 3206  O   HOH A 882      16.468   9.187  19.411  1.00 16.76           O  
HETATM 3207  O   HOH A 883      18.028   8.238  17.463  1.00 39.24           O  
HETATM 3208  O   HOH A 884       2.081  12.310  13.351  1.00 50.44           O  
HETATM 3209  O   HOH A 885      13.446   9.011   7.069  1.00 28.17           O  
HETATM 3210  O   HOH A 886       7.041  13.709  -0.978  1.00 96.10           O  
HETATM 3211  O   HOH A 887      23.177  10.691  10.793  1.00 34.03           O  
HETATM 3212  O   HOH A 888      14.291   6.500  15.733  1.00 48.26           O  
HETATM 3213  O   HOH A 889      21.371  10.327  17.409  1.00 24.84           O  
HETATM 3214  O   HOH A 891      18.799   8.559   1.283  1.00 23.32           O  
HETATM 3215  O   HOH A 892      38.178  26.920   9.948  1.00 26.10           O  
HETATM 3216  O   HOH A 893      37.867  22.371   8.508  1.00 20.26           O  
HETATM 3217  O   HOH A 894      38.524  23.208  11.023  1.00 17.53           O  
HETATM 3218  O   HOH A 895      40.563  24.350  14.447  1.00 31.91           O  
HETATM 3219  O   HOH A 896      38.819  17.369  13.097  1.00 25.09           O  
HETATM 3220  O   HOH A 897      37.422  15.385  12.099  1.00 32.54           O  
HETATM 3221  O   HOH A 898      36.420  11.148   9.731  1.00 20.05           O  
HETATM 3222  O   HOH A 899      36.345   7.926   5.226  1.00 56.63           O  
HETATM 3223  O   HOH A 900      40.089  11.528   2.864  1.00 35.44           O  
HETATM 3224  O   HOH A 901      41.985  19.071  13.969  1.00 31.45           O  
HETATM 3225  O   HOH A 902      29.064  13.758   4.649  1.00 63.12           O  
HETATM 3226  O   HOH A 903      37.045   8.006  21.293  1.00 91.55           O  
HETATM 3227  O   HOH A 905      26.281  14.285  28.105  1.00 23.26           O  
HETATM 3228  O   HOH A 908      11.732  50.294  35.134  1.00 19.64           O  
HETATM 3229  O   HOH A 909      18.691  41.857  35.827  1.00 88.52           O  
HETATM 3230  O   HOH A 910      16.644  54.321  36.685  1.00 25.95           O  
HETATM 3231  O   HOH A 911      12.643  56.215  37.577  1.00 29.81           O  
HETATM 3232  O   HOH A 912      10.851  58.506  37.091  1.00 33.41           O  
HETATM 3233  O   HOH A 913      14.781  59.536  25.202  1.00 49.43           O  
HETATM 3234  O   HOH A 914      20.839  54.864  26.706  1.00 20.08           O  
HETATM 3235  O   HOH A 915      19.985  54.279  30.707  1.00 24.30           O  
HETATM 3236  O   HOH A 917       3.115  55.154  34.182  1.00 25.50           O  
HETATM 3237  O   HOH A 918       2.504  53.266  36.163  1.00 24.18           O  
HETATM 3238  O   HOH A 919       5.251  45.720  35.308  1.00 52.72           O  
HETATM 3239  O   HOH A 920       3.077  44.323  29.025  1.00 29.48           O  
HETATM 3240  O   HOH A 921      -1.169  46.274  24.018  1.00 37.43           O  
HETATM 3241  O   HOH A 922      -1.612  45.929  26.817  1.00 20.05           O  
HETATM 3242  O   HOH A 923       4.302  42.411  27.902  1.00 20.93           O  
HETATM 3243  O   HOH A 924      12.222  47.073  13.525  1.00 47.79           O  
HETATM 3244  O   HOH A 925      21.022  49.754  14.455  1.00 22.52           O  
HETATM 3245  O   HOH A 926      30.912  48.711  12.041  1.00 56.84           O  
HETATM 3246  O   HOH A 927      31.734  51.096  15.772  1.00 34.85           O  
HETATM 3247  O   HOH A 928      11.802  55.299  13.602  1.00 39.74           O  
HETATM 3248  O   HOH A 929      12.279  59.787  24.682  1.00 36.43           O  
HETATM 3249  O   HOH A 930      23.428  31.808  33.707  1.00 69.09           O  
HETATM 3250  O   HOH A 931       0.885  20.766   4.229  1.00 26.63           O  
HETATM 3251  O   HOH A 932      41.182  20.141  10.001  1.00 17.70           O  
HETATM 3252  O   HOH A 934       0.893  24.262  33.126  1.00 17.01           O  
HETATM 3253  O   HOH A 935      -4.892  23.670  28.808  1.00 29.60           O  
HETATM 3254  O   HOH A 936      33.231   7.748  16.040  1.00 38.31           O  
HETATM 3255  O   HOH A 937     -10.148  35.842   3.999  1.00 41.46           O  
HETATM 3256  O   HOH A 938      -4.969  31.985   4.889  1.00 43.29           O  
HETATM 3257  O   HOH A 939      -2.065  35.089   3.985  1.00 47.61           O  
HETATM 3258  O   HOH A 940      20.335  45.262  13.166  1.00 25.56           O  
HETATM 3259  O   HOH A 951      20.479  17.034  -4.789  1.00 62.24           O  
HETATM 3260  O   HOH A 953      25.567  26.641  -5.524  1.00 44.91           O  
HETATM 3261  O   HOH A 954      25.679  26.530  -8.560  1.00 64.03           O  
HETATM 3262  O   HOH A 955      22.861  27.393  -5.708  1.00 33.73           O  
HETATM 3263  O   HOH A 956      28.038  30.331  -3.442  1.00 32.81           O  
HETATM 3264  O   HOH A 957      12.972  40.923  -1.673  1.00 61.09           O  
HETATM 3265  O   HOH A 958      21.416  36.740   0.963  1.00 39.10           O  
HETATM 3266  O   HOH A 959      21.444  38.832   4.008  1.00 50.46           O  
HETATM 3267  O   HOH A 960      -0.869  30.908   4.291  1.00 28.84           O  
HETATM 3268  O   HOH A 961       0.637  26.479   5.746  1.00 25.86           O  
HETATM 3269  O   HOH A 962       3.791  35.316   3.358  1.00 68.18           O  
HETATM 3270  O   HOH A 963       0.957  38.072   0.239  1.00 75.37           O  
HETATM 3271  O   HOH A 964      13.854  36.407  19.937  1.00 51.72           O  
HETATM 3272  O   HOH A 965      14.873  37.265  17.439  1.00 22.13           O  
HETATM 3273  O   HOH A 966       4.985  42.506  16.102  1.00 30.12           O  
HETATM 3274  O   HOH A 967      13.566  39.223  12.860  1.00 33.84           O  
HETATM 3275  O   HOH A 968      -0.244  41.840   9.735  1.00 34.38           O  
HETATM 3276  O   HOH A 969      -2.328  42.138   8.221  1.00 29.29           O  
HETATM 3277  O   HOH A 970       7.116  44.818  12.598  1.00 33.97           O  
HETATM 3278  O   HOH A 971      -4.691  39.942  21.975  1.00100.00           O  
HETATM 3279  O   HOH A 973      -6.346  44.846  21.555  1.00 45.55           O  
HETATM 3280  O   HOH A 974      -2.783  35.965  24.990  1.00 44.97           O  
HETATM 3281  O   HOH A 975      -2.865  40.438  24.591  1.00 78.37           O  
HETATM 3282  O   HOH A 976      14.253  23.133  21.074  1.00 43.90           O  
HETATM 3283  O   HOH A 977      13.045  20.972  22.260  1.00 77.93           O  
HETATM 3284  O   HOH A 978      14.420  22.469  23.663  1.00 34.29           O  
HETATM 3285  O   HOH A 979       3.347  15.493  20.704  1.00 27.56           O  
HETATM 3286  O   HOH A 980       1.098  14.567  17.883  1.00 31.88           O  
HETATM 3287  O   HOH A 981       9.345  16.269  28.269  1.00 73.17           O  
HETATM 3288  O   HOH A 982      13.112  22.496  28.446  1.00 18.68           O  
HETATM 3289  O   HOH A 983      14.839  16.926  26.249  1.00 49.61           O  
HETATM 3290  O   HOH A 984      14.676  19.202  27.771  1.00 39.18           O  
HETATM 3291  O   HOH A 985       4.090  12.812  30.690  1.00 22.58           O  
HETATM 3292  O   HOH A 986       7.604  14.791  33.128  1.00 19.34           O  
HETATM 3293  O   HOH A 987       4.881  19.096  36.341  1.00 41.64           O  
HETATM 3294  O   HOH A 989      10.208  29.079  26.635  1.00 44.46           O  
HETATM 3295  O   HOH A 990       2.395  35.241  27.991  1.00 35.52           O  
HETATM 3296  O   HOH A 991       5.559  36.178  24.669  1.00 32.91           O  
HETATM 3297  O   HOH A 992      -3.400  30.570  27.667  1.00 43.35           O  
HETATM 3298  O   HOH A 993      -8.641  29.950  21.211  1.00 31.09           O  
HETATM 3299  O   HOH A 994     -10.116  23.230  19.424  1.00 47.42           O  
HETATM 3300  O   HOH A 995     -13.403  28.587   9.995  1.00 42.60           O  
HETATM 3301  O   HOH A 996      -4.856  16.246  12.596  1.00 21.65           O  
HETATM 3302  O   HOH A 997      -3.983  13.455  20.139  1.00 22.35           O  
HETATM 3303  O   HOH A 998      -1.102  13.288  11.271  1.00 31.27           O  
HETATM 3304  O   HOH A 999       5.472  30.360  -2.893  1.00 89.30           O  
HETATM 3305  O   HOH A1000       5.352  23.517  -2.722  1.00 25.20           O  
HETATM 3306  O   HOH A1001       6.266  26.974  -4.861  1.00 25.34           O  
HETATM 3307  O   HOH A1002      13.651  22.927 -14.605  1.00 23.47           O  
HETATM 3308  O   HOH A1003      15.951  24.794 -14.961  1.00 32.25           O  
HETATM 3309  O   HOH A1004      12.046  27.782 -14.132  1.00 68.56           O  
HETATM 3310  O   HOH A1005      19.686  27.670  -8.987  1.00 28.02           O  
HETATM 3311  O   HOH A1006      17.279  14.441  -4.933  1.00 32.39           O  
HETATM 3312  O   HOH A1007      25.566  12.125  24.744  1.00 33.65           O  
HETATM 3313  O   HOH A1008      22.156  13.857  24.474  1.00 29.61           O  
HETATM 3314  O   HOH A1009      18.574   7.640   5.650  1.00 66.58           O  
HETATM 3315  O   HOH A1010      20.333   9.854  11.144  1.00 36.60           O  
HETATM 3316  O   HOH A1011      26.563  11.201  10.049  1.00 53.71           O  
HETATM 3317  O   HOH A1012      31.043  15.435   3.014  1.00 35.28           O  
HETATM 3318  O   HOH A1013      37.914  12.371  11.672  1.00 38.87           O  
HETATM 3319  O   HOH A1014      38.741  16.244   8.423  1.00 33.49           O  
HETATM 3320  O   HOH A1015      36.964  11.720   3.343  1.00 20.31           O  
HETATM 3321  O   HOH A1017      42.418   7.440  16.528  1.00 34.93           O  
HETATM 3322  O   HOH A1018      38.294  10.800  22.077  1.00 47.74           O  
HETATM 3323  O   HOH A1019      34.362   7.679  18.341  1.00 91.38           O  
HETATM 3324  O   HOH A1020      35.257   4.078  12.559  1.00 56.84           O  
HETATM 3325  O   HOH A1021      28.146  12.222  28.310  1.00 33.32           O  
HETATM 3326  O   HOH A1022      22.967  20.305  30.403  1.00 49.97           O  
HETATM 3327  O   HOH A1023      23.745  25.909  32.180  1.00 60.39           O  
HETATM 3328  O   HOH A1024      21.278  40.633  36.576  1.00 68.58           O  
HETATM 3329  O   HOH A1025      16.931  37.079  33.211  1.00 75.44           O  
HETATM 3330  O   HOH A1026      11.360  46.134  33.819  1.00 31.17           O  
HETATM 3331  O   HOH A1027      15.621  47.418  35.410  1.00 56.22           O  
HETATM 3332  O   HOH A1028      13.032  51.332  37.180  1.00 23.50           O  
HETATM 3333  O   HOH A1029       4.519  55.089  37.516  1.00 87.91           O  
HETATM 3334  O   HOH A1030       5.940  52.403  38.407  1.00 29.47           O  
HETATM 3335  O   HOH A1031       5.007  49.888  37.468  1.00 41.12           O  
HETATM 3336  O   HOH A1032      18.160  51.899  36.748  1.00 35.40           O  
HETATM 3337  O   HOH A1033       5.062  61.439  37.546  1.00 65.08           O  
HETATM 3338  O   HOH A1034      -1.658  54.618  32.688  1.00 60.16           O  
HETATM 3339  O   HOH A1035      -1.873  43.993  31.492  1.00 84.69           O  
HETATM 3340  O   HOH A1036      -2.856  44.348  34.370  1.00 65.40           O  
HETATM 3341  O   HOH A1037       2.376  52.643  14.631  1.00 57.10           O  
HETATM 3342  O   HOH A1038      15.934  41.334  13.248  1.00 26.70           O  
HETATM 3343  O   HOH A1041      17.425  53.216  14.269  1.00 42.16           O  
HETATM 3344  O   HOH A1042      23.934  47.172  11.685  1.00 35.94           O  
HETATM 3345  O   HOH A1044      -2.172  54.142  22.100  1.00 49.47           O  
HETATM 3346  O   HOH A1045      24.915  55.227  24.174  1.00 29.87           O  
HETATM 3347  O   HOH A1046      33.670  45.855  15.834  1.00 43.04           O  
HETATM 3348  O   HOH A1047      21.953  48.158  35.303  1.00 35.07           O  
HETATM 3349  O   HOH A1048      25.625  41.083  35.213  1.00 33.86           O  
HETATM 3350  O   HOH A1050      23.199  17.273  29.702  1.00 54.55           O  
HETATM 3351  O   HOH A1051      40.944  13.600  29.596  1.00100.00           O  
HETATM 3352  O   HOH A1052      43.101  24.755  23.989  1.00 31.43           O  
HETATM 3353  O   HOH A1053      19.583  34.062  13.526  1.00 10.85           O  
HETATM 3354  O   HOH A1054      23.277  36.025  12.051  1.00 35.34           O  
HETATM 3355  O   HOH A1055      44.329  21.552  18.753  1.00 56.97           O  
HETATM 3356  O   HOH A1056      43.826  30.000  12.417  1.00 34.46           O  
HETATM 3357  O   HOH A1061      15.028  32.322   4.947  1.00  8.71           O  
HETATM 3358  O   HOH A1062      20.413  36.450  10.013  1.00 24.60           O  
HETATM 3359  O   HOH A1063      25.975  43.375  12.857  1.00 26.87           O  
HETATM 3360  O   HOH A1064      35.758  29.980  33.004  1.00 15.72           O  
HETATM 3361  O   HOH A1065      37.719  28.477  33.789  1.00 29.48           O  
HETATM 3362  O   HOH A1066      36.208  13.818  33.450  1.00 37.47           O  
HETATM 3363  O   HOH A1067      39.647  14.753  31.937  1.00 46.66           O  
HETATM 3364  O   HOH A1068      40.197  18.845  32.474  1.00 27.98           O  
HETATM 3365  O   HOH A1069      22.351  52.880  27.832  1.00 22.06           O  
HETATM 3366  O   HOH A1070       2.564  50.743  35.325  1.00 39.64           O  
HETATM 3367  O   HOH A1071      42.258  22.304  31.806  1.00 31.85           O  
HETATM 3368  O   HOH A1072      21.279  11.018  13.998  1.00 34.94           O  
HETATM 3369  O   HOH A1073      24.256   8.795  17.307  1.00 48.29           O  
HETATM 3370  O   HOH A1074      26.180   9.949  15.857  1.00 47.62           O  
HETATM 3371  O   HOH A1075       2.856  40.033  28.067  1.00 29.87           O  
HETATM 3372  O   HOH A1076      19.608  51.563  34.390  1.00 31.23           O  
HETATM 3373  O   HOH A1077      33.386  38.986  31.107  1.00 33.66           O  
HETATM 3374  O   HOH A1078      43.361  18.169  19.688  1.00 33.46           O  
HETATM 3375  O   HOH A1079       2.321  31.341   3.185  1.00 43.49           O  
HETATM 3376  O   HOH A1080       6.766  18.229  -3.707  1.00 30.20           O  
HETATM 3377  O   HOH A1081      -1.605  40.499   6.185  1.00 25.31           O  
HETATM 3378  O   HOH A1082      30.022  40.784  12.775  1.00 48.84           O  
HETATM 3379  O   HOH A1083       9.024   6.524  20.490  1.00 31.67           O  
HETATM 3380  O   HOH A1084       4.987  13.934  33.858  1.00 53.25           O  
HETATM 3381  O   HOH A1085       0.588  10.248  23.651  1.00 36.83           O  
CONECT 2909 2914 2986 2987 2988                                                 
CONECT 2909 2989 2990                                                           
CONECT 2910 2990                                                                
CONECT 2913 2914 2915 2916 2920                                                 
CONECT 2914 2909 2913                                                           
CONECT 2915 2913                                                                
CONECT 2916 2913                                                                
CONECT 2917 2918 2919 2920 2921                                                 
CONECT 2918 2917                                                                
CONECT 2919 2917                                                                
CONECT 2920 2913 2917                                                           
CONECT 2921 2917 2922                                                           
CONECT 2922 2921 2923                                                           
CONECT 2923 2922 2924 2925                                                      
CONECT 2924 2923 2929                                                           
CONECT 2925 2923 2926 2927                                                      
CONECT 2926 2925                                                                
CONECT 2927 2925 2928 2929                                                      
CONECT 2928 2927                                                                
CONECT 2929 2924 2927 2930                                                      
CONECT 2930 2929 2931 2939                                                      
CONECT 2931 2930 2932                                                           
CONECT 2932 2931 2933                                                           
CONECT 2933 2932 2934 2939                                                      
CONECT 2934 2933 2935 2936                                                      
CONECT 2935 2934                                                                
CONECT 2936 2934 2937                                                           
CONECT 2937 2936 2938                                                           
CONECT 2938 2937 2939                                                           
CONECT 2939 2930 2933 2938                                                      
CONECT 2986 2909                                                                
CONECT 2987 2909                                                                
CONECT 2988 2909                                                                
CONECT 2989 2909                                                                
CONECT 2990 2909 2910                                                           
MASTER      304    0    5   14   16    0   12    6 3380    1   35   30          
END                                                                             
