HEADER    HYDROLASE                               21-APR-98   1BA0              
TITLE     HEAT-SHOCK COGNATE 70KD PROTEIN 44KD ATPASE N-TERMINAL 1NGE 3         
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 1BA0    1       REMARK                                   
REVDAT   4   03-NOV-21 1BA0    1       REMARK SEQADV LINK                       
REVDAT   3   24-FEB-09 1BA0    1       VERSN                                    
REVDAT   2   01-APR-03 1BA0    1       JRNL                                     
REVDAT   1   15-JUL-98 1BA0    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.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.1                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
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)   (%) : 88.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 34106                          
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) : 0.216                           
REMARK   3   FREE R VALUE                     : 0.275                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3357                            
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           : 15                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.94                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1867                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2970                       
REMARK   3   BIN FREE R VALUE                    : 0.3120                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 212                          
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          : 36                                      
REMARK   3   SOLVENT ATOMS            : 423                                     
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) : 0.007                           
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: NULL                                      
REMARK   4                                                                      
REMARK   4 1BA0 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_1000171509.                                   
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 3.1                                            
REMARK 200 STARTING MODEL: PDB ENTRY 1HPM                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.77                                     
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       71.65000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       23.25000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       31.90000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       23.25000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       71.65000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       31.90000            
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     LYS A 137    CG   CD   CE   NZ                                   
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    LYS A 361       19.71   -142.47                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 490  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  10   OD2                                                    
REMARK 620 2 TYR A  15   O   112.8                                              
REMARK 620 3 ADP A 486   O2B 129.2  99.6                                        
REMARK 620 4 HOH A 558   O    93.8  88.5 126.1                                  
REMARK 620 5 HOH A 563   O    77.6 167.1  67.5  98.7                            
REMARK 620 N                    1     2     3     4                             
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   O2B                                                    
REMARK 620 2 PO4 A 488   O2   91.0                                              
REMARK 620 3 HOH A 560   O    91.2  83.0                                        
REMARK 620 4 HOH A 561   O   173.4  89.5  95.4                                  
REMARK 620 5 HOH A 562   O    89.0  90.2 173.3  84.5                            
REMARK 620 6 HOH A 563   O    86.9 169.7  87.0  93.7  99.8                      
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 PO4 A 488                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 490                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 451                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 455                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 486                 
DBREF  1BA0 A    1   386  UNP    P19120   HSP7C_BOVIN      1    386             
SEQADV 1BA0 LYS A  206  UNP  P19120    ASP   206 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 CYS 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 LYS 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    PO4  A 488       5                                                       
HET     NA  A 490       1                                                       
HET     CL  A 451       1                                                       
HET     CL  A 455       1                                                       
HET    ADP  A 486      27                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM      NA SODIUM ION                                                       
HETNAM      CL CHLORIDE ION                                                     
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
FORMUL   2   MG    MG 2+                                                        
FORMUL   3  PO4    O4 P 3-                                                      
FORMUL   4   NA    NA 1+                                                        
FORMUL   5   CL    2(CL 1-)                                                     
FORMUL   7  ADP    C10 H15 N5 O10 P2                                            
FORMUL   8  HOH   *423(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 CYS 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         OD2 ASP A  10                NA    NA A 490     1555   1555  2.45  
LINK         O   TYR A  15                NA    NA A 490     1555   1555  2.44  
LINK         O2B ADP A 486                MG    MG A 487     1555   1555  2.05  
LINK         O2B ADP A 486                NA    NA A 490     1555   1555  2.37  
LINK        MG    MG A 487                 O2  PO4 A 488     1555   1555  2.15  
LINK        MG    MG A 487                 O   HOH A 560     1555   1555  2.17  
LINK        MG    MG A 487                 O   HOH A 561     1555   1555  2.05  
LINK        MG    MG A 487                 O   HOH A 562     1555   1555  2.05  
LINK        MG    MG A 487                 O   HOH A 563     1555   1555  2.15  
LINK        NA    NA A 490                 O   HOH A 558     1555   1555  2.31  
LINK        NA    NA A 490                 O   HOH A 563     1555   1555  2.80  
CISPEP   1 GLY A    4    PRO A    5          0         0.15                     
SITE     1 AC1  7 ADP A 486  PO4 A 488   NA A 490  HOH A 560                    
SITE     2 AC1  7 HOH A 561  HOH A 562  HOH A 563                               
SITE     1 AC2 14 GLY A  12  THR A  13  LYS A  71  PRO A 147                    
SITE     2 AC2 14 GLU A 175  THR A 204  LYS A 206  ADP A 486                    
SITE     3 AC2 14  MG A 487  HOH A 545  HOH A 560  HOH A 561                    
SITE     4 AC2 14 HOH A 562  HOH A1057                                          
SITE     1 AC3  6 ASP A  10  TYR A  15  ADP A 486   MG A 487                    
SITE     2 AC3  6 HOH A 558  HOH A 563                                          
SITE     1 AC4  5 TYR A 183  LYS A 345  LYS A 348  HOH A 537                    
SITE     2 AC4  5 HOH A 892                                                     
SITE     1 AC5  4 ASN A  31  ASP A  32  GLN A  33  LYS A 126                    
SITE     1 AC6 28 THR A  13  THR A  14  TYR A  15  GLY A 201                    
SITE     2 AC6 28 GLY A 202  GLY A 230  GLU A 268  LYS A 271                    
SITE     3 AC6 28 ARG A 272  SER A 275  GLY A 338  GLY A 339                    
SITE     4 AC6 28 SER A 340  ARG A 342  ASP A 366   MG A 487                    
SITE     5 AC6 28 PO4 A 488   NA A 490  HOH A 545  HOH A 558                    
SITE     6 AC6 28 HOH A 560  HOH A 562  HOH A 563  HOH A 564                    
SITE     7 AC6 28 HOH A 587  HOH A 799  HOH A 965  HOH A1053                    
CRYST1  143.300   63.800   46.500  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      0.006978  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015674  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.021505        0.00000                         
ATOM      1  N   GLY A   4      16.657  15.664  -6.944  1.00 40.41           N  
ATOM      2  CA  GLY A   4      15.835  16.835  -6.562  1.00 40.71           C  
ATOM      3  C   GLY A   4      16.249  18.108  -7.279  1.00 39.72           C  
ATOM      4  O   GLY A   4      15.624  18.472  -8.274  1.00 42.82           O  
ATOM      5  N   PRO A   5      17.336  18.773  -6.847  1.00 37.89           N  
ATOM      6  CA  PRO A   5      18.211  18.407  -5.725  1.00 35.51           C  
ATOM      7  C   PRO A   5      17.518  18.320  -4.359  1.00 31.94           C  
ATOM      8  O   PRO A   5      16.387  18.779  -4.183  1.00 30.64           O  
ATOM      9  CB  PRO A   5      19.273  19.511  -5.749  1.00 35.62           C  
ATOM     10  CG  PRO A   5      18.519  20.688  -6.274  1.00 36.50           C  
ATOM     11  CD  PRO A   5      17.741  20.073  -7.412  1.00 37.21           C  
ATOM     12  N   ALA A   6      18.178  17.646  -3.424  1.00 27.87           N  
ATOM     13  CA  ALA A   6      17.646  17.493  -2.081  1.00 21.68           C  
ATOM     14  C   ALA A   6      18.140  18.699  -1.295  1.00 18.77           C  
ATOM     15  O   ALA A   6      19.220  19.224  -1.577  1.00 19.76           O  
ATOM     16  CB  ALA A   6      18.148  16.205  -1.463  1.00 17.62           C  
ATOM     17  N   VAL A   7      17.347  19.161  -0.336  1.00 15.00           N  
ATOM     18  CA  VAL A   7      17.738  20.321   0.452  1.00 14.72           C  
ATOM     19  C   VAL A   7      17.962  19.981   1.915  1.00 12.14           C  
ATOM     20  O   VAL A   7      17.473  18.965   2.415  1.00 13.04           O  
ATOM     21  CB  VAL A   7      16.701  21.478   0.345  1.00 14.88           C  
ATOM     22  CG1 VAL A   7      16.499  21.874  -1.119  1.00 11.80           C  
ATOM     23  CG2 VAL A   7      15.371  21.085   1.002  1.00 13.68           C  
ATOM     24  N   GLY A   8      18.744  20.815   2.581  1.00 10.17           N  
ATOM     25  CA  GLY A   8      19.016  20.611   3.988  1.00 10.75           C  
ATOM     26  C   GLY A   8      18.242  21.650   4.756  1.00  7.67           C  
ATOM     27  O   GLY A   8      18.353  22.844   4.469  1.00 11.15           O  
ATOM     28  N   ILE A   9      17.442  21.212   5.716  1.00 10.64           N  
ATOM     29  CA  ILE A   9      16.650  22.149   6.499  1.00 11.31           C  
ATOM     30  C   ILE A   9      16.889  22.047   7.994  1.00  9.63           C  
ATOM     31  O   ILE A   9      16.840  20.964   8.587  1.00  9.89           O  
ATOM     32  CB  ILE A   9      15.123  21.991   6.251  1.00  9.24           C  
ATOM     33  CG1 ILE A   9      14.800  22.114   4.762  1.00 10.89           C  
ATOM     34  CG2 ILE A   9      14.353  23.081   7.009  1.00  9.74           C  
ATOM     35  CD1 ILE A   9      13.359  21.787   4.432  1.00  7.10           C  
ATOM     36  N   ASP A  10      17.178  23.201   8.575  1.00 10.01           N  
ATOM     37  CA  ASP A  10      17.381  23.350  10.002  1.00 10.27           C  
ATOM     38  C   ASP A  10      16.033  23.881  10.514  1.00  9.61           C  
ATOM     39  O   ASP A  10      15.657  25.019  10.220  1.00  8.27           O  
ATOM     40  CB  ASP A  10      18.507  24.372  10.265  1.00  9.23           C  
ATOM     41  CG  ASP A  10      18.472  24.966  11.674  1.00  8.92           C  
ATOM     42  OD1 ASP A  10      17.955  24.329  12.614  1.00 10.54           O  
ATOM     43  OD2 ASP A  10      18.985  26.087  11.840  1.00 11.04           O  
ATOM     44  N   LEU A  11      15.282  23.027  11.201  1.00  7.89           N  
ATOM     45  CA  LEU A  11      14.002  23.413  11.772  1.00  6.47           C  
ATOM     46  C   LEU A  11      14.353  23.851  13.189  1.00  6.50           C  
ATOM     47  O   LEU A  11      14.447  23.017  14.094  1.00  8.49           O  
ATOM     48  CB  LEU A  11      13.053  22.207  11.791  1.00  6.90           C  
ATOM     49  CG  LEU A  11      11.679  22.395  12.439  1.00  5.97           C  
ATOM     50  CD1 LEU A  11      10.930  23.567  11.795  1.00  7.60           C  
ATOM     51  CD2 LEU A  11      10.885  21.109  12.319  1.00  5.02           C  
ATOM     52  N   GLY A  12      14.594  25.147  13.372  1.00  6.62           N  
ATOM     53  CA  GLY A  12      14.994  25.640  14.681  1.00  8.10           C  
ATOM     54  C   GLY A  12      13.902  26.028  15.656  1.00  9.65           C  
ATOM     55  O   GLY A  12      12.740  26.226  15.280  1.00  8.50           O  
ATOM     56  N   THR A  13      14.275  26.117  16.928  1.00 11.90           N  
ATOM     57  CA  THR A  13      13.339  26.504  17.976  1.00 10.15           C  
ATOM     58  C   THR A  13      12.829  27.914  17.704  1.00 11.53           C  
ATOM     59  O   THR A  13      11.632  28.174  17.795  1.00 11.26           O  
ATOM     60  CB  THR A  13      14.007  26.488  19.378  1.00 10.07           C  
ATOM     61  OG1 THR A  13      14.493  25.172  19.667  1.00 10.31           O  
ATOM     62  CG2 THR A  13      13.018  26.896  20.446  1.00  7.25           C  
ATOM     63  N   THR A  14      13.741  28.815  17.360  1.00  9.23           N  
ATOM     64  CA  THR A  14      13.381  30.201  17.091  1.00 10.22           C  
ATOM     65  C   THR A  14      13.499  30.605  15.612  1.00  8.54           C  
ATOM     66  O   THR A  14      12.675  31.369  15.108  1.00  7.79           O  
ATOM     67  CB  THR A  14      14.202  31.171  17.999  1.00 12.78           C  
ATOM     68  OG1 THR A  14      15.598  31.102  17.667  1.00 15.45           O  
ATOM     69  CG2 THR A  14      14.025  30.788  19.476  1.00 13.51           C  
ATOM     70  N   TYR A  15      14.527  30.112  14.924  1.00  9.81           N  
ATOM     71  CA  TYR A  15      14.722  30.428  13.506  1.00  8.63           C  
ATOM     72  C   TYR A  15      15.123  29.190  12.744  1.00  9.42           C  
ATOM     73  O   TYR A  15      15.918  28.375  13.233  1.00  8.08           O  
ATOM     74  CB  TYR A  15      15.803  31.494  13.285  1.00  8.07           C  
ATOM     75  CG  TYR A  15      15.397  32.895  13.660  1.00  8.15           C  
ATOM     76  CD1 TYR A  15      15.427  33.310  14.994  1.00  8.97           C  
ATOM     77  CD2 TYR A  15      14.998  33.812  12.690  1.00  6.43           C  
ATOM     78  CE1 TYR A  15      15.066  34.595  15.355  1.00 12.43           C  
ATOM     79  CE2 TYR A  15      14.635  35.109  13.039  1.00  7.90           C  
ATOM     80  CZ  TYR A  15      14.672  35.492  14.377  1.00 14.05           C  
ATOM     81  OH  TYR A  15      14.317  36.764  14.758  1.00 15.20           O  
ATOM     82  N   SER A  16      14.580  29.073  11.536  1.00  8.39           N  
ATOM     83  CA  SER A  16      14.845  27.960  10.643  1.00  7.96           C  
ATOM     84  C   SER A  16      15.688  28.439   9.463  1.00  8.31           C  
ATOM     85  O   SER A  16      15.737  29.637   9.169  1.00  8.71           O  
ATOM     86  CB  SER A  16      13.528  27.345  10.181  1.00  9.05           C  
ATOM     87  OG  SER A  16      12.898  26.701  11.277  1.00  7.32           O  
ATOM     88  N   CYS A  17      16.332  27.503   8.775  1.00  7.29           N  
ATOM     89  CA  CYS A  17      17.205  27.854   7.667  1.00  7.97           C  
ATOM     90  C   CYS A  17      17.240  26.727   6.643  1.00  5.93           C  
ATOM     91  O   CYS A  17      17.138  25.555   7.002  1.00  7.72           O  
ATOM     92  CB  CYS A  17      18.607  28.122   8.231  1.00 10.31           C  
ATOM     93  SG  CYS A  17      19.824  28.741   7.091  1.00 10.12           S  
ATOM     94  N   VAL A  18      17.340  27.079   5.366  1.00  9.53           N  
ATOM     95  CA  VAL A  18      17.389  26.077   4.305  1.00  8.74           C  
ATOM     96  C   VAL A  18      18.553  26.324   3.350  1.00  8.17           C  
ATOM     97  O   VAL A  18      18.879  27.466   3.016  1.00 10.06           O  
ATOM     98  CB  VAL A  18      16.043  26.002   3.520  1.00  5.23           C  
ATOM     99  CG1 VAL A  18      15.748  27.312   2.823  1.00  5.08           C  
ATOM    100  CG2 VAL A  18      16.071  24.848   2.523  1.00  6.65           C  
ATOM    101  N   GLY A  19      19.200  25.244   2.938  1.00 12.36           N  
ATOM    102  CA  GLY A  19      20.316  25.361   2.024  1.00  9.79           C  
ATOM    103  C   GLY A  19      20.274  24.238   1.014  1.00 12.41           C  
ATOM    104  O   GLY A  19      19.640  23.203   1.249  1.00 12.35           O  
ATOM    105  N   VAL A  20      20.937  24.442  -0.117  1.00 11.94           N  
ATOM    106  CA  VAL A  20      20.985  23.434  -1.166  1.00 12.88           C  
ATOM    107  C   VAL A  20      22.412  23.400  -1.695  1.00 12.76           C  
ATOM    108  O   VAL A  20      23.037  24.444  -1.892  1.00 14.46           O  
ATOM    109  CB  VAL A  20      19.961  23.729  -2.315  1.00  9.65           C  
ATOM    110  CG1 VAL A  20      20.261  25.061  -2.988  1.00 11.67           C  
ATOM    111  CG2 VAL A  20      19.944  22.587  -3.324  1.00  8.46           C  
ATOM    112  N   PHE A  21      22.941  22.194  -1.847  1.00 15.71           N  
ATOM    113  CA  PHE A  21      24.297  21.995  -2.332  1.00 15.54           C  
ATOM    114  C   PHE A  21      24.264  21.784  -3.849  1.00 16.35           C  
ATOM    115  O   PHE A  21      23.630  20.849  -4.343  1.00 16.19           O  
ATOM    116  CB  PHE A  21      24.907  20.787  -1.613  1.00 18.69           C  
ATOM    117  CG  PHE A  21      26.370  20.580  -1.881  1.00 17.78           C  
ATOM    118  CD1 PHE A  21      27.322  21.208  -1.097  1.00 20.12           C  
ATOM    119  CD2 PHE A  21      26.792  19.720  -2.887  1.00 20.10           C  
ATOM    120  CE1 PHE A  21      28.673  20.980  -1.301  1.00 21.20           C  
ATOM    121  CE2 PHE A  21      28.141  19.484  -3.102  1.00 20.25           C  
ATOM    122  CZ  PHE A  21      29.083  20.115  -2.306  1.00 21.28           C  
ATOM    123  N   GLN A  22      24.885  22.702  -4.582  1.00 16.07           N  
ATOM    124  CA  GLN A  22      24.947  22.622  -6.032  1.00 16.90           C  
ATOM    125  C   GLN A  22      26.328  23.064  -6.474  1.00 16.12           C  
ATOM    126  O   GLN A  22      26.907  23.984  -5.895  1.00 15.41           O  
ATOM    127  CB  GLN A  22      23.881  23.512  -6.688  1.00 18.16           C  
ATOM    128  CG  GLN A  22      22.448  23.150  -6.326  1.00 21.82           C  
ATOM    129  CD  GLN A  22      21.429  23.707  -7.308  1.00 26.78           C  
ATOM    130  OE1 GLN A  22      20.760  22.949  -8.016  1.00 30.92           O  
ATOM    131  NE2 GLN A  22      21.301  25.026  -7.357  1.00 22.74           N  
ATOM    132  N   HIS A  23      26.866  22.366  -7.469  1.00 16.13           N  
ATOM    133  CA  HIS A  23      28.185  22.655  -8.016  1.00 13.90           C  
ATOM    134  C   HIS A  23      29.268  22.757  -6.949  1.00 15.99           C  
ATOM    135  O   HIS A  23      30.047  23.710  -6.921  1.00 15.14           O  
ATOM    136  CB  HIS A  23      28.138  23.910  -8.892  1.00 15.63           C  
ATOM    137  CG  HIS A  23      27.389  23.708 -10.174  1.00 20.15           C  
ATOM    138  ND1 HIS A  23      26.349  24.518 -10.568  1.00 21.55           N  
ATOM    139  CD2 HIS A  23      27.502  22.748 -11.125  1.00 18.84           C  
ATOM    140  CE1 HIS A  23      25.848  24.066 -11.706  1.00 22.35           C  
ATOM    141  NE2 HIS A  23      26.529  22.995 -12.064  1.00 21.74           N  
ATOM    142  N   GLY A  24      29.290  21.766  -6.062  1.00 18.09           N  
ATOM    143  CA  GLY A  24      30.275  21.718  -4.995  1.00 21.27           C  
ATOM    144  C   GLY A  24      30.199  22.827  -3.961  1.00 22.74           C  
ATOM    145  O   GLY A  24      31.102  22.951  -3.130  1.00 23.42           O  
ATOM    146  N   LYS A  25      29.115  23.602  -3.979  1.00 22.38           N  
ATOM    147  CA  LYS A  25      28.931  24.714  -3.049  1.00 20.37           C  
ATOM    148  C   LYS A  25      27.533  24.703  -2.464  1.00 18.41           C  
ATOM    149  O   LYS A  25      26.576  24.295  -3.121  1.00 15.86           O  
ATOM    150  CB  LYS A  25      29.125  26.053  -3.766  1.00 21.36           C  
ATOM    151  CG  LYS A  25      30.539  26.360  -4.186  1.00 28.88           C  
ATOM    152  CD  LYS A  25      30.573  27.513  -5.178  1.00 32.32           C  
ATOM    153  CE  LYS A  25      30.006  27.097  -6.530  1.00 36.75           C  
ATOM    154  NZ  LYS A  25      30.066  28.205  -7.517  1.00 41.24           N  
ATOM    155  N   VAL A  26      27.424  25.160  -1.225  1.00 17.62           N  
ATOM    156  CA  VAL A  26      26.137  25.245  -0.552  1.00 14.08           C  
ATOM    157  C   VAL A  26      25.595  26.657  -0.732  1.00 11.92           C  
ATOM    158  O   VAL A  26      26.327  27.642  -0.600  1.00 11.48           O  
ATOM    159  CB  VAL A  26      26.256  24.973   0.982  1.00 12.25           C  
ATOM    160  CG1 VAL A  26      24.923  25.247   1.677  1.00 10.96           C  
ATOM    161  CG2 VAL A  26      26.673  23.550   1.237  1.00 12.22           C  
ATOM    162  N   GLU A  27      24.319  26.745  -1.073  1.00 10.93           N  
ATOM    163  CA  GLU A  27      23.660  28.022  -1.209  1.00 10.85           C  
ATOM    164  C   GLU A  27      22.655  28.129  -0.063  1.00 12.08           C  
ATOM    165  O   GLU A  27      21.704  27.342   0.001  1.00 12.79           O  
ATOM    166  CB  GLU A  27      22.911  28.112  -2.537  1.00 12.89           C  
ATOM    167  CG  GLU A  27      22.000  29.339  -2.648  1.00 14.59           C  
ATOM    168  CD  GLU A  27      22.762  30.641  -2.869  1.00 19.14           C  
ATOM    169  OE1 GLU A  27      23.954  30.587  -3.235  1.00 18.63           O  
ATOM    170  OE2 GLU A  27      22.161  31.725  -2.692  1.00 17.16           O  
ATOM    171  N   ILE A  28      22.920  29.013   0.894  1.00 11.09           N  
ATOM    172  CA  ILE A  28      21.971  29.234   1.981  1.00 12.65           C  
ATOM    173  C   ILE A  28      20.976  30.182   1.314  1.00 11.04           C  
ATOM    174  O   ILE A  28      21.323  31.299   0.917  1.00 12.67           O  
ATOM    175  CB  ILE A  28      22.624  29.887   3.213  1.00 11.21           C  
ATOM    176  CG1 ILE A  28      23.646  28.927   3.846  1.00  9.78           C  
ATOM    177  CG2 ILE A  28      21.545  30.300   4.220  1.00  9.50           C  
ATOM    178  CD1 ILE A  28      23.064  27.623   4.366  1.00  7.43           C  
ATOM    179  N   ILE A  29      19.753  29.700   1.151  1.00 13.33           N  
ATOM    180  CA  ILE A  29      18.702  30.429   0.454  1.00 11.40           C  
ATOM    181  C   ILE A  29      17.955  31.503   1.249  1.00 11.80           C  
ATOM    182  O   ILE A  29      17.385  31.230   2.308  1.00 11.24           O  
ATOM    183  CB  ILE A  29      17.690  29.420  -0.143  1.00 10.30           C  
ATOM    184  CG1 ILE A  29      18.450  28.276  -0.823  1.00  9.65           C  
ATOM    185  CG2 ILE A  29      16.771  30.119  -1.142  1.00 12.04           C  
ATOM    186  CD1 ILE A  29      17.630  27.032  -1.071  1.00  7.29           C  
ATOM    187  N   ALA A  30      17.942  32.718   0.706  1.00 10.74           N  
ATOM    188  CA  ALA A  30      17.251  33.843   1.329  1.00  9.53           C  
ATOM    189  C   ALA A  30      15.755  33.777   1.008  1.00 13.96           C  
ATOM    190  O   ALA A  30      15.362  33.363  -0.095  1.00 10.83           O  
ATOM    191  CB  ALA A  30      17.831  35.153   0.834  1.00 10.58           C  
ATOM    192  N   ASN A  31      14.925  34.178   1.968  1.00 13.27           N  
ATOM    193  CA  ASN A  31      13.474  34.154   1.771  1.00 15.56           C  
ATOM    194  C   ASN A  31      12.960  35.381   1.009  1.00 15.15           C  
ATOM    195  O   ASN A  31      13.751  36.224   0.575  1.00 13.55           O  
ATOM    196  CB  ASN A  31      12.727  33.945   3.105  1.00 11.85           C  
ATOM    197  CG  ASN A  31      12.843  35.122   4.063  1.00 10.04           C  
ATOM    198  OD1 ASN A  31      13.021  36.267   3.657  1.00 12.52           O  
ATOM    199  ND2 ASN A  31      12.704  34.839   5.351  1.00 10.12           N  
ATOM    200  N   ASP A  32      11.644  35.481   0.845  1.00 15.42           N  
ATOM    201  CA  ASP A  32      11.039  36.598   0.118  1.00 14.96           C  
ATOM    202  C   ASP A  32      11.451  37.965   0.625  1.00 14.93           C  
ATOM    203  O   ASP A  32      11.494  38.921  -0.143  1.00 18.57           O  
ATOM    204  CB  ASP A  32       9.513  36.495   0.121  1.00 17.38           C  
ATOM    205  CG  ASP A  32       9.002  35.290  -0.649  1.00 25.69           C  
ATOM    206  OD1 ASP A  32       9.820  34.545  -1.235  1.00 26.76           O  
ATOM    207  OD2 ASP A  32       7.767  35.084  -0.672  1.00 27.68           O  
ATOM    208  N   GLN A  33      11.749  38.067   1.915  1.00 13.93           N  
ATOM    209  CA  GLN A  33      12.161  39.344   2.494  1.00 14.65           C  
ATOM    210  C   GLN A  33      13.681  39.519   2.455  1.00 15.05           C  
ATOM    211  O   GLN A  33      14.212  40.470   3.023  1.00 18.61           O  
ATOM    212  CB  GLN A  33      11.677  39.464   3.947  1.00 15.44           C  
ATOM    213  CG  GLN A  33      10.158  39.428   4.141  1.00 17.91           C  
ATOM    214  CD  GLN A  33       9.521  38.121   3.686  1.00 14.31           C  
ATOM    215  OE1 GLN A  33       8.706  38.110   2.775  1.00 19.56           O  
ATOM    216  NE2 GLN A  33       9.920  37.018   4.291  1.00  9.44           N  
ATOM    217  N   GLY A  34      14.379  38.583   1.823  1.00 14.53           N  
ATOM    218  CA  GLY A  34      15.828  38.661   1.742  1.00 11.99           C  
ATOM    219  C   GLY A  34      16.537  38.173   2.995  1.00 13.04           C  
ATOM    220  O   GLY A  34      17.736  38.382   3.155  1.00 12.38           O  
ATOM    221  N   ASN A  35      15.814  37.492   3.876  1.00 11.80           N  
ATOM    222  CA  ASN A  35      16.414  36.992   5.105  1.00 12.39           C  
ATOM    223  C   ASN A  35      16.924  35.565   4.949  1.00 10.65           C  
ATOM    224  O   ASN A  35      16.214  34.692   4.437  1.00 12.59           O  
ATOM    225  CB  ASN A  35      15.428  37.099   6.262  1.00  9.54           C  
ATOM    226  CG  ASN A  35      15.005  38.527   6.524  1.00 11.93           C  
ATOM    227  OD1 ASN A  35      15.842  39.425   6.631  1.00 12.26           O  
ATOM    228  ND2 ASN A  35      13.701  38.752   6.615  1.00 13.06           N  
ATOM    229  N   ARG A  36      18.159  35.345   5.395  1.00  9.24           N  
ATOM    230  CA  ARG A  36      18.828  34.048   5.310  1.00 10.15           C  
ATOM    231  C   ARG A  36      18.330  33.000   6.309  1.00  8.92           C  
ATOM    232  O   ARG A  36      18.634  31.813   6.173  1.00  7.32           O  
ATOM    233  CB  ARG A  36      20.345  34.245   5.384  1.00 10.20           C  
ATOM    234  CG  ARG A  36      20.892  35.045   4.199  1.00 10.94           C  
ATOM    235  CD  ARG A  36      22.343  35.497   4.392  1.00 12.36           C  
ATOM    236  NE  ARG A  36      23.296  34.386   4.397  1.00 15.07           N  
ATOM    237  CZ  ARG A  36      23.869  33.873   3.310  1.00 15.04           C  
ATOM    238  NH1 ARG A  36      23.597  34.361   2.106  1.00 12.58           N  
ATOM    239  NH2 ARG A  36      24.721  32.865   3.429  1.00 12.64           N  
ATOM    240  N   THR A  37      17.580  33.451   7.312  1.00 11.43           N  
ATOM    241  CA  THR A  37      16.961  32.574   8.307  1.00 11.18           C  
ATOM    242  C   THR A  37      15.518  33.075   8.437  1.00 11.20           C  
ATOM    243  O   THR A  37      15.235  34.252   8.176  1.00 10.17           O  
ATOM    244  CB  THR A  37      17.674  32.585   9.693  1.00  8.26           C  
ATOM    245  OG1 THR A  37      17.685  33.908  10.235  1.00 11.07           O  
ATOM    246  CG2 THR A  37      19.097  32.061   9.569  1.00  8.52           C  
ATOM    247  N   THR A  38      14.620  32.186   8.840  1.00 10.53           N  
ATOM    248  CA  THR A  38      13.199  32.496   8.945  1.00 10.81           C  
ATOM    249  C   THR A  38      12.635  32.101  10.308  1.00  9.73           C  
ATOM    250  O   THR A  38      12.804  30.963  10.736  1.00 10.39           O  
ATOM    251  CB  THR A  38      12.424  31.721   7.843  1.00  8.67           C  
ATOM    252  OG1 THR A  38      12.848  32.171   6.552  1.00  9.67           O  
ATOM    253  CG2 THR A  38      10.919  31.926   7.977  1.00 10.93           C  
ATOM    254  N   PRO A  39      11.915  33.024  10.983  1.00 12.81           N  
ATOM    255  CA  PRO A  39      11.309  32.787  12.305  1.00 13.60           C  
ATOM    256  C   PRO A  39      10.397  31.557  12.317  1.00 12.35           C  
ATOM    257  O   PRO A  39       9.547  31.396  11.429  1.00 12.74           O  
ATOM    258  CB  PRO A  39      10.475  34.056  12.531  1.00 12.19           C  
ATOM    259  CG  PRO A  39      11.193  35.098  11.743  1.00 14.72           C  
ATOM    260  CD  PRO A  39      11.556  34.364  10.482  1.00 10.42           C  
ATOM    261  N   SER A  40      10.560  30.700  13.323  1.00 10.72           N  
ATOM    262  CA  SER A  40       9.726  29.510  13.440  1.00 10.80           C  
ATOM    263  C   SER A  40       8.391  29.903  14.085  1.00 10.92           C  
ATOM    264  O   SER A  40       8.030  29.407  15.158  1.00  9.45           O  
ATOM    265  CB  SER A  40      10.445  28.435  14.252  1.00  6.66           C  
ATOM    266  OG  SER A  40      11.617  28.011  13.578  1.00  6.61           O  
ATOM    267  N   TYR A  41       7.675  30.798  13.405  1.00 13.51           N  
ATOM    268  CA  TYR A  41       6.388  31.335  13.852  1.00 13.08           C  
ATOM    269  C   TYR A  41       5.273  31.058  12.852  1.00 14.02           C  
ATOM    270  O   TYR A  41       5.509  30.978  11.644  1.00 14.39           O  
ATOM    271  CB  TYR A  41       6.477  32.858  14.008  1.00 12.23           C  
ATOM    272  CG  TYR A  41       7.088  33.343  15.296  1.00 14.59           C  
ATOM    273  CD1 TYR A  41       8.354  32.917  15.696  1.00 18.34           C  
ATOM    274  CD2 TYR A  41       6.404  34.242  16.115  1.00 17.76           C  
ATOM    275  CE1 TYR A  41       8.927  33.375  16.879  1.00 21.29           C  
ATOM    276  CE2 TYR A  41       6.968  34.708  17.301  1.00 18.42           C  
ATOM    277  CZ  TYR A  41       8.230  34.267  17.677  1.00 21.52           C  
ATOM    278  OH  TYR A  41       8.795  34.702  18.853  1.00 26.49           O  
ATOM    279  N   VAL A  42       4.053  30.946  13.366  1.00 15.99           N  
ATOM    280  CA  VAL A  42       2.863  30.728  12.548  1.00 14.29           C  
ATOM    281  C   VAL A  42       1.765  31.506  13.277  1.00 15.42           C  
ATOM    282  O   VAL A  42       1.647  31.409  14.500  1.00 14.21           O  
ATOM    283  CB  VAL A  42       2.463  29.223  12.453  1.00 14.30           C  
ATOM    284  CG1 VAL A  42       1.347  29.042  11.436  1.00 20.37           C  
ATOM    285  CG2 VAL A  42       3.644  28.371  12.029  1.00 15.89           C  
ATOM    286  N   ALA A  43       1.012  32.324  12.549  1.00 15.15           N  
ATOM    287  CA  ALA A  43      -0.065  33.119  13.147  1.00 14.24           C  
ATOM    288  C   ALA A  43      -1.391  32.829  12.457  1.00 13.57           C  
ATOM    289  O   ALA A  43      -1.426  32.510  11.271  1.00 13.60           O  
ATOM    290  CB  ALA A  43       0.255  34.602  13.058  1.00  9.93           C  
ATOM    291  N   PHE A  44      -2.480  32.953  13.205  1.00 13.78           N  
ATOM    292  CA  PHE A  44      -3.816  32.703  12.676  1.00 13.77           C  
ATOM    293  C   PHE A  44      -4.661  33.938  12.951  1.00 15.35           C  
ATOM    294  O   PHE A  44      -4.586  34.523  14.034  1.00 14.10           O  
ATOM    295  CB  PHE A  44      -4.427  31.473  13.353  1.00 14.37           C  
ATOM    296  CG  PHE A  44      -3.578  30.227  13.238  1.00 15.52           C  
ATOM    297  CD1 PHE A  44      -2.523  29.999  14.125  1.00 11.21           C  
ATOM    298  CD2 PHE A  44      -3.829  29.289  12.239  1.00 13.54           C  
ATOM    299  CE1 PHE A  44      -1.734  28.848  14.020  1.00 10.92           C  
ATOM    300  CE2 PHE A  44      -3.042  28.130  12.124  1.00 12.66           C  
ATOM    301  CZ  PHE A  44      -1.994  27.913  13.017  1.00 10.87           C  
ATOM    302  N   THR A  45      -5.423  34.371  11.956  1.00 15.62           N  
ATOM    303  CA  THR A  45      -6.259  35.552  12.103  1.00 16.44           C  
ATOM    304  C   THR A  45      -7.677  35.244  11.632  1.00 16.36           C  
ATOM    305  O   THR A  45      -8.003  34.094  11.329  1.00 14.35           O  
ATOM    306  CB  THR A  45      -5.682  36.747  11.289  1.00 18.00           C  
ATOM    307  OG1 THR A  45      -5.784  36.473   9.887  1.00 17.35           O  
ATOM    308  CG2 THR A  45      -4.207  36.976  11.639  1.00 16.83           C  
ATOM    309  N   ASP A  46      -8.525  36.266  11.607  1.00 16.29           N  
ATOM    310  CA  ASP A  46      -9.903  36.107  11.161  1.00 18.03           C  
ATOM    311  C   ASP A  46      -9.953  35.728   9.690  1.00 17.57           C  
ATOM    312  O   ASP A  46     -10.901  35.089   9.239  1.00 18.68           O  
ATOM    313  CB  ASP A  46     -10.683  37.416  11.334  1.00 19.40           C  
ATOM    314  CG  ASP A  46     -11.090  37.685  12.770  1.00 19.65           C  
ATOM    315  OD1 ASP A  46     -11.086  36.749  13.596  1.00 23.59           O  
ATOM    316  OD2 ASP A  46     -11.444  38.847  13.067  1.00 24.70           O  
ATOM    317  N   THR A  47      -8.919  36.097   8.946  1.00 16.31           N  
ATOM    318  CA  THR A  47      -8.907  35.833   7.523  1.00 16.99           C  
ATOM    319  C   THR A  47      -7.758  35.018   6.969  1.00 19.35           C  
ATOM    320  O   THR A  47      -7.892  34.424   5.895  1.00 19.08           O  
ATOM    321  CB  THR A  47      -8.957  37.156   6.731  1.00 18.56           C  
ATOM    322  OG1 THR A  47      -7.851  37.987   7.108  1.00 15.21           O  
ATOM    323  CG2 THR A  47     -10.258  37.899   7.013  1.00 18.67           C  
ATOM    324  N   GLU A  48      -6.631  34.977   7.670  1.00 18.89           N  
ATOM    325  CA  GLU A  48      -5.499  34.246   7.133  1.00 20.72           C  
ATOM    326  C   GLU A  48      -4.563  33.600   8.136  1.00 19.63           C  
ATOM    327  O   GLU A  48      -4.675  33.807   9.341  1.00 14.93           O  
ATOM    328  CB  GLU A  48      -4.703  35.157   6.194  1.00 24.77           C  
ATOM    329  CG  GLU A  48      -4.180  36.418   6.851  1.00 29.38           C  
ATOM    330  CD  GLU A  48      -3.485  37.360   5.879  1.00 32.20           C  
ATOM    331  OE1 GLU A  48      -3.302  37.002   4.695  1.00 32.65           O  
ATOM    332  OE2 GLU A  48      -3.112  38.469   6.310  1.00 35.07           O  
ATOM    333  N   ARG A  49      -3.671  32.771   7.605  1.00 17.35           N  
ATOM    334  CA  ARG A  49      -2.666  32.070   8.385  1.00 17.43           C  
ATOM    335  C   ARG A  49      -1.338  32.602   7.860  1.00 15.74           C  
ATOM    336  O   ARG A  49      -1.108  32.622   6.647  1.00 15.97           O  
ATOM    337  CB  ARG A  49      -2.783  30.567   8.154  1.00 19.72           C  
ATOM    338  CG  ARG A  49      -1.722  29.727   8.840  1.00 26.38           C  
ATOM    339  CD  ARG A  49      -1.911  28.257   8.502  1.00 29.40           C  
ATOM    340  NE  ARG A  49      -2.608  28.117   7.225  1.00 36.76           N  
ATOM    341  CZ  ARG A  49      -3.263  27.027   6.841  1.00 44.00           C  
ATOM    342  NH1 ARG A  49      -3.288  25.947   7.619  1.00 46.22           N  
ATOM    343  NH2 ARG A  49      -3.878  27.017   5.665  1.00 42.40           N  
ATOM    344  N   LEU A  50      -0.492  33.076   8.767  1.00 14.10           N  
ATOM    345  CA  LEU A  50       0.798  33.648   8.407  1.00 12.23           C  
ATOM    346  C   LEU A  50       1.936  32.764   8.914  1.00 13.25           C  
ATOM    347  O   LEU A  50       1.811  32.128   9.957  1.00 15.86           O  
ATOM    348  CB  LEU A  50       0.896  35.057   8.995  1.00 10.18           C  
ATOM    349  CG  LEU A  50      -0.254  35.984   8.585  1.00 11.19           C  
ATOM    350  CD1 LEU A  50      -0.303  37.239   9.439  1.00 12.38           C  
ATOM    351  CD2 LEU A  50      -0.128  36.333   7.121  1.00 11.31           C  
ATOM    352  N   ILE A  51       3.027  32.691   8.161  1.00 15.25           N  
ATOM    353  CA  ILE A  51       4.171  31.868   8.559  1.00 15.27           C  
ATOM    354  C   ILE A  51       5.474  32.645   8.382  1.00 14.59           C  
ATOM    355  O   ILE A  51       5.593  33.462   7.468  1.00 16.37           O  
ATOM    356  CB  ILE A  51       4.266  30.544   7.727  1.00 14.88           C  
ATOM    357  CG1 ILE A  51       2.995  29.703   7.878  1.00 13.93           C  
ATOM    358  CG2 ILE A  51       5.452  29.705   8.191  1.00 12.04           C  
ATOM    359  CD1 ILE A  51       2.050  29.817   6.720  1.00 17.80           C  
ATOM    360  N   GLY A  52       6.428  32.420   9.279  1.00 12.03           N  
ATOM    361  CA  GLY A  52       7.715  33.081   9.175  1.00  8.93           C  
ATOM    362  C   GLY A  52       7.711  34.556   9.508  1.00  9.72           C  
ATOM    363  O   GLY A  52       7.087  34.964  10.484  1.00 12.22           O  
ATOM    364  N   ASP A  53       8.404  35.356   8.699  1.00  7.33           N  
ATOM    365  CA  ASP A  53       8.496  36.801   8.917  1.00  8.88           C  
ATOM    366  C   ASP A  53       7.135  37.462   9.099  1.00  8.87           C  
ATOM    367  O   ASP A  53       6.945  38.249  10.020  1.00 10.75           O  
ATOM    368  CB  ASP A  53       9.231  37.490   7.757  1.00  8.68           C  
ATOM    369  CG  ASP A  53      10.730  37.202   7.744  1.00 12.27           C  
ATOM    370  OD1 ASP A  53      11.329  36.990   8.823  1.00 13.26           O  
ATOM    371  OD2 ASP A  53      11.316  37.205   6.646  1.00 13.04           O  
ATOM    372  N   ALA A  54       6.203  37.152   8.205  1.00 11.50           N  
ATOM    373  CA  ALA A  54       4.859  37.720   8.257  1.00 11.30           C  
ATOM    374  C   ALA A  54       4.187  37.452   9.600  1.00 12.35           C  
ATOM    375  O   ALA A  54       3.412  38.281  10.084  1.00 16.25           O  
ATOM    376  CB  ALA A  54       4.006  37.166   7.128  1.00 10.15           C  
ATOM    377  N   ALA A  55       4.477  36.295  10.193  1.00 10.08           N  
ATOM    378  CA  ALA A  55       3.894  35.932  11.478  1.00 10.80           C  
ATOM    379  C   ALA A  55       4.569  36.661  12.637  1.00 13.69           C  
ATOM    380  O   ALA A  55       3.898  37.270  13.471  1.00 12.37           O  
ATOM    381  CB  ALA A  55       3.951  34.433  11.682  1.00 10.70           C  
ATOM    382  N   LYS A  56       5.896  36.640  12.679  1.00 15.15           N  
ATOM    383  CA  LYS A  56       6.597  37.318  13.763  1.00 15.34           C  
ATOM    384  C   LYS A  56       6.373  38.827  13.704  1.00 14.15           C  
ATOM    385  O   LYS A  56       6.329  39.496  14.733  1.00 14.98           O  
ATOM    386  CB  LYS A  56       8.097  36.992  13.745  1.00 19.44           C  
ATOM    387  CG  LYS A  56       8.821  37.418  15.020  1.00 18.93           C  
ATOM    388  CD  LYS A  56      10.182  36.751  15.166  1.00 23.71           C  
ATOM    389  CE  LYS A  56      10.858  37.174  16.469  1.00 24.53           C  
ATOM    390  NZ  LYS A  56      12.163  36.495  16.682  1.00 26.77           N  
ATOM    391  N   ASN A  57       6.183  39.363  12.506  1.00 16.11           N  
ATOM    392  CA  ASN A  57       5.967  40.798  12.365  1.00 20.42           C  
ATOM    393  C   ASN A  57       4.703  41.324  13.046  1.00 21.52           C  
ATOM    394  O   ASN A  57       4.629  42.502  13.386  1.00 26.04           O  
ATOM    395  CB  ASN A  57       5.992  41.214  10.890  1.00 23.16           C  
ATOM    396  CG  ASN A  57       7.388  41.150  10.291  1.00 26.43           C  
ATOM    397  OD1 ASN A  57       8.375  40.928  11.002  1.00 28.00           O  
ATOM    398  ND2 ASN A  57       7.478  41.334   8.979  1.00 25.60           N  
ATOM    399  N   GLN A  58       3.725  40.456  13.281  1.00 21.46           N  
ATOM    400  CA  GLN A  58       2.483  40.879  13.924  1.00 20.35           C  
ATOM    401  C   GLN A  58       2.236  40.221  15.297  1.00 23.94           C  
ATOM    402  O   GLN A  58       1.138  40.328  15.865  1.00 25.01           O  
ATOM    403  CB  GLN A  58       1.301  40.634  12.975  1.00 14.77           C  
ATOM    404  CG  GLN A  58       1.175  39.205  12.454  1.00 11.22           C  
ATOM    405  CD  GLN A  58       0.464  38.283  13.424  1.00 14.76           C  
ATOM    406  OE1 GLN A  58      -0.766  38.286  13.517  1.00 18.54           O  
ATOM    407  NE2 GLN A  58       1.227  37.496  14.160  1.00 15.69           N  
ATOM    408  N   VAL A  59       3.270  39.590  15.849  1.00 23.03           N  
ATOM    409  CA  VAL A  59       3.173  38.906  17.139  1.00 21.73           C  
ATOM    410  C   VAL A  59       2.763  39.830  18.293  1.00 22.90           C  
ATOM    411  O   VAL A  59       2.052  39.413  19.212  1.00 21.64           O  
ATOM    412  CB  VAL A  59       4.505  38.177  17.484  1.00 20.84           C  
ATOM    413  CG1 VAL A  59       5.637  39.180  17.689  1.00 18.36           C  
ATOM    414  CG2 VAL A  59       4.326  37.288  18.703  1.00 22.25           C  
ATOM    415  N   ALA A  60       3.161  41.098  18.200  1.00 24.83           N  
ATOM    416  CA  ALA A  60       2.864  42.102  19.221  1.00 24.72           C  
ATOM    417  C   ALA A  60       1.387  42.485  19.324  1.00 26.49           C  
ATOM    418  O   ALA A  60       0.941  42.985  20.361  1.00 27.73           O  
ATOM    419  CB  ALA A  60       3.710  43.348  18.984  1.00 23.94           C  
ATOM    420  N   MET A  61       0.629  42.253  18.256  1.00 25.62           N  
ATOM    421  CA  MET A  61      -0.790  42.600  18.243  1.00 24.09           C  
ATOM    422  C   MET A  61      -1.716  41.388  18.252  1.00 20.56           C  
ATOM    423  O   MET A  61      -2.914  41.523  18.501  1.00 21.73           O  
ATOM    424  CB  MET A  61      -1.108  43.487  17.031  1.00 24.41           C  
ATOM    425  CG  MET A  61      -0.966  42.792  15.689  1.00 23.46           C  
ATOM    426  SD  MET A  61      -1.405  43.861  14.313  1.00 29.97           S  
ATOM    427  CE  MET A  61      -3.169  43.737  14.353  1.00 26.58           C  
ATOM    428  N   ASN A  62      -1.154  40.207  18.016  1.00 18.01           N  
ATOM    429  CA  ASN A  62      -1.925  38.967  17.976  1.00 15.56           C  
ATOM    430  C   ASN A  62      -1.215  37.889  18.814  1.00 16.71           C  
ATOM    431  O   ASN A  62      -1.109  36.738  18.393  1.00 20.70           O  
ATOM    432  CB  ASN A  62      -2.041  38.538  16.504  1.00 17.51           C  
ATOM    433  CG  ASN A  62      -2.889  37.301  16.301  1.00 17.80           C  
ATOM    434  OD1 ASN A  62      -3.734  36.962  17.132  1.00 22.58           O  
ATOM    435  ND2 ASN A  62      -2.683  36.629  15.175  1.00 15.45           N  
ATOM    436  N   PRO A  63      -0.815  38.223  20.058  1.00 16.36           N  
ATOM    437  CA  PRO A  63      -0.115  37.279  20.941  1.00 15.07           C  
ATOM    438  C   PRO A  63      -0.801  35.944  21.204  1.00 15.93           C  
ATOM    439  O   PRO A  63      -0.135  34.916  21.321  1.00 15.58           O  
ATOM    440  CB  PRO A  63       0.044  38.078  22.232  1.00 15.29           C  
ATOM    441  CG  PRO A  63      -1.175  38.948  22.240  1.00 17.07           C  
ATOM    442  CD  PRO A  63      -1.204  39.430  20.814  1.00 16.63           C  
ATOM    443  N   THR A  64      -2.126  35.959  21.295  1.00 14.67           N  
ATOM    444  CA  THR A  64      -2.894  34.753  21.569  1.00 17.41           C  
ATOM    445  C   THR A  64      -2.953  33.739  20.426  1.00 17.65           C  
ATOM    446  O   THR A  64      -3.013  32.527  20.660  1.00 18.57           O  
ATOM    447  CB  THR A  64      -4.331  35.134  21.986  1.00 21.48           C  
ATOM    448  OG1 THR A  64      -4.299  35.764  23.275  1.00 25.76           O  
ATOM    449  CG2 THR A  64      -5.246  33.921  22.017  1.00 23.04           C  
ATOM    450  N   ASN A  65      -2.921  34.225  19.190  1.00 16.46           N  
ATOM    451  CA  ASN A  65      -3.019  33.331  18.046  1.00 15.21           C  
ATOM    452  C   ASN A  65      -1.747  33.215  17.223  1.00 14.84           C  
ATOM    453  O   ASN A  65      -1.782  32.751  16.086  1.00 16.56           O  
ATOM    454  CB  ASN A  65      -4.204  33.738  17.160  1.00 16.53           C  
ATOM    455  CG  ASN A  65      -5.518  33.814  17.935  1.00 15.35           C  
ATOM    456  OD1 ASN A  65      -5.988  32.823  18.500  1.00 15.37           O  
ATOM    457  ND2 ASN A  65      -6.106  34.998  17.973  1.00 11.99           N  
ATOM    458  N   THR A  66      -0.630  33.660  17.787  1.00 15.42           N  
ATOM    459  CA  THR A  66       0.666  33.570  17.115  1.00 12.64           C  
ATOM    460  C   THR A  66       1.467  32.509  17.873  1.00 11.67           C  
ATOM    461  O   THR A  66       1.812  32.680  19.044  1.00 12.72           O  
ATOM    462  CB  THR A  66       1.408  34.920  17.118  1.00 11.74           C  
ATOM    463  OG1 THR A  66       0.587  35.907  16.487  1.00 11.29           O  
ATOM    464  CG2 THR A  66       2.726  34.813  16.348  1.00  9.77           C  
ATOM    465  N   VAL A  67       1.705  31.389  17.206  1.00 11.05           N  
ATOM    466  CA  VAL A  67       2.410  30.270  17.798  1.00 11.12           C  
ATOM    467  C   VAL A  67       3.897  30.253  17.476  1.00 10.63           C  
ATOM    468  O   VAL A  67       4.311  30.559  16.357  1.00 10.97           O  
ATOM    469  CB  VAL A  67       1.783  28.935  17.334  1.00  9.11           C  
ATOM    470  CG1 VAL A  67       2.385  27.775  18.091  1.00  9.13           C  
ATOM    471  CG2 VAL A  67       0.271  28.968  17.527  1.00 14.23           C  
ATOM    472  N   PHE A  68       4.686  29.890  18.475  1.00  9.52           N  
ATOM    473  CA  PHE A  68       6.131  29.781  18.346  1.00 11.69           C  
ATOM    474  C   PHE A  68       6.522  28.723  19.375  1.00 12.13           C  
ATOM    475  O   PHE A  68       5.661  28.239  20.113  1.00 12.78           O  
ATOM    476  CB  PHE A  68       6.823  31.134  18.615  1.00  9.41           C  
ATOM    477  CG  PHE A  68       6.540  31.705  19.978  1.00 11.00           C  
ATOM    478  CD1 PHE A  68       7.331  31.364  21.070  1.00 10.83           C  
ATOM    479  CD2 PHE A  68       5.466  32.559  20.174  1.00  8.62           C  
ATOM    480  CE1 PHE A  68       7.051  31.856  22.339  1.00 12.00           C  
ATOM    481  CE2 PHE A  68       5.177  33.056  21.437  1.00 15.15           C  
ATOM    482  CZ  PHE A  68       5.972  32.703  22.523  1.00 10.65           C  
ATOM    483  N   ASP A  69       7.789  28.319  19.389  1.00 12.69           N  
ATOM    484  CA  ASP A  69       8.262  27.310  20.339  1.00 11.33           C  
ATOM    485  C   ASP A  69       7.616  25.931  20.196  1.00 11.18           C  
ATOM    486  O   ASP A  69       7.630  25.137  21.145  1.00 10.07           O  
ATOM    487  CB  ASP A  69       8.073  27.796  21.779  1.00 12.07           C  
ATOM    488  CG  ASP A  69       9.249  28.585  22.296  1.00 14.37           C  
ATOM    489  OD1 ASP A  69      10.222  28.818  21.545  1.00 14.73           O  
ATOM    490  OD2 ASP A  69       9.198  28.967  23.477  1.00 13.20           O  
ATOM    491  N   ALA A  70       7.097  25.622  19.012  1.00  9.64           N  
ATOM    492  CA  ALA A  70       6.461  24.323  18.787  1.00 10.78           C  
ATOM    493  C   ALA A  70       7.460  23.194  19.023  1.00  9.73           C  
ATOM    494  O   ALA A  70       7.090  22.110  19.477  1.00  8.24           O  
ATOM    495  CB  ALA A  70       5.895  24.240  17.375  1.00  9.65           C  
ATOM    496  N   LYS A  71       8.735  23.474  18.760  1.00  8.59           N  
ATOM    497  CA  LYS A  71       9.801  22.488  18.935  1.00  9.39           C  
ATOM    498  C   LYS A  71       9.927  22.018  20.391  1.00  9.16           C  
ATOM    499  O   LYS A  71      10.400  20.914  20.663  1.00  8.21           O  
ATOM    500  CB  LYS A  71      11.137  23.071  18.448  1.00  8.65           C  
ATOM    501  CG  LYS A  71      12.230  22.035  18.232  1.00  7.52           C  
ATOM    502  CD  LYS A  71      13.472  22.677  17.633  1.00  6.14           C  
ATOM    503  CE  LYS A  71      14.567  21.655  17.413  1.00  6.90           C  
ATOM    504  NZ  LYS A  71      15.696  22.276  16.680  1.00  7.43           N  
ATOM    505  N   ARG A  72       9.480  22.852  21.324  1.00 11.42           N  
ATOM    506  CA  ARG A  72       9.540  22.508  22.742  1.00  9.78           C  
ATOM    507  C   ARG A  72       8.464  21.484  23.122  1.00 11.09           C  
ATOM    508  O   ARG A  72       8.573  20.802  24.148  1.00 11.78           O  
ATOM    509  CB  ARG A  72       9.418  23.768  23.600  1.00  6.75           C  
ATOM    510  CG  ARG A  72      10.588  24.729  23.444  1.00  7.88           C  
ATOM    511  CD  ARG A  72      10.514  25.842  24.473  1.00  9.69           C  
ATOM    512  NE  ARG A  72      11.629  26.786  24.376  1.00 12.94           N  
ATOM    513  CZ  ARG A  72      12.804  26.636  24.987  1.00 11.68           C  
ATOM    514  NH1 ARG A  72      13.036  25.576  25.744  1.00 13.61           N  
ATOM    515  NH2 ARG A  72      13.752  27.550  24.839  1.00 10.79           N  
ATOM    516  N   LEU A  73       7.443  21.366  22.276  1.00 11.84           N  
ATOM    517  CA  LEU A  73       6.336  20.437  22.494  1.00 10.26           C  
ATOM    518  C   LEU A  73       6.423  19.194  21.625  1.00  9.56           C  
ATOM    519  O   LEU A  73       5.909  18.137  21.988  1.00  9.58           O  
ATOM    520  CB  LEU A  73       5.007  21.117  22.160  1.00 11.79           C  
ATOM    521  CG  LEU A  73       4.491  22.270  23.009  1.00 11.95           C  
ATOM    522  CD1 LEU A  73       3.349  22.947  22.282  1.00 12.40           C  
ATOM    523  CD2 LEU A  73       4.057  21.755  24.375  1.00 12.77           C  
ATOM    524  N   ILE A  74       7.031  19.339  20.456  1.00 11.44           N  
ATOM    525  CA  ILE A  74       7.116  18.249  19.501  1.00 10.90           C  
ATOM    526  C   ILE A  74       7.616  16.897  20.035  1.00 13.63           C  
ATOM    527  O   ILE A  74       8.682  16.791  20.652  1.00 13.09           O  
ATOM    528  CB  ILE A  74       7.850  18.709  18.204  1.00 14.51           C  
ATOM    529  CG1 ILE A  74       7.352  17.905  16.997  1.00 11.59           C  
ATOM    530  CG2 ILE A  74       9.359  18.601  18.361  1.00 13.53           C  
ATOM    531  CD1 ILE A  74       7.748  18.491  15.651  1.00  8.73           C  
ATOM    532  N   GLY A  75       6.776  15.883  19.846  1.00 11.78           N  
ATOM    533  CA  GLY A  75       7.075  14.532  20.277  1.00 13.13           C  
ATOM    534  C   GLY A  75       6.905  14.250  21.762  1.00 12.23           C  
ATOM    535  O   GLY A  75       7.241  13.156  22.220  1.00 15.06           O  
ATOM    536  N   ARG A  76       6.381  15.213  22.514  1.00 12.16           N  
ATOM    537  CA  ARG A  76       6.198  15.050  23.954  1.00 12.90           C  
ATOM    538  C   ARG A  76       4.757  14.795  24.357  1.00 13.22           C  
ATOM    539  O   ARG A  76       3.826  15.153  23.639  1.00 13.48           O  
ATOM    540  CB  ARG A  76       6.697  16.285  24.697  1.00 12.92           C  
ATOM    541  CG  ARG A  76       8.175  16.549  24.557  1.00 16.34           C  
ATOM    542  CD  ARG A  76       8.514  17.804  25.321  1.00 20.09           C  
ATOM    543  NE  ARG A  76       9.915  18.191  25.200  1.00 24.82           N  
ATOM    544  CZ  ARG A  76      10.911  17.670  25.911  1.00 23.14           C  
ATOM    545  NH1 ARG A  76      10.682  16.709  26.797  1.00 21.66           N  
ATOM    546  NH2 ARG A  76      12.144  18.111  25.721  1.00 25.71           N  
ATOM    547  N   ARG A  77       4.580  14.180  25.523  1.00 14.20           N  
ATOM    548  CA  ARG A  77       3.250  13.902  26.040  1.00 13.40           C  
ATOM    549  C   ARG A  77       2.806  15.125  26.829  1.00 15.38           C  
ATOM    550  O   ARG A  77       3.636  15.873  27.344  1.00 14.37           O  
ATOM    551  CB  ARG A  77       3.276  12.671  26.924  1.00 15.44           C  
ATOM    552  N   PHE A  78       1.499  15.342  26.908  1.00 16.00           N  
ATOM    553  CA  PHE A  78       0.963  16.490  27.632  1.00 18.71           C  
ATOM    554  C   PHE A  78       1.435  16.494  29.085  1.00 19.21           C  
ATOM    555  O   PHE A  78       1.771  17.534  29.641  1.00 20.03           O  
ATOM    556  CB  PHE A  78      -0.574  16.485  27.581  1.00 17.78           C  
ATOM    557  CG  PHE A  78      -1.208  17.670  28.256  1.00 14.22           C  
ATOM    558  CD1 PHE A  78      -1.291  18.891  27.603  1.00 13.33           C  
ATOM    559  CD2 PHE A  78      -1.697  17.566  29.557  1.00 15.78           C  
ATOM    560  CE1 PHE A  78      -1.848  19.998  28.233  1.00 15.09           C  
ATOM    561  CE2 PHE A  78      -2.258  18.667  30.200  1.00 14.12           C  
ATOM    562  CZ  PHE A  78      -2.334  19.885  29.538  1.00 14.95           C  
ATOM    563  N   ASP A  79       1.492  15.309  29.673  1.00 22.86           N  
ATOM    564  CA  ASP A  79       1.901  15.146  31.054  1.00 26.74           C  
ATOM    565  C   ASP A  79       3.356  15.467  31.335  1.00 27.60           C  
ATOM    566  O   ASP A  79       3.770  15.524  32.498  1.00 29.65           O  
ATOM    567  CB  ASP A  79       1.614  13.722  31.497  1.00 36.10           C  
ATOM    568  CG  ASP A  79       0.541  13.663  32.540  1.00 45.45           C  
ATOM    569  OD1 ASP A  79       0.878  13.890  33.723  1.00 53.16           O  
ATOM    570  OD2 ASP A  79      -0.633  13.414  32.186  1.00 48.73           O  
ATOM    571  N   ASP A  80       4.134  15.631  30.272  1.00 25.13           N  
ATOM    572  CA  ASP A  80       5.555  15.916  30.385  1.00 21.50           C  
ATOM    573  C   ASP A  80       5.795  17.148  31.244  1.00 17.02           C  
ATOM    574  O   ASP A  80       5.289  18.226  30.950  1.00 16.49           O  
ATOM    575  CB  ASP A  80       6.150  16.117  28.989  1.00 22.30           C  
ATOM    576  CG  ASP A  80       7.649  15.903  28.949  1.00 25.92           C  
ATOM    577  OD1 ASP A  80       8.360  16.357  29.875  1.00 31.85           O  
ATOM    578  OD2 ASP A  80       8.123  15.284  27.973  1.00 27.94           O  
ATOM    579  N   ALA A  81       6.604  16.981  32.286  1.00 17.97           N  
ATOM    580  CA  ALA A  81       6.935  18.066  33.208  1.00 18.37           C  
ATOM    581  C   ALA A  81       7.444  19.311  32.484  1.00 17.11           C  
ATOM    582  O   ALA A  81       7.125  20.432  32.875  1.00 18.28           O  
ATOM    583  CB  ALA A  81       7.968  17.593  34.230  1.00 18.22           C  
ATOM    584  N   VAL A  82       8.237  19.122  31.433  1.00 18.43           N  
ATOM    585  CA  VAL A  82       8.752  20.265  30.687  1.00 18.89           C  
ATOM    586  C   VAL A  82       7.611  20.961  29.942  1.00 15.46           C  
ATOM    587  O   VAL A  82       7.588  22.185  29.846  1.00 14.78           O  
ATOM    588  CB  VAL A  82       9.899  19.871  29.713  1.00 22.15           C  
ATOM    589  CG1 VAL A  82       9.391  18.980  28.612  1.00 28.57           C  
ATOM    590  CG2 VAL A  82      10.521  21.109  29.116  1.00 25.61           C  
ATOM    591  N   VAL A  83       6.651  20.187  29.442  1.00 13.84           N  
ATOM    592  CA  VAL A  83       5.510  20.771  28.742  1.00 15.12           C  
ATOM    593  C   VAL A  83       4.715  21.594  29.760  1.00 14.25           C  
ATOM    594  O   VAL A  83       4.437  22.777  29.547  1.00 14.63           O  
ATOM    595  CB  VAL A  83       4.602  19.674  28.112  1.00 15.88           C  
ATOM    596  CG1 VAL A  83       3.307  20.286  27.578  1.00 16.48           C  
ATOM    597  CG2 VAL A  83       5.341  18.960  26.984  1.00 14.45           C  
ATOM    598  N   GLN A  84       4.450  20.987  30.913  1.00 16.47           N  
ATOM    599  CA  GLN A  84       3.699  21.644  31.978  1.00 17.82           C  
ATOM    600  C   GLN A  84       4.363  22.948  32.429  1.00 15.43           C  
ATOM    601  O   GLN A  84       3.681  23.932  32.722  1.00 15.29           O  
ATOM    602  CB  GLN A  84       3.496  20.675  33.149  1.00 19.22           C  
ATOM    603  CG  GLN A  84       2.668  19.439  32.784  1.00 19.81           C  
ATOM    604  CD  GLN A  84       1.287  19.815  32.276  1.00 25.32           C  
ATOM    605  OE1 GLN A  84       0.908  19.489  31.149  1.00 24.78           O  
ATOM    606  NE2 GLN A  84       0.527  20.498  33.107  1.00 28.64           N  
ATOM    607  N   SER A  85       5.694  22.962  32.434  1.00 18.43           N  
ATOM    608  CA  SER A  85       6.456  24.146  32.826  1.00 18.51           C  
ATOM    609  C   SER A  85       6.382  25.225  31.751  1.00 14.30           C  
ATOM    610  O   SER A  85       6.043  26.375  32.031  1.00 15.56           O  
ATOM    611  CB  SER A  85       7.931  23.789  33.046  1.00 21.93           C  
ATOM    612  OG  SER A  85       8.092  22.780  34.027  1.00 35.29           O  
ATOM    613  N   ASP A  86       6.705  24.842  30.520  1.00 15.48           N  
ATOM    614  CA  ASP A  86       6.717  25.771  29.390  1.00 15.48           C  
ATOM    615  C   ASP A  86       5.385  26.475  29.153  1.00 17.05           C  
ATOM    616  O   ASP A  86       5.350  27.685  28.903  1.00 15.32           O  
ATOM    617  CB  ASP A  86       7.156  25.049  28.112  1.00 14.03           C  
ATOM    618  CG  ASP A  86       8.623  24.631  28.133  1.00 15.67           C  
ATOM    619  OD1 ASP A  86       9.406  25.145  28.958  1.00 15.72           O  
ATOM    620  OD2 ASP A  86       9.001  23.782  27.304  1.00 14.83           O  
ATOM    621  N   MET A  87       4.300  25.709  29.241  1.00 18.29           N  
ATOM    622  CA  MET A  87       2.941  26.211  29.040  1.00 20.50           C  
ATOM    623  C   MET A  87       2.627  27.490  29.804  1.00 20.88           C  
ATOM    624  O   MET A  87       1.913  28.362  29.315  1.00 20.68           O  
ATOM    625  CB  MET A  87       1.932  25.146  29.469  1.00 22.22           C  
ATOM    626  CG  MET A  87       1.734  24.023  28.485  1.00 25.35           C  
ATOM    627  SD  MET A  87       0.777  22.708  29.234  1.00 26.29           S  
ATOM    628  CE  MET A  87      -0.675  23.574  29.718  1.00 28.84           C  
ATOM    629  N   LYS A  88       3.170  27.595  31.008  1.00 21.88           N  
ATOM    630  CA  LYS A  88       2.933  28.748  31.853  1.00 23.09           C  
ATOM    631  C   LYS A  88       3.481  30.053  31.298  1.00 25.06           C  
ATOM    632  O   LYS A  88       3.029  31.135  31.677  1.00 26.60           O  
ATOM    633  CB  LYS A  88       3.514  28.492  33.235  1.00 26.67           C  
ATOM    634  CG  LYS A  88       2.973  27.240  33.886  1.00 31.49           C  
ATOM    635  CD  LYS A  88       3.436  27.155  35.317  1.00 38.73           C  
ATOM    636  CE  LYS A  88       3.043  25.839  35.953  1.00 42.57           C  
ATOM    637  NZ  LYS A  88       3.931  25.591  37.116  1.00 47.92           N  
ATOM    638  N   HIS A  89       4.446  29.957  30.391  1.00 23.19           N  
ATOM    639  CA  HIS A  89       5.060  31.148  29.818  1.00 23.07           C  
ATOM    640  C   HIS A  89       4.518  31.567  28.457  1.00 21.22           C  
ATOM    641  O   HIS A  89       4.734  32.703  28.028  1.00 23.38           O  
ATOM    642  CB  HIS A  89       6.575  30.959  29.733  1.00 25.44           C  
ATOM    643  CG  HIS A  89       7.209  30.642  31.049  1.00 29.80           C  
ATOM    644  ND1 HIS A  89       7.348  31.572  32.053  1.00 32.34           N  
ATOM    645  CD2 HIS A  89       7.720  29.482  31.537  1.00 32.00           C  
ATOM    646  CE1 HIS A  89       7.915  31.006  33.106  1.00 33.48           C  
ATOM    647  NE2 HIS A  89       8.149  29.739  32.815  1.00 36.04           N  
ATOM    648  N   TRP A  90       3.804  30.670  27.788  1.00 16.79           N  
ATOM    649  CA  TRP A  90       3.267  30.967  26.467  1.00 14.05           C  
ATOM    650  C   TRP A  90       1.940  31.702  26.490  1.00 14.54           C  
ATOM    651  O   TRP A  90       1.066  31.392  27.301  1.00 15.45           O  
ATOM    652  CB  TRP A  90       3.109  29.684  25.669  1.00 14.60           C  
ATOM    653  CG  TRP A  90       4.395  29.001  25.356  1.00 12.15           C  
ATOM    654  CD1 TRP A  90       5.587  29.593  25.039  1.00  8.36           C  
ATOM    655  CD2 TRP A  90       4.621  27.585  25.293  1.00 11.83           C  
ATOM    656  NE1 TRP A  90       6.530  28.632  24.781  1.00  8.63           N  
ATOM    657  CE2 TRP A  90       5.970  27.405  24.920  1.00  9.50           C  
ATOM    658  CE3 TRP A  90       3.801  26.468  25.505  1.00 12.50           C  
ATOM    659  CZ2 TRP A  90       6.526  26.125  24.769  1.00  9.82           C  
ATOM    660  CZ3 TRP A  90       4.360  25.201  25.351  1.00 11.76           C  
ATOM    661  CH2 TRP A  90       5.710  25.041  24.980  1.00 11.26           C  
ATOM    662  N   PRO A  91       1.775  32.694  25.590  1.00 14.65           N  
ATOM    663  CA  PRO A  91       0.533  33.476  25.495  1.00 15.72           C  
ATOM    664  C   PRO A  91      -0.584  32.729  24.747  1.00 17.12           C  
ATOM    665  O   PRO A  91      -1.750  33.129  24.793  1.00 17.63           O  
ATOM    666  CB  PRO A  91       0.999  34.738  24.760  1.00 11.85           C  
ATOM    667  CG  PRO A  91       2.048  34.207  23.843  1.00 14.70           C  
ATOM    668  CD  PRO A  91       2.823  33.265  24.733  1.00 14.39           C  
ATOM    669  N   PHE A  92      -0.223  31.654  24.049  1.00 17.57           N  
ATOM    670  CA  PHE A  92      -1.193  30.843  23.315  1.00 17.09           C  
ATOM    671  C   PHE A  92      -1.576  29.639  24.173  1.00 18.35           C  
ATOM    672  O   PHE A  92      -0.844  29.277  25.097  1.00 17.56           O  
ATOM    673  CB  PHE A  92      -0.621  30.385  21.962  1.00 14.65           C  
ATOM    674  CG  PHE A  92       0.737  29.732  22.056  1.00 14.22           C  
ATOM    675  CD1 PHE A  92       0.858  28.378  22.353  1.00 12.22           C  
ATOM    676  CD2 PHE A  92       1.896  30.478  21.839  1.00 14.05           C  
ATOM    677  CE1 PHE A  92       2.109  27.776  22.431  1.00 14.43           C  
ATOM    678  CE2 PHE A  92       3.154  29.887  21.915  1.00 12.59           C  
ATOM    679  CZ  PHE A  92       3.264  28.535  22.210  1.00 11.11           C  
ATOM    680  N   MET A  93      -2.709  29.017  23.873  1.00 17.69           N  
ATOM    681  CA  MET A  93      -3.160  27.869  24.648  1.00 19.19           C  
ATOM    682  C   MET A  93      -2.646  26.526  24.184  1.00 17.06           C  
ATOM    683  O   MET A  93      -2.497  26.279  22.991  1.00 16.77           O  
ATOM    684  CB  MET A  93      -4.684  27.788  24.674  1.00 26.77           C  
ATOM    685  CG  MET A  93      -5.338  28.624  25.736  1.00 40.11           C  
ATOM    686  SD  MET A  93      -7.045  28.113  25.945  1.00 55.73           S  
ATOM    687  CE  MET A  93      -7.740  28.606  24.346  1.00 47.47           C  
ATOM    688  N   VAL A  94      -2.402  25.652  25.153  1.00 15.60           N  
ATOM    689  CA  VAL A  94      -1.960  24.292  24.892  1.00 15.33           C  
ATOM    690  C   VAL A  94      -2.976  23.443  25.640  1.00 14.53           C  
ATOM    691  O   VAL A  94      -3.185  23.630  26.841  1.00 15.75           O  
ATOM    692  CB  VAL A  94      -0.550  23.998  25.446  1.00 13.33           C  
ATOM    693  CG1 VAL A  94      -0.152  22.562  25.120  1.00 12.45           C  
ATOM    694  CG2 VAL A  94       0.460  24.973  24.859  1.00 15.38           C  
ATOM    695  N   VAL A  95      -3.637  22.554  24.917  1.00 12.81           N  
ATOM    696  CA  VAL A  95      -4.647  21.690  25.498  1.00 16.92           C  
ATOM    697  C   VAL A  95      -4.221  20.234  25.450  1.00 16.87           C  
ATOM    698  O   VAL A  95      -3.278  19.861  24.744  1.00 16.89           O  
ATOM    699  CB  VAL A  95      -6.019  21.846  24.771  1.00 15.96           C  
ATOM    700  CG1 VAL A  95      -6.475  23.304  24.813  1.00 15.46           C  
ATOM    701  CG2 VAL A  95      -5.932  21.346  23.331  1.00 13.42           C  
ATOM    702  N   ASN A  96      -4.919  19.413  26.219  1.00 17.80           N  
ATOM    703  CA  ASN A  96      -4.639  17.995  26.253  1.00 17.98           C  
ATOM    704  C   ASN A  96      -5.642  17.270  25.372  1.00 20.12           C  
ATOM    705  O   ASN A  96      -6.852  17.415  25.542  1.00 22.16           O  
ATOM    706  CB  ASN A  96      -4.738  17.470  27.680  1.00 15.28           C  
ATOM    707  CG  ASN A  96      -4.330  16.022  27.799  1.00 14.87           C  
ATOM    708  OD1 ASN A  96      -3.995  15.370  26.812  1.00 16.30           O  
ATOM    709  ND2 ASN A  96      -4.344  15.508  29.016  1.00 18.14           N  
ATOM    710  N   ASP A  97      -5.136  16.538  24.391  1.00 19.52           N  
ATOM    711  CA  ASP A  97      -5.982  15.762  23.504  1.00 20.97           C  
ATOM    712  C   ASP A  97      -5.517  14.316  23.620  1.00 21.93           C  
ATOM    713  O   ASP A  97      -4.527  13.915  22.997  1.00 21.66           O  
ATOM    714  CB  ASP A  97      -5.851  16.246  22.063  1.00 23.58           C  
ATOM    715  CG  ASP A  97      -6.885  15.618  21.142  1.00 26.02           C  
ATOM    716  OD1 ASP A  97      -6.939  14.374  21.039  1.00 25.76           O  
ATOM    717  OD2 ASP A  97      -7.648  16.377  20.515  1.00 29.97           O  
ATOM    718  N   ALA A  98      -6.209  13.546  24.455  1.00 21.46           N  
ATOM    719  CA  ALA A  98      -5.877  12.140  24.670  1.00 21.61           C  
ATOM    720  C   ALA A  98      -4.427  11.948  25.135  1.00 22.21           C  
ATOM    721  O   ALA A  98      -3.759  10.994  24.732  1.00 22.27           O  
ATOM    722  CB  ALA A  98      -6.142  11.335  23.392  1.00 21.49           C  
ATOM    723  N   GLY A  99      -3.950  12.866  25.974  1.00 21.39           N  
ATOM    724  CA  GLY A  99      -2.596  12.785  26.492  1.00 18.82           C  
ATOM    725  C   GLY A  99      -1.554  13.440  25.610  1.00 19.25           C  
ATOM    726  O   GLY A  99      -0.363  13.399  25.914  1.00 17.72           O  
ATOM    727  N   ARG A 100      -1.995  14.048  24.518  1.00 19.37           N  
ATOM    728  CA  ARG A 100      -1.088  14.709  23.592  1.00 19.54           C  
ATOM    729  C   ARG A 100      -1.331  16.198  23.594  1.00 16.06           C  
ATOM    730  O   ARG A 100      -2.473  16.638  23.552  1.00 17.30           O  
ATOM    731  CB  ARG A 100      -1.304  14.204  22.171  1.00 22.20           C  
ATOM    732  CG  ARG A 100      -0.899  12.773  21.937  1.00 29.03           C  
ATOM    733  CD  ARG A 100      -0.920  12.477  20.454  1.00 31.87           C  
ATOM    734  NE  ARG A 100      -0.028  13.385  19.737  1.00 36.02           N  
ATOM    735  CZ  ARG A 100       0.491  13.147  18.536  1.00 37.82           C  
ATOM    736  NH1 ARG A 100       0.211  12.020  17.894  1.00 39.12           N  
ATOM    737  NH2 ARG A 100       1.309  14.036  17.985  1.00 35.09           N  
ATOM    738  N   PRO A 101      -0.256  16.998  23.628  1.00 16.13           N  
ATOM    739  CA  PRO A 101      -0.420  18.452  23.625  1.00 14.28           C  
ATOM    740  C   PRO A 101      -0.793  18.983  22.235  1.00 12.78           C  
ATOM    741  O   PRO A 101      -0.315  18.478  21.215  1.00 12.09           O  
ATOM    742  CB  PRO A 101       0.968  18.948  24.049  1.00 14.65           C  
ATOM    743  CG  PRO A 101       1.881  17.940  23.441  1.00 12.50           C  
ATOM    744  CD  PRO A 101       1.170  16.626  23.730  1.00 15.51           C  
ATOM    745  N   LYS A 102      -1.683  19.967  22.204  1.00 11.94           N  
ATOM    746  CA  LYS A 102      -2.089  20.602  20.957  1.00 12.21           C  
ATOM    747  C   LYS A 102      -2.221  22.077  21.261  1.00 12.33           C  
ATOM    748  O   LYS A 102      -2.636  22.445  22.360  1.00 14.42           O  
ATOM    749  CB  LYS A 102      -3.433  20.070  20.448  1.00 10.15           C  
ATOM    750  CG  LYS A 102      -3.464  18.581  20.157  1.00  8.29           C  
ATOM    751  CD  LYS A 102      -4.717  18.199  19.394  1.00 10.34           C  
ATOM    752  CE  LYS A 102      -4.684  18.773  17.996  1.00 14.00           C  
ATOM    753  NZ  LYS A 102      -5.913  18.474  17.219  1.00 15.77           N  
ATOM    754  N   VAL A 103      -1.789  22.932  20.340  1.00 12.79           N  
ATOM    755  CA  VAL A 103      -1.937  24.359  20.569  1.00 15.59           C  
ATOM    756  C   VAL A 103      -3.322  24.689  20.034  1.00 14.30           C  
ATOM    757  O   VAL A 103      -3.758  24.119  19.034  1.00 14.97           O  
ATOM    758  CB  VAL A 103      -0.843  25.214  19.865  1.00 15.37           C  
ATOM    759  CG1 VAL A 103       0.547  24.697  20.245  1.00 15.74           C  
ATOM    760  CG2 VAL A 103      -1.040  25.232  18.359  1.00 17.12           C  
ATOM    761  N   GLN A 104      -4.040  25.541  20.751  1.00 16.02           N  
ATOM    762  CA  GLN A 104      -5.381  25.924  20.355  1.00 16.23           C  
ATOM    763  C   GLN A 104      -5.400  27.411  20.050  1.00 14.54           C  
ATOM    764  O   GLN A 104      -4.953  28.229  20.856  1.00 16.79           O  
ATOM    765  CB  GLN A 104      -6.367  25.574  21.471  1.00 19.83           C  
ATOM    766  CG  GLN A 104      -7.830  25.683  21.085  1.00 21.91           C  
ATOM    767  CD  GLN A 104      -8.745  25.101  22.149  1.00 23.52           C  
ATOM    768  OE1 GLN A 104      -9.022  25.741  23.162  1.00 26.36           O  
ATOM    769  NE2 GLN A 104      -9.201  23.876  21.933  1.00 25.93           N  
ATOM    770  N   VAL A 105      -5.890  27.750  18.866  1.00 16.29           N  
ATOM    771  CA  VAL A 105      -5.958  29.136  18.417  1.00 16.00           C  
ATOM    772  C   VAL A 105      -7.310  29.426  17.773  1.00 16.80           C  
ATOM    773  O   VAL A 105      -8.143  28.535  17.595  1.00 16.60           O  
ATOM    774  CB  VAL A 105      -4.876  29.427  17.331  1.00 17.25           C  
ATOM    775  CG1 VAL A 105      -3.467  29.306  17.906  1.00 15.00           C  
ATOM    776  CG2 VAL A 105      -5.053  28.467  16.153  1.00 18.01           C  
ATOM    777  N   GLU A 106      -7.513  30.692  17.438  1.00 17.44           N  
ATOM    778  CA  GLU A 106      -8.713  31.128  16.757  1.00 16.44           C  
ATOM    779  C   GLU A 106      -8.266  31.375  15.329  1.00 16.36           C  
ATOM    780  O   GLU A 106      -7.236  32.011  15.089  1.00 13.58           O  
ATOM    781  CB  GLU A 106      -9.249  32.432  17.350  1.00 17.90           C  
ATOM    782  CG  GLU A 106      -9.877  32.286  18.719  1.00 22.48           C  
ATOM    783  CD  GLU A 106     -11.004  31.276  18.732  1.00 25.20           C  
ATOM    784  OE1 GLU A 106     -12.006  31.483  18.013  1.00 25.39           O  
ATOM    785  OE2 GLU A 106     -10.882  30.267  19.457  1.00 27.69           O  
ATOM    786  N   TYR A 107      -9.003  30.814  14.385  1.00 15.95           N  
ATOM    787  CA  TYR A 107      -8.705  30.994  12.983  1.00 14.03           C  
ATOM    788  C   TYR A 107     -10.041  31.132  12.279  1.00 16.72           C  
ATOM    789  O   TYR A 107     -10.908  30.255  12.392  1.00 16.14           O  
ATOM    790  CB  TYR A 107      -7.951  29.794  12.427  1.00 14.45           C  
ATOM    791  CG  TYR A 107      -7.712  29.920  10.946  1.00 19.79           C  
ATOM    792  CD1 TYR A 107      -7.075  31.043  10.420  1.00 16.86           C  
ATOM    793  CD2 TYR A 107      -8.130  28.924  10.066  1.00 23.65           C  
ATOM    794  CE1 TYR A 107      -6.858  31.171   9.062  1.00 21.30           C  
ATOM    795  CE2 TYR A 107      -7.921  29.044   8.702  1.00 23.38           C  
ATOM    796  CZ  TYR A 107      -7.279  30.168   8.207  1.00 26.98           C  
ATOM    797  OH  TYR A 107      -7.026  30.274   6.860  1.00 29.61           O  
ATOM    798  N   LYS A 108     -10.214  32.246  11.576  1.00 17.45           N  
ATOM    799  CA  LYS A 108     -11.454  32.522  10.860  1.00 19.64           C  
ATOM    800  C   LYS A 108     -12.671  32.380  11.792  1.00 20.25           C  
ATOM    801  O   LYS A 108     -13.647  31.693  11.466  1.00 19.88           O  
ATOM    802  CB  LYS A 108     -11.580  31.602   9.638  1.00 23.01           C  
ATOM    803  CG  LYS A 108     -10.533  31.826   8.543  1.00 26.21           C  
ATOM    804  CD  LYS A 108     -10.733  30.842   7.408  1.00 32.11           C  
ATOM    805  CE  LYS A 108      -9.839  31.156   6.222  1.00 36.99           C  
ATOM    806  NZ  LYS A 108      -9.571  29.900   5.451  1.00 39.35           N  
ATOM    807  N   GLY A 109     -12.573  32.998  12.969  1.00 17.87           N  
ATOM    808  CA  GLY A 109     -13.645  32.962  13.947  1.00 20.49           C  
ATOM    809  C   GLY A 109     -13.908  31.636  14.645  1.00 22.97           C  
ATOM    810  O   GLY A 109     -14.744  31.571  15.550  1.00 25.56           O  
ATOM    811  N   GLU A 110     -13.207  30.579  14.251  1.00 21.20           N  
ATOM    812  CA  GLU A 110     -13.419  29.280  14.873  1.00 22.50           C  
ATOM    813  C   GLU A 110     -12.209  28.788  15.660  1.00 22.22           C  
ATOM    814  O   GLU A 110     -11.068  29.095  15.311  1.00 22.27           O  
ATOM    815  CB  GLU A 110     -13.808  28.240  13.821  1.00 24.63           C  
ATOM    816  CG  GLU A 110     -14.993  28.633  12.937  1.00 32.36           C  
ATOM    817  CD  GLU A 110     -16.223  29.081  13.718  1.00 35.77           C  
ATOM    818  OE1 GLU A 110     -16.513  28.509  14.793  1.00 39.44           O  
ATOM    819  OE2 GLU A 110     -16.907  30.012  13.243  1.00 38.38           O  
ATOM    820  N   THR A 111     -12.469  28.041  16.729  1.00 19.21           N  
ATOM    821  CA  THR A 111     -11.409  27.487  17.564  1.00 20.59           C  
ATOM    822  C   THR A 111     -10.853  26.234  16.893  1.00 20.93           C  
ATOM    823  O   THR A 111     -11.605  25.326  16.532  1.00 19.63           O  
ATOM    824  CB  THR A 111     -11.930  27.096  18.962  1.00 22.32           C  
ATOM    825  OG1 THR A 111     -12.671  28.184  19.529  1.00 22.69           O  
ATOM    826  CG2 THR A 111     -10.775  26.761  19.884  1.00 22.14           C  
ATOM    827  N   LYS A 112      -9.538  26.189  16.724  1.00 17.84           N  
ATOM    828  CA  LYS A 112      -8.886  25.053  16.091  1.00 17.56           C  
ATOM    829  C   LYS A 112      -7.669  24.664  16.930  1.00 16.63           C  
ATOM    830  O   LYS A 112      -7.139  25.483  17.680  1.00 15.87           O  
ATOM    831  CB  LYS A 112      -8.456  25.419  14.660  1.00 21.83           C  
ATOM    832  CG  LYS A 112      -9.556  26.108  13.825  1.00 28.57           C  
ATOM    833  CD  LYS A 112      -9.695  25.508  12.429  1.00 29.97           C  
ATOM    834  CE  LYS A 112     -11.022  25.896  11.756  1.00 32.22           C  
ATOM    835  NZ  LYS A 112     -11.021  27.221  11.058  1.00 32.87           N  
ATOM    836  N   SER A 113      -7.274  23.398  16.867  1.00 16.10           N  
ATOM    837  CA  SER A 113      -6.110  22.936  17.614  1.00 17.41           C  
ATOM    838  C   SER A 113      -5.200  22.207  16.647  1.00 18.74           C  
ATOM    839  O   SER A 113      -5.671  21.519  15.736  1.00 19.08           O  
ATOM    840  CB  SER A 113      -6.516  22.010  18.761  1.00 16.20           C  
ATOM    841  OG  SER A 113      -7.210  20.872  18.286  1.00 16.35           O  
ATOM    842  N   PHE A 114      -3.896  22.370  16.830  1.00 19.08           N  
ATOM    843  CA  PHE A 114      -2.930  21.734  15.956  1.00 14.94           C  
ATOM    844  C   PHE A 114      -1.894  20.980  16.757  1.00 13.04           C  
ATOM    845  O   PHE A 114      -1.487  21.425  17.831  1.00 13.65           O  
ATOM    846  CB  PHE A 114      -2.213  22.790  15.108  1.00 13.86           C  
ATOM    847  CG  PHE A 114      -3.134  23.643  14.292  1.00 17.06           C  
ATOM    848  CD1 PHE A 114      -3.690  24.802  14.829  1.00 14.99           C  
ATOM    849  CD2 PHE A 114      -3.466  23.278  12.992  1.00 18.63           C  
ATOM    850  CE1 PHE A 114      -4.562  25.581  14.080  1.00 20.25           C  
ATOM    851  CE2 PHE A 114      -4.339  24.051  12.235  1.00 20.83           C  
ATOM    852  CZ  PHE A 114      -4.889  25.205  12.782  1.00 21.41           C  
ATOM    853  N   TYR A 115      -1.503  19.815  16.259  1.00 12.12           N  
ATOM    854  CA  TYR A 115      -0.460  19.039  16.906  1.00 13.69           C  
ATOM    855  C   TYR A 115       0.833  19.809  16.627  1.00 12.59           C  
ATOM    856  O   TYR A 115       0.906  20.573  15.656  1.00 10.85           O  
ATOM    857  CB  TYR A 115      -0.359  17.648  16.278  1.00 15.53           C  
ATOM    858  CG  TYR A 115      -1.460  16.709  16.690  1.00 16.76           C  
ATOM    859  CD1 TYR A 115      -1.554  16.255  18.004  1.00 15.52           C  
ATOM    860  CD2 TYR A 115      -2.418  16.285  15.772  1.00 16.44           C  
ATOM    861  CE1 TYR A 115      -2.581  15.404  18.399  1.00 18.61           C  
ATOM    862  CE2 TYR A 115      -3.452  15.434  16.155  1.00 19.82           C  
ATOM    863  CZ  TYR A 115      -3.527  15.000  17.471  1.00 20.72           C  
ATOM    864  OH  TYR A 115      -4.561  14.184  17.862  1.00 22.88           O  
ATOM    865  N   PRO A 116       1.857  19.643  17.481  1.00 12.76           N  
ATOM    866  CA  PRO A 116       3.127  20.350  17.267  1.00 11.40           C  
ATOM    867  C   PRO A 116       3.709  20.086  15.872  1.00  9.50           C  
ATOM    868  O   PRO A 116       4.212  21.001  15.222  1.00 11.50           O  
ATOM    869  CB  PRO A 116       4.014  19.786  18.375  1.00 10.43           C  
ATOM    870  CG  PRO A 116       3.027  19.563  19.497  1.00 12.14           C  
ATOM    871  CD  PRO A 116       1.866  18.918  18.765  1.00 11.89           C  
ATOM    872  N   GLU A 117       3.603  18.848  15.394  1.00 12.08           N  
ATOM    873  CA  GLU A 117       4.120  18.516  14.066  1.00 14.07           C  
ATOM    874  C   GLU A 117       3.354  19.213  12.950  1.00 13.45           C  
ATOM    875  O   GLU A 117       3.903  19.440  11.875  1.00 10.76           O  
ATOM    876  CB  GLU A 117       4.202  17.000  13.816  1.00 16.87           C  
ATOM    877  CG  GLU A 117       3.007  16.181  14.247  1.00 21.30           C  
ATOM    878  CD  GLU A 117       3.143  15.682  15.673  1.00 24.19           C  
ATOM    879  OE1 GLU A 117       3.751  14.609  15.877  1.00 24.97           O  
ATOM    880  OE2 GLU A 117       2.655  16.371  16.589  1.00 23.23           O  
ATOM    881  N   GLU A 118       2.102  19.582  13.213  1.00 11.11           N  
ATOM    882  CA  GLU A 118       1.316  20.293  12.217  1.00  9.82           C  
ATOM    883  C   GLU A 118       1.817  21.733  12.142  1.00 11.20           C  
ATOM    884  O   GLU A 118       1.947  22.295  11.056  1.00 11.75           O  
ATOM    885  CB  GLU A 118      -0.179  20.235  12.549  1.00 12.54           C  
ATOM    886  CG  GLU A 118      -0.716  18.813  12.509  1.00 13.77           C  
ATOM    887  CD  GLU A 118      -2.213  18.718  12.721  1.00 18.19           C  
ATOM    888  OE1 GLU A 118      -2.718  19.295  13.701  1.00 16.05           O  
ATOM    889  OE2 GLU A 118      -2.880  18.029  11.915  1.00 20.23           O  
ATOM    890  N   VAL A 119       2.135  22.325  13.289  1.00  9.63           N  
ATOM    891  CA  VAL A 119       2.649  23.691  13.303  1.00 10.45           C  
ATOM    892  C   VAL A 119       4.016  23.689  12.611  1.00 10.31           C  
ATOM    893  O   VAL A 119       4.284  24.525  11.744  1.00 10.81           O  
ATOM    894  CB  VAL A 119       2.796  24.236  14.741  1.00 11.46           C  
ATOM    895  CG1 VAL A 119       3.347  25.651  14.711  1.00  7.89           C  
ATOM    896  CG2 VAL A 119       1.452  24.213  15.451  1.00  9.80           C  
ATOM    897  N   SER A 120       4.858  22.721  12.967  1.00 11.23           N  
ATOM    898  CA  SER A 120       6.189  22.599  12.374  1.00  9.98           C  
ATOM    899  C   SER A 120       6.136  22.286  10.882  1.00 11.42           C  
ATOM    900  O   SER A 120       7.021  22.703  10.130  1.00  8.91           O  
ATOM    901  CB  SER A 120       7.018  21.548  13.116  1.00  9.86           C  
ATOM    902  OG  SER A 120       7.284  21.992  14.436  1.00 11.57           O  
ATOM    903  N   SER A 121       5.098  21.567  10.449  1.00 10.83           N  
ATOM    904  CA  SER A 121       4.950  21.240   9.029  1.00  9.39           C  
ATOM    905  C   SER A 121       4.705  22.531   8.252  1.00 10.41           C  
ATOM    906  O   SER A 121       5.095  22.654   7.092  1.00 11.80           O  
ATOM    907  CB  SER A 121       3.787  20.264   8.795  1.00  8.79           C  
ATOM    908  OG  SER A 121       2.530  20.923   8.800  1.00 10.19           O  
ATOM    909  N   MET A 122       4.048  23.491   8.895  1.00 10.36           N  
ATOM    910  CA  MET A 122       3.774  24.772   8.265  1.00  9.81           C  
ATOM    911  C   MET A 122       5.089  25.518   8.090  1.00 13.27           C  
ATOM    912  O   MET A 122       5.317  26.168   7.064  1.00 11.09           O  
ATOM    913  CB  MET A 122       2.819  25.597   9.123  1.00  8.94           C  
ATOM    914  CG  MET A 122       1.408  25.054   9.158  1.00 14.79           C  
ATOM    915  SD  MET A 122       0.416  25.853  10.432  1.00 14.64           S  
ATOM    916  CE  MET A 122      -0.683  24.499  10.912  1.00 20.72           C  
ATOM    917  N   VAL A 123       5.941  25.449   9.109  1.00 10.71           N  
ATOM    918  CA  VAL A 123       7.237  26.108   9.045  1.00 11.92           C  
ATOM    919  C   VAL A 123       8.075  25.425   7.967  1.00  9.50           C  
ATOM    920  O   VAL A 123       8.743  26.092   7.183  1.00 12.71           O  
ATOM    921  CB  VAL A 123       7.974  26.087  10.412  1.00 10.78           C  
ATOM    922  CG1 VAL A 123       9.363  26.701  10.269  1.00 10.97           C  
ATOM    923  CG2 VAL A 123       7.184  26.887  11.438  1.00 13.10           C  
ATOM    924  N   LEU A 124       8.011  24.100   7.906  1.00  9.43           N  
ATOM    925  CA  LEU A 124       8.760  23.361   6.901  1.00  9.27           C  
ATOM    926  C   LEU A 124       8.243  23.698   5.504  1.00 11.67           C  
ATOM    927  O   LEU A 124       9.028  23.826   4.567  1.00 12.06           O  
ATOM    928  CB  LEU A 124       8.694  21.856   7.164  1.00 10.61           C  
ATOM    929  CG  LEU A 124       9.443  21.397   8.418  1.00  8.91           C  
ATOM    930  CD1 LEU A 124       9.330  19.906   8.584  1.00  7.00           C  
ATOM    931  CD2 LEU A 124      10.909  21.796   8.317  1.00 12.19           C  
ATOM    932  N   THR A 125       6.932  23.875   5.371  1.00 10.28           N  
ATOM    933  CA  THR A 125       6.338  24.226   4.084  1.00  9.60           C  
ATOM    934  C   THR A 125       6.948  25.542   3.591  1.00 10.83           C  
ATOM    935  O   THR A 125       7.335  25.661   2.422  1.00 11.02           O  
ATOM    936  CB  THR A 125       4.802  24.346   4.206  1.00 10.33           C  
ATOM    937  OG1 THR A 125       4.257  23.055   4.514  1.00 11.98           O  
ATOM    938  CG2 THR A 125       4.184  24.856   2.918  1.00 10.74           C  
ATOM    939  N   LYS A 126       7.066  26.510   4.496  1.00 10.26           N  
ATOM    940  CA  LYS A 126       7.654  27.809   4.180  1.00  7.97           C  
ATOM    941  C   LYS A 126       9.097  27.632   3.701  1.00 10.07           C  
ATOM    942  O   LYS A 126       9.493  28.196   2.678  1.00  9.55           O  
ATOM    943  CB  LYS A 126       7.617  28.713   5.418  1.00  7.07           C  
ATOM    944  CG  LYS A 126       8.515  29.959   5.358  1.00 10.24           C  
ATOM    945  CD  LYS A 126       8.140  30.919   4.238  1.00  7.84           C  
ATOM    946  CE  LYS A 126       6.769  31.526   4.449  1.00 10.11           C  
ATOM    947  NZ  LYS A 126       6.495  32.563   3.423  1.00 10.94           N  
ATOM    948  N   MET A 127       9.871  26.832   4.431  1.00 11.51           N  
ATOM    949  CA  MET A 127      11.263  26.589   4.076  1.00 10.87           C  
ATOM    950  C   MET A 127      11.354  25.918   2.715  1.00  9.77           C  
ATOM    951  O   MET A 127      12.199  26.276   1.894  1.00 11.36           O  
ATOM    952  CB  MET A 127      11.957  25.729   5.139  1.00 11.75           C  
ATOM    953  CG  MET A 127      12.017  26.373   6.530  1.00  8.66           C  
ATOM    954  SD  MET A 127      12.189  28.167   6.555  1.00  8.79           S  
ATOM    955  CE  MET A 127      13.899  28.400   6.068  1.00  8.30           C  
ATOM    956  N   LYS A 128      10.456  24.969   2.472  1.00 10.74           N  
ATOM    957  CA  LYS A 128      10.394  24.236   1.212  1.00 10.78           C  
ATOM    958  C   LYS A 128      10.099  25.184   0.055  1.00 11.51           C  
ATOM    959  O   LYS A 128      10.728  25.093  -0.995  1.00 14.34           O  
ATOM    960  CB  LYS A 128       9.302  23.163   1.286  1.00 10.62           C  
ATOM    961  CG  LYS A 128       9.155  22.324   0.027  1.00 12.42           C  
ATOM    962  CD  LYS A 128       7.923  21.441   0.087  1.00 18.16           C  
ATOM    963  CE  LYS A 128       6.694  22.292   0.337  1.00 27.06           C  
ATOM    964  NZ  LYS A 128       5.467  21.702  -0.264  1.00 33.20           N  
ATOM    965  N   GLU A 129       9.136  26.084   0.249  1.00 12.24           N  
ATOM    966  CA  GLU A 129       8.763  27.058  -0.780  1.00 13.06           C  
ATOM    967  C   GLU A 129       9.881  28.062  -1.016  1.00 13.80           C  
ATOM    968  O   GLU A 129      10.043  28.575  -2.125  1.00 12.13           O  
ATOM    969  CB  GLU A 129       7.475  27.785  -0.395  1.00 13.23           C  
ATOM    970  CG  GLU A 129       6.263  26.869  -0.356  1.00 15.25           C  
ATOM    971  CD  GLU A 129       5.026  27.522   0.237  1.00 17.22           C  
ATOM    972  OE1 GLU A 129       5.145  28.568   0.911  1.00 16.85           O  
ATOM    973  OE2 GLU A 129       3.922  26.970   0.035  1.00 21.16           O  
ATOM    974  N   ILE A 130      10.642  28.359   0.033  1.00 13.59           N  
ATOM    975  CA  ILE A 130      11.764  29.284  -0.088  1.00 13.18           C  
ATOM    976  C   ILE A 130      12.786  28.655  -1.032  1.00  9.75           C  
ATOM    977  O   ILE A 130      13.303  29.320  -1.939  1.00 12.26           O  
ATOM    978  CB  ILE A 130      12.411  29.581   1.293  1.00 12.94           C  
ATOM    979  CG1 ILE A 130      11.450  30.416   2.146  1.00 13.29           C  
ATOM    980  CG2 ILE A 130      13.724  30.335   1.118  1.00 11.44           C  
ATOM    981  CD1 ILE A 130      11.884  30.593   3.576  1.00  9.99           C  
ATOM    982  N   ALA A 131      13.034  27.363  -0.846  1.00 10.56           N  
ATOM    983  CA  ALA A 131      13.979  26.629  -1.682  1.00 11.82           C  
ATOM    984  C   ALA A 131      13.446  26.526  -3.107  1.00 13.46           C  
ATOM    985  O   ALA A 131      14.196  26.674  -4.070  1.00 14.45           O  
ATOM    986  CB  ALA A 131      14.230  25.234  -1.109  1.00 10.50           C  
ATOM    987  N   GLU A 132      12.146  26.280  -3.235  1.00 11.09           N  
ATOM    988  CA  GLU A 132      11.512  26.163  -4.545  1.00 12.66           C  
ATOM    989  C   GLU A 132      11.557  27.443  -5.375  1.00 10.43           C  
ATOM    990  O   GLU A 132      11.747  27.389  -6.587  1.00 13.17           O  
ATOM    991  CB  GLU A 132      10.074  25.677  -4.396  1.00 10.65           C  
ATOM    992  CG  GLU A 132       9.992  24.250  -3.909  1.00 14.70           C  
ATOM    993  CD  GLU A 132       8.573  23.747  -3.779  1.00 18.59           C  
ATOM    994  OE1 GLU A 132       7.662  24.579  -3.591  1.00 21.16           O  
ATOM    995  OE2 GLU A 132       8.369  22.517  -3.848  1.00 18.49           O  
ATOM    996  N   ALA A 133      11.390  28.590  -4.730  1.00 12.50           N  
ATOM    997  CA  ALA A 133      11.423  29.870  -5.430  1.00 14.81           C  
ATOM    998  C   ALA A 133      12.816  30.113  -5.997  1.00 15.76           C  
ATOM    999  O   ALA A 133      12.970  30.711  -7.060  1.00 16.87           O  
ATOM   1000  CB  ALA A 133      11.035  31.002  -4.483  1.00 11.96           C  
ATOM   1001  N   TYR A 134      13.829  29.669  -5.261  1.00 15.55           N  
ATOM   1002  CA  TYR A 134      15.218  29.822  -5.670  1.00 14.93           C  
ATOM   1003  C   TYR A 134      15.588  28.819  -6.767  1.00 17.66           C  
ATOM   1004  O   TYR A 134      16.243  29.168  -7.756  1.00 16.21           O  
ATOM   1005  CB  TYR A 134      16.137  29.635  -4.456  1.00 13.88           C  
ATOM   1006  CG  TYR A 134      17.589  29.467  -4.828  1.00 18.51           C  
ATOM   1007  CD1 TYR A 134      18.342  30.552  -5.278  1.00 19.85           C  
ATOM   1008  CD2 TYR A 134      18.190  28.208  -4.802  1.00 15.74           C  
ATOM   1009  CE1 TYR A 134      19.655  30.383  -5.705  1.00 21.05           C  
ATOM   1010  CE2 TYR A 134      19.499  28.031  -5.226  1.00 18.26           C  
ATOM   1011  CZ  TYR A 134      20.225  29.121  -5.678  1.00 18.60           C  
ATOM   1012  OH  TYR A 134      21.512  28.943  -6.136  1.00 20.61           O  
ATOM   1013  N   LEU A 135      15.193  27.565  -6.567  1.00 17.27           N  
ATOM   1014  CA  LEU A 135      15.477  26.493  -7.510  1.00 18.36           C  
ATOM   1015  C   LEU A 135      14.596  26.510  -8.752  1.00 19.40           C  
ATOM   1016  O   LEU A 135      14.965  25.945  -9.782  1.00 20.91           O  
ATOM   1017  CB  LEU A 135      15.321  25.135  -6.824  1.00 19.18           C  
ATOM   1018  CG  LEU A 135      16.324  24.802  -5.721  1.00 20.29           C  
ATOM   1019  CD1 LEU A 135      15.988  23.436  -5.137  1.00 20.28           C  
ATOM   1020  CD2 LEU A 135      17.740  24.819  -6.278  1.00 15.26           C  
ATOM   1021  N   GLY A 136      13.422  27.128  -8.643  1.00 19.01           N  
ATOM   1022  CA  GLY A 136      12.489  27.175  -9.758  1.00 19.16           C  
ATOM   1023  C   GLY A 136      12.010  25.774 -10.097  1.00 20.72           C  
ATOM   1024  O   GLY A 136      11.497  25.519 -11.193  1.00 22.27           O  
ATOM   1025  N   LYS A 137      12.175  24.866  -9.140  1.00 19.77           N  
ATOM   1026  CA  LYS A 137      11.799  23.471  -9.304  1.00 18.42           C  
ATOM   1027  C   LYS A 137      11.168  22.966  -8.015  1.00 18.55           C  
ATOM   1028  O   LYS A 137      11.345  23.563  -6.947  1.00 15.73           O  
ATOM   1029  CB  LYS A 137      13.044  22.623  -9.657  1.00 17.59           C  
ATOM   1030  N   THR A 138      10.420  21.874  -8.125  1.00 18.70           N  
ATOM   1031  CA  THR A 138       9.765  21.271  -6.974  1.00 19.01           C  
ATOM   1032  C   THR A 138      10.806  20.585  -6.099  1.00 15.22           C  
ATOM   1033  O   THR A 138      11.652  19.840  -6.598  1.00 15.16           O  
ATOM   1034  CB  THR A 138       8.710  20.221  -7.413  1.00 20.80           C  
ATOM   1035  OG1 THR A 138       7.653  20.876  -8.122  1.00 24.16           O  
ATOM   1036  CG2 THR A 138       8.123  19.499  -6.205  1.00 21.61           C  
ATOM   1037  N   VAL A 139      10.767  20.885  -4.805  1.00 15.05           N  
ATOM   1038  CA  VAL A 139      11.678  20.288  -3.836  1.00 16.12           C  
ATOM   1039  C   VAL A 139      10.899  19.180  -3.139  1.00 16.18           C  
ATOM   1040  O   VAL A 139       9.800  19.412  -2.623  1.00 16.27           O  
ATOM   1041  CB  VAL A 139      12.171  21.325  -2.797  1.00 15.07           C  
ATOM   1042  CG1 VAL A 139      12.942  20.635  -1.680  1.00 16.29           C  
ATOM   1043  CG2 VAL A 139      13.054  22.356  -3.474  1.00 11.77           C  
ATOM   1044  N   THR A 140      11.445  17.972  -3.169  1.00 16.58           N  
ATOM   1045  CA  THR A 140      10.791  16.832  -2.553  1.00 19.33           C  
ATOM   1046  C   THR A 140      11.640  16.226  -1.445  1.00 16.27           C  
ATOM   1047  O   THR A 140      11.193  16.105  -0.309  1.00 19.31           O  
ATOM   1048  CB  THR A 140      10.482  15.747  -3.603  1.00 22.42           C  
ATOM   1049  OG1 THR A 140       9.758  16.332  -4.696  1.00 24.86           O  
ATOM   1050  CG2 THR A 140       9.647  14.634  -2.987  1.00 26.09           C  
ATOM   1051  N   ASN A 141      12.881  15.894  -1.773  1.00 16.61           N  
ATOM   1052  CA  ASN A 141      13.796  15.275  -0.820  1.00 14.86           C  
ATOM   1053  C   ASN A 141      14.465  16.279   0.105  1.00 15.45           C  
ATOM   1054  O   ASN A 141      14.840  17.380  -0.321  1.00 13.40           O  
ATOM   1055  CB  ASN A 141      14.862  14.469  -1.564  1.00 15.41           C  
ATOM   1056  CG  ASN A 141      14.272  13.322  -2.363  1.00 18.93           C  
ATOM   1057  OD1 ASN A 141      13.347  12.657  -1.911  1.00 19.45           O  
ATOM   1058  ND2 ASN A 141      14.806  13.085  -3.552  1.00 20.13           N  
ATOM   1059  N   ALA A 142      14.624  15.895   1.368  1.00 14.86           N  
ATOM   1060  CA  ALA A 142      15.262  16.772   2.339  1.00 16.09           C  
ATOM   1061  C   ALA A 142      15.821  16.047   3.546  1.00 15.39           C  
ATOM   1062  O   ALA A 142      15.388  14.946   3.887  1.00 12.54           O  
ATOM   1063  CB  ALA A 142      14.284  17.844   2.806  1.00 13.66           C  
ATOM   1064  N   VAL A 143      16.838  16.657   4.143  1.00 15.75           N  
ATOM   1065  CA  VAL A 143      17.440  16.151   5.365  1.00 16.03           C  
ATOM   1066  C   VAL A 143      17.045  17.198   6.401  1.00 13.72           C  
ATOM   1067  O   VAL A 143      17.228  18.399   6.176  1.00 15.43           O  
ATOM   1068  CB  VAL A 143      18.976  16.041   5.270  1.00 14.25           C  
ATOM   1069  CG1 VAL A 143      19.593  15.927   6.675  1.00 14.02           C  
ATOM   1070  CG2 VAL A 143      19.345  14.813   4.462  1.00 15.01           C  
ATOM   1071  N   VAL A 144      16.426  16.755   7.488  1.00 13.99           N  
ATOM   1072  CA  VAL A 144      15.995  17.672   8.535  1.00 12.76           C  
ATOM   1073  C   VAL A 144      16.808  17.371   9.802  1.00 12.49           C  
ATOM   1074  O   VAL A 144      17.066  16.212  10.135  1.00 11.91           O  
ATOM   1075  CB  VAL A 144      14.454  17.571   8.773  1.00 11.36           C  
ATOM   1076  CG1 VAL A 144      13.989  18.602   9.813  1.00  8.58           C  
ATOM   1077  CG2 VAL A 144      13.716  17.794   7.449  1.00  8.41           C  
ATOM   1078  N   THR A 145      17.279  18.426  10.455  1.00 12.56           N  
ATOM   1079  CA  THR A 145      18.095  18.286  11.651  1.00 12.37           C  
ATOM   1080  C   THR A 145      17.302  18.369  12.957  1.00 11.23           C  
ATOM   1081  O   THR A 145      16.203  18.931  12.990  1.00 12.95           O  
ATOM   1082  CB  THR A 145      19.204  19.359  11.651  1.00 11.44           C  
ATOM   1083  OG1 THR A 145      18.612  20.652  11.466  1.00  7.83           O  
ATOM   1084  CG2 THR A 145      20.185  19.109  10.521  1.00  7.55           C  
ATOM   1085  N   VAL A 146      17.854  17.771  14.014  1.00 10.76           N  
ATOM   1086  CA  VAL A 146      17.262  17.781  15.361  1.00 12.93           C  
ATOM   1087  C   VAL A 146      18.378  17.864  16.425  1.00 14.92           C  
ATOM   1088  O   VAL A 146      19.554  17.613  16.128  1.00 12.19           O  
ATOM   1089  CB  VAL A 146      16.431  16.491  15.669  1.00 12.19           C  
ATOM   1090  CG1 VAL A 146      15.255  16.357  14.716  1.00  9.75           C  
ATOM   1091  CG2 VAL A 146      17.321  15.254  15.636  1.00 10.00           C  
ATOM   1092  N   PRO A 147      18.038  18.297  17.653  1.00 12.94           N  
ATOM   1093  CA  PRO A 147      19.054  18.385  18.709  1.00 11.59           C  
ATOM   1094  C   PRO A 147      19.512  16.966  19.033  1.00 11.33           C  
ATOM   1095  O   PRO A 147      18.728  16.020  18.920  1.00 10.87           O  
ATOM   1096  CB  PRO A 147      18.276  18.986  19.881  1.00  8.78           C  
ATOM   1097  CG  PRO A 147      17.246  19.819  19.208  1.00 12.38           C  
ATOM   1098  CD  PRO A 147      16.775  18.914  18.093  1.00 10.29           C  
ATOM   1099  N   ALA A 148      20.764  16.818  19.456  1.00 10.08           N  
ATOM   1100  CA  ALA A 148      21.306  15.502  19.775  1.00 11.72           C  
ATOM   1101  C   ALA A 148      20.511  14.787  20.856  1.00 12.09           C  
ATOM   1102  O   ALA A 148      20.429  13.557  20.864  1.00 13.97           O  
ATOM   1103  CB  ALA A 148      22.760  15.619  20.193  1.00 13.01           C  
ATOM   1104  N   TYR A 149      19.913  15.558  21.757  1.00 12.85           N  
ATOM   1105  CA  TYR A 149      19.142  14.979  22.846  1.00 15.32           C  
ATOM   1106  C   TYR A 149      17.755  14.435  22.468  1.00 15.75           C  
ATOM   1107  O   TYR A 149      17.130  13.743  23.276  1.00 16.57           O  
ATOM   1108  CB  TYR A 149      19.030  15.975  24.008  1.00 16.26           C  
ATOM   1109  CG  TYR A 149      17.756  16.795  24.017  1.00 24.37           C  
ATOM   1110  CD1 TYR A 149      17.666  17.989  23.308  1.00 25.48           C  
ATOM   1111  CD2 TYR A 149      16.634  16.366  24.735  1.00 27.96           C  
ATOM   1112  CE1 TYR A 149      16.494  18.741  23.310  1.00 29.13           C  
ATOM   1113  CE2 TYR A 149      15.455  17.107  24.744  1.00 28.08           C  
ATOM   1114  CZ  TYR A 149      15.392  18.292  24.029  1.00 31.37           C  
ATOM   1115  OH  TYR A 149      14.230  19.030  24.035  1.00 32.93           O  
ATOM   1116  N   PHE A 150      17.263  14.745  21.269  1.00 14.38           N  
ATOM   1117  CA  PHE A 150      15.938  14.268  20.861  1.00 12.83           C  
ATOM   1118  C   PHE A 150      15.824  12.756  20.910  1.00 12.07           C  
ATOM   1119  O   PHE A 150      16.745  12.042  20.501  1.00 14.16           O  
ATOM   1120  CB  PHE A 150      15.570  14.761  19.455  1.00  8.62           C  
ATOM   1121  CG  PHE A 150      14.773  16.036  19.454  1.00 11.98           C  
ATOM   1122  CD1 PHE A 150      14.893  16.958  20.495  1.00 11.65           C  
ATOM   1123  CD2 PHE A 150      13.910  16.328  18.399  1.00 12.90           C  
ATOM   1124  CE1 PHE A 150      14.144  18.140  20.502  1.00 11.80           C  
ATOM   1125  CE2 PHE A 150      13.156  17.508  18.399  1.00 11.72           C  
ATOM   1126  CZ  PHE A 150      13.283  18.419  19.445  1.00 13.14           C  
ATOM   1127  N   ASN A 151      14.709  12.276  21.452  1.00 11.41           N  
ATOM   1128  CA  ASN A 151      14.453  10.842  21.548  1.00 11.74           C  
ATOM   1129  C   ASN A 151      13.736  10.373  20.278  1.00 11.35           C  
ATOM   1130  O   ASN A 151      13.528  11.158  19.352  1.00 11.66           O  
ATOM   1131  CB  ASN A 151      13.638  10.500  22.811  1.00 12.63           C  
ATOM   1132  CG  ASN A 151      12.264  11.165  22.842  1.00 15.91           C  
ATOM   1133  OD1 ASN A 151      11.623  11.361  21.811  1.00 16.53           O  
ATOM   1134  ND2 ASN A 151      11.805  11.507  24.039  1.00 15.00           N  
ATOM   1135  N   ASP A 152      13.342   9.107  20.242  1.00 12.03           N  
ATOM   1136  CA  ASP A 152      12.668   8.556  19.071  1.00 15.26           C  
ATOM   1137  C   ASP A 152      11.344   9.222  18.727  1.00 14.49           C  
ATOM   1138  O   ASP A 152      11.047   9.432  17.550  1.00 14.35           O  
ATOM   1139  CB  ASP A 152      12.474   7.047  19.223  1.00 15.70           C  
ATOM   1140  CG  ASP A 152      13.792   6.285  19.214  1.00 20.47           C  
ATOM   1141  OD1 ASP A 152      14.810   6.825  18.721  1.00 21.68           O  
ATOM   1142  OD2 ASP A 152      13.807   5.140  19.702  1.00 22.36           O  
ATOM   1143  N   SER A 153      10.547   9.548  19.741  1.00 13.20           N  
ATOM   1144  CA  SER A 153       9.258  10.195  19.514  1.00 12.72           C  
ATOM   1145  C   SER A 153       9.459  11.590  18.935  1.00 13.70           C  
ATOM   1146  O   SER A 153       8.781  11.983  17.984  1.00 14.75           O  
ATOM   1147  CB  SER A 153       8.454  10.285  20.816  1.00 14.55           C  
ATOM   1148  OG  SER A 153       7.215  10.944  20.607  1.00 13.88           O  
ATOM   1149  N   GLN A 154      10.393  12.341  19.509  1.00 11.90           N  
ATOM   1150  CA  GLN A 154      10.684  13.688  19.038  1.00 11.33           C  
ATOM   1151  C   GLN A 154      11.197  13.666  17.601  1.00  9.36           C  
ATOM   1152  O   GLN A 154      10.856  14.536  16.800  1.00 11.07           O  
ATOM   1153  CB  GLN A 154      11.695  14.365  19.964  1.00 11.24           C  
ATOM   1154  CG  GLN A 154      11.136  14.699  21.338  1.00  8.83           C  
ATOM   1155  CD  GLN A 154      12.211  15.171  22.288  1.00 10.25           C  
ATOM   1156  OE1 GLN A 154      13.196  14.476  22.520  1.00 11.47           O  
ATOM   1157  NE2 GLN A 154      12.033  16.354  22.839  1.00  9.17           N  
ATOM   1158  N   ARG A 155      12.007  12.664  17.276  1.00 10.50           N  
ATOM   1159  CA  ARG A 155      12.549  12.515  15.926  1.00 11.52           C  
ATOM   1160  C   ARG A 155      11.448  12.113  14.940  1.00 10.86           C  
ATOM   1161  O   ARG A 155      11.346  12.682  13.852  1.00 10.41           O  
ATOM   1162  CB  ARG A 155      13.696  11.498  15.919  1.00 10.16           C  
ATOM   1163  CG  ARG A 155      14.924  12.011  16.637  1.00  9.93           C  
ATOM   1164  CD  ARG A 155      15.953  10.919  16.885  1.00 13.20           C  
ATOM   1165  NE  ARG A 155      17.000  11.408  17.777  1.00 13.01           N  
ATOM   1166  CZ  ARG A 155      18.117  12.002  17.368  1.00 14.23           C  
ATOM   1167  NH1 ARG A 155      18.384  12.121  16.073  1.00  9.80           N  
ATOM   1168  NH2 ARG A 155      18.997  12.431  18.260  1.00 17.17           N  
ATOM   1169  N   GLN A 156      10.607  11.165  15.345  1.00 11.79           N  
ATOM   1170  CA  GLN A 156       9.495  10.692  14.523  1.00 11.23           C  
ATOM   1171  C   GLN A 156       8.556  11.858  14.215  1.00 11.24           C  
ATOM   1172  O   GLN A 156       8.138  12.041  13.072  1.00 11.69           O  
ATOM   1173  CB  GLN A 156       8.717   9.599  15.263  1.00 11.28           C  
ATOM   1174  CG  GLN A 156       7.495   9.080  14.517  1.00 11.66           C  
ATOM   1175  CD  GLN A 156       7.859   8.218  13.331  1.00  9.92           C  
ATOM   1176  OE1 GLN A 156       8.297   7.082  13.491  1.00 12.07           O  
ATOM   1177  NE2 GLN A 156       7.689   8.751  12.133  1.00 15.03           N  
ATOM   1178  N   ALA A 157       8.233  12.641  15.241  1.00 12.08           N  
ATOM   1179  CA  ALA A 157       7.353  13.797  15.093  1.00 14.52           C  
ATOM   1180  C   ALA A 157       7.962  14.849  14.156  1.00 16.04           C  
ATOM   1181  O   ALA A 157       7.248  15.490  13.373  1.00 12.66           O  
ATOM   1182  CB  ALA A 157       7.053  14.400  16.451  1.00 13.71           C  
ATOM   1183  N   THR A 158       9.281  15.017  14.227  1.00 13.68           N  
ATOM   1184  CA  THR A 158       9.968  15.974  13.364  1.00 11.76           C  
ATOM   1185  C   THR A 158       9.904  15.467  11.923  1.00  9.04           C  
ATOM   1186  O   THR A 158       9.645  16.237  10.997  1.00  9.46           O  
ATOM   1187  CB  THR A 158      11.429  16.180  13.808  1.00 12.23           C  
ATOM   1188  OG1 THR A 158      11.441  16.736  15.127  1.00 14.11           O  
ATOM   1189  CG2 THR A 158      12.159  17.125  12.861  1.00  8.39           C  
ATOM   1190  N   LYS A 159      10.095  14.164  11.744  1.00 10.08           N  
ATOM   1191  CA  LYS A 159      10.030  13.568  10.413  1.00 12.16           C  
ATOM   1192  C   LYS A 159       8.601  13.694   9.885  1.00 11.31           C  
ATOM   1193  O   LYS A 159       8.390  13.995   8.710  1.00 11.85           O  
ATOM   1194  CB  LYS A 159      10.427  12.092  10.449  1.00 12.89           C  
ATOM   1195  CG  LYS A 159      10.283  11.414   9.099  1.00 16.66           C  
ATOM   1196  CD  LYS A 159      10.197   9.905   9.216  1.00 24.16           C  
ATOM   1197  CE  LYS A 159       9.808   9.287   7.875  1.00 30.27           C  
ATOM   1198  NZ  LYS A 159       9.723   7.793   7.892  1.00 32.70           N  
ATOM   1199  N   ASP A 160       7.628  13.476  10.765  1.00  9.89           N  
ATOM   1200  CA  ASP A 160       6.215  13.571  10.394  1.00 12.68           C  
ATOM   1201  C   ASP A 160       5.861  14.962   9.903  1.00  9.94           C  
ATOM   1202  O   ASP A 160       5.100  15.111   8.950  1.00 12.08           O  
ATOM   1203  CB  ASP A 160       5.310  13.186  11.571  1.00 10.63           C  
ATOM   1204  CG  ASP A 160       5.368  11.708  11.889  1.00 11.91           C  
ATOM   1205  OD1 ASP A 160       5.862  10.927  11.047  1.00 14.52           O  
ATOM   1206  OD2 ASP A 160       4.921  11.323  12.988  1.00 14.03           O  
ATOM   1207  N   ALA A 161       6.424  15.979  10.550  1.00 10.62           N  
ATOM   1208  CA  ALA A 161       6.188  17.358  10.160  1.00  8.56           C  
ATOM   1209  C   ALA A 161       6.661  17.544   8.718  1.00 10.33           C  
ATOM   1210  O   ALA A 161       6.005  18.219   7.922  1.00  9.34           O  
ATOM   1211  CB  ALA A 161       6.929  18.297  11.087  1.00  9.75           C  
ATOM   1212  N   GLY A 162       7.788  16.919   8.385  1.00 10.15           N  
ATOM   1213  CA  GLY A 162       8.327  17.009   7.037  1.00 10.04           C  
ATOM   1214  C   GLY A 162       7.397  16.350   6.035  1.00  9.46           C  
ATOM   1215  O   GLY A 162       7.086  16.916   4.985  1.00 10.45           O  
ATOM   1216  N   THR A 163       6.940  15.151   6.375  1.00 10.79           N  
ATOM   1217  CA  THR A 163       6.026  14.385   5.531  1.00 13.51           C  
ATOM   1218  C   THR A 163       4.767  15.202   5.238  1.00 14.15           C  
ATOM   1219  O   THR A 163       4.374  15.352   4.079  1.00 13.93           O  
ATOM   1220  CB  THR A 163       5.650  13.060   6.220  1.00 12.36           C  
ATOM   1221  OG1 THR A 163       6.820  12.237   6.332  1.00 16.85           O  
ATOM   1222  CG2 THR A 163       4.585  12.319   5.441  1.00 10.59           C  
ATOM   1223  N   ILE A 164       4.183  15.774   6.288  1.00 15.39           N  
ATOM   1224  CA  ILE A 164       2.974  16.593   6.184  1.00 12.94           C  
ATOM   1225  C   ILE A 164       3.212  17.785   5.254  1.00 13.99           C  
ATOM   1226  O   ILE A 164       2.317  18.186   4.499  1.00 12.90           O  
ATOM   1227  CB  ILE A 164       2.537  17.080   7.588  1.00 10.79           C  
ATOM   1228  CG1 ILE A 164       2.159  15.877   8.451  1.00 10.87           C  
ATOM   1229  CG2 ILE A 164       1.378  18.063   7.495  1.00  9.39           C  
ATOM   1230  CD1 ILE A 164       1.988  16.202   9.928  1.00 15.27           C  
ATOM   1231  N   ALA A 165       4.434  18.311   5.278  1.00 11.36           N  
ATOM   1232  CA  ALA A 165       4.812  19.444   4.436  1.00 11.18           C  
ATOM   1233  C   ALA A 165       5.077  19.022   2.992  1.00 10.57           C  
ATOM   1234  O   ALA A 165       5.382  19.861   2.145  1.00 14.82           O  
ATOM   1235  CB  ALA A 165       6.044  20.153   5.013  1.00  9.57           C  
ATOM   1236  N   GLY A 166       4.982  17.726   2.718  1.00  9.34           N  
ATOM   1237  CA  GLY A 166       5.213  17.235   1.370  1.00 12.72           C  
ATOM   1238  C   GLY A 166       6.673  16.943   1.071  1.00 14.82           C  
ATOM   1239  O   GLY A 166       7.083  16.907  -0.090  1.00 13.42           O  
ATOM   1240  N   LEU A 167       7.460  16.729   2.119  1.00 12.56           N  
ATOM   1241  CA  LEU A 167       8.871  16.435   1.957  1.00 14.35           C  
ATOM   1242  C   LEU A 167       9.127  14.972   2.241  1.00 16.32           C  
ATOM   1243  O   LEU A 167       8.469  14.366   3.093  1.00 15.80           O  
ATOM   1244  CB  LEU A 167       9.714  17.260   2.939  1.00 11.44           C  
ATOM   1245  CG  LEU A 167       9.775  18.785   2.811  1.00 15.31           C  
ATOM   1246  CD1 LEU A 167      10.525  19.364   4.006  1.00 14.55           C  
ATOM   1247  CD2 LEU A 167      10.458  19.173   1.498  1.00 20.20           C  
ATOM   1248  N   ASN A 168      10.051  14.392   1.488  1.00 17.16           N  
ATOM   1249  CA  ASN A 168      10.446  13.016   1.715  1.00 16.78           C  
ATOM   1250  C   ASN A 168      11.713  13.198   2.528  1.00 15.11           C  
ATOM   1251  O   ASN A 168      12.733  13.650   2.001  1.00 12.75           O  
ATOM   1252  CB  ASN A 168      10.766  12.293   0.409  1.00 17.44           C  
ATOM   1253  CG  ASN A 168      11.420  10.944   0.647  1.00 19.03           C  
ATOM   1254  OD1 ASN A 168      10.963  10.165   1.480  1.00 19.15           O  
ATOM   1255  ND2 ASN A 168      12.510  10.674  -0.059  1.00 20.73           N  
ATOM   1256  N   VAL A 169      11.619  12.947   3.828  1.00 15.98           N  
ATOM   1257  CA  VAL A 169      12.768  13.102   4.710  1.00 14.12           C  
ATOM   1258  C   VAL A 169      13.751  11.948   4.519  1.00 16.04           C  
ATOM   1259  O   VAL A 169      13.490  10.811   4.925  1.00 15.60           O  
ATOM   1260  CB  VAL A 169      12.334  13.246   6.198  1.00 12.02           C  
ATOM   1261  CG1 VAL A 169      13.554  13.368   7.104  1.00  9.95           C  
ATOM   1262  CG2 VAL A 169      11.437  14.468   6.361  1.00 11.07           C  
ATOM   1263  N   LEU A 170      14.846  12.246   3.822  1.00 14.70           N  
ATOM   1264  CA  LEU A 170      15.896  11.274   3.546  1.00 16.28           C  
ATOM   1265  C   LEU A 170      16.509  10.763   4.843  1.00 18.67           C  
ATOM   1266  O   LEU A 170      16.758   9.563   4.990  1.00 19.21           O  
ATOM   1267  CB  LEU A 170      16.991  11.906   2.675  1.00 15.79           C  
ATOM   1268  CG  LEU A 170      16.608  12.317   1.247  1.00 16.26           C  
ATOM   1269  CD1 LEU A 170      17.762  13.031   0.565  1.00 15.38           C  
ATOM   1270  CD2 LEU A 170      16.206  11.087   0.452  1.00 16.27           C  
ATOM   1271  N   ARG A 171      16.734  11.670   5.787  1.00 17.53           N  
ATOM   1272  CA  ARG A 171      17.328  11.293   7.058  1.00 18.51           C  
ATOM   1273  C   ARG A 171      17.173  12.424   8.067  1.00 16.68           C  
ATOM   1274  O   ARG A 171      17.007  13.587   7.688  1.00 15.55           O  
ATOM   1275  CB  ARG A 171      18.818  10.959   6.865  1.00 20.55           C  
ATOM   1276  CG  ARG A 171      19.395  10.045   7.949  1.00 28.84           C  
ATOM   1277  CD  ARG A 171      20.754   9.435   7.577  1.00 34.22           C  
ATOM   1278  NE  ARG A 171      20.761   8.341   6.584  1.00 41.59           N  
ATOM   1279  CZ  ARG A 171      19.699   7.660   6.132  1.00 45.06           C  
ATOM   1280  NH1 ARG A 171      18.455   7.907   6.554  1.00 45.67           N  
ATOM   1281  NH2 ARG A 171      19.883   6.691   5.242  1.00 48.07           N  
ATOM   1282  N   ILE A 172      17.119  12.055   9.344  1.00 15.85           N  
ATOM   1283  CA  ILE A 172      17.044  13.016  10.440  1.00 14.40           C  
ATOM   1284  C   ILE A 172      18.443  12.929  11.045  1.00 13.63           C  
ATOM   1285  O   ILE A 172      18.875  11.840  11.435  1.00 12.66           O  
ATOM   1286  CB  ILE A 172      16.011  12.597  11.532  1.00 11.80           C  
ATOM   1287  CG1 ILE A 172      14.574  12.766  11.029  1.00  7.89           C  
ATOM   1288  CG2 ILE A 172      16.198  13.447  12.777  1.00  9.55           C  
ATOM   1289  CD1 ILE A 172      14.117  14.217  10.952  1.00 10.83           C  
ATOM   1290  N   ILE A 173      19.183  14.033  11.050  1.00 15.39           N  
ATOM   1291  CA  ILE A 173      20.529  14.018  11.620  1.00 13.28           C  
ATOM   1292  C   ILE A 173      20.674  15.058  12.728  1.00 13.02           C  
ATOM   1293  O   ILE A 173      19.917  16.036  12.786  1.00 13.33           O  
ATOM   1294  CB  ILE A 173      21.648  14.221  10.538  1.00 16.18           C  
ATOM   1295  CG1 ILE A 173      21.716  15.672  10.063  1.00 17.60           C  
ATOM   1296  CG2 ILE A 173      21.412  13.303   9.345  1.00 15.21           C  
ATOM   1297  CD1 ILE A 173      22.829  15.932   9.051  1.00 18.86           C  
ATOM   1298  N   ASN A 174      21.644  14.845  13.610  1.00 11.45           N  
ATOM   1299  CA  ASN A 174      21.886  15.768  14.718  1.00 11.84           C  
ATOM   1300  C   ASN A 174      22.459  17.106  14.271  1.00  8.96           C  
ATOM   1301  O   ASN A 174      23.345  17.166  13.421  1.00  9.44           O  
ATOM   1302  CB  ASN A 174      22.834  15.148  15.746  1.00 11.32           C  
ATOM   1303  CG  ASN A 174      22.169  14.089  16.595  1.00 15.53           C  
ATOM   1304  OD1 ASN A 174      20.943  13.956  16.604  1.00 14.92           O  
ATOM   1305  ND2 ASN A 174      22.977  13.323  17.318  1.00 14.65           N  
ATOM   1306  N   GLU A 175      21.978  18.177  14.886  1.00 10.49           N  
ATOM   1307  CA  GLU A 175      22.442  19.526  14.586  1.00  9.05           C  
ATOM   1308  C   GLU A 175      23.956  19.681  14.778  1.00 10.26           C  
ATOM   1309  O   GLU A 175      24.621  20.279  13.936  1.00  9.10           O  
ATOM   1310  CB  GLU A 175      21.671  20.550  15.422  1.00  8.98           C  
ATOM   1311  CG  GLU A 175      20.207  20.680  15.001  1.00  5.75           C  
ATOM   1312  CD  GLU A 175      19.325  21.336  16.044  1.00 12.43           C  
ATOM   1313  OE1 GLU A 175      19.848  21.974  16.989  1.00 11.68           O  
ATOM   1314  OE2 GLU A 175      18.087  21.210  15.912  1.00 10.19           O  
ATOM   1315  N   PRO A 176      24.518  19.162  15.886  1.00 10.95           N  
ATOM   1316  CA  PRO A 176      25.969  19.315  16.051  1.00 11.88           C  
ATOM   1317  C   PRO A 176      26.765  18.564  14.969  1.00 11.99           C  
ATOM   1318  O   PRO A 176      27.798  19.045  14.503  1.00 12.58           O  
ATOM   1319  CB  PRO A 176      26.224  18.769  17.461  1.00 11.49           C  
ATOM   1320  CG  PRO A 176      25.061  17.831  17.706  1.00 14.53           C  
ATOM   1321  CD  PRO A 176      23.908  18.578  17.100  1.00 12.37           C  
ATOM   1322  N   THR A 177      26.266  17.402  14.552  1.00 10.51           N  
ATOM   1323  CA  THR A 177      26.922  16.621  13.510  1.00 11.33           C  
ATOM   1324  C   THR A 177      26.861  17.397  12.193  1.00 11.63           C  
ATOM   1325  O   THR A 177      27.837  17.437  11.444  1.00 13.41           O  
ATOM   1326  CB  THR A 177      26.257  15.243  13.353  1.00 11.70           C  
ATOM   1327  OG1 THR A 177      26.513  14.459  14.525  1.00 18.76           O  
ATOM   1328  CG2 THR A 177      26.784  14.513  12.130  1.00 12.97           C  
ATOM   1329  N   ALA A 178      25.723  18.037  11.933  1.00 11.69           N  
ATOM   1330  CA  ALA A 178      25.532  18.840  10.725  1.00 10.86           C  
ATOM   1331  C   ALA A 178      26.538  19.992  10.685  1.00 12.97           C  
ATOM   1332  O   ALA A 178      27.118  20.288   9.630  1.00  9.94           O  
ATOM   1333  CB  ALA A 178      24.114  19.388  10.678  1.00 11.03           C  
ATOM   1334  N   ALA A 179      26.748  20.633  11.837  1.00 12.61           N  
ATOM   1335  CA  ALA A 179      27.693  21.746  11.942  1.00 10.31           C  
ATOM   1336  C   ALA A 179      29.106  21.263  11.616  1.00  9.45           C  
ATOM   1337  O   ALA A 179      29.876  21.957  10.946  1.00  9.52           O  
ATOM   1338  CB  ALA A 179      27.645  22.359  13.337  1.00  7.26           C  
ATOM   1339  N   ALA A 180      29.438  20.063  12.078  1.00 10.18           N  
ATOM   1340  CA  ALA A 180      30.754  19.483  11.828  1.00 10.61           C  
ATOM   1341  C   ALA A 180      30.919  19.183  10.339  1.00 12.60           C  
ATOM   1342  O   ALA A 180      31.993  19.405   9.757  1.00 13.05           O  
ATOM   1343  CB  ALA A 180      30.927  18.223  12.643  1.00 10.44           C  
ATOM   1344  N   ILE A 181      29.850  18.687   9.722  1.00 11.53           N  
ATOM   1345  CA  ILE A 181      29.856  18.373   8.300  1.00 11.59           C  
ATOM   1346  C   ILE A 181      30.071  19.645   7.489  1.00 11.73           C  
ATOM   1347  O   ILE A 181      30.819  19.634   6.516  1.00 13.55           O  
ATOM   1348  CB  ILE A 181      28.543  17.667   7.865  1.00 11.51           C  
ATOM   1349  CG1 ILE A 181      28.516  16.240   8.418  1.00 11.25           C  
ATOM   1350  CG2 ILE A 181      28.419  17.638   6.339  1.00 11.19           C  
ATOM   1351  CD1 ILE A 181      27.233  15.502   8.164  1.00 11.96           C  
ATOM   1352  N   ALA A 182      29.447  20.742   7.912  1.00 10.35           N  
ATOM   1353  CA  ALA A 182      29.580  22.026   7.224  1.00 10.04           C  
ATOM   1354  C   ALA A 182      31.045  22.452   7.066  1.00 12.56           C  
ATOM   1355  O   ALA A 182      31.423  23.042   6.050  1.00 12.41           O  
ATOM   1356  CB  ALA A 182      28.798  23.098   7.964  1.00  8.60           C  
ATOM   1357  N   TYR A 183      31.865  22.158   8.073  1.00 12.59           N  
ATOM   1358  CA  TYR A 183      33.287  22.508   8.038  1.00 12.78           C  
ATOM   1359  C   TYR A 183      34.189  21.412   7.457  1.00 14.39           C  
ATOM   1360  O   TYR A 183      35.415  21.531   7.491  1.00 16.08           O  
ATOM   1361  CB  TYR A 183      33.778  22.923   9.432  1.00  9.95           C  
ATOM   1362  CG  TYR A 183      33.375  24.325   9.815  1.00  9.19           C  
ATOM   1363  CD1 TYR A 183      34.105  25.419   9.371  1.00  4.67           C  
ATOM   1364  CD2 TYR A 183      32.239  24.564  10.587  1.00 10.31           C  
ATOM   1365  CE1 TYR A 183      33.730  26.713   9.684  1.00  5.53           C  
ATOM   1366  CE2 TYR A 183      31.850  25.866  10.910  1.00  8.27           C  
ATOM   1367  CZ  TYR A 183      32.600  26.932  10.449  1.00  8.07           C  
ATOM   1368  OH  TYR A 183      32.242  28.216  10.758  1.00  8.18           O  
ATOM   1369  N   GLY A 184      33.582  20.354   6.928  1.00 14.38           N  
ATOM   1370  CA  GLY A 184      34.340  19.260   6.344  1.00 13.74           C  
ATOM   1371  C   GLY A 184      35.077  18.418   7.367  1.00 16.79           C  
ATOM   1372  O   GLY A 184      35.941  17.615   7.016  1.00 17.21           O  
ATOM   1373  N   LEU A 185      34.704  18.553   8.633  1.00 15.81           N  
ATOM   1374  CA  LEU A 185      35.358  17.800   9.695  1.00 16.79           C  
ATOM   1375  C   LEU A 185      35.037  16.313   9.623  1.00 17.98           C  
ATOM   1376  O   LEU A 185      35.626  15.507  10.340  1.00 18.75           O  
ATOM   1377  CB  LEU A 185      34.992  18.378  11.068  1.00 15.55           C  
ATOM   1378  CG  LEU A 185      35.418  19.839  11.264  1.00 19.68           C  
ATOM   1379  CD1 LEU A 185      34.943  20.364  12.604  1.00 18.40           C  
ATOM   1380  CD2 LEU A 185      36.930  19.958  11.151  1.00 19.06           C  
ATOM   1381  N   ASP A 186      34.098  15.953   8.753  1.00 19.10           N  
ATOM   1382  CA  ASP A 186      33.705  14.562   8.569  1.00 20.91           C  
ATOM   1383  C   ASP A 186      34.612  13.836   7.571  1.00 22.41           C  
ATOM   1384  O   ASP A 186      34.573  12.613   7.477  1.00 23.46           O  
ATOM   1385  CB  ASP A 186      32.240  14.469   8.120  1.00 22.35           C  
ATOM   1386  CG  ASP A 186      31.979  15.165   6.787  1.00 24.16           C  
ATOM   1387  OD1 ASP A 186      32.478  16.292   6.570  1.00 24.69           O  
ATOM   1388  OD2 ASP A 186      31.251  14.582   5.955  1.00 31.32           O  
ATOM   1389  N   LYS A 187      35.410  14.588   6.814  1.00 24.38           N  
ATOM   1390  CA  LYS A 187      36.324  13.987   5.842  1.00 27.42           C  
ATOM   1391  C   LYS A 187      37.294  13.056   6.565  1.00 27.87           C  
ATOM   1392  O   LYS A 187      37.794  13.383   7.643  1.00 26.24           O  
ATOM   1393  CB  LYS A 187      37.113  15.059   5.091  1.00 29.67           C  
ATOM   1394  CG  LYS A 187      36.285  15.957   4.192  1.00 32.24           C  
ATOM   1395  CD  LYS A 187      37.206  16.925   3.481  1.00 35.14           C  
ATOM   1396  CE  LYS A 187      36.462  17.868   2.568  1.00 36.38           C  
ATOM   1397  NZ  LYS A 187      37.438  18.732   1.843  1.00 40.53           N  
ATOM   1398  N   LYS A 188      37.568  11.907   5.961  1.00 30.33           N  
ATOM   1399  CA  LYS A 188      38.456  10.921   6.559  1.00 36.52           C  
ATOM   1400  C   LYS A 188      39.908  11.379   6.647  1.00 40.00           C  
ATOM   1401  O   LYS A 188      40.437  11.992   5.716  1.00 41.72           O  
ATOM   1402  CB  LYS A 188      38.370   9.611   5.795  1.00 36.70           C  
ATOM   1403  N   VAL A 189      40.548  11.065   7.768  1.00 44.23           N  
ATOM   1404  CA  VAL A 189      41.949  11.415   7.985  1.00 47.98           C  
ATOM   1405  C   VAL A 189      42.641  10.302   8.793  1.00 50.35           C  
ATOM   1406  O   VAL A 189      43.810  10.419   9.174  1.00 50.87           O  
ATOM   1407  CB  VAL A 189      42.090  12.818   8.672  1.00 48.64           C  
ATOM   1408  CG1 VAL A 189      41.794  12.736  10.168  1.00 48.94           C  
ATOM   1409  CG2 VAL A 189      43.464  13.422   8.392  1.00 45.90           C  
ATOM   1410  N   GLY A 190      41.924   9.197   9.001  1.00 52.93           N  
ATOM   1411  CA  GLY A 190      42.476   8.072   9.741  1.00 54.85           C  
ATOM   1412  C   GLY A 190      42.397   8.248  11.244  1.00 56.03           C  
ATOM   1413  O   GLY A 190      41.586   7.600  11.910  1.00 57.37           O  
ATOM   1414  N   ALA A 191      43.228   9.139  11.778  1.00 56.26           N  
ATOM   1415  CA  ALA A 191      43.251   9.407  13.210  1.00 53.98           C  
ATOM   1416  C   ALA A 191      42.011  10.195  13.632  1.00 52.60           C  
ATOM   1417  O   ALA A 191      41.579  11.120  12.932  1.00 49.84           O  
ATOM   1418  CB  ALA A 191      44.517  10.166  13.581  1.00 55.04           C  
ATOM   1419  N   GLU A 192      41.429   9.806  14.761  1.00 51.29           N  
ATOM   1420  CA  GLU A 192      40.239  10.472  15.276  1.00 50.49           C  
ATOM   1421  C   GLU A 192      40.523  11.897  15.747  1.00 47.73           C  
ATOM   1422  O   GLU A 192      41.639  12.223  16.162  1.00 46.39           O  
ATOM   1423  CB  GLU A 192      39.603   9.659  16.410  1.00 51.85           C  
ATOM   1424  CG  GLU A 192      40.494   9.451  17.624  1.00 56.88           C  
ATOM   1425  CD  GLU A 192      39.795   8.706  18.749  1.00 60.01           C  
ATOM   1426  OE1 GLU A 192      39.072   7.725  18.465  1.00 62.13           O  
ATOM   1427  OE2 GLU A 192      39.971   9.103  19.921  1.00 61.31           O  
ATOM   1428  N   ARG A 193      39.502  12.742  15.672  1.00 45.02           N  
ATOM   1429  CA  ARG A 193      39.613  14.132  16.088  1.00 41.65           C  
ATOM   1430  C   ARG A 193      38.472  14.461  17.049  1.00 37.52           C  
ATOM   1431  O   ARG A 193      37.371  13.924  16.926  1.00 37.09           O  
ATOM   1432  CB  ARG A 193      39.554  15.055  14.866  1.00 45.55           C  
ATOM   1433  CG  ARG A 193      40.670  14.851  13.842  1.00 52.42           C  
ATOM   1434  CD  ARG A 193      42.001  15.446  14.295  1.00 58.53           C  
ATOM   1435  NE  ARG A 193      43.090  15.135  13.364  1.00 62.59           N  
ATOM   1436  CZ  ARG A 193      43.840  14.036  13.426  1.00 64.27           C  
ATOM   1437  NH1 ARG A 193      43.627  13.136  14.377  1.00 63.91           N  
ATOM   1438  NH2 ARG A 193      44.803  13.831  12.534  1.00 63.63           N  
ATOM   1439  N   ASN A 194      38.752  15.309  18.034  1.00 34.12           N  
ATOM   1440  CA  ASN A 194      37.749  15.710  19.015  1.00 29.87           C  
ATOM   1441  C   ASN A 194      37.247  17.106  18.679  1.00 26.33           C  
ATOM   1442  O   ASN A 194      38.031  18.061  18.628  1.00 22.87           O  
ATOM   1443  CB  ASN A 194      38.337  15.688  20.427  1.00 30.58           C  
ATOM   1444  CG  ASN A 194      38.631  14.283  20.916  1.00 31.17           C  
ATOM   1445  OD1 ASN A 194      37.857  13.346  20.681  1.00 32.40           O  
ATOM   1446  ND2 ASN A 194      39.747  14.129  21.614  1.00 30.02           N  
ATOM   1447  N   VAL A 195      35.946  17.209  18.426  1.00 22.89           N  
ATOM   1448  CA  VAL A 195      35.314  18.472  18.061  1.00 20.26           C  
ATOM   1449  C   VAL A 195      34.280  18.900  19.109  1.00 16.56           C  
ATOM   1450  O   VAL A 195      33.503  18.083  19.611  1.00 15.19           O  
ATOM   1451  CB  VAL A 195      34.612  18.355  16.672  1.00 20.53           C  
ATOM   1452  CG1 VAL A 195      34.033  19.695  16.237  1.00 17.08           C  
ATOM   1453  CG2 VAL A 195      35.591  17.834  15.627  1.00 21.97           C  
ATOM   1454  N   LEU A 196      34.300  20.179  19.459  1.00 15.55           N  
ATOM   1455  CA  LEU A 196      33.349  20.713  20.419  1.00 15.02           C  
ATOM   1456  C   LEU A 196      32.419  21.662  19.682  1.00 12.40           C  
ATOM   1457  O   LEU A 196      32.872  22.615  19.043  1.00 13.69           O  
ATOM   1458  CB  LEU A 196      34.068  21.454  21.556  1.00 15.37           C  
ATOM   1459  CG  LEU A 196      33.200  22.039  22.677  1.00 14.75           C  
ATOM   1460  CD1 LEU A 196      33.923  21.885  24.006  1.00 15.81           C  
ATOM   1461  CD2 LEU A 196      32.852  23.506  22.412  1.00 15.21           C  
ATOM   1462  N   ILE A 197      31.124  21.374  19.735  1.00 13.20           N  
ATOM   1463  CA  ILE A 197      30.125  22.219  19.095  1.00 13.62           C  
ATOM   1464  C   ILE A 197      29.505  23.093  20.190  1.00 12.91           C  
ATOM   1465  O   ILE A 197      28.892  22.586  21.131  1.00 14.30           O  
ATOM   1466  CB  ILE A 197      29.008  21.376  18.408  1.00 12.59           C  
ATOM   1467  CG1 ILE A 197      29.621  20.290  17.514  1.00 12.08           C  
ATOM   1468  CG2 ILE A 197      28.085  22.287  17.599  1.00 12.75           C  
ATOM   1469  CD1 ILE A 197      30.534  20.808  16.400  1.00  8.97           C  
ATOM   1470  N   PHE A 198      29.732  24.396  20.094  1.00 12.94           N  
ATOM   1471  CA  PHE A 198      29.206  25.362  21.053  1.00 13.63           C  
ATOM   1472  C   PHE A 198      28.036  26.052  20.344  1.00 12.81           C  
ATOM   1473  O   PHE A 198      28.227  26.883  19.454  1.00  9.74           O  
ATOM   1474  CB  PHE A 198      30.306  26.366  21.413  1.00 13.05           C  
ATOM   1475  CG  PHE A 198      29.904  27.380  22.446  1.00 11.04           C  
ATOM   1476  CD1 PHE A 198      29.301  28.576  22.069  1.00  7.85           C  
ATOM   1477  CD2 PHE A 198      30.181  27.163  23.791  1.00 14.07           C  
ATOM   1478  CE1 PHE A 198      28.985  29.544  23.009  1.00 12.13           C  
ATOM   1479  CE2 PHE A 198      29.867  28.131  24.748  1.00 11.92           C  
ATOM   1480  CZ  PHE A 198      29.271  29.324  24.355  1.00 11.32           C  
ATOM   1481  N   ASP A 199      26.826  25.706  20.758  1.00 10.73           N  
ATOM   1482  CA  ASP A 199      25.622  26.235  20.136  1.00  9.56           C  
ATOM   1483  C   ASP A 199      24.799  27.093  21.092  1.00  9.37           C  
ATOM   1484  O   ASP A 199      24.168  26.585  22.020  1.00 10.24           O  
ATOM   1485  CB  ASP A 199      24.791  25.051  19.619  1.00  7.37           C  
ATOM   1486  CG  ASP A 199      23.661  25.463  18.683  1.00  9.90           C  
ATOM   1487  OD1 ASP A 199      23.138  26.601  18.784  1.00  6.77           O  
ATOM   1488  OD2 ASP A 199      23.273  24.605  17.855  1.00  8.70           O  
ATOM   1489  N   LEU A 200      24.822  28.399  20.858  1.00  9.40           N  
ATOM   1490  CA  LEU A 200      24.056  29.343  21.652  1.00  8.79           C  
ATOM   1491  C   LEU A 200      23.076  29.976  20.672  1.00  8.36           C  
ATOM   1492  O   LEU A 200      23.444  30.853  19.886  1.00 10.91           O  
ATOM   1493  CB  LEU A 200      24.965  30.407  22.274  1.00  7.79           C  
ATOM   1494  CG  LEU A 200      24.298  31.414  23.215  1.00 10.20           C  
ATOM   1495  CD1 LEU A 200      23.672  30.700  24.400  1.00 10.04           C  
ATOM   1496  CD2 LEU A 200      25.308  32.440  23.680  1.00  7.21           C  
ATOM   1497  N   GLY A 201      21.836  29.500  20.695  1.00  9.59           N  
ATOM   1498  CA  GLY A 201      20.827  30.011  19.783  1.00  9.20           C  
ATOM   1499  C   GLY A 201      19.912  31.101  20.305  1.00  7.46           C  
ATOM   1500  O   GLY A 201      20.317  31.967  21.080  1.00  9.72           O  
ATOM   1501  N   GLY A 202      18.678  31.084  19.822  1.00  7.79           N  
ATOM   1502  CA  GLY A 202      17.698  32.066  20.238  1.00  8.49           C  
ATOM   1503  C   GLY A 202      16.969  31.656  21.503  1.00  8.75           C  
ATOM   1504  O   GLY A 202      16.516  32.507  22.265  1.00 10.35           O  
ATOM   1505  N   GLY A 203      16.871  30.356  21.744  1.00 10.33           N  
ATOM   1506  CA  GLY A 203      16.182  29.896  22.933  1.00 11.51           C  
ATOM   1507  C   GLY A 203      16.878  28.835  23.757  1.00  9.77           C  
ATOM   1508  O   GLY A 203      16.567  28.692  24.937  1.00 12.22           O  
ATOM   1509  N   THR A 204      17.827  28.109  23.169  1.00 10.52           N  
ATOM   1510  CA  THR A 204      18.525  27.047  23.894  1.00 10.11           C  
ATOM   1511  C   THR A 204      20.035  27.101  23.717  1.00 11.61           C  
ATOM   1512  O   THR A 204      20.540  27.578  22.695  1.00  8.97           O  
ATOM   1513  CB  THR A 204      18.059  25.648  23.425  1.00 12.12           C  
ATOM   1514  OG1 THR A 204      18.462  25.442  22.065  1.00 14.06           O  
ATOM   1515  CG2 THR A 204      16.526  25.522  23.516  1.00 12.21           C  
ATOM   1516  N   PHE A 205      20.746  26.584  24.711  1.00 11.08           N  
ATOM   1517  CA  PHE A 205      22.204  26.536  24.688  1.00 11.77           C  
ATOM   1518  C   PHE A 205      22.595  25.070  24.755  1.00 10.30           C  
ATOM   1519  O   PHE A 205      22.077  24.324  25.591  1.00 10.43           O  
ATOM   1520  CB  PHE A 205      22.786  27.299  25.887  1.00 10.79           C  
ATOM   1521  CG  PHE A 205      24.271  27.128  26.050  1.00 12.83           C  
ATOM   1522  CD1 PHE A 205      25.135  27.335  24.973  1.00 11.38           C  
ATOM   1523  CD2 PHE A 205      24.808  26.741  27.277  1.00 10.81           C  
ATOM   1524  CE1 PHE A 205      26.509  27.151  25.117  1.00  9.38           C  
ATOM   1525  CE2 PHE A 205      26.177  26.556  27.428  1.00 12.39           C  
ATOM   1526  CZ  PHE A 205      27.032  26.764  26.346  1.00 10.59           C  
ATOM   1527  N   LYS A 206      23.494  24.645  23.871  1.00 10.79           N  
ATOM   1528  CA  LYS A 206      23.918  23.252  23.848  1.00 10.37           C  
ATOM   1529  C   LYS A 206      25.328  23.048  23.342  1.00 11.32           C  
ATOM   1530  O   LYS A 206      25.753  23.659  22.366  1.00 13.01           O  
ATOM   1531  CB  LYS A 206      22.929  22.366  23.062  1.00 11.99           C  
ATOM   1532  CG  LYS A 206      22.536  22.842  21.657  1.00  9.94           C  
ATOM   1533  CD  LYS A 206      21.682  24.122  21.677  1.00 11.00           C  
ATOM   1534  CE  LYS A 206      21.051  24.410  20.323  1.00  9.42           C  
ATOM   1535  NZ  LYS A 206      20.625  25.834  20.194  1.00  9.75           N  
ATOM   1536  N   VAL A 207      26.040  22.164  24.024  1.00 12.06           N  
ATOM   1537  CA  VAL A 207      27.411  21.829  23.698  1.00 13.06           C  
ATOM   1538  C   VAL A 207      27.511  20.327  23.525  1.00 13.61           C  
ATOM   1539  O   VAL A 207      26.986  19.559  24.336  1.00 19.41           O  
ATOM   1540  CB  VAL A 207      28.360  22.240  24.851  1.00 13.52           C  
ATOM   1541  CG1 VAL A 207      29.789  21.765  24.570  1.00 15.40           C  
ATOM   1542  CG2 VAL A 207      28.316  23.740  25.053  1.00  9.31           C  
ATOM   1543  N   SER A 208      28.162  19.905  22.456  1.00 14.48           N  
ATOM   1544  CA  SER A 208      28.366  18.489  22.213  1.00 17.23           C  
ATOM   1545  C   SER A 208      29.840  18.308  21.913  1.00 17.47           C  
ATOM   1546  O   SER A 208      30.483  19.211  21.373  1.00 16.67           O  
ATOM   1547  CB  SER A 208      27.525  17.993  21.028  1.00 17.27           C  
ATOM   1548  OG  SER A 208      26.142  18.022  21.330  1.00 21.26           O  
ATOM   1549  N   ILE A 209      30.394  17.186  22.349  1.00 19.55           N  
ATOM   1550  CA  ILE A 209      31.787  16.877  22.081  1.00 23.56           C  
ATOM   1551  C   ILE A 209      31.711  15.609  21.263  1.00 25.00           C  
ATOM   1552  O   ILE A 209      31.109  14.617  21.686  1.00 24.27           O  
ATOM   1553  CB  ILE A 209      32.611  16.670  23.371  1.00 23.78           C  
ATOM   1554  CG1 ILE A 209      32.676  17.991  24.150  1.00 22.82           C  
ATOM   1555  CG2 ILE A 209      34.014  16.167  23.024  1.00 21.50           C  
ATOM   1556  CD1 ILE A 209      33.612  17.988  25.337  1.00 25.75           C  
ATOM   1557  N   LEU A 210      32.229  15.686  20.047  1.00 26.82           N  
ATOM   1558  CA  LEU A 210      32.199  14.563  19.127  1.00 28.41           C  
ATOM   1559  C   LEU A 210      33.606  14.083  18.849  1.00 30.25           C  
ATOM   1560  O   LEU A 210      34.558  14.863  18.866  1.00 30.75           O  
ATOM   1561  CB  LEU A 210      31.558  14.991  17.801  1.00 25.57           C  
ATOM   1562  CG  LEU A 210      30.277  15.832  17.846  1.00 24.32           C  
ATOM   1563  CD1 LEU A 210      29.929  16.349  16.451  1.00 21.24           C  
ATOM   1564  CD2 LEU A 210      29.144  15.015  18.419  1.00 21.62           C  
ATOM   1565  N   THR A 211      33.728  12.790  18.599  1.00 32.90           N  
ATOM   1566  CA  THR A 211      35.004  12.189  18.267  1.00 35.96           C  
ATOM   1567  C   THR A 211      34.754  11.643  16.863  1.00 34.70           C  
ATOM   1568  O   THR A 211      33.819  10.869  16.642  1.00 32.81           O  
ATOM   1569  CB  THR A 211      35.379  11.075  19.263  1.00 36.08           C  
ATOM   1570  OG1 THR A 211      35.351  11.607  20.593  1.00 36.03           O  
ATOM   1571  CG2 THR A 211      36.780  10.558  18.977  1.00 35.84           C  
ATOM   1572  N   ILE A 212      35.521  12.137  15.900  1.00 36.26           N  
ATOM   1573  CA  ILE A 212      35.348  11.732  14.516  1.00 40.06           C  
ATOM   1574  C   ILE A 212      36.503  10.915  13.960  1.00 42.13           C  
ATOM   1575  O   ILE A 212      37.638  11.390  13.882  1.00 39.91           O  
ATOM   1576  CB  ILE A 212      35.136  12.971  13.605  1.00 39.76           C  
ATOM   1577  CG1 ILE A 212      34.010  13.850  14.164  1.00 37.05           C  
ATOM   1578  CG2 ILE A 212      34.807  12.530  12.176  1.00 37.81           C  
ATOM   1579  CD1 ILE A 212      33.928  15.225  13.537  1.00 33.76           C  
ATOM   1580  N   GLU A 213      36.202   9.678  13.581  1.00 47.07           N  
ATOM   1581  CA  GLU A 213      37.194   8.801  12.982  1.00 52.52           C  
ATOM   1582  C   GLU A 213      36.582   8.161  11.745  1.00 54.03           C  
ATOM   1583  O   GLU A 213      35.534   7.507  11.820  1.00 52.35           O  
ATOM   1584  CB  GLU A 213      37.669   7.722  13.954  1.00 56.01           C  
ATOM   1585  CG  GLU A 213      38.809   6.881  13.380  1.00 60.30           C  
ATOM   1586  CD  GLU A 213      39.411   5.920  14.381  1.00 61.54           C  
ATOM   1587  OE1 GLU A 213      40.260   6.357  15.188  1.00 61.96           O  
ATOM   1588  OE2 GLU A 213      39.047   4.725  14.350  1.00 64.20           O  
ATOM   1589  N   ASP A 214      37.198   8.440  10.600  1.00 57.34           N  
ATOM   1590  CA  ASP A 214      36.769   7.914   9.309  1.00 59.74           C  
ATOM   1591  C   ASP A 214      35.289   8.195   9.038  1.00 59.63           C  
ATOM   1592  O   ASP A 214      34.529   7.294   8.668  1.00 59.77           O  
ATOM   1593  CB  ASP A 214      37.068   6.412   9.214  1.00 64.42           C  
ATOM   1594  CG  ASP A 214      38.525   6.079   9.531  1.00 69.20           C  
ATOM   1595  OD1 ASP A 214      39.433   6.813   9.073  1.00 67.98           O  
ATOM   1596  OD2 ASP A 214      38.758   5.080  10.249  1.00 73.45           O  
ATOM   1597  N   GLY A 215      34.888   9.443   9.265  1.00 56.98           N  
ATOM   1598  CA  GLY A 215      33.513   9.845   9.029  1.00 55.63           C  
ATOM   1599  C   GLY A 215      32.464   9.385  10.025  1.00 55.14           C  
ATOM   1600  O   GLY A 215      31.308   9.795   9.921  1.00 57.43           O  
ATOM   1601  N   ILE A 216      32.837   8.531  10.973  1.00 54.62           N  
ATOM   1602  CA  ILE A 216      31.883   8.052  11.973  1.00 52.26           C  
ATOM   1603  C   ILE A 216      31.915   8.965  13.202  1.00 49.38           C  
ATOM   1604  O   ILE A 216      32.975   9.180  13.801  1.00 45.74           O  
ATOM   1605  CB  ILE A 216      32.159   6.574  12.362  1.00 53.61           C  
ATOM   1606  CG1 ILE A 216      31.882   5.667  11.155  1.00 52.46           C  
ATOM   1607  CG2 ILE A 216      31.295   6.158  13.550  1.00 54.62           C  
ATOM   1608  CD1 ILE A 216      32.046   4.183  11.427  1.00 52.38           C  
ATOM   1609  N   PHE A 217      30.753   9.517  13.548  1.00 48.62           N  
ATOM   1610  CA  PHE A 217      30.626  10.432  14.680  1.00 48.82           C  
ATOM   1611  C   PHE A 217      30.302   9.783  16.014  1.00 49.70           C  
ATOM   1612  O   PHE A 217      29.199   9.271  16.221  1.00 49.72           O  
ATOM   1613  CB  PHE A 217      29.584  11.514  14.387  1.00 46.85           C  
ATOM   1614  CG  PHE A 217      30.084  12.621  13.510  1.00 46.98           C  
ATOM   1615  CD1 PHE A 217      30.953  12.363  12.457  1.00 48.83           C  
ATOM   1616  CD2 PHE A 217      29.674  13.925  13.729  1.00 47.79           C  
ATOM   1617  CE1 PHE A 217      31.402  13.392  11.637  1.00 49.52           C  
ATOM   1618  CE2 PHE A 217      30.118  14.959  12.914  1.00 48.32           C  
ATOM   1619  CZ  PHE A 217      30.982  14.693  11.866  1.00 47.24           C  
ATOM   1620  N   GLU A 218      31.268   9.842  16.926  1.00 49.98           N  
ATOM   1621  CA  GLU A 218      31.121   9.293  18.266  1.00 49.74           C  
ATOM   1622  C   GLU A 218      30.883  10.448  19.237  1.00 47.79           C  
ATOM   1623  O   GLU A 218      31.790  11.237  19.506  1.00 44.90           O  
ATOM   1624  CB  GLU A 218      32.389   8.532  18.672  1.00 51.68           C  
ATOM   1625  CG  GLU A 218      32.350   7.962  20.096  1.00 55.93           C  
ATOM   1626  CD  GLU A 218      33.678   7.368  20.557  1.00 56.65           C  
ATOM   1627  OE1 GLU A 218      34.706   7.544  19.864  1.00 58.14           O  
ATOM   1628  OE2 GLU A 218      33.692   6.729  21.630  1.00 55.66           O  
ATOM   1629  N   VAL A 219      29.651  10.581  19.715  1.00 47.54           N  
ATOM   1630  CA  VAL A 219      29.322  11.638  20.666  1.00 47.22           C  
ATOM   1631  C   VAL A 219      29.996  11.316  21.994  1.00 46.58           C  
ATOM   1632  O   VAL A 219      29.611  10.373  22.686  1.00 48.06           O  
ATOM   1633  CB  VAL A 219      27.801  11.757  20.897  1.00 47.08           C  
ATOM   1634  CG1 VAL A 219      27.510  12.822  21.947  1.00 45.97           C  
ATOM   1635  CG2 VAL A 219      27.096  12.091  19.590  1.00 48.44           C  
ATOM   1636  N   LYS A 220      31.026  12.084  22.326  1.00 45.25           N  
ATOM   1637  CA  LYS A 220      31.755  11.879  23.561  1.00 43.10           C  
ATOM   1638  C   LYS A 220      31.004  12.433  24.776  1.00 43.16           C  
ATOM   1639  O   LYS A 220      31.069  11.851  25.862  1.00 43.28           O  
ATOM   1640  CB  LYS A 220      33.156  12.472  23.448  1.00 43.56           C  
ATOM   1641  CG  LYS A 220      34.165  11.817  24.367  1.00 47.27           C  
ATOM   1642  CD  LYS A 220      34.111  10.296  24.266  1.00 49.89           C  
ATOM   1643  CE  LYS A 220      34.657   9.777  22.943  1.00 50.00           C  
ATOM   1644  NZ  LYS A 220      36.143   9.875  22.863  1.00 48.72           N  
ATOM   1645  N   SER A 221      30.280  13.537  24.596  1.00 40.27           N  
ATOM   1646  CA  SER A 221      29.502  14.128  25.689  1.00 37.28           C  
ATOM   1647  C   SER A 221      28.581  15.244  25.221  1.00 35.44           C  
ATOM   1648  O   SER A 221      28.677  15.716  24.087  1.00 35.81           O  
ATOM   1649  CB  SER A 221      30.418  14.651  26.802  1.00 33.47           C  
ATOM   1650  OG  SER A 221      31.283  15.659  26.322  1.00 32.19           O  
ATOM   1651  N   THR A 222      27.672  15.646  26.100  1.00 34.44           N  
ATOM   1652  CA  THR A 222      26.717  16.708  25.812  1.00 32.49           C  
ATOM   1653  C   THR A 222      26.381  17.459  27.099  1.00 30.88           C  
ATOM   1654  O   THR A 222      26.486  16.903  28.202  1.00 31.15           O  
ATOM   1655  CB  THR A 222      25.419  16.142  25.193  1.00 32.62           C  
ATOM   1656  OG1 THR A 222      25.139  14.853  25.758  1.00 37.68           O  
ATOM   1657  CG2 THR A 222      25.548  16.016  23.685  1.00 31.42           C  
ATOM   1658  N   ALA A 223      26.014  18.730  26.954  1.00 26.54           N  
ATOM   1659  CA  ALA A 223      25.655  19.582  28.084  1.00 23.75           C  
ATOM   1660  C   ALA A 223      24.972  20.838  27.551  1.00 20.88           C  
ATOM   1661  O   ALA A 223      25.008  21.103  26.350  1.00 23.66           O  
ATOM   1662  CB  ALA A 223      26.908  19.957  28.884  1.00 22.68           C  
ATOM   1663  N   GLY A 224      24.323  21.596  28.425  1.00 18.50           N  
ATOM   1664  CA  GLY A 224      23.669  22.807  27.974  1.00 18.01           C  
ATOM   1665  C   GLY A 224      22.575  23.310  28.890  1.00 19.92           C  
ATOM   1666  O   GLY A 224      22.441  22.858  30.034  1.00 20.12           O  
ATOM   1667  N   ASP A 225      21.793  24.252  28.376  1.00 17.25           N  
ATOM   1668  CA  ASP A 225      20.701  24.855  29.116  1.00 16.44           C  
ATOM   1669  C   ASP A 225      19.585  25.110  28.110  1.00 16.71           C  
ATOM   1670  O   ASP A 225      19.687  25.996  27.256  1.00 12.59           O  
ATOM   1671  CB  ASP A 225      21.170  26.170  29.754  1.00 17.62           C  
ATOM   1672  CG  ASP A 225      20.129  26.791  30.685  1.00 20.82           C  
ATOM   1673  OD1 ASP A 225      18.938  26.424  30.623  1.00 20.83           O  
ATOM   1674  OD2 ASP A 225      20.507  27.673  31.482  1.00 24.32           O  
ATOM   1675  N   THR A 226      18.514  24.332  28.234  1.00 17.94           N  
ATOM   1676  CA  THR A 226      17.356  24.435  27.348  1.00 18.82           C  
ATOM   1677  C   THR A 226      16.645  25.773  27.452  1.00 16.90           C  
ATOM   1678  O   THR A 226      15.753  26.077  26.657  1.00 14.78           O  
ATOM   1679  CB  THR A 226      16.329  23.317  27.634  1.00 20.99           C  
ATOM   1680  OG1 THR A 226      15.937  23.357  29.015  1.00 24.65           O  
ATOM   1681  CG2 THR A 226      16.918  21.957  27.312  1.00 24.76           C  
ATOM   1682  N   HIS A 227      17.019  26.561  28.452  1.00 14.55           N  
ATOM   1683  CA  HIS A 227      16.401  27.858  28.652  1.00 15.27           C  
ATOM   1684  C   HIS A 227      17.373  29.029  28.694  1.00 13.66           C  
ATOM   1685  O   HIS A 227      17.219  29.963  29.482  1.00 14.44           O  
ATOM   1686  CB  HIS A 227      15.474  27.818  29.870  1.00 17.14           C  
ATOM   1687  CG  HIS A 227      14.292  26.928  29.675  1.00 19.64           C  
ATOM   1688  ND1 HIS A 227      13.155  27.329  28.999  1.00 22.10           N  
ATOM   1689  CD2 HIS A 227      14.085  25.624  30.001  1.00 19.72           C  
ATOM   1690  CE1 HIS A 227      12.310  26.321  28.916  1.00 17.48           C  
ATOM   1691  NE2 HIS A 227      12.850  25.279  29.514  1.00 21.24           N  
ATOM   1692  N   LEU A 228      18.368  28.975  27.818  1.00 12.27           N  
ATOM   1693  CA  LEU A 228      19.349  30.041  27.703  1.00 12.41           C  
ATOM   1694  C   LEU A 228      19.517  30.297  26.215  1.00 11.44           C  
ATOM   1695  O   LEU A 228      19.877  29.391  25.472  1.00 13.89           O  
ATOM   1696  CB  LEU A 228      20.696  29.635  28.306  1.00 14.07           C  
ATOM   1697  CG  LEU A 228      21.804  30.685  28.147  1.00 13.21           C  
ATOM   1698  CD1 LEU A 228      21.481  31.923  28.977  1.00 12.96           C  
ATOM   1699  CD2 LEU A 228      23.150  30.101  28.555  1.00 15.13           C  
ATOM   1700  N   GLY A 229      19.261  31.527  25.790  1.00  9.22           N  
ATOM   1701  CA  GLY A 229      19.389  31.863  24.390  1.00 10.61           C  
ATOM   1702  C   GLY A 229      19.318  33.360  24.187  1.00  9.52           C  
ATOM   1703  O   GLY A 229      19.183  34.122  25.150  1.00  8.28           O  
ATOM   1704  N   GLY A 230      19.373  33.777  22.928  1.00  9.10           N  
ATOM   1705  CA  GLY A 230      19.324  35.188  22.596  1.00 10.41           C  
ATOM   1706  C   GLY A 230      18.148  35.949  23.178  1.00  9.91           C  
ATOM   1707  O   GLY A 230      18.277  37.118  23.530  1.00  7.75           O  
ATOM   1708  N   GLU A 231      17.004  35.289  23.297  1.00 12.94           N  
ATOM   1709  CA  GLU A 231      15.817  35.927  23.846  1.00 16.40           C  
ATOM   1710  C   GLU A 231      16.022  36.397  25.278  1.00 14.58           C  
ATOM   1711  O   GLU A 231      15.419  37.374  25.709  1.00 13.36           O  
ATOM   1712  CB  GLU A 231      14.615  34.995  23.727  1.00 22.15           C  
ATOM   1713  CG  GLU A 231      14.261  34.714  22.272  1.00 35.42           C  
ATOM   1714  CD  GLU A 231      12.899  34.082  22.091  1.00 40.83           C  
ATOM   1715  OE1 GLU A 231      12.503  33.252  22.937  1.00 43.71           O  
ATOM   1716  OE2 GLU A 231      12.231  34.417  21.088  1.00 44.91           O  
ATOM   1717  N   ASP A 232      16.922  35.739  25.994  1.00 12.40           N  
ATOM   1718  CA  ASP A 232      17.216  36.131  27.363  1.00 13.36           C  
ATOM   1719  C   ASP A 232      18.045  37.404  27.374  1.00 11.44           C  
ATOM   1720  O   ASP A 232      17.906  38.231  28.274  1.00  9.29           O  
ATOM   1721  CB  ASP A 232      17.929  35.001  28.093  1.00 14.58           C  
ATOM   1722  CG  ASP A 232      17.084  33.753  28.168  1.00 17.05           C  
ATOM   1723  OD1 ASP A 232      16.002  33.811  28.790  1.00 20.39           O  
ATOM   1724  OD2 ASP A 232      17.474  32.729  27.577  1.00 17.61           O  
ATOM   1725  N   PHE A 233      18.859  37.582  26.335  1.00 12.24           N  
ATOM   1726  CA  PHE A 233      19.700  38.774  26.219  1.00 11.23           C  
ATOM   1727  C   PHE A 233      18.817  39.957  25.832  1.00 12.60           C  
ATOM   1728  O   PHE A 233      19.006  41.065  26.337  1.00 13.24           O  
ATOM   1729  CB  PHE A 233      20.832  38.569  25.195  1.00  8.64           C  
ATOM   1730  CG  PHE A 233      21.633  37.308  25.423  1.00  9.58           C  
ATOM   1731  CD1 PHE A 233      21.831  36.805  26.714  1.00  8.38           C  
ATOM   1732  CD2 PHE A 233      22.153  36.595  24.346  1.00  9.42           C  
ATOM   1733  CE1 PHE A 233      22.524  35.615  26.917  1.00 11.19           C  
ATOM   1734  CE2 PHE A 233      22.848  35.402  24.539  1.00  8.91           C  
ATOM   1735  CZ  PHE A 233      23.035  34.911  25.827  1.00 10.75           C  
ATOM   1736  N   ASP A 234      17.833  39.716  24.960  1.00 12.84           N  
ATOM   1737  CA  ASP A 234      16.905  40.777  24.545  1.00 11.87           C  
ATOM   1738  C   ASP A 234      16.188  41.259  25.797  1.00  8.43           C  
ATOM   1739  O   ASP A 234      16.008  42.447  25.995  1.00 12.51           O  
ATOM   1740  CB  ASP A 234      15.866  40.258  23.558  1.00  8.02           C  
ATOM   1741  CG  ASP A 234      16.484  39.648  22.320  1.00 11.98           C  
ATOM   1742  OD1 ASP A 234      17.536  40.131  21.863  1.00 12.83           O  
ATOM   1743  OD2 ASP A 234      15.904  38.684  21.805  1.00 15.60           O  
ATOM   1744  N   ASN A 235      15.802  40.308  26.638  1.00 12.03           N  
ATOM   1745  CA  ASN A 235      15.120  40.591  27.893  1.00 18.17           C  
ATOM   1746  C   ASN A 235      15.856  41.556  28.815  1.00 15.84           C  
ATOM   1747  O   ASN A 235      15.255  42.473  29.381  1.00 15.53           O  
ATOM   1748  CB  ASN A 235      14.892  39.311  28.655  1.00 23.83           C  
ATOM   1749  CG  ASN A 235      13.525  38.757  28.440  1.00 35.15           C  
ATOM   1750  OD1 ASN A 235      13.257  38.077  27.465  1.00 41.36           O  
ATOM   1751  ND2 ASN A 235      12.654  38.999  29.422  1.00 40.28           N  
ATOM   1752  N   ARG A 236      17.141  41.298  29.022  1.00 14.16           N  
ATOM   1753  CA  ARG A 236      17.940  42.151  29.883  1.00 13.93           C  
ATOM   1754  C   ARG A 236      17.918  43.571  29.346  1.00 12.88           C  
ATOM   1755  O   ARG A 236      17.891  44.537  30.109  1.00 13.85           O  
ATOM   1756  CB  ARG A 236      19.377  41.645  29.981  1.00 12.69           C  
ATOM   1757  CG  ARG A 236      19.509  40.295  30.668  1.00 12.19           C  
ATOM   1758  CD  ARG A 236      19.099  40.376  32.128  1.00 12.34           C  
ATOM   1759  NE  ARG A 236      19.311  39.117  32.843  1.00 11.56           N  
ATOM   1760  CZ  ARG A 236      20.470  38.741  33.375  1.00 12.52           C  
ATOM   1761  NH1 ARG A 236      21.546  39.506  33.247  1.00 11.57           N  
ATOM   1762  NH2 ARG A 236      20.561  37.583  34.018  1.00 13.64           N  
ATOM   1763  N   MET A 237      17.913  43.694  28.024  1.00 12.22           N  
ATOM   1764  CA  MET A 237      17.884  44.995  27.379  1.00 12.55           C  
ATOM   1765  C   MET A 237      16.513  45.640  27.557  1.00 11.98           C  
ATOM   1766  O   MET A 237      16.413  46.853  27.779  1.00 12.64           O  
ATOM   1767  CB  MET A 237      18.182  44.859  25.897  1.00 16.48           C  
ATOM   1768  CG  MET A 237      19.507  44.218  25.561  1.00 16.42           C  
ATOM   1769  SD  MET A 237      19.605  44.025  23.776  1.00 21.96           S  
ATOM   1770  CE  MET A 237      19.545  45.815  23.245  1.00  9.88           C  
ATOM   1771  N   VAL A 238      15.459  44.833  27.453  1.00 13.85           N  
ATOM   1772  CA  VAL A 238      14.083  45.321  27.606  1.00 14.83           C  
ATOM   1773  C   VAL A 238      13.895  45.968  28.976  1.00 15.97           C  
ATOM   1774  O   VAL A 238      13.422  47.103  29.079  1.00 16.08           O  
ATOM   1775  CB  VAL A 238      13.040  44.176  27.439  1.00 14.69           C  
ATOM   1776  CG1 VAL A 238      11.642  44.676  27.795  1.00 12.88           C  
ATOM   1777  CG2 VAL A 238      13.050  43.645  26.014  1.00 14.64           C  
ATOM   1778  N   ASN A 239      14.296  45.255  30.024  1.00 15.73           N  
ATOM   1779  CA  ASN A 239      14.155  45.760  31.390  1.00 17.31           C  
ATOM   1780  C   ASN A 239      14.970  47.019  31.595  1.00 15.80           C  
ATOM   1781  O   ASN A 239      14.529  47.947  32.271  1.00 17.62           O  
ATOM   1782  CB  ASN A 239      14.556  44.692  32.407  1.00 19.66           C  
ATOM   1783  CG  ASN A 239      13.628  43.492  32.385  1.00 19.38           C  
ATOM   1784  OD1 ASN A 239      14.049  42.364  32.643  1.00 23.52           O  
ATOM   1785  ND2 ASN A 239      12.360  43.727  32.082  1.00 16.56           N  
ATOM   1786  N   HIS A 240      16.142  47.059  30.977  1.00 14.49           N  
ATOM   1787  CA  HIS A 240      17.020  48.217  31.061  1.00 17.10           C  
ATOM   1788  C   HIS A 240      16.332  49.442  30.456  1.00 18.73           C  
ATOM   1789  O   HIS A 240      16.387  50.545  31.008  1.00 19.66           O  
ATOM   1790  CB  HIS A 240      18.317  47.926  30.309  1.00 14.17           C  
ATOM   1791  CG  HIS A 240      19.243  49.095  30.210  1.00 14.80           C  
ATOM   1792  ND1 HIS A 240      19.979  49.552  31.279  1.00 16.87           N  
ATOM   1793  CD2 HIS A 240      19.596  49.864  29.153  1.00 15.31           C  
ATOM   1794  CE1 HIS A 240      20.751  50.551  30.887  1.00 13.98           C  
ATOM   1795  NE2 HIS A 240      20.537  50.759  29.602  1.00 17.30           N  
ATOM   1796  N   PHE A 241      15.681  49.248  29.316  1.00 20.30           N  
ATOM   1797  CA  PHE A 241      14.998  50.347  28.655  1.00 16.54           C  
ATOM   1798  C   PHE A 241      13.659  50.708  29.271  1.00 14.56           C  
ATOM   1799  O   PHE A 241      13.199  51.838  29.133  1.00 17.03           O  
ATOM   1800  CB  PHE A 241      14.917  50.101  27.152  1.00 16.02           C  
ATOM   1801  CG  PHE A 241      16.226  50.313  26.456  1.00 16.16           C  
ATOM   1802  CD1 PHE A 241      16.879  51.537  26.554  1.00 14.82           C  
ATOM   1803  CD2 PHE A 241      16.828  49.287  25.740  1.00 18.37           C  
ATOM   1804  CE1 PHE A 241      18.112  51.736  25.955  1.00 15.95           C  
ATOM   1805  CE2 PHE A 241      18.064  49.479  25.135  1.00 17.27           C  
ATOM   1806  CZ  PHE A 241      18.704  50.705  25.242  1.00 15.36           C  
ATOM   1807  N   ILE A 242      13.026  49.762  29.954  1.00 16.20           N  
ATOM   1808  CA  ILE A 242      11.775  50.069  30.632  1.00 18.58           C  
ATOM   1809  C   ILE A 242      12.154  51.062  31.742  1.00 19.62           C  
ATOM   1810  O   ILE A 242      11.467  52.065  31.959  1.00 20.78           O  
ATOM   1811  CB  ILE A 242      11.114  48.804  31.227  1.00 19.27           C  
ATOM   1812  CG1 ILE A 242      10.497  47.965  30.106  1.00 17.52           C  
ATOM   1813  CG2 ILE A 242      10.036  49.191  32.241  1.00 20.02           C  
ATOM   1814  CD1 ILE A 242       9.912  46.646  30.571  1.00 15.70           C  
ATOM   1815  N   ALA A 243      13.289  50.810  32.393  1.00 22.97           N  
ATOM   1816  CA  ALA A 243      13.790  51.687  33.456  1.00 22.57           C  
ATOM   1817  C   ALA A 243      14.128  53.074  32.904  1.00 22.58           C  
ATOM   1818  O   ALA A 243      13.813  54.092  33.522  1.00 22.86           O  
ATOM   1819  CB  ALA A 243      15.022  51.071  34.119  1.00 20.95           C  
ATOM   1820  N   GLU A 244      14.746  53.109  31.727  1.00 22.29           N  
ATOM   1821  CA  GLU A 244      15.125  54.368  31.089  1.00 23.14           C  
ATOM   1822  C   GLU A 244      13.920  55.232  30.711  1.00 23.27           C  
ATOM   1823  O   GLU A 244      13.915  56.446  30.939  1.00 24.82           O  
ATOM   1824  CB  GLU A 244      15.973  54.094  29.853  1.00 20.86           C  
ATOM   1825  CG  GLU A 244      16.605  55.334  29.271  1.00 19.44           C  
ATOM   1826  CD  GLU A 244      17.443  55.035  28.052  1.00 21.38           C  
ATOM   1827  OE1 GLU A 244      18.361  54.195  28.147  1.00 25.11           O  
ATOM   1828  OE2 GLU A 244      17.180  55.637  26.995  1.00 23.77           O  
ATOM   1829  N   PHE A 245      12.905  54.602  30.127  1.00 23.75           N  
ATOM   1830  CA  PHE A 245      11.688  55.296  29.724  1.00 22.64           C  
ATOM   1831  C   PHE A 245      10.998  55.863  30.969  1.00 24.98           C  
ATOM   1832  O   PHE A 245      10.539  57.008  30.975  1.00 24.50           O  
ATOM   1833  CB  PHE A 245      10.751  54.325  29.001  1.00 20.97           C  
ATOM   1834  CG  PHE A 245       9.595  54.996  28.309  1.00 26.88           C  
ATOM   1835  CD1 PHE A 245       8.395  55.223  28.986  1.00 26.37           C  
ATOM   1836  CD2 PHE A 245       9.709  55.418  26.984  1.00 28.33           C  
ATOM   1837  CE1 PHE A 245       7.329  55.865  28.356  1.00 28.89           C  
ATOM   1838  CE2 PHE A 245       8.649  56.062  26.341  1.00 28.17           C  
ATOM   1839  CZ  PHE A 245       7.456  56.286  27.030  1.00 29.70           C  
ATOM   1840  N   LYS A 246      10.946  55.051  32.021  1.00 26.68           N  
ATOM   1841  CA  LYS A 246      10.328  55.425  33.289  1.00 27.10           C  
ATOM   1842  C   LYS A 246      11.027  56.623  33.916  1.00 26.68           C  
ATOM   1843  O   LYS A 246      10.378  57.486  34.504  1.00 25.53           O  
ATOM   1844  CB  LYS A 246      10.355  54.236  34.246  1.00 28.68           C  
ATOM   1845  CG  LYS A 246       9.574  54.421  35.526  1.00 31.90           C  
ATOM   1846  CD  LYS A 246       9.554  53.110  36.291  1.00 35.79           C  
ATOM   1847  CE  LYS A 246       8.758  53.205  37.579  1.00 37.21           C  
ATOM   1848  NZ  LYS A 246       8.611  51.847  38.180  1.00 38.17           N  
ATOM   1849  N   ARG A 247      12.350  56.671  33.798  1.00 28.23           N  
ATOM   1850  CA  ARG A 247      13.120  57.783  34.339  1.00 31.14           C  
ATOM   1851  C   ARG A 247      12.824  59.074  33.591  1.00 32.73           C  
ATOM   1852  O   ARG A 247      12.459  60.085  34.192  1.00 33.87           O  
ATOM   1853  CB  ARG A 247      14.619  57.521  34.236  1.00 31.76           C  
ATOM   1854  CG  ARG A 247      15.218  56.751  35.381  1.00 33.62           C  
ATOM   1855  CD  ARG A 247      16.730  56.923  35.383  1.00 36.35           C  
ATOM   1856  NE  ARG A 247      17.342  56.579  34.098  1.00 37.21           N  
ATOM   1857  CZ  ARG A 247      17.448  55.339  33.621  1.00 35.44           C  
ATOM   1858  NH1 ARG A 247      16.980  54.310  34.316  1.00 29.99           N  
ATOM   1859  NH2 ARG A 247      18.033  55.131  32.450  1.00 38.86           N  
ATOM   1860  N   LYS A 248      12.990  59.026  32.274  1.00 32.05           N  
ATOM   1861  CA  LYS A 248      12.785  60.189  31.425  1.00 32.22           C  
ATOM   1862  C   LYS A 248      11.338  60.632  31.260  1.00 31.52           C  
ATOM   1863  O   LYS A 248      11.067  61.809  31.045  1.00 33.93           O  
ATOM   1864  CB  LYS A 248      13.414  59.946  30.052  1.00 32.36           C  
ATOM   1865  N   HIS A 249      10.401  59.702  31.357  1.00 30.77           N  
ATOM   1866  CA  HIS A 249       9.007  60.061  31.154  1.00 30.16           C  
ATOM   1867  C   HIS A 249       8.081  59.812  32.332  1.00 29.71           C  
ATOM   1868  O   HIS A 249       6.892  60.108  32.256  1.00 29.79           O  
ATOM   1869  CB  HIS A 249       8.486  59.352  29.901  1.00 29.79           C  
ATOM   1870  CG  HIS A 249       9.309  59.622  28.676  1.00 27.23           C  
ATOM   1871  ND1 HIS A 249       9.482  60.887  28.160  1.00 27.37           N  
ATOM   1872  CD2 HIS A 249      10.014  58.789  27.873  1.00 26.32           C  
ATOM   1873  CE1 HIS A 249      10.257  60.825  27.090  1.00 24.25           C  
ATOM   1874  NE2 HIS A 249      10.592  59.563  26.896  1.00 26.03           N  
ATOM   1875  N   LYS A 250       8.631  59.293  33.425  1.00 31.25           N  
ATOM   1876  CA  LYS A 250       7.853  58.993  34.623  1.00 31.37           C  
ATOM   1877  C   LYS A 250       6.656  58.084  34.305  1.00 31.63           C  
ATOM   1878  O   LYS A 250       5.615  58.154  34.966  1.00 32.08           O  
ATOM   1879  CB  LYS A 250       7.400  60.288  35.312  1.00 33.65           C  
ATOM   1880  N   LYS A 251       6.825  57.223  33.303  1.00 29.39           N  
ATOM   1881  CA  LYS A 251       5.791  56.279  32.891  1.00 26.77           C  
ATOM   1882  C   LYS A 251       6.371  54.871  32.805  1.00 25.10           C  
ATOM   1883  O   LYS A 251       7.482  54.679  32.308  1.00 25.11           O  
ATOM   1884  CB  LYS A 251       5.200  56.671  31.534  1.00 29.50           C  
ATOM   1885  CG  LYS A 251       4.378  57.938  31.562  1.00 31.55           C  
ATOM   1886  CD  LYS A 251       3.793  58.237  30.199  1.00 36.54           C  
ATOM   1887  CE  LYS A 251       3.058  59.571  30.193  1.00 39.38           C  
ATOM   1888  NZ  LYS A 251       1.864  59.583  31.088  1.00 41.16           N  
ATOM   1889  N   ASP A 252       5.605  53.893  33.274  1.00 22.02           N  
ATOM   1890  CA  ASP A 252       6.017  52.499  33.267  1.00 22.42           C  
ATOM   1891  C   ASP A 252       5.239  51.763  32.181  1.00 21.49           C  
ATOM   1892  O   ASP A 252       4.026  51.586  32.297  1.00 23.52           O  
ATOM   1893  CB  ASP A 252       5.732  51.878  34.639  1.00 26.52           C  
ATOM   1894  CG  ASP A 252       6.180  50.432  34.735  1.00 31.08           C  
ATOM   1895  OD1 ASP A 252       7.345  50.147  34.387  1.00 38.95           O  
ATOM   1896  OD2 ASP A 252       5.370  49.581  35.159  1.00 32.41           O  
ATOM   1897  N   ILE A 253       5.930  51.313  31.141  1.00 19.90           N  
ATOM   1898  CA  ILE A 253       5.268  50.613  30.033  1.00 18.65           C  
ATOM   1899  C   ILE A 253       5.081  49.111  30.249  1.00 19.76           C  
ATOM   1900  O   ILE A 253       4.437  48.443  29.443  1.00 20.33           O  
ATOM   1901  CB  ILE A 253       6.032  50.811  28.694  1.00 16.89           C  
ATOM   1902  CG1 ILE A 253       7.320  49.979  28.682  1.00 15.50           C  
ATOM   1903  CG2 ILE A 253       6.366  52.282  28.491  1.00 14.44           C  
ATOM   1904  CD1 ILE A 253       8.051  49.984  27.348  1.00 14.86           C  
ATOM   1905  N   SER A 254       5.623  48.593  31.345  1.00 19.87           N  
ATOM   1906  CA  SER A 254       5.571  47.168  31.656  1.00 19.99           C  
ATOM   1907  C   SER A 254       4.248  46.448  31.447  1.00 21.91           C  
ATOM   1908  O   SER A 254       4.230  45.281  31.057  1.00 20.36           O  
ATOM   1909  CB  SER A 254       6.025  46.936  33.092  1.00 21.03           C  
ATOM   1910  OG  SER A 254       7.275  47.557  33.319  1.00 29.48           O  
ATOM   1911  N   GLU A 255       3.141  47.128  31.711  1.00 22.90           N  
ATOM   1912  CA  GLU A 255       1.847  46.488  31.588  1.00 24.49           C  
ATOM   1913  C   GLU A 255       1.196  46.610  30.233  1.00 23.43           C  
ATOM   1914  O   GLU A 255       0.081  46.135  30.027  1.00 24.20           O  
ATOM   1915  CB  GLU A 255       0.914  46.963  32.692  1.00 27.53           C  
ATOM   1916  CG  GLU A 255       1.448  46.652  34.083  1.00 29.84           C  
ATOM   1917  CD  GLU A 255       1.835  45.191  34.251  1.00 34.09           C  
ATOM   1918  OE1 GLU A 255       1.083  44.306  33.786  1.00 32.93           O  
ATOM   1919  OE2 GLU A 255       2.898  44.928  34.854  1.00 39.06           O  
ATOM   1920  N   ASN A 256       1.881  47.262  29.310  1.00 23.57           N  
ATOM   1921  CA  ASN A 256       1.354  47.391  27.972  1.00 24.03           C  
ATOM   1922  C   ASN A 256       2.038  46.325  27.126  1.00 24.55           C  
ATOM   1923  O   ASN A 256       3.134  46.543  26.603  1.00 26.17           O  
ATOM   1924  CB  ASN A 256       1.624  48.774  27.413  1.00 27.35           C  
ATOM   1925  CG  ASN A 256       0.682  49.119  26.301  1.00 35.11           C  
ATOM   1926  OD1 ASN A 256       1.023  48.969  25.126  1.00 33.74           O  
ATOM   1927  ND2 ASN A 256      -0.544  49.497  26.655  1.00 40.60           N  
ATOM   1928  N   LYS A 257       1.399  45.161  27.031  1.00 23.82           N  
ATOM   1929  CA  LYS A 257       1.922  44.025  26.279  1.00 24.21           C  
ATOM   1930  C   LYS A 257       2.487  44.382  24.916  1.00 24.18           C  
ATOM   1931  O   LYS A 257       3.565  43.917  24.548  1.00 26.09           O  
ATOM   1932  CB  LYS A 257       0.848  42.945  26.110  1.00 23.57           C  
ATOM   1933  CG  LYS A 257       0.564  42.154  27.367  1.00 26.74           C  
ATOM   1934  CD  LYS A 257      -0.455  41.073  27.101  1.00 30.98           C  
ATOM   1935  CE  LYS A 257      -0.579  40.125  28.280  1.00 35.23           C  
ATOM   1936  NZ  LYS A 257      -1.047  40.806  29.510  1.00 39.69           N  
ATOM   1937  N   ARG A 258       1.769  45.204  24.165  1.00 23.68           N  
ATOM   1938  CA  ARG A 258       2.244  45.582  22.851  1.00 25.66           C  
ATOM   1939  C   ARG A 258       3.503  46.436  22.913  1.00 25.48           C  
ATOM   1940  O   ARG A 258       4.461  46.173  22.183  1.00 27.26           O  
ATOM   1941  CB  ARG A 258       1.150  46.279  22.048  1.00 28.82           C  
ATOM   1942  CG  ARG A 258       1.599  46.632  20.649  1.00 28.99           C  
ATOM   1943  CD  ARG A 258       0.436  46.899  19.720  1.00 27.70           C  
ATOM   1944  NE  ARG A 258       0.905  47.471  18.463  1.00 23.73           N  
ATOM   1945  CZ  ARG A 258       1.179  48.759  18.290  1.00 17.40           C  
ATOM   1946  NH1 ARG A 258       1.021  49.612  19.288  1.00 19.44           N  
ATOM   1947  NH2 ARG A 258       1.624  49.190  17.118  1.00 20.88           N  
ATOM   1948  N   ALA A 259       3.518  47.440  23.789  1.00 21.97           N  
ATOM   1949  CA  ALA A 259       4.685  48.311  23.930  1.00 19.73           C  
ATOM   1950  C   ALA A 259       5.938  47.494  24.252  1.00 20.26           C  
ATOM   1951  O   ALA A 259       7.013  47.728  23.685  1.00 18.83           O  
ATOM   1952  CB  ALA A 259       4.446  49.347  25.014  1.00 16.90           C  
ATOM   1953  N   VAL A 260       5.782  46.520  25.145  1.00 20.12           N  
ATOM   1954  CA  VAL A 260       6.875  45.644  25.558  1.00 20.72           C  
ATOM   1955  C   VAL A 260       7.399  44.789  24.397  1.00 22.19           C  
ATOM   1956  O   VAL A 260       8.612  44.641  24.229  1.00 17.28           O  
ATOM   1957  CB  VAL A 260       6.443  44.739  26.738  1.00 17.35           C  
ATOM   1958  CG1 VAL A 260       7.508  43.691  27.036  1.00 19.11           C  
ATOM   1959  CG2 VAL A 260       6.184  45.594  27.973  1.00 17.95           C  
ATOM   1960  N   ARG A 261       6.488  44.237  23.598  1.00 21.15           N  
ATOM   1961  CA  ARG A 261       6.883  43.415  22.461  1.00 22.94           C  
ATOM   1962  C   ARG A 261       7.572  44.261  21.391  1.00 20.87           C  
ATOM   1963  O   ARG A 261       8.509  43.807  20.740  1.00 20.69           O  
ATOM   1964  CB  ARG A 261       5.678  42.682  21.866  1.00 25.55           C  
ATOM   1965  CG  ARG A 261       6.076  41.507  20.979  1.00 25.63           C  
ATOM   1966  CD  ARG A 261       6.819  40.465  21.796  1.00 26.21           C  
ATOM   1967  NE  ARG A 261       7.476  39.462  20.968  1.00 30.73           N  
ATOM   1968  CZ  ARG A 261       8.570  39.685  20.245  1.00 33.19           C  
ATOM   1969  NH1 ARG A 261       9.139  40.885  20.234  1.00 32.57           N  
ATOM   1970  NH2 ARG A 261       9.115  38.694  19.552  1.00 34.78           N  
ATOM   1971  N   ARG A 262       7.112  45.493  21.215  1.00 19.31           N  
ATOM   1972  CA  ARG A 262       7.718  46.395  20.242  1.00 20.59           C  
ATOM   1973  C   ARG A 262       9.126  46.778  20.694  1.00 21.52           C  
ATOM   1974  O   ARG A 262      10.047  46.860  19.879  1.00 20.43           O  
ATOM   1975  CB  ARG A 262       6.860  47.647  20.057  1.00 22.49           C  
ATOM   1976  CG  ARG A 262       5.477  47.353  19.490  1.00 24.86           C  
ATOM   1977  CD  ARG A 262       4.744  48.632  19.132  1.00 24.97           C  
ATOM   1978  NE  ARG A 262       5.420  49.350  18.059  1.00 24.76           N  
ATOM   1979  CZ  ARG A 262       5.542  50.672  17.993  1.00 22.31           C  
ATOM   1980  NH1 ARG A 262       5.044  51.445  18.949  1.00 25.36           N  
ATOM   1981  NH2 ARG A 262       6.176  51.221  16.969  1.00 22.08           N  
ATOM   1982  N   LEU A 263       9.282  47.037  21.991  1.00 20.57           N  
ATOM   1983  CA  LEU A 263      10.583  47.374  22.558  1.00 18.34           C  
ATOM   1984  C   LEU A 263      11.507  46.163  22.429  1.00 14.56           C  
ATOM   1985  O   LEU A 263      12.686  46.313  22.115  1.00 17.01           O  
ATOM   1986  CB  LEU A 263      10.442  47.767  24.034  1.00 17.13           C  
ATOM   1987  CG  LEU A 263      11.726  47.981  24.851  1.00 14.74           C  
ATOM   1988  CD1 LEU A 263      12.543  49.138  24.301  1.00 14.30           C  
ATOM   1989  CD2 LEU A 263      11.349  48.239  26.294  1.00 12.63           C  
ATOM   1990  N   ARG A 264      10.961  44.968  22.649  1.00 14.45           N  
ATOM   1991  CA  ARG A 264      11.731  43.721  22.557  1.00 19.11           C  
ATOM   1992  C   ARG A 264      12.314  43.543  21.146  1.00 21.03           C  
ATOM   1993  O   ARG A 264      13.492  43.224  20.988  1.00 20.36           O  
ATOM   1994  CB  ARG A 264      10.850  42.522  22.941  1.00 18.26           C  
ATOM   1995  CG  ARG A 264      11.602  41.215  23.206  1.00 23.60           C  
ATOM   1996  CD  ARG A 264      10.655  40.071  23.593  1.00 28.74           C  
ATOM   1997  NE  ARG A 264       9.954  40.244  24.869  1.00 34.52           N  
ATOM   1998  CZ  ARG A 264      10.501  40.058  26.062  1.00 38.62           C  
ATOM   1999  NH1 ARG A 264      11.754  39.605  26.187  1.00 38.36           N  
ATOM   2000  NH2 ARG A 264       9.796  40.270  27.172  1.00 39.95           N  
ATOM   2001  N   THR A 265      11.491  43.776  20.128  1.00 19.23           N  
ATOM   2002  CA  THR A 265      11.916  43.673  18.735  1.00 17.92           C  
ATOM   2003  C   THR A 265      13.059  44.666  18.471  1.00 16.46           C  
ATOM   2004  O   THR A 265      14.068  44.326  17.851  1.00 15.42           O  
ATOM   2005  CB  THR A 265      10.726  43.987  17.791  1.00 19.27           C  
ATOM   2006  OG1 THR A 265       9.661  43.064  18.048  1.00 20.56           O  
ATOM   2007  CG2 THR A 265      11.139  43.891  16.322  1.00 21.76           C  
ATOM   2008  N   ALA A 266      12.904  45.883  18.982  1.00 16.50           N  
ATOM   2009  CA  ALA A 266      13.901  46.933  18.813  1.00 15.82           C  
ATOM   2010  C   ALA A 266      15.227  46.543  19.475  1.00 18.09           C  
ATOM   2011  O   ALA A 266      16.306  46.848  18.960  1.00 13.39           O  
ATOM   2012  CB  ALA A 266      13.377  48.236  19.380  1.00 17.14           C  
ATOM   2013  N   CYS A 267      15.118  45.877  20.624  1.00 16.75           N  
ATOM   2014  CA  CYS A 267      16.289  45.393  21.352  1.00 16.45           C  
ATOM   2015  C   CYS A 267      16.983  44.239  20.616  1.00 14.76           C  
ATOM   2016  O   CYS A 267      18.204  44.231  20.544  1.00 16.85           O  
ATOM   2017  CB  CYS A 267      15.900  44.951  22.760  1.00 10.45           C  
ATOM   2018  SG  CYS A 267      15.539  46.309  23.867  1.00 14.25           S  
ATOM   2019  N   GLU A 268      16.212  43.286  20.100  1.00 15.03           N  
ATOM   2020  CA  GLU A 268      16.762  42.158  19.356  1.00 17.78           C  
ATOM   2021  C   GLU A 268      17.555  42.700  18.194  1.00 19.36           C  
ATOM   2022  O   GLU A 268      18.645  42.224  17.880  1.00 18.71           O  
ATOM   2023  CB  GLU A 268      15.644  41.317  18.763  1.00 22.46           C  
ATOM   2024  CG  GLU A 268      15.797  39.781  18.985  1.00 33.88           C  
ATOM   2025  CD  GLU A 268      14.956  38.972  17.967  1.00 39.25           C  
ATOM   2026  OE1 GLU A 268      13.842  39.422  17.674  1.00 43.19           O  
ATOM   2027  OE2 GLU A 268      15.379  37.896  17.492  1.00 40.90           O  
ATOM   2028  N   ARG A 269      16.995  43.704  17.533  1.00 20.97           N  
ATOM   2029  CA  ARG A 269      17.673  44.306  16.391  1.00 22.03           C  
ATOM   2030  C   ARG A 269      18.941  45.043  16.763  1.00 18.96           C  
ATOM   2031  O   ARG A 269      19.978  44.887  16.104  1.00 18.71           O  
ATOM   2032  CB  ARG A 269      16.739  45.248  15.642  1.00 28.16           C  
ATOM   2033  CG  ARG A 269      17.375  45.863  14.424  1.00 39.91           C  
ATOM   2034  CD  ARG A 269      16.303  46.406  13.524  1.00 51.67           C  
ATOM   2035  NE  ARG A 269      16.344  47.862  13.412  1.00 61.98           N  
ATOM   2036  CZ  ARG A 269      15.533  48.702  14.053  1.00 67.15           C  
ATOM   2037  NH1 ARG A 269      14.601  48.269  14.899  1.00 69.09           N  
ATOM   2038  NH2 ARG A 269      15.670  49.997  13.831  1.00 71.54           N  
ATOM   2039  N   ALA A 270      18.851  45.874  17.790  1.00 16.34           N  
ATOM   2040  CA  ALA A 270      20.005  46.627  18.270  1.00 14.98           C  
ATOM   2041  C   ALA A 270      21.120  45.648  18.648  1.00 13.88           C  
ATOM   2042  O   ALA A 270      22.298  45.890  18.364  1.00 15.40           O  
ATOM   2043  CB  ALA A 270      19.610  47.487  19.477  1.00 12.00           C  
ATOM   2044  N   LYS A 271      20.726  44.527  19.245  1.00 11.82           N  
ATOM   2045  CA  LYS A 271      21.645  43.477  19.673  1.00 12.85           C  
ATOM   2046  C   LYS A 271      22.500  42.942  18.522  1.00 14.64           C  
ATOM   2047  O   LYS A 271      23.705  42.755  18.679  1.00 12.42           O  
ATOM   2048  CB  LYS A 271      20.859  42.340  20.326  1.00 13.21           C  
ATOM   2049  CG  LYS A 271      21.693  41.139  20.726  1.00 11.07           C  
ATOM   2050  CD  LYS A 271      20.827  39.991  21.204  1.00 10.67           C  
ATOM   2051  CE  LYS A 271      20.038  39.373  20.071  1.00  7.37           C  
ATOM   2052  NZ  LYS A 271      19.255  38.206  20.567  1.00  6.19           N  
ATOM   2053  N   ARG A 272      21.879  42.665  17.377  1.00 15.79           N  
ATOM   2054  CA  ARG A 272      22.622  42.171  16.213  1.00 17.30           C  
ATOM   2055  C   ARG A 272      23.637  43.202  15.743  1.00 16.61           C  
ATOM   2056  O   ARG A 272      24.796  42.883  15.454  1.00 17.51           O  
ATOM   2057  CB  ARG A 272      21.680  41.846  15.067  1.00 23.08           C  
ATOM   2058  CG  ARG A 272      21.091  40.481  15.139  1.00 31.96           C  
ATOM   2059  CD  ARG A 272      19.615  40.568  15.267  1.00 41.59           C  
ATOM   2060  NE  ARG A 272      18.961  40.927  14.013  1.00 50.66           N  
ATOM   2061  CZ  ARG A 272      17.668  41.222  13.900  1.00 56.39           C  
ATOM   2062  NH1 ARG A 272      16.884  41.248  14.977  1.00 57.51           N  
ATOM   2063  NH2 ARG A 272      17.173  41.590  12.724  1.00 55.92           N  
ATOM   2064  N   THR A 273      23.188  44.447  15.674  1.00 14.93           N  
ATOM   2065  CA  THR A 273      24.037  45.540  15.254  1.00 15.25           C  
ATOM   2066  C   THR A 273      25.246  45.621  16.187  1.00 16.22           C  
ATOM   2067  O   THR A 273      26.369  45.808  15.729  1.00 18.41           O  
ATOM   2068  CB  THR A 273      23.243  46.854  15.239  1.00 16.91           C  
ATOM   2069  OG1 THR A 273      22.208  46.759  14.250  1.00 14.10           O  
ATOM   2070  CG2 THR A 273      24.142  48.029  14.908  1.00 18.07           C  
ATOM   2071  N   LEU A 274      25.029  45.376  17.477  1.00 14.22           N  
ATOM   2072  CA  LEU A 274      26.112  45.415  18.453  1.00 13.72           C  
ATOM   2073  C   LEU A 274      27.172  44.323  18.250  1.00 14.37           C  
ATOM   2074  O   LEU A 274      28.225  44.353  18.887  1.00 13.32           O  
ATOM   2075  CB  LEU A 274      25.564  45.379  19.884  1.00 11.14           C  
ATOM   2076  CG  LEU A 274      24.883  46.662  20.370  1.00 11.50           C  
ATOM   2077  CD1 LEU A 274      24.273  46.447  21.727  1.00 10.35           C  
ATOM   2078  CD2 LEU A 274      25.875  47.803  20.408  1.00 11.61           C  
ATOM   2079  N   SER A 275      26.900  43.354  17.381  1.00 13.69           N  
ATOM   2080  CA  SER A 275      27.873  42.301  17.111  1.00 15.20           C  
ATOM   2081  C   SER A 275      28.893  42.787  16.087  1.00 17.98           C  
ATOM   2082  O   SER A 275      29.952  42.182  15.922  1.00 16.44           O  
ATOM   2083  CB  SER A 275      27.193  41.022  16.608  1.00 15.27           C  
ATOM   2084  OG  SER A 275      26.461  40.384  17.643  1.00 11.88           O  
ATOM   2085  N   SER A 276      28.570  43.880  15.399  1.00 19.29           N  
ATOM   2086  CA  SER A 276      29.463  44.438  14.394  1.00 22.78           C  
ATOM   2087  C   SER A 276      29.812  45.904  14.635  1.00 24.24           C  
ATOM   2088  O   SER A 276      30.782  46.416  14.071  1.00 27.34           O  
ATOM   2089  CB  SER A 276      28.894  44.225  12.984  1.00 21.05           C  
ATOM   2090  OG  SER A 276      27.507  44.481  12.935  1.00 26.54           O  
ATOM   2091  N   SER A 277      29.036  46.572  15.484  1.00 25.16           N  
ATOM   2092  CA  SER A 277      29.277  47.973  15.823  1.00 25.04           C  
ATOM   2093  C   SER A 277      29.337  48.079  17.342  1.00 23.77           C  
ATOM   2094  O   SER A 277      28.755  47.258  18.052  1.00 21.09           O  
ATOM   2095  CB  SER A 277      28.152  48.872  15.294  1.00 27.30           C  
ATOM   2096  OG  SER A 277      28.022  48.782  13.883  1.00 30.58           O  
ATOM   2097  N   THR A 278      30.028  49.095  17.842  1.00 20.65           N  
ATOM   2098  CA  THR A 278      30.150  49.288  19.278  1.00 21.04           C  
ATOM   2099  C   THR A 278      28.982  50.091  19.856  1.00 20.25           C  
ATOM   2100  O   THR A 278      28.923  50.350  21.059  1.00 19.80           O  
ATOM   2101  CB  THR A 278      31.502  49.944  19.629  1.00 21.66           C  
ATOM   2102  OG1 THR A 278      31.731  51.065  18.763  1.00 23.52           O  
ATOM   2103  CG2 THR A 278      32.642  48.934  19.478  1.00 20.27           C  
ATOM   2104  N   GLN A 279      28.028  50.436  18.995  1.00 22.80           N  
ATOM   2105  CA  GLN A 279      26.853  51.202  19.399  1.00 25.80           C  
ATOM   2106  C   GLN A 279      25.681  50.918  18.473  1.00 24.18           C  
ATOM   2107  O   GLN A 279      25.870  50.561  17.307  1.00 22.09           O  
ATOM   2108  CB  GLN A 279      27.153  52.715  19.407  1.00 31.68           C  
ATOM   2109  CG  GLN A 279      27.664  53.299  18.075  1.00 42.94           C  
ATOM   2110  CD  GLN A 279      29.135  53.007  17.810  1.00 48.29           C  
ATOM   2111  OE1 GLN A 279      29.576  52.948  16.657  1.00 52.17           O  
ATOM   2112  NE2 GLN A 279      29.893  52.788  18.872  1.00 50.50           N  
ATOM   2113  N   ALA A 280      24.473  51.062  19.008  1.00 23.50           N  
ATOM   2114  CA  ALA A 280      23.250  50.840  18.245  1.00 23.02           C  
ATOM   2115  C   ALA A 280      22.196  51.849  18.687  1.00 20.13           C  
ATOM   2116  O   ALA A 280      22.142  52.227  19.854  1.00 18.64           O  
ATOM   2117  CB  ALA A 280      22.746  49.416  18.454  1.00 20.40           C  
ATOM   2118  N   SER A 281      21.400  52.329  17.737  1.00 22.75           N  
ATOM   2119  CA  SER A 281      20.341  53.283  18.035  1.00 24.39           C  
ATOM   2120  C   SER A 281      19.002  52.567  18.087  1.00 23.48           C  
ATOM   2121  O   SER A 281      18.791  51.574  17.391  1.00 26.75           O  
ATOM   2122  CB  SER A 281      20.284  54.382  16.971  1.00 26.39           C  
ATOM   2123  OG  SER A 281      21.434  55.208  17.034  1.00 34.20           O  
ATOM   2124  N   ILE A 282      18.111  53.062  18.934  1.00 23.72           N  
ATOM   2125  CA  ILE A 282      16.776  52.499  19.085  1.00 22.86           C  
ATOM   2126  C   ILE A 282      15.830  53.669  18.889  1.00 25.20           C  
ATOM   2127  O   ILE A 282      15.942  54.678  19.577  1.00 25.99           O  
ATOM   2128  CB  ILE A 282      16.587  51.883  20.492  1.00 21.55           C  
ATOM   2129  CG1 ILE A 282      17.271  50.514  20.549  1.00 21.16           C  
ATOM   2130  CG2 ILE A 282      15.108  51.795  20.859  1.00 17.02           C  
ATOM   2131  CD1 ILE A 282      17.107  49.797  21.861  1.00 22.89           C  
ATOM   2132  N   GLU A 283      14.946  53.571  17.906  1.00 27.70           N  
ATOM   2133  CA  GLU A 283      14.013  54.657  17.641  1.00 30.58           C  
ATOM   2134  C   GLU A 283      12.629  54.099  17.370  1.00 30.92           C  
ATOM   2135  O   GLU A 283      12.330  53.663  16.257  1.00 31.58           O  
ATOM   2136  CB  GLU A 283      14.500  55.493  16.456  1.00 35.86           C  
ATOM   2137  CG  GLU A 283      15.965  55.893  16.572  1.00 43.93           C  
ATOM   2138  CD  GLU A 283      16.357  57.039  15.667  1.00 50.18           C  
ATOM   2139  OE1 GLU A 283      15.781  57.164  14.561  1.00 54.02           O  
ATOM   2140  OE2 GLU A 283      17.247  57.821  16.071  1.00 51.97           O  
ATOM   2141  N   ILE A 284      11.803  54.069  18.410  1.00 29.44           N  
ATOM   2142  CA  ILE A 284      10.446  53.554  18.299  1.00 27.63           C  
ATOM   2143  C   ILE A 284       9.448  54.708  18.315  1.00 28.88           C  
ATOM   2144  O   ILE A 284       9.574  55.645  19.108  1.00 28.15           O  
ATOM   2145  CB  ILE A 284      10.119  52.589  19.462  1.00 26.31           C  
ATOM   2146  CG1 ILE A 284      11.265  51.593  19.656  1.00 21.96           C  
ATOM   2147  CG2 ILE A 284       8.816  51.835  19.182  1.00 21.19           C  
ATOM   2148  CD1 ILE A 284      11.100  50.706  20.866  1.00 19.96           C  
ATOM   2149  N   ASP A 285       8.483  54.663  17.406  1.00 30.76           N  
ATOM   2150  CA  ASP A 285       7.467  55.699  17.340  1.00 30.01           C  
ATOM   2151  C   ASP A 285       6.217  55.209  18.052  1.00 28.53           C  
ATOM   2152  O   ASP A 285       5.862  54.029  17.972  1.00 30.24           O  
ATOM   2153  CB  ASP A 285       7.162  56.084  15.886  1.00 30.33           C  
ATOM   2154  CG  ASP A 285       8.273  56.921  15.253  1.00 31.07           C  
ATOM   2155  OD1 ASP A 285       9.037  57.565  15.998  1.00 30.68           O  
ATOM   2156  OD2 ASP A 285       8.379  56.945  14.009  1.00 31.27           O  
ATOM   2157  N   SER A 286       5.602  56.114  18.806  1.00 29.68           N  
ATOM   2158  CA  SER A 286       4.392  55.849  19.562  1.00 28.79           C  
ATOM   2159  C   SER A 286       4.575  54.612  20.423  1.00 26.29           C  
ATOM   2160  O   SER A 286       3.774  53.673  20.359  1.00 26.59           O  
ATOM   2161  CB  SER A 286       3.206  55.673  18.611  1.00 31.91           C  
ATOM   2162  OG  SER A 286       1.981  55.601  19.323  1.00 38.65           O  
ATOM   2163  N   LEU A 287       5.641  54.603  21.217  1.00 25.77           N  
ATOM   2164  CA  LEU A 287       5.909  53.461  22.082  1.00 22.49           C  
ATOM   2165  C   LEU A 287       4.836  53.360  23.161  1.00 19.84           C  
ATOM   2166  O   LEU A 287       4.215  52.304  23.337  1.00 19.76           O  
ATOM   2167  CB  LEU A 287       7.296  53.567  22.728  1.00 18.37           C  
ATOM   2168  CG  LEU A 287       7.690  52.392  23.631  1.00 17.92           C  
ATOM   2169  CD1 LEU A 287       7.687  51.080  22.853  1.00 15.37           C  
ATOM   2170  CD2 LEU A 287       9.067  52.647  24.234  1.00 17.58           C  
ATOM   2171  N   TYR A 288       4.585  54.471  23.844  1.00 20.71           N  
ATOM   2172  CA  TYR A 288       3.590  54.490  24.911  1.00 21.03           C  
ATOM   2173  C   TYR A 288       2.926  55.851  24.985  1.00 20.52           C  
ATOM   2174  O   TYR A 288       3.608  56.869  25.071  1.00 17.88           O  
ATOM   2175  CB  TYR A 288       4.266  54.179  26.248  1.00 18.96           C  
ATOM   2176  CG  TYR A 288       3.322  53.870  27.387  1.00 18.16           C  
ATOM   2177  CD1 TYR A 288       2.757  52.602  27.518  1.00 19.76           C  
ATOM   2178  CD2 TYR A 288       3.041  54.822  28.369  1.00 18.09           C  
ATOM   2179  CE1 TYR A 288       1.945  52.281  28.600  1.00 21.14           C  
ATOM   2180  CE2 TYR A 288       2.226  54.514  29.458  1.00 20.43           C  
ATOM   2181  CZ  TYR A 288       1.682  53.240  29.568  1.00 22.34           C  
ATOM   2182  OH  TYR A 288       0.890  52.908  30.644  1.00 22.56           O  
ATOM   2183  N   GLU A 289       1.597  55.854  24.929  1.00 19.80           N  
ATOM   2184  CA  GLU A 289       0.800  57.075  25.003  1.00 21.61           C  
ATOM   2185  C   GLU A 289       1.267  58.156  24.031  1.00 23.63           C  
ATOM   2186  O   GLU A 289       1.343  59.337  24.377  1.00 22.45           O  
ATOM   2187  CB  GLU A 289       0.766  57.598  26.444  1.00 22.75           C  
ATOM   2188  CG  GLU A 289       0.063  56.633  27.406  1.00 28.43           C  
ATOM   2189  CD  GLU A 289      -0.104  57.168  28.824  1.00 29.79           C  
ATOM   2190  OE1 GLU A 289       0.260  58.333  29.089  1.00 29.54           O  
ATOM   2191  OE2 GLU A 289      -0.612  56.411  29.676  1.00 31.48           O  
ATOM   2192  N   GLY A 290       1.587  57.735  22.810  1.00 26.07           N  
ATOM   2193  CA  GLY A 290       2.039  58.666  21.793  1.00 26.85           C  
ATOM   2194  C   GLY A 290       3.451  59.175  22.000  1.00 28.44           C  
ATOM   2195  O   GLY A 290       3.896  60.078  21.292  1.00 31.51           O  
ATOM   2196  N   ILE A 291       4.163  58.603  22.965  1.00 29.49           N  
ATOM   2197  CA  ILE A 291       5.528  59.014  23.248  1.00 29.18           C  
ATOM   2198  C   ILE A 291       6.527  58.128  22.507  1.00 29.49           C  
ATOM   2199  O   ILE A 291       6.448  56.888  22.555  1.00 27.22           O  
ATOM   2200  CB  ILE A 291       5.861  58.963  24.757  1.00 29.41           C  
ATOM   2201  CG1 ILE A 291       4.831  59.759  25.567  1.00 27.08           C  
ATOM   2202  CG2 ILE A 291       7.256  59.545  25.009  1.00 33.28           C  
ATOM   2203  CD1 ILE A 291       5.023  59.638  27.060  1.00 22.80           C  
ATOM   2204  N   ASP A 292       7.422  58.775  21.767  1.00 28.80           N  
ATOM   2205  CA  ASP A 292       8.461  58.092  21.003  1.00 27.05           C  
ATOM   2206  C   ASP A 292       9.659  57.838  21.898  1.00 25.30           C  
ATOM   2207  O   ASP A 292       9.922  58.591  22.833  1.00 22.78           O  
ATOM   2208  CB  ASP A 292       8.904  58.946  19.825  1.00 28.87           C  
ATOM   2209  CG  ASP A 292       7.791  59.149  18.804  1.00 27.62           C  
ATOM   2210  OD1 ASP A 292       6.687  58.600  18.946  1.00 29.27           O  
ATOM   2211  OD2 ASP A 292       8.023  59.880  17.818  1.00 27.01           O  
ATOM   2212  N   PHE A 293      10.375  56.768  21.592  1.00 24.37           N  
ATOM   2213  CA  PHE A 293      11.546  56.411  22.370  1.00 24.77           C  
ATOM   2214  C   PHE A 293      12.739  56.302  21.439  1.00 23.19           C  
ATOM   2215  O   PHE A 293      12.870  55.338  20.690  1.00 21.12           O  
ATOM   2216  CB  PHE A 293      11.309  55.094  23.102  1.00 26.55           C  
ATOM   2217  CG  PHE A 293      12.309  54.809  24.185  1.00 27.37           C  
ATOM   2218  CD1 PHE A 293      12.645  55.791  25.113  1.00 27.25           C  
ATOM   2219  CD2 PHE A 293      12.902  53.552  24.289  1.00 30.54           C  
ATOM   2220  CE1 PHE A 293      13.563  55.528  26.130  1.00 27.94           C  
ATOM   2221  CE2 PHE A 293      13.820  53.277  25.302  1.00 30.71           C  
ATOM   2222  CZ  PHE A 293      14.149  54.265  26.225  1.00 28.40           C  
ATOM   2223  N   TYR A 294      13.541  57.357  21.422  1.00 24.97           N  
ATOM   2224  CA  TYR A 294      14.738  57.416  20.598  1.00 27.03           C  
ATOM   2225  C   TYR A 294      15.908  57.406  21.569  1.00 27.45           C  
ATOM   2226  O   TYR A 294      16.037  58.308  22.397  1.00 28.19           O  
ATOM   2227  CB  TYR A 294      14.750  58.700  19.764  1.00 29.00           C  
ATOM   2228  CG  TYR A 294      13.789  58.706  18.589  1.00 31.57           C  
ATOM   2229  CD1 TYR A 294      12.540  58.085  18.664  1.00 32.06           C  
ATOM   2230  CD2 TYR A 294      14.138  59.329  17.395  1.00 35.58           C  
ATOM   2231  CE1 TYR A 294      11.671  58.083  17.576  1.00 33.69           C  
ATOM   2232  CE2 TYR A 294      13.277  59.334  16.304  1.00 37.13           C  
ATOM   2233  CZ  TYR A 294      12.049  58.710  16.398  1.00 36.71           C  
ATOM   2234  OH  TYR A 294      11.216  58.706  15.305  1.00 40.66           O  
ATOM   2235  N   THR A 295      16.744  56.379  21.481  1.00 27.44           N  
ATOM   2236  CA  THR A 295      17.882  56.230  22.378  1.00 25.41           C  
ATOM   2237  C   THR A 295      18.975  55.402  21.698  1.00 24.92           C  
ATOM   2238  O   THR A 295      18.949  55.207  20.480  1.00 21.79           O  
ATOM   2239  CB  THR A 295      17.431  55.538  23.696  1.00 22.77           C  
ATOM   2240  OG1 THR A 295      18.518  55.521  24.634  1.00 26.44           O  
ATOM   2241  CG2 THR A 295      16.951  54.112  23.427  1.00 19.86           C  
ATOM   2242  N   SER A 296      19.945  54.941  22.482  1.00 24.41           N  
ATOM   2243  CA  SER A 296      21.034  54.126  21.962  1.00 22.43           C  
ATOM   2244  C   SER A 296      21.640  53.282  23.077  1.00 21.47           C  
ATOM   2245  O   SER A 296      21.351  53.482  24.261  1.00 20.12           O  
ATOM   2246  CB  SER A 296      22.111  55.002  21.308  1.00 22.12           C  
ATOM   2247  OG  SER A 296      22.722  55.872  22.242  1.00 23.76           O  
ATOM   2248  N   ILE A 297      22.482  52.336  22.691  1.00 19.29           N  
ATOM   2249  CA  ILE A 297      23.121  51.456  23.648  1.00 17.60           C  
ATOM   2250  C   ILE A 297      24.482  51.010  23.118  1.00 17.09           C  
ATOM   2251  O   ILE A 297      24.651  50.744  21.923  1.00 19.25           O  
ATOM   2252  CB  ILE A 297      22.209  50.237  23.969  1.00 15.09           C  
ATOM   2253  CG1 ILE A 297      22.884  49.316  24.984  1.00 13.50           C  
ATOM   2254  CG2 ILE A 297      21.801  49.510  22.687  1.00 11.72           C  
ATOM   2255  CD1 ILE A 297      21.995  48.211  25.502  1.00 12.19           C  
ATOM   2256  N   THR A 298      25.467  50.996  24.002  1.00 17.54           N  
ATOM   2257  CA  THR A 298      26.814  50.599  23.629  1.00 17.41           C  
ATOM   2258  C   THR A 298      27.014  49.101  23.794  1.00 17.39           C  
ATOM   2259  O   THR A 298      26.291  48.440  24.549  1.00 17.38           O  
ATOM   2260  CB  THR A 298      27.854  51.308  24.507  1.00 18.55           C  
ATOM   2261  OG1 THR A 298      27.713  50.864  25.863  1.00 17.29           O  
ATOM   2262  CG2 THR A 298      27.644  52.818  24.450  1.00 20.49           C  
ATOM   2263  N   ARG A 299      28.019  48.576  23.101  1.00 16.32           N  
ATOM   2264  CA  ARG A 299      28.357  47.163  23.188  1.00 15.54           C  
ATOM   2265  C   ARG A 299      28.709  46.840  24.638  1.00 16.61           C  
ATOM   2266  O   ARG A 299      28.276  45.822  25.178  1.00 17.86           O  
ATOM   2267  CB  ARG A 299      29.552  46.846  22.287  1.00 15.95           C  
ATOM   2268  CG  ARG A 299      29.999  45.393  22.358  1.00 13.86           C  
ATOM   2269  CD  ARG A 299      31.155  45.118  21.430  1.00 16.39           C  
ATOM   2270  NE  ARG A 299      30.840  45.483  20.057  1.00 16.02           N  
ATOM   2271  CZ  ARG A 299      31.574  45.127  19.007  1.00 17.57           C  
ATOM   2272  NH1 ARG A 299      32.748  44.525  19.182  1.00 20.73           N  
ATOM   2273  NH2 ARG A 299      31.216  45.497  17.783  1.00 18.72           N  
ATOM   2274  N   ALA A 300      29.477  47.733  25.264  1.00 18.08           N  
ATOM   2275  CA  ALA A 300      29.896  47.569  26.653  1.00 17.12           C  
ATOM   2276  C   ALA A 300      28.685  47.462  27.581  1.00 18.69           C  
ATOM   2277  O   ALA A 300      28.655  46.615  28.477  1.00 18.91           O  
ATOM   2278  CB  ALA A 300      30.780  48.730  27.077  1.00 14.71           C  
ATOM   2279  N   ARG A 301      27.682  48.311  27.353  1.00 17.84           N  
ATOM   2280  CA  ARG A 301      26.471  48.302  28.165  1.00 18.84           C  
ATOM   2281  C   ARG A 301      25.744  46.966  27.984  1.00 15.58           C  
ATOM   2282  O   ARG A 301      25.329  46.334  28.956  1.00 15.24           O  
ATOM   2283  CB  ARG A 301      25.550  49.454  27.757  1.00 21.73           C  
ATOM   2284  CG  ARG A 301      24.388  49.654  28.701  1.00 23.68           C  
ATOM   2285  CD  ARG A 301      24.866  50.285  29.987  1.00 26.45           C  
ATOM   2286  NE  ARG A 301      24.330  49.609  31.159  1.00 34.12           N  
ATOM   2287  CZ  ARG A 301      24.169  50.188  32.344  1.00 35.30           C  
ATOM   2288  NH1 ARG A 301      24.500  51.461  32.511  1.00 39.46           N  
ATOM   2289  NH2 ARG A 301      23.682  49.494  33.364  1.00 40.09           N  
ATOM   2290  N   PHE A 302      25.588  46.556  26.729  1.00 15.75           N  
ATOM   2291  CA  PHE A 302      24.937  45.297  26.388  1.00 14.68           C  
ATOM   2292  C   PHE A 302      25.668  44.138  27.083  1.00 14.89           C  
ATOM   2293  O   PHE A 302      25.039  43.225  27.610  1.00 15.30           O  
ATOM   2294  CB  PHE A 302      24.936  45.123  24.854  1.00 13.78           C  
ATOM   2295  CG  PHE A 302      24.529  43.748  24.384  1.00 14.02           C  
ATOM   2296  CD1 PHE A 302      23.198  43.337  24.449  1.00 13.77           C  
ATOM   2297  CD2 PHE A 302      25.485  42.855  23.905  1.00  9.60           C  
ATOM   2298  CE1 PHE A 302      22.826  42.052  24.048  1.00 12.61           C  
ATOM   2299  CE2 PHE A 302      25.129  41.575  23.504  1.00 10.39           C  
ATOM   2300  CZ  PHE A 302      23.791  41.169  23.576  1.00 13.96           C  
ATOM   2301  N   GLU A 303      26.999  44.190  27.095  1.00 17.61           N  
ATOM   2302  CA  GLU A 303      27.805  43.152  27.738  1.00 16.57           C  
ATOM   2303  C   GLU A 303      27.591  43.145  29.249  1.00 16.22           C  
ATOM   2304  O   GLU A 303      27.435  42.088  29.853  1.00 17.09           O  
ATOM   2305  CB  GLU A 303      29.285  43.343  27.400  1.00 16.23           C  
ATOM   2306  CG  GLU A 303      29.593  43.010  25.950  1.00 15.66           C  
ATOM   2307  CD  GLU A 303      30.976  43.440  25.492  1.00 17.83           C  
ATOM   2308  OE1 GLU A 303      31.675  44.170  26.233  1.00 21.90           O  
ATOM   2309  OE2 GLU A 303      31.358  43.055  24.369  1.00 15.43           O  
ATOM   2310  N   GLU A 304      27.544  44.332  29.844  1.00 18.43           N  
ATOM   2311  CA  GLU A 304      27.334  44.487  31.282  1.00 17.67           C  
ATOM   2312  C   GLU A 304      25.990  43.887  31.695  1.00 16.03           C  
ATOM   2313  O   GLU A 304      25.922  43.082  32.625  1.00 12.60           O  
ATOM   2314  CB  GLU A 304      27.394  45.975  31.654  1.00 22.48           C  
ATOM   2315  CG  GLU A 304      27.194  46.295  33.145  1.00 32.10           C  
ATOM   2316  CD  GLU A 304      25.747  46.623  33.513  1.00 37.03           C  
ATOM   2317  OE1 GLU A 304      24.999  47.108  32.636  1.00 40.65           O  
ATOM   2318  OE2 GLU A 304      25.360  46.408  34.685  1.00 36.73           O  
ATOM   2319  N   LEU A 305      24.934  44.258  30.975  1.00 14.93           N  
ATOM   2320  CA  LEU A 305      23.584  43.771  31.255  1.00 13.68           C  
ATOM   2321  C   LEU A 305      23.461  42.258  31.182  1.00 11.98           C  
ATOM   2322  O   LEU A 305      22.587  41.679  31.827  1.00 14.19           O  
ATOM   2323  CB  LEU A 305      22.572  44.391  30.280  1.00 14.09           C  
ATOM   2324  CG  LEU A 305      22.297  45.894  30.337  1.00 12.32           C  
ATOM   2325  CD1 LEU A 305      21.422  46.281  29.160  1.00 17.50           C  
ATOM   2326  CD2 LEU A 305      21.620  46.251  31.639  1.00 12.90           C  
ATOM   2327  N   ASN A 306      24.335  41.623  30.404  1.00 12.48           N  
ATOM   2328  CA  ASN A 306      24.301  40.171  30.228  1.00 12.54           C  
ATOM   2329  C   ASN A 306      25.525  39.409  30.755  1.00 12.10           C  
ATOM   2330  O   ASN A 306      25.625  38.192  30.584  1.00 11.18           O  
ATOM   2331  CB  ASN A 306      24.095  39.840  28.742  1.00 13.44           C  
ATOM   2332  CG  ASN A 306      22.753  40.310  28.224  1.00 10.73           C  
ATOM   2333  OD1 ASN A 306      22.645  41.358  27.587  1.00 13.67           O  
ATOM   2334  ND2 ASN A 306      21.715  39.548  28.519  1.00 10.95           N  
ATOM   2335  N   ALA A 307      26.419  40.115  31.435  1.00 13.12           N  
ATOM   2336  CA  ALA A 307      27.644  39.530  31.971  1.00 12.30           C  
ATOM   2337  C   ALA A 307      27.508  38.138  32.587  1.00 12.37           C  
ATOM   2338  O   ALA A 307      28.219  37.216  32.198  1.00 14.09           O  
ATOM   2339  CB  ALA A 307      28.286  40.487  32.962  1.00 12.44           C  
ATOM   2340  N   ASP A 308      26.590  37.984  33.535  1.00 14.63           N  
ATOM   2341  CA  ASP A 308      26.388  36.701  34.207  1.00 12.53           C  
ATOM   2342  C   ASP A 308      25.914  35.593  33.273  1.00 11.50           C  
ATOM   2343  O   ASP A 308      26.376  34.453  33.365  1.00  9.50           O  
ATOM   2344  CB  ASP A 308      25.401  36.862  35.366  1.00 15.06           C  
ATOM   2345  CG  ASP A 308      24.024  37.285  34.902  1.00 13.76           C  
ATOM   2346  OD1 ASP A 308      23.915  38.348  34.264  1.00 15.15           O  
ATOM   2347  OD2 ASP A 308      23.056  36.538  35.157  1.00 20.21           O  
ATOM   2348  N   LEU A 309      24.986  35.936  32.381  1.00 12.65           N  
ATOM   2349  CA  LEU A 309      24.433  34.978  31.429  1.00 11.77           C  
ATOM   2350  C   LEU A 309      25.506  34.519  30.444  1.00 10.05           C  
ATOM   2351  O   LEU A 309      25.641  33.323  30.166  1.00 11.06           O  
ATOM   2352  CB  LEU A 309      23.255  35.603  30.671  1.00 10.73           C  
ATOM   2353  CG  LEU A 309      22.021  36.004  31.480  1.00 10.50           C  
ATOM   2354  CD1 LEU A 309      21.000  36.691  30.578  1.00  8.84           C  
ATOM   2355  CD2 LEU A 309      21.419  34.774  32.138  1.00 10.45           C  
ATOM   2356  N   PHE A 310      26.274  35.473  29.931  1.00 11.82           N  
ATOM   2357  CA  PHE A 310      27.344  35.169  28.981  1.00 11.74           C  
ATOM   2358  C   PHE A 310      28.349  34.209  29.604  1.00 11.22           C  
ATOM   2359  O   PHE A 310      28.632  33.145  29.058  1.00 10.69           O  
ATOM   2360  CB  PHE A 310      28.066  36.455  28.559  1.00  9.19           C  
ATOM   2361  CG  PHE A 310      27.284  37.332  27.612  1.00  9.37           C  
ATOM   2362  CD1 PHE A 310      26.045  36.939  27.112  1.00  8.40           C  
ATOM   2363  CD2 PHE A 310      27.810  38.555  27.200  1.00 11.64           C  
ATOM   2364  CE1 PHE A 310      25.350  37.753  26.215  1.00  7.18           C  
ATOM   2365  CE2 PHE A 310      27.118  39.375  26.303  1.00  8.84           C  
ATOM   2366  CZ  PHE A 310      25.890  38.971  25.813  1.00  9.28           C  
ATOM   2367  N   ARG A 311      28.847  34.563  30.779  1.00 13.42           N  
ATOM   2368  CA  ARG A 311      29.826  33.728  31.458  1.00 15.62           C  
ATOM   2369  C   ARG A 311      29.326  32.346  31.840  1.00 15.54           C  
ATOM   2370  O   ARG A 311      30.092  31.377  31.801  1.00 16.60           O  
ATOM   2371  CB  ARG A 311      30.362  34.417  32.708  1.00 19.17           C  
ATOM   2372  CG  ARG A 311      31.415  33.574  33.418  1.00 33.56           C  
ATOM   2373  CD  ARG A 311      31.954  34.231  34.657  1.00 40.59           C  
ATOM   2374  NE  ARG A 311      31.269  35.473  34.965  1.00 49.31           N  
ATOM   2375  CZ  ARG A 311      31.653  36.676  34.530  1.00 53.29           C  
ATOM   2376  NH1 ARG A 311      32.724  36.833  33.745  1.00 55.71           N  
ATOM   2377  NH2 ARG A 311      30.904  37.737  34.800  1.00 51.46           N  
ATOM   2378  N   GLY A 312      28.046  32.250  32.193  1.00 13.79           N  
ATOM   2379  CA  GLY A 312      27.475  30.971  32.573  1.00 10.80           C  
ATOM   2380  C   GLY A 312      27.571  29.907  31.498  1.00  9.48           C  
ATOM   2381  O   GLY A 312      27.443  28.717  31.789  1.00 11.46           O  
ATOM   2382  N   THR A 313      27.822  30.319  30.258  1.00 11.24           N  
ATOM   2383  CA  THR A 313      27.927  29.365  29.160  1.00 10.67           C  
ATOM   2384  C   THR A 313      29.132  28.439  29.329  1.00 12.18           C  
ATOM   2385  O   THR A 313      29.132  27.311  28.833  1.00 11.51           O  
ATOM   2386  CB  THR A 313      28.002  30.072  27.771  1.00 12.55           C  
ATOM   2387  OG1 THR A 313      29.186  30.875  27.686  1.00 10.65           O  
ATOM   2388  CG2 THR A 313      26.782  30.954  27.547  1.00  9.56           C  
ATOM   2389  N   LEU A 314      30.132  28.899  30.080  1.00 13.39           N  
ATOM   2390  CA  LEU A 314      31.347  28.120  30.317  1.00 11.27           C  
ATOM   2391  C   LEU A 314      31.165  26.904  31.229  1.00 12.20           C  
ATOM   2392  O   LEU A 314      31.867  25.901  31.080  1.00 11.02           O  
ATOM   2393  CB  LEU A 314      32.467  29.030  30.829  1.00  9.53           C  
ATOM   2394  CG  LEU A 314      32.925  30.079  29.808  1.00 10.07           C  
ATOM   2395  CD1 LEU A 314      33.945  31.012  30.425  1.00 12.79           C  
ATOM   2396  CD2 LEU A 314      33.497  29.399  28.583  1.00  8.29           C  
ATOM   2397  N   ASP A 315      30.199  26.966  32.142  1.00 13.70           N  
ATOM   2398  CA  ASP A 315      29.953  25.843  33.040  1.00 14.58           C  
ATOM   2399  C   ASP A 315      29.595  24.582  32.257  1.00 14.17           C  
ATOM   2400  O   ASP A 315      30.190  23.528  32.483  1.00 14.88           O  
ATOM   2401  CB  ASP A 315      28.887  26.187  34.088  1.00 19.29           C  
ATOM   2402  CG  ASP A 315      29.407  27.121  35.173  1.00 21.98           C  
ATOM   2403  OD1 ASP A 315      30.632  27.124  35.421  1.00 24.15           O  
ATOM   2404  OD2 ASP A 315      28.592  27.845  35.788  1.00 23.45           O  
ATOM   2405  N   PRO A 316      28.611  24.662  31.336  1.00 14.95           N  
ATOM   2406  CA  PRO A 316      28.252  23.471  30.556  1.00 13.15           C  
ATOM   2407  C   PRO A 316      29.429  22.976  29.701  1.00 14.72           C  
ATOM   2408  O   PRO A 316      29.512  21.789  29.377  1.00 16.90           O  
ATOM   2409  CB  PRO A 316      27.102  23.970  29.688  1.00 11.37           C  
ATOM   2410  CG  PRO A 316      26.435  24.962  30.575  1.00 12.74           C  
ATOM   2411  CD  PRO A 316      27.620  25.731  31.110  1.00 13.64           C  
ATOM   2412  N   VAL A 317      30.335  23.886  29.339  1.00 14.19           N  
ATOM   2413  CA  VAL A 317      31.517  23.532  28.547  1.00 15.35           C  
ATOM   2414  C   VAL A 317      32.461  22.677  29.404  1.00 17.44           C  
ATOM   2415  O   VAL A 317      32.952  21.639  28.947  1.00 16.33           O  
ATOM   2416  CB  VAL A 317      32.269  24.786  28.049  1.00 14.17           C  
ATOM   2417  CG1 VAL A 317      33.569  24.383  27.350  1.00 12.21           C  
ATOM   2418  CG2 VAL A 317      31.381  25.594  27.103  1.00 11.29           C  
ATOM   2419  N   GLU A 318      32.720  23.119  30.634  1.00 20.49           N  
ATOM   2420  CA  GLU A 318      33.573  22.362  31.543  1.00 23.92           C  
ATOM   2421  C   GLU A 318      32.933  21.001  31.789  1.00 21.38           C  
ATOM   2422  O   GLU A 318      33.604  19.972  31.753  1.00 22.15           O  
ATOM   2423  CB  GLU A 318      33.714  23.070  32.887  1.00 27.75           C  
ATOM   2424  CG  GLU A 318      34.481  24.338  32.872  1.00 36.15           C  
ATOM   2425  CD  GLU A 318      34.927  24.742  34.290  1.00 43.95           C  
ATOM   2426  OE1 GLU A 318      34.146  25.422  34.993  1.00 49.34           O  
ATOM   2427  OE2 GLU A 318      36.035  24.326  34.735  1.00 48.03           O  
ATOM   2428  N   LYS A 319      31.630  21.015  32.053  1.00 23.16           N  
ATOM   2429  CA  LYS A 319      30.868  19.797  32.295  1.00 24.78           C  
ATOM   2430  C   LYS A 319      31.043  18.787  31.162  1.00 25.48           C  
ATOM   2431  O   LYS A 319      31.373  17.622  31.399  1.00 26.42           O  
ATOM   2432  CB  LYS A 319      29.381  20.121  32.479  1.00 24.74           C  
ATOM   2433  CG  LYS A 319      28.490  18.893  32.516  1.00 28.44           C  
ATOM   2434  CD  LYS A 319      27.648  18.865  33.769  1.00 32.50           C  
ATOM   2435  CE  LYS A 319      27.404  17.442  34.269  1.00 37.06           C  
ATOM   2436  NZ  LYS A 319      26.650  16.547  33.336  1.00 43.88           N  
ATOM   2437  N   ALA A 320      30.837  19.244  29.932  1.00 24.77           N  
ATOM   2438  CA  ALA A 320      30.976  18.389  28.760  1.00 24.77           C  
ATOM   2439  C   ALA A 320      32.376  17.776  28.683  1.00 25.39           C  
ATOM   2440  O   ALA A 320      32.515  16.565  28.526  1.00 27.52           O  
ATOM   2441  CB  ALA A 320      30.660  19.174  27.490  1.00 24.02           C  
ATOM   2442  N   LEU A 321      33.409  18.605  28.815  1.00 25.75           N  
ATOM   2443  CA  LEU A 321      34.794  18.133  28.771  1.00 27.74           C  
ATOM   2444  C   LEU A 321      35.034  17.056  29.823  1.00 30.32           C  
ATOM   2445  O   LEU A 321      35.573  15.991  29.526  1.00 30.38           O  
ATOM   2446  CB  LEU A 321      35.769  19.293  28.998  1.00 25.77           C  
ATOM   2447  CG  LEU A 321      36.028  20.229  27.819  1.00 27.57           C  
ATOM   2448  CD1 LEU A 321      36.751  21.480  28.295  1.00 25.89           C  
ATOM   2449  CD2 LEU A 321      36.844  19.502  26.756  1.00 24.27           C  
ATOM   2450  N   ARG A 322      34.600  17.337  31.046  1.00 33.30           N  
ATOM   2451  CA  ARG A 322      34.747  16.418  32.165  1.00 36.09           C  
ATOM   2452  C   ARG A 322      34.075  15.081  31.860  1.00 36.78           C  
ATOM   2453  O   ARG A 322      34.672  14.022  32.058  1.00 38.40           O  
ATOM   2454  CB  ARG A 322      34.149  17.050  33.426  1.00 38.76           C  
ATOM   2455  CG  ARG A 322      34.233  16.198  34.682  1.00 42.73           C  
ATOM   2456  CD  ARG A 322      33.856  16.995  35.933  1.00 46.25           C  
ATOM   2457  NE  ARG A 322      32.505  17.561  35.873  1.00 49.03           N  
ATOM   2458  CZ  ARG A 322      32.243  18.864  35.816  1.00 49.11           C  
ATOM   2459  NH1 ARG A 322      33.239  19.741  35.785  1.00 49.13           N  
ATOM   2460  NH2 ARG A 322      30.986  19.293  35.767  1.00 49.48           N  
ATOM   2461  N   ASP A 323      32.849  15.134  31.345  1.00 37.01           N  
ATOM   2462  CA  ASP A 323      32.098  13.925  31.003  1.00 37.26           C  
ATOM   2463  C   ASP A 323      32.704  13.189  29.815  1.00 38.59           C  
ATOM   2464  O   ASP A 323      32.579  11.971  29.700  1.00 39.72           O  
ATOM   2465  CB  ASP A 323      30.640  14.262  30.698  1.00 35.94           C  
ATOM   2466  CG  ASP A 323      29.893  14.795  31.904  1.00 36.61           C  
ATOM   2467  OD1 ASP A 323      30.350  14.598  33.053  1.00 35.72           O  
ATOM   2468  OD2 ASP A 323      28.829  15.410  31.692  1.00 39.89           O  
ATOM   2469  N   ALA A 324      33.325  13.939  28.913  1.00 38.45           N  
ATOM   2470  CA  ALA A 324      33.968  13.355  27.745  1.00 39.70           C  
ATOM   2471  C   ALA A 324      35.320  12.804  28.186  1.00 42.95           C  
ATOM   2472  O   ALA A 324      36.042  12.190  27.393  1.00 44.79           O  
ATOM   2473  CB  ALA A 324      34.162  14.410  26.671  1.00 36.14           C  
ATOM   2474  N   LYS A 325      35.660  13.056  29.451  1.00 43.79           N  
ATOM   2475  CA  LYS A 325      36.914  12.618  30.039  1.00 44.02           C  
ATOM   2476  C   LYS A 325      38.014  13.218  29.174  1.00 43.55           C  
ATOM   2477  O   LYS A 325      39.022  12.571  28.868  1.00 45.22           O  
ATOM   2478  CB  LYS A 325      36.977  11.089  30.056  1.00 47.36           C  
ATOM   2479  CG  LYS A 325      38.086  10.501  30.907  1.00 54.09           C  
ATOM   2480  CD  LYS A 325      37.979   8.982  30.952  1.00 60.01           C  
ATOM   2481  CE  LYS A 325      37.053   8.491  32.068  1.00 61.60           C  
ATOM   2482  NZ  LYS A 325      35.727   9.176  32.153  1.00 63.54           N  
ATOM   2483  N   LEU A 326      37.799  14.471  28.784  1.00 40.43           N  
ATOM   2484  CA  LEU A 326      38.729  15.197  27.932  1.00 39.51           C  
ATOM   2485  C   LEU A 326      39.199  16.498  28.567  1.00 38.98           C  
ATOM   2486  O   LEU A 326      38.474  17.132  29.335  1.00 40.07           O  
ATOM   2487  CB  LEU A 326      38.065  15.498  26.584  1.00 39.31           C  
ATOM   2488  CG  LEU A 326      38.647  14.894  25.307  1.00 36.56           C  
ATOM   2489  CD1 LEU A 326      38.791  13.397  25.447  1.00 37.52           C  
ATOM   2490  CD2 LEU A 326      37.739  15.227  24.142  1.00 37.58           C  
ATOM   2491  N   ASP A 327      40.418  16.886  28.223  1.00 38.77           N  
ATOM   2492  CA  ASP A 327      41.042  18.110  28.710  1.00 39.98           C  
ATOM   2493  C   ASP A 327      40.880  19.152  27.596  1.00 37.52           C  
ATOM   2494  O   ASP A 327      40.728  18.792  26.426  1.00 36.42           O  
ATOM   2495  CB  ASP A 327      42.526  17.806  29.009  1.00 45.52           C  
ATOM   2496  CG  ASP A 327      43.346  19.036  29.381  1.00 50.54           C  
ATOM   2497  OD1 ASP A 327      42.845  19.934  30.089  1.00 55.29           O  
ATOM   2498  OD2 ASP A 327      44.534  19.075  28.990  1.00 52.41           O  
ATOM   2499  N   LYS A 328      40.882  20.432  27.964  1.00 33.83           N  
ATOM   2500  CA  LYS A 328      40.738  21.529  27.007  1.00 30.37           C  
ATOM   2501  C   LYS A 328      41.602  21.312  25.777  1.00 31.88           C  
ATOM   2502  O   LYS A 328      41.141  21.457  24.643  1.00 28.82           O  
ATOM   2503  CB  LYS A 328      41.166  22.859  27.633  1.00 28.37           C  
ATOM   2504  CG  LYS A 328      40.277  23.398  28.717  1.00 23.65           C  
ATOM   2505  CD  LYS A 328      40.826  24.731  29.205  1.00 21.99           C  
ATOM   2506  CE  LYS A 328      40.035  25.268  30.382  1.00 18.09           C  
ATOM   2507  NZ  LYS A 328      40.495  26.612  30.806  1.00 18.99           N  
ATOM   2508  N   SER A 329      42.859  20.952  26.022  1.00 33.53           N  
ATOM   2509  CA  SER A 329      43.840  20.728  24.969  1.00 33.18           C  
ATOM   2510  C   SER A 329      43.497  19.613  23.984  1.00 32.05           C  
ATOM   2511  O   SER A 329      44.017  19.591  22.870  1.00 34.48           O  
ATOM   2512  CB  SER A 329      45.212  20.470  25.594  1.00 35.42           C  
ATOM   2513  OG  SER A 329      45.163  19.351  26.463  1.00 36.37           O  
ATOM   2514  N   GLN A 330      42.649  18.672  24.388  1.00 33.09           N  
ATOM   2515  CA  GLN A 330      42.277  17.588  23.482  1.00 36.82           C  
ATOM   2516  C   GLN A 330      41.279  17.996  22.399  1.00 34.71           C  
ATOM   2517  O   GLN A 330      41.047  17.232  21.454  1.00 36.14           O  
ATOM   2518  CB  GLN A 330      41.739  16.371  24.235  1.00 40.91           C  
ATOM   2519  CG  GLN A 330      42.805  15.370  24.646  1.00 50.13           C  
ATOM   2520  CD  GLN A 330      43.368  15.663  26.002  1.00 52.26           C  
ATOM   2521  OE1 GLN A 330      42.624  15.885  26.947  1.00 54.99           O  
ATOM   2522  NE2 GLN A 330      44.691  15.655  26.114  1.00 59.13           N  
ATOM   2523  N   ILE A 331      40.668  19.171  22.548  1.00 31.15           N  
ATOM   2524  CA  ILE A 331      39.707  19.659  21.560  1.00 29.02           C  
ATOM   2525  C   ILE A 331      40.471  20.244  20.372  1.00 28.18           C  
ATOM   2526  O   ILE A 331      41.170  21.254  20.507  1.00 26.89           O  
ATOM   2527  CB  ILE A 331      38.765  20.750  22.148  1.00 26.91           C  
ATOM   2528  CG1 ILE A 331      38.048  20.226  23.395  1.00 22.04           C  
ATOM   2529  CG2 ILE A 331      37.734  21.179  21.103  1.00 23.87           C  
ATOM   2530  CD1 ILE A 331      37.175  19.013  23.147  1.00 23.01           C  
ATOM   2531  N   HIS A 332      40.336  19.607  19.212  1.00 28.39           N  
ATOM   2532  CA  HIS A 332      41.021  20.062  18.002  1.00 27.02           C  
ATOM   2533  C   HIS A 332      40.253  21.144  17.258  1.00 25.09           C  
ATOM   2534  O   HIS A 332      40.856  21.997  16.595  1.00 21.76           O  
ATOM   2535  CB  HIS A 332      41.292  18.888  17.065  1.00 31.03           C  
ATOM   2536  CG  HIS A 332      41.952  17.730  17.734  1.00 34.75           C  
ATOM   2537  ND1 HIS A 332      41.454  16.447  17.665  1.00 36.00           N  
ATOM   2538  CD2 HIS A 332      43.058  17.662  18.519  1.00 36.84           C  
ATOM   2539  CE1 HIS A 332      42.220  15.640  18.382  1.00 37.28           C  
ATOM   2540  NE2 HIS A 332      43.195  16.353  18.907  1.00 38.31           N  
ATOM   2541  N   ASP A 333      38.926  21.106  17.355  1.00 23.08           N  
ATOM   2542  CA  ASP A 333      38.095  22.097  16.686  1.00 22.43           C  
ATOM   2543  C   ASP A 333      36.941  22.548  17.556  1.00 18.91           C  
ATOM   2544  O   ASP A 333      36.327  21.742  18.259  1.00 18.60           O  
ATOM   2545  CB  ASP A 333      37.543  21.546  15.367  1.00 22.43           C  
ATOM   2546  CG  ASP A 333      38.634  21.190  14.388  1.00 20.77           C  
ATOM   2547  OD1 ASP A 333      39.122  22.098  13.683  1.00 19.92           O  
ATOM   2548  OD2 ASP A 333      39.017  20.005  14.344  1.00 21.29           O  
ATOM   2549  N   ILE A 334      36.678  23.848  17.515  1.00 18.53           N  
ATOM   2550  CA  ILE A 334      35.581  24.455  18.255  1.00 19.83           C  
ATOM   2551  C   ILE A 334      34.705  25.125  17.197  1.00 19.00           C  
ATOM   2552  O   ILE A 334      35.123  26.092  16.546  1.00 18.23           O  
ATOM   2553  CB  ILE A 334      36.074  25.534  19.243  1.00 20.00           C  
ATOM   2554  CG1 ILE A 334      37.068  24.933  20.238  1.00 16.36           C  
ATOM   2555  CG2 ILE A 334      34.884  26.140  19.993  1.00 18.68           C  
ATOM   2556  CD1 ILE A 334      37.772  25.981  21.059  1.00 18.28           C  
ATOM   2557  N   VAL A 335      33.501  24.599  17.021  1.00 15.21           N  
ATOM   2558  CA  VAL A 335      32.575  25.126  16.032  1.00 13.56           C  
ATOM   2559  C   VAL A 335      31.469  25.944  16.688  1.00 11.53           C  
ATOM   2560  O   VAL A 335      30.819  25.489  17.633  1.00 10.72           O  
ATOM   2561  CB  VAL A 335      31.951  23.976  15.206  1.00 13.84           C  
ATOM   2562  CG1 VAL A 335      31.023  24.528  14.132  1.00 12.92           C  
ATOM   2563  CG2 VAL A 335      33.051  23.123  14.581  1.00 13.97           C  
ATOM   2564  N   LEU A 336      31.295  27.169  16.207  1.00 10.40           N  
ATOM   2565  CA  LEU A 336      30.261  28.056  16.719  1.00 11.84           C  
ATOM   2566  C   LEU A 336      28.962  27.856  15.941  1.00 10.53           C  
ATOM   2567  O   LEU A 336      28.953  27.874  14.704  1.00 10.38           O  
ATOM   2568  CB  LEU A 336      30.694  29.515  16.585  1.00 11.37           C  
ATOM   2569  CG  LEU A 336      31.926  29.955  17.371  1.00  8.16           C  
ATOM   2570  CD1 LEU A 336      32.111  31.443  17.185  1.00  9.22           C  
ATOM   2571  CD2 LEU A 336      31.751  29.615  18.843  1.00 10.33           C  
ATOM   2572  N   VAL A 337      27.869  27.647  16.662  1.00 10.06           N  
ATOM   2573  CA  VAL A 337      26.566  27.467  16.028  1.00 10.46           C  
ATOM   2574  C   VAL A 337      25.575  28.317  16.815  1.00 10.80           C  
ATOM   2575  O   VAL A 337      25.768  28.553  18.013  1.00  8.90           O  
ATOM   2576  CB  VAL A 337      26.107  25.984  16.036  1.00 10.32           C  
ATOM   2577  CG1 VAL A 337      24.834  25.816  15.208  1.00  5.71           C  
ATOM   2578  CG2 VAL A 337      27.215  25.066  15.513  1.00 10.46           C  
ATOM   2579  N   GLY A 338      24.530  28.788  16.142  1.00  9.76           N  
ATOM   2580  CA  GLY A 338      23.538  29.615  16.802  1.00  9.04           C  
ATOM   2581  C   GLY A 338      23.871  31.073  16.600  1.00  9.69           C  
ATOM   2582  O   GLY A 338      25.034  31.459  16.697  1.00 10.86           O  
ATOM   2583  N   GLY A 339      22.855  31.881  16.312  1.00  6.03           N  
ATOM   2584  CA  GLY A 339      23.059  33.298  16.078  1.00  7.09           C  
ATOM   2585  C   GLY A 339      23.725  34.054  17.218  1.00 11.11           C  
ATOM   2586  O   GLY A 339      24.430  35.036  16.985  1.00 10.72           O  
ATOM   2587  N   SER A 340      23.530  33.590  18.449  1.00 12.41           N  
ATOM   2588  CA  SER A 340      24.122  34.253  19.603  1.00 12.97           C  
ATOM   2589  C   SER A 340      25.646  34.104  19.723  1.00 12.30           C  
ATOM   2590  O   SER A 340      26.285  34.896  20.424  1.00 12.87           O  
ATOM   2591  CB  SER A 340      23.436  33.797  20.890  1.00 12.88           C  
ATOM   2592  OG  SER A 340      22.066  34.150  20.879  1.00 14.83           O  
ATOM   2593  N   THR A 341      26.233  33.112  19.055  1.00 11.42           N  
ATOM   2594  CA  THR A 341      27.686  32.942  19.107  1.00 10.57           C  
ATOM   2595  C   THR A 341      28.392  34.018  18.273  1.00 12.08           C  
ATOM   2596  O   THR A 341      29.623  34.076  18.225  1.00 13.13           O  
ATOM   2597  CB  THR A 341      28.133  31.538  18.656  1.00 10.56           C  
ATOM   2598  OG1 THR A 341      27.673  31.267  17.324  1.00 11.26           O  
ATOM   2599  CG2 THR A 341      27.594  30.491  19.604  1.00 10.59           C  
ATOM   2600  N   ARG A 342      27.604  34.858  17.607  1.00 12.51           N  
ATOM   2601  CA  ARG A 342      28.133  35.955  16.809  1.00 10.84           C  
ATOM   2602  C   ARG A 342      28.475  37.130  17.722  1.00 11.13           C  
ATOM   2603  O   ARG A 342      29.123  38.090  17.299  1.00 10.18           O  
ATOM   2604  CB  ARG A 342      27.120  36.374  15.737  1.00 13.93           C  
ATOM   2605  CG  ARG A 342      26.893  35.288  14.689  1.00 14.05           C  
ATOM   2606  CD  ARG A 342      25.751  35.604  13.734  1.00 17.07           C  
ATOM   2607  NE  ARG A 342      26.083  36.660  12.783  1.00 15.38           N  
ATOM   2608  CZ  ARG A 342      25.563  36.753  11.563  1.00 19.49           C  
ATOM   2609  NH1 ARG A 342      24.685  35.851  11.131  1.00 18.60           N  
ATOM   2610  NH2 ARG A 342      25.898  37.766  10.780  1.00 16.52           N  
ATOM   2611  N   ILE A 343      28.045  37.050  18.981  1.00  9.94           N  
ATOM   2612  CA  ILE A 343      28.330  38.099  19.959  1.00 10.59           C  
ATOM   2613  C   ILE A 343      29.831  38.038  20.297  1.00  9.80           C  
ATOM   2614  O   ILE A 343      30.323  37.027  20.799  1.00  9.89           O  
ATOM   2615  CB  ILE A 343      27.488  37.918  21.258  1.00 10.61           C  
ATOM   2616  CG1 ILE A 343      25.992  38.004  20.935  1.00 10.59           C  
ATOM   2617  CG2 ILE A 343      27.853  38.986  22.284  1.00  6.76           C  
ATOM   2618  CD1 ILE A 343      25.082  37.730  22.112  1.00  9.12           C  
ATOM   2619  N   PRO A 344      30.567  39.129  20.035  1.00 11.95           N  
ATOM   2620  CA  PRO A 344      32.007  39.203  20.302  1.00 12.77           C  
ATOM   2621  C   PRO A 344      32.416  38.785  21.715  1.00 11.26           C  
ATOM   2622  O   PRO A 344      33.406  38.074  21.880  1.00 12.16           O  
ATOM   2623  CB  PRO A 344      32.318  40.673  20.031  1.00 14.20           C  
ATOM   2624  CG  PRO A 344      31.347  41.010  18.926  1.00 12.75           C  
ATOM   2625  CD  PRO A 344      30.082  40.400  19.463  1.00 13.77           C  
ATOM   2626  N   LYS A 345      31.659  39.211  22.725  1.00  8.33           N  
ATOM   2627  CA  LYS A 345      31.975  38.864  24.114  1.00  9.63           C  
ATOM   2628  C   LYS A 345      31.901  37.359  24.361  1.00  9.52           C  
ATOM   2629  O   LYS A 345      32.685  36.816  25.135  1.00  8.91           O  
ATOM   2630  CB  LYS A 345      31.039  39.597  25.083  1.00 12.10           C  
ATOM   2631  CG  LYS A 345      31.406  39.449  26.562  1.00 10.27           C  
ATOM   2632  CD  LYS A 345      32.736  40.139  26.863  1.00 15.06           C  
ATOM   2633  CE  LYS A 345      33.009  40.199  28.350  1.00 18.44           C  
ATOM   2634  NZ  LYS A 345      34.198  41.043  28.646  1.00 20.60           N  
ATOM   2635  N   ILE A 346      30.958  36.690  23.704  1.00  9.72           N  
ATOM   2636  CA  ILE A 346      30.800  35.246  23.850  1.00  9.02           C  
ATOM   2637  C   ILE A 346      32.024  34.568  23.253  1.00  9.95           C  
ATOM   2638  O   ILE A 346      32.591  33.651  23.843  1.00  8.20           O  
ATOM   2639  CB  ILE A 346      29.509  34.738  23.136  1.00 10.60           C  
ATOM   2640  CG1 ILE A 346      28.265  35.096  23.959  1.00 13.17           C  
ATOM   2641  CG2 ILE A 346      29.578  33.225  22.880  1.00 10.71           C  
ATOM   2642  CD1 ILE A 346      28.117  34.308  25.252  1.00  9.76           C  
ATOM   2643  N   GLN A 347      32.441  35.037  22.085  1.00  9.98           N  
ATOM   2644  CA  GLN A 347      33.602  34.463  21.422  1.00 10.82           C  
ATOM   2645  C   GLN A 347      34.842  34.625  22.294  1.00 10.63           C  
ATOM   2646  O   GLN A 347      35.623  33.687  22.449  1.00 14.66           O  
ATOM   2647  CB  GLN A 347      33.802  35.110  20.053  1.00 10.14           C  
ATOM   2648  CG  GLN A 347      32.600  34.935  19.137  1.00 12.30           C  
ATOM   2649  CD  GLN A 347      32.839  35.429  17.722  1.00 17.35           C  
ATOM   2650  OE1 GLN A 347      33.870  36.037  17.426  1.00 15.96           O  
ATOM   2651  NE2 GLN A 347      31.891  35.158  16.837  1.00 11.54           N  
ATOM   2652  N   LYS A 348      34.980  35.789  22.921  1.00 12.93           N  
ATOM   2653  CA  LYS A 348      36.121  36.055  23.794  1.00 11.97           C  
ATOM   2654  C   LYS A 348      36.130  35.080  24.972  1.00 13.91           C  
ATOM   2655  O   LYS A 348      37.148  34.451  25.248  1.00 12.97           O  
ATOM   2656  CB  LYS A 348      36.077  37.492  24.315  1.00 10.61           C  
ATOM   2657  CG  LYS A 348      37.210  37.835  25.271  1.00 13.53           C  
ATOM   2658  CD  LYS A 348      37.137  39.276  25.733  1.00 13.97           C  
ATOM   2659  CE  LYS A 348      38.428  39.701  26.416  1.00 16.08           C  
ATOM   2660  NZ  LYS A 348      38.727  38.934  27.651  1.00 11.68           N  
ATOM   2661  N   LEU A 349      34.992  34.949  25.651  1.00 11.29           N  
ATOM   2662  CA  LEU A 349      34.875  34.052  26.800  1.00 11.03           C  
ATOM   2663  C   LEU A 349      35.269  32.622  26.468  1.00 11.94           C  
ATOM   2664  O   LEU A 349      35.996  31.973  27.228  1.00 10.22           O  
ATOM   2665  CB  LEU A 349      33.445  34.068  27.343  1.00 12.24           C  
ATOM   2666  CG  LEU A 349      33.035  35.233  28.240  1.00 12.34           C  
ATOM   2667  CD1 LEU A 349      31.507  35.361  28.246  1.00  5.60           C  
ATOM   2668  CD2 LEU A 349      33.592  35.005  29.652  1.00 11.43           C  
ATOM   2669  N   LEU A 350      34.772  32.132  25.334  1.00 11.36           N  
ATOM   2670  CA  LEU A 350      35.048  30.776  24.872  1.00  9.88           C  
ATOM   2671  C   LEU A 350      36.521  30.613  24.484  1.00 10.42           C  
ATOM   2672  O   LEU A 350      37.146  29.607  24.822  1.00 11.42           O  
ATOM   2673  CB  LEU A 350      34.128  30.416  23.692  1.00  7.43           C  
ATOM   2674  CG  LEU A 350      34.163  28.981  23.154  1.00  6.06           C  
ATOM   2675  CD1 LEU A 350      33.810  27.982  24.251  1.00  6.73           C  
ATOM   2676  CD2 LEU A 350      33.205  28.844  21.980  1.00  7.36           C  
ATOM   2677  N   GLN A 351      37.081  31.603  23.794  1.00 12.88           N  
ATOM   2678  CA  GLN A 351      38.494  31.541  23.400  1.00 15.72           C  
ATOM   2679  C   GLN A 351      39.401  31.578  24.618  1.00 13.42           C  
ATOM   2680  O   GLN A 351      40.371  30.819  24.710  1.00 13.35           O  
ATOM   2681  CB  GLN A 351      38.870  32.703  22.497  1.00 18.20           C  
ATOM   2682  CG  GLN A 351      38.221  32.666  21.146  1.00 32.49           C  
ATOM   2683  CD  GLN A 351      38.931  33.560  20.163  1.00 37.78           C  
ATOM   2684  OE1 GLN A 351      38.389  33.879  19.100  1.00 43.48           O  
ATOM   2685  NE2 GLN A 351      40.098  34.044  20.541  1.00 40.87           N  
ATOM   2686  N   ASP A 352      39.106  32.505  25.524  1.00 13.41           N  
ATOM   2687  CA  ASP A 352      39.875  32.660  26.754  1.00 12.37           C  
ATOM   2688  C   ASP A 352      39.854  31.340  27.509  1.00 13.07           C  
ATOM   2689  O   ASP A 352      40.895  30.838  27.932  1.00 12.24           O  
ATOM   2690  CB  ASP A 352      39.294  33.793  27.611  1.00  9.00           C  
ATOM   2691  CG  ASP A 352      39.561  35.172  27.021  1.00 10.38           C  
ATOM   2692  OD1 ASP A 352      40.242  35.270  25.975  1.00 13.87           O  
ATOM   2693  OD2 ASP A 352      39.103  36.171  27.606  1.00 11.49           O  
ATOM   2694  N   PHE A 353      38.672  30.744  27.616  1.00 10.95           N  
ATOM   2695  CA  PHE A 353      38.543  29.469  28.292  1.00 12.79           C  
ATOM   2696  C   PHE A 353      39.429  28.425  27.614  1.00 13.06           C  
ATOM   2697  O   PHE A 353      40.033  27.591  28.281  1.00 12.47           O  
ATOM   2698  CB  PHE A 353      37.091  28.993  28.290  1.00 11.38           C  
ATOM   2699  CG  PHE A 353      36.888  27.702  29.020  1.00 12.93           C  
ATOM   2700  CD1 PHE A 353      36.801  27.683  30.410  1.00 14.81           C  
ATOM   2701  CD2 PHE A 353      36.810  26.501  28.323  1.00 10.10           C  
ATOM   2702  CE1 PHE A 353      36.643  26.486  31.089  1.00 15.71           C  
ATOM   2703  CE2 PHE A 353      36.654  25.301  28.992  1.00 12.33           C  
ATOM   2704  CZ  PHE A 353      36.569  25.288  30.376  1.00 13.45           C  
ATOM   2705  N   PHE A 354      39.491  28.458  26.287  1.00 13.51           N  
ATOM   2706  CA  PHE A 354      40.320  27.507  25.556  1.00 12.98           C  
ATOM   2707  C   PHE A 354      41.730  28.020  25.329  1.00 12.95           C  
ATOM   2708  O   PHE A 354      42.425  27.596  24.399  1.00 13.66           O  
ATOM   2709  CB  PHE A 354      39.657  27.074  24.249  1.00 10.50           C  
ATOM   2710  CG  PHE A 354      38.678  25.959  24.430  1.00 10.53           C  
ATOM   2711  CD1 PHE A 354      39.124  24.650  24.581  1.00 12.35           C  
ATOM   2712  CD2 PHE A 354      37.312  26.216  24.500  1.00 10.69           C  
ATOM   2713  CE1 PHE A 354      38.225  23.608  24.805  1.00 13.41           C  
ATOM   2714  CE2 PHE A 354      36.403  25.181  24.724  1.00  8.00           C  
ATOM   2715  CZ  PHE A 354      36.859  23.876  24.878  1.00 10.87           C  
ATOM   2716  N   ASN A 355      42.118  28.969  26.176  1.00 12.76           N  
ATOM   2717  CA  ASN A 355      43.445  29.563  26.170  1.00 13.46           C  
ATOM   2718  C   ASN A 355      43.954  30.094  24.829  1.00 13.83           C  
ATOM   2719  O   ASN A 355      45.093  29.831  24.451  1.00 15.55           O  
ATOM   2720  CB  ASN A 355      44.440  28.560  26.775  1.00 12.08           C  
ATOM   2721  CG  ASN A 355      44.076  28.164  28.202  1.00 10.52           C  
ATOM   2722  OD1 ASN A 355      43.724  29.013  29.020  1.00 13.15           O  
ATOM   2723  ND2 ASN A 355      44.155  26.878  28.499  1.00 12.17           N  
ATOM   2724  N   GLY A 356      43.115  30.836  24.114  1.00 13.00           N  
ATOM   2725  CA  GLY A 356      43.532  31.409  22.842  1.00 11.94           C  
ATOM   2726  C   GLY A 356      43.276  30.616  21.573  1.00 13.42           C  
ATOM   2727  O   GLY A 356      43.576  31.098  20.479  1.00 13.92           O  
ATOM   2728  N   LYS A 357      42.706  29.422  21.701  1.00 15.46           N  
ATOM   2729  CA  LYS A 357      42.404  28.577  20.545  1.00 15.67           C  
ATOM   2730  C   LYS A 357      41.469  29.296  19.572  1.00 17.10           C  
ATOM   2731  O   LYS A 357      40.561  30.016  19.991  1.00 17.02           O  
ATOM   2732  CB  LYS A 357      41.751  27.274  21.001  1.00 17.20           C  
ATOM   2733  CG  LYS A 357      41.221  26.408  19.861  1.00 20.87           C  
ATOM   2734  CD  LYS A 357      42.098  25.203  19.614  1.00 28.03           C  
ATOM   2735  CE  LYS A 357      41.546  24.327  18.500  1.00 32.39           C  
ATOM   2736  NZ  LYS A 357      41.958  24.804  17.145  1.00 36.31           N  
ATOM   2737  N   GLU A 358      41.707  29.120  18.276  1.00 17.10           N  
ATOM   2738  CA  GLU A 358      40.869  29.754  17.263  1.00 18.32           C  
ATOM   2739  C   GLU A 358      39.557  29.014  17.093  1.00 15.11           C  
ATOM   2740  O   GLU A 358      39.501  27.789  17.189  1.00 16.45           O  
ATOM   2741  CB  GLU A 358      41.599  29.858  15.919  1.00 22.13           C  
ATOM   2742  CG  GLU A 358      42.832  30.763  15.939  1.00 32.09           C  
ATOM   2743  CD  GLU A 358      42.513  32.245  16.118  1.00 38.14           C  
ATOM   2744  OE1 GLU A 358      41.497  32.591  16.749  1.00 45.77           O  
ATOM   2745  OE2 GLU A 358      43.295  33.082  15.626  1.00 43.21           O  
ATOM   2746  N   LEU A 359      38.501  29.775  16.839  1.00 16.15           N  
ATOM   2747  CA  LEU A 359      37.168  29.226  16.666  1.00 14.61           C  
ATOM   2748  C   LEU A 359      36.768  29.150  15.194  1.00 16.68           C  
ATOM   2749  O   LEU A 359      37.079  30.051  14.401  1.00 18.32           O  
ATOM   2750  CB  LEU A 359      36.154  30.107  17.399  1.00 14.64           C  
ATOM   2751  CG  LEU A 359      36.505  30.624  18.800  1.00 13.19           C  
ATOM   2752  CD1 LEU A 359      35.431  31.593  19.266  1.00 12.49           C  
ATOM   2753  CD2 LEU A 359      36.669  29.473  19.782  1.00  7.44           C  
ATOM   2754  N   ASN A 360      36.097  28.061  14.831  1.00 17.93           N  
ATOM   2755  CA  ASN A 360      35.596  27.873  13.473  1.00 17.23           C  
ATOM   2756  C   ASN A 360      34.325  28.707  13.429  1.00 15.20           C  
ATOM   2757  O   ASN A 360      33.306  28.327  14.009  1.00 14.05           O  
ATOM   2758  CB  ASN A 360      35.256  26.407  13.218  1.00 16.64           C  
ATOM   2759  CG  ASN A 360      36.483  25.560  12.962  1.00 20.50           C  
ATOM   2760  OD1 ASN A 360      36.531  24.792  12.006  1.00 23.20           O  
ATOM   2761  ND2 ASN A 360      37.484  25.688  13.819  1.00 22.39           N  
ATOM   2762  N   LYS A 361      34.395  29.855  12.767  1.00 14.89           N  
ATOM   2763  CA  LYS A 361      33.254  30.756  12.691  1.00 15.79           C  
ATOM   2764  C   LYS A 361      33.103  31.452  11.338  1.00 15.73           C  
ATOM   2765  O   LYS A 361      32.420  32.473  11.247  1.00 18.61           O  
ATOM   2766  CB  LYS A 361      33.384  31.812  13.794  1.00 16.32           C  
ATOM   2767  CG  LYS A 361      34.567  32.757  13.625  1.00 14.77           C  
ATOM   2768  CD  LYS A 361      34.724  33.660  14.827  1.00 19.21           C  
ATOM   2769  CE  LYS A 361      35.602  34.859  14.517  1.00 21.95           C  
ATOM   2770  NZ  LYS A 361      36.964  34.493  14.063  1.00 20.13           N  
ATOM   2771  N   SER A 362      33.719  30.903  10.292  1.00 12.91           N  
ATOM   2772  CA  SER A 362      33.644  31.503   8.962  1.00 10.48           C  
ATOM   2773  C   SER A 362      32.262  31.343   8.332  1.00 10.23           C  
ATOM   2774  O   SER A 362      31.877  32.125   7.472  1.00 11.63           O  
ATOM   2775  CB  SER A 362      34.723  30.923   8.048  1.00  7.39           C  
ATOM   2776  OG  SER A 362      34.830  29.519   8.222  1.00 10.56           O  
ATOM   2777  N   ILE A 363      31.538  30.302   8.729  1.00 11.58           N  
ATOM   2778  CA  ILE A 363      30.188  30.074   8.226  1.00 11.38           C  
ATOM   2779  C   ILE A 363      29.254  30.688   9.271  1.00 12.50           C  
ATOM   2780  O   ILE A 363      29.402  30.399  10.466  1.00 10.80           O  
ATOM   2781  CB  ILE A 363      29.869  28.566   8.116  1.00 10.69           C  
ATOM   2782  CG1 ILE A 363      30.825  27.878   7.140  1.00  9.05           C  
ATOM   2783  CG2 ILE A 363      28.417  28.370   7.687  1.00 10.97           C  
ATOM   2784  CD1 ILE A 363      30.689  26.355   7.091  1.00  8.06           C  
ATOM   2785  N   ASN A 364      28.344  31.564   8.842  1.00 11.88           N  
ATOM   2786  CA  ASN A 364      27.392  32.195   9.766  1.00 11.19           C  
ATOM   2787  C   ASN A 364      26.869  31.116  10.696  1.00  8.79           C  
ATOM   2788  O   ASN A 364      26.289  30.129  10.242  1.00  8.31           O  
ATOM   2789  CB  ASN A 364      26.231  32.845   9.009  1.00 13.13           C  
ATOM   2790  CG  ASN A 364      26.513  34.284   8.635  1.00 15.34           C  
ATOM   2791  OD1 ASN A 364      27.412  34.916   9.186  1.00 16.32           O  
ATOM   2792  ND2 ASN A 364      25.722  34.823   7.721  1.00 14.84           N  
ATOM   2793  N   PRO A 365      27.113  31.266  12.014  1.00  8.60           N  
ATOM   2794  CA  PRO A 365      26.688  30.303  13.038  1.00  9.13           C  
ATOM   2795  C   PRO A 365      25.226  29.893  12.960  1.00  8.22           C  
ATOM   2796  O   PRO A 365      24.883  28.723  13.160  1.00 10.72           O  
ATOM   2797  CB  PRO A 365      27.035  31.023  14.338  1.00  6.05           C  
ATOM   2798  CG  PRO A 365      28.275  31.761  13.961  1.00  8.77           C  
ATOM   2799  CD  PRO A 365      27.868  32.369  12.632  1.00  8.72           C  
ATOM   2800  N   ASP A 366      24.364  30.854  12.670  1.00 10.69           N  
ATOM   2801  CA  ASP A 366      22.933  30.584  12.535  1.00 12.38           C  
ATOM   2802  C   ASP A 366      22.574  29.850  11.224  1.00 11.73           C  
ATOM   2803  O   ASP A 366      21.415  29.502  10.993  1.00 13.45           O  
ATOM   2804  CB  ASP A 366      22.109  31.878  12.715  1.00  9.52           C  
ATOM   2805  CG  ASP A 366      22.630  33.058  11.891  1.00 13.50           C  
ATOM   2806  OD1 ASP A 366      23.848  33.166  11.624  1.00 16.19           O  
ATOM   2807  OD2 ASP A 366      21.808  33.926  11.544  1.00 12.10           O  
ATOM   2808  N   GLU A 367      23.583  29.576  10.400  1.00 10.82           N  
ATOM   2809  CA  GLU A 367      23.395  28.883   9.129  1.00  8.95           C  
ATOM   2810  C   GLU A 367      24.173  27.573   9.042  1.00  8.49           C  
ATOM   2811  O   GLU A 367      23.920  26.761   8.153  1.00  8.19           O  
ATOM   2812  CB  GLU A 367      23.826  29.784   7.973  1.00  8.86           C  
ATOM   2813  CG  GLU A 367      23.045  31.075   7.870  1.00  9.67           C  
ATOM   2814  CD  GLU A 367      23.678  32.074   6.940  1.00 11.90           C  
ATOM   2815  OE1 GLU A 367      24.504  31.685   6.085  1.00 13.89           O  
ATOM   2816  OE2 GLU A 367      23.347  33.265   7.071  1.00 11.93           O  
ATOM   2817  N   ALA A 368      25.118  27.374   9.961  1.00  9.80           N  
ATOM   2818  CA  ALA A 368      25.964  26.179   9.973  1.00  7.55           C  
ATOM   2819  C   ALA A 368      25.212  24.847   9.944  1.00  9.39           C  
ATOM   2820  O   ALA A 368      25.630  23.900   9.261  1.00  6.24           O  
ATOM   2821  CB  ALA A 368      26.919  26.229  11.158  1.00 10.55           C  
ATOM   2822  N   VAL A 369      24.111  24.763  10.688  1.00 10.18           N  
ATOM   2823  CA  VAL A 369      23.312  23.539  10.725  1.00  7.10           C  
ATOM   2824  C   VAL A 369      22.675  23.250   9.355  1.00  7.70           C  
ATOM   2825  O   VAL A 369      22.761  22.128   8.843  1.00  9.00           O  
ATOM   2826  CB  VAL A 369      22.227  23.607  11.838  1.00  7.40           C  
ATOM   2827  CG1 VAL A 369      21.291  22.423  11.732  1.00  7.28           C  
ATOM   2828  CG2 VAL A 369      22.894  23.603  13.221  1.00  6.06           C  
ATOM   2829  N   ALA A 370      22.050  24.259   8.758  1.00  7.62           N  
ATOM   2830  CA  ALA A 370      21.425  24.094   7.445  1.00  9.58           C  
ATOM   2831  C   ALA A 370      22.473  23.765   6.378  1.00 10.56           C  
ATOM   2832  O   ALA A 370      22.239  22.952   5.477  1.00 12.07           O  
ATOM   2833  CB  ALA A 370      20.684  25.352   7.067  1.00  8.85           C  
ATOM   2834  N   TYR A 371      23.622  24.427   6.487  1.00 10.92           N  
ATOM   2835  CA  TYR A 371      24.749  24.257   5.575  1.00  9.86           C  
ATOM   2836  C   TYR A 371      25.162  22.787   5.556  1.00  9.74           C  
ATOM   2837  O   TYR A 371      25.199  22.152   4.496  1.00 11.28           O  
ATOM   2838  CB  TYR A 371      25.901  25.151   6.055  1.00 10.52           C  
ATOM   2839  CG  TYR A 371      27.051  25.362   5.091  1.00  7.65           C  
ATOM   2840  CD1 TYR A 371      27.886  24.307   4.727  1.00 10.88           C  
ATOM   2841  CD2 TYR A 371      27.347  26.636   4.607  1.00  7.37           C  
ATOM   2842  CE1 TYR A 371      28.993  24.513   3.914  1.00  8.80           C  
ATOM   2843  CE2 TYR A 371      28.451  26.858   3.792  1.00  7.35           C  
ATOM   2844  CZ  TYR A 371      29.270  25.786   3.452  1.00 10.45           C  
ATOM   2845  OH  TYR A 371      30.368  25.982   2.647  1.00 10.82           O  
ATOM   2846  N   GLY A 372      25.420  22.238   6.740  1.00 11.20           N  
ATOM   2847  CA  GLY A 372      25.815  20.845   6.853  1.00 11.09           C  
ATOM   2848  C   GLY A 372      24.731  19.894   6.389  1.00 11.97           C  
ATOM   2849  O   GLY A 372      25.015  18.865   5.769  1.00 10.73           O  
ATOM   2850  N   ALA A 373      23.483  20.235   6.695  1.00 12.14           N  
ATOM   2851  CA  ALA A 373      22.349  19.416   6.295  1.00 10.14           C  
ATOM   2852  C   ALA A 373      22.269  19.368   4.768  1.00 11.10           C  
ATOM   2853  O   ALA A 373      22.038  18.307   4.196  1.00 10.23           O  
ATOM   2854  CB  ALA A 373      21.059  19.970   6.889  1.00  7.81           C  
ATOM   2855  N   ALA A 374      22.510  20.508   4.119  1.00  9.47           N  
ATOM   2856  CA  ALA A 374      22.482  20.610   2.659  1.00  9.10           C  
ATOM   2857  C   ALA A 374      23.560  19.720   2.036  1.00 14.34           C  
ATOM   2858  O   ALA A 374      23.334  19.069   1.006  1.00 12.47           O  
ATOM   2859  CB  ALA A 374      22.682  22.047   2.241  1.00  6.70           C  
ATOM   2860  N   VAL A 375      24.733  19.688   2.667  1.00 15.39           N  
ATOM   2861  CA  VAL A 375      25.840  18.856   2.203  1.00 15.19           C  
ATOM   2862  C   VAL A 375      25.447  17.380   2.326  1.00 16.31           C  
ATOM   2863  O   VAL A 375      25.552  16.619   1.367  1.00 17.01           O  
ATOM   2864  CB  VAL A 375      27.127  19.115   3.029  1.00 17.50           C  
ATOM   2865  CG1 VAL A 375      28.213  18.114   2.651  1.00 19.51           C  
ATOM   2866  CG2 VAL A 375      27.624  20.536   2.802  1.00 17.06           C  
ATOM   2867  N   GLN A 376      24.948  16.989   3.493  1.00 15.18           N  
ATOM   2868  CA  GLN A 376      24.550  15.607   3.718  1.00 14.80           C  
ATOM   2869  C   GLN A 376      23.405  15.175   2.796  1.00 15.03           C  
ATOM   2870  O   GLN A 376      23.377  14.040   2.325  1.00 17.29           O  
ATOM   2871  CB  GLN A 376      24.173  15.394   5.189  1.00 17.16           C  
ATOM   2872  CG  GLN A 376      24.150  13.936   5.625  1.00 17.53           C  
ATOM   2873  CD  GLN A 376      25.450  13.204   5.306  1.00 20.74           C  
ATOM   2874  OE1 GLN A 376      25.446  11.998   5.061  1.00 23.15           O  
ATOM   2875  NE2 GLN A 376      26.561  13.926   5.302  1.00 18.95           N  
ATOM   2876  N   ALA A 377      22.471  16.080   2.526  1.00 14.91           N  
ATOM   2877  CA  ALA A 377      21.344  15.769   1.653  1.00 14.91           C  
ATOM   2878  C   ALA A 377      21.865  15.424   0.269  1.00 17.61           C  
ATOM   2879  O   ALA A 377      21.402  14.470  -0.357  1.00 17.87           O  
ATOM   2880  CB  ALA A 377      20.385  16.951   1.574  1.00 12.51           C  
ATOM   2881  N   ALA A 378      22.851  16.190  -0.189  1.00 18.82           N  
ATOM   2882  CA  ALA A 378      23.451  15.969  -1.499  1.00 20.80           C  
ATOM   2883  C   ALA A 378      24.085  14.586  -1.525  1.00 22.21           C  
ATOM   2884  O   ALA A 378      23.886  13.823  -2.465  1.00 24.64           O  
ATOM   2885  CB  ALA A 378      24.493  17.032  -1.785  1.00 19.19           C  
ATOM   2886  N   ILE A 379      24.811  14.260  -0.463  1.00 23.84           N  
ATOM   2887  CA  ILE A 379      25.476  12.969  -0.335  1.00 23.16           C  
ATOM   2888  C   ILE A 379      24.470  11.812  -0.364  1.00 24.46           C  
ATOM   2889  O   ILE A 379      24.728  10.774  -0.967  1.00 25.12           O  
ATOM   2890  CB  ILE A 379      26.306  12.909   0.967  1.00 21.90           C  
ATOM   2891  CG1 ILE A 379      27.358  14.020   0.961  1.00 23.78           C  
ATOM   2892  CG2 ILE A 379      26.987  11.564   1.101  1.00 25.56           C  
ATOM   2893  CD1 ILE A 379      28.149  14.144   2.247  1.00 23.03           C  
ATOM   2894  N   LEU A 380      23.324  11.999   0.281  1.00 25.80           N  
ATOM   2895  CA  LEU A 380      22.292  10.968   0.328  1.00 27.54           C  
ATOM   2896  C   LEU A 380      21.461  10.857  -0.953  1.00 31.86           C  
ATOM   2897  O   LEU A 380      20.757   9.865  -1.146  1.00 34.38           O  
ATOM   2898  CB  LEU A 380      21.352  11.206   1.512  1.00 23.71           C  
ATOM   2899  CG  LEU A 380      21.933  11.182   2.924  1.00 21.41           C  
ATOM   2900  CD1 LEU A 380      20.857  11.556   3.910  1.00 21.09           C  
ATOM   2901  CD2 LEU A 380      22.490   9.815   3.247  1.00 22.44           C  
ATOM   2902  N   SER A 381      21.517  11.877  -1.804  1.00 35.89           N  
ATOM   2903  CA  SER A 381      20.747  11.886  -3.047  1.00 40.49           C  
ATOM   2904  C   SER A 381      21.325  11.009  -4.154  1.00 42.78           C  
ATOM   2905  O   SER A 381      20.512  10.516  -4.969  1.00 44.44           O  
ATOM   2906  CB  SER A 381      20.580  13.316  -3.566  1.00 41.34           C  
ATOM   2907  OG  SER A 381      19.740  14.069  -2.713  1.00 43.54           O  
TER    2908      SER A 381                                                      
HETATM 2909 MG    MG A 487      19.779  26.148  16.146  1.00 11.80          MG  
HETATM 2910  P   PO4 A 488      17.751  24.745  18.374  1.00 13.17           P  
HETATM 2911  O1  PO4 A 488      18.183  23.338  18.609  1.00 15.51           O  
HETATM 2912  O2  PO4 A 488      18.922  25.587  18.035  1.00 11.81           O  
HETATM 2913  O3  PO4 A 488      16.801  24.802  17.233  1.00 13.88           O  
HETATM 2914  O4  PO4 A 488      17.155  25.294  19.597  1.00 12.45           O  
HETATM 2915 NA    NA A 490      18.250  27.722  13.513  1.00 10.32          NA  
HETATM 2916 CL    CL A 451      35.728  25.274   6.095  1.00 23.83          CL  
HETATM 2917 CL    CL A 455       9.348  34.088   2.809  1.00 12.53          CL  
HETATM 2918  PB  ADP A 486      17.839  28.764  16.634  1.00 10.18           P  
HETATM 2919  O1B ADP A 486      18.573  29.017  17.907  1.00 13.52           O  
HETATM 2920  O2B ADP A 486      18.343  27.591  15.882  1.00 12.46           O  
HETATM 2921  O3B ADP A 486      16.362  28.799  16.755  1.00 13.86           O  
HETATM 2922  PA  ADP A 486      19.457  30.890  15.344  1.00 10.10           P  
HETATM 2923  O1A ADP A 486      20.644  30.007  15.388  1.00  9.48           O  
HETATM 2924  O2A ADP A 486      19.155  31.613  14.090  1.00 12.50           O  
HETATM 2925  O3A ADP A 486      18.135  30.081  15.810  1.00 12.21           O  
HETATM 2926  O5' ADP A 486      19.661  31.940  16.490  1.00 10.93           O  
HETATM 2927  C5' ADP A 486      18.654  32.891  16.773  1.00  9.23           C  
HETATM 2928  C4' ADP A 486      19.202  33.875  17.800  1.00 11.04           C  
HETATM 2929  O4' ADP A 486      20.398  34.501  17.291  1.00 11.84           O  
HETATM 2930  C3' ADP A 486      18.202  34.976  18.101  1.00  8.86           C  
HETATM 2931  O3' ADP A 486      18.221  35.189  19.521  1.00  9.74           O  
HETATM 2932  C2' ADP A 486      18.794  36.123  17.326  1.00 10.50           C  
HETATM 2933  O2' ADP A 486      18.374  37.390  17.885  1.00 13.10           O  
HETATM 2934  C1' ADP A 486      20.297  35.896  17.528  1.00 11.31           C  
HETATM 2935  N9  ADP A 486      21.161  36.568  16.539  1.00 13.66           N  
HETATM 2936  C8  ADP A 486      21.095  36.530  15.146  1.00 11.64           C  
HETATM 2937  N7  ADP A 486      22.060  37.203  14.563  1.00 11.89           N  
HETATM 2938  C5  ADP A 486      22.805  37.720  15.618  1.00 12.91           C  
HETATM 2939  C6  ADP A 486      23.941  38.534  15.634  1.00 11.05           C  
HETATM 2940  N6  ADP A 486      24.457  39.028  14.518  1.00 11.92           N  
HETATM 2941  N1  ADP A 486      24.429  38.871  16.827  1.00 10.62           N  
HETATM 2942  C2  ADP A 486      23.818  38.432  17.941  1.00 11.07           C  
HETATM 2943  N3  ADP A 486      22.743  37.676  18.074  1.00 11.32           N  
HETATM 2944  C4  ADP A 486      22.275  37.345  16.835  1.00 13.18           C  
HETATM 2945  O   HOH A 504       9.680  26.083  17.515  1.00  7.90           O  
HETATM 2946  O   HOH A 505      17.147  30.036   4.716  1.00  7.70           O  
HETATM 2947  O   HOH A 506      14.019  36.521   9.320  1.00  9.71           O  
HETATM 2948  O   HOH A 507      10.059  29.967  19.097  1.00 13.01           O  
HETATM 2949  O   HOH A 508      25.554  30.186   0.532  1.00 11.69           O  
HETATM 2950  O   HOH A 510      35.887  20.692  35.435  1.00 43.71           O  
HETATM 2951  O   HOH A 511      30.563  22.305  35.656  1.00 20.14           O  
HETATM 2952  O   HOH A 512      -8.916  35.831  19.047  1.00 35.39           O  
HETATM 2953  O   HOH A 513      14.261  20.232  14.558  1.00  9.45           O  
HETATM 2954  O   HOH A 514      17.185  21.845  13.395  1.00  7.76           O  
HETATM 2955  O   HOH A 515      10.337  18.523  22.153  1.00 10.08           O  
HETATM 2956  O   HOH A 517      -2.563  13.231  29.962  1.00 33.14           O  
HETATM 2957  O   HOH A 518      -5.210  18.359  14.410  1.00 18.08           O  
HETATM 2958  O   HOH A 520      14.139  17.319  -3.863  1.00 16.59           O  
HETATM 2959  O   HOH A 521      16.384   9.116  10.000  1.00 13.42           O  
HETATM 2960  O   HOH A 522      23.498  12.573  13.266  1.00 15.55           O  
HETATM 2961  O   HOH A 524      36.017  21.186   3.503  1.00 22.24           O  
HETATM 2962  O   HOH A 525      10.538  24.523  15.139  1.00  7.61           O  
HETATM 2963  O   HOH A 526      42.799  11.306   4.455  1.00 20.71           O  
HETATM 2964  O   HOH A 527      24.477  28.115  31.643  1.00 52.62           O  
HETATM 2965  O   HOH A 529      11.839  39.757  19.389  1.00 21.88           O  
HETATM 2966  O   HOH A 530       1.881  52.330  18.558  1.00 32.50           O  
HETATM 2967  O   HOH A 532      30.033  41.592  22.597  1.00 14.92           O  
HETATM 2968  O   HOH A 533      40.464  20.828  30.842  1.00 26.50           O  
HETATM 2969  O   HOH A 534      24.555  52.511  26.713  1.00 15.04           O  
HETATM 2970  O   HOH A 535      38.597  25.520  16.317  1.00 21.89           O  
HETATM 2971  O   HOH A 536      30.229  28.728  12.428  1.00 17.21           O  
HETATM 2972  O   HOH A 537      36.963  35.859  29.302  1.00  8.39           O  
HETATM 2973  O   HOH A 538      38.822  32.834  16.718  1.00 18.43           O  
HETATM 2974  O   HOH A 539      36.976  35.873  17.801  1.00 28.34           O  
HETATM 2975  O   HOH A 540      41.397  29.559  30.879  1.00 13.43           O  
HETATM 2976  O   HOH A 541      46.539  28.205  22.577  1.00 16.91           O  
HETATM 2977  O   HOH A 544      25.692  41.477  20.076  1.00  9.05           O  
HETATM 2978  O   HOH A 545      17.590  27.919  20.018  1.00  7.42           O  
HETATM 2979  O   HOH A 546      24.189  22.058  17.936  1.00 15.94           O  
HETATM 2980  O   HOH A 547      21.534  36.689  20.775  1.00 15.03           O  
HETATM 2981  O   HOH A 548       0.406  27.692  27.186  1.00 14.12           O  
HETATM 2982  O   HOH A 549      16.452  48.693  16.946  1.00 23.73           O  
HETATM 2983  O   HOH A 550      25.881  21.638  20.152  1.00  7.86           O  
HETATM 2984  O   HOH A 552      29.981  25.100   0.173  1.00 18.89           O  
HETATM 2985  O   HOH A 553      12.734  29.646  22.945  1.00 13.64           O  
HETATM 2986  O   HOH A 554      33.493  43.949  28.853  1.00 24.80           O  
HETATM 2987  O   HOH A 555       9.714  21.616  15.440  1.00  6.66           O  
HETATM 2988  O   HOH A 556       7.319  26.976  16.371  1.00  9.76           O  
HETATM 2989  O   HOH A 558      18.853  29.544  12.224  1.00  6.43           O  
HETATM 2990  O   HOH A 559      13.046  38.359  21.501  1.00 19.66           O  
HETATM 2991  O   HOH A 560      20.962  27.489  17.382  1.00  8.69           O  
HETATM 2992  O   HOH A 561      21.071  24.568  16.285  1.00 13.36           O  
HETATM 2993  O   HOH A 562      18.558  24.808  15.184  1.00  9.23           O  
HETATM 2994  O   HOH A 563      20.789  27.006  14.448  1.00  7.89           O  
HETATM 2995  O   HOH A 564      19.083  33.785  12.646  1.00 13.84           O  
HETATM 2996  O   HOH A 568      21.623  19.971  -0.812  1.00 13.01           O  
HETATM 2997  O   HOH A 569      11.704  19.581  15.427  1.00 12.09           O  
HETATM 2998  O   HOH A 570       8.000  24.894  14.421  1.00  8.95           O  
HETATM 2999  O   HOH A 571      29.343  29.975   1.510  1.00 15.27           O  
HETATM 3000  O   HOH A 572      15.330  32.006   5.310  1.00  9.15           O  
HETATM 3001  O   HOH A 573      22.839  26.819  12.562  1.00  6.10           O  
HETATM 3002  O   HOH A 574       0.651  34.192   4.051  1.00 70.74           O  
HETATM 3003  O   HOH A 575      -4.947  38.794   8.699  1.00 16.15           O  
HETATM 3004  O   HOH A 576       2.395  35.005  20.495  1.00 18.38           O  
HETATM 3005  O   HOH A 577      -4.350  30.541  22.020  1.00 13.77           O  
HETATM 3006  O   HOH A 578      -4.211  37.825  20.316  1.00 22.51           O  
HETATM 3007  O   HOH A 580      19.984  22.759  25.360  1.00 11.99           O  
HETATM 3008  O   HOH A 581      15.436  30.780  26.517  1.00 13.70           O  
HETATM 3009  O   HOH A 582       3.673  50.240  21.481  1.00 27.28           O  
HETATM 3010  O   HOH A 583      28.335  37.216   8.195  1.00 16.90           O  
HETATM 3011  O   HOH A 584      29.816  35.276  12.596  1.00 64.18           O  
HETATM 3012  O   HOH A 585      43.203  31.588  29.244  1.00 20.11           O  
HETATM 3013  O   HOH A 586      10.611  32.446  19.749  1.00 22.75           O  
HETATM 3014  O   HOH A 587      16.106  36.549  20.161  1.00 15.53           O  
HETATM 3015  O   HOH A 590      21.869  34.674   8.707  1.00 12.56           O  
HETATM 3016  O   HOH A 591      21.650  36.342   1.057  1.00 12.61           O  
HETATM 3017  O   HOH A 592      14.060  32.034  -2.323  1.00 17.83           O  
HETATM 3018  O   HOH A 593      -2.554  40.426  12.765  1.00 21.88           O  
HETATM 3019  O   HOH A 594      17.926  10.410  13.679  1.00 18.54           O  
HETATM 3020  O   HOH A 596      20.339  20.561  27.024  1.00 27.19           O  
HETATM 3021  O   HOH A 597      17.659  18.601  27.788  1.00 72.20           O  
HETATM 3022  O   HOH A 598      14.376  14.117  25.063  1.00 39.42           O  
HETATM 3023  O   HOH A 599      12.374  33.704  16.547  1.00 27.96           O  
HETATM 3024  O   HOH A 602      11.081  38.725  11.015  1.00 25.18           O  
HETATM 3025  O   HOH A 606      31.849  20.691   3.890  1.00 28.02           O  
HETATM 3026  O   HOH A 609      26.895  30.187   5.241  1.00 12.09           O  
HETATM 3027  O   HOH A 611      19.435  32.641  -1.884  1.00 19.18           O  
HETATM 3028  O   HOH A 612       9.098  34.234   6.038  1.00  8.15           O  
HETATM 3029  O   HOH A 613      15.853  41.746   4.935  1.00 57.55           O  
HETATM 3030  O   HOH A 614      24.161  38.159   3.295  1.00 26.74           O  
HETATM 3031  O   HOH A 615      19.644  37.556   6.223  1.00 17.54           O  
HETATM 3032  O   HOH A 617      16.421  37.838   9.865  1.00 45.45           O  
HETATM 3033  O   HOH A 618      18.366  36.145   8.924  1.00 23.29           O  
HETATM 3034  O   HOH A 620       6.848  36.264  20.946  1.00 25.75           O  
HETATM 3035  O   HOH A 625       6.904  47.655   5.782  1.00 31.10           O  
HETATM 3036  O   HOH A 627       7.770  45.207  16.533  1.00 24.52           O  
HETATM 3037  O   HOH A 632       7.931  40.243   1.211  1.00 23.97           O  
HETATM 3038  O   HOH A 633       4.426  41.783   7.460  1.00 33.11           O  
HETATM 3039  O   HOH A 635      -1.664  42.781  23.100  1.00 15.25           O  
HETATM 3040  O   HOH A 636      -2.243  47.071  22.745  1.00 28.54           O  
HETATM 3041  O   HOH A 638      -6.646  42.572  14.781  1.00 19.29           O  
HETATM 3042  O   HOH A 645      -9.394  17.510  17.329  1.00100.00           O  
HETATM 3043  O   HOH A 651      14.236   7.186  22.356  1.00 26.34           O  
HETATM 3044  O   HOH A 653      10.647   8.043  22.451  1.00 16.30           O  
HETATM 3045  O   HOH A 654      25.574  11.841  14.891  1.00 31.29           O  
HETATM 3046  O   HOH A 655      37.808  19.928  -1.261  1.00 67.71           O  
HETATM 3047  O   HOH A 656      32.069  18.043   4.432  1.00 47.80           O  
HETATM 3048  O   HOH A 658      40.146  17.654  10.364  1.00 31.44           O  
HETATM 3049  O   HOH A 659      40.260  21.274   7.816  1.00 23.20           O  
HETATM 3050  O   HOH A 663      45.183  10.752   5.845  1.00 17.56           O  
HETATM 3051  O   HOH A 664      37.049  21.953   0.299  1.00 23.89           O  
HETATM 3052  O   HOH A 665      38.753  15.933   0.083  1.00 15.67           O  
HETATM 3053  O   HOH A 669      24.526  31.186  31.645  1.00 22.29           O  
HETATM 3054  O   HOH A 672      18.598  22.957  30.814  1.00 43.83           O  
HETATM 3055  O   HOH A 673      25.192  20.543  37.518  1.00 29.13           O  
HETATM 3056  O   HOH A 678      18.529  44.165  32.656  1.00 14.10           O  
HETATM 3057  O   HOH A 679      20.995  43.231  33.665  1.00 16.83           O  
HETATM 3058  O   HOH A 680      22.565  45.028  35.232  1.00 39.21           O  
HETATM 3059  O   HOH A 681      19.757  48.383  33.813  1.00 37.53           O  
HETATM 3060  O   HOH A 686      -1.572  49.557  21.620  1.00 33.50           O  
HETATM 3061  O   HOH A 694       9.008  53.110  15.074  1.00 23.55           O  
HETATM 3062  O   HOH A 696      21.801  51.193  14.867  1.00 25.37           O  
HETATM 3063  O   HOH A 697      26.039  42.148  13.116  1.00 21.00           O  
HETATM 3064  O   HOH A 698      27.925  42.646  21.207  1.00 10.88           O  
HETATM 3065  O   HOH A 699      30.663  38.658  15.066  1.00 26.21           O  
HETATM 3066  O   HOH A 700      34.344  42.573  17.711  1.00 60.22           O  
HETATM 3067  O   HOH A 702      31.163  49.985  23.706  1.00 16.12           O  
HETATM 3068  O   HOH A 703      27.282  39.602  13.162  1.00 15.87           O  
HETATM 3069  O   HOH A 705       7.831  43.875   3.584  1.00 43.57           O  
HETATM 3070  O   HOH A 706       1.434  54.840  22.046  1.00 17.84           O  
HETATM 3071  O   HOH A 708      30.562  38.149  30.757  1.00 10.46           O  
HETATM 3072  O   HOH A 712      31.929  36.278  14.162  1.00 19.44           O  
HETATM 3073  O   HOH A 713      38.628  38.284  15.819  1.00 38.97           O  
HETATM 3074  O   HOH A 716      36.184  34.095  10.213  1.00 19.08           O  
HETATM 3075  O   HOH A 717       2.208  40.512   8.905  1.00 25.33           O  
HETATM 3076  O   HOH A 721      10.137  48.083  17.408  1.00 32.74           O  
HETATM 3077  O   HOH A 723      14.624  50.931  16.572  1.00 18.99           O  
HETATM 3078  O   HOH A 724       2.046  49.759  31.888  1.00 38.20           O  
HETATM 3079  O   HOH A 725       8.673  52.385  31.370  1.00 19.58           O  
HETATM 3080  O   HOH A 727      40.071  36.203  23.038  1.00 15.54           O  
HETATM 3081  O   HOH A 728      43.520  21.539  15.458  1.00 40.28           O  
HETATM 3082  O   HOH A 729      44.965  24.409  27.143  1.00 32.79           O  
HETATM 3083  O   HOH A 730      16.798  42.493  34.034  1.00 25.82           O  
HETATM 3084  O   HOH A 731      17.855  46.440  34.079  1.00 21.87           O  
HETATM 3085  O   HOH A 732      12.857  47.738  34.466  1.00 27.33           O  
HETATM 3086  O   HOH A 733      18.070  52.171  32.337  1.00 19.25           O  
HETATM 3087  O   HOH A 734      14.139  54.007  36.384  1.00 28.89           O  
HETATM 3088  O   HOH A 735      13.206  33.324  27.190  1.00 57.32           O  
HETATM 3089  O   HOH A 737      29.836  40.693  29.497  1.00 12.40           O  
HETATM 3090  O   HOH A 738      30.431  52.483  22.452  1.00 51.73           O  
HETATM 3091  O   HOH A 739      19.069  49.074  16.222  1.00 22.49           O  
HETATM 3092  O   HOH A 740      25.677  51.450  14.514  1.00 37.61           O  
HETATM 3093  O   HOH A 741       9.288  11.754   4.816  1.00 17.51           O  
HETATM 3094  O   HOH A 742       4.250  16.292  18.778  1.00 15.92           O  
HETATM 3095  O   HOH A 743      -7.855  34.645  14.750  1.00 16.80           O  
HETATM 3096  O   HOH A 744     -10.384  34.270  14.118  1.00 21.52           O  
HETATM 3097  O   HOH A 745      -7.649  38.830  13.630  1.00  8.99           O  
HETATM 3098  O   HOH A 746      -7.167  39.584   4.884  1.00 25.41           O  
HETATM 3099  O   HOH A 748      -6.610  20.520  13.289  1.00 55.02           O  
HETATM 3100  O   HOH A 750      -6.623  20.738  28.213  1.00 20.84           O  
HETATM 3101  O   HOH A 751       7.154  21.998  26.225  1.00 11.61           O  
HETATM 3102  O   HOH A 752      11.170  23.706  30.694  1.00 37.42           O  
HETATM 3103  O   HOH A 753       9.728  20.775  35.688  1.00 23.80           O  
HETATM 3104  O   HOH A 754      11.550  23.276  26.662  1.00 14.60           O  
HETATM 3105  O   HOH A 755      10.575  30.955  24.786  1.00 48.01           O  
HETATM 3106  O   HOH A 756       0.271  30.961  30.176  1.00 55.51           O  
HETATM 3107  O   HOH A 757       5.723  33.580  32.700  1.00 63.05           O  
HETATM 3108  O   HOH A 758      -2.066  26.816  27.981  1.00 28.29           O  
HETATM 3109  O   HOH A 759      -8.296  19.025  20.737  1.00 28.36           O  
HETATM 3110  O   HOH A 760      -6.153  42.808   5.349  1.00 28.15           O  
HETATM 3111  O   HOH A 761      27.436   9.649  12.317  1.00 49.17           O  
HETATM 3112  O   HOH A 764      18.390  10.088  21.888  1.00 45.39           O  
HETATM 3113  O   HOH A 767      29.034  28.616  -0.923  1.00 16.26           O  
HETATM 3114  O   HOH A 769      12.018  32.963  -1.059  1.00 72.26           O  
HETATM 3115  O   HOH A 770       8.207  28.827  -4.085  1.00 24.30           O  
HETATM 3116  O   HOH A 771       6.750  31.198   0.738  1.00 21.81           O  
HETATM 3117  O   HOH A 772       3.323  32.829   2.963  1.00 84.90           O  
HETATM 3118  O   HOH A 773       4.335  29.227   3.627  1.00 26.25           O  
HETATM 3119  O   HOH A 774       6.598  35.513   5.753  1.00 14.24           O  
HETATM 3120  O   HOH A 775      13.939  35.137  18.557  1.00 44.65           O  
HETATM 3121  O   HOH A 777      37.387  26.693  36.087  1.00 35.09           O  
HETATM 3122  O   HOH A 778      38.201  24.002  33.327  1.00 32.97           O  
HETATM 3123  O   HOH A 779      37.989  22.033  31.514  1.00 32.10           O  
HETATM 3124  O   HOH A 781       6.325  33.115  25.581  1.00 35.27           O  
HETATM 3125  O   HOH A 782      -6.401  37.081  15.499  1.00 58.27           O  
HETATM 3126  O   HOH A 783      -5.117  40.235  13.892  1.00 50.89           O  
HETATM 3127  O   HOH A 785      25.388  21.069 -14.814  1.00 23.01           O  
HETATM 3128  O   HOH A 786       1.595  54.632  32.624  1.00 34.99           O  
HETATM 3129  O   HOH A 787       9.070  26.240  -8.094  1.00 49.76           O  
HETATM 3130  O   HOH A 788       6.473  20.844 -11.088  1.00 17.86           O  
HETATM 3131  O   HOH A 789       3.404  27.360   5.190  1.00 26.14           O  
HETATM 3132  O   HOH A 790      36.250  20.129  32.669  1.00 34.12           O  
HETATM 3133  O   HOH A 791      37.888  18.014  31.954  1.00 38.33           O  
HETATM 3134  O   HOH A 792      20.832  18.721  23.939  1.00 56.03           O  
HETATM 3135  O   HOH A 793      34.784  32.146  34.417  1.00 25.25           O  
HETATM 3136  O   HOH A 794      32.790  31.538  36.792  1.00 73.99           O  
HETATM 3137  O   HOH A 795      41.384  11.128  27.459  1.00 56.90           O  
HETATM 3138  O   HOH A 796      42.204  23.073  22.576  1.00 39.39           O  
HETATM 3139  O   HOH A 797      44.385  28.003  17.567  1.00 34.91           O  
HETATM 3140  O   HOH A 798      25.008  37.965   7.498  1.00 19.85           O  
HETATM 3141  O   HOH A 799      22.978  39.584  11.899  1.00 27.20           O  
HETATM 3142  O   HOH A 800      34.395  37.870  15.364  1.00 52.34           O  
HETATM 3143  O   HOH A 801      35.813  38.983  20.507  1.00 28.38           O  
HETATM 3144  O   HOH A 802      34.579  35.058  33.247  1.00 45.51           O  
HETATM 3145  O   HOH A 803      29.704  31.681  35.824  1.00 24.13           O  
HETATM 3146  O   HOH A 804      33.213  27.525  34.392  1.00 44.05           O  
HETATM 3147  O   HOH A 806      37.888  28.500  33.998  1.00 31.87           O  
HETATM 3148  O   HOH A 810      -5.945  27.584   7.496  1.00 76.52           O  
HETATM 3149  O   HOH A 813      -0.023  53.605  24.369  1.00 38.25           O  
HETATM 3150  O   HOH A 814       1.485  52.181  22.373  1.00 55.33           O  
HETATM 3151  O   HOH A 815       1.291  49.425  22.631  1.00 35.23           O  
HETATM 3152  O   HOH A 816      -3.760  51.070  24.578  1.00 43.38           O  
HETATM 3153  O   HOH A 818      -8.595  18.478  23.314  1.00 37.21           O  
HETATM 3154  O   HOH A 819      13.192  29.816  27.675  1.00 26.60           O  
HETATM 3155  O   HOH A 820       7.366  12.714  29.280  1.00 73.23           O  
HETATM 3156  O   HOH A 821      33.239  25.644  -1.936  1.00 76.62           O  
HETATM 3157  O   HOH A 822      33.727  20.684   1.904  1.00 92.86           O  
HETATM 3158  O   HOH A 823      27.112  30.919   2.714  1.00 10.17           O  
HETATM 3159  O   HOH A 824      23.849  32.170   0.046  1.00 12.17           O  
HETATM 3160  O   HOH A 826      17.973  34.272  -3.732  1.00 25.15           O  
HETATM 3161  O   HOH A 827      15.159  36.785  -1.932  1.00 42.41           O  
HETATM 3162  O   HOH A 830       5.722  34.944   1.493  1.00 35.43           O  
HETATM 3163  O   HOH A 831       6.106  36.897   3.410  1.00 23.28           O  
HETATM 3164  O   HOH A 832       9.981  42.301   1.213  1.00 44.16           O  
HETATM 3165  O   HOH A 833       9.510  41.042   6.871  1.00 25.77           O  
HETATM 3166  O   HOH A 834      22.407  37.175   7.851  1.00 42.64           O  
HETATM 3167  O   HOH A 835       4.205  36.482  21.954  1.00 21.47           O  
HETATM 3168  O   HOH A 836       3.586  39.044  21.541  1.00 21.65           O  
HETATM 3169  O   HOH A 837       4.552  41.703  25.470  1.00 20.64           O  
HETATM 3170  O   HOH A 838       7.086  40.825  24.895  1.00 28.33           O  
HETATM 3171  O   HOH A 839       2.633  40.135  24.027  1.00 15.36           O  
HETATM 3172  O   HOH A 840       0.966  41.824  22.798  1.00 22.11           O  
HETATM 3173  O   HOH A 841       1.514  38.379  25.525  1.00 33.79           O  
HETATM 3174  O   HOH A 842      -1.125  37.602  26.028  1.00 23.08           O  
HETATM 3175  O   HOH A 843      -5.132  40.282  16.624  1.00 39.87           O  
HETATM 3176  O   HOH A 844       1.233  39.595   6.280  1.00 39.31           O  
HETATM 3177  O   HOH A 845     -12.503  40.667  10.362  1.00 27.76           O  
HETATM 3178  O   HOH A 846     -15.342  40.991  10.495  1.00 37.54           O  
HETATM 3179  O   HOH A 847      -7.739  30.618   2.164  1.00 42.51           O  
HETATM 3180  O   HOH A 848      14.100  42.572  15.727  1.00 30.61           O  
HETATM 3181  O   HOH A 849       6.832  43.260  18.088  1.00 67.83           O  
HETATM 3182  O   HOH A 850      -3.339  40.737   9.884  1.00 43.48           O  
HETATM 3183  O   HOH A 852       2.323  49.128  14.483  1.00 54.75           O  
HETATM 3184  O   HOH A 853      -7.158  31.643  20.955  1.00 41.48           O  
HETATM 3185  O   HOH A 856       8.752   9.396  24.102  1.00 38.12           O  
HETATM 3186  O   HOH A 857       8.896  12.259  24.371  1.00 18.59           O  
HETATM 3187  O   HOH A 859       0.030  12.990  28.680  1.00 17.43           O  
HETATM 3188  O   HOH A 860       7.190  13.100  26.451  1.00 19.17           O  
HETATM 3189  O   HOH A 861       1.968  16.257  35.276  1.00 32.44           O  
HETATM 3190  O   HOH A 862      -0.058  16.835  33.400  1.00 54.29           O  
HETATM 3191  O   HOH A 863      -2.395  17.661  34.193  1.00 35.64           O  
HETATM 3192  O   HOH A 864       9.816  26.090  31.552  1.00 20.47           O  
HETATM 3193  O   HOH A 865      11.123  23.154  33.332  1.00 30.38           O  
HETATM 3194  O   HOH A 866      12.616  37.452  24.681  1.00 68.73           O  
HETATM 3195  O   HOH A 867      15.434  32.620  31.494  1.00 72.57           O  
HETATM 3196  O   HOH A 868      16.756  37.563  31.003  1.00 25.20           O  
HETATM 3197  O   HOH A 869      13.379  35.816  28.610  1.00 73.71           O  
HETATM 3198  O   HOH A 873       0.810  16.302  20.353  1.00 29.37           O  
HETATM 3199  O   HOH A 875      -9.217  21.430  15.733  1.00 46.19           O  
HETATM 3200  O   HOH A 876       1.974  22.103   6.206  1.00 24.04           O  
HETATM 3201  O   HOH A 877      15.046  33.214  -4.949  1.00 36.22           O  
HETATM 3202  O   HOH A 878      17.703  25.481 -10.555  1.00 56.20           O  
HETATM 3203  O   HOH A 880      12.087  16.849  -6.228  1.00 79.48           O  
HETATM 3204  O   HOH A 881       7.170  17.772  -2.847  1.00 37.72           O  
HETATM 3205  O   HOH A 882      16.703   8.878  19.613  1.00 29.47           O  
HETATM 3206  O   HOH A 883      18.571   7.905  17.673  1.00 40.69           O  
HETATM 3207  O   HOH A 884       1.699  12.407  13.498  1.00 45.12           O  
HETATM 3208  O   HOH A 885      12.149   8.511   3.811  1.00 40.79           O  
HETATM 3209  O   HOH A 886       6.843  13.046   0.055  1.00 78.13           O  
HETATM 3210  O   HOH A 887      23.570  10.106   6.354  1.00 43.74           O  
HETATM 3211  O   HOH A 888      19.128   8.820  11.005  1.00 57.56           O  
HETATM 3212  O   HOH A 889      21.301  10.718  14.470  1.00 34.56           O  
HETATM 3213  O   HOH A 891      19.193   8.445   1.040  1.00 39.30           O  
HETATM 3214  O   HOH A 892      38.349  25.151   7.731  1.00 66.76           O  
HETATM 3215  O   HOH A 893      37.906  22.540   8.391  1.00 39.47           O  
HETATM 3216  O   HOH A 894      38.695  23.205  11.011  1.00 22.12           O  
HETATM 3217  O   HOH A 895      40.512  24.381  14.825  1.00 31.83           O  
HETATM 3218  O   HOH A 896      38.886  17.619  16.102  1.00100.00           O  
HETATM 3219  O   HOH A 897      37.765  15.414  12.008  1.00 32.72           O  
HETATM 3220  O   HOH A 898      37.121  11.418   9.846  1.00 38.06           O  
HETATM 3221  O   HOH A 899      36.480   7.497   5.162  1.00 30.68           O  
HETATM 3222  O   HOH A 900      39.653   9.470  10.945  1.00 32.56           O  
HETATM 3223  O   HOH A 901      44.869  16.916  21.012  1.00 67.98           O  
HETATM 3224  O   HOH A 902      29.169  10.848   4.229  1.00 38.50           O  
HETATM 3225  O   HOH A 905      27.676  13.607  28.479  1.00 32.89           O  
HETATM 3226  O   HOH A 908      11.534  49.827  35.618  1.00 22.41           O  
HETATM 3227  O   HOH A 909      19.881  41.480  36.067  1.00 40.11           O  
HETATM 3228  O   HOH A 910      16.664  53.636  36.862  1.00 44.25           O  
HETATM 3229  O   HOH A 911      12.471  55.826  37.888  1.00 26.28           O  
HETATM 3230  O   HOH A 912      10.566  57.740  37.354  1.00 91.86           O  
HETATM 3231  O   HOH A 913      12.526  60.406  22.406  1.00 48.63           O  
HETATM 3232  O   HOH A 914      22.197  52.563  27.738  1.00 33.15           O  
HETATM 3233  O   HOH A 915      19.394  53.695  30.606  1.00 28.96           O  
HETATM 3234  O   HOH A 917       3.339  54.606  34.881  1.00 29.94           O  
HETATM 3235  O   HOH A 918       2.461  52.237  36.185  1.00 54.47           O  
HETATM 3236  O   HOH A 919       4.213  47.559  36.575  1.00 45.94           O  
HETATM 3237  O   HOH A 920       2.783  43.620  29.596  1.00 35.06           O  
HETATM 3238  O   HOH A 921      -1.350  45.080  24.504  1.00 35.16           O  
HETATM 3239  O   HOH A 922      -1.867  45.058  27.332  1.00 22.74           O  
HETATM 3240  O   HOH A 923       3.947  41.650  28.121  1.00 59.09           O  
HETATM 3241  O   HOH A 924      12.193  47.769  15.805  1.00 51.91           O  
HETATM 3242  O   HOH A 926      32.435  47.834  12.094  1.00 85.72           O  
HETATM 3243  O   HOH A 927      31.157  50.794  15.884  1.00 54.81           O  
HETATM 3244  O   HOH A 928      11.893  55.597  14.077  1.00 51.55           O  
HETATM 3245  O   HOH A 929      12.860  59.351  24.990  1.00 42.40           O  
HETATM 3246  O   HOH A 930      23.761  32.061  34.284  1.00 48.32           O  
HETATM 3247  O   HOH A 931       2.099  21.118   2.348  1.00 59.42           O  
HETATM 3248  O   HOH A 932      40.693  21.056  10.630  1.00 88.05           O  
HETATM 3249  O   HOH A 934       1.118  23.575  33.685  1.00 32.96           O  
HETATM 3250  O   HOH A 935      -4.657  23.473  29.020  1.00 26.54           O  
HETATM 3251  O   HOH A 936      34.772   8.102  15.671  1.00 68.94           O  
HETATM 3252  O   HOH A 937     -11.072  34.987   4.967  1.00 63.85           O  
HETATM 3253  O   HOH A 938      -4.071  31.001   0.062  1.00 61.62           O  
HETATM 3254  O   HOH A 939       0.227  36.954   3.692  1.00 96.68           O  
HETATM 3255  O   HOH A 940      20.613  44.580  13.167  1.00 64.64           O  
HETATM 3256  O   HOH A 951      21.714  18.714  -3.703  1.00 42.11           O  
HETATM 3257  O   HOH A 952      28.841  18.973  -6.446  1.00 49.66           O  
HETATM 3258  O   HOH A 953      25.491  26.380  -4.968  1.00 26.82           O  
HETATM 3259  O   HOH A 954      25.343  26.764  -8.087  1.00 42.29           O  
HETATM 3260  O   HOH A 955      22.811  26.505  -5.536  1.00 23.61           O  
HETATM 3261  O   HOH A 956      28.295  30.001  -3.202  1.00 15.88           O  
HETATM 3262  O   HOH A 957      13.645  40.421  -1.250  1.00 77.67           O  
HETATM 3263  O   HOH A 958      19.932  38.420   1.605  1.00 25.36           O  
HETATM 3264  O   HOH A 959      18.825  40.105   6.946  1.00 64.04           O  
HETATM 3265  O   HOH A 960      -0.939  29.043   4.494  1.00 33.85           O  
HETATM 3266  O   HOH A 961       0.609  26.860   5.448  1.00 44.88           O  
HETATM 3267  O   HOH A 962       3.092  34.074   5.329  1.00 14.22           O  
HETATM 3268  O   HOH A 963       3.025  37.252   3.669  1.00 67.22           O  
HETATM 3269  O   HOH A 964      11.139  36.845  20.071  1.00 53.64           O  
HETATM 3270  O   HOH A 965      17.243  38.982  16.098  1.00 75.75           O  
HETATM 3271  O   HOH A 966       4.915  42.171  16.322  1.00 28.35           O  
HETATM 3272  O   HOH A 967       9.572  41.551  13.554  1.00 42.29           O  
HETATM 3273  O   HOH A 968      -0.599  41.677   9.587  1.00 91.30           O  
HETATM 3274  O   HOH A 969      -1.315  40.671   7.050  1.00 52.98           O  
HETATM 3275  O   HOH A 970       8.036  43.932  13.982  1.00 47.37           O  
HETATM 3276  O   HOH A 971      -3.120  43.208  20.793  1.00 33.47           O  
HETATM 3277  O   HOH A 972      -2.311  45.736  20.336  1.00 91.42           O  
HETATM 3278  O   HOH A 973      -4.616  45.769  21.772  1.00 38.73           O  
HETATM 3279  O   HOH A 974      -2.787  35.478  25.580  1.00 47.09           O  
HETATM 3280  O   HOH A 975      -4.006  38.790  26.712  1.00 99.53           O  
HETATM 3281  O   HOH A 976      14.179  22.875  21.204  1.00 25.41           O  
HETATM 3282  O   HOH A 977      11.457  21.090  24.852  1.00 20.94           O  
HETATM 3283  O   HOH A 979       3.285  15.542  20.937  1.00 29.61           O  
HETATM 3284  O   HOH A 980       3.732  11.992  20.956  1.00 38.02           O  
HETATM 3285  O   HOH A 981      10.951  15.222  29.911  1.00 31.79           O  
HETATM 3286  O   HOH A 982      13.377  22.304  28.588  1.00 24.52           O  
HETATM 3287  O   HOH A 983      13.714  16.516  27.548  1.00 43.11           O  
HETATM 3288  O   HOH A 984      14.257  20.088  29.889  1.00 90.59           O  
HETATM 3289  O   HOH A 985      -0.091  10.727  32.095  1.00 77.66           O  
HETATM 3290  O   HOH A 986       7.902  14.435  32.454  1.00 29.17           O  
HETATM 3291  O   HOH A 987       4.648  18.759  36.061  1.00 28.84           O  
HETATM 3292  O   HOH A 989      10.054  28.510  26.995  1.00 22.79           O  
HETATM 3293  O   HOH A 990       2.097  34.789  28.731  1.00 41.95           O  
HETATM 3294  O   HOH A 991       4.531  35.965  25.690  1.00 48.62           O  
HETATM 3295  O   HOH A 992      -3.858  31.048  26.991  1.00 39.54           O  
HETATM 3296  O   HOH A 993      -9.001  29.397  21.373  1.00 28.91           O  
HETATM 3297  O   HOH A 994     -10.111  22.958  19.434  1.00 45.48           O  
HETATM 3298  O   HOH A 995     -14.087  28.883  10.028  1.00 43.97           O  
HETATM 3299  O   HOH A 996      -4.863  15.505  12.847  1.00 40.63           O  
HETATM 3300  O   HOH A 997      -0.771  13.697  13.582  1.00 51.66           O  
HETATM 3301  O   HOH A 998      -1.984  13.301  11.101  1.00 40.05           O  
HETATM 3302  O   HOH A1000       5.273  23.329  -2.954  1.00 32.42           O  
HETATM 3303  O   HOH A1001       6.640  26.774  -4.633  1.00 28.66           O  
HETATM 3304  O   HOH A1002      14.650  20.217  -6.118  1.00 42.08           O  
HETATM 3305  O   HOH A1003      17.507  24.929 -13.872  1.00 74.96           O  
HETATM 3306  O   HOH A1004      11.632  27.697 -13.577  1.00 44.65           O  
HETATM 3307  O   HOH A1005      18.752  27.982  -9.155  1.00 43.83           O  
HETATM 3308  O   HOH A1006      17.242  14.368  -4.776  1.00 37.14           O  
HETATM 3309  O   HOH A1007      22.672  13.979  23.366  1.00 34.15           O  
HETATM 3310  O   HOH A1008      18.016  12.306  25.539  1.00 39.52           O  
HETATM 3311  O   HOH A1009      10.026   6.951   4.549  1.00 76.58           O  
HETATM 3312  O   HOH A1010      24.382  11.324   8.832  1.00 77.45           O  
HETATM 3313  O   HOH A1011      27.506  11.469   9.939  1.00 58.81           O  
HETATM 3314  O   HOH A1012      31.745  15.576   2.961  1.00 47.55           O  
HETATM 3315  O   HOH A1013      38.697  17.592  13.255  1.00 60.35           O  
HETATM 3316  O   HOH A1014      38.737  16.131   7.972  1.00 24.91           O  
HETATM 3317  O   HOH A1015      36.836  12.032   3.156  1.00 39.28           O  
HETATM 3318  O   HOH A1016      37.012  16.951  -1.978  1.00 78.07           O  
HETATM 3319  O   HOH A1017      43.217   7.887  16.045  1.00 78.96           O  
HETATM 3320  O   HOH A1018      38.754  11.015  22.192  1.00 54.83           O  
HETATM 3321  O   HOH A1020      34.979   4.995  12.524  1.00 64.46           O  
HETATM 3322  O   HOH A1021      29.780  11.693  28.648  1.00 48.61           O  
HETATM 3323  O   HOH A1022      25.025  17.431  30.862  1.00 87.31           O  
HETATM 3324  O   HOH A1023      23.680  23.304  32.696  1.00 35.66           O  
HETATM 3325  O   HOH A1024      25.002  41.647  35.088  1.00 44.74           O  
HETATM 3326  O   HOH A1025      17.318  36.286  33.511  1.00 61.16           O  
HETATM 3327  O   HOH A1026      11.181  45.445  34.149  1.00 45.85           O  
HETATM 3328  O   HOH A1028      13.013  51.352  37.161  1.00 27.28           O  
HETATM 3329  O   HOH A1029       5.879  55.306  36.423  1.00 81.76           O  
HETATM 3330  O   HOH A1030       5.715  51.311  38.572  1.00 44.49           O  
HETATM 3331  O   HOH A1031       2.077  47.375  37.890  1.00 38.21           O  
HETATM 3332  O   HOH A1032      18.151  47.302  36.704  1.00100.00           O  
HETATM 3333  O   HOH A1034      -0.546  53.638  34.113  1.00 41.97           O  
HETATM 3334  O   HOH A1035      -1.746  44.253  30.715  1.00 50.35           O  
HETATM 3335  O   HOH A1036      -2.105  45.338  33.669  1.00 53.91           O  
HETATM 3336  O   HOH A1037       1.775  52.057  15.170  1.00 85.83           O  
HETATM 3337  O   HOH A1038      13.065  38.661  13.085  1.00 32.07           O  
HETATM 3338  O   HOH A1039      13.909  44.723  13.396  1.00 56.42           O  
HETATM 3339  O   HOH A1040      15.146  44.880  10.663  1.00 85.69           O  
HETATM 3340  O   HOH A1041      17.208  52.192  14.231  1.00 42.29           O  
HETATM 3341  O   HOH A1042      23.873  44.923  11.514  1.00 50.15           O  
HETATM 3342  O   HOH A1043      24.341  54.823  17.259  1.00 56.03           O  
HETATM 3343  O   HOH A1044      -1.000  55.950  21.680  1.00 28.32           O  
HETATM 3344  O   HOH A1045      24.716  54.950  24.934  1.00 35.38           O  
HETATM 3345  O   HOH A1048      27.211  40.211  35.876  1.00 58.43           O  
HETATM 3346  O   HOH A1050      22.994  15.463  31.329  1.00 66.08           O  
HETATM 3347  O   HOH A1051      41.805  13.812  28.549  1.00 85.07           O  
HETATM 3348  O   HOH A1052      43.500  24.616  24.622  1.00 34.71           O  
HETATM 3349  O   HOH A1053      21.596  36.871  11.760  1.00 27.85           O  
HETATM 3350  O   HOH A1054      30.434  34.083  10.356  1.00 30.60           O  
HETATM 3351  O   HOH A1055      43.005  27.694  14.304  1.00 42.36           O  
HETATM 3352  O   HOH A1056      43.812  30.060  12.509  1.00 41.17           O  
HETATM 3353  O   HOH A1057      17.450  22.287  21.309  1.00 12.69           O  
HETATM 3354  O   HOH A1058      21.151  26.686  10.322  1.00 12.79           O  
HETATM 3355  O   HOH A1059      21.672  21.466  18.823  1.00 15.05           O  
HETATM 3356  O   HOH A1060      22.306  19.118  20.123  1.00 18.27           O  
HETATM 3357  O   HOH A1061      23.818  18.939  24.228  1.00 33.09           O  
HETATM 3358  O   HOH A1062      23.510  33.890  -1.911  1.00 11.93           O  
HETATM 3359  O   HOH A1063      25.444  32.917  -3.539  1.00 19.71           O  
HETATM 3360  O   HOH A1064      25.846  28.867  -3.967  1.00 20.04           O  
HETATM 3361  O   HOH A1065       0.458  24.269   5.483  1.00 31.55           O  
HETATM 3362  O   HOH A1066       3.887  26.832  -4.063  1.00 60.96           O  
HETATM 3363  O   HOH A1067      -4.386  13.118  20.364  1.00 16.20           O  
HETATM 3364  O   HOH A1068      25.796  14.484  17.187  1.00 22.36           O  
HETATM 3365  O   HOH A1069      25.804  14.884  20.163  1.00 26.86           O  
HETATM 3366  O   HOH A1070      19.311  51.476  34.664  1.00 64.27           O  
HETATM 3367  O   HOH A1071      14.068  21.659  23.553  1.00 31.82           O  
CONECT   43 2915                                                                
CONECT   73 2915                                                                
CONECT 2909 2912 2920 2991 2992                                                 
CONECT 2909 2993 2994                                                           
CONECT 2910 2911 2912 2913 2914                                                 
CONECT 2911 2910                                                                
CONECT 2912 2909 2910                                                           
CONECT 2913 2910                                                                
CONECT 2914 2910                                                                
CONECT 2915   43   73 2920 2989                                                 
CONECT 2915 2994                                                                
CONECT 2918 2919 2920 2921 2925                                                 
CONECT 2919 2918                                                                
CONECT 2920 2909 2915 2918                                                      
CONECT 2921 2918                                                                
CONECT 2922 2923 2924 2925 2926                                                 
CONECT 2923 2922                                                                
CONECT 2924 2922                                                                
CONECT 2925 2918 2922                                                           
CONECT 2926 2922 2927                                                           
CONECT 2927 2926 2928                                                           
CONECT 2928 2927 2929 2930                                                      
CONECT 2929 2928 2934                                                           
CONECT 2930 2928 2931 2932                                                      
CONECT 2931 2930                                                                
CONECT 2932 2930 2933 2934                                                      
CONECT 2933 2932                                                                
CONECT 2934 2929 2932 2935                                                      
CONECT 2935 2934 2936 2944                                                      
CONECT 2936 2935 2937                                                           
CONECT 2937 2936 2938                                                           
CONECT 2938 2937 2939 2944                                                      
CONECT 2939 2938 2940 2941                                                      
CONECT 2940 2939                                                                
CONECT 2941 2939 2942                                                           
CONECT 2942 2941 2943                                                           
CONECT 2943 2942 2944                                                           
CONECT 2944 2935 2938 2943                                                      
CONECT 2989 2915                                                                
CONECT 2991 2909                                                                
CONECT 2992 2909                                                                
CONECT 2993 2909                                                                
CONECT 2994 2909 2915                                                           
MASTER      308    0    6   14   16    0   18    6 3366    1   43   30          
END                                                                             
