HEADER    LIGASE                                  10-APR-08   2ZLZ              
OBSLTE     11-JAN-12 2ZLZ      4A91                                             
TITLE     CRYSTAL STRUCTURE OF THE E. COLI GLUTAMYL-TRNAASP SYNTHETASE COMPLEXED
TITLE    2 TO L-GLU AT 1.75 A RESOLUTION                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUTAMYL-Q TRNA(ASP) SYNTHETASE;                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: GLU-Q-RSS;                                                  
COMPND   5 EC: 6.1.1.-;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21 ROSETTA 2;                            
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PDEST14                                   
KEYWDS    TRNA SYNTHETASE, QUEUOSINE, TRNA MODIFICATION, GLUTAMYL-TRNA          
KEYWDS   2 SYNTHETASE, LIGASE                                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.BLAISE,V.OLIERIC,C.SAUTER,B.LORBER,B.ROY,S.KARMAKAR,R.BANERJEE,     
AUTHOR   2 H.D.BECKER,D.KERN                                                    
REVDAT   4   11-JAN-12 2ZLZ    1       OBSLTE                                   
REVDAT   3   24-FEB-09 2ZLZ    1       VERSN                                    
REVDAT   2   09-SEP-08 2ZLZ    1       AUTHOR                                   
REVDAT   1   02-SEP-08 2ZLZ    0                                                
JRNL        AUTH   M.BLAISE,V.OLIERIC,C.SAUTER,B.LORBER,B.ROY,S.KARMAKAR,       
JRNL        AUTH 2 R.BANERJEE,H.D.BECKER,D.KERN                                 
JRNL        TITL   CRYSTAL STRUCTURE OF GLUTAMYL-QUEUOSINE TRNAASP SYNTHETASE   
JRNL        TITL 2 COMPLEXED WITH L-GLUTAMATE: STRUCTURAL ELEMENTS MEDIATING    
JRNL        TITL 3 TRNA-INDEPENDENT ACTIVATION OF GLUTAMATE AND GLUTAMYLATION   
JRNL        TITL 4 OF TRNAASP ANTICODON.                                        
JRNL        REF    J.MOL.BIOL.                   V. 381  1224 2008              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   18602926                                                     
JRNL        DOI    10.1016/J.JMB.2008.06.053                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.75 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 34396                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.187                           
REMARK   3   FREE R VALUE                     : 0.214                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 1729                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.75                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2363                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 11                                      
REMARK   3   SOLVENT ATOMS            : 438                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 16.60                          
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) : 0.18                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.07                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 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) : 1.30                            
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  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : 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 2ZLZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-APR-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB028139.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.933                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 34396                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.750                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 60.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.04600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 25.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.09500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 7.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: PDB ENTRY 1NZJ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.33                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MG-ACETATE, NA-CACODYLATE, 0.2M     
REMARK 280  KCL, 10% PEG 8000, 2MM L-GLU, PH 5.5, VAPOR DIFFUSION, SITTING      
REMARK 280  DROP, TEMPERATURE 293K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       77.20000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       77.20000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       19.55000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       57.51500            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       19.55000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       57.51500            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       77.20000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       19.55000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       57.51500            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       77.20000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       19.55000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       57.51500            
REMARK 290   SMTRY3   8  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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 693  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     THR A     2                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   CB   ALA A   227     CB   CYS A   298              2.05            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    HIS A 234   C     HIS A 234   O      -0.268                       
REMARK 500    PRO A 236   CG    PRO A 236   CD     -0.396                       
REMARK 500    PRO A 236   CD    PRO A 236   N      -0.114                       
REMARK 500    ALA A 237   N     ALA A 237   CA     -0.240                       
REMARK 500    ALA A 237   C     ALA A 237   O       0.237                       
REMARK 500    ALA A 237   C     LEU A 238   N       0.156                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A 236   C   -  N   -  CD  ANGL. DEV. = -16.4 DEGREES          
REMARK 500    ALA A 237   CB  -  CA  -  C   ANGL. DEV. =  15.0 DEGREES          
REMARK 500    ALA A 237   N   -  CA  -  C   ANGL. DEV. =  17.2 DEGREES          
REMARK 500    ALA A 237   C   -  N   -  CA  ANGL. DEV. = -18.4 DEGREES          
REMARK 500    LEU A 238   C   -  N   -  CA  ANGL. DEV. = -28.7 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    SER A 230       45.53    -86.45                                   
REMARK 500    LYS A 231     -118.82    -72.46                                   
REMARK 500    HIS A 234       63.94    143.04                                   
REMARK 500    PRO A 236     -159.77    -37.72                                   
REMARK 500    ALA A 296     -160.67    -78.11                                   
REMARK 500    SER A 297      -69.13   -126.26                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 PRO A  236     ALA A  237                 -138.78                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    HIS A 234        25.0      L          L   OUTSIDE RANGE           
REMARK 500    ALA A 237         1.6      L          L   EXPECTING SP3           
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                              ZN A 300  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 101   SG                                                     
REMARK 620 2 CYS A 103   SG  108.2                                              
REMARK 620 3 TYR A 115   OH  106.1 113.3                                        
REMARK 620 4 CYS A 119   SG  118.5 107.5 103.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 300                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GLU A 301                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1NZJ   RELATED DB: PDB                                   
DBREF  2ZLZ A    1   298  UNP    P27305   GLUQ_ECOLI       1    298             
SEQRES   1 A  298  MET THR ASP THR GLN TYR ILE GLY ARG PHE ALA PRO SER          
SEQRES   2 A  298  PRO SER GLY GLU LEU HIS PHE GLY SER LEU ILE ALA ALA          
SEQRES   3 A  298  LEU GLY SER TYR LEU GLN ALA ARG ALA ARG GLN GLY ARG          
SEQRES   4 A  298  TRP LEU VAL ARG ILE GLU ASP ILE ASP PRO PRO ARG GLU          
SEQRES   5 A  298  VAL PRO GLY ALA ALA GLU THR ILE LEU ARG GLN LEU GLU          
SEQRES   6 A  298  HIS TYR GLY LEU HIS TRP ASP GLY ASP VAL LEU TRP GLN          
SEQRES   7 A  298  SER GLN ARG HIS ASP ALA TYR ARG GLU ALA LEU ALA TRP          
SEQRES   8 A  298  LEU HIS GLU GLN GLY LEU SER TYR TYR CYS THR CYS THR          
SEQRES   9 A  298  ARG ALA ARG ILE GLN SER ILE GLY GLY ILE TYR ASP GLY          
SEQRES  10 A  298  HIS CYS ARG VAL LEU HIS HIS GLY PRO ASP ASN ALA ALA          
SEQRES  11 A  298  VAL ARG ILE ARG GLN GLN HIS PRO VAL THR GLN PHE THR          
SEQRES  12 A  298  ASP GLN LEU ARG GLY ILE ILE HIS ALA ASP GLU LYS LEU          
SEQRES  13 A  298  ALA ARG GLU ASP PHE ILE ILE HIS ARG ARG ASP GLY LEU          
SEQRES  14 A  298  PHE ALA TYR ASN LEU ALA VAL VAL VAL ASP ASP HIS PHE          
SEQRES  15 A  298  GLN GLY VAL THR GLU ILE VAL ARG GLY ALA ASP LEU ILE          
SEQRES  16 A  298  GLU PRO THR VAL ARG GLN ILE SER LEU TYR GLN LEU PHE          
SEQRES  17 A  298  GLY TRP LYS VAL PRO ASP TYR ILE HIS LEU PRO LEU ALA          
SEQRES  18 A  298  LEU ASN PRO GLN GLY ALA LYS LEU SER LYS GLN ASN HIS          
SEQRES  19 A  298  ALA PRO ALA LEU PRO LYS GLY ASP PRO ARG PRO VAL LEU          
SEQRES  20 A  298  ILE ALA ALA LEU GLN PHE LEU GLY GLN GLN ALA GLU ALA          
SEQRES  21 A  298  HIS TRP GLN ASP PHE SER VAL GLU GLN ILE LEU GLN SER          
SEQRES  22 A  298  ALA VAL LYS ASN TRP ARG LEU THR ALA VAL PRO GLU SER          
SEQRES  23 A  298  ALA ILE VAL ASN SER THR PHE SER ASN ALA SER CYS              
HET     ZN  A 300       1                                                       
HET    GLU  A 301      10                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     GLU GLUTAMIC ACID                                                    
FORMUL   2   ZN    ZN 2+                                                        
FORMUL   3  GLU    C5 H9 N O4                                                   
FORMUL   4  HOH   *438(H2 O)                                                    
HELIX    1   1 HIS A   19  ARG A   36  1                                  18    
HELIX    2   2 ASP A   48  GLU A   52  5                                   5    
HELIX    3   3 GLY A   55  TYR A   67  1                                  13    
HELIX    4   4 ARG A   81  GLN A   95  1                                  15    
HELIX    5   5 THR A  104  ILE A  111  1                                   8    
HELIX    6   6 ASP A  153  GLU A  159  1                                   7    
HELIX    7   7 ALA A  171  GLN A  183  1                                  13    
HELIX    8   8 GLY A  191  GLU A  196  5                                   6    
HELIX    9   9 PRO A  197  GLY A  209  1                                  13    
HELIX   10  10 PRO A  243  LEU A  254  1                                  12    
HELIX   11  11 HIS A  261  PHE A  265  5                                   5    
HELIX   12  12 SER A  266  ASN A  277  1                                  12    
HELIX   13  13 ARG A  279  VAL A  283  5                                   5    
HELIX   14  14 ASN A  290  SER A  294  5                                   5    
SHEET    1   A 3 ILE A   7  PHE A  10  0                                        
SHEET    2   A 3 ARG A  39  ILE A  44  1  O  ARG A  39   N  GLY A   8           
SHEET    3   A 3 LEU A  76  TRP A  77  1  O  LEU A  76   N  ILE A  44           
SHEET    1   B 3 SER A  98  CYS A 101  0                                        
SHEET    2   B 3 ALA A 130  ILE A 133 -1  O  ALA A 130   N  CYS A 101           
SHEET    3   B 3 ILE A 162  HIS A 164 -1  O  ILE A 163   N  VAL A 131           
SHEET    1   C 2 GLN A 141  ASP A 144  0                                        
SHEET    2   C 2 GLY A 148  HIS A 151 -1  O  ILE A 150   N  PHE A 142           
SHEET    1   D 2 GLU A 187  ARG A 190  0                                        
SHEET    2   D 2 ASP A 214  HIS A 217  1  O  ASP A 214   N  ILE A 188           
SHEET    1   E 2 LEU A 220  LEU A 222  0                                        
SHEET    2   E 2 SER A 286  ILE A 288  1  O  ALA A 287   N  LEU A 222           
LINK         SG  CYS A 101                ZN    ZN A 300     1555   1555  2.37  
LINK         SG  CYS A 103                ZN    ZN A 300     1555   1555  2.38  
LINK         OH  TYR A 115                ZN    ZN A 300     1555   1555  2.08  
LINK         SG  CYS A 119                ZN    ZN A 300     1555   1555  2.33  
SITE     1 AC1  4 CYS A 101  CYS A 103  TYR A 115  CYS A 119                    
SITE     1 AC2 11 ARG A   9  ALA A  11  SER A  13  TYR A 172                    
SITE     2 AC2 11 ARG A 190  LEU A 194  HOH A 303  HOH A 561                    
SITE     3 AC2 11 HOH A 602  HOH A 614  HOH A 657                               
CRYST1   39.100  115.030  154.400  90.00  90.00  90.00 C 2 2 21      8          
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      0.025575  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008693  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006477        0.00000                         
ATOM      1  N   ASP A   3      31.836  57.298   4.111  1.00 51.06           N  
ATOM      2  CA  ASP A   3      31.414  58.310   3.099  1.00 50.07           C  
ATOM      3  C   ASP A   3      29.907  58.236   2.852  1.00 48.12           C  
ATOM      4  O   ASP A   3      29.242  59.262   2.690  1.00 48.27           O  
ATOM      5  CB  ASP A   3      32.171  58.083   1.787  1.00 52.38           C  
ATOM      6  CG  ASP A   3      31.837  59.121   0.735  1.00 54.35           C  
ATOM      7  OD1 ASP A   3      30.693  59.113   0.228  1.00 55.99           O  
ATOM      8  OD2 ASP A   3      32.718  59.951   0.420  1.00 55.71           O  
ATOM      9  N   THR A   4      29.375  57.017   2.825  1.00 44.82           N  
ATOM     10  CA  THR A   4      27.947  56.816   2.610  1.00 40.79           C  
ATOM     11  C   THR A   4      27.199  57.270   3.866  1.00 36.83           C  
ATOM     12  O   THR A   4      27.750  57.269   4.965  1.00 35.85           O  
ATOM     13  CB  THR A   4      27.619  55.329   2.314  1.00 41.80           C  
ATOM     14  OG1 THR A   4      26.295  55.235   1.771  1.00 43.35           O  
ATOM     15  CG2 THR A   4      27.702  54.489   3.588  1.00 42.21           C  
ATOM     16  N   GLN A   5      25.945  57.661   3.700  1.00 32.31           N  
ATOM     17  CA  GLN A   5      25.176  58.139   4.829  1.00 28.27           C  
ATOM     18  C   GLN A   5      24.903  57.053   5.864  1.00 24.30           C  
ATOM     19  O   GLN A   5      24.789  55.868   5.548  1.00 24.01           O  
ATOM     20  CB  GLN A   5      23.845  58.735   4.349  1.00 30.46           C  
ATOM     21  CG  GLN A   5      23.086  59.521   5.420  1.00 32.24           C  
ATOM     22  CD  GLN A   5      21.796  60.155   4.907  1.00 34.57           C  
ATOM     23  OE1 GLN A   5      21.191  60.997   5.584  1.00 34.73           O  
ATOM     24  NE2 GLN A   5      21.365  59.751   3.715  1.00 34.74           N  
ATOM     25  N   TYR A   6      24.836  57.483   7.112  1.00 20.48           N  
ATOM     26  CA  TYR A   6      24.519  56.604   8.223  1.00 15.72           C  
ATOM     27  C   TYR A   6      23.068  56.182   8.007  1.00 13.61           C  
ATOM     28  O   TYR A   6      22.237  56.999   7.600  1.00 13.28           O  
ATOM     29  CB  TYR A   6      24.613  57.398   9.535  1.00 15.02           C  
ATOM     30  CG  TYR A   6      24.161  56.657  10.770  1.00 13.51           C  
ATOM     31  CD1 TYR A   6      25.084  56.237  11.723  1.00 12.90           C  
ATOM     32  CD2 TYR A   6      22.800  56.421  11.012  1.00 13.99           C  
ATOM     33  CE1 TYR A   6      24.675  55.605  12.897  1.00 11.99           C  
ATOM     34  CE2 TYR A   6      22.377  55.789  12.180  1.00 12.36           C  
ATOM     35  CZ  TYR A   6      23.329  55.386  13.118  1.00 12.13           C  
ATOM     36  OH  TYR A   6      22.956  54.767  14.280  1.00 12.40           O  
ATOM     37  N   ILE A   7      22.771  54.911   8.250  1.00 12.42           N  
ATOM     38  CA  ILE A   7      21.407  54.426   8.145  1.00 11.72           C  
ATOM     39  C   ILE A   7      21.149  53.522   9.346  1.00  9.64           C  
ATOM     40  O   ILE A   7      21.832  52.489   9.520  1.00 10.78           O  
ATOM     41  CB  ILE A   7      21.156  53.609   6.858  1.00 11.73           C  
ATOM     42  CG1 ILE A   7      21.352  54.494   5.622  1.00 13.28           C  
ATOM     43  CG2 ILE A   7      19.718  53.052   6.876  1.00 12.76           C  
ATOM     44  CD1 ILE A   7      21.157  53.735   4.305  1.00 15.12           C  
ATOM     45  N   GLY A   8      20.176  53.918  10.165  1.00 10.36           N  
ATOM     46  CA  GLY A   8      19.801  53.135  11.342  1.00  9.06           C  
ATOM     47  C   GLY A   8      18.322  52.757  11.267  1.00 10.07           C  
ATOM     48  O   GLY A   8      17.622  53.175  10.345  1.00 10.95           O  
ATOM     49  N   ARG A   9      17.819  51.970  12.219  1.00  9.38           N  
ATOM     50  CA  ARG A   9      16.400  51.607  12.137  1.00  9.02           C  
ATOM     51  C   ARG A   9      15.800  51.100  13.439  1.00  9.60           C  
ATOM     52  O   ARG A   9      16.524  50.697  14.351  1.00  9.55           O  
ATOM     53  CB  ARG A   9      16.205  50.511  11.082  1.00  8.92           C  
ATOM     54  CG  ARG A   9      16.475  49.078  11.603  1.00  9.58           C  
ATOM     55  CD  ARG A   9      17.929  48.834  12.063  1.00 11.70           C  
ATOM     56  NE  ARG A   9      18.140  47.405  12.294  1.00 11.67           N  
ATOM     57  CZ  ARG A   9      17.845  46.764  13.426  1.00 10.38           C  
ATOM     58  NH1 ARG A   9      18.044  45.453  13.516  1.00  8.85           N  
ATOM     59  NH2 ARG A   9      17.385  47.438  14.483  1.00 12.30           N  
ATOM     60  N   PHE A  10      14.468  51.144  13.502  1.00  8.37           N  
ATOM     61  CA  PHE A  10      13.700  50.625  14.635  1.00  8.26           C  
ATOM     62  C   PHE A  10      12.900  49.493  13.986  1.00  9.97           C  
ATOM     63  O   PHE A  10      12.192  49.722  13.010  1.00 10.08           O  
ATOM     64  CB  PHE A  10      12.766  51.702  15.195  1.00  9.33           C  
ATOM     65  CG  PHE A  10      11.873  51.215  16.303  1.00  9.30           C  
ATOM     66  CD1 PHE A  10      12.385  50.476  17.364  1.00 10.52           C  
ATOM     67  CD2 PHE A  10      10.508  51.470  16.263  1.00 10.38           C  
ATOM     68  CE1 PHE A  10      11.538  49.986  18.370  1.00  8.97           C  
ATOM     69  CE2 PHE A  10       9.657  50.990  17.259  1.00  8.80           C  
ATOM     70  CZ  PHE A  10      10.176  50.242  18.312  1.00  8.32           C  
ATOM     71  N   ALA A  11      13.032  48.282  14.517  1.00  9.14           N  
ATOM     72  CA  ALA A  11      12.379  47.118  13.925  1.00  9.54           C  
ATOM     73  C   ALA A  11      11.539  46.328  14.910  1.00  9.62           C  
ATOM     74  O   ALA A  11      11.853  45.179  15.224  1.00 12.57           O  
ATOM     75  CB  ALA A  11      13.460  46.217  13.336  1.00  9.64           C  
ATOM     76  N   PRO A  12      10.418  46.901  15.365  1.00  9.96           N  
ATOM     77  CA  PRO A  12       9.577  46.193  16.335  1.00 11.67           C  
ATOM     78  C   PRO A  12       8.791  44.984  15.848  1.00 13.36           C  
ATOM     79  O   PRO A  12       8.448  44.894  14.677  1.00 13.01           O  
ATOM     80  CB  PRO A  12       8.639  47.285  16.824  1.00 11.46           C  
ATOM     81  CG  PRO A  12       8.373  48.058  15.544  1.00  9.33           C  
ATOM     82  CD  PRO A  12       9.802  48.177  14.955  1.00  9.81           C  
ATOM     83  N   SER A  13       8.507  44.075  16.781  1.00 13.98           N  
ATOM     84  CA  SER A  13       7.692  42.895  16.495  1.00 15.71           C  
ATOM     85  C   SER A  13       6.282  43.297  16.939  1.00 15.36           C  
ATOM     86  O   SER A  13       6.100  43.778  18.056  1.00 17.50           O  
ATOM     87  CB  SER A  13       8.161  41.702  17.321  1.00 16.07           C  
ATOM     88  OG  SER A  13       9.459  41.288  16.930  1.00 20.03           O  
ATOM     89  N   PRO A  14       5.277  43.092  16.082  1.00 16.41           N  
ATOM     90  CA  PRO A  14       3.903  43.462  16.440  1.00 16.42           C  
ATOM     91  C   PRO A  14       3.183  42.459  17.324  1.00 17.38           C  
ATOM     92  O   PRO A  14       2.060  42.064  17.034  1.00 16.86           O  
ATOM     93  CB  PRO A  14       3.230  43.631  15.084  1.00 17.83           C  
ATOM     94  CG  PRO A  14       3.912  42.556  14.257  1.00 16.63           C  
ATOM     95  CD  PRO A  14       5.370  42.692  14.667  1.00 15.61           C  
ATOM     96  N   SER A  15       3.827  42.064  18.413  1.00 18.27           N  
ATOM     97  CA  SER A  15       3.218  41.114  19.336  1.00 18.78           C  
ATOM     98  C   SER A  15       2.485  41.871  20.433  1.00 18.51           C  
ATOM     99  O   SER A  15       1.875  41.274  21.314  1.00 18.46           O  
ATOM    100  CB  SER A  15       4.294  40.203  19.934  1.00 20.42           C  
ATOM    101  OG  SER A  15       5.331  40.962  20.524  1.00 24.18           O  
ATOM    102  N   GLY A  16       2.553  43.198  20.367  1.00 17.64           N  
ATOM    103  CA  GLY A  16       1.897  44.045  21.346  1.00 17.70           C  
ATOM    104  C   GLY A  16       2.131  45.478  20.914  1.00 17.40           C  
ATOM    105  O   GLY A  16       2.783  45.694  19.897  1.00 19.19           O  
ATOM    106  N   GLU A  17       1.613  46.454  21.647  1.00 17.56           N  
ATOM    107  CA  GLU A  17       1.845  47.841  21.248  1.00 17.40           C  
ATOM    108  C   GLU A  17       3.154  48.264  21.901  1.00 17.53           C  
ATOM    109  O   GLU A  17       3.786  47.462  22.601  1.00 16.38           O  
ATOM    110  CB  GLU A  17       0.687  48.743  21.697  1.00 20.70           C  
ATOM    111  CG  GLU A  17       0.432  48.794  23.201  1.00 24.32           C  
ATOM    112  CD  GLU A  17      -0.757  49.691  23.549  1.00 28.83           C  
ATOM    113  OE1 GLU A  17      -1.891  49.174  23.673  1.00 29.80           O  
ATOM    114  OE2 GLU A  17      -0.559  50.920  23.686  1.00 29.54           O  
ATOM    115  N   LEU A  18       3.578  49.499  21.680  1.00 17.05           N  
ATOM    116  CA  LEU A  18       4.832  49.939  22.277  1.00 18.03           C  
ATOM    117  C   LEU A  18       4.711  50.057  23.781  1.00 17.18           C  
ATOM    118  O   LEU A  18       3.667  50.440  24.297  1.00 18.94           O  
ATOM    119  CB  LEU A  18       5.265  51.294  21.718  1.00 20.79           C  
ATOM    120  CG  LEU A  18       5.580  51.335  20.221  1.00 23.73           C  
ATOM    121  CD1 LEU A  18       6.119  52.705  19.877  1.00 26.71           C  
ATOM    122  CD2 LEU A  18       6.595  50.251  19.864  1.00 24.56           C  
ATOM    123  N   HIS A  19       5.786  49.700  24.474  1.00 16.34           N  
ATOM    124  CA  HIS A  19       5.854  49.824  25.922  1.00 18.02           C  
ATOM    125  C   HIS A  19       7.126  50.644  26.196  1.00 17.16           C  
ATOM    126  O   HIS A  19       7.851  50.999  25.259  1.00 14.67           O  
ATOM    127  CB  HIS A  19       5.892  48.445  26.605  1.00 19.32           C  
ATOM    128  CG  HIS A  19       6.964  47.534  26.097  1.00 22.40           C  
ATOM    129  ND1 HIS A  19       6.746  46.604  25.102  1.00 24.67           N  
ATOM    130  CD2 HIS A  19       8.269  47.419  26.440  1.00 22.63           C  
ATOM    131  CE1 HIS A  19       7.871  45.957  24.855  1.00 22.83           C  
ATOM    132  NE2 HIS A  19       8.810  46.434  25.654  1.00 24.84           N  
ATOM    133  N   PHE A  20       7.408  50.957  27.456  1.00 16.16           N  
ATOM    134  CA  PHE A  20       8.573  51.799  27.735  1.00 15.59           C  
ATOM    135  C   PHE A  20       9.871  51.274  27.141  1.00 14.27           C  
ATOM    136  O   PHE A  20      10.627  52.044  26.563  1.00 13.38           O  
ATOM    137  CB  PHE A  20       8.737  52.007  29.238  1.00 16.97           C  
ATOM    138  CG  PHE A  20       9.628  53.161  29.588  1.00 16.22           C  
ATOM    139  CD1 PHE A  20       9.226  54.465  29.334  1.00 17.65           C  
ATOM    140  CD2 PHE A  20      10.867  52.941  30.162  1.00 19.27           C  
ATOM    141  CE1 PHE A  20      10.047  55.548  29.649  1.00 18.62           C  
ATOM    142  CE2 PHE A  20      11.701  54.024  30.484  1.00 18.73           C  
ATOM    143  CZ  PHE A  20      11.285  55.321  30.226  1.00 15.94           C  
ATOM    144  N   GLY A  21      10.117  49.971  27.269  1.00 13.66           N  
ATOM    145  CA  GLY A  21      11.338  49.385  26.735  1.00 14.93           C  
ATOM    146  C   GLY A  21      11.456  49.536  25.230  1.00 14.98           C  
ATOM    147  O   GLY A  21      12.534  49.850  24.706  1.00 13.85           O  
ATOM    148  N   SER A  22      10.367  49.302  24.501  1.00 13.53           N  
ATOM    149  CA  SER A  22      10.472  49.466  23.058  1.00 14.41           C  
ATOM    150  C   SER A  22      10.540  50.948  22.691  1.00 14.09           C  
ATOM    151  O   SER A  22      11.140  51.290  21.677  1.00 12.42           O  
ATOM    152  CB  SER A  22       9.339  48.742  22.303  1.00 15.39           C  
ATOM    153  OG  SER A  22       8.104  48.836  22.967  1.00 18.19           O  
ATOM    154  N   LEU A  23       9.956  51.837  23.506  1.00 12.92           N  
ATOM    155  CA  LEU A  23      10.070  53.278  23.223  1.00 13.14           C  
ATOM    156  C   LEU A  23      11.551  53.655  23.355  1.00 12.31           C  
ATOM    157  O   LEU A  23      12.078  54.460  22.576  1.00 12.68           O  
ATOM    158  CB  LEU A  23       9.242  54.123  24.211  1.00 13.80           C  
ATOM    159  CG  LEU A  23       9.464  55.644  24.082  1.00 13.45           C  
ATOM    160  CD1 LEU A  23       9.037  56.111  22.705  1.00 14.02           C  
ATOM    161  CD2 LEU A  23       8.676  56.404  25.158  1.00 15.31           C  
ATOM    162  N   ILE A  24      12.223  53.072  24.350  1.00 12.12           N  
ATOM    163  CA  ILE A  24      13.644  53.346  24.555  1.00 12.59           C  
ATOM    164  C   ILE A  24      14.421  52.967  23.294  1.00 12.72           C  
ATOM    165  O   ILE A  24      15.296  53.699  22.860  1.00 13.06           O  
ATOM    166  CB  ILE A  24      14.202  52.562  25.781  1.00 13.23           C  
ATOM    167  CG1 ILE A  24      13.602  53.128  27.069  1.00 18.32           C  
ATOM    168  CG2 ILE A  24      15.734  52.632  25.830  1.00 14.70           C  
ATOM    169  CD1 ILE A  24      13.898  54.585  27.298  1.00 16.88           C  
ATOM    170  N   ALA A  25      14.099  51.816  22.709  1.00 12.54           N  
ATOM    171  CA  ALA A  25      14.777  51.369  21.500  1.00 11.88           C  
ATOM    172  C   ALA A  25      14.488  52.299  20.323  1.00 11.45           C  
ATOM    173  O   ALA A  25      15.399  52.645  19.564  1.00  9.69           O  
ATOM    174  CB  ALA A  25      14.356  49.944  21.160  1.00 13.02           C  
ATOM    175  N   ALA A  26      13.228  52.715  20.170  1.00 10.77           N  
ATOM    176  CA  ALA A  26      12.878  53.616  19.071  1.00  9.54           C  
ATOM    177  C   ALA A  26      13.550  54.968  19.251  1.00 10.30           C  
ATOM    178  O   ALA A  26      14.151  55.500  18.324  1.00 11.03           O  
ATOM    179  CB  ALA A  26      11.363  53.803  18.987  1.00 10.31           C  
ATOM    180  N   LEU A  27      13.468  55.521  20.459  1.00  9.88           N  
ATOM    181  CA  LEU A  27      14.054  56.826  20.722  1.00  9.53           C  
ATOM    182  C   LEU A  27      15.578  56.806  20.611  1.00 10.44           C  
ATOM    183  O   LEU A  27      16.180  57.709  20.004  1.00 11.46           O  
ATOM    184  CB  LEU A  27      13.626  57.318  22.117  1.00 10.81           C  
ATOM    185  CG  LEU A  27      14.080  58.735  22.502  1.00 11.12           C  
ATOM    186  CD1 LEU A  27      13.502  59.728  21.517  1.00 10.47           C  
ATOM    187  CD2 LEU A  27      13.639  59.071  23.940  1.00 11.72           C  
ATOM    188  N   GLY A  28      16.203  55.787  21.194  1.00 10.79           N  
ATOM    189  CA  GLY A  28      17.656  55.691  21.139  1.00 12.14           C  
ATOM    190  C   GLY A  28      18.165  55.573  19.709  1.00 12.36           C  
ATOM    191  O   GLY A  28      19.120  56.254  19.312  1.00 10.26           O  
ATOM    192  N   SER A  29      17.535  54.716  18.907  1.00 10.36           N  
ATOM    193  CA  SER A  29      17.995  54.570  17.526  1.00 10.53           C  
ATOM    194  C   SER A  29      17.716  55.837  16.713  1.00 10.09           C  
ATOM    195  O   SER A  29      18.513  56.212  15.856  1.00 10.58           O  
ATOM    196  CB  SER A  29      17.361  53.337  16.850  1.00  9.87           C  
ATOM    197  OG  SER A  29      15.943  53.425  16.827  1.00 10.72           O  
ATOM    198  N   TYR A  30      16.593  56.500  16.983  1.00  9.68           N  
ATOM    199  CA  TYR A  30      16.243  57.736  16.280  1.00 11.17           C  
ATOM    200  C   TYR A  30      17.242  58.853  16.608  1.00 11.07           C  
ATOM    201  O   TYR A  30      17.783  59.519  15.712  1.00  9.91           O  
ATOM    202  CB  TYR A  30      14.815  58.159  16.684  1.00 10.69           C  
ATOM    203  CG  TYR A  30      14.370  59.516  16.190  1.00 11.08           C  
ATOM    204  CD1 TYR A  30      14.687  60.674  16.894  1.00 10.68           C  
ATOM    205  CD2 TYR A  30      13.654  59.638  14.997  1.00 13.93           C  
ATOM    206  CE1 TYR A  30      14.308  61.929  16.410  1.00 13.16           C  
ATOM    207  CE2 TYR A  30      13.265  60.876  14.511  1.00 14.33           C  
ATOM    208  CZ  TYR A  30      13.599  62.019  15.221  1.00 14.72           C  
ATOM    209  OH  TYR A  30      13.234  63.256  14.731  1.00 16.16           O  
ATOM    210  N   LEU A  31      17.515  59.046  17.893  1.00 10.73           N  
ATOM    211  CA  LEU A  31      18.412  60.124  18.286  1.00 12.18           C  
ATOM    212  C   LEU A  31      19.831  59.917  17.746  1.00 12.84           C  
ATOM    213  O   LEU A  31      20.457  60.857  17.255  1.00 12.29           O  
ATOM    214  CB  LEU A  31      18.417  60.272  19.812  1.00 11.18           C  
ATOM    215  CG  LEU A  31      17.100  60.790  20.421  1.00 10.93           C  
ATOM    216  CD1 LEU A  31      17.265  60.824  21.926  1.00 10.09           C  
ATOM    217  CD2 LEU A  31      16.747  62.219  19.894  1.00 13.22           C  
ATOM    218  N   GLN A  32      20.336  58.688  17.818  1.00 13.38           N  
ATOM    219  CA  GLN A  32      21.674  58.408  17.301  1.00 13.09           C  
ATOM    220  C   GLN A  32      21.699  58.607  15.779  1.00 13.39           C  
ATOM    221  O   GLN A  32      22.651  59.182  15.244  1.00 13.25           O  
ATOM    222  CB  GLN A  32      22.098  56.980  17.678  1.00 14.33           C  
ATOM    223  CG  GLN A  32      23.356  56.467  16.971  1.00 15.65           C  
ATOM    224  CD  GLN A  32      24.664  57.087  17.455  1.00 17.84           C  
ATOM    225  OE1 GLN A  32      24.686  58.003  18.289  1.00 16.69           O  
ATOM    226  NE2 GLN A  32      25.772  56.584  16.914  1.00 16.67           N  
ATOM    227  N   ALA A  33      20.661  58.143  15.080  1.00 12.51           N  
ATOM    228  CA  ALA A  33      20.599  58.310  13.628  1.00 12.99           C  
ATOM    229  C   ALA A  33      20.578  59.794  13.247  1.00 13.51           C  
ATOM    230  O   ALA A  33      21.367  60.243  12.409  1.00 13.66           O  
ATOM    231  CB  ALA A  33      19.353  57.608  13.059  1.00 14.29           C  
ATOM    232  N   ARG A  34      19.682  60.559  13.864  1.00 12.09           N  
ATOM    233  CA  ARG A  34      19.585  61.988  13.556  1.00 13.81           C  
ATOM    234  C   ARG A  34      20.834  62.777  13.975  1.00 14.85           C  
ATOM    235  O   ARG A  34      21.219  63.736  13.300  1.00 14.47           O  
ATOM    236  CB  ARG A  34      18.344  62.599  14.215  1.00 14.03           C  
ATOM    237  CG  ARG A  34      17.013  62.027  13.717  1.00 18.76           C  
ATOM    238  CD  ARG A  34      16.916  61.971  12.202  1.00 23.14           C  
ATOM    239  NE  ARG A  34      15.579  61.543  11.771  1.00 24.55           N  
ATOM    240  CZ  ARG A  34      15.314  60.981  10.595  1.00 24.06           C  
ATOM    241  NH1 ARG A  34      14.066  60.629  10.287  1.00 22.06           N  
ATOM    242  NH2 ARG A  34      16.299  60.755   9.730  1.00 21.31           N  
ATOM    243  N   ALA A  35      21.458  62.387  15.083  1.00 14.54           N  
ATOM    244  CA  ALA A  35      22.663  63.066  15.548  1.00 17.36           C  
ATOM    245  C   ALA A  35      23.788  62.834  14.546  1.00 18.72           C  
ATOM    246  O   ALA A  35      24.627  63.711  14.332  1.00 20.20           O  
ATOM    247  CB  ALA A  35      23.074  62.553  16.926  1.00 15.55           C  
ATOM    248  N   ARG A  36      23.792  61.655  13.931  1.00 17.45           N  
ATOM    249  CA  ARG A  36      24.810  61.291  12.943  1.00 16.90           C  
ATOM    250  C   ARG A  36      24.420  61.754  11.533  1.00 18.09           C  
ATOM    251  O   ARG A  36      25.053  61.367  10.545  1.00 18.23           O  
ATOM    252  CB  ARG A  36      25.033  59.773  12.969  1.00 16.47           C  
ATOM    253  CG  ARG A  36      25.788  59.265  14.210  1.00 18.91           C  
ATOM    254  CD  ARG A  36      27.292  59.559  14.116  1.00 21.13           C  
ATOM    255  NE  ARG A  36      27.903  58.806  13.021  1.00 22.07           N  
ATOM    256  CZ  ARG A  36      28.302  57.534  13.102  1.00 21.89           C  
ATOM    257  NH1 ARG A  36      28.826  56.939  12.044  1.00 24.17           N  
ATOM    258  NH2 ARG A  36      28.217  56.863  14.240  1.00 23.75           N  
ATOM    259  N   GLN A  37      23.386  62.590  11.464  1.00 17.61           N  
ATOM    260  CA  GLN A  37      22.876  63.140  10.206  1.00 21.72           C  
ATOM    261  C   GLN A  37      22.530  62.063   9.193  1.00 20.30           C  
ATOM    262  O   GLN A  37      22.718  62.229   7.984  1.00 19.46           O  
ATOM    263  CB  GLN A  37      23.891  64.128   9.620  1.00 25.85           C  
ATOM    264  CG  GLN A  37      24.037  65.364  10.491  1.00 31.39           C  
ATOM    265  CD  GLN A  37      24.928  66.422   9.876  1.00 35.57           C  
ATOM    266  OE1 GLN A  37      26.137  66.232   9.743  1.00 39.05           O  
ATOM    267  NE2 GLN A  37      24.333  67.545   9.496  1.00 37.62           N  
ATOM    268  N   GLY A  38      21.984  60.961   9.701  1.00 17.26           N  
ATOM    269  CA  GLY A  38      21.629  59.855   8.829  1.00 16.02           C  
ATOM    270  C   GLY A  38      20.145  59.607   8.679  1.00 14.85           C  
ATOM    271  O   GLY A  38      19.316  60.412   9.091  1.00 15.99           O  
ATOM    272  N   ARG A  39      19.810  58.475   8.079  1.00 14.11           N  
ATOM    273  CA  ARG A  39      18.412  58.122   7.880  1.00 14.91           C  
ATOM    274  C   ARG A  39      17.980  57.185   9.011  1.00 12.75           C  
ATOM    275  O   ARG A  39      18.805  56.474   9.575  1.00 13.88           O  
ATOM    276  CB  ARG A  39      18.239  57.423   6.528  1.00 17.16           C  
ATOM    277  CG  ARG A  39      18.748  58.250   5.343  1.00 25.40           C  
ATOM    278  CD  ARG A  39      17.685  58.379   4.259  1.00 29.57           C  
ATOM    279  NE  ARG A  39      17.148  57.070   3.900  1.00 34.30           N  
ATOM    280  CZ  ARG A  39      17.860  56.102   3.328  1.00 36.88           C  
ATOM    281  NH1 ARG A  39      17.295  54.931   3.046  1.00 33.41           N  
ATOM    282  NH2 ARG A  39      19.135  56.316   3.016  1.00 39.96           N  
ATOM    283  N   TRP A  40      16.690  57.215   9.346  1.00 12.12           N  
ATOM    284  CA  TRP A  40      16.137  56.353  10.390  1.00 11.28           C  
ATOM    285  C   TRP A  40      14.948  55.651   9.760  1.00 11.07           C  
ATOM    286  O   TRP A  40      13.970  56.292   9.375  1.00 12.17           O  
ATOM    287  CB  TRP A  40      15.659  57.168  11.586  1.00 10.89           C  
ATOM    288  CG  TRP A  40      15.130  56.318  12.711  1.00 10.49           C  
ATOM    289  CD1 TRP A  40      15.841  55.439  13.500  1.00 10.77           C  
ATOM    290  CD2 TRP A  40      13.789  56.316  13.211  1.00  9.61           C  
ATOM    291  NE1 TRP A  40      15.012  54.902  14.472  1.00 10.60           N  
ATOM    292  CE2 TRP A  40      13.751  55.424  14.314  1.00 10.44           C  
ATOM    293  CE3 TRP A  40      12.614  56.988  12.838  1.00 11.41           C  
ATOM    294  CZ2 TRP A  40      12.577  55.187  15.043  1.00 11.47           C  
ATOM    295  CZ3 TRP A  40      11.440  56.752  13.569  1.00 13.54           C  
ATOM    296  CH2 TRP A  40      11.436  55.856  14.659  1.00 12.19           C  
ATOM    297  N   LEU A  41      15.048  54.334   9.640  1.00 10.29           N  
ATOM    298  CA  LEU A  41      13.998  53.544   9.014  1.00 10.43           C  
ATOM    299  C   LEU A  41      13.161  52.769  10.009  1.00 11.85           C  
ATOM    300  O   LEU A  41      13.601  52.514  11.121  1.00 12.01           O  
ATOM    301  CB  LEU A  41      14.633  52.532   8.054  1.00  9.53           C  
ATOM    302  CG  LEU A  41      15.704  53.105   7.126  1.00 10.46           C  
ATOM    303  CD1 LEU A  41      16.262  52.002   6.230  1.00 12.57           C  
ATOM    304  CD2 LEU A  41      15.114  54.222   6.302  1.00 14.26           C  
ATOM    305  N   VAL A  42      11.951  52.384   9.602  1.00 10.13           N  
ATOM    306  CA  VAL A  42      11.116  51.557  10.466  1.00 10.42           C  
ATOM    307  C   VAL A  42      10.726  50.294   9.698  1.00 12.49           C  
ATOM    308  O   VAL A  42      10.285  50.368   8.548  1.00 13.95           O  
ATOM    309  CB  VAL A  42       9.834  52.300  10.925  1.00 11.79           C  
ATOM    310  CG1 VAL A  42       8.858  51.319  11.584  1.00 12.53           C  
ATOM    311  CG2 VAL A  42      10.205  53.389  11.895  1.00 12.69           C  
ATOM    312  N   ARG A  43      10.932  49.138  10.327  1.00 10.64           N  
ATOM    313  CA  ARG A  43      10.584  47.858   9.732  1.00 11.06           C  
ATOM    314  C   ARG A  43       9.688  47.088  10.692  1.00 10.41           C  
ATOM    315  O   ARG A  43      10.022  46.922  11.869  1.00 10.91           O  
ATOM    316  CB  ARG A  43      11.846  47.034   9.440  1.00 10.52           C  
ATOM    317  CG  ARG A  43      11.569  45.597   8.945  1.00 11.98           C  
ATOM    318  CD  ARG A  43      12.867  44.911   8.497  1.00 12.90           C  
ATOM    319  NE  ARG A  43      13.737  44.557   9.623  1.00  9.97           N  
ATOM    320  CZ  ARG A  43      14.985  45.000   9.787  1.00 11.46           C  
ATOM    321  NH1 ARG A  43      15.537  45.830   8.910  1.00 11.48           N  
ATOM    322  NH2 ARG A  43      15.693  44.577  10.823  1.00 12.46           N  
ATOM    323  N   ILE A  44       8.542  46.629  10.203  1.00  8.76           N  
ATOM    324  CA  ILE A  44       7.646  45.847  11.054  1.00  9.26           C  
ATOM    325  C   ILE A  44       8.056  44.400  10.883  1.00 10.82           C  
ATOM    326  O   ILE A  44       8.027  43.870   9.769  1.00 11.53           O  
ATOM    327  CB  ILE A  44       6.178  45.983  10.637  1.00  9.83           C  
ATOM    328  CG1 ILE A  44       5.735  47.437  10.769  1.00  9.77           C  
ATOM    329  CG2 ILE A  44       5.319  45.080  11.503  1.00 10.57           C  
ATOM    330  CD1 ILE A  44       5.774  47.977  12.204  1.00 13.77           C  
ATOM    331  N   GLU A  45       8.445  43.760  11.977  1.00 11.41           N  
ATOM    332  CA  GLU A  45       8.894  42.377  11.882  1.00 12.80           C  
ATOM    333  C   GLU A  45       7.736  41.413  12.135  1.00 13.34           C  
ATOM    334  O   GLU A  45       7.716  40.656  13.115  1.00 15.00           O  
ATOM    335  CB  GLU A  45      10.070  42.160  12.842  1.00 15.44           C  
ATOM    336  CG  GLU A  45      11.226  43.132  12.535  1.00 16.12           C  
ATOM    337  CD  GLU A  45      12.626  42.548  12.807  1.00 16.88           C  
ATOM    338  OE1 GLU A  45      12.790  41.822  13.805  1.00 17.65           O  
ATOM    339  OE2 GLU A  45      13.567  42.831  12.024  1.00 17.92           O  
ATOM    340  N   ASP A  46       6.770  41.460  11.224  1.00 14.20           N  
ATOM    341  CA  ASP A  46       5.592  40.610  11.316  1.00 15.91           C  
ATOM    342  C   ASP A  46       5.854  39.322  10.548  1.00 17.73           C  
ATOM    343  O   ASP A  46       5.169  38.982   9.580  1.00 17.38           O  
ATOM    344  CB  ASP A  46       4.363  41.358  10.790  1.00 16.58           C  
ATOM    345  CG  ASP A  46       4.474  41.767   9.331  1.00 18.47           C  
ATOM    346  OD1 ASP A  46       5.592  41.998   8.813  1.00 16.57           O  
ATOM    347  OD2 ASP A  46       3.406  41.882   8.692  1.00 18.25           O  
ATOM    348  N   ILE A  47       6.854  38.601  11.033  1.00 19.19           N  
ATOM    349  CA  ILE A  47       7.293  37.356  10.426  1.00 22.73           C  
ATOM    350  C   ILE A  47       6.700  36.102  11.077  1.00 25.84           C  
ATOM    351  O   ILE A  47       6.998  34.982  10.650  1.00 27.43           O  
ATOM    352  CB  ILE A  47       8.835  37.291  10.481  1.00 24.50           C  
ATOM    353  CG1 ILE A  47       9.358  36.280   9.466  1.00 25.92           C  
ATOM    354  CG2 ILE A  47       9.287  36.925  11.881  1.00 22.96           C  
ATOM    355  CD1 ILE A  47      10.876  36.235   9.390  1.00 29.83           C  
ATOM    356  N   ASP A  48       5.872  36.284  12.107  1.00 27.46           N  
ATOM    357  CA  ASP A  48       5.255  35.155  12.803  1.00 31.54           C  
ATOM    358  C   ASP A  48       3.785  35.425  13.133  1.00 32.44           C  
ATOM    359  O   ASP A  48       3.441  35.834  14.244  1.00 31.04           O  
ATOM    360  CB  ASP A  48       6.049  34.830  14.070  1.00 32.85           C  
ATOM    361  CG  ASP A  48       5.435  33.697  14.875  1.00 36.99           C  
ATOM    362  OD1 ASP A  48       4.732  32.846  14.293  1.00 38.20           O  
ATOM    363  OD2 ASP A  48       5.676  33.654  16.097  1.00 40.07           O  
ATOM    364  N   PRO A  49       2.901  35.189  12.153  1.00 34.86           N  
ATOM    365  CA  PRO A  49       1.449  35.371  12.220  1.00 36.69           C  
ATOM    366  C   PRO A  49       0.805  34.932  13.531  1.00 37.82           C  
ATOM    367  O   PRO A  49       0.027  35.684  14.115  1.00 37.95           O  
ATOM    368  CB  PRO A  49       0.947  34.559  11.028  1.00 37.00           C  
ATOM    369  CG  PRO A  49       2.045  34.751  10.027  1.00 36.77           C  
ATOM    370  CD  PRO A  49       3.285  34.564  10.872  1.00 36.11           C  
ATOM    371  N   PRO A  50       1.126  33.713  14.012  1.00 38.98           N  
ATOM    372  CA  PRO A  50       0.559  33.196  15.263  1.00 39.18           C  
ATOM    373  C   PRO A  50       0.639  34.159  16.442  1.00 38.31           C  
ATOM    374  O   PRO A  50      -0.380  34.459  17.067  1.00 39.72           O  
ATOM    375  CB  PRO A  50       1.371  31.927  15.511  1.00 40.13           C  
ATOM    376  CG  PRO A  50       1.628  31.436  14.131  1.00 40.66           C  
ATOM    377  CD  PRO A  50       2.023  32.711  13.406  1.00 40.19           C  
ATOM    378  N   ARG A  51       1.848  34.627  16.741  1.00 36.21           N  
ATOM    379  CA  ARG A  51       2.080  35.541  17.856  1.00 36.06           C  
ATOM    380  C   ARG A  51       1.826  37.016  17.550  1.00 32.69           C  
ATOM    381  O   ARG A  51       2.027  37.875  18.409  1.00 33.90           O  
ATOM    382  CB  ARG A  51       3.511  35.381  18.372  1.00 40.55           C  
ATOM    383  CG  ARG A  51       3.723  34.182  19.277  1.00 45.64           C  
ATOM    384  CD  ARG A  51       5.124  34.197  19.884  1.00 50.04           C  
ATOM    385  NE  ARG A  51       6.141  33.734  18.945  1.00 53.86           N  
ATOM    386  CZ  ARG A  51       6.194  32.497  18.461  1.00 55.98           C  
ATOM    387  NH1 ARG A  51       7.155  32.155  17.611  1.00 57.60           N  
ATOM    388  NH2 ARG A  51       5.283  31.600  18.823  1.00 57.29           N  
ATOM    389  N   GLU A  52       1.407  37.323  16.332  1.00 27.59           N  
ATOM    390  CA  GLU A  52       1.135  38.712  15.992  1.00 25.47           C  
ATOM    391  C   GLU A  52      -0.269  39.063  16.481  1.00 22.55           C  
ATOM    392  O   GLU A  52      -1.134  38.200  16.600  1.00 21.45           O  
ATOM    393  CB  GLU A  52       1.216  38.942  14.478  1.00 26.98           C  
ATOM    394  CG  GLU A  52       0.915  40.384  14.066  1.00 30.28           C  
ATOM    395  CD  GLU A  52       0.973  40.617  12.568  1.00 31.21           C  
ATOM    396  OE1 GLU A  52       1.286  39.666  11.820  1.00 33.78           O  
ATOM    397  OE2 GLU A  52       0.708  41.759  12.136  1.00 32.54           O  
ATOM    398  N   VAL A  53      -0.479  40.330  16.800  1.00 18.35           N  
ATOM    399  CA  VAL A  53      -1.797  40.761  17.233  1.00 16.40           C  
ATOM    400  C   VAL A  53      -2.355  41.662  16.145  1.00 15.30           C  
ATOM    401  O   VAL A  53      -1.724  42.658  15.765  1.00 15.68           O  
ATOM    402  CB  VAL A  53      -1.746  41.573  18.562  1.00 13.70           C  
ATOM    403  CG1 VAL A  53      -3.164  42.045  18.942  1.00 13.56           C  
ATOM    404  CG2 VAL A  53      -1.165  40.721  19.684  1.00 15.45           C  
ATOM    405  N   PRO A  54      -3.535  41.321  15.603  1.00 15.12           N  
ATOM    406  CA  PRO A  54      -4.119  42.171  14.562  1.00 15.40           C  
ATOM    407  C   PRO A  54      -4.228  43.616  15.065  1.00 14.13           C  
ATOM    408  O   PRO A  54      -4.697  43.863  16.180  1.00 13.79           O  
ATOM    409  CB  PRO A  54      -5.498  41.552  14.343  1.00 16.77           C  
ATOM    410  CG  PRO A  54      -5.245  40.091  14.616  1.00 18.79           C  
ATOM    411  CD  PRO A  54      -4.357  40.115  15.832  1.00 16.40           C  
ATOM    412  N   GLY A  55      -3.781  44.556  14.241  1.00 12.50           N  
ATOM    413  CA  GLY A  55      -3.843  45.956  14.608  1.00 14.13           C  
ATOM    414  C   GLY A  55      -2.663  46.491  15.403  1.00 13.17           C  
ATOM    415  O   GLY A  55      -2.526  47.707  15.527  1.00 13.90           O  
ATOM    416  N   ALA A  56      -1.808  45.618  15.933  1.00 12.41           N  
ATOM    417  CA  ALA A  56      -0.674  46.090  16.728  1.00 12.10           C  
ATOM    418  C   ALA A  56       0.347  46.871  15.901  1.00 12.83           C  
ATOM    419  O   ALA A  56       0.861  47.893  16.356  1.00 12.91           O  
ATOM    420  CB  ALA A  56       0.002  44.921  17.429  1.00 12.57           C  
ATOM    421  N   ALA A  57       0.643  46.391  14.692  1.00 12.95           N  
ATOM    422  CA  ALA A  57       1.604  47.077  13.832  1.00 13.22           C  
ATOM    423  C   ALA A  57       1.121  48.495  13.587  1.00 14.17           C  
ATOM    424  O   ALA A  57       1.879  49.451  13.726  1.00 14.45           O  
ATOM    425  CB  ALA A  57       1.765  46.329  12.503  1.00 14.61           C  
ATOM    426  N   GLU A  58      -0.155  48.634  13.241  1.00 13.82           N  
ATOM    427  CA  GLU A  58      -0.713  49.951  12.992  1.00 14.51           C  
ATOM    428  C   GLU A  58      -0.654  50.815  14.255  1.00 12.48           C  
ATOM    429  O   GLU A  58      -0.383  52.010  14.175  1.00 12.00           O  
ATOM    430  CB  GLU A  58      -2.161  49.818  12.525  1.00 17.20           C  
ATOM    431  CG  GLU A  58      -2.339  49.181  11.139  1.00 22.65           C  
ATOM    432  CD  GLU A  58      -1.975  47.689  11.049  1.00 25.83           C  
ATOM    433  OE1 GLU A  58      -2.002  46.947  12.068  1.00 22.04           O  
ATOM    434  OE2 GLU A  58      -1.671  47.251   9.914  1.00 29.72           O  
ATOM    435  N   THR A  59      -0.937  50.221  15.411  1.00 12.98           N  
ATOM    436  CA  THR A  59      -0.889  50.986  16.667  1.00 11.71           C  
ATOM    437  C   THR A  59       0.511  51.530  16.899  1.00 12.60           C  
ATOM    438  O   THR A  59       0.691  52.691  17.281  1.00 12.08           O  
ATOM    439  CB  THR A  59      -1.284  50.115  17.863  1.00 10.69           C  
ATOM    440  OG1 THR A  59      -2.670  49.773  17.741  1.00 12.55           O  
ATOM    441  CG2 THR A  59      -1.052  50.838  19.181  1.00 12.57           C  
ATOM    442  N   ILE A  60       1.497  50.672  16.671  1.00 11.67           N  
ATOM    443  CA  ILE A  60       2.900  51.054  16.844  1.00 11.94           C  
ATOM    444  C   ILE A  60       3.270  52.228  15.946  1.00 11.21           C  
ATOM    445  O   ILE A  60       3.881  53.192  16.406  1.00 11.75           O  
ATOM    446  CB  ILE A  60       3.829  49.868  16.544  1.00 13.76           C  
ATOM    447  CG1 ILE A  60       3.634  48.786  17.613  1.00 15.55           C  
ATOM    448  CG2 ILE A  60       5.291  50.337  16.512  1.00 13.20           C  
ATOM    449  CD1 ILE A  60       4.215  47.414  17.237  1.00 18.17           C  
ATOM    450  N   LEU A  61       2.905  52.163  14.670  1.00 11.30           N  
ATOM    451  CA  LEU A  61       3.253  53.258  13.771  1.00 11.74           C  
ATOM    452  C   LEU A  61       2.565  54.539  14.240  1.00 13.33           C  
ATOM    453  O   LEU A  61       3.170  55.615  14.219  1.00 13.15           O  
ATOM    454  CB  LEU A  61       2.847  52.933  12.325  1.00 13.66           C  
ATOM    455  CG  LEU A  61       3.547  51.696  11.735  1.00 12.43           C  
ATOM    456  CD1 LEU A  61       3.027  51.423  10.336  1.00 14.43           C  
ATOM    457  CD2 LEU A  61       5.059  51.915  11.726  1.00 14.57           C  
ATOM    458  N   ARG A  62       1.308  54.420  14.674  1.00 12.36           N  
ATOM    459  CA  ARG A  62       0.567  55.588  15.161  1.00 14.95           C  
ATOM    460  C   ARG A  62       1.233  56.125  16.425  1.00 14.28           C  
ATOM    461  O   ARG A  62       1.335  57.335  16.617  1.00 14.61           O  
ATOM    462  CB  ARG A  62      -0.885  55.210  15.470  1.00 19.69           C  
ATOM    463  CG  ARG A  62      -1.720  56.330  16.081  1.00 25.72           C  
ATOM    464  CD  ARG A  62      -3.091  55.794  16.470  1.00 32.13           C  
ATOM    465  NE  ARG A  62      -3.369  54.557  15.739  1.00 37.53           N  
ATOM    466  CZ  ARG A  62      -4.471  53.825  15.872  1.00 40.23           C  
ATOM    467  NH1 ARG A  62      -5.428  54.201  16.719  1.00 40.56           N  
ATOM    468  NH2 ARG A  62      -4.606  52.708  15.161  1.00 36.53           N  
ATOM    469  N   GLN A  63       1.688  55.226  17.289  1.00 13.01           N  
ATOM    470  CA  GLN A  63       2.363  55.656  18.511  1.00 13.95           C  
ATOM    471  C   GLN A  63       3.677  56.374  18.201  1.00 13.82           C  
ATOM    472  O   GLN A  63       4.010  57.368  18.844  1.00 13.30           O  
ATOM    473  CB  GLN A  63       2.657  54.468  19.429  1.00 14.40           C  
ATOM    474  CG  GLN A  63       1.444  53.915  20.182  1.00 15.06           C  
ATOM    475  CD  GLN A  63       1.802  52.657  20.976  1.00 16.91           C  
ATOM    476  OE1 GLN A  63       2.232  51.660  20.406  1.00 17.63           O  
ATOM    477  NE2 GLN A  63       1.650  52.715  22.291  1.00 19.51           N  
ATOM    478  N   LEU A  64       4.435  55.872  17.231  1.00 13.10           N  
ATOM    479  CA  LEU A  64       5.702  56.535  16.906  1.00 14.12           C  
ATOM    480  C   LEU A  64       5.439  57.978  16.486  1.00 15.39           C  
ATOM    481  O   LEU A  64       6.111  58.902  16.934  1.00 15.65           O  
ATOM    482  CB  LEU A  64       6.435  55.791  15.787  1.00 13.11           C  
ATOM    483  CG  LEU A  64       6.981  54.417  16.200  1.00 12.40           C  
ATOM    484  CD1 LEU A  64       7.488  53.685  14.970  1.00 14.34           C  
ATOM    485  CD2 LEU A  64       8.123  54.581  17.225  1.00 11.62           C  
ATOM    486  N   GLU A  65       4.428  58.170  15.649  1.00 16.78           N  
ATOM    487  CA  GLU A  65       4.105  59.515  15.188  1.00 17.37           C  
ATOM    488  C   GLU A  65       3.644  60.410  16.337  1.00 16.36           C  
ATOM    489  O   GLU A  65       4.009  61.593  16.401  1.00 17.11           O  
ATOM    490  CB  GLU A  65       3.034  59.443  14.116  1.00 18.80           C  
ATOM    491  CG  GLU A  65       3.475  58.688  12.896  1.00 26.94           C  
ATOM    492  CD  GLU A  65       2.413  58.678  11.831  1.00 32.17           C  
ATOM    493  OE1 GLU A  65       1.275  58.264  12.146  1.00 35.66           O  
ATOM    494  OE2 GLU A  65       2.717  59.077  10.684  1.00 35.44           O  
ATOM    495  N   HIS A  66       2.856  59.834  17.237  1.00 16.91           N  
ATOM    496  CA  HIS A  66       2.318  60.539  18.404  1.00 18.68           C  
ATOM    497  C   HIS A  66       3.448  61.028  19.308  1.00 19.42           C  
ATOM    498  O   HIS A  66       3.331  62.083  19.953  1.00 19.59           O  
ATOM    499  CB  HIS A  66       1.371  59.598  19.170  1.00 19.94           C  
ATOM    500  CG  HIS A  66       0.753  60.207  20.394  1.00 23.62           C  
ATOM    501  ND1 HIS A  66      -0.021  61.348  20.353  1.00 25.52           N  
ATOM    502  CD2 HIS A  66       0.769  59.811  21.689  1.00 25.48           C  
ATOM    503  CE1 HIS A  66      -0.458  61.626  21.568  1.00 25.26           C  
ATOM    504  NE2 HIS A  66       0.005  60.709  22.398  1.00 27.18           N  
ATOM    505  N   TYR A  67       4.540  60.267  19.351  1.00 16.73           N  
ATOM    506  CA  TYR A  67       5.698  60.618  20.160  1.00 17.43           C  
ATOM    507  C   TYR A  67       6.719  61.439  19.371  1.00 17.69           C  
ATOM    508  O   TYR A  67       7.840  61.659  19.827  1.00 18.92           O  
ATOM    509  CB  TYR A  67       6.333  59.345  20.728  1.00 19.61           C  
ATOM    510  CG  TYR A  67       5.584  58.826  21.929  1.00 20.04           C  
ATOM    511  CD1 TYR A  67       6.014  59.121  23.218  1.00 23.25           C  
ATOM    512  CD2 TYR A  67       4.396  58.114  21.782  1.00 23.19           C  
ATOM    513  CE1 TYR A  67       5.280  58.722  24.330  1.00 21.77           C  
ATOM    514  CE2 TYR A  67       3.653  57.714  22.893  1.00 25.74           C  
ATOM    515  CZ  TYR A  67       4.107  58.023  24.164  1.00 23.92           C  
ATOM    516  OH  TYR A  67       3.399  57.616  25.269  1.00 24.95           O  
ATOM    517  N   GLY A  68       6.315  61.875  18.181  1.00 17.01           N  
ATOM    518  CA  GLY A  68       7.160  62.703  17.330  1.00 17.24           C  
ATOM    519  C   GLY A  68       8.289  62.038  16.564  1.00 17.11           C  
ATOM    520  O   GLY A  68       9.145  62.727  16.008  1.00 18.57           O  
ATOM    521  N   LEU A  69       8.269  60.713  16.494  1.00 14.72           N  
ATOM    522  CA  LEU A  69       9.326  59.950  15.823  1.00 16.07           C  
ATOM    523  C   LEU A  69       8.925  59.595  14.397  1.00 16.98           C  
ATOM    524  O   LEU A  69       8.226  58.606  14.172  1.00 20.82           O  
ATOM    525  CB  LEU A  69       9.612  58.675  16.631  1.00 15.03           C  
ATOM    526  CG  LEU A  69       9.981  58.937  18.094  1.00 15.85           C  
ATOM    527  CD1 LEU A  69      10.070  57.624  18.860  1.00 18.03           C  
ATOM    528  CD2 LEU A  69      11.295  59.690  18.157  1.00 16.90           C  
ATOM    529  N   HIS A  70       9.376  60.402  13.438  1.00 16.25           N  
ATOM    530  CA  HIS A  70       9.048  60.198  12.030  1.00 16.33           C  
ATOM    531  C   HIS A  70      10.184  59.535  11.280  1.00 16.32           C  
ATOM    532  O   HIS A  70      11.344  59.952  11.368  1.00 17.02           O  
ATOM    533  CB  HIS A  70       8.688  61.544  11.390  1.00 18.20           C  
ATOM    534  CG  HIS A  70       7.524  62.209  12.047  1.00 21.14           C  
ATOM    535  ND1 HIS A  70       6.252  61.680  12.007  1.00 24.42           N  
ATOM    536  CD2 HIS A  70       7.451  63.309  12.833  1.00 21.97           C  
ATOM    537  CE1 HIS A  70       5.445  62.425  12.741  1.00 24.22           C  
ATOM    538  NE2 HIS A  70       6.147  63.419  13.255  1.00 23.71           N  
ATOM    539  N   TRP A  71       9.839  58.487  10.547  1.00 16.04           N  
ATOM    540  CA  TRP A  71      10.813  57.716   9.799  1.00 15.21           C  
ATOM    541  C   TRP A  71      10.984  58.192   8.364  1.00 17.07           C  
ATOM    542  O   TRP A  71      10.152  58.935   7.825  1.00 15.65           O  
ATOM    543  CB  TRP A  71      10.397  56.240   9.811  1.00 15.78           C  
ATOM    544  CG  TRP A  71       8.993  56.007   9.297  1.00 14.90           C  
ATOM    545  CD1 TRP A  71       8.609  55.800   7.994  1.00 15.56           C  
ATOM    546  CD2 TRP A  71       7.795  55.989  10.072  1.00 15.05           C  
ATOM    547  NE1 TRP A  71       7.245  55.659   7.917  1.00 14.92           N  
ATOM    548  CE2 TRP A  71       6.721  55.770   9.181  1.00 16.71           C  
ATOM    549  CE3 TRP A  71       7.519  56.142  11.443  1.00 16.03           C  
ATOM    550  CZ2 TRP A  71       5.395  55.693   9.613  1.00 16.21           C  
ATOM    551  CZ3 TRP A  71       6.184  56.065  11.875  1.00 13.89           C  
ATOM    552  CH2 TRP A  71       5.146  55.844  10.961  1.00 16.65           C  
ATOM    553  N   ASP A  72      12.073  57.751   7.749  1.00 16.62           N  
ATOM    554  CA  ASP A  72      12.367  58.100   6.372  1.00 17.84           C  
ATOM    555  C   ASP A  72      11.867  57.004   5.442  1.00 18.82           C  
ATOM    556  O   ASP A  72      11.939  55.816   5.765  1.00 19.02           O  
ATOM    557  CB  ASP A  72      13.873  58.261   6.172  1.00 18.37           C  
ATOM    558  CG  ASP A  72      14.466  59.331   7.054  1.00 19.10           C  
ATOM    559  OD1 ASP A  72      13.855  60.417   7.180  1.00 22.19           O  
ATOM    560  OD2 ASP A  72      15.555  59.095   7.608  1.00 20.24           O  
ATOM    561  N   GLY A  73      11.366  57.402   4.280  1.00 19.94           N  
ATOM    562  CA  GLY A  73      10.894  56.422   3.318  1.00 20.16           C  
ATOM    563  C   GLY A  73       9.657  55.647   3.717  1.00 19.63           C  
ATOM    564  O   GLY A  73       8.846  56.104   4.530  1.00 19.84           O  
ATOM    565  N   ASP A  74       9.506  54.463   3.129  1.00 18.40           N  
ATOM    566  CA  ASP A  74       8.362  53.615   3.415  1.00 18.64           C  
ATOM    567  C   ASP A  74       8.697  52.579   4.476  1.00 17.26           C  
ATOM    568  O   ASP A  74       9.840  52.149   4.604  1.00 17.23           O  
ATOM    569  CB  ASP A  74       7.906  52.854   2.164  1.00 20.80           C  
ATOM    570  CG  ASP A  74       7.531  53.770   1.013  1.00 24.52           C  
ATOM    571  OD1 ASP A  74       6.987  54.861   1.274  1.00 26.77           O  
ATOM    572  OD2 ASP A  74       7.766  53.380  -0.156  1.00 28.24           O  
ATOM    573  N   VAL A  75       7.685  52.185   5.233  1.00 16.04           N  
ATOM    574  CA  VAL A  75       7.852  51.157   6.246  1.00 13.75           C  
ATOM    575  C   VAL A  75       8.044  49.830   5.498  1.00 14.76           C  
ATOM    576  O   VAL A  75       7.316  49.543   4.537  1.00 15.63           O  
ATOM    577  CB  VAL A  75       6.576  51.060   7.138  1.00 13.94           C  
ATOM    578  CG1 VAL A  75       6.642  49.832   8.029  1.00 14.03           C  
ATOM    579  CG2 VAL A  75       6.433  52.332   7.996  1.00 15.33           C  
ATOM    580  N   LEU A  76       9.030  49.037   5.904  1.00 13.72           N  
ATOM    581  CA  LEU A  76       9.246  47.721   5.287  1.00 12.86           C  
ATOM    582  C   LEU A  76       8.510  46.713   6.157  1.00 12.42           C  
ATOM    583  O   LEU A  76       8.586  46.787   7.391  1.00 11.79           O  
ATOM    584  CB  LEU A  76      10.736  47.356   5.250  1.00 13.29           C  
ATOM    585  CG  LEU A  76      11.045  46.094   4.429  1.00 15.61           C  
ATOM    586  CD1 LEU A  76      10.931  46.442   2.951  1.00 19.56           C  
ATOM    587  CD2 LEU A  76      12.431  45.565   4.723  1.00 16.87           C  
ATOM    588  N   TRP A  77       7.791  45.777   5.530  1.00 12.46           N  
ATOM    589  CA  TRP A  77       7.038  44.756   6.268  1.00 12.63           C  
ATOM    590  C   TRP A  77       7.625  43.370   5.988  1.00 12.94           C  
ATOM    591  O   TRP A  77       7.666  42.947   4.827  1.00 14.33           O  
ATOM    592  CB  TRP A  77       5.559  44.771   5.827  1.00 13.91           C  
ATOM    593  CG  TRP A  77       4.866  46.077   6.072  1.00 15.12           C  
ATOM    594  CD1 TRP A  77       5.023  47.227   5.367  1.00 17.14           C  
ATOM    595  CD2 TRP A  77       3.937  46.373   7.125  1.00 15.54           C  
ATOM    596  NE1 TRP A  77       4.250  48.229   5.912  1.00 17.70           N  
ATOM    597  CE2 TRP A  77       3.577  47.732   6.993  1.00 16.77           C  
ATOM    598  CE3 TRP A  77       3.379  45.624   8.166  1.00 17.94           C  
ATOM    599  CZ2 TRP A  77       2.680  48.361   7.865  1.00 18.15           C  
ATOM    600  CZ3 TRP A  77       2.481  46.249   9.035  1.00 19.13           C  
ATOM    601  CH2 TRP A  77       2.145  47.610   8.875  1.00 17.94           C  
ATOM    602  N   GLN A  78       8.060  42.659   7.029  1.00 10.56           N  
ATOM    603  CA  GLN A  78       8.649  41.335   6.814  1.00 11.32           C  
ATOM    604  C   GLN A  78       7.657  40.349   6.201  1.00 12.90           C  
ATOM    605  O   GLN A  78       8.057  39.395   5.520  1.00 13.14           O  
ATOM    606  CB  GLN A  78       9.261  40.803   8.116  1.00 12.09           C  
ATOM    607  CG  GLN A  78      10.524  41.616   8.476  1.00 12.90           C  
ATOM    608  CD  GLN A  78      11.410  40.972   9.530  1.00 12.57           C  
ATOM    609  OE1 GLN A  78      12.652  41.137   9.505  1.00 17.86           O  
ATOM    610  NE2 GLN A  78      10.805  40.268  10.464  1.00 11.05           N  
ATOM    611  N   SER A  79       6.366  40.589   6.408  1.00 13.48           N  
ATOM    612  CA  SER A  79       5.353  39.712   5.821  1.00 13.67           C  
ATOM    613  C   SER A  79       5.382  39.817   4.289  1.00 14.48           C  
ATOM    614  O   SER A  79       4.794  38.982   3.592  1.00 15.09           O  
ATOM    615  CB  SER A  79       3.962  40.058   6.367  1.00 14.16           C  
ATOM    616  OG  SER A  79       3.633  41.418   6.128  1.00 14.96           O  
ATOM    617  N   GLN A  80       6.055  40.841   3.767  1.00 12.77           N  
ATOM    618  CA  GLN A  80       6.180  41.049   2.325  1.00 14.52           C  
ATOM    619  C   GLN A  80       7.623  40.795   1.880  1.00 15.08           C  
ATOM    620  O   GLN A  80       8.068  41.303   0.849  1.00 17.72           O  
ATOM    621  CB  GLN A  80       5.802  42.488   1.947  1.00 14.42           C  
ATOM    622  CG  GLN A  80       4.386  42.888   2.366  1.00 18.20           C  
ATOM    623  CD  GLN A  80       3.986  44.255   1.830  1.00 20.95           C  
ATOM    624  OE1 GLN A  80       4.773  45.206   1.861  1.00 21.53           O  
ATOM    625  NE2 GLN A  80       2.750  44.362   1.337  1.00 22.73           N  
ATOM    626  N   ARG A  81       8.350  40.005   2.657  1.00 13.36           N  
ATOM    627  CA  ARG A  81       9.738  39.727   2.343  1.00 12.96           C  
ATOM    628  C   ARG A  81      10.052  38.233   2.292  1.00 12.88           C  
ATOM    629  O   ARG A  81      11.223  37.850   2.215  1.00 13.23           O  
ATOM    630  CB  ARG A  81      10.635  40.402   3.396  1.00 12.57           C  
ATOM    631  CG  ARG A  81      10.623  41.928   3.304  1.00 12.97           C  
ATOM    632  CD  ARG A  81      11.523  42.440   2.170  1.00 13.25           C  
ATOM    633  NE  ARG A  81      12.931  42.136   2.450  1.00 12.48           N  
ATOM    634  CZ  ARG A  81      13.905  42.119   1.545  1.00 15.82           C  
ATOM    635  NH1 ARG A  81      15.149  41.813   1.920  1.00 15.62           N  
ATOM    636  NH2 ARG A  81      13.652  42.408   0.268  1.00 14.95           N  
ATOM    637  N   HIS A  82       9.023  37.390   2.310  1.00 13.40           N  
ATOM    638  CA  HIS A  82       9.262  35.958   2.316  1.00 14.51           C  
ATOM    639  C   HIS A  82      10.064  35.471   1.119  1.00 14.02           C  
ATOM    640  O   HIS A  82      10.848  34.538   1.256  1.00 13.81           O  
ATOM    641  CB  HIS A  82       7.948  35.173   2.434  1.00 17.31           C  
ATOM    642  CG  HIS A  82       7.322  35.257   3.797  1.00 21.07           C  
ATOM    643  ND1 HIS A  82       6.566  34.239   4.337  1.00 24.82           N  
ATOM    644  CD2 HIS A  82       7.345  36.242   4.728  1.00 21.57           C  
ATOM    645  CE1 HIS A  82       6.152  34.591   5.543  1.00 24.74           C  
ATOM    646  NE2 HIS A  82       6.610  35.803   5.803  1.00 24.20           N  
ATOM    647  N   ASP A  83       9.879  36.088  -0.043  1.00 14.86           N  
ATOM    648  CA  ASP A  83      10.647  35.658  -1.210  1.00 15.76           C  
ATOM    649  C   ASP A  83      12.118  35.989  -1.014  1.00 14.99           C  
ATOM    650  O   ASP A  83      12.985  35.253  -1.475  1.00 15.58           O  
ATOM    651  CB  ASP A  83      10.111  36.310  -2.486  1.00 20.37           C  
ATOM    652  CG  ASP A  83      10.162  37.816  -2.441  1.00 24.61           C  
ATOM    653  OD1 ASP A  83       9.918  38.382  -1.354  1.00 29.56           O  
ATOM    654  OD2 ASP A  83      10.430  38.438  -3.496  1.00 31.07           O  
ATOM    655  N   ALA A  84      12.402  37.089  -0.323  1.00 14.17           N  
ATOM    656  CA  ALA A  84      13.793  37.472  -0.069  1.00 14.34           C  
ATOM    657  C   ALA A  84      14.468  36.493   0.876  1.00 13.08           C  
ATOM    658  O   ALA A  84      15.642  36.176   0.701  1.00 13.33           O  
ATOM    659  CB  ALA A  84      13.868  38.885   0.500  1.00 12.45           C  
ATOM    660  N   TYR A  85      13.747  36.027   1.896  1.00 11.86           N  
ATOM    661  CA  TYR A  85      14.342  35.063   2.815  1.00 10.48           C  
ATOM    662  C   TYR A  85      14.565  33.751   2.058  1.00 12.99           C  
ATOM    663  O   TYR A  85      15.589  33.080   2.221  1.00 11.65           O  
ATOM    664  CB  TYR A  85      13.426  34.815   4.002  1.00 10.10           C  
ATOM    665  CG  TYR A  85      13.022  36.100   4.700  1.00  9.23           C  
ATOM    666  CD1 TYR A  85      13.930  37.154   4.847  1.00 12.25           C  
ATOM    667  CD2 TYR A  85      11.720  36.274   5.172  1.00 12.06           C  
ATOM    668  CE1 TYR A  85      13.541  38.374   5.450  1.00 10.71           C  
ATOM    669  CE2 TYR A  85      11.320  37.478   5.767  1.00 11.54           C  
ATOM    670  CZ  TYR A  85      12.232  38.521   5.899  1.00 12.87           C  
ATOM    671  OH  TYR A  85      11.802  39.720   6.448  1.00 13.37           O  
ATOM    672  N   ARG A  86      13.589  33.392   1.233  1.00 12.89           N  
ATOM    673  CA  ARG A  86      13.690  32.174   0.425  1.00 15.88           C  
ATOM    674  C   ARG A  86      14.940  32.202  -0.439  1.00 14.40           C  
ATOM    675  O   ARG A  86      15.687  31.220  -0.524  1.00 14.99           O  
ATOM    676  CB  ARG A  86      12.459  32.054  -0.490  1.00 18.26           C  
ATOM    677  CG  ARG A  86      12.509  30.872  -1.455  1.00 25.21           C  
ATOM    678  CD  ARG A  86      12.666  29.570  -0.696  1.00 30.17           C  
ATOM    679  NE  ARG A  86      11.566  29.309   0.228  1.00 34.79           N  
ATOM    680  CZ  ARG A  86      11.578  28.342   1.141  1.00 37.02           C  
ATOM    681  NH1 ARG A  86      10.537  28.173   1.935  1.00 40.90           N  
ATOM    682  NH2 ARG A  86      12.640  27.551   1.268  1.00 39.00           N  
ATOM    683  N   GLU A  87      15.143  33.334  -1.087  1.00 14.57           N  
ATOM    684  CA  GLU A  87      16.269  33.558  -1.980  1.00 16.59           C  
ATOM    685  C   GLU A  87      17.596  33.439  -1.249  1.00 16.99           C  
ATOM    686  O   GLU A  87      18.539  32.841  -1.765  1.00 14.18           O  
ATOM    687  CB  GLU A  87      16.121  34.944  -2.613  1.00 20.47           C  
ATOM    688  CG  GLU A  87      17.331  35.501  -3.326  1.00 26.13           C  
ATOM    689  CD  GLU A  87      17.063  36.891  -3.887  1.00 31.74           C  
ATOM    690  OE1 GLU A  87      16.464  36.986  -4.985  1.00 34.08           O  
ATOM    691  OE2 GLU A  87      17.430  37.890  -3.220  1.00 31.92           O  
ATOM    692  N   ALA A  88      17.670  33.996  -0.039  1.00 13.39           N  
ATOM    693  CA  ALA A  88      18.919  33.922   0.715  1.00 13.93           C  
ATOM    694  C   ALA A  88      19.203  32.487   1.157  1.00 13.18           C  
ATOM    695  O   ALA A  88      20.360  32.051   1.167  1.00 14.65           O  
ATOM    696  CB  ALA A  88      18.868  34.875   1.931  1.00 12.05           C  
ATOM    697  N   LEU A  89      18.161  31.751   1.517  1.00 12.76           N  
ATOM    698  CA  LEU A  89      18.318  30.357   1.920  1.00 14.75           C  
ATOM    699  C   LEU A  89      18.774  29.512   0.732  1.00 14.74           C  
ATOM    700  O   LEU A  89      19.580  28.605   0.885  1.00 14.39           O  
ATOM    701  CB  LEU A  89      17.007  29.786   2.453  1.00 15.00           C  
ATOM    702  CG  LEU A  89      16.593  30.318   3.831  1.00 17.97           C  
ATOM    703  CD1 LEU A  89      15.178  29.877   4.170  1.00 19.18           C  
ATOM    704  CD2 LEU A  89      17.573  29.796   4.861  1.00 20.26           C  
ATOM    705  N   ALA A  90      18.245  29.814  -0.447  1.00 14.71           N  
ATOM    706  CA  ALA A  90      18.629  29.071  -1.652  1.00 14.44           C  
ATOM    707  C   ALA A  90      20.116  29.273  -1.933  1.00 14.22           C  
ATOM    708  O   ALA A  90      20.836  28.337  -2.305  1.00 15.53           O  
ATOM    709  CB  ALA A  90      17.802  29.550  -2.840  1.00 15.18           C  
ATOM    710  N   TRP A  91      20.579  30.500  -1.758  1.00 13.61           N  
ATOM    711  CA  TRP A  91      21.975  30.812  -1.998  1.00 14.76           C  
ATOM    712  C   TRP A  91      22.860  30.062  -0.997  1.00 14.03           C  
ATOM    713  O   TRP A  91      23.865  29.462  -1.369  1.00 13.49           O  
ATOM    714  CB  TRP A  91      22.201  32.320  -1.877  1.00 14.80           C  
ATOM    715  CG  TRP A  91      23.610  32.755  -2.213  1.00 16.97           C  
ATOM    716  CD1 TRP A  91      24.093  33.115  -3.450  1.00 18.62           C  
ATOM    717  CD2 TRP A  91      24.701  32.896  -1.301  1.00 16.79           C  
ATOM    718  NE1 TRP A  91      25.421  33.476  -3.353  1.00 18.65           N  
ATOM    719  CE2 TRP A  91      25.819  33.352  -2.048  1.00 17.30           C  
ATOM    720  CE3 TRP A  91      24.849  32.682   0.079  1.00 17.20           C  
ATOM    721  CZ2 TRP A  91      27.068  33.602  -1.456  1.00 18.84           C  
ATOM    722  CZ3 TRP A  91      26.092  32.930   0.664  1.00 16.59           C  
ATOM    723  CH2 TRP A  91      27.185  33.386  -0.105  1.00 18.36           C  
ATOM    724  N   LEU A  92      22.491  30.081   0.283  1.00 12.65           N  
ATOM    725  CA  LEU A  92      23.295  29.373   1.267  1.00 13.19           C  
ATOM    726  C   LEU A  92      23.380  27.880   0.933  1.00 13.88           C  
ATOM    727  O   LEU A  92      24.439  27.256   1.062  1.00 15.27           O  
ATOM    728  CB  LEU A  92      22.704  29.548   2.675  1.00 12.46           C  
ATOM    729  CG  LEU A  92      22.827  30.951   3.272  1.00 10.84           C  
ATOM    730  CD1 LEU A  92      21.966  30.986   4.543  1.00 12.47           C  
ATOM    731  CD2 LEU A  92      24.283  31.303   3.602  1.00 13.03           C  
ATOM    732  N   HIS A  93      22.268  27.300   0.502  1.00 13.59           N  
ATOM    733  CA  HIS A  93      22.282  25.882   0.191  1.00 15.79           C  
ATOM    734  C   HIS A  93      23.175  25.589  -1.010  1.00 15.74           C  
ATOM    735  O   HIS A  93      23.967  24.646  -0.984  1.00 15.22           O  
ATOM    736  CB  HIS A  93      20.876  25.357  -0.093  1.00 17.99           C  
ATOM    737  CG  HIS A  93      20.834  23.870  -0.250  1.00 22.51           C  
ATOM    738  ND1 HIS A  93      21.025  23.008   0.810  1.00 26.42           N  
ATOM    739  CD2 HIS A  93      20.716  23.094  -1.351  1.00 25.60           C  
ATOM    740  CE1 HIS A  93      21.029  21.764   0.365  1.00 27.62           C  
ATOM    741  NE2 HIS A  93      20.845  21.789  -0.943  1.00 28.09           N  
ATOM    742  N   GLU A  94      23.044  26.389  -2.058  1.00 16.36           N  
ATOM    743  CA  GLU A  94      23.852  26.186  -3.258  1.00 18.40           C  
ATOM    744  C   GLU A  94      25.340  26.373  -2.961  1.00 18.52           C  
ATOM    745  O   GLU A  94      26.192  25.735  -3.584  1.00 15.93           O  
ATOM    746  CB  GLU A  94      23.397  27.152  -4.356  1.00 24.21           C  
ATOM    747  CG  GLU A  94      21.921  26.969  -4.734  1.00 30.55           C  
ATOM    748  CD  GLU A  94      21.409  28.050  -5.672  1.00 35.13           C  
ATOM    749  OE1 GLU A  94      20.189  28.065  -5.967  1.00 37.14           O  
ATOM    750  OE2 GLU A  94      22.229  28.884  -6.116  1.00 38.76           O  
ATOM    751  N   GLN A  95      25.646  27.238  -1.995  1.00 14.80           N  
ATOM    752  CA  GLN A  95      27.032  27.510  -1.615  1.00 16.40           C  
ATOM    753  C   GLN A  95      27.602  26.502  -0.613  1.00 14.33           C  
ATOM    754  O   GLN A  95      28.765  26.608  -0.213  1.00 14.26           O  
ATOM    755  CB  GLN A  95      27.135  28.931  -1.039  1.00 18.16           C  
ATOM    756  CG  GLN A  95      26.763  30.009  -2.033  1.00 22.22           C  
ATOM    757  CD  GLN A  95      27.628  29.972  -3.274  1.00 29.84           C  
ATOM    758  OE1 GLN A  95      27.352  29.236  -4.226  1.00 30.62           O  
ATOM    759  NE2 GLN A  95      28.691  30.763  -3.266  1.00 33.06           N  
ATOM    760  N   GLY A  96      26.781  25.538  -0.201  1.00 13.89           N  
ATOM    761  CA  GLY A  96      27.219  24.520   0.741  1.00 14.34           C  
ATOM    762  C   GLY A  96      27.350  25.081   2.142  1.00 16.74           C  
ATOM    763  O   GLY A  96      28.169  24.616   2.939  1.00 16.17           O  
ATOM    764  N   LEU A  97      26.528  26.075   2.450  1.00 14.53           N  
ATOM    765  CA  LEU A  97      26.585  26.728   3.755  1.00 15.68           C  
ATOM    766  C   LEU A  97      25.413  26.454   4.684  1.00 16.18           C  
ATOM    767  O   LEU A  97      25.279  27.104   5.721  1.00 17.91           O  
ATOM    768  CB  LEU A  97      26.726  28.228   3.555  1.00 15.06           C  
ATOM    769  CG  LEU A  97      28.075  28.671   3.007  1.00 17.60           C  
ATOM    770  CD1 LEU A  97      27.986  30.123   2.568  1.00 19.22           C  
ATOM    771  CD2 LEU A  97      29.150  28.478   4.070  1.00 20.72           C  
ATOM    772  N   SER A  98      24.559  25.513   4.309  1.00 15.62           N  
ATOM    773  CA  SER A  98      23.415  25.151   5.141  1.00 15.17           C  
ATOM    774  C   SER A  98      23.073  23.687   4.900  1.00 16.98           C  
ATOM    775  O   SER A  98      23.515  23.092   3.917  1.00 16.55           O  
ATOM    776  CB  SER A  98      22.202  26.015   4.792  1.00 15.29           C  
ATOM    777  OG  SER A  98      21.716  25.704   3.498  1.00 15.38           O  
ATOM    778  N   TYR A  99      22.293  23.106   5.803  1.00 15.33           N  
ATOM    779  CA  TYR A  99      21.875  21.716   5.658  1.00 16.75           C  
ATOM    780  C   TYR A  99      20.527  21.518   6.328  1.00 17.50           C  
ATOM    781  O   TYR A  99      20.087  22.357   7.122  1.00 17.86           O  
ATOM    782  CB  TYR A  99      22.924  20.761   6.251  1.00 16.46           C  
ATOM    783  CG  TYR A  99      23.258  20.974   7.712  1.00 15.45           C  
ATOM    784  CD1 TYR A  99      22.554  20.306   8.719  1.00 16.01           C  
ATOM    785  CD2 TYR A  99      24.313  21.807   8.085  1.00 16.42           C  
ATOM    786  CE1 TYR A  99      22.909  20.454  10.061  1.00 15.93           C  
ATOM    787  CE2 TYR A  99      24.668  21.965   9.414  1.00 16.73           C  
ATOM    788  CZ  TYR A  99      23.966  21.280  10.396  1.00 16.38           C  
ATOM    789  OH  TYR A  99      24.359  21.390  11.702  1.00 16.97           O  
ATOM    790  N   TYR A 100      19.856  20.422   5.992  1.00 17.11           N  
ATOM    791  CA  TYR A 100      18.555  20.128   6.573  1.00 18.45           C  
ATOM    792  C   TYR A 100      18.677  19.220   7.785  1.00 19.58           C  
ATOM    793  O   TYR A 100      19.364  18.197   7.748  1.00 20.55           O  
ATOM    794  CB  TYR A 100      17.644  19.500   5.515  1.00 20.29           C  
ATOM    795  CG  TYR A 100      17.420  20.428   4.346  1.00 21.91           C  
ATOM    796  CD1 TYR A 100      18.115  20.259   3.144  1.00 22.98           C  
ATOM    797  CD2 TYR A 100      16.553  21.508   4.458  1.00 24.20           C  
ATOM    798  CE1 TYR A 100      17.948  21.153   2.082  1.00 24.84           C  
ATOM    799  CE2 TYR A 100      16.379  22.407   3.407  1.00 26.38           C  
ATOM    800  CZ  TYR A 100      17.078  22.225   2.227  1.00 26.50           C  
ATOM    801  OH  TYR A 100      16.902  23.128   1.205  1.00 28.90           O  
ATOM    802  N   CYS A 101      18.008  19.604   8.867  1.00 19.36           N  
ATOM    803  CA  CYS A 101      18.063  18.844  10.114  1.00 18.58           C  
ATOM    804  C   CYS A 101      16.703  18.263  10.472  1.00 19.63           C  
ATOM    805  O   CYS A 101      15.710  18.982  10.523  1.00 19.38           O  
ATOM    806  CB  CYS A 101      18.564  19.756  11.249  1.00 16.43           C  
ATOM    807  SG  CYS A 101      18.343  19.094  12.908  1.00 17.38           S  
ATOM    808  N   THR A 102      16.677  16.955  10.719  1.00 19.64           N  
ATOM    809  CA  THR A 102      15.451  16.246  11.067  1.00 20.84           C  
ATOM    810  C   THR A 102      15.360  15.891  12.546  1.00 21.42           C  
ATOM    811  O   THR A 102      14.468  15.138  12.949  1.00 22.15           O  
ATOM    812  CB  THR A 102      15.329  14.942  10.243  1.00 19.77           C  
ATOM    813  OG1 THR A 102      16.528  14.163  10.397  1.00 21.97           O  
ATOM    814  CG2 THR A 102      15.139  15.270   8.771  1.00 21.43           C  
ATOM    815  N   CYS A 103      16.270  16.424  13.357  1.00 21.05           N  
ATOM    816  CA  CYS A 103      16.271  16.130  14.793  1.00 22.50           C  
ATOM    817  C   CYS A 103      15.088  16.732  15.534  1.00 24.07           C  
ATOM    818  O   CYS A 103      14.663  17.853  15.245  1.00 25.31           O  
ATOM    819  CB  CYS A 103      17.562  16.628  15.439  1.00 21.97           C  
ATOM    820  SG  CYS A 103      19.045  15.819  14.810  1.00 20.76           S  
ATOM    821  N   THR A 104      14.570  15.988  16.507  1.00 24.90           N  
ATOM    822  CA  THR A 104      13.434  16.446  17.293  1.00 26.59           C  
ATOM    823  C   THR A 104      13.896  17.348  18.425  1.00 28.15           C  
ATOM    824  O   THR A 104      15.075  17.366  18.775  1.00 26.95           O  
ATOM    825  CB  THR A 104      12.677  15.267  17.928  1.00 27.59           C  
ATOM    826  OG1 THR A 104      13.547  14.590  18.843  1.00 27.35           O  
ATOM    827  CG2 THR A 104      12.210  14.290  16.861  1.00 27.12           C  
ATOM    828  N   ARG A 105      12.957  18.091  19.000  1.00 29.47           N  
ATOM    829  CA  ARG A 105      13.270  18.975  20.114  1.00 30.32           C  
ATOM    830  C   ARG A 105      13.716  18.132  21.302  1.00 28.32           C  
ATOM    831  O   ARG A 105      14.595  18.526  22.061  1.00 28.72           O  
ATOM    832  CB  ARG A 105      12.035  19.790  20.497  1.00 34.48           C  
ATOM    833  CG  ARG A 105      11.608  20.802  19.453  1.00 39.42           C  
ATOM    834  CD  ARG A 105      10.220  21.362  19.771  1.00 44.35           C  
ATOM    835  NE  ARG A 105       9.863  22.504  18.927  1.00 47.28           N  
ATOM    836  CZ  ARG A 105      10.369  23.728  19.064  1.00 48.60           C  
ATOM    837  NH1 ARG A 105       9.983  24.702  18.247  1.00 49.36           N  
ATOM    838  NH2 ARG A 105      11.253  23.982  20.022  1.00 48.59           N  
ATOM    839  N   ALA A 106      13.109  16.960  21.451  1.00 26.25           N  
ATOM    840  CA  ALA A 106      13.439  16.067  22.548  1.00 25.27           C  
ATOM    841  C   ALA A 106      14.895  15.631  22.470  1.00 23.83           C  
ATOM    842  O   ALA A 106      15.593  15.591  23.484  1.00 23.58           O  
ATOM    843  CB  ALA A 106      12.514  14.842  22.533  1.00 26.94           C  
ATOM    844  N   ARG A 107      15.359  15.303  21.269  1.00 23.06           N  
ATOM    845  CA  ARG A 107      16.744  14.884  21.114  1.00 22.16           C  
ATOM    846  C   ARG A 107      17.701  16.005  21.543  1.00 21.98           C  
ATOM    847  O   ARG A 107      18.638  15.780  22.317  1.00 19.50           O  
ATOM    848  CB  ARG A 107      17.038  14.488  19.662  1.00 22.66           C  
ATOM    849  CG  ARG A 107      18.531  14.275  19.455  1.00 23.16           C  
ATOM    850  CD  ARG A 107      18.969  13.854  18.065  1.00 23.79           C  
ATOM    851  NE  ARG A 107      20.375  13.487  18.194  1.00 24.45           N  
ATOM    852  CZ  ARG A 107      21.395  14.336  18.120  1.00 23.86           C  
ATOM    853  NH1 ARG A 107      22.627  13.885  18.302  1.00 22.65           N  
ATOM    854  NH2 ARG A 107      21.198  15.614  17.797  1.00 23.22           N  
ATOM    855  N   ILE A 108      17.456  17.213  21.048  1.00 21.31           N  
ATOM    856  CA  ILE A 108      18.310  18.348  21.381  1.00 22.48           C  
ATOM    857  C   ILE A 108      18.333  18.613  22.882  1.00 21.88           C  
ATOM    858  O   ILE A 108      19.377  18.878  23.462  1.00 21.07           O  
ATOM    859  CB  ILE A 108      17.846  19.629  20.657  1.00 22.69           C  
ATOM    860  CG1 ILE A 108      17.771  19.379  19.145  1.00 25.65           C  
ATOM    861  CG2 ILE A 108      18.768  20.784  21.015  1.00 23.79           C  
ATOM    862  CD1 ILE A 108      18.859  18.502  18.594  1.00 25.02           C  
ATOM    863  N   GLN A 109      17.168  18.536  23.510  1.00 23.31           N  
ATOM    864  CA  GLN A 109      17.083  18.754  24.941  1.00 23.92           C  
ATOM    865  C   GLN A 109      17.896  17.706  25.695  1.00 23.07           C  
ATOM    866  O   GLN A 109      18.560  18.024  26.681  1.00 21.53           O  
ATOM    867  CB  GLN A 109      15.623  18.684  25.394  1.00 27.34           C  
ATOM    868  CG  GLN A 109      15.086  19.969  26.010  1.00 35.13           C  
ATOM    869  CD  GLN A 109      14.991  21.123  25.024  1.00 38.52           C  
ATOM    870  OE1 GLN A 109      16.004  21.681  24.584  1.00 39.34           O  
ATOM    871  NE2 GLN A 109      13.761  21.491  24.671  1.00 41.39           N  
ATOM    872  N   SER A 110      17.855  16.463  25.212  1.00 22.68           N  
ATOM    873  CA  SER A 110      18.563  15.363  25.866  1.00 22.54           C  
ATOM    874  C   SER A 110      20.084  15.484  25.863  1.00 22.33           C  
ATOM    875  O   SER A 110      20.750  14.891  26.710  1.00 21.11           O  
ATOM    876  CB  SER A 110      18.163  14.021  25.234  1.00 24.57           C  
ATOM    877  OG  SER A 110      18.795  13.838  23.975  1.00 26.88           O  
ATOM    878  N   ILE A 111      20.640  16.241  24.920  1.00 20.87           N  
ATOM    879  CA  ILE A 111      22.090  16.400  24.874  1.00 21.39           C  
ATOM    880  C   ILE A 111      22.562  17.753  25.399  1.00 21.89           C  
ATOM    881  O   ILE A 111      23.703  18.158  25.163  1.00 22.33           O  
ATOM    882  CB  ILE A 111      22.651  16.203  23.448  1.00 21.50           C  
ATOM    883  CG1 ILE A 111      22.131  17.295  22.518  1.00 20.50           C  
ATOM    884  CG2 ILE A 111      22.261  14.819  22.919  1.00 22.38           C  
ATOM    885  CD1 ILE A 111      22.763  17.234  21.131  1.00 19.50           C  
ATOM    886  N   GLY A 112      21.685  18.456  26.109  1.00 21.89           N  
ATOM    887  CA  GLY A 112      22.086  19.728  26.685  1.00 21.78           C  
ATOM    888  C   GLY A 112      21.444  20.984  26.135  1.00 21.51           C  
ATOM    889  O   GLY A 112      21.722  22.079  26.634  1.00 22.83           O  
ATOM    890  N   GLY A 113      20.613  20.841  25.108  1.00 20.95           N  
ATOM    891  CA  GLY A 113      19.925  21.993  24.542  1.00 21.93           C  
ATOM    892  C   GLY A 113      20.635  22.716  23.410  1.00 21.44           C  
ATOM    893  O   GLY A 113      20.042  23.568  22.746  1.00 23.34           O  
ATOM    894  N   ILE A 114      21.902  22.392  23.192  1.00 20.23           N  
ATOM    895  CA  ILE A 114      22.672  23.020  22.125  1.00 19.70           C  
ATOM    896  C   ILE A 114      22.964  21.969  21.060  1.00 18.67           C  
ATOM    897  O   ILE A 114      23.484  20.896  21.360  1.00 17.98           O  
ATOM    898  CB  ILE A 114      24.001  23.612  22.662  1.00 21.56           C  
ATOM    899  CG1 ILE A 114      23.707  24.752  23.645  1.00 24.89           C  
ATOM    900  CG2 ILE A 114      24.833  24.167  21.509  1.00 21.68           C  
ATOM    901  CD1 ILE A 114      22.994  24.317  24.915  1.00 28.97           C  
ATOM    902  N   TYR A 115      22.630  22.283  19.812  1.00 17.87           N  
ATOM    903  CA  TYR A 115      22.825  21.337  18.717  1.00 18.10           C  
ATOM    904  C   TYR A 115      24.268  20.855  18.580  1.00 18.20           C  
ATOM    905  O   TYR A 115      25.212  21.628  18.760  1.00 18.50           O  
ATOM    906  CB  TYR A 115      22.343  21.959  17.405  1.00 17.50           C  
ATOM    907  CG  TYR A 115      22.140  20.941  16.316  1.00 16.38           C  
ATOM    908  CD1 TYR A 115      21.317  19.829  16.523  1.00 16.66           C  
ATOM    909  CD2 TYR A 115      22.793  21.059  15.095  1.00 15.34           C  
ATOM    910  CE1 TYR A 115      21.161  18.859  15.547  1.00 16.60           C  
ATOM    911  CE2 TYR A 115      22.639  20.088  14.105  1.00 16.92           C  
ATOM    912  CZ  TYR A 115      21.825  18.993  14.345  1.00 16.71           C  
ATOM    913  OH  TYR A 115      21.706  18.021  13.394  1.00 17.91           O  
ATOM    914  N   ASP A 116      24.418  19.575  18.239  1.00 17.91           N  
ATOM    915  CA  ASP A 116      25.724  18.923  18.100  1.00 19.58           C  
ATOM    916  C   ASP A 116      26.212  18.750  16.659  1.00 19.77           C  
ATOM    917  O   ASP A 116      27.273  18.163  16.427  1.00 20.02           O  
ATOM    918  CB  ASP A 116      25.662  17.552  18.781  1.00 20.08           C  
ATOM    919  CG  ASP A 116      24.721  16.583  18.066  1.00 19.68           C  
ATOM    920  OD1 ASP A 116      23.799  17.037  17.350  1.00 18.96           O  
ATOM    921  OD2 ASP A 116      24.883  15.354  18.241  1.00 19.80           O  
ATOM    922  N   GLY A 117      25.440  19.244  15.692  1.00 18.87           N  
ATOM    923  CA  GLY A 117      25.840  19.121  14.300  1.00 19.12           C  
ATOM    924  C   GLY A 117      25.529  17.753  13.711  1.00 20.30           C  
ATOM    925  O   GLY A 117      26.104  17.368  12.690  1.00 19.80           O  
ATOM    926  N   HIS A 118      24.608  17.026  14.340  1.00 19.56           N  
ATOM    927  CA  HIS A 118      24.249  15.677  13.883  1.00 21.39           C  
ATOM    928  C   HIS A 118      23.975  15.520  12.380  1.00 20.37           C  
ATOM    929  O   HIS A 118      24.550  14.647  11.732  1.00 21.76           O  
ATOM    930  CB  HIS A 118      23.038  15.163  14.685  1.00 22.58           C  
ATOM    931  CG  HIS A 118      22.612  13.770  14.324  1.00 24.33           C  
ATOM    932  ND1 HIS A 118      21.636  13.507  13.386  1.00 25.68           N  
ATOM    933  CD2 HIS A 118      23.023  12.563  14.786  1.00 25.69           C  
ATOM    934  CE1 HIS A 118      21.460  12.199  13.290  1.00 25.06           C  
ATOM    935  NE2 HIS A 118      22.289  11.605  14.129  1.00 27.41           N  
ATOM    936  N   CYS A 119      23.114  16.360  11.817  1.00 18.99           N  
ATOM    937  CA  CYS A 119      22.770  16.243  10.398  1.00 18.60           C  
ATOM    938  C   CYS A 119      23.716  16.941   9.426  1.00 19.03           C  
ATOM    939  O   CYS A 119      23.489  16.916   8.215  1.00 19.60           O  
ATOM    940  CB  CYS A 119      21.351  16.774  10.173  1.00 17.13           C  
ATOM    941  SG  CYS A 119      20.110  15.909  11.164  1.00 18.50           S  
ATOM    942  N   ARG A 120      24.782  17.529   9.959  1.00 20.01           N  
ATOM    943  CA  ARG A 120      25.735  18.298   9.164  1.00 22.70           C  
ATOM    944  C   ARG A 120      26.173  17.662   7.845  1.00 25.64           C  
ATOM    945  O   ARG A 120      26.256  18.345   6.830  1.00 26.05           O  
ATOM    946  CB  ARG A 120      26.951  18.655  10.030  1.00 24.54           C  
ATOM    947  CG  ARG A 120      27.794  19.804   9.498  1.00 27.77           C  
ATOM    948  CD  ARG A 120      28.805  20.294  10.538  1.00 28.56           C  
ATOM    949  NE  ARG A 120      29.871  21.083   9.920  1.00 31.06           N  
ATOM    950  CZ  ARG A 120      30.124  22.365  10.178  1.00 32.33           C  
ATOM    951  NH1 ARG A 120      31.126  22.968   9.548  1.00 33.94           N  
ATOM    952  NH2 ARG A 120      29.383  23.049  11.052  1.00 27.61           N  
ATOM    953  N   VAL A 121      26.452  16.364   7.841  1.00 26.74           N  
ATOM    954  CA  VAL A 121      26.861  15.724   6.596  1.00 29.08           C  
ATOM    955  C   VAL A 121      26.008  14.509   6.241  1.00 28.47           C  
ATOM    956  O   VAL A 121      26.486  13.591   5.575  1.00 29.56           O  
ATOM    957  CB  VAL A 121      28.348  15.296   6.650  1.00 29.63           C  
ATOM    958  CG1 VAL A 121      29.230  16.509   6.926  1.00 31.16           C  
ATOM    959  CG2 VAL A 121      28.551  14.239   7.722  1.00 31.02           C  
ATOM    960  N   LEU A 122      24.745  14.507   6.662  1.00 28.21           N  
ATOM    961  CA  LEU A 122      23.851  13.383   6.381  1.00 28.99           C  
ATOM    962  C   LEU A 122      23.017  13.569   5.113  1.00 29.74           C  
ATOM    963  O   LEU A 122      22.321  12.652   4.674  1.00 29.94           O  
ATOM    964  CB  LEU A 122      22.917  13.127   7.577  1.00 27.97           C  
ATOM    965  CG  LEU A 122      23.563  12.812   8.935  1.00 27.98           C  
ATOM    966  CD1 LEU A 122      22.470  12.468   9.932  1.00 26.01           C  
ATOM    967  CD2 LEU A 122      24.548  11.656   8.814  1.00 28.81           C  
ATOM    968  N   HIS A 123      23.087  14.761   4.537  1.00 30.21           N  
ATOM    969  CA  HIS A 123      22.360  15.088   3.315  1.00 30.81           C  
ATOM    970  C   HIS A 123      20.868  14.785   3.304  1.00 31.36           C  
ATOM    971  O   HIS A 123      20.334  14.285   2.313  1.00 31.54           O  
ATOM    972  CB  HIS A 123      23.039  14.423   2.114  1.00 32.06           C  
ATOM    973  CG  HIS A 123      24.484  14.779   1.988  1.00 32.58           C  
ATOM    974  ND1 HIS A 123      25.490  14.000   2.517  1.00 34.54           N  
ATOM    975  CD2 HIS A 123      25.088  15.882   1.484  1.00 33.22           C  
ATOM    976  CE1 HIS A 123      26.651  14.608   2.348  1.00 33.30           C  
ATOM    977  NE2 HIS A 123      26.434  15.751   1.724  1.00 33.60           N  
ATOM    978  N   HIS A 124      20.191  15.100   4.401  1.00 29.96           N  
ATOM    979  CA  HIS A 124      18.752  14.895   4.478  1.00 30.71           C  
ATOM    980  C   HIS A 124      18.074  15.846   3.501  1.00 30.76           C  
ATOM    981  O   HIS A 124      18.651  16.861   3.098  1.00 28.52           O  
ATOM    982  CB  HIS A 124      18.222  15.189   5.887  1.00 29.69           C  
ATOM    983  CG  HIS A 124      18.619  14.176   6.911  1.00 31.30           C  
ATOM    984  ND1 HIS A 124      18.384  12.827   6.752  1.00 31.96           N  
ATOM    985  CD2 HIS A 124      19.215  14.315   8.118  1.00 31.97           C  
ATOM    986  CE1 HIS A 124      18.821  12.178   7.816  1.00 33.14           C  
ATOM    987  NE2 HIS A 124      19.330  13.058   8.661  1.00 32.09           N  
ATOM    988  N   GLY A 125      16.842  15.509   3.137  1.00 32.25           N  
ATOM    989  CA  GLY A 125      16.077  16.335   2.224  1.00 34.73           C  
ATOM    990  C   GLY A 125      15.464  17.526   2.941  1.00 37.16           C  
ATOM    991  O   GLY A 125      15.503  17.595   4.170  1.00 35.56           O  
ATOM    992  N   PRO A 126      14.870  18.470   2.190  1.00 39.38           N  
ATOM    993  CA  PRO A 126      14.223  19.703   2.650  1.00 41.37           C  
ATOM    994  C   PRO A 126      12.907  19.684   3.431  1.00 43.46           C  
ATOM    995  O   PRO A 126      12.718  20.517   4.316  1.00 44.86           O  
ATOM    996  CB  PRO A 126      14.092  20.512   1.365  1.00 41.98           C  
ATOM    997  CG  PRO A 126      13.866  19.459   0.345  1.00 41.49           C  
ATOM    998  CD  PRO A 126      14.915  18.440   0.716  1.00 40.32           C  
ATOM    999  N   ASP A 127      11.985  18.777   3.135  1.00 45.13           N  
ATOM   1000  CA  ASP A 127      10.729  18.832   3.879  1.00 45.33           C  
ATOM   1001  C   ASP A 127      10.648  18.012   5.163  1.00 44.45           C  
ATOM   1002  O   ASP A 127      11.216  16.921   5.278  1.00 43.37           O  
ATOM   1003  CB  ASP A 127       9.534  18.547   2.952  1.00 47.55           C  
ATOM   1004  CG  ASP A 127       9.648  17.231   2.227  1.00 48.86           C  
ATOM   1005  OD1 ASP A 127      10.733  16.943   1.677  1.00 49.31           O  
ATOM   1006  OD2 ASP A 127       8.640  16.489   2.196  1.00 50.07           O  
ATOM   1007  N   ASN A 128       9.936  18.588   6.129  1.00 42.73           N  
ATOM   1008  CA  ASN A 128       9.755  18.023   7.460  1.00 40.68           C  
ATOM   1009  C   ASN A 128      11.090  18.143   8.189  1.00 37.42           C  
ATOM   1010  O   ASN A 128      11.385  17.408   9.135  1.00 38.20           O  
ATOM   1011  CB  ASN A 128       9.301  16.568   7.387  1.00 44.12           C  
ATOM   1012  CG  ASN A 128       8.488  16.156   8.602  1.00 45.84           C  
ATOM   1013  OD1 ASN A 128       7.905  15.073   8.636  1.00 47.45           O  
ATOM   1014  ND2 ASN A 128       8.442  17.028   9.607  1.00 46.22           N  
ATOM   1015  N   ALA A 129      11.892  19.094   7.725  1.00 32.05           N  
ATOM   1016  CA  ALA A 129      13.197  19.365   8.306  1.00 28.48           C  
ATOM   1017  C   ALA A 129      13.386  20.868   8.508  1.00 24.60           C  
ATOM   1018  O   ALA A 129      12.727  21.686   7.865  1.00 25.15           O  
ATOM   1019  CB  ALA A 129      14.301  18.829   7.395  1.00 28.15           C  
ATOM   1020  N   ALA A 130      14.290  21.219   9.414  1.00 20.79           N  
ATOM   1021  CA  ALA A 130      14.615  22.614   9.682  1.00 17.42           C  
ATOM   1022  C   ALA A 130      15.890  22.872   8.897  1.00 17.60           C  
ATOM   1023  O   ALA A 130      16.585  21.925   8.527  1.00 18.36           O  
ATOM   1024  CB  ALA A 130      14.897  22.809  11.156  1.00 16.75           C  
ATOM   1025  N   VAL A 131      16.198  24.136   8.632  1.00 14.45           N  
ATOM   1026  CA  VAL A 131      17.441  24.455   7.942  1.00 14.31           C  
ATOM   1027  C   VAL A 131      18.394  25.040   8.973  1.00 13.60           C  
ATOM   1028  O   VAL A 131      18.028  25.981   9.695  1.00 14.61           O  
ATOM   1029  CB  VAL A 131      17.240  25.519   6.856  1.00 13.87           C  
ATOM   1030  CG1 VAL A 131      18.587  25.886   6.236  1.00 15.64           C  
ATOM   1031  CG2 VAL A 131      16.273  25.008   5.802  1.00 15.56           C  
ATOM   1032  N   ARG A 132      19.601  24.486   9.062  1.00 13.35           N  
ATOM   1033  CA  ARG A 132      20.605  25.019   9.984  1.00 13.22           C  
ATOM   1034  C   ARG A 132      21.768  25.606   9.208  1.00 14.07           C  
ATOM   1035  O   ARG A 132      22.072  25.178   8.084  1.00 13.39           O  
ATOM   1036  CB  ARG A 132      21.131  23.933  10.931  1.00 12.82           C  
ATOM   1037  CG  ARG A 132      20.146  23.550  12.025  1.00 12.20           C  
ATOM   1038  CD  ARG A 132      20.679  22.381  12.853  1.00 13.96           C  
ATOM   1039  NE  ARG A 132      19.699  21.962  13.855  1.00 15.22           N  
ATOM   1040  CZ  ARG A 132      19.460  22.619  14.990  1.00 15.05           C  
ATOM   1041  NH1 ARG A 132      20.139  23.727  15.283  1.00 15.60           N  
ATOM   1042  NH2 ARG A 132      18.509  22.193  15.815  1.00 16.80           N  
ATOM   1043  N   ILE A 133      22.412  26.606   9.794  1.00 12.40           N  
ATOM   1044  CA  ILE A 133      23.569  27.220   9.156  1.00 12.43           C  
ATOM   1045  C   ILE A 133      24.759  26.300   9.426  1.00 13.14           C  
ATOM   1046  O   ILE A 133      24.834  25.679  10.482  1.00 13.40           O  
ATOM   1047  CB  ILE A 133      23.863  28.620   9.750  1.00 11.63           C  
ATOM   1048  CG1 ILE A 133      25.013  29.277   8.975  1.00 14.99           C  
ATOM   1049  CG2 ILE A 133      24.218  28.503  11.233  1.00 12.12           C  
ATOM   1050  CD1 ILE A 133      24.641  29.663   7.553  1.00 16.71           C  
ATOM   1051  N   ARG A 134      25.674  26.175   8.467  1.00 14.43           N  
ATOM   1052  CA  ARG A 134      26.849  25.331   8.677  1.00 15.24           C  
ATOM   1053  C   ARG A 134      27.989  26.272   9.066  1.00 16.05           C  
ATOM   1054  O   ARG A 134      28.696  26.782   8.204  1.00 15.99           O  
ATOM   1055  CB  ARG A 134      27.221  24.568   7.389  1.00 17.92           C  
ATOM   1056  CG  ARG A 134      28.374  23.572   7.573  1.00 20.20           C  
ATOM   1057  CD  ARG A 134      28.930  23.108   6.225  1.00 20.39           C  
ATOM   1058  NE  ARG A 134      27.858  22.670   5.335  1.00 23.52           N  
ATOM   1059  CZ  ARG A 134      27.280  21.475   5.392  1.00 24.30           C  
ATOM   1060  NH1 ARG A 134      26.300  21.170   4.551  1.00 24.24           N  
ATOM   1061  NH2 ARG A 134      27.701  20.576   6.270  1.00 25.43           N  
ATOM   1062  N   GLN A 135      28.159  26.518  10.359  1.00 16.14           N  
ATOM   1063  CA  GLN A 135      29.198  27.446  10.789  1.00 17.58           C  
ATOM   1064  C   GLN A 135      30.604  26.954  10.459  1.00 19.14           C  
ATOM   1065  O   GLN A 135      30.882  25.753  10.482  1.00 20.31           O  
ATOM   1066  CB  GLN A 135      29.078  27.733  12.280  1.00 17.67           C  
ATOM   1067  CG  GLN A 135      27.840  28.525  12.648  1.00 18.21           C  
ATOM   1068  CD  GLN A 135      28.148  29.654  13.625  1.00 17.60           C  
ATOM   1069  OE1 GLN A 135      28.943  30.545  13.324  1.00 17.83           O  
ATOM   1070  NE2 GLN A 135      27.518  29.622  14.788  1.00 18.50           N  
ATOM   1071  N   GLN A 136      31.472  27.903  10.133  1.00 20.05           N  
ATOM   1072  CA  GLN A 136      32.855  27.617   9.777  1.00 22.47           C  
ATOM   1073  C   GLN A 136      33.811  28.219  10.798  1.00 22.88           C  
ATOM   1074  O   GLN A 136      34.713  27.542  11.295  1.00 24.22           O  
ATOM   1075  CB  GLN A 136      33.141  28.182   8.389  1.00 25.27           C  
ATOM   1076  CG  GLN A 136      32.178  27.657   7.331  1.00 29.25           C  
ATOM   1077  CD  GLN A 136      32.220  26.145   7.216  1.00 32.62           C  
ATOM   1078  OE1 GLN A 136      31.206  25.505   6.937  1.00 34.97           O  
ATOM   1079  NE2 GLN A 136      33.398  25.566   7.423  1.00 32.84           N  
ATOM   1080  N   HIS A 137      33.609  29.497  11.107  1.00 21.85           N  
ATOM   1081  CA  HIS A 137      34.440  30.203  12.080  1.00 21.82           C  
ATOM   1082  C   HIS A 137      33.512  31.092  12.895  1.00 19.96           C  
ATOM   1083  O   HIS A 137      33.387  32.298  12.636  1.00 19.84           O  
ATOM   1084  CB  HIS A 137      35.495  31.059  11.377  1.00 26.70           C  
ATOM   1085  CG  HIS A 137      36.534  30.257  10.657  1.00 29.80           C  
ATOM   1086  ND1 HIS A 137      36.493  30.034   9.299  1.00 32.18           N  
ATOM   1087  CD2 HIS A 137      37.626  29.599  11.115  1.00 32.00           C  
ATOM   1088  CE1 HIS A 137      37.517  29.275   8.948  1.00 33.98           C  
ATOM   1089  NE2 HIS A 137      38.220  28.997  10.032  1.00 33.75           N  
ATOM   1090  N   PRO A 138      32.851  30.507  13.894  1.00 18.46           N  
ATOM   1091  CA  PRO A 138      31.926  31.268  14.728  1.00 17.56           C  
ATOM   1092  C   PRO A 138      32.540  32.476  15.404  1.00 17.99           C  
ATOM   1093  O   PRO A 138      33.641  32.411  15.965  1.00 16.72           O  
ATOM   1094  CB  PRO A 138      31.456  30.246  15.753  1.00 18.58           C  
ATOM   1095  CG  PRO A 138      31.593  28.945  15.041  1.00 19.65           C  
ATOM   1096  CD  PRO A 138      32.911  29.104  14.337  1.00 19.42           C  
ATOM   1097  N   VAL A 139      31.800  33.572  15.354  1.00 15.10           N  
ATOM   1098  CA  VAL A 139      32.195  34.805  16.000  1.00 15.27           C  
ATOM   1099  C   VAL A 139      31.804  34.618  17.471  1.00 14.83           C  
ATOM   1100  O   VAL A 139      30.692  34.176  17.762  1.00 13.82           O  
ATOM   1101  CB  VAL A 139      31.408  35.994  15.400  1.00 13.82           C  
ATOM   1102  CG1 VAL A 139      31.626  37.244  16.235  1.00 12.99           C  
ATOM   1103  CG2 VAL A 139      31.867  36.238  13.953  1.00 13.97           C  
ATOM   1104  N   THR A 140      32.713  34.935  18.395  1.00 13.81           N  
ATOM   1105  CA  THR A 140      32.414  34.787  19.816  1.00 14.68           C  
ATOM   1106  C   THR A 140      32.531  36.092  20.610  1.00 14.65           C  
ATOM   1107  O   THR A 140      32.265  36.110  21.814  1.00 13.29           O  
ATOM   1108  CB  THR A 140      33.330  33.759  20.471  1.00 16.03           C  
ATOM   1109  OG1 THR A 140      34.688  34.173  20.289  1.00 16.43           O  
ATOM   1110  CG2 THR A 140      33.132  32.367  19.822  1.00 17.71           C  
ATOM   1111  N   GLN A 141      32.950  37.163  19.939  1.00 13.35           N  
ATOM   1112  CA  GLN A 141      33.075  38.477  20.577  1.00 12.91           C  
ATOM   1113  C   GLN A 141      32.708  39.533  19.551  1.00 13.28           C  
ATOM   1114  O   GLN A 141      32.884  39.311  18.355  1.00 12.96           O  
ATOM   1115  CB  GLN A 141      34.522  38.765  20.993  1.00 15.36           C  
ATOM   1116  CG  GLN A 141      35.253  37.681  21.730  1.00 18.53           C  
ATOM   1117  CD  GLN A 141      36.680  38.126  22.049  1.00 19.71           C  
ATOM   1118  OE1 GLN A 141      36.887  39.061  22.823  1.00 25.33           O  
ATOM   1119  NE2 GLN A 141      37.658  37.477  21.437  1.00 24.60           N  
ATOM   1120  N   PHE A 142      32.199  40.680  19.994  1.00  9.90           N  
ATOM   1121  CA  PHE A 142      31.910  41.746  19.038  1.00 11.15           C  
ATOM   1122  C   PHE A 142      32.128  43.107  19.653  1.00 11.30           C  
ATOM   1123  O   PHE A 142      32.241  43.246  20.872  1.00 12.19           O  
ATOM   1124  CB  PHE A 142      30.489  41.653  18.459  1.00 11.17           C  
ATOM   1125  CG  PHE A 142      29.407  42.118  19.391  1.00 10.76           C  
ATOM   1126  CD1 PHE A 142      28.896  43.415  19.300  1.00 11.25           C  
ATOM   1127  CD2 PHE A 142      28.872  41.244  20.325  1.00 10.45           C  
ATOM   1128  CE1 PHE A 142      27.848  43.838  20.134  1.00 10.99           C  
ATOM   1129  CE2 PHE A 142      27.831  41.646  21.161  1.00 10.12           C  
ATOM   1130  CZ  PHE A 142      27.313  42.949  21.064  1.00 12.57           C  
ATOM   1131  N   THR A 143      32.235  44.110  18.790  1.00 11.27           N  
ATOM   1132  CA  THR A 143      32.425  45.477  19.252  1.00 10.68           C  
ATOM   1133  C   THR A 143      31.094  46.202  19.370  1.00 11.12           C  
ATOM   1134  O   THR A 143      30.324  46.264  18.408  1.00 10.23           O  
ATOM   1135  CB  THR A 143      33.277  46.300  18.266  1.00 12.27           C  
ATOM   1136  OG1 THR A 143      34.578  45.710  18.151  1.00 12.23           O  
ATOM   1137  CG2 THR A 143      33.404  47.759  18.754  1.00 12.49           C  
ATOM   1138  N   ASP A 144      30.816  46.740  20.552  1.00 11.31           N  
ATOM   1139  CA  ASP A 144      29.616  47.537  20.743  1.00 11.19           C  
ATOM   1140  C   ASP A 144      30.186  48.960  20.844  1.00 12.70           C  
ATOM   1141  O   ASP A 144      31.107  49.203  21.626  1.00 11.85           O  
ATOM   1142  CB  ASP A 144      28.887  47.111  22.029  1.00 11.69           C  
ATOM   1143  CG  ASP A 144      27.586  47.864  22.235  1.00 12.47           C  
ATOM   1144  OD1 ASP A 144      27.641  49.084  22.503  1.00 12.80           O  
ATOM   1145  OD2 ASP A 144      26.503  47.237  22.133  1.00 11.99           O  
ATOM   1146  N   GLN A 145      29.662  49.889  20.042  1.00 11.70           N  
ATOM   1147  CA  GLN A 145      30.169  51.263  20.008  1.00 13.03           C  
ATOM   1148  C   GLN A 145      29.981  52.039  21.305  1.00 14.53           C  
ATOM   1149  O   GLN A 145      30.629  53.062  21.525  1.00 16.48           O  
ATOM   1150  CB  GLN A 145      29.547  52.024  18.822  1.00 13.18           C  
ATOM   1151  CG  GLN A 145      29.858  51.372  17.453  1.00 14.51           C  
ATOM   1152  CD  GLN A 145      31.365  51.217  17.157  1.00 16.53           C  
ATOM   1153  OE1 GLN A 145      31.801  50.220  16.554  1.00 16.74           O  
ATOM   1154  NE2 GLN A 145      32.152  52.197  17.565  1.00 12.54           N  
ATOM   1155  N   LEU A 146      29.119  51.529  22.172  1.00 12.60           N  
ATOM   1156  CA  LEU A 146      28.864  52.161  23.460  1.00 14.84           C  
ATOM   1157  C   LEU A 146      29.490  51.353  24.602  1.00 14.05           C  
ATOM   1158  O   LEU A 146      30.185  51.899  25.464  1.00 15.61           O  
ATOM   1159  CB  LEU A 146      27.350  52.284  23.679  1.00 14.42           C  
ATOM   1160  CG  LEU A 146      26.866  52.658  25.091  1.00 16.20           C  
ATOM   1161  CD1 LEU A 146      27.369  54.044  25.444  1.00 15.97           C  
ATOM   1162  CD2 LEU A 146      25.331  52.620  25.145  1.00 17.29           C  
ATOM   1163  N   ARG A 147      29.268  50.044  24.595  1.00 13.28           N  
ATOM   1164  CA  ARG A 147      29.757  49.185  25.669  1.00 12.12           C  
ATOM   1165  C   ARG A 147      31.170  48.627  25.533  1.00 13.33           C  
ATOM   1166  O   ARG A 147      31.700  48.061  26.498  1.00 15.35           O  
ATOM   1167  CB  ARG A 147      28.795  48.018  25.870  1.00 13.50           C  
ATOM   1168  CG  ARG A 147      27.349  48.448  26.120  1.00 11.69           C  
ATOM   1169  CD  ARG A 147      26.428  47.255  26.003  1.00 13.65           C  
ATOM   1170  NE  ARG A 147      25.074  47.540  26.463  1.00 15.04           N  
ATOM   1171  CZ  ARG A 147      24.606  47.221  27.665  1.00 17.60           C  
ATOM   1172  NH1 ARG A 147      25.381  46.600  28.551  1.00 19.97           N  
ATOM   1173  NH2 ARG A 147      23.350  47.503  27.978  1.00 17.88           N  
ATOM   1174  N   GLY A 148      31.773  48.775  24.361  1.00 11.22           N  
ATOM   1175  CA  GLY A 148      33.112  48.236  24.156  1.00 11.94           C  
ATOM   1176  C   GLY A 148      33.018  46.802  23.663  1.00 12.19           C  
ATOM   1177  O   GLY A 148      31.983  46.398  23.149  1.00 11.74           O  
ATOM   1178  N   ILE A 149      34.079  46.022  23.814  1.00 12.01           N  
ATOM   1179  CA  ILE A 149      34.061  44.630  23.333  1.00 12.38           C  
ATOM   1180  C   ILE A 149      33.296  43.713  24.270  1.00 14.15           C  
ATOM   1181  O   ILE A 149      33.556  43.683  25.479  1.00 13.27           O  
ATOM   1182  CB  ILE A 149      35.507  44.127  23.134  1.00 14.12           C  
ATOM   1183  CG1 ILE A 149      36.136  44.913  21.975  1.00 15.25           C  
ATOM   1184  CG2 ILE A 149      35.533  42.606  22.869  1.00 10.79           C  
ATOM   1185  CD1 ILE A 149      37.603  44.627  21.744  1.00 17.55           C  
ATOM   1186  N   ILE A 150      32.347  42.971  23.708  1.00 13.19           N  
ATOM   1187  CA  ILE A 150      31.507  42.050  24.466  1.00 13.50           C  
ATOM   1188  C   ILE A 150      31.868  40.606  24.147  1.00 15.27           C  
ATOM   1189  O   ILE A 150      32.022  40.241  22.978  1.00 13.23           O  
ATOM   1190  CB  ILE A 150      30.005  42.270  24.129  1.00 16.83           C  
ATOM   1191  CG1 ILE A 150      29.600  43.706  24.483  1.00 17.47           C  
ATOM   1192  CG2 ILE A 150      29.137  41.269  24.903  1.00 16.63           C  
ATOM   1193  CD1 ILE A 150      28.114  43.945  24.520  1.00 22.27           C  
ATOM   1194  N   HIS A 151      32.007  39.789  25.188  1.00 15.59           N  
ATOM   1195  CA  HIS A 151      32.334  38.375  24.998  1.00 18.45           C  
ATOM   1196  C   HIS A 151      31.057  37.566  25.158  1.00 18.14           C  
ATOM   1197  O   HIS A 151      30.461  37.541  26.228  1.00 19.00           O  
ATOM   1198  CB  HIS A 151      33.367  37.924  26.032  1.00 22.72           C  
ATOM   1199  CG  HIS A 151      34.618  38.744  26.020  1.00 27.06           C  
ATOM   1200  ND1 HIS A 151      34.685  40.008  26.569  1.00 31.68           N  
ATOM   1201  CD2 HIS A 151      35.831  38.510  25.467  1.00 30.39           C  
ATOM   1202  CE1 HIS A 151      35.884  40.518  26.351  1.00 31.80           C  
ATOM   1203  NE2 HIS A 151      36.598  39.630  25.683  1.00 31.70           N  
ATOM   1204  N   ALA A 152      30.638  36.901  24.091  1.00 19.08           N  
ATOM   1205  CA  ALA A 152      29.411  36.111  24.122  1.00 20.03           C  
ATOM   1206  C   ALA A 152      29.614  34.722  24.730  1.00 20.33           C  
ATOM   1207  O   ALA A 152      30.742  34.285  24.948  1.00 20.67           O  
ATOM   1208  CB  ALA A 152      28.857  35.974  22.698  1.00 20.31           C  
ATOM   1209  N   ASP A 153      28.505  34.043  25.010  1.00 20.57           N  
ATOM   1210  CA  ASP A 153      28.541  32.677  25.541  1.00 21.82           C  
ATOM   1211  C   ASP A 153      29.094  31.832  24.388  1.00 21.61           C  
ATOM   1212  O   ASP A 153      28.505  31.800  23.311  1.00 20.45           O  
ATOM   1213  CB  ASP A 153      27.116  32.232  25.897  1.00 25.04           C  
ATOM   1214  CG  ASP A 153      27.052  30.804  26.404  1.00 28.52           C  
ATOM   1215  OD1 ASP A 153      27.187  29.862  25.596  1.00 27.78           O  
ATOM   1216  OD2 ASP A 153      26.872  30.625  27.628  1.00 32.93           O  
ATOM   1217  N   GLU A 154      30.221  31.162  24.610  1.00 21.64           N  
ATOM   1218  CA  GLU A 154      30.875  30.365  23.572  1.00 23.10           C  
ATOM   1219  C   GLU A 154      30.045  29.234  22.965  1.00 22.09           C  
ATOM   1220  O   GLU A 154      29.984  29.100  21.742  1.00 20.89           O  
ATOM   1221  CB  GLU A 154      32.182  29.775  24.111  1.00 27.48           C  
ATOM   1222  CG  GLU A 154      33.228  30.800  24.548  1.00 33.65           C  
ATOM   1223  CD  GLU A 154      34.106  31.288  23.404  1.00 37.24           C  
ATOM   1224  OE1 GLU A 154      34.567  30.446  22.600  1.00 40.47           O  
ATOM   1225  OE2 GLU A 154      34.353  32.511  23.321  1.00 41.35           O  
ATOM   1226  N   LYS A 155      29.430  28.409  23.811  1.00 22.65           N  
ATOM   1227  CA  LYS A 155      28.629  27.287  23.315  1.00 23.83           C  
ATOM   1228  C   LYS A 155      27.509  27.742  22.394  1.00 21.86           C  
ATOM   1229  O   LYS A 155      27.346  27.206  21.295  1.00 21.59           O  
ATOM   1230  CB  LYS A 155      28.020  26.491  24.469  1.00 27.07           C  
ATOM   1231  CG  LYS A 155      28.817  25.282  24.896  1.00 33.50           C  
ATOM   1232  CD  LYS A 155      30.149  25.659  25.500  1.00 36.88           C  
ATOM   1233  CE  LYS A 155      30.734  24.471  26.248  1.00 38.99           C  
ATOM   1234  NZ  LYS A 155      32.032  24.817  26.884  1.00 42.13           N  
ATOM   1235  N   LEU A 156      26.728  28.720  22.843  1.00 20.96           N  
ATOM   1236  CA  LEU A 156      25.633  29.228  22.020  1.00 18.78           C  
ATOM   1237  C   LEU A 156      26.147  29.856  20.729  1.00 17.77           C  
ATOM   1238  O   LEU A 156      25.555  29.666  19.660  1.00 17.38           O  
ATOM   1239  CB  LEU A 156      24.822  30.275  22.769  1.00 20.89           C  
ATOM   1240  CG  LEU A 156      23.791  29.861  23.811  1.00 24.43           C  
ATOM   1241  CD1 LEU A 156      23.147  31.138  24.362  1.00 24.32           C  
ATOM   1242  CD2 LEU A 156      22.732  28.943  23.178  1.00 24.44           C  
ATOM   1243  N   ALA A 157      27.239  30.617  20.826  1.00 15.32           N  
ATOM   1244  CA  ALA A 157      27.808  31.276  19.654  1.00 15.07           C  
ATOM   1245  C   ALA A 157      28.288  30.309  18.572  1.00 15.36           C  
ATOM   1246  O   ALA A 157      28.239  30.624  17.389  1.00 14.95           O  
ATOM   1247  CB  ALA A 157      28.971  32.176  20.067  1.00 15.47           C  
ATOM   1248  N   ARG A 158      28.762  29.137  18.982  1.00 14.38           N  
ATOM   1249  CA  ARG A 158      29.302  28.162  18.033  1.00 15.31           C  
ATOM   1250  C   ARG A 158      28.294  27.177  17.462  1.00 16.28           C  
ATOM   1251  O   ARG A 158      28.637  26.348  16.614  1.00 18.26           O  
ATOM   1252  CB  ARG A 158      30.444  27.386  18.703  1.00 16.55           C  
ATOM   1253  CG  ARG A 158      31.643  28.261  19.063  1.00 18.06           C  
ATOM   1254  CD  ARG A 158      32.708  27.460  19.810  1.00 22.87           C  
ATOM   1255  NE  ARG A 158      33.817  28.304  20.253  1.00 25.15           N  
ATOM   1256  CZ  ARG A 158      34.721  28.852  19.445  1.00 26.83           C  
ATOM   1257  NH1 ARG A 158      34.661  28.649  18.139  1.00 28.38           N  
ATOM   1258  NH2 ARG A 158      35.687  29.615  19.949  1.00 28.40           N  
ATOM   1259  N   GLU A 159      27.054  27.266  17.913  1.00 15.54           N  
ATOM   1260  CA  GLU A 159      26.021  26.352  17.447  1.00 16.48           C  
ATOM   1261  C   GLU A 159      25.639  26.541  15.973  1.00 14.81           C  
ATOM   1262  O   GLU A 159      25.633  27.663  15.468  1.00 14.61           O  
ATOM   1263  CB  GLU A 159      24.767  26.531  18.318  1.00 18.67           C  
ATOM   1264  CG  GLU A 159      23.661  25.520  18.074  1.00 21.58           C  
ATOM   1265  CD  GLU A 159      22.493  25.709  19.031  1.00 25.64           C  
ATOM   1266  OE1 GLU A 159      21.648  24.795  19.132  1.00 24.98           O  
ATOM   1267  OE2 GLU A 159      22.420  26.774  19.693  1.00 28.04           O  
ATOM   1268  N   ASP A 160      25.344  25.438  15.277  1.00 14.13           N  
ATOM   1269  CA  ASP A 160      24.860  25.539  13.901  1.00 14.23           C  
ATOM   1270  C   ASP A 160      23.379  25.853  14.124  1.00 14.41           C  
ATOM   1271  O   ASP A 160      22.525  24.944  14.125  1.00 13.81           O  
ATOM   1272  CB  ASP A 160      24.983  24.203  13.154  1.00 14.67           C  
ATOM   1273  CG  ASP A 160      26.374  23.964  12.580  1.00 18.31           C  
ATOM   1274  OD1 ASP A 160      27.232  24.883  12.620  1.00 16.41           O  
ATOM   1275  OD2 ASP A 160      26.598  22.839  12.070  1.00 17.26           O  
ATOM   1276  N   PHE A 161      23.076  27.134  14.319  1.00 13.22           N  
ATOM   1277  CA  PHE A 161      21.721  27.550  14.619  1.00 13.17           C  
ATOM   1278  C   PHE A 161      20.704  27.491  13.491  1.00 13.47           C  
ATOM   1279  O   PHE A 161      21.042  27.405  12.304  1.00 12.80           O  
ATOM   1280  CB  PHE A 161      21.719  28.945  15.264  1.00 13.13           C  
ATOM   1281  CG  PHE A 161      22.375  30.008  14.434  1.00 13.50           C  
ATOM   1282  CD1 PHE A 161      23.733  30.290  14.575  1.00 12.83           C  
ATOM   1283  CD2 PHE A 161      21.632  30.728  13.501  1.00 14.72           C  
ATOM   1284  CE1 PHE A 161      24.343  31.282  13.792  1.00 13.89           C  
ATOM   1285  CE2 PHE A 161      22.232  31.714  12.722  1.00 14.56           C  
ATOM   1286  CZ  PHE A 161      23.594  31.990  12.870  1.00 13.26           C  
ATOM   1287  N   ILE A 162      19.440  27.531  13.889  1.00 13.77           N  
ATOM   1288  CA  ILE A 162      18.334  27.444  12.940  1.00 13.66           C  
ATOM   1289  C   ILE A 162      18.096  28.707  12.118  1.00 13.36           C  
ATOM   1290  O   ILE A 162      18.100  29.836  12.639  1.00 11.94           O  
ATOM   1291  CB  ILE A 162      17.035  27.047  13.682  1.00 13.57           C  
ATOM   1292  CG1 ILE A 162      17.197  25.637  14.252  1.00 15.01           C  
ATOM   1293  CG2 ILE A 162      15.834  27.121  12.724  1.00 16.25           C  
ATOM   1294  CD1 ILE A 162      16.125  25.229  15.230  1.00 21.46           C  
ATOM   1295  N   ILE A 163      17.884  28.501  10.817  1.00 11.24           N  
ATOM   1296  CA  ILE A 163      17.624  29.590   9.880  1.00 12.29           C  
ATOM   1297  C   ILE A 163      16.170  29.529   9.394  1.00 12.01           C  
ATOM   1298  O   ILE A 163      15.567  30.550   9.071  1.00 11.68           O  
ATOM   1299  CB  ILE A 163      18.487  29.474   8.619  1.00 13.18           C  
ATOM   1300  CG1 ILE A 163      19.975  29.469   8.964  1.00 14.88           C  
ATOM   1301  CG2 ILE A 163      18.222  30.659   7.724  1.00 22.42           C  
ATOM   1302  CD1 ILE A 163      20.863  29.292   7.738  1.00 16.31           C  
ATOM   1303  N   HIS A 164      15.636  28.314   9.321  1.00 11.45           N  
ATOM   1304  CA  HIS A 164      14.267  28.092   8.833  1.00 12.92           C  
ATOM   1305  C   HIS A 164      13.719  26.976   9.716  1.00 13.48           C  
ATOM   1306  O   HIS A 164      14.239  25.855   9.738  1.00 13.40           O  
ATOM   1307  CB  HIS A 164      14.347  27.671   7.357  1.00 13.95           C  
ATOM   1308  CG  HIS A 164      13.076  27.847   6.584  1.00 17.48           C  
ATOM   1309  ND1 HIS A 164      11.899  28.282   7.153  1.00 20.96           N  
ATOM   1310  CD2 HIS A 164      12.798  27.612   5.278  1.00 18.74           C  
ATOM   1311  CE1 HIS A 164      10.948  28.304   6.232  1.00 18.72           C  
ATOM   1312  NE2 HIS A 164      11.467  27.902   5.087  1.00 21.95           N  
ATOM   1313  N   ARG A 165      12.670  27.292  10.467  1.00 15.67           N  
ATOM   1314  CA  ARG A 165      12.118  26.331  11.397  1.00 18.07           C  
ATOM   1315  C   ARG A 165      11.371  25.203  10.733  1.00 19.34           C  
ATOM   1316  O   ARG A 165      10.881  25.338   9.612  1.00 19.89           O  
ATOM   1317  CB  ARG A 165      11.213  27.045  12.392  1.00 20.05           C  
ATOM   1318  CG  ARG A 165      11.919  28.152  13.152  1.00 23.12           C  
ATOM   1319  CD  ARG A 165      11.017  28.700  14.250  1.00 32.07           C  
ATOM   1320  NE  ARG A 165      10.457  27.604  15.040  1.00 37.51           N  
ATOM   1321  CZ  ARG A 165       9.539  27.744  15.994  1.00 41.69           C  
ATOM   1322  NH1 ARG A 165       9.057  28.945  16.296  1.00 42.11           N  
ATOM   1323  NH2 ARG A 165       9.100  26.672  16.644  1.00 42.82           N  
ATOM   1324  N   ARG A 166      11.290  24.088  11.442  1.00 22.82           N  
ATOM   1325  CA  ARG A 166      10.606  22.918  10.923  1.00 26.67           C  
ATOM   1326  C   ARG A 166       9.164  23.288  10.595  1.00 26.22           C  
ATOM   1327  O   ARG A 166       8.608  22.787   9.620  1.00 26.38           O  
ATOM   1328  CB  ARG A 166      10.651  21.782  11.950  1.00 29.40           C  
ATOM   1329  CG  ARG A 166      10.220  20.426  11.404  1.00 35.87           C  
ATOM   1330  CD  ARG A 166      10.608  19.313  12.371  1.00 39.06           C  
ATOM   1331  NE  ARG A 166      10.660  18.006  11.719  1.00 44.28           N  
ATOM   1332  CZ  ARG A 166      11.209  16.921  12.259  1.00 45.50           C  
ATOM   1333  NH1 ARG A 166      11.211  15.772  11.592  1.00 46.53           N  
ATOM   1334  NH2 ARG A 166      11.759  16.982  13.466  1.00 46.79           N  
ATOM   1335  N   ASP A 167       8.574  24.187  11.383  1.00 25.66           N  
ATOM   1336  CA  ASP A 167       7.190  24.601  11.143  1.00 26.09           C  
ATOM   1337  C   ASP A 167       7.024  25.556   9.957  1.00 25.43           C  
ATOM   1338  O   ASP A 167       5.910  25.978   9.637  1.00 25.82           O  
ATOM   1339  CB  ASP A 167       6.559  25.204  12.416  1.00 27.51           C  
ATOM   1340  CG  ASP A 167       7.180  26.529  12.830  1.00 30.32           C  
ATOM   1341  OD1 ASP A 167       6.757  27.073  13.880  1.00 31.31           O  
ATOM   1342  OD2 ASP A 167       8.077  27.032  12.125  1.00 26.65           O  
ATOM   1343  N   GLY A 168       8.136  25.887   9.305  1.00 23.53           N  
ATOM   1344  CA  GLY A 168       8.084  26.751   8.136  1.00 21.28           C  
ATOM   1345  C   GLY A 168       8.354  28.232   8.334  1.00 20.40           C  
ATOM   1346  O   GLY A 168       8.451  28.980   7.360  1.00 22.25           O  
ATOM   1347  N   LEU A 169       8.474  28.669   9.579  1.00 17.99           N  
ATOM   1348  CA  LEU A 169       8.720  30.082   9.848  1.00 16.62           C  
ATOM   1349  C   LEU A 169      10.190  30.421   9.665  1.00 14.15           C  
ATOM   1350  O   LEU A 169      11.059  29.624  10.010  1.00 14.62           O  
ATOM   1351  CB  LEU A 169       8.298  30.426  11.279  1.00 20.26           C  
ATOM   1352  CG  LEU A 169       6.803  30.222  11.553  1.00 22.72           C  
ATOM   1353  CD1 LEU A 169       6.484  30.532  13.018  1.00 25.42           C  
ATOM   1354  CD2 LEU A 169       5.998  31.121  10.620  1.00 23.76           C  
ATOM   1355  N   PHE A 170      10.461  31.601   9.114  1.00 14.65           N  
ATOM   1356  CA  PHE A 170      11.838  32.045   8.933  1.00 13.69           C  
ATOM   1357  C   PHE A 170      12.362  32.537  10.280  1.00 14.25           C  
ATOM   1358  O   PHE A 170      11.648  33.204  11.034  1.00 15.26           O  
ATOM   1359  CB  PHE A 170      11.885  33.134   7.859  1.00 14.80           C  
ATOM   1360  CG  PHE A 170      11.483  32.636   6.498  1.00 14.67           C  
ATOM   1361  CD1 PHE A 170      10.223  32.925   5.976  1.00 16.76           C  
ATOM   1362  CD2 PHE A 170      12.347  31.836   5.761  1.00 14.67           C  
ATOM   1363  CE1 PHE A 170       9.835  32.417   4.729  1.00 18.64           C  
ATOM   1364  CE2 PHE A 170      11.967  31.323   4.514  1.00 16.18           C  
ATOM   1365  CZ  PHE A 170      10.711  31.616   4.001  1.00 17.19           C  
ATOM   1366  N   ALA A 171      13.602  32.181  10.606  1.00 12.30           N  
ATOM   1367  CA  ALA A 171      14.164  32.584  11.893  1.00 12.49           C  
ATOM   1368  C   ALA A 171      14.517  34.051  11.922  1.00 11.71           C  
ATOM   1369  O   ALA A 171      14.900  34.626  10.907  1.00 10.41           O  
ATOM   1370  CB  ALA A 171      15.403  31.756  12.199  1.00 12.02           C  
ATOM   1371  N   TYR A 172      14.356  34.658  13.098  1.00 11.66           N  
ATOM   1372  CA  TYR A 172      14.710  36.049  13.299  1.00 11.17           C  
ATOM   1373  C   TYR A 172      16.183  36.308  12.904  1.00 10.33           C  
ATOM   1374  O   TYR A 172      16.471  37.292  12.239  1.00 10.04           O  
ATOM   1375  CB  TYR A 172      14.478  36.415  14.777  1.00 11.41           C  
ATOM   1376  CG  TYR A 172      15.273  37.614  15.254  1.00 10.08           C  
ATOM   1377  CD1 TYR A 172      15.025  38.885  14.749  1.00 12.59           C  
ATOM   1378  CD2 TYR A 172      16.299  37.461  16.180  1.00 10.75           C  
ATOM   1379  CE1 TYR A 172      15.795  39.990  15.155  1.00 13.42           C  
ATOM   1380  CE2 TYR A 172      17.070  38.550  16.595  1.00 13.69           C  
ATOM   1381  CZ  TYR A 172      16.812  39.811  16.076  1.00 13.61           C  
ATOM   1382  OH  TYR A 172      17.586  40.897  16.466  1.00 13.54           O  
ATOM   1383  N   ASN A 173      17.116  35.436  13.302  1.00 10.98           N  
ATOM   1384  CA  ASN A 173      18.527  35.666  12.969  1.00  9.87           C  
ATOM   1385  C   ASN A 173      18.755  35.804  11.466  1.00 10.94           C  
ATOM   1386  O   ASN A 173      19.598  36.598  11.029  1.00 12.15           O  
ATOM   1387  CB  ASN A 173      19.417  34.546  13.515  1.00 10.46           C  
ATOM   1388  CG  ASN A 173      19.698  34.686  15.000  1.00 13.75           C  
ATOM   1389  OD1 ASN A 173      19.929  33.689  15.690  1.00 16.57           O  
ATOM   1390  ND2 ASN A 173      19.707  35.915  15.496  1.00  9.23           N  
ATOM   1391  N   LEU A 174      18.012  35.027  10.681  1.00 10.24           N  
ATOM   1392  CA  LEU A 174      18.109  35.095   9.229  1.00  9.13           C  
ATOM   1393  C   LEU A 174      17.463  36.369   8.701  1.00 10.23           C  
ATOM   1394  O   LEU A 174      18.081  37.138   7.960  1.00 10.71           O  
ATOM   1395  CB  LEU A 174      17.408  33.895   8.576  1.00 11.58           C  
ATOM   1396  CG  LEU A 174      17.282  34.010   7.045  1.00 12.74           C  
ATOM   1397  CD1 LEU A 174      18.665  33.862   6.411  1.00 15.04           C  
ATOM   1398  CD2 LEU A 174      16.304  32.966   6.508  1.00 13.99           C  
ATOM   1399  N   ALA A 175      16.212  36.604   9.083  1.00  9.77           N  
ATOM   1400  CA  ALA A 175      15.486  37.766   8.582  1.00  9.36           C  
ATOM   1401  C   ALA A 175      16.118  39.108   8.922  1.00 10.54           C  
ATOM   1402  O   ALA A 175      16.164  40.016   8.090  1.00  9.82           O  
ATOM   1403  CB  ALA A 175      14.041  37.730   9.096  1.00 10.41           C  
ATOM   1404  N   VAL A 176      16.631  39.237  10.138  1.00  9.95           N  
ATOM   1405  CA  VAL A 176      17.204  40.516  10.512  1.00  8.89           C  
ATOM   1406  C   VAL A 176      18.464  40.840   9.701  1.00 10.64           C  
ATOM   1407  O   VAL A 176      18.694  42.005   9.341  1.00 11.28           O  
ATOM   1408  CB  VAL A 176      17.459  40.578  12.060  1.00  9.82           C  
ATOM   1409  CG1 VAL A 176      18.688  39.748  12.459  1.00 11.05           C  
ATOM   1410  CG2 VAL A 176      17.578  42.028  12.505  1.00  9.90           C  
ATOM   1411  N   VAL A 177      19.262  39.822   9.390  1.00  8.39           N  
ATOM   1412  CA  VAL A 177      20.489  40.038   8.617  1.00  9.91           C  
ATOM   1413  C   VAL A 177      20.119  40.351   7.169  1.00  9.68           C  
ATOM   1414  O   VAL A 177      20.593  41.330   6.593  1.00 10.01           O  
ATOM   1415  CB  VAL A 177      21.421  38.797   8.698  1.00  8.00           C  
ATOM   1416  CG1 VAL A 177      22.636  38.971   7.747  1.00  7.63           C  
ATOM   1417  CG2 VAL A 177      21.924  38.634  10.156  1.00 10.81           C  
ATOM   1418  N   VAL A 178      19.252  39.527   6.586  1.00 10.76           N  
ATOM   1419  CA  VAL A 178      18.821  39.772   5.212  1.00 11.83           C  
ATOM   1420  C   VAL A 178      18.180  41.150   5.034  1.00 11.49           C  
ATOM   1421  O   VAL A 178      18.476  41.869   4.064  1.00 10.37           O  
ATOM   1422  CB  VAL A 178      17.835  38.673   4.743  1.00 12.23           C  
ATOM   1423  CG1 VAL A 178      17.243  39.031   3.373  1.00 12.74           C  
ATOM   1424  CG2 VAL A 178      18.565  37.346   4.656  1.00 13.00           C  
ATOM   1425  N   ASP A 179      17.301  41.538   5.956  1.00 10.46           N  
ATOM   1426  CA  ASP A 179      16.645  42.824   5.828  1.00 10.62           C  
ATOM   1427  C   ASP A 179      17.507  44.040   6.174  1.00 11.31           C  
ATOM   1428  O   ASP A 179      17.390  45.068   5.513  1.00 11.13           O  
ATOM   1429  CB  ASP A 179      15.339  42.864   6.637  1.00 10.76           C  
ATOM   1430  CG  ASP A 179      14.236  42.027   6.010  1.00 13.36           C  
ATOM   1431  OD1 ASP A 179      14.374  41.634   4.832  1.00 13.30           O  
ATOM   1432  OD2 ASP A 179      13.231  41.767   6.695  1.00 11.80           O  
ATOM   1433  N   ASP A 180      18.372  43.944   7.185  1.00  9.57           N  
ATOM   1434  CA  ASP A 180      19.213  45.101   7.489  1.00 10.24           C  
ATOM   1435  C   ASP A 180      20.159  45.334   6.292  1.00 10.63           C  
ATOM   1436  O   ASP A 180      20.406  46.470   5.896  1.00 11.32           O  
ATOM   1437  CB  ASP A 180      20.021  44.895   8.782  1.00 10.07           C  
ATOM   1438  CG  ASP A 180      19.193  45.174  10.057  1.00 11.74           C  
ATOM   1439  OD1 ASP A 180      18.238  45.970   9.991  1.00 12.23           O  
ATOM   1440  OD2 ASP A 180      19.517  44.613  11.130  1.00 11.26           O  
ATOM   1441  N   HIS A 181      20.672  44.254   5.713  1.00 10.43           N  
ATOM   1442  CA  HIS A 181      21.563  44.370   4.561  1.00 11.41           C  
ATOM   1443  C   HIS A 181      20.790  44.988   3.381  1.00 13.07           C  
ATOM   1444  O   HIS A 181      21.273  45.917   2.711  1.00 12.63           O  
ATOM   1445  CB  HIS A 181      22.106  42.980   4.193  1.00 11.78           C  
ATOM   1446  CG  HIS A 181      22.945  42.967   2.950  1.00 14.74           C  
ATOM   1447  ND1 HIS A 181      22.521  42.387   1.774  1.00 18.48           N  
ATOM   1448  CD2 HIS A 181      24.164  43.493   2.692  1.00 18.42           C  
ATOM   1449  CE1 HIS A 181      23.443  42.558   0.843  1.00 19.22           C  
ATOM   1450  NE2 HIS A 181      24.448  43.227   1.372  1.00 18.92           N  
ATOM   1451  N   PHE A 182      19.583  44.479   3.140  1.00 12.69           N  
ATOM   1452  CA  PHE A 182      18.745  44.967   2.051  1.00 13.98           C  
ATOM   1453  C   PHE A 182      18.446  46.457   2.205  1.00 14.85           C  
ATOM   1454  O   PHE A 182      18.421  47.200   1.225  1.00 15.14           O  
ATOM   1455  CB  PHE A 182      17.428  44.193   2.020  1.00 14.15           C  
ATOM   1456  CG  PHE A 182      16.413  44.755   1.052  1.00 16.24           C  
ATOM   1457  CD1 PHE A 182      16.620  44.677  -0.318  1.00 18.33           C  
ATOM   1458  CD2 PHE A 182      15.256  45.370   1.521  1.00 16.45           C  
ATOM   1459  CE1 PHE A 182      15.682  45.211  -1.216  1.00 16.60           C  
ATOM   1460  CE2 PHE A 182      14.315  45.903   0.646  1.00 17.72           C  
ATOM   1461  CZ  PHE A 182      14.530  45.823  -0.733  1.00 19.57           C  
ATOM   1462  N   GLN A 183      18.223  46.889   3.444  1.00 13.05           N  
ATOM   1463  CA  GLN A 183      17.903  48.288   3.699  1.00 14.31           C  
ATOM   1464  C   GLN A 183      19.122  49.187   3.851  1.00 13.99           C  
ATOM   1465  O   GLN A 183      18.987  50.392   4.075  1.00 15.61           O  
ATOM   1466  CB  GLN A 183      16.991  48.405   4.920  1.00 12.81           C  
ATOM   1467  CG  GLN A 183      15.628  47.755   4.704  1.00 14.41           C  
ATOM   1468  CD  GLN A 183      14.641  48.124   5.782  1.00 15.02           C  
ATOM   1469  OE1 GLN A 183      14.640  47.548   6.870  1.00 15.43           O  
ATOM   1470  NE2 GLN A 183      13.801  49.111   5.491  1.00 17.07           N  
ATOM   1471  N   GLY A 184      20.304  48.594   3.723  1.00 14.64           N  
ATOM   1472  CA  GLY A 184      21.539  49.357   3.809  1.00 12.98           C  
ATOM   1473  C   GLY A 184      21.893  49.864   5.186  1.00 13.77           C  
ATOM   1474  O   GLY A 184      22.655  50.827   5.318  1.00 12.61           O  
ATOM   1475  N   VAL A 185      21.338  49.221   6.213  1.00 12.36           N  
ATOM   1476  CA  VAL A 185      21.601  49.608   7.599  1.00 11.84           C  
ATOM   1477  C   VAL A 185      23.099  49.578   7.905  1.00 12.29           C  
ATOM   1478  O   VAL A 185      23.784  48.583   7.629  1.00 10.28           O  
ATOM   1479  CB  VAL A 185      20.839  48.676   8.560  1.00 10.99           C  
ATOM   1480  CG1 VAL A 185      21.256  48.943  10.030  1.00 11.42           C  
ATOM   1481  CG2 VAL A 185      19.338  48.925   8.402  1.00 11.82           C  
ATOM   1482  N   THR A 186      23.604  50.678   8.462  1.00 10.78           N  
ATOM   1483  CA  THR A 186      25.020  50.779   8.785  1.00 11.61           C  
ATOM   1484  C   THR A 186      25.299  50.645  10.272  1.00 11.46           C  
ATOM   1485  O   THR A 186      26.421  50.348  10.662  1.00 11.17           O  
ATOM   1486  CB  THR A 186      25.640  52.112   8.306  1.00 11.45           C  
ATOM   1487  OG1 THR A 186      25.088  53.208   9.052  1.00 12.06           O  
ATOM   1488  CG2 THR A 186      25.385  52.317   6.809  1.00 13.97           C  
ATOM   1489  N   GLU A 187      24.285  50.890  11.099  1.00 10.84           N  
ATOM   1490  CA  GLU A 187      24.453  50.754  12.551  1.00 10.51           C  
ATOM   1491  C   GLU A 187      23.121  50.326  13.142  1.00  9.63           C  
ATOM   1492  O   GLU A 187      22.078  50.883  12.808  1.00 11.40           O  
ATOM   1493  CB  GLU A 187      24.896  52.074  13.192  1.00 11.91           C  
ATOM   1494  CG  GLU A 187      25.140  51.922  14.707  1.00 12.77           C  
ATOM   1495  CD  GLU A 187      25.788  53.149  15.331  1.00 15.82           C  
ATOM   1496  OE1 GLU A 187      27.021  53.130  15.559  1.00 16.96           O  
ATOM   1497  OE2 GLU A 187      25.070  54.128  15.594  1.00 15.93           O  
ATOM   1498  N   ILE A 188      23.183  49.326  14.010  1.00  8.44           N  
ATOM   1499  CA  ILE A 188      22.015  48.755  14.664  1.00  8.71           C  
ATOM   1500  C   ILE A 188      22.047  49.205  16.124  1.00  7.80           C  
ATOM   1501  O   ILE A 188      22.956  48.830  16.862  1.00  9.16           O  
ATOM   1502  CB  ILE A 188      22.084  47.207  14.582  1.00 10.15           C  
ATOM   1503  CG1 ILE A 188      21.897  46.763  13.122  1.00 11.70           C  
ATOM   1504  CG2 ILE A 188      21.039  46.576  15.506  1.00 10.63           C  
ATOM   1505  CD1 ILE A 188      22.248  45.301  12.852  1.00 10.90           C  
ATOM   1506  N   VAL A 189      21.061  50.015  16.514  1.00  9.16           N  
ATOM   1507  CA  VAL A 189      20.952  50.548  17.875  1.00  7.05           C  
ATOM   1508  C   VAL A 189      19.687  49.908  18.421  1.00  8.30           C  
ATOM   1509  O   VAL A 189      18.582  50.203  17.963  1.00  9.70           O  
ATOM   1510  CB  VAL A 189      20.830  52.093  17.836  1.00  7.63           C  
ATOM   1511  CG1 VAL A 189      20.664  52.661  19.267  1.00  7.22           C  
ATOM   1512  CG2 VAL A 189      22.077  52.683  17.157  1.00  6.90           C  
ATOM   1513  N   ARG A 190      19.846  49.013  19.386  1.00  9.09           N  
ATOM   1514  CA  ARG A 190      18.684  48.290  19.900  1.00  8.12           C  
ATOM   1515  C   ARG A 190      18.761  47.954  21.383  1.00  9.33           C  
ATOM   1516  O   ARG A 190      19.726  48.314  22.064  1.00  9.82           O  
ATOM   1517  CB  ARG A 190      18.491  47.005  19.086  1.00  9.13           C  
ATOM   1518  CG  ARG A 190      19.661  46.037  19.189  1.00  8.67           C  
ATOM   1519  CD  ARG A 190      19.550  44.918  18.136  1.00 10.06           C  
ATOM   1520  NE  ARG A 190      20.701  44.022  18.185  1.00  9.86           N  
ATOM   1521  CZ  ARG A 190      20.941  43.062  17.294  1.00 13.46           C  
ATOM   1522  NH1 ARG A 190      22.026  42.298  17.411  1.00 11.63           N  
ATOM   1523  NH2 ARG A 190      20.092  42.859  16.284  1.00 11.96           N  
ATOM   1524  N   GLY A 191      17.710  47.287  21.859  1.00  9.53           N  
ATOM   1525  CA  GLY A 191      17.603  46.906  23.262  1.00 11.69           C  
ATOM   1526  C   GLY A 191      18.670  45.960  23.786  1.00 11.57           C  
ATOM   1527  O   GLY A 191      19.229  45.137  23.057  1.00 10.98           O  
ATOM   1528  N   ALA A 192      18.943  46.078  25.081  1.00 11.52           N  
ATOM   1529  CA  ALA A 192      19.939  45.247  25.753  1.00 12.29           C  
ATOM   1530  C   ALA A 192      19.626  43.755  25.656  1.00 13.54           C  
ATOM   1531  O   ALA A 192      20.526  42.921  25.680  1.00 13.87           O  
ATOM   1532  CB  ALA A 192      20.031  45.655  27.211  1.00 13.41           C  
ATOM   1533  N   ASP A 193      18.344  43.427  25.560  1.00 15.88           N  
ATOM   1534  CA  ASP A 193      17.943  42.033  25.472  1.00 19.41           C  
ATOM   1535  C   ASP A 193      18.390  41.343  24.186  1.00 18.57           C  
ATOM   1536  O   ASP A 193      18.318  40.117  24.078  1.00 19.72           O  
ATOM   1537  CB  ASP A 193      16.419  41.896  25.646  1.00 21.68           C  
ATOM   1538  CG  ASP A 193      15.629  42.903  24.824  1.00 26.40           C  
ATOM   1539  OD1 ASP A 193      14.669  42.481  24.133  1.00 27.89           O  
ATOM   1540  OD2 ASP A 193      15.945  44.120  24.878  1.00 27.20           O  
ATOM   1541  N   LEU A 194      18.862  42.117  23.215  1.00 18.91           N  
ATOM   1542  CA  LEU A 194      19.307  41.555  21.945  1.00 18.96           C  
ATOM   1543  C   LEU A 194      20.818  41.419  21.826  1.00 19.70           C  
ATOM   1544  O   LEU A 194      21.355  41.163  20.742  1.00 20.19           O  
ATOM   1545  CB  LEU A 194      18.762  42.406  20.786  1.00 22.63           C  
ATOM   1546  CG  LEU A 194      17.258  42.257  20.526  1.00 24.77           C  
ATOM   1547  CD1 LEU A 194      16.444  42.562  21.759  1.00 28.05           C  
ATOM   1548  CD2 LEU A 194      16.864  43.184  19.428  1.00 28.09           C  
ATOM   1549  N   ILE A 195      21.527  41.577  22.937  1.00 17.75           N  
ATOM   1550  CA  ILE A 195      22.972  41.469  22.886  1.00 16.71           C  
ATOM   1551  C   ILE A 195      23.473  40.071  22.526  1.00 16.55           C  
ATOM   1552  O   ILE A 195      24.326  39.921  21.648  1.00 15.44           O  
ATOM   1553  CB  ILE A 195      23.621  41.888  24.235  1.00 18.28           C  
ATOM   1554  CG1 ILE A 195      23.547  43.410  24.389  1.00 20.61           C  
ATOM   1555  CG2 ILE A 195      25.086  41.446  24.286  1.00 19.84           C  
ATOM   1556  CD1 ILE A 195      24.088  43.928  25.724  1.00 22.38           C  
ATOM   1557  N   GLU A 196      22.935  39.039  23.176  1.00 15.89           N  
ATOM   1558  CA  GLU A 196      23.442  37.696  22.932  1.00 16.87           C  
ATOM   1559  C   GLU A 196      23.390  37.163  21.502  1.00 16.01           C  
ATOM   1560  O   GLU A 196      24.348  36.559  21.038  1.00 14.68           O  
ATOM   1561  CB  GLU A 196      22.782  36.693  23.889  1.00 20.75           C  
ATOM   1562  CG  GLU A 196      23.668  35.488  24.179  1.00 24.34           C  
ATOM   1563  CD  GLU A 196      24.996  35.854  24.869  1.00 27.43           C  
ATOM   1564  OE1 GLU A 196      25.989  35.129  24.662  1.00 23.27           O  
ATOM   1565  OE2 GLU A 196      25.050  36.851  25.624  1.00 28.84           O  
ATOM   1566  N   PRO A 197      22.281  37.379  20.780  1.00 13.80           N  
ATOM   1567  CA  PRO A 197      22.250  36.861  19.404  1.00 13.23           C  
ATOM   1568  C   PRO A 197      23.140  37.632  18.425  1.00 13.19           C  
ATOM   1569  O   PRO A 197      23.345  37.182  17.310  1.00 12.13           O  
ATOM   1570  CB  PRO A 197      20.771  36.978  19.012  1.00 15.16           C  
ATOM   1571  CG  PRO A 197      20.060  36.885  20.328  1.00 17.47           C  
ATOM   1572  CD  PRO A 197      20.931  37.737  21.238  1.00 14.55           C  
ATOM   1573  N   THR A 198      23.669  38.785  18.834  1.00 11.30           N  
ATOM   1574  CA  THR A 198      24.498  39.580  17.931  1.00  9.84           C  
ATOM   1575  C   THR A 198      25.629  38.792  17.273  1.00  9.17           C  
ATOM   1576  O   THR A 198      25.831  38.901  16.068  1.00  8.47           O  
ATOM   1577  CB  THR A 198      25.135  40.805  18.654  1.00 10.28           C  
ATOM   1578  OG1 THR A 198      24.096  41.633  19.184  1.00 11.67           O  
ATOM   1579  CG2 THR A 198      25.966  41.640  17.669  1.00 10.93           C  
ATOM   1580  N   VAL A 199      26.365  37.989  18.037  1.00 10.22           N  
ATOM   1581  CA  VAL A 199      27.488  37.278  17.405  1.00 10.95           C  
ATOM   1582  C   VAL A 199      27.025  36.302  16.322  1.00 11.25           C  
ATOM   1583  O   VAL A 199      27.717  36.114  15.332  1.00 10.98           O  
ATOM   1584  CB  VAL A 199      28.404  36.542  18.452  1.00 10.80           C  
ATOM   1585  CG1 VAL A 199      29.140  37.580  19.330  1.00 11.49           C  
ATOM   1586  CG2 VAL A 199      27.588  35.598  19.311  1.00 12.89           C  
ATOM   1587  N   ARG A 200      25.847  35.706  16.497  1.00 11.35           N  
ATOM   1588  CA  ARG A 200      25.320  34.774  15.499  1.00 11.91           C  
ATOM   1589  C   ARG A 200      24.986  35.523  14.213  1.00 10.40           C  
ATOM   1590  O   ARG A 200      25.211  35.022  13.108  1.00 11.89           O  
ATOM   1591  CB  ARG A 200      24.060  34.087  16.029  1.00 11.92           C  
ATOM   1592  CG  ARG A 200      24.354  33.033  17.071  1.00 11.53           C  
ATOM   1593  CD  ARG A 200      23.050  32.444  17.607  1.00 11.61           C  
ATOM   1594  NE  ARG A 200      23.309  31.246  18.391  1.00 13.54           N  
ATOM   1595  CZ  ARG A 200      22.367  30.376  18.731  1.00 14.00           C  
ATOM   1596  NH1 ARG A 200      22.680  29.302  19.443  1.00 17.48           N  
ATOM   1597  NH2 ARG A 200      21.112  30.589  18.358  1.00 14.80           N  
ATOM   1598  N   GLN A 201      24.425  36.722  14.360  1.00  9.24           N  
ATOM   1599  CA  GLN A 201      24.088  37.554  13.215  1.00  8.07           C  
ATOM   1600  C   GLN A 201      25.362  37.980  12.489  1.00 11.33           C  
ATOM   1601  O   GLN A 201      25.412  37.988  11.250  1.00 10.47           O  
ATOM   1602  CB  GLN A 201      23.262  38.766  13.676  1.00  9.09           C  
ATOM   1603  CG  GLN A 201      21.915  38.310  14.192  1.00 10.27           C  
ATOM   1604  CD  GLN A 201      21.196  39.333  15.065  1.00 12.26           C  
ATOM   1605  OE1 GLN A 201      21.514  40.526  15.054  1.00 12.66           O  
ATOM   1606  NE2 GLN A 201      20.204  38.861  15.812  1.00 12.50           N  
ATOM   1607  N   ILE A 202      26.408  38.316  13.242  1.00  9.20           N  
ATOM   1608  CA  ILE A 202      27.661  38.700  12.600  1.00  9.68           C  
ATOM   1609  C   ILE A 202      28.231  37.486  11.850  1.00 10.50           C  
ATOM   1610  O   ILE A 202      28.697  37.619  10.709  1.00 11.34           O  
ATOM   1611  CB  ILE A 202      28.675  39.230  13.638  1.00  7.36           C  
ATOM   1612  CG1 ILE A 202      28.116  40.522  14.255  1.00  8.04           C  
ATOM   1613  CG2 ILE A 202      30.034  39.522  12.956  1.00  9.55           C  
ATOM   1614  CD1 ILE A 202      28.992  41.115  15.425  1.00  8.80           C  
ATOM   1615  N   SER A 203      28.172  36.305  12.465  1.00 11.19           N  
ATOM   1616  CA  SER A 203      28.674  35.111  11.778  1.00 12.44           C  
ATOM   1617  C   SER A 203      27.932  34.951  10.447  1.00 12.91           C  
ATOM   1618  O   SER A 203      28.532  34.576   9.427  1.00 11.42           O  
ATOM   1619  CB  SER A 203      28.471  33.856  12.640  1.00 12.53           C  
ATOM   1620  OG  SER A 203      29.253  33.928  13.824  1.00 14.85           O  
ATOM   1621  N   LEU A 204      26.632  35.238  10.449  1.00 11.45           N  
ATOM   1622  CA  LEU A 204      25.845  35.109   9.230  1.00 12.60           C  
ATOM   1623  C   LEU A 204      26.232  36.149   8.166  1.00 12.17           C  
ATOM   1624  O   LEU A 204      26.326  35.821   6.986  1.00 12.01           O  
ATOM   1625  CB  LEU A 204      24.347  35.158   9.565  1.00 12.94           C  
ATOM   1626  CG  LEU A 204      23.359  34.821   8.451  1.00 16.85           C  
ATOM   1627  CD1 LEU A 204      23.690  33.461   7.833  1.00 16.69           C  
ATOM   1628  CD2 LEU A 204      21.955  34.785   9.043  1.00 16.55           C  
ATOM   1629  N   TYR A 205      26.479  37.395   8.566  1.00 10.04           N  
ATOM   1630  CA  TYR A 205      26.913  38.426   7.610  1.00 10.10           C  
ATOM   1631  C   TYR A 205      28.191  37.948   6.923  1.00 10.21           C  
ATOM   1632  O   TYR A 205      28.363  38.100   5.710  1.00 13.54           O  
ATOM   1633  CB  TYR A 205      27.251  39.724   8.349  1.00 10.76           C  
ATOM   1634  CG  TYR A 205      26.094  40.685   8.510  1.00 12.00           C  
ATOM   1635  CD1 TYR A 205      25.674  41.480   7.445  1.00 11.36           C  
ATOM   1636  CD2 TYR A 205      25.459  40.837   9.748  1.00 12.74           C  
ATOM   1637  CE1 TYR A 205      24.658  42.406   7.602  1.00 14.05           C  
ATOM   1638  CE2 TYR A 205      24.441  41.762   9.919  1.00 12.38           C  
ATOM   1639  CZ  TYR A 205      24.046  42.546   8.848  1.00 12.17           C  
ATOM   1640  OH  TYR A 205      23.049  43.474   9.016  1.00 11.36           O  
ATOM   1641  N   GLN A 206      29.090  37.392   7.724  1.00 11.57           N  
ATOM   1642  CA  GLN A 206      30.377  36.916   7.223  1.00 12.07           C  
ATOM   1643  C   GLN A 206      30.221  35.785   6.225  1.00 13.46           C  
ATOM   1644  O   GLN A 206      30.947  35.733   5.223  1.00 14.21           O  
ATOM   1645  CB  GLN A 206      31.264  36.475   8.387  1.00 13.39           C  
ATOM   1646  CG  GLN A 206      31.760  37.673   9.206  1.00 15.10           C  
ATOM   1647  CD  GLN A 206      32.683  37.286  10.349  1.00 16.34           C  
ATOM   1648  OE1 GLN A 206      33.335  38.144  10.948  1.00 19.74           O  
ATOM   1649  NE2 GLN A 206      32.740  36.004  10.660  1.00 16.42           N  
ATOM   1650  N   LEU A 207      29.273  34.897   6.486  1.00 13.44           N  
ATOM   1651  CA  LEU A 207      29.033  33.772   5.585  1.00 14.60           C  
ATOM   1652  C   LEU A 207      28.420  34.232   4.267  1.00 16.07           C  
ATOM   1653  O   LEU A 207      28.703  33.645   3.210  1.00 16.94           O  
ATOM   1654  CB  LEU A 207      28.162  32.729   6.280  1.00 15.98           C  
ATOM   1655  CG  LEU A 207      28.880  32.047   7.452  1.00 19.02           C  
ATOM   1656  CD1 LEU A 207      27.967  31.026   8.111  1.00 20.84           C  
ATOM   1657  CD2 LEU A 207      30.148  31.378   6.952  1.00 22.14           C  
ATOM   1658  N   PHE A 208      27.595  35.277   4.320  1.00 14.98           N  
ATOM   1659  CA  PHE A 208      26.998  35.847   3.107  1.00 16.24           C  
ATOM   1660  C   PHE A 208      28.043  36.698   2.378  1.00 16.22           C  
ATOM   1661  O   PHE A 208      27.855  37.069   1.215  1.00 17.56           O  
ATOM   1662  CB  PHE A 208      25.815  36.775   3.429  1.00 14.77           C  
ATOM   1663  CG  PHE A 208      24.514  36.069   3.652  1.00 16.42           C  
ATOM   1664  CD1 PHE A 208      23.945  35.285   2.646  1.00 15.37           C  
ATOM   1665  CD2 PHE A 208      23.825  36.217   4.857  1.00 16.55           C  
ATOM   1666  CE1 PHE A 208      22.710  34.657   2.837  1.00 15.62           C  
ATOM   1667  CE2 PHE A 208      22.586  35.592   5.054  1.00 18.09           C  
ATOM   1668  CZ  PHE A 208      22.028  34.807   4.034  1.00 16.86           C  
ATOM   1669  N   GLY A 209      29.129  37.023   3.069  1.00 15.55           N  
ATOM   1670  CA  GLY A 209      30.151  37.866   2.477  1.00 16.73           C  
ATOM   1671  C   GLY A 209      29.702  39.320   2.422  1.00 17.52           C  
ATOM   1672  O   GLY A 209      30.073  40.056   1.513  1.00 19.58           O  
ATOM   1673  N   TRP A 210      28.895  39.737   3.400  1.00 15.69           N  
ATOM   1674  CA  TRP A 210      28.380  41.100   3.469  1.00 16.00           C  
ATOM   1675  C   TRP A 210      29.069  41.937   4.546  1.00 15.21           C  
ATOM   1676  O   TRP A 210      29.589  41.398   5.524  1.00 17.15           O  
ATOM   1677  CB  TRP A 210      26.880  41.104   3.775  1.00 16.37           C  
ATOM   1678  CG  TRP A 210      26.010  40.445   2.737  1.00 14.70           C  
ATOM   1679  CD1 TRP A 210      26.289  40.278   1.406  1.00 16.21           C  
ATOM   1680  CD2 TRP A 210      24.682  39.964   2.932  1.00 15.31           C  
ATOM   1681  NE1 TRP A 210      25.205  39.723   0.758  1.00 13.80           N  
ATOM   1682  CE2 TRP A 210      24.204  39.525   1.674  1.00 15.66           C  
ATOM   1683  CE3 TRP A 210      23.837  39.866   4.048  1.00 14.35           C  
ATOM   1684  CZ2 TRP A 210      22.924  38.999   1.504  1.00 16.09           C  
ATOM   1685  CZ3 TRP A 210      22.564  39.341   3.878  1.00 15.10           C  
ATOM   1686  CH2 TRP A 210      22.119  38.914   2.611  1.00 16.81           C  
ATOM   1687  N   LYS A 211      29.039  43.254   4.367  1.00 15.45           N  
ATOM   1688  CA  LYS A 211      29.660  44.160   5.326  1.00 17.07           C  
ATOM   1689  C   LYS A 211      28.915  44.108   6.659  1.00 16.19           C  
ATOM   1690  O   LYS A 211      27.693  44.235   6.703  1.00 16.53           O  
ATOM   1691  CB  LYS A 211      29.652  45.590   4.799  1.00 20.12           C  
ATOM   1692  CG  LYS A 211      30.369  46.569   5.723  1.00 24.46           C  
ATOM   1693  CD  LYS A 211      30.567  47.927   5.068  1.00 29.81           C  
ATOM   1694  CE  LYS A 211      31.119  48.939   6.069  1.00 29.57           C  
ATOM   1695  NZ  LYS A 211      32.286  48.395   6.808  1.00 33.86           N  
ATOM   1696  N   VAL A 212      29.668  43.917   7.733  1.00 14.99           N  
ATOM   1697  CA  VAL A 212      29.100  43.845   9.081  1.00 13.13           C  
ATOM   1698  C   VAL A 212      28.849  45.265   9.580  1.00 13.15           C  
ATOM   1699  O   VAL A 212      29.743  46.122   9.531  1.00 13.87           O  
ATOM   1700  CB  VAL A 212      30.088  43.130  10.039  1.00 13.15           C  
ATOM   1701  CG1 VAL A 212      29.536  43.119  11.459  1.00 14.93           C  
ATOM   1702  CG2 VAL A 212      30.340  41.689   9.552  1.00 13.59           C  
ATOM   1703  N   PRO A 213      27.624  45.550  10.061  1.00 12.44           N  
ATOM   1704  CA  PRO A 213      27.327  46.898  10.557  1.00 11.34           C  
ATOM   1705  C   PRO A 213      27.883  47.110  11.954  1.00  9.88           C  
ATOM   1706  O   PRO A 213      28.438  46.191  12.557  1.00 10.80           O  
ATOM   1707  CB  PRO A 213      25.805  46.938  10.568  1.00 12.57           C  
ATOM   1708  CG  PRO A 213      25.446  45.500  10.929  1.00 14.14           C  
ATOM   1709  CD  PRO A 213      26.418  44.696  10.064  1.00 13.47           C  
ATOM   1710  N   ASP A 214      27.720  48.327  12.460  1.00 10.09           N  
ATOM   1711  CA  ASP A 214      28.155  48.647  13.816  1.00  9.86           C  
ATOM   1712  C   ASP A 214      26.964  48.357  14.733  1.00 11.23           C  
ATOM   1713  O   ASP A 214      25.812  48.299  14.274  1.00 11.35           O  
ATOM   1714  CB  ASP A 214      28.562  50.117  13.927  1.00 10.61           C  
ATOM   1715  CG  ASP A 214      29.930  50.396  13.302  1.00 13.43           C  
ATOM   1716  OD1 ASP A 214      30.705  49.434  13.102  1.00 12.94           O  
ATOM   1717  OD2 ASP A 214      30.235  51.582  13.032  1.00 16.04           O  
ATOM   1718  N   TYR A 215      27.248  48.169  16.019  1.00  9.86           N  
ATOM   1719  CA  TYR A 215      26.214  47.842  16.995  1.00  9.53           C  
ATOM   1720  C   TYR A 215      26.259  48.715  18.236  1.00 10.36           C  
ATOM   1721  O   TYR A 215      27.342  49.067  18.711  1.00  9.89           O  
ATOM   1722  CB  TYR A 215      26.385  46.406  17.480  1.00  9.69           C  
ATOM   1723  CG  TYR A 215      26.118  45.381  16.416  1.00 10.33           C  
ATOM   1724  CD1 TYR A 215      27.134  44.952  15.560  1.00  9.10           C  
ATOM   1725  CD2 TYR A 215      24.828  44.893  16.223  1.00 11.30           C  
ATOM   1726  CE1 TYR A 215      26.863  44.053  14.528  1.00 11.10           C  
ATOM   1727  CE2 TYR A 215      24.546  44.002  15.195  1.00 10.48           C  
ATOM   1728  CZ  TYR A 215      25.568  43.589  14.355  1.00 10.59           C  
ATOM   1729  OH  TYR A 215      25.281  42.719  13.334  1.00 10.74           O  
ATOM   1730  N   ILE A 216      25.076  49.025  18.759  1.00 10.30           N  
ATOM   1731  CA  ILE A 216      24.948  49.767  20.010  1.00  8.64           C  
ATOM   1732  C   ILE A 216      23.771  49.147  20.750  1.00  9.09           C  
ATOM   1733  O   ILE A 216      22.652  49.123  20.226  1.00 10.41           O  
ATOM   1734  CB  ILE A 216      24.653  51.278  19.805  1.00  7.99           C  
ATOM   1735  CG1 ILE A 216      25.905  51.991  19.278  1.00  8.44           C  
ATOM   1736  CG2 ILE A 216      24.226  51.917  21.150  1.00 10.63           C  
ATOM   1737  CD1 ILE A 216      25.667  53.418  18.794  1.00  9.74           C  
ATOM   1738  N   HIS A 217      24.019  48.636  21.956  1.00  8.26           N  
ATOM   1739  CA  HIS A 217      22.933  48.094  22.764  1.00  9.01           C  
ATOM   1740  C   HIS A 217      22.673  49.053  23.923  1.00  9.73           C  
ATOM   1741  O   HIS A 217      23.575  49.417  24.682  1.00  9.33           O  
ATOM   1742  CB  HIS A 217      23.249  46.677  23.208  1.00  9.60           C  
ATOM   1743  CG  HIS A 217      23.277  45.719  22.059  1.00  9.97           C  
ATOM   1744  ND1 HIS A 217      24.397  45.524  21.277  1.00  9.74           N  
ATOM   1745  CD2 HIS A 217      22.284  44.997  21.484  1.00 11.37           C  
ATOM   1746  CE1 HIS A 217      24.091  44.722  20.268  1.00 11.20           C  
ATOM   1747  NE2 HIS A 217      22.813  44.390  20.370  1.00  9.70           N  
ATOM   1748  N   LEU A 218      21.421  49.501  23.973  1.00  8.71           N  
ATOM   1749  CA  LEU A 218      20.940  50.480  24.940  1.00  8.80           C  
ATOM   1750  C   LEU A 218      20.921  49.946  26.374  1.00  8.05           C  
ATOM   1751  O   LEU A 218      21.148  48.768  26.605  1.00 10.32           O  
ATOM   1752  CB  LEU A 218      19.568  50.973  24.463  1.00  9.10           C  
ATOM   1753  CG  LEU A 218      19.674  51.596  23.051  1.00  9.86           C  
ATOM   1754  CD1 LEU A 218      18.287  51.917  22.482  1.00 10.16           C  
ATOM   1755  CD2 LEU A 218      20.529  52.849  23.107  1.00 12.40           C  
ATOM   1756  N   PRO A 219      20.641  50.817  27.367  1.00 10.42           N  
ATOM   1757  CA  PRO A 219      20.635  50.348  28.759  1.00 11.04           C  
ATOM   1758  C   PRO A 219      19.676  49.207  29.065  1.00 11.59           C  
ATOM   1759  O   PRO A 219      18.565  49.165  28.532  1.00 12.45           O  
ATOM   1760  CB  PRO A 219      20.263  51.606  29.571  1.00  9.96           C  
ATOM   1761  CG  PRO A 219      20.515  52.777  28.645  1.00 12.29           C  
ATOM   1762  CD  PRO A 219      20.179  52.213  27.269  1.00 11.10           C  
ATOM   1763  N   LEU A 220      20.121  48.299  29.930  1.00 10.74           N  
ATOM   1764  CA  LEU A 220      19.314  47.175  30.399  1.00 14.06           C  
ATOM   1765  C   LEU A 220      18.278  47.821  31.329  1.00 15.35           C  
ATOM   1766  O   LEU A 220      18.637  48.520  32.278  1.00 15.17           O  
ATOM   1767  CB  LEU A 220      20.181  46.203  31.203  1.00 15.35           C  
ATOM   1768  CG  LEU A 220      19.414  45.099  31.945  1.00 17.55           C  
ATOM   1769  CD1 LEU A 220      18.699  44.191  30.936  1.00 18.63           C  
ATOM   1770  CD2 LEU A 220      20.394  44.297  32.799  1.00 16.39           C  
ATOM   1771  N   ALA A 221      17.001  47.591  31.061  1.00 15.35           N  
ATOM   1772  CA  ALA A 221      15.957  48.196  31.879  1.00 15.29           C  
ATOM   1773  C   ALA A 221      15.659  47.348  33.114  1.00 15.84           C  
ATOM   1774  O   ALA A 221      15.426  46.134  33.017  1.00 17.28           O  
ATOM   1775  CB  ALA A 221      14.693  48.392  31.045  1.00 15.18           C  
ATOM   1776  N   LEU A 222      15.671  47.995  34.276  1.00 15.81           N  
ATOM   1777  CA  LEU A 222      15.389  47.318  35.541  1.00 15.69           C  
ATOM   1778  C   LEU A 222      14.123  47.919  36.157  1.00 15.40           C  
ATOM   1779  O   LEU A 222      13.836  49.097  35.946  1.00 15.61           O  
ATOM   1780  CB  LEU A 222      16.550  47.519  36.522  1.00 17.34           C  
ATOM   1781  CG  LEU A 222      17.954  47.138  36.053  1.00 18.74           C  
ATOM   1782  CD1 LEU A 222      18.968  47.481  37.137  1.00 19.66           C  
ATOM   1783  CD2 LEU A 222      17.995  45.661  35.721  1.00 18.97           C  
ATOM   1784  N   ASN A 223      13.366  47.113  36.901  1.00 17.14           N  
ATOM   1785  CA  ASN A 223      12.181  47.641  37.575  1.00 18.47           C  
ATOM   1786  C   ASN A 223      12.704  48.351  38.835  1.00 18.36           C  
ATOM   1787  O   ASN A 223      13.890  48.256  39.154  1.00 17.86           O  
ATOM   1788  CB  ASN A 223      11.186  46.525  37.949  1.00 21.01           C  
ATOM   1789  CG  ASN A 223      11.784  45.467  38.857  1.00 22.20           C  
ATOM   1790  OD1 ASN A 223      12.550  45.763  39.770  1.00 23.12           O  
ATOM   1791  ND2 ASN A 223      11.414  44.214  38.617  1.00 25.41           N  
ATOM   1792  N   PRO A 224      11.833  49.070  39.565  1.00 18.41           N  
ATOM   1793  CA  PRO A 224      12.285  49.776  40.775  1.00 18.62           C  
ATOM   1794  C   PRO A 224      12.987  48.922  41.828  1.00 17.93           C  
ATOM   1795  O   PRO A 224      13.789  49.437  42.610  1.00 17.97           O  
ATOM   1796  CB  PRO A 224      10.999  50.397  41.314  1.00 19.16           C  
ATOM   1797  CG  PRO A 224      10.234  50.702  40.061  1.00 19.93           C  
ATOM   1798  CD  PRO A 224      10.447  49.440  39.230  1.00 18.53           C  
ATOM   1799  N   GLN A 225      12.683  47.627  41.849  1.00 19.82           N  
ATOM   1800  CA  GLN A 225      13.271  46.729  42.829  1.00 22.20           C  
ATOM   1801  C   GLN A 225      14.666  46.277  42.432  1.00 23.45           C  
ATOM   1802  O   GLN A 225      15.378  45.659  43.223  1.00 22.25           O  
ATOM   1803  CB  GLN A 225      12.352  45.521  43.050  1.00 25.62           C  
ATOM   1804  CG  GLN A 225      11.043  45.872  43.768  1.00 28.19           C  
ATOM   1805  CD  GLN A 225      10.117  46.749  42.937  1.00 31.48           C  
ATOM   1806  OE1 GLN A 225       9.451  47.642  43.468  1.00 33.84           O  
ATOM   1807  NE2 GLN A 225      10.056  46.491  41.630  1.00 30.56           N  
ATOM   1808  N   GLY A 226      15.058  46.610  41.205  1.00 22.50           N  
ATOM   1809  CA  GLY A 226      16.377  46.249  40.731  1.00 22.12           C  
ATOM   1810  C   GLY A 226      16.425  44.986  39.889  1.00 24.18           C  
ATOM   1811  O   GLY A 226      17.511  44.520  39.548  1.00 26.12           O  
ATOM   1812  N   ALA A 227      15.264  44.433  39.556  1.00 25.65           N  
ATOM   1813  CA  ALA A 227      15.187  43.221  38.742  1.00 26.50           C  
ATOM   1814  C   ALA A 227      14.980  43.609  37.281  1.00 27.24           C  
ATOM   1815  O   ALA A 227      14.514  44.709  36.999  1.00 26.11           O  
ATOM   1816  CB  ALA A 227      14.029  42.354  39.209  1.00 27.50           C  
ATOM   1817  N   LYS A 228      15.313  42.705  36.358  1.00 29.10           N  
ATOM   1818  CA  LYS A 228      15.141  42.983  34.929  1.00 31.84           C  
ATOM   1819  C   LYS A 228      13.683  43.249  34.596  1.00 33.65           C  
ATOM   1820  O   LYS A 228      12.819  42.408  34.835  1.00 34.73           O  
ATOM   1821  CB  LYS A 228      15.647  41.813  34.080  1.00 31.90           C  
ATOM   1822  CG  LYS A 228      17.155  41.729  33.983  1.00 32.97           C  
ATOM   1823  CD  LYS A 228      17.585  40.631  33.012  1.00 34.65           C  
ATOM   1824  CE  LYS A 228      19.097  40.505  32.960  1.00 36.60           C  
ATOM   1825  NZ  LYS A 228      19.533  39.445  32.002  1.00 39.07           N  
ATOM   1826  N   LEU A 229      13.414  44.419  34.026  1.00 36.63           N  
ATOM   1827  CA  LEU A 229      12.055  44.807  33.679  1.00 40.42           C  
ATOM   1828  C   LEU A 229      11.369  43.793  32.774  1.00 44.14           C  
ATOM   1829  O   LEU A 229      10.143  43.793  32.649  1.00 44.63           O  
ATOM   1830  CB  LEU A 229      12.052  46.173  32.999  1.00 39.96           C  
ATOM   1831  CG  LEU A 229      10.674  46.780  32.741  1.00 39.60           C  
ATOM   1832  CD1 LEU A 229       9.951  46.982  34.071  1.00 39.82           C  
ATOM   1833  CD2 LEU A 229      10.830  48.105  32.006  1.00 39.69           C  
ATOM   1834  N   SER A 230      12.157  42.933  32.140  1.00 47.47           N  
ATOM   1835  CA  SER A 230      11.595  41.926  31.251  1.00 51.84           C  
ATOM   1836  C   SER A 230      11.195  40.675  32.024  1.00 53.75           C  
ATOM   1837  O   SER A 230      11.490  39.556  31.603  1.00 54.69           O  
ATOM   1838  CB  SER A 230      12.600  41.565  30.150  1.00 51.69           C  
ATOM   1839  OG  SER A 230      13.812  41.080  30.698  1.00 52.49           O  
ATOM   1840  N   LYS A 231      10.524  40.869  33.157  1.00 56.73           N  
ATOM   1841  CA  LYS A 231      10.078  39.745  33.973  1.00 59.00           C  
ATOM   1842  C   LYS A 231       8.917  39.072  33.243  1.00 60.70           C  
ATOM   1843  O   LYS A 231       9.076  38.576  32.126  1.00 61.35           O  
ATOM   1844  CB  LYS A 231       9.598  40.213  35.354  1.00 59.13           C  
ATOM   1845  CG  LYS A 231      10.201  41.512  35.878  1.00 58.79           C  
ATOM   1846  CD  LYS A 231       9.343  42.704  35.482  1.00 58.88           C  
ATOM   1847  CE  LYS A 231       9.510  43.868  36.446  1.00 58.47           C  
ATOM   1848  NZ  LYS A 231       8.525  44.959  36.190  1.00 58.44           N  
ATOM   1849  N   GLN A 232       7.749  39.054  33.880  1.00 62.34           N  
ATOM   1850  CA  GLN A 232       6.563  38.460  33.275  1.00 63.81           C  
ATOM   1851  C   GLN A 232       6.197  39.303  32.058  1.00 64.46           C  
ATOM   1852  O   GLN A 232       6.619  40.457  31.953  1.00 64.20           O  
ATOM   1853  CB  GLN A 232       5.405  38.451  34.281  1.00 64.32           C  
ATOM   1854  CG  GLN A 232       4.073  37.958  33.718  1.00 64.95           C  
ATOM   1855  CD  GLN A 232       4.179  36.586  33.079  1.00 65.56           C  
ATOM   1856  OE1 GLN A 232       4.626  35.629  33.711  1.00 66.27           O  
ATOM   1857  NE2 GLN A 232       3.765  36.485  31.821  1.00 65.78           N  
ATOM   1858  N   ASN A 233       5.416  38.729  31.149  1.00 65.09           N  
ATOM   1859  CA  ASN A 233       4.991  39.438  29.949  1.00 65.68           C  
ATOM   1860  C   ASN A 233       3.819  40.375  30.222  1.00 65.66           C  
ATOM   1861  O   ASN A 233       2.910  40.041  30.981  1.00 66.07           O  
ATOM   1862  CB  ASN A 233       4.626  38.448  28.842  1.00 66.32           C  
ATOM   1863  CG  ASN A 233       4.166  39.136  27.572  1.00 66.94           C  
ATOM   1864  OD1 ASN A 233       4.118  40.364  27.500  1.00 67.12           O  
ATOM   1865  ND2 ASN A 233       3.825  38.346  26.561  1.00 67.24           N  
ATOM   1866  N   HIS A 234       3.899  41.640  29.911  1.00 65.38           N  
ATOM   1867  CA  HIS A 234       2.858  42.588  30.039  1.00 64.87           C  
ATOM   1868  C   HIS A 234       3.224  43.867  30.433  1.00 64.11           C  
ATOM   1869  O   HIS A 234       2.691  44.247  31.136  1.00 64.50           O  
ATOM   1870  CB  HIS A 234       1.619  42.231  30.946  1.00 65.66           C  
ATOM   1871  CG  HIS A 234       0.575  41.410  30.255  1.00 66.59           C  
ATOM   1872  ND1 HIS A 234       0.047  40.265  30.789  1.00 66.97           N  
ATOM   1873  CD2 HIS A 234       0.109  41.458  28.972  1.00 66.99           C  
ATOM   1874  CE1 HIS A 234      -0.710  39.651  29.900  1.00 67.19           C  
ATOM   1875  NE2 HIS A 234      -0.670  40.333  28.783  1.00 67.36           N  
ATOM   1876  N   ALA A 235       3.939  44.662  29.819  1.00 62.59           N  
ATOM   1877  CA  ALA A 235       4.423  45.901  30.416  1.00 60.77           C  
ATOM   1878  C   ALA A 235       3.543  47.073  29.996  1.00 59.17           C  
ATOM   1879  O   ALA A 235       3.422  47.375  28.809  1.00 60.04           O  
ATOM   1880  CB  ALA A 235       5.869  46.151  30.019  1.00 60.91           C  
ATOM   1881  N   PRO A 236       2.926  47.728  30.974  1.00 57.16           N  
ATOM   1882  CA  PRO A 236       2.060  48.789  30.706  1.00 55.72           C  
ATOM   1883  C   PRO A 236       2.478  49.644  29.613  1.00 54.49           C  
ATOM   1884  O   PRO A 236       3.286  49.473  28.755  1.00 53.94           O  
ATOM   1885  CB  PRO A 236       2.319  49.634  31.850  1.00 55.88           C  
ATOM   1886  CG  PRO A 236       3.225  48.939  32.432  1.00 56.25           C  
ATOM   1887  CD  PRO A 236       3.791  48.122  31.947  1.00 56.65           C  
ATOM   1888  N   ALA A 237       1.867  50.809  29.723  1.00 52.87           N  
ATOM   1889  CA  ALA A 237       1.560  51.075  28.574  1.00 50.73           C  
ATOM   1890  C   ALA A 237       1.686  52.391  27.858  1.00 49.10           C  
ATOM   1891  O   ALA A 237       0.942  53.549  28.362  1.00 49.62           O  
ATOM   1892  CB  ALA A 237       0.936  49.796  27.978  1.00 49.36           C  
ATOM   1893  N   LEU A 238       2.727  52.399  26.789  1.00 48.45           N  
ATOM   1894  CA  LEU A 238       2.790  53.856  26.755  1.00 46.25           C  
ATOM   1895  C   LEU A 238       1.398  54.482  26.759  1.00 45.90           C  
ATOM   1896  O   LEU A 238       0.486  53.997  26.089  1.00 45.33           O  
ATOM   1897  CB  LEU A 238       3.575  54.329  25.530  1.00 45.85           C  
ATOM   1898  CG  LEU A 238       5.024  53.851  25.427  1.00 44.79           C  
ATOM   1899  CD1 LEU A 238       5.656  54.326  24.128  1.00 46.13           C  
ATOM   1900  CD2 LEU A 238       5.833  54.322  26.626  1.00 45.38           C  
ATOM   1901  N   PRO A 239       1.245  55.563  27.517  1.00 45.23           N  
ATOM   1902  CA  PRO A 239      -0.030  56.278  27.596  1.00 44.41           C  
ATOM   1903  C   PRO A 239      -0.442  56.848  26.239  1.00 43.62           C  
ATOM   1904  O   PRO A 239       0.413  57.215  25.426  1.00 43.62           O  
ATOM   1905  CB  PRO A 239       0.261  57.374  28.613  1.00 43.85           C  
ATOM   1906  CG  PRO A 239       1.252  56.723  29.522  1.00 44.89           C  
ATOM   1907  CD  PRO A 239       2.183  56.061  28.539  1.00 45.44           C  
ATOM   1908  N   LYS A 240      -1.750  56.909  25.997  1.00 42.65           N  
ATOM   1909  CA  LYS A 240      -2.273  57.452  24.747  1.00 41.97           C  
ATOM   1910  C   LYS A 240      -2.400  58.965  24.865  1.00 40.36           C  
ATOM   1911  O   LYS A 240      -2.583  59.664  23.866  1.00 41.54           O  
ATOM   1912  CB  LYS A 240      -3.644  56.844  24.427  1.00 43.29           C  
ATOM   1913  CG  LYS A 240      -3.600  55.355  24.130  1.00 44.60           C  
ATOM   1914  CD  LYS A 240      -4.980  54.789  23.827  1.00 46.46           C  
ATOM   1915  CE  LYS A 240      -4.887  53.306  23.474  1.00 47.50           C  
ATOM   1916  NZ  LYS A 240      -6.221  52.692  23.257  1.00 49.10           N  
ATOM   1917  N   GLY A 241      -2.302  59.461  26.095  1.00 37.58           N  
ATOM   1918  CA  GLY A 241      -2.408  60.889  26.334  1.00 35.23           C  
ATOM   1919  C   GLY A 241      -1.131  61.652  26.029  1.00 33.04           C  
ATOM   1920  O   GLY A 241      -0.355  61.262  25.151  1.00 32.81           O  
ATOM   1921  N   ASP A 242      -0.914  62.739  26.765  1.00 30.20           N  
ATOM   1922  CA  ASP A 242       0.259  63.597  26.583  1.00 27.38           C  
ATOM   1923  C   ASP A 242       1.542  62.778  26.619  1.00 23.69           C  
ATOM   1924  O   ASP A 242       1.912  62.237  27.654  1.00 23.59           O  
ATOM   1925  CB  ASP A 242       0.306  64.650  27.687  1.00 25.81           C  
ATOM   1926  CG  ASP A 242       1.279  65.790  27.385  1.00 25.73           C  
ATOM   1927  OD1 ASP A 242       2.108  65.675  26.457  1.00 21.83           O  
ATOM   1928  OD2 ASP A 242       1.211  66.812  28.101  1.00 25.07           O  
ATOM   1929  N   PRO A 243       2.245  62.694  25.489  1.00 23.11           N  
ATOM   1930  CA  PRO A 243       3.487  61.919  25.457  1.00 19.89           C  
ATOM   1931  C   PRO A 243       4.709  62.599  26.069  1.00 17.86           C  
ATOM   1932  O   PRO A 243       5.711  61.944  26.321  1.00 16.98           O  
ATOM   1933  CB  PRO A 243       3.682  61.652  23.968  1.00 22.48           C  
ATOM   1934  CG  PRO A 243       3.141  62.895  23.350  1.00 25.03           C  
ATOM   1935  CD  PRO A 243       1.885  63.169  24.141  1.00 22.52           C  
ATOM   1936  N   ARG A 244       4.624  63.899  26.330  1.00 16.20           N  
ATOM   1937  CA  ARG A 244       5.775  64.625  26.857  1.00 15.60           C  
ATOM   1938  C   ARG A 244       6.451  64.095  28.116  1.00 14.23           C  
ATOM   1939  O   ARG A 244       7.664  63.904  28.125  1.00 13.46           O  
ATOM   1940  CB  ARG A 244       5.419  66.104  27.017  1.00 15.78           C  
ATOM   1941  CG  ARG A 244       5.222  66.794  25.673  1.00 16.48           C  
ATOM   1942  CD  ARG A 244       4.837  68.253  25.847  1.00 17.85           C  
ATOM   1943  NE  ARG A 244       3.532  68.371  26.478  1.00 19.95           N  
ATOM   1944  CZ  ARG A 244       2.947  69.524  26.796  1.00 21.73           C  
ATOM   1945  NH1 ARG A 244       3.555  70.679  26.547  1.00 21.28           N  
ATOM   1946  NH2 ARG A 244       1.743  69.514  27.352  1.00 22.33           N  
ATOM   1947  N   PRO A 245       5.700  63.858  29.198  1.00 15.26           N  
ATOM   1948  CA  PRO A 245       6.398  63.347  30.385  1.00 15.04           C  
ATOM   1949  C   PRO A 245       7.033  61.962  30.168  1.00 15.42           C  
ATOM   1950  O   PRO A 245       8.019  61.614  30.818  1.00 14.49           O  
ATOM   1951  CB  PRO A 245       5.307  63.333  31.463  1.00 17.13           C  
ATOM   1952  CG  PRO A 245       4.036  63.235  30.681  1.00 16.40           C  
ATOM   1953  CD  PRO A 245       4.280  64.126  29.489  1.00 15.74           C  
ATOM   1954  N   VAL A 246       6.461  61.188  29.250  1.00 14.20           N  
ATOM   1955  CA  VAL A 246       6.973  59.855  28.934  1.00 15.70           C  
ATOM   1956  C   VAL A 246       8.292  59.999  28.164  1.00 14.18           C  
ATOM   1957  O   VAL A 246       9.260  59.279  28.422  1.00 13.60           O  
ATOM   1958  CB  VAL A 246       5.969  59.075  28.068  1.00 15.94           C  
ATOM   1959  CG1 VAL A 246       6.490  57.679  27.807  1.00 14.96           C  
ATOM   1960  CG2 VAL A 246       4.619  59.005  28.781  1.00 18.47           C  
ATOM   1961  N   LEU A 247       8.317  60.933  27.220  1.00 14.41           N  
ATOM   1962  CA  LEU A 247       9.521  61.187  26.440  1.00 14.53           C  
ATOM   1963  C   LEU A 247      10.613  61.696  27.389  1.00 15.70           C  
ATOM   1964  O   LEU A 247      11.783  61.323  27.276  1.00 14.91           O  
ATOM   1965  CB  LEU A 247       9.226  62.225  25.364  1.00 17.38           C  
ATOM   1966  CG  LEU A 247      10.319  62.605  24.378  1.00 21.92           C  
ATOM   1967  CD1 LEU A 247      10.743  61.364  23.585  1.00 24.46           C  
ATOM   1968  CD2 LEU A 247       9.771  63.682  23.427  1.00 24.55           C  
ATOM   1969  N   ILE A 248      10.230  62.558  28.325  1.00 14.38           N  
ATOM   1970  CA  ILE A 248      11.207  63.072  29.283  1.00 14.37           C  
ATOM   1971  C   ILE A 248      11.777  61.936  30.127  1.00 13.94           C  
ATOM   1972  O   ILE A 248      12.980  61.904  30.394  1.00 14.69           O  
ATOM   1973  CB  ILE A 248      10.577  64.127  30.220  1.00 15.17           C  
ATOM   1974  CG1 ILE A 248      10.232  65.385  29.420  1.00 16.64           C  
ATOM   1975  CG2 ILE A 248      11.513  64.418  31.386  1.00 18.90           C  
ATOM   1976  CD1 ILE A 248      11.386  65.995  28.682  1.00 15.79           C  
ATOM   1977  N   ALA A 249      10.928  61.006  30.557  1.00 14.10           N  
ATOM   1978  CA  ALA A 249      11.421  59.878  31.346  1.00 12.84           C  
ATOM   1979  C   ALA A 249      12.342  59.005  30.486  1.00 13.63           C  
ATOM   1980  O   ALA A 249      13.318  58.441  30.995  1.00 12.99           O  
ATOM   1981  CB  ALA A 249      10.269  59.036  31.876  1.00 13.90           C  
ATOM   1982  N   ALA A 250      12.029  58.876  29.193  1.00 13.05           N  
ATOM   1983  CA  ALA A 250      12.871  58.047  28.312  1.00 12.46           C  
ATOM   1984  C   ALA A 250      14.248  58.689  28.123  1.00 12.95           C  
ATOM   1985  O   ALA A 250      15.277  57.994  28.070  1.00 12.84           O  
ATOM   1986  CB  ALA A 250      12.174  57.828  26.937  1.00 12.79           C  
ATOM   1987  N   LEU A 251      14.279  60.015  28.015  1.00 14.13           N  
ATOM   1988  CA  LEU A 251      15.547  60.711  27.867  1.00 14.18           C  
ATOM   1989  C   LEU A 251      16.386  60.555  29.139  1.00 15.41           C  
ATOM   1990  O   LEU A 251      17.606  60.368  29.073  1.00 14.60           O  
ATOM   1991  CB  LEU A 251      15.305  62.195  27.547  1.00 14.73           C  
ATOM   1992  CG  LEU A 251      14.728  62.486  26.158  1.00 12.84           C  
ATOM   1993  CD1 LEU A 251      14.275  63.944  26.081  1.00 14.10           C  
ATOM   1994  CD2 LEU A 251      15.779  62.196  25.084  1.00 13.22           C  
ATOM   1995  N   GLN A 252      15.742  60.609  30.303  1.00 14.58           N  
ATOM   1996  CA  GLN A 252      16.481  60.441  31.555  1.00 15.56           C  
ATOM   1997  C   GLN A 252      17.041  59.018  31.656  1.00 14.94           C  
ATOM   1998  O   GLN A 252      18.161  58.809  32.120  1.00 15.00           O  
ATOM   1999  CB  GLN A 252      15.559  60.752  32.732  1.00 17.14           C  
ATOM   2000  CG  GLN A 252      15.016  62.171  32.645  1.00 21.84           C  
ATOM   2001  CD  GLN A 252      13.965  62.485  33.692  1.00 22.41           C  
ATOM   2002  OE1 GLN A 252      13.132  61.641  34.026  1.00 24.15           O  
ATOM   2003  NE2 GLN A 252      13.988  63.713  34.201  1.00 24.52           N  
ATOM   2004  N   PHE A 253      16.255  58.041  31.211  1.00 13.01           N  
ATOM   2005  CA  PHE A 253      16.671  56.645  31.213  1.00 11.83           C  
ATOM   2006  C   PHE A 253      17.954  56.544  30.380  1.00 11.81           C  
ATOM   2007  O   PHE A 253      18.915  55.868  30.774  1.00 11.64           O  
ATOM   2008  CB  PHE A 253      15.551  55.784  30.595  1.00 13.60           C  
ATOM   2009  CG  PHE A 253      15.861  54.315  30.524  1.00 12.76           C  
ATOM   2010  CD1 PHE A 253      15.369  53.436  31.492  1.00 14.35           C  
ATOM   2011  CD2 PHE A 253      16.626  53.798  29.475  1.00 13.82           C  
ATOM   2012  CE1 PHE A 253      15.628  52.061  31.413  1.00 13.27           C  
ATOM   2013  CE2 PHE A 253      16.897  52.426  29.390  1.00 10.58           C  
ATOM   2014  CZ  PHE A 253      16.395  51.554  30.358  1.00 13.04           C  
ATOM   2015  N   LEU A 254      17.966  57.236  29.244  1.00 11.86           N  
ATOM   2016  CA  LEU A 254      19.115  57.223  28.331  1.00 12.27           C  
ATOM   2017  C   LEU A 254      20.256  58.146  28.765  1.00 13.78           C  
ATOM   2018  O   LEU A 254      21.183  58.399  27.995  1.00 11.84           O  
ATOM   2019  CB  LEU A 254      18.671  57.603  26.912  1.00 13.13           C  
ATOM   2020  CG  LEU A 254      17.789  56.582  26.181  1.00 12.80           C  
ATOM   2021  CD1 LEU A 254      17.208  57.229  24.924  1.00 11.28           C  
ATOM   2022  CD2 LEU A 254      18.604  55.328  25.846  1.00 14.74           C  
ATOM   2023  N   GLY A 255      20.176  58.642  29.995  1.00 15.20           N  
ATOM   2024  CA  GLY A 255      21.214  59.516  30.526  1.00 15.46           C  
ATOM   2025  C   GLY A 255      21.377  60.862  29.846  1.00 16.87           C  
ATOM   2026  O   GLY A 255      22.446  61.485  29.941  1.00 16.49           O  
ATOM   2027  N   GLN A 256      20.322  61.322  29.177  1.00 14.75           N  
ATOM   2028  CA  GLN A 256      20.348  62.588  28.453  1.00 15.96           C  
ATOM   2029  C   GLN A 256      19.721  63.731  29.250  1.00 16.94           C  
ATOM   2030  O   GLN A 256      19.013  63.508  30.236  1.00 17.70           O  
ATOM   2031  CB  GLN A 256      19.590  62.445  27.120  1.00 14.34           C  
ATOM   2032  CG  GLN A 256      20.066  61.263  26.260  1.00 12.71           C  
ATOM   2033  CD  GLN A 256      21.542  61.365  25.897  1.00 12.39           C  
ATOM   2034  OE1 GLN A 256      22.356  60.483  26.249  1.00 15.41           O  
ATOM   2035  NE2 GLN A 256      21.902  62.438  25.210  1.00 11.05           N  
ATOM   2036  N   GLN A 257      20.009  64.951  28.819  1.00 20.37           N  
ATOM   2037  CA  GLN A 257      19.440  66.138  29.442  1.00 24.23           C  
ATOM   2038  C   GLN A 257      17.932  66.045  29.234  1.00 26.81           C  
ATOM   2039  O   GLN A 257      17.470  65.657  28.158  1.00 25.44           O  
ATOM   2040  CB  GLN A 257      19.980  67.396  28.761  1.00 27.89           C  
ATOM   2041  CG  GLN A 257      21.426  67.703  29.102  1.00 32.10           C  
ATOM   2042  CD  GLN A 257      22.154  68.412  27.973  1.00 35.68           C  
ATOM   2043  OE1 GLN A 257      22.909  67.790  27.210  1.00 36.97           O  
ATOM   2044  NE2 GLN A 257      21.923  69.716  27.850  1.00 35.19           N  
ATOM   2045  N   ALA A 258      17.162  66.387  30.261  1.00 29.25           N  
ATOM   2046  CA  ALA A 258      15.710  66.320  30.143  1.00 32.76           C  
ATOM   2047  C   ALA A 258      15.043  67.499  30.839  1.00 34.42           C  
ATOM   2048  O   ALA A 258      15.230  67.710  32.034  1.00 34.72           O  
ATOM   2049  CB  ALA A 258      15.200  65.008  30.725  1.00 33.39           C  
ATOM   2050  N   GLU A 259      14.262  68.256  30.074  1.00 35.95           N  
ATOM   2051  CA  GLU A 259      13.551  69.421  30.585  1.00 38.29           C  
ATOM   2052  C   GLU A 259      12.510  69.040  31.630  1.00 38.13           C  
ATOM   2053  O   GLU A 259      11.514  68.388  31.319  1.00 37.98           O  
ATOM   2054  CB  GLU A 259      12.861  70.152  29.430  1.00 40.75           C  
ATOM   2055  CG  GLU A 259      13.334  71.586  29.217  1.00 45.01           C  
ATOM   2056  CD  GLU A 259      12.891  72.529  30.325  1.00 46.75           C  
ATOM   2057  OE1 GLU A 259      13.280  73.715  30.279  1.00 49.08           O  
ATOM   2058  OE2 GLU A 259      12.154  72.091  31.235  1.00 48.47           O  
ATOM   2059  N   ALA A 260      12.740  69.460  32.869  1.00 38.60           N  
ATOM   2060  CA  ALA A 260      11.813  69.181  33.958  1.00 38.57           C  
ATOM   2061  C   ALA A 260      10.456  69.838  33.687  1.00 38.32           C  
ATOM   2062  O   ALA A 260       9.409  69.218  33.889  1.00 38.99           O  
ATOM   2063  CB  ALA A 260      12.391  69.692  35.275  1.00 39.65           C  
ATOM   2064  N   HIS A 261      10.485  71.091  33.233  1.00 37.47           N  
ATOM   2065  CA  HIS A 261       9.267  71.842  32.932  1.00 36.40           C  
ATOM   2066  C   HIS A 261       8.906  71.724  31.454  1.00 33.30           C  
ATOM   2067  O   HIS A 261       8.911  72.706  30.709  1.00 32.04           O  
ATOM   2068  CB  HIS A 261       9.447  73.319  33.302  1.00 41.13           C  
ATOM   2069  CG  HIS A 261       9.877  73.536  34.721  1.00 45.10           C  
ATOM   2070  ND1 HIS A 261       9.234  72.950  35.791  1.00 47.16           N  
ATOM   2071  CD2 HIS A 261      10.880  74.280  35.246  1.00 47.01           C  
ATOM   2072  CE1 HIS A 261       9.823  73.323  36.913  1.00 47.62           C  
ATOM   2073  NE2 HIS A 261      10.825  74.130  36.611  1.00 47.84           N  
ATOM   2074  N   TRP A 262       8.574  70.507  31.046  1.00 29.12           N  
ATOM   2075  CA  TRP A 262       8.220  70.222  29.664  1.00 25.92           C  
ATOM   2076  C   TRP A 262       6.908  70.840  29.186  1.00 23.89           C  
ATOM   2077  O   TRP A 262       6.612  70.805  27.999  1.00 22.06           O  
ATOM   2078  CB  TRP A 262       8.156  68.707  29.457  1.00 24.14           C  
ATOM   2079  CG  TRP A 262       7.345  67.998  30.505  1.00 22.57           C  
ATOM   2080  CD1 TRP A 262       7.818  67.357  31.615  1.00 23.81           C  
ATOM   2081  CD2 TRP A 262       5.917  67.879  30.552  1.00 23.21           C  
ATOM   2082  NE1 TRP A 262       6.774  66.844  32.351  1.00 22.96           N  
ATOM   2083  CE2 TRP A 262       5.596  67.152  31.723  1.00 23.50           C  
ATOM   2084  CE3 TRP A 262       4.877  68.319  29.723  1.00 22.57           C  
ATOM   2085  CZ2 TRP A 262       4.274  66.851  32.083  1.00 24.02           C  
ATOM   2086  CZ3 TRP A 262       3.566  68.021  30.080  1.00 22.90           C  
ATOM   2087  CH2 TRP A 262       3.278  67.294  31.252  1.00 23.36           C  
ATOM   2088  N   GLN A 263       6.130  71.409  30.101  1.00 23.62           N  
ATOM   2089  CA  GLN A 263       4.840  71.993  29.737  1.00 23.80           C  
ATOM   2090  C   GLN A 263       4.915  73.134  28.737  1.00 22.30           C  
ATOM   2091  O   GLN A 263       3.950  73.403  28.033  1.00 21.68           O  
ATOM   2092  CB  GLN A 263       4.091  72.473  30.990  1.00 24.00           C  
ATOM   2093  CG  GLN A 263       3.656  71.352  31.919  1.00 26.30           C  
ATOM   2094  CD  GLN A 263       4.753  70.900  32.874  1.00 26.87           C  
ATOM   2095  OE1 GLN A 263       5.894  71.366  32.807  1.00 26.96           O  
ATOM   2096  NE2 GLN A 263       4.405  69.986  33.775  1.00 28.82           N  
ATOM   2097  N   ASP A 264       6.057  73.804  28.671  1.00 23.58           N  
ATOM   2098  CA  ASP A 264       6.203  74.926  27.757  1.00 23.50           C  
ATOM   2099  C   ASP A 264       6.884  74.536  26.458  1.00 22.63           C  
ATOM   2100  O   ASP A 264       7.369  75.389  25.720  1.00 21.26           O  
ATOM   2101  CB  ASP A 264       6.974  76.047  28.441  1.00 26.74           C  
ATOM   2102  CG  ASP A 264       6.282  76.524  29.698  1.00 30.02           C  
ATOM   2103  OD1 ASP A 264       5.145  77.035  29.582  1.00 30.65           O  
ATOM   2104  OD2 ASP A 264       6.865  76.371  30.797  1.00 33.32           O  
ATOM   2105  N   PHE A 265       6.916  73.241  26.171  1.00 22.00           N  
ATOM   2106  CA  PHE A 265       7.539  72.786  24.940  1.00 21.03           C  
ATOM   2107  C   PHE A 265       6.670  71.748  24.254  1.00 19.77           C  
ATOM   2108  O   PHE A 265       5.912  71.040  24.908  1.00 19.24           O  
ATOM   2109  CB  PHE A 265       8.906  72.178  25.231  1.00 22.47           C  
ATOM   2110  CG  PHE A 265       9.860  73.130  25.876  1.00 25.16           C  
ATOM   2111  CD1 PHE A 265       9.947  73.216  27.260  1.00 27.23           C  
ATOM   2112  CD2 PHE A 265      10.643  73.976  25.095  1.00 26.51           C  
ATOM   2113  CE1 PHE A 265      10.803  74.137  27.867  1.00 29.00           C  
ATOM   2114  CE2 PHE A 265      11.504  74.905  25.687  1.00 28.28           C  
ATOM   2115  CZ  PHE A 265      11.583  74.985  27.075  1.00 29.34           C  
ATOM   2116  N   SER A 266       6.775  71.669  22.935  1.00 17.50           N  
ATOM   2117  CA  SER A 266       6.010  70.678  22.188  1.00 17.75           C  
ATOM   2118  C   SER A 266       6.869  69.428  22.093  1.00 18.93           C  
ATOM   2119  O   SER A 266       8.080  69.473  22.329  1.00 17.47           O  
ATOM   2120  CB  SER A 266       5.714  71.164  20.773  1.00 16.74           C  
ATOM   2121  OG  SER A 266       6.912  71.402  20.050  1.00 17.06           O  
ATOM   2122  N   VAL A 267       6.239  68.314  21.742  1.00 18.21           N  
ATOM   2123  CA  VAL A 267       6.970  67.065  21.581  1.00 19.90           C  
ATOM   2124  C   VAL A 267       8.103  67.251  20.576  1.00 19.98           C  
ATOM   2125  O   VAL A 267       9.234  66.824  20.814  1.00 20.73           O  
ATOM   2126  CB  VAL A 267       6.040  65.947  21.076  1.00 20.85           C  
ATOM   2127  CG1 VAL A 267       6.866  64.774  20.545  1.00 22.76           C  
ATOM   2128  CG2 VAL A 267       5.140  65.486  22.203  1.00 21.21           C  
ATOM   2129  N   GLU A 268       7.802  67.880  19.445  1.00 19.27           N  
ATOM   2130  CA  GLU A 268       8.820  68.089  18.421  1.00 20.25           C  
ATOM   2131  C   GLU A 268       9.988  68.940  18.927  1.00 18.55           C  
ATOM   2132  O   GLU A 268      11.135  68.686  18.575  1.00 17.64           O  
ATOM   2133  CB  GLU A 268       8.199  68.713  17.166  1.00 23.15           C  
ATOM   2134  CG  GLU A 268       7.623  70.102  17.362  1.00 29.78           C  
ATOM   2135  CD  GLU A 268       6.696  70.517  16.230  1.00 33.66           C  
ATOM   2136  OE1 GLU A 268       7.138  70.551  15.054  1.00 36.59           O  
ATOM   2137  OE2 GLU A 268       5.521  70.811  16.522  1.00 36.65           O  
ATOM   2138  N   GLN A 269       9.704  69.938  19.762  1.00 18.41           N  
ATOM   2139  CA  GLN A 269      10.771  70.781  20.300  1.00 17.58           C  
ATOM   2140  C   GLN A 269      11.659  69.982  21.250  1.00 16.63           C  
ATOM   2141  O   GLN A 269      12.882  70.130  21.242  1.00 15.68           O  
ATOM   2142  CB  GLN A 269      10.189  71.989  21.043  1.00 18.06           C  
ATOM   2143  CG  GLN A 269       9.653  73.078  20.120  1.00 20.49           C  
ATOM   2144  CD  GLN A 269       9.028  74.230  20.891  1.00 21.89           C  
ATOM   2145  OE1 GLN A 269       8.233  74.016  21.810  1.00 19.40           O  
ATOM   2146  NE2 GLN A 269       9.375  75.456  20.513  1.00 21.64           N  
ATOM   2147  N   ILE A 270      11.040  69.132  22.062  1.00 15.32           N  
ATOM   2148  CA  ILE A 270      11.786  68.324  23.015  1.00 16.18           C  
ATOM   2149  C   ILE A 270      12.714  67.393  22.249  1.00 16.10           C  
ATOM   2150  O   ILE A 270      13.877  67.211  22.623  1.00 14.92           O  
ATOM   2151  CB  ILE A 270      10.821  67.523  23.922  1.00 16.94           C  
ATOM   2152  CG1 ILE A 270      10.109  68.493  24.871  1.00 18.81           C  
ATOM   2153  CG2 ILE A 270      11.585  66.467  24.719  1.00 16.74           C  
ATOM   2154  CD1 ILE A 270       8.934  67.889  25.648  1.00 20.93           C  
ATOM   2155  N   LEU A 271      12.208  66.822  21.161  1.00 16.54           N  
ATOM   2156  CA  LEU A 271      13.026  65.929  20.339  1.00 17.18           C  
ATOM   2157  C   LEU A 271      14.139  66.656  19.586  1.00 18.22           C  
ATOM   2158  O   LEU A 271      15.254  66.141  19.480  1.00 17.36           O  
ATOM   2159  CB  LEU A 271      12.148  65.173  19.341  1.00 17.80           C  
ATOM   2160  CG  LEU A 271      11.380  64.002  19.928  1.00 20.96           C  
ATOM   2161  CD1 LEU A 271      10.436  63.442  18.855  1.00 22.79           C  
ATOM   2162  CD2 LEU A 271      12.367  62.923  20.387  1.00 21.15           C  
ATOM   2163  N   GLN A 272      13.842  67.837  19.049  1.00 17.85           N  
ATOM   2164  CA  GLN A 272      14.857  68.598  18.335  1.00 19.23           C  
ATOM   2165  C   GLN A 272      16.016  68.879  19.285  1.00 19.43           C  
ATOM   2166  O   GLN A 272      17.185  68.750  18.917  1.00 18.89           O  
ATOM   2167  CB  GLN A 272      14.300  69.931  17.837  1.00 23.75           C  
ATOM   2168  CG  GLN A 272      13.196  69.836  16.824  1.00 29.73           C  
ATOM   2169  CD  GLN A 272      12.768  71.209  16.327  1.00 32.42           C  
ATOM   2170  OE1 GLN A 272      12.584  72.145  17.117  1.00 34.51           O  
ATOM   2171  NE2 GLN A 272      12.603  71.334  15.015  1.00 35.19           N  
ATOM   2172  N   SER A 273      15.689  69.292  20.506  1.00 19.54           N  
ATOM   2173  CA  SER A 273      16.715  69.564  21.495  1.00 18.54           C  
ATOM   2174  C   SER A 273      17.471  68.286  21.847  1.00 17.71           C  
ATOM   2175  O   SER A 273      18.692  68.316  21.994  1.00 17.87           O  
ATOM   2176  CB  SER A 273      16.102  70.175  22.762  1.00 21.63           C  
ATOM   2177  OG  SER A 273      15.648  71.496  22.496  1.00 25.80           O  
ATOM   2178  N   ALA A 274      16.754  67.168  21.969  1.00 13.74           N  
ATOM   2179  CA  ALA A 274      17.407  65.899  22.300  1.00 14.34           C  
ATOM   2180  C   ALA A 274      18.422  65.512  21.218  1.00 14.17           C  
ATOM   2181  O   ALA A 274      19.498  65.006  21.536  1.00 15.65           O  
ATOM   2182  CB  ALA A 274      16.373  64.783  22.485  1.00 12.40           C  
ATOM   2183  N   VAL A 275      18.085  65.743  19.952  1.00 14.47           N  
ATOM   2184  CA  VAL A 275      19.032  65.445  18.870  1.00 14.58           C  
ATOM   2185  C   VAL A 275      20.274  66.342  19.013  1.00 16.48           C  
ATOM   2186  O   VAL A 275      21.419  65.874  18.976  1.00 15.33           O  
ATOM   2187  CB  VAL A 275      18.400  65.681  17.484  1.00 14.91           C  
ATOM   2188  CG1 VAL A 275      19.467  65.568  16.397  1.00 15.74           C  
ATOM   2189  CG2 VAL A 275      17.262  64.682  17.243  1.00 14.11           C  
ATOM   2190  N   LYS A 276      20.051  67.641  19.183  1.00 19.00           N  
ATOM   2191  CA  LYS A 276      21.176  68.561  19.329  1.00 20.32           C  
ATOM   2192  C   LYS A 276      22.050  68.213  20.533  1.00 19.41           C  
ATOM   2193  O   LYS A 276      23.275  68.295  20.458  1.00 19.05           O  
ATOM   2194  CB  LYS A 276      20.676  70.005  19.471  1.00 22.96           C  
ATOM   2195  CG  LYS A 276      20.133  70.613  18.193  1.00 28.95           C  
ATOM   2196  CD  LYS A 276      19.662  72.044  18.427  1.00 32.85           C  
ATOM   2197  CE  LYS A 276      19.058  72.651  17.165  1.00 36.74           C  
ATOM   2198  NZ  LYS A 276      20.037  72.698  16.036  1.00 38.00           N  
ATOM   2199  N   ASN A 277      21.421  67.807  21.633  1.00 18.26           N  
ATOM   2200  CA  ASN A 277      22.145  67.480  22.856  1.00 17.95           C  
ATOM   2201  C   ASN A 277      22.505  66.011  23.066  1.00 17.12           C  
ATOM   2202  O   ASN A 277      22.960  65.626  24.151  1.00 17.84           O  
ATOM   2203  CB  ASN A 277      21.355  67.977  24.066  1.00 20.48           C  
ATOM   2204  CG  ASN A 277      21.243  69.486  24.096  1.00 23.40           C  
ATOM   2205  OD1 ASN A 277      22.248  70.178  24.000  1.00 26.21           O  
ATOM   2206  ND2 ASN A 277      20.026  70.001  24.230  1.00 25.37           N  
ATOM   2207  N   TRP A 278      22.325  65.194  22.033  1.00 16.24           N  
ATOM   2208  CA  TRP A 278      22.621  63.769  22.146  1.00 14.95           C  
ATOM   2209  C   TRP A 278      24.088  63.502  22.448  1.00 17.32           C  
ATOM   2210  O   TRP A 278      24.979  63.986  21.742  1.00 17.59           O  
ATOM   2211  CB  TRP A 278      22.223  63.042  20.849  1.00 14.28           C  
ATOM   2212  CG  TRP A 278      22.512  61.559  20.840  1.00 13.55           C  
ATOM   2213  CD1 TRP A 278      23.477  60.908  20.102  1.00 14.56           C  
ATOM   2214  CD2 TRP A 278      21.849  60.546  21.608  1.00 13.42           C  
ATOM   2215  NE1 TRP A 278      23.447  59.549  20.368  1.00 12.11           N  
ATOM   2216  CE2 TRP A 278      22.459  59.300  21.285  1.00 14.15           C  
ATOM   2217  CE3 TRP A 278      20.794  60.564  22.534  1.00 13.43           C  
ATOM   2218  CZ2 TRP A 278      22.045  58.083  21.864  1.00 11.06           C  
ATOM   2219  CZ3 TRP A 278      20.387  59.366  23.105  1.00 12.34           C  
ATOM   2220  CH2 TRP A 278      21.012  58.137  22.766  1.00 14.83           C  
ATOM   2221  N   ARG A 279      24.325  62.736  23.505  1.00 16.50           N  
ATOM   2222  CA  ARG A 279      25.675  62.346  23.892  1.00 17.41           C  
ATOM   2223  C   ARG A 279      25.640  60.841  24.096  1.00 15.14           C  
ATOM   2224  O   ARG A 279      25.174  60.362  25.120  1.00 12.15           O  
ATOM   2225  CB  ARG A 279      26.100  63.009  25.204  1.00 19.86           C  
ATOM   2226  CG  ARG A 279      26.368  64.509  25.128  1.00 27.63           C  
ATOM   2227  CD  ARG A 279      27.562  64.869  26.028  1.00 32.51           C  
ATOM   2228  NE  ARG A 279      27.497  64.184  27.321  1.00 36.74           N  
ATOM   2229  CZ  ARG A 279      28.515  63.522  27.870  1.00 38.10           C  
ATOM   2230  NH1 ARG A 279      29.680  63.454  27.244  1.00 41.02           N  
ATOM   2231  NH2 ARG A 279      28.366  62.915  29.039  1.00 39.78           N  
ATOM   2232  N   LEU A 280      26.124  60.090  23.116  1.00 14.35           N  
ATOM   2233  CA  LEU A 280      26.125  58.640  23.237  1.00 13.86           C  
ATOM   2234  C   LEU A 280      26.895  58.156  24.464  1.00 14.93           C  
ATOM   2235  O   LEU A 280      26.484  57.211  25.152  1.00 14.31           O  
ATOM   2236  CB  LEU A 280      26.731  58.030  21.977  1.00 14.25           C  
ATOM   2237  CG  LEU A 280      26.917  56.514  21.962  1.00 16.92           C  
ATOM   2238  CD1 LEU A 280      25.570  55.803  22.089  1.00 16.86           C  
ATOM   2239  CD2 LEU A 280      27.611  56.128  20.658  1.00 15.06           C  
ATOM   2240  N   THR A 281      28.022  58.796  24.760  1.00 16.45           N  
ATOM   2241  CA  THR A 281      28.805  58.335  25.905  1.00 17.43           C  
ATOM   2242  C   THR A 281      28.084  58.464  27.248  1.00 17.60           C  
ATOM   2243  O   THR A 281      28.449  57.790  28.214  1.00 18.52           O  
ATOM   2244  CB  THR A 281      30.179  59.039  25.963  1.00 19.98           C  
ATOM   2245  OG1 THR A 281      29.999  60.451  26.095  1.00 21.96           O  
ATOM   2246  CG2 THR A 281      30.960  58.749  24.686  1.00 20.03           C  
ATOM   2247  N   ALA A 282      27.049  59.300  27.305  1.00 15.76           N  
ATOM   2248  CA  ALA A 282      26.278  59.470  28.538  1.00 15.39           C  
ATOM   2249  C   ALA A 282      25.222  58.375  28.719  1.00 15.73           C  
ATOM   2250  O   ALA A 282      24.594  58.284  29.772  1.00 13.69           O  
ATOM   2251  CB  ALA A 282      25.603  60.856  28.559  1.00 17.66           C  
ATOM   2252  N   VAL A 283      25.007  57.553  27.693  1.00 13.11           N  
ATOM   2253  CA  VAL A 283      24.026  56.468  27.803  1.00 12.69           C  
ATOM   2254  C   VAL A 283      24.601  55.390  28.721  1.00 12.38           C  
ATOM   2255  O   VAL A 283      25.689  54.857  28.474  1.00 12.89           O  
ATOM   2256  CB  VAL A 283      23.708  55.852  26.416  1.00 12.08           C  
ATOM   2257  CG1 VAL A 283      22.735  54.685  26.561  1.00 12.65           C  
ATOM   2258  CG2 VAL A 283      23.135  56.933  25.500  1.00 12.61           C  
ATOM   2259  N   PRO A 284      23.878  55.048  29.796  1.00 12.43           N  
ATOM   2260  CA  PRO A 284      24.349  54.029  30.746  1.00 14.30           C  
ATOM   2261  C   PRO A 284      24.155  52.592  30.284  1.00 15.17           C  
ATOM   2262  O   PRO A 284      23.463  52.341  29.299  1.00 13.53           O  
ATOM   2263  CB  PRO A 284      23.531  54.332  31.999  1.00 14.50           C  
ATOM   2264  CG  PRO A 284      22.206  54.724  31.409  1.00 15.36           C  
ATOM   2265  CD  PRO A 284      22.604  55.639  30.246  1.00 12.99           C  
ATOM   2266  N   GLU A 285      24.771  51.648  31.004  1.00 14.83           N  
ATOM   2267  CA  GLU A 285      24.643  50.227  30.684  1.00 15.93           C  
ATOM   2268  C   GLU A 285      23.371  49.627  31.301  1.00 14.65           C  
ATOM   2269  O   GLU A 285      22.935  48.544  30.918  1.00 14.13           O  
ATOM   2270  CB  GLU A 285      25.867  49.458  31.180  1.00 18.06           C  
ATOM   2271  CG  GLU A 285      27.133  49.718  30.359  1.00 23.24           C  
ATOM   2272  CD  GLU A 285      28.380  49.184  31.043  1.00 28.27           C  
ATOM   2273  OE1 GLU A 285      28.894  49.864  31.958  1.00 32.61           O  
ATOM   2274  OE2 GLU A 285      28.837  48.082  30.681  1.00 32.04           O  
ATOM   2275  N   SER A 286      22.799  50.326  32.277  1.00 13.62           N  
ATOM   2276  CA  SER A 286      21.551  49.888  32.902  1.00 12.77           C  
ATOM   2277  C   SER A 286      20.856  51.114  33.482  1.00 11.58           C  
ATOM   2278  O   SER A 286      21.498  52.138  33.756  1.00 12.30           O  
ATOM   2279  CB  SER A 286      21.809  48.853  34.010  1.00 14.78           C  
ATOM   2280  OG  SER A 286      22.533  49.422  35.094  1.00 14.81           O  
ATOM   2281  N   ALA A 287      19.540  51.026  33.656  1.00 12.50           N  
ATOM   2282  CA  ALA A 287      18.791  52.138  34.218  1.00 11.63           C  
ATOM   2283  C   ALA A 287      17.523  51.606  34.843  1.00 14.62           C  
ATOM   2284  O   ALA A 287      16.979  50.582  34.411  1.00 13.78           O  
ATOM   2285  CB  ALA A 287      18.469  53.185  33.151  1.00 13.63           C  
ATOM   2286  N   ILE A 288      17.068  52.305  35.874  1.00 14.96           N  
ATOM   2287  CA  ILE A 288      15.868  51.907  36.609  1.00 16.14           C  
ATOM   2288  C   ILE A 288      14.677  52.727  36.154  1.00 17.35           C  
ATOM   2289  O   ILE A 288      14.723  53.947  36.193  1.00 18.58           O  
ATOM   2290  CB  ILE A 288      16.095  52.129  38.116  1.00 17.58           C  
ATOM   2291  CG1 ILE A 288      17.198  51.185  38.600  1.00 18.28           C  
ATOM   2292  CG2 ILE A 288      14.787  51.920  38.886  1.00 18.07           C  
ATOM   2293  CD1 ILE A 288      17.952  51.681  39.825  1.00 19.19           C  
ATOM   2294  N   VAL A 289      13.608  52.061  35.725  1.00 17.62           N  
ATOM   2295  CA  VAL A 289      12.422  52.772  35.270  1.00 21.66           C  
ATOM   2296  C   VAL A 289      11.534  53.137  36.461  1.00 23.77           C  
ATOM   2297  O   VAL A 289      11.549  52.444  37.479  1.00 25.24           O  
ATOM   2298  CB  VAL A 289      11.615  51.910  34.283  1.00 19.57           C  
ATOM   2299  CG1 VAL A 289      12.534  51.387  33.190  1.00 20.35           C  
ATOM   2300  CG2 VAL A 289      10.947  50.753  35.015  1.00 23.17           C  
ATOM   2301  N   ASN A 290      10.772  54.220  36.356  1.00 26.06           N  
ATOM   2302  CA  ASN A 290       9.903  54.572  37.475  1.00 29.59           C  
ATOM   2303  C   ASN A 290       8.662  53.676  37.502  1.00 29.86           C  
ATOM   2304  O   ASN A 290       8.284  53.080  36.489  1.00 28.60           O  
ATOM   2305  CB  ASN A 290       9.518  56.056  37.442  1.00 32.98           C  
ATOM   2306  CG  ASN A 290       8.938  56.486  36.124  1.00 36.39           C  
ATOM   2307  OD1 ASN A 290       7.989  55.884  35.625  1.00 41.17           O  
ATOM   2308  ND2 ASN A 290       9.496  57.552  35.553  1.00 38.71           N  
ATOM   2309  N   SER A 291       8.047  53.575  38.678  1.00 31.07           N  
ATOM   2310  CA  SER A 291       6.874  52.731  38.901  1.00 32.43           C  
ATOM   2311  C   SER A 291       5.774  52.810  37.850  1.00 33.65           C  
ATOM   2312  O   SER A 291       5.080  51.826  37.611  1.00 34.24           O  
ATOM   2313  CB  SER A 291       6.268  53.042  40.271  1.00 32.64           C  
ATOM   2314  OG  SER A 291       5.883  54.403  40.341  1.00 33.94           O  
ATOM   2315  N   THR A 292       5.611  53.971  37.229  1.00 34.68           N  
ATOM   2316  CA  THR A 292       4.570  54.145  36.221  1.00 37.44           C  
ATOM   2317  C   THR A 292       4.731  53.213  35.021  1.00 38.39           C  
ATOM   2318  O   THR A 292       3.757  52.916  34.322  1.00 37.23           O  
ATOM   2319  CB  THR A 292       4.524  55.605  35.733  1.00 38.78           C  
ATOM   2320  OG1 THR A 292       4.197  56.455  36.841  1.00 39.86           O  
ATOM   2321  CG2 THR A 292       3.473  55.779  34.639  1.00 40.30           C  
ATOM   2322  N   PHE A 293       5.956  52.741  34.793  1.00 38.41           N  
ATOM   2323  CA  PHE A 293       6.230  51.844  33.674  1.00 39.79           C  
ATOM   2324  C   PHE A 293       6.526  50.418  34.129  1.00 41.95           C  
ATOM   2325  O   PHE A 293       7.178  49.652  33.421  1.00 41.75           O  
ATOM   2326  CB  PHE A 293       7.410  52.373  32.857  1.00 38.14           C  
ATOM   2327  CG  PHE A 293       7.267  53.808  32.455  1.00 36.52           C  
ATOM   2328  CD1 PHE A 293       8.082  54.785  33.018  1.00 36.01           C  
ATOM   2329  CD2 PHE A 293       6.295  54.194  31.539  1.00 36.02           C  
ATOM   2330  CE1 PHE A 293       7.928  56.128  32.676  1.00 35.14           C  
ATOM   2331  CE2 PHE A 293       6.134  55.532  31.191  1.00 35.47           C  
ATOM   2332  CZ  PHE A 293       6.953  56.501  31.762  1.00 36.35           C  
ATOM   2333  N   SER A 294       6.038  50.055  35.308  1.00 44.70           N  
ATOM   2334  CA  SER A 294       6.272  48.718  35.836  1.00 47.56           C  
ATOM   2335  C   SER A 294       5.090  48.266  36.686  1.00 49.53           C  
ATOM   2336  O   SER A 294       4.420  49.085  37.317  1.00 50.67           O  
ATOM   2337  CB  SER A 294       7.557  48.712  36.672  1.00 47.44           C  
ATOM   2338  OG  SER A 294       7.790  47.442  37.254  1.00 48.51           O  
ATOM   2339  N   ASN A 295       4.840  46.961  36.699  1.00 51.70           N  
ATOM   2340  CA  ASN A 295       3.739  46.399  37.473  1.00 53.17           C  
ATOM   2341  C   ASN A 295       4.229  45.468  38.577  1.00 53.25           C  
ATOM   2342  O   ASN A 295       3.770  45.546  39.717  1.00 52.93           O  
ATOM   2343  CB  ASN A 295       2.762  45.660  36.557  1.00 55.41           C  
ATOM   2344  CG  ASN A 295       2.333  46.496  35.367  1.00 57.84           C  
ATOM   2345  OD1 ASN A 295       1.731  47.558  35.524  1.00 59.54           O  
ATOM   2346  ND2 ASN A 295       2.643  46.020  34.167  1.00 59.11           N  
ATOM   2347  N   ALA A 296       5.163  44.588  38.231  1.00 52.90           N  
ATOM   2348  CA  ALA A 296       5.716  43.640  39.192  1.00 54.55           C  
ATOM   2349  C   ALA A 296       6.741  44.310  40.100  1.00 55.84           C  
ATOM   2350  O   ALA A 296       6.765  45.535  40.229  1.00 58.62           O  
ATOM   2351  CB  ALA A 296       6.339  42.456  38.469  1.00 52.37           C  
ATOM   2352  N   SER A 297       7.586  43.500  40.729  1.00 60.01           N  
ATOM   2353  CA  SER A 297       8.614  44.013  41.628  1.00 60.34           C  
ATOM   2354  C   SER A 297       9.995  43.500  41.235  1.00 60.61           C  
ATOM   2355  O   SER A 297      10.842  44.264  40.772  1.00 61.69           O  
ATOM   2356  CB  SER A 297       8.304  43.626  43.075  1.00 59.46           C  
ATOM   2357  OG  SER A 297       8.339  42.219  43.246  1.00 63.76           O  
ATOM   2358  N   CYS A 298      10.216  42.204  41.424  1.00 59.22           N  
ATOM   2359  CA  CYS A 298      11.494  41.587  41.090  1.00 60.31           C  
ATOM   2360  C   CYS A 298      12.485  41.716  42.242  1.00 59.52           C  
ATOM   2361  O   CYS A 298      13.698  41.666  42.038  1.00 61.12           O  
ATOM   2362  CB  CYS A 298      12.077  42.214  39.822  1.00 59.65           C  
ATOM   2363  SG  CYS A 298      11.103  41.922  38.329  1.00 67.14           S  
TER    2364      CYS A 298                                                      
HETATM 2365 ZN    ZN A 300      19.809  17.236  13.053  1.00 18.08          ZN  
HETATM 2366  N   GLU A 301      11.659  42.560  16.146  1.00 20.73           N  
HETATM 2367  CA  GLU A 301      12.896  42.335  16.935  1.00 23.27           C  
HETATM 2368  C   GLU A 301      12.697  42.831  18.366  1.00 25.32           C  
HETATM 2369  O   GLU A 301      12.099  43.914  18.541  1.00 25.61           O  
HETATM 2370  CB  GLU A 301      14.070  43.048  16.233  1.00 23.87           C  
HETATM 2371  CG  GLU A 301      15.079  43.670  17.150  1.00 20.05           C  
HETATM 2372  CD  GLU A 301      16.295  44.260  16.426  1.00 18.94           C  
HETATM 2373  OE1 GLU A 301      17.126  43.489  15.898  1.00 14.24           O  
HETATM 2374  OE2 GLU A 301      16.422  45.506  16.403  1.00 13.91           O  
HETATM 2375  OXT GLU A 301      13.110  42.118  19.310  1.00 27.65           O  
HETATM 2376  O   HOH A 302      13.290  57.361  33.598  1.00 15.74           O  
HETATM 2377  O   HOH A 303      14.618  47.491  16.844  1.00 10.79           O  
HETATM 2378  O   HOH A 304       7.802  48.523   1.781  1.00 21.24           O  
HETATM 2379  O   HOH A 305      28.416  33.229  16.339  1.00 13.33           O  
HETATM 2380  O   HOH A 306      19.891  51.530  14.255  1.00  9.50           O  
HETATM 2381  O   HOH A 307      30.583  45.760  14.055  1.00 18.63           O  
HETATM 2382  O   HOH A 308       4.939  53.186   4.631  1.00 24.69           O  
HETATM 2383  O   HOH A 309      30.156  47.837  16.346  1.00 12.99           O  
HETATM 2384  O   HOH A 310      19.960  33.422  18.731  1.00 15.30           O  
HETATM 2385  O   HOH A 311      -2.519  47.439  19.316  1.00 12.66           O  
HETATM 2386  O   HOH A 312      16.154  49.745  16.969  1.00 14.68           O  
HETATM 2387  O   HOH A 313      17.360  38.047  -0.504  1.00 19.66           O  
HETATM 2388  O   HOH A 314      11.303  53.504   6.934  1.00 16.48           O  
HETATM 2389  O   HOH A 315      19.834  56.564  33.400  1.00 15.14           O  
HETATM 2390  O   HOH A 316      -7.762  44.111  16.096  1.00 15.96           O  
HETATM 2391  O   HOH A 317      22.774  42.019  13.166  1.00 13.42           O  
HETATM 2392  O   HOH A 318      21.199  42.676  10.956  1.00 10.94           O  
HETATM 2393  O   HOH A 319      26.672  60.053  18.338  1.00 19.09           O  
HETATM 2394  O   HOH A 320      21.390  16.884   6.370  1.00 20.19           O  
HETATM 2395  O   HOH A 321       5.995  37.632   1.495  1.00 17.36           O  
HETATM 2396  O   HOH A 322      12.643  23.995  14.103  1.00 22.55           O  
HETATM 2397  O   HOH A 323      34.545  51.458  18.822  1.00 17.02           O  
HETATM 2398  O   HOH A 324      19.060  27.185  16.884  1.00 29.49           O  
HETATM 2399  O   HOH A 325      -3.411  48.540  21.686  1.00 15.99           O  
HETATM 2400  O   HOH A 326      17.192  40.975   0.105  1.00 15.79           O  
HETATM 2401  O   HOH A 327      20.279  54.328  14.716  1.00 10.76           O  
HETATM 2402  O   HOH A 328      30.700  48.582  10.478  1.00 17.02           O  
HETATM 2403  O   HOH A 329      24.343  33.705  20.574  1.00 17.06           O  
HETATM 2404  O   HOH A 330       3.300  68.386  21.969  1.00 23.71           O  
HETATM 2405  O   HOH A 331      23.562  45.613   7.311  1.00 14.10           O  
HETATM 2406  O   HOH A 332      -0.251  43.680  13.655  1.00 17.05           O  
HETATM 2407  O   HOH A 333      21.188  54.535  35.034  1.00 16.26           O  
HETATM 2408  O   HOH A 334      19.581  41.158   1.614  1.00 20.44           O  
HETATM 2409  O   HOH A 335      20.818  38.871  25.126  1.00 29.21           O  
HETATM 2410  O   HOH A 336      25.412  45.051   5.283  1.00 20.74           O  
HETATM 2411  O   HOH A 337      14.881  44.336  31.031  1.00 27.11           O  
HETATM 2412  O   HOH A 338      22.312  65.117  26.866  1.00 20.87           O  
HETATM 2413  O   HOH A 339      33.549  50.448  21.296  1.00 17.07           O  
HETATM 2414  O   HOH A 340      14.525  15.325  26.088  1.00 32.56           O  
HETATM 2415  O   HOH A 341      18.285  31.116  15.009  1.00 17.56           O  
HETATM 2416  O   HOH A 342       6.132  59.307  10.297  1.00 32.24           O  
HETATM 2417  O   HOH A 343       4.680  38.515  13.591  1.00 33.80           O  
HETATM 2418  O   HOH A 344      27.269  53.978  10.391  1.00 20.29           O  
HETATM 2419  O   HOH A 345      19.600  64.004  24.208  1.00 16.64           O  
HETATM 2420  O   HOH A 346       5.182  68.351  18.269  1.00 20.68           O  
HETATM 2421  O   HOH A 347      16.558  33.401  15.270  1.00 11.27           O  
HETATM 2422  O   HOH A 348      15.004  67.711  25.108  1.00 23.45           O  
HETATM 2423  O   HOH A 349      30.638  30.748  10.940  1.00 17.72           O  
HETATM 2424  O   HOH A 350      19.351  26.996   2.986  1.00 16.40           O  
HETATM 2425  O   HOH A 351       9.582  24.412  14.189  1.00 32.67           O  
HETATM 2426  O   HOH A 352       8.390  62.320  33.233  1.00 21.61           O  
HETATM 2427  O   HOH A 353      28.602  57.958  17.313  1.00 23.35           O  
HETATM 2428  O   HOH A 354      16.371  46.180  28.604  1.00 22.86           O  
HETATM 2429  O   HOH A 355      24.052  20.505  24.121  1.00 23.67           O  
HETATM 2430  O   HOH A 356      12.345  39.140  12.519  1.00 21.90           O  
HETATM 2431  O   HOH A 357      -1.723  36.472  18.755  1.00 26.66           O  
HETATM 2432  O   HOH A 358       8.168  33.354   8.558  1.00 17.15           O  
HETATM 2433  O   HOH A 359      28.354  24.746  20.784  1.00 23.94           O  
HETATM 2434  O   HOH A 360      24.085  51.901   3.379  1.00 20.60           O  
HETATM 2435  O   HOH A 361      11.470  66.984  16.255  1.00 17.67           O  
HETATM 2436  O   HOH A 362      19.221  24.768  17.879  1.00 34.73           O  
HETATM 2437  O   HOH A 363      15.733  42.903  43.053  1.00 31.96           O  
HETATM 2438  O   HOH A 364       7.317  45.849   2.637  1.00 16.49           O  
HETATM 2439  O   HOH A 365      28.319  53.750  13.108  1.00 19.27           O  
HETATM 2440  O   HOH A 366      18.738  54.636  36.691  1.00 21.25           O  
HETATM 2441  O   HOH A 367      19.290  32.784  -4.381  1.00 26.73           O  
HETATM 2442  O   HOH A 368      25.889  22.743  16.283  1.00 18.97           O  
HETATM 2443  O   HOH A 369      10.794  63.061  13.789  1.00 21.19           O  
HETATM 2444  O   HOH A 370       1.283  67.011  24.302  1.00 38.47           O  
HETATM 2445  O   HOH A 371      31.510  40.720  27.869  1.00 25.31           O  
HETATM 2446  O   HOH A 372      18.157  65.803  25.670  1.00 27.38           O  
HETATM 2447  O   HOH A 373      -3.079  36.674  15.014  1.00 29.14           O  
HETATM 2448  O   HOH A 374      34.962  36.514  17.627  1.00 19.83           O  
HETATM 2449  O   HOH A 375      27.269  61.311  20.797  1.00 18.93           O  
HETATM 2450  O   HOH A 376      -0.326  59.333  15.652  1.00 26.61           O  
HETATM 2451  O   HOH A 377      13.953  65.664  16.107  1.00 17.91           O  
HETATM 2452  O   HOH A 378       8.735  43.994   0.721  1.00 23.45           O  
HETATM 2453  O   HOH A 379      31.895  39.956   5.885  1.00 26.98           O  
HETATM 2454  O   HOH A 380      17.489  48.291  26.341  1.00 17.13           O  
HETATM 2455  O   HOH A 381      -2.616  46.962  25.119  1.00 22.20           O  
HETATM 2456  O   HOH A 382       8.238  58.412   5.642  1.00 29.44           O  
HETATM 2457  O   HOH A 383      25.413  66.713  21.857  1.00 28.31           O  
HETATM 2458  O   HOH A 384      19.329  11.911  11.158  1.00 27.10           O  
HETATM 2459  O   HOH A 385      32.577  43.687   7.323  1.00 21.30           O  
HETATM 2460  O   HOH A 386      31.184  33.308   9.867  1.00 24.82           O  
HETATM 2461  O   HOH A 387      11.103  44.354  -0.615  1.00 32.99           O  
HETATM 2462  O   HOH A 388      25.591  60.306   7.943  1.00 22.45           O  
HETATM 2463  O   HOH A 389       5.973  69.795  12.478  1.00 31.83           O  
HETATM 2464  O   HOH A 390      23.953  17.351   4.982  1.00 26.73           O  
HETATM 2465  O   HOH A 391      31.063  54.754  25.555  1.00 30.25           O  
HETATM 2466  O   HOH A 392      20.973  18.406   4.131  1.00 20.07           O  
HETATM 2467  O   HOH A 393      30.377  55.569  23.074  1.00 29.45           O  
HETATM 2468  O   HOH A 394      14.261  19.062  13.047  1.00 28.25           O  
HETATM 2469  O   HOH A 395      18.543  20.366  27.877  1.00 37.15           O  
HETATM 2470  O   HOH A 396      23.886  61.814  32.190  1.00 35.85           O  
HETATM 2471  O   HOH A 397      26.444  38.329  21.054  1.00 19.57           O  
HETATM 2472  O   HOH A 398      17.682  68.343  25.454  1.00 22.47           O  
HETATM 2473  O   HOH A 399      27.715  60.353  10.577  1.00 28.36           O  
HETATM 2474  O   HOH A 400      26.336  33.586  22.394  1.00 21.20           O  
HETATM 2475  O   HOH A 401      26.378  20.458  21.489  1.00 25.17           O  
HETATM 2476  O   HOH A 402      10.718  40.460  -0.941  1.00 29.74           O  
HETATM 2477  O   HOH A 403      27.818  44.294   1.868  1.00 24.67           O  
HETATM 2478  O   HOH A 404      11.187  55.667  33.752  1.00 33.93           O  
HETATM 2479  O   HOH A 405      25.437  52.062  33.964  1.00 30.94           O  
HETATM 2480  O   HOH A 406      32.691  45.882  27.216  1.00 32.58           O  
HETATM 2481  O   HOH A 407      17.091  38.063  22.775  1.00 36.07           O  
HETATM 2482  O   HOH A 408      26.014  18.257  22.830  1.00 25.01           O  
HETATM 2483  O   HOH A 409      16.618  48.822  -0.243  1.00 27.50           O  
HETATM 2484  O   HOH A 410       8.980  39.315  15.168  1.00 25.06           O  
HETATM 2485  O   HOH A 411      -0.047  66.975  30.408  1.00 42.09           O  
HETATM 2486  O   HOH A 412       3.289  76.400  31.390  1.00 43.66           O  
HETATM 2487  O   HOH A 413      28.854  50.323   9.335  1.00 22.55           O  
HETATM 2488  O   HOH A 414      29.508  28.308  26.865  1.00 50.30           O  
HETATM 2489  O   HOH A 415       5.644  50.450  29.567  1.00 22.54           O  
HETATM 2490  O   HOH A 416      19.264  63.025   9.292  1.00 32.79           O  
HETATM 2491  O   HOH A 417      12.746  33.191  15.189  1.00 27.15           O  
HETATM 2492  O   HOH A 418      28.866  54.753  16.609  1.00 25.82           O  
HETATM 2493  O   HOH A 419       4.911  36.828   7.884  1.00 23.73           O  
HETATM 2494  O   HOH A 420      29.830  60.342  21.681  1.00 43.09           O  
HETATM 2495  O   HOH A 421      12.258  24.559   6.974  1.00 32.04           O  
HETATM 2496  O   HOH A 422      17.729  69.101  16.059  1.00 29.47           O  
HETATM 2497  O   HOH A 423       5.836  66.370  13.913  1.00 57.02           O  
HETATM 2498  O   HOH A 424      31.517  31.236  27.271  1.00 29.83           O  
HETATM 2499  O   HOH A 425      29.171  24.926  14.422  1.00 26.45           O  
HETATM 2500  O   HOH A 426      16.993  22.501  -1.275  1.00 41.27           O  
HETATM 2501  O   HOH A 427       0.753  55.480  10.683  1.00 41.83           O  
HETATM 2502  O   HOH A 428      14.042  72.647  20.132  1.00 33.89           O  
HETATM 2503  O   HOH A 429      17.350  52.065   2.726  1.00 32.83           O  
HETATM 2504  O   HOH A 430      19.743  46.770  -1.215  1.00 35.81           O  
HETATM 2505  O   HOH A 431       3.493  53.180  29.617  1.00 36.69           O  
HETATM 2506  O   HOH A 432      24.098  45.690  31.097  1.00 27.49           O  
HETATM 2507  O   HOH A 433       9.011  65.450  15.929  1.00 24.08           O  
HETATM 2508  O   HOH A 434      15.133  62.816   7.279  1.00 34.23           O  
HETATM 2509  O   HOH A 435       1.401  38.115  21.272  1.00 31.67           O  
HETATM 2510  O   HOH A 436      -2.319  53.203  26.461  1.00 37.24           O  
HETATM 2511  O   HOH A 437      26.611  14.872  10.234  1.00 29.64           O  
HETATM 2512  O   HOH A 438      22.322  41.102  31.894  1.00 37.22           O  
HETATM 2513  O   HOH A 439      15.399  55.942  38.505  1.00 28.06           O  
HETATM 2514  O   HOH A 440      26.296  64.280  29.779  1.00 39.71           O  
HETATM 2515  O   HOH A 441      23.384  35.948  27.656  1.00 43.88           O  
HETATM 2516  O   HOH A 442       6.938  57.221   2.477  1.00 43.98           O  
HETATM 2517  O   HOH A 443      10.375  16.369  20.465  1.00 33.04           O  
HETATM 2518  O   HOH A 444      27.807  23.236  18.665  1.00 35.05           O  
HETATM 2519  O   HOH A 445      29.844  36.178  -1.063  1.00 30.05           O  
HETATM 2520  O   HOH A 446      14.373  26.425   3.185  1.00 24.14           O  
HETATM 2521  O   HOH A 447      -1.013  53.477  12.016  1.00 25.64           O  
HETATM 2522  O   HOH A 448      10.240  18.223  17.708  1.00 38.72           O  
HETATM 2523  O   HOH A 449      25.083  39.667  -2.422  1.00 32.16           O  
HETATM 2524  O   HOH A 450       7.268  49.886  42.053  1.00 43.72           O  
HETATM 2525  O   HOH A 451      29.435  52.010  28.215  1.00 26.00           O  
HETATM 2526  O   HOH A 452      12.126  61.657   5.643  1.00 34.83           O  
HETATM 2527  O   HOH A 453      17.047  25.743   2.216  1.00 24.83           O  
HETATM 2528  O   HOH A 454      19.498  40.160  18.506  1.00 30.70           O  
HETATM 2529  O   HOH A 455       9.599  33.777  12.560  1.00 25.19           O  
HETATM 2530  O   HOH A 456      -4.935  47.396  11.320  1.00 26.45           O  
HETATM 2531  O   HOH A 457      24.286  50.469  27.243  1.00 24.59           O  
HETATM 2532  O   HOH A 458       9.406  54.101  41.070  1.00 40.77           O  
HETATM 2533  O   HOH A 459      14.926  70.625  33.827  1.00 47.16           O  
HETATM 2534  O   HOH A 460       6.571  69.150  35.267  1.00 42.82           O  
HETATM 2535  O   HOH A 461      12.710  26.963  -1.980  1.00 54.53           O  
HETATM 2536  O   HOH A 462      10.611  61.732   7.961  1.00 40.51           O  
HETATM 2537  O   HOH A 463      13.088  12.296  20.403  1.00 40.74           O  
HETATM 2538  O   HOH A 464       7.605  38.319  -0.773  1.00 37.32           O  
HETATM 2539  O   HOH A 465      15.136  28.536  -0.680  1.00 25.60           O  
HETATM 2540  O   HOH A 466      26.840  47.439   7.154  1.00 30.24           O  
HETATM 2541  O   HOH A 467      15.610  41.838  -2.116  1.00 34.30           O  
HETATM 2542  O   HOH A 468      15.634  13.200  16.459  1.00 27.95           O  
HETATM 2543  O   HOH A 469      25.053  58.634  32.327  1.00 34.15           O  
HETATM 2544  O   HOH A 470      -2.293  44.294  11.844  1.00 34.38           O  
HETATM 2545  O   HOH A 471      24.262  30.082  -5.809  1.00 38.00           O  
HETATM 2546  O   HOH A 472      32.134  54.405  19.232  1.00 42.21           O  
HETATM 2547  O   HOH A 473      26.729  61.977  16.674  1.00 25.65           O  
HETATM 2548  O   HOH A 474      -3.220  33.342  17.548  1.00 33.50           O  
HETATM 2549  O   HOH A 475      24.019  21.977  28.742  1.00 39.75           O  
HETATM 2550  O   HOH A 476      27.639  52.498  32.576  1.00 35.84           O  
HETATM 2551  O   HOH A 477      27.959  53.920  29.452  1.00 36.42           O  
HETATM 2552  O   HOH A 478      23.644  66.383  17.565  1.00 33.41           O  
HETATM 2553  O   HOH A 479       9.178  47.676  29.099  1.00 33.01           O  
HETATM 2554  O   HOH A 480      10.608  61.975  34.667  1.00 32.29           O  
HETATM 2555  O   HOH A 481      16.711  64.147   9.025  1.00 27.38           O  
HETATM 2556  O   HOH A 482      28.156  46.292  28.952  1.00 29.53           O  
HETATM 2557  O   HOH A 483       3.110  51.193   5.742  1.00 33.53           O  
HETATM 2558  O   HOH A 484       7.000  31.354   6.693  1.00 32.89           O  
HETATM 2559  O   HOH A 485       1.024  37.587  10.481  1.00 59.22           O  
HETATM 2560  O   HOH A 486      -2.117  52.900  22.310  1.00 36.56           O  
HETATM 2561  O   HOH A 487      -3.273  50.800  25.159  1.00 33.96           O  
HETATM 2562  O   HOH A 488      33.789  40.941  10.382  1.00 33.67           O  
HETATM 2563  O   HOH A 489      20.924  16.801  28.796  1.00 32.53           O  
HETATM 2564  O   HOH A 490      31.011  22.993  23.690  1.00 49.32           O  
HETATM 2565  O   HOH A 491      32.602  45.950   9.168  1.00 33.27           O  
HETATM 2566  O   HOH A 492      13.994  50.665   2.868  1.00 29.57           O  
HETATM 2567  O   HOH A 493      21.095  41.880  28.213  1.00 35.94           O  
HETATM 2568  O   HOH A 494      -1.226  52.386  29.796  1.00 37.33           O  
HETATM 2569  O   HOH A 495      13.595  72.744  33.309  1.00 56.52           O  
HETATM 2570  O   HOH A 496       1.573  51.741  24.708  1.00 44.96           O  
HETATM 2571  O   HOH A 497       7.241  64.633  34.380  1.00 42.13           O  
HETATM 2572  O   HOH A 498      18.614  41.195  29.094  1.00 34.38           O  
HETATM 2573  O   HOH A 499      29.430  32.566  -5.646  1.00 48.03           O  
HETATM 2574  O   HOH A 500       1.059  61.300  30.137  1.00 32.93           O  
HETATM 2575  O   HOH A 501      -1.215  33.284  19.817  1.00 56.92           O  
HETATM 2576  O   HOH A 502      30.864  32.623   2.247  1.00 31.81           O  
HETATM 2577  O   HOH A 503      34.656  34.560  11.910  1.00 36.14           O  
HETATM 2578  O   HOH A 504      14.001  15.522   5.161  1.00 37.08           O  
HETATM 2579  O   HOH A 505      11.704  21.552  16.357  1.00 50.68           O  
HETATM 2580  O   HOH A 506      11.512  50.737   6.181  1.00 26.51           O  
HETATM 2581  O   HOH A 507      18.445  67.627  32.329  1.00 43.50           O  
HETATM 2582  O   HOH A 508      11.001  60.219   3.696  1.00 34.53           O  
HETATM 2583  O   HOH A 509      12.724  25.927  15.928  1.00 38.19           O  
HETATM 2584  O   HOH A 510      30.374  55.540  27.977  1.00 37.41           O  
HETATM 2585  O   HOH A 511       8.835  77.599  25.668  1.00 33.73           O  
HETATM 2586  O   HOH A 512      29.867  59.141  31.404  1.00 55.70           O  
HETATM 2587  O   HOH A 513      -0.910  70.669  28.827  1.00 36.84           O  
HETATM 2588  O   HOH A 514       4.654  30.551  15.917  1.00 37.91           O  
HETATM 2589  O   HOH A 515      17.622  72.954  21.305  1.00 57.86           O  
HETATM 2590  O   HOH A 516      15.375  55.782  34.143  1.00 21.30           O  
HETATM 2591  O   HOH A 517      17.127  23.451  18.470  1.00 37.43           O  
HETATM 2592  O   HOH A 518      10.107  49.628   0.744  1.00 33.52           O  
HETATM 2593  O   HOH A 519      28.359  49.392   7.008  1.00 37.17           O  
HETATM 2594  O   HOH A 520      17.696  56.965  35.027  1.00 15.87           O  
HETATM 2595  O   HOH A 521      18.049  29.185  17.007  1.00 33.52           O  
HETATM 2596  O   HOH A 522      -2.497  59.145  28.675  1.00 41.34           O  
HETATM 2597  O   HOH A 523      10.870  47.045  20.279  1.00 29.43           O  
HETATM 2598  O   HOH A 524      13.347  24.154   2.531  1.00 30.97           O  
HETATM 2599  O   HOH A 525      16.655  26.600  -0.539  1.00 27.01           O  
HETATM 2600  O   HOH A 526      17.065  25.517  -2.737  1.00 30.69           O  
HETATM 2601  O   HOH A 527      11.278  38.072  14.714  1.00 22.33           O  
HETATM 2602  O   HOH A 528      10.618  35.383  14.995  1.00 27.69           O  
HETATM 2603  O   HOH A 529       6.930  37.902  16.073  1.00 29.47           O  
HETATM 2604  O   HOH A 530      34.504  49.819  15.394  1.00 14.86           O  
HETATM 2605  O   HOH A 531      15.299  46.400  20.844  1.00 21.33           O  
HETATM 2606  O   HOH A 532      15.142  48.774  25.053  1.00 30.56           O  
HETATM 2607  O   HOH A 533      31.661  24.764   3.809  1.00 47.65           O  
HETATM 2608  O   HOH A 534       5.488  55.310   5.702  1.00 28.64           O  
HETATM 2609  O   HOH A 535      23.708  63.790  29.037  1.00 30.96           O  
HETATM 2610  O   HOH A 536      11.295  50.764   2.876  1.00 48.73           O  
HETATM 2611  O   HOH A 537       2.650  36.507   6.697  1.00 37.23           O  
HETATM 2612  O   HOH A 538      11.886  54.002  40.031  1.00 28.57           O  
HETATM 2613  O   HOH A 539      31.566  52.345  10.987  1.00 38.26           O  
HETATM 2614  O   HOH A 540       6.426  48.910  39.524  1.00 58.72           O  
HETATM 2615  O   HOH A 541      17.248  69.399  33.966  1.00 41.82           O  
HETATM 2616  O   HOH A 542       7.023  41.929  34.136  1.00 53.11           O  
HETATM 2617  O   HOH A 543      -0.018  41.192  23.110  1.00 33.50           O  
HETATM 2618  O   HOH A 544       4.998  33.814   8.570  1.00 47.40           O  
HETATM 2619  O   HOH A 545      16.719  69.657  27.855  1.00 41.87           O  
HETATM 2620  O   HOH A 546      15.601  11.958   8.729  1.00 44.06           O  
HETATM 2621  O   HOH A 547      16.052  20.869  15.375  1.00 37.92           O  
HETATM 2622  O   HOH A 548      12.786  59.345  35.221  1.00 34.88           O  
HETATM 2623  O   HOH A 549      18.677  40.020  -4.002  1.00 40.67           O  
HETATM 2624  O   HOH A 550       3.291  24.847  10.020  1.00 47.48           O  
HETATM 2625  O   HOH A 551      11.579  64.617  35.987  1.00 46.07           O  
HETATM 2626  O   HOH A 552      19.664  28.614  20.109  1.00 36.31           O  
HETATM 2627  O   HOH A 553      32.237  43.247  28.027  1.00 32.39           O  
HETATM 2628  O   HOH A 554      33.452  34.863  24.411  1.00 36.93           O  
HETATM 2629  O   HOH A 555      34.677  27.441  22.476  1.00 44.62           O  
HETATM 2630  O   HOH A 556      -3.571  55.479  27.432  1.00 49.69           O  
HETATM 2631  O   HOH A 557      19.528  11.421   4.410  1.00 47.36           O  
HETATM 2632  O   HOH A 558      35.766  26.337   5.605  1.00 44.90           O  
HETATM 2633  O   HOH A 559      11.986  18.822  24.603  1.00 49.24           O  
HETATM 2634  O   HOH A 560       7.504  43.677  31.966  1.00 60.06           O  
HETATM 2635  O   HOH A 561      13.125  46.649  18.976  1.00 22.04           O  
HETATM 2636  O   HOH A 562      10.492  21.908   6.239  1.00 59.01           O  
HETATM 2637  O   HOH A 563      16.167  42.823  29.024  1.00 43.28           O  
HETATM 2638  O   HOH A 564      22.740  51.714   0.900  1.00 32.79           O  
HETATM 2639  O   HOH A 565      22.809  49.063   0.092  1.00 33.70           O  
HETATM 2640  O   HOH A 566      17.975  50.918   0.382  1.00 34.79           O  
HETATM 2641  O   HOH A 567      13.134  70.899  25.443  1.00 42.92           O  
HETATM 2642  O   HOH A 568       7.058  79.514  25.138  1.00 37.54           O  
HETATM 2643  O   HOH A 569       8.126  80.153  22.684  1.00 29.85           O  
HETATM 2644  O   HOH A 570      31.831  25.490  13.710  1.00 42.33           O  
HETATM 2645  O   HOH A 571      33.178  25.963  16.463  1.00 32.65           O  
HETATM 2646  O   HOH A 572      35.928  26.641  14.630  1.00 42.29           O  
HETATM 2647  O   HOH A 573      37.119  29.021  14.182  1.00 35.10           O  
HETATM 2648  O   HOH A 574      33.445  33.117   7.891  1.00 51.42           O  
HETATM 2649  O   HOH A 575      -3.197  53.726  19.923  1.00 25.69           O  
HETATM 2650  O   HOH A 576      -0.280  56.793  21.328  1.00 41.71           O  
HETATM 2651  O   HOH A 577      -2.332  58.973  18.585  1.00 48.84           O  
HETATM 2652  O   HOH A 578      -0.094  62.089  16.039  1.00 37.81           O  
HETATM 2653  O   HOH A 579      15.937  67.271  14.780  1.00 27.37           O  
HETATM 2654  O   HOH A 580      13.969  68.552  13.164  1.00 40.15           O  
HETATM 2655  O   HOH A 581       8.214  69.806  10.224  1.00 35.29           O  
HETATM 2656  O   HOH A 582       0.477  65.300  21.805  1.00 31.19           O  
HETATM 2657  O   HOH A 583      -1.923  64.214  23.634  1.00 45.32           O  
HETATM 2658  O   HOH A 584      -5.194  51.579  11.100  1.00 36.84           O  
HETATM 2659  O   HOH A 585      -5.713  49.313  13.073  1.00 19.88           O  
HETATM 2660  O   HOH A 586      34.306  22.158  11.794  1.00 53.31           O  
HETATM 2661  O   HOH A 587      33.530  43.622  10.539  1.00 45.44           O  
HETATM 2662  O   HOH A 588      33.632  41.034   7.785  1.00 31.69           O  
HETATM 2663  O   HOH A 589      34.785  37.095   6.963  1.00 43.41           O  
HETATM 2664  O   HOH A 590      23.714  36.798  -1.572  1.00 36.60           O  
HETATM 2665  O   HOH A 591      21.490  36.094  -0.738  1.00 44.60           O  
HETATM 2666  O   HOH A 592      19.827  38.481   0.257  1.00 27.99           O  
HETATM 2667  O   HOH A 593      21.111  39.784  -1.806  1.00 38.85           O  
HETATM 2668  O   HOH A 594      25.982  37.006  -1.009  1.00 38.02           O  
HETATM 2669  O   HOH A 595      27.023  36.775  -3.766  1.00 40.58           O  
HETATM 2670  O   HOH A 596       3.990  38.559  15.921  1.00 48.91           O  
HETATM 2671  O   HOH A 597      22.230  11.125  19.670  1.00 38.42           O  
HETATM 2672  O   HOH A 598       5.008  59.965   7.931  1.00 55.88           O  
HETATM 2673  O   HOH A 599      24.538  54.337   3.378  1.00 36.66           O  
HETATM 2674  O   HOH A 600      15.062  67.013  27.555  1.00 36.12           O  
HETATM 2675  O   HOH A 601      30.413  17.938  17.686  1.00 46.04           O  
HETATM 2676  O   HOH A 602      14.047  39.294  18.440  1.00 33.48           O  
HETATM 2677  O   HOH A 603       3.201  36.878   4.316  1.00 34.47           O  
HETATM 2678  O   HOH A 604      28.990  61.554  23.792  1.00 34.48           O  
HETATM 2679  O   HOH A 605      14.446  40.085  11.693  1.00 35.39           O  
HETATM 2680  O   HOH A 606      17.013  11.644   4.551  1.00 48.11           O  
HETATM 2681  O   HOH A 607      17.943  13.301  13.307  1.00 40.72           O  
HETATM 2682  O   HOH A 608       6.482  46.300  22.098  1.00 49.16           O  
HETATM 2683  O   HOH A 609       4.687  24.920   6.969  1.00 51.86           O  
HETATM 2684  O   HOH A 610      13.289  22.837   4.692  1.00 44.33           O  
HETATM 2685  O   HOH A 611      30.496  45.204  28.702  1.00 42.19           O  
HETATM 2686  O   HOH A 612      14.210  46.498  23.972  1.00 30.01           O  
HETATM 2687  O   HOH A 613      19.404  26.220  -3.598  1.00 31.97           O  
HETATM 2688  O   HOH A 614       9.738  44.335  19.330  1.00 29.80           O  
HETATM 2689  O   HOH A 615      -3.142  64.029  28.144  1.00 39.62           O  
HETATM 2690  O   HOH A 616      23.635  47.008   1.968  1.00 29.04           O  
HETATM 2691  O   HOH A 617       3.722  47.698   1.801  1.00 42.34           O  
HETATM 2692  O   HOH A 618      -0.823  59.140  13.213  1.00 46.63           O  
HETATM 2693  O   HOH A 619       9.960  22.266   3.555  1.00 45.66           O  
HETATM 2694  O   HOH A 620       6.533  44.860  34.127  1.00 57.77           O  
HETATM 2695  O   HOH A 621      27.017  33.595  -5.569  1.00 36.67           O  
HETATM 2696  O   HOH A 622       3.445  63.487  14.838  1.00 40.10           O  
HETATM 2697  O   HOH A 623      -0.214  54.641  23.304  1.00 49.58           O  
HETATM 2698  O   HOH A 624      19.850  65.318  11.604  1.00 45.98           O  
HETATM 2699  O   HOH A 625      20.140  22.980   3.308  1.00 45.47           O  
HETATM 2700  O   HOH A 626       8.852  72.698  14.837  1.00 41.54           O  
HETATM 2701  O   HOH A 627      35.793  34.038  14.016  1.00 45.09           O  
HETATM 2702  O   HOH A 628       2.024  64.376  19.647  1.00 32.92           O  
HETATM 2703  O   HOH A 629      19.233  60.516  33.965  1.00 37.01           O  
HETATM 2704  O   HOH A 630      26.604  52.197  28.198  1.00 36.85           O  
HETATM 2705  O   HOH A 631      26.412  64.299  12.505  1.00 51.30           O  
HETATM 2706  O   HOH A 632       5.417  55.615  -0.810  1.00 42.64           O  
HETATM 2707  O   HOH A 633      -3.634  53.549  12.251  1.00 42.70           O  
HETATM 2708  O   HOH A 634      23.864  30.947  28.237  1.00 50.65           O  
HETATM 2709  O   HOH A 635      36.289  40.526  11.679  1.00 36.54           O  
HETATM 2710  O   HOH A 636      19.342  62.885  32.742  1.00 48.01           O  
HETATM 2711  O   HOH A 637      13.152  63.148  11.710  1.00 43.32           O  
HETATM 2712  O   HOH A 638      35.723  30.820  15.623  1.00 40.44           O  
HETATM 2713  O   HOH A 639      21.295  29.579  -8.538  1.00 53.94           O  
HETATM 2714  O   HOH A 640      26.714  44.367  30.895  1.00 52.89           O  
HETATM 2715  O   HOH A 641      22.609   9.714   5.415  1.00 51.27           O  
HETATM 2716  O   HOH A 642       1.558  43.357  10.049  1.00 41.61           O  
HETATM 2717  O   HOH A 643      30.855  20.096   7.156  1.00 46.44           O  
HETATM 2718  O   HOH A 644      32.924  37.891   4.683  1.00 35.70           O  
HETATM 2719  O   HOH A 645      31.052  34.898  28.377  1.00 54.77           O  
HETATM 2720  O   HOH A 646      19.320  18.128   0.479  1.00 43.69           O  
HETATM 2721  O   HOH A 647       4.942  50.058   3.340  1.00 35.24           O  
HETATM 2722  O   HOH A 648      35.827  38.133  12.655  1.00 40.40           O  
HETATM 2723  O   HOH A 649      28.003  37.516  27.231  1.00 46.24           O  
HETATM 2724  O   HOH A 650      32.757  49.681   9.377  1.00 44.83           O  
HETATM 2725  O   HOH A 651       9.340  66.566  34.926  1.00 48.05           O  
HETATM 2726  O   HOH A 652      11.459  53.887   1.228  1.00 40.93           O  
HETATM 2727  O   HOH A 653       9.166  13.686   6.641  1.00 52.14           O  
HETATM 2728  O   HOH A 654      24.511  21.867  -0.564  1.00 39.08           O  
HETATM 2729  O   HOH A 655      24.597  23.182   1.466  1.00 34.68           O  
HETATM 2730  O   HOH A 656      26.972  38.250  23.988  1.00 34.78           O  
HETATM 2731  O   HOH A 657      12.788  43.413  21.762  1.00 45.63           O  
HETATM 2732  O   HOH A 658       0.802  51.800   7.451  1.00 42.42           O  
HETATM 2733  O   HOH A 659      32.792  33.355   4.596  1.00 44.91           O  
HETATM 2734  O   HOH A 660       6.192  45.780  19.728  1.00 48.29           O  
HETATM 2735  O   HOH A 661      30.290  32.869  -2.859  1.00 51.78           O  
HETATM 2736  O   HOH A 662      16.080  65.658  33.586  1.00 56.07           O  
HETATM 2737  O   HOH A 663      14.383  34.194   8.501  1.00 65.65           O  
HETATM 2738  O   HOH A 664      14.141  69.170  26.986  1.00 51.15           O  
HETATM 2739  O   HOH A 665      15.511  13.176   3.207  1.00 58.00           O  
HETATM 2740  O   HOH A 666      -0.843  45.246  26.057  1.00 38.76           O  
HETATM 2741  O   HOH A 667      29.437  52.895   8.930  1.00 40.20           O  
HETATM 2742  O   HOH A 668      29.014  53.785   6.404  1.00 46.04           O  
HETATM 2743  O   HOH A 669      13.558  21.558  14.373  1.00 46.32           O  
HETATM 2744  O   HOH A 670      13.965  29.095  15.487  1.00 42.43           O  
HETATM 2745  O   HOH A 671      21.549  33.568  20.950  1.00 22.50           O  
HETATM 2746  O   HOH A 672      20.155  34.354  22.993  1.00 30.78           O  
HETATM 2747  O   HOH A 673      15.897  33.925  17.755  1.00 35.48           O  
HETATM 2748  O   HOH A 674      22.892  44.113  29.534  1.00 43.36           O  
HETATM 2749  O   HOH A 675      15.668  55.463  41.321  1.00 29.18           O  
HETATM 2750  O   HOH A 676      13.452  54.275  41.996  1.00 22.72           O  
HETATM 2751  O   HOH A 677      31.039  57.579  21.526  1.00 36.82           O  
HETATM 2752  O   HOH A 678      31.374  55.034  15.590  1.00 55.94           O  
HETATM 2753  O   HOH A 679      12.168  38.152  17.226  1.00 32.93           O  
HETATM 2754  O   HOH A 680      10.069  38.381  18.791  1.00 48.69           O  
HETATM 2755  O   HOH A 681       8.439  35.423  16.545  1.00 38.20           O  
HETATM 2756  O   HOH A 682       7.321  59.421   8.284  1.00 32.37           O  
HETATM 2757  O   HOH A 683       0.637  45.378  24.067  1.00 35.70           O  
HETATM 2758  O   HOH A 684      33.596  26.228   4.210  1.00 31.40           O  
HETATM 2759  O   HOH A 685      32.724  31.138   9.345  1.00 49.17           O  
HETATM 2760  O   HOH A 686      28.175  21.910  14.889  1.00 42.66           O  
HETATM 2761  O   HOH A 687      14.939  56.673   2.797  1.00 32.70           O  
HETATM 2762  O   HOH A 688      36.494  33.955  22.154  1.00 46.82           O  
HETATM 2763  O   HOH A 689      25.343  61.676   5.347  1.00 45.76           O  
HETATM 2764  O   HOH A 690       7.192  38.656  19.106  1.00 44.57           O  
HETATM 2765  O   HOH A 691      28.307  58.053   8.978  1.00 47.05           O  
HETATM 2766  O   HOH A 692      37.360  31.245  18.209  1.00 46.10           O  
HETATM 2767  O   HOH A 693      19.565  43.240  38.607  0.50 37.28           O  
HETATM 2768  O   HOH A 694       1.814  38.210   2.859  1.00 49.74           O  
HETATM 2769  O   HOH A 695      21.489  34.922  -4.445  1.00 43.38           O  
HETATM 2770  O   HOH A 696      15.861  16.204  28.598  1.00 46.79           O  
HETATM 2771  O   HOH A 697      14.847  22.051  18.428  1.00 49.82           O  
HETATM 2772  O   HOH A 698      19.979  20.559  30.284  1.00 52.03           O  
HETATM 2773  O   HOH A 699      31.053  24.602  21.576  1.00 38.33           O  
HETATM 2774  O   HOH A 700      39.052  26.220   8.705  1.00 45.60           O  
HETATM 2775  O   HOH A 701      42.199  28.686  11.910  1.00 43.42           O  
HETATM 2776  O   HOH A 702      26.803  55.856  33.175  1.00 36.22           O  
HETATM 2777  O   HOH A 703      21.409  67.821  32.092  1.00 44.19           O  
HETATM 2778  O   HOH A 704      16.576  59.382  36.192  1.00 40.80           O  
HETATM 2779  O   HOH A 705      21.304  58.554  33.912  1.00 37.71           O  
HETATM 2780  O   HOH A 706      23.680  57.858  34.352  1.00 44.63           O  
HETATM 2781  O   HOH A 707       4.488  51.654  31.310  1.00 45.47           O  
HETATM 2782  O   HOH A 708       2.693  60.163  32.196  1.00 47.34           O  
HETATM 2783  O   HOH A 709       5.030  58.849  32.353  1.00 43.77           O  
HETATM 2784  O   HOH A 710      12.963  35.747  18.100  1.00 44.09           O  
HETATM 2785  O   HOH A 711      10.678  32.038  18.442  1.00 35.93           O  
HETATM 2786  O   HOH A 712      11.879  46.019  22.720  1.00 47.24           O  
HETATM 2787  O   HOH A 713      18.681  36.037  24.130  1.00 43.28           O  
HETATM 2788  O   HOH A 714      21.136  33.899  25.494  1.00 41.52           O  
HETATM 2789  O   HOH A 715      20.547  26.408  21.505  1.00 38.99           O  
HETATM 2790  O   HOH A 716      20.372  26.527  24.358  1.00 42.44           O  
HETATM 2791  O   HOH A 717      17.959  24.887  26.123  1.00 49.76           O  
HETATM 2792  O   HOH A 718      32.302  45.697  12.044  1.00 47.33           O  
HETATM 2793  O   HOH A 719      27.702  47.304   2.023  1.00 51.44           O  
HETATM 2794  O   HOH A 720      19.979  36.102  -2.727  1.00 54.26           O  
HETATM 2795  O   HOH A 721      19.919  42.650  -0.826  1.00 41.75           O  
HETATM 2796  O   HOH A 722       8.774  15.359   4.369  1.00 40.24           O  
HETATM 2797  O   HOH A 723      17.117  66.026  12.990  1.00 36.72           O  
HETATM 2798  O   HOH A 724      10.171  65.226  11.848  1.00 42.71           O  
HETATM 2799  O   HOH A 725      11.532  63.385   9.645  1.00 46.17           O  
HETATM 2800  O   HOH A 726      15.063  64.963  11.944  1.00 44.43           O  
HETATM 2801  O   HOH A 727      20.268  68.863  15.162  1.00 37.87           O  
HETATM 2802  O   HOH A 728      26.011  64.549  18.049  1.00 38.24           O  
HETATM 2803  O   HOH A 729      28.966  62.570  15.399  1.00 42.96           O  
HETATM 2804  O   HOH A 730      13.620  54.339   2.860  1.00 40.77           O  
HETATM 2805  O   HOH A 731      11.430  47.710  -0.563  1.00 34.98           O  
HETATM 2806  O   HOH A 732      12.096  48.005  -3.231  1.00 39.67           O  
HETATM 2807  O   HOH A 733      -1.027  49.181   7.749  1.00 49.57           O  
HETATM 2808  O   HOH A 734      23.287  41.459  -1.780  1.00 43.80           O  
HETATM 2809  O   HOH A 735      14.055  28.716  -3.359  1.00 34.35           O  
HETATM 2810  O   HOH A 736       2.225  33.513   5.464  1.00 42.84           O  
HETATM 2811  O   HOH A 737      17.510  70.282  30.241  1.00 39.22           O  
HETATM 2812  O   HOH A 738      10.067  78.095  27.965  1.00 43.26           O  
HETATM 2813  O   HOH A 739       6.629  72.900  35.115  1.00 47.59           O  
CONECT  807 2365                                                                
CONECT  820 2365                                                                
CONECT  913 2365                                                                
CONECT  941 2365                                                                
CONECT 2365  807  820  913  941                                                 
MASTER      380    0    2   14   12    0    4    6 2812    1    5   23          
END                                                                             
