path: root/plip/test/pdb/1aku.pdb

HEADER    ELECTRON TRANSPORT                      27-MAY-97   1AKU              
TITLE     D95A HYDROQUINONE FLAVODOXIN MUTANT FROM D. VULGARIS                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FLAVODOXIN;                                                
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES;                                                       
COMPND   6 OTHER_DETAILS: HYDROQUINONE                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: DESULFOVIBRIO VULGARIS SUBSP.                   
SOURCE   3 VULGARIS STR. HILDENBOROUGH;                                         
SOURCE   4 ORGANISM_TAXID: 882;                                                 
SOURCE   5 STRAIN: HILDENBOROUGH;                                               
SOURCE   6 CELLULAR_LOCATION: CYTOPLASM;                                        
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: TG2                                        
KEYWDS    ELECTRON TRANSPORT, ELECTRON TRANSFER, FLAVOPROTEIN, FMN,             
KEYWDS   2 FLAVODOXIN, MUTANT                                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.MCCARTHY,M.WALSH,T.HIGGINS                                          
REVDAT   3   24-FEB-09 1AKU    1       VERSN                                    
REVDAT   2   23-DEC-02 1AKU    1       JRNL                                     
REVDAT   1   02-DEC-98 1AKU    0                                                
JRNL        AUTH   A.A.MCCARTHY,M.A.WALSH,C.S.VERMA,D.P.O'CONNELL,              
JRNL        AUTH 2 M.REINHOLD,G.N.YALLOWAY,D.D'ARCY,T.M.HIGGINS,                
JRNL        AUTH 3 G.VOORDOUW,S.G.MAYHEW                                        
JRNL        TITL   CRYSTALLOGRAPHIC INVESTIGATION OF THE ROLE OF                
JRNL        TITL 2 ASPARTATE 95 IN THE MODULATION OF THE REDOX                  
JRNL        TITL 3 POTENTIALS OF DESULFOVIBRIO VULGARIS FLAVODOXIN.             
JRNL        REF    BIOCHEMISTRY                  V.  41 10950 2002              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   12206666                                                     
JRNL        DOI    10.1021/BI020225H                                            
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   A.MCCARTHY                                                   
REMARK   1  TITL   X-RAY CRYSTALLOGRAPHIC STUDIES ON THE FLAVIN                 
REMARK   1  TITL 2 BINDING SITE OF FLAVODOXIN FROM DESULFOVIBRIO                
REMARK   1  TITL 3 VULGARIS                                                     
REMARK   1  REF    THESIS, NATIONAL UNIVERSITY                1997              
REMARK   1  REF  2 OF IRELAND                                                   
REMARK   1  PUBL   DUBLIN : NATIONAL UNIVERSITY OF IRELAND (THESIS)             
REMARK   1  REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PROLSQ                                               
REMARK   3   AUTHORS     : KONNERT,HENDRICKSON                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 12.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 16098                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.215                           
REMARK   3   R VALUE            (WORKING SET) : 0.212                           
REMARK   3   FREE R VALUE                     : 0.270                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 805                             
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.2150                 
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.2120                 
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.270                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.000                  
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 805                    
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 16098                  
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1101                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 41                                      
REMARK   3   SOLVENT ATOMS            : 155                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 21.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.60                          
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) : 0.15                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.25                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 12.00                           
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.015 ; 0.020               
REMARK   3    ANGLE DISTANCE                  (A) : 0.047 ; 0.050               
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : 0.045 ; 0.040               
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : 0.170 ; 0.150               
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : 0.180 ; 0.300               
REMARK   3    MULTIPLE TORSION                (A) : 0.260 ; 0.300               
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : 2.340 ; 3.000               
REMARK   3    STAGGERED                 (DEGREES) : 19.460; 15.000              
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; 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  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1AKU COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : AUG-95                             
REMARK 200  TEMPERATURE           (KELVIN) : 120                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG                 
REMARK 200  BEAMLINE                       : X11                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.937                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 16098                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 10.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY                : 4.400                              
REMARK 200  R MERGE                    (I) : 0.42000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.7800                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.92                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.32000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 60-70% AMMONIUM SULFATE, 100MM TRIS      
REMARK 280  -HCL, PH=7.0.                                                       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
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   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
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       70.13000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       26.30000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       26.30000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      105.19500            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       26.30000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       26.30000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       35.06500            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       26.30000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       26.30000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      105.19500            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       26.30000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       26.30000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       35.06500            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       70.13000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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   OE1  GLU A    32     O    HOH A   259              2.01            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   249     O    HOH A   261     4455     1.87            
REMARK 500   O    HOH A   220     O    HOH A   261     4455     2.16            
REMARK 500   O    HOH A   253     O    HOH A   257     6565     2.19            
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    ARG A  24   NE  -  CZ  -  NH1 ANGL. DEV. =   4.3 DEGREES          
REMARK 500    ASP A  28   CB  -  CG  -  OD1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    TYR A  31   CB  -  CG  -  CD2 ANGL. DEV. =  -4.9 DEGREES          
REMARK 500    TYR A  31   CB  -  CG  -  CD1 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    GLU A  32   OE1 -  CD  -  OE2 ANGL. DEV. =  10.2 DEGREES          
REMARK 500    GLY A  61   CA  -  C   -  O   ANGL. DEV. =  11.3 DEGREES          
REMARK 500    ASP A  62   CB  -  CG  -  OD2 ANGL. DEV. =  -7.0 DEGREES          
REMARK 500    ASP A  63   CA  -  CB  -  CG  ANGL. DEV. =  15.0 DEGREES          
REMARK 500    ASP A  63   CB  -  CG  -  OD1 ANGL. DEV. =   7.9 DEGREES          
REMARK 500    ASP A  63   CA  -  C   -  O   ANGL. DEV. =  14.3 DEGREES          
REMARK 500    ASP A  63   O   -  C   -  N   ANGL. DEV. =  -9.8 DEGREES          
REMARK 500    GLU A  66   CA  -  CB  -  CG  ANGL. DEV. =  13.4 DEGREES          
REMARK 500    ASP A  70   CB  -  CG  -  OD2 ANGL. DEV. =   6.7 DEGREES          
REMARK 500    ARG A  86   NE  -  CZ  -  NH1 ANGL. DEV. =   4.6 DEGREES          
REMARK 500    TYR A  98   CB  -  CG  -  CD1 ANGL. DEV. =   4.0 DEGREES          
REMARK 500    ASP A 106   CB  -  CG  -  OD1 ANGL. DEV. =  -7.4 DEGREES          
REMARK 500    ASP A 106   CB  -  CG  -  OD2 ANGL. DEV. =   8.8 DEGREES          
REMARK 500    LYS A 113   CA  -  CB  -  CG  ANGL. DEV. =  15.9 DEGREES          
REMARK 500    GLN A 121   CA  -  CB  -  CG  ANGL. DEV. =  17.9 DEGREES          
REMARK 500    ARG A 125   NE  -  CZ  -  NH1 ANGL. DEV. =  -8.4 DEGREES          
REMARK 500    ASP A 129   CB  -  CG  -  OD1 ANGL. DEV. =   9.7 DEGREES          
REMARK 500    ASP A 129   CB  -  CG  -  OD2 ANGL. DEV. =  -6.1 DEGREES          
REMARK 500    ARG A 134   CG  -  CD  -  NE  ANGL. DEV. = -13.3 DEGREES          
REMARK 500    ARG A 134   CD  -  NE  -  CZ  ANGL. DEV. =   9.4 DEGREES          
REMARK 500    ARG A 134   NH1 -  CZ  -  NH2 ANGL. DEV. =   9.4 DEGREES          
REMARK 500    ARG A 134   NE  -  CZ  -  NH2 ANGL. DEV. =  -7.5 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  64       90.70   -169.32                                   
REMARK 500    TYR A 100       79.32   -108.88                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 228        DISTANCE =  8.12 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: FMN                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: FMN CO-FACTOR.                                     
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1                   
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 149                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMN A 150                 
DBREF  1AKU A    2   148  UNP    P00323   FLAV_DESVH       2    148             
SEQADV 1AKU ALA A   95  UNP  P00323    ASP    95 ENGINEERED                     
SEQRES   1 A  147  PRO LYS ALA LEU ILE VAL TYR GLY SER THR THR GLY ASN          
SEQRES   2 A  147  THR GLU TYR THR ALA GLU THR ILE ALA ARG GLU LEU ALA          
SEQRES   3 A  147  ASP ALA GLY TYR GLU VAL ASP SER ARG ASP ALA ALA SER          
SEQRES   4 A  147  VAL GLU ALA GLY GLY LEU PHE GLU GLY PHE ASP LEU VAL          
SEQRES   5 A  147  LEU LEU GLY CYS SER THR TRP GLY ASP ASP SER ILE GLU          
SEQRES   6 A  147  LEU GLN ASP ASP PHE ILE PRO LEU PHE ASP SER LEU GLU          
SEQRES   7 A  147  GLU THR GLY ALA GLN GLY ARG LYS VAL ALA CYS PHE GLY          
SEQRES   8 A  147  CYS GLY ALA SER SER TYR GLU TYR PHE CYS GLY ALA VAL          
SEQRES   9 A  147  ASP ALA ILE GLU GLU LYS LEU LYS ASN LEU GLY ALA GLU          
SEQRES  10 A  147  ILE VAL GLN ASP GLY LEU ARG ILE ASP GLY ASP PRO ARG          
SEQRES  11 A  147  ALA ALA ARG ASP ASP ILE VAL GLY TRP ALA HIS ASP VAL          
SEQRES  12 A  147  ARG GLY ALA ILE                                              
HET    SO4  A   1       5                                                       
HET    SO4  A 149       5                                                       
HET    FMN  A 150      31                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     FMN FLAVIN MONONUCLEOTIDE                                            
HETSYN     FMN RIBOFLAVIN MONOPHOSPHATE                                         
FORMUL   2  SO4    2(O4 S 2-)                                                   
FORMUL   4  FMN    C17 H21 N4 O9 P                                              
FORMUL   5  HOH   *155(H2 O)                                                    
HELIX    1   1 ASN A   14  ASP A   28  1                                  15    
HELIX    2   2 ALA A   38  SER A   40  5                                   3    
HELIX    3   3 ASP A   69  GLU A   80  1                                  12    
HELIX    4   4 GLY A  103  ASN A  114  1                                  12    
HELIX    5   5 PRO A  130  ALA A  132  5                                   3    
HELIX    6   6 ARG A  134  GLY A  146  1                                  13    
SHEET    1   A 5 GLU A  32  ASP A  37  0                                        
SHEET    2   A 5 LYS A   3  GLY A   9  1  N  ALA A   4   O  GLU A  32           
SHEET    3   A 5 LEU A  52  CYS A  57  1  N  LEU A  52   O  LEU A   5           
SHEET    4   A 5 VAL A  88  GLY A  94  1  N  ALA A  89   O  VAL A  53           
SHEET    5   A 5 LEU A 124  ASP A 127  1  N  LEU A 124   O  GLY A  92           
SITE     1 FMN  1 FMN A 150                                                     
SITE     1 AC1  3 GLU A  48  GLY A  49  ARG A  86                               
SITE     1 AC2  3 TYR A  17  ARG A 131  HOH A 214                               
SITE     1 AC3 24 SER A  10  THR A  11  THR A  12  GLY A  13                    
SITE     2 AC3 24 ASN A  14  THR A  15  ASP A  28  SER A  58                    
SITE     3 AC3 24 THR A  59  TRP A  60  GLY A  61  CYS A  93                    
SITE     4 AC3 24 GLY A  94  ALA A  95  TYR A  98  TYR A 100                    
SITE     5 AC3 24 PHE A 101  CYS A 102  HOH A 171  HOH A 173                    
SITE     6 AC3 24 HOH A 185  HOH A 195  HOH A 225  HOH A 244                    
CRYST1   52.600   52.600  140.260  90.00  90.00  90.00 P 43 21 2     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      0.019011  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.019011  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007130        0.00000                         
ATOM      1  N   PRO A   2       2.201  26.003  -7.393  1.00 17.99           N  
ATOM      2  CA  PRO A   2       3.317  26.075  -6.387  1.00 20.18           C  
ATOM      3  C   PRO A   2       2.936  25.266  -5.164  1.00 17.44           C  
ATOM      4  O   PRO A   2       1.746  24.988  -4.959  1.00 19.16           O  
ATOM      5  CB  PRO A   2       3.639  27.555  -6.048  1.00 19.52           C  
ATOM      6  CG  PRO A   2       2.890  28.318  -7.128  1.00 17.16           C  
ATOM      7  CD  PRO A   2       1.735  27.429  -7.543  1.00 16.46           C  
ATOM      8  N   LYS A   3       3.909  24.829  -4.361  1.00 22.63           N  
ATOM      9  CA  LYS A   3       3.693  24.043  -3.147  1.00 20.00           C  
ATOM     10  C   LYS A   3       4.112  24.888  -1.922  1.00 15.28           C  
ATOM     11  O   LYS A   3       5.285  25.243  -1.804  1.00 16.34           O  
ATOM     12  CB  LYS A   3       4.543  22.765  -3.055  1.00 23.35           C  
ATOM     13  CG  LYS A   3       4.520  22.028  -4.370  1.00 34.29           C  
ATOM     14  CD  LYS A   3       5.327  20.743  -4.329  1.00 48.37           C  
ATOM     15  CE  LYS A   3       4.998  19.927  -5.583  1.00 55.02           C  
ATOM     16  NZ  LYS A   3       6.077  18.988  -5.998  1.00 67.66           N  
ATOM     17  N   ALA A   4       3.112  25.133  -1.094  1.00 18.10           N  
ATOM     18  CA  ALA A   4       3.365  25.925   0.111  1.00 17.74           C  
ATOM     19  C   ALA A   4       3.185  25.068   1.373  1.00 17.39           C  
ATOM     20  O   ALA A   4       2.408  24.122   1.467  1.00 17.07           O  
ATOM     21  CB  ALA A   4       2.407  27.119   0.204  1.00 12.34           C  
ATOM     22  N   LEU A   5       3.987  25.381   2.401  1.00 15.37           N  
ATOM     23  CA  LEU A   5       3.899  24.735   3.695  1.00 16.24           C  
ATOM     24  C   LEU A   5       3.500  25.874   4.666  1.00 12.18           C  
ATOM     25  O   LEU A   5       4.096  26.919   4.541  1.00 13.08           O  
ATOM     26  CB  LEU A   5       5.267  24.297   4.169  1.00 17.07           C  
ATOM     27  CG  LEU A   5       5.510  23.144   5.114  1.00 20.87           C  
ATOM     28  CD1 LEU A   5       6.709  23.554   5.979  1.00 19.02           C  
ATOM     29  CD2 LEU A   5       4.378  22.576   5.905  1.00 13.53           C  
ATOM     30  N   ILE A   6       2.527  25.707   5.572  1.00 17.20           N  
ATOM     31  CA  ILE A   6       2.093  26.667   6.576  1.00  9.35           C  
ATOM     32  C   ILE A   6       2.346  25.978   7.942  1.00 10.33           C  
ATOM     33  O   ILE A   6       1.851  24.872   8.125  1.00 12.16           O  
ATOM     34  CB  ILE A   6       0.616  27.112   6.473  1.00 11.23           C  
ATOM     35  CG1 ILE A   6       0.398  27.848   5.100  1.00  9.01           C  
ATOM     36  CG2 ILE A   6       0.152  28.149   7.504  1.00 10.22           C  
ATOM     37  CD1 ILE A   6      -1.086  28.094   4.826  1.00  8.83           C  
ATOM     38  N   VAL A   7       3.167  26.541   8.836  1.00 14.72           N  
ATOM     39  CA  VAL A   7       3.371  25.874  10.160  1.00 17.23           C  
ATOM     40  C   VAL A   7       2.916  26.931  11.184  1.00 14.58           C  
ATOM     41  O   VAL A   7       3.374  28.088  11.057  1.00 14.55           O  
ATOM     42  CB  VAL A   7       4.785  25.419  10.482  1.00 20.04           C  
ATOM     43  CG1 VAL A   7       4.853  24.954  11.941  1.00 19.25           C  
ATOM     44  CG2 VAL A   7       5.299  24.267   9.599  1.00 18.69           C  
ATOM     45  N   TYR A   8       1.962  26.601  12.077  1.00 15.58           N  
ATOM     46  CA  TYR A   8       1.505  27.626  13.021  1.00 13.53           C  
ATOM     47  C   TYR A   8       1.659  27.187  14.497  1.00 12.40           C  
ATOM     48  O   TYR A   8       1.599  25.998  14.768  1.00 11.72           O  
ATOM     49  CB  TYR A   8       0.037  28.109  12.734  1.00 14.19           C  
ATOM     50  CG  TYR A   8      -0.899  26.921  12.746  1.00 17.84           C  
ATOM     51  CD1 TYR A   8      -1.038  26.140  11.587  1.00 15.69           C  
ATOM     52  CD2 TYR A   8      -1.552  26.551  13.940  1.00 13.52           C  
ATOM     53  CE1 TYR A   8      -1.838  25.018  11.615  1.00 17.19           C  
ATOM     54  CE2 TYR A   8      -2.329  25.401  13.974  1.00 15.16           C  
ATOM     55  CZ  TYR A   8      -2.480  24.666  12.809  1.00 18.94           C  
ATOM     56  OH  TYR A   8      -3.257  23.526  12.831  1.00 15.69           O  
ATOM     57  N   GLY A   9       1.912  28.098  15.426  1.00 16.90           N  
ATOM     58  CA  GLY A   9       2.011  27.921  16.872  1.00 15.19           C  
ATOM     59  C   GLY A   9       0.780  28.739  17.373  1.00 11.98           C  
ATOM     60  O   GLY A   9       0.754  29.978  17.241  1.00 12.11           O  
ATOM     61  N   SER A  10      -0.218  28.088  17.971  1.00 12.52           N  
ATOM     62  CA  SER A  10      -1.421  28.760  18.451  1.00 11.03           C  
ATOM     63  C   SER A  10      -1.911  28.240  19.812  1.00 13.05           C  
ATOM     64  O   SER A  10      -2.069  27.008  19.907  1.00 12.25           O  
ATOM     65  CB  SER A  10      -2.546  28.545  17.413  1.00  8.91           C  
ATOM     66  OG  SER A  10      -3.573  29.488  17.816  1.00 12.44           O  
ATOM     67  N   THR A  11      -2.100  29.092  20.819  1.00 10.69           N  
ATOM     68  CA  THR A  11      -2.516  28.615  22.175  1.00 13.49           C  
ATOM     69  C   THR A  11      -4.035  28.687  22.294  1.00 15.49           C  
ATOM     70  O   THR A  11      -4.661  27.704  22.709  1.00 14.52           O  
ATOM     71  CB  THR A  11      -1.796  29.400  23.313  1.00 11.23           C  
ATOM     72  OG1 THR A  11      -0.422  28.970  23.475  1.00 15.57           O  
ATOM     73  CG2 THR A  11      -2.449  29.286  24.696  1.00 10.76           C  
ATOM     74  N   THR A  12      -4.673  29.790  21.975  1.00 12.10           N  
ATOM     75  CA  THR A  12      -6.107  30.003  22.035  1.00 14.58           C  
ATOM     76  C   THR A  12      -6.804  29.834  20.677  1.00 18.17           C  
ATOM     77  O   THR A  12      -8.027  30.065  20.669  1.00 14.81           O  
ATOM     78  CB  THR A  12      -6.471  31.350  22.693  1.00 18.71           C  
ATOM     79  OG1 THR A  12      -6.348  32.575  21.968  1.00 19.95           O  
ATOM     80  CG2 THR A  12      -5.549  31.527  23.937  1.00 15.82           C  
ATOM     81  N   GLY A  13      -6.059  29.496  19.623  1.00 15.79           N  
ATOM     82  CA  GLY A  13      -6.595  29.288  18.285  1.00 16.70           C  
ATOM     83  C   GLY A  13      -6.731  30.461  17.333  1.00 12.92           C  
ATOM     84  O   GLY A  13      -7.347  30.362  16.278  1.00 16.25           O  
ATOM     85  N   ASN A  14      -6.255  31.645  17.643  1.00  9.46           N  
ATOM     86  CA  ASN A  14      -6.375  32.824  16.786  1.00 10.76           C  
ATOM     87  C   ASN A  14      -5.373  32.666  15.627  1.00 15.27           C  
ATOM     88  O   ASN A  14      -5.775  32.834  14.469  1.00 13.58           O  
ATOM     89  CB  ASN A  14      -6.142  34.105  17.586  1.00  6.76           C  
ATOM     90  CG  ASN A  14      -7.333  34.505  18.448  1.00 12.83           C  
ATOM     91  OD1 ASN A  14      -8.481  34.077  18.273  1.00 14.95           O  
ATOM     92  ND2 ASN A  14      -7.017  35.377  19.392  1.00 12.54           N  
ATOM     93  N   THR A  15      -4.097  32.303  15.899  1.00 11.60           N  
ATOM     94  CA  THR A  15      -3.118  32.107  14.855  1.00 12.36           C  
ATOM     95  C   THR A  15      -3.499  30.857  14.056  1.00 16.94           C  
ATOM     96  O   THR A  15      -3.234  30.774  12.856  1.00 16.04           O  
ATOM     97  CB  THR A  15      -1.679  31.989  15.377  1.00 12.61           C  
ATOM     98  OG1 THR A  15      -1.432  33.192  16.173  1.00 13.75           O  
ATOM     99  CG2 THR A  15      -0.702  31.965  14.213  1.00  9.76           C  
ATOM    100  N   GLU A  16      -4.156  29.882  14.676  1.00 10.45           N  
ATOM    101  CA  GLU A  16      -4.578  28.727  13.891  1.00 11.69           C  
ATOM    102  C   GLU A  16      -5.705  29.144  12.958  1.00 17.64           C  
ATOM    103  O   GLU A  16      -5.715  28.677  11.812  1.00 15.38           O  
ATOM    104  CB  GLU A  16      -5.042  27.644  14.840  1.00 13.44           C  
ATOM    105  CG  GLU A  16      -5.678  26.512  14.009  1.00 14.94           C  
ATOM    106  CD  GLU A  16      -6.129  25.393  14.940  1.00 21.72           C  
ATOM    107  OE1 GLU A  16      -6.765  25.590  16.002  1.00 25.49           O  
ATOM    108  OE2 GLU A  16      -5.840  24.255  14.542  1.00 24.71           O  
ATOM    109  N   TYR A  17      -6.638  30.002  13.391  1.00 15.26           N  
ATOM    110  CA  TYR A  17      -7.725  30.490  12.561  1.00 13.35           C  
ATOM    111  C   TYR A  17      -7.053  31.320  11.452  1.00 16.52           C  
ATOM    112  O   TYR A  17      -7.530  31.214  10.316  1.00 15.61           O  
ATOM    113  CB  TYR A  17      -8.759  31.315  13.328  1.00  9.95           C  
ATOM    114  CG  TYR A  17      -9.647  32.157  12.443  1.00 12.47           C  
ATOM    115  CD1 TYR A  17      -9.264  33.402  11.959  1.00 12.59           C  
ATOM    116  CD2 TYR A  17     -10.921  31.663  12.115  1.00 16.89           C  
ATOM    117  CE1 TYR A  17     -10.096  34.146  11.109  1.00 13.54           C  
ATOM    118  CE2 TYR A  17     -11.764  32.393  11.287  1.00 16.53           C  
ATOM    119  CZ  TYR A  17     -11.341  33.616  10.792  1.00 18.78           C  
ATOM    120  OH  TYR A  17     -12.217  34.335   9.988  1.00 23.85           O  
ATOM    121  N   THR A  18      -6.033  32.119  11.657  1.00 16.52           N  
ATOM    122  CA  THR A  18      -5.348  32.900  10.608  1.00 18.36           C  
ATOM    123  C   THR A  18      -4.697  31.961   9.589  1.00 19.13           C  
ATOM    124  O   THR A  18      -4.772  32.125   8.344  1.00 18.29           O  
ATOM    125  CB  THR A  18      -4.281  33.806  11.241  1.00 16.65           C  
ATOM    126  OG1 THR A  18      -5.006  34.616  12.216  1.00 14.28           O  
ATOM    127  CG2 THR A  18      -3.611  34.773  10.279  1.00  9.00           C  
ATOM    128  N   ALA A  19      -4.057  30.902  10.024  1.00 13.77           N  
ATOM    129  CA  ALA A  19      -3.414  29.906   9.182  1.00 12.86           C  
ATOM    130  C   ALA A  19      -4.454  29.246   8.285  1.00 14.93           C  
ATOM    131  O   ALA A  19      -4.197  29.054   7.087  1.00 15.31           O  
ATOM    132  CB  ALA A  19      -2.725  28.798  10.001  1.00 16.42           C  
ATOM    133  N   GLU A  20      -5.619  28.882   8.803  1.00 14.68           N  
ATOM    134  CA  GLU A  20      -6.673  28.255   7.992  1.00 16.24           C  
ATOM    135  C   GLU A  20      -7.250  29.200   6.954  1.00 14.60           C  
ATOM    136  O   GLU A  20      -7.663  28.774   5.869  1.00 16.44           O  
ATOM    137  CB  GLU A  20      -7.844  27.808   8.851  1.00 20.51           C  
ATOM    138  CG  GLU A  20      -7.447  26.686   9.820  1.00 23.16           C  
ATOM    139  CD  GLU A  20      -8.473  26.532  10.945  1.00 31.50           C  
ATOM    140  OE1 GLU A  20      -9.246  27.496  11.208  1.00 25.26           O  
ATOM    141  OE2 GLU A  20      -8.464  25.422  11.556  1.00 28.73           O  
ATOM    142  N   THR A  21      -7.347  30.482   7.237  1.00 13.35           N  
ATOM    143  CA  THR A  21      -7.866  31.506   6.304  1.00 13.51           C  
ATOM    144  C   THR A  21      -6.867  31.661   5.143  1.00 14.76           C  
ATOM    145  O   THR A  21      -7.260  31.745   3.949  1.00 13.36           O  
ATOM    146  CB  THR A  21      -8.098  32.838   7.058  1.00 16.95           C  
ATOM    147  OG1 THR A  21      -9.164  32.659   7.987  1.00 12.29           O  
ATOM    148  CG2 THR A  21      -8.454  33.999   6.134  1.00 16.82           C  
ATOM    149  N   ILE A  22      -5.575  31.761   5.475  1.00  9.75           N  
ATOM    150  CA  ILE A  22      -4.453  31.842   4.540  1.00 11.94           C  
ATOM    151  C   ILE A  22      -4.420  30.532   3.730  1.00 12.87           C  
ATOM    152  O   ILE A  22      -4.282  30.587   2.489  1.00 14.71           O  
ATOM    153  CB  ILE A  22      -3.096  32.104   5.223  1.00  8.93           C  
ATOM    154  CG1 ILE A  22      -3.009  33.518   5.844  1.00  8.35           C  
ATOM    155  CG2 ILE A  22      -1.969  31.942   4.196  1.00 13.09           C  
ATOM    156  CD1 ILE A  22      -1.759  33.541   6.764  1.00 10.01           C  
ATOM    157  N   ALA A  23      -4.588  29.313   4.293  1.00 12.31           N  
ATOM    158  CA  ALA A  23      -4.589  28.066   3.551  1.00 12.85           C  
ATOM    159  C   ALA A  23      -5.700  28.027   2.472  1.00 17.41           C  
ATOM    160  O   ALA A  23      -5.471  27.562   1.338  1.00 17.40           O  
ATOM    161  CB  ALA A  23      -4.709  26.817   4.418  1.00  9.24           C  
ATOM    162  N   ARG A  24      -6.894  28.466   2.793  1.00 13.94           N  
ATOM    163  CA  ARG A  24      -8.017  28.506   1.844  1.00 15.64           C  
ATOM    164  C   ARG A  24      -7.793  29.493   0.682  1.00 16.17           C  
ATOM    165  O   ARG A  24      -8.140  29.145  -0.457  1.00 15.04           O  
ATOM    166  CB  ARG A  24      -9.294  28.806   2.632  1.00 13.03           C  
ATOM    167  CG  ARG A  24     -10.559  28.934   1.771  1.00 14.69           C  
ATOM    168  CD  ARG A  24     -10.818  27.557   1.152  1.00 19.17           C  
ATOM    169  NE  ARG A  24     -12.010  27.666   0.269  1.00 30.00           N  
ATOM    170  CZ  ARG A  24     -13.256  27.480   0.732  1.00 37.44           C  
ATOM    171  NH1 ARG A  24     -13.562  27.202   2.012  1.00 28.41           N  
ATOM    172  NH2 ARG A  24     -14.265  27.578  -0.140  1.00 34.34           N  
ATOM    173  N   GLU A  25      -7.267  30.693   0.935  1.00 15.12           N  
ATOM    174  CA  GLU A  25      -6.957  31.687  -0.081  1.00 17.82           C  
ATOM    175  C   GLU A  25      -5.980  31.096  -1.110  1.00 20.59           C  
ATOM    176  O   GLU A  25      -6.160  31.120  -2.345  1.00 17.50           O  
ATOM    177  CB  GLU A  25      -6.345  32.962   0.544  1.00 14.67           C  
ATOM    178  CG  GLU A  25      -7.411  33.801   1.261  1.00 31.97           C  
ATOM    179  CD  GLU A  25      -8.603  34.134   0.348  1.00 40.34           C  
ATOM    180  OE1 GLU A  25      -8.402  34.852  -0.654  1.00 40.08           O  
ATOM    181  OE2 GLU A  25      -9.757  33.695   0.598  1.00 31.32           O  
ATOM    182  N   LEU A  26      -4.897  30.457  -0.647  1.00 18.00           N  
ATOM    183  CA  LEU A  26      -3.875  29.797  -1.442  1.00 19.24           C  
ATOM    184  C   LEU A  26      -4.442  28.605  -2.213  1.00 20.77           C  
ATOM    185  O   LEU A  26      -4.060  28.504  -3.406  1.00 17.21           O  
ATOM    186  CB  LEU A  26      -2.678  29.326  -0.588  1.00 15.99           C  
ATOM    187  CG  LEU A  26      -1.482  30.262  -0.466  1.00 18.33           C  
ATOM    188  CD1 LEU A  26      -1.761  31.731  -0.604  1.00 13.22           C  
ATOM    189  CD2 LEU A  26      -0.659  29.984   0.800  1.00 18.93           C  
ATOM    190  N   ALA A  27      -5.283  27.770  -1.619  1.00 18.17           N  
ATOM    191  CA  ALA A  27      -5.889  26.618  -2.282  1.00 14.11           C  
ATOM    192  C   ALA A  27      -6.902  27.033  -3.357  1.00 17.59           C  
ATOM    193  O   ALA A  27      -7.021  26.405  -4.438  1.00 16.28           O  
ATOM    194  CB  ALA A  27      -6.553  25.760  -1.227  1.00 12.35           C  
ATOM    195  N   ASP A  28      -7.621  28.133  -3.116  1.00 18.60           N  
ATOM    196  CA  ASP A  28      -8.616  28.686  -4.036  1.00 17.48           C  
ATOM    197  C   ASP A  28      -7.934  29.214  -5.307  1.00 19.09           C  
ATOM    198  O   ASP A  28      -8.562  29.299  -6.393  1.00 15.92           O  
ATOM    199  CB  ASP A  28      -9.408  29.852  -3.435  1.00 13.13           C  
ATOM    200  CG  ASP A  28     -10.489  29.364  -2.503  1.00 20.17           C  
ATOM    201  OD1 ASP A  28     -10.861  28.162  -2.432  1.00 18.19           O  
ATOM    202  OD2 ASP A  28     -10.960  30.271  -1.785  1.00 18.72           O  
ATOM    203  N   ALA A  29      -6.672  29.612  -5.170  1.00 13.37           N  
ATOM    204  CA  ALA A  29      -5.950  30.100  -6.341  1.00 17.10           C  
ATOM    205  C   ALA A  29      -5.215  28.981  -7.098  1.00 17.12           C  
ATOM    206  O   ALA A  29      -4.522  29.302  -8.088  1.00 19.58           O  
ATOM    207  CB  ALA A  29      -4.974  31.216  -5.963  1.00 17.66           C  
ATOM    208  N   GLY A  30      -5.313  27.711  -6.679  1.00 13.63           N  
ATOM    209  CA  GLY A  30      -4.651  26.583  -7.296  1.00 12.99           C  
ATOM    210  C   GLY A  30      -3.343  26.147  -6.636  1.00 18.66           C  
ATOM    211  O   GLY A  30      -2.705  25.186  -7.138  1.00 16.21           O  
ATOM    212  N   TYR A  31      -2.852  26.788  -5.535  1.00 13.95           N  
ATOM    213  CA  TYR A  31      -1.623  26.258  -4.949  1.00 15.44           C  
ATOM    214  C   TYR A  31      -1.923  24.902  -4.262  1.00 15.75           C  
ATOM    215  O   TYR A  31      -3.034  24.501  -3.900  1.00 16.03           O  
ATOM    216  CB  TYR A  31      -1.140  27.074  -3.747  1.00 13.84           C  
ATOM    217  CG  TYR A  31      -0.310  28.268  -4.096  1.00 18.02           C  
ATOM    218  CD1 TYR A  31      -0.610  29.175  -5.105  1.00 15.31           C  
ATOM    219  CD2 TYR A  31       0.845  28.460  -3.332  1.00 19.74           C  
ATOM    220  CE1 TYR A  31       0.195  30.257  -5.350  1.00 13.81           C  
ATOM    221  CE2 TYR A  31       1.669  29.533  -3.591  1.00 22.10           C  
ATOM    222  CZ  TYR A  31       1.338  30.432  -4.584  1.00 20.58           C  
ATOM    223  OH  TYR A  31       2.214  31.475  -4.765  1.00 21.31           O  
ATOM    224  N   GLU A  32      -0.866  24.142  -4.097  1.00 15.38           N  
ATOM    225  CA  GLU A  32      -0.842  22.868  -3.358  1.00 16.55           C  
ATOM    226  C   GLU A  32      -0.424  23.356  -1.935  1.00 17.75           C  
ATOM    227  O   GLU A  32       0.533  24.145  -1.749  1.00 16.09           O  
ATOM    228  CB  GLU A  32       0.162  21.974  -4.026  1.00 24.79           C  
ATOM    229  CG  GLU A  32      -0.073  20.580  -3.456  1.00 44.47           C  
ATOM    230  CD  GLU A  32       1.077  19.684  -3.931  1.00 53.03           C  
ATOM    231  OE1 GLU A  32       1.374  19.888  -5.139  1.00 43.90           O  
ATOM    232  OE2 GLU A  32       1.543  18.925  -3.040  1.00 56.05           O  
ATOM    233  N   VAL A  33      -1.227  23.083  -0.932  1.00 18.98           N  
ATOM    234  CA  VAL A  33      -1.069  23.549   0.458  1.00 20.18           C  
ATOM    235  C   VAL A  33      -1.022  22.461   1.541  1.00 23.43           C  
ATOM    236  O   VAL A  33      -1.917  21.636   1.775  1.00 22.84           O  
ATOM    237  CB  VAL A  33      -2.265  24.483   0.811  1.00 20.59           C  
ATOM    238  CG1 VAL A  33      -2.132  25.104   2.229  1.00 20.63           C  
ATOM    239  CG2 VAL A  33      -2.401  25.628  -0.203  1.00 19.39           C  
ATOM    240  N   ASP A  34       0.077  22.470   2.297  1.00 21.83           N  
ATOM    241  CA  ASP A  34       0.346  21.561   3.434  1.00 20.47           C  
ATOM    242  C   ASP A  34       0.342  22.425   4.732  1.00 20.29           C  
ATOM    243  O   ASP A  34       1.289  23.207   4.937  1.00 17.65           O  
ATOM    244  CB  ASP A  34       1.697  20.926   3.069  1.00 20.51           C  
ATOM    245  CG  ASP A  34       2.079  19.725   3.890  1.00 33.18           C  
ATOM    246  OD1 ASP A  34       1.692  19.649   5.094  1.00 29.64           O  
ATOM    247  OD2 ASP A  34       2.785  18.839   3.352  1.00 33.32           O  
ATOM    248  N   SER A  35      -0.694  22.310   5.583  1.00 15.04           N  
ATOM    249  CA  SER A  35      -0.817  23.142   6.805  1.00 20.09           C  
ATOM    250  C   SER A  35      -0.580  22.291   8.042  1.00 23.49           C  
ATOM    251  O   SER A  35      -1.232  21.265   8.251  1.00 25.37           O  
ATOM    252  CB  SER A  35      -2.153  23.892   6.665  1.00 20.07           C  
ATOM    253  OG  SER A  35      -2.306  24.884   7.679  1.00 38.07           O  
ATOM    254  N   ARG A  36       0.408  22.594   8.891  1.00 17.84           N  
ATOM    255  CA  ARG A  36       0.786  21.810  10.056  1.00 21.82           C  
ATOM    256  C   ARG A  36       0.921  22.599  11.367  1.00 16.31           C  
ATOM    257  O   ARG A  36       1.405  23.713  11.372  1.00 17.04           O  
ATOM    258  CB  ARG A  36       2.183  21.122   9.848  1.00 18.83           C  
ATOM    259  CG  ARG A  36       2.229  20.230   8.594  1.00 17.28           C  
ATOM    260  CD  ARG A  36       3.541  19.447   8.476  1.00 22.69           C  
ATOM    261  NE  ARG A  36       3.805  19.023   7.095  1.00 27.07           N  
ATOM    262  CZ  ARG A  36       4.947  18.660   6.525  1.00 26.45           C  
ATOM    263  NH1 ARG A  36       6.048  18.636   7.268  1.00 24.27           N  
ATOM    264  NH2 ARG A  36       5.031  18.345   5.231  1.00 22.36           N  
ATOM    265  N   ASP A  37       0.396  22.014  12.432  1.00 19.89           N  
ATOM    266  CA  ASP A  37       0.512  22.638  13.762  1.00 15.41           C  
ATOM    267  C   ASP A  37       1.982  22.489  14.165  1.00 13.96           C  
ATOM    268  O   ASP A  37       2.544  21.371  14.063  1.00 14.99           O  
ATOM    269  CB  ASP A  37      -0.443  21.887  14.723  1.00 19.84           C  
ATOM    270  CG  ASP A  37      -0.594  22.541  16.094  1.00 22.44           C  
ATOM    271  OD1 ASP A  37       0.409  23.023  16.676  1.00 18.85           O  
ATOM    272  OD2 ASP A  37      -1.733  22.686  16.610  1.00 21.31           O  
ATOM    273  N   ALA A  38       2.673  23.517  14.679  1.00 13.11           N  
ATOM    274  CA  ALA A  38       4.075  23.428  15.088  1.00 17.09           C  
ATOM    275  C   ALA A  38       4.323  22.315  16.115  1.00 21.37           C  
ATOM    276  O   ALA A  38       5.451  21.826  16.310  1.00 20.37           O  
ATOM    277  CB  ALA A  38       4.522  24.739  15.740  1.00 14.89           C  
ATOM    278  N   ALA A  39       3.288  21.905  16.838  1.00 20.66           N  
ATOM    279  CA  ALA A  39       3.334  20.860  17.860  1.00 22.28           C  
ATOM    280  C   ALA A  39       3.599  19.491  17.270  1.00 23.93           C  
ATOM    281  O   ALA A  39       4.193  18.646  17.939  1.00 25.87           O  
ATOM    282  CB  ALA A  39       2.005  20.787  18.628  1.00 19.91           C  
ATOM    283  N   SER A  40       3.233  19.233  16.041  1.00 27.70           N  
ATOM    284  CA  SER A  40       3.409  17.988  15.323  1.00 34.57           C  
ATOM    285  C   SER A  40       4.604  17.889  14.368  1.00 37.29           C  
ATOM    286  O   SER A  40       4.776  16.873  13.669  1.00 36.97           O  
ATOM    287  CB  SER A  40       2.189  17.874  14.343  1.00 40.59           C  
ATOM    288  OG  SER A  40       2.249  18.806  13.250  1.00 31.56           O  
ATOM    289  N   VAL A  41       5.396  18.941  14.287  1.00 35.13           N  
ATOM    290  CA  VAL A  41       6.490  19.094  13.338  1.00 32.06           C  
ATOM    291  C   VAL A  41       7.879  18.803  13.843  1.00 35.77           C  
ATOM    292  O   VAL A  41       8.197  19.001  15.024  1.00 29.31           O  
ATOM    293  CB  VAL A  41       6.213  20.575  12.872  1.00 28.90           C  
ATOM    294  CG1 VAL A  41       7.292  21.600  13.135  1.00 25.25           C  
ATOM    295  CG2 VAL A  41       5.625  20.630  11.493  1.00 25.65           C  
ATOM    296  N   GLU A  42       8.728  18.297  12.933  1.00 35.73           N  
ATOM    297  CA  GLU A  42      10.139  18.030  13.211  1.00 37.92           C  
ATOM    298  C   GLU A  42      10.903  19.050  12.345  1.00 36.58           C  
ATOM    299  O   GLU A  42      10.612  19.185  11.147  1.00 37.84           O  
ATOM    300  CB  GLU A  42      10.627  16.629  12.942  1.00 53.16           C  
ATOM    301  CG  GLU A  42      10.097  15.576  13.886  1.00 72.84           C  
ATOM    302  CD  GLU A  42      10.430  15.599  15.358  1.00 81.89           C  
ATOM    303  OE1 GLU A  42      10.532  16.570  16.146  1.00 78.85           O  
ATOM    304  OE2 GLU A  42      10.601  14.433  15.820  1.00 90.07           O  
ATOM    305  N   ALA A  43      11.836  19.780  12.955  1.00 33.19           N  
ATOM    306  CA  ALA A  43      12.554  20.797  12.204  1.00 32.24           C  
ATOM    307  C   ALA A  43      13.415  20.202  11.095  1.00 32.04           C  
ATOM    308  O   ALA A  43      13.455  20.827  10.034  1.00 31.44           O  
ATOM    309  CB  ALA A  43      13.393  21.719  13.085  1.00 18.78           C  
ATOM    310  N   GLY A  44      14.077  19.080  11.304  1.00 30.86           N  
ATOM    311  CA  GLY A  44      14.974  18.439  10.361  1.00 32.46           C  
ATOM    312  C   GLY A  44      14.526  18.381   8.926  1.00 28.09           C  
ATOM    313  O   GLY A  44      13.653  17.572   8.595  1.00 31.87           O  
ATOM    314  N   GLY A  45      15.095  19.228   8.075  1.00 31.03           N  
ATOM    315  CA  GLY A  45      14.757  19.350   6.650  1.00 29.84           C  
ATOM    316  C   GLY A  45      13.271  19.674   6.429  1.00 26.17           C  
ATOM    317  O   GLY A  45      12.699  19.422   5.346  1.00 25.38           O  
ATOM    318  N   LEU A  46      12.575  20.279   7.379  1.00 20.48           N  
ATOM    319  CA  LEU A  46      11.147  20.560   7.220  1.00 21.21           C  
ATOM    320  C   LEU A  46      10.694  21.315   5.967  1.00 21.53           C  
ATOM    321  O   LEU A  46       9.584  21.018   5.457  1.00 20.34           O  
ATOM    322  CB  LEU A  46      10.719  21.296   8.503  1.00 18.13           C  
ATOM    323  CG  LEU A  46       9.253  21.661   8.706  1.00 18.59           C  
ATOM    324  CD1 LEU A  46       8.347  20.453   8.745  1.00 18.56           C  
ATOM    325  CD2 LEU A  46       9.206  22.512   9.967  1.00 22.50           C  
ATOM    326  N   PHE A  47      11.464  22.307   5.504  1.00 17.30           N  
ATOM    327  CA  PHE A  47      11.092  23.127   4.379  1.00 20.87           C  
ATOM    328  C   PHE A  47      11.467  22.532   3.026  1.00 22.09           C  
ATOM    329  O   PHE A  47      11.211  23.161   2.002  1.00 23.16           O  
ATOM    330  CB  PHE A  47      11.743  24.518   4.489  1.00 18.94           C  
ATOM    331  CG  PHE A  47      11.508  25.276   5.771  1.00 14.91           C  
ATOM    332  CD1 PHE A  47      10.511  24.918   6.664  1.00 14.35           C  
ATOM    333  CD2 PHE A  47      12.275  26.405   6.034  1.00 17.38           C  
ATOM    334  CE1 PHE A  47      10.312  25.643   7.820  1.00 20.19           C  
ATOM    335  CE2 PHE A  47      12.054  27.147   7.180  1.00 22.76           C  
ATOM    336  CZ  PHE A  47      11.068  26.774   8.103  1.00 13.24           C  
ATOM    337  N   GLU A  48      12.098  21.370   3.074  1.00 22.15           N  
ATOM    338  CA  GLU A  48      12.539  20.722   1.839  1.00 26.56           C  
ATOM    339  C   GLU A  48      11.322  20.351   0.988  1.00 25.47           C  
ATOM    340  O   GLU A  48      10.286  19.843   1.406  1.00 22.04           O  
ATOM    341  CB  GLU A  48      13.539  19.581   2.059  1.00 23.91           C  
ATOM    342  CG  GLU A  48      14.929  20.153   2.317  1.00 35.14           C  
ATOM    343  CD  GLU A  48      15.990  19.313   3.015  1.00 42.27           C  
ATOM    344  OE1 GLU A  48      15.716  18.097   3.203  1.00 39.14           O  
ATOM    345  OE2 GLU A  48      17.066  19.901   3.376  1.00 42.12           O  
ATOM    346  N   GLY A  49      11.495  20.716  -0.285  1.00 25.45           N  
ATOM    347  CA  GLY A  49      10.513  20.501  -1.335  1.00 23.62           C  
ATOM    348  C   GLY A  49       9.437  21.568  -1.384  1.00 24.99           C  
ATOM    349  O   GLY A  49       8.511  21.292  -2.153  1.00 24.44           O  
ATOM    350  N   PHE A  50       9.501  22.689  -0.655  1.00 25.43           N  
ATOM    351  CA  PHE A  50       8.453  23.702  -0.688  1.00 21.48           C  
ATOM    352  C   PHE A  50       8.862  24.958  -1.437  1.00 19.39           C  
ATOM    353  O   PHE A  50       9.998  25.434  -1.258  1.00 16.71           O  
ATOM    354  CB  PHE A  50       7.987  24.064   0.752  1.00 14.07           C  
ATOM    355  CG  PHE A  50       7.178  22.946   1.322  1.00 14.11           C  
ATOM    356  CD1 PHE A  50       5.841  22.764   0.952  1.00 12.30           C  
ATOM    357  CD2 PHE A  50       7.768  22.068   2.227  1.00 17.88           C  
ATOM    358  CE1 PHE A  50       5.162  21.674   1.481  1.00 16.02           C  
ATOM    359  CE2 PHE A  50       7.068  21.002   2.768  1.00 16.62           C  
ATOM    360  CZ  PHE A  50       5.745  20.794   2.389  1.00 14.57           C  
ATOM    361  N   ASP A  51       7.936  25.527  -2.245  1.00 15.85           N  
ATOM    362  CA  ASP A  51       8.250  26.748  -2.975  1.00 14.31           C  
ATOM    363  C   ASP A  51       8.098  27.983  -2.084  1.00 14.20           C  
ATOM    364  O   ASP A  51       8.738  29.025  -2.258  1.00 14.68           O  
ATOM    365  CB  ASP A  51       7.340  26.938  -4.232  1.00 16.19           C  
ATOM    366  CG  ASP A  51       7.509  25.751  -5.175  1.00 23.17           C  
ATOM    367  OD1 ASP A  51       8.637  25.470  -5.695  1.00 22.25           O  
ATOM    368  OD2 ASP A  51       6.521  25.017  -5.395  1.00 18.40           O  
ATOM    369  N   LEU A  52       7.168  27.829  -1.138  1.00 14.83           N  
ATOM    370  CA  LEU A  52       6.883  28.904  -0.211  1.00 15.68           C  
ATOM    371  C   LEU A  52       6.598  28.253   1.169  1.00 14.61           C  
ATOM    372  O   LEU A  52       5.938  27.225   1.268  1.00 16.58           O  
ATOM    373  CB  LEU A  52       5.573  29.572  -0.613  1.00 15.18           C  
ATOM    374  CG  LEU A  52       5.180  31.006  -0.384  1.00 20.01           C  
ATOM    375  CD1 LEU A  52       3.709  31.109  -0.014  1.00 18.94           C  
ATOM    376  CD2 LEU A  52       6.056  31.892   0.456  1.00 12.50           C  
ATOM    377  N   VAL A  53       7.107  28.905   2.206  1.00 17.35           N  
ATOM    378  CA  VAL A  53       6.907  28.446   3.601  1.00 15.40           C  
ATOM    379  C   VAL A  53       6.394  29.655   4.387  1.00 15.62           C  
ATOM    380  O   VAL A  53       7.004  30.761   4.366  1.00 13.34           O  
ATOM    381  CB  VAL A  53       8.183  27.826   4.214  1.00 23.32           C  
ATOM    382  CG1 VAL A  53       7.932  27.528   5.695  1.00 13.20           C  
ATOM    383  CG2 VAL A  53       8.683  26.546   3.521  1.00 15.35           C  
ATOM    384  N   LEU A  54       5.215  29.518   5.046  1.00 14.79           N  
ATOM    385  CA  LEU A  54       4.563  30.564   5.840  1.00 13.31           C  
ATOM    386  C   LEU A  54       4.544  30.086   7.304  1.00 13.16           C  
ATOM    387  O   LEU A  54       4.076  28.995   7.665  1.00 14.81           O  
ATOM    388  CB  LEU A  54       3.156  30.837   5.312  1.00 11.37           C  
ATOM    389  CG  LEU A  54       3.092  31.333   3.846  1.00  9.35           C  
ATOM    390  CD1 LEU A  54       1.583  31.558   3.544  1.00 11.84           C  
ATOM    391  CD2 LEU A  54       3.866  32.593   3.594  1.00  8.10           C  
ATOM    392  N   LEU A  55       5.124  30.909   8.169  1.00 13.84           N  
ATOM    393  CA  LEU A  55       5.269  30.591   9.612  1.00 12.59           C  
ATOM    394  C   LEU A  55       4.423  31.531  10.432  1.00  9.02           C  
ATOM    395  O   LEU A  55       4.571  32.775  10.349  1.00 12.02           O  
ATOM    396  CB  LEU A  55       6.777  30.740   9.924  1.00 13.75           C  
ATOM    397  CG  LEU A  55       7.717  29.567   9.934  1.00 21.66           C  
ATOM    398  CD1 LEU A  55       7.364  28.301   9.170  1.00 15.65           C  
ATOM    399  CD2 LEU A  55       9.170  29.960   9.647  1.00 24.30           C  
ATOM    400  N   GLY A  56       3.550  30.895  11.229  1.00 13.06           N  
ATOM    401  CA  GLY A  56       2.626  31.648  12.071  1.00  9.14           C  
ATOM    402  C   GLY A  56       2.910  31.459  13.571  1.00 11.51           C  
ATOM    403  O   GLY A  56       3.126  30.318  13.950  1.00 11.18           O  
ATOM    404  N   CYS A  57       2.922  32.527  14.339  1.00 12.33           N  
ATOM    405  CA  CYS A  57       3.219  32.456  15.790  1.00 13.79           C  
ATOM    406  C   CYS A  57       2.704  33.644  16.574  1.00  8.84           C  
ATOM    407  O   CYS A  57       2.904  34.844  16.274  1.00 12.01           O  
ATOM    408  CB  CYS A  57       4.779  32.309  15.926  1.00 11.36           C  
ATOM    409  SG  CYS A  57       5.223  31.892  17.667  1.00 13.50           S  
ATOM    410  N   SER A  58       1.972  33.354  17.687  1.00 14.10           N  
ATOM    411  CA  SER A  58       1.464  34.393  18.632  1.00 13.40           C  
ATOM    412  C   SER A  58       2.571  34.775  19.642  1.00 11.75           C  
ATOM    413  O   SER A  58       3.548  34.039  19.843  1.00 11.33           O  
ATOM    414  CB  SER A  58       0.153  34.010  19.361  1.00  7.32           C  
ATOM    415  OG  SER A  58       0.305  32.720  19.999  1.00 12.04           O  
ATOM    416  N   THR A  59       2.493  35.955  20.268  1.00  9.84           N  
ATOM    417  CA  THR A  59       3.436  36.551  21.192  1.00 12.32           C  
ATOM    418  C   THR A  59       2.849  36.495  22.639  1.00 17.25           C  
ATOM    419  O   THR A  59       1.651  36.653  22.922  1.00  8.12           O  
ATOM    420  CB  THR A  59       3.687  38.028  20.837  1.00 11.89           C  
ATOM    421  OG1 THR A  59       4.130  37.977  19.454  1.00 16.76           O  
ATOM    422  CG2 THR A  59       4.803  38.634  21.686  1.00 11.72           C  
ATOM    423  N   TRP A  60       3.725  36.117  23.558  1.00 14.15           N  
ATOM    424  CA  TRP A  60       3.482  35.864  24.979  1.00 16.76           C  
ATOM    425  C   TRP A  60       4.508  36.583  25.853  1.00 17.90           C  
ATOM    426  O   TRP A  60       5.415  37.257  25.329  1.00 13.29           O  
ATOM    427  CB  TRP A  60       3.462  34.296  25.204  1.00  7.81           C  
ATOM    428  CG  TRP A  60       2.269  33.701  24.512  1.00 11.61           C  
ATOM    429  CD1 TRP A  60       2.290  33.200  23.216  1.00 11.27           C  
ATOM    430  CD2 TRP A  60       0.899  33.675  24.926  1.00 14.30           C  
ATOM    431  NE1 TRP A  60       1.030  32.866  22.821  1.00 12.24           N  
ATOM    432  CE2 TRP A  60       0.144  33.133  23.868  1.00 13.78           C  
ATOM    433  CE3 TRP A  60       0.244  34.070  26.113  1.00  9.37           C  
ATOM    434  CZ2 TRP A  60      -1.223  32.932  23.934  1.00 11.49           C  
ATOM    435  CZ3 TRP A  60      -1.129  33.863  26.189  1.00  9.00           C  
ATOM    436  CH2 TRP A  60      -1.869  33.315  25.101  1.00 14.29           C  
ATOM    437  N   GLY A  61       4.388  36.455  27.193  1.00 14.79           N  
ATOM    438  CA  GLY A  61       5.384  37.158  28.006  1.00 14.60           C  
ATOM    439  C   GLY A  61       4.779  38.509  28.371  1.00 20.72           C  
ATOM    440  O   GLY A  61       3.828  39.132  27.912  1.00 19.15           O  
ATOM    441  N   ASP A  62       5.454  39.045  29.391  1.00 25.06           N  
ATOM    442  CA  ASP A  62       5.038  40.362  29.884  1.00 23.96           C  
ATOM    443  C   ASP A  62       6.085  41.370  29.466  1.00 28.48           C  
ATOM    444  O   ASP A  62       7.069  41.675  30.168  1.00 26.17           O  
ATOM    445  CB  ASP A  62       4.879  40.261  31.381  1.00 35.60           C  
ATOM    446  CG  ASP A  62       4.371  41.563  31.988  1.00 42.07           C  
ATOM    447  OD1 ASP A  62       3.816  42.426  31.262  1.00 46.07           O  
ATOM    448  OD2 ASP A  62       4.585  41.605  33.223  1.00 42.46           O  
ATOM    449  N   ASP A  63       5.915  41.872  28.243  1.00 36.06           N  
ATOM    450  CA  ASP A  63       6.854  42.842  27.632  1.00 42.24           C  
ATOM    451  C   ASP A  63       8.315  42.390  27.876  1.00 43.27           C  
ATOM    452  O   ASP A  63       9.305  42.910  28.408  1.00 40.47           O  
ATOM    453  CB  ASP A  63       6.503  44.261  28.037  1.00 52.78           C  
ATOM    454  CG  ASP A  63       5.166  44.956  27.956  1.00 58.52           C  
ATOM    455  OD1 ASP A  63       4.213  44.648  27.193  1.00 57.34           O  
ATOM    456  OD2 ASP A  63       5.036  45.958  28.748  1.00 62.32           O  
ATOM    457  N   SER A  64       8.555  41.161  27.424  1.00 40.36           N  
ATOM    458  CA  SER A  64       9.701  40.284  27.394  1.00 33.69           C  
ATOM    459  C   SER A  64       9.148  39.188  26.440  1.00 33.26           C  
ATOM    460  O   SER A  64       8.459  38.291  26.928  1.00 33.77           O  
ATOM    461  CB  SER A  64      10.089  39.765  28.740  1.00 18.25           C  
ATOM    462  OG  SER A  64      11.321  39.104  28.662  1.00 23.38           O  
ATOM    463  N   ILE A  65       9.425  39.436  25.162  1.00 31.28           N  
ATOM    464  CA  ILE A  65       8.887  38.546  24.136  1.00 30.91           C  
ATOM    465  C   ILE A  65       9.182  37.082  24.437  1.00 26.51           C  
ATOM    466  O   ILE A  65      10.287  36.646  24.712  1.00 26.14           O  
ATOM    467  CB  ILE A  65       9.362  38.890  22.709  1.00 23.55           C  
ATOM    468  CG1 ILE A  65       8.837  40.255  22.239  1.00 20.55           C  
ATOM    469  CG2 ILE A  65       8.982  37.855  21.648  1.00 25.67           C  
ATOM    470  CD1 ILE A  65       9.792  40.769  21.179  1.00 16.61           C  
ATOM    471  N   GLU A  66       8.137  36.290  24.387  1.00 22.86           N  
ATOM    472  CA  GLU A  66       8.204  34.830  24.568  1.00 22.81           C  
ATOM    473  C   GLU A  66       7.415  34.278  23.334  1.00 20.55           C  
ATOM    474  O   GLU A  66       6.339  34.806  23.021  1.00 19.69           O  
ATOM    475  CB  GLU A  66       7.606  34.343  25.882  1.00 26.32           C  
ATOM    476  CG  GLU A  66       8.359  33.921  27.113  1.00 48.80           C  
ATOM    477  CD  GLU A  66       7.938  34.494  28.458  1.00 49.68           C  
ATOM    478  OE1 GLU A  66       6.969  33.956  29.038  1.00 45.93           O  
ATOM    479  OE2 GLU A  66       8.544  35.465  29.011  1.00 51.18           O  
ATOM    480  N   LEU A  67       7.882  33.267  22.621  1.00 20.75           N  
ATOM    481  CA  LEU A  67       7.142  32.676  21.500  1.00 18.92           C  
ATOM    482  C   LEU A  67       6.078  31.696  21.988  1.00 18.54           C  
ATOM    483  O   LEU A  67       6.221  31.155  23.100  1.00 16.14           O  
ATOM    484  CB  LEU A  67       8.147  31.940  20.601  1.00 17.09           C  
ATOM    485  CG  LEU A  67       8.814  32.719  19.468  1.00 21.10           C  
ATOM    486  CD1 LEU A  67       9.295  34.123  19.829  1.00 17.74           C  
ATOM    487  CD2 LEU A  67       9.896  31.813  18.865  1.00 20.43           C  
ATOM    488  N   GLN A  68       5.001  31.476  21.238  1.00 16.75           N  
ATOM    489  CA  GLN A  68       3.957  30.513  21.567  1.00 16.66           C  
ATOM    490  C   GLN A  68       4.668  29.169  21.841  1.00 15.62           C  
ATOM    491  O   GLN A  68       5.621  28.779  21.154  1.00 13.40           O  
ATOM    492  CB  GLN A  68       2.896  30.430  20.485  1.00 13.61           C  
ATOM    493  CG  GLN A  68       1.679  29.590  20.685  1.00  9.15           C  
ATOM    494  CD  GLN A  68       1.776  28.096  20.646  1.00  9.24           C  
ATOM    495  OE1 GLN A  68       1.033  27.304  21.321  1.00 13.20           O  
ATOM    496  NE2 GLN A  68       2.658  27.611  19.808  1.00 10.14           N  
ATOM    497  N   ASP A  69       4.226  28.500  22.919  1.00 13.63           N  
ATOM    498  CA  ASP A  69       4.802  27.268  23.444  1.00 13.80           C  
ATOM    499  C   ASP A  69       5.214  26.169  22.493  1.00 15.87           C  
ATOM    500  O   ASP A  69       6.350  25.624  22.542  1.00 14.61           O  
ATOM    501  CB  ASP A  69       3.876  26.719  24.569  1.00 10.81           C  
ATOM    502  CG  ASP A  69       4.515  25.597  25.331  1.00 15.81           C  
ATOM    503  OD1 ASP A  69       5.534  25.801  26.007  1.00 20.85           O  
ATOM    504  OD2 ASP A  69       4.056  24.460  25.187  1.00 19.51           O  
ATOM    505  N   ASP A  70       4.323  25.786  21.596  1.00 15.64           N  
ATOM    506  CA  ASP A  70       4.545  24.762  20.595  1.00 13.07           C  
ATOM    507  C   ASP A  70       5.532  25.233  19.540  1.00 13.90           C  
ATOM    508  O   ASP A  70       6.164  24.323  18.982  1.00 19.31           O  
ATOM    509  CB  ASP A  70       3.207  24.462  19.934  1.00 14.93           C  
ATOM    510  CG  ASP A  70       2.148  23.933  20.858  1.00 16.36           C  
ATOM    511  OD1 ASP A  70       2.453  22.978  21.604  1.00 20.35           O  
ATOM    512  OD2 ASP A  70       0.964  24.310  20.874  1.00 17.12           O  
ATOM    513  N   PHE A  71       5.663  26.530  19.270  1.00 13.62           N  
ATOM    514  CA  PHE A  71       6.597  26.991  18.254  1.00 11.23           C  
ATOM    515  C   PHE A  71       8.037  27.049  18.708  1.00 17.56           C  
ATOM    516  O   PHE A  71       9.024  27.007  17.942  1.00 14.15           O  
ATOM    517  CB  PHE A  71       6.126  28.407  17.875  1.00 10.88           C  
ATOM    518  CG  PHE A  71       6.561  28.698  16.460  1.00 15.05           C  
ATOM    519  CD1 PHE A  71       7.803  29.240  16.206  1.00 18.27           C  
ATOM    520  CD2 PHE A  71       5.705  28.368  15.406  1.00 13.16           C  
ATOM    521  CE1 PHE A  71       8.256  29.492  14.910  1.00 17.01           C  
ATOM    522  CE2 PHE A  71       6.145  28.629  14.116  1.00 17.57           C  
ATOM    523  CZ  PHE A  71       7.402  29.186  13.866  1.00 13.24           C  
ATOM    524  N   ILE A  72       8.279  27.153  20.038  1.00 18.59           N  
ATOM    525  CA  ILE A  72       9.639  27.260  20.580  1.00 16.77           C  
ATOM    526  C   ILE A  72      10.637  26.265  20.054  1.00 18.35           C  
ATOM    527  O   ILE A  72      11.720  26.654  19.552  1.00 19.43           O  
ATOM    528  CB  ILE A  72       9.647  27.366  22.125  1.00 19.65           C  
ATOM    529  CG1 ILE A  72       8.989  28.668  22.552  1.00 15.33           C  
ATOM    530  CG2 ILE A  72      11.057  27.324  22.737  1.00 18.74           C  
ATOM    531  CD1 ILE A  72       8.658  28.632  24.063  1.00 14.68           C  
ATOM    532  N   PRO A  73      10.401  24.960  20.109  1.00 20.08           N  
ATOM    533  CA  PRO A  73      11.283  23.915  19.590  1.00 21.89           C  
ATOM    534  C   PRO A  73      11.678  24.121  18.118  1.00 22.99           C  
ATOM    535  O   PRO A  73      12.873  23.993  17.762  1.00 16.25           O  
ATOM    536  CB  PRO A  73      10.618  22.546  19.843  1.00 17.90           C  
ATOM    537  CG  PRO A  73       9.546  22.939  20.836  1.00 18.32           C  
ATOM    538  CD  PRO A  73       9.184  24.400  20.684  1.00 20.11           C  
ATOM    539  N   LEU A  74      10.703  24.461  17.263  1.00 21.37           N  
ATOM    540  CA  LEU A  74      11.002  24.732  15.841  1.00 18.93           C  
ATOM    541  C   LEU A  74      11.892  25.946  15.701  1.00 20.45           C  
ATOM    542  O   LEU A  74      12.907  25.902  14.987  1.00 19.08           O  
ATOM    543  CB  LEU A  74       9.697  24.902  15.054  1.00 19.25           C  
ATOM    544  CG  LEU A  74       9.909  25.243  13.547  1.00 17.71           C  
ATOM    545  CD1 LEU A  74      10.712  24.155  12.861  1.00 19.27           C  
ATOM    546  CD2 LEU A  74       8.485  25.447  13.056  1.00 14.79           C  
ATOM    547  N   PHE A  75      11.567  27.064  16.405  1.00 16.33           N  
ATOM    548  CA  PHE A  75      12.391  28.260  16.346  1.00 12.95           C  
ATOM    549  C   PHE A  75      13.815  27.891  16.769  1.00 20.84           C  
ATOM    550  O   PHE A  75      14.819  28.325  16.186  1.00 19.22           O  
ATOM    551  CB  PHE A  75      11.893  29.398  17.272  1.00 15.68           C  
ATOM    552  CG  PHE A  75      12.679  30.688  17.281  1.00 20.79           C  
ATOM    553  CD1 PHE A  75      12.463  31.709  16.356  1.00 20.21           C  
ATOM    554  CD2 PHE A  75      13.673  30.925  18.246  1.00 26.22           C  
ATOM    555  CE1 PHE A  75      13.146  32.898  16.374  1.00 18.96           C  
ATOM    556  CE2 PHE A  75      14.377  32.120  18.292  1.00 20.51           C  
ATOM    557  CZ  PHE A  75      14.120  33.120  17.355  1.00 25.49           C  
ATOM    558  N   ASP A  76      13.947  27.078  17.841  1.00 19.54           N  
ATOM    559  CA  ASP A  76      15.269  26.684  18.322  1.00 26.12           C  
ATOM    560  C   ASP A  76      16.108  25.878  17.326  1.00 26.43           C  
ATOM    561  O   ASP A  76      17.343  25.939  17.385  1.00 28.29           O  
ATOM    562  CB  ASP A  76      15.163  25.912  19.654  1.00 26.26           C  
ATOM    563  CG  ASP A  76      14.921  26.796  20.877  1.00 32.04           C  
ATOM    564  OD1 ASP A  76      15.147  28.045  20.817  1.00 26.24           O  
ATOM    565  OD2 ASP A  76      14.494  26.152  21.895  1.00 36.64           O  
ATOM    566  N   SER A  77      15.436  25.109  16.475  1.00 24.12           N  
ATOM    567  CA  SER A  77      16.167  24.324  15.471  1.00 23.21           C  
ATOM    568  C   SER A  77      15.930  24.838  14.066  1.00 19.95           C  
ATOM    569  O   SER A  77      16.011  24.056  13.124  1.00 21.31           O  
ATOM    570  CB  SER A  77      15.646  22.880  15.603  1.00 22.11           C  
ATOM    571  OG  SER A  77      15.957  22.553  16.965  1.00 33.85           O  
ATOM    572  N   LEU A  78      15.640  26.113  13.846  1.00 18.28           N  
ATOM    573  CA  LEU A  78      15.372  26.667  12.538  1.00 17.12           C  
ATOM    574  C   LEU A  78      16.522  26.526  11.558  1.00 22.71           C  
ATOM    575  O   LEU A  78      16.340  26.523  10.337  1.00 19.39           O  
ATOM    576  CB  LEU A  78      15.023  28.141  12.626  1.00 18.01           C  
ATOM    577  CG  LEU A  78      13.585  28.602  12.491  1.00 19.73           C  
ATOM    578  CD1 LEU A  78      13.668  30.098  12.211  1.00 20.94           C  
ATOM    579  CD2 LEU A  78      12.773  27.784  11.531  1.00  9.46           C  
ATOM    580  N   GLU A  79      17.743  26.422  12.068  1.00 23.23           N  
ATOM    581  CA  GLU A  79      18.969  26.242  11.321  1.00 26.93           C  
ATOM    582  C   GLU A  79      18.992  24.856  10.658  1.00 25.31           C  
ATOM    583  O   GLU A  79      19.836  24.662   9.750  1.00 28.09           O  
ATOM    584  CB  GLU A  79      20.263  26.491  12.123  1.00 26.12           C  
ATOM    585  CG  GLU A  79      20.593  25.548  13.244  1.00 42.49           C  
ATOM    586  CD  GLU A  79      19.744  25.494  14.505  1.00 43.90           C  
ATOM    587  OE1 GLU A  79      18.976  26.460  14.791  1.00 38.35           O  
ATOM    588  OE2 GLU A  79      19.866  24.465  15.241  1.00 43.54           O  
ATOM    589  N   GLU A  80      18.111  23.923  11.005  1.00 21.29           N  
ATOM    590  CA  GLU A  80      18.070  22.609  10.393  1.00 24.10           C  
ATOM    591  C   GLU A  80      16.932  22.448   9.354  1.00 23.32           C  
ATOM    592  O   GLU A  80      16.804  21.378   8.737  1.00 20.67           O  
ATOM    593  CB  GLU A  80      17.820  21.500  11.410  1.00 26.63           C  
ATOM    594  CG  GLU A  80      18.700  21.201  12.612  1.00 49.64           C  
ATOM    595  CD  GLU A  80      17.957  20.152  13.457  1.00 62.32           C  
ATOM    596  OE1 GLU A  80      17.906  18.965  13.026  1.00 72.13           O  
ATOM    597  OE2 GLU A  80      17.384  20.480  14.522  1.00 69.37           O  
ATOM    598  N   THR A  81      16.079  23.456   9.166  1.00 22.22           N  
ATOM    599  CA  THR A  81      14.921  23.341   8.291  1.00 18.26           C  
ATOM    600  C   THR A  81      15.171  23.450   6.788  1.00 21.61           C  
ATOM    601  O   THR A  81      14.302  23.050   5.995  1.00 22.09           O  
ATOM    602  CB  THR A  81      13.884  24.411   8.728  1.00 15.95           C  
ATOM    603  OG1 THR A  81      14.549  25.685   8.559  1.00 15.10           O  
ATOM    604  CG2 THR A  81      13.307  24.256  10.127  1.00 14.47           C  
ATOM    605  N   GLY A  82      16.315  24.011   6.420  1.00 22.06           N  
ATOM    606  CA  GLY A  82      16.610  24.227   4.999  1.00 23.39           C  
ATOM    607  C   GLY A  82      15.988  25.567   4.575  1.00 20.03           C  
ATOM    608  O   GLY A  82      15.306  25.647   3.535  1.00 22.28           O  
ATOM    609  N   ALA A  83      16.200  26.628   5.325  1.00 17.37           N  
ATOM    610  CA  ALA A  83      15.656  27.954   5.060  1.00 16.27           C  
ATOM    611  C   ALA A  83      16.538  28.751   4.126  1.00 14.45           C  
ATOM    612  O   ALA A  83      16.145  29.758   3.572  1.00 19.04           O  
ATOM    613  CB  ALA A  83      15.614  28.798   6.363  1.00 21.87           C  
ATOM    614  N   GLN A  84      17.802  28.383   3.969  1.00 16.26           N  
ATOM    615  CA  GLN A  84      18.697  29.116   3.096  1.00 18.84           C  
ATOM    616  C   GLN A  84      18.123  29.182   1.683  1.00 19.91           C  
ATOM    617  O   GLN A  84      17.809  28.131   1.106  1.00 19.89           O  
ATOM    618  CB  GLN A  84      20.039  28.375   3.117  1.00 24.79           C  
ATOM    619  CG  GLN A  84      21.205  28.903   2.342  1.00 39.36           C  
ATOM    620  CD  GLN A  84      21.833  30.238   2.639  1.00 52.59           C  
ATOM    621  OE1 GLN A  84      21.619  31.233   1.895  1.00 61.51           O  
ATOM    622  NE2 GLN A  84      22.653  30.326   3.699  1.00 56.20           N  
ATOM    623  N   GLY A  85      17.933  30.363   1.107  1.00 22.13           N  
ATOM    624  CA  GLY A  85      17.398  30.508  -0.253  1.00 24.35           C  
ATOM    625  C   GLY A  85      15.918  30.238  -0.407  1.00 22.39           C  
ATOM    626  O   GLY A  85      15.396  30.301  -1.517  1.00 24.39           O  
ATOM    627  N   ARG A  86      15.226  29.928   0.674  1.00 22.32           N  
ATOM    628  CA  ARG A  86      13.805  29.618   0.697  1.00 19.56           C  
ATOM    629  C   ARG A  86      12.967  30.880   0.789  1.00 20.88           C  
ATOM    630  O   ARG A  86      13.335  31.804   1.551  1.00 19.30           O  
ATOM    631  CB  ARG A  86      13.471  28.729   1.891  1.00 18.63           C  
ATOM    632  CG  ARG A  86      12.067  28.211   1.972  1.00 19.52           C  
ATOM    633  CD  ARG A  86      11.904  26.885   1.258  1.00 24.30           C  
ATOM    634  NE  ARG A  86      13.037  25.988   1.451  1.00 25.86           N  
ATOM    635  CZ  ARG A  86      13.306  24.914   0.730  1.00 26.55           C  
ATOM    636  NH1 ARG A  86      12.594  24.500  -0.303  1.00 18.08           N  
ATOM    637  NH2 ARG A  86      14.346  24.131   0.993  1.00 28.13           N  
ATOM    638  N   LYS A  87      11.885  30.859  -0.031  1.00 15.85           N  
ATOM    639  CA  LYS A  87      10.962  31.995  -0.013  1.00 16.26           C  
ATOM    640  C   LYS A  87      10.000  31.719   1.174  1.00 14.68           C  
ATOM    641  O   LYS A  87       9.385  30.638   1.230  1.00 12.11           O  
ATOM    642  CB  LYS A  87      10.088  32.128  -1.285  1.00 21.25           C  
ATOM    643  CG  LYS A  87      10.991  32.580  -2.442  1.00 22.93           C  
ATOM    644  CD  LYS A  87      10.255  32.546  -3.772  1.00 31.37           C  
ATOM    645  CE  LYS A  87      11.252  32.076  -4.820  1.00 44.79           C  
ATOM    646  NZ  LYS A  87      11.490  33.105  -5.870  1.00 59.03           N  
ATOM    647  N   VAL A  88      10.020  32.721   2.059  1.00 16.58           N  
ATOM    648  CA  VAL A  88       9.258  32.696   3.304  1.00 16.63           C  
ATOM    649  C   VAL A  88       8.554  34.000   3.627  1.00 14.35           C  
ATOM    650  O   VAL A  88       8.870  35.120   3.184  1.00 18.98           O  
ATOM    651  CB  VAL A  88      10.226  32.347   4.508  1.00 14.67           C  
ATOM    652  CG1 VAL A  88      11.181  31.171   4.301  1.00 13.89           C  
ATOM    653  CG2 VAL A  88      11.097  33.539   4.869  1.00 14.77           C  
ATOM    654  N   ALA A  89       7.518  33.952   4.487  1.00 14.31           N  
ATOM    655  CA  ALA A  89       6.799  35.140   4.965  1.00 15.43           C  
ATOM    656  C   ALA A  89       6.225  34.714   6.355  1.00 14.09           C  
ATOM    657  O   ALA A  89       5.953  33.526   6.575  1.00 11.69           O  
ATOM    658  CB  ALA A  89       5.739  35.738   4.060  1.00 14.79           C  
ATOM    659  N   CYS A  90       6.075  35.689   7.260  1.00 15.80           N  
ATOM    660  CA  CYS A  90       5.558  35.341   8.609  1.00 16.72           C  
ATOM    661  C   CYS A  90       4.279  36.057   8.943  1.00 13.58           C  
ATOM    662  O   CYS A  90       3.955  37.104   8.391  1.00 14.26           O  
ATOM    663  CB  CYS A  90       6.637  35.728   9.642  1.00 12.88           C  
ATOM    664  SG  CYS A  90       8.260  34.970   9.380  1.00 16.61           S  
ATOM    665  N   PHE A  91       3.554  35.516   9.939  1.00 13.60           N  
ATOM    666  CA  PHE A  91       2.280  36.073  10.384  1.00 14.60           C  
ATOM    667  C   PHE A  91       2.060  35.737  11.873  1.00 14.87           C  
ATOM    668  O   PHE A  91       2.735  34.841  12.401  1.00 15.38           O  
ATOM    669  CB  PHE A  91       1.052  35.486   9.611  1.00 12.44           C  
ATOM    670  CG  PHE A  91       0.750  33.986   9.590  1.00 10.63           C  
ATOM    671  CD1 PHE A  91       1.434  33.099   8.787  1.00 12.27           C  
ATOM    672  CD2 PHE A  91      -0.285  33.454  10.370  1.00  7.87           C  
ATOM    673  CE1 PHE A  91       1.175  31.728   8.770  1.00 13.48           C  
ATOM    674  CE2 PHE A  91      -0.555  32.103  10.378  1.00  9.70           C  
ATOM    675  CZ  PHE A  91       0.171  31.215   9.563  1.00 13.68           C  
ATOM    676  N   GLY A  92       1.095  36.375  12.494  1.00 19.04           N  
ATOM    677  CA  GLY A  92       0.794  36.037  13.895  1.00 18.92           C  
ATOM    678  C   GLY A  92      -0.219  37.029  14.438  1.00 14.88           C  
ATOM    679  O   GLY A  92      -0.527  38.061  13.857  1.00 11.95           O  
ATOM    680  N   CYS A  93      -0.701  36.662  15.633  1.00 15.04           N  
ATOM    681  CA  CYS A  93      -1.673  37.465  16.385  1.00 16.32           C  
ATOM    682  C   CYS A  93      -1.004  38.015  17.657  1.00 13.05           C  
ATOM    683  O   CYS A  93      -0.080  37.390  18.189  1.00 13.02           O  
ATOM    684  CB  CYS A  93      -2.905  36.627  16.734  1.00 20.71           C  
ATOM    685  SG  CYS A  93      -3.862  36.155  15.270  1.00 16.45           S  
ATOM    686  N   GLY A  94      -1.457  39.207  18.045  1.00 14.40           N  
ATOM    687  CA  GLY A  94      -0.926  39.921  19.201  1.00 13.94           C  
ATOM    688  C   GLY A  94      -1.920  40.990  19.644  1.00 15.92           C  
ATOM    689  O   GLY A  94      -3.142  40.931  19.394  1.00 14.79           O  
ATOM    690  N   ALA A  95      -1.371  41.965  20.370  1.00 16.25           N  
ATOM    691  CA  ALA A  95      -2.182  43.069  20.925  1.00 21.77           C  
ATOM    692  C   ALA A  95      -1.427  44.368  20.706  1.00 19.89           C  
ATOM    693  O   ALA A  95      -0.326  44.600  21.201  1.00 22.31           O  
ATOM    694  CB  ALA A  95      -2.461  42.859  22.412  1.00 23.94           C  
ATOM    695  N   SER A  96      -1.997  45.224  19.847  1.00 20.88           N  
ATOM    696  CA  SER A  96      -1.402  46.479  19.449  1.00 26.84           C  
ATOM    697  C   SER A  96      -1.071  47.440  20.573  1.00 30.95           C  
ATOM    698  O   SER A  96      -0.190  48.297  20.425  1.00 31.01           O  
ATOM    699  CB  SER A  96      -2.155  47.182  18.309  1.00 32.87           C  
ATOM    700  OG  SER A  96      -3.182  48.033  18.765  1.00 53.85           O  
ATOM    701  N   SER A  97      -1.695  47.309  21.725  1.00 35.72           N  
ATOM    702  CA  SER A  97      -1.571  48.014  22.970  1.00 35.42           C  
ATOM    703  C   SER A  97      -0.228  47.683  23.649  1.00 35.51           C  
ATOM    704  O   SER A  97       0.340  48.532  24.351  1.00 39.10           O  
ATOM    705  CB  SER A  97      -2.722  47.598  23.933  1.00 33.65           C  
ATOM    706  OG  SER A  97      -3.779  46.801  23.374  1.00 47.07           O  
ATOM    707  N   TYR A  98       0.326  46.475  23.470  1.00 32.66           N  
ATOM    708  CA  TYR A  98       1.561  46.040  24.112  1.00 29.62           C  
ATOM    709  C   TYR A  98       2.866  46.621  23.620  1.00 29.71           C  
ATOM    710  O   TYR A  98       2.896  47.183  22.545  1.00 30.16           O  
ATOM    711  CB  TYR A  98       1.674  44.500  24.110  1.00 27.59           C  
ATOM    712  CG  TYR A  98       0.510  43.929  24.888  1.00 26.85           C  
ATOM    713  CD1 TYR A  98      -0.553  44.672  25.396  1.00 30.98           C  
ATOM    714  CD2 TYR A  98       0.491  42.581  25.111  1.00 26.45           C  
ATOM    715  CE1 TYR A  98      -1.594  44.104  26.074  1.00 35.34           C  
ATOM    716  CE2 TYR A  98      -0.525  41.953  25.786  1.00 27.67           C  
ATOM    717  CZ  TYR A  98      -1.564  42.723  26.268  1.00 36.04           C  
ATOM    718  OH  TYR A  98      -2.604  42.085  26.924  1.00 37.41           O  
ATOM    719  N   GLU A  99       3.926  46.536  24.409  1.00 31.01           N  
ATOM    720  CA  GLU A  99       5.249  47.062  24.028  1.00 33.11           C  
ATOM    721  C   GLU A  99       5.741  46.370  22.753  1.00 28.67           C  
ATOM    722  O   GLU A  99       6.087  47.126  21.822  1.00 31.78           O  
ATOM    723  CB  GLU A  99       6.222  46.948  25.191  1.00 35.10           C  
ATOM    724  CG  GLU A  99       7.569  47.616  25.222  1.00 43.99           C  
ATOM    725  CD  GLU A  99       7.625  49.091  24.878  1.00 59.58           C  
ATOM    726  OE1 GLU A  99       6.790  49.917  25.341  1.00 67.79           O  
ATOM    727  OE2 GLU A  99       8.544  49.474  24.089  1.00 65.71           O  
ATOM    728  N   TYR A 100       5.757  45.034  22.711  1.00 25.77           N  
ATOM    729  CA  TYR A 100       6.197  44.304  21.509  1.00 18.65           C  
ATOM    730  C   TYR A 100       4.978  43.650  20.851  1.00 15.33           C  
ATOM    731  O   TYR A 100       4.723  42.451  20.985  1.00 20.29           O  
ATOM    732  CB  TYR A 100       7.258  43.259  21.887  1.00 18.96           C  
ATOM    733  CG  TYR A 100       8.390  43.880  22.705  1.00 25.27           C  
ATOM    734  CD1 TYR A 100       9.231  44.843  22.159  1.00 24.39           C  
ATOM    735  CD2 TYR A 100       8.586  43.537  24.034  1.00 27.71           C  
ATOM    736  CE1 TYR A 100      10.245  45.457  22.872  1.00 27.54           C  
ATOM    737  CE2 TYR A 100       9.574  44.152  24.780  1.00 31.85           C  
ATOM    738  CZ  TYR A 100      10.394  45.118  24.212  1.00 33.44           C  
ATOM    739  OH  TYR A 100      11.387  45.700  24.999  1.00 30.99           O  
ATOM    740  N   PHE A 101       4.226  44.451  20.118  1.00 16.17           N  
ATOM    741  CA  PHE A 101       3.050  44.005  19.368  1.00 20.34           C  
ATOM    742  C   PHE A 101       3.529  43.003  18.296  1.00 19.90           C  
ATOM    743  O   PHE A 101       4.347  43.328  17.411  1.00 20.29           O  
ATOM    744  CB  PHE A 101       2.351  45.140  18.642  1.00 20.88           C  
ATOM    745  CG  PHE A 101       1.253  44.776  17.667  1.00 22.66           C  
ATOM    746  CD1 PHE A 101       0.316  43.799  17.963  1.00 19.70           C  
ATOM    747  CD2 PHE A 101       1.164  45.415  16.437  1.00 19.32           C  
ATOM    748  CE1 PHE A 101      -0.709  43.465  17.120  1.00 15.28           C  
ATOM    749  CE2 PHE A 101       0.128  45.115  15.584  1.00 19.26           C  
ATOM    750  CZ  PHE A 101      -0.794  44.137  15.915  1.00 16.11           C  
ATOM    751  N   CYS A 102       3.053  41.769  18.391  1.00 15.23           N  
ATOM    752  CA  CYS A 102       3.488  40.702  17.489  1.00 11.68           C  
ATOM    753  C   CYS A 102       4.992  40.616  17.501  1.00 13.82           C  
ATOM    754  O   CYS A 102       5.588  40.294  16.459  1.00 16.64           O  
ATOM    755  CB  CYS A 102       2.901  40.708  16.071  1.00  7.56           C  
ATOM    756  SG  CYS A 102       1.128  40.464  16.063  1.00 13.16           S  
ATOM    757  N   GLY A 103       5.700  40.793  18.629  1.00 11.79           N  
ATOM    758  CA  GLY A 103       7.151  40.704  18.686  1.00  6.67           C  
ATOM    759  C   GLY A 103       7.576  39.313  18.280  1.00  9.86           C  
ATOM    760  O   GLY A 103       8.774  39.173  17.857  1.00 11.36           O  
ATOM    761  N   ALA A 104       6.768  38.243  18.373  1.00 12.20           N  
ATOM    762  CA  ALA A 104       7.236  36.937  17.917  1.00 12.95           C  
ATOM    763  C   ALA A 104       7.399  36.953  16.359  1.00 17.78           C  
ATOM    764  O   ALA A 104       8.342  36.244  15.939  1.00 16.46           O  
ATOM    765  CB  ALA A 104       6.375  35.748  18.264  1.00 14.41           C  
ATOM    766  N   VAL A 105       6.576  37.663  15.588  1.00 16.36           N  
ATOM    767  CA  VAL A 105       6.732  37.746  14.131  1.00 13.12           C  
ATOM    768  C   VAL A 105       8.062  38.408  13.823  1.00 14.71           C  
ATOM    769  O   VAL A 105       8.754  37.909  12.944  1.00 16.81           O  
ATOM    770  CB  VAL A 105       5.576  38.499  13.441  1.00 18.79           C  
ATOM    771  CG1 VAL A 105       5.851  38.620  11.949  1.00 13.75           C  
ATOM    772  CG2 VAL A 105       4.280  37.793  13.816  1.00 12.66           C  
ATOM    773  N   ASP A 106       8.510  39.499  14.470  1.00 14.27           N  
ATOM    774  CA  ASP A 106       9.792  40.124  14.229  1.00 13.35           C  
ATOM    775  C   ASP A 106      10.988  39.235  14.515  1.00 17.52           C  
ATOM    776  O   ASP A 106      12.012  39.244  13.832  1.00 17.20           O  
ATOM    777  CB  ASP A 106      10.113  41.322  15.129  1.00 19.52           C  
ATOM    778  CG  ASP A 106       9.013  42.344  15.166  1.00 27.85           C  
ATOM    779  OD1 ASP A 106       8.297  42.254  14.168  1.00 40.03           O  
ATOM    780  OD2 ASP A 106       8.772  43.149  16.073  1.00 32.26           O  
ATOM    781  N   ALA A 107      10.918  38.480  15.635  1.00 18.21           N  
ATOM    782  CA  ALA A 107      11.972  37.588  16.045  1.00 16.59           C  
ATOM    783  C   ALA A 107      12.189  36.449  15.050  1.00 14.48           C  
ATOM    784  O   ALA A 107      13.335  36.093  14.741  1.00 12.72           O  
ATOM    785  CB  ALA A 107      11.631  36.972  17.420  1.00 13.85           C  
ATOM    786  N   ILE A 108      11.072  35.885  14.599  1.00 13.28           N  
ATOM    787  CA  ILE A 108      11.140  34.770  13.607  1.00 14.93           C  
ATOM    788  C   ILE A 108      11.689  35.317  12.279  1.00 15.59           C  
ATOM    789  O   ILE A 108      12.576  34.691  11.677  1.00 15.15           O  
ATOM    790  CB  ILE A 108       9.787  34.054  13.434  1.00 14.66           C  
ATOM    791  CG1 ILE A 108       9.342  33.351  14.764  1.00 12.65           C  
ATOM    792  CG2 ILE A 108       9.812  32.992  12.310  1.00 12.56           C  
ATOM    793  CD1 ILE A 108       7.842  33.218  14.847  1.00 13.94           C  
ATOM    794  N   GLU A 109      11.234  36.471  11.777  1.00 17.35           N  
ATOM    795  CA  GLU A 109      11.724  37.108  10.555  1.00 16.84           C  
ATOM    796  C   GLU A 109      13.224  37.376  10.649  1.00 18.22           C  
ATOM    797  O   GLU A 109      13.993  37.053   9.743  1.00 18.08           O  
ATOM    798  CB  GLU A 109      11.060  38.480  10.287  1.00 15.53           C  
ATOM    799  CG  GLU A 109       9.595  38.273   9.913  1.00 17.86           C  
ATOM    800  CD  GLU A 109       9.005  39.486   9.231  1.00 25.82           C  
ATOM    801  OE1 GLU A 109       9.720  40.482   9.315  1.00 27.68           O  
ATOM    802  OE2 GLU A 109       7.884  39.377   8.695  1.00 26.36           O  
ATOM    803  N   GLU A 110      13.686  37.960  11.764  1.00 21.22           N  
ATOM    804  CA  GLU A 110      15.111  38.233  11.962  1.00 21.17           C  
ATOM    805  C   GLU A 110      15.970  36.992  11.916  1.00 17.48           C  
ATOM    806  O   GLU A 110      17.077  37.061  11.337  1.00 21.35           O  
ATOM    807  CB  GLU A 110      15.360  39.082  13.210  1.00 20.67           C  
ATOM    808  CG  GLU A 110      16.833  39.378  13.472  1.00 32.15           C  
ATOM    809  CD  GLU A 110      17.175  40.849  13.560  1.00 42.74           C  
ATOM    810  OE1 GLU A 110      16.256  41.656  13.847  1.00 48.15           O  
ATOM    811  OE2 GLU A 110      18.330  41.293  13.334  1.00 46.94           O  
ATOM    812  N   LYS A 111      15.592  35.846  12.488  1.00 17.56           N  
ATOM    813  CA  LYS A 111      16.358  34.629  12.452  1.00 16.63           C  
ATOM    814  C   LYS A 111      16.339  34.090  11.002  1.00 18.09           C  
ATOM    815  O   LYS A 111      17.371  33.642  10.498  1.00 18.20           O  
ATOM    816  CB  LYS A 111      15.814  33.537  13.387  1.00 14.56           C  
ATOM    817  CG  LYS A 111      16.787  32.378  13.465  1.00 15.85           C  
ATOM    818  CD  LYS A 111      16.340  31.417  14.558  1.00 21.54           C  
ATOM    819  CE  LYS A 111      17.620  30.866  15.192  1.00 30.18           C  
ATOM    820  NZ  LYS A 111      17.369  29.777  16.195  1.00 26.12           N  
ATOM    821  N   LEU A 112      15.165  34.103  10.354  1.00 15.74           N  
ATOM    822  CA  LEU A 112      15.102  33.601   8.952  1.00 17.01           C  
ATOM    823  C   LEU A 112      16.058  34.383   8.053  1.00 17.73           C  
ATOM    824  O   LEU A 112      16.755  33.752   7.245  1.00 19.71           O  
ATOM    825  CB  LEU A 112      13.652  33.688   8.440  1.00 11.95           C  
ATOM    826  CG  LEU A 112      12.696  32.638   8.998  1.00 11.14           C  
ATOM    827  CD1 LEU A 112      11.254  33.007   8.626  1.00 16.12           C  
ATOM    828  CD2 LEU A 112      13.044  31.219   8.574  1.00 12.23           C  
ATOM    829  N   LYS A 113      16.099  35.712   8.173  1.00 20.50           N  
ATOM    830  CA  LYS A 113      16.948  36.635   7.448  1.00 23.12           C  
ATOM    831  C   LYS A 113      18.418  36.229   7.667  1.00 27.63           C  
ATOM    832  O   LYS A 113      19.199  36.112   6.711  1.00 24.54           O  
ATOM    833  CB  LYS A 113      16.840  38.090   7.870  1.00 29.33           C  
ATOM    834  CG  LYS A 113      16.121  39.217   7.203  1.00 46.21           C  
ATOM    835  CD  LYS A 113      14.648  39.380   7.528  1.00 63.51           C  
ATOM    836  CE  LYS A 113      14.032  40.722   7.875  1.00 65.50           C  
ATOM    837  NZ  LYS A 113      13.860  40.988   9.348  1.00 64.25           N  
ATOM    838  N   ASN A 114      18.798  36.020   8.937  1.00 26.50           N  
ATOM    839  CA  ASN A 114      20.142  35.605   9.338  1.00 24.05           C  
ATOM    840  C   ASN A 114      20.432  34.224   8.741  1.00 26.73           C  
ATOM    841  O   ASN A 114      21.588  33.903   8.479  1.00 26.84           O  
ATOM    842  CB  ASN A 114      20.299  35.447  10.849  1.00 22.43           C  
ATOM    843  CG  ASN A 114      20.151  36.611  11.812  1.00 27.53           C  
ATOM    844  OD1 ASN A 114      19.916  36.350  13.022  1.00 27.38           O  
ATOM    845  ND2 ASN A 114      20.277  37.826  11.292  1.00 19.49           N  
ATOM    846  N   LEU A 115      19.452  33.345   8.509  1.00 22.64           N  
ATOM    847  CA  LEU A 115      19.677  32.020   7.965  1.00 21.73           C  
ATOM    848  C   LEU A 115      19.706  31.911   6.442  1.00 18.55           C  
ATOM    849  O   LEU A 115      19.751  30.783   5.905  1.00 18.93           O  
ATOM    850  CB  LEU A 115      18.585  31.086   8.543  1.00 20.47           C  
ATOM    851  CG  LEU A 115      18.796  30.706  10.009  1.00 19.34           C  
ATOM    852  CD1 LEU A 115      17.637  29.876  10.564  1.00 18.47           C  
ATOM    853  CD2 LEU A 115      20.072  29.881  10.160  1.00 16.95           C  
ATOM    854  N   GLY A 116      19.628  33.047   5.786  1.00 18.41           N  
ATOM    855  CA  GLY A 116      19.633  33.142   4.319  1.00 20.96           C  
ATOM    856  C   GLY A 116      18.291  32.947   3.619  1.00 23.12           C  
ATOM    857  O   GLY A 116      18.268  32.671   2.385  1.00 19.80           O  
ATOM    858  N   ALA A 117      17.144  33.033   4.304  1.00 20.20           N  
ATOM    859  CA  ALA A 117      15.837  32.857   3.676  1.00 17.01           C  
ATOM    860  C   ALA A 117      15.521  34.116   2.868  1.00 19.90           C  
ATOM    861  O   ALA A 117      16.153  35.184   3.063  1.00 17.90           O  
ATOM    862  CB  ALA A 117      14.703  32.612   4.685  1.00 14.98           C  
ATOM    863  N   GLU A 118      14.538  34.026   1.956  1.00 16.23           N  
ATOM    864  CA  GLU A 118      14.173  35.226   1.210  1.00 19.02           C  
ATOM    865  C   GLU A 118      12.811  35.682   1.757  1.00 16.71           C  
ATOM    866  O   GLU A 118      11.883  34.919   1.432  1.00 18.58           O  
ATOM    867  CB  GLU A 118      14.047  34.958  -0.310  1.00 25.33           C  
ATOM    868  CG  GLU A 118      13.654  36.202  -1.115  1.00 29.63           C  
ATOM    869  CD  GLU A 118      13.305  35.913  -2.569  1.00 38.17           C  
ATOM    870  OE1 GLU A 118      13.713  34.873  -3.142  1.00 36.11           O  
ATOM    871  OE2 GLU A 118      12.594  36.745  -3.185  1.00 34.79           O  
ATOM    872  N   ILE A 119      12.747  36.789   2.493  1.00 18.90           N  
ATOM    873  CA  ILE A 119      11.462  37.262   3.063  1.00 19.52           C  
ATOM    874  C   ILE A 119      10.740  37.908   1.880  1.00 18.52           C  
ATOM    875  O   ILE A 119      11.230  38.961   1.483  1.00 20.04           O  
ATOM    876  CB  ILE A 119      11.659  38.274   4.212  1.00 20.88           C  
ATOM    877  CG1 ILE A 119      12.570  37.768   5.332  1.00 26.93           C  
ATOM    878  CG2 ILE A 119      10.410  38.807   4.874  1.00 14.51           C  
ATOM    879  CD1 ILE A 119      12.506  36.381   5.860  1.00 26.64           C  
ATOM    880  N   VAL A 120       9.674  37.324   1.385  1.00 19.91           N  
ATOM    881  CA  VAL A 120       8.928  37.791   0.213  1.00 21.42           C  
ATOM    882  C   VAL A 120       7.961  38.911   0.514  1.00 24.75           C  
ATOM    883  O   VAL A 120       7.639  39.717  -0.356  1.00 23.54           O  
ATOM    884  CB  VAL A 120       8.160  36.698  -0.561  1.00 21.61           C  
ATOM    885  CG1 VAL A 120       9.147  35.600  -1.021  1.00 22.49           C  
ATOM    886  CG2 VAL A 120       7.022  36.003   0.147  1.00 13.84           C  
ATOM    887  N   GLN A 121       7.533  38.953   1.774  1.00 23.67           N  
ATOM    888  CA  GLN A 121       6.577  39.986   2.221  1.00 23.30           C  
ATOM    889  C   GLN A 121       6.828  40.267   3.713  1.00 14.93           C  
ATOM    890  O   GLN A 121       7.226  39.376   4.451  1.00 18.08           O  
ATOM    891  CB  GLN A 121       5.198  39.349   2.041  1.00 24.37           C  
ATOM    892  CG  GLN A 121       3.878  39.947   1.779  1.00 39.80           C  
ATOM    893  CD  GLN A 121       3.817  41.033   0.723  1.00 50.16           C  
ATOM    894  OE1 GLN A 121       4.378  40.926  -0.375  1.00 52.18           O  
ATOM    895  NE2 GLN A 121       3.128  42.142   1.041  1.00 48.89           N  
ATOM    896  N   ASP A 122       6.562  41.506   4.101  1.00 17.06           N  
ATOM    897  CA  ASP A 122       6.694  41.832   5.543  1.00 23.53           C  
ATOM    898  C   ASP A 122       5.552  41.091   6.285  1.00 22.60           C  
ATOM    899  O   ASP A 122       4.435  40.938   5.724  1.00 20.84           O  
ATOM    900  CB  ASP A 122       6.589  43.324   5.776  1.00 27.33           C  
ATOM    901  CG  ASP A 122       7.745  44.169   5.228  1.00 37.27           C  
ATOM    902  OD1 ASP A 122       8.905  43.698   5.054  1.00 49.08           O  
ATOM    903  OD2 ASP A 122       7.442  45.368   4.991  1.00 37.00           O  
ATOM    904  N   GLY A 123       5.821  40.620   7.499  1.00 23.18           N  
ATOM    905  CA  GLY A 123       4.893  39.883   8.306  1.00 17.34           C  
ATOM    906  C   GLY A 123       3.523  40.492   8.512  1.00 14.91           C  
ATOM    907  O   GLY A 123       3.355  41.708   8.663  1.00 19.80           O  
ATOM    908  N   LEU A 124       2.496  39.644   8.538  1.00 14.87           N  
ATOM    909  CA  LEU A 124       1.122  40.014   8.803  1.00 11.79           C  
ATOM    910  C   LEU A 124       1.021  39.972  10.372  1.00 16.46           C  
ATOM    911  O   LEU A 124       1.313  38.962  11.031  1.00 14.14           O  
ATOM    912  CB  LEU A 124       0.180  38.958   8.320  1.00 12.48           C  
ATOM    913  CG  LEU A 124      -1.307  39.211   8.585  1.00 11.67           C  
ATOM    914  CD1 LEU A 124      -1.765  40.540   8.007  1.00 16.22           C  
ATOM    915  CD2 LEU A 124      -2.007  38.030   7.932  1.00 13.25           C  
ATOM    916  N   ARG A 125       0.682  41.103  10.933  1.00 14.33           N  
ATOM    917  CA  ARG A 125       0.542  41.252  12.395  1.00 15.84           C  
ATOM    918  C   ARG A 125      -0.903  41.620  12.733  1.00 17.06           C  
ATOM    919  O   ARG A 125      -1.368  42.776  12.485  1.00 19.72           O  
ATOM    920  CB  ARG A 125       1.459  42.389  12.852  1.00 13.87           C  
ATOM    921  CG  ARG A 125       2.923  42.101  12.684  1.00 13.95           C  
ATOM    922  CD  ARG A 125       3.724  43.391  13.040  1.00 38.59           C  
ATOM    923  NE  ARG A 125       4.926  43.189  12.207  1.00 61.23           N  
ATOM    924  CZ  ARG A 125       6.080  42.707  12.645  1.00 67.61           C  
ATOM    925  NH1 ARG A 125       6.056  42.473  13.967  1.00 70.19           N  
ATOM    926  NH2 ARG A 125       7.130  42.483  11.844  1.00 59.90           N  
ATOM    927  N   ILE A 126      -1.669  40.678  13.271  1.00 19.06           N  
ATOM    928  CA  ILE A 126      -3.100  40.873  13.607  1.00 17.29           C  
ATOM    929  C   ILE A 126      -3.345  41.381  15.038  1.00 17.45           C  
ATOM    930  O   ILE A 126      -2.790  40.799  15.997  1.00 13.94           O  
ATOM    931  CB  ILE A 126      -3.875  39.551  13.397  1.00 15.86           C  
ATOM    932  CG1 ILE A 126      -3.712  39.011  11.957  1.00 18.20           C  
ATOM    933  CG2 ILE A 126      -5.374  39.621  13.769  1.00 16.46           C  
ATOM    934  CD1 ILE A 126      -4.292  39.979  10.947  1.00 24.20           C  
ATOM    935  N   ASP A 127      -4.148  42.429  15.132  1.00 15.23           N  
ATOM    936  CA  ASP A 127      -4.501  42.995  16.426  1.00 14.83           C  
ATOM    937  C   ASP A 127      -5.818  42.394  16.895  1.00 14.91           C  
ATOM    938  O   ASP A 127      -6.730  42.398  16.069  1.00 19.70           O  
ATOM    939  CB  ASP A 127      -4.647  44.521  16.325  1.00 18.60           C  
ATOM    940  CG  ASP A 127      -4.775  45.155  17.704  1.00 25.74           C  
ATOM    941  OD1 ASP A 127      -4.480  44.537  18.757  1.00 26.59           O  
ATOM    942  OD2 ASP A 127      -5.180  46.329  17.757  1.00 27.86           O  
ATOM    943  N   GLY A 128      -5.936  41.867  18.128  1.00 15.53           N  
ATOM    944  CA  GLY A 128      -7.208  41.338  18.501  1.00 16.04           C  
ATOM    945  C   GLY A 128      -7.645  40.078  17.794  1.00 16.09           C  
ATOM    946  O   GLY A 128      -6.910  39.177  17.394  1.00 18.59           O  
ATOM    947  N   ASP A 129      -8.979  39.955  17.691  1.00 17.95           N  
ATOM    948  CA  ASP A 129      -9.625  38.783  17.096  1.00 18.94           C  
ATOM    949  C   ASP A 129      -9.380  38.819  15.591  1.00 18.66           C  
ATOM    950  O   ASP A 129      -9.790  39.814  15.008  1.00 18.48           O  
ATOM    951  CB  ASP A 129     -11.156  38.815  17.323  1.00 14.41           C  
ATOM    952  CG  ASP A 129     -11.833  37.501  17.039  1.00 16.84           C  
ATOM    953  OD1 ASP A 129     -11.401  36.540  16.350  1.00 16.07           O  
ATOM    954  OD2 ASP A 129     -12.986  37.423  17.588  1.00 21.31           O  
ATOM    955  N   PRO A 130      -8.805  37.774  15.042  1.00 20.42           N  
ATOM    956  CA  PRO A 130      -8.520  37.673  13.623  1.00 16.21           C  
ATOM    957  C   PRO A 130      -9.788  37.533  12.823  1.00 18.12           C  
ATOM    958  O   PRO A 130      -9.824  37.879  11.625  1.00 19.56           O  
ATOM    959  CB  PRO A 130      -7.677  36.377  13.480  1.00 16.08           C  
ATOM    960  CG  PRO A 130      -8.026  35.546  14.704  1.00 16.04           C  
ATOM    961  CD  PRO A 130      -8.373  36.587  15.785  1.00 16.99           C  
ATOM    962  N   ARG A 131     -10.893  37.053  13.420  1.00 14.94           N  
ATOM    963  CA  ARG A 131     -12.142  36.904  12.662  1.00 12.42           C  
ATOM    964  C   ARG A 131     -12.687  38.211  12.169  1.00 14.55           C  
ATOM    965  O   ARG A 131     -13.556  38.373  11.311  1.00 20.84           O  
ATOM    966  CB  ARG A 131     -13.176  36.177  13.532  1.00 11.10           C  
ATOM    967  CG  ARG A 131     -12.780  34.753  13.822  1.00  9.98           C  
ATOM    968  CD  ARG A 131     -13.488  34.131  15.010  1.00 13.04           C  
ATOM    969  NE  ARG A 131     -12.725  32.936  15.417  1.00 18.23           N  
ATOM    970  CZ  ARG A 131     -11.585  32.818  16.126  1.00 14.86           C  
ATOM    971  NH1 ARG A 131     -10.969  33.875  16.608  1.00 16.57           N  
ATOM    972  NH2 ARG A 131     -10.993  31.649  16.350  1.00 14.55           N  
ATOM    973  N   ALA A 132     -12.254  39.326  12.731  1.00 15.70           N  
ATOM    974  CA  ALA A 132     -12.596  40.696  12.481  1.00 19.98           C  
ATOM    975  C   ALA A 132     -11.537  41.360  11.592  1.00 21.68           C  
ATOM    976  O   ALA A 132     -11.702  42.569  11.331  1.00 23.53           O  
ATOM    977  CB  ALA A 132     -12.686  41.539  13.774  1.00 18.00           C  
ATOM    978  N   ALA A 133     -10.542  40.563  11.188  1.00 20.72           N  
ATOM    979  CA  ALA A 133      -9.470  41.158  10.349  1.00 22.09           C  
ATOM    980  C   ALA A 133      -9.324  40.326   9.079  1.00 20.97           C  
ATOM    981  O   ALA A 133      -8.293  40.344   8.428  1.00 18.25           O  
ATOM    982  CB  ALA A 133      -8.162  41.243  11.150  1.00 19.76           C  
ATOM    983  N   ARG A 134     -10.385  39.579   8.746  1.00 22.36           N  
ATOM    984  CA  ARG A 134     -10.453  38.676   7.609  1.00 23.91           C  
ATOM    985  C   ARG A 134     -10.010  39.231   6.262  1.00 27.26           C  
ATOM    986  O   ARG A 134      -9.257  38.596   5.493  1.00 23.61           O  
ATOM    987  CB  ARG A 134     -11.905  38.204   7.559  1.00 26.11           C  
ATOM    988  CG  ARG A 134     -11.984  36.731   7.458  1.00 21.73           C  
ATOM    989  CD  ARG A 134     -13.284  36.200   6.819  1.00 24.98           C  
ATOM    990  NE  ARG A 134     -12.989  34.787   6.876  1.00 42.57           N  
ATOM    991  CZ  ARG A 134     -12.543  33.930   5.989  1.00 46.04           C  
ATOM    992  NH1 ARG A 134     -12.350  34.352   4.750  1.00 45.09           N  
ATOM    993  NH2 ARG A 134     -12.320  32.714   6.507  1.00 47.85           N  
ATOM    994  N   ASP A 135     -10.449  40.467   5.943  1.00 26.84           N  
ATOM    995  CA  ASP A 135     -10.074  41.150   4.711  1.00 25.75           C  
ATOM    996  C   ASP A 135      -8.574  41.443   4.675  1.00 24.26           C  
ATOM    997  O   ASP A 135      -8.029  41.322   3.572  1.00 26.05           O  
ATOM    998  CB  ASP A 135     -10.882  42.418   4.456  1.00 31.52           C  
ATOM    999  CG  ASP A 135     -12.360  42.171   4.193  1.00 28.73           C  
ATOM   1000  OD1 ASP A 135     -12.750  41.147   3.597  1.00 34.11           O  
ATOM   1001  OD2 ASP A 135     -13.154  43.028   4.639  1.00 40.77           O  
ATOM   1002  N   ASP A 136      -7.854  41.773   5.731  1.00 20.42           N  
ATOM   1003  CA  ASP A 136      -6.421  42.001   5.745  1.00 21.21           C  
ATOM   1004  C   ASP A 136      -5.649  40.694   5.562  1.00 21.16           C  
ATOM   1005  O   ASP A 136      -4.567  40.615   4.964  1.00 25.28           O  
ATOM   1006  CB  ASP A 136      -5.952  42.589   7.086  1.00 27.24           C  
ATOM   1007  CG  ASP A 136      -6.513  43.950   7.451  1.00 34.91           C  
ATOM   1008  OD1 ASP A 136      -6.949  44.710   6.558  1.00 34.97           O  
ATOM   1009  OD2 ASP A 136      -6.509  44.316   8.656  1.00 34.29           O  
ATOM   1010  N   ILE A 137      -6.176  39.616   6.165  1.00 19.15           N  
ATOM   1011  CA  ILE A 137      -5.528  38.301   6.063  1.00 18.06           C  
ATOM   1012  C   ILE A 137      -5.580  37.892   4.583  1.00 17.43           C  
ATOM   1013  O   ILE A 137      -4.584  37.526   3.984  1.00 15.40           O  
ATOM   1014  CB  ILE A 137      -6.264  37.272   6.938  1.00 15.49           C  
ATOM   1015  CG1 ILE A 137      -6.274  37.670   8.428  1.00 21.21           C  
ATOM   1016  CG2 ILE A 137      -5.615  35.919   6.718  1.00 15.05           C  
ATOM   1017  CD1 ILE A 137      -7.029  36.750   9.386  1.00 16.70           C  
ATOM   1018  N   VAL A 138      -6.775  37.950   3.991  1.00 19.65           N  
ATOM   1019  CA  VAL A 138      -7.026  37.625   2.585  1.00 18.00           C  
ATOM   1020  C   VAL A 138      -6.162  38.443   1.650  1.00 16.38           C  
ATOM   1021  O   VAL A 138      -5.532  37.969   0.695  1.00 18.57           O  
ATOM   1022  CB  VAL A 138      -8.529  37.857   2.317  1.00 22.16           C  
ATOM   1023  CG1 VAL A 138      -8.825  38.024   0.823  1.00 21.77           C  
ATOM   1024  CG2 VAL A 138      -9.312  36.676   2.882  1.00 17.89           C  
ATOM   1025  N   GLY A 139      -6.064  39.753   1.904  1.00 13.92           N  
ATOM   1026  CA  GLY A 139      -5.278  40.717   1.161  1.00 12.72           C  
ATOM   1027  C   GLY A 139      -3.789  40.408   1.298  1.00 19.19           C  
ATOM   1028  O   GLY A 139      -3.050  40.466   0.296  1.00 16.06           O  
ATOM   1029  N   TRP A 140      -3.297  40.049   2.498  1.00 14.47           N  
ATOM   1030  CA  TRP A 140      -1.881  39.706   2.673  1.00 14.92           C  
ATOM   1031  C   TRP A 140      -1.526  38.423   1.931  1.00 15.71           C  
ATOM   1032  O   TRP A 140      -0.429  38.308   1.341  1.00 20.26           O  
ATOM   1033  CB  TRP A 140      -1.660  39.493   4.186  1.00 15.81           C  
ATOM   1034  CG  TRP A 140      -0.233  39.157   4.551  1.00  7.90           C  
ATOM   1035  CD1 TRP A 140       0.730  40.076   4.732  1.00  7.50           C  
ATOM   1036  CD2 TRP A 140       0.360  37.876   4.765  1.00 11.32           C  
ATOM   1037  NE1 TRP A 140       1.922  39.458   5.032  1.00 13.38           N  
ATOM   1038  CE2 TRP A 140       1.720  38.092   5.101  1.00 12.90           C  
ATOM   1039  CE3 TRP A 140      -0.115  36.552   4.742  1.00 15.93           C  
ATOM   1040  CZ2 TRP A 140       2.627  37.084   5.436  1.00  8.65           C  
ATOM   1041  CZ3 TRP A 140       0.792  35.529   5.025  1.00 13.46           C  
ATOM   1042  CH2 TRP A 140       2.133  35.807   5.361  1.00 12.73           C  
ATOM   1043  N   ALA A 141      -2.399  37.414   1.882  1.00 15.74           N  
ATOM   1044  CA  ALA A 141      -2.149  36.140   1.210  1.00 15.46           C  
ATOM   1045  C   ALA A 141      -2.085  36.343  -0.311  1.00 20.91           C  
ATOM   1046  O   ALA A 141      -1.295  35.738  -1.020  1.00 16.67           O  
ATOM   1047  CB  ALA A 141      -3.175  35.102   1.628  1.00 14.60           C  
ATOM   1048  N   HIS A 142      -2.903  37.267  -0.833  1.00 23.29           N  
ATOM   1049  CA  HIS A 142      -2.920  37.630  -2.256  1.00 25.42           C  
ATOM   1050  C   HIS A 142      -1.570  38.246  -2.594  1.00 19.26           C  
ATOM   1051  O   HIS A 142      -0.936  37.884  -3.592  1.00 22.61           O  
ATOM   1052  CB  HIS A 142      -4.037  38.607  -2.642  1.00 24.24           C  
ATOM   1053  CG  HIS A 142      -4.055  39.073  -4.071  1.00 34.89           C  
ATOM   1054  ND1 HIS A 142      -3.681  40.346  -4.477  1.00 35.98           N  
ATOM   1055  CD2 HIS A 142      -4.441  38.448  -5.217  1.00 42.64           C  
ATOM   1056  CE1 HIS A 142      -3.842  40.480  -5.777  1.00 37.24           C  
ATOM   1057  NE2 HIS A 142      -4.293  39.335  -6.259  1.00 45.36           N  
ATOM   1058  N   ASP A 143      -1.089  39.180  -1.798  1.00 17.79           N  
ATOM   1059  CA  ASP A 143       0.199  39.826  -2.016  1.00 19.16           C  
ATOM   1060  C   ASP A 143       1.373  38.862  -1.932  1.00 22.37           C  
ATOM   1061  O   ASP A 143       2.374  39.054  -2.674  1.00 24.04           O  
ATOM   1062  CB  ASP A 143       0.368  40.924  -0.971  1.00 18.57           C  
ATOM   1063  CG  ASP A 143      -0.532  42.127  -1.133  1.00 28.00           C  
ATOM   1064  OD1 ASP A 143      -1.299  42.262  -2.122  1.00 32.74           O  
ATOM   1065  OD2 ASP A 143      -0.451  42.964  -0.204  1.00 31.00           O  
ATOM   1066  N   VAL A 144       1.352  37.852  -1.034  1.00 17.94           N  
ATOM   1067  CA  VAL A 144       2.497  36.922  -0.975  1.00 17.82           C  
ATOM   1068  C   VAL A 144       2.609  36.150  -2.293  1.00 16.08           C  
ATOM   1069  O   VAL A 144       3.721  35.915  -2.748  1.00 18.80           O  
ATOM   1070  CB  VAL A 144       2.344  35.955   0.235  1.00 15.55           C  
ATOM   1071  CG1 VAL A 144       3.228  34.755   0.197  1.00 16.39           C  
ATOM   1072  CG2 VAL A 144       2.608  36.758   1.514  1.00 19.93           C  
ATOM   1073  N   ARG A 145       1.478  35.741  -2.885  1.00 17.70           N  
ATOM   1074  CA  ARG A 145       1.342  34.991  -4.133  1.00 18.30           C  
ATOM   1075  C   ARG A 145       1.965  35.768  -5.304  1.00 18.39           C  
ATOM   1076  O   ARG A 145       2.695  35.289  -6.157  1.00 18.93           O  
ATOM   1077  CB  ARG A 145      -0.135  34.709  -4.452  1.00 18.74           C  
ATOM   1078  CG  ARG A 145      -0.659  33.502  -3.720  1.00 13.62           C  
ATOM   1079  CD  ARG A 145      -1.971  32.964  -4.273  1.00 15.65           C  
ATOM   1080  NE  ARG A 145      -3.123  33.785  -4.077  1.00 17.06           N  
ATOM   1081  CZ  ARG A 145      -3.721  34.586  -4.924  1.00 29.00           C  
ATOM   1082  NH1 ARG A 145      -3.216  34.714  -6.173  1.00 35.89           N  
ATOM   1083  NH2 ARG A 145      -4.827  35.209  -4.503  1.00 32.04           N  
ATOM   1084  N   GLY A 146       1.694  37.065  -5.313  1.00 19.95           N  
ATOM   1085  CA  GLY A 146       2.213  37.980  -6.297  1.00 26.12           C  
ATOM   1086  C   GLY A 146       3.681  38.237  -5.964  1.00 30.88           C  
ATOM   1087  O   GLY A 146       4.379  38.681  -6.884  1.00 34.98           O  
ATOM   1088  N   ALA A 147       4.194  37.992  -4.761  1.00 29.46           N  
ATOM   1089  CA  ALA A 147       5.580  38.262  -4.419  1.00 31.03           C  
ATOM   1090  C   ALA A 147       6.531  37.107  -4.653  1.00 33.11           C  
ATOM   1091  O   ALA A 147       7.775  37.266  -4.587  1.00 30.96           O  
ATOM   1092  CB  ALA A 147       5.668  38.683  -2.951  1.00 22.52           C  
ATOM   1093  N   ILE A 148       5.982  35.905  -4.903  1.00 34.47           N  
ATOM   1094  CA  ILE A 148       6.875  34.773  -5.123  1.00 38.69           C  
ATOM   1095  C   ILE A 148       7.278  34.713  -6.599  1.00 48.24           C  
ATOM   1096  O   ILE A 148       7.875  33.671  -6.973  1.00 56.21           O  
ATOM   1097  CB  ILE A 148       6.419  33.427  -4.556  1.00 34.61           C  
ATOM   1098  CG1 ILE A 148       5.201  32.809  -5.268  1.00 35.29           C  
ATOM   1099  CG2 ILE A 148       6.134  33.510  -3.056  1.00 28.02           C  
ATOM   1100  CD1 ILE A 148       5.093  31.314  -4.944  1.00 32.89           C  
ATOM   1101  OXT ILE A 148       7.089  35.629  -7.445  1.00 51.57           O  
TER    1102      ILE A 148                                                      
HETATM 1103  S   SO4 A   1      14.843  21.501  -1.857  1.00 41.13           S  
HETATM 1104  O1  SO4 A   1      14.125  21.916  -0.625  1.00 53.96           O  
HETATM 1105  O2  SO4 A   1      15.611  22.635  -2.442  1.00 53.97           O  
HETATM 1106  O3  SO4 A   1      15.655  20.279  -1.543  1.00 55.74           O  
HETATM 1107  O4  SO4 A   1      13.790  21.107  -2.878  1.00 57.87           O  
HETATM 1108  S   SO4 A 149     -13.673  29.571  14.301  1.00 69.15           S  
HETATM 1109  O1  SO4 A 149     -14.332  29.528  15.665  1.00 70.83           O  
HETATM 1110  O2  SO4 A 149     -13.478  31.031  13.925  1.00 70.06           O  
HETATM 1111  O3  SO4 A 149     -12.367  28.804  14.363  1.00 67.82           O  
HETATM 1112  O4  SO4 A 149     -14.500  28.996  13.173  1.00 71.07           O  
HETATM 1113  N1  FMN A 150       0.574  40.235  22.229  1.00 12.36           N  
HETATM 1114  C2  FMN A 150       1.607  41.032  21.792  1.00 11.89           C  
HETATM 1115  O2  FMN A 150       1.465  41.647  20.603  1.00 17.40           O  
HETATM 1116  N3  FMN A 150       2.721  41.267  22.554  1.00 18.84           N  
HETATM 1117  C4  FMN A 150       2.889  40.622  23.808  1.00 17.97           C  
HETATM 1118  O4  FMN A 150       4.049  40.808  24.551  1.00 18.76           O  
HETATM 1119  C4A FMN A 150       1.844  39.770  24.269  1.00 19.47           C  
HETATM 1120  N5  FMN A 150       2.003  39.112  25.490  1.00 16.85           N  
HETATM 1121  C5A FMN A 150       0.882  38.458  26.071  1.00 18.25           C  
HETATM 1122  C6  FMN A 150       0.945  37.963  27.412  1.00 16.39           C  
HETATM 1123  C7  FMN A 150      -0.180  37.336  27.988  1.00 19.84           C  
HETATM 1124  C7M FMN A 150      -0.222  36.801  29.340  1.00 15.19           C  
HETATM 1125  C8  FMN A 150      -1.337  37.199  27.207  1.00 18.24           C  
HETATM 1126  C8M FMN A 150      -2.529  36.582  27.701  1.00 14.11           C  
HETATM 1127  C9  FMN A 150      -1.388  37.693  25.862  1.00 15.61           C  
HETATM 1128  C9A FMN A 150      -0.278  38.342  25.269  1.00 18.29           C  
HETATM 1129  N10 FMN A 150      -0.362  38.788  23.914  1.00 18.06           N  
HETATM 1130  C10 FMN A 150       0.694  39.590  23.467  1.00 12.51           C  
HETATM 1131  C1' FMN A 150      -1.507  38.669  23.091  1.00 12.62           C  
HETATM 1132  C2' FMN A 150      -1.629  37.283  22.453  1.00  9.97           C  
HETATM 1133  O2' FMN A 150      -0.539  37.006  21.577  1.00 15.37           O  
HETATM 1134  C3' FMN A 150      -2.893  37.307  21.572  1.00 11.36           C  
HETATM 1135  O3' FMN A 150      -3.989  37.158  22.494  1.00 13.62           O  
HETATM 1136  C4' FMN A 150      -2.954  36.301  20.474  1.00 11.25           C  
HETATM 1137  O4' FMN A 150      -4.243  36.514  19.780  1.00 16.71           O  
HETATM 1138  C5' FMN A 150      -2.895  34.945  20.908  1.00  9.35           C  
HETATM 1139  O5' FMN A 150      -2.950  34.111  19.788  1.00 12.14           O  
HETATM 1140  P   FMN A 150      -3.082  32.468  19.750  1.00 11.76           P  
HETATM 1141  O1P FMN A 150      -2.037  31.661  20.758  1.00 12.93           O  
HETATM 1142  O2P FMN A 150      -2.791  31.884  18.195  1.00 14.25           O  
HETATM 1143  O3P FMN A 150      -4.638  32.055  20.139  1.00 11.71           O  
HETATM 1144  O   HOH A 151       2.604  37.271  17.252  1.00 10.01           O  
HETATM 1145  O   HOH A 152       7.428  38.078   6.739  1.00 11.50           O  
HETATM 1146  O   HOH A 153      -2.626  25.019  17.880  1.00 28.64           O  
HETATM 1147  O   HOH A 154      -4.057  31.825  -9.388  1.00 20.19           O  
HETATM 1148  O   HOH A 155       9.906  31.811  26.468  1.00 36.90           O  
HETATM 1149  O   HOH A 156      -9.562  31.341  18.547  1.00 31.31           O  
HETATM 1150  O   HOH A 157      -0.174  24.629  -8.009  1.00 15.31           O  
HETATM 1151  O   HOH A 158      15.601  36.301  16.426  1.00 16.32           O  
HETATM 1152  O   HOH A 159      -8.960  28.078  15.798  1.00 22.73           O  
HETATM 1153  O   HOH A 160      -8.428  26.066   5.349  1.00 22.39           O  
HETATM 1154  O   HOH A 161      -0.290  26.279  24.507  1.00 17.91           O  
HETATM 1155  O   HOH A 162      -4.907  22.604  -2.931  1.00 25.25           O  
HETATM 1156  O   HOH A 163       6.462  28.150  27.139  1.00 18.70           O  
HETATM 1157  O   HOH A 164      -5.371  43.715  12.902  1.00 19.82           O  
HETATM 1158  O   HOH A 165     -10.077  25.600  -2.076  1.00 23.56           O  
HETATM 1159  O   HOH A 166       3.225  23.228  -7.640  1.00 24.37           O  
HETATM 1160  O   HOH A 167       2.044  29.673  24.522  1.00 11.11           O  
HETATM 1161  O   HOH A 168      -1.141  19.177  12.274  1.00 21.98           O  
HETATM 1162  O   HOH A 169      10.093  41.741   2.617  1.00 39.23           O  
HETATM 1163  O   HOH A 170     -10.258  32.847  -2.237  1.00 26.15           O  
HETATM 1164  O   HOH A 171      -4.748  38.958  19.003  1.00 15.52           O  
HETATM 1165  O   HOH A 172      -8.104  45.950  16.978  1.00 32.44           O  
HETATM 1166  O   HOH A 173       3.116  41.858  27.252  1.00 21.06           O  
HETATM 1167  O   HOH A 174      -7.880  24.815   2.729  1.00 25.60           O  
HETATM 1168  O   HOH A 175       3.413  17.138  10.881  1.00 38.47           O  
HETATM 1169  O   HOH A 176       9.223  39.917  -3.082  1.00 46.63           O  
HETATM 1170  O   HOH A 177       7.503  37.834  30.845  1.00 23.89           O  
HETATM 1171  O   HOH A 178      -9.903  32.219   2.933  1.00 24.34           O  
HETATM 1172  O   HOH A 179      17.794  26.628   7.822  1.00 26.45           O  
HETATM 1173  O   HOH A 180      19.689  25.923   5.089  1.00 33.18           O  
HETATM 1174  O   HOH A 181       0.332  43.653   9.179  1.00 26.85           O  
HETATM 1175  O   HOH A 182     -15.095  37.069   9.968  1.00 25.35           O  
HETATM 1176  O   HOH A 183      -5.034  26.264  18.347  1.00 19.47           O  
HETATM 1177  O   HOH A 184       0.065  25.267  18.376  1.00 15.17           O  
HETATM 1178  O   HOH A 185       4.939  43.423  24.722  1.00 21.09           O  
HETATM 1179  O   HOH A 186      -4.754  24.838   8.821  1.00 37.67           O  
HETATM 1180  O   HOH A 187     -12.110  42.192   7.538  1.00 25.50           O  
HETATM 1181  O   HOH A 188       3.684  25.918  -9.905  1.00 16.31           O  
HETATM 1182  O   HOH A 189       2.175  32.830  -7.173  1.00 26.37           O  
HETATM 1183  O   HOH A 190      -5.748  24.051   2.242  1.00 19.96           O  
HETATM 1184  O   HOH A 191      -4.187  21.647  15.597  1.00 35.34           O  
HETATM 1185  O   HOH A 192      11.854  28.764  -2.180  1.00 20.87           O  
HETATM 1186  O   HOH A 193      19.135  23.943   6.878  1.00 28.98           O  
HETATM 1187  O   HOH A 194      11.414  41.874  11.608  1.00 31.65           O  
HETATM 1188  O   HOH A 195      -5.570  35.207  24.035  1.00 33.39           O  
HETATM 1189  O   HOH A 196       6.668  34.016  31.573  1.00 20.62           O  
HETATM 1190  O   HOH A 197      10.332  32.425  23.560  1.00 25.82           O  
HETATM 1191  O   HOH A 198      -2.901  24.620  21.387  1.00 37.02           O  
HETATM 1192  O   HOH A 199     -11.724  39.748   0.979  1.00 40.17           O  
HETATM 1193  O   HOH A 200      -1.853  21.685  19.282  1.00 28.58           O  
HETATM 1194  O   HOH A 201     -15.169  37.634  16.290  1.00 33.82           O  
HETATM 1195  O   HOH A 202       8.036  22.676  17.023  1.00 36.57           O  
HETATM 1196  O   HOH A 203      -4.318  34.619  -1.936  1.00 28.46           O  
HETATM 1197  O   HOH A 204      -5.590  22.358  -0.067  1.00 26.16           O  
HETATM 1198  O   HOH A 205       1.825  46.323  11.114  1.00 42.33           O  
HETATM 1199  O   HOH A 206       4.103  18.347  21.240  1.00 43.87           O  
HETATM 1200  O   HOH A 207      -3.041  43.884   1.848  1.00 43.55           O  
HETATM 1201  O   HOH A 208      -8.821  42.177  14.343  1.00 26.52           O  
HETATM 1202  O   HOH A 209      -3.843  20.893   4.678  1.00 51.40           O  
HETATM 1203  O   HOH A 210       8.851  26.131  26.621  1.00 34.93           O  
HETATM 1204  O   HOH A 211      13.278  31.298  22.506  1.00 34.49           O  
HETATM 1205  O   HOH A 212      18.531  36.652   4.089  1.00 35.46           O  
HETATM 1206  O   HOH A 213      -6.455  25.977  20.596  1.00 30.77           O  
HETATM 1207  O   HOH A 214     -10.315  27.647  13.976  1.00 29.51           O  
HETATM 1208  O   HOH A 215       6.179  23.301  -7.491  1.00 25.69           O  
HETATM 1209  O   HOH A 216      18.278  25.268   1.535  1.00 27.53           O  
HETATM 1210  O   HOH A 217       8.236  42.911   8.797  1.00 36.22           O  
HETATM 1211  O   HOH A 218      -6.965  24.027  -4.791  1.00 18.13           O  
HETATM 1212  O   HOH A 219      -0.283  21.263  21.630  1.00 38.49           O  
HETATM 1213  O   HOH A 220      -3.795  32.685  28.060  1.00 21.25           O  
HETATM 1214  O   HOH A 221       2.374  21.552  -0.472  1.00 25.32           O  
HETATM 1215  O   HOH A 222     -11.400  28.719   9.563  1.00 30.69           O  
HETATM 1216  O   HOH A 223      -5.593  34.150  26.758  1.00 17.70           O  
HETATM 1217  O   HOH A 224     -13.592  40.233   9.201  1.00 23.47           O  
HETATM 1218  O   HOH A 225       6.176  40.159  25.455  1.00 24.96           O  
HETATM 1219  O   HOH A 226      10.831  17.265   8.925  1.00 33.82           O  
HETATM 1220  O   HOH A 227     -11.121  30.451   7.752  1.00 34.18           O  
HETATM 1221  O   HOH A 228      -3.102  35.492  31.635  1.00 28.51           O  
HETATM 1222  O   HOH A 229      15.714  44.417  14.899  1.00 48.82           O  
HETATM 1223  O   HOH A 230      14.968  32.280  -3.033  1.00 38.82           O  
HETATM 1224  O   HOH A 231       9.912  18.396   3.623  1.00 35.18           O  
HETATM 1225  O   HOH A 232     -12.879  44.775   1.727  1.00 48.14           O  
HETATM 1226  O   HOH A 233      -2.896  47.827  27.319  1.00 34.47           O  
HETATM 1227  O   HOH A 234       1.964  15.686   4.464  1.00 62.24           O  
HETATM 1228  O   HOH A 235       3.102  41.112  -4.187  1.00 28.16           O  
HETATM 1229  O   HOH A 236       6.586  17.230  10.306  1.00 38.14           O  
HETATM 1230  O   HOH A 237      12.505  24.940  -3.743  1.00 43.27           O  
HETATM 1231  O   HOH A 238      -4.653  43.326  10.299  1.00 24.97           O  
HETATM 1232  O   HOH A 239       4.840  21.364  21.901  1.00 31.62           O  
HETATM 1233  O   HOH A 240      10.937  46.328  27.984  1.00 51.22           O  
HETATM 1234  O   HOH A 241      -6.395  23.983   6.586  1.00 36.32           O  
HETATM 1235  O   HOH A 242       0.164  19.025  -0.157  1.00 43.99           O  
HETATM 1236  O   HOH A 243       2.888  18.627  -8.700  1.00 43.64           O  
HETATM 1237  O   HOH A 244      20.179  40.050  13.748  1.00 16.19           O  
HETATM 1238  O   HOH A 245      -3.722  43.522  29.631  1.00 53.05           O  
HETATM 1239  O   HOH A 246      -9.677  24.672   0.665  1.00 30.51           O  
HETATM 1240  O   HOH A 247       5.123  21.835  26.103  1.00 40.22           O  
HETATM 1241  O   HOH A 248     -13.764  44.502  11.355  1.00 48.34           O  
HETATM 1242  O   HOH A 249      -5.101  29.026  27.743  1.00 39.66           O  
HETATM 1243  O   HOH A 250      -3.164  43.093   4.504  1.00 30.97           O  
HETATM 1244  O   HOH A 251       8.344  24.656  24.352  1.00 31.39           O  
HETATM 1245  O   HOH A 252      -4.175  26.258  26.742  1.00 23.25           O  
HETATM 1246  O   HOH A 253      20.118  34.367  14.094  1.00 23.35           O  
HETATM 1247  O   HOH A 254     -13.382  27.407  -2.968  1.00 28.08           O  
HETATM 1248  O   HOH A 255      -2.882  20.083  -2.148  1.00 32.66           O  
HETATM 1249  O   HOH A 256       1.173  43.389   6.512  1.00 42.61           O  
HETATM 1250  O   HOH A 257      -5.341  46.370  21.809  1.00 34.47           O  
HETATM 1251  O   HOH A 258       3.397  17.785   1.046  1.00 29.38           O  
HETATM 1252  O   HOH A 259       1.643  21.098  -6.716  1.00 30.37           O  
HETATM 1253  O   HOH A 260     -14.059  37.068   3.421  1.00 33.35           O  
HETATM 1254  O   HOH A 261      -4.245  22.230  -6.952  1.00 31.36           O  
HETATM 1255  O   HOH A 262       8.757  40.259  32.188  1.00 33.12           O  
HETATM 1256  O   HOH A 263      -8.070  21.871  -0.920  1.00 48.03           O  
HETATM 1257  O   HOH A 264      -5.920  23.784  11.367  1.00 33.41           O  
HETATM 1258  O   HOH A 265       2.209  23.046  24.177  1.00 44.33           O  
HETATM 1259  O   HOH A 266       1.460  48.935  17.460  1.00 45.76           O  
HETATM 1260  O   HOH A 267       6.557  21.649  19.871  1.00 31.69           O  
HETATM 1261  O   HOH A 268      -2.845  21.144  22.971  1.00 43.45           O  
HETATM 1262  O   HOH A 269      -0.785  39.128  -6.192  1.00 37.59           O  
HETATM 1263  O   HOH A 270     -10.413  28.229  18.332  1.00 27.50           O  
HETATM 1264  O   HOH A 271       3.032  23.120 -10.551  1.00 40.15           O  
HETATM 1265  O   HOH A 272      12.135  20.471  16.706  1.00 37.92           O  
HETATM 1266  O   HOH A 273      10.339  36.282  -5.062  1.00 36.17           O  
HETATM 1267  O   HOH A 274     -11.499  31.071   4.672  1.00 39.81           O  
HETATM 1268  O   HOH A 275     -10.522  36.780  -2.339  1.00 38.67           O  
HETATM 1269  O   HOH A 276      14.857  39.154   2.471  1.00 35.96           O  
HETATM 1270  O   HOH A 277       2.419  47.110  27.534  1.00 51.20           O  
HETATM 1271  O   HOH A 278       1.320  41.278  29.822  1.00 49.19           O  
HETATM 1272  O   HOH A 279     -11.957  26.535   4.895  1.00 40.89           O  
HETATM 1273  O   HOH A 280      -5.154  48.978  20.866  1.00 42.04           O  
HETATM 1274  O   HOH A 281       4.452  35.447  -7.965  1.00 42.86           O  
HETATM 1275  O   HOH A 282     -12.985  30.947  -0.293  1.00 35.31           O  
HETATM 1276  O   HOH A 283      17.326  29.481  19.620  1.00 36.22           O  
HETATM 1277  O   HOH A 284      17.670  34.535  16.077  1.00 27.51           O  
HETATM 1278  O   HOH A 285     -17.088  27.276   2.082  1.00 37.88           O  
HETATM 1279  O   HOH A 286      -4.367  43.261  -1.362  1.00 44.23           O  
HETATM 1280  O   HOH A 287      -7.646  44.265  12.937  1.00 45.19           O  
HETATM 1281  O   HOH A 288      12.007  39.264  -2.152  1.00 42.79           O  
HETATM 1282  O   HOH A 289      11.254  48.090  24.681  1.00 37.59           O  
HETATM 1283  O   HOH A 290      13.359  43.105  14.904  1.00 75.59           O  
HETATM 1284  O   HOH A 291      17.690  32.760  20.712  1.00 39.32           O  
HETATM 1285  O   HOH A 292      -0.469  18.461  16.126  1.00 49.34           O  
HETATM 1286  O   HOH A 293       0.549  42.760   2.238  1.00 31.82           O  
HETATM 1287  O   HOH A 294      15.472  18.344  15.806  1.00 47.09           O  
HETATM 1288  O   HOH A 295      -1.200  37.695  -8.216  1.00 45.29           O  
HETATM 1289  O   HOH A 296      -6.904  38.983  -8.209  1.00 48.06           O  
HETATM 1290  O   HOH A 297      -6.288  46.331  14.117  1.00 38.63           O  
HETATM 1291  O   HOH A 298      -2.485  44.219   9.183  1.00 38.39           O  
HETATM 1292  O   HOH A 299      10.402  22.790  -5.240  1.00 52.71           O  
HETATM 1293  O   HOH A 300      -0.562  40.740  28.446  1.00 45.87           O  
HETATM 1294  O   HOH A 301     -15.510  44.771   2.782  1.00 43.38           O  
HETATM 1295  O   HOH A 302      19.536  28.133  16.273  1.00 49.65           O  
HETATM 1296  O   HOH A 303       5.393  43.208   9.828  1.00 40.07           O  
HETATM 1297  O   HOH A 304       9.315  44.036  18.605  1.00 51.47           O  
HETATM 1298  O   HOH A 305       7.981  18.092   0.433  1.00 49.66           O  
CONECT 1103 1104 1105 1106 1107                                                 
CONECT 1104 1103                                                                
CONECT 1105 1103                                                                
CONECT 1106 1103                                                                
CONECT 1107 1103                                                                
CONECT 1108 1109 1110 1111 1112                                                 
CONECT 1109 1108                                                                
CONECT 1110 1108                                                                
CONECT 1111 1108                                                                
CONECT 1112 1108                                                                
CONECT 1113 1114 1130                                                           
CONECT 1114 1113 1115 1116                                                      
CONECT 1115 1114                                                                
CONECT 1116 1114 1117                                                           
CONECT 1117 1116 1118 1119                                                      
CONECT 1118 1117                                                                
CONECT 1119 1117 1120 1130                                                      
CONECT 1120 1119 1121                                                           
CONECT 1121 1120 1122 1128                                                      
CONECT 1122 1121 1123                                                           
CONECT 1123 1122 1124 1125                                                      
CONECT 1124 1123                                                                
CONECT 1125 1123 1126 1127                                                      
CONECT 1126 1125                                                                
CONECT 1127 1125 1128                                                           
CONECT 1128 1121 1127 1129                                                      
CONECT 1129 1128 1130 1131                                                      
CONECT 1130 1113 1119 1129                                                      
CONECT 1131 1129 1132                                                           
CONECT 1132 1131 1133 1134                                                      
CONECT 1133 1132                                                                
CONECT 1134 1132 1135 1136                                                      
CONECT 1135 1134                                                                
CONECT 1136 1134 1137 1138                                                      
CONECT 1137 1136                                                                
CONECT 1138 1136 1139                                                           
CONECT 1139 1138 1140                                                           
CONECT 1140 1139 1141 1142 1143                                                 
CONECT 1141 1140                                                                
CONECT 1142 1140                                                                
CONECT 1143 1140                                                                
MASTER      340    0    3    6    5    0    9    6 1297    1   41   12          
END