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Database: PDB
Entry: 6G5M
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Original site: 6G5M 
HEADER    OXIDOREDUCTASE                          29-MAR-18   6G5M              
TITLE     THE STRUCTURE OF THIOCYANATE DEHYDROGENASE FROM THIOALKALIVIBRIO      
TITLE    2 PARADOXUS COMPLEX WITH CU(I) IONS.                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: THIOCYANATE DEHYDROGENASE;                                 
COMPND   3 CHAIN: A, B, C, D                                                    
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: THIOALKALIVIBRIO PARADOXUS ARH 1;               
SOURCE   3 ORGANISM_TAXID: 713585                                               
KEYWDS    OXIDOREDUCTASE, THIOCYANATE DEHYDROGENASE, COPPER CENTERS             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.M.POLYAKOV,S.I.TSALLAGOV,T.V.TIKHKONOVA,V.O.POPOV                   
REVDAT   1   10-APR-19 6G5M    0                                                
JRNL        AUTH   K.M.POLYAKOV,S.I.TSALLAGOV,T.V.TIKHKONOVA,V.O.POPOV          
JRNL        TITL   THE STRUCTURE OF THIOCYANATE DEHYDROGENASE FROM              
JRNL        TITL 2 THIOALKALIVIBRIO PARADOXUS COMPLEX WITH CU(I) IONS.          
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.31 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0158                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.31                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.58                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 91028                          
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) : 0.136                           
REMARK   3   R VALUE            (WORKING SET) : 0.132                           
REMARK   3   FREE R VALUE                     : 0.206                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4591                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.31                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.37                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 6249                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 89.53                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1980                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 307                          
REMARK   3   BIN FREE R VALUE                    : 0.2780                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 14516                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 29                                      
REMARK   3   SOLVENT ATOMS            : 912                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 37.56                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -9.73000                                             
REMARK   3    B22 (A**2) : 18.54000                                             
REMARK   3    B33 (A**2) : -8.81000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.71000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.049         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.043         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.111         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.426         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.969                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.920                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 14999 ; 0.018 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 20426 ; 2.145 ; 1.942       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1858 ; 8.805 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   665 ;36.955 ;24.496       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2353 ;18.016 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    67 ;20.138 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2215 ; 0.144 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 11527 ; 0.011 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  7452 ; 3.399 ; 3.721       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  9304 ; 4.727 ; 5.564       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  7547 ; 3.832 ; 8.734       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 24270 ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):    15 ;19.812 ; 5.000       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TWIN DETAILS                                                        
REMARK   3   NUMBER OF TWIN DOMAINS  : 2                                        
REMARK   3      TWIN DOMAIN   : 1                                               
REMARK   3      TWIN OPERATOR : H, K, L                                         
REMARK   3      TWIN FRACTION : 0.474                                           
REMARK   3      TWIN DOMAIN   : 2                                               
REMARK   3      TWIN OPERATOR : L, -K, H                                        
REMARK   3      TWIN FRACTION : 0.526                                           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6G5M COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 02-APR-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200009423.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-DEC-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.976                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 6M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 95620                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.310                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.580                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.7                               
REMARK 200  DATA REDUNDANCY                : 2.530                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.3400                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.31                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.45                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.32                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.360                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 5F30                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.10                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN SOLUTION: 10 MG/ML PROTEIN, 25   
REMARK 280  MM BORATE BUFFER (PH 9.5) RESERVOIR SOLUTION: 0.2 SODIUM            
REMARK 280  MALONATE PH 6.0, 20% W/V PEG 3350. PRIOR TO DATA COLLECTION         
REMARK 280  CRYSTAL ADDITIONALLY TREATED BY A MIXTURE OF 0.2 MM CU(2+) AND 5    
REMARK 280  MM ASCORBATE TO INCREASE COPPER INCORPORATION., VAPOR DIFFUSION,    
REMARK 280  HANGING DROP, TEMPERATURE 294K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       81.18500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7300 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 28220 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -210.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D                                  
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 16150 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 54750 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -402.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6970 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 28410 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -187.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLU A   171                                                      
REMARK 465     ASP A   172                                                      
REMARK 465     PRO A   173                                                      
REMARK 465     GLU B   171                                                      
REMARK 465     ARG D   429                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A 306    NE   CZ   NH1  NH2                                  
REMARK 470     LYS B  82    CG   CD   CE   NZ                                   
REMARK 470     CSD B 131    OD1  OD2                                            
REMARK 470     THR B 169    OG1  CG2                                            
REMARK 470     VAL B 170    CG1  CG2                                            
REMARK 470     CSD C 131    OD1  OD2                                            
REMARK 470     VAL C 449    O                                                   
REMARK 470     CSD D 131    OD1                                                 
REMARK 470     LYS D 147    CE   NZ                                             
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  CU     CU B   602     O    HOH B   772              1.53            
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    LEU A 161   CA  -  CB  -  CG  ANGL. DEV. =  14.1 DEGREES          
REMARK 500    LEU A 161   CB  -  CG  -  CD2 ANGL. DEV. = -12.4 DEGREES          
REMARK 500    PRO A 458   C   -  N   -  CA  ANGL. DEV. =  -9.6 DEGREES          
REMARK 500    PRO C 101   C   -  N   -  CA  ANGL. DEV. =  10.2 DEGREES          
REMARK 500    PRO C 132   C   -  N   -  CA  ANGL. DEV. =  13.8 DEGREES          
REMARK 500    PRO C 332   C   -  N   -  CA  ANGL. DEV. = -14.3 DEGREES          
REMARK 500    PRO C 332   C   -  N   -  CD  ANGL. DEV. =  14.5 DEGREES          
REMARK 500    PRO C 387   C   -  N   -  CA  ANGL. DEV. =  10.9 DEGREES          
REMARK 500    PRO C 426   C   -  N   -  CA  ANGL. DEV. =   9.3 DEGREES          
REMARK 500    GLY C 430   N   -  CA  -  C   ANGL. DEV. = -17.8 DEGREES          
REMARK 500    ARG D 231   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    ARG D 231   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    ARG D 274   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ASP D 314   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ASP D 480   CB  -  CG  -  OD1 ANGL. DEV. =   6.4 DEGREES          
REMARK 500    ASP D 480   CB  -  CG  -  OD2 ANGL. DEV. =  -6.0 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    LYS A 103     -113.36     59.86                                   
REMARK 500    ALA A 120      151.69    177.87                                   
REMARK 500    HIS A 135      -78.10   -109.33                                   
REMARK 500    ASP A 144       78.21   -152.41                                   
REMARK 500    GLU A 148      132.00   -173.04                                   
REMARK 500    TYR A 164     -158.04   -105.69                                   
REMARK 500    PRO A 167       62.86    -63.98                                   
REMARK 500    THR A 187      -53.13   -138.28                                   
REMARK 500    VAL A 205     -137.56   -107.68                                   
REMARK 500    ALA A 213       16.21     59.22                                   
REMARK 500    ASP A 234       17.84     56.92                                   
REMARK 500    ASP A 276       52.84   -110.97                                   
REMARK 500    PRO A 291      157.02    -40.46                                   
REMARK 500    ALA A 312       81.68     19.31                                   
REMARK 500    LYS A 323      -51.22     84.00                                   
REMARK 500    PRO A 356     -161.35    -67.72                                   
REMARK 500    ASP A 365     -155.17   -131.16                                   
REMARK 500    HIS A 381      -91.93   -148.15                                   
REMARK 500    LEU A 398      -86.21     91.74                                   
REMARK 500    LYS A 473      151.76    173.68                                   
REMARK 500    LEU A 477      -59.28   -130.80                                   
REMARK 500    HIS A 482     -137.95   -112.76                                   
REMARK 500    TYR A 500       17.94     55.27                                   
REMARK 500    GLN A 501       -3.24     88.18                                   
REMARK 500    ASN A 502      -17.00   -140.41                                   
REMARK 500    THR A 503     -166.77   -115.21                                   
REMARK 500    ALA A 504      130.08    -38.10                                   
REMARK 500    HIS A 527      119.69    -24.58                                   
REMARK 500    SER A 543     -150.19   -114.39                                   
REMARK 500    SER A 545      -61.59   -147.60                                   
REMARK 500    LYS B 103     -119.44     54.34                                   
REMARK 500    HIS B 135      -82.06    -97.87                                   
REMARK 500    ASN B 160      -33.82    -39.96                                   
REMARK 500    PHE B 162       21.66    -73.81                                   
REMARK 500    TYR B 164     -158.19   -103.27                                   
REMARK 500    THR B 187      -51.49   -145.75                                   
REMARK 500    VAL B 205     -124.94   -116.79                                   
REMARK 500    LYS B 249       64.89    -65.91                                   
REMARK 500    PRO B 271      153.67    -42.69                                   
REMARK 500    ASP B 276       57.96   -109.03                                   
REMARK 500    PRO B 291       95.33    -55.11                                   
REMARK 500    LYS B 323      -49.96     64.69                                   
REMARK 500    ASP B 366      -12.67    -40.96                                   
REMARK 500    HIS B 381      -92.89   -147.09                                   
REMARK 500    ALA B 383      134.39   -170.96                                   
REMARK 500    LEU B 398      -67.09     82.81                                   
REMARK 500    ALA B 466       33.92    -99.55                                   
REMARK 500    TRP B 469       65.97     69.05                                   
REMARK 500    HIS B 482     -107.02   -113.36                                   
REMARK 500    ASN B 502      -17.75   -140.61                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     106 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 LEU B  497     SER B  498                 -149.04                    
REMARK 500 ASP C  427     TRP C  428                  -31.00                    
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 D 938        DISTANCE =  6.02 ANGSTROMS                       
REMARK 525    HOH D 939        DISTANCE =  6.22 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU A 602  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 135   NE2                                                    
REMARK 620 2 HIS A 528   ND1 139.9                                              
REMARK 620 3 HOH A 826   O    96.0 119.2                                        
REMARK 620 4 HOH A 894   O   119.1  94.2  65.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU A 605  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 136   NE2                                                    
REMARK 620 2 HOH A 826   O   131.6                                              
REMARK 620 3 HOH A 894   O   115.7  64.8                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU A 601  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 206   NE2                                                    
REMARK 620 2 ASP A 314   OD2  89.2                                              
REMARK 620 3 HIS A 381   NE2 173.7  85.8                                        
REMARK 620 4 HOH A 711   O   101.2 121.7  78.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU A 607  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 309   NE2                                                    
REMARK 620 2 HOH A 881   O    86.3                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU A 604  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 437   NE2                                                    
REMARK 620 2 HIS A 482   ND1 142.7                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU A 603  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TRP A 452   NE1                                                    
REMARK 620 2 ASP A 480   OD1  82.3                                              
REMARK 620 3 HIS A 482   NE2 124.3  72.9                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU B 602  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 135   NE2                                                    
REMARK 620 2 HIS B 528   ND1 130.2                                              
REMARK 620 3  CU B 605  CU    86.0 136.4                                        
REMARK 620 4 HOH B 867   O   129.7  91.0  46.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU B 605  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 136   NE2                                                    
REMARK 620 2 HOH B 815   O   113.5                                              
REMARK 620 3 HOH B 819   O   142.3  76.0                                        
REMARK 620 4 HOH B 867   O   116.2  58.9 100.1                                  
REMARK 620 5 HOH B 772   O   131.9 111.1  66.2  73.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU B 601  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 206   NE2                                                    
REMARK 620 2 ASP B 314   OD2  98.0                                              
REMARK 620 3 HIS B 381   NE2 169.1  87.8                                        
REMARK 620 4 HOH B 815   O    79.1 164.7  97.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU B 604  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 437   NE2                                                    
REMARK 620 2 HIS B 482   ND1 146.0                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU B 603  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 480   OD1                                                    
REMARK 620 2 HIS B 482   NE2  75.6                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU C 602  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 135   NE2                                                    
REMARK 620 2 HIS C 528   ND1 141.6                                              
REMARK 620 3 HOH C 835   O    82.5 130.6                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU C 606  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C 171   OE2                                                    
REMARK 620 2 HOH C 900   O   110.6                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU C 601  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 206   NE2                                                    
REMARK 620 2 ASP C 314   OD1 101.5                                              
REMARK 620 3 ASP C 314   OD2  91.5  55.9                                        
REMARK 620 4 HIS C 381   NE2 165.0  92.8  93.1                                  
REMARK 620 5 HOH C 803   O    82.4 139.5 164.3  89.4                            
REMARK 620 6 HOH C 756   O    74.9 143.7  87.9  91.1  76.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU C 608  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 309   NE2                                                    
REMARK 620 2 HOH C 887   O   105.1                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU C 607  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 411   ND1                                                    
REMARK 620 2 ASP C 412   OD1 135.6                                              
REMARK 620 3 HOH C 737   O    76.7  72.5                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU C 604  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 437   NE2                                                    
REMARK 620 2 HIS C 482   ND1 168.5                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU C 603  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C 480   OD1                                                    
REMARK 620 2 HIS C 482   NE2  75.3                                              
REMARK 620 3 HOH C 745   O    97.6 100.8                                        
REMARK 620 4 HOH C 894   O   115.0 168.8  82.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU D 602  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D 135   NE2                                                    
REMARK 620 2 HIS D 528   ND1 124.0                                              
REMARK 620 3 HOH D 746   O    97.6 136.9                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU D 605  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D 136   NE2                                                    
REMARK 620 2 HOH D 746   O   141.4                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU D 601  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D 206   NE2                                                    
REMARK 620 2 ASP D 314   OD2  95.4                                              
REMARK 620 3 HIS D 381   NE2 173.0  83.1                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU D 608  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D 309   NE2                                                    
REMARK 620 2 HOH D 874   O    99.4                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU D 604  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D 437   NE2                                                    
REMARK 620 2 HIS D 482   ND1 149.0                                              
REMARK 620 3 HOH D 885   O    96.5 113.9                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU D 603  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 480   OD1                                                    
REMARK 620 2 HIS D 482   NE2  71.6                                              
REMARK 620 3 HOH D 847   O    91.6 153.9                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU D 606  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 489   OD2                                                    
REMARK 620 2 HOH D 889   O   116.5                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU A 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU A 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU A 603                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU A 604                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU A 605                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU A 606                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU A 607                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU B 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU B 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU B 603                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU B 604                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU B 605                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU B 606                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU C 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU C 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU C 603                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU C 604                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU C 605                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU C 606                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU C 607                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU C 608                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU D 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU D 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU D 603                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU D 604                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU D 605                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU D 606                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU D 607                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU D 608                  
DBREF  6G5M A   82   548  UNP    W0DP94   W0DP94_9GAMM    82    548             
DBREF  6G5M B   82   548  UNP    W0DP94   W0DP94_9GAMM    82    548             
DBREF  6G5M C   82   548  UNP    W0DP94   W0DP94_9GAMM    82    548             
DBREF  6G5M D   82   548  UNP    W0DP94   W0DP94_9GAMM    82    548             
SEQRES   1 A  467  LYS TYR VAL LYS VAL GLN ASP PHE TYR ASP GLN LEU GLY          
SEQRES   2 A  467  LYS TYR VAL LEU VAL ALA PRO GLY LYS PHE SER GLY THR          
SEQRES   3 A  467  VAL ALA ALA THR ASP LEU SER THR GLY TRP THR MET ALA          
SEQRES   4 A  467  TRP LEU ALA ALA TRP ASN TYR GLY ASP THR CSD PRO ILE          
SEQRES   5 A  467  MET HIS HIS MET ALA ALA PHE PRO SER PRO ASP PRO TYR          
SEQRES   6 A  467  LYS GLU PHE GLU PHE VAL VAL ASN THR GLN GLY GLY LYS          
SEQRES   7 A  467  ASN LEU PHE ILE TYR GLY VAL PRO VAL THR VAL GLU ASP          
SEQRES   8 A  467  PRO GLY GLU GLY MET LYS ILE TYR ARG ILE LYS TYR ASP          
SEQRES   9 A  467  GLY THR ARG MET ASN LEU GLN ARG ASP ALA ALA GLU VAL          
SEQRES  10 A  467  SER GLY LEU GLY LEU GLY VAL HIS VAL THR ILE THR PRO          
SEQRES  11 A  467  GLU ALA ASP GLY TYR ALA VAL GLY ASP GLY GLN LYS ASP          
SEQRES  12 A  467  ILE CYS ALA GLU PHE ASP ARG GLU THR ASP MET VAL ARG          
SEQRES  13 A  467  TYR ALA TRP ALA PHE ASP TRP ASP PRO ASN VAL LYS ASP          
SEQRES  14 A  467  LEU LYS ARG ALA TRP LEU ASP GLY GLY THR MET THR ILE          
SEQRES  15 A  467  LYS ARG LEU LYS PRO THR LEU PRO GLY GLY ARG TYR ASP          
SEQRES  16 A  467  LEU GLN GLY SER LYS GLY ASN LYS ILE ASP TRP GLU LEU          
SEQRES  17 A  467  VAL PRO GLY GLY GLU LEU ALA ILE GLU ASP GLY LYS VAL          
SEQRES  18 A  467  SER GLY ASP ARG PRO LEU HIS SER VAL ALA ASN ASP ALA          
SEQRES  19 A  467  LEU VAL PHE ASP PRO ARG GLY LYS TRP ALA VAL ALA SER          
SEQRES  20 A  467  MET ARG LEU PRO GLY VAL CYS VAL VAL PHE ASP ARG GLU          
SEQRES  21 A  467  ASN GLN VAL PRO VAL ALA VAL LEU ALA GLY PRO LYS GLY          
SEQRES  22 A  467  THR PRO SER GLN PHE GLN LEU VAL LYS VAL ASP ASP ASP          
SEQRES  23 A  467  THR TRP THR VAL ASP ILE PRO GLU VAL ILE SER ALA GLY          
SEQRES  24 A  467  HIS GLN ALA GLY PHE SER PRO ASP GLY GLN SER PHE LEU          
SEQRES  25 A  467  PHE MET ASN SER LEU ARG GLN ASN ASN ILE MET VAL TRP          
SEQRES  26 A  467  ASP SER SER ASN HIS ASP ASP PRO THR THR TRP GLU LYS          
SEQRES  27 A  467  LYS ALA VAL VAL GLU SER PRO ASP TRP ARG GLY ALA TYR          
SEQRES  28 A  467  PRO ASN THR PHE HIS MET VAL PHE THR PRO ASP ALA LYS          
SEQRES  29 A  467  LYS ILE TYR VAL THR MET TRP TRP PRO SER PRO THR PRO          
SEQRES  30 A  467  ASN GLY ILE ALA VAL ILE ASP ALA VAL ASN TRP GLU VAL          
SEQRES  31 A  467  LEU LYS GLU VAL ASP LEU GLY PRO ASP MET HIS THR LEU          
SEQRES  32 A  467  ALA ILE THR TYR ASP GLY LYS PHE VAL VAL GLY THR LEU          
SEQRES  33 A  467  SER GLY TYR GLN ASN THR ALA SER ALA ILE VAL VAL MET          
SEQRES  34 A  467  GLU THR GLU THR ASP GLU VAL LEU GLY PHE LEU PRO SER          
SEQRES  35 A  467  PRO MET GLY HIS HIS ASP ASN VAL ILE VAL PRO ARG THR          
SEQRES  36 A  467  LEU GLU ASP LEU ARG ILE SER ARG SER THR THR THR              
SEQRES   1 B  467  LYS TYR VAL LYS VAL GLN ASP PHE TYR ASP GLN LEU GLY          
SEQRES   2 B  467  LYS TYR VAL LEU VAL ALA PRO GLY LYS PHE SER GLY THR          
SEQRES   3 B  467  VAL ALA ALA THR ASP LEU SER THR GLY TRP THR MET ALA          
SEQRES   4 B  467  TRP LEU ALA ALA TRP ASN TYR GLY ASP THR CSD PRO ILE          
SEQRES   5 B  467  MET HIS HIS MET ALA ALA PHE PRO SER PRO ASP PRO TYR          
SEQRES   6 B  467  LYS GLU PHE GLU PHE VAL VAL ASN THR GLN GLY GLY LYS          
SEQRES   7 B  467  ASN LEU PHE ILE TYR GLY VAL PRO VAL THR VAL GLU ASP          
SEQRES   8 B  467  PRO GLY GLU GLY MET LYS ILE TYR ARG ILE LYS TYR ASP          
SEQRES   9 B  467  GLY THR ARG MET ASN LEU GLN ARG ASP ALA ALA GLU VAL          
SEQRES  10 B  467  SER GLY LEU GLY LEU GLY VAL HIS VAL THR ILE THR PRO          
SEQRES  11 B  467  GLU ALA ASP GLY TYR ALA VAL GLY ASP GLY GLN LYS ASP          
SEQRES  12 B  467  ILE CYS ALA GLU PHE ASP ARG GLU THR ASP MET VAL ARG          
SEQRES  13 B  467  TYR ALA TRP ALA PHE ASP TRP ASP PRO ASN VAL LYS ASP          
SEQRES  14 B  467  LEU LYS ARG ALA TRP LEU ASP GLY GLY THR MET THR ILE          
SEQRES  15 B  467  LYS ARG LEU LYS PRO THR LEU PRO GLY GLY ARG TYR ASP          
SEQRES  16 B  467  LEU GLN GLY SER LYS GLY ASN LYS ILE ASP TRP GLU LEU          
SEQRES  17 B  467  VAL PRO GLY GLY GLU LEU ALA ILE GLU ASP GLY LYS VAL          
SEQRES  18 B  467  SER GLY ASP ARG PRO LEU HIS SER VAL ALA ASN ASP ALA          
SEQRES  19 B  467  LEU VAL PHE ASP PRO ARG GLY LYS TRP ALA VAL ALA SER          
SEQRES  20 B  467  MET ARG LEU PRO GLY VAL CYS VAL VAL PHE ASP ARG GLU          
SEQRES  21 B  467  ASN GLN VAL PRO VAL ALA VAL LEU ALA GLY PRO LYS GLY          
SEQRES  22 B  467  THR PRO SER GLN PHE GLN LEU VAL LYS VAL ASP ASP ASP          
SEQRES  23 B  467  THR TRP THR VAL ASP ILE PRO GLU VAL ILE SER ALA GLY          
SEQRES  24 B  467  HIS GLN ALA GLY PHE SER PRO ASP GLY GLN SER PHE LEU          
SEQRES  25 B  467  PHE MET ASN SER LEU ARG GLN ASN ASN ILE MET VAL TRP          
SEQRES  26 B  467  ASP SER SER ASN HIS ASP ASP PRO THR THR TRP GLU LYS          
SEQRES  27 B  467  LYS ALA VAL VAL GLU SER PRO ASP TRP ARG GLY ALA TYR          
SEQRES  28 B  467  PRO ASN THR PHE HIS MET VAL PHE THR PRO ASP ALA LYS          
SEQRES  29 B  467  LYS ILE TYR VAL THR MET TRP TRP PRO SER PRO THR PRO          
SEQRES  30 B  467  ASN GLY ILE ALA VAL ILE ASP ALA VAL ASN TRP GLU VAL          
SEQRES  31 B  467  LEU LYS GLU VAL ASP LEU GLY PRO ASP MET HIS THR LEU          
SEQRES  32 B  467  ALA ILE THR TYR ASP GLY LYS PHE VAL VAL GLY THR LEU          
SEQRES  33 B  467  SER GLY TYR GLN ASN THR ALA SER ALA ILE VAL VAL MET          
SEQRES  34 B  467  GLU THR GLU THR ASP GLU VAL LEU GLY PHE LEU PRO SER          
SEQRES  35 B  467  PRO MET GLY HIS HIS ASP ASN VAL ILE VAL PRO ARG THR          
SEQRES  36 B  467  LEU GLU ASP LEU ARG ILE SER ARG SER THR THR THR              
SEQRES   1 C  467  LYS TYR VAL LYS VAL GLN ASP PHE TYR ASP GLN LEU GLY          
SEQRES   2 C  467  LYS TYR VAL LEU VAL ALA PRO GLY LYS PHE SER GLY THR          
SEQRES   3 C  467  VAL ALA ALA THR ASP LEU SER THR GLY TRP THR MET ALA          
SEQRES   4 C  467  TRP LEU ALA ALA TRP ASN TYR GLY ASP THR CSD PRO ILE          
SEQRES   5 C  467  MET HIS HIS MET ALA ALA PHE PRO SER PRO ASP PRO TYR          
SEQRES   6 C  467  LYS GLU PHE GLU PHE VAL VAL ASN THR GLN GLY GLY LYS          
SEQRES   7 C  467  ASN LEU PHE ILE TYR GLY VAL PRO VAL THR VAL GLU ASP          
SEQRES   8 C  467  PRO GLY GLU GLY MET LYS ILE TYR ARG ILE LYS TYR ASP          
SEQRES   9 C  467  GLY THR ARG MET ASN LEU GLN ARG ASP ALA ALA GLU VAL          
SEQRES  10 C  467  SER GLY LEU GLY LEU GLY VAL HIS VAL THR ILE THR PRO          
SEQRES  11 C  467  GLU ALA ASP GLY TYR ALA VAL GLY ASP GLY GLN LYS ASP          
SEQRES  12 C  467  ILE CYS ALA GLU PHE ASP ARG GLU THR ASP MET VAL ARG          
SEQRES  13 C  467  TYR ALA TRP ALA PHE ASP TRP ASP PRO ASN VAL LYS ASP          
SEQRES  14 C  467  LEU LYS ARG ALA TRP LEU ASP GLY GLY THR MET THR ILE          
SEQRES  15 C  467  LYS ARG LEU LYS PRO THR LEU PRO GLY GLY ARG TYR ASP          
SEQRES  16 C  467  LEU GLN GLY SER LYS GLY ASN LYS ILE ASP TRP GLU LEU          
SEQRES  17 C  467  VAL PRO GLY GLY GLU LEU ALA ILE GLU ASP GLY LYS VAL          
SEQRES  18 C  467  SER GLY ASP ARG PRO LEU HIS SER VAL ALA ASN ASP ALA          
SEQRES  19 C  467  LEU VAL PHE ASP PRO ARG GLY LYS TRP ALA VAL ALA SER          
SEQRES  20 C  467  MET ARG LEU PRO GLY VAL CYS VAL VAL PHE ASP ARG GLU          
SEQRES  21 C  467  ASN GLN VAL PRO VAL ALA VAL LEU ALA GLY PRO LYS GLY          
SEQRES  22 C  467  THR PRO SER GLN PHE GLN LEU VAL LYS VAL ASP ASP ASP          
SEQRES  23 C  467  THR TRP THR VAL ASP ILE PRO GLU VAL ILE SER ALA GLY          
SEQRES  24 C  467  HIS GLN ALA GLY PHE SER PRO ASP GLY GLN SER PHE LEU          
SEQRES  25 C  467  PHE MET ASN SER LEU ARG GLN ASN ASN ILE MET VAL TRP          
SEQRES  26 C  467  ASP SER SER ASN HIS ASP ASP PRO THR THR TRP GLU LYS          
SEQRES  27 C  467  LYS ALA VAL VAL GLU SER PRO ASP TRP ARG GLY ALA TYR          
SEQRES  28 C  467  PRO ASN THR PHE HIS MET VAL PHE THR PRO ASP ALA LYS          
SEQRES  29 C  467  LYS ILE TYR VAL THR MET TRP TRP PRO SER PRO THR PRO          
SEQRES  30 C  467  ASN GLY ILE ALA VAL ILE ASP ALA VAL ASN TRP GLU VAL          
SEQRES  31 C  467  LEU LYS GLU VAL ASP LEU GLY PRO ASP MET HIS THR LEU          
SEQRES  32 C  467  ALA ILE THR TYR ASP GLY LYS PHE VAL VAL GLY THR LEU          
SEQRES  33 C  467  SER GLY TYR GLN ASN THR ALA SER ALA ILE VAL VAL MET          
SEQRES  34 C  467  GLU THR GLU THR ASP GLU VAL LEU GLY PHE LEU PRO SER          
SEQRES  35 C  467  PRO MET GLY HIS HIS ASP ASN VAL ILE VAL PRO ARG THR          
SEQRES  36 C  467  LEU GLU ASP LEU ARG ILE SER ARG SER THR THR THR              
SEQRES   1 D  467  LYS TYR VAL LYS VAL GLN ASP PHE TYR ASP GLN LEU GLY          
SEQRES   2 D  467  LYS TYR VAL LEU VAL ALA PRO GLY LYS PHE SER GLY THR          
SEQRES   3 D  467  VAL ALA ALA THR ASP LEU SER THR GLY TRP THR MET ALA          
SEQRES   4 D  467  TRP LEU ALA ALA TRP ASN TYR GLY ASP THR CSD PRO ILE          
SEQRES   5 D  467  MET HIS HIS MET ALA ALA PHE PRO SER PRO ASP PRO TYR          
SEQRES   6 D  467  LYS GLU PHE GLU PHE VAL VAL ASN THR GLN GLY GLY LYS          
SEQRES   7 D  467  ASN LEU PHE ILE TYR GLY VAL PRO VAL THR VAL GLU ASP          
SEQRES   8 D  467  PRO GLY GLU GLY MET LYS ILE TYR ARG ILE LYS TYR ASP          
SEQRES   9 D  467  GLY THR ARG MET ASN LEU GLN ARG ASP ALA ALA GLU VAL          
SEQRES  10 D  467  SER GLY LEU GLY LEU GLY VAL HIS VAL THR ILE THR PRO          
SEQRES  11 D  467  GLU ALA ASP GLY TYR ALA VAL GLY ASP GLY GLN LYS ASP          
SEQRES  12 D  467  ILE CYS ALA GLU PHE ASP ARG GLU THR ASP MET VAL ARG          
SEQRES  13 D  467  TYR ALA TRP ALA PHE ASP TRP ASP PRO ASN VAL LYS ASP          
SEQRES  14 D  467  LEU LYS ARG ALA TRP LEU ASP GLY GLY THR MET THR ILE          
SEQRES  15 D  467  LYS ARG LEU LYS PRO THR LEU PRO GLY GLY ARG TYR ASP          
SEQRES  16 D  467  LEU GLN GLY SER LYS GLY ASN LYS ILE ASP TRP GLU LEU          
SEQRES  17 D  467  VAL PRO GLY GLY GLU LEU ALA ILE GLU ASP GLY LYS VAL          
SEQRES  18 D  467  SER GLY ASP ARG PRO LEU HIS SER VAL ALA ASN ASP ALA          
SEQRES  19 D  467  LEU VAL PHE ASP PRO ARG GLY LYS TRP ALA VAL ALA SER          
SEQRES  20 D  467  MET ARG LEU PRO GLY VAL CYS VAL VAL PHE ASP ARG GLU          
SEQRES  21 D  467  ASN GLN VAL PRO VAL ALA VAL LEU ALA GLY PRO LYS GLY          
SEQRES  22 D  467  THR PRO SER GLN PHE GLN LEU VAL LYS VAL ASP ASP ASP          
SEQRES  23 D  467  THR TRP THR VAL ASP ILE PRO GLU VAL ILE SER ALA GLY          
SEQRES  24 D  467  HIS GLN ALA GLY PHE SER PRO ASP GLY GLN SER PHE LEU          
SEQRES  25 D  467  PHE MET ASN SER LEU ARG GLN ASN ASN ILE MET VAL TRP          
SEQRES  26 D  467  ASP SER SER ASN HIS ASP ASP PRO THR THR TRP GLU LYS          
SEQRES  27 D  467  LYS ALA VAL VAL GLU SER PRO ASP TRP ARG GLY ALA TYR          
SEQRES  28 D  467  PRO ASN THR PHE HIS MET VAL PHE THR PRO ASP ALA LYS          
SEQRES  29 D  467  LYS ILE TYR VAL THR MET TRP TRP PRO SER PRO THR PRO          
SEQRES  30 D  467  ASN GLY ILE ALA VAL ILE ASP ALA VAL ASN TRP GLU VAL          
SEQRES  31 D  467  LEU LYS GLU VAL ASP LEU GLY PRO ASP MET HIS THR LEU          
SEQRES  32 D  467  ALA ILE THR TYR ASP GLY LYS PHE VAL VAL GLY THR LEU          
SEQRES  33 D  467  SER GLY TYR GLN ASN THR ALA SER ALA ILE VAL VAL MET          
SEQRES  34 D  467  GLU THR GLU THR ASP GLU VAL LEU GLY PHE LEU PRO SER          
SEQRES  35 D  467  PRO MET GLY HIS HIS ASP ASN VAL ILE VAL PRO ARG THR          
SEQRES  36 D  467  LEU GLU ASP LEU ARG ILE SER ARG SER THR THR THR              
MODRES 6G5M CSD A  131  CYS  MODIFIED RESIDUE                                   
MODRES 6G5M CSD B  131  CYS  MODIFIED RESIDUE                                   
MODRES 6G5M CSD C  131  CYS  MODIFIED RESIDUE                                   
MODRES 6G5M CSD D  131  CYS  MODIFIED RESIDUE                                   
HET    CSD  A 131       8                                                       
HET    CSD  B 131       8                                                       
HET    CSD  C 131       7                                                       
HET    CSD  D 131       7                                                       
HET     CU  A 601       1                                                       
HET     CU  A 602       1                                                       
HET     CU  A 603       1                                                       
HET     CU  A 604       1                                                       
HET     CU  A 605       1                                                       
HET     CU  A 606       1                                                       
HET     CU  A 607       1                                                       
HET     CU  B 601       1                                                       
HET     CU  B 602       1                                                       
HET     CU  B 603       1                                                       
HET     CU  B 604       1                                                       
HET     CU  B 605       1                                                       
HET     CU  B 606       1                                                       
HET     CU  C 601       1                                                       
HET     CU  C 602       1                                                       
HET     CU  C 603       1                                                       
HET     CU  C 604       1                                                       
HET     CU  C 605       1                                                       
HET     CU  C 606       1                                                       
HET     CU  C 607       1                                                       
HET     CU  C 608       1                                                       
HET     CU  D 601       1                                                       
HET     CU  D 602       1                                                       
HET     CU  D 603       1                                                       
HET     CU  D 604       1                                                       
HET     CU  D 605       1                                                       
HET     CU  D 606       1                                                       
HET     CU  D 607       1                                                       
HET     CU  D 608       1                                                       
HETNAM     CSD 3-SULFINOALANINE                                                 
HETNAM      CU COPPER (II) ION                                                  
HETSYN     CSD S-CYSTEINESULFINIC ACID; S-SULFINOCYSTEINE                       
FORMUL   1  CSD    4(C3 H7 N O4 S)                                              
FORMUL   5   CU    29(CU 2+)                                                    
FORMUL  34  HOH   *912(H2 O)                                                    
HELIX    1 AA1 VAL A   86  GLN A   92  1                                   7    
HELIX    2 AA2 LYS A  103  SER A  105  5                                   3    
HELIX    3 AA3 TRP A  125  GLY A  128  5                                   4    
HELIX    4 AA4 GLY A  158  ILE A  163  5                                   6    
HELIX    5 AA5 ALA A  195  GLY A  200  1                                   6    
HELIX    6 AA6 GLY A  293  ASP A  299  1                                   7    
HELIX    7 AA7 ARG A  306  SER A  310  5                                   5    
HELIX    8 AA8 ASP A  413  TRP A  417  5                                   5    
HELIX    9 AA9 SER A  425  ARG A  429  5                                   5    
HELIX   10 AB1 TYR A  500  ASN A  502  5                                   3    
HELIX   11 AB2 GLU A  538  SER A  543  5                                   6    
HELIX   12 AB3 LYS B   85  GLN B   92  1                                   8    
HELIX   13 AB4 LYS B  103  SER B  105  5                                   3    
HELIX   14 AB5 TRP B  125  GLY B  128  5                                   4    
HELIX   15 AB6 GLY B  157  TYR B  164  5                                   8    
HELIX   16 AB7 ALA B  195  GLY B  200  1                                   6    
HELIX   17 AB8 LEU B  270  ARG B  274  5                                   5    
HELIX   18 AB9 GLY B  293  ASP B  299  1                                   7    
HELIX   19 AC1 ARG B  306  SER B  310  5                                   5    
HELIX   20 AC2 ASP B  413  TRP B  417  5                                   5    
HELIX   21 AC3 TYR B  500  ASN B  502  5                                   3    
HELIX   22 AC4 GLU B  538  SER B  543  5                                   6    
HELIX   23 AC5 LYS C   85  GLN C   92  1                                   8    
HELIX   24 AC6 LYS C  103  SER C  105  5                                   3    
HELIX   25 AC7 TRP C  125  GLY C  128  5                                   4    
HELIX   26 AC8 GLY C  157  ILE C  163  5                                   7    
HELIX   27 AC9 ALA C  195  GLY C  200  1                                   6    
HELIX   28 AD1 LEU C  270  ARG C  274  5                                   5    
HELIX   29 AD2 GLY C  293  ASP C  299  1                                   7    
HELIX   30 AD3 ARG C  306  SER C  310  5                                   5    
HELIX   31 AD4 ASP C  413  TRP C  417  5                                   5    
HELIX   32 AD5 TYR C  500  ASN C  502  5                                   3    
HELIX   33 AD6 THR C  536  ARG C  541  1                                   6    
HELIX   34 AD7 VAL D   86  GLN D   92  1                                   7    
HELIX   35 AD8 LYS D  103  SER D  105  5                                   3    
HELIX   36 AD9 TRP D  125  GLY D  128  5                                   4    
HELIX   37 AE1 GLY D  158  ILE D  163  5                                   6    
HELIX   38 AE2 ALA D  195  GLY D  200  1                                   6    
HELIX   39 AE3 LEU D  270  ARG D  274  5                                   5    
HELIX   40 AE4 GLY D  292  ASP D  299  1                                   8    
HELIX   41 AE5 TYR D  500  ASN D  502  5                                   3    
HELIX   42 AE6 GLU D  538  SER D  543  5                                   6    
SHEET    1 AA1 4 THR A 118  ALA A 123  0                                        
SHEET    2 AA1 4 THR A 107  ASP A 112 -1  N  VAL A 108   O  LEU A 122           
SHEET    3 AA1 4 VAL A  97  PRO A 101 -1  N  LEU A  98   O  THR A 111           
SHEET    4 AA1 4 VAL A 531  ILE A 532 -1  O  VAL A 531   N  VAL A  99           
SHEET    1 AA2 4 ILE A 133  ALA A 139  0                                        
SHEET    2 AA2 4 PHE A 149  GLN A 156 -1  O  ASN A 154   N  HIS A 135           
SHEET    3 AA2 4 GLY A 176  TYR A 184 -1  O  TYR A 184   N  PHE A 149           
SHEET    4 AA2 4 MET A 189  ASP A 194 -1  O  GLN A 192   N  ARG A 181           
SHEET    1 AA3 7 VAL A 207  ILE A 209  0                                        
SHEET    2 AA3 7 GLY A 215  ASP A 220 -1  O  ALA A 217   N  THR A 208           
SHEET    3 AA3 7 ILE A 225  ASP A 230 -1  O  PHE A 229   N  TYR A 216           
SHEET    4 AA3 7 VAL A 236  PRO A 246 -1  O  ARG A 237   N  GLU A 228           
SHEET    5 AA3 7 GLY A 259  ARG A 265 -1  O  LYS A 264   N  ALA A 241           
SHEET    6 AA3 7 THR A 368  ILE A 373 -1  O  TRP A 369   N  ILE A 263           
SHEET    7 AA3 7 LEU A 361  LYS A 363 -1  N  VAL A 362   O  THR A 370           
SHEET    1 AA4 5 ASN A 313  PHE A 318  0                                        
SHEET    2 AA4 5 TRP A 324  MET A 329 -1  O  VAL A 326   N  VAL A 317           
SHEET    3 AA4 5 VAL A 334  ASP A 339 -1  O  PHE A 338   N  ALA A 325           
SHEET    4 AA4 5 VAL A 344  ALA A 350 -1  O  ALA A 347   N  VAL A 337           
SHEET    5 AA4 5 GLN A 358  PHE A 359 -1  O  PHE A 359   N  VAL A 348           
SHEET    1 AA5 4 ALA A 379  PHE A 385  0                                        
SHEET    2 AA5 4 SER A 391  SER A 397 -1  O  SER A 397   N  ALA A 379           
SHEET    3 AA5 4 ASN A 402  ASP A 407 -1  O  MET A 404   N  PHE A 394           
SHEET    4 AA5 4 GLU A 418  VAL A 423 -1  O  GLU A 418   N  ASP A 407           
SHEET    1 AA6 4 MET A 438  PHE A 440  0                                        
SHEET    2 AA6 4 LYS A 446  MET A 451 -1  O  TYR A 448   N  VAL A 439           
SHEET    3 AA6 4 ASN A 459  ASP A 465 -1  O  ILE A 464   N  ILE A 447           
SHEET    4 AA6 4 VAL A 471  GLY A 478 -1  O  LEU A 477   N  ASN A 459           
SHEET    1 AA7 4 MET A 481  ILE A 486  0                                        
SHEET    2 AA7 4 PHE A 492  SER A 498 -1  O  THR A 496   N  HIS A 482           
SHEET    3 AA7 4 SER A 505  GLU A 511 -1  O  ALA A 506   N  LEU A 497           
SHEET    4 AA7 4 VAL A 517  PRO A 522 -1  O  LEU A 521   N  ILE A 507           
SHEET    1 AA8 4 THR B 118  ALA B 123  0                                        
SHEET    2 AA8 4 THR B 107  ASP B 112 -1  N  ALA B 110   O  ALA B 120           
SHEET    3 AA8 4 VAL B  97  PRO B 101 -1  N  LEU B  98   O  THR B 111           
SHEET    4 AA8 4 VAL B 531  ILE B 532 -1  O  VAL B 531   N  VAL B  99           
SHEET    1 AA9 4 ILE B 133  ALA B 139  0                                        
SHEET    2 AA9 4 PHE B 149  GLN B 156 -1  O  ASN B 154   N  HIS B 135           
SHEET    3 AA9 4 ILE B 179  TYR B 184 -1  O  ILE B 182   N  PHE B 151           
SHEET    4 AA9 4 MET B 189  ASP B 194 -1  O  ASN B 190   N  LYS B 183           
SHEET    1 AB1 7 VAL B 207  ILE B 209  0                                        
SHEET    2 AB1 7 GLY B 215  ASP B 220 -1  O  ALA B 217   N  THR B 208           
SHEET    3 AB1 7 ILE B 225  ASP B 230 -1  O  PHE B 229   N  TYR B 216           
SHEET    4 AB1 7 VAL B 236  PRO B 246 -1  O  TRP B 240   N  CYS B 226           
SHEET    5 AB1 7 GLY B 259  ARG B 265 -1  O  LYS B 264   N  ALA B 241           
SHEET    6 AB1 7 THR B 368  ILE B 373 -1  O  ILE B 373   N  GLY B 259           
SHEET    7 AB1 7 LEU B 361  ASP B 365 -1  N  VAL B 362   O  THR B 370           
SHEET    1 AB2 5 ASN B 313  PHE B 318  0                                        
SHEET    2 AB2 5 TRP B 324  MET B 329 -1  O  VAL B 326   N  VAL B 317           
SHEET    3 AB2 5 VAL B 334  ASP B 339 -1  O  VAL B 336   N  ALA B 327           
SHEET    4 AB2 5 VAL B 344  ALA B 350 -1  O  VAL B 346   N  VAL B 337           
SHEET    5 AB2 5 GLN B 358  PHE B 359 -1  O  PHE B 359   N  VAL B 348           
SHEET    1 AB3 4 ALA B 379  PHE B 385  0                                        
SHEET    2 AB3 4 SER B 391  SER B 397 -1  O  SER B 397   N  ALA B 379           
SHEET    3 AB3 4 ASN B 402  ASP B 407 -1  O  MET B 404   N  PHE B 394           
SHEET    4 AB3 4 GLU B 418  VAL B 423 -1  O  VAL B 423   N  ILE B 403           
SHEET    1 AB4 4 ASN B 434  PHE B 440  0                                        
SHEET    2 AB4 4 LYS B 446  TRP B 452 -1  O  TRP B 452   N  ASN B 434           
SHEET    3 AB4 4 ASN B 459  ASP B 465 -1  O  ALA B 462   N  VAL B 449           
SHEET    4 AB4 4 GLU B 470  GLY B 478 -1  O  LYS B 473   N  VAL B 463           
SHEET    1 AB5 4 MET B 481  ILE B 486  0                                        
SHEET    2 AB5 4 PHE B 492  SER B 498 -1  O  VAL B 494   N  ALA B 485           
SHEET    3 AB5 4 SER B 505  GLU B 511 -1  O  ALA B 506   N  LEU B 497           
SHEET    4 AB5 4 VAL B 517  PRO B 522 -1  O  LEU B 518   N  VAL B 509           
SHEET    1 AB6 4 THR C 118  ALA C 123  0                                        
SHEET    2 AB6 4 THR C 107  ASP C 112 -1  N  ALA C 110   O  ALA C 120           
SHEET    3 AB6 4 VAL C  97  PRO C 101 -1  N  LEU C  98   O  THR C 111           
SHEET    4 AB6 4 VAL C 531  ILE C 532 -1  O  VAL C 531   N  VAL C  99           
SHEET    1 AB7 4 ILE C 133  ALA C 139  0                                        
SHEET    2 AB7 4 PHE C 149  GLN C 156 -1  O  VAL C 152   N  ALA C 138           
SHEET    3 AB7 4 ILE C 179  TYR C 184 -1  O  ILE C 182   N  PHE C 151           
SHEET    4 AB7 4 MET C 189  ASP C 194 -1  O  ASN C 190   N  LYS C 183           
SHEET    1 AB8 7 VAL C 207  ILE C 209  0                                        
SHEET    2 AB8 7 GLY C 215  ASP C 220 -1  O  ALA C 217   N  THR C 208           
SHEET    3 AB8 7 ILE C 225  ASP C 230 -1  O  PHE C 229   N  TYR C 216           
SHEET    4 AB8 7 VAL C 236  PRO C 246 -1  O  ARG C 237   N  GLU C 228           
SHEET    5 AB8 7 GLY C 259  ARG C 265 -1  O  THR C 260   N  ASP C 245           
SHEET    6 AB8 7 THR C 368  ILE C 373 -1  O  ILE C 373   N  GLY C 259           
SHEET    7 AB8 7 LEU C 361  LYS C 363 -1  N  VAL C 362   O  THR C 370           
SHEET    1 AB9 5 ASN C 313  PHE C 318  0                                        
SHEET    2 AB9 5 TRP C 324  MET C 329 -1  O  VAL C 326   N  VAL C 317           
SHEET    3 AB9 5 VAL C 334  ASP C 339 -1  O  PHE C 338   N  ALA C 325           
SHEET    4 AB9 5 VAL C 344  ALA C 350 -1  O  VAL C 344   N  ASP C 339           
SHEET    5 AB9 5 GLN C 358  PHE C 359 -1  O  PHE C 359   N  VAL C 348           
SHEET    1 AC1 4 ALA C 379  PHE C 385  0                                        
SHEET    2 AC1 4 SER C 391  SER C 397 -1  O  MET C 395   N  GLN C 382           
SHEET    3 AC1 4 ASN C 402  ASP C 407 -1  O  TRP C 406   N  PHE C 392           
SHEET    4 AC1 4 GLU C 418  VAL C 423 -1  O  GLU C 418   N  ASP C 407           
SHEET    1 AC2 4 VAL C 439  PHE C 440  0                                        
SHEET    2 AC2 4 LYS C 446  TYR C 448 -1  O  TYR C 448   N  VAL C 439           
SHEET    3 AC2 4 ASN C 459  ASP C 465 -1  O  ILE C 464   N  ILE C 447           
SHEET    4 AC2 4 GLU C 470  GLY C 478 -1  O  GLU C 470   N  ASP C 465           
SHEET    1 AC3 4 MET C 481  ILE C 486  0                                        
SHEET    2 AC3 4 PHE C 492  SER C 498 -1  O  THR C 496   N  HIS C 482           
SHEET    3 AC3 4 SER C 505  GLU C 511 -1  O  MET C 510   N  VAL C 493           
SHEET    4 AC3 4 GLU C 516  LEU C 521 -1  O  GLY C 519   N  VAL C 509           
SHEET    1 AC4 4 THR D 118  ALA D 123  0                                        
SHEET    2 AC4 4 THR D 107  ASP D 112 -1  N  ALA D 110   O  ALA D 120           
SHEET    3 AC4 4 VAL D  97  PRO D 101 -1  N  LEU D  98   O  THR D 111           
SHEET    4 AC4 4 VAL D 531  ILE D 532 -1  O  VAL D 531   N  VAL D  99           
SHEET    1 AC5 4 ILE D 133  ALA D 139  0                                        
SHEET    2 AC5 4 PHE D 149  GLN D 156 -1  O  ASN D 154   N  HIS D 135           
SHEET    3 AC5 4 GLY D 176  TYR D 184 -1  O  TYR D 184   N  PHE D 149           
SHEET    4 AC5 4 MET D 189  ASP D 194 -1  O  ARG D 193   N  ARG D 181           
SHEET    1 AC6 7 VAL D 207  ILE D 209  0                                        
SHEET    2 AC6 7 GLY D 215  ASP D 220 -1  O  ALA D 217   N  THR D 208           
SHEET    3 AC6 7 ILE D 225  ASP D 230 -1  O  PHE D 229   N  TYR D 216           
SHEET    4 AC6 7 VAL D 236  PRO D 246 -1  O  TRP D 240   N  CYS D 226           
SHEET    5 AC6 7 GLY D 259  ARG D 265 -1  O  LYS D 264   N  ALA D 241           
SHEET    6 AC6 7 THR D 368  ILE D 373 -1  O  ILE D 373   N  GLY D 259           
SHEET    7 AC6 7 LEU D 361  ASP D 365 -1  N  VAL D 364   O  THR D 368           
SHEET    1 AC7 4 ASN D 313  PHE D 318  0                                        
SHEET    2 AC7 4 TRP D 324  MET D 329 -1  O  VAL D 326   N  VAL D 317           
SHEET    3 AC7 4 VAL D 334  ASP D 339 -1  O  VAL D 336   N  ALA D 327           
SHEET    4 AC7 4 VAL D 344  ALA D 350 -1  O  LEU D 349   N  CYS D 335           
SHEET    1 AC8 4 ALA D 379  PHE D 385  0                                        
SHEET    2 AC8 4 SER D 391  SER D 397 -1  O  MET D 395   N  GLN D 382           
SHEET    3 AC8 4 ASN D 402  ASP D 407 -1  O  TRP D 406   N  PHE D 392           
SHEET    4 AC8 4 GLU D 418  VAL D 423 -1  O  GLU D 418   N  ASP D 407           
SHEET    1 AC9 4 MET D 438  PHE D 440  0                                        
SHEET    2 AC9 4 LYS D 446  MET D 451 -1  O  TYR D 448   N  VAL D 439           
SHEET    3 AC9 4 ASN D 459  ASP D 465 -1  O  GLY D 460   N  MET D 451           
SHEET    4 AC9 4 GLU D 470  GLY D 478 -1  O  LYS D 473   N  VAL D 463           
SHEET    1 AD1 4 MET D 481  ILE D 486  0                                        
SHEET    2 AD1 4 PHE D 492  SER D 498 -1  O  THR D 496   N  HIS D 482           
SHEET    3 AD1 4 SER D 505  GLU D 511 -1  O  VAL D 508   N  GLY D 495           
SHEET    4 AD1 4 VAL D 517  PRO D 522 -1  O  GLY D 519   N  VAL D 509           
LINK         C   THR A 130                 N   CSD A 131     1555   1555  1.35  
LINK         C   CSD A 131                 N   PRO A 132     1555   1555  1.36  
LINK         NE2 HIS A 135                CU    CU A 602     1555   1555  1.98  
LINK         NE2 HIS A 136                CU    CU A 605     1555   1555  1.93  
LINK         NE2 HIS A 206                CU    CU A 601     1555   1555  1.97  
LINK         NE2 HIS A 309                CU    CU A 607     1555   1555  2.22  
LINK         OD2 ASP A 314                CU    CU A 601     1555   1555  1.92  
LINK         NE2 HIS A 381                CU    CU A 601     1555   1555  2.02  
LINK         ND1 HIS A 411                CU    CU A 606     1555   1555  2.22  
LINK         NE2 HIS A 437                CU    CU A 604     1555   1555  1.84  
LINK         NE1 TRP A 452                CU    CU A 603     1555   1555  2.27  
LINK         OD1 ASP A 480                CU    CU A 603     1555   1555  2.17  
LINK         ND1 HIS A 482                CU    CU A 604     1555   1555  2.12  
LINK         NE2 HIS A 482                CU    CU A 603     1555   1555  2.18  
LINK         ND1 HIS A 528                CU    CU A 602     1555   1555  1.97  
LINK         C   THR B 130                 N   CSD B 131     1555   1555  1.35  
LINK         C   CSD B 131                 N   PRO B 132     1555   1555  1.35  
LINK         NE2 HIS B 135                CU    CU B 602     1555   1555  1.97  
LINK         NE2 HIS B 136                CU    CU B 605     1555   1555  2.00  
LINK         NE2 HIS B 206                CU    CU B 601     1555   1555  1.99  
LINK         OD2 ASP B 314                CU    CU B 601     1555   1555  1.94  
LINK         NE2 HIS B 381                CU    CU B 601     1555   1555  1.98  
LINK         ND1 HIS B 411                CU    CU B 606     1555   1555  1.93  
LINK         NE2 HIS B 437                CU    CU B 604     1555   1555  2.13  
LINK         OD1 ASP B 480                CU    CU B 603     1555   1555  1.75  
LINK         ND1 HIS B 482                CU    CU B 604     1555   1555  2.03  
LINK         NE2 HIS B 482                CU    CU B 603     1555   1555  2.47  
LINK         ND1 HIS B 528                CU    CU B 602     1555   1555  1.93  
LINK         C   THR C 130                 N   CSD C 131     1555   1555  1.32  
LINK         C   CSD C 131                 N   PRO C 132     1555   1555  1.36  
LINK         NE2 HIS C 135                CU    CU C 602     1555   1555  1.97  
LINK         NE2 HIS C 136                CU    CU C 605     1555   1555  1.78  
LINK         OE2 GLU C 171                CU    CU C 606     1555   1555  2.42  
LINK         NE2 HIS C 206                CU    CU C 601     1555   1555  2.00  
LINK         NE2 HIS C 309                CU    CU C 608     1555   1555  2.00  
LINK         OD1 ASP C 314                CU    CU C 601     1555   1555  2.64  
LINK         OD2 ASP C 314                CU    CU C 601     1555   1555  1.94  
LINK         NE2 HIS C 381                CU    CU C 601     1555   1555  2.00  
LINK         ND1 HIS C 411                CU    CU C 607     1555   1555  2.04  
LINK         OD1 ASP C 412                CU    CU C 607     1555   1555  2.33  
LINK         NE2 HIS C 437                CU    CU C 604     1555   1555  2.11  
LINK         OD1 ASP C 480                CU    CU C 603     1555   1555  1.98  
LINK         ND1 HIS C 482                CU    CU C 604     1555   1555  2.12  
LINK         NE2 HIS C 482                CU    CU C 603     1555   1555  2.07  
LINK         ND1 HIS C 528                CU    CU C 602     1555   1555  1.96  
LINK         C   THR D 130                 N   CSD D 131     1555   1555  1.34  
LINK         C   CSD D 131                 N   PRO D 132     1555   1555  1.35  
LINK         NE2 HIS D 135                CU    CU D 602     1555   1555  2.02  
LINK         NE2 HIS D 136                CU    CU D 605     1555   1555  1.92  
LINK         NE2 HIS D 206                CU    CU D 601     1555   1555  2.01  
LINK         NE2 HIS D 309                CU    CU D 608     1555   1555  2.01  
LINK         OD2 ASP D 314                CU    CU D 601     1555   1555  1.99  
LINK         NE2 HIS D 381                CU    CU D 601     1555   1555  2.02  
LINK         ND1 HIS D 411                CU    CU D 607     1555   1555  2.19  
LINK         NE2 HIS D 437                CU    CU D 604     1555   1555  1.94  
LINK         OD1 ASP D 480                CU    CU D 603     1555   1555  2.28  
LINK         ND1 HIS D 482                CU    CU D 604     1555   1555  2.07  
LINK         NE2 HIS D 482                CU    CU D 603     1555   1555  2.64  
LINK         OD2 ASP D 489                CU    CU D 606     1555   1555  2.08  
LINK         ND1 HIS D 528                CU    CU D 602     1555   1555  1.97  
LINK        CU    CU A 601                 O   HOH A 711     1555   1555  2.26  
LINK        CU    CU A 602                 O   HOH A 826     1555   1555  1.84  
LINK        CU    CU A 602                 O   HOH A 894     1555   1555  2.59  
LINK        CU    CU A 605                 O   HOH A 826     1555   1555  2.56  
LINK        CU    CU A 605                 O   HOH A 894     1555   1555  1.99  
LINK        CU    CU A 607                 O   HOH A 881     1555   1555  2.41  
LINK        CU    CU B 601                 O   HOH B 815     1555   1555  2.45  
LINK        CU    CU B 602                CU    CU B 605     1555   1555  2.65  
LINK        CU    CU B 602                 O   HOH B 867     1555   1555  2.63  
LINK        CU    CU B 605                 O   HOH B 815     1555   1555  2.36  
LINK        CU    CU B 605                 O   HOH B 819     1555   1555  1.97  
LINK        CU    CU B 605                 O   HOH B 867     1555   1555  2.07  
LINK        CU    CU B 605                 O   HOH B 772     1555   1555  2.28  
LINK        CU    CU C 601                 O   HOH C 803     1555   1555  2.25  
LINK        CU    CU C 601                 O   HOH C 756     1555   1555  2.29  
LINK        CU    CU C 602                 O   HOH C 835     1555   1555  2.54  
LINK        CU    CU C 603                 O   HOH C 745     1555   1555  2.65  
LINK        CU    CU C 603                 O   HOH C 894     1555   1555  2.37  
LINK        CU    CU C 606                 O   HOH C 900     1555   1555  2.29  
LINK        CU    CU C 607                 O   HOH C 737     1555   1555  2.04  
LINK        CU    CU C 608                 O   HOH C 887     1555   1555  2.48  
LINK        CU    CU D 602                 O   HOH D 746     1555   1555  2.52  
LINK        CU    CU D 603                 O   HOH D 847     1555   1555  1.88  
LINK        CU    CU D 604                 O   HOH D 885     1555   1555  2.41  
LINK        CU    CU D 605                 O   HOH D 746     1555   1555  1.72  
LINK        CU    CU D 606                 O   HOH D 889     1555   1555  2.14  
LINK        CU    CU D 608                 O   HOH D 874     1555   1555  2.12  
CISPEP   1 TYR A  432    PRO A  433          0         7.69                     
CISPEP   2 SER A  455    PRO A  456          0         8.81                     
CISPEP   3 TYR B  432    PRO B  433          0        10.39                     
CISPEP   4 SER B  455    PRO B  456          0         9.40                     
CISPEP   5 TYR C  432    PRO C  433          0        -0.08                     
CISPEP   6 SER C  455    PRO C  456          0         6.89                     
CISPEP   7 TYR D  432    PRO D  433          0        12.20                     
CISPEP   8 SER D  455    PRO D  456          0         3.69                     
SITE     1 AC1  4 HIS A 206  ASP A 314  HIS A 381  HOH A 711                    
SITE     1 AC2  7 LYS A 103  HIS A 135  HIS A 136  HIS A 528                    
SITE     2 AC2  7  CU A 605  HOH A 826  HOH A 894                               
SITE     1 AC3  4 TRP A 452  ASP A 480  HIS A 482  HOH A 907                    
SITE     1 AC4  4 PHE A 436  HIS A 437  HIS A 482  HIS A 528                    
SITE     1 AC5  6 HIS A 135  HIS A 136   CU A 602  HOH A 826                    
SITE     2 AC5  6 HOH A 878  HOH A 894                                          
SITE     1 AC6  2 HIS A 411  ASP A 412                                          
SITE     1 AC7  2 HIS A 309  HOH A 881                                          
SITE     1 AC8  4 HIS B 206  ASP B 314  HIS B 381  HOH B 815                    
SITE     1 AC9  6 HIS B 135  HIS B 136  HIS B 528   CU B 605                    
SITE     2 AC9  6 HOH B 772  HOH B 867                                          
SITE     1 AD1  4 TRP B 452  ASP B 480  HIS B 482  HOH B 829                    
SITE     1 AD2  3 HIS B 437  HIS B 482  HOH B 867                               
SITE     1 AD3  7 HIS B 135  HIS B 136   CU B 602  HOH B 772                    
SITE     2 AD3  7 HOH B 815  HOH B 819  HOH B 867                               
SITE     1 AD4  2 HIS B 411  ASP B 412                                          
SITE     1 AD5  5 HIS C 206  ASP C 314  HIS C 381  HOH C 756                    
SITE     2 AD5  5 HOH C 803                                                     
SITE     1 AD6  5 LYS C 103  HIS C 135  HIS C 528   CU C 605                    
SITE     2 AD6  5 HOH C 835                                                     
SITE     1 AD7  5 TRP C 452  ASP C 480  HIS C 482  HOH C 745                    
SITE     2 AD7  5 HOH C 894                                                     
SITE     1 AD8  4 PHE C 436  HIS C 437  HIS C 482  HOH C 875                    
SITE     1 AD9  5 HIS C 135  HIS C 136   CU C 602  HOH C 835                    
SITE     2 AD9  5 HOH C 875                                                     
SITE     1 AE1  2 GLU C 171  HOH C 900                                          
SITE     1 AE2  3 HIS C 411  ASP C 412  HOH C 737                               
SITE     1 AE3  2 HIS C 309  HOH C 887                                          
SITE     1 AE4  3 HIS D 206  ASP D 314  HIS D 381                               
SITE     1 AE5  6 LYS D 103  HIS D 135  HIS D 136  HIS D 528                    
SITE     2 AE5  6  CU D 605  HOH D 746                                          
SITE     1 AE6  6 TRP D 452  ASP D 480  HIS D 482  HIS D 528                    
SITE     2 AE6  6 HOH D 825  HOH D 847                                          
SITE     1 AE7  5 PHE D 436  HIS D 437  HIS D 482  HIS D 528                    
SITE     2 AE7  5 HOH D 885                                                     
SITE     1 AE8  8 HIS D 135  HIS D 136  VAL D 205  HIS D 206                    
SITE     2 AE8  8 GLU D 288   CU D 602  HOH D 746  HOH D 885                    
SITE     1 AE9  4 LEU D  93  TYR D  96  ASP D 489  HOH D 889                    
SITE     1 AF1  1 HIS D 411                                                     
SITE     1 AF2  2 HIS D 309  HOH D 874                                          
CRYST1   90.640  162.370   90.710  90.00 119.64  90.00 P 1 21 1      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      0.011033  0.000000  0.006278        0.00000                         
SCALE2      0.000000  0.006159  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012684        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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