GenomeNet

Database: PDB
Entry: 6G50
LinkDB: 6G50
Original site: 6G50 
HEADER    OXIDOREDUCTASE                          28-MAR-18   6G50              
TITLE     THE STRUCTURE OF THIOCYANATE DEHYDROGENASE FROM THIOALKALIVIBRIO      
TITLE    2 PARADOXUS AS ISOLATED.                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UNCHARACTERIZED PROTEIN;                                   
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   3   22-JUL-20 6G50    1       JRNL                                     
REVDAT   2   14-AUG-19 6G50    1       SPRSDE REMARK                            
REVDAT   1   10-APR-19 6G50    0                                                
SPRSDE     14-AUG-19 6G50      5F30                                             
JRNL        AUTH   T.V.TIKHONOVA,D.Y.SOROKIN,W.R.HAGEN,M.G.KHRENOVA,G.MUYZER,   
JRNL        AUTH 2 T.V.RAKITINA,I.G.SHABALIN,A.A.TROFIMOV,S.I.TSALLAGOV,        
JRNL        AUTH 3 V.O.POPOV                                                    
JRNL        TITL   TRINUCLEAR COPPER BIOCATALYTIC CENTER FORMS AN ACTIVE SITE   
JRNL        TITL 2 OF THIOCYANATE DEHYDROGENASE.                                
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 117  5280 2020              
JRNL        REFN                   ESSN 1091-6490                               
JRNL        PMID   32094184                                                     
JRNL        DOI    10.1073/PNAS.1922133117                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.65 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) : 1.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.31                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 238854                         
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) : 0.147                           
REMARK   3   R VALUE            (WORKING SET) : 0.143                           
REMARK   3   FREE R VALUE                     : 0.207                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 26618                           
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) : 1.65                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.69                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4859                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.30                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2210                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 14118                        
REMARK   3   BIN FREE R VALUE                    : 0.3010                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 14572                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 69                                      
REMARK   3   SOLVENT ATOMS            : 1531                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.44                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -4.43000                                             
REMARK   3    B22 (A**2) : 8.37000                                              
REMARK   3    B33 (A**2) : -3.95000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.36000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.016         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.019         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.036         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.978         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.969                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.960                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 15207 ; 0.016 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 20729 ; 1.901 ; 1.944       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1878 ; 7.862 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   682 ;35.268 ;24.457       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2403 ;14.413 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    70 ;20.494 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2247 ; 0.133 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 11678 ; 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):  7503 ; 1.407 ; 1.749       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  9380 ; 1.939 ; 2.625       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  7704 ; 1.982 ;36.760       
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): 24820 ; 4.121 ;25.712       
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):     1 ;12.756 ; 5.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):     3 ;10.831 ; 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 : 0.551                                           
REMARK   3      TWIN DOMAIN   : 2                                               
REMARK   3      TWIN OPERATOR : L, -K, H                                        
REMARK   3      TWIN FRACTION : 0.449                                           
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 6G50 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-MAR-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200009402.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-FEB-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98400                            
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   : 691361                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.650                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.400                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.3                               
REMARK 200  DATA REDUNDANCY                : 2.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.2000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.70                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.650                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
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   (%): 56.11                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PRECIPITANT SOLUTION: 0.2 M LITHIUM      
REMARK 280  SULFATE, 0.1 M BIS-TRIS, PH 5.5, 25% W/V PEG 3350. PROTEIN          
REMARK 280  SOLUTION: TCDH 10 MG/ML 25 MM BORATE, PH 9.5, VAPOR DIFFUSION,      
REMARK 280  HANGING DROP, TEMPERATURE 290K                                      
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       81.14000            
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: 7110 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 28500 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -159.0 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: 16100 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 55570 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -324.0 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: 7250 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 28800 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -170.0 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 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   CB  -  CG  -  CD2 ANGL. DEV. = -10.3 DEGREES          
REMARK 500    ARG A 231   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    ASP A 529   CB  -  CG  -  OD1 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ARG B 188   NE  -  CZ  -  NH1 ANGL. DEV. =   4.4 DEGREES          
REMARK 500    ASP B 214   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ASP B 388   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ASP C 214   CB  -  CG  -  OD1 ANGL. DEV. =   6.7 DEGREES          
REMARK 500    ASP C 407   CB  -  CG  -  OD1 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ARG C 535   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    ARG D 231   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    ARG D 237   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG D 237   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    THR D 435   CA  -  CB  -  CG2 ANGL. DEV. =  -9.2 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     -117.64     53.28                                   
REMARK 500    CYS A 131       70.00   -158.64                                   
REMARK 500    HIS A 135      -77.06    -96.39                                   
REMARK 500    THR A 187      -50.56   -133.67                                   
REMARK 500    VAL A 205     -132.76   -109.96                                   
REMARK 500    ASP A 276       54.37   -113.32                                   
REMARK 500    LYS A 323      -44.44     68.50                                   
REMARK 500    GLN A 382      146.18     64.08                                   
REMARK 500    ALA A 383      -56.82   -124.25                                   
REMARK 500    LEU A 398      -75.78     81.93                                   
REMARK 500    PHE A 436      -77.87   -108.02                                   
REMARK 500    ASP A 480       62.59     62.75                                   
REMARK 500    HIS A 482      -91.30   -109.34                                   
REMARK 500    GLN A 501       -1.95     75.81                                   
REMARK 500    THR A 503     -158.72   -123.86                                   
REMARK 500    SER A 543     -156.61   -123.75                                   
REMARK 500    SER A 545      -59.66   -154.16                                   
REMARK 500    LYS B 103     -112.15     50.47                                   
REMARK 500    THR B 115      -17.55   -144.22                                   
REMARK 500    CYS B 131       69.82   -151.35                                   
REMARK 500    HIS B 135      -80.82    -96.35                                   
REMARK 500    THR B 187      -54.32   -129.00                                   
REMARK 500    VAL B 205     -129.25   -106.70                                   
REMARK 500    ASP B 276       56.83   -116.20                                   
REMARK 500    ARG B 306       59.25   -149.52                                   
REMARK 500    LYS B 323      -50.17     68.84                                   
REMARK 500    PRO B 356      173.56    -57.92                                   
REMARK 500    LEU B 398      -73.67     77.82                                   
REMARK 500    PHE B 436      -86.41   -107.43                                   
REMARK 500    HIS B 482      -90.38   -109.45                                   
REMARK 500    GLN B 501       -4.10     66.27                                   
REMARK 500    THR B 503     -148.60   -115.44                                   
REMARK 500    SER B 543     -157.00   -126.24                                   
REMARK 500    SER B 545      -57.63   -144.13                                   
REMARK 500    LYS C 103     -112.41     58.78                                   
REMARK 500    HIS C 135      -83.49   -104.78                                   
REMARK 500    GLU C 148      144.01   -172.26                                   
REMARK 500    THR C 187      -51.38   -136.86                                   
REMARK 500    VAL C 205     -131.50   -117.22                                   
REMARK 500    ASP C 276       55.63   -117.77                                   
REMARK 500    ARG C 306       46.62   -152.02                                   
REMARK 500    ALA C 312       61.20     60.95                                   
REMARK 500    LYS C 323      -49.83     69.34                                   
REMARK 500    HIS C 381      -85.47   -153.07                                   
REMARK 500    HIS C 381     -112.07   -164.16                                   
REMARK 500    GLN C 382      130.76    -18.13                                   
REMARK 500    LEU C 398      -80.44     75.68                                   
REMARK 500    ASP C 413       87.97   -152.12                                   
REMARK 500    HIS C 482      -89.80   -112.82                                   
REMARK 500    ASN C 502       -5.44   -142.79                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      74 RAMACHANDRAN OUTLIERS.                        
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 A1082        DISTANCE =  6.18 ANGSTROMS                       
REMARK 525    HOH A1083        DISTANCE =  6.70 ANGSTROMS                       
REMARK 525    HOH C1099        DISTANCE =  9.51 ANGSTROMS                       
REMARK 525    HOH D1092        DISTANCE =  5.90 ANGSTROMS                       
REMARK 525    HOH D1093        DISTANCE =  8.19 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 601  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 206   NE2                                                    
REMARK 620 2 ASP A 314   OD2  90.5                                              
REMARK 620 3 ASP A 314   OD2  88.0   5.8                                        
REMARK 620 4 HIS A 381   NE2 174.7  88.1  91.0                                  
REMARK 620 N                    1     2     3                                   
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 111.4                                              
REMARK 620 3 SO4 B 605   O4  133.6 101.5                                        
REMARK 620 4 HOH B 769   O    92.4 102.4 111.8                                  
REMARK 620 N                    1     2     3                                   
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 HOH B1001   O   149.4                                              
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 100.5                                              
REMARK 620 3 ASP C 314   OD2 104.9  55.1                                        
REMARK 620 4 HIS C 381   NE2 162.0  93.7  92.2                                  
REMARK 620 5 HOH C 716   O    87.9 122.5  67.7  93.6                            
REMARK 620 N                    1     2     3     4                             
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 SER C 397   OG                                                     
REMARK 620 2 HOH C 779   O   137.8                                              
REMARK 620 N                    1                                               
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 114.7                                              
REMARK 620 3 SO4 D 604   O3  112.6 105.7                                        
REMARK 620 4 HOH D 763   O    97.9 110.8 115.4                                  
REMARK 620 N                    1     2     3                                   
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 100.1                                              
REMARK 620 3 HIS D 381   NE2 172.4  75.6                                        
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 SER D 397   OG                                                     
REMARK 620 2 HOH D 842   O   136.6                                              
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 SO4 A 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU B 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU B 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU B 603                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU B 604                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU C 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU C 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU C 603                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO C 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU D 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU D 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU D 603                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 607                 
DBREF  6G50 A   82   548  UNP    W0DP94   W0DP94_9GAMM    82    548             
DBREF  6G50 B   82   548  UNP    W0DP94   W0DP94_9GAMM    82    548             
DBREF  6G50 C   82   548  UNP    W0DP94   W0DP94_9GAMM    82    548             
DBREF  6G50 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 CYS 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 CYS 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 CYS 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 CYS 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              
HET     CU  A 601       1                                                       
HET     CU  A 602       1                                                       
HET     CU  A 603       1                                                       
HET    SO4  A 604       5                                                       
HET     CU  B 601       1                                                       
HET     CU  B 602       1                                                       
HET     CU  B 603       1                                                       
HET     CU  B 604       1                                                       
HET    SO4  B 605       5                                                       
HET     CU  C 601       1                                                       
HET     CU  C 602       1                                                       
HET     CU  C 603       1                                                       
HET    SO4  C 604       5                                                       
HET    SO4  C 605       5                                                       
HET    SO4  C 606      10                                                       
HET    SO4  C 607       5                                                       
HET    EDO  C 608       4                                                       
HET    EDO  C 609       4                                                       
HET     CU  D 601       1                                                       
HET     CU  D 602       1                                                       
HET     CU  D 603       1                                                       
HET    SO4  D 604       5                                                       
HET    SO4  D 605       5                                                       
HET    EDO  D 606       4                                                       
HET    EDO  D 607       4                                                       
HETNAM      CU COPPER (II) ION                                                  
HETNAM     SO4 SULFATE ION                                                      
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   5   CU    13(CU 2+)                                                    
FORMUL   8  SO4    8(O4 S 2-)                                                   
FORMUL  21  EDO    4(C2 H6 O2)                                                  
FORMUL  30  HOH   *1531(H2 O)                                                   
HELIX    1 AA1 LYS A   85  GLN A   92  1                                   8    
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 LEU A  270  ARG A  274  5                                   5    
HELIX    7 AA7 GLY A  292  ASP A  299  1                                   8    
HELIX    8 AA8 ARG A  306  SER A  310  5                                   5    
HELIX    9 AA9 ASP A  413  TRP A  417  5                                   5    
HELIX   10 AB1 SER A  425  ARG A  429  5                                   5    
HELIX   11 AB2 GLY A  499  ASN A  502  5                                   4    
HELIX   12 AB3 THR A  536  ARG A  541  1                                   6    
HELIX   13 AB4 LYS B   85  GLN B   92  1                                   8    
HELIX   14 AB5 LYS B  103  SER B  105  5                                   3    
HELIX   15 AB6 TRP B  125  GLY B  128  5                                   4    
HELIX   16 AB7 GLY B  158  ILE B  163  5                                   6    
HELIX   17 AB8 ALA B  195  GLY B  200  1                                   6    
HELIX   18 AB9 GLY B  292  ASP B  299  1                                   8    
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 THR B  536  ARG B  541  1                                   6    
HELIX   23 AC5 VAL C   86  GLY C   94  1                                   9    
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  158  ILE C  163  5                                   6    
HELIX   27 AC9 ALA C  195  GLY C  200  1                                   6    
HELIX   28 AD1 GLY C  292  ASP C  299  1                                   8    
HELIX   29 AD2 ARG C  306  SER C  310  5                                   5    
HELIX   30 AD3 ASP C  413  TRP C  417  5                                   5    
HELIX   31 AD4 SER C  425  ARG C  429  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 ARG D  306  SER D  310  5                                   5    
HELIX   42 AE6 ASP D  413  TRP D  417  5                                   5    
HELIX   43 AE7 TYR D  500  ASN D  502  5                                   3    
HELIX   44 AE8 THR D  536  ARG D  541  1                                   6    
SHEET    1 AA1 4 THR A 118  ALA A 123  0                                        
SHEET    2 AA1 4 THR A 107  ASP A 112 -1  N  ALA A 110   O  MET A 119           
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  ASP A 365 -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  VAL A 344   N  ASP A 339           
SHEET    5 AA4 5 GLN A 358  PHE A 359 -1  O  PHE A 359   N  VAL A 348           
SHEET    1 AA5 4 GLY A 384  PHE A 385  0                                        
SHEET    2 AA5 4 SER A 391  ASN A 396 -1  O  LEU A 393   N  GLY A 384           
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  LYS A 420   N  VAL A 405           
SHEET    1 AA6 4 ASN A 434  PHE A 440  0                                        
SHEET    2 AA6 4 LYS A 446  TRP A 452 -1  O  THR A 450   N  PHE A 436           
SHEET    3 AA6 4 ASN A 459  ASP A 465 -1  O  ALA A 462   N  VAL A 449           
SHEET    4 AA6 4 GLU A 470  GLY A 478 -1  O  GLU A 470   N  ASP A 465           
SHEET    1 AA7 4 MET A 481  ILE A 486  0                                        
SHEET    2 AA7 4 PHE A 492  LEU A 497 -1  O  THR A 496   N  HIS A 482           
SHEET    3 AA7 4 ALA A 506  GLU A 511 -1  O  MET A 510   N  VAL A 493           
SHEET    4 AA7 4 GLU A 516  PRO A 522 -1  O  LEU A 518   N  VAL A 509           
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  MET B 119           
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 GLY B 176  TYR B 184 -1  O  TYR B 184   N  PHE B 149           
SHEET    4 AA9 4 MET B 189  ASP B 194 -1  O  GLN B 192   N  ARG B 181           
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  ARG B 237   N  GLU B 228           
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  PHE B 338   N  ALA B 325           
SHEET    4 AB2 5 VAL B 344  ALA B 350 -1  O  ALA B 347   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  LEU B 393   N  GLY B 384           
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  GLU B 418   N  ASP B 407           
SHEET    1 AB4 4 ASN B 434  PHE B 440  0                                        
SHEET    2 AB4 4 LYS B 446  TRP B 452 -1  O  THR B 450   N  PHE B 436           
SHEET    3 AB4 4 ASN B 459  ASP B 465 -1  O  ILE B 464   N  ILE B 447           
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  MET B 510   N  VAL B 493           
SHEET    4 AB5 4 GLU B 516  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  ASN C 154   N  HIS C 135           
SHEET    3 AB7 4 GLY C 176  TYR C 184 -1  O  TYR C 184   N  PHE C 149           
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  LYS C 264   N  ALA C 241           
SHEET    6 AB8 7 THR C 368  ILE C 373 -1  O  TRP C 369   N  ILE C 263           
SHEET    7 AB8 7 LEU C 361  ASP C 365 -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 346   N  VAL C 337           
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  LYS C 420   N  VAL C 405           
SHEET    1 AC2 4 ASN C 434  PHE C 440  0                                        
SHEET    2 AC2 4 LYS C 446  TRP C 452 -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  PRO C 522 -1  O  LEU C 518   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 180   N  VAL D 153           
SHEET    4 AC5 4 MET D 189  ASP D 194 -1  O  GLN D 192   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  ARG D 237   N  GLU D 228           
SHEET    5 AC6 7 GLY D 259  LEU D 266 -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 5 ASN D 313  PHE D 318  0                                        
SHEET    2 AC7 5 TRP D 324  MET D 329 -1  O  VAL D 326   N  VAL D 317           
SHEET    3 AC7 5 VAL D 334  ASP D 339 -1  O  PHE D 338   N  ALA D 325           
SHEET    4 AC7 5 VAL D 344  ALA D 350 -1  O  ALA D 347   N  VAL D 337           
SHEET    5 AC7 5 GLN D 358  PHE D 359 -1  O  PHE D 359   N  VAL D 348           
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  MET D 404   N  PHE D 394           
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  ILE D 464   N  ILE D 447           
SHEET    4 AC9 4 GLU D 470  GLY D 478 -1  O  LEU D 477   N  ASN D 459           
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  MET D 510   N  VAL D 493           
SHEET    4 AD1 4 GLU D 516  PRO D 522 -1  O  LEU D 518   N  VAL D 509           
LINK         OD2 ASP A  88                CU    CU A 603     1555   1555  2.09  
LINK         NH1 ARG A 193                CU    CU A 602     1555   1555  1.85  
LINK         NE2 HIS A 206                CU    CU A 601     1555   1555  2.06  
LINK         OD2AASP A 314                CU    CU A 601     1555   1555  1.93  
LINK         OD2BASP A 314                CU    CU A 601     1555   1555  1.95  
LINK         NE2AHIS A 381                CU    CU A 601     1555   1555  2.00  
LINK         NE2 HIS B 135                CU    CU B 602     1555   1555  2.26  
LINK         NH2 ARG B 193                CU    CU B 603     1555   1555  2.07  
LINK         NE2 HIS B 206                CU    CU B 601     1555   1555  2.05  
LINK         OG  SER B 397                CU    CU B 604     1555   1555  2.24  
LINK         ND1 HIS B 528                CU    CU B 602     1555   1555  2.02  
LINK         OD1 ASP C  88                CU    CU C 603     1555   1555  2.21  
LINK         NE2 HIS C 206                CU    CU C 601     1555   1555  2.05  
LINK         OD1AASP C 314                CU    CU C 601     1555   1555  2.55  
LINK         OD2AASP C 314                CU    CU C 601     1555   1555  1.98  
LINK         NE2AHIS C 381                CU    CU C 601     1555   1555  2.01  
LINK         OG  SER C 397                CU    CU C 602     1555   1555  1.71  
LINK         NE2 HIS D 135                CU    CU D 602     1555   1555  2.18  
LINK         NE2 HIS D 206                CU    CU D 601     1555   1555  2.05  
LINK         OD2 ASP D 314                CU    CU D 601     1555   1555  1.98  
LINK         NE2AHIS D 381                CU    CU D 601     1555   1555  2.01  
LINK         OG  SER D 397                CU    CU D 603     1555   1555  1.83  
LINK         ND1 HIS D 528                CU    CU D 602     1555   1555  1.88  
LINK        CU    CU B 601                 O   HOH B1001     1555   1555  2.43  
LINK        CU    CU B 602                 O4  SO4 B 605     1555   1555  1.99  
LINK        CU    CU B 602                 O   HOH B 769     1555   1555  1.96  
LINK        CU    CU C 601                 O   HOH C 716     1555   1555  2.52  
LINK        CU    CU C 602                 O   HOH C 779     1555   1555  1.83  
LINK        CU    CU D 602                 O3  SO4 D 604     1555   1555  1.81  
LINK        CU    CU D 602                 O   HOH D 763     1555   1555  2.01  
LINK        CU    CU D 603                 O   HOH D 842     1555   1555  1.84  
CISPEP   1 TYR A  432    PRO A  433          0         9.06                     
CISPEP   2 SER A  455    PRO A  456          0         6.10                     
CISPEP   3 TYR B  432    PRO B  433          0         2.10                     
CISPEP   4 SER B  455    PRO B  456          0        16.85                     
CISPEP   5 TYR C  432    PRO C  433          0         2.20                     
CISPEP   6 SER C  455    PRO C  456          0        12.12                     
CISPEP   7 TYR D  432    PRO D  433          0         2.69                     
CISPEP   8 SER D  455    PRO D  456          0         5.12                     
SITE     1 AC1  5 HIS A 206  ASP A 314  HIS A 381  HIS A 437                    
SITE     2 AC1  5 SO4 A 604                                                     
SITE     1 AC2  2 ARG A 181  ARG A 193                                          
SITE     1 AC3  3 VAL A  84  LYS A  85  ASP A  88                               
SITE     1 AC4 11 HIS A 135  HIS A 136  HIS A 206  GLU A 288                    
SITE     2 AC4 11 HIS A 381  PHE A 436  HIS A 437  HIS A 482                    
SITE     3 AC4 11 HIS A 528   CU A 601  HOH A 782                               
SITE     1 AC5  4 HIS B 206  HIS B 437  SO4 B 605  HOH B1001                    
SITE     1 AC6  4 HIS B 135  HIS B 528  SO4 B 605  HOH B 769                    
SITE     1 AC7  3 ARG B 193  ARG B 231  GLU B 232                               
SITE     1 AC8  4 ASN B 396  SER B 397  ASN B 434  THR B 435                    
SITE     1 AC9  9 HIS B 135  HIS B 136  HIS B 206  HIS B 437                    
SITE     2 AC9  9 HIS B 528   CU B 601   CU B 602  HOH B 713                    
SITE     3 AC9  9 HOH B 823                                                     
SITE     1 AD1  5 HIS C 206  ASP C 314  HIS C 381  SO4 C 606                    
SITE     2 AD1  5 HOH C 716                                                     
SITE     1 AD2  7 HIS C 381  ASN C 396  SER C 397  ASN C 434                    
SITE     2 AD2  7 THR C 435  HOH C 727  HOH C 779                               
SITE     1 AD3  3 GLN C  87  ASP C  88  ASP C  91                               
SITE     1 AD4  7 ARG C 399  HOH C 736  HOH C 750  LYS D 183                    
SITE     2 AD4  7 GLN D 192  EDO D 606  EDO D 607                               
SITE     1 AD5  6 LYS C 183  GLN C 192  EDO C 608  EDO C 609                    
SITE     2 AD5  6 HOH C 772  ARG D 399                                          
SITE     1 AD6 15 HIS C 135  HIS C 136  VAL C 205  HIS C 206                    
SITE     2 AD6 15 GLU C 288  HIS C 381  PHE C 436  HIS C 437                    
SITE     3 AD6 15 HIS C 482  HIS C 528   CU C 601  HOH C 701                    
SITE     4 AD6 15 HOH C 703  HOH C 897  HOH C 972                               
SITE     1 AD7  7 GLY C 128  ASP C 129  THR C 130  GLY C 174                    
SITE     2 AD7  7 LYS C 178  HOH C 785  HOH C 817                               
SITE     1 AD8  7 ARG C 193  SO4 C 605  EDO C 609  HOH C 849                    
SITE     2 AD8  7 LEU D 398  ARG D 399  ALA D 431                               
SITE     1 AD9  7 GLU C 150  ARG C 181  GLN C 192  ARG C 193                    
SITE     2 AD9  7 ASP C 234  SO4 C 605  EDO C 608                               
SITE     1 AE1  4 HIS D 206  ASP D 314  HIS D 381  SO4 D 604                    
SITE     1 AE2  5 LYS D 103  HIS D 135  HIS D 528  SO4 D 604                    
SITE     2 AE2  5 HOH D 763                                                     
SITE     1 AE3  6 HIS D 381  ASN D 396  SER D 397  ASN D 434                    
SITE     2 AE3  6 THR D 435  HOH D 842                                          
SITE     1 AE4 11 HIS D 135  HIS D 136  PHE D 436  HIS D 437                    
SITE     2 AE4 11 HIS D 482  HIS D 528   CU D 601   CU D 602                    
SITE     3 AE4 11 HOH D 717  HOH D 740  HOH D 934                               
SITE     1 AE5  6 GLY D 128  ASP D 129  THR D 130  LYS D 178                    
SITE     2 AE5  6 HOH D 806  HOH D 831                                          
SITE     1 AE6  6 LEU C 398  ALA C 431  SO4 C 604  ARG D 193                    
SITE     2 AE6  6 EDO D 607  HOH D 788                                          
SITE     1 AE7  6 SO4 C 604  ARG D 181  GLN D 192  ARG D 193                    
SITE     2 AE7  6 ASP D 234  EDO D 606                                          
CRYST1   90.630  162.280   90.570  90.00 119.51  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      0.011034  0.000000  0.006245        0.00000                         
SCALE2      0.000000  0.006162  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012687        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system