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Database: PDB
Entry: 6SJI
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Original site: 6SJI 
HEADER    OXIDOREDUCTASE                          13-AUG-19   6SJI              
TITLE     THE STRUCTURE OF THIOCYANATE DEHYDROGENASE FROM THIOALKALIVIBRIO      
TITLE    2 PARADOXUS MUTANT WITH HIS 482 REPLACED BY GLN                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: THIOCYANATE DEHYDROGENASE;                                 
COMPND   3 CHAIN: A, B, J, K;                                                   
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: THIOALKALIVIBRIO PARADOXUS ARH 1;               
SOURCE   3 ORGANISM_TAXID: 713585;                                              
SOURCE   4 GENE: THITH_13335;                                                   
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008                                      
KEYWDS    OXIDOREDUCTASE, THIOCYANATE DEHYDROGENASE, COPPER CENTERS             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.M.POLYAKOV,T.V.TIKHONOVA,T.V.RAKITINA,E.OSIPOV,V.O.POPOV            
REVDAT   3   18-MAR-20 6SJI    1       JRNL                                     
REVDAT   2   04-MAR-20 6SJI    1       JRNL                                     
REVDAT   1   18-SEP-19 6SJI    0                                                
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.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0158 2016/10/03                           
REMARK   3   AUTHORS     : NULL                                                 
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 89.97                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 176251                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : FREE R-VALUE                    
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.159                           
REMARK   3   FREE R VALUE                     : 0.198                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 8761                            
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) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.85                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 12547                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.81                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2300                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 669                          
REMARK   3   BIN FREE R VALUE                    : 0.2720                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 14585                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 24                                      
REMARK   3   SOLVENT ATOMS            : 1183                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.99                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.11200                                              
REMARK   3    B22 (A**2) : 0.17600                                              
REMARK   3    B33 (A**2) : 0.03200                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -1.12800                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.115         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.113         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.094         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.105         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.971                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.956                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 15094 ; 0.020 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 20558 ; 1.937 ; 1.943       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1869 ; 7.447 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   674 ;34.672 ;24.540       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2371 ;13.884 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    70 ;20.739 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2236 ; 0.145 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 11606 ; 0.012 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A): 13902 ; 0.197 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A): 20452 ; 0.306 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  2420 ; 0.119 ; 0.200       
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):  7482 ; 1.897 ; 2.180       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  9346 ; 2.538 ; 3.259       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  7611 ; 3.011 ;47.910       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 11211 ; 4.336 ; 3.539       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  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):     9 ;16.629 ; 5.000       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
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: HYDROGENS HAVE BEEN ADDED IN THEIR        
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 6SJI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-AUG-19.                  
REMARK 100 THE DEPOSITION ID IS D_1292103828.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-DEC-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID30B                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.968623                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 176251                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 90.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.2                               
REMARK 200  DATA REDUNDANCY                : 2.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.6300                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.85                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.57                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.200                              
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: 5OEX                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.45                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.17M AMMONIUM ACETATE, 0.085 M SODIUM   
REMARK 280  CACJDILATE PH 6.5, 25.5 % V/V POLYATILEN GLYCOL 8000, 15% V/V       
REMARK 280  GLYCEROL, VAPOR DIFFUSION, 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       80.20500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 13960 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 55740 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -211.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, J, K                            
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     ALA B    79                                                      
REMARK 465     MET B    80                                                      
REMARK 465     GLY B    81                                                      
REMARK 465     ALA J    79                                                      
REMARK 465     MET J    80                                                      
REMARK 465     GLY J    81                                                      
REMARK 465     ALA K    79                                                      
REMARK 465     MET K    80                                                      
REMARK 465     GLY K    81                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU J 538   CD    GLU J 538   OE1     0.071                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 193   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    ARG A 193   NE  -  CZ  -  NH1 ANGL. DEV. =   3.9 DEGREES          
REMARK 500    ARG A 193   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    ASP A 214   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    LEU A 398   CA  -  CB  -  CG  ANGL. DEV. =  17.2 DEGREES          
REMARK 500    LEU A 398   CB  -  CG  -  CD2 ANGL. DEV. = -10.2 DEGREES          
REMARK 500    ARG A 399   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ARG A 399   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    LEU A 472   CA  -  CB  -  CG  ANGL. DEV. =  14.6 DEGREES          
REMARK 500    ARG A 535   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.9 DEGREES          
REMARK 500    ARG A 535   NE  -  CZ  -  NH2 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    ASP B 388   CB  -  CG  -  OD1 ANGL. DEV. =   8.0 DEGREES          
REMARK 500    ASP B 443   CB  -  CG  -  OD1 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ARG J 188   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ARG J 193   NE  -  CZ  -  NH1 ANGL. DEV. =   6.7 DEGREES          
REMARK 500    ARG J 193   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    ASP J 214   CB  -  CG  -  OD1 ANGL. DEV. =   8.3 DEGREES          
REMARK 500    ARG J 306   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ASP J 319   CB  -  CG  -  OD1 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ASP J 319   CB  -  CG  -  OD2 ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    ASP J 407   CB  -  CG  -  OD1 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ASP J 407   CB  -  CG  -  OD2 ANGL. DEV. =  -5.4 DEGREES          
REMARK 500    ASP J 443   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ARG J 544   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG J 544   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    ARG K 188   NE  -  CZ  -  NH1 ANGL. DEV. =   4.4 DEGREES          
REMARK 500    ASP K 214   CB  -  CG  -  OD1 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ARG K 429   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    ASP K 443   CB  -  CG  -  OD1 ANGL. DEV. =   7.4 DEGREES          
REMARK 500    ARG K 535   NE  -  CZ  -  NH1 ANGL. DEV. =   5.1 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    MET A  80       -8.10    120.51                                   
REMARK 500    LYS A 103     -118.51     55.94                                   
REMARK 500    THR A 115      -17.43   -144.56                                   
REMARK 500    CYS A 131       68.35   -151.78                                   
REMARK 500    HIS A 135      -91.29   -110.93                                   
REMARK 500    GLU A 148      145.98   -170.39                                   
REMARK 500    THR A 187      -48.89   -132.12                                   
REMARK 500    VAL A 205     -130.57   -113.21                                   
REMARK 500    ASP A 234       18.32     59.78                                   
REMARK 500    ASP A 276       58.84   -118.47                                   
REMARK 500    ARG A 306       53.14   -144.17                                   
REMARK 500    LYS A 323      -48.03     76.48                                   
REMARK 500    HIS A 381      -85.16   -146.27                                   
REMARK 500    SER A 397       26.11   -153.93                                   
REMARK 500    LEU A 398      -63.54   -138.67                                   
REMARK 500    THR A 435       66.05   -103.85                                   
REMARK 500    GLN A 482     -110.96   -114.18                                   
REMARK 500    GLN A 501       -0.71     71.13                                   
REMARK 500    ASN A 502       -5.29   -141.44                                   
REMARK 500    THR A 503     -149.38   -124.74                                   
REMARK 500    SER A 523       89.89   -157.69                                   
REMARK 500    HIS A 527      121.53    -29.53                                   
REMARK 500    SER A 543     -161.21   -119.13                                   
REMARK 500    SER A 545      -56.61   -153.76                                   
REMARK 500    LYS B 103     -114.84     61.32                                   
REMARK 500    ALA B 120      149.81   -170.08                                   
REMARK 500    CYS B 131       74.93   -150.30                                   
REMARK 500    HIS B 135      -90.27   -107.90                                   
REMARK 500    ASP B 172       60.34   -113.66                                   
REMARK 500    THR B 187      -49.31   -132.14                                   
REMARK 500    VAL B 205     -135.32   -109.08                                   
REMARK 500    LYS B 249       49.80    -83.54                                   
REMARK 500    ASP B 276       60.10   -118.79                                   
REMARK 500    LEU B 277       36.83   -140.53                                   
REMARK 500    ARG B 306       49.49   -141.54                                   
REMARK 500    ASP B 314      -53.23   -120.27                                   
REMARK 500    LYS B 323      -48.16     76.55                                   
REMARK 500    HIS B 381      -82.26   -142.45                                   
REMARK 500    SER B 397       31.61   -147.51                                   
REMARK 500    LEU B 398      -74.62   -140.04                                   
REMARK 500    THR B 435       66.36   -105.88                                   
REMARK 500    ASP B 480       67.38     62.32                                   
REMARK 500    GLN B 482     -112.49   -118.40                                   
REMARK 500    ASN B 502       -6.12   -141.74                                   
REMARK 500    THR B 503     -148.56   -124.29                                   
REMARK 500    HIS B 527      119.72    -29.82                                   
REMARK 500    SER B 543     -157.03   -122.69                                   
REMARK 500    SER B 545      -56.73   -149.26                                   
REMARK 500    LYS J 103     -116.10     58.66                                   
REMARK 500    CYS J 131       74.96   -150.35                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      88 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 B1013        DISTANCE =  5.97 ANGSTROMS                       
REMARK 525    HOH B1014        DISTANCE =  9.68 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 140.8                                              
REMARK 620 3 HOH A 838   O   102.5 115.2                                        
REMARK 620 4 HOH A 824   O    99.7  90.8  90.2                                  
REMARK 620 N                    1     2     3                                   
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   OD1  93.4                                              
REMARK 620 3 ASP A 314   OD2  89.2  53.5                                        
REMARK 620 4 HIS A 381   NE2 178.9  87.6  90.9                                  
REMARK 620 5 HOH A 945   O    91.2 131.0 175.4  88.6                            
REMARK 620 N                    1     2     3     4                             
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 146.8                                              
REMARK 620 3 HOH B 738   O   105.5  84.7                                        
REMARK 620 4 HOH B 894   O   101.8 109.5  91.4                                  
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 ASP B 314   OD1  94.0                                              
REMARK 620 3 ASP B 314   OD2  90.5  55.0                                        
REMARK 620 4 HIS B 381   NE2 172.4  91.6  88.6                                  
REMARK 620 5 HOH B 890   O    90.5 127.5 177.2  90.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU J 602  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS J 135   NE2                                                    
REMARK 620 2 HIS J 528   ND1 142.8                                              
REMARK 620 3 HOH J 821   O    96.3  89.1                                        
REMARK 620 4 HOH J 807   O   103.5 113.1  91.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU J 601  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS J 206   NE2                                                    
REMARK 620 2 ASP J 314   OD1  92.5                                              
REMARK 620 3 ASP J 314   OD2  90.0  54.5                                        
REMARK 620 4 HIS J 381   NE2 175.0  92.5  93.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU K 602  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LYS K 103   NZ                                                     
REMARK 620 2 HIS K 135   NE2  86.8                                              
REMARK 620 3 HIS K 528   ND1  96.9 140.4                                        
REMARK 620 4 HOH K 790   O    82.0 103.5 116.1                                  
REMARK 620 5 HOH K 734   O   163.4 102.3  84.9  82.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU K 601  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS K 206   NE2                                                    
REMARK 620 2 ASP K 314   OD1  95.9                                              
REMARK 620 3 ASP K 314   OD2  92.1  53.3                                        
REMARK 620 4 HIS K 381   NE2 173.9  89.0  87.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU K 603  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS K 411   ND1                                                    
REMARK 620 2 ALA A  79   N    39.3                                              
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 SO4 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 J 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU J 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU K 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU K 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU K 603                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 K 604                 
DBREF  6SJI A   82   548  UNP    W0DP94   W0DP94_9GAMM    82    548             
DBREF  6SJI B   82   548  UNP    W0DP94   W0DP94_9GAMM    82    548             
DBREF  6SJI J   82   548  UNP    W0DP94   W0DP94_9GAMM    82    548             
DBREF  6SJI K   82   548  UNP    W0DP94   W0DP94_9GAMM    82    548             
SEQADV 6SJI ALA A   79  UNP  W0DP94              EXPRESSION TAG                 
SEQADV 6SJI MET A   80  UNP  W0DP94              EXPRESSION TAG                 
SEQADV 6SJI GLY A   81  UNP  W0DP94              EXPRESSION TAG                 
SEQADV 6SJI GLN A  482  UNP  W0DP94    HIS   482 CONFLICT                       
SEQADV 6SJI ALA B   79  UNP  W0DP94              EXPRESSION TAG                 
SEQADV 6SJI MET B   80  UNP  W0DP94              EXPRESSION TAG                 
SEQADV 6SJI GLY B   81  UNP  W0DP94              EXPRESSION TAG                 
SEQADV 6SJI GLN B  482  UNP  W0DP94    HIS   482 CONFLICT                       
SEQADV 6SJI ALA J   79  UNP  W0DP94              EXPRESSION TAG                 
SEQADV 6SJI MET J   80  UNP  W0DP94              EXPRESSION TAG                 
SEQADV 6SJI GLY J   81  UNP  W0DP94              EXPRESSION TAG                 
SEQADV 6SJI GLN J  482  UNP  W0DP94    HIS   482 CONFLICT                       
SEQADV 6SJI ALA K   79  UNP  W0DP94              EXPRESSION TAG                 
SEQADV 6SJI MET K   80  UNP  W0DP94              EXPRESSION TAG                 
SEQADV 6SJI GLY K   81  UNP  W0DP94              EXPRESSION TAG                 
SEQADV 6SJI GLN K  482  UNP  W0DP94    HIS   482 CONFLICT                       
SEQRES   1 A  470  ALA MET GLY LYS TYR VAL LYS VAL GLN ASP PHE TYR ASP          
SEQRES   2 A  470  GLN LEU GLY LYS TYR VAL LEU VAL ALA PRO GLY LYS PHE          
SEQRES   3 A  470  SER GLY THR VAL ALA ALA THR ASP LEU SER THR GLY TRP          
SEQRES   4 A  470  THR MET ALA TRP LEU ALA ALA TRP ASN TYR GLY ASP THR          
SEQRES   5 A  470  CYS PRO ILE MET HIS HIS MET ALA ALA PHE PRO SER PRO          
SEQRES   6 A  470  ASP PRO TYR LYS GLU PHE GLU PHE VAL VAL ASN THR GLN          
SEQRES   7 A  470  GLY GLY LYS ASN LEU PHE ILE TYR GLY VAL PRO VAL THR          
SEQRES   8 A  470  VAL GLU ASP PRO GLY GLU GLY MET LYS ILE TYR ARG ILE          
SEQRES   9 A  470  LYS TYR ASP GLY THR ARG MET ASN LEU GLN ARG ASP ALA          
SEQRES  10 A  470  ALA GLU VAL SER GLY LEU GLY LEU GLY VAL HIS VAL THR          
SEQRES  11 A  470  ILE THR PRO GLU ALA ASP GLY TYR ALA VAL GLY ASP GLY          
SEQRES  12 A  470  GLN LYS ASP ILE CYS ALA GLU PHE ASP ARG GLU THR ASP          
SEQRES  13 A  470  MET VAL ARG TYR ALA TRP ALA PHE ASP TRP ASP PRO ASN          
SEQRES  14 A  470  VAL LYS ASP LEU LYS ARG ALA TRP LEU ASP GLY GLY THR          
SEQRES  15 A  470  MET THR ILE LYS ARG LEU LYS PRO THR LEU PRO GLY GLY          
SEQRES  16 A  470  ARG TYR ASP LEU GLN GLY SER LYS GLY ASN LYS ILE ASP          
SEQRES  17 A  470  TRP GLU LEU VAL PRO GLY GLY GLU LEU ALA ILE GLU ASP          
SEQRES  18 A  470  GLY LYS VAL SER GLY ASP ARG PRO LEU HIS SER VAL ALA          
SEQRES  19 A  470  ASN ASP ALA LEU VAL PHE ASP PRO ARG GLY LYS TRP ALA          
SEQRES  20 A  470  VAL ALA SER MET ARG LEU PRO GLY VAL CYS VAL VAL PHE          
SEQRES  21 A  470  ASP ARG GLU ASN GLN VAL PRO VAL ALA VAL LEU ALA GLY          
SEQRES  22 A  470  PRO LYS GLY THR PRO SER GLN PHE GLN LEU VAL LYS VAL          
SEQRES  23 A  470  ASP ASP ASP THR TRP THR VAL ASP ILE PRO GLU VAL ILE          
SEQRES  24 A  470  SER ALA GLY HIS GLN ALA GLY PHE SER PRO ASP GLY GLN          
SEQRES  25 A  470  SER PHE LEU PHE MET ASN SER LEU ARG GLN ASN ASN ILE          
SEQRES  26 A  470  MET VAL TRP ASP SER SER ASN HIS ASP ASP PRO THR THR          
SEQRES  27 A  470  TRP GLU LYS LYS ALA VAL VAL GLU SER PRO ASP TRP ARG          
SEQRES  28 A  470  GLY ALA TYR PRO ASN THR PHE HIS MET VAL PHE THR PRO          
SEQRES  29 A  470  ASP ALA LYS LYS ILE TYR VAL THR MET TRP TRP PRO SER          
SEQRES  30 A  470  PRO THR PRO ASN GLY ILE ALA VAL ILE ASP ALA VAL ASN          
SEQRES  31 A  470  TRP GLU VAL LEU LYS GLU VAL ASP LEU GLY PRO ASP MET          
SEQRES  32 A  470  GLN THR LEU ALA ILE THR TYR ASP GLY LYS PHE VAL VAL          
SEQRES  33 A  470  GLY THR LEU SER GLY TYR GLN ASN THR ALA SER ALA ILE          
SEQRES  34 A  470  VAL VAL MET GLU THR GLU THR ASP GLU VAL LEU GLY PHE          
SEQRES  35 A  470  LEU PRO SER PRO MET GLY HIS HIS ASP ASN VAL ILE VAL          
SEQRES  36 A  470  PRO ARG THR LEU GLU ASP LEU ARG ILE SER ARG SER THR          
SEQRES  37 A  470  THR THR                                                      
SEQRES   1 B  470  ALA MET GLY LYS TYR VAL LYS VAL GLN ASP PHE TYR ASP          
SEQRES   2 B  470  GLN LEU GLY LYS TYR VAL LEU VAL ALA PRO GLY LYS PHE          
SEQRES   3 B  470  SER GLY THR VAL ALA ALA THR ASP LEU SER THR GLY TRP          
SEQRES   4 B  470  THR MET ALA TRP LEU ALA ALA TRP ASN TYR GLY ASP THR          
SEQRES   5 B  470  CYS PRO ILE MET HIS HIS MET ALA ALA PHE PRO SER PRO          
SEQRES   6 B  470  ASP PRO TYR LYS GLU PHE GLU PHE VAL VAL ASN THR GLN          
SEQRES   7 B  470  GLY GLY LYS ASN LEU PHE ILE TYR GLY VAL PRO VAL THR          
SEQRES   8 B  470  VAL GLU ASP PRO GLY GLU GLY MET LYS ILE TYR ARG ILE          
SEQRES   9 B  470  LYS TYR ASP GLY THR ARG MET ASN LEU GLN ARG ASP ALA          
SEQRES  10 B  470  ALA GLU VAL SER GLY LEU GLY LEU GLY VAL HIS VAL THR          
SEQRES  11 B  470  ILE THR PRO GLU ALA ASP GLY TYR ALA VAL GLY ASP GLY          
SEQRES  12 B  470  GLN LYS ASP ILE CYS ALA GLU PHE ASP ARG GLU THR ASP          
SEQRES  13 B  470  MET VAL ARG TYR ALA TRP ALA PHE ASP TRP ASP PRO ASN          
SEQRES  14 B  470  VAL LYS ASP LEU LYS ARG ALA TRP LEU ASP GLY GLY THR          
SEQRES  15 B  470  MET THR ILE LYS ARG LEU LYS PRO THR LEU PRO GLY GLY          
SEQRES  16 B  470  ARG TYR ASP LEU GLN GLY SER LYS GLY ASN LYS ILE ASP          
SEQRES  17 B  470  TRP GLU LEU VAL PRO GLY GLY GLU LEU ALA ILE GLU ASP          
SEQRES  18 B  470  GLY LYS VAL SER GLY ASP ARG PRO LEU HIS SER VAL ALA          
SEQRES  19 B  470  ASN ASP ALA LEU VAL PHE ASP PRO ARG GLY LYS TRP ALA          
SEQRES  20 B  470  VAL ALA SER MET ARG LEU PRO GLY VAL CYS VAL VAL PHE          
SEQRES  21 B  470  ASP ARG GLU ASN GLN VAL PRO VAL ALA VAL LEU ALA GLY          
SEQRES  22 B  470  PRO LYS GLY THR PRO SER GLN PHE GLN LEU VAL LYS VAL          
SEQRES  23 B  470  ASP ASP ASP THR TRP THR VAL ASP ILE PRO GLU VAL ILE          
SEQRES  24 B  470  SER ALA GLY HIS GLN ALA GLY PHE SER PRO ASP GLY GLN          
SEQRES  25 B  470  SER PHE LEU PHE MET ASN SER LEU ARG GLN ASN ASN ILE          
SEQRES  26 B  470  MET VAL TRP ASP SER SER ASN HIS ASP ASP PRO THR THR          
SEQRES  27 B  470  TRP GLU LYS LYS ALA VAL VAL GLU SER PRO ASP TRP ARG          
SEQRES  28 B  470  GLY ALA TYR PRO ASN THR PHE HIS MET VAL PHE THR PRO          
SEQRES  29 B  470  ASP ALA LYS LYS ILE TYR VAL THR MET TRP TRP PRO SER          
SEQRES  30 B  470  PRO THR PRO ASN GLY ILE ALA VAL ILE ASP ALA VAL ASN          
SEQRES  31 B  470  TRP GLU VAL LEU LYS GLU VAL ASP LEU GLY PRO ASP MET          
SEQRES  32 B  470  GLN THR LEU ALA ILE THR TYR ASP GLY LYS PHE VAL VAL          
SEQRES  33 B  470  GLY THR LEU SER GLY TYR GLN ASN THR ALA SER ALA ILE          
SEQRES  34 B  470  VAL VAL MET GLU THR GLU THR ASP GLU VAL LEU GLY PHE          
SEQRES  35 B  470  LEU PRO SER PRO MET GLY HIS HIS ASP ASN VAL ILE VAL          
SEQRES  36 B  470  PRO ARG THR LEU GLU ASP LEU ARG ILE SER ARG SER THR          
SEQRES  37 B  470  THR THR                                                      
SEQRES   1 J  470  ALA MET GLY LYS TYR VAL LYS VAL GLN ASP PHE TYR ASP          
SEQRES   2 J  470  GLN LEU GLY LYS TYR VAL LEU VAL ALA PRO GLY LYS PHE          
SEQRES   3 J  470  SER GLY THR VAL ALA ALA THR ASP LEU SER THR GLY TRP          
SEQRES   4 J  470  THR MET ALA TRP LEU ALA ALA TRP ASN TYR GLY ASP THR          
SEQRES   5 J  470  CYS PRO ILE MET HIS HIS MET ALA ALA PHE PRO SER PRO          
SEQRES   6 J  470  ASP PRO TYR LYS GLU PHE GLU PHE VAL VAL ASN THR GLN          
SEQRES   7 J  470  GLY GLY LYS ASN LEU PHE ILE TYR GLY VAL PRO VAL THR          
SEQRES   8 J  470  VAL GLU ASP PRO GLY GLU GLY MET LYS ILE TYR ARG ILE          
SEQRES   9 J  470  LYS TYR ASP GLY THR ARG MET ASN LEU GLN ARG ASP ALA          
SEQRES  10 J  470  ALA GLU VAL SER GLY LEU GLY LEU GLY VAL HIS VAL THR          
SEQRES  11 J  470  ILE THR PRO GLU ALA ASP GLY TYR ALA VAL GLY ASP GLY          
SEQRES  12 J  470  GLN LYS ASP ILE CYS ALA GLU PHE ASP ARG GLU THR ASP          
SEQRES  13 J  470  MET VAL ARG TYR ALA TRP ALA PHE ASP TRP ASP PRO ASN          
SEQRES  14 J  470  VAL LYS ASP LEU LYS ARG ALA TRP LEU ASP GLY GLY THR          
SEQRES  15 J  470  MET THR ILE LYS ARG LEU LYS PRO THR LEU PRO GLY GLY          
SEQRES  16 J  470  ARG TYR ASP LEU GLN GLY SER LYS GLY ASN LYS ILE ASP          
SEQRES  17 J  470  TRP GLU LEU VAL PRO GLY GLY GLU LEU ALA ILE GLU ASP          
SEQRES  18 J  470  GLY LYS VAL SER GLY ASP ARG PRO LEU HIS SER VAL ALA          
SEQRES  19 J  470  ASN ASP ALA LEU VAL PHE ASP PRO ARG GLY LYS TRP ALA          
SEQRES  20 J  470  VAL ALA SER MET ARG LEU PRO GLY VAL CYS VAL VAL PHE          
SEQRES  21 J  470  ASP ARG GLU ASN GLN VAL PRO VAL ALA VAL LEU ALA GLY          
SEQRES  22 J  470  PRO LYS GLY THR PRO SER GLN PHE GLN LEU VAL LYS VAL          
SEQRES  23 J  470  ASP ASP ASP THR TRP THR VAL ASP ILE PRO GLU VAL ILE          
SEQRES  24 J  470  SER ALA GLY HIS GLN ALA GLY PHE SER PRO ASP GLY GLN          
SEQRES  25 J  470  SER PHE LEU PHE MET ASN SER LEU ARG GLN ASN ASN ILE          
SEQRES  26 J  470  MET VAL TRP ASP SER SER ASN HIS ASP ASP PRO THR THR          
SEQRES  27 J  470  TRP GLU LYS LYS ALA VAL VAL GLU SER PRO ASP TRP ARG          
SEQRES  28 J  470  GLY ALA TYR PRO ASN THR PHE HIS MET VAL PHE THR PRO          
SEQRES  29 J  470  ASP ALA LYS LYS ILE TYR VAL THR MET TRP TRP PRO SER          
SEQRES  30 J  470  PRO THR PRO ASN GLY ILE ALA VAL ILE ASP ALA VAL ASN          
SEQRES  31 J  470  TRP GLU VAL LEU LYS GLU VAL ASP LEU GLY PRO ASP MET          
SEQRES  32 J  470  GLN THR LEU ALA ILE THR TYR ASP GLY LYS PHE VAL VAL          
SEQRES  33 J  470  GLY THR LEU SER GLY TYR GLN ASN THR ALA SER ALA ILE          
SEQRES  34 J  470  VAL VAL MET GLU THR GLU THR ASP GLU VAL LEU GLY PHE          
SEQRES  35 J  470  LEU PRO SER PRO MET GLY HIS HIS ASP ASN VAL ILE VAL          
SEQRES  36 J  470  PRO ARG THR LEU GLU ASP LEU ARG ILE SER ARG SER THR          
SEQRES  37 J  470  THR THR                                                      
SEQRES   1 K  470  ALA MET GLY LYS TYR VAL LYS VAL GLN ASP PHE TYR ASP          
SEQRES   2 K  470  GLN LEU GLY LYS TYR VAL LEU VAL ALA PRO GLY LYS PHE          
SEQRES   3 K  470  SER GLY THR VAL ALA ALA THR ASP LEU SER THR GLY TRP          
SEQRES   4 K  470  THR MET ALA TRP LEU ALA ALA TRP ASN TYR GLY ASP THR          
SEQRES   5 K  470  CYS PRO ILE MET HIS HIS MET ALA ALA PHE PRO SER PRO          
SEQRES   6 K  470  ASP PRO TYR LYS GLU PHE GLU PHE VAL VAL ASN THR GLN          
SEQRES   7 K  470  GLY GLY LYS ASN LEU PHE ILE TYR GLY VAL PRO VAL THR          
SEQRES   8 K  470  VAL GLU ASP PRO GLY GLU GLY MET LYS ILE TYR ARG ILE          
SEQRES   9 K  470  LYS TYR ASP GLY THR ARG MET ASN LEU GLN ARG ASP ALA          
SEQRES  10 K  470  ALA GLU VAL SER GLY LEU GLY LEU GLY VAL HIS VAL THR          
SEQRES  11 K  470  ILE THR PRO GLU ALA ASP GLY TYR ALA VAL GLY ASP GLY          
SEQRES  12 K  470  GLN LYS ASP ILE CYS ALA GLU PHE ASP ARG GLU THR ASP          
SEQRES  13 K  470  MET VAL ARG TYR ALA TRP ALA PHE ASP TRP ASP PRO ASN          
SEQRES  14 K  470  VAL LYS ASP LEU LYS ARG ALA TRP LEU ASP GLY GLY THR          
SEQRES  15 K  470  MET THR ILE LYS ARG LEU LYS PRO THR LEU PRO GLY GLY          
SEQRES  16 K  470  ARG TYR ASP LEU GLN GLY SER LYS GLY ASN LYS ILE ASP          
SEQRES  17 K  470  TRP GLU LEU VAL PRO GLY GLY GLU LEU ALA ILE GLU ASP          
SEQRES  18 K  470  GLY LYS VAL SER GLY ASP ARG PRO LEU HIS SER VAL ALA          
SEQRES  19 K  470  ASN ASP ALA LEU VAL PHE ASP PRO ARG GLY LYS TRP ALA          
SEQRES  20 K  470  VAL ALA SER MET ARG LEU PRO GLY VAL CYS VAL VAL PHE          
SEQRES  21 K  470  ASP ARG GLU ASN GLN VAL PRO VAL ALA VAL LEU ALA GLY          
SEQRES  22 K  470  PRO LYS GLY THR PRO SER GLN PHE GLN LEU VAL LYS VAL          
SEQRES  23 K  470  ASP ASP ASP THR TRP THR VAL ASP ILE PRO GLU VAL ILE          
SEQRES  24 K  470  SER ALA GLY HIS GLN ALA GLY PHE SER PRO ASP GLY GLN          
SEQRES  25 K  470  SER PHE LEU PHE MET ASN SER LEU ARG GLN ASN ASN ILE          
SEQRES  26 K  470  MET VAL TRP ASP SER SER ASN HIS ASP ASP PRO THR THR          
SEQRES  27 K  470  TRP GLU LYS LYS ALA VAL VAL GLU SER PRO ASP TRP ARG          
SEQRES  28 K  470  GLY ALA TYR PRO ASN THR PHE HIS MET VAL PHE THR PRO          
SEQRES  29 K  470  ASP ALA LYS LYS ILE TYR VAL THR MET TRP TRP PRO SER          
SEQRES  30 K  470  PRO THR PRO ASN GLY ILE ALA VAL ILE ASP ALA VAL ASN          
SEQRES  31 K  470  TRP GLU VAL LEU LYS GLU VAL ASP LEU GLY PRO ASP MET          
SEQRES  32 K  470  GLN THR LEU ALA ILE THR TYR ASP GLY LYS PHE VAL VAL          
SEQRES  33 K  470  GLY THR LEU SER GLY TYR GLN ASN THR ALA SER ALA ILE          
SEQRES  34 K  470  VAL VAL MET GLU THR GLU THR ASP GLU VAL LEU GLY PHE          
SEQRES  35 K  470  LEU PRO SER PRO MET GLY HIS HIS ASP ASN VAL ILE VAL          
SEQRES  36 K  470  PRO ARG THR LEU GLU ASP LEU ARG ILE SER ARG SER THR          
SEQRES  37 K  470  THR THR                                                      
HET     CU  A 601       1                                                       
HET     CU  A 602       1                                                       
HET    SO4  A 603       5                                                       
HET    SO4  A 604       5                                                       
HET     CU  B 601       1                                                       
HET     CU  B 602       1                                                       
HET     CU  J 601       1                                                       
HET     CU  J 602       1                                                       
HET     CU  K 601       1                                                       
HET     CU  K 602       1                                                       
HET     CU  K 603       1                                                       
HET    SO4  K 604       5                                                       
HETNAM      CU COPPER (II) ION                                                  
HETNAM     SO4 SULFATE ION                                                      
FORMUL   5   CU    9(CU 2+)                                                     
FORMUL   7  SO4    3(O4 S 2-)                                                   
FORMUL  17  HOH   *1183(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 LEU A  270  ARG A  274  5                                   5    
HELIX    7 AA7 GLY A  293  ASP A  299  1                                   7    
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 TYR A  500  ASN A  502  5                                   3    
HELIX   11 AB2 THR A  536  ARG A  541  1                                   6    
HELIX   12 AB3 VAL B   86  GLN B   92  1                                   7    
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  158  ILE B  163  5                                   6    
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 THR B  536  ARG B  541  1                                   6    
HELIX   23 AC5 LYS J   85  GLN J   92  1                                   8    
HELIX   24 AC6 LYS J  103  SER J  105  5                                   3    
HELIX   25 AC7 TRP J  125  GLY J  128  5                                   4    
HELIX   26 AC8 GLY J  158  ILE J  163  5                                   6    
HELIX   27 AC9 ALA J  195  GLY J  200  1                                   6    
HELIX   28 AD1 GLY J  293  ASP J  299  1                                   7    
HELIX   29 AD2 ARG J  306  SER J  310  5                                   5    
HELIX   30 AD3 ASP J  413  TRP J  417  5                                   5    
HELIX   31 AD4 TYR J  500  ASN J  502  5                                   3    
HELIX   32 AD5 LEU J  537  SER J  543  5                                   7    
HELIX   33 AD6 VAL K   86  GLY K   94  1                                   9    
HELIX   34 AD7 LYS K  103  SER K  105  5                                   3    
HELIX   35 AD8 TRP K  125  GLY K  128  5                                   4    
HELIX   36 AD9 GLY K  158  ILE K  163  5                                   6    
HELIX   37 AE1 ALA K  195  GLY K  200  1                                   6    
HELIX   38 AE2 GLY K  292  ASP K  299  1                                   8    
HELIX   39 AE3 ARG K  306  SER K  310  5                                   5    
HELIX   40 AE4 ASP K  413  TRP K  417  5                                   5    
HELIX   41 AE5 TYR K  500  ASN K  502  5                                   3    
HELIX   42 AE6 GLU K  538  SER K  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  ALA A 110   O  ALA A 120           
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  ARG A 193   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  ILE A 373   N  GLY A 259           
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 346   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 GLY A 380  PHE A 385  0                                        
SHEET    2 AA5 4 SER A 391  SER A 397 -1  O  LEU A 393   N  GLY A 384           
SHEET    3 AA5 4 ASN A 401  ASP A 407 -1  O  TRP A 406   N  PHE A 392           
SHEET    4 AA5 4 GLU A 418  VAL A 423 -1  O  LYS A 420   N  VAL A 405           
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 GLU A 470  GLY A 478 -1  O  LEU A 472   N  VAL A 463           
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  GLN A 482           
SHEET    3 AA7 4 SER A 505  GLU A 511 -1  O  MET A 510   N  VAL A 493           
SHEET    4 AA7 4 VAL A 517  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  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 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  ARG B 193   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  TRP B 369   N  ILE B 263           
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  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 GLY B 380  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 401  ASP B 407 -1  O  TRP B 406   N  PHE B 392           
SHEET    4 AB3 4 GLU B 418  VAL B 423 -1  O  GLU B 418   N  ASP B 407           
SHEET    1 AB4 4 MET B 438  PHE B 440  0                                        
SHEET    2 AB4 4 LYS B 446  MET B 451 -1  O  TYR B 448   N  VAL B 439           
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  GLU B 470   N  ASP B 465           
SHEET    1 AB5 4 MET B 481  ILE B 486  0                                        
SHEET    2 AB5 4 PHE B 492  SER B 498 -1  O  THR B 496   N  GLN B 482           
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 J 118  ALA J 123  0                                        
SHEET    2 AB6 4 THR J 107  ASP J 112 -1  N  ALA J 110   O  MET J 119           
SHEET    3 AB6 4 VAL J  97  PRO J 101 -1  N  LEU J  98   O  THR J 111           
SHEET    4 AB6 4 VAL J 531  ILE J 532 -1  O  VAL J 531   N  VAL J  99           
SHEET    1 AB7 4 ILE J 133  ALA J 139  0                                        
SHEET    2 AB7 4 PHE J 149  GLN J 156 -1  O  ASN J 154   N  HIS J 135           
SHEET    3 AB7 4 GLY J 176  TYR J 184 -1  O  ILE J 182   N  PHE J 151           
SHEET    4 AB7 4 MET J 189  ASP J 194 -1  O  GLN J 192   N  ARG J 181           
SHEET    1 AB8 7 VAL J 207  ILE J 209  0                                        
SHEET    2 AB8 7 GLY J 215  ASP J 220 -1  O  ALA J 217   N  THR J 208           
SHEET    3 AB8 7 ILE J 225  ASP J 230 -1  O  PHE J 229   N  TYR J 216           
SHEET    4 AB8 7 VAL J 236  PRO J 246 -1  O  ARG J 237   N  GLU J 228           
SHEET    5 AB8 7 GLY J 259  ARG J 265 -1  O  LYS J 264   N  ALA J 241           
SHEET    6 AB8 7 THR J 368  ILE J 373 -1  O  ILE J 373   N  GLY J 259           
SHEET    7 AB8 7 LEU J 361  ASP J 365 -1  N  VAL J 364   O  THR J 368           
SHEET    1 AB9 5 ASN J 313  PHE J 318  0                                        
SHEET    2 AB9 5 TRP J 324  MET J 329 -1  O  VAL J 326   N  VAL J 317           
SHEET    3 AB9 5 VAL J 334  ASP J 339 -1  O  PHE J 338   N  ALA J 325           
SHEET    4 AB9 5 VAL J 344  ALA J 350 -1  O  VAL J 344   N  ASP J 339           
SHEET    5 AB9 5 GLN J 358  PHE J 359 -1  O  PHE J 359   N  VAL J 348           
SHEET    1 AC1 4 GLY J 380  PHE J 385  0                                        
SHEET    2 AC1 4 SER J 391  SER J 397 -1  O  LEU J 393   N  GLY J 384           
SHEET    3 AC1 4 ASN J 401  ASP J 407 -1  O  TRP J 406   N  PHE J 392           
SHEET    4 AC1 4 GLU J 418  VAL J 423 -1  O  GLU J 418   N  ASP J 407           
SHEET    1 AC2 4 MET J 438  PHE J 440  0                                        
SHEET    2 AC2 4 LYS J 446  MET J 451 -1  O  TYR J 448   N  VAL J 439           
SHEET    3 AC2 4 ASN J 459  ASP J 465 -1  O  ILE J 464   N  ILE J 447           
SHEET    4 AC2 4 GLU J 470  GLY J 478 -1  O  GLU J 470   N  ASP J 465           
SHEET    1 AC3 4 MET J 481  ILE J 486  0                                        
SHEET    2 AC3 4 PHE J 492  SER J 498 -1  O  THR J 496   N  GLN J 482           
SHEET    3 AC3 4 SER J 505  GLU J 511 -1  O  MET J 510   N  VAL J 493           
SHEET    4 AC3 4 GLU J 516  PRO J 522 -1  O  LEU J 521   N  ILE J 507           
SHEET    1 AC4 4 THR K 118  ALA K 123  0                                        
SHEET    2 AC4 4 THR K 107  ASP K 112 -1  N  ALA K 110   O  ALA K 120           
SHEET    3 AC4 4 VAL K  97  PRO K 101 -1  N  LEU K  98   O  THR K 111           
SHEET    4 AC4 4 VAL K 531  ILE K 532 -1  O  VAL K 531   N  VAL K  99           
SHEET    1 AC5 4 ILE K 133  ALA K 139  0                                        
SHEET    2 AC5 4 PHE K 149  GLN K 156 -1  O  ASN K 154   N  HIS K 135           
SHEET    3 AC5 4 GLY K 176  TYR K 184 -1  O  TYR K 184   N  PHE K 149           
SHEET    4 AC5 4 MET K 189  ASP K 194 -1  O  ARG K 193   N  ARG K 181           
SHEET    1 AC6 7 VAL K 207  ILE K 209  0                                        
SHEET    2 AC6 7 GLY K 215  ASP K 220 -1  O  ALA K 217   N  THR K 208           
SHEET    3 AC6 7 ILE K 225  ASP K 230 -1  O  PHE K 229   N  TYR K 216           
SHEET    4 AC6 7 VAL K 236  PRO K 246 -1  O  ARG K 237   N  GLU K 228           
SHEET    5 AC6 7 GLY K 259  ARG K 265 -1  O  LYS K 264   N  ALA K 241           
SHEET    6 AC6 7 THR K 368  ILE K 373 -1  O  VAL K 371   N  MET K 261           
SHEET    7 AC6 7 VAL K 362  ASP K 365 -1  N  VAL K 364   O  THR K 368           
SHEET    1 AC7 5 ASN K 313  PHE K 318  0                                        
SHEET    2 AC7 5 TRP K 324  MET K 329 -1  O  VAL K 326   N  VAL K 317           
SHEET    3 AC7 5 VAL K 334  ASP K 339 -1  O  PHE K 338   N  ALA K 325           
SHEET    4 AC7 5 VAL K 344  ALA K 350 -1  O  VAL K 344   N  ASP K 339           
SHEET    5 AC7 5 GLN K 358  PHE K 359 -1  O  PHE K 359   N  VAL K 348           
SHEET    1 AC8 4 GLY K 380  PHE K 385  0                                        
SHEET    2 AC8 4 SER K 391  ASN K 396 -1  O  LEU K 393   N  GLY K 384           
SHEET    3 AC8 4 ASN K 402  ASP K 407 -1  O  TRP K 406   N  PHE K 392           
SHEET    4 AC8 4 GLU K 418  VAL K 423 -1  O  LYS K 420   N  VAL K 405           
SHEET    1 AC9 4 MET K 438  PHE K 440  0                                        
SHEET    2 AC9 4 LYS K 446  MET K 451 -1  O  TYR K 448   N  VAL K 439           
SHEET    3 AC9 4 ASN K 459  ASP K 465 -1  O  ILE K 464   N  ILE K 447           
SHEET    4 AC9 4 GLU K 470  GLY K 478 -1  O  LYS K 473   N  VAL K 463           
SHEET    1 AD1 4 MET K 481  ILE K 486  0                                        
SHEET    2 AD1 4 PHE K 492  SER K 498 -1  O  THR K 496   N  GLN K 482           
SHEET    3 AD1 4 SER K 505  GLU K 511 -1  O  MET K 510   N  VAL K 493           
SHEET    4 AD1 4 GLU K 516  PRO K 522 -1  O  LEU K 521   N  ILE K 507           
LINK         NE2 HIS A 135                CU    CU A 602     1555   1555  1.94  
LINK         NE2 HIS A 206                CU    CU A 601     1555   1555  1.93  
LINK         OD1 ASP A 314                CU    CU A 601     1555   1555  2.48  
LINK         OD2 ASP A 314                CU    CU A 601     1555   1555  2.43  
LINK         NE2 HIS A 381                CU    CU A 601     1555   1555  1.95  
LINK         ND1 HIS A 528                CU    CU A 602     1555   1555  1.92  
LINK         NE2 HIS B 135                CU    CU B 602     1555   1555  2.01  
LINK         NE2 HIS B 206                CU    CU B 601     1555   1555  1.90  
LINK         OD1 ASP B 314                CU    CU B 601     1555   1555  2.48  
LINK         OD2 ASP B 314                CU    CU B 601     1555   1555  2.42  
LINK         NE2 HIS B 381                CU    CU B 601     1555   1555  1.95  
LINK         ND1 HIS B 528                CU    CU B 602     1555   1555  1.96  
LINK         NE2 HIS J 135                CU    CU J 602     1555   1555  1.95  
LINK         NE2 HIS J 206                CU    CU J 601     1555   1555  1.96  
LINK         OD1 ASP J 314                CU    CU J 601     1555   1555  2.53  
LINK         OD2 ASP J 314                CU    CU J 601     1555   1555  2.40  
LINK         NE2 HIS J 381                CU    CU J 601     1555   1555  1.96  
LINK         ND1 HIS J 528                CU    CU J 602     1555   1555  1.95  
LINK         NZ  LYS K 103                CU    CU K 602     1555   1555  2.56  
LINK         NE2 HIS K 135                CU    CU K 602     1555   1555  1.96  
LINK         NE2 HIS K 206                CU    CU K 601     1555   1555  1.94  
LINK         OD1 ASP K 314                CU    CU K 601     1555   1555  2.47  
LINK         OD2 ASP K 314                CU    CU K 601     1555   1555  2.41  
LINK         NE2 HIS K 381                CU    CU K 601     1555   1555  1.94  
LINK         ND1 HIS K 411                CU    CU K 603     1555   1555  1.95  
LINK         ND1 HIS K 528                CU    CU K 602     1555   1555  1.92  
LINK        CU    CU A 601                 O   HOH A 945     1555   1555  2.65  
LINK        CU    CU A 602                 O   HOH A 838     1555   1555  2.02  
LINK        CU    CU A 602                 O   HOH A 824     1555   1555  1.97  
LINK        CU    CU B 601                 O   HOH B 890     1555   1555  2.15  
LINK        CU    CU B 602                 O   HOH B 738     1555   1555  1.95  
LINK        CU    CU B 602                 O   HOH B 894     1555   1555  2.02  
LINK        CU    CU J 602                 O   HOH J 821     1555   1555  1.99  
LINK        CU    CU J 602                 O   HOH J 807     1555   1555  2.04  
LINK        CU    CU K 602                 O   HOH K 790     1555   1555  2.01  
LINK        CU    CU K 602                 O   HOH K 734     1555   1555  1.95  
LINK         N   ALA A  79                CU    CU K 603     1555   2545  1.98  
CISPEP   1 TYR A  432    PRO A  433          0         2.03                     
CISPEP   2 SER A  455    PRO A  456          0        12.78                     
CISPEP   3 TYR B  432    PRO B  433          0         2.48                     
CISPEP   4 SER B  455    PRO B  456          0        12.51                     
CISPEP   5 TYR J  432    PRO J  433          0        -2.12                     
CISPEP   6 SER J  455    PRO J  456          0         5.57                     
CISPEP   7 TYR K  432    PRO K  433          0         8.50                     
CISPEP   8 SER K  455    PRO K  456          0         6.17                     
SITE     1 AC1  4 HIS A 206  ASP A 314  HIS A 381  HOH A 945                    
SITE     1 AC2  5 LYS A 103  HIS A 135  HIS A 528  HOH A 824                    
SITE     2 AC2  5 HOH A 838                                                     
SITE     1 AC3  6 LYS A 183  GLN A 192  ARG A 193  HOH A 847                    
SITE     2 AC3  6 HOH A 875  ARG K 399                                          
SITE     1 AC4  6 GLY A 128  ASP A 129  THR A 130  LYS A 178                    
SITE     2 AC4  6 HOH A 763  HOH A 863                                          
SITE     1 AC5  4 HIS B 206  ASP B 314  HIS B 381  HOH B 890                    
SITE     1 AC6  5 LYS B 103  HIS B 135  HIS B 528  HOH B 738                    
SITE     2 AC6  5 HOH B 894                                                     
SITE     1 AC7  3 HIS J 206  ASP J 314  HIS J 381                               
SITE     1 AC8  5 LYS J 103  HIS J 135  HIS J 528  HOH J 807                    
SITE     2 AC8  5 HOH J 821                                                     
SITE     1 AC9  4 HIS K 206  ASP K 314  HIS K 381  HOH K 948                    
SITE     1 AD1  5 LYS K 103  HIS K 135  HIS K 528  HOH K 734                    
SITE     2 AD1  5 HOH K 790                                                     
SITE     1 AD2  1 HIS K 411                                                     
SITE     1 AD3  5 GLY K 128  THR K 130  LYS K 178  HOH K 855                    
SITE     2 AD3  5 HOH K 870                                                     
CRYST1   70.080  160.410   90.880  90.00  98.11  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      0.014269  0.000000  0.002034        0.00000                         
SCALE2      0.000000  0.006234  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011115        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system