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Database: PDB
Entry: 6I3Q
LinkDB: 6I3Q
Original site: 6I3Q 
HEADER    OXIDOREDUCTASE                          07-NOV-18   6I3Q              
TITLE     THE STRUCTURE OF THIOCYANATE DEHYDROGENASE FROM THIOALKALIVIBRIO      
TITLE    2 PARADOXUS COMPLEX WITH ACETATE IONS.                                 
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,A.N.POPOV,T.V.TIKHKONOVA,V.O.POPOV,A.A.TROFIMOV          
REVDAT   2   22-JUL-20 6I3Q    1       JRNL                                     
REVDAT   1   28-NOV-18 6I3Q    0                                                
SPRSDE     28-NOV-18 6I3Q      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.    1.45 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0073                                      
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) : 1.45                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.48                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 372619                         
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  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.143                           
REMARK   3   R VALUE            (WORKING SET) : 0.142                           
REMARK   3   FREE R VALUE                     : 0.165                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 19501                           
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) : 1.45                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.49                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 27443                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.70                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2170                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 1412                         
REMARK   3   BIN FREE R VALUE                    : 0.2600                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 14539                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 61                                      
REMARK   3   SOLVENT ATOMS            : 1664                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.74                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.00000                                             
REMARK   3    B22 (A**2) : 6.23000                                              
REMARK   3    B33 (A**2) : -4.23000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.12000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.010         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.011         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.024         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.591         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.974                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.965                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 15118 ; 0.013 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 20574 ; 1.717 ; 1.943       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1868 ; 7.297 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   675 ;34.465 ;24.563       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2368 ;13.067 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    67 ;19.003 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2228 ; 0.113 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 11650 ; 0.010 ; 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):  7487 ; 1.061 ; 1.584       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  9344 ; 1.462 ; 2.381       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  7631 ; 1.508 ;  NULL       
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): 25763 ; 3.530 ;  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):     8 ; 5.898 ; 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 : 0.439                                           
REMARK   3      TWIN DOMAIN   : 2                                               
REMARK   3      TWIN OPERATOR : L, -K, H                                        
REMARK   3      TWIN FRACTION : 0.561                                           
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 6I3Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 07-NOV-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200012764.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-NOV-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97242                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 392121                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.450                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.0                               
REMARK 200  DATA REDUNDANCY                : 2.600                              
REMARK 200  R MERGE                    (I) : 0.08000                            
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) : 1.45                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.50                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.63000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
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: IN-HOUSE SAD STRUCTURE                               
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.52                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN SOLUTION: 10 MG/ML PROT., 25     
REMARK 280  0.17 M AMMONIUM ACETATE, 0.085 M TRI-SODIUM CITRATE (PH 5.6),       
REMARK 280  25.5 % W/V PEG 4000, 15 % GLYCEROL. V1/V2=1/1, VAPOR DIFFUSION,     
REMARK 280  HANGING DROP, TEMPERATURE 293K, VAPOR DIFFUSION, SITTING DROP       
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       81.35000            
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: 7220 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 28390 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -94.0 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: 15940 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 54790 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -188.0 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: 6930 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 28190 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -91.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     ASN A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     ASP A     5                                                      
REMARK 465     HIS A     6                                                      
REMARK 465     ILE A     7                                                      
REMARK 465     ASP A     8                                                      
REMARK 465     GLY A     9                                                      
REMARK 465     LYS A    10                                                      
REMARK 465     ASP A    11                                                      
REMARK 465     LEU A    12                                                      
REMARK 465     SER A    13                                                      
REMARK 465     GLU A    14                                                      
REMARK 465     PRO A    15                                                      
REMARK 465     ASN A    16                                                      
REMARK 465     ILE A    17                                                      
REMARK 465     ALA A    18                                                      
REMARK 465     ALA A    19                                                      
REMARK 465     GLU A    20                                                      
REMARK 465     THR A    21                                                      
REMARK 465     ALA A    22                                                      
REMARK 465     GLU A    23                                                      
REMARK 465     GLY A    24                                                      
REMARK 465     SER A    25                                                      
REMARK 465     VAL A    26                                                      
REMARK 465     GLU A    27                                                      
REMARK 465     ASP A    28                                                      
REMARK 465     THR A    29                                                      
REMARK 465     GLY A    30                                                      
REMARK 465     ALA A    31                                                      
REMARK 465     SER A    32                                                      
REMARK 465     GLU A    33                                                      
REMARK 465     SER A    34                                                      
REMARK 465     ARG A    35                                                      
REMARK 465     ARG A    36                                                      
REMARK 465     LYS A    37                                                      
REMARK 465     PHE A    38                                                      
REMARK 465     LEU A    39                                                      
REMARK 465     LYS A    40                                                      
REMARK 465     THR A    41                                                      
REMARK 465     VAL A    42                                                      
REMARK 465     GLY A    43                                                      
REMARK 465     ILE A    44                                                      
REMARK 465     GLY A    45                                                      
REMARK 465     THR A    46                                                      
REMARK 465     GLY A    47                                                      
REMARK 465     ALA A    48                                                      
REMARK 465     ALA A    49                                                      
REMARK 465     PHE A    50                                                      
REMARK 465     ALA A    51                                                      
REMARK 465     ALA A    52                                                      
REMARK 465     THR A    53                                                      
REMARK 465     ALA A    54                                                      
REMARK 465     ALA A    55                                                      
REMARK 465     ALA A    56                                                      
REMARK 465     PRO A    57                                                      
REMARK 465     PHE A    58                                                      
REMARK 465     MET A    59                                                      
REMARK 465     PRO A    60                                                      
REMARK 465     GLU A    61                                                      
REMARK 465     SER A    62                                                      
REMARK 465     VAL A    63                                                      
REMARK 465     ARG A    64                                                      
REMARK 465     GLY A    65                                                      
REMARK 465     LEU A    66                                                      
REMARK 465     VAL A    67                                                      
REMARK 465     THR A    68                                                      
REMARK 465     GLN A    69                                                      
REMARK 465     ASP A    70                                                      
REMARK 465     ALA A    71                                                      
REMARK 465     GLN A    72                                                      
REMARK 465     ALA A    73                                                      
REMARK 465     GLN A    74                                                      
REMARK 465     ILE A    75                                                      
REMARK 465     PHE A    76                                                      
REMARK 465     GLY A    77                                                      
REMARK 465     ARG A    78                                                      
REMARK 465     SER A    79                                                      
REMARK 465     GLY A    80                                                      
REMARK 465     SER A    81                                                      
REMARK 465     MET B     1                                                      
REMARK 465     SER B     2                                                      
REMARK 465     ASN B     3                                                      
REMARK 465     SER B     4                                                      
REMARK 465     ASP B     5                                                      
REMARK 465     HIS B     6                                                      
REMARK 465     ILE B     7                                                      
REMARK 465     ASP B     8                                                      
REMARK 465     GLY B     9                                                      
REMARK 465     LYS B    10                                                      
REMARK 465     ASP B    11                                                      
REMARK 465     LEU B    12                                                      
REMARK 465     SER B    13                                                      
REMARK 465     GLU B    14                                                      
REMARK 465     PRO B    15                                                      
REMARK 465     ASN B    16                                                      
REMARK 465     ILE B    17                                                      
REMARK 465     ALA B    18                                                      
REMARK 465     ALA B    19                                                      
REMARK 465     GLU B    20                                                      
REMARK 465     THR B    21                                                      
REMARK 465     ALA B    22                                                      
REMARK 465     GLU B    23                                                      
REMARK 465     GLY B    24                                                      
REMARK 465     SER B    25                                                      
REMARK 465     VAL B    26                                                      
REMARK 465     GLU B    27                                                      
REMARK 465     ASP B    28                                                      
REMARK 465     THR B    29                                                      
REMARK 465     GLY B    30                                                      
REMARK 465     ALA B    31                                                      
REMARK 465     SER B    32                                                      
REMARK 465     GLU B    33                                                      
REMARK 465     SER B    34                                                      
REMARK 465     ARG B    35                                                      
REMARK 465     ARG B    36                                                      
REMARK 465     LYS B    37                                                      
REMARK 465     PHE B    38                                                      
REMARK 465     LEU B    39                                                      
REMARK 465     LYS B    40                                                      
REMARK 465     THR B    41                                                      
REMARK 465     VAL B    42                                                      
REMARK 465     GLY B    43                                                      
REMARK 465     ILE B    44                                                      
REMARK 465     GLY B    45                                                      
REMARK 465     THR B    46                                                      
REMARK 465     GLY B    47                                                      
REMARK 465     ALA B    48                                                      
REMARK 465     ALA B    49                                                      
REMARK 465     PHE B    50                                                      
REMARK 465     ALA B    51                                                      
REMARK 465     ALA B    52                                                      
REMARK 465     THR B    53                                                      
REMARK 465     ALA B    54                                                      
REMARK 465     ALA B    55                                                      
REMARK 465     ALA B    56                                                      
REMARK 465     PRO B    57                                                      
REMARK 465     PHE B    58                                                      
REMARK 465     MET B    59                                                      
REMARK 465     PRO B    60                                                      
REMARK 465     GLU B    61                                                      
REMARK 465     SER B    62                                                      
REMARK 465     VAL B    63                                                      
REMARK 465     ARG B    64                                                      
REMARK 465     GLY B    65                                                      
REMARK 465     LEU B    66                                                      
REMARK 465     VAL B    67                                                      
REMARK 465     THR B    68                                                      
REMARK 465     GLN B    69                                                      
REMARK 465     ASP B    70                                                      
REMARK 465     ALA B    71                                                      
REMARK 465     GLN B    72                                                      
REMARK 465     ALA B    73                                                      
REMARK 465     GLN B    74                                                      
REMARK 465     ILE B    75                                                      
REMARK 465     PHE B    76                                                      
REMARK 465     GLY B    77                                                      
REMARK 465     ARG B    78                                                      
REMARK 465     SER B    79                                                      
REMARK 465     GLY B    80                                                      
REMARK 465     SER B    81                                                      
REMARK 465     MET C     1                                                      
REMARK 465     SER C     2                                                      
REMARK 465     ASN C     3                                                      
REMARK 465     SER C     4                                                      
REMARK 465     ASP C     5                                                      
REMARK 465     HIS C     6                                                      
REMARK 465     ILE C     7                                                      
REMARK 465     ASP C     8                                                      
REMARK 465     GLY C     9                                                      
REMARK 465     LYS C    10                                                      
REMARK 465     ASP C    11                                                      
REMARK 465     LEU C    12                                                      
REMARK 465     SER C    13                                                      
REMARK 465     GLU C    14                                                      
REMARK 465     PRO C    15                                                      
REMARK 465     ASN C    16                                                      
REMARK 465     ILE C    17                                                      
REMARK 465     ALA C    18                                                      
REMARK 465     ALA C    19                                                      
REMARK 465     GLU C    20                                                      
REMARK 465     THR C    21                                                      
REMARK 465     ALA C    22                                                      
REMARK 465     GLU C    23                                                      
REMARK 465     GLY C    24                                                      
REMARK 465     SER C    25                                                      
REMARK 465     VAL C    26                                                      
REMARK 465     GLU C    27                                                      
REMARK 465     ASP C    28                                                      
REMARK 465     THR C    29                                                      
REMARK 465     GLY C    30                                                      
REMARK 465     ALA C    31                                                      
REMARK 465     SER C    32                                                      
REMARK 465     GLU C    33                                                      
REMARK 465     SER C    34                                                      
REMARK 465     ARG C    35                                                      
REMARK 465     ARG C    36                                                      
REMARK 465     LYS C    37                                                      
REMARK 465     PHE C    38                                                      
REMARK 465     LEU C    39                                                      
REMARK 465     LYS C    40                                                      
REMARK 465     THR C    41                                                      
REMARK 465     VAL C    42                                                      
REMARK 465     GLY C    43                                                      
REMARK 465     ILE C    44                                                      
REMARK 465     GLY C    45                                                      
REMARK 465     THR C    46                                                      
REMARK 465     GLY C    47                                                      
REMARK 465     ALA C    48                                                      
REMARK 465     ALA C    49                                                      
REMARK 465     PHE C    50                                                      
REMARK 465     ALA C    51                                                      
REMARK 465     ALA C    52                                                      
REMARK 465     THR C    53                                                      
REMARK 465     ALA C    54                                                      
REMARK 465     ALA C    55                                                      
REMARK 465     ALA C    56                                                      
REMARK 465     PRO C    57                                                      
REMARK 465     PHE C    58                                                      
REMARK 465     MET C    59                                                      
REMARK 465     PRO C    60                                                      
REMARK 465     GLU C    61                                                      
REMARK 465     SER C    62                                                      
REMARK 465     VAL C    63                                                      
REMARK 465     ARG C    64                                                      
REMARK 465     GLY C    65                                                      
REMARK 465     LEU C    66                                                      
REMARK 465     VAL C    67                                                      
REMARK 465     THR C    68                                                      
REMARK 465     GLN C    69                                                      
REMARK 465     ASP C    70                                                      
REMARK 465     ALA C    71                                                      
REMARK 465     GLN C    72                                                      
REMARK 465     ALA C    73                                                      
REMARK 465     GLN C    74                                                      
REMARK 465     ILE C    75                                                      
REMARK 465     PHE C    76                                                      
REMARK 465     GLY C    77                                                      
REMARK 465     ARG C    78                                                      
REMARK 465     SER C    79                                                      
REMARK 465     GLY C    80                                                      
REMARK 465     SER C    81                                                      
REMARK 465     LYS C    82                                                      
REMARK 465     MET D     1                                                      
REMARK 465     SER D     2                                                      
REMARK 465     ASN D     3                                                      
REMARK 465     SER D     4                                                      
REMARK 465     ASP D     5                                                      
REMARK 465     HIS D     6                                                      
REMARK 465     ILE D     7                                                      
REMARK 465     ASP D     8                                                      
REMARK 465     GLY D     9                                                      
REMARK 465     LYS D    10                                                      
REMARK 465     ASP D    11                                                      
REMARK 465     LEU D    12                                                      
REMARK 465     SER D    13                                                      
REMARK 465     GLU D    14                                                      
REMARK 465     PRO D    15                                                      
REMARK 465     ASN D    16                                                      
REMARK 465     ILE D    17                                                      
REMARK 465     ALA D    18                                                      
REMARK 465     ALA D    19                                                      
REMARK 465     GLU D    20                                                      
REMARK 465     THR D    21                                                      
REMARK 465     ALA D    22                                                      
REMARK 465     GLU D    23                                                      
REMARK 465     GLY D    24                                                      
REMARK 465     SER D    25                                                      
REMARK 465     VAL D    26                                                      
REMARK 465     GLU D    27                                                      
REMARK 465     ASP D    28                                                      
REMARK 465     THR D    29                                                      
REMARK 465     GLY D    30                                                      
REMARK 465     ALA D    31                                                      
REMARK 465     SER D    32                                                      
REMARK 465     GLU D    33                                                      
REMARK 465     SER D    34                                                      
REMARK 465     ARG D    35                                                      
REMARK 465     ARG D    36                                                      
REMARK 465     LYS D    37                                                      
REMARK 465     PHE D    38                                                      
REMARK 465     LEU D    39                                                      
REMARK 465     LYS D    40                                                      
REMARK 465     THR D    41                                                      
REMARK 465     VAL D    42                                                      
REMARK 465     GLY D    43                                                      
REMARK 465     ILE D    44                                                      
REMARK 465     GLY D    45                                                      
REMARK 465     THR D    46                                                      
REMARK 465     GLY D    47                                                      
REMARK 465     ALA D    48                                                      
REMARK 465     ALA D    49                                                      
REMARK 465     PHE D    50                                                      
REMARK 465     ALA D    51                                                      
REMARK 465     ALA D    52                                                      
REMARK 465     THR D    53                                                      
REMARK 465     ALA D    54                                                      
REMARK 465     ALA D    55                                                      
REMARK 465     ALA D    56                                                      
REMARK 465     PRO D    57                                                      
REMARK 465     PHE D    58                                                      
REMARK 465     MET D    59                                                      
REMARK 465     PRO D    60                                                      
REMARK 465     GLU D    61                                                      
REMARK 465     SER D    62                                                      
REMARK 465     VAL D    63                                                      
REMARK 465     ARG D    64                                                      
REMARK 465     GLY D    65                                                      
REMARK 465     LEU D    66                                                      
REMARK 465     VAL D    67                                                      
REMARK 465     THR D    68                                                      
REMARK 465     GLN D    69                                                      
REMARK 465     ASP D    70                                                      
REMARK 465     ALA D    71                                                      
REMARK 465     GLN D    72                                                      
REMARK 465     ALA D    73                                                      
REMARK 465     GLN D    74                                                      
REMARK 465     ILE D    75                                                      
REMARK 465     PHE D    76                                                      
REMARK 465     GLY D    77                                                      
REMARK 465     ARG D    78                                                      
REMARK 465     SER D    79                                                      
REMARK 465     GLY D    80                                                      
REMARK 465     SER D    81                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A 306    NE   CZ   NH1  NH2                                  
REMARK 470     LYS B  82    CG   CD   CE   NZ                                   
REMARK 470     GLU B 171    CG   CD   OE1  OE2                                  
REMARK 470     ARG C 429    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D  82    CG   CD   CE   NZ                                   
REMARK 470     LYS D 147    CE   NZ                                             
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. =   3.2 DEGREES          
REMARK 500    ARG B 237   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    MET B 329   CG  -  SD  -  CE  ANGL. DEV. = -12.8 DEGREES          
REMARK 500    MET B 329   CG  -  SD  -  CE  ANGL. DEV. =  -9.7 DEGREES          
REMARK 500    ARG C 340   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 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     -119.70     51.42                                   
REMARK 500    THR A 115      -17.22   -142.67                                   
REMARK 500    CYS A 131       75.58   -150.91                                   
REMARK 500    HIS A 135      -94.07   -109.77                                   
REMARK 500    GLU A 148      143.13   -172.86                                   
REMARK 500    THR A 187      -48.41   -130.52                                   
REMARK 500    VAL A 205     -132.27   -112.03                                   
REMARK 500    ASP A 234       19.05     58.20                                   
REMARK 500    ASP A 276       55.12   -113.46                                   
REMARK 500    LYS A 323      -47.78     72.07                                   
REMARK 500    HIS A 381      -89.84   -146.15                                   
REMARK 500    LEU A 398      -86.31     85.87                                   
REMARK 500    LEU A 477      -50.29   -124.24                                   
REMARK 500    ASP A 480       63.54     64.37                                   
REMARK 500    HIS A 482     -125.04   -114.60                                   
REMARK 500    ASN A 502       -5.96   -142.31                                   
REMARK 500    THR A 503     -149.30   -127.41                                   
REMARK 500    HIS A 527      130.19    -37.64                                   
REMARK 500    SER A 543     -160.76   -118.12                                   
REMARK 500    SER A 545      -54.99   -149.85                                   
REMARK 500    LYS B 103     -114.74     55.39                                   
REMARK 500    HIS B 135      -88.17   -106.91                                   
REMARK 500    THR B 187      -45.76   -130.20                                   
REMARK 500    VAL B 205     -132.96   -111.53                                   
REMARK 500    ASP B 276       59.98   -112.97                                   
REMARK 500    ARG B 306       61.46   -153.52                                   
REMARK 500    ASP B 314      -52.22   -121.85                                   
REMARK 500    LYS B 323      -50.07     75.05                                   
REMARK 500    HIS B 381      -88.93   -147.57                                   
REMARK 500    LEU B 398      -76.47     77.41                                   
REMARK 500    ASP B 480       63.83     62.91                                   
REMARK 500    HIS B 482     -119.90   -110.03                                   
REMARK 500    GLN B 501       -2.37     74.96                                   
REMARK 500    THR B 503     -151.48   -120.40                                   
REMARK 500    HIS B 527      123.24    -33.84                                   
REMARK 500    SER B 543     -157.91   -121.47                                   
REMARK 500    SER B 545      -57.20   -150.02                                   
REMARK 500    LYS C 103     -116.66     54.16                                   
REMARK 500    ALA C 120      146.27   -173.51                                   
REMARK 500    HIS C 135      -95.89   -110.91                                   
REMARK 500    GLU C 148      141.38   -173.21                                   
REMARK 500    THR C 187      -51.30   -134.58                                   
REMARK 500    ARG C 193      177.09    178.89                                   
REMARK 500    VAL C 205     -129.59   -107.25                                   
REMARK 500    LYS C 249       34.73    -83.86                                   
REMARK 500    ASP C 276       56.93   -115.35                                   
REMARK 500    ARG C 306       54.30   -146.00                                   
REMARK 500    ASP C 314      -57.68   -120.30                                   
REMARK 500    LYS C 323      -52.39     74.37                                   
REMARK 500    HIS C 381      -90.27   -142.81                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      78 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 A1112        DISTANCE =  6.87 ANGSTROMS                       
REMARK 525    HOH B1100        DISTANCE =  6.48 ANGSTROMS                       
REMARK 525    HOH B1101        DISTANCE =  7.24 ANGSTROMS                       
REMARK 525    HOH D1115        DISTANCE =  5.99 ANGSTROMS                       
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     PEG D  607                                                       
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 120.0                                              
REMARK 620 3 ACT A 604   OXT  78.3 155.5                                        
REMARK 620 4 HOH A 830   O   105.8 102.7  85.7                                  
REMARK 620 5 HOH A 702   O   158.3  81.7  81.2  65.3                            
REMARK 620 N                    1     2     3     4                             
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  88.4                                              
REMARK 620 3 HIS A 381   NE2 177.7  93.9                                        
REMARK 620 4 ACT A 603   OXT  91.5 176.4  86.3                                  
REMARK 620 5 HOH A 757   O    90.0  92.4  90.3  84.0                            
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 115.5                                              
REMARK 620 3 HOH B 702   O   150.3  87.0                                        
REMARK 620 4 ACT B 604   OXT  89.0 150.5  64.8                                  
REMARK 620 5 HOH B 918   O   100.8 100.2  93.5  90.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU B 601  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 206   NE2                                                    
REMARK 620 2 ASP B 314   OD2  91.5                                              
REMARK 620 3 HIS B 381   NE2 173.3  87.8                                        
REMARK 620 4 HOH B 705   O    93.3  92.8  93.4                                  
REMARK 620 5 ACT B 603   O    87.2 176.8  93.1  90.2                            
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 HIS C 135   NE2                                                    
REMARK 620 2 HIS C 528   ND1 114.6                                              
REMARK 620 3 ACT C 604   O    91.4 148.0                                        
REMARK 620 4 HOH C 702   O   164.3  78.5  73.5                                  
REMARK 620 5 HOH C 801   O   106.1  97.5  92.3  79.5                            
REMARK 620 N                    1     2     3     4                             
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   OD2  92.2                                              
REMARK 620 3 HIS C 381   NE2 173.5  83.3                                        
REMARK 620 4 ACT C 603   OXT  90.1 175.7  94.7                                  
REMARK 620 5 HOH C 744   O    90.6  92.8  94.3  83.6                            
REMARK 620 N                    1     2     3     4                             
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 114.4                                              
REMARK 620 3 ACT D 604   O    92.8 145.3                                        
REMARK 620 4 HOH D 801   O    99.9 101.4  94.2                                  
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  93.4                                              
REMARK 620 3 HIS D 381   NE2 177.0  89.3                                        
REMARK 620 4 ACT D 603   O    85.8 172.9  91.7                                  
REMARK 620 5 HOH D 767   O    93.2  85.2  88.3  87.8                            
REMARK 620 N                    1     2     3     4                             
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 B 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU B 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU C 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU C 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU D 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU D 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT D 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT D 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT D 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG D 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues ACT A 603 and ACT A      
REMARK 800  604                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues ACT A 603 and ACT A      
REMARK 800  604                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues ACT B 603 and ACT B      
REMARK 800  604                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues ACT B 603 and ACT B      
REMARK 800  604                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues ACT C 603 and ACT C      
REMARK 800  604                                                                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residues ACT C 603 and ACT C      
REMARK 800  604                                                                 
DBREF  6I3Q A    1   548  UNP    W0DP94   W0DP94_9GAMM     1    548             
DBREF  6I3Q B    1   548  UNP    W0DP94   W0DP94_9GAMM     1    548             
DBREF  6I3Q C    1   548  UNP    W0DP94   W0DP94_9GAMM     1    548             
DBREF  6I3Q D    1   548  UNP    W0DP94   W0DP94_9GAMM     1    548             
SEQRES   1 A  548  MET SER ASN SER ASP HIS ILE ASP GLY LYS ASP LEU SER          
SEQRES   2 A  548  GLU PRO ASN ILE ALA ALA GLU THR ALA GLU GLY SER VAL          
SEQRES   3 A  548  GLU ASP THR GLY ALA SER GLU SER ARG ARG LYS PHE LEU          
SEQRES   4 A  548  LYS THR VAL GLY ILE GLY THR GLY ALA ALA PHE ALA ALA          
SEQRES   5 A  548  THR ALA ALA ALA PRO PHE MET PRO GLU SER VAL ARG GLY          
SEQRES   6 A  548  LEU VAL THR GLN ASP ALA GLN ALA GLN ILE PHE GLY ARG          
SEQRES   7 A  548  SER GLY SER LYS TYR VAL LYS VAL GLN ASP PHE TYR ASP          
SEQRES   8 A  548  GLN LEU GLY LYS TYR VAL LEU VAL ALA PRO GLY LYS PHE          
SEQRES   9 A  548  SER GLY THR VAL ALA ALA THR ASP LEU SER THR GLY TRP          
SEQRES  10 A  548  THR MET ALA TRP LEU ALA ALA TRP ASN TYR GLY ASP THR          
SEQRES  11 A  548  CYS PRO ILE MET HIS HIS MET ALA ALA PHE PRO SER PRO          
SEQRES  12 A  548  ASP PRO TYR LYS GLU PHE GLU PHE VAL VAL ASN THR GLN          
SEQRES  13 A  548  GLY GLY LYS ASN LEU PHE ILE TYR GLY VAL PRO VAL THR          
SEQRES  14 A  548  VAL GLU ASP PRO GLY GLU GLY MET LYS ILE TYR ARG ILE          
SEQRES  15 A  548  LYS TYR ASP GLY THR ARG MET ASN LEU GLN ARG ASP ALA          
SEQRES  16 A  548  ALA GLU VAL SER GLY LEU GLY LEU GLY VAL HIS VAL THR          
SEQRES  17 A  548  ILE THR PRO GLU ALA ASP GLY TYR ALA VAL GLY ASP GLY          
SEQRES  18 A  548  GLN LYS ASP ILE CYS ALA GLU PHE ASP ARG GLU THR ASP          
SEQRES  19 A  548  MET VAL ARG TYR ALA TRP ALA PHE ASP TRP ASP PRO ASN          
SEQRES  20 A  548  VAL LYS ASP LEU LYS ARG ALA TRP LEU ASP GLY GLY THR          
SEQRES  21 A  548  MET THR ILE LYS ARG LEU LYS PRO THR LEU PRO GLY GLY          
SEQRES  22 A  548  ARG TYR ASP LEU GLN GLY SER LYS GLY ASN LYS ILE ASP          
SEQRES  23 A  548  TRP GLU LEU VAL PRO GLY GLY GLU LEU ALA ILE GLU ASP          
SEQRES  24 A  548  GLY LYS VAL SER GLY ASP ARG PRO LEU HIS SER VAL ALA          
SEQRES  25 A  548  ASN ASP ALA LEU VAL PHE ASP PRO ARG GLY LYS TRP ALA          
SEQRES  26 A  548  VAL ALA SER MET ARG LEU PRO GLY VAL CYS VAL VAL PHE          
SEQRES  27 A  548  ASP ARG GLU ASN GLN VAL PRO VAL ALA VAL LEU ALA GLY          
SEQRES  28 A  548  PRO LYS GLY THR PRO SER GLN PHE GLN LEU VAL LYS VAL          
SEQRES  29 A  548  ASP ASP ASP THR TRP THR VAL ASP ILE PRO GLU VAL ILE          
SEQRES  30 A  548  SER ALA GLY HIS GLN ALA GLY PHE SER PRO ASP GLY GLN          
SEQRES  31 A  548  SER PHE LEU PHE MET ASN SER LEU ARG GLN ASN ASN ILE          
SEQRES  32 A  548  MET VAL TRP ASP SER SER ASN HIS ASP ASP PRO THR THR          
SEQRES  33 A  548  TRP GLU LYS LYS ALA VAL VAL GLU SER PRO ASP TRP ARG          
SEQRES  34 A  548  GLY ALA TYR PRO ASN THR PHE HIS MET VAL PHE THR PRO          
SEQRES  35 A  548  ASP ALA LYS LYS ILE TYR VAL THR MET TRP TRP PRO SER          
SEQRES  36 A  548  PRO THR PRO ASN GLY ILE ALA VAL ILE ASP ALA VAL ASN          
SEQRES  37 A  548  TRP GLU VAL LEU LYS GLU VAL ASP LEU GLY PRO ASP MET          
SEQRES  38 A  548  HIS THR LEU ALA ILE THR TYR ASP GLY LYS PHE VAL VAL          
SEQRES  39 A  548  GLY THR LEU SER GLY TYR GLN ASN THR ALA SER ALA ILE          
SEQRES  40 A  548  VAL VAL MET GLU THR GLU THR ASP GLU VAL LEU GLY PHE          
SEQRES  41 A  548  LEU PRO SER PRO MET GLY HIS HIS ASP ASN VAL ILE VAL          
SEQRES  42 A  548  PRO ARG THR LEU GLU ASP LEU ARG ILE SER ARG SER THR          
SEQRES  43 A  548  THR THR                                                      
SEQRES   1 B  548  MET SER ASN SER ASP HIS ILE ASP GLY LYS ASP LEU SER          
SEQRES   2 B  548  GLU PRO ASN ILE ALA ALA GLU THR ALA GLU GLY SER VAL          
SEQRES   3 B  548  GLU ASP THR GLY ALA SER GLU SER ARG ARG LYS PHE LEU          
SEQRES   4 B  548  LYS THR VAL GLY ILE GLY THR GLY ALA ALA PHE ALA ALA          
SEQRES   5 B  548  THR ALA ALA ALA PRO PHE MET PRO GLU SER VAL ARG GLY          
SEQRES   6 B  548  LEU VAL THR GLN ASP ALA GLN ALA GLN ILE PHE GLY ARG          
SEQRES   7 B  548  SER GLY SER LYS TYR VAL LYS VAL GLN ASP PHE TYR ASP          
SEQRES   8 B  548  GLN LEU GLY LYS TYR VAL LEU VAL ALA PRO GLY LYS PHE          
SEQRES   9 B  548  SER GLY THR VAL ALA ALA THR ASP LEU SER THR GLY TRP          
SEQRES  10 B  548  THR MET ALA TRP LEU ALA ALA TRP ASN TYR GLY ASP THR          
SEQRES  11 B  548  CYS PRO ILE MET HIS HIS MET ALA ALA PHE PRO SER PRO          
SEQRES  12 B  548  ASP PRO TYR LYS GLU PHE GLU PHE VAL VAL ASN THR GLN          
SEQRES  13 B  548  GLY GLY LYS ASN LEU PHE ILE TYR GLY VAL PRO VAL THR          
SEQRES  14 B  548  VAL GLU ASP PRO GLY GLU GLY MET LYS ILE TYR ARG ILE          
SEQRES  15 B  548  LYS TYR ASP GLY THR ARG MET ASN LEU GLN ARG ASP ALA          
SEQRES  16 B  548  ALA GLU VAL SER GLY LEU GLY LEU GLY VAL HIS VAL THR          
SEQRES  17 B  548  ILE THR PRO GLU ALA ASP GLY TYR ALA VAL GLY ASP GLY          
SEQRES  18 B  548  GLN LYS ASP ILE CYS ALA GLU PHE ASP ARG GLU THR ASP          
SEQRES  19 B  548  MET VAL ARG TYR ALA TRP ALA PHE ASP TRP ASP PRO ASN          
SEQRES  20 B  548  VAL LYS ASP LEU LYS ARG ALA TRP LEU ASP GLY GLY THR          
SEQRES  21 B  548  MET THR ILE LYS ARG LEU LYS PRO THR LEU PRO GLY GLY          
SEQRES  22 B  548  ARG TYR ASP LEU GLN GLY SER LYS GLY ASN LYS ILE ASP          
SEQRES  23 B  548  TRP GLU LEU VAL PRO GLY GLY GLU LEU ALA ILE GLU ASP          
SEQRES  24 B  548  GLY LYS VAL SER GLY ASP ARG PRO LEU HIS SER VAL ALA          
SEQRES  25 B  548  ASN ASP ALA LEU VAL PHE ASP PRO ARG GLY LYS TRP ALA          
SEQRES  26 B  548  VAL ALA SER MET ARG LEU PRO GLY VAL CYS VAL VAL PHE          
SEQRES  27 B  548  ASP ARG GLU ASN GLN VAL PRO VAL ALA VAL LEU ALA GLY          
SEQRES  28 B  548  PRO LYS GLY THR PRO SER GLN PHE GLN LEU VAL LYS VAL          
SEQRES  29 B  548  ASP ASP ASP THR TRP THR VAL ASP ILE PRO GLU VAL ILE          
SEQRES  30 B  548  SER ALA GLY HIS GLN ALA GLY PHE SER PRO ASP GLY GLN          
SEQRES  31 B  548  SER PHE LEU PHE MET ASN SER LEU ARG GLN ASN ASN ILE          
SEQRES  32 B  548  MET VAL TRP ASP SER SER ASN HIS ASP ASP PRO THR THR          
SEQRES  33 B  548  TRP GLU LYS LYS ALA VAL VAL GLU SER PRO ASP TRP ARG          
SEQRES  34 B  548  GLY ALA TYR PRO ASN THR PHE HIS MET VAL PHE THR PRO          
SEQRES  35 B  548  ASP ALA LYS LYS ILE TYR VAL THR MET TRP TRP PRO SER          
SEQRES  36 B  548  PRO THR PRO ASN GLY ILE ALA VAL ILE ASP ALA VAL ASN          
SEQRES  37 B  548  TRP GLU VAL LEU LYS GLU VAL ASP LEU GLY PRO ASP MET          
SEQRES  38 B  548  HIS THR LEU ALA ILE THR TYR ASP GLY LYS PHE VAL VAL          
SEQRES  39 B  548  GLY THR LEU SER GLY TYR GLN ASN THR ALA SER ALA ILE          
SEQRES  40 B  548  VAL VAL MET GLU THR GLU THR ASP GLU VAL LEU GLY PHE          
SEQRES  41 B  548  LEU PRO SER PRO MET GLY HIS HIS ASP ASN VAL ILE VAL          
SEQRES  42 B  548  PRO ARG THR LEU GLU ASP LEU ARG ILE SER ARG SER THR          
SEQRES  43 B  548  THR THR                                                      
SEQRES   1 C  548  MET SER ASN SER ASP HIS ILE ASP GLY LYS ASP LEU SER          
SEQRES   2 C  548  GLU PRO ASN ILE ALA ALA GLU THR ALA GLU GLY SER VAL          
SEQRES   3 C  548  GLU ASP THR GLY ALA SER GLU SER ARG ARG LYS PHE LEU          
SEQRES   4 C  548  LYS THR VAL GLY ILE GLY THR GLY ALA ALA PHE ALA ALA          
SEQRES   5 C  548  THR ALA ALA ALA PRO PHE MET PRO GLU SER VAL ARG GLY          
SEQRES   6 C  548  LEU VAL THR GLN ASP ALA GLN ALA GLN ILE PHE GLY ARG          
SEQRES   7 C  548  SER GLY SER LYS TYR VAL LYS VAL GLN ASP PHE TYR ASP          
SEQRES   8 C  548  GLN LEU GLY LYS TYR VAL LEU VAL ALA PRO GLY LYS PHE          
SEQRES   9 C  548  SER GLY THR VAL ALA ALA THR ASP LEU SER THR GLY TRP          
SEQRES  10 C  548  THR MET ALA TRP LEU ALA ALA TRP ASN TYR GLY ASP THR          
SEQRES  11 C  548  CYS PRO ILE MET HIS HIS MET ALA ALA PHE PRO SER PRO          
SEQRES  12 C  548  ASP PRO TYR LYS GLU PHE GLU PHE VAL VAL ASN THR GLN          
SEQRES  13 C  548  GLY GLY LYS ASN LEU PHE ILE TYR GLY VAL PRO VAL THR          
SEQRES  14 C  548  VAL GLU ASP PRO GLY GLU GLY MET LYS ILE TYR ARG ILE          
SEQRES  15 C  548  LYS TYR ASP GLY THR ARG MET ASN LEU GLN ARG ASP ALA          
SEQRES  16 C  548  ALA GLU VAL SER GLY LEU GLY LEU GLY VAL HIS VAL THR          
SEQRES  17 C  548  ILE THR PRO GLU ALA ASP GLY TYR ALA VAL GLY ASP GLY          
SEQRES  18 C  548  GLN LYS ASP ILE CYS ALA GLU PHE ASP ARG GLU THR ASP          
SEQRES  19 C  548  MET VAL ARG TYR ALA TRP ALA PHE ASP TRP ASP PRO ASN          
SEQRES  20 C  548  VAL LYS ASP LEU LYS ARG ALA TRP LEU ASP GLY GLY THR          
SEQRES  21 C  548  MET THR ILE LYS ARG LEU LYS PRO THR LEU PRO GLY GLY          
SEQRES  22 C  548  ARG TYR ASP LEU GLN GLY SER LYS GLY ASN LYS ILE ASP          
SEQRES  23 C  548  TRP GLU LEU VAL PRO GLY GLY GLU LEU ALA ILE GLU ASP          
SEQRES  24 C  548  GLY LYS VAL SER GLY ASP ARG PRO LEU HIS SER VAL ALA          
SEQRES  25 C  548  ASN ASP ALA LEU VAL PHE ASP PRO ARG GLY LYS TRP ALA          
SEQRES  26 C  548  VAL ALA SER MET ARG LEU PRO GLY VAL CYS VAL VAL PHE          
SEQRES  27 C  548  ASP ARG GLU ASN GLN VAL PRO VAL ALA VAL LEU ALA GLY          
SEQRES  28 C  548  PRO LYS GLY THR PRO SER GLN PHE GLN LEU VAL LYS VAL          
SEQRES  29 C  548  ASP ASP ASP THR TRP THR VAL ASP ILE PRO GLU VAL ILE          
SEQRES  30 C  548  SER ALA GLY HIS GLN ALA GLY PHE SER PRO ASP GLY GLN          
SEQRES  31 C  548  SER PHE LEU PHE MET ASN SER LEU ARG GLN ASN ASN ILE          
SEQRES  32 C  548  MET VAL TRP ASP SER SER ASN HIS ASP ASP PRO THR THR          
SEQRES  33 C  548  TRP GLU LYS LYS ALA VAL VAL GLU SER PRO ASP TRP ARG          
SEQRES  34 C  548  GLY ALA TYR PRO ASN THR PHE HIS MET VAL PHE THR PRO          
SEQRES  35 C  548  ASP ALA LYS LYS ILE TYR VAL THR MET TRP TRP PRO SER          
SEQRES  36 C  548  PRO THR PRO ASN GLY ILE ALA VAL ILE ASP ALA VAL ASN          
SEQRES  37 C  548  TRP GLU VAL LEU LYS GLU VAL ASP LEU GLY PRO ASP MET          
SEQRES  38 C  548  HIS THR LEU ALA ILE THR TYR ASP GLY LYS PHE VAL VAL          
SEQRES  39 C  548  GLY THR LEU SER GLY TYR GLN ASN THR ALA SER ALA ILE          
SEQRES  40 C  548  VAL VAL MET GLU THR GLU THR ASP GLU VAL LEU GLY PHE          
SEQRES  41 C  548  LEU PRO SER PRO MET GLY HIS HIS ASP ASN VAL ILE VAL          
SEQRES  42 C  548  PRO ARG THR LEU GLU ASP LEU ARG ILE SER ARG SER THR          
SEQRES  43 C  548  THR THR                                                      
SEQRES   1 D  548  MET SER ASN SER ASP HIS ILE ASP GLY LYS ASP LEU SER          
SEQRES   2 D  548  GLU PRO ASN ILE ALA ALA GLU THR ALA GLU GLY SER VAL          
SEQRES   3 D  548  GLU ASP THR GLY ALA SER GLU SER ARG ARG LYS PHE LEU          
SEQRES   4 D  548  LYS THR VAL GLY ILE GLY THR GLY ALA ALA PHE ALA ALA          
SEQRES   5 D  548  THR ALA ALA ALA PRO PHE MET PRO GLU SER VAL ARG GLY          
SEQRES   6 D  548  LEU VAL THR GLN ASP ALA GLN ALA GLN ILE PHE GLY ARG          
SEQRES   7 D  548  SER GLY SER LYS TYR VAL LYS VAL GLN ASP PHE TYR ASP          
SEQRES   8 D  548  GLN LEU GLY LYS TYR VAL LEU VAL ALA PRO GLY LYS PHE          
SEQRES   9 D  548  SER GLY THR VAL ALA ALA THR ASP LEU SER THR GLY TRP          
SEQRES  10 D  548  THR MET ALA TRP LEU ALA ALA TRP ASN TYR GLY ASP THR          
SEQRES  11 D  548  CYS PRO ILE MET HIS HIS MET ALA ALA PHE PRO SER PRO          
SEQRES  12 D  548  ASP PRO TYR LYS GLU PHE GLU PHE VAL VAL ASN THR GLN          
SEQRES  13 D  548  GLY GLY LYS ASN LEU PHE ILE TYR GLY VAL PRO VAL THR          
SEQRES  14 D  548  VAL GLU ASP PRO GLY GLU GLY MET LYS ILE TYR ARG ILE          
SEQRES  15 D  548  LYS TYR ASP GLY THR ARG MET ASN LEU GLN ARG ASP ALA          
SEQRES  16 D  548  ALA GLU VAL SER GLY LEU GLY LEU GLY VAL HIS VAL THR          
SEQRES  17 D  548  ILE THR PRO GLU ALA ASP GLY TYR ALA VAL GLY ASP GLY          
SEQRES  18 D  548  GLN LYS ASP ILE CYS ALA GLU PHE ASP ARG GLU THR ASP          
SEQRES  19 D  548  MET VAL ARG TYR ALA TRP ALA PHE ASP TRP ASP PRO ASN          
SEQRES  20 D  548  VAL LYS ASP LEU LYS ARG ALA TRP LEU ASP GLY GLY THR          
SEQRES  21 D  548  MET THR ILE LYS ARG LEU LYS PRO THR LEU PRO GLY GLY          
SEQRES  22 D  548  ARG TYR ASP LEU GLN GLY SER LYS GLY ASN LYS ILE ASP          
SEQRES  23 D  548  TRP GLU LEU VAL PRO GLY GLY GLU LEU ALA ILE GLU ASP          
SEQRES  24 D  548  GLY LYS VAL SER GLY ASP ARG PRO LEU HIS SER VAL ALA          
SEQRES  25 D  548  ASN ASP ALA LEU VAL PHE ASP PRO ARG GLY LYS TRP ALA          
SEQRES  26 D  548  VAL ALA SER MET ARG LEU PRO GLY VAL CYS VAL VAL PHE          
SEQRES  27 D  548  ASP ARG GLU ASN GLN VAL PRO VAL ALA VAL LEU ALA GLY          
SEQRES  28 D  548  PRO LYS GLY THR PRO SER GLN PHE GLN LEU VAL LYS VAL          
SEQRES  29 D  548  ASP ASP ASP THR TRP THR VAL ASP ILE PRO GLU VAL ILE          
SEQRES  30 D  548  SER ALA GLY HIS GLN ALA GLY PHE SER PRO ASP GLY GLN          
SEQRES  31 D  548  SER PHE LEU PHE MET ASN SER LEU ARG GLN ASN ASN ILE          
SEQRES  32 D  548  MET VAL TRP ASP SER SER ASN HIS ASP ASP PRO THR THR          
SEQRES  33 D  548  TRP GLU LYS LYS ALA VAL VAL GLU SER PRO ASP TRP ARG          
SEQRES  34 D  548  GLY ALA TYR PRO ASN THR PHE HIS MET VAL PHE THR PRO          
SEQRES  35 D  548  ASP ALA LYS LYS ILE TYR VAL THR MET TRP TRP PRO SER          
SEQRES  36 D  548  PRO THR PRO ASN GLY ILE ALA VAL ILE ASP ALA VAL ASN          
SEQRES  37 D  548  TRP GLU VAL LEU LYS GLU VAL ASP LEU GLY PRO ASP MET          
SEQRES  38 D  548  HIS THR LEU ALA ILE THR TYR ASP GLY LYS PHE VAL VAL          
SEQRES  39 D  548  GLY THR LEU SER GLY TYR GLN ASN THR ALA SER ALA ILE          
SEQRES  40 D  548  VAL VAL MET GLU THR GLU THR ASP GLU VAL LEU GLY PHE          
SEQRES  41 D  548  LEU PRO SER PRO MET GLY HIS HIS ASP ASN VAL ILE VAL          
SEQRES  42 D  548  PRO ARG THR LEU GLU ASP LEU ARG ILE SER ARG SER THR          
SEQRES  43 D  548  THR THR                                                      
HET     CU  A 601       1                                                       
HET     CU  A 602       1                                                       
HET    ACT  A 603       4                                                       
HET    ACT  A 604       4                                                       
HET     CU  B 601       1                                                       
HET     CU  B 602       1                                                       
HET    ACT  B 603       4                                                       
HET    ACT  B 604       4                                                       
HET     CU  C 601       1                                                       
HET     CU  C 602       1                                                       
HET    ACT  C 603       4                                                       
HET    ACT  C 604       4                                                       
HET    GOL  C 605       6                                                       
HET     CU  D 601       1                                                       
HET     CU  D 602       1                                                       
HET    ACT  D 603       4                                                       
HET    ACT  D 604       4                                                       
HET    ACT  D 605       4                                                       
HET    GOL  D 606       6                                                       
HET    PEG  D 607       5                                                       
HETNAM      CU COPPER (II) ION                                                  
HETNAM     ACT ACETATE ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   5   CU    8(CU 2+)                                                     
FORMUL   7  ACT    9(C2 H3 O2 1-)                                               
FORMUL  17  GOL    2(C3 H8 O3)                                                  
FORMUL  24  PEG    C4 H10 O3                                                    
FORMUL  25  HOH   *1664(H2 O)                                                   
HELIX    1 AA1 VAL A   86  GLY A   94  1                                   9    
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 TYR A  500  ASN A  502  5                                   3    
HELIX   12 AB3 GLU A  538  SER A  543  5                                   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 LEU B  270  ARG B  274  5                                   5    
HELIX   19 AC1 GLY B  292  ASP B  299  1                                   8    
HELIX   20 AC2 ARG B  306  SER B  310  5                                   5    
HELIX   21 AC3 ASP B  413  TRP B  417  5                                   5    
HELIX   22 AC4 TYR B  500  ASN B  502  5                                   3    
HELIX   23 AC5 THR B  536  ARG B  541  1                                   6    
HELIX   24 AC6 VAL C   86  GLN C   92  1                                   7    
HELIX   25 AC7 LYS C  103  SER C  105  5                                   3    
HELIX   26 AC8 TRP C  125  GLY C  128  5                                   4    
HELIX   27 AC9 GLY C  158  ILE C  163  5                                   6    
HELIX   28 AD1 ALA C  195  GLY C  200  1                                   6    
HELIX   29 AD2 LEU C  270  ARG C  274  5                                   5    
HELIX   30 AD3 GLY C  292  ASP C  299  1                                   8    
HELIX   31 AD4 ARG C  306  SER C  310  5                                   5    
HELIX   32 AD5 ASP C  413  TRP C  417  5                                   5    
HELIX   33 AD6 TYR C  500  ASN C  502  5                                   3    
HELIX   34 AD7 GLU C  538  SER C  543  5                                   6    
HELIX   35 AD8 LYS D   85  GLN D   92  1                                   8    
HELIX   36 AD9 LYS D  103  SER D  105  5                                   3    
HELIX   37 AE1 TRP D  125  GLY D  128  5                                   4    
HELIX   38 AE2 GLY D  158  ILE D  163  5                                   6    
HELIX   39 AE3 ALA D  195  GLY D  200  1                                   6    
HELIX   40 AE4 LEU D  270  ARG D  274  5                                   5    
HELIX   41 AE5 GLY D  292  ASP D  299  1                                   8    
HELIX   42 AE6 ARG D  306  SER D  310  5                                   5    
HELIX   43 AE7 ASP D  413  TRP D  417  5                                   5    
HELIX   44 AE8 TYR D  500  ASN D  502  5                                   3    
HELIX   45 AE9 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  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  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  ILE A 373   N  GLY A 259           
SHEET    7 AA3 7 LEU A 361  ASP A 365 -1  N  VAL A 364   O  THR A 368           
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  ASN A 396 -1  O  LEU A 393   N  GLY A 384           
SHEET    3 AA5 4 ASN A 402  ASP A 407 -1  O  TRP A 406   N  PHE A 392           
SHEET    4 AA5 4 GLU A 418  VAL A 423 -1  O  GLU A 418   N  ASP A 407           
SHEET    1 AA6 4 MET A 438  PHE A 440  0                                        
SHEET    2 AA6 4 LYS A 446  MET A 451 -1  O  TYR A 448   N  VAL A 439           
SHEET    3 AA6 4 ASN A 459  ASP A 465 -1  O  ILE A 464   N  ILE A 447           
SHEET    4 AA6 4 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  SER A 498 -1  O  THR A 496   N  HIS 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  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 364   O  THR B 368           
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  ASN B 396 -1  O  LEU B 393   N  GLY B 384           
SHEET    3 AB3 4 ASN B 402  ASP B 407 -1  O  TRP B 406   N  PHE B 392           
SHEET    4 AB3 4 GLU B 418  VAL B 423 -1  O  LYS B 420   N  VAL B 405           
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  HIS 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 VAL B 517  PRO B 522 -1  O  LEU B 521   N  ILE B 507           
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  THR C 262   N  ASP C 243           
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 364   O  THR C 368           
SHEET    1 AB9 5 ASN C 313  PHE C 318  0                                        
SHEET    2 AB9 5 TRP C 324  MET C 329 -1  O  VAL C 326   N  VAL C 317           
SHEET    3 AB9 5 VAL C 334  ASP C 339 -1  O  PHE C 338   N  ALA C 325           
SHEET    4 AB9 5 VAL C 344  ALA C 350 -1  O  VAL C 344   N  ASP C 339           
SHEET    5 AB9 5 GLN C 358  PHE C 359 -1  O  PHE C 359   N  VAL C 348           
SHEET    1 AC1 4 GLY C 380  PHE C 385  0                                        
SHEET    2 AC1 4 SER C 391  ASN C 396 -1  O  LEU C 393   N  GLY C 384           
SHEET    3 AC1 4 ASN C 402  ASP C 407 -1  O  TRP C 406   N  PHE C 392           
SHEET    4 AC1 4 GLU C 418  VAL C 423 -1  O  GLU C 418   N  ASP C 407           
SHEET    1 AC2 4 MET C 438  PHE C 440  0                                        
SHEET    2 AC2 4 LYS C 446  MET C 451 -1  O  TYR C 448   N  VAL C 439           
SHEET    3 AC2 4 ASN C 459  ASP C 465 -1  O  ALA C 462   N  VAL C 449           
SHEET    4 AC2 4 GLU C 470  GLY C 478 -1  O  LEU C 472   N  VAL C 463           
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 VAL C 517  PRO C 522 -1  O  LEU C 521   N  ILE C 507           
SHEET    1 AC4 4 THR D 118  ALA D 123  0                                        
SHEET    2 AC4 4 THR D 107  ASP D 112 -1  N  ALA D 110   O  ALA D 120           
SHEET    3 AC4 4 VAL D  97  PRO D 101 -1  N  LEU D  98   O  THR D 111           
SHEET    4 AC4 4 VAL D 531  ILE D 532 -1  O  VAL D 531   N  VAL D  99           
SHEET    1 AC5 4 ILE D 133  ALA D 139  0                                        
SHEET    2 AC5 4 PHE D 149  GLN D 156 -1  O  ASN D 154   N  HIS D 135           
SHEET    3 AC5 4 GLY D 176  TYR D 184 -1  O  TYR D 184   N  PHE D 149           
SHEET    4 AC5 4 MET D 189  ASP D 194 -1  O  ASN D 190   N  LYS D 183           
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  ARG D 265 -1  O  LYS D 264   N  ALA D 241           
SHEET    6 AC6 7 THR D 368  ILE D 373 -1  O  ILE D 373   N  GLY D 259           
SHEET    7 AC6 7 LEU D 361  ASP D 365 -1  N  VAL D 364   O  THR D 368           
SHEET    1 AC7 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  VAL D 346   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 GLY D 380  PHE D 385  0                                        
SHEET    2 AC8 4 SER D 391  ASN D 396 -1  O  LEU D 393   N  GLY D 384           
SHEET    3 AC8 4 ASN D 402  ASP D 407 -1  O  TRP D 406   N  PHE D 392           
SHEET    4 AC8 4 GLU D 418  VAL D 423 -1  O  LYS D 420   N  VAL D 405           
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  GLU D 470   N  ASP D 465           
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  ALA D 506   N  LEU D 497           
SHEET    4 AD1 4 VAL D 517  PRO D 522 -1  O  LEU D 518   N  VAL D 509           
LINK         NE2 HIS A 135                CU    CU A 602     1555   1555  2.08  
LINK         NE2 HIS A 206                CU    CU A 601     1555   1555  1.97  
LINK         OD2 ASP A 314                CU    CU A 601     1555   1555  2.07  
LINK         NE2 HIS A 381                CU    CU A 601     1555   1555  2.00  
LINK         ND1 HIS A 528                CU    CU A 602     1555   1555  1.99  
LINK         NE2 HIS B 135                CU    CU B 602     1555   1555  1.95  
LINK         NE2 HIS B 206                CU    CU B 601     1555   1555  1.97  
LINK         OD2 ASP B 314                CU    CU B 601     1555   1555  2.07  
LINK         NE2 HIS B 381                CU    CU B 601     1555   1555  2.00  
LINK         ND1 HIS B 528                CU    CU B 602     1555   1555  2.00  
LINK         NE2 HIS C 135                CU    CU C 602     1555   1555  2.02  
LINK         NE2 HIS C 206                CU    CU C 601     1555   1555  2.04  
LINK         OD2 ASP C 314                CU    CU C 601     1555   1555  2.19  
LINK         NE2 HIS C 381                CU    CU C 601     1555   1555  2.01  
LINK         ND1 HIS C 528                CU    CU C 602     1555   1555  2.00  
LINK         NE2 HIS D 135                CU    CU D 602     1555   1555  1.99  
LINK         NE2 HIS D 206                CU    CU D 601     1555   1555  1.96  
LINK         OD2 ASP D 314                CU    CU D 601     1555   1555  2.06  
LINK         NE2 HIS D 381                CU    CU D 601     1555   1555  2.01  
LINK         ND1 HIS D 528                CU    CU D 602     1555   1555  2.00  
LINK        CU    CU A 601                 OXT ACT A 603     1555   1555  1.95  
LINK        CU    CU A 601                 O   HOH A 757     1555   1555  2.44  
LINK        CU    CU A 602                 OXT ACT A 604     1555   1555  2.04  
LINK        CU    CU A 602                 O   HOH A 830     1555   1555  2.10  
LINK        CU    CU A 602                 O   HOH A 702     1555   1555  2.50  
LINK         C   ACT A 603                 CH3 ACT A 604     1555   1555  1.54  
LINK         CH3 ACT A 603                 C   ACT A 604     1555   1555  1.47  
LINK        CU    CU B 601                 O   HOH B 705     1555   1555  2.64  
LINK        CU    CU B 601                 O   ACT B 603     1555   1555  1.90  
LINK        CU    CU B 602                 O   HOH B 702     1555   1555  2.17  
LINK        CU    CU B 602                 OXT ACT B 604     1555   1555  1.96  
LINK        CU    CU B 602                 O   HOH B 918     1555   1555  2.24  
LINK         C   ACT B 603                 CH3 ACT B 604     1555   1555  1.59  
LINK         CH3 ACT B 603                 C   ACT B 604     1555   1555  1.55  
LINK        CU    CU C 601                 OXT ACT C 603     1555   1555  2.07  
LINK        CU    CU C 601                 O   HOH C 744     1555   1555  2.45  
LINK        CU    CU C 602                 O   ACT C 604     1555   1555  1.87  
LINK        CU    CU C 602                 O   HOH C 702     1555   1555  2.44  
LINK        CU    CU C 602                 O   HOH C 801     1555   1555  2.33  
LINK         C   ACT C 603                 CH3 ACT C 604     1555   1555  1.18  
LINK         CH3 ACT C 603                 C   ACT C 604     1555   1555  1.50  
LINK        CU    CU D 601                 O   ACT D 603     1555   1555  1.96  
LINK        CU    CU D 601                 O   HOH D 767     1555   1555  2.42  
LINK        CU    CU D 602                 O   ACT D 604     1555   1555  1.96  
LINK        CU    CU D 602                 O   HOH D 801     1555   1555  2.18  
CISPEP   1 TYR A  432    PRO A  433          0         4.68                     
CISPEP   2 SER A  455    PRO A  456          0         6.45                     
CISPEP   3 TYR B  432    PRO B  433          0         3.66                     
CISPEP   4 SER B  455    PRO B  456          0        11.56                     
CISPEP   5 TYR C  432    PRO C  433          0         6.45                     
CISPEP   6 SER C  455    PRO C  456          0         8.47                     
CISPEP   7 TYR D  432    PRO D  433          0         3.75                     
CISPEP   8 SER D  455    PRO D  456          0         4.24                     
SITE     1 AC1  6 HIS A 206  ASP A 314  HIS A 381  ACT A 603                    
SITE     2 AC1  6 ACT A 604  HOH A 757                                          
SITE     1 AC2  6 LYS A 103  HIS A 135  HIS A 528  ACT A 604                    
SITE     2 AC2  6 HOH A 702  HOH A 830                                          
SITE     1 AC3  6 HIS B 206  ASP B 314  HIS B 381  ACT B 603                    
SITE     2 AC3  6 ACT B 604  HOH B 705                                          
SITE     1 AC4  6 LYS B 103  HIS B 135  HIS B 528  ACT B 604                    
SITE     2 AC4  6 HOH B 702  HOH B 918                                          
SITE     1 AC5  6 HIS C 206  ASP C 314  HIS C 381  ACT C 603                    
SITE     2 AC5  6 ACT C 604  HOH C 744                                          
SITE     1 AC6  7 LYS C 103  HIS C 135  HIS C 136  HIS C 528                    
SITE     2 AC6  7 ACT C 604  HOH C 702  HOH C 801                               
SITE     1 AC7 11 MET C 451  TRP C 453  PRO C 458  ASN C 459                    
SITE     2 AC7 11 GLY C 460  GLU C 474  VAL C 475  ASP C 476                    
SITE     3 AC7 11 HOH C 714  GLY D 272  HOH D 735                               
SITE     1 AC8  6 HIS D 206  ASP D 314  HIS D 381  ACT D 603                    
SITE     2 AC8  6 ACT D 604  HOH D 767                                          
SITE     1 AC9  5 LYS D 103  HIS D 135  HIS D 528  ACT D 604                    
SITE     2 AC9  5 HOH D 801                                                     
SITE     1 AD1  9 HIS D 136  HIS D 206  HIS D 381  HIS D 437                    
SITE     2 AD1  9  CU D 601  ACT D 604  GOL D 606  HOH D 767                    
SITE     3 AD1  9 HOH D 796                                                     
SITE     1 AD2  9 HIS D 135  HIS D 136  HIS D 206  GLU D 288                    
SITE     2 AD2  9  CU D 601   CU D 602  ACT D 603  HOH D 801                    
SITE     3 AD2  9 HOH D1030                                                     
SITE     1 AD3  1 ASP D 243                                                     
SITE     1 AD4 12 PRO D 291  PHE D 436  HIS D 437  TRP D 452                    
SITE     2 AD4 12 MET D 481  HIS D 482  ACT D 603  HOH D 701                    
SITE     3 AD4 12 HOH D 781  HOH D 825  HOH D 863  HOH D 883                    
SITE     1 AD5  4 ASN D 410  THR D 416  HOH D 877  HOH D 978                    
SITE     1 AD6 12 HIS A 135  HIS A 136  HIS A 206  GLU A 288                    
SITE     2 AD6 12 HIS A 381  HIS A 437   CU A 601   CU A 602                    
SITE     3 AD6 12 HOH A 702  HOH A 757  HOH A 775  HOH A 830                    
SITE     1 AD7 12 HIS A 135  HIS A 136  HIS A 206  GLU A 288                    
SITE     2 AD7 12 HIS A 381  HIS A 437   CU A 601   CU A 602                    
SITE     3 AD7 12 HOH A 702  HOH A 757  HOH A 775  HOH A 830                    
SITE     1 AD8 11 HIS B 135  HIS B 136  HIS B 206  ASP B 314                    
SITE     2 AD8 11 HIS B 381  HIS B 437   CU B 601   CU B 602                    
SITE     3 AD8 11 HOH B 702  HOH B 723  HOH B 918                               
SITE     1 AD9 11 HIS B 135  HIS B 136  HIS B 206  ASP B 314                    
SITE     2 AD9 11 HIS B 381  HIS B 437   CU B 601   CU B 602                    
SITE     3 AD9 11 HOH B 702  HOH B 723  HOH B 918                               
SITE     1 AE1 12 HIS C 135  HIS C 136  HIS C 206  GLU C 288                    
SITE     2 AE1 12 HIS C 381  HIS C 437   CU C 601   CU C 602                    
SITE     3 AE1 12 HOH C 702  HOH C 744  HOH C 801  HOH C 806                    
SITE     1 AE2 12 HIS C 135  HIS C 136  HIS C 206  GLU C 288                    
SITE     2 AE2 12 HIS C 381  HIS C 437   CU C 601   CU C 602                    
SITE     3 AE2 12 HOH C 702  HOH C 744  HOH C 801  HOH C 806                    
CRYST1   90.960  162.700   90.938  90.00 119.93  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      0.010994  0.000000  0.006330        0.00000                         
SCALE2      0.000000  0.006146  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012689        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system