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Database: PDB
Entry: 5F75
LinkDB: 5F75
Original site: 5F75 
HEADER    OXIDOREDUCTASE                          07-DEC-15   5F75              
TITLE     THIOCYANATE DEHYDROGENASE FROM THIOALKALIVIBRIO PARADOXUS             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: THIOCYANATE DEHYDROGENASE;                                 
COMPND   3 CHAIN: A, B, C, D                                                    
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: THIOALKALIVIBRIO THIOCYANOXIDANS;               
SOURCE   3 ORGANISM_TAXID: 108010                                               
KEYWDS    OXIDOREDUCTASE, THIOCYANATE DEHYDROGENASE, COPPER CENTERS             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.I.TSALLAGOV,K.M.POLYAKOV,T.V.TIKHONOVA,A.A.TROFIMOV,I.G.SHABALIN,   
AUTHOR   2 A.N.POPOV,V.O.POPOV                                                  
REVDAT   1   14-DEC-16 5F75    0                                                
JRNL        AUTH   S.I.TSALLAGOV,K.M.POLYAKOV,T.V.TIKHONOVA,A.A.TROFIMOV,       
JRNL        AUTH 2 I.G.SHABALIN,A.N.POPOV,V.O.POPOV                             
JRNL        TITL   THIOCYANATE DEHYDROGENASE FROM THIOALKALIVIBRIO PARADOXUS    
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0073                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 118269                         
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) : 0.188                           
REMARK   3   R VALUE            (WORKING SET) : 0.186                           
REMARK   3   FREE R VALUE                     : 0.244                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6063                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 8915                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.85                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3350                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 444                          
REMARK   3   BIN FREE R VALUE                    : 0.3710                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 14504                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 8                                       
REMARK   3   SOLVENT ATOMS            : 513                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 39.52                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.26000                                              
REMARK   3    B22 (A**2) : -1.93000                                             
REMARK   3    B33 (A**2) : -0.34000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.07000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.196         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.180         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.161         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.305         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.968                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.944                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 14951 ; 0.015 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 20396 ; 1.764 ; 1.939       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1877 ; 7.589 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   648 ;36.191 ;24.475       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2255 ;15.200 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    62 ;18.148 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2226 ; 0.119 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 11544 ; 0.009 ; 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):  7520 ; 3.041 ; 3.927       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  9393 ; 4.114 ; 5.875       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  7431 ; 3.686 ; 4.046       
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): 23564 ; 6.421 ;33.427       
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):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
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 5F75 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 07-DEC-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000216133.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-APR-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
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) : 0.97625                            
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   : 124334                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.0                               
REMARK 200  DATA REDUNDANCY                : 2.900                              
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.15                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.66000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: 5F30                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 40.44                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROT: 10 MG/ML PROT, 25 MM BORATE        
REMARK 280  BUFFER (PH 9.0), 150 MM NACL. PREC: 0.04 M POTASSIUM DIHYDROGEN     
REMARK 280  PHOSPHATE, 16 % W/V PEG 8000, 20 % GLYCEROL. VPROT/VPREC=1/1, PH    
REMARK 280  5.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 287K                
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       47.71000            
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                                                    
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: 6000 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 28900 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -88.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 5700 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27870 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -87.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 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     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     LYS B    82                                                      
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     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 465     LYS D    82                                                      
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     SER A  81    OG                                                  
REMARK 470     GLU A 171    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 172    CG   OD1  OD2                                       
REMARK 470     LYS A 301    CG   CD   CE   NZ                                   
REMARK 470     GLU A 341    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 429    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 538    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 171    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 249    CG   CD   CE   NZ                                   
REMARK 470     ASP B 250    CG   OD1  OD2                                       
REMARK 470     LYS B 252    CG   CD   CE   NZ                                   
REMARK 470     GLU B 294    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 301    CG   CD   CE   NZ                                   
REMARK 470     GLU B 341    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 375    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 398    CG   CD1  CD2                                       
REMARK 470     SER B 425    OG                                                  
REMARK 470     ASP B 427    CG   OD1  OD2                                       
REMARK 470     ARG B 429    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 470    CG   CD   OE1  OE2                                  
REMARK 470     GLN C  74    CG   CD   OE1  NE2                                  
REMARK 470     ARG C  78    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER C  79    OG                                                  
REMARK 470     SER C  81    OG                                                  
REMARK 470     LYS C  82    CG   CD   CE   NZ                                   
REMARK 470     ARG C 306    NE   CZ   NH1  NH2                                  
REMARK 470     GLU C 341    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 353    CG   CD   CE   NZ                                   
REMARK 470     ARG C 429    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     MET C 451    CE                                                  
REMARK 470     GLU D 232    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 264    CG   CD   CE   NZ                                   
REMARK 470     LYS D 267    CG   CD   CE   NZ                                   
REMARK 470     ARG D 306    NE   CZ   NH1  NH2                                  
REMARK 470     LYS D 323    CG   CD   CE   NZ                                   
REMARK 470     GLU D 341    CG   CD   OE1  OE2                                  
REMARK 470     GLN D 360    CG   CD   OE1  NE2                                  
REMARK 470     LEU D 398    CG   CD1  CD2                                       
REMARK 470     ASP D 427    CG   OD1  OD2                                       
REMARK 470     ARG D 429    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG D 535    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU D 538    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500  CU     CU B   602     O    HOH B   712              1.62            
REMARK 500  CU     CU C   602     O    HOH C   713              1.64            
REMARK 500   OE1  GLU A   148     NZ   LYS A   183              2.07            
REMARK 500   O    GLY B   380     O    HOH B   701              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A 214   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ARG A 306   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ASP A 367   CB  -  CG  -  OD1 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ASP B 214   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A 103     -118.68     53.51                                   
REMARK 500    HIS A 135      -95.60   -111.60                                   
REMARK 500    THR A 187      -47.18   -135.27                                   
REMARK 500    VAL A 205     -130.89   -113.47                                   
REMARK 500    ASP A 276       54.55   -116.74                                   
REMARK 500    LYS A 323      -49.63     64.12                                   
REMARK 500    ASP A 365     -172.96   -170.93                                   
REMARK 500    HIS A 381      -93.26   -149.39                                   
REMARK 500    SER A 397       33.61   -154.08                                   
REMARK 500    LEU A 398      -57.97   -147.06                                   
REMARK 500    ALA A 431     -110.31     94.38                                   
REMARK 500    ALA A 444        5.78     59.96                                   
REMARK 500    LEU A 477      -54.90   -129.00                                   
REMARK 500    ASP A 480       63.69     60.08                                   
REMARK 500    HIS A 482     -121.87   -110.45                                   
REMARK 500    THR A 503     -147.57   -124.15                                   
REMARK 500    SER A 523       88.74   -158.93                                   
REMARK 500    HIS A 527      116.97    -22.17                                   
REMARK 500    SER A 543     -159.00   -117.96                                   
REMARK 500    SER A 545      -58.08   -150.52                                   
REMARK 500    LYS B 103     -119.18     57.03                                   
REMARK 500    HIS B 135      -92.50   -103.36                                   
REMARK 500    GLU B 148      149.11   -177.81                                   
REMARK 500    THR B 187      -53.69   -130.93                                   
REMARK 500    VAL B 205     -132.68   -107.62                                   
REMARK 500    LYS B 249       42.78    -66.13                                   
REMARK 500    ASP B 276       57.85   -118.29                                   
REMARK 500    VAL B 290     -179.45    -69.02                                   
REMARK 500    LYS B 323      -50.00     69.74                                   
REMARK 500    HIS B 381      -88.99   -163.49                                   
REMARK 500    LEU B 398      -74.05     61.24                                   
REMARK 500    LEU B 477      -51.12   -123.31                                   
REMARK 500    HIS B 482     -115.65   -117.32                                   
REMARK 500    GLN B 501       -2.65     69.39                                   
REMARK 500    THR B 503     -146.74   -121.59                                   
REMARK 500    HIS B 527      121.53    -37.36                                   
REMARK 500    ASN B 530      147.46   -171.90                                   
REMARK 500    SER B 545      -51.68   -149.02                                   
REMARK 500    SER C  79       -9.51    -59.50                                   
REMARK 500    LYS C 103     -116.25     55.87                                   
REMARK 500    THR C 115      -17.12   -140.75                                   
REMARK 500    HIS C 135      -92.60   -116.41                                   
REMARK 500    VAL C 205     -130.18   -107.19                                   
REMARK 500    ASP C 276       58.99   -116.59                                   
REMARK 500    LYS C 323      -52.86     76.91                                   
REMARK 500    ASP C 365     -168.91   -161.84                                   
REMARK 500    HIS C 381      -80.81   -150.86                                   
REMARK 500    LEU C 398      -89.64     77.98                                   
REMARK 500    ALA C 444       11.77     51.49                                   
REMARK 500    HIS C 482     -115.22   -115.97                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      76 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLY A  430     ALA A  431                   41.02                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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 LYS A 103   NZ                                                     
REMARK 620 2 HIS A 135   NE2  95.6                                              
REMARK 620 3 HIS A 528   ND1  98.3 139.7                                        
REMARK 620 4 HOH A 719   O   173.5  83.1  86.6                                  
REMARK 620 5 HOH A 756   O    93.4  97.1 119.5  80.4                            
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   OD1  96.7                                              
REMARK 620 3 ASP A 314   OD2  91.5  57.7                                        
REMARK 620 4 HIS A 381   NE2 176.1  83.9  92.1                                  
REMARK 620 5 HOH A 729   O    84.6 140.8  83.0  97.5                            
REMARK 620 6 HOH A 840   O    85.4 114.3 171.1  90.8 104.9                      
REMARK 620 N                    1     2     3     4     5                       
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 LYS B 103   NZ                                                     
REMARK 620 2 HIS B 135   NE2  95.9                                              
REMARK 620 3 HIS B 528   ND1  97.5 143.9                                        
REMARK 620 4 HOH B 714   O    73.8 100.0 116.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU B 601  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 206   NE2                                                    
REMARK 620 2 ASP B 314   OD1  92.3                                              
REMARK 620 3 ASP B 314   OD2  91.0  53.5                                        
REMARK 620 4 HIS B 381   NE2 173.2  91.4  86.7                                  
REMARK 620 5 HOH B 751   O    87.2 152.1  98.7  86.9                            
REMARK 620 6 HOH B 828   O    92.0 114.7 167.9  91.6  93.1                      
REMARK 620 N                    1     2     3     4     5                       
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 LYS C 103   NZ                                                     
REMARK 620 2 HIS C 135   NE2  91.1                                              
REMARK 620 3 HIS C 528   ND1  93.0 140.9                                        
REMARK 620 4 HOH C 706   O    82.4  99.9 119.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU C 601  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 206   NE2                                                    
REMARK 620 2 ASP C 314   OD1  94.6                                              
REMARK 620 3 ASP C 314   OD2  91.9  55.9                                        
REMARK 620 4 HIS C 381   NE2 170.8  91.4  85.8                                  
REMARK 620 5 HOH C 769   O    83.4 149.3  93.4  87.9                            
REMARK 620 6 HOH C 810   O    87.6 117.4 173.3  95.7  93.2                      
REMARK 620 N                    1     2     3     4     5                       
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 LYS D 103   NZ                                                     
REMARK 620 2 HIS D 135   NE2  87.4                                              
REMARK 620 3 HIS D 528   ND1  94.1 140.6                                        
REMARK 620 4 HOH D 749   O    81.8 102.4 116.8                                  
REMARK 620 5 HOH D 709   O   173.1  86.4  92.7  96.7                            
REMARK 620 N                    1     2     3     4                             
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  93.7                                              
REMARK 620 3 HIS D 381   NE2 174.8  84.3                                        
REMARK 620 4 HOH D 783   O    89.9 166.9  93.1                                  
REMARK 620 5 HOH D 736   O    81.2 104.2  94.6  88.8                            
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 CU D 601                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU D 602                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5F30   RELATED DB: PDB                                   
DBREF  5F75 A    1   548  UNP    W0DP94   W0DP94_9GAMM     1    548             
DBREF  5F75 B    1   548  UNP    W0DP94   W0DP94_9GAMM     1    548             
DBREF  5F75 C    1   548  UNP    W0DP94   W0DP94_9GAMM     1    548             
DBREF  5F75 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     CU  B 601       1                                                       
HET     CU  B 602       1                                                       
HET     CU  C 601       1                                                       
HET     CU  C 602       1                                                       
HET     CU  D 601       1                                                       
HET     CU  D 602       1                                                       
HETNAM      CU COPPER (II) ION                                                  
FORMUL   5   CU    8(CU 2+)                                                     
FORMUL  13  HOH   *513(H2 O)                                                    
HELIX    1 AA1 LYS A   85  GLY A   94  1                                  10    
HELIX    2 AA2 LYS A  103  SER A  105  5                                   3    
HELIX    3 AA3 TRP A  125  GLY A  128  5                                   4    
HELIX    4 AA4 GLY A  158  ILE A  163  5                                   6    
HELIX    5 AA5 ALA A  195  GLY A  200  1                                   6    
HELIX    6 AA6 LEU A  270  ARG A  274  5                                   5    
HELIX    7 AA7 GLY A  293  ASP A  299  1                                   7    
HELIX    8 AA8 ARG A  306  SER A  310  5                                   5    
HELIX    9 AA9 ASP A  413  TRP A  417  5                                   5    
HELIX   10 AB1 TYR A  500  ASN A  502  5                                   3    
HELIX   11 AB2 THR A  536  ARG A  541  1                                   6    
HELIX   12 AB3 LYS B   85  GLY B   94  1                                  10    
HELIX   13 AB4 LYS B  103  SER B  105  5                                   3    
HELIX   14 AB5 TRP B  125  GLY B  128  5                                   4    
HELIX   15 AB6 GLY B  158  ILE B  163  5                                   6    
HELIX   16 AB7 ALA B  195  GLY B  200  1                                   6    
HELIX   17 AB8 ASP B  250  TRP B  255  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 SER B  425  ARG B  429  5                                   5    
HELIX   23 AC5 TYR B  500  ASN B  502  5                                   3    
HELIX   24 AC6 THR B  536  ARG B  541  1                                   6    
HELIX   25 AC7 LYS C   85  GLN C   92  1                                   8    
HELIX   26 AC8 LYS C  103  SER C  105  5                                   3    
HELIX   27 AC9 TRP C  125  GLY C  128  5                                   4    
HELIX   28 AD1 GLY C  158  ILE C  163  5                                   6    
HELIX   29 AD2 ALA C  195  GLY C  200  1                                   6    
HELIX   30 AD3 LEU C  270  ARG C  274  5                                   5    
HELIX   31 AD4 GLY C  292  ASP C  299  1                                   8    
HELIX   32 AD5 ARG C  306  SER C  310  5                                   5    
HELIX   33 AD6 ASP C  413  TRP C  417  5                                   5    
HELIX   34 AD7 SER C  425  ARG C  429  5                                   5    
HELIX   35 AD8 TYR C  500  ASN C  502  5                                   3    
HELIX   36 AD9 GLU C  538  SER C  543  5                                   6    
HELIX   37 AE1 VAL D   86  GLY D   94  1                                   9    
HELIX   38 AE2 LYS D  103  SER D  105  5                                   3    
HELIX   39 AE3 TRP D  125  GLY D  128  5                                   4    
HELIX   40 AE4 GLY D  158  ILE D  163  5                                   6    
HELIX   41 AE5 ALA D  195  GLY D  200  1                                   6    
HELIX   42 AE6 GLY D  292  ASP D  299  1                                   8    
HELIX   43 AE7 ARG D  306  SER D  310  5                                   5    
HELIX   44 AE8 ASP D  413  TRP D  417  5                                   5    
HELIX   45 AE9 SER D  425  ARG D  429  5                                   5    
HELIX   46 AF1 TYR D  500  ASN D  502  5                                   3    
HELIX   47 AF2 GLU D  538  SER D  543  5                                   6    
SHEET    1 AA1 4 THR A 118  ALA A 123  0                                        
SHEET    2 AA1 4 THR A 107  ASP A 112 -1  N  ALA A 110   O  ALA A 120           
SHEET    3 AA1 4 VAL A  97  PRO A 101 -1  N  LEU A  98   O  THR A 111           
SHEET    4 AA1 4 VAL A 531  ILE A 532 -1  O  VAL A 531   N  VAL A  99           
SHEET    1 AA2 4 ILE A 133  ALA A 139  0                                        
SHEET    2 AA2 4 PHE A 149  GLN A 156 -1  O  ASN A 154   N  HIS A 135           
SHEET    3 AA2 4 GLY A 176  TYR A 184 -1  O  TYR A 184   N  PHE A 149           
SHEET    4 AA2 4 MET A 189  ASP A 194 -1  O  ARG A 193   N  ARG A 181           
SHEET    1 AA3 7 VAL A 207  ILE A 209  0                                        
SHEET    2 AA3 7 GLY A 215  ASP A 220 -1  O  ALA A 217   N  THR A 208           
SHEET    3 AA3 7 ILE A 225  ASP A 230 -1  O  PHE A 229   N  TYR A 216           
SHEET    4 AA3 7 VAL A 236  PRO A 246 -1  O  TRP A 240   N  CYS A 226           
SHEET    5 AA3 7 GLY A 259  ARG A 265 -1  O  THR A 260   N  ASP A 245           
SHEET    6 AA3 7 THR A 368  ILE A 373 -1  O  VAL A 371   N  MET A 261           
SHEET    7 AA3 7 VAL A 362  ASP A 365 -1  N  VAL A 362   O  THR A 370           
SHEET    1 AA4 5 ASN A 313  PHE A 318  0                                        
SHEET    2 AA4 5 TRP A 324  MET A 329 -1  O  VAL A 326   N  VAL A 317           
SHEET    3 AA4 5 VAL A 334  ASP A 339 -1  O  PHE A 338   N  ALA A 325           
SHEET    4 AA4 5 VAL A 344  ALA A 350 -1  O  VAL A 344   N  ASP A 339           
SHEET    5 AA4 5 GLN A 358  PHE A 359 -1  O  PHE A 359   N  VAL A 348           
SHEET    1 AA5 4 GLY A 380  PHE A 385  0                                        
SHEET    2 AA5 4 SER A 391  SER A 397 -1  O  LEU A 393   N  GLY A 384           
SHEET    3 AA5 4 ASN A 401  ASP A 407 -1  O  TRP A 406   N  PHE A 392           
SHEET    4 AA5 4 GLU A 418  VAL A 423 -1  O  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  LYS A 473   N  VAL A 463           
SHEET    1 AA7 4 MET A 481  ILE A 486  0                                        
SHEET    2 AA7 4 PHE A 492  SER A 498 -1  O  THR A 496   N  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 GLU A 516  PRO A 522 -1  O  LEU A 521   N  ILE A 507           
SHEET    1 AA8 4 THR B 118  ALA B 123  0                                        
SHEET    2 AA8 4 THR B 107  ASP B 112 -1  N  ALA B 110   O  ALA B 120           
SHEET    3 AA8 4 VAL B  97  PRO B 101 -1  N  LEU B  98   O  THR B 111           
SHEET    4 AA8 4 VAL B 531  ILE B 532 -1  O  VAL B 531   N  VAL B  99           
SHEET    1 AA9 4 ILE B 133  ALA B 139  0                                        
SHEET    2 AA9 4 PHE B 149  GLN B 156 -1  O  ASN B 154   N  HIS B 135           
SHEET    3 AA9 4 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  THR B 262   N  ASP B 243           
SHEET    6 AB1 7 THR B 368  ILE B 373 -1  O  TRP B 369   N  ILE B 263           
SHEET    7 AB1 7 LEU B 361  ASP B 365 -1  N  VAL B 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 ALA B 379  PHE B 385  0                                        
SHEET    2 AB3 4 SER B 391  SER B 397 -1  O  LEU B 393   N  GLY B 384           
SHEET    3 AB3 4 ASN B 402  ASP B 407 -1  O  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  LEU B 477   N  ASN B 459           
SHEET    1 AB5 4 MET B 481  ILE B 486  0                                        
SHEET    2 AB5 4 PHE B 492  SER B 498 -1  O  VAL B 494   N  ALA B 485           
SHEET    3 AB5 4 SER B 505  GLU B 511 -1  O  VAL B 508   N  GLY B 495           
SHEET    4 AB5 4 GLU B 516  PRO B 522 -1  O  LEU B 518   N  VAL B 509           
SHEET    1 AB6 4 THR C 118  ALA C 123  0                                        
SHEET    2 AB6 4 THR C 107  ASP C 112 -1  N  ALA C 110   O  MET C 119           
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 180   N  VAL C 153           
SHEET    4 AB7 4 MET C 189  ASP C 194 -1  O  GLN C 192   N  ARG C 181           
SHEET    1 AB8 7 VAL C 207  ILE C 209  0                                        
SHEET    2 AB8 7 GLY C 215  ASP C 220 -1  O  ALA C 217   N  THR C 208           
SHEET    3 AB8 7 ILE C 225  ASP C 230 -1  O  PHE C 229   N  TYR C 216           
SHEET    4 AB8 7 VAL C 236  PRO C 246 -1  O  ARG C 237   N  GLU C 228           
SHEET    5 AB8 7 GLY C 259  ARG C 265 -1  O  LYS C 264   N  ALA C 241           
SHEET    6 AB8 7 THR C 368  ILE C 373 -1  O  ILE C 373   N  GLY C 259           
SHEET    7 AB8 7 VAL C 362  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  LEU C 349   N  CYS C 335           
SHEET    5 AB9 5 GLN C 358  PHE C 359 -1  O  PHE C 359   N  VAL C 348           
SHEET    1 AC1 4 ALA C 379  PHE C 385  0                                        
SHEET    2 AC1 4 SER C 391  SER C 397 -1  O  MET C 395   N  GLN C 382           
SHEET    3 AC1 4 ASN C 402  ASP C 407 -1  O  TRP C 406   N  PHE C 392           
SHEET    4 AC1 4 GLU C 418  VAL C 423 -1  O  LYS C 420   N  VAL C 405           
SHEET    1 AC2 4 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  ILE C 464   N  ILE C 447           
SHEET    4 AC2 4 GLU C 470  GLY C 478 -1  O  GLU C 470   N  ASP C 465           
SHEET    1 AC3 4 MET C 481  ILE C 486  0                                        
SHEET    2 AC3 4 PHE C 492  SER C 498 -1  O  THR C 496   N  HIS C 482           
SHEET    3 AC3 4 SER C 505  GLU C 511 -1  O  ALA C 506   N  LEU C 497           
SHEET    4 AC3 4 GLU C 516  PRO C 522 -1  O  LEU C 518   N  VAL C 509           
SHEET    1 AC4 4 THR D 118  ALA D 123  0                                        
SHEET    2 AC4 4 THR D 107  ASP D 112 -1  N  ALA D 110   O  MET D 119           
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  VAL D 152   N  ALA D 138           
SHEET    3 AC5 4 GLY D 176  TYR D 184 -1  O  ILE D 182   N  PHE D 151           
SHEET    4 AC5 4 MET D 189  ASP D 194 -1  O  GLN D 192   N  ARG D 181           
SHEET    1 AC6 7 VAL D 207  ILE D 209  0                                        
SHEET    2 AC6 7 GLY D 215  VAL D 218 -1  O  ALA D 217   N  THR D 208           
SHEET    3 AC6 7 ILE D 225  ASP D 230 -1  O  PHE D 229   N  TYR D 216           
SHEET    4 AC6 7 VAL D 236  PRO D 246 -1  O  TRP D 240   N  CYS D 226           
SHEET    5 AC6 7 GLY D 259  ARG D 265 -1  O  THR D 260   N  ASP D 245           
SHEET    6 AC6 7 THR D 368  ILE D 373 -1  O  TRP D 369   N  ILE D 263           
SHEET    7 AC6 7 VAL D 362  ASP D 365 -1  N  VAL D 362   O  THR D 370           
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 344   N  ASP D 339           
SHEET    5 AC7 5 GLN D 358  PHE D 359 -1  O  PHE D 359   N  VAL D 348           
SHEET    1 AC8 4 ALA D 379  PHE D 385  0                                        
SHEET    2 AC8 4 SER D 391  SER D 397 -1  O  SER D 397   N  ALA D 379           
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  ALA D 421   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  ALA D 462   N  VAL D 449           
SHEET    4 AC9 4 GLU D 470  GLY D 478 -1  O  LEU D 472   N  VAL D 463           
SHEET    1 AD1 4 MET D 481  ILE D 486  0                                        
SHEET    2 AD1 4 PHE D 492  SER D 498 -1  O  VAL D 494   N  ALA D 485           
SHEET    3 AD1 4 SER D 505  GLU D 511 -1  O  MET D 510   N  VAL D 493           
SHEET    4 AD1 4 GLU D 516  PRO D 522 -1  O  LEU D 521   N  ILE D 507           
LINK         NZ  LYS A 103                CU    CU A 602     1555   1555  2.21  
LINK         NE2 HIS A 135                CU    CU A 602     1555   1555  2.03  
LINK         NE2 HIS A 206                CU    CU A 601     1555   1555  2.01  
LINK         OD1 ASP A 314                CU    CU A 601     1555   1555  2.57  
LINK         OD2 ASP A 314                CU    CU A 601     1555   1555  2.01  
LINK         NE2 HIS A 381                CU    CU A 601     1555   1555  1.99  
LINK         ND1 HIS A 528                CU    CU A 602     1555   1555  2.00  
LINK         NZ  LYS B 103                CU    CU B 602     1555   1555  2.51  
LINK         NE2 HIS B 135                CU    CU B 602     1555   1555  2.02  
LINK         NE2 HIS B 206                CU    CU B 601     1555   1555  2.05  
LINK         OD1 ASP B 314                CU    CU B 601     1555   1555  2.60  
LINK         OD2 ASP B 314                CU    CU B 601     1555   1555  1.99  
LINK         NE2 HIS B 381                CU    CU B 601     1555   1555  2.05  
LINK         ND1 HIS B 528                CU    CU B 602     1555   1555  1.99  
LINK         NZ  LYS C 103                CU    CU C 602     1555   1555  2.39  
LINK         NE2 HIS C 135                CU    CU C 602     1555   1555  2.00  
LINK         NE2 HIS C 206                CU    CU C 601     1555   1555  2.02  
LINK         OD1 ASP C 314                CU    CU C 601     1555   1555  2.57  
LINK         OD2 ASP C 314                CU    CU C 601     1555   1555  2.01  
LINK         NE2 HIS C 381                CU    CU C 601     1555   1555  1.98  
LINK         ND1 HIS C 528                CU    CU C 602     1555   1555  1.97  
LINK         NZ  LYS D 103                CU    CU D 602     1555   1555  2.62  
LINK         NE2 HIS D 135                CU    CU D 602     1555   1555  2.01  
LINK         NE2 HIS D 206                CU    CU D 601     1555   1555  2.01  
LINK         OD2 ASP D 314                CU    CU D 601     1555   1555  1.94  
LINK         NE2 HIS D 381                CU    CU D 601     1555   1555  1.99  
LINK         ND1 HIS D 528                CU    CU D 602     1555   1555  2.00  
LINK        CU    CU A 601                 O   HOH A 729     1555   1555  1.90  
LINK        CU    CU A 601                 O   HOH A 840     1555   1555  2.56  
LINK        CU    CU A 602                 O   HOH A 719     1555   1555  1.80  
LINK        CU    CU A 602                 O   HOH A 756     1555   1555  2.10  
LINK        CU    CU B 601                 O   HOH B 751     1555   1555  2.47  
LINK        CU    CU B 601                 O   HOH B 828     1555   1555  2.32  
LINK        CU    CU B 602                 O   HOH B 714     1555   1555  2.27  
LINK        CU    CU C 601                 O   HOH C 769     1555   1555  2.25  
LINK        CU    CU C 601                 O   HOH C 810     1555   1555  2.30  
LINK        CU    CU C 602                 O   HOH C 706     1555   1555  2.25  
LINK        CU    CU D 601                 O   HOH D 783     1555   1555  2.61  
LINK        CU    CU D 601                 O   HOH D 736     1555   1555  2.41  
LINK        CU    CU D 602                 O   HOH D 749     1555   1555  2.31  
LINK        CU    CU D 602                 O   HOH D 709     1555   1555  1.78  
CISPEP   1 TYR A  432    PRO A  433          0        -4.97                     
CISPEP   2 SER A  455    PRO A  456          0         7.75                     
CISPEP   3 TYR B  432    PRO B  433          0         3.21                     
CISPEP   4 SER B  455    PRO B  456          0        10.32                     
CISPEP   5 TYR C  432    PRO C  433          0         3.51                     
CISPEP   6 SER C  455    PRO C  456          0        12.69                     
CISPEP   7 TYR D  432    PRO D  433          0         5.51                     
CISPEP   8 SER D  455    PRO D  456          0         9.85                     
SITE     1 AC1  5 HIS A 206  ASP A 314  HIS A 381  HOH A 729                    
SITE     2 AC1  5 HOH A 840                                                     
SITE     1 AC2  5 LYS A 103  HIS A 135  HIS A 528  HOH A 719                    
SITE     2 AC2  5 HOH A 756                                                     
SITE     1 AC3  5 HIS B 206  ASP B 314  HIS B 381  HOH B 751                    
SITE     2 AC3  5 HOH B 828                                                     
SITE     1 AC4  5 LYS B 103  HIS B 135  HIS B 528  HOH B 712                    
SITE     2 AC4  5 HOH B 714                                                     
SITE     1 AC5  5 HIS C 206  ASP C 314  HIS C 381  HOH C 769                    
SITE     2 AC5  5 HOH C 810                                                     
SITE     1 AC6  5 LYS C 103  HIS C 135  HIS C 528  HOH C 706                    
SITE     2 AC6  5 HOH C 713                                                     
SITE     1 AC7  5 HIS D 206  ASP D 314  HIS D 381  HOH D 736                    
SITE     2 AC7  5 HOH D 783                                                     
SITE     1 AC8  5 LYS D 103  HIS D 135  HIS D 528  HOH D 709                    
SITE     2 AC8  5 HOH D 749                                                     
CRYST1   98.780   95.420  107.000  90.00 100.66  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      0.010124  0.000000  0.001905        0.00000                         
SCALE2      0.000000  0.010480  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009510        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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