GenomeNet

Database: PDB
Entry: 1SOS
LinkDB: 1SOS
Original site: 1SOS 
HEADER    OXIDOREDUCTASE (SUPEROXIDE ACCEPTOR)    11-FEB-92   1SOS              
TITLE     ATOMIC STRUCTURES OF WILD-TYPE AND THERMOSTABLE MUTANT                
TITLE    2 RECOMBINANT HUMAN CU, ZN SUPEROXIDE DISMUTASE                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE;                                      
COMPND   3 CHAIN: A, F, B, G, C, H, D, I, E, J;                                 
COMPND   4 EC: 1.15.1.1;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606                                                 
KEYWDS    OXIDOREDUCTASE (SUPEROXIDE ACCEPTOR)                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.E.PARGE,R.A.HALLEWELL,J.A.TAINER                                    
REVDAT   3   24-FEB-09 1SOS    1       VERSN                                    
REVDAT   2   31-JUL-94 1SOS    1       SHEET                                    
REVDAT   1   15-APR-93 1SOS    0                                                
JRNL        AUTH   H.E.PARGE,R.A.HALLEWELL,J.A.TAINER                           
JRNL        TITL   ATOMIC STRUCTURES OF WILD-TYPE AND THERMOSTABLE              
JRNL        TITL 2 MUTANT RECOMBINANT HUMAN CU,ZN SUPEROXIDE                    
JRNL        TITL 3 DISMUTASE.                                                   
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V.  89  6109 1992              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   1463506                                                      
JRNL        DOI    10.1073/PNAS.89.13.6109                                      
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR                                               
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : NULL                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : NULL                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.202                           
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 11120                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 30                                      
REMARK   3   SOLVENT ATOMS            : 499                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.017                           
REMARK   3   BOND ANGLES            (DEGREES) : 3.50                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1SOS COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : NULL                               
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 68.80                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.94                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-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        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       72.75000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       72.75000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000      102.60000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       83.50000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000      102.60000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       83.50000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       72.75000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000      102.60000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       83.50000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       72.75000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000      102.60000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       83.50000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5                                           
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: 1900 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13630 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, F                                  
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: 1990 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13750 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, G                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1890 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13830 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, H                                  
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: 4                                                       
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: 2100 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13680 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -47.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, I                                  
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: 5                                                       
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: 1910 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13620 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -37.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, J                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    HIS A  43   NE2   HIS A  43   CD2    -0.073                       
REMARK 500    HIS A  48   NE2   HIS A  48   CD2    -0.078                       
REMARK 500    HIS A  71   NE2   HIS A  71   CD2    -0.071                       
REMARK 500    HIS A  80   NE2   HIS A  80   CD2    -0.080                       
REMARK 500    HIS A 110   NE2   HIS A 110   CD2    -0.069                       
REMARK 500    HIS A 120   NE2   HIS A 120   CD2    -0.072                       
REMARK 500    HIS F  46   NE2   HIS F  46   CD2    -0.072                       
REMARK 500    HIS F  48   NE2   HIS F  48   CD2    -0.075                       
REMARK 500    HIS F  71   NE2   HIS F  71   CD2    -0.074                       
REMARK 500    HIS F  80   NE2   HIS F  80   CD2    -0.079                       
REMARK 500    HIS F 110   NE2   HIS F 110   CD2    -0.077                       
REMARK 500    HIS F 120   NE2   HIS F 120   CD2    -0.074                       
REMARK 500    HIS B  43   NE2   HIS B  43   CD2    -0.071                       
REMARK 500    HIS B  46   NE2   HIS B  46   CD2    -0.087                       
REMARK 500    HIS B  63   NE2   HIS B  63   CD2    -0.073                       
REMARK 500    HIS B  71   NE2   HIS B  71   CD2    -0.091                       
REMARK 500    HIS G  43   NE2   HIS G  43   CD2    -0.088                       
REMARK 500    HIS G  46   NE2   HIS G  46   CD2    -0.074                       
REMARK 500    HIS G  63   NE2   HIS G  63   CD2    -0.078                       
REMARK 500    HIS G  71   NE2   HIS G  71   CD2    -0.079                       
REMARK 500    HIS G  80   NE2   HIS G  80   CD2    -0.072                       
REMARK 500    HIS G 110   NE2   HIS G 110   CD2    -0.079                       
REMARK 500    HIS G 120   NE2   HIS G 120   CD2    -0.072                       
REMARK 500    HIS C  43   NE2   HIS C  43   CD2    -0.078                       
REMARK 500    HIS C  46   NE2   HIS C  46   CD2    -0.071                       
REMARK 500    HIS C  71   NE2   HIS C  71   CD2    -0.092                       
REMARK 500    HIS C  80   NE2   HIS C  80   CD2    -0.085                       
REMARK 500    HIS C 120   NE2   HIS C 120   CD2    -0.073                       
REMARK 500    HIS H  43   NE2   HIS H  43   CD2    -0.068                       
REMARK 500    HIS H  46   NE2   HIS H  46   CD2    -0.068                       
REMARK 500    HIS H  71   NE2   HIS H  71   CD2    -0.078                       
REMARK 500    HIS H  80   NE2   HIS H  80   CD2    -0.076                       
REMARK 500    HIS H 110   NE2   HIS H 110   CD2    -0.079                       
REMARK 500    HIS D  43   NE2   HIS D  43   CD2    -0.075                       
REMARK 500    HIS D  46   NE2   HIS D  46   CD2    -0.072                       
REMARK 500    HIS D  48   NE2   HIS D  48   CD2    -0.068                       
REMARK 500    HIS D  71   NE2   HIS D  71   CD2    -0.095                       
REMARK 500    HIS D  80   NE2   HIS D  80   CD2    -0.083                       
REMARK 500    HIS D 120   NE2   HIS D 120   CD2    -0.072                       
REMARK 500    HIS I  43   NE2   HIS I  43   CD2    -0.070                       
REMARK 500    HIS I  46   NE2   HIS I  46   CD2    -0.083                       
REMARK 500    HIS I  48   NE2   HIS I  48   CD2    -0.069                       
REMARK 500    HIS I  71   NE2   HIS I  71   CD2    -0.079                       
REMARK 500    HIS I  80   NE2   HIS I  80   CD2    -0.071                       
REMARK 500    HIS I 110   NE2   HIS I 110   CD2    -0.072                       
REMARK 500    HIS I 120   NE2   HIS I 120   CD2    -0.084                       
REMARK 500    HIS E  71   NE2   HIS E  71   CD2    -0.077                       
REMARK 500    HIS E  80   NE2   HIS E  80   CD2    -0.074                       
REMARK 500    HIS E 110   NE2   HIS E 110   CD2    -0.071                       
REMARK 500    HIS J  43   NE2   HIS J  43   CD2    -0.070                       
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      54 BOND DEVIATIONS.                              
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    TRP A  32   CD1 -  CG  -  CD2 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    TRP A  32   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.4 DEGREES          
REMARK 500    ARG A  69   CB  -  CG  -  CD  ANGL. DEV. = -17.2 DEGREES          
REMARK 500    ARG A  69   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG A  69   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.6 DEGREES          
REMARK 500    ARG A  79   NE  -  CZ  -  NH1 ANGL. DEV. =   4.5 DEGREES          
REMARK 500    GLU A 100   N   -  CA  -  C   ANGL. DEV. = -18.6 DEGREES          
REMARK 500    ARG A 115   NE  -  CZ  -  NH1 ANGL. DEV. =   4.8 DEGREES          
REMARK 500    TRP F  32   CD1 -  CG  -  CD2 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    TRP F  32   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.0 DEGREES          
REMARK 500    ARG F  79   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ARG F  79   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    HIS F  80   CA  -  CB  -  CG  ANGL. DEV. =  11.2 DEGREES          
REMARK 500    ARG F 115   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ARG F 143   NE  -  CZ  -  NH1 ANGL. DEV. =   4.3 DEGREES          
REMARK 500    CYS F 146   CA  -  CB  -  SG  ANGL. DEV. =   6.6 DEGREES          
REMARK 500    VAL B  14   CG1 -  CB  -  CG2 ANGL. DEV. = -10.9 DEGREES          
REMARK 500    TRP B  32   CD1 -  CG  -  CD2 ANGL. DEV. =   6.6 DEGREES          
REMARK 500    TRP B  32   CB  -  CG  -  CD1 ANGL. DEV. =  -8.2 DEGREES          
REMARK 500    TRP B  32   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    TRP B  32   CG  -  CD2 -  CE3 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    LYS B  70   CA  -  CB  -  CG  ANGL. DEV. = -13.4 DEGREES          
REMARK 500    ARG B  79   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    ASP B  83   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ARG B 143   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    TRP G  32   CD1 -  CG  -  CD2 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    TRP G  32   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.0 DEGREES          
REMARK 500    ARG G 115   NE  -  CZ  -  NH1 ANGL. DEV. =   4.4 DEGREES          
REMARK 500    GLU G 133   N   -  CA  -  CB  ANGL. DEV. = -11.3 DEGREES          
REMARK 500    ARG G 143   NE  -  CZ  -  NH1 ANGL. DEV. =   4.6 DEGREES          
REMARK 500    ARG G 143   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.6 DEGREES          
REMARK 500    TRP C  32   CD1 -  CG  -  CD2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    TRP C  32   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    ARG C  79   NE  -  CZ  -  NH1 ANGL. DEV. =   7.4 DEGREES          
REMARK 500    ARG C  79   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    ASP C  83   CB  -  CG  -  OD1 ANGL. DEV. =   7.4 DEGREES          
REMARK 500    ASP C  83   CB  -  CG  -  OD2 ANGL. DEV. =  -6.4 DEGREES          
REMARK 500    VAL C 118   CG1 -  CB  -  CG2 ANGL. DEV. = -10.2 DEGREES          
REMARK 500    TRP H  32   CD1 -  CG  -  CD2 ANGL. DEV. =   6.8 DEGREES          
REMARK 500    TRP H  32   CB  -  CG  -  CD1 ANGL. DEV. =  -8.9 DEGREES          
REMARK 500    TRP H  32   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.9 DEGREES          
REMARK 500    TRP H  32   CG  -  CD2 -  CE3 ANGL. DEV. =   6.6 DEGREES          
REMARK 500    ARG H  79   NE  -  CZ  -  NH1 ANGL. DEV. =   6.6 DEGREES          
REMARK 500    ARG H  79   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.8 DEGREES          
REMARK 500    TRP D  32   CD1 -  CG  -  CD2 ANGL. DEV. =   5.2 DEGREES          
REMARK 500    TRP D  32   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.1 DEGREES          
REMARK 500    ARG D  69   NE  -  CZ  -  NH1 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ARG D  69   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.1 DEGREES          
REMARK 500    ARG D 115   NE  -  CZ  -  NH1 ANGL. DEV. =   3.5 DEGREES          
REMARK 500    LYS I  30   CA  -  CB  -  CG  ANGL. DEV. =  15.0 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      70 ANGLE DEVIATIONS.                             
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    ASP A 125       21.64    -77.18                                   
REMARK 500    LEU A 126       27.89     43.64                                   
REMARK 500    ASN A 131      160.58    171.47                                   
REMARK 500    ASP F  90     -170.32    -68.51                                   
REMARK 500    GLU B  40      129.77    -33.39                                   
REMARK 500    ALA B  55       31.63    -86.62                                   
REMARK 500    SER B  68       61.29     32.01                                   
REMARK 500    ARG B  69     -169.34   -105.44                                   
REMARK 500    LYS B 128       45.16    -96.20                                   
REMARK 500    ALA G  55       36.94    -90.98                                   
REMARK 500    SER G  68       58.93     39.56                                   
REMARK 500    ARG G  69     -167.82   -105.92                                   
REMARK 500    ASP C  90     -172.95    -64.46                                   
REMARK 500    SER C  98       89.33   -158.02                                   
REMARK 500    LYS C 136      -61.23   -104.64                                   
REMARK 500    ASP H  92        4.24    -66.09                                   
REMARK 500    ASP H 125       31.97    -87.51                                   
REMARK 500    LEU H 126       20.09     37.92                                   
REMARK 500    SER D  25      -36.41    -12.10                                   
REMARK 500    ASN D  26       28.15   -153.77                                   
REMARK 500    ALA D  55       47.76    -94.26                                   
REMARK 500    SER D  68       70.67     29.96                                   
REMARK 500    LYS D  91       -5.56    -59.09                                   
REMARK 500    SER D  98      107.33   -165.27                                   
REMARK 500    LEU D 126       19.65     48.97                                   
REMARK 500    ASN D 131      162.38    175.47                                   
REMARK 500    ALA I  55       50.27   -112.08                                   
REMARK 500    ASN I  65       69.08   -150.75                                   
REMARK 500    ASP I  90     -167.40    -73.74                                   
REMARK 500    LYS I 136      -60.14   -107.68                                   
REMARK 500    SER E  25      -34.85    -30.57                                   
REMARK 500    PHE E  64      109.59    -57.16                                   
REMARK 500    SER E  68       73.34     40.12                                   
REMARK 500    ASP E  90      176.85    -59.97                                   
REMARK 500    VAL E 103      -45.27   -148.87                                   
REMARK 500    LYS E 128       36.83    -72.40                                   
REMARK 500    LYS E 136      -76.64   -102.71                                   
REMARK 500    GLU J  24      123.31    158.05                                   
REMARK 500    SER J  25      -25.78    -25.33                                   
REMARK 500    ASN J  26       44.64   -159.01                                   
REMARK 500    ASN J  53       61.99   -105.81                                   
REMARK 500    ALA J  55       49.21   -102.67                                   
REMARK 500    SER J  59        6.62    -67.96                                   
REMARK 500    ASP J  92       64.75   -103.74                                   
REMARK 500    VAL J 103      -32.72   -148.82                                   
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 D   12     PRO D   13                 -129.84                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH D 156        DISTANCE =  8.59 ANGSTROMS                       
REMARK 525    HOH G 156        DISTANCE =  5.15 ANGSTROMS                       
REMARK 525    HOH B 157        DISTANCE =  5.65 ANGSTROMS                       
REMARK 525    HOH D 159        DISTANCE = 17.57 ANGSTROMS                       
REMARK 525    HOH E 160        DISTANCE =  5.29 ANGSTROMS                       
REMARK 525    HOH F 361        DISTANCE =  6.07 ANGSTROMS                       
REMARK 525    HOH A 161        DISTANCE =  7.43 ANGSTROMS                       
REMARK 525    HOH C 162        DISTANCE = 10.21 ANGSTROMS                       
REMARK 525    HOH G 162        DISTANCE =  5.84 ANGSTROMS                       
REMARK 525    HOH J 162        DISTANCE =  6.08 ANGSTROMS                       
REMARK 525    HOH C 164        DISTANCE =  5.42 ANGSTROMS                       
REMARK 525    HOH C 166        DISTANCE =  6.06 ANGSTROMS                       
REMARK 525    HOH H 167        DISTANCE =  5.12 ANGSTROMS                       
REMARK 525    HOH E 168        DISTANCE =  5.27 ANGSTROMS                       
REMARK 525    HOH F 369        DISTANCE =  5.71 ANGSTROMS                       
REMARK 525    HOH A 169        DISTANCE =  8.41 ANGSTROMS                       
REMARK 525    HOH C 170        DISTANCE =  7.01 ANGSTROMS                       
REMARK 525    HOH D 170        DISTANCE =  6.43 ANGSTROMS                       
REMARK 525    HOH I 372        DISTANCE =  5.75 ANGSTROMS                       
REMARK 525    HOH D 172        DISTANCE =  6.27 ANGSTROMS                       
REMARK 525    HOH H 172        DISTANCE =  5.27 ANGSTROMS                       
REMARK 525    HOH D 173        DISTANCE =  6.21 ANGSTROMS                       
REMARK 525    HOH I 375        DISTANCE =  5.69 ANGSTROMS                       
REMARK 525    HOH B 174        DISTANCE =  5.22 ANGSTROMS                       
REMARK 525    HOH C 174        DISTANCE =  5.92 ANGSTROMS                       
REMARK 525    HOH H 175        DISTANCE =  5.07 ANGSTROMS                       
REMARK 525    HOH B 176        DISTANCE =  7.44 ANGSTROMS                       
REMARK 525    HOH H 177        DISTANCE =  5.83 ANGSTROMS                       
REMARK 525    HOH E 179        DISTANCE =  6.15 ANGSTROMS                       
REMARK 525    HOH H 179        DISTANCE =  5.34 ANGSTROMS                       
REMARK 525    HOH D 180        DISTANCE =  5.90 ANGSTROMS                       
REMARK 525    HOH G 180        DISTANCE =  5.50 ANGSTROMS                       
REMARK 525    HOH F 383        DISTANCE =  7.45 ANGSTROMS                       
REMARK 525    HOH D 183        DISTANCE =  6.88 ANGSTROMS                       
REMARK 525    HOH C 184        DISTANCE =  5.54 ANGSTROMS                       
REMARK 525    HOH C 186        DISTANCE =  5.96 ANGSTROMS                       
REMARK 525    HOH G 188        DISTANCE =  7.23 ANGSTROMS                       
REMARK 525    HOH E 190        DISTANCE =  5.81 ANGSTROMS                       
REMARK 525    HOH H 191        DISTANCE =  7.37 ANGSTROMS                       
REMARK 525    HOH G 193        DISTANCE =  5.53 ANGSTROMS                       
REMARK 525    HOH H 193        DISTANCE =  6.11 ANGSTROMS                       
REMARK 525    HOH B 194        DISTANCE =  7.24 ANGSTROMS                       
REMARK 525    HOH D 195        DISTANCE =  5.09 ANGSTROMS                       
REMARK 525    HOH G 195        DISTANCE =  5.86 ANGSTROMS                       
REMARK 525    HOH A 196        DISTANCE =  6.04 ANGSTROMS                       
REMARK 525    HOH B 202        DISTANCE =  7.33 ANGSTROMS                       
REMARK 525    HOH B 208        DISTANCE =  5.31 ANGSTROMS                       
REMARK 525    HOH B 209        DISTANCE =  6.15 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU A 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  48   NE2                                                    
REMARK 620 2 HIS A  63   NE2 100.5                                              
REMARK 620 3 HIS A 120   NE2 108.1 151.2                                        
REMARK 620 4 HIS A  46   ND1 131.9  72.9  85.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  71   ND1                                                    
REMARK 620 2 ASP A  83   OD1  84.8                                              
REMARK 620 3 HIS A  63   ND1 105.0 116.8                                        
REMARK 620 4 HIS A  80   ND1 112.4 111.4 120.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU B 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  63   NE2                                                    
REMARK 620 2 HIS B 120   NE2 152.4                                              
REMARK 620 3 HIS B  48   NE2 102.0 102.3                                        
REMARK 620 4 HIS B  46   ND1  84.1  89.0 132.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  80   ND1                                                    
REMARK 620 2 ASP B  83   OD1 100.8                                              
REMARK 620 3 HIS B  63   ND1 109.7 106.0                                        
REMARK 620 4 HIS B  71   ND1 132.4 106.3  99.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU C 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  48   NE2                                                    
REMARK 620 2 HIS C 120   NE2 110.9                                              
REMARK 620 3 HIS C  46   ND1 142.6  94.7                                        
REMARK 620 4 HIS C  63   NE2  96.6 144.9  74.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  71   ND1                                                    
REMARK 620 2 ASP C  83   OD1  89.6                                              
REMARK 620 3 HIS C  80   ND1 111.0  98.4                                        
REMARK 620 4 HIS C  63   ND1 106.8 132.7 115.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU D 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D  46   ND1                                                    
REMARK 620 2 HIS D  48   NE2 142.6                                              
REMARK 620 3 HIS D  63   NE2  75.3  97.7                                        
REMARK 620 4 HIS D 120   NE2  95.4 105.4 151.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D  63   ND1                                                    
REMARK 620 2 HIS D  71   ND1 107.9                                              
REMARK 620 3 HIS D  80   ND1 112.4 116.4                                        
REMARK 620 4 ASP D  83   OD1 117.2  91.1 110.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU E 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS E  48   NE2                                                    
REMARK 620 2 HIS E  46   ND1 135.1                                              
REMARK 620 3 HIS E 120   NE2 105.6  92.2                                        
REMARK 620 4 HIS E  63   NE2  95.6  86.3 151.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN E 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS E  80   ND1                                                    
REMARK 620 2 HIS E  71   ND1 112.0                                              
REMARK 620 3 ASP E  83   OD2  76.3  68.6                                        
REMARK 620 4 HIS E  63   ND1 117.0 118.4 156.1                                  
REMARK 620 5 ASP E  83   OD1 101.3 102.9  54.7 101.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU F 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS F  48   NE2                                                    
REMARK 620 2 HIS F  63   NE2  89.8                                              
REMARK 620 3 HIS F 120   NE2 108.7 157.7                                        
REMARK 620 4 HIS F  46   ND1 132.0  83.2  92.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN F 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP F  83   OD1                                                    
REMARK 620 2 HIS F  71   ND1 103.1                                              
REMARK 620 3 HIS F  63   ND1 114.6 111.2                                        
REMARK 620 4 HIS F  80   ND1 101.9 112.9 112.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU G 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS G  48   NE2                                                    
REMARK 620 2 HIS G 120   NE2  99.4                                              
REMARK 620 3 HIS G  63   NE2  94.6 165.2                                        
REMARK 620 4 HIS G  46   ND1 132.7  96.1  77.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN G 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP G  83   OD1                                                    
REMARK 620 2 HIS G  63   ND1 102.8                                              
REMARK 620 3 ASP G  83   OD2  52.2 155.0                                        
REMARK 620 4 HIS G  80   ND1 107.3 109.4  81.3                                  
REMARK 620 5 HIS G  71   ND1 101.9 112.4  78.1 121.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU H 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS H  46   ND1                                                    
REMARK 620 2 HIS H  48   NE2 137.4                                              
REMARK 620 3 HIS H 120   NE2  93.1 105.8                                        
REMARK 620 4 HIS H  63   NE2  75.1  94.8 158.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN H 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS H  71   ND1                                                    
REMARK 620 2 HIS H  63   ND1 104.5                                              
REMARK 620 3 HIS H  80   ND1 119.9 106.9                                        
REMARK 620 4 ASP H  83   OD1 108.1 121.6  96.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU I 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS I 120   NE2                                                    
REMARK 620 2 HIS I  63   NE2 143.4                                              
REMARK 620 3 HIS I  46   ND1  81.8  78.5                                        
REMARK 620 4 HIS I  48   NE2 109.5 106.5 133.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN I 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS I  63   ND1                                                    
REMARK 620 2 HIS I  80   ND1 115.8                                              
REMARK 620 3 HIS I  71   ND1 103.4 129.3                                        
REMARK 620 4 ASP I  83   OD1 107.6  97.4 100.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU J 154  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS J  46   ND1                                                    
REMARK 620 2 HIS J  63   NE2  74.7                                              
REMARK 620 3 HIS J 120   NE2  87.1 143.2                                        
REMARK 620 4 HIS J  48   NE2 145.5 110.1 103.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN J 155  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP J  83   OD1                                                    
REMARK 620 2 HIS J  80   ND1 107.9                                              
REMARK 620 3 HIS J  71   ND1 101.8 103.3                                        
REMARK 620 4 HIS J  63   ND1 118.7 110.3 113.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 THE SHEETS PRESENTED ON SHEET RECORDS BELOW ARE ACTUALLY             
REMARK 700 EIGHT-STRANDED BETA-BARRELS.  EACH ONE IS REPRESENTED BY A           
REMARK 700 NINE-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE          
REMARK 700 IDENTICAL.                                                           
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: CUA                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800 SITE_IDENTIFIER: ZNA                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800 SITE_IDENTIFIER: CUF                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800 SITE_IDENTIFIER: ZNF                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800 SITE_IDENTIFIER: CUB                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800 SITE_IDENTIFIER: ZNB                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800 SITE_IDENTIFIER: CUG                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800 SITE_IDENTIFIER: ZNG                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800 SITE_IDENTIFIER: CUC                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800 SITE_IDENTIFIER: ZNC                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800 SITE_IDENTIFIER: CUH                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800 SITE_IDENTIFIER: ZNH                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800 SITE_IDENTIFIER: CUD                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800 SITE_IDENTIFIER: ZND                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800 SITE_IDENTIFIER: CUI                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800 SITE_IDENTIFIER: ZNI                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800 SITE_IDENTIFIER: CUE                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800 SITE_IDENTIFIER: ZNE                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800 SITE_IDENTIFIER: CUJ                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800 SITE_IDENTIFIER: ZNJ                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU A 154                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 155                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU F 154                  
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN F 155                  
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU B 154                  
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 155                  
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU G 154                  
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN G 155                  
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU C 154                  
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 155                  
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU H 154                  
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN H 155                  
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU D 154                  
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 155                  
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU I 154                  
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN I 155                  
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU E 154                  
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 155                  
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU J 154                  
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN J 155                  
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 F 356                 
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 I 357                 
DBREF  1SOS A    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  1SOS F    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  1SOS B    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  1SOS G    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  1SOS C    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  1SOS H    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  1SOS D    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  1SOS I    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  1SOS E    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  1SOS J    1   153  UNP    P00441   SODC_HUMAN       1    153             
SEQRES   1 A  154  ACE ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY          
SEQRES   2 A  154  PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER          
SEQRES   3 A  154  ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU          
SEQRES   4 A  154  THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY          
SEQRES   5 A  154  ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE          
SEQRES   6 A  154  ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU          
SEQRES   7 A  154  GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP          
SEQRES   8 A  154  LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL          
SEQRES   9 A  154  ILE SER LEU SER GLY ASP HIS SER ILE ILE GLY ARG THR          
SEQRES  10 A  154  LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY          
SEQRES  11 A  154  GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER          
SEQRES  12 A  154  ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                  
SEQRES   1 F  154  ACE ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY          
SEQRES   2 F  154  PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER          
SEQRES   3 F  154  ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU          
SEQRES   4 F  154  THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY          
SEQRES   5 F  154  ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE          
SEQRES   6 F  154  ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU          
SEQRES   7 F  154  GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP          
SEQRES   8 F  154  LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL          
SEQRES   9 F  154  ILE SER LEU SER GLY ASP HIS SER ILE ILE GLY ARG THR          
SEQRES  10 F  154  LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY          
SEQRES  11 F  154  GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER          
SEQRES  12 F  154  ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                  
SEQRES   1 B  154  ACE ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY          
SEQRES   2 B  154  PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER          
SEQRES   3 B  154  ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU          
SEQRES   4 B  154  THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY          
SEQRES   5 B  154  ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE          
SEQRES   6 B  154  ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU          
SEQRES   7 B  154  GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP          
SEQRES   8 B  154  LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL          
SEQRES   9 B  154  ILE SER LEU SER GLY ASP HIS SER ILE ILE GLY ARG THR          
SEQRES  10 B  154  LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY          
SEQRES  11 B  154  GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER          
SEQRES  12 B  154  ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                  
SEQRES   1 G  154  ACE ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY          
SEQRES   2 G  154  PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER          
SEQRES   3 G  154  ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU          
SEQRES   4 G  154  THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY          
SEQRES   5 G  154  ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE          
SEQRES   6 G  154  ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU          
SEQRES   7 G  154  GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP          
SEQRES   8 G  154  LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL          
SEQRES   9 G  154  ILE SER LEU SER GLY ASP HIS SER ILE ILE GLY ARG THR          
SEQRES  10 G  154  LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY          
SEQRES  11 G  154  GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER          
SEQRES  12 G  154  ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                  
SEQRES   1 C  154  ACE ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY          
SEQRES   2 C  154  PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER          
SEQRES   3 C  154  ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU          
SEQRES   4 C  154  THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY          
SEQRES   5 C  154  ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE          
SEQRES   6 C  154  ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU          
SEQRES   7 C  154  GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP          
SEQRES   8 C  154  LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL          
SEQRES   9 C  154  ILE SER LEU SER GLY ASP HIS SER ILE ILE GLY ARG THR          
SEQRES  10 C  154  LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY          
SEQRES  11 C  154  GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER          
SEQRES  12 C  154  ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                  
SEQRES   1 H  154  ACE ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY          
SEQRES   2 H  154  PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER          
SEQRES   3 H  154  ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU          
SEQRES   4 H  154  THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY          
SEQRES   5 H  154  ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE          
SEQRES   6 H  154  ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU          
SEQRES   7 H  154  GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP          
SEQRES   8 H  154  LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL          
SEQRES   9 H  154  ILE SER LEU SER GLY ASP HIS SER ILE ILE GLY ARG THR          
SEQRES  10 H  154  LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY          
SEQRES  11 H  154  GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER          
SEQRES  12 H  154  ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                  
SEQRES   1 D  154  ACE ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY          
SEQRES   2 D  154  PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER          
SEQRES   3 D  154  ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU          
SEQRES   4 D  154  THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY          
SEQRES   5 D  154  ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE          
SEQRES   6 D  154  ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU          
SEQRES   7 D  154  GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP          
SEQRES   8 D  154  LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL          
SEQRES   9 D  154  ILE SER LEU SER GLY ASP HIS SER ILE ILE GLY ARG THR          
SEQRES  10 D  154  LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY          
SEQRES  11 D  154  GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER          
SEQRES  12 D  154  ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                  
SEQRES   1 I  154  ACE ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY          
SEQRES   2 I  154  PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER          
SEQRES   3 I  154  ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU          
SEQRES   4 I  154  THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY          
SEQRES   5 I  154  ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE          
SEQRES   6 I  154  ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU          
SEQRES   7 I  154  GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP          
SEQRES   8 I  154  LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL          
SEQRES   9 I  154  ILE SER LEU SER GLY ASP HIS SER ILE ILE GLY ARG THR          
SEQRES  10 I  154  LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY          
SEQRES  11 I  154  GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER          
SEQRES  12 I  154  ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                  
SEQRES   1 E  154  ACE ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY          
SEQRES   2 E  154  PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER          
SEQRES   3 E  154  ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU          
SEQRES   4 E  154  THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY          
SEQRES   5 E  154  ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE          
SEQRES   6 E  154  ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU          
SEQRES   7 E  154  GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP          
SEQRES   8 E  154  LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL          
SEQRES   9 E  154  ILE SER LEU SER GLY ASP HIS SER ILE ILE GLY ARG THR          
SEQRES  10 E  154  LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY          
SEQRES  11 E  154  GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER          
SEQRES  12 E  154  ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                  
SEQRES   1 J  154  ACE ALA THR LYS ALA VAL ALA VAL LEU LYS GLY ASP GLY          
SEQRES   2 J  154  PRO VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER          
SEQRES   3 J  154  ASN GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU          
SEQRES   4 J  154  THR GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY          
SEQRES   5 J  154  ASP ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE          
SEQRES   6 J  154  ASN PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU          
SEQRES   7 J  154  GLU ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP          
SEQRES   8 J  154  LYS ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL          
SEQRES   9 J  154  ILE SER LEU SER GLY ASP HIS SER ILE ILE GLY ARG THR          
SEQRES  10 J  154  LEU VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY          
SEQRES  11 J  154  GLY ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER          
SEQRES  12 J  154  ARG LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                  
HET    ACE  A   0       3                                                       
HET    ACE  F   0       3                                                       
HET    ACE  B   0       3                                                       
HET    ACE  G   0       3                                                       
HET    ACE  C   0       3                                                       
HET    ACE  H   0       3                                                       
HET    ACE  D   0       3                                                       
HET    ACE  I   0       3                                                       
HET    ACE  E   0       3                                                       
HET    ACE  J   0       3                                                       
HET     CU  A 154       1                                                       
HET     ZN  A 155       1                                                       
HET     CU  F 154       1                                                       
HET     ZN  F 155       1                                                       
HET     CU  B 154       1                                                       
HET     ZN  B 155       1                                                       
HET     CU  G 154       1                                                       
HET     ZN  G 155       1                                                       
HET     CU  C 154       1                                                       
HET     ZN  C 155       1                                                       
HET     CU  H 154       1                                                       
HET     ZN  H 155       1                                                       
HET     CU  D 154       1                                                       
HET     ZN  D 155       1                                                       
HET     CU  I 154       1                                                       
HET     ZN  I 155       1                                                       
HET     CU  E 154       1                                                       
HET     ZN  E 155       1                                                       
HET     CU  J 154       1                                                       
HET     ZN  J 155       1                                                       
HET    SO4  F 356       5                                                       
HET    SO4  I 357       5                                                       
HETNAM     ACE ACETYL GROUP                                                     
HETNAM      CU COPPER (II) ION                                                  
HETNAM      ZN ZINC ION                                                         
HETNAM     SO4 SULFATE ION                                                      
FORMUL   1  ACE    10(C2 H4 O)                                                  
FORMUL  11   CU    10(CU 2+)                                                    
FORMUL  12   ZN    10(ZN 2+)                                                    
FORMUL  31  SO4    2(O4 S 2-)                                                   
FORMUL  33  HOH   *499(H2 O)                                                    
HELIX    1  HA GLU A  133  THR A  137  1SINGLE-LOOP ALPHA-HELIX            5    
HELIX    2  HF GLU F  133  THR F  137  1SINGLE-LOOP ALPHA-HELIX            5    
HELIX    3  HB GLU B  133  THR B  137  1SINGLE-LOOP ALPHA-HELIX            5    
HELIX    4  HG GLU G  133  THR G  137  1SINGLE-LOOP ALPHA-HELIX            5    
HELIX    5  HC GLU C  133  THR C  137  1SINGLE-LOOP ALPHA-HELIX            5    
HELIX    6  HH GLU H  133  THR H  137  1SINGLE-LOOP ALPHA-HELIX            5    
HELIX    7  HD GLU D  133  THR D  137  1SINGLE-LOOP ALPHA-HELIX            5    
HELIX    8  HI GLU I  133  THR I  137  1SINGLE-LOOP ALPHA-HELIX            5    
HELIX    9  HE GLU E  133  THR E  137  1SINGLE-LOOP ALPHA-HELIX            5    
HELIX   10  HJ GLU J  133  THR J  137  1SINGLE-LOOP ALPHA-HELIX            5    
SHEET    1  SA 9 ALA A   4  LYS A   9  0                                        
SHEET    2  SA 9 GLN A  15  GLU A  21 -1  N  PHE A  20   O  ALA A   4           
SHEET    3  SA 9 VAL A  29  LYS A  30  1  N  LYS A  30   O  GLU A  21           
SHEET    4  SA 9 VAL A  94  ASP A 101 -1  N  ILE A  99   O  VAL A  31           
SHEET    5  SA 9 GLY A  85  ALA A  89  1                                        
SHEET    6  SA 9 GLY A  41  HIS A  48 -1  N  HIS A  43   O  VAL A  87           
SHEET    7  SA 9 ARG A 115  HIS A 120  1  N  VAL A 118   O  HIS A  46           
SHEET    8  SA 9 CYS A 146  GLY A 150 -1  N  GLY A 147   O  LEU A 117           
SHEET    9  SA 9 ALA A   4  LYS A   9 -1  N  VAL A   7   O  VAL A 148           
SHEET    1  SF 9 ALA F   4  LYS F   9  0                                        
SHEET    2  SF 9 GLN F  15  GLU F  21 -1  N  PHE F  20   O  ALA F   4           
SHEET    3  SF 9 VAL F  29  LYS F  30  1  N  LYS F  30   O  GLU F  21           
SHEET    4  SF 9 VAL F  94  ASP F 101 -1  N  ILE F  99   O  VAL F  31           
SHEET    5  SF 9 GLY F  85  ALA F  89  1                                        
SHEET    6  SF 9 GLY F  41  HIS F  48 -1  N  HIS F  43   O  VAL F  87           
SHEET    7  SF 9 ARG F 115  HIS F 120  1  N  VAL F 118   O  HIS F  46           
SHEET    8  SF 9 CYS F 146  GLY F 150 -1  N  GLY F 147   O  LEU F 117           
SHEET    9  SF 9 ALA F   4  LYS F   9 -1  N  VAL F   7   O  VAL F 148           
SHEET    1  SB 9 ALA B   4  LYS B   9  0                                        
SHEET    2  SB 9 GLN B  15  GLU B  21 -1  N  PHE B  20   O  ALA B   4           
SHEET    3  SB 9 VAL B  29  LYS B  30  1  N  LYS B  30   O  GLU B  21           
SHEET    4  SB 9 VAL B  94  ASP B 101 -1  N  ILE B  99   O  VAL B  31           
SHEET    5  SB 9 GLY B  85  ALA B  89  1                                        
SHEET    6  SB 9 GLY B  41  HIS B  48 -1  N  HIS B  43   O  VAL B  87           
SHEET    7  SB 9 ARG B 115  HIS B 120  1  N  VAL B 118   O  HIS B  46           
SHEET    8  SB 9 CYS B 146  GLY B 150 -1  N  GLY B 147   O  LEU B 117           
SHEET    9  SB 9 ALA B   4  LYS B   9 -1  N  VAL B   7   O  VAL B 148           
SHEET    1  SG 9 ALA G   4  LYS G   9  0                                        
SHEET    2  SG 9 GLN G  15  GLU G  21 -1  N  PHE G  20   O  ALA G   4           
SHEET    3  SG 9 VAL G  29  LYS G  30  1  N  LYS G  30   O  GLU G  21           
SHEET    4  SG 9 VAL G  94  ASP G 101 -1  N  ILE G  99   O  VAL G  31           
SHEET    5  SG 9 GLY G  85  ALA G  89  1                                        
SHEET    6  SG 9 GLY G  41  HIS G  48 -1  N  HIS G  43   O  VAL G  87           
SHEET    7  SG 9 ARG G 115  HIS G 120  1  N  VAL G 118   O  HIS G  46           
SHEET    8  SG 9 CYS G 146  GLY G 150 -1  N  GLY G 147   O  LEU G 117           
SHEET    9  SG 9 ALA G   4  LYS G   9 -1  N  VAL G   7   O  VAL G 148           
SHEET    1  SC 9 ALA C   4  LYS C   9  0                                        
SHEET    2  SC 9 GLN C  15  GLU C  21 -1  N  PHE C  20   O  ALA C   4           
SHEET    3  SC 9 VAL C  29  LYS C  30  1  N  LYS C  30   O  GLU C  21           
SHEET    4  SC 9 VAL C  94  ASP C 101 -1  N  ILE C  99   O  VAL C  31           
SHEET    5  SC 9 GLY C  85  ALA C  89  1                                        
SHEET    6  SC 9 GLY C  41  HIS C  48 -1  N  HIS C  43   O  VAL C  87           
SHEET    7  SC 9 ARG C 115  HIS C 120  1  N  VAL C 118   O  HIS C  46           
SHEET    8  SC 9 CYS C 146  GLY C 150 -1  N  GLY C 147   O  LEU C 117           
SHEET    9  SC 9 ALA C   4  LYS C   9 -1  N  VAL C   7   O  VAL C 148           
SHEET    1  SH 9 ALA H   4  LYS H   9  0                                        
SHEET    2  SH 9 GLN H  15  GLU H  21 -1  N  PHE H  20   O  ALA H   4           
SHEET    3  SH 9 VAL H  29  LYS H  30  1  N  LYS H  30   O  GLU H  21           
SHEET    4  SH 9 VAL H  94  ASP H 101 -1  N  ILE H  99   O  VAL H  31           
SHEET    5  SH 9 GLY H  85  ALA H  89  1                                        
SHEET    6  SH 9 GLY H  41  HIS H  48 -1  N  HIS H  43   O  VAL H  87           
SHEET    7  SH 9 ARG H 115  HIS H 120  1  N  VAL H 118   O  HIS H  46           
SHEET    8  SH 9 CYS H 146  GLY H 150 -1  N  GLY H 147   O  LEU H 117           
SHEET    9  SH 9 ALA H   4  LYS H   9 -1  N  VAL H   7   O  VAL H 148           
SHEET    1  SD 9 ALA D   4  LYS D   9  0                                        
SHEET    2  SD 9 GLN D  15  GLU D  21 -1  N  PHE D  20   O  ALA D   4           
SHEET    3  SD 9 VAL D  29  LYS D  30  1  N  LYS D  30   O  GLU D  21           
SHEET    4  SD 9 VAL D  94  ASP D 101 -1  N  ILE D  99   O  VAL D  31           
SHEET    5  SD 9 GLY D  85  ALA D  89  1                                        
SHEET    6  SD 9 GLY D  41  HIS D  48 -1  N  HIS D  43   O  VAL D  87           
SHEET    7  SD 9 ARG D 115  HIS D 120  1  N  VAL D 118   O  HIS D  46           
SHEET    8  SD 9 CYS D 146  GLY D 150 -1  N  GLY D 147   O  LEU D 117           
SHEET    9  SD 9 ALA D   4  LYS D   9 -1  N  VAL D   7   O  VAL D 148           
SHEET    1  SI 9 ALA I   4  LYS I   9  0                                        
SHEET    2  SI 9 GLN I  15  GLU I  21 -1  N  PHE I  20   O  ALA I   4           
SHEET    3  SI 9 VAL I  29  LYS I  30  1  N  LYS I  30   O  GLU I  21           
SHEET    4  SI 9 VAL I  94  ASP I 101 -1  N  ILE I  99   O  VAL I  31           
SHEET    5  SI 9 GLY I  85  ALA I  89  1                                        
SHEET    6  SI 9 GLY I  41  HIS I  48 -1  N  HIS I  43   O  VAL I  87           
SHEET    7  SI 9 ARG I 115  HIS I 120  1  N  VAL I 118   O  HIS I  46           
SHEET    8  SI 9 CYS I 146  GLY I 150 -1  N  GLY I 147   O  LEU I 117           
SHEET    9  SI 9 ALA I   4  LYS I   9 -1  N  VAL I   7   O  VAL I 148           
SHEET    1  SE 9 ALA E   4  LYS E   9  0                                        
SHEET    2  SE 9 GLN E  15  GLU E  21 -1  N  PHE E  20   O  ALA E   4           
SHEET    3  SE 9 VAL E  29  LYS E  30  1  N  LYS E  30   O  GLU E  21           
SHEET    4  SE 9 VAL E  94  ASP E 101 -1  N  ILE E  99   O  VAL E  31           
SHEET    5  SE 9 GLY E  85  ALA E  89  1                                        
SHEET    6  SE 9 GLY E  41  HIS E  48 -1  N  HIS E  43   O  VAL E  87           
SHEET    7  SE 9 ARG E 115  HIS E 120  1  N  VAL E 118   O  HIS E  46           
SHEET    8  SE 9 CYS E 146  GLY E 150 -1  N  GLY E 147   O  LEU E 117           
SHEET    9  SE 9 ALA E   4  LYS E   9 -1  N  VAL E   7   O  VAL E 148           
SHEET    1  SJ 9 ALA J   4  LYS J   9  0                                        
SHEET    2  SJ 9 GLN J  15  GLU J  21 -1  N  PHE J  20   O  ALA J   4           
SHEET    3  SJ 9 VAL J  29  LYS J  30  1  N  LYS J  30   O  GLU J  21           
SHEET    4  SJ 9 VAL J  94  ASP J 101 -1  N  ILE J  99   O  VAL J  31           
SHEET    5  SJ 9 GLY J  85  ALA J  89  1                                        
SHEET    6  SJ 9 GLY J  41  HIS J  48 -1  N  HIS J  43   O  VAL J  87           
SHEET    7  SJ 9 ARG J 115  HIS J 120  1  N  VAL J 118   O  HIS J  46           
SHEET    8  SJ 9 CYS J 146  GLY J 150 -1  N  GLY J 147   O  LEU J 117           
SHEET    9  SJ 9 ALA J   4  LYS J   9 -1  N  VAL J   7   O  VAL J 148           
SSBOND   1 CYS A   57    CYS A  146                          1555   1555  2.01  
SSBOND   2 CYS F   57    CYS F  146                          1555   1555  2.02  
SSBOND   3 CYS B   57    CYS B  146                          1555   1555  2.03  
SSBOND   4 CYS G   57    CYS G  146                          1555   1555  2.02  
SSBOND   5 CYS C   57    CYS C  146                          1555   1555  2.00  
SSBOND   6 CYS H   57    CYS H  146                          1555   1555  2.00  
SSBOND   7 CYS D   57    CYS D  146                          1555   1555  2.00  
SSBOND   8 CYS I   57    CYS I  146                          1555   1555  2.02  
SSBOND   9 CYS E   57    CYS E  146                          1555   1555  2.03  
SSBOND  10 CYS J   57    CYS J  146                          1555   1555  2.02  
LINK         C   ACE A   0                 N   ALA A   1     1555   1555  1.34  
LINK         C   ACE F   0                 N   ALA F   1     1555   1555  1.36  
LINK         C   ACE B   0                 N   ALA B   1     1555   1555  1.34  
LINK         C   ACE G   0                 N   ALA G   1     1555   1555  1.34  
LINK         C   ACE C   0                 N   ALA C   1     1555   1555  1.35  
LINK         C   ACE H   0                 N   ALA H   1     1555   1555  1.34  
LINK         C   ACE D   0                 N   ALA D   1     1555   1555  1.36  
LINK         C   ACE I   0                 N   ALA I   1     1555   1555  1.35  
LINK         C   ACE E   0                 N   ALA E   1     1555   1555  1.34  
LINK         C   ACE J   0                 N   ALA J   1     1555   1555  1.34  
LINK        CU    CU A 154                 NE2 HIS A  48     1555   1555  2.06  
LINK        CU    CU A 154                 NE2 HIS A  63     1555   1555  2.12  
LINK        CU    CU A 154                 NE2 HIS A 120     1555   1555  2.07  
LINK        CU    CU A 154                 ND1 HIS A  46     1555   1555  2.07  
LINK        ZN    ZN A 155                 ND1 HIS A  71     1555   1555  2.06  
LINK        ZN    ZN A 155                 OD1 ASP A  83     1555   1555  1.92  
LINK        ZN    ZN A 155                 ND1 HIS A  63     1555   1555  2.10  
LINK        ZN    ZN A 155                 ND1 HIS A  80     1555   1555  2.04  
LINK        CU    CU B 154                 NE2 HIS B  63     1555   1555  2.12  
LINK        CU    CU B 154                 NE2 HIS B 120     1555   1555  2.04  
LINK        CU    CU B 154                 NE2 HIS B  48     1555   1555  2.08  
LINK        CU    CU B 154                 ND1 HIS B  46     1555   1555  2.03  
LINK        ZN    ZN B 155                 ND1 HIS B  80     1555   1555  2.06  
LINK        ZN    ZN B 155                 OD1 ASP B  83     1555   1555  1.97  
LINK        ZN    ZN B 155                 ND1 HIS B  63     1555   1555  2.12  
LINK        ZN    ZN B 155                 ND1 HIS B  71     1555   1555  2.08  
LINK        CU    CU C 154                 NE2 HIS C  48     1555   1555  2.09  
LINK        CU    CU C 154                 NE2 HIS C 120     1555   1555  2.04  
LINK        CU    CU C 154                 ND1 HIS C  46     1555   1555  2.07  
LINK        CU    CU C 154                 NE2 HIS C  63     1555   1555  2.08  
LINK        ZN    ZN C 155                 ND1 HIS C  71     1555   1555  2.06  
LINK        ZN    ZN C 155                 OD1 ASP C  83     1555   1555  1.94  
LINK        ZN    ZN C 155                 ND1 HIS C  80     1555   1555  2.05  
LINK        ZN    ZN C 155                 ND1 HIS C  63     1555   1555  2.08  
LINK        CU    CU D 154                 ND1 HIS D  46     1555   1555  2.04  
LINK        CU    CU D 154                 NE2 HIS D  48     1555   1555  2.09  
LINK        CU    CU D 154                 NE2 HIS D  63     1555   1555  2.11  
LINK        CU    CU D 154                 NE2 HIS D 120     1555   1555  2.05  
LINK        ZN    ZN D 155                 ND1 HIS D  63     1555   1555  2.13  
LINK        ZN    ZN D 155                 ND1 HIS D  71     1555   1555  2.08  
LINK        ZN    ZN D 155                 ND1 HIS D  80     1555   1555  2.09  
LINK        ZN    ZN D 155                 OD1 ASP D  83     1555   1555  1.96  
LINK        CU    CU E 154                 NE2 HIS E  48     1555   1555  2.08  
LINK        CU    CU E 154                 ND1 HIS E  46     1555   1555  2.04  
LINK        CU    CU E 154                 NE2 HIS E 120     1555   1555  2.05  
LINK        CU    CU E 154                 NE2 HIS E  63     1555   1555  2.12  
LINK        ZN    ZN E 155                 ND1 HIS E  80     1555   1555  2.08  
LINK        ZN    ZN E 155                 ND1 HIS E  71     1555   1555  2.10  
LINK        ZN    ZN E 155                 OD2 ASP E  83     1555   1555  2.51  
LINK        ZN    ZN E 155                 ND1 HIS E  63     1555   1555  2.12  
LINK        ZN    ZN E 155                 OD1 ASP E  83     1555   1555  1.96  
LINK        CU    CU F 154                 NE2 HIS F  48     1555   1555  2.09  
LINK        CU    CU F 154                 NE2 HIS F  63     1555   1555  2.12  
LINK        CU    CU F 154                 NE2 HIS F 120     1555   1555  2.06  
LINK        CU    CU F 154                 ND1 HIS F  46     1555   1555  2.03  
LINK        ZN    ZN F 155                 OD1 ASP F  83     1555   1555  1.95  
LINK        ZN    ZN F 155                 ND1 HIS F  71     1555   1555  2.05  
LINK        ZN    ZN F 155                 ND1 HIS F  63     1555   1555  2.09  
LINK        ZN    ZN F 155                 ND1 HIS F  80     1555   1555  2.06  
LINK        CU    CU G 154                 NE2 HIS G  48     1555   1555  2.08  
LINK        CU    CU G 154                 NE2 HIS G 120     1555   1555  2.06  
LINK        CU    CU G 154                 NE2 HIS G  63     1555   1555  2.07  
LINK        CU    CU G 154                 ND1 HIS G  46     1555   1555  2.05  
LINK        ZN    ZN G 155                 OD1 ASP G  83     1555   1555  1.95  
LINK        ZN    ZN G 155                 ND1 HIS G  63     1555   1555  2.07  
LINK        ZN    ZN G 155                 OD2 ASP G  83     1555   1555  2.69  
LINK        ZN    ZN G 155                 ND1 HIS G  80     1555   1555  2.05  
LINK        ZN    ZN G 155                 ND1 HIS G  71     1555   1555  2.07  
LINK        CU    CU H 154                 ND1 HIS H  46     1555   1555  2.04  
LINK        CU    CU H 154                 NE2 HIS H  48     1555   1555  2.08  
LINK        CU    CU H 154                 NE2 HIS H 120     1555   1555  2.05  
LINK        CU    CU H 154                 NE2 HIS H  63     1555   1555  2.09  
LINK        ZN    ZN H 155                 ND1 HIS H  71     1555   1555  2.05  
LINK        ZN    ZN H 155                 ND1 HIS H  63     1555   1555  2.11  
LINK        ZN    ZN H 155                 ND1 HIS H  80     1555   1555  2.09  
LINK        ZN    ZN H 155                 OD1 ASP H  83     1555   1555  1.92  
LINK        CU    CU I 154                 NE2 HIS I 120     1555   1555  2.05  
LINK        CU    CU I 154                 NE2 HIS I  63     1555   1555  2.12  
LINK        CU    CU I 154                 ND1 HIS I  46     1555   1555  2.03  
LINK        CU    CU I 154                 NE2 HIS I  48     1555   1555  2.06  
LINK        ZN    ZN I 155                 ND1 HIS I  63     1555   1555  2.11  
LINK        ZN    ZN I 155                 ND1 HIS I  80     1555   1555  2.04  
LINK        ZN    ZN I 155                 ND1 HIS I  71     1555   1555  2.05  
LINK        ZN    ZN I 155                 OD1 ASP I  83     1555   1555  1.95  
LINK        CU    CU J 154                 ND1 HIS J  46     1555   1555  2.04  
LINK        CU    CU J 154                 NE2 HIS J  63     1555   1555  2.09  
LINK        CU    CU J 154                 NE2 HIS J 120     1555   1555  2.07  
LINK        CU    CU J 154                 NE2 HIS J  48     1555   1555  2.07  
LINK        ZN    ZN J 155                 OD1 ASP J  83     1555   1555  1.93  
LINK        ZN    ZN J 155                 ND1 HIS J  80     1555   1555  2.06  
LINK        ZN    ZN J 155                 ND1 HIS J  71     1555   1555  2.07  
LINK        ZN    ZN J 155                 ND1 HIS J  63     1555   1555  2.08  
SITE     1 CUA  4 HIS A  46  HIS A  48  HIS A  63  HIS A 120                    
SITE     1 ZNA  4 HIS A  63  HIS A  71  HIS A  80  ASP A  83                    
SITE     1 CUF  4 HIS F  46  HIS F  48  HIS F  63  HIS F 120                    
SITE     1 ZNF  4 HIS F  63  HIS F  71  HIS F  80  ASP F  83                    
SITE     1 CUB  4 HIS B  46  HIS B  48  HIS B  63  HIS B 120                    
SITE     1 ZNB  4 HIS B  63  HIS B  71  HIS B  80  ASP B  83                    
SITE     1 CUG  4 HIS G  46  HIS G  48  HIS G  63  HIS G 120                    
SITE     1 ZNG  4 HIS G  63  HIS G  71  HIS G  80  ASP G  83                    
SITE     1 CUC  4 HIS C  46  HIS C  48  HIS C  63  HIS C 120                    
SITE     1 ZNC  4 HIS C  63  HIS C  71  HIS C  80  ASP C  83                    
SITE     1 CUH  4 HIS H  46  HIS H  48  HIS H  63  HIS H 120                    
SITE     1 ZNH  4 HIS H  63  HIS H  71  HIS H  80  ASP H  83                    
SITE     1 CUD  4 HIS D  46  HIS D  48  HIS D  63  HIS D 120                    
SITE     1 ZND  4 HIS D  63  HIS D  71  HIS D  80  ASP D  83                    
SITE     1 CUI  4 HIS I  46  HIS I  48  HIS I  63  HIS I 120                    
SITE     1 ZNI  4 HIS I  63  HIS I  71  HIS I  80  ASP I  83                    
SITE     1 CUE  4 HIS E  46  HIS E  48  HIS E  63  HIS E 120                    
SITE     1 ZNE  4 HIS E  63  HIS E  71  HIS E  80  ASP E  83                    
SITE     1 CUJ  4 HIS J  46  HIS J  48  HIS J  63  HIS J 120                    
SITE     1 ZNJ  4 HIS J  63  HIS J  71  HIS J  80  ASP J  83                    
SITE     1 AC1  4 HIS A  46  HIS A  48  HIS A  63  HIS A 120                    
SITE     1 AC2  4 HIS A  63  HIS A  71  HIS A  80  ASP A  83                    
SITE     1 AC3  4 HIS F  46  HIS F  48  HIS F  63  HIS F 120                    
SITE     1 AC4  4 HIS F  63  HIS F  71  HIS F  80  ASP F  83                    
SITE     1 AC5  4 HIS B  46  HIS B  48  HIS B  63  HIS B 120                    
SITE     1 AC6  4 HIS B  63  HIS B  71  HIS B  80  ASP B  83                    
SITE     1 AC7  4 HIS G  46  HIS G  48  HIS G  63  HIS G 120                    
SITE     1 AC8  4 HIS G  63  HIS G  71  HIS G  80  ASP G  83                    
SITE     1 AC9  4 HIS C  46  HIS C  48  HIS C  63  HIS C 120                    
SITE     1 BC1  4 HIS C  63  HIS C  71  HIS C  80  ASP C  83                    
SITE     1 BC2  4 HIS H  46  HIS H  48  HIS H  63  HIS H 120                    
SITE     1 BC3  4 HIS H  63  HIS H  71  HIS H  80  ASP H  83                    
SITE     1 BC4  4 HIS D  46  HIS D  48  HIS D  63  HIS D 120                    
SITE     1 BC5  4 HIS D  63  HIS D  71  HIS D  80  ASP D  83                    
SITE     1 BC6  4 HIS I  46  HIS I  48  HIS I  63  HIS I 120                    
SITE     1 BC7  4 HIS I  63  HIS I  71  HIS I  80  ASP I  83                    
SITE     1 BC8  4 HIS E  46  HIS E  48  HIS E  63  HIS E 120                    
SITE     1 BC9  5 HIS E  63  HIS E  71  HIS E  80  ASP E  83                    
SITE     2 BC9  5 LYS E 136                                                     
SITE     1 CC1  4 HIS J  46  HIS J  48  HIS J  63  HIS J 120                    
SITE     1 CC2  4 HIS J  63  HIS J  71  HIS J  80  ASP J  83                    
SITE     1 CC3  3 LYS F  75  LYS F 128  LYS G 128                               
SITE     1 CC4  5 LYS C 128  LYS I  75  LYS I 128  HOH I 358                    
SITE     2 CC4  5 LYS J 128                                                     
CRYST1  205.200  167.000  145.500  90.00  90.00  90.00 C 2 2 21     80          
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      0.004873  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005988  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006873        0.00000                         
MTRIX1   1 -0.982700  0.008000  0.185000      120.63000    1                    
MTRIX2   1  0.018200 -0.990100  0.139400       56.45800    1                    
MTRIX3   1  0.184300  0.140300  0.972800      -15.30400    1                    
MTRIX1   2 -0.463700 -0.885800  0.015100      106.40600    1                    
MTRIX2   2  0.886000 -0.463700  0.008200      -66.09600    1                    
MTRIX3   2 -0.000200  0.017200  0.999900        0.01700    1                    
MTRIX1   3  0.467000  0.867400  0.171900       15.10400    1                    
MTRIX2   3 -0.883700  0.450900  0.125700      123.62500    1                    
MTRIX3   3  0.031500 -0.210600  0.977100       -4.28600    1                    
MTRIX1   4 -0.534900  0.842700  0.060800      111.29400    1                    
MTRIX2   4 -0.844400 -0.535700 -0.003200       61.00000    1                    
MTRIX3   4  0.029900 -0.053000  0.998100       -3.26200    1                    
MTRIX1   5  0.522700 -0.838500  0.154100       10.87600    1                    
MTRIX2   5  0.832900  0.540800  0.117600       -2.13100    1                    
MTRIX3   5 -0.181900  0.066900  0.981000       11.15100    1                    
MTRIX1   6 -0.981000 -0.026900 -0.192300      208.83600    1                    
MTRIX2   6  0.028200 -0.999600 -0.004000       28.44200    1                    
MTRIX3   6 -0.192200 -0.009400  0.981300       29.48700    1                    
MTRIX1   7  0.936100  0.007600  0.351500      -79.86000    1                    
MTRIX2   7 -0.056900  0.989900  0.130100       33.91200    1                    
MTRIX3   7 -0.347000 -0.141900  0.927100       53.15700    1                    
MTRIX1   8  0.476600  0.879000  0.010300      -19.71400    1                    
MTRIX2   8 -0.877900  0.476600 -0.046600      102.41300    1                    
MTRIX3   8 -0.045800  0.013200  0.998900        9.15900    1                    
MTRIX1   9 -0.475300 -0.865900  0.155600      142.20700    1                    
MTRIX2   9  0.876000 -0.449400  0.175200      -44.74400    1                    
MTRIX3   9 -0.081800  0.219600  0.972200        5.36500    1                    
HETATM    1  C   ACE A   0      53.275  28.140   5.578  1.00 34.09           C  
HETATM    2  O   ACE A   0      52.151  27.619   5.540  1.00 34.04           O  
HETATM    3  CH3 ACE A   0      54.133  28.277   4.327  1.00 33.82           C  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system