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Database: PDB
Entry: 1PU0
LinkDB: 1PU0
Original site: 1PU0 
HEADER    OXIDOREDUCTASE                          23-JUN-03   1PU0              
TITLE     STRUCTURE OF HUMAN CU,ZN SUPEROXIDE DISMUTASE                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [CU-ZN];                              
COMPND   3 CHAIN: A, B, C, D, E, F, G, H, I, 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;                                                
SOURCE   5 GENE: SOD1;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    ALS, FALS, LOU GEHRIG'S DISEASE, OXIDOREDUCTASE                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.DIDONATO,L.CRAIG,M.E.HUFF,M.M.THAYER,R.M.F.CARDOSO,                 
AUTHOR   2 C.J.KASSMANN,T.P.LO,C.K.BRUNS,E.T.POWERS,J.W.KELLY,                  
AUTHOR   3 E.D.GETZOFF,J.A.TAINER                                               
REVDAT   2   24-FEB-09 1PU0    1       VERSN                                    
REVDAT   1   09-SEP-03 1PU0    0                                                
JRNL        AUTH   M.DIDONATO,L.CRAIG,M.E.HUFF,M.M.THAYER,                      
JRNL        AUTH 2 R.M.F.CARDOSO,C.J.KASSMANN,T.P.LO,C.K.BRUNS,                 
JRNL        AUTH 3 E.T.POWERS,J.W.KELLY,E.D.GETZOFF,J.A.TAINER                  
JRNL        TITL   ALS MUTANTS OF HUMAN SUPEROXIDE DISMUTASE FORM               
JRNL        TITL 2 FIBROUS AGGREGATES VIA FRAMEWORK DESTABILIZATION             
JRNL        REF    J.MOL.BIOL.                   V. 332   601 2003              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   12963370                                                     
JRNL        DOI    10.1016/S0022-2836(03)00889-1                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : SHELXL-97                                            
REMARK   3   AUTHORS     : G.M.SHELDRICK                                        
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.6                           
REMARK   3   CROSS-VALIDATION METHOD           : FREE R                         
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).                         
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.211                  
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.210                  
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.243                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5.300                  
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 13096                  
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 262366                 
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).                     
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : 0.202                  
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : 0.202                  
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : 0.233                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5.300                  
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : 11627                  
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 221399                 
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS      : 11140                                         
REMARK   3   NUCLEIC ACID ATOMS : 0                                             
REMARK   3   HETEROGEN ATOMS    : 35                                            
REMARK   3   SOLVENT ATOMS      : 1047                                          
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 12181.50                
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 0.00                    
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 20                      
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 49294                   
REMARK   3   NUMBER OF RESTRAINTS                     : 45691                   
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : 0.020                   
REMARK   3   ANGLE DISTANCES                      (A) : 0.025                   
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000                   
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.029                   
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.041                   
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.053                   
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.014                   
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.003                   
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.084                   
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.000                   
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED: NULL                                                  
REMARK   3                                                                      
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER                        
REMARK   3   SPECIAL CASE: NULL                                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1PU0 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-JUN-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB019562.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-MAR-99                          
REMARK 200  TEMPERATURE           (KELVIN) : 96                                 
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRL                               
REMARK 200  BEAMLINE                       : BL7-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.08                               
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MAR                                
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 262366                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.06100                            
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) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.76                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.32000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: 1SOS                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 67.96                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.28                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULPHATE, SODIUM CHLORIDE,      
REMARK 280  PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K             
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       72.07500            
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       72.07500            
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      101.79000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       82.84000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000      101.79000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       82.84000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       72.07500            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000      101.79000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       82.84000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       72.07500            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000      101.79000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       82.84000            
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A HOMODIMER. THE ASYMMETRIC       
REMARK 300 UNIT CONTAIN 5 HOMODIMERS.                                           
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: 1430 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13730 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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: 1560 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13920 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1390 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13700 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, 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: 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: 1540 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13800 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, 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: 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: 1540 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13660 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, 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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH D1252  LIES ON A SPECIAL POSITION.                          
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG B 115   NE  -  CZ  -  NH2 ANGL. DEV. =   5.0 DEGREES          
REMARK 500    ARG D 115   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ARG D 115   NE  -  CZ  -  NH2 ANGL. DEV. =   3.7 DEGREES          
REMARK 500    ASP D 125   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ARG E 115   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500    ARG E 115   NE  -  CZ  -  NH2 ANGL. DEV. =   4.2 DEGREES          
REMARK 500    ARG H  79   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.1 DEGREES          
REMARK 500    ARG H  79   NE  -  CZ  -  NH2 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    ARG H 143   NE  -  CZ  -  NH2 ANGL. DEV. =   3.6 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER B  25      -65.22    -12.70                                   
REMARK 500    SER C  68       54.69     35.01                                   
REMARK 500    ARG C  69     -142.04    -99.94                                   
REMARK 500    LYS C 128       51.73   -105.53                                   
REMARK 500    ALA D  55       53.26   -119.22                                   
REMARK 500    SER G  25      -63.84    -14.18                                   
REMARK 500    SER G  98       84.12   -152.82                                   
REMARK 500    GLU G 132      -27.30    -39.00                                   
REMARK 500    LYS I 136      -64.67    -90.98                                   
REMARK 500    ARG J 115     -169.98   -102.20                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 201  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  83   OD1                                                    
REMARK 620 2 HIS A  63   ND1 103.3                                              
REMARK 620 3 HIS A  71   ND1  96.0 102.0                                        
REMARK 620 4 HIS A  80   ND1 120.2 109.1 123.3                                  
REMARK 620 5 ASP A  83   OD2  52.3 155.0  78.4  90.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CU1 A 200  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  46   ND1                                                    
REMARK 620 2 HIS A  48   NE2 135.1                                              
REMARK 620 3 HIS A 120   NE2 104.3 120.2                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 201  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B  83   OD1                                                    
REMARK 620 2 HIS B  63   ND1 105.8                                              
REMARK 620 3 HIS B  71   ND1 102.1 106.4                                        
REMARK 620 4 HIS B  80   ND1 112.4 108.2 120.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CU1 B 200  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  46   ND1                                                    
REMARK 620 2 HIS B  48   NE2 137.4                                              
REMARK 620 3 HIS B 120   NE2  98.5 124.0                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 201  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP C  83   OD1                                                    
REMARK 620 2 HIS C  63   ND1  90.7                                              
REMARK 620 3 HIS C  71   ND1  95.5 103.9                                        
REMARK 620 4 HIS C  80   ND1 117.5 116.4 125.8                                  
REMARK 620 5 ASP C  83   OD2  54.6 143.7  72.8  92.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CU1 C 200  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  46   ND1                                                    
REMARK 620 2 HIS C  48   NE2 141.6                                              
REMARK 620 3 HIS C 120   NE2  99.5 118.8                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D 201  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D  83   OD1                                                    
REMARK 620 2 HIS D  63   ND1 104.6                                              
REMARK 620 3 HIS D  71   ND1  99.5 106.0                                        
REMARK 620 4 HIS D  80   ND1 117.3 108.7 119.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CU1 D 200  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D  46   ND1                                                    
REMARK 620 2 HIS D  48   NE2 141.5                                              
REMARK 620 3 HIS D 120   NE2  99.9 118.4                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN E 201  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP E  83   OD1                                                    
REMARK 620 2 HIS E  63   ND1 104.1                                              
REMARK 620 3 HIS E  71   ND1  96.1 106.1                                        
REMARK 620 4 HIS E  80   ND1 114.7 112.1 121.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CU1 E 200  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS E  46   ND1                                                    
REMARK 620 2 HIS E  48   NE2 141.2                                              
REMARK 620 3 HIS E 120   NE2  98.8 119.4                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN F 201  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP F  83   OD1                                                    
REMARK 620 2 HIS F  63   ND1 102.7                                              
REMARK 620 3 HIS F  71   ND1 100.7 104.9                                        
REMARK 620 4 HIS F  80   ND1 112.9 112.2 121.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CU1 F 200  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS F  46   ND1                                                    
REMARK 620 2 HIS F  48   NE2 139.2                                              
REMARK 620 3 HIS F 120   NE2  98.5 122.0                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN G 201  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP G  83   OD1                                                    
REMARK 620 2 HIS G  63   ND1 104.9                                              
REMARK 620 3 HIS G  71   ND1  98.2 101.0                                        
REMARK 620 4 HIS G  80   ND1 119.7 109.6 120.9                                  
REMARK 620 5 ASP G  83   OD2  52.7 157.3  81.1  87.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CU1 G 200  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS G  46   ND1                                                    
REMARK 620 2 HIS G  48   NE2 138.2                                              
REMARK 620 3 HIS G 120   NE2 103.0 117.1                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN H 201  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP H  83   OD1                                                    
REMARK 620 2 HIS H  63   ND1 104.0                                              
REMARK 620 3 HIS H  71   ND1 103.3 105.4                                        
REMARK 620 4 HIS H  80   ND1 115.9 107.9 119.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CU1 H 200  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS H  46   ND1                                                    
REMARK 620 2 HIS H  48   NE2 137.1                                              
REMARK 620 3 HIS H 120   NE2 104.9 117.8                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN I 201  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP I  83   OD1                                                    
REMARK 620 2 HIS I  63   ND1 101.2                                              
REMARK 620 3 HIS I  71   ND1  99.2 109.9                                        
REMARK 620 4 HIS I  80   ND1 117.0 109.4 118.5                                  
REMARK 620 5 ASP I  83   OD2  54.5 155.7  76.6  85.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CU1 I 200  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS I  46   ND1                                                    
REMARK 620 2 HIS I  48   NE2 137.5                                              
REMARK 620 3 HIS I 120   NE2  98.4 123.5                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN J 201  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP J  83   OD1                                                    
REMARK 620 2 HIS J  63   ND1 105.8                                              
REMARK 620 3 HIS J  71   ND1  97.3 103.3                                        
REMARK 620 4 HIS J  80   ND1 116.1 110.9 121.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CU1 J 200  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS J  46   ND1                                                    
REMARK 620 2 HIS J  48   NE2 141.2                                              
REMARK 620 3 HIS J 120   NE2 100.0 118.6                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 A 200                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 201                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 B 200                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 201                  
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 C 200                 
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 201                  
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 D 200                 
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 201                  
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 E 200                 
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 201                  
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 F 200                 
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN F 201                  
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 G 200                 
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN G 201                  
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 H 200                 
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN H 201                  
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 I 200                 
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN I 201                  
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 J 200                 
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN J 201                  
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 300                 
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 J 301                 
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 J 302                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1PTZ   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE HUMAN C,ZN SUPEROXIDE DISMUTASE,            
REMARK 900 FAMILIAL AMYOTROPHIC LATERAL SCLEROSIS (FALS) MUTANT H43R.           
DBREF  1PU0 A    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  1PU0 B    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  1PU0 C    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  1PU0 D    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  1PU0 E    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  1PU0 F    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  1PU0 G    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  1PU0 H    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  1PU0 I    1   153  UNP    P00441   SODC_HUMAN       1    153             
DBREF  1PU0 J    1   153  UNP    P00441   SODC_HUMAN       1    153             
SEQRES   1 A  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 A  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 A  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 A  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 A  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 A  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 A  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 A  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 A  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 A  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 A  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 A  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 B  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 B  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 B  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 B  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 B  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 B  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 B  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 B  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 B  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 B  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 B  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 B  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 C  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 C  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 C  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 C  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 C  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 C  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 C  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 C  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 C  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 C  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 C  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 C  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 D  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 D  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 D  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 D  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 D  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 D  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 D  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 D  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 D  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 D  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 D  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 D  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 E  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 E  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 E  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 E  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 E  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 E  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 E  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 E  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 E  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 E  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 E  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 E  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 F  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 F  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 F  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 F  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 F  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 F  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 F  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 F  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 F  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 F  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 F  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 F  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 G  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 G  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 G  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 G  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 G  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 G  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 G  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 G  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 G  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 G  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 G  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 G  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 H  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 H  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 H  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 H  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 H  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 H  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 H  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 H  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 H  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 H  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 H  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 H  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 I  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 I  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 I  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 I  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 I  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 I  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 I  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 I  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 I  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 I  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 I  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 I  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
SEQRES   1 J  153  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 J  153  VAL GLN GLY ILE ILE ASN PHE GLU GLN LYS GLU SER ASN          
SEQRES   3 J  153  GLY PRO VAL LYS VAL TRP GLY SER ILE LYS GLY LEU THR          
SEQRES   4 J  153  GLU GLY LEU HIS GLY PHE HIS VAL HIS GLU PHE GLY ASP          
SEQRES   5 J  153  ASN THR ALA GLY CYS THR SER ALA GLY PRO HIS PHE ASN          
SEQRES   6 J  153  PRO LEU SER ARG LYS HIS GLY GLY PRO LYS ASP GLU GLU          
SEQRES   7 J  153  ARG HIS VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS          
SEQRES   8 J  153  ASP GLY VAL ALA ASP VAL SER ILE GLU ASP SER VAL ILE          
SEQRES   9 J  153  SER LEU SER GLY ASP HIS CYS ILE ILE GLY ARG THR LEU          
SEQRES  10 J  153  VAL VAL HIS GLU LYS ALA ASP ASP LEU GLY LYS GLY GLY          
SEQRES  11 J  153  ASN GLU GLU SER THR LYS THR GLY ASN ALA GLY SER ARG          
SEQRES  12 J  153  LEU ALA CYS GLY VAL ILE GLY ILE ALA GLN                      
HET    CU1  A 200       1                                                       
HET     ZN  A 201       1                                                       
HET    CU1  B 200       1                                                       
HET     ZN  B 201       1                                                       
HET    CU1  C 200       1                                                       
HET     ZN  C 201       1                                                       
HET    CU1  D 200       1                                                       
HET     ZN  D 201       1                                                       
HET    CU1  E 200       1                                                       
HET     ZN  E 201       1                                                       
HET    CU1  F 200       1                                                       
HET     ZN  F 201       1                                                       
HET    CU1  G 200       1                                                       
HET     ZN  G 201       1                                                       
HET    CU1  H 200       1                                                       
HET     ZN  H 201       1                                                       
HET    CU1  I 200       1                                                       
HET     ZN  I 201       1                                                       
HET    CU1  J 200       1                                                       
HET     ZN  J 201       1                                                       
HET    SO4  B 300       5                                                       
HET    SO4  J 301       5                                                       
HET    SO4  J 302       5                                                       
HETNAM     CU1 COPPER (I) ION                                                   
HETNAM      ZN ZINC ION                                                         
HETNAM     SO4 SULFATE ION                                                      
FORMUL  11  CU1    10(CU 1+)                                                    
FORMUL  12   ZN    10(ZN 2+)                                                    
FORMUL  31  SO4    3(O4 S 2-)                                                   
FORMUL  34  HOH   *1047(H2 O)                                                   
HELIX    1   1 ALA A   55  GLY A   61  5                                   7    
HELIX    2   2 GLU A  133  GLY A  138  1                                   6    
HELIX    3   3 ALA B   55  GLY B   61  5                                   7    
HELIX    4   4 GLU B  133  GLY B  138  1                                   6    
HELIX    5   5 ALA C   55  GLY C   61  5                                   7    
HELIX    6   6 ASN C  131  THR C  137  1                                   7    
HELIX    7   7 ALA D   55  GLY D   61  5                                   7    
HELIX    8   8 SER D  107  CYS D  111  5                                   5    
HELIX    9   9 GLU D  133  GLY D  138  1                                   6    
HELIX   10  10 ALA E   55  GLY E   61  5                                   7    
HELIX   11  11 GLU E  133  GLY E  138  1                                   6    
HELIX   12  12 ALA F   55  GLY F   61  5                                   7    
HELIX   13  13 GLU F  133  GLY F  138  1                                   6    
HELIX   14  14 ALA G   55  GLY G   61  5                                   7    
HELIX   15  15 GLU G  133  GLY G  138  1                                   6    
HELIX   16  16 ALA H   55  GLY H   61  5                                   7    
HELIX   17  17 GLU H  133  GLY H  138  1                                   6    
HELIX   18  18 ALA I   55  GLY I   61  5                                   7    
HELIX   19  19 ASN I  131  GLY I  138  1                                   8    
HELIX   20  20 ALA J   55  GLY J   61  5                                   7    
HELIX   21  21 GLU J  133  GLY J  138  1                                   6    
SHEET    1   A 5 ALA A  95  ASP A 101  0                                        
SHEET    2   A 5 VAL A  29  LYS A  36 -1  N  ILE A  35   O  ALA A  95           
SHEET    3   A 5 GLN A  15  GLN A  22 -1  N  ASN A  19   O  TRP A  32           
SHEET    4   A 5 THR A   2  LEU A   8 -1  N  THR A   2   O  GLN A  22           
SHEET    5   A 5 GLY A 150  ILE A 151 -1  O  GLY A 150   N  VAL A   5           
SHEET    1   B 4 ASP A  83  ALA A  89  0                                        
SHEET    2   B 4 GLY A  41  HIS A  48 -1  N  GLY A  41   O  ALA A  89           
SHEET    3   B 4 THR A 116  HIS A 120 -1  O  THR A 116   N  HIS A  48           
SHEET    4   B 4 ARG A 143  VAL A 148 -1  O  ALA A 145   N  VAL A 119           
SHEET    1   C 5 ALA B  95  ASP B 101  0                                        
SHEET    2   C 5 VAL B  29  LYS B  36 -1  N  ILE B  35   O  ALA B  95           
SHEET    3   C 5 GLN B  15  GLN B  22 -1  N  ASN B  19   O  TRP B  32           
SHEET    4   C 5 THR B   2  LEU B   8 -1  N  LEU B   8   O  GLY B  16           
SHEET    5   C 5 GLY B 150  ILE B 151 -1  O  GLY B 150   N  VAL B   5           
SHEET    1   D 4 ASP B  83  ALA B  89  0                                        
SHEET    2   D 4 GLY B  41  HIS B  48 -1  N  GLY B  41   O  ALA B  89           
SHEET    3   D 4 THR B 116  HIS B 120 -1  O  THR B 116   N  HIS B  48           
SHEET    4   D 4 ARG B 143  VAL B 148 -1  O  GLY B 147   N  LEU B 117           
SHEET    1   E 5 ALA C  95  ASP C 101  0                                        
SHEET    2   E 5 VAL C  29  LYS C  36 -1  N  VAL C  29   O  ASP C 101           
SHEET    3   E 5 GLN C  15  GLN C  22 -1  N  GLN C  15   O  LYS C  36           
SHEET    4   E 5 THR C   2  LEU C   8 -1  N  THR C   2   O  GLN C  22           
SHEET    5   E 5 GLY C 150  ILE C 151 -1  O  GLY C 150   N  VAL C   5           
SHEET    1   F 4 ASP C  83  ALA C  89  0                                        
SHEET    2   F 4 GLY C  41  HIS C  48 -1  N  GLY C  41   O  ALA C  89           
SHEET    3   F 4 THR C 116  HIS C 120 -1  O  THR C 116   N  HIS C  48           
SHEET    4   F 4 ARG C 143  VAL C 148 -1  O  GLY C 147   N  LEU C 117           
SHEET    1   G 5 ALA D  95  ASP D 101  0                                        
SHEET    2   G 5 VAL D  29  LYS D  36 -1  N  ILE D  35   O  ALA D  95           
SHEET    3   G 5 GLN D  15  GLU D  21 -1  N  ASN D  19   O  TRP D  32           
SHEET    4   G 5 LYS D   3  LEU D   8 -1  N  CYS D   6   O  ILE D  18           
SHEET    5   G 5 GLY D 150  ILE D 151 -1  O  GLY D 150   N  VAL D   5           
SHEET    1   H 4 ASP D  83  ALA D  89  0                                        
SHEET    2   H 4 GLY D  41  HIS D  48 -1  N  GLY D  41   O  ALA D  89           
SHEET    3   H 4 THR D 116  HIS D 120 -1  O  THR D 116   N  HIS D  48           
SHEET    4   H 4 ARG D 143  VAL D 148 -1  O  ALA D 145   N  VAL D 119           
SHEET    1   I 5 ALA E  95  ASP E 101  0                                        
SHEET    2   I 5 VAL E  29  LYS E  36 -1  N  VAL E  31   O  ILE E  99           
SHEET    3   I 5 GLN E  15  GLN E  22 -1  N  ASN E  19   O  TRP E  32           
SHEET    4   I 5 THR E   2  LYS E   9 -1  N  THR E   2   O  GLN E  22           
SHEET    5   I 5 GLY E 150  ILE E 151 -1  O  GLY E 150   N  VAL E   5           
SHEET    1   J 4 ASP E  83  ALA E  89  0                                        
SHEET    2   J 4 GLY E  41  HIS E  48 -1  N  GLY E  41   O  ALA E  89           
SHEET    3   J 4 THR E 116  HIS E 120 -1  O  THR E 116   N  HIS E  48           
SHEET    4   J 4 ARG E 143  VAL E 148 -1  O  ALA E 145   N  VAL E 119           
SHEET    1   K 5 ALA F  95  ASP F 101  0                                        
SHEET    2   K 5 VAL F  29  LYS F  36 -1  N  ILE F  35   O  ALA F  95           
SHEET    3   K 5 GLN F  15  GLN F  22 -1  N  ASN F  19   O  TRP F  32           
SHEET    4   K 5 THR F   2  LEU F   8 -1  N  LEU F   8   O  GLY F  16           
SHEET    5   K 5 GLY F 150  ILE F 151 -1  O  GLY F 150   N  VAL F   5           
SHEET    1   L 4 ASP F  83  ALA F  89  0                                        
SHEET    2   L 4 GLY F  41  HIS F  48 -1  N  GLY F  41   O  ALA F  89           
SHEET    3   L 4 THR F 116  HIS F 120 -1  O  THR F 116   N  HIS F  48           
SHEET    4   L 4 ARG F 143  VAL F 148 -1  O  ALA F 145   N  VAL F 119           
SHEET    1   M 5 ALA G  95  ASP G 101  0                                        
SHEET    2   M 5 VAL G  29  LYS G  36 -1  N  VAL G  31   O  ILE G  99           
SHEET    3   M 5 GLN G  15  GLN G  22 -1  N  GLU G  21   O  LYS G  30           
SHEET    4   M 5 THR G   2  LEU G   8 -1  N  CYS G   6   O  ILE G  18           
SHEET    5   M 5 GLY G 150  ILE G 151 -1  O  GLY G 150   N  VAL G   5           
SHEET    1   N 4 ASP G  83  ALA G  89  0                                        
SHEET    2   N 4 GLY G  41  HIS G  48 -1  N  GLY G  41   O  ALA G  89           
SHEET    3   N 4 THR G 116  HIS G 120 -1  O  THR G 116   N  HIS G  48           
SHEET    4   N 4 ARG G 143  VAL G 148 -1  O  LEU G 144   N  VAL G 119           
SHEET    1   O 5 ALA H  95  ASP H 101  0                                        
SHEET    2   O 5 VAL H  29  LYS H  36 -1  N  VAL H  29   O  ASP H 101           
SHEET    3   O 5 GLN H  15  GLU H  21 -1  N  ASN H  19   O  TRP H  32           
SHEET    4   O 5 LYS H   3  LEU H   8 -1  N  CYS H   6   O  ILE H  18           
SHEET    5   O 5 GLY H 150  ILE H 151 -1  O  GLY H 150   N  VAL H   5           
SHEET    1   P 4 ASP H  83  ALA H  89  0                                        
SHEET    2   P 4 GLY H  41  HIS H  48 -1  N  HIS H  43   O  VAL H  87           
SHEET    3   P 4 THR H 116  HIS H 120 -1  O  THR H 116   N  HIS H  48           
SHEET    4   P 4 ARG H 143  VAL H 148 -1  O  ALA H 145   N  VAL H 119           
SHEET    1   Q 5 ALA I  95  ASP I 101  0                                        
SHEET    2   Q 5 VAL I  29  LYS I  36 -1  N  VAL I  31   O  ILE I  99           
SHEET    3   Q 5 GLN I  15  GLN I  22 -1  N  ASN I  19   O  TRP I  32           
SHEET    4   Q 5 THR I   2  LEU I   8 -1  N  LEU I   8   O  GLY I  16           
SHEET    5   Q 5 GLY I 150  ILE I 151 -1  O  GLY I 150   N  VAL I   5           
SHEET    1   R 4 ASP I  83  ALA I  89  0                                        
SHEET    2   R 4 GLY I  41  HIS I  48 -1  N  GLY I  41   O  ALA I  89           
SHEET    3   R 4 THR I 116  HIS I 120 -1  O  THR I 116   N  HIS I  48           
SHEET    4   R 4 ARG I 143  VAL I 148 -1  O  GLY I 147   N  LEU I 117           
SHEET    1   S 5 ALA J  95  ASP J 101  0                                        
SHEET    2   S 5 VAL J  29  LYS J  36 -1  N  ILE J  35   O  ALA J  95           
SHEET    3   S 5 GLN J  15  GLN J  22 -1  N  ASN J  19   O  TRP J  32           
SHEET    4   S 5 THR J   2  LEU J   8 -1  N  LEU J   8   O  GLY J  16           
SHEET    5   S 5 GLY J 150  ILE J 151 -1  O  GLY J 150   N  VAL J   5           
SHEET    1   T 4 ASP J  83  ALA J  89  0                                        
SHEET    2   T 4 GLY J  41  HIS J  48 -1  N  GLY J  41   O  ALA J  89           
SHEET    3   T 4 THR J 116  HIS J 120 -1  O  THR J 116   N  HIS J  48           
SHEET    4   T 4 ARG J 143  VAL J 148 -1  O  ALA J 145   N  VAL J 119           
SSBOND   1 CYS A   57    CYS A  146                          1555   1555  2.05  
SSBOND   2 CYS B   57    CYS B  146                          1555   1555  2.04  
SSBOND   3 CYS C   57    CYS C  146                          1555   1555  2.05  
SSBOND   4 CYS D   57    CYS D  146                          1555   1555  2.05  
SSBOND   5 CYS E   57    CYS E  146                          1555   1555  2.05  
SSBOND   6 CYS F   57    CYS F  146                          1555   1555  2.04  
SSBOND   7 CYS G   57    CYS G  146                          1555   1555  2.04  
SSBOND   8 CYS H   57    CYS H  146                          1555   1555  2.05  
SSBOND   9 CYS I   57    CYS I  146                          1555   1555  2.04  
SSBOND  10 CYS J   57    CYS J  146                          1555   1555  2.04  
LINK        ZN    ZN A 201                 OD1 ASP A  83     1555   1555  1.99  
LINK        ZN    ZN A 201                 ND1 HIS A  63     1555   1555  1.99  
LINK        ZN    ZN A 201                 ND1 HIS A  71     1555   1555  2.05  
LINK        ZN    ZN A 201                 ND1 HIS A  80     1555   1555  2.08  
LINK        CU   CU1 A 200                 ND1 HIS A  46     1555   1555  2.08  
LINK        CU   CU1 A 200                 NE2 HIS A  48     1555   1555  2.03  
LINK        CU   CU1 A 200                 NE2 HIS A 120     1555   1555  2.06  
LINK        ZN    ZN B 201                 OD1 ASP B  83     1555   1555  1.93  
LINK        ZN    ZN B 201                 ND1 HIS B  63     1555   1555  2.03  
LINK        ZN    ZN B 201                 ND1 HIS B  71     1555   1555  2.02  
LINK        ZN    ZN B 201                 ND1 HIS B  80     1555   1555  2.06  
LINK        CU   CU1 B 200                 ND1 HIS B  46     1555   1555  2.03  
LINK        CU   CU1 B 200                 NE2 HIS B  48     1555   1555  2.00  
LINK        CU   CU1 B 200                 NE2 HIS B 120     1555   1555  2.04  
LINK        ZN    ZN C 201                 OD1 ASP C  83     1555   1555  1.99  
LINK        ZN    ZN C 201                 ND1 HIS C  63     1555   1555  2.22  
LINK        ZN    ZN C 201                 ND1 HIS C  71     1555   1555  2.03  
LINK        ZN    ZN C 201                 ND1 HIS C  80     1555   1555  1.95  
LINK        CU   CU1 C 200                 ND1 HIS C  46     1555   1555  2.05  
LINK        CU   CU1 C 200                 NE2 HIS C  48     1555   1555  1.97  
LINK        CU   CU1 C 200                 NE2 HIS C 120     1555   1555  1.96  
LINK        ZN    ZN D 201                 OD1 ASP D  83     1555   1555  1.90  
LINK        ZN    ZN D 201                 ND1 HIS D  63     1555   1555  1.96  
LINK        ZN    ZN D 201                 ND1 HIS D  71     1555   1555  2.03  
LINK        ZN    ZN D 201                 ND1 HIS D  80     1555   1555  2.03  
LINK        CU   CU1 D 200                 ND1 HIS D  46     1555   1555  2.03  
LINK        CU   CU1 D 200                 NE2 HIS D  48     1555   1555  2.00  
LINK        CU   CU1 D 200                 NE2 HIS D 120     1555   1555  2.01  
LINK        ZN    ZN E 201                 OD1 ASP E  83     1555   1555  1.97  
LINK        ZN    ZN E 201                 ND1 HIS E  63     1555   1555  2.07  
LINK        ZN    ZN E 201                 ND1 HIS E  71     1555   1555  2.08  
LINK        ZN    ZN E 201                 ND1 HIS E  80     1555   1555  2.00  
LINK        CU   CU1 E 200                 ND1 HIS E  46     1555   1555  2.01  
LINK        CU   CU1 E 200                 NE2 HIS E  48     1555   1555  1.97  
LINK        CU   CU1 E 200                 NE2 HIS E 120     1555   1555  2.03  
LINK        ZN    ZN F 201                 OD1 ASP F  83     1555   1555  1.97  
LINK        ZN    ZN F 201                 ND1 HIS F  63     1555   1555  1.96  
LINK        ZN    ZN F 201                 ND1 HIS F  71     1555   1555  2.04  
LINK        ZN    ZN F 201                 ND1 HIS F  80     1555   1555  2.00  
LINK        CU   CU1 F 200                 ND1 HIS F  46     1555   1555  2.08  
LINK        CU   CU1 F 200                 NE2 HIS F  48     1555   1555  1.98  
LINK        CU   CU1 F 200                 NE2 HIS F 120     1555   1555  2.00  
LINK        ZN    ZN G 201                 OD1 ASP G  83     1555   1555  1.88  
LINK        ZN    ZN G 201                 ND1 HIS G  63     1555   1555  2.01  
LINK        ZN    ZN G 201                 ND1 HIS G  71     1555   1555  2.06  
LINK        ZN    ZN G 201                 ND1 HIS G  80     1555   1555  1.95  
LINK        CU   CU1 G 200                 ND1 HIS G  46     1555   1555  1.95  
LINK        CU   CU1 G 200                 NE2 HIS G  48     1555   1555  2.10  
LINK        CU   CU1 G 200                 NE2 HIS G 120     1555   1555  1.96  
LINK        ZN    ZN H 201                 OD1 ASP H  83     1555   1555  1.92  
LINK        ZN    ZN H 201                 ND1 HIS H  63     1555   1555  2.02  
LINK        ZN    ZN H 201                 ND1 HIS H  71     1555   1555  2.01  
LINK        ZN    ZN H 201                 ND1 HIS H  80     1555   1555  2.07  
LINK        CU   CU1 H 200                 ND1 HIS H  46     1555   1555  1.99  
LINK        CU   CU1 H 200                 NE2 HIS H  48     1555   1555  2.01  
LINK        CU   CU1 H 200                 NE2 HIS H 120     1555   1555  2.02  
LINK        ZN    ZN I 201                 OD1 ASP I  83     1555   1555  1.91  
LINK        ZN    ZN I 201                 ND1 HIS I  63     1555   1555  2.06  
LINK        ZN    ZN I 201                 ND1 HIS I  71     1555   1555  2.02  
LINK        ZN    ZN I 201                 ND1 HIS I  80     1555   1555  2.05  
LINK        CU   CU1 I 200                 ND1 HIS I  46     1555   1555  2.02  
LINK        CU   CU1 I 200                 NE2 HIS I  48     1555   1555  2.04  
LINK        CU   CU1 I 200                 NE2 HIS I 120     1555   1555  1.99  
LINK        ZN    ZN J 201                 OD1 ASP J  83     1555   1555  1.95  
LINK        ZN    ZN J 201                 ND1 HIS J  63     1555   1555  2.01  
LINK        ZN    ZN J 201                 ND1 HIS J  71     1555   1555  2.07  
LINK        ZN    ZN J 201                 ND1 HIS J  80     1555   1555  2.02  
LINK        CU   CU1 J 200                 ND1 HIS J  46     1555   1555  2.11  
LINK        CU   CU1 J 200                 NE2 HIS J  48     1555   1555  1.98  
LINK        CU   CU1 J 200                 NE2 HIS J 120     1555   1555  2.07  
LINK        ZN    ZN A 201                 OD2 ASP A  83     1555   1555  2.74  
LINK        ZN    ZN C 201                 OD2 ASP C  83     1555   1555  2.58  
LINK        ZN    ZN G 201                 OD2 ASP G  83     1555   1555  2.75  
LINK        ZN    ZN I 201                 OD2 ASP I  83     1555   1555  2.61  
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 B  46  HIS B  48  HIS B  63  HIS B 120                    
SITE     1 AC4  4 HIS B  63  HIS B  71  HIS B  80  ASP B  83                    
SITE     1 AC5  4 HIS C  46  HIS C  48  HIS C  63  HIS C 120                    
SITE     1 AC6  4 HIS C  63  HIS C  71  HIS C  80  ASP C  83                    
SITE     1 AC7  4 HIS D  46  HIS D  48  HIS D  63  HIS D 120                    
SITE     1 AC8  4 HIS D  63  HIS D  71  HIS D  80  ASP D  83                    
SITE     1 AC9  4 HIS E  46  HIS E  48  HIS E  63  HIS E 120                    
SITE     1 BC1  4 HIS E  63  HIS E  71  HIS E  80  ASP E  83                    
SITE     1 BC2  4 HIS F  46  HIS F  48  HIS F  63  HIS F 120                    
SITE     1 BC3  4 HIS F  63  HIS F  71  HIS F  80  ASP F  83                    
SITE     1 BC4  4 HIS G  46  HIS G  48  HIS G  63  HIS G 120                    
SITE     1 BC5  5 HIS G  63  HIS G  71  HIS G  80  ASP G  83                    
SITE     2 BC5  5 LYS G 136                                                     
SITE     1 BC6  4 HIS H  46  HIS H  48  HIS H  63  HIS H 120                    
SITE     1 BC7  4 HIS H  63  HIS H  71  HIS H  80  ASP H  83                    
SITE     1 BC8  4 HIS I  46  HIS I  48  HIS I  63  HIS I 120                    
SITE     1 BC9  4 HIS I  63  HIS I  71  HIS I  80  ASP I  83                    
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  4 LYS B  75  LYS D 128  HOH D 692  HOH D1022                    
SITE     1 CC4  7 LYS E 128  HOH E1004  HOH E1386  HOH E1430                    
SITE     2 CC4  7 LYS H  75  LYS H 128  LYS J 128                               
SITE     1 CC5  2 THR J  39  GLU J  40                                          
CRYST1  203.580  165.680  144.150  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      0.004912  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006036  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006937        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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