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Database: PDB
Entry: 2ZOW
LinkDB: 2ZOW
Original site: 2ZOW 
HEADER    OXIDOREDUCTASE                          11-JUN-08   2ZOW              
TITLE     CRYSTAL STRUCTURE OF H2O2 TREATED CU,ZN-SOD                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [CU-ZN];                              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 1.15.1.1                                                         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE   3 ORGANISM_COMMON: BOVINE;                                             
SOURCE   4 ORGANISM_TAXID: 9913;                                                
SOURCE   5 CELL: ERYTHROCYTE;                                                   
SOURCE   6 OTHER_DETAILS: SIGMA-ALDRICH CHEMICAL COMPANY                        
KEYWDS    METALLOPROTEIN, DISMUTASE, SOD, ACETYLATION, ANTIOXIDANT,             
KEYWDS   2 COPPER, CYTOPLASM, METAL-BINDING, OXIDOREDUCTASE, ZINC               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.ITO,T.ISHII,H.SAKAI,K.UCHIDA                                        
REVDAT   1   30-JUN-09 2ZOW    0                                                
JRNL        AUTH   S.ITO,T.ISHII,H.SAKAI,K.UCHIDA                               
JRNL        TITL   CRYSTAL STRUCTURES OF H2O2-TREATED CU,ZN-SUPEROXIDE          
JRNL        TITL 2 DISMUTASE                                                    
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.45 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.45                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 27.94                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1245479.950                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 58010                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.196                           
REMARK   3   FREE R VALUE                     : 0.221                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3041                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.004                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.45                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.54                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.40                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 9241                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2480                       
REMARK   3   BIN FREE R VALUE                    : 0.2830                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.60                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 448                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.013                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2184                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 4                                       
REMARK   3   SOLVENT ATOMS            : 443                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 18.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.30                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 5.55000                                              
REMARK   3    B22 (A**2) : -3.46000                                             
REMARK   3    B33 (A**2) : -2.09000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.16                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.12                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.19                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.14                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.021                           
REMARK   3   BOND ANGLES            (DEGREES) : 2.00                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 26.60                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.45                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
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  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.34                                                 
REMARK   3   BSOL        : 37.53                                                
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  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2ZOW COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-JUN-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB028240.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-MAR-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 93                                 
REMARK 200  PH                             : 6.4-6.7                            
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-17A                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000000                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 270                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 61462                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.450                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 27.940                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
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) : 1.45                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.50                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.33000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ID 1Q0E                                          
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.21                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% (W/V) PEG 4000, 20% (W/V) ISO-       
REMARK 280  PROPANOL, 0.09M MES, 1MM EDTA, PH 6.4, VAPOR DIFFUSION,             
REMARK 280  SITTING DROP, TEMPERATURE 295K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   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       22.81550            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       73.49500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       25.50450            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       73.49500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       22.81550            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       25.50450            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1420 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13660 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 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 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH B   357     O    HOH B   432              1.96            
REMARK 500   OE1  GLU B   119     O    HOH B   494              2.15            
REMARK 500   O    HOH B   432     O    HOH B   495              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG B 113   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 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    ARG B 113     -168.29   -100.48                                   
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                             CU1 A 301  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  44   ND1                                                    
REMARK 620 2 HIS A  46   NE2 141.6                                              
REMARK 620 3 HIS A 118   NE2  99.0 119.1                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 300  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  61   ND1                                                    
REMARK 620 2 HIS A  69   ND1 105.9                                              
REMARK 620 3 HIS A  78   ND1 110.0 120.2                                        
REMARK 620 4 ASP A  81   OD1 109.5  96.7 113.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CU1 B 301  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  44   ND1                                                    
REMARK 620 2 HIS B  46   NE2 142.4                                              
REMARK 620 3 HIS B 118   NE2  99.1 118.3                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 300  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  61   ND1                                                    
REMARK 620 2 HIS B  69   ND1 108.4                                              
REMARK 620 3 HIS B  78   ND1 111.3 116.8                                        
REMARK 620 4 ASP B  81   OD1 101.3  97.4 119.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 300                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 A 301                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 300                  
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU1 B 301                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2Z7U   RELATED DB: PDB                                   
REMARK 900 THE MOST SEVERELY MODIFIED CU,ZN-SOD                                 
REMARK 900 RELATED ID: 2Z7W   RELATED DB: PDB                                   
REMARK 900 SEVERELY MODIFIED CU,ZN-SOD                                          
REMARK 900 RELATED ID: 2Z7Y   RELATED DB: PDB                                   
REMARK 900 H2O2 TREATMENT WAS PERFORMED UNDER MILD CONDITION                    
REMARK 900 RELATED ID: 2Z7Z   RELATED DB: PDB                                   
REMARK 900 H2O2 TREATMENT WAS PERFORMED COEXISTENT WITH BICARBONATE             
DBREF  2ZOW A    1   151  UNP    P00442   SODC_BOVIN       2    152             
DBREF  2ZOW B    1   151  UNP    P00442   SODC_BOVIN       2    152             
SEQRES   1 A  151  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 A  151  VAL GLN GLY THR ILE HIS PHE GLU ALA LYS GLY ASP THR          
SEQRES   3 A  151  VAL VAL VAL THR GLY SER ILE THR GLY LEU THR GLU GLY          
SEQRES   4 A  151  ASP HIS GLY PHE HIS VAL HIS GLN PHE GLY ASP ASN THR          
SEQRES   5 A  151  GLN GLY CYS THR SER ALA GLY PRO HIS PHE ASN PRO LEU          
SEQRES   6 A  151  SER LYS LYS HIS GLY GLY PRO LYS ASP GLU GLU ARG HIS          
SEQRES   7 A  151  VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS ASN GLY          
SEQRES   8 A  151  VAL ALA ILE VAL ASP ILE VAL ASP PRO LEU ILE SER LEU          
SEQRES   9 A  151  SER GLY GLU TYR SER ILE ILE GLY ARG THR MET VAL VAL          
SEQRES  10 A  151  HIS GLU LYS PRO ASP ASP LEU GLY ARG GLY GLY ASN GLU          
SEQRES  11 A  151  GLU SER THR LYS THR GLY ASN ALA GLY SER ARG LEU ALA          
SEQRES  12 A  151  CYS GLY VAL ILE GLY ILE ALA LYS                              
SEQRES   1 B  151  ALA THR LYS ALA VAL CYS VAL LEU LYS GLY ASP GLY PRO          
SEQRES   2 B  151  VAL GLN GLY THR ILE HIS PHE GLU ALA LYS GLY ASP THR          
SEQRES   3 B  151  VAL VAL VAL THR GLY SER ILE THR GLY LEU THR GLU GLY          
SEQRES   4 B  151  ASP HIS GLY PHE HIS VAL HIS GLN PHE GLY ASP ASN THR          
SEQRES   5 B  151  GLN GLY CYS THR SER ALA GLY PRO HIS PHE ASN PRO LEU          
SEQRES   6 B  151  SER LYS LYS HIS GLY GLY PRO LYS ASP GLU GLU ARG HIS          
SEQRES   7 B  151  VAL GLY ASP LEU GLY ASN VAL THR ALA ASP LYS ASN GLY          
SEQRES   8 B  151  VAL ALA ILE VAL ASP ILE VAL ASP PRO LEU ILE SER LEU          
SEQRES   9 B  151  SER GLY GLU TYR SER ILE ILE GLY ARG THR MET VAL VAL          
SEQRES  10 B  151  HIS GLU LYS PRO ASP ASP LEU GLY ARG GLY GLY ASN GLU          
SEQRES  11 B  151  GLU SER THR LYS THR GLY ASN ALA GLY SER ARG LEU ALA          
SEQRES  12 B  151  CYS GLY VAL ILE GLY ILE ALA LYS                              
HET     ZN  A 300       1                                                       
HET    CU1  A 301       1                                                       
HET     ZN  B 300       1                                                       
HET    CU1  B 301       1                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     CU1 COPPER (I) ION                                                   
FORMUL   3   ZN    2(ZN 2+)                                                     
FORMUL   4  CU1    2(CU 1+)                                                     
FORMUL   7  HOH   *443(H2 O)                                                    
HELIX    1   1 CYS A   55  GLY A   59  5                                   5    
HELIX    2   2 GLU A  131  GLY A  136  1                                   6    
HELIX    3   3 GLN B   53  GLY B   59  5                                   7    
HELIX    4   4 GLU B  131  GLY B  136  1                                   6    
SHEET    1   A 5 ALA A  93  ASP A  99  0                                        
SHEET    2   A 5 THR A  26  THR A  34 -1  N  VAL A  29   O  ILE A  97           
SHEET    3   A 5 GLN A  15  LYS A  23 -1  N  GLU A  21   O  VAL A  28           
SHEET    4   A 5 LYS A   3  LEU A   8 -1  N  CYS A   6   O  ILE A  18           
SHEET    5   A 5 GLY A 148  ILE A 149 -1  O  GLY A 148   N  VAL A   5           
SHEET    1   B 4 ASP A  81  ALA A  87  0                                        
SHEET    2   B 4 GLY A  39  HIS A  46 -1  N  GLY A  39   O  ALA A  87           
SHEET    3   B 4 THR A 114  HIS A 118 -1  O  THR A 114   N  HIS A  46           
SHEET    4   B 4 ARG A 141  VAL A 146 -1  O  GLY A 145   N  MET A 115           
SHEET    1   C 5 ALA B  93  ASP B  99  0                                        
SHEET    2   C 5 THR B  26  THR B  34 -1  N  VAL B  29   O  ILE B  97           
SHEET    3   C 5 GLN B  15  LYS B  23 -1  N  GLN B  15   O  THR B  34           
SHEET    4   C 5 LYS B   3  LEU B   8 -1  N  CYS B   6   O  ILE B  18           
SHEET    5   C 5 GLY B 148  ILE B 149 -1  O  GLY B 148   N  VAL B   5           
SHEET    1   D 4 ASP B  81  ALA B  87  0                                        
SHEET    2   D 4 GLY B  39  HIS B  46 -1  N  GLY B  39   O  ALA B  87           
SHEET    3   D 4 THR B 114  HIS B 118 -1  O  THR B 114   N  HIS B  46           
SHEET    4   D 4 ARG B 141  VAL B 146 -1  O  ALA B 143   N  VAL B 117           
SSBOND   1 CYS A   55    CYS A  144                          1555   1555  2.17  
SSBOND   2 CYS B   55    CYS B  144                          1555   1555  2.22  
LINK         ND1 HIS A  44                CU   CU1 A 301     1555   1555  2.02  
LINK         NE2 HIS A  46                CU   CU1 A 301     1555   1555  1.98  
LINK         ND1 HIS A  61                ZN    ZN A 300     1555   1555  2.03  
LINK         ND1 HIS A  69                ZN    ZN A 300     1555   1555  2.08  
LINK         ND1 HIS A  78                ZN    ZN A 300     1555   1555  2.08  
LINK         OD1 ASP A  81                ZN    ZN A 300     1555   1555  1.93  
LINK         NE2 HIS A 118                CU   CU1 A 301     1555   1555  2.00  
LINK         ND1 HIS B  44                CU   CU1 B 301     1555   1555  2.02  
LINK         NE2 HIS B  46                CU   CU1 B 301     1555   1555  2.00  
LINK         ND1 HIS B  61                ZN    ZN B 300     1555   1555  2.04  
LINK         ND1 HIS B  69                ZN    ZN B 300     1555   1555  2.06  
LINK         ND1 HIS B  78                ZN    ZN B 300     1555   1555  1.95  
LINK         OD1 ASP B  81                ZN    ZN B 300     1555   1555  1.98  
LINK         NE2 HIS B 118                CU   CU1 B 301     1555   1555  2.06  
SITE     1 AC1  4 HIS A  61  HIS A  69  HIS A  78  ASP A  81                    
SITE     1 AC2  4 HIS A  44  HIS A  46  HIS A  61  HIS A 118                    
SITE     1 AC3  4 HIS B  61  HIS B  69  HIS B  78  ASP B  81                    
SITE     1 AC4  4 HIS B  44  HIS B  46  HIS B  61  HIS B 118                    
CRYST1   45.631   51.009  146.990  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.021915  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.019604  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006803        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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