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Database: PDB
Entry: 1EQW
LinkDB: 1EQW
Original site: 1EQW 
HEADER    OXIDOREDUCTASE                          06-APR-00   1EQW              
TITLE     CRYSTAL STRUCTURE OF SALMONELLA TYPHIMURIUM CU,ZN                     
TITLE    2 SUPEROXIDE DISMUTASE                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CU,ZN SUPEROXIDE DISMUTASE;                                
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 EC: 1.15.1.1;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SALMONELLA TYPHIMURIUM;                         
SOURCE   3 ORGANISM_TAXID: 602;                                                 
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 EXPRESSION_SYSTEM_VECTOR: QC871                                      
KEYWDS    SUPEROXIDE DISMUTASE, GREEK KEY B-BARREL, OXIDOREDUCTASE              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.PESCE,A.BATTISTONI,M.E.STROPPOLO,F.POLIZIO,M.NARDINI,               
AUTHOR   2 J.S.KROLL,P.R.LANGFORD,P.O'NEILL,M.SETTE,A.DESIDERI,                 
AUTHOR   3 M.BOLOGNESI                                                          
REVDAT   3   24-FEB-09 1EQW    1       VERSN                                    
REVDAT   2   01-APR-03 1EQW    1       JRNL                                     
REVDAT   1   08-SEP-00 1EQW    0                                                
JRNL        AUTH   A.PESCE,A.BATTISTONI,M.E.STROPPOLO,F.POLIZIO,                
JRNL        AUTH 2 M.NARDINI,J.S.KROLL,P.R.LANGFORD,P.O'NEILL,M.SETTE,          
JRNL        AUTH 3 A.DESIDERI,M.BOLOGNESI                                       
JRNL        TITL   FUNCTIONAL AND CRYSTALLOGRAPHIC CHARACTERIZATION             
JRNL        TITL 2 OF SALMONELLA TYPHIMURIUM CU,ZN SUPEROXIDE                   
JRNL        TITL 3 DISMUTASE CODED BY THE SODCI VIRULENCE GENE.                 
JRNL        REF    J.MOL.BIOL.                   V. 302   465 2000              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   10970746                                                     
JRNL        DOI    10.1006/JMBI.2000.4074                                       
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
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 : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 22.60                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 96.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 27119                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.226                           
REMARK   3   FREE R VALUE                     : 0.283                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 2712                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4445                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 8                                       
REMARK   3   SOLVENT ATOMS            : 178                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 40.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.35                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1EQW COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-APR-00.                  
REMARK 100 THE RCSB ID CODE IS RCSB010832.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-MAY-98                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27119                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 22.600                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.2                               
REMARK 200  DATA REDUNDANCY                : 3.000                              
REMARK 200  R MERGE                    (I) : 0.06200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.34                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 1302.0                             
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.35600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.15                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, SODIUM CHLORIDE, SODIUM        
REMARK 280  ACETATE, PH 4.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE         
REMARK 280  294K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       71.07000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       20.32950            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       71.07000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       20.32950            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1510 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13300 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1430 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 12950 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     LYS A   149                                                      
REMARK 465     GLU C   148                                                      
REMARK 465     LYS C   149                                                      
REMARK 465     GLU D   148                                                      
REMARK 465     LYS D   149                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A  53C   CG   CD   CE   NZ                                   
REMARK 470     LYS A 131    CG   CD   CE   NZ                                   
REMARK 470     GLU A 148    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  53C   CG   CD   CE   NZ                                   
REMARK 470     LYS B  53F   CG   CD   CE   NZ                                   
REMARK 470     LYS B 149    CG   CD   CE   NZ                                   
REMARK 470     GLU C  17    CG   CD   OE1  OE2                                  
REMARK 470     ASP C  75    CG   OD1  OD2                                       
REMARK 470     LYS C 131    CG   CD   CE   NZ                                   
REMARK 470     LYS D   7    CG   CD   CE   NZ                                   
REMARK 470     LYS D  53C   CG   CD   CE   NZ                                   
REMARK 470     ASP D  53D   CG   OD1  OD2                                       
REMARK 470     LYS D  53F   CG   CD   CE   NZ                                   
REMARK 470     LYS D  66    CG   CD   CE   NZ                                   
REMARK 470     LYS D  76    CG   CD   CE   NZ                                   
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     ASN A    2   N                                                   
REMARK 480     LYS B   53C  CB                                                  
REMARK 480     SER D  106   OG                                                  
REMARK 480     SER D  125   OG                                                  
REMARK 480     LEU D  135   CG    CD1   CD2                                     
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A  66       50.41     33.50                                   
REMARK 500    ASN A  88     -170.62    -64.03                                   
REMARK 500    ASP A 122      116.77   -163.54                                   
REMARK 500    ILE A 147       98.99   -161.28                                   
REMARK 500    PRO B  49       49.57    -70.20                                   
REMARK 500    LYS B  53F     140.30    171.35                                   
REMARK 500    GLU B  65       -8.10    -53.18                                   
REMARK 500    ASP B 122      107.66   -160.94                                   
REMARK 500    ILE B 147      -88.73    -91.35                                   
REMARK 500    GLU B 148     -143.18   -152.54                                   
REMARK 500    PRO C  49       48.23    -79.09                                   
REMARK 500    MET C  57        1.59    -63.28                                   
REMARK 500    LYS C  66       44.16     34.03                                   
REMARK 500    ASP C  75       -4.98    -56.30                                   
REMARK 500    PRO D  49       36.77    -80.48                                   
REMARK 500    LEU D  62      109.29    -56.63                                   
REMARK 500    HIS D  78      124.00    -37.03                                   
REMARK 500    ASP D 122      113.04   -163.63                                   
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 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  61   ND1                                                    
REMARK 620 2 HIS A  69   ND1 118.4                                              
REMARK 620 3 HIS A  78   ND1 115.6 110.9                                        
REMARK 620 4 ASP A  81   OD1 108.5  89.5 110.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU A 502  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  46   NE2                                                    
REMARK 620 2 HIS A  61   NE2  95.7                                              
REMARK 620 3 HIS A 118   NE2 124.8 120.6                                        
REMARK 620 4 HIS A  44   ND1 137.6  76.9  93.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 503  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  61   ND1                                                    
REMARK 620 2 HIS B  78   ND1 107.6                                              
REMARK 620 3 HIS B  69   ND1 105.9 114.6                                        
REMARK 620 4 ASP B  81   OD1 106.1 125.0  95.9                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU B 504  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 118   NE2                                                    
REMARK 620 2 HIS B  61   NE2 132.8                                              
REMARK 620 3 HIS B  46   NE2 116.0  96.8                                        
REMARK 620 4 HIS B  44   ND1  95.9  81.2 135.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 505  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  78   ND1                                                    
REMARK 620 2 ASP C  81   OD1 122.0                                              
REMARK 620 3 HIS C  69   ND1 120.9  95.9                                        
REMARK 620 4 HIS C  61   ND1  95.2 111.6 112.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU C 506  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  61   NE2                                                    
REMARK 620 2 HIS C  44   ND1  74.1                                              
REMARK 620 3 HIS C 118   NE2 128.6  95.6                                        
REMARK 620 4 HIS C  46   NE2  93.9 138.4 121.3                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN D 507  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D  78   ND1                                                    
REMARK 620 2 HIS D  61   ND1  87.4                                              
REMARK 620 3 HIS D  69   ND1 116.7 120.4                                        
REMARK 620 4 ASP D  81   OD1 124.2 111.0  98.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU D 508  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D  46   NE2                                                    
REMARK 620 2 HIS D 118   NE2 114.3                                              
REMARK 620 3 HIS D  44   ND1 142.5 101.1                                        
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 ZN A 501                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU A 502                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 503                  
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU B 504                  
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 505                  
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU C 506                  
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 507                  
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CU D 508                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1BZO   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF PROKARYOTIC CU,ZN SUPEROXIDE DISMUTASE          
REMARK 900 FROM P.LEIOGNATHI                                                    
REMARK 900 RELATED ID: 1ESO   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF PROKARYOTIC CU,ZN SUPEROXIDE DISMUTASE          
REMARK 900 FROM E.COLI                                                          
DBREF  1EQW A    2   149  UNP    P53636   SODC1_SALTY     22    177             
DBREF  1EQW B    2   149  UNP    P53636   SODC1_SALTY     22    177             
DBREF  1EQW C    2   149  UNP    P53636   SODC1_SALTY     22    177             
DBREF  1EQW D    2   149  UNP    P53636   SODC1_SALTY     22    177             
SEQADV 1EQW MET A  116  UNP  P53636    THR   148 CONFLICT                       
SEQADV 1EQW MET B  116  UNP  P53636    THR   148 CONFLICT                       
SEQADV 1EQW MET C  116  UNP  P53636    THR   148 CONFLICT                       
SEQADV 1EQW MET D  116  UNP  P53636    THR   148 CONFLICT                       
SEQRES   1 A  156  ASN THR LEU THR VAL LYS MET ASN ASP ALA LEU SER SER          
SEQRES   2 A  156  GLY THR GLY GLU ASN ILE GLY GLU ILE THR VAL SER GLU          
SEQRES   3 A  156  THR PRO TYR GLY LEU LEU PHE THR PRO HIS LEU ASN GLY          
SEQRES   4 A  156  LEU THR PRO GLY ILE HIS GLY PHE HIS VAL HIS THR ASN          
SEQRES   5 A  156  PRO SER CYS MET PRO GLY MET LYS ASP GLY LYS GLU VAL          
SEQRES   6 A  156  PRO ALA LEU MET ALA GLY GLY HIS LEU ASP PRO GLU LYS          
SEQRES   7 A  156  THR GLY LYS HIS LEU GLY PRO TYR ASN ASP LYS GLY HIS          
SEQRES   8 A  156  LEU GLY ASP LEU PRO GLY LEU VAL VAL ASN ALA ASP GLY          
SEQRES   9 A  156  THR ALA THR TYR PRO LEU LEU ALA PRO ARG LEU LYS SER          
SEQRES  10 A  156  LEU SER GLU LEU LYS GLY HIS SER LEU MET ILE HIS LYS          
SEQRES  11 A  156  GLY GLY ASP ASN TYR SER ASP LYS PRO ALA PRO LEU GLY          
SEQRES  12 A  156  GLY GLY GLY ALA ARG PHE ALA CYS GLY VAL ILE GLU LYS          
SEQRES   1 B  156  ASN THR LEU THR VAL LYS MET ASN ASP ALA LEU SER SER          
SEQRES   2 B  156  GLY THR GLY GLU ASN ILE GLY GLU ILE THR VAL SER GLU          
SEQRES   3 B  156  THR PRO TYR GLY LEU LEU PHE THR PRO HIS LEU ASN GLY          
SEQRES   4 B  156  LEU THR PRO GLY ILE HIS GLY PHE HIS VAL HIS THR ASN          
SEQRES   5 B  156  PRO SER CYS MET PRO GLY MET LYS ASP GLY LYS GLU VAL          
SEQRES   6 B  156  PRO ALA LEU MET ALA GLY GLY HIS LEU ASP PRO GLU LYS          
SEQRES   7 B  156  THR GLY LYS HIS LEU GLY PRO TYR ASN ASP LYS GLY HIS          
SEQRES   8 B  156  LEU GLY ASP LEU PRO GLY LEU VAL VAL ASN ALA ASP GLY          
SEQRES   9 B  156  THR ALA THR TYR PRO LEU LEU ALA PRO ARG LEU LYS SER          
SEQRES  10 B  156  LEU SER GLU LEU LYS GLY HIS SER LEU MET ILE HIS LYS          
SEQRES  11 B  156  GLY GLY ASP ASN TYR SER ASP LYS PRO ALA PRO LEU GLY          
SEQRES  12 B  156  GLY GLY GLY ALA ARG PHE ALA CYS GLY VAL ILE GLU LYS          
SEQRES   1 C  156  ASN THR LEU THR VAL LYS MET ASN ASP ALA LEU SER SER          
SEQRES   2 C  156  GLY THR GLY GLU ASN ILE GLY GLU ILE THR VAL SER GLU          
SEQRES   3 C  156  THR PRO TYR GLY LEU LEU PHE THR PRO HIS LEU ASN GLY          
SEQRES   4 C  156  LEU THR PRO GLY ILE HIS GLY PHE HIS VAL HIS THR ASN          
SEQRES   5 C  156  PRO SER CYS MET PRO GLY MET LYS ASP GLY LYS GLU VAL          
SEQRES   6 C  156  PRO ALA LEU MET ALA GLY GLY HIS LEU ASP PRO GLU LYS          
SEQRES   7 C  156  THR GLY LYS HIS LEU GLY PRO TYR ASN ASP LYS GLY HIS          
SEQRES   8 C  156  LEU GLY ASP LEU PRO GLY LEU VAL VAL ASN ALA ASP GLY          
SEQRES   9 C  156  THR ALA THR TYR PRO LEU LEU ALA PRO ARG LEU LYS SER          
SEQRES  10 C  156  LEU SER GLU LEU LYS GLY HIS SER LEU MET ILE HIS LYS          
SEQRES  11 C  156  GLY GLY ASP ASN TYR SER ASP LYS PRO ALA PRO LEU GLY          
SEQRES  12 C  156  GLY GLY GLY ALA ARG PHE ALA CYS GLY VAL ILE GLU LYS          
SEQRES   1 D  156  ASN THR LEU THR VAL LYS MET ASN ASP ALA LEU SER SER          
SEQRES   2 D  156  GLY THR GLY GLU ASN ILE GLY GLU ILE THR VAL SER GLU          
SEQRES   3 D  156  THR PRO TYR GLY LEU LEU PHE THR PRO HIS LEU ASN GLY          
SEQRES   4 D  156  LEU THR PRO GLY ILE HIS GLY PHE HIS VAL HIS THR ASN          
SEQRES   5 D  156  PRO SER CYS MET PRO GLY MET LYS ASP GLY LYS GLU VAL          
SEQRES   6 D  156  PRO ALA LEU MET ALA GLY GLY HIS LEU ASP PRO GLU LYS          
SEQRES   7 D  156  THR GLY LYS HIS LEU GLY PRO TYR ASN ASP LYS GLY HIS          
SEQRES   8 D  156  LEU GLY ASP LEU PRO GLY LEU VAL VAL ASN ALA ASP GLY          
SEQRES   9 D  156  THR ALA THR TYR PRO LEU LEU ALA PRO ARG LEU LYS SER          
SEQRES  10 D  156  LEU SER GLU LEU LYS GLY HIS SER LEU MET ILE HIS LYS          
SEQRES  11 D  156  GLY GLY ASP ASN TYR SER ASP LYS PRO ALA PRO LEU GLY          
SEQRES  12 D  156  GLY GLY GLY ALA ARG PHE ALA CYS GLY VAL ILE GLU LYS          
HET     ZN  A 501       1                                                       
HET     CU  A 502       1                                                       
HET     ZN  B 503       1                                                       
HET     CU  B 504       1                                                       
HET     ZN  C 505       1                                                       
HET     CU  C 506       1                                                       
HET     ZN  D 507       1                                                       
HET     CU  D 508       1                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM      CU COPPER (II) ION                                                  
FORMUL   5   ZN    4(ZN 2+)                                                     
FORMUL   6   CU    4(CU 2+)                                                     
FORMUL  13  HOH   *178(H2 O)                                                    
HELIX    1   1 ALA A   55  GLY A   59  5                                   5    
HELIX    2   2 SER A  106  LYS A  111  5                                   6    
HELIX    3   3 PRO A  134  GLY A  138  5                                   5    
HELIX    4   4 ALA B   55  GLY B   59  5                                   5    
HELIX    5   5 SER B  106  LYS B  111  5                                   6    
HELIX    6   6 ALA B  133  GLY B  138  5                                   6    
HELIX    7   7 ALA C   55  GLY C   59  5                                   5    
HELIX    8   8 ALA C  133  GLY C  138  5                                   6    
HELIX    9   9 ALA D   55  GLY D   59  5                                   5    
HELIX   10  10 SER D  106  LEU D  110  5                                   5    
HELIX   11  11 ALA D  133  GLY D  138  5                                   6    
SHEET    1   A 7 PHE A  43  HIS A  46  0                                        
SHEET    2   A 7 HIS A 113  HIS A 118 -1  O  SER A 114   N  HIS A  46           
SHEET    3   A 7 ARG A 141  ILE A 147 -1  N  PHE A 142   O  ILE A 117           
SHEET    4   A 7 THR A   3  ALA A   9B-1  O  ASN A   9   N  CYS A 144           
SHEET    5   A 7 THR A  11  THR A  23 -1  N  GLY A  12   O  ASP A   9A          
SHEET    6   A 7 GLY A  26  LEU A  33 -1  N  GLY A  26   O  THR A  23           
SHEET    7   A 7 LEU A  97  ALA A  99 -1  O  LEU A  97   N  PHE A  29           
SHEET    1   B 2 GLY A  39  HIS A  41  0                                        
SHEET    2   B 2 LEU A  85  VAL A  87 -1  N  LEU A  85   O  HIS A  41           
SHEET    1   C 2 GLY A  53A LYS A  53C 0                                        
SHEET    2   C 2 LYS A  53F VAL A  53H-1  O  LYS A  53F  N  LYS A  53C          
SHEET    1   D 7 PHE B  43  HIS B  46  0                                        
SHEET    2   D 7 SER B 114  HIS B 118 -1  O  SER B 114   N  HIS B  46           
SHEET    3   D 7 ARG B 141  VAL B 146 -1  N  PHE B 142   O  ILE B 117           
SHEET    4   D 7 THR B   3  ALA B   9B-1  N  ASN B   9   O  CYS B 144           
SHEET    5   D 7 THR B  11  THR B  23 -1  N  GLY B  12   O  ASP B   9A          
SHEET    6   D 7 GLY B  26  LEU B  33 -1  O  GLY B  26   N  THR B  23           
SHEET    7   D 7 LEU B  97  ALA B  99 -1  O  LEU B  97   N  PHE B  29           
SHEET    1   E 2 GLY B  39  HIS B  41  0                                        
SHEET    2   E 2 LEU B  85  VAL B  87 -1  N  LEU B  85   O  HIS B  41           
SHEET    1   F 2 GLY B  53A MET B  53B 0                                        
SHEET    2   F 2 GLU B  53G VAL B  53H-1  N  VAL B  53H  O  GLY B  53A          
SHEET    1   G 7 PHE C  43  HIS C  46  0                                        
SHEET    2   G 7 HIS C 113  HIS C 118 -1  O  SER C 114   N  HIS C  46           
SHEET    3   G 7 ARG C 141  ILE C 147 -1  N  PHE C 142   O  ILE C 117           
SHEET    4   G 7 LEU C   4  LEU C   9C-1  O  ASN C   9   N  CYS C 144           
SHEET    5   G 7 GLY C  10  THR C  23 -1  O  GLY C  10   N  LEU C   9C          
SHEET    6   G 7 GLY C  26  LEU C  33 -1  N  GLY C  26   O  THR C  23           
SHEET    7   G 7 LEU C  97  ALA C  99 -1  O  LEU C  97   N  PHE C  29           
SHEET    1   H 2 GLY C  39  HIS C  41  0                                        
SHEET    2   H 2 LEU C  85  VAL C  87 -1  N  LEU C  85   O  HIS C  41           
SHEET    1   I 2 GLY C  53A LYS C  53C 0                                        
SHEET    2   I 2 LYS C  53F VAL C  53H-1  O  LYS C  53F  N  LYS C  53C          
SHEET    1   J 7 PHE D  43  HIS D  46  0                                        
SHEET    2   J 7 SER D 114  HIS D 118 -1  O  SER D 114   N  HIS D  46           
SHEET    3   J 7 ARG D 141  VAL D 146 -1  N  PHE D 142   O  ILE D 117           
SHEET    4   J 7 THR D   3  LEU D   9C-1  N  ASN D   9   O  CYS D 144           
SHEET    5   J 7 GLY D  10  THR D  23 -1  O  GLY D  10   N  LEU D   9C          
SHEET    6   J 7 GLY D  26  LEU D  33 -1  O  GLY D  26   N  THR D  23           
SHEET    7   J 7 LEU D  97  ALA D  99 -1  O  LEU D  97   N  PHE D  29           
SHEET    1   K 2 GLY D  39  HIS D  41  0                                        
SHEET    2   K 2 LEU D  85  VAL D  87 -1  N  LEU D  85   O  HIS D  41           
SHEET    1   L 2 GLY D  53A MET D  53B 0                                        
SHEET    2   L 2 GLU D  53G VAL D  53H-1  N  VAL D  53H  O  GLY D  53A          
SSBOND   1 CYS A   51    CYS A  144                          1555   1555  2.10  
SSBOND   2 CYS B   51    CYS B  144                          1555   1555  1.71  
SSBOND   3 CYS C   51    CYS C  144                          1555   1555  1.98  
SSBOND   4 CYS D   51    CYS D  144                          1555   1555  1.69  
LINK        ZN    ZN A 501                 ND1 HIS A  61     1555   1555  2.11  
LINK        ZN    ZN A 501                 ND1 HIS A  69     1555   1555  1.92  
LINK        ZN    ZN A 501                 ND1 HIS A  78     1555   1555  2.05  
LINK        ZN    ZN A 501                 OD1 ASP A  81     1555   1555  2.11  
LINK        CU    CU A 502                 NE2 HIS A  46     1555   1555  2.02  
LINK        CU    CU A 502                 NE2 HIS A  61     1555   1555  2.47  
LINK        CU    CU A 502                 NE2 HIS A 118     1555   1555  1.92  
LINK        CU    CU A 502                 ND1 HIS A  44     1555   1555  2.29  
LINK        ZN    ZN B 503                 ND1 HIS B  61     1555   1555  2.19  
LINK        ZN    ZN B 503                 ND1 HIS B  78     1555   1555  2.33  
LINK        ZN    ZN B 503                 ND1 HIS B  69     1555   1555  2.02  
LINK        ZN    ZN B 503                 OD1 ASP B  81     1555   1555  2.06  
LINK        CU    CU B 504                 NE2 HIS B 118     1555   1555  1.95  
LINK        CU    CU B 504                 NE2 HIS B  61     1555   1555  2.50  
LINK        CU    CU B 504                 NE2 HIS B  46     1555   1555  2.16  
LINK        CU    CU B 504                 ND1 HIS B  44     1555   1555  2.20  
LINK        ZN    ZN C 505                 ND1 HIS C  78     1555   1555  1.96  
LINK        ZN    ZN C 505                 OD1 ASP C  81     1555   1555  2.00  
LINK        ZN    ZN C 505                 ND1 HIS C  69     1555   1555  1.98  
LINK        ZN    ZN C 505                 ND1 HIS C  61     1555   1555  1.94  
LINK        CU    CU C 506                 NE2 HIS C  61     1555   1555  2.67  
LINK        CU    CU C 506                 ND1 HIS C  44     1555   1555  2.21  
LINK        CU    CU C 506                 NE2 HIS C 118     1555   1555  1.93  
LINK        CU    CU C 506                 NE2 HIS C  46     1555   1555  2.09  
LINK        ZN    ZN D 507                 ND1 HIS D  78     1555   1555  2.30  
LINK        ZN    ZN D 507                 ND1 HIS D  61     1555   1555  2.28  
LINK        ZN    ZN D 507                 ND1 HIS D  69     1555   1555  2.02  
LINK        ZN    ZN D 507                 OD1 ASP D  81     1555   1555  1.98  
LINK        CU    CU D 508                 NE2 HIS D  46     1555   1555  2.20  
LINK        CU    CU D 508                 NE2 HIS D 118     1555   1555  1.95  
LINK        CU    CU D 508                 ND1 HIS D  44     1555   1555  2.04  
CISPEP   1 LYS A  131    PRO A  132          0         0.52                     
CISPEP   2 LYS B  131    PRO B  132          0         0.04                     
CISPEP   3 LYS C  131    PRO C  132          0         0.33                     
CISPEP   4 LYS D  131    PRO D  132          0         0.80                     
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                    
SITE     1 AC5  4 HIS C  61  HIS C  69  HIS C  78  ASP C  81                    
SITE     1 AC6  4 HIS C  44  HIS C  46  HIS C  61  HIS C 118                    
SITE     1 AC7  4 HIS D  61  HIS D  69  HIS D  78  ASP D  81                    
SITE     1 AC8  4 HIS D  44  HIS D  46  HIS D  61  HIS D 118                    
CRYST1  142.140   40.659  114.254  90.00 107.73  90.00 C 1 2 1      16          
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      0.007035  0.000000  0.002249        0.00000                         
SCALE2      0.000000  0.024595  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009189        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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