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Database: PDB
Entry: 1WB8
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HEADER    OXIDOREDUCTASE                          31-OCT-04   1WB8              
TITLE     IRON SUPEROXIDE DISMUTASE (FE-SOD) FROM THE                           
TITLE    2 HYPERTHERMOPHILE SULFOLOBUS SOLFATARICUS. 2.3 A RESOLUTION           
TITLE    3 STRUCTURE OF RECOMBINANT PROTEIN WITH A COVALENTLY                   
TITLE    4 MODIFIED TYROSIN IN THE ACTIVE SITE.                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [FE];                                 
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 1.15.1.1;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 OTHER_DETAILS: COVALENT MODIFICATION OF TYR 41 CONSISTING            
COMPND   7  OF HET GROUP PMS (PHENYL METHYL SULFONATE, BENZYLSULFINIC           
COMPND   8  ACID)                                                               
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SULFOLOBUS SOLFATARICUS;                        
SOURCE   3 ORGANISM_TAXID: 2287;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: JM109(DE3);                                
SOURCE   7 EXPRESSION_SYSTEM_VECTOR: VSOD;                                      
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PT7-7                                     
KEYWDS    SUPEROXIDE DISMUTASE, SOD, IRON, OXIDOREDUCTASE, SUPEROXIDE           
KEYWDS   2 RADICAL DISPROPORTIONATION, SULFOLOBUS SOLFTARICUS,                  
KEYWDS   3 THERMOSTABLE                                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.URSBY,B.S.ADINOLFI,S.AL-KARADAGHI,E.DE VENDITTIS,                   
AUTHOR   2 V.BOCCHINI                                                           
REVDAT   2   24-FEB-09 1WB8    1       VERSN                                    
REVDAT   1   08-NOV-04 1WB8    0                                                
SPRSDE     08-NOV-04 1WB8      1SSS                                             
JRNL        AUTH   T.URSBY,B.S.ADINOLFI,S.AL-KARADAGHI,E.DE VENDITTIS,          
JRNL        AUTH 2 V.BOCCHINI                                                   
JRNL        TITL   IRON SUPEROXIDE DISMUTASE FROM THE ARCHAEON                  
JRNL        TITL 2 SULFOLOBUS SOLFATARICUS: ANALYSIS OF STRUCTURE AND           
JRNL        TITL 3 THERMOSTABILITY                                              
JRNL        REF    J.MOL.BIOL.                   V. 286   189 1999              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   9931259                                                      
JRNL        DOI    10.1006/JMBI.1998.2471                                       
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   E.DE VENDITTIS,T.URSBY,R.RULLO,M.A.GOGLIETTINO,              
REMARK   1  AUTH 2 M.MASULLO,V.BOCCHINI                                         
REMARK   1  TITL   PHENYLMETHANESULFONYL FLUORIDE INACTIVATES AN                
REMARK   1  TITL 2 ARCHAEAL SUPEROXIDE DISMUTASE BY CHEMICAL                    
REMARK   1  TITL 3 MODIFICATION OF A SPECIFIC TYROSINE RESIDUE                  
REMARK   1  REF    EUR.J.BIOCHEM.                V. 268  1794 2001              
REMARK   1  REFN                   ISSN 0014-2956                               
REMARK   1  PMID   11248699                                                     
REMARK   1  DOI    10.1046/J.1432-1327.2001.02052.X                             
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.3  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 : MAXIMUM LIKELIHOOD USING AMPLITUDES             
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 22.91                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0                            
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 3370580.24                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 95.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 18643                          
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) : 0.167                           
REMARK   3   FREE R VALUE                     : 0.187                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.1                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 955                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.006                           
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) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.44                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 92.4                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2834                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.208                        
REMARK   3   BIN FREE R VALUE                    : 0.247                        
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.2                          
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 157                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.020                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3342                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 22                                      
REMARK   3   SOLVENT ATOMS            : 173                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 14.9                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.3                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -3.11                                                
REMARK   3    B22 (A**2) : 4.85                                                 
REMARK   3    B33 (A**2) : -1.75                                                
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : -0.41                                                
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.21                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.19                            
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) : 0.25                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.22                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.3                             
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.2                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.74                            
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) : 0.35  ; 0.50                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 0.64  ; 1.00                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.78  ; 3.00                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.91  ; 3.50                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.294185                                             
REMARK   3   BSOL        : 32.1856                                              
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  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : PMS.PAR                                        
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : PMS.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NOTE THAT RESIDUES 1-3 AND 209- -210      
REMARK   3  OF THE COMPLETE SEQUENCE ARE MISSING IN THIS ENTRY DUE TO           
REMARK   3  DISORDER IN THE CRYSTAL. THE NCS USED IN THE REFINEMENT             
REMARK   3  INCLUDED MOLECULE A EXCEPT 19 RESIDUES, THE IRON ION AND 68         
REMARK   3  WATER MOLECULES AND THE CORRESPONDING NCS RELEATED ATOMS. THE       
REMARK   3  RMS DEVIATION FOR THE ATOMS USED FOR NCS IN THE REFINEMENT IS       
REMARK   3  0.006 A.                                                            
REMARK   4                                                                      
REMARK   4 1WB8 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON  01-NOV-04.                 
REMARK 100 THE PDBE ID CODE IS EBI-20803.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-JUL-97                          
REMARK 200  TEMPERATURE           (KELVIN) : 294.0                              
REMARK 200  PH                             : 8.50                               
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 ROTAFLEX RU-2               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54                               
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 : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18647                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 62.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.3                               
REMARK 200  DATA REDUNDANCY                : 4.200                              
REMARK 200  R MERGE                    (I) : 0.09000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.4000                             
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) : 2.36                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.31000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.300                              
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: PDB ENTRY 1ABM                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS WERE GROWN BY VAPOR             
REMARK 280  DIFFUSION IN HANGING DROPS AT 21C IN A 1 TO 1 MIX OF THE            
REMARK 280  RESERVOIR SOLUTION (8% PEG 8000, 0.1 M TRIS/HCL PH 8.5)             
REMARK 280  AND A PROTEIN SOLUTION (2.0 MG/ML SSSOD).                           
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       38.13300            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       62.16200            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       38.13300            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       62.16200            
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 GENERATING THE BIOMOLECULE                                           
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PQS                                                   
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   BIOMT1   2 -1.000000  0.000000  0.000000      -37.72316            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       47.00208            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375      HOH A2069  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B2058  LIES ON A SPECIAL POSITION.                          
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     THR A     1                                                      
REMARK 465     LEU A     2                                                      
REMARK 465     GLN A     3                                                      
REMARK 465     THR A   209                                                      
REMARK 465     LYS A   210                                                      
REMARK 465     THR B     1                                                      
REMARK 465     LEU B     2                                                      
REMARK 465     GLN B     3                                                      
REMARK 465     THR B   209                                                      
REMARK 465     LYS B   210                                                      
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 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    ASN A 154     -153.92     58.57                                   
REMARK 500    ASN A 158        3.85     90.05                                   
REMARK 500    GLU A 162      -23.69     55.01                                   
REMARK 500    TYR A 176      -16.21   -149.26                                   
REMARK 500    LYS A 181     -133.89     55.04                                   
REMARK 500    ASN B 154     -153.95     58.23                                   
REMARK 500    ASN B 158        3.91     89.00                                   
REMARK 500    GLU B 162      -23.96     55.00                                   
REMARK 500    TYR B 176      -16.37   -149.54                                   
REMARK 500    LYS B 181     -133.80     54.78                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 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                              FE A 212  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  84   NE2                                                    
REMARK 620 2 ASP A 170   OD2 116.0                                              
REMARK 620 3 HOH A2077   O    90.8  85.1                                        
REMARK 620 4 HIS A  33   NE2  96.0  90.1 172.9                                  
REMARK 620 5 HIS A 174   NE2 124.5 119.4  90.1  87.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE B 211  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 174   NE2                                                    
REMARK 620 2 HIS B  84   NE2 124.7                                              
REMARK 620 3 ASP B 170   OD2 119.9 115.1                                        
REMARK 620 4 HOH B2065   O    90.1  90.0  84.4                                  
REMARK 620 5 HIS B  33   NE2  88.5  96.2  90.6 173.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  FE A 212                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  FE B 211                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PMS A 213                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PMS B 214                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1WB7   RELATED DB: PDB                                   
REMARK 900  IRON SUPEROXIDE DISMUTASE (FE-SOD) FROM THE                         
REMARK 900   HYPERTHERMOPHILE SULFOLOBUS SOLFATARICUS.                          
REMARK 900  CRYSTAL STRUCTURE OF THE Y41F MUTANT.                               
DBREF  1WB8 A    1   210  UNP    P80857   SODF_SULSO       1    210             
DBREF  1WB8 B    1   210  UNP    P80857   SODF_SULSO       1    210             
SEQRES   1 A  210  THR LEU GLN ILE GLN PHE LYS LYS TYR GLU LEU PRO PRO          
SEQRES   2 A  210  LEU PRO TYR LYS ILE ASP ALA LEU GLU PRO TYR ILE SER          
SEQRES   3 A  210  LYS ASP ILE ILE ASP VAL HIS TYR ASN GLY HIS HIS LYS          
SEQRES   4 A  210  GLY TYR VAL ASN GLY ALA ASN SER LEU LEU GLU ARG LEU          
SEQRES   5 A  210  GLU LYS VAL VAL LYS GLY ASP LEU GLN THR GLY GLN TYR          
SEQRES   6 A  210  ASP ILE GLN GLY ILE ILE ARG GLY LEU THR PHE ASN ILE          
SEQRES   7 A  210  ASN GLY HIS LYS LEU HIS ALA LEU TYR TRP GLU ASN MET          
SEQRES   8 A  210  ALA PRO SER GLY LYS GLY GLY GLY LYS PRO GLY GLY ALA          
SEQRES   9 A  210  LEU ALA ASP LEU ILE ASN LYS GLN TYR GLY SER PHE ASP          
SEQRES  10 A  210  ARG PHE LYS GLN VAL PHE THR GLU THR ALA ASN SER LEU          
SEQRES  11 A  210  PRO GLY THR GLY TRP ALA VAL LEU TYR TYR ASP THR GLU          
SEQRES  12 A  210  SER GLY ASN LEU GLN ILE MET THR PHE GLU ASN HIS PHE          
SEQRES  13 A  210  GLN ASN HIS ILE ALA GLU ILE PRO ILE ILE LEU ILE LEU          
SEQRES  14 A  210  ASP GLU PHE GLU HIS ALA TYR TYR LEU GLN TYR LYS ASN          
SEQRES  15 A  210  LYS ARG ALA ASP TYR VAL ASN ALA TRP TRP ASN VAL VAL          
SEQRES  16 A  210  ASN TRP ASP ALA ALA GLU LYS LYS LEU GLN LYS TYR LEU          
SEQRES  17 A  210  THR LYS                                                      
SEQRES   1 B  210  THR LEU GLN ILE GLN PHE LYS LYS TYR GLU LEU PRO PRO          
SEQRES   2 B  210  LEU PRO TYR LYS ILE ASP ALA LEU GLU PRO TYR ILE SER          
SEQRES   3 B  210  LYS ASP ILE ILE ASP VAL HIS TYR ASN GLY HIS HIS LYS          
SEQRES   4 B  210  GLY TYR VAL ASN GLY ALA ASN SER LEU LEU GLU ARG LEU          
SEQRES   5 B  210  GLU LYS VAL VAL LYS GLY ASP LEU GLN THR GLY GLN TYR          
SEQRES   6 B  210  ASP ILE GLN GLY ILE ILE ARG GLY LEU THR PHE ASN ILE          
SEQRES   7 B  210  ASN GLY HIS LYS LEU HIS ALA LEU TYR TRP GLU ASN MET          
SEQRES   8 B  210  ALA PRO SER GLY LYS GLY GLY GLY LYS PRO GLY GLY ALA          
SEQRES   9 B  210  LEU ALA ASP LEU ILE ASN LYS GLN TYR GLY SER PHE ASP          
SEQRES  10 B  210  ARG PHE LYS GLN VAL PHE THR GLU THR ALA ASN SER LEU          
SEQRES  11 B  210  PRO GLY THR GLY TRP ALA VAL LEU TYR TYR ASP THR GLU          
SEQRES  12 B  210  SER GLY ASN LEU GLN ILE MET THR PHE GLU ASN HIS PHE          
SEQRES  13 B  210  GLN ASN HIS ILE ALA GLU ILE PRO ILE ILE LEU ILE LEU          
SEQRES  14 B  210  ASP GLU PHE GLU HIS ALA TYR TYR LEU GLN TYR LYS ASN          
SEQRES  15 B  210  LYS ARG ALA ASP TYR VAL ASN ALA TRP TRP ASN VAL VAL          
SEQRES  16 B  210  ASN TRP ASP ALA ALA GLU LYS LYS LEU GLN LYS TYR LEU          
SEQRES  17 B  210  THR LYS                                                      
HET     FE  A 212       1                                                       
HET     FE  B 211       1                                                       
HET    PMS  A 213      10                                                       
HET    PMS  B 214      10                                                       
HETNAM      FE FE (III) ION                                                     
HETNAM     PMS BENZYLSULFINIC ACID                                              
FORMUL   3   FE    2(FE 3+)                                                     
FORMUL   5  PMS    2(C7 H8 O2 S)                                                
FORMUL   7  HOH   *173(H2 O1)                                                   
HELIX    1   1 SER A   26  GLY A   36  1                                  11    
HELIX    2   2 GLY A   36  GLY A   58  1                                  23    
HELIX    3   3 ASP A   66  ASN A   90  1                                  25    
HELIX    4   4 GLY A  102  GLY A  114  1                                  13    
HELIX    5   5 SER A  115  SER A  129  1                                  15    
HELIX    6   6 PHE A  172  ALA A  175  5                                   4    
HELIX    7   7 TYR A  176  LYS A  181  1                                   6    
HELIX    8   8 LYS A  183  TRP A  192  1                                  10    
HELIX    9   9 ASN A  196  TYR A  207  1                                  12    
HELIX   10  10 SER B   26  GLY B   36  1                                  11    
HELIX   11  11 GLY B   36  GLY B   58  1                                  23    
HELIX   12  12 ASP B   66  ASN B   90  1                                  25    
HELIX   13  13 GLY B  102  GLY B  114  1                                  13    
HELIX   14  14 SER B  115  SER B  129  1                                  15    
HELIX   15  15 PHE B  172  ALA B  175  5                                   4    
HELIX   16  16 TYR B  176  LYS B  181  1                                   6    
HELIX   17  17 LYS B  183  TRP B  192  1                                  10    
HELIX   18  18 ASN B  196  TYR B  207  1                                  12    
SHEET    1  AA 3 LEU A 147  GLU A 153  0                                        
SHEET    2  AA 3 GLY A 134  TYR A 140 -1  O  TRP A 135   N  PHE A 152           
SHEET    3  AA 3 ILE A 165  ASP A 170 -1  N  ILE A 166   O  LEU A 138           
SHEET    1  BA 3 LEU B 147  GLU B 153  0                                        
SHEET    2  BA 3 GLY B 134  TYR B 140 -1  O  TRP B 135   N  PHE B 152           
SHEET    3  BA 3 ILE B 165  ASP B 170 -1  N  ILE B 166   O  LEU B 138           
LINK         OH  TYR A  41                 S   PMS A 213     1555   1555  1.55  
LINK        FE    FE A 212                 OD2 ASP A 170     1555   1555  1.94  
LINK        FE    FE A 212                 O   HOH A2077     1555   1555  2.22  
LINK        FE    FE A 212                 NE2 HIS A  33     1555   1555  2.16  
LINK        FE    FE A 212                 NE2 HIS A 174     1555   1555  2.12  
LINK        FE    FE A 212                 NE2 HIS A  84     1555   1555  2.17  
LINK         OH  TYR B  41                 S   PMS B 214     1555   1555  1.55  
LINK        FE    FE B 211                 O   HOH B2065     1555   1555  2.24  
LINK        FE    FE B 211                 NE2 HIS B  33     1555   1555  2.14  
LINK        FE    FE B 211                 OD2 ASP B 170     1555   1555  1.95  
LINK        FE    FE B 211                 NE2 HIS B  84     1555   1555  2.19  
LINK        FE    FE B 211                 NE2 HIS B 174     1555   1555  2.10  
CISPEP   1 GLU A   22    PRO A   23          0         0.26                     
CISPEP   2 GLU B   22    PRO B   23          0         0.23                     
SITE     1 AC1  5 HIS A  33  HIS A  84  ASP A 170  HIS A 174                    
SITE     2 AC1  5 HOH A2077                                                     
SITE     1 AC2  5 HIS B  33  HIS B  84  ASP B 170  HIS B 174                    
SITE     2 AC2  5 HOH B2065                                                     
SITE     1 AC3  8 HIS A  37  TYR A  41  PHE A  76  PHE A 172                    
SITE     2 AC3  8 HIS A 174  LEU B 130  GLY B 132  ARG B 184                    
SITE     1 AC4  8 LEU A 130  GLY A 132  ARG A 184  HIS B  37                    
SITE     2 AC4  8 TYR B  41  PHE B  76  PHE B 172  HIS B 174                    
CRYST1   76.266  124.324   60.268  90.00 128.75  90.00 C 1 2 1       8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013112  0.000000  0.010523        0.00000                         
SCALE2      0.000000  0.008043  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.021276        0.00000                         
MTRIX1   1  0.906660 -0.001740  0.421850      -11.57396    1                    
MTRIX2   1 -0.001680 -1.000000 -0.000520       96.02196    1                    
MTRIX3   1  0.421850 -0.000230 -0.906660       52.78307    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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