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Database: PDB
Entry: 1WB7
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HEADER    OXIDOREDUCTASE                          31-OCT-04   1WB7              
TITLE     IRON SUPEROXIDE DISMUTASE (FE-SOD) FROM THE HYPERTHERMOPHILE          
TITLE    2 SULFOLOBUS SOLFATARICUS. CRYSTAL STRUCTURE OF THE Y41F MUTANT.       
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 MUTATION: YES                                                        
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 RADICAL   
KEYWDS   2 DISPROPORTIONATION, SULFOLOBUS SOLFTARICUS, THERMOSTABLE             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.A.GOGLIETTINO,F.TANFANI,A.SCIRE,T.URSBY,B.S.ADINOLFI,T.CACCIAMANI,  
AUTHOR   2 E.DE VENDITTIS                                                       
REVDAT   3   17-JAN-18 1WB7    1       REMARK                                   
REVDAT   2   24-FEB-09 1WB7    1       VERSN                                    
REVDAT   1   08-NOV-04 1WB7    0                                                
JRNL        AUTH   M.A.GOGLIETTINO,F.TANFANI,A.SCIRE,T.URSBY,B.S.ADINOLFI,      
JRNL        AUTH 2 T.CACCIAMANI,E.DE VENDITTIS                                  
JRNL        TITL   THE ROLE OF TYR41 AND HIS155 IN THE FUNCTIONAL PROPERTIES OF 
JRNL        TITL 2 SUPEROXIDE DISMUTASE FROM THE ARCHAEON SULFOLOBUS            
JRNL        TITL 3 SOLFATARICUS                                                 
JRNL        REF    BIOCHEMISTRY                  V.  43  2199 2004              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   14979716                                                     
JRNL        DOI    10.1021/BI035661Y                                            
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   T.URSBY,B.S.ADINOLFI,S.AL-KARADAGHI,E.DE VENDITTIS,          
REMARK   1  AUTH 2 V.BOCCHINI                                                   
REMARK   1  TITL   IRON SUPEROXIDE DISMUTASE FROM THE ARCHAEON SULFOLOBUS       
REMARK   1  TITL 2 SOLFATARICUS: ANALYSIS OF STRUCTURE AND THERMOSTABILITY      
REMARK   1  REF    J.MOL.BIOL.                   V. 286   189 1999              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1  PMID   9931259                                                      
REMARK   1  DOI    10.1006/JMBI.1998.2471                                       
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   E.DE VENDITTIS,T.URSBY,R.RULLO,M.A.GOGLIETTINO,M.MASULLO,    
REMARK   1  AUTH 2 V.BOCCHINI                                                   
REMARK   1  TITL   PHENYLMETHANESULFONYL FLUORIDE INACTIVATES AN ARCHAEAL       
REMARK   1  TITL 2 SUPEROXIDE DISMUTASE BY CHEMICAL MODIFICATION OF A SPECIFIC  
REMARK   1  TITL 3 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.    2.24 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) : 2.24                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.07                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1649340.810                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 19994                          
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) : 0.181                           
REMARK   3   FREE R VALUE                     : 0.209                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1023                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.007                           
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) : 2.24                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.38                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.80                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3153                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2120                       
REMARK   3   BIN FREE R VALUE                    : 0.2370                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.30                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 176                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.018                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3340                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 2                                       
REMARK   3   SOLVENT ATOMS            : 224                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 12.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 17.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.08000                                              
REMARK   3    B22 (A**2) : -0.16000                                             
REMARK   3    B33 (A**2) : -0.92000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 2.61000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.23                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.18                            
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) : 0.27                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.20                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.300                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.50                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.760                           
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) : 0.300 ; 0.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 0.540 ; 1.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.440 ; 3.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.270 ; 3.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.38                                                 
REMARK   3   BSOL        : 44.59                                                
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  : 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   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NOTE THAT RESIDUES 1-3 AND 209- -210 OF   
REMARK   3  THE COMPLETE SEQUENCE ARE MISSING IN THIS ENTRY DUE TO DISORDER     
REMARK   3  IN THE CRYSTAL. THE NCS USED IN THE REFINEMENT INCLUDED MOLECULE    
REMARK   3  A EXCEPT 7 RESIDUES, THE IRON ION AND 48 WATER MOLECULES AND THE    
REMARK   3  CORRESPONDING NCS RELEATED ATOMS. THE RMS DEVIATION FOR THE         
REMARK   3  ATOMS USED FOR NCS IN THE REFINEMENT IS 0.005 A.                    
REMARK   4                                                                      
REMARK   4 1WB7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 31-OCT-04.                  
REMARK 100 THE DEPOSITION ID IS D_1290020695.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-OCT-98                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 8.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : MAX II                             
REMARK 200  BEAMLINE                       : I711                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.986                              
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : PT-COATED MIRROR AND SI            
REMARK 200                                   MONOCHROMATOR                      
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19994                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.240                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 60.900                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 4.100                              
REMARK 200  R MERGE                    (I) : 0.09000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.24                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.39                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.26000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: PDB ENTRY 1SSS                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS WERE GROWN BY VAPOR DIFFUSION   
REMARK 280  IN HANGING DROPS AT 21C IN A 1 TO 1 MIX OF THE RESERVOIR            
REMARK 280  SOLUTION (8% PEG 8000, 0.1 M TRIS/HCL PH 8.5) AND A PROTEIN         
REMARK 280  SOLUTION (1.45 MG/ML Y41F-SSSOD, 20 MM TRIS/HCL PH 7.8, 1%          
REMARK 280  GLYCEROL)., PH 8.50                                                 
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       37.59400            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       60.87650            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       37.59400            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       60.87650            
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: 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      -37.18428            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       46.34723            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A2081  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B2085  LIES ON A SPECIAL POSITION.                          
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 ENGINEERED RESIDUE CHAIN A,B TYR 41 PHE                              
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                                                                      
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    GLN A   5     -179.98   -175.31                                   
REMARK 500    ASN A 154     -159.58     63.11                                   
REMARK 500    ASN A 158        1.84     90.91                                   
REMARK 500    GLU A 162      -18.36     57.25                                   
REMARK 500    TYR A 176      -17.74   -150.56                                   
REMARK 500    LYS A 181     -134.50     54.48                                   
REMARK 500    ASN B 154     -159.68     63.33                                   
REMARK 500    ASN B 158        2.01     90.68                                   
REMARK 500    GLU B 162      -18.29     56.97                                   
REMARK 500    TYR B 176      -17.91   -150.70                                   
REMARK 500    LYS B 181     -136.73     55.05                                   
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                              FE A 212  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  33   NE2                                                    
REMARK 620 2 ASP A 170   OD2  88.9                                              
REMARK 620 3 HOH A2088   O   173.8  88.0                                        
REMARK 620 4 HIS A  84   NE2  97.6 118.9  88.6                                  
REMARK 620 5 HIS A 174   NE2  91.1 122.7  86.0 117.8                            
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 ASP B 170   OD2                                                    
REMARK 620 2 HIS B 174   NE2 123.5                                              
REMARK 620 3 HOH B2093   O    88.4  86.6                                        
REMARK 620 4 HIS B  33   NE2  89.0  90.9 174.7                                  
REMARK 620 5 HIS B  84   NE2 118.6 117.5  88.6  96.7                            
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 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1SSS   RELATED DB: PDB                                   
REMARK 900 IRON SUPEROXIDE DISMUTASE (FE-SOD) FROM THE HYPERTHERMOPHILE         
REMARK 900 SULFOLOBUS SOLFATARICUS. 2.3 A RESOLUTION STRUCTURE OF RECOMBINANT   
REMARK 900 PROTEIN WITH A COVALENTLY MODIFIED TYROSINE IN THE ACTIVE SITE.      
REMARK 900 RELATED ID: 1WB8   RELATED DB: PDB                                   
REMARK 900 IRON SUPEROXIDE DISMUTASE (FE-SOD) FROM THE HYPERTHERMOPHILE         
REMARK 900 SULFOLOBUS SOLFATARICUS. 2.3 A RESOLUTION STRUCTURE OF RECOMBINANT   
REMARK 900 PROTEIN WITH A COVALENTLY MODIFIED TYROSIN IN THE ACTIVE SITE.       
DBREF  1WB7 A    1   210  UNP    P80857   SODF_SULSO       1    210             
DBREF  1WB7 B    1   210  UNP    P80857   SODF_SULSO       1    210             
SEQADV 1WB7 PHE A   41  UNP  P80857    TYR    41 ENGINEERED MUTATION            
SEQADV 1WB7 PHE B   41  UNP  P80857    TYR    41 ENGINEERED MUTATION            
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 PHE 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 PHE 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                                                       
HETNAM      FE FE (III) ION                                                     
FORMUL   3   FE    2(FE 3+)                                                     
FORMUL   5  HOH   *224(H2 O)                                                    
HELIX    1   1 SER A   26  GLY A   36  1                                  11    
HELIX    2   2 GLY A   36  LYS A   57  1                                  22    
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  LYS A  206  1                                  11    
HELIX   10  10 SER B   26  GLY B   36  1                                  11    
HELIX   11  11 GLY B   36  LYS B   57  1                                  22    
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  LYS B  206  1                                  11    
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        FE    FE A 212                 NE2 HIS A  33     1555   1555  2.16  
LINK        FE    FE A 212                 OD2 ASP A 170     1555   1555  1.94  
LINK        FE    FE A 212                 O   HOH A2088     1555   1555  2.38  
LINK        FE    FE A 212                 NE2 HIS A  84     1555   1555  2.13  
LINK        FE    FE A 212                 NE2 HIS A 174     1555   1555  2.15  
LINK        FE    FE B 211                 OD2 ASP B 170     1555   1555  1.93  
LINK        FE    FE B 211                 NE2 HIS B 174     1555   1555  2.14  
LINK        FE    FE B 211                 O   HOH B2093     1555   1555  2.36  
LINK        FE    FE B 211                 NE2 HIS B  33     1555   1555  2.17  
LINK        FE    FE B 211                 NE2 HIS B  84     1555   1555  2.15  
CISPEP   1 GLU A   22    PRO A   23          0         0.19                     
CISPEP   2 GLU B   22    PRO B   23          0         0.19                     
SITE     1 AC1  5 HIS A  33  HIS A  84  ASP A 170  HIS A 174                    
SITE     2 AC1  5 HOH A2088                                                     
SITE     1 AC2  5 HIS B  33  HIS B  84  ASP B 170  HIS B 174                    
SITE     2 AC2  5 HOH B2093                                                     
CRYST1   75.188  121.753   59.420  90.00 128.74  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      0.013300  0.000000  0.010671        0.00000                         
SCALE2      0.000000  0.008213  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.021576        0.00000                         
MTRIX1   1  0.907590 -0.000509  0.419858      -11.42300    1                    
MTRIX2   1 -0.000775 -1.000000  0.000463       98.11900    1                    
MTRIX3   1  0.419858 -0.000745 -0.907590       52.09600    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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