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Database: PDB
Entry: 1GN3
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Original site: 1GN3 
HEADER    OXIDOREDUCTASE                          02-OCT-01   1GN3              
TITLE     H145Q MUTANT OF MYCOBACTERIUM TUBERCULOSIS IRON-SUPEROXIDE            
TITLE    2 DISMUTASE.                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE;                                      
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: MYCOBACTERIUM TUBERCULOSIS;                     
SOURCE   3 ORGANISM_TAXID: 1773;                                                
SOURCE   4 EXPRESSION_SYSTEM: MYCOBACTERIUM VACCAE;                             
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 1810                                        
KEYWDS    OXIDOREDUCTASE                                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.A.BUNTING,J.B.COOPER,M.O.BADASSO,I.J.TICKLE,M.NEWTON,               
AUTHOR   2 S.P.WOOD,Y.ZHANG,D.B.YOUNG                                           
REVDAT   3   01-SEP-09 1GN3    1       REMARK                                   
REVDAT   2   24-FEB-09 1GN3    1       VERSN                                    
REVDAT   1   05-OCT-01 1GN3    0                                                
JRNL        AUTH   K.A.BUNTING,J.B.COOPER,M.O.BADASSO,I.J.TICKLE,               
JRNL        AUTH 2 M.NEWTON,S.P.WOOD,D.B.YOUNG                                  
JRNL        TITL   ENGINEERING A CHANGE IN THE METAL-ION SPECIFICITY            
JRNL        TITL 2 OF THE IRON-DEPEDENT SUPEROXIDE DISMUTASE FROM               
JRNL        TITL 3 MYCOBACTERIUM TUBERCULOSIS. X-RAY STRUCTURE                  
JRNL        TITL 4 ANALYSIS OF SITE-DIRECTED MUTANTS.                           
JRNL        REF    EUR.J.BIOCHEM.                V. 251   795 1998              
JRNL        REFN                   ISSN 0014-2956                               
JRNL        PMID   9490054                                                      
JRNL        DOI    10.1046/J.1432-1327.1998.2510795.X                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    4.0  ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 4.0                            
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.0                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0                            
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 5069                           
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 + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.168                           
REMARK   3   FREE R VALUE                     : 0.184                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3134                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 2                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
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 OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): NULL          
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.015 ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : 0.045 ; NULL                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : 0.021 ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : 0.019 ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; 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  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1GN3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON  03-OCT-01.                 
REMARK 100 THE PDBE ID CODE IS EBI-8656.                                        
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 293.0                              
REMARK 200  PH                             : 7.00                               
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          : ENRAF-NONIUS FR591                 
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
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 : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 5069                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 4.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 99.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY                : 9.200                              
REMARK 200  R MERGE                    (I) : 0.16300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.22100                            
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: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CCP4                                                  
REMARK 200 STARTING MODEL: PDB ENTRY 1IDS                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS  (%): 48                                         
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM TRIS-HCL PH 7.0,                   
REMARK 280 25% PEG 6000, PROTEIN CONCENTRATION = 3 MG/ML,                       
REMARK 280 4 DEGREES CENTIGRADE.                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       23.30667            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       46.61333            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       46.61333            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       23.30667            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 13260 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 27700 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -86.86 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -0.500000  0.866025  0.000000       -0.00000            
REMARK 350   BIOMT2   2  0.866025  0.500000  0.000000       -0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      -69.92000            
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     MET A     1                                                      
REMARK 465     GLN A   200                                                      
REMARK 465     THR A   201                                                      
REMARK 465     LYS A   202                                                      
REMARK 465     GLY A   203                                                      
REMARK 465     LEU A   204                                                      
REMARK 465     ILE A   205                                                      
REMARK 465     PHE A   206                                                      
REMARK 465     GLY A   207                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLN B   200                                                      
REMARK 465     THR B   201                                                      
REMARK 465     LYS B   202                                                      
REMARK 465     GLY B   203                                                      
REMARK 465     LEU B   204                                                      
REMARK 465     ILE B   205                                                      
REMARK 465     PHE B   206                                                      
REMARK 465     GLY B   207                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500                                                                      
REMARK 500   OD1  ASP A    89     O    GLY B   104     5664      1.98           
REMARK 500   O    GLY B   104     OD1  ASP A    89     5564      1.98           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    TYR A   4   CA  -  C   -  O   ANGL. DEV. = -13.9 DEGREES          
REMARK 500    TYR A   4   CB  -  CG  -  CD1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    TRP A  11   CA  -  C   -  O   ANGL. DEV. =  15.3 DEGREES          
REMARK 500    ASP A  12   CB  -  CG  -  OD1 ANGL. DEV. =  -6.5 DEGREES          
REMARK 500    ASP A  12   CB  -  CG  -  OD2 ANGL. DEV. =  -7.5 DEGREES          
REMARK 500    ASP A  12   OD1 -  CG  -  OD2 ANGL. DEV. =  14.1 DEGREES          
REMARK 500    TRP A  11   CA  -  C   -  N   ANGL. DEV. = -15.0 DEGREES          
REMARK 500    LEU A  27   CB  -  CG  -  CD2 ANGL. DEV. = -11.2 DEGREES          
REMARK 500    LEU A  47   CA  -  CB  -  CG  ANGL. DEV. = -15.0 DEGREES          
REMARK 500    ARG A  51   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    LEU A  70   CB  -  CG  -  CD2 ANGL. DEV. = -13.3 DEGREES          
REMARK 500    LYS A  90   CD  -  CE  -  NZ  ANGL. DEV. =  21.0 DEGREES          
REMARK 500    VAL A 120   CA  -  CB  -  CG1 ANGL. DEV. =  -9.1 DEGREES          
REMARK 500    ASP A 131   CB  -  CG  -  OD1 ANGL. DEV. =  11.6 DEGREES          
REMARK 500    ASP A 131   CB  -  CG  -  OD2 ANGL. DEV. =  -9.3 DEGREES          
REMARK 500    LEU A 133   CA  -  CB  -  CG  ANGL. DEV. = -17.7 DEGREES          
REMARK 500    LYS A 136   O   -  C   -  N   ANGL. DEV. =  10.0 DEGREES          
REMARK 500    ASP A 160   CB  -  CG  -  OD1 ANGL. DEV. =  13.0 DEGREES          
REMARK 500    VAL A 173   CA  -  CB  -  CG2 ANGL. DEV. =  11.4 DEGREES          
REMARK 500    PHE A 181   CG  -  CD2 -  CE2 ANGL. DEV. =  -9.0 DEGREES          
REMARK 500    PHE A 181   CZ  -  CE2 -  CD2 ANGL. DEV. =   8.8 DEGREES          
REMARK 500    VAL A 190   CA  -  CB  -  CG2 ANGL. DEV. = -10.6 DEGREES          
REMARK 500    ARG A 193   NE  -  CZ  -  NH1 ANGL. DEV. =  -7.0 DEGREES          
REMARK 500    ARG A 193   NE  -  CZ  -  NH2 ANGL. DEV. =   8.3 DEGREES          
REMARK 500    TYR B   4   CA  -  C   -  O   ANGL. DEV. = -13.9 DEGREES          
REMARK 500    TYR B   4   CB  -  CG  -  CD1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    TRP B  11   CA  -  C   -  O   ANGL. DEV. =  15.3 DEGREES          
REMARK 500    ASP B  12   CB  -  CG  -  OD1 ANGL. DEV. =  -6.5 DEGREES          
REMARK 500    ASP B  12   CB  -  CG  -  OD2 ANGL. DEV. =  -7.5 DEGREES          
REMARK 500    ASP B  12   OD1 -  CG  -  OD2 ANGL. DEV. =  14.1 DEGREES          
REMARK 500    TRP B  11   CA  -  C   -  N   ANGL. DEV. = -15.0 DEGREES          
REMARK 500    LEU B  27   CB  -  CG  -  CD2 ANGL. DEV. = -11.2 DEGREES          
REMARK 500    LEU B  47   CA  -  CB  -  CG  ANGL. DEV. = -15.0 DEGREES          
REMARK 500    ARG B  51   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    LEU B  70   CB  -  CG  -  CD2 ANGL. DEV. = -13.3 DEGREES          
REMARK 500    LYS B  90   CD  -  CE  -  NZ  ANGL. DEV. =  21.0 DEGREES          
REMARK 500    VAL B 120   CA  -  CB  -  CG1 ANGL. DEV. =  -9.1 DEGREES          
REMARK 500    ASP B 131   CB  -  CG  -  OD1 ANGL. DEV. =  11.7 DEGREES          
REMARK 500    ASP B 131   CB  -  CG  -  OD2 ANGL. DEV. =  -9.3 DEGREES          
REMARK 500    LEU B 133   CA  -  CB  -  CG  ANGL. DEV. = -17.7 DEGREES          
REMARK 500    LYS B 136   O   -  C   -  N   ANGL. DEV. =  10.0 DEGREES          
REMARK 500    ASP B 160   CB  -  CG  -  OD1 ANGL. DEV. =  12.9 DEGREES          
REMARK 500    VAL B 173   CA  -  CB  -  CG2 ANGL. DEV. =  11.4 DEGREES          
REMARK 500    PHE B 181   CG  -  CD2 -  CE2 ANGL. DEV. =  -9.0 DEGREES          
REMARK 500    PHE B 181   CZ  -  CE2 -  CD2 ANGL. DEV. =   8.8 DEGREES          
REMARK 500    VAL B 190   CA  -  CB  -  CG2 ANGL. DEV. = -10.6 DEGREES          
REMARK 500    ARG B 193   NE  -  CZ  -  NH1 ANGL. DEV. =  -7.0 DEGREES          
REMARK 500    ARG B 193   NE  -  CZ  -  NH2 ANGL. DEV. =   8.4 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500 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  31      -75.63   -104.13                                   
REMARK 500    HIS A  56       42.48   -108.29                                   
REMARK 500    ASP A  89     -128.43     56.75                                   
REMARK 500    ASN A 135       51.40     36.75                                   
REMARK 500    ASP A 144     -112.01     52.23                                   
REMARK 500    ASN A 148       26.12    102.14                                   
REMARK 500    LEU A 156      -64.98   -122.12                                   
REMARK 500    HIS A 164        6.62    -68.21                                   
REMARK 500    PHE A 166        1.32   -162.53                                   
REMARK 500    LYS A 171     -133.80     56.95                                   
REMARK 500    LYS B  31      -75.67   -104.13                                   
REMARK 500    HIS B  56       42.53   -108.29                                   
REMARK 500    ASP B  89     -128.47     56.81                                   
REMARK 500    ASN B 135       51.43     36.77                                   
REMARK 500    ASP B 144     -112.00     52.21                                   
REMARK 500    ASN B 148       26.17    102.12                                   
REMARK 500    LEU B 156      -65.01   -122.15                                   
REMARK 500    HIS B 164        6.61    -68.17                                   
REMARK 500    PHE B 166        1.31   -162.55                                   
REMARK 500    LYS B 171     -133.80     56.94                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    LEU A  16        22.3      L          L   OUTSIDE RANGE           
REMARK 500    SER A  21        20.6      L          L   OUTSIDE RANGE           
REMARK 500    ASN A  75        22.4      L          L   OUTSIDE RANGE           
REMARK 500    ASN A 148        22.7      L          L   OUTSIDE RANGE           
REMARK 500    VAL A 175        23.5      L          L   OUTSIDE RANGE           
REMARK 500    LEU B  16        22.2      L          L   OUTSIDE RANGE           
REMARK 500    SER B  21        20.6      L          L   OUTSIDE RANGE           
REMARK 500    ASN B  75        22.4      L          L   OUTSIDE RANGE           
REMARK 500    ASN B 148        22.7      L          L   OUTSIDE RANGE           
REMARK 500    VAL B 175        23.4      L          L   OUTSIDE RANGE           
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 A1200  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  28   NE2                                                    
REMARK 620 2 ASP A 160   OD2  78.5                                              
REMARK 620 3 HIS A 164   NE2  87.2 110.8                                        
REMARK 620 4 HIS A  76   NE2  87.9  92.8 154.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE B1200  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  28   NE2                                                    
REMARK 620 2 ASP B 160   OD2  78.5                                              
REMARK 620 3 HIS B 164   NE2  87.2 110.8                                        
REMARK 620 4 HIS B  76   NE2  87.9  92.9 154.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  FE A1200                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  FE B1200                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1GN2   RELATED DB: PDB                                   
REMARK 900  S123C MUTANT OF THE IRON-SUPEROXIDE                                 
REMARK 900  DISMUTASE FROM MYCOBACTERIUM TUBERCULOSIS.                          
REMARK 900 RELATED ID: 1GN4   RELATED DB: PDB                                   
REMARK 900  H145E MUTANT OF THE IRON-SUPEROXIDE                                 
REMARK 900  DISMUTASE FROM MYCOBACTERIUM TUBERCULOSIS.                          
REMARK 900 RELATED ID: 1GN6   RELATED DB: PDB                                   
REMARK 900  G152A MUTANT OF THE IRON-SUPEROXIDE                                 
REMARK 900  DISMUTASE FROM MYCOBACTERIUM TUBERCULOSIS.                          
REMARK 900 RELATED ID: 1IDS   RELATED DB: PDB                                   
REMARK 900  IRON-DEPENDENT SUPEROXIDE DISMUTASE (FE-                            
REMARK 900  SUPEROXIDE DISMUTASE, FE-SOD)                                       
DBREF  1GN3 A    1   207  UNP    P17670   SODF_MYCTU       1    207             
DBREF  1GN3 B    1   207  UNP    P17670   SODF_MYCTU       1    207             
SEQADV 1GN3 GLN B  145  UNP  P17670    HIS   145 ENGINEERED MUTATION            
SEQRES   1 A  207  MET ALA GLU TYR THR LEU PRO ASP LEU ASP TRP ASP TYR          
SEQRES   2 A  207  GLY ALA LEU GLU PRO HIS ILE SER GLY GLN ILE ASN GLU          
SEQRES   3 A  207  LEU HIS HIS SER LYS HIS HIS ALA THR TYR VAL LYS GLY          
SEQRES   4 A  207  ALA ASN ASP ALA VAL ALA LYS LEU GLU GLU ALA ARG ALA          
SEQRES   5 A  207  LYS GLU ASP HIS SER ALA ILE LEU LEU ASN GLU LYS ASN          
SEQRES   6 A  207  LEU ALA PHE ASN LEU ALA GLY HIS VAL ASN HIS THR ILE          
SEQRES   7 A  207  TRP TRP LYS ASN LEU SER PRO ASN GLY GLY ASP LYS PRO          
SEQRES   8 A  207  THR GLY GLU LEU ALA ALA ALA ILE ALA ASP ALA PHE GLY          
SEQRES   9 A  207  SER PHE ASP LYS PHE ARG ALA GLN PHE HIS ALA ALA ALA          
SEQRES  10 A  207  THR THR VAL GLN GLY SER GLY TRP ALA ALA LEU GLY TRP          
SEQRES  11 A  207  ASP THR LEU GLY ASN LYS LEU LEU ILE PHE GLN VAL TYR          
SEQRES  12 A  207  ASP GLN GLN THR ASN PHE PRO LEU GLY ILE VAL PRO LEU          
SEQRES  13 A  207  LEU LEU LEU ASP MET TRP GLU HIS ALA PHE TYR LEU GLN          
SEQRES  14 A  207  TYR LYS ASN VAL LYS VAL ASP PHE ALA LYS ALA PHE TRP          
SEQRES  15 A  207  ASN VAL VAL ASN TRP ALA ASP VAL GLN SER ARG TYR ALA          
SEQRES  16 A  207  ALA ALA THR SER GLN THR LYS GLY LEU ILE PHE GLY              
SEQRES   1 B  207  MET ALA GLU TYR THR LEU PRO ASP LEU ASP TRP ASP TYR          
SEQRES   2 B  207  GLY ALA LEU GLU PRO HIS ILE SER GLY GLN ILE ASN GLU          
SEQRES   3 B  207  LEU HIS HIS SER LYS HIS HIS ALA THR TYR VAL LYS GLY          
SEQRES   4 B  207  ALA ASN ASP ALA VAL ALA LYS LEU GLU GLU ALA ARG ALA          
SEQRES   5 B  207  LYS GLU ASP HIS SER ALA ILE LEU LEU ASN GLU LYS ASN          
SEQRES   6 B  207  LEU ALA PHE ASN LEU ALA GLY HIS VAL ASN HIS THR ILE          
SEQRES   7 B  207  TRP TRP LYS ASN LEU SER PRO ASN GLY GLY ASP LYS PRO          
SEQRES   8 B  207  THR GLY GLU LEU ALA ALA ALA ILE ALA ASP ALA PHE GLY          
SEQRES   9 B  207  SER PHE ASP LYS PHE ARG ALA GLN PHE HIS ALA ALA ALA          
SEQRES  10 B  207  THR THR VAL GLN GLY SER GLY TRP ALA ALA LEU GLY TRP          
SEQRES  11 B  207  ASP THR LEU GLY ASN LYS LEU LEU ILE PHE GLN VAL TYR          
SEQRES  12 B  207  ASP GLN GLN THR ASN PHE PRO LEU GLY ILE VAL PRO LEU          
SEQRES  13 B  207  LEU LEU LEU ASP MET TRP GLU HIS ALA PHE TYR LEU GLN          
SEQRES  14 B  207  TYR LYS ASN VAL LYS VAL ASP PHE ALA LYS ALA PHE TRP          
SEQRES  15 B  207  ASN VAL VAL ASN TRP ALA ASP VAL GLN SER ARG TYR ALA          
SEQRES  16 B  207  ALA ALA THR SER GLN THR LYS GLY LEU ILE PHE GLY              
HET     FE  A1200       1                                                       
HET     FE  B1200       1                                                       
HETNAM      FE FE (III) ION                                                     
FORMUL   3   FE    2(FE 3+)                                                     
HELIX    1   1 ASP A   12  GLU A   17  5                                   6    
HELIX    2   2 SER A   21  LYS A   31  1                                  11    
HELIX    3   3 LYS A   31  LYS A   53  1                                  23    
HELIX    4   4 ALA A   58  LEU A   83  1                                  26    
HELIX    5   5 THR A   92  GLY A  104  1                                  13    
HELIX    6   6 SER A  105  THR A  119  1                                  15    
HELIX    7   7 TRP A  162  PHE A  166  5                                   5    
HELIX    8   8 VAL A  173  PHE A  181  1                                   9    
HELIX    9   9 TRP A  182  VAL A  184  5                                   3    
HELIX   10  10 ASN A  186  SER A  199  1                                  14    
HELIX   11  11 ASP B   12  GLU B   17  5                                   6    
HELIX   12  12 SER B   21  LYS B   31  1                                  11    
HELIX   13  13 LYS B   31  LYS B   53  1                                  23    
HELIX   14  14 ALA B   58  LEU B   83  1                                  26    
HELIX   15  15 THR B   92  GLY B  104  1                                  13    
HELIX   16  16 SER B  105  THR B  119  1                                  15    
HELIX   17  17 TRP B  162  PHE B  166  5                                   5    
HELIX   18  18 VAL B  173  PHE B  181  1                                   9    
HELIX   19  19 TRP B  182  VAL B  184  5                                   3    
HELIX   20  20 ASN B  186  SER B  199  1                                  14    
SHEET    1  AA 3 LYS A 136  TYR A 143  0                                        
SHEET    2  AA 3 GLY A 124  ASP A 131 -1  O  TRP A 125   N  VAL A 142           
SHEET    3  AA 3 ILE A 153  ASP A 160 -1  O  VAL A 154   N  TRP A 130           
SHEET    1  BA 3 LYS B 136  TYR B 143  0                                        
SHEET    2  BA 3 GLY B 124  ASP B 131 -1  O  TRP B 125   N  VAL B 142           
SHEET    3  BA 3 ILE B 153  ASP B 160 -1  O  VAL B 154   N  TRP B 130           
LINK        FE    FE A1200                 NE2 HIS A  28     1555   1555  2.24  
LINK        FE    FE A1200                 OD2 ASP A 160     1555   1555  1.97  
LINK        FE    FE A1200                 NE2 HIS A 164     1555   1555  2.03  
LINK        FE    FE A1200                 NE2 HIS A  76     1555   1555  1.98  
LINK        FE    FE B1200                 OD2 ASP B 160     1555   1555  1.97  
LINK        FE    FE B1200                 NE2 HIS B 164     1555   1555  2.03  
LINK        FE    FE B1200                 NE2 HIS B  76     1555   1555  1.98  
LINK        FE    FE B1200                 NE2 HIS B  28     1555   1555  2.24  
CISPEP   1 GLU A   17    PRO A   18          0         0.30                     
CISPEP   2 GLU B   17    PRO B   18          0         0.27                     
SITE     1 AC1  4 HIS A  28  HIS A  76  ASP A 160  HIS A 164                    
SITE     1 AC2  4 HIS B  28  HIS B  76  ASP B 160  HIS B 164                    
CRYST1  103.880  103.880   69.920  90.00  90.00 120.00 P 31 2 1      6          
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      0.009626  0.005558  0.000000        0.00000                         
SCALE2      0.000000  0.011116  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014302        0.00000                         
MTRIX1   1 -0.993600 -0.001700  0.112900       45.09800    1                    
MTRIX2   1 -0.006400 -0.997400 -0.071600       69.06800    1                    
MTRIX3   1  0.112700 -0.071900  0.991000       -0.01800    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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