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Database: PDB
Entry: 1GN4
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Original site: 1GN4 
HEADER    OXIDOREDUCTASE                          02-OCT-01   1GN4              
TITLE     H145E MUTANT OF MYCOBACTERIUM TUBERCULOSIS IRON-SUPEROXIDE            
TITLE    2 DISMUTASE.                                                           
CAVEAT     1GN4    THERE ARE CHIRALITY ERRORS IN C-ALPHA CENTERS                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE;                                      
COMPND   3 CHAIN: A, B, C, D;                                                   
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, IRON                                                  
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   2   24-FEB-09 1GN4    1       VERSN                                    
REVDAT   1   05-OCT-01 1GN4    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.    2.5  ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CCP4                                                 
REMARK   3   AUTHORS     : NULL                                                 
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.5                            
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.0                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0                            
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 27288                          
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) : 0.172                           
REMARK   3   FREE R VALUE                     : 0.225                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6268                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 4                                       
REMARK   3   SOLVENT ATOMS            : 288                                     
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.012 ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : 0.025 ; 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) : 0.010 ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : 0.012 ; 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 1GN4 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-8655.                                        
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   : 207000                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
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     (%) : 94.4                               
REMARK 200  DATA REDUNDANCY                : 7.600                              
REMARK 200  R MERGE                    (I) : 0.10700                            
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) : 0.29700                            
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: 1IDS                                                 
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): 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 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       53.83000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       36.97000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       51.43000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       36.97000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       53.83000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       51.43000            
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, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400  ENGINEERED MUTATION: HIS(145)GLU                                    
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 465     MET C     1                                                      
REMARK 465     GLN C   200                                                      
REMARK 465     THR C   201                                                      
REMARK 465     LYS C   202                                                      
REMARK 465     GLY C   203                                                      
REMARK 465     LEU C   204                                                      
REMARK 465     ILE C   205                                                      
REMARK 465     PHE C   206                                                      
REMARK 465     GLY C   207                                                      
REMARK 465     MET D     1                                                      
REMARK 465     GLN D   200                                                      
REMARK 465     THR D   201                                                      
REMARK 465     LYS D   202                                                      
REMARK 465     GLY D   203                                                      
REMARK 465     LEU D   204                                                      
REMARK 465     ILE D   205                                                      
REMARK 465     PHE D   206                                                      
REMARK 465     GLY D   207                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    SER A  30   CA    SER A  30   CB      0.147                       
REMARK 500    THR A  35   CB    THR A  35   OG1     0.124                       
REMARK 500    VAL A  37   N     VAL A  37   CA      0.153                       
REMARK 500    LYS A  38   N     LYS A  38   CA      0.129                       
REMARK 500    ALA A  40   CA    ALA A  40   CB      0.129                       
REMARK 500    GLU A  63   N     GLU A  63   CA      0.142                       
REMARK 500    THR A  92   CA    THR A  92   CB      0.171                       
REMARK 500    ALA A  97   N     ALA A  97   CA      0.136                       
REMARK 500    SER A 105   CA    SER A 105   CB      0.104                       
REMARK 500    PHE A 109   N     PHE A 109   CA      0.134                       
REMARK 500    HIS A 114   N     HIS A 114   CA      0.197                       
REMARK 500    ALA A 115   N     ALA A 115   CA      0.127                       
REMARK 500    ALA A 126   N     ALA A 126   CA      0.152                       
REMARK 500    LEU A 157   N     LEU A 157   CA      0.156                       
REMARK 500    MET A 161   CA    MET A 161   CB     -0.138                       
REMARK 500    VAL A 175   N     VAL A 175   CA      0.200                       
REMARK 500    ALA A 178   CA    ALA A 178   CB      0.128                       
REMARK 500    ALA A 180   CA    ALA A 180   CB      0.142                       
REMARK 500    SER A 192   CA    SER A 192   CB      0.105                       
REMARK 500    ARG A 193   N     ARG A 193   CA      0.128                       
REMARK 500    ALA A 195   N     ALA A 195   CA      0.124                       
REMARK 500    ALA A 196   CA    ALA A 196   CB      0.131                       
REMARK 500    ASP B  12   N     ASP B  12   CA      0.148                       
REMARK 500    LEU B  27   N     LEU B  27   CA      0.135                       
REMARK 500    THR B  35   N     THR B  35   CA      0.134                       
REMARK 500    LYS B  38   N     LYS B  38   CA      0.127                       
REMARK 500    ALA B  40   CA    ALA B  40   CB      0.158                       
REMARK 500    ALA B  40   N     ALA B  40   CA      0.140                       
REMARK 500    ASN B  41   N     ASN B  41   CA      0.130                       
REMARK 500    VAL B  44   N     VAL B  44   CA      0.147                       
REMARK 500    LYS B  46   CA    LYS B  46   CB      0.169                       
REMARK 500    LYS B  46   N     LYS B  46   CA      0.159                       
REMARK 500    LEU B  47   N     LEU B  47   CA      0.163                       
REMARK 500    ALA B  50   N     ALA B  50   CA      0.129                       
REMARK 500    GLU B  63   N     GLU B  63   CA      0.164                       
REMARK 500    LYS B  64   N     LYS B  64   CA      0.124                       
REMARK 500    ALA B  67   N     ALA B  67   CA      0.154                       
REMARK 500    PHE B  68   N     PHE B  68   CA      0.138                       
REMARK 500    LEU B  70   N     LEU B  70   CA      0.136                       
REMARK 500    VAL B  74   N     VAL B  74   CA      0.129                       
REMARK 500    HIS B  76   N     HIS B  76   CA      0.177                       
REMARK 500    ILE B  78   N     ILE B  78   CA      0.138                       
REMARK 500    TRP B  79   N     TRP B  79   CA      0.148                       
REMARK 500    ALA B 117   N     ALA B 117   CA      0.166                       
REMARK 500    VAL B 142   N     VAL B 142   CA      0.129                       
REMARK 500    GLU B 145   N     GLU B 145   CA      0.130                       
REMARK 500    TRP B 162   N     TRP B 162   CA      0.120                       
REMARK 500    GLN B 169   N     GLN B 169   CA      0.136                       
REMARK 500    ALA B 178   CA    ALA B 178   CB      0.133                       
REMARK 500    SER C  21   CA    SER C  21   CB      0.104                       
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    GLU A   3   N   -  CA  -  CB  ANGL. DEV. = -11.0 DEGREES          
REMARK 500    ASP A  12   N   -  CA  -  CB  ANGL. DEV. = -14.6 DEGREES          
REMARK 500    ALA A  15   N   -  CA  -  CB  ANGL. DEV. = -11.7 DEGREES          
REMARK 500    ALA A  34   CB  -  CA  -  C   ANGL. DEV. =  -9.4 DEGREES          
REMARK 500    VAL A  37   CG1 -  CB  -  CG2 ANGL. DEV. =   9.6 DEGREES          
REMARK 500    ALA A  40   CB  -  CA  -  C   ANGL. DEV. = -10.5 DEGREES          
REMARK 500    ALA A  43   N   -  CA  -  CB  ANGL. DEV. =  -9.8 DEGREES          
REMARK 500    VAL A  44   N   -  CA  -  CB  ANGL. DEV. = -13.4 DEGREES          
REMARK 500    ALA A  52   N   -  CA  -  CB  ANGL. DEV. = -11.5 DEGREES          
REMARK 500    LYS A  53   CB  -  CA  -  C   ANGL. DEV. = -13.0 DEGREES          
REMARK 500    GLU A  63   N   -  CA  -  CB  ANGL. DEV. = -11.0 DEGREES          
REMARK 500    VAL A  74   CB  -  CA  -  C   ANGL. DEV. = -13.5 DEGREES          
REMARK 500    ASN A  82   CB  -  CA  -  C   ANGL. DEV. = -13.1 DEGREES          
REMARK 500    THR A  92   CA  -  CB  -  CG2 ANGL. DEV. = -16.2 DEGREES          
REMARK 500    THR A  92   CB  -  CA  -  C   ANGL. DEV. = -18.0 DEGREES          
REMARK 500    THR A  92   N   -  CA  -  CB  ANGL. DEV. = -13.8 DEGREES          
REMARK 500    ALA A  96   CB  -  CA  -  C   ANGL. DEV. =  -9.9 DEGREES          
REMARK 500    ASP A 101   N   -  CA  -  CB  ANGL. DEV. = -11.4 DEGREES          
REMARK 500    SER A 105   N   -  CA  -  CB  ANGL. DEV. = -15.3 DEGREES          
REMARK 500    ASP A 107   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    PHE A 109   N   -  CA  -  CB  ANGL. DEV. = -16.2 DEGREES          
REMARK 500    HIS A 114   N   -  CA  -  CB  ANGL. DEV. = -15.1 DEGREES          
REMARK 500    THR A 119   CA  -  CB  -  CG2 ANGL. DEV. =  -9.2 DEGREES          
REMARK 500    TRP A 125   CB  -  CA  -  C   ANGL. DEV. = -17.7 DEGREES          
REMARK 500    ALA A 126   N   -  CA  -  C   ANGL. DEV. = -17.9 DEGREES          
REMARK 500    TRP A 130   N   -  CA  -  CB  ANGL. DEV. = -10.9 DEGREES          
REMARK 500    THR A 132   CA  -  CB  -  CG2 ANGL. DEV. =  -9.1 DEGREES          
REMARK 500    LYS A 136   CB  -  CA  -  C   ANGL. DEV. = -14.7 DEGREES          
REMARK 500    LEU A 138   N   -  CA  -  CB  ANGL. DEV. = -12.5 DEGREES          
REMARK 500    TYR A 143   CA  -  CB  -  CG  ANGL. DEV. =  12.1 DEGREES          
REMARK 500    ASP A 144   CB  -  CG  -  OD1 ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    GLN A 146   N   -  CA  -  C   ANGL. DEV. =  16.5 DEGREES          
REMARK 500    ILE A 153   CA  -  CB  -  CG1 ANGL. DEV. = -14.5 DEGREES          
REMARK 500    LEU A 159   CB  -  CG  -  CD1 ANGL. DEV. =  12.4 DEGREES          
REMARK 500    ASP A 160   CB  -  CG  -  OD1 ANGL. DEV. =  -7.1 DEGREES          
REMARK 500    MET A 161   CG  -  SD  -  CE  ANGL. DEV. =  15.0 DEGREES          
REMARK 500    VAL A 175   N   -  CA  -  CB  ANGL. DEV. = -13.4 DEGREES          
REMARK 500    VAL A 175   C   -  N   -  CA  ANGL. DEV. = -15.1 DEGREES          
REMARK 500    ALA A 178   CB  -  CA  -  C   ANGL. DEV. = -10.8 DEGREES          
REMARK 500    ASN A 186   N   -  CA  -  CB  ANGL. DEV. = -12.1 DEGREES          
REMARK 500    SER A 192   N   -  CA  -  CB  ANGL. DEV. =  -9.8 DEGREES          
REMARK 500    ALA A 195   N   -  CA  -  CB  ANGL. DEV. = -11.7 DEGREES          
REMARK 500    ALA A 196   N   -  CA  -  CB  ANGL. DEV. =  -9.8 DEGREES          
REMARK 500    THR A 198   CA  -  CB  -  CG2 ANGL. DEV. =  -9.6 DEGREES          
REMARK 500    ASP B  10   CB  -  CA  -  C   ANGL. DEV. = -12.4 DEGREES          
REMARK 500    TRP B  11   CB  -  CA  -  C   ANGL. DEV. =  13.5 DEGREES          
REMARK 500    LEU B  27   N   -  CA  -  CB  ANGL. DEV. = -12.2 DEGREES          
REMARK 500    THR B  35   CA  -  CB  -  CG2 ANGL. DEV. = -11.1 DEGREES          
REMARK 500    TYR B  36   N   -  CA  -  CB  ANGL. DEV. = -12.0 DEGREES          
REMARK 500    ALA B  40   N   -  CA  -  CB  ANGL. DEV. = -17.8 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     179 ANGLE DEVIATIONS                              
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    ASP A  10       30.33    -92.11                                   
REMARK 500    ALA A  15       -9.66    -59.56                                   
REMARK 500    ASN A  25      -37.03    -36.77                                   
REMARK 500    LYS A  31      -53.23   -128.41                                   
REMARK 500    HIS A  56       32.47    -93.09                                   
REMARK 500    SER A  84      137.96   -173.56                                   
REMARK 500    ASP A  89     -149.37     82.69                                   
REMARK 500    ASN A 135       72.94     47.45                                   
REMARK 500    ASP A 144     -121.57     63.84                                   
REMARK 500    ASN A 148       35.74     80.24                                   
REMARK 500    PHE A 166      -15.24   -155.97                                   
REMARK 500    LYS A 171     -126.25     61.97                                   
REMARK 500    ASP B  89     -142.58     68.18                                   
REMARK 500    ASP B 144     -121.73     64.06                                   
REMARK 500    ASN B 148       42.86     88.80                                   
REMARK 500    PHE B 166       -9.72   -162.80                                   
REMARK 500    LYS B 171     -131.90     51.63                                   
REMARK 500    ALA B 178        3.37    -62.38                                   
REMARK 500    LYS C  31      -74.71   -100.94                                   
REMARK 500    SER C  84      139.33   -174.86                                   
REMARK 500    ASP C  89     -119.31     93.03                                   
REMARK 500    ASP C 144     -121.07     60.85                                   
REMARK 500    GLN C 146       48.20   -143.88                                   
REMARK 500    ASN C 148       32.47     79.23                                   
REMARK 500    PHE C 166      -21.00   -145.22                                   
REMARK 500    LYS C 171     -140.37     51.49                                   
REMARK 500    LYS D  31      -74.61    -90.28                                   
REMARK 500    ASP D  89     -122.76     70.06                                   
REMARK 500    ASN D 135       63.48     33.14                                   
REMARK 500    ASP D 144     -121.00     63.33                                   
REMARK 500    ASN D 148       36.02     88.56                                   
REMARK 500    LYS D 171     -116.47     51.31                                   
REMARK 500    THR D 198       43.01    -95.21                                   
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    ASP A  12        47.3      L          L   OUTSIDE RANGE           
REMARK 500    ASN A  41        23.0      L          L   OUTSIDE RANGE           
REMARK 500    SER A  57        20.1      L          L   OUTSIDE RANGE           
REMARK 500    PRO A  91        46.1      L          L   OUTSIDE RANGE           
REMARK 500    ALA A  97        45.7      L          L   OUTSIDE RANGE           
REMARK 500    PHE A 109        48.7      L          L   OUTSIDE RANGE           
REMARK 500    HIS A 114        46.7      L          L   OUTSIDE RANGE           
REMARK 500    LEU A 128        46.7      L          L   OUTSIDE RANGE           
REMARK 500    LEU A 138        50.0      L          L   OUTSIDE RANGE           
REMARK 500    ILE A 139        45.6      L          L   OUTSIDE RANGE           
REMARK 500    ASP A 144        22.9      L          L   OUTSIDE RANGE           
REMARK 500    GLU A 145        45.1      L          L   OUTSIDE RANGE           
REMARK 500    ASN A 148        21.8      L          L   OUTSIDE RANGE           
REMARK 500    MET A 161        17.5      L          L   OUTSIDE RANGE           
REMARK 500    VAL A 175        46.0      L          L   OUTSIDE RANGE           
REMARK 500    VAL A 184        19.5      L          L   OUTSIDE RANGE           
REMARK 500    ASN A 186        48.6      L          L   OUTSIDE RANGE           
REMARK 500    SER A 199        23.1      L          L   OUTSIDE RANGE           
REMARK 500    TYR B   4        45.1      L          L   OUTSIDE RANGE           
REMARK 500    LEU B   9        46.3      L          L   OUTSIDE RANGE           
REMARK 500    TRP B  11        24.5      L          L   OUTSIDE RANGE           
REMARK 500    ASP B  12        45.4      L          L   OUTSIDE RANGE           
REMARK 500    LEU B  16        23.3      L          L   OUTSIDE RANGE           
REMARK 500    LEU B  27        48.3      L          L   OUTSIDE RANGE           
REMARK 500    TYR B  36        45.1      L          L   OUTSIDE RANGE           
REMARK 500    ALA B  40        47.7      L          L   OUTSIDE RANGE           
REMARK 500    VAL B  44        46.7      L          L   OUTSIDE RANGE           
REMARK 500    LYS B  46        45.2      L          L   OUTSIDE RANGE           
REMARK 500    LEU B  47        48.9      L          L   OUTSIDE RANGE           
REMARK 500    SER B  57        23.0      L          L   OUTSIDE RANGE           
REMARK 500    GLU B  94        22.5      L          L   OUTSIDE RANGE           
REMARK 500    ILE B 139        45.9      L          L   OUTSIDE RANGE           
REMARK 500    TYR B 143        47.0      L          L   OUTSIDE RANGE           
REMARK 500    ASN B 148        22.7      L          L   OUTSIDE RANGE           
REMARK 500    LEU B 158        46.5      L          L   OUTSIDE RANGE           
REMARK 500    GLU B 163        22.7      L          L   OUTSIDE RANGE           
REMARK 500    VAL B 173        22.2      L          L   OUTSIDE RANGE           
REMARK 500    ALA C  15        23.7      L          L   OUTSIDE RANGE           
REMARK 500    ILE C  20        45.6      L          L   OUTSIDE RANGE           
REMARK 500    ALA C  40        47.9      L          L   OUTSIDE RANGE           
REMARK 500    ASP C  55        49.0      L          L   OUTSIDE RANGE           
REMARK 500    LEU C  66        45.4      L          L   OUTSIDE RANGE           
REMARK 500    PHE C 109        48.2      L          L   OUTSIDE RANGE           
REMARK 500    LEU C 138        45.3      L          L   OUTSIDE RANGE           
REMARK 500    LEU C 157        45.6      L          L   OUTSIDE RANGE           
REMARK 500    TRP C 162        45.2      L          L   OUTSIDE RANGE           
REMARK 500    TYR C 167        18.2      L          L   OUTSIDE RANGE           
REMARK 500    LYS C 171        22.1      L          L   OUTSIDE RANGE           
REMARK 500    LYS C 174        21.7      L          L   OUTSIDE RANGE           
REMARK 500    PHE C 177        47.9      L          L   OUTSIDE RANGE           
REMARK 500    ASN C 186        47.5      L          L   OUTSIDE RANGE           
REMARK 500    TYR D   4        47.0      L          L   OUTSIDE RANGE           
REMARK 500    ALA D  15        23.1      L          L   OUTSIDE RANGE           
REMARK 500    SER D  30        21.4      L          L   OUTSIDE RANGE           
REMARK 500    HIS D  73        45.1      L          L   OUTSIDE RANGE           
REMARK 500    ALA D 102        12.7      L          L   OUTSIDE RANGE           
REMARK 500    ALA D 111        47.7      L          L   OUTSIDE RANGE           
REMARK 500    GLN D 121        52.1      L          L   OUTSIDE RANGE           
REMARK 500    GLN D 141        51.8      L          L   OUTSIDE RANGE           
REMARK 500    ASN D 148        20.6      L          L   OUTSIDE RANGE           
REMARK 500    MET D 161        -0.9      L          D   EXPECTING SP3           
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                              MN A1200  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  76   NE2                                                    
REMARK 620 2 HIS A  28   NE2  85.1                                              
REMARK 620 3 ASP A 160   OD2 107.2  88.7                                        
REMARK 620 4 HIS A 164   NE2 129.6  91.5 123.1                                  
REMARK 620 5 HOH A2070   O    91.7 176.4  90.7  91.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN B1200  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B2081   O                                                      
REMARK 620 2 ASP B 160   OD2 112.6                                              
REMARK 620 3 HIS B  76   NE2  84.3 108.1                                        
REMARK 620 4 HIS B 164   NE2  80.9 122.4 129.3                                  
REMARK 620 5 HIS B  28   NE2 157.5  87.5  79.7  97.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN C1200  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  28   NE2                                                    
REMARK 620 2 ASP C 160   OD2  89.2                                              
REMARK 620 3 HIS C  76   NE2  86.1 116.5                                        
REMARK 620 4 HIS C 164   NE2  87.7 112.4 130.6                                  
REMARK 620 5 HOH C2069   O   174.3  85.4  97.7  92.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN D1200  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D  28   NE2                                                    
REMARK 620 2 HIS D  76   NE2  91.2                                              
REMARK 620 3 HIS D 164   NE2  84.1 132.9                                        
REMARK 620 4 ASP D 160   OD2  82.6 122.5 103.3                                  
REMARK 620 5 HOH D2068   O   169.0  79.0  99.0 106.7                            
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  MN A1200                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MN B1200                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MN C1200                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MN D1200                 
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: 1GN3   RELATED DB: PDB                                   
REMARK 900  H145Q MUTANT OF MYCOBACTERIUM TUBERCULOSIS                          
REMARK 900  IRON-SUPEROXIDE DISMUTASE.                                          
REMARK 900 RELATED ID: 1GN6   RELATED DB: PDB                                   
REMARK 900  G152A MUTANT OF MYCOBACTERIUM TUBERCULOSIS                          
REMARK 900  IRON-SUPEROXIDE DISMUTASE.                                          
REMARK 900 RELATED ID: 1IDS   RELATED DB: PDB                                   
REMARK 900  IRON-DEPENDENT SUPEROXIDE DISMUTASE (FE-                            
REMARK 900  SUPEROXIDE DISMUTASE, FE-SOD)                                       
DBREF  1GN4 A    1   207  UNP    P17670   SODF_MYCTU       1    207             
DBREF  1GN4 B    1   207  UNP    P17670   SODF_MYCTU       1    207             
DBREF  1GN4 C    1   207  UNP    P17670   SODF_MYCTU       1    207             
DBREF  1GN4 D    1   207  UNP    P17670   SODF_MYCTU       1    207             
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 GLU 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 GLU 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              
SEQRES   1 C  207  MET ALA GLU TYR THR LEU PRO ASP LEU ASP TRP ASP TYR          
SEQRES   2 C  207  GLY ALA LEU GLU PRO HIS ILE SER GLY GLN ILE ASN GLU          
SEQRES   3 C  207  LEU HIS HIS SER LYS HIS HIS ALA THR TYR VAL LYS GLY          
SEQRES   4 C  207  ALA ASN ASP ALA VAL ALA LYS LEU GLU GLU ALA ARG ALA          
SEQRES   5 C  207  LYS GLU ASP HIS SER ALA ILE LEU LEU ASN GLU LYS ASN          
SEQRES   6 C  207  LEU ALA PHE ASN LEU ALA GLY HIS VAL ASN HIS THR ILE          
SEQRES   7 C  207  TRP TRP LYS ASN LEU SER PRO ASN GLY GLY ASP LYS PRO          
SEQRES   8 C  207  THR GLY GLU LEU ALA ALA ALA ILE ALA ASP ALA PHE GLY          
SEQRES   9 C  207  SER PHE ASP LYS PHE ARG ALA GLN PHE HIS ALA ALA ALA          
SEQRES  10 C  207  THR THR VAL GLN GLY SER GLY TRP ALA ALA LEU GLY TRP          
SEQRES  11 C  207  ASP THR LEU GLY ASN LYS LEU LEU ILE PHE GLN VAL TYR          
SEQRES  12 C  207  ASP GLU GLN THR ASN PHE PRO LEU GLY ILE VAL PRO LEU          
SEQRES  13 C  207  LEU LEU LEU ASP MET TRP GLU HIS ALA PHE TYR LEU GLN          
SEQRES  14 C  207  TYR LYS ASN VAL LYS VAL ASP PHE ALA LYS ALA PHE TRP          
SEQRES  15 C  207  ASN VAL VAL ASN TRP ALA ASP VAL GLN SER ARG TYR ALA          
SEQRES  16 C  207  ALA ALA THR SER GLN THR LYS GLY LEU ILE PHE GLY              
SEQRES   1 D  207  MET ALA GLU TYR THR LEU PRO ASP LEU ASP TRP ASP TYR          
SEQRES   2 D  207  GLY ALA LEU GLU PRO HIS ILE SER GLY GLN ILE ASN GLU          
SEQRES   3 D  207  LEU HIS HIS SER LYS HIS HIS ALA THR TYR VAL LYS GLY          
SEQRES   4 D  207  ALA ASN ASP ALA VAL ALA LYS LEU GLU GLU ALA ARG ALA          
SEQRES   5 D  207  LYS GLU ASP HIS SER ALA ILE LEU LEU ASN GLU LYS ASN          
SEQRES   6 D  207  LEU ALA PHE ASN LEU ALA GLY HIS VAL ASN HIS THR ILE          
SEQRES   7 D  207  TRP TRP LYS ASN LEU SER PRO ASN GLY GLY ASP LYS PRO          
SEQRES   8 D  207  THR GLY GLU LEU ALA ALA ALA ILE ALA ASP ALA PHE GLY          
SEQRES   9 D  207  SER PHE ASP LYS PHE ARG ALA GLN PHE HIS ALA ALA ALA          
SEQRES  10 D  207  THR THR VAL GLN GLY SER GLY TRP ALA ALA LEU GLY TRP          
SEQRES  11 D  207  ASP THR LEU GLY ASN LYS LEU LEU ILE PHE GLN VAL TYR          
SEQRES  12 D  207  ASP GLU GLN THR ASN PHE PRO LEU GLY ILE VAL PRO LEU          
SEQRES  13 D  207  LEU LEU LEU ASP MET TRP GLU HIS ALA PHE TYR LEU GLN          
SEQRES  14 D  207  TYR LYS ASN VAL LYS VAL ASP PHE ALA LYS ALA PHE TRP          
SEQRES  15 D  207  ASN VAL VAL ASN TRP ALA ASP VAL GLN SER ARG TYR ALA          
SEQRES  16 D  207  ALA ALA THR SER GLN THR LYS GLY LEU ILE PHE GLY              
HET     MN  A1200       1                                                       
HET     MN  B1200       1                                                       
HET     MN  C1200       1                                                       
HET     MN  D1200       1                                                       
HETNAM      MN MANGANESE (II) ION                                               
FORMUL   5   MN    4(MN 2+)                                                     
FORMUL   9  HOH   *288(H2 O1)                                                   
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  ASN A   82  1                                  25    
HELIX    5   5 GLY A   93  GLY A  104  1                                  12    
HELIX    6   6 SER A  105  THR A  119  1                                  15    
HELIX    7   7 TRP A  162  ALA A  165  5                                   4    
HELIX    8   8 PHE A  166  LYS A  171  1                                   6    
HELIX    9   9 VAL A  173  PHE A  181  1                                   9    
HELIX   10  10 TRP A  182  VAL A  184  5                                   3    
HELIX   11  11 ASN A  186  THR A  198  1                                  13    
HELIX   12  12 SER B   21  HIS B   29  1                                   9    
HELIX   13  13 LYS B   31  GLU B   54  1                                  24    
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  ALA B  165  5                                   4    
HELIX   18  18 PHE B  166  LYS B  171  1                                   6    
HELIX   19  19 VAL B  173  PHE B  181  1                                   9    
HELIX   20  20 TRP B  182  VAL B  184  5                                   3    
HELIX   21  21 ASN B  186  THR B  198  1                                  13    
HELIX   22  22 ASP C   12  GLU C   17  5                                   6    
HELIX   23  23 SER C   21  LYS C   31  1                                  11    
HELIX   24  24 LYS C   31  LYS C   53  1                                  23    
HELIX   25  25 ALA C   58  ASN C   82  1                                  25    
HELIX   26  26 GLY C   93  GLY C  104  1                                  12    
HELIX   27  27 SER C  105  THR C  119  1                                  15    
HELIX   28  28 TRP C  162  ALA C  165  5                                   4    
HELIX   29  29 PHE C  166  LYS C  171  1                                   6    
HELIX   30  30 VAL C  173  TRP C  182  1                                  10    
HELIX   31  31 ASN C  186  THR C  198  1                                  13    
HELIX   32  32 SER D   21  LYS D   31  1                                  11    
HELIX   33  33 LYS D   31  GLU D   54  1                                  24    
HELIX   34  34 ALA D   58  ASN D   82  1                                  25    
HELIX   35  35 GLY D   93  PHE D  103  1                                  11    
HELIX   36  36 SER D  105  THR D  118  1                                  14    
HELIX   37  37 TRP D  162  ALA D  165  5                                   4    
HELIX   38  38 PHE D  166  LYS D  171  1                                   6    
HELIX   39  39 VAL D  173  TRP D  182  1                                  10    
HELIX   40  40 ASN D  186  THR D  198  1                                  13    
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 VAL B 154  ASP B 160 -1  O  VAL B 154   N  TRP B 130           
SHEET    1  CA 3 LYS C 136  TYR C 143  0                                        
SHEET    2  CA 3 GLY C 124  ASP C 131 -1  O  TRP C 125   N  VAL C 142           
SHEET    3  CA 3 VAL C 154  ASP C 160 -1  O  VAL C 154   N  TRP C 130           
SHEET    1  DA 3 LYS D 136  TYR D 143  0                                        
SHEET    2  DA 3 GLY D 124  ASP D 131 -1  O  TRP D 125   N  VAL D 142           
SHEET    3  DA 3 VAL D 154  ASP D 160 -1  O  VAL D 154   N  TRP D 130           
LINK        MN    MN A1200                 NE2 HIS A  76     1555   1555  2.35  
LINK        MN    MN A1200                 NE2 HIS A  28     1555   1555  2.33  
LINK        MN    MN A1200                 OD2 ASP A 160     1555   1555  2.02  
LINK        MN    MN A1200                 NE2 HIS A 164     1555   1555  2.17  
LINK        MN    MN A1200                 O   HOH A2070     1555   1555  2.21  
LINK        MN    MN B1200                 O   HOH B2081     1555   1555  2.01  
LINK        MN    MN B1200                 OD2 ASP B 160     1555   1555  1.99  
LINK        MN    MN B1200                 NE2 HIS B  76     1555   1555  2.39  
LINK        MN    MN B1200                 NE2 HIS B 164     1555   1555  2.14  
LINK        MN    MN B1200                 NE2 HIS B  28     1555   1555  2.25  
LINK        MN    MN C1200                 OD2 ASP C 160     1555   1555  1.98  
LINK        MN    MN C1200                 NE2 HIS C  76     1555   1555  2.14  
LINK        MN    MN C1200                 NE2 HIS C 164     1555   1555  2.35  
LINK        MN    MN C1200                 O   HOH C2069     1555   1555  1.86  
LINK        MN    MN C1200                 NE2 HIS C  28     1555   1555  2.31  
LINK        MN    MN D1200                 NE2 HIS D  76     1555   1555  2.18  
LINK        MN    MN D1200                 NE2 HIS D 164     1555   1555  2.37  
LINK        MN    MN D1200                 OD2 ASP D 160     1555   1555  2.03  
LINK        MN    MN D1200                 O   HOH D2068     1555   1555  2.09  
LINK        MN    MN D1200                 NE2 HIS D  28     1555   1555  2.55  
CISPEP   1 GLU A   17    PRO A   18          0         0.10                     
CISPEP   2 GLU B   17    PRO B   18          0         1.20                     
CISPEP   3 GLU C   17    PRO C   18          0         1.08                     
CISPEP   4 GLU D   17    PRO D   18          0        -1.34                     
SITE     1 AC1  5 HIS A  28  HIS A  76  ASP A 160  HIS A 164                    
SITE     2 AC1  5 HOH A2070                                                     
SITE     1 AC2  5 HIS B  28  HIS B  76  ASP B 160  HIS B 164                    
SITE     2 AC2  5 HOH B2081                                                     
SITE     1 AC3  5 HIS C  28  HIS C  76  ASP C 160  HIS C 164                    
SITE     2 AC3  5 HOH C2069                                                     
SITE     1 AC4  5 HIS D  28  HIS D  76  ASP D 160  HIS D 164                    
SITE     2 AC4  5 HOH D2068                                                     
CRYST1  107.660  102.860   73.940  90.00  90.00  90.00 P 21 21 21    4          
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      0.009288  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009722  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013524        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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