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Database: PDB
Entry: 1ISA
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HEADER    OXIDOREDUCTASE(SUPEROXIDE ACCEPTOR)     12-JUL-94   1ISA              
TITLE     STRUCTURE-FUNCTION IN E. COLI IRON SUPEROXIDE DISMUTASE:              
TITLE    2 COMPARISONS WITH THE MANGANESE ENZYME FROM T. THERMOPHILUS           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: IRON(II) SUPEROXIDE DISMUTASE;                             
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 1.15.1.1;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 EXPRESSION_SYSTEM_STRAIN: K12                                        
KEYWDS    OXIDOREDUCTASE(SUPEROXIDE ACCEPTOR)                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.S.LAH,M.DIXON,K.A.PATTRIDGE,W.C.STALLINGS,J.A.FEE,                  
AUTHOR   2 M.L.LUDWIG                                                           
REVDAT   2   24-FEB-09 1ISA    1       VERSN                                    
REVDAT   1   30-SEP-94 1ISA    0                                                
JRNL        AUTH   M.S.LAH,M.M.DIXON,K.A.PATTRIDGE,W.C.STALLINGS,               
JRNL        AUTH 2 J.A.FEE,M.L.LUDWIG                                           
JRNL        TITL   STRUCTURE-FUNCTION IN ESCHERICHIA COLI IRON                  
JRNL        TITL 2 SUPEROXIDE DISMUTASE: COMPARISONS WITH THE                   
JRNL        TITL 3 MANGANESE ENZYME FROM THERMUS THERMOPHILUS.                  
JRNL        REF    BIOCHEMISTRY                  V.  34  1646 1995              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   7849024                                                      
JRNL        DOI    10.1021/BI00005A021                                          
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   W.C.STALLINGS,C.BULL,J.A.FEE,M.S.LAH,M.L.LUDWIG              
REMARK   1  TITL   IRON AND MANGANESE SUPEROXIDE DISMUTASES:                    
REMARK   1  TITL 2 CATALYTIC INFERENCES FROM THE STRUCTURES                     
REMARK   1  EDIT   J.G.SCANDALIOS                                               
REMARK   1  REF    MOLECULAR BIOLOGY OF FREE              193 1992              
REMARK   1  REF  2 RADICAL SCAVENGING SYSTEMS                                   
REMARK   1  PUBL   COLD SPRING HARBOR LAB.PRESS, PLAINVIEW,N.Y.                 
REMARK   1  REFN                                                                
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   A.CARLIOZ,M.L.LUDWIG,W.C.STALLINGS,J.A.FEE,                  
REMARK   1  AUTH 2 H.M.STEINMAN,D.TOUATI                                        
REMARK   1  TITL   IRON SUPEROXIDE DISMUTASE: NUCLEOTIDE SEQUENCE OF            
REMARK   1  TITL 2 THE GENE FROM ESCHERICHIA COLI K12 AND CORRELATION           
REMARK   1  TITL 3 WITH CRYSTAL STRUCTURES                                      
REMARK   1  REF    J.BIOL.CHEM.                  V. 263  1555 1988              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR                                               
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 37923                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.188                           
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3006                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 2                                       
REMARK   3   SOLVENT ATOMS            : 236                                     
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  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.013                           
REMARK   3   BOND ANGLES            (DEGREES) : 2.74                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1ISA COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : NULL                               
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
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) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.45                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.59                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
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       40.77500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       35.76500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       37.54000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       35.76500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       40.77500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       37.54000            
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 300 REMARK:                                                              
REMARK 300 THE TRANSFORMATION PRESENTED ON *MTRIX* RECORDS BELOW WILL           
REMARK 300 YIELD APPROXIMATE COORDINATES FOR CHAIN *B* WHEN APPLIED TO          
REMARK 300 CHAIN *A*.                                                           
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1840 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16440 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 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 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    HIS A  17   NE2   HIS A  17   CD2    -0.075                       
REMARK 500    HIS A  30   NE2   HIS A  30   CD2    -0.068                       
REMARK 500    HIS A 176   NE2   HIS A 176   CD2    -0.069                       
REMARK 500    HIS B  17   NE2   HIS B  17   CD2    -0.071                       
REMARK 500    HIS B  31   NE2   HIS B  31   CD2    -0.073                       
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    ARG A  57   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    TRP A  71   CD1 -  CG  -  CD2 ANGL. DEV. =   7.3 DEGREES          
REMARK 500    TRP A  71   CG  -  CD1 -  NE1 ANGL. DEV. =  -6.2 DEGREES          
REMARK 500    TRP A  71   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.9 DEGREES          
REMARK 500    TRP A  77   CD1 -  CG  -  CD2 ANGL. DEV. =   5.2 DEGREES          
REMARK 500    TRP A  77   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    TRP A 122   CD1 -  CG  -  CD2 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    TRP A 122   CE2 -  CD2 -  CG  ANGL. DEV. =  -4.9 DEGREES          
REMARK 500    TRP A 124   CD1 -  CG  -  CD2 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    TRP A 124   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    TRP A 158   CD1 -  CG  -  CD2 ANGL. DEV. =   5.2 DEGREES          
REMARK 500    TRP A 158   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.0 DEGREES          
REMARK 500    ARG A 167   NE  -  CZ  -  NH1 ANGL. DEV. =   3.2 DEGREES          
REMARK 500    TRP A 178   CD1 -  CG  -  CD2 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    TRP A 178   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.0 DEGREES          
REMARK 500    TRP A 183   CD1 -  CG  -  CD2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    TRP A 183   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    ARG B  57   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG B  57   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    TRP B  71   CD1 -  CG  -  CD2 ANGL. DEV. =   7.2 DEGREES          
REMARK 500    TRP B  71   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.0 DEGREES          
REMARK 500    TRP B  77   CD1 -  CG  -  CD2 ANGL. DEV. =   6.6 DEGREES          
REMARK 500    TRP B  77   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.2 DEGREES          
REMARK 500    TRP B 122   CD1 -  CG  -  CD2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    TRP B 122   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    TRP B 124   CD1 -  CG  -  CD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    TRP B 124   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    TRP B 158   CD1 -  CG  -  CD2 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    TRP B 158   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.2 DEGREES          
REMARK 500    TRP B 178   CD1 -  CG  -  CD2 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    TRP B 178   CE2 -  CD2 -  CG  ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    TRP B 183   CD1 -  CG  -  CD2 ANGL. DEV. =   6.4 DEGREES          
REMARK 500    TRP B 183   CE2 -  CD2 -  CG  ANGL. DEV. =  -6.1 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                                                                      
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    ALA A  84     -140.46   -138.77                                   
REMARK 500    ASN A 140     -104.02     53.42                                   
REMARK 500    ARG A 167     -125.57     45.23                                   
REMARK 500    ALA A 191       75.83   -115.78                                   
REMARK 500    ALA B  84     -136.95   -136.48                                   
REMARK 500    ASN B 140     -108.27     52.90                                   
REMARK 500    ARG B 167     -127.84     53.38                                   
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                             FE2 A 193  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 156   OD2                                                    
REMARK 620 2 HOH A 194   O    89.0                                              
REMARK 620 3 HIS A 160   NE2 121.6  90.0                                        
REMARK 620 4 HIS A  26   NE2  84.9 173.9  93.0                                  
REMARK 620 5 HIS A  73   NE2 111.4  87.2 126.9  95.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FE2 B 193  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  73   NE2                                                    
REMARK 620 2 ASP B 156   OD2 114.3                                              
REMARK 620 3 HIS B 160   NE2 126.2 119.4                                        
REMARK 620 4 HOH B 194   O    87.2  89.2  90.6                                  
REMARK 620 5 HIS B  26   NE2  95.4  85.0  92.0 174.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 650                                                                      
REMARK 650 HELIX                                                                
REMARK 650 ASSIGNMENTS OF SECONDARY STRUCTURE ARE BASED ON THE                  
REMARK 650 ALGORITHM OF KABSCH AND SANDER.  EXCEPTIONS: THE FIRST               
REMARK 650 HELIX HAS A KINK NEAR RESIDUE 28; SUCCESSIVE 3/10 TURNS              
REMARK 650 ARE GIVEN PRIORITY OVER SHORT HELICES.                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: FEA                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800 SITE_IDENTIFIER: FEB                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: NULL                                               
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 A 193                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 B 193                 
DBREF  1ISA A    1   192  UNP    P09157   SODF_ECOLI       1    192             
DBREF  1ISA B    1   192  UNP    P09157   SODF_ECOLI       1    192             
SEQRES   1 A  192  SER PHE GLU LEU PRO ALA LEU PRO TYR ALA LYS ASP ALA          
SEQRES   2 A  192  LEU ALA PRO HIS ILE SER ALA GLU THR ILE GLU TYR HIS          
SEQRES   3 A  192  TYR GLY LYS HIS HIS GLN THR TYR VAL THR ASN LEU ASN          
SEQRES   4 A  192  ASN LEU ILE LYS GLY THR ALA PHE GLU GLY LYS SER LEU          
SEQRES   5 A  192  GLU GLU ILE ILE ARG SER SER GLU GLY GLY VAL PHE ASN          
SEQRES   6 A  192  ASN ALA ALA GLN VAL TRP ASN HIS THR PHE TYR TRP ASN          
SEQRES   7 A  192  CYS LEU ALA PRO ASN ALA GLY GLY GLU PRO THR GLY LYS          
SEQRES   8 A  192  VAL ALA GLU ALA ILE ALA ALA SER PHE GLY SER PHE ALA          
SEQRES   9 A  192  ASP PHE LYS ALA GLN PHE THR ASP ALA ALA ILE LYS ASN          
SEQRES  10 A  192  PHE GLY SER GLY TRP THR TRP LEU VAL LYS ASN SER ASP          
SEQRES  11 A  192  GLY LYS LEU ALA ILE VAL SER THR SER ASN ALA GLY THR          
SEQRES  12 A  192  PRO LEU THR THR ASP ALA THR PRO LEU LEU THR VAL ASP          
SEQRES  13 A  192  VAL TRP GLU HIS ALA TYR TYR ILE ASP TYR ARG ASN ALA          
SEQRES  14 A  192  ARG PRO GLY TYR LEU GLU HIS PHE TRP ALA LEU VAL ASN          
SEQRES  15 A  192  TRP GLU PHE VAL ALA LYS ASN LEU ALA ALA                      
SEQRES   1 B  192  SER PHE GLU LEU PRO ALA LEU PRO TYR ALA LYS ASP ALA          
SEQRES   2 B  192  LEU ALA PRO HIS ILE SER ALA GLU THR ILE GLU TYR HIS          
SEQRES   3 B  192  TYR GLY LYS HIS HIS GLN THR TYR VAL THR ASN LEU ASN          
SEQRES   4 B  192  ASN LEU ILE LYS GLY THR ALA PHE GLU GLY LYS SER LEU          
SEQRES   5 B  192  GLU GLU ILE ILE ARG SER SER GLU GLY GLY VAL PHE ASN          
SEQRES   6 B  192  ASN ALA ALA GLN VAL TRP ASN HIS THR PHE TYR TRP ASN          
SEQRES   7 B  192  CYS LEU ALA PRO ASN ALA GLY GLY GLU PRO THR GLY LYS          
SEQRES   8 B  192  VAL ALA GLU ALA ILE ALA ALA SER PHE GLY SER PHE ALA          
SEQRES   9 B  192  ASP PHE LYS ALA GLN PHE THR ASP ALA ALA ILE LYS ASN          
SEQRES  10 B  192  PHE GLY SER GLY TRP THR TRP LEU VAL LYS ASN SER ASP          
SEQRES  11 B  192  GLY LYS LEU ALA ILE VAL SER THR SER ASN ALA GLY THR          
SEQRES  12 B  192  PRO LEU THR THR ASP ALA THR PRO LEU LEU THR VAL ASP          
SEQRES  13 B  192  VAL TRP GLU HIS ALA TYR TYR ILE ASP TYR ARG ASN ALA          
SEQRES  14 B  192  ARG PRO GLY TYR LEU GLU HIS PHE TRP ALA LEU VAL ASN          
SEQRES  15 B  192  TRP GLU PHE VAL ALA LYS ASN LEU ALA ALA                      
HET    FE2  A 193       1                                                       
HET    FE2  B 193       1                                                       
HETNAM     FE2 FE (II) ION                                                      
FORMUL   3  FE2    2(FE 2+)                                                     
FORMUL   5  HOH   *236(H2 O)                                                    
HELIX    1 HA1 ALA A   20  ILE A   42  1                                  23    
HELIX    2 HA2 LEU A   52  SER A   58  1                                   7    
HELIX    3 HA3 GLY A   61  ASN A   78  1                                  18    
HELIX    4 HA4 GLY A   90  PHE A  100  1                                  11    
HELIX    5 HA5 PHE A  103  LYS A  116  1                                  14    
HELIX    6 HA6 PRO A  144  THR A  146  5                                   3    
HELIX    7 HA7 ARG A  170  TRP A  178  1                                   9    
HELIX    8 HA8 TRP A  183  LEU A  190  1                                   8    
HELIX    9 HB1 ALA B   20  ILE B   42  1                                  23    
HELIX   10 HB2 LEU B   52  SER B   58  1                                   7    
HELIX   11 HB3 GLY B   61  ASN B   78  1                                  18    
HELIX   12 HB4 GLY B   90  PHE B  100  1                                  11    
HELIX   13 HB5 PHE B  103  LYS B  116  1                                  14    
HELIX   14 HB6 PRO B  144  THR B  146  5                                   3    
HELIX   15 HB7 ARG B  170  PHE B  177  1                                   8    
HELIX   16 HB8 TRP B  183  ALA B  191  1                                   9    
SHEET    1 B1A 3 LEU A 133  SER A 139  0                                        
SHEET    2 B1A 3 GLY A 121  LYS A 127 -1  O  TRP A 122   N  THR A 138           
SHEET    3 B1A 3 THR A 150  ASP A 156 -1  N  THR A 150   O  LYS A 127           
SHEET    1 B1B 3 LEU B 133  SER B 139  0                                        
SHEET    2 B1B 3 GLY B 121  LYS B 127 -1  O  TRP B 122   N  THR B 138           
SHEET    3 B1B 3 THR B 150  ASP B 156 -1  N  THR B 150   O  LYS B 127           
LINK        FE   FE2 A 193                 OD2 ASP A 156     1555   1555  1.95  
LINK        FE   FE2 A 193                 O   HOH A 194     1555   1555  2.03  
LINK        FE   FE2 A 193                 NE2 HIS A 160     1555   1555  2.13  
LINK        FE   FE2 A 193                 NE2 HIS A  26     1555   1555  2.19  
LINK        FE   FE2 A 193                 NE2 HIS A  73     1555   1555  2.06  
LINK        FE   FE2 B 193                 NE2 HIS B  73     1555   1555  2.03  
LINK        FE   FE2 B 193                 OD2 ASP B 156     1555   1555  1.92  
LINK        FE   FE2 B 193                 NE2 HIS B 160     1555   1555  2.11  
LINK        FE   FE2 B 193                 O   HOH B 194     1555   1555  2.06  
LINK        FE   FE2 B 193                 NE2 HIS B  26     1555   1555  2.18  
CISPEP   1 ALA A   15    PRO A   16          0         3.80                     
CISPEP   2 ALA B   15    PRO B   16          0         3.03                     
SITE     1 FEA  5 HIS A  26  HIS A  73  ASP A 156  HIS A 160                    
SITE     2 FEA  5 HOH A 194                                                     
SITE     1 FEB  5 HIS B  26  HIS B  73  ASP B 156  HIS B 160                    
SITE     2 FEB  5 HOH B 194                                                     
SITE     1 AC1  5 HIS A  26  HIS A  73  ASP A 156  HIS A 160                    
SITE     2 AC1  5 HOH A 194                                                     
SITE     1 AC2  5 HIS B  26  HIS B  73  ASP B 156  HIS B 160                    
SITE     2 AC2  5 HOH B 194                                                     
CRYST1   81.550   75.080   71.530  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.012262  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013319  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013980        0.00000                         
MTRIX1   1 -0.146500 -0.954200  0.260700       56.43737    1                    
MTRIX2   1 -0.954800  0.067400 -0.289600       67.15103    1                    
MTRIX3   1  0.258800 -0.291300 -0.921000       61.27833    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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