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Database: PDB
Entry: 2GOJ
LinkDB: 2GOJ
Original site: 2GOJ 
HEADER    OXIDOREDUCTASE                          13-APR-06   2GOJ              
TITLE     THE CRYSTAL STRUCTURE OF THE ENZYME FE-SUPEROXIDE DISMUTASE FROM      
TITLE    2 PLASMODIUM FALCIPARUM                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FE-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: PLASMODIUM FALCIPARUM;                          
SOURCE   3 ORGANISM_TAXID: 137071;                                              
SOURCE   4 STRAIN: HB3;                                                         
SOURCE   5 GENE: SOD;                                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI K12;                             
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 83333;                                      
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: K12;                                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    BETA+ALPHA STRUCTURE, OXIDOREDUCTASE                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.V.A.S.NAVARRO,R.C.GARRATT                                           
REVDAT   5   13-JUL-11 2GOJ    1       VERSN                                    
REVDAT   4   18-AUG-09 2GOJ    1       JRNL                                     
REVDAT   3   12-MAY-09 2GOJ    1       JRNL                                     
REVDAT   2   24-FEB-09 2GOJ    1       VERSN                                    
REVDAT   1   28-AUG-07 2GOJ    0                                                
JRNL        AUTH   J.F.BACHEGA,M.V.NAVARRO,L.BLEICHER,R.K.BORTOLETO-BUGS,       
JRNL        AUTH 2 D.DIVE,P.HOFFMANN,E.VISCOGLIOSI,R.C.GARRATT                  
JRNL        TITL   SYSTEMATIC STRUCTURAL STUDIES OF IRON SUPEROXIDE DISMUTASES  
JRNL        TITL 2 FROM HUMAN PARASITES AND A STATISTICAL COUPLING ANALYSIS OF  
JRNL        TITL 3 METAL BINDING SPECIFICITY                                    
JRNL        REF    PROTEINS                      V.  77    26 2009              
JRNL        REFN                   ISSN 0887-3585                               
JRNL        PMID   19384994                                                     
JRNL        DOI    10.1002/PROT.22412                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 31.62                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 24057                          
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) : 0.158                           
REMARK   3   R VALUE            (WORKING SET) : 0.156                           
REMARK   3   FREE R VALUE                     : 0.194                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1266                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.11                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2582                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2010                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 136                          
REMARK   3   BIN FREE R VALUE                    : 0.2420                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3175                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 2                                       
REMARK   3   SOLVENT ATOMS            : 305                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 14.50                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.01000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.191         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.153         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.101         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.711         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.955                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3315 ; 0.009 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  2768 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4511 ; 1.107 ; 1.899       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  6507 ; 0.796 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   397 ; 5.576 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   461 ; 0.072 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3733 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   679 ; 0.004 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   738 ; 0.195 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  3172 ; 0.232 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1626 ; 0.084 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   210 ; 0.143 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     2 ; 0.040 ; 0.200       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):     6 ; 0.135 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    41 ; 0.273 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    15 ; 0.216 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1953 ; 0.550 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3142 ; 1.053 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1362 ; 1.558 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1365 ; 2.525 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 2GOJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-APR-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB037365.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-FEB-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU                             
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          : RIGAKU RAXIS IIC                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 25131                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 31.620                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.3                               
REMARK 200  DATA REDUNDANCY                : 6.400                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.09800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.5000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 73.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.80                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.37000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: PDB ENTRY 1ISA                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 41.98                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25.5% PEG 4000 (W/V), 0.17 M SODIUM      
REMARK 280  ACETATE, 0.085 M TRIS-HCL, PH 8.5, VAPOR DIFFUSION, HANGING DROP,   
REMARK 280  TEMPERATURE 291K                                                    
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       27.70100            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       44.18450            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       39.20850            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       44.18450            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       27.70100            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       39.20850            
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: THE ASSYMETRIC UNIT CONTAINS A DIMER, WHICH REPRESENTS THE   
REMARK 300 MOLECULAR ASSEMBLY                                                   
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 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 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     LYS A   197                                                      
REMARK 465     LYS B   196                                                      
REMARK 465     LYS B   197                                                      
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    ASP B  99   CB  -  CG  -  OD2 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    LYS A  29      -62.70   -108.86                                   
REMARK 500    PRO A  46       -9.85    -59.09                                   
REMARK 500    CYS A  84     -146.31   -116.34                                   
REMARK 500    ASP A 140     -115.28     61.19                                   
REMARK 500    ARG A 168     -129.28     52.00                                   
REMARK 500    LYS B  29      -60.15   -107.44                                   
REMARK 500    CYS B  84     -148.52   -115.84                                   
REMARK 500    ASP B 140     -112.45     56.75                                   
REMARK 500    ARG B 168     -127.28     51.09                                   
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 198  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  26   NE2                                                    
REMARK 620 2 HIS A  73   NE2  90.1                                              
REMARK 620 3 ASP A 157   OD2  84.1 113.4                                        
REMARK 620 4 HIS A 161   NE2  92.6 124.5 122.1                                  
REMARK 620 5 HOH A 199   O   175.6  90.8  91.7  90.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FE2 B 198  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  26   NE2                                                    
REMARK 620 2 HIS B  73   NE2  92.4                                              
REMARK 620 3 ASP B 157   OD2  86.8 115.5                                        
REMARK 620 4 HIS B 161   NE2  90.0 124.4 120.1                                  
REMARK 620 5 HOH B 199   O   178.7  87.8  92.0  91.0                            
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 FE2 A 198                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE2 B 198                 
DBREF  2GOJ A    1   197  GB     861077   CAA89971         2    198             
DBREF  2GOJ B    1   197  GB     861077   CAA89971         2    198             
SEQRES   1 A  197  VAL ILE THR LEU PRO LYS LEU LYS TYR ALA LEU ASN ALA          
SEQRES   2 A  197  LEU SER PRO HIS ILE SER GLU GLU THR LEU ASN PHE HIS          
SEQRES   3 A  197  TYR ASN LYS HIS HIS ALA GLY TYR VAL ASN LYS LEU ASN          
SEQRES   4 A  197  THR LEU ILE LYS ASP THR PRO PHE ALA GLU LYS SER LEU          
SEQRES   5 A  197  LEU ASP ILE VAL LYS GLU SER SER GLY ALA ILE PHE ASN          
SEQRES   6 A  197  ASN ALA ALA GLN ILE TRP ASN HIS THR PHE TYR TRP ASP          
SEQRES   7 A  197  SER MET GLY PRO ASP CYS GLY GLY GLU PRO HIS GLY GLU          
SEQRES   8 A  197  ILE LYS GLU LYS ILE GLN GLU ASP PHE GLY SER PHE ASN          
SEQRES   9 A  197  ASN PHE LYS GLU GLN PHE SER ASN ILE LEU CYS GLY HIS          
SEQRES  10 A  197  PHE GLY SER GLY TRP GLY TRP LEU ALA LEU ASN ASN ASN          
SEQRES  11 A  197  ASN LYS LEU VAL ILE LEU GLN THR HIS ASP ALA GLY ASN          
SEQRES  12 A  197  PRO ILE LYS ASP ASN THR GLY ILE PRO ILE LEU THR CYS          
SEQRES  13 A  197  ASP ILE TRP GLU HIS ALA TYR TYR ILE ASP TYR ARG ASN          
SEQRES  14 A  197  ASP ARG ALA SER TYR VAL LYS ALA TRP TRP ASN LEU VAL          
SEQRES  15 A  197  ASN TRP ASN PHE ALA ASN GLU ASN LEU LYS LYS ALA MET          
SEQRES  16 A  197  LYS LYS                                                      
SEQRES   1 B  197  VAL ILE THR LEU PRO LYS LEU LYS TYR ALA LEU ASN ALA          
SEQRES   2 B  197  LEU SER PRO HIS ILE SER GLU GLU THR LEU ASN PHE HIS          
SEQRES   3 B  197  TYR ASN LYS HIS HIS ALA GLY TYR VAL ASN LYS LEU ASN          
SEQRES   4 B  197  THR LEU ILE LYS ASP THR PRO PHE ALA GLU LYS SER LEU          
SEQRES   5 B  197  LEU ASP ILE VAL LYS GLU SER SER GLY ALA ILE PHE ASN          
SEQRES   6 B  197  ASN ALA ALA GLN ILE TRP ASN HIS THR PHE TYR TRP ASP          
SEQRES   7 B  197  SER MET GLY PRO ASP CYS GLY GLY GLU PRO HIS GLY GLU          
SEQRES   8 B  197  ILE LYS GLU LYS ILE GLN GLU ASP PHE GLY SER PHE ASN          
SEQRES   9 B  197  ASN PHE LYS GLU GLN PHE SER ASN ILE LEU CYS GLY HIS          
SEQRES  10 B  197  PHE GLY SER GLY TRP GLY TRP LEU ALA LEU ASN ASN ASN          
SEQRES  11 B  197  ASN LYS LEU VAL ILE LEU GLN THR HIS ASP ALA GLY ASN          
SEQRES  12 B  197  PRO ILE LYS ASP ASN THR GLY ILE PRO ILE LEU THR CYS          
SEQRES  13 B  197  ASP ILE TRP GLU HIS ALA TYR TYR ILE ASP TYR ARG ASN          
SEQRES  14 B  197  ASP ARG ALA SER TYR VAL LYS ALA TRP TRP ASN LEU VAL          
SEQRES  15 B  197  ASN TRP ASN PHE ALA ASN GLU ASN LEU LYS LYS ALA MET          
SEQRES  16 B  197  LYS LYS                                                      
HET    FE2  A 198       1                                                       
HET    FE2  B 198       1                                                       
HETNAM     FE2 FE (II) ION                                                      
FORMUL   3  FE2    2(FE 2+)                                                     
FORMUL   5  HOH   *305(H2 O)                                                    
HELIX    1   1 SER A   19  LYS A   29  1                                  11    
HELIX    2   2 LYS A   29  LYS A   43  1                                  15    
HELIX    3   3 SER A   51  SER A   59  1                                   9    
HELIX    4   4 SER A   60  SER A   79  1                                  20    
HELIX    5   5 GLY A   90  GLY A  101  1                                  12    
HELIX    6   6 SER A  102  HIS A  117  1                                  16    
HELIX    7   7 TRP A  159  ALA A  162  5                                   4    
HELIX    8   8 TYR A  163  ARG A  168  1                                   6    
HELIX    9   9 ASP A  170  TRP A  179  1                                  10    
HELIX   10  10 ASN A  183  LYS A  196  1                                  14    
HELIX   11  11 SER B   19  LYS B   29  1                                  11    
HELIX   12  12 LYS B   29  LYS B   43  1                                  15    
HELIX   13  13 THR B   45  LYS B   50  5                                   6    
HELIX   14  14 SER B   51  SER B   59  1                                   9    
HELIX   15  15 SER B   60  SER B   79  1                                  20    
HELIX   16  16 GLY B   90  GLY B  101  1                                  12    
HELIX   17  17 SER B  102  HIS B  117  1                                  16    
HELIX   18  18 ASN B  143  ASN B  148  1                                   6    
HELIX   19  19 TRP B  159  ALA B  162  5                                   4    
HELIX   20  20 TYR B  163  ARG B  168  1                                   6    
HELIX   21  21 ASP B  170  TRP B  179  1                                  10    
HELIX   22  22 ASN B  183  MET B  195  1                                  13    
SHEET    1   A 3 LEU A 133  HIS A 139  0                                        
SHEET    2   A 3 GLY A 121  LEU A 127 -1  N  TRP A 124   O  LEU A 136           
SHEET    3   A 3 ILE A 151  ASP A 157 -1  O  ILE A 153   N  LEU A 125           
SHEET    1   B 3 LEU B 133  HIS B 139  0                                        
SHEET    2   B 3 GLY B 121  LEU B 127 -1  N  TRP B 124   O  LEU B 136           
SHEET    3   B 3 ILE B 151  ASP B 157 -1  O  ILE B 153   N  LEU B 125           
LINK         NE2 HIS A  26                FE   FE2 A 198     1555   1555  2.23  
LINK         NE2 HIS A  73                FE   FE2 A 198     1555   1555  2.24  
LINK         OD2 ASP A 157                FE   FE2 A 198     1555   1555  1.93  
LINK         NE2 HIS A 161                FE   FE2 A 198     1555   1555  2.09  
LINK         NE2 HIS B  26                FE   FE2 B 198     1555   1555  2.26  
LINK         NE2 HIS B  73                FE   FE2 B 198     1555   1555  2.24  
LINK         OD2 ASP B 157                FE   FE2 B 198     1555   1555  1.91  
LINK         NE2 HIS B 161                FE   FE2 B 198     1555   1555  2.18  
LINK        FE   FE2 A 198                 O   HOH A 199     1555   1555  2.04  
LINK        FE   FE2 B 198                 O   HOH B 199     1555   1555  2.10  
CISPEP   1 SER A   15    PRO A   16          0        -1.85                     
CISPEP   2 SER B   15    PRO B   16          0         1.42                     
SITE     1 AC1  5 HIS A  26  HIS A  73  ASP A 157  HIS A 161                    
SITE     2 AC1  5 HOH A 199                                                     
SITE     1 AC2  5 HIS B  26  HIS B  73  ASP B 157  HIS B 161                    
SITE     2 AC2  5 HOH B 199                                                     
CRYST1   55.402   78.417   88.369  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      0.018050  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012752  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011316        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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