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Database: PDB
Entry: 1ZA5
LinkDB: 1ZA5
Original site: 1ZA5 
HEADER    OXIDOREDUCTASE                          05-APR-05   1ZA5              
TITLE     Q69H-FESOD                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUPEROXIDE DISMUTASE [FE];                                 
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 1.15.1.1;                                                        
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 GENE: SODB;                                                          
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: QC774                                      
KEYWDS    H-BONDING REDOX TUNING SUPEROXIDE DISMUTASE PROTON-COUPLED            
KEYWDS   2 ELECTRON TRANSFER, OXIDOREDUCTASE                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.YIKILMAZ,D.W.RODGERS,A.F.MILLER                                     
REVDAT   2   24-FEB-09 1ZA5    1       VERSN                                    
REVDAT   1   14-MAR-06 1ZA5    0                                                
JRNL        AUTH   E.YIKILMAZ,D.W.RODGERS,A.F.MILLER                            
JRNL        TITL   THE CRUCIAL IMPORTANCE OF CHEMISTRY IN THE                   
JRNL        TITL 2 STRUCTURE-FUNCTION LINK: MANIPULATING HYDROGEN               
JRNL        TITL 3 BONDING IN IRON-CONTAINING SUPEROXIDE DISMUTASE.             
JRNL        REF    BIOCHEMISTRY                  V.  45  1151 2006              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   16430211                                                     
JRNL        DOI    10.1021/BI051495D                                            
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.96                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 973646.610                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 87.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 32845                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.199                           
REMARK   3   FREE R VALUE                     : 0.237                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 3289                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.004                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.91                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 49.10                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2732                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3440                       
REMARK   3   BIN FREE R VALUE                    : 0.3880                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.00                        
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 302                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.022                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3008                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 34                                      
REMARK   3   SOLVENT ATOMS            : 459                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 22.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 8.31000                                              
REMARK   3    B22 (A**2) : -7.40000                                             
REMARK   3    B33 (A**2) : -0.91000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 8.96000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.22                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.14                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.27                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.20                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.005                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.70                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.20                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.30                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.120 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.620 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.890 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.670 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.36                                                 
REMARK   3   BSOL        : 49.74                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : TRS.PAR                                        
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : TRS.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1ZA5 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-APR-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB032490.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.66                               
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 RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
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 : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 32845                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 88.0                               
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) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.88                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 43.0                               
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: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.12                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: MGCL2, PEG8000, PH 8.66, VAPOR           
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 277K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       42.46050            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 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 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    SER A  58       22.73   -150.66                                   
REMARK 500    ALA A  84     -141.22   -135.94                                   
REMARK 500    ASN A 117      105.23    -54.68                                   
REMARK 500    ASN A 140     -114.12     55.69                                   
REMARK 500    ARG A 167     -132.66     51.93                                   
REMARK 500    ALA B 284     -138.40   -131.96                                   
REMARK 500    ASN B 340     -112.66     55.51                                   
REMARK 500    THR B 347     -168.90   -124.68                                   
REMARK 500    ARG B 367     -133.09     55.55                                   
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 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B 612        DISTANCE =  5.32 ANGSTROMS                       
REMARK 525    HOH A 319        DISTANCE =  7.69 ANGSTROMS                       
REMARK 525    HOH A 320        DISTANCE =  7.96 ANGSTROMS                       
REMARK 525    HOH B 653        DISTANCE =  5.67 ANGSTROMS                       
REMARK 525    HOH A 330        DISTANCE =  5.66 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE A 193  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  26   NE2                                                    
REMARK 620 2 HIS A  73   NE2  92.3                                              
REMARK 620 3 ASP A 156   OD1  86.2 113.4                                        
REMARK 620 4 HIS A 160   NE2  94.6 126.8 119.6                                  
REMARK 620 5 HOH A 196   O   173.3  92.0  87.4  87.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE B 393  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 226   NE2                                                    
REMARK 620 2 HIS B 273   NE2  90.3                                              
REMARK 620 3 ASP B 356   OD1  88.2 112.8                                        
REMARK 620 4 HIS B 360   NE2  91.2 128.1 119.1                                  
REMARK 620 5 HOH B 394   O   175.3  89.9  87.4  92.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE A 193                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE B 393                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS A 194                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS A 195                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS B 1                   
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS B 4                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1ISB   RELATED DB: PDB                                   
REMARK 900 FESOD, OXIDIZED                                                      
REMARK 900 RELATED ID: 1ISA   RELATED DB: PDB                                   
REMARK 900 FESOD, REDUCED                                                       
DBREF  1ZA5 A    1   192  UNP    P0AGD3   SODF_ECOLI       1    192             
DBREF  1ZA5 B  201   392  UNP    P0AGD3   SODF_ECOLI       1    192             
SEQADV 1ZA5 HIS A   69  UNP  P0AGD3    GLN    69 ENGINEERED                     
SEQADV 1ZA5 HIS B  269  UNP  P0AGD3    GLN    69 ENGINEERED                     
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 HIS 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 HIS 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     FE  A 193       1                                                       
HET     FE  B 393       1                                                       
HET    TRS  A 194       8                                                       
HET    TRS  A 195       8                                                       
HET    TRS  B   1       8                                                       
HET    TRS  B   4       8                                                       
HETNAM      FE FE (III) ION                                                     
HETNAM     TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL                         
HETSYN     TRS TRIS BUFFER                                                      
FORMUL   3   FE    2(FE 3+)                                                     
FORMUL   5  TRS    4(C4 H12 N O3 1+)                                            
FORMUL   9  HOH   *459(H2 O)                                                    
HELIX    1   1 SER A   19  TYR A   27  1                                   9    
HELIX    2   2 LYS A   29  LYS A   43  1                                  15    
HELIX    3   3 SER A   51  ARG A   57  1                                   7    
HELIX    4   4 GLU A   60  LEU A   80  1                                  21    
HELIX    5   5 THR A   89  GLY A  101  1                                  13    
HELIX    6   6 SER A  102  ASN A  117  1                                  16    
HELIX    7   7 THR A  143  THR A  147  5                                   5    
HELIX    8   8 TRP A  158  ALA A  161  5                                   4    
HELIX    9   9 TYR A  162  ARG A  167  1                                   6    
HELIX   10  10 ALA A  169  ALA A  179  1                                  11    
HELIX   11  11 ASN A  182  ALA A  192  1                                  11    
HELIX   12  12 SER B  219  TYR B  227  1                                   9    
HELIX   13  13 LYS B  229  LYS B  243  1                                  15    
HELIX   14  14 SER B  251  ARG B  257  1                                   7    
HELIX   15  15 GLU B  260  CYS B  279  1                                  20    
HELIX   16  16 THR B  289  GLY B  301  1                                  13    
HELIX   17  17 SER B  302  ASN B  317  1                                  16    
HELIX   18  18 THR B  343  THR B  347  5                                   5    
HELIX   19  19 TRP B  358  ALA B  361  5                                   4    
HELIX   20  20 TYR B  362  ARG B  367  1                                   6    
HELIX   21  21 ALA B  369  ALA B  379  1                                  11    
HELIX   22  22 ASN B  382  ALA B  392  1                                  11    
SHEET    1   A 3 LEU A 133  SER A 139  0                                        
SHEET    2   A 3 GLY A 121  LYS A 127 -1  N  TRP A 124   O  VAL A 136           
SHEET    3   A 3 THR A 150  ASP A 156 -1  O  LEU A 152   N  LEU A 125           
SHEET    1   B 3 LEU B 333  SER B 339  0                                        
SHEET    2   B 3 GLY B 321  LYS B 327 -1  N  TRP B 324   O  VAL B 336           
SHEET    3   B 3 THR B 350  ASP B 356 -1  O  THR B 350   N  LYS B 327           
LINK         NE2 HIS A  26                FE    FE A 193     1555   1555  2.19  
LINK         NE2 HIS A  73                FE    FE A 193     1555   1555  2.16  
LINK         OD1 ASP A 156                FE    FE A 193     1555   1555  2.01  
LINK         NE2 HIS A 160                FE    FE A 193     1555   1555  2.17  
LINK        FE    FE A 193                 O   HOH A 196     1555   1555  2.17  
LINK         NE2 HIS B 226                FE    FE B 393     1555   1555  2.18  
LINK         NE2 HIS B 273                FE    FE B 393     1555   1555  2.12  
LINK         OD1 ASP B 356                FE    FE B 393     1555   1555  1.93  
LINK         NE2 HIS B 360                FE    FE B 393     1555   1555  2.07  
LINK        FE    FE B 393                 O   HOH B 394     1555   1555  2.23  
CISPEP   1 ALA A   15    PRO A   16          0         0.10                     
CISPEP   2 ALA B  215    PRO B  216          0        -0.01                     
SITE     1 AC1  5 HIS A  26  HIS A  73  ASP A 156  HIS A 160                    
SITE     2 AC1  5 HOH A 196                                                     
SITE     1 AC2  5 HIS B 226  HIS B 273  ASP B 356  HIS B 360                    
SITE     2 AC2  5 HOH B 394                                                     
SITE     1 AC3  5 SER A  51  GLU A  54  TRS B   1  GLY B 249                    
SITE     2 AC3  5 HOH B 429                                                     
SITE     1 AC4  5 ASP A 165  HOH A 230  HOH A 266  HOH A 269                    
SITE     2 AC4  5 GLU B 260                                                     
SITE     1 AC5  6 GLY A  49  TRS A 194  GLY B 249  LYS B 250                    
SITE     2 AC5  6 SER B 251  GLU B 254                                          
SITE     1 AC6  7 HOH A 372  GLU B 221  ARG B 257  SER B 258                    
SITE     2 AC6  7 SER B 259  HOH B 513  HOH B 560                               
CRYST1   41.202   84.921   61.634  90.00 108.37  90.00 P 1 21 1      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      0.024271  0.000000  0.008059        0.00000                         
SCALE2      0.000000  0.011776  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017096        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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