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Database: PDB
Entry: 1B06
LinkDB: 1B06
Original site: 1B06 
HEADER    OXIDOREDUCTASE                          16-NOV-98   1B06              
TITLE     SUPEROXIDE DISMUTASE FROM SULFOLOBUS ACIDOCALDARIUS                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEIN (SUPEROXIDE DISMUTASE);                            
COMPND   3 CHAIN: A, B, C, D, E, F;                                             
COMPND   4 EC: 1.15.1.1                                                         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SULFOLOBUS ACIDOCALDARIUS;                      
SOURCE   3 ORGANISM_TAXID: 330779;                                              
SOURCE   4 STRAIN: DSM 639;                                                     
SOURCE   5 ATCC: DSM 639;                                                       
SOURCE   6 COLLECTION: DSM 639;                                                 
SOURCE   7 CELLULAR_LOCATION: CYTOSOL;                                          
SOURCE   8 OTHER_DETAILS: GERMAN COLLECTION OF MICROORGANISMS                   
KEYWDS    SUPEROXIDE DISMUTASE, OXIDOREDUCTASE                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.KNAPP,S.KARDINAHL,H.NIKLAS,G.TIBBELIN,G.SCHAFER,R.LADENSTEIN        
REVDAT   3   13-JUL-11 1B06    1       VERSN                                    
REVDAT   2   24-FEB-09 1B06    1       VERSN                                    
REVDAT   1   18-NOV-99 1B06    0                                                
JRNL        AUTH   S.KNAPP,S.KARDINAHL,N.HELLGREN,G.TIBBELIN,G.SCHAFER,         
JRNL        AUTH 2 R.LADENSTEIN                                                 
JRNL        TITL   REFINED CRYSTAL STRUCTURE OF A SUPEROXIDE DISMUTASE FROM THE 
JRNL        TITL 2 HYPERTHERMOPHILIC ARCHAEON SULFOLOBUS ACIDOCALDARIUS AT 2.2  
JRNL        TITL 3 A RESOLUTION.                                                
JRNL        REF    J.MOL.BIOL.                   V. 285   689 1999              
JRNL        PUBL   ACADEMIC PRESS                                               
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   9878438                                                      
JRNL        DOI    10.1006/JMBI.1998.2344                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.8                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.00                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 69271                          
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) : 0.174                           
REMARK   3   FREE R VALUE                     : 0.223                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
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            : 10176                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 6                                       
REMARK   3   SOLVENT ATOMS            : 321                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 23.00                          
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) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.16                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.36                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.59                            
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) : 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 : RESTRAINTS                                              
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  : PARAM19X.PRO                                   
REMARK   3  PARAMETER FILE  2  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPH19X.PRO                                    
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1B06 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-JUL-99.                  
REMARK 100 THE RCSB ID CODE IS RCSB007333.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 286                                
REMARK 200  PH                             : 7.5                                
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          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NI FILTER                          
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 69271                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : 0.10100                            
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: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
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   (%): 45.73                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.5                                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       84.05000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       45.65000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       84.05000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       45.65000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000      166.00616            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       85.67442            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 14250 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 28540 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -59.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, E, F                            
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH B 365  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B 362  LIES ON A SPECIAL POSITION.                          
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     THR A     1                                                      
REMARK 465     GLN A     2                                                      
REMARK 465     THR B     1                                                      
REMARK 465     GLN B     2                                                      
REMARK 465     THR C     1                                                      
REMARK 465     GLN C     2                                                      
REMARK 465     THR D     1                                                      
REMARK 465     GLN D     2                                                      
REMARK 465     THR E     1                                                      
REMARK 465     GLN E     2                                                      
REMARK 465     THR F     1                                                      
REMARK 465     GLN F     2                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   325     O    HOH A   325     2656     1.30            
REMARK 500   O    HOH E   357     O    HOH E   357     2656     1.92            
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    ILE A   4       95.77     44.67                                   
REMARK 500    ALA A  94      -62.21    -20.17                                   
REMARK 500    ASN A 154     -148.71     57.08                                   
REMARK 500    ASN A 158        3.94     92.35                                   
REMARK 500    GLU A 162      -12.11     69.30                                   
REMARK 500    TYR A 176      -11.23   -150.94                                   
REMARK 500    LYS A 181     -135.92     56.10                                   
REMARK 500    ILE B   4       96.30     45.55                                   
REMARK 500    ALA B  94      -61.05    -22.80                                   
REMARK 500    ASN B 154     -148.98     58.83                                   
REMARK 500    ASN B 158        8.12     88.60                                   
REMARK 500    GLU B 162      -12.00     66.59                                   
REMARK 500    TYR B 176      -12.74   -148.70                                   
REMARK 500    LYS B 181     -136.15     58.09                                   
REMARK 500    ILE C   4       96.22     45.27                                   
REMARK 500    ALA C  94      -61.76    -21.57                                   
REMARK 500    ASN C 154     -146.67     60.61                                   
REMARK 500    ASN C 158        3.88     89.34                                   
REMARK 500    GLU C 162      -10.15     69.56                                   
REMARK 500    TYR C 176      -15.41   -147.88                                   
REMARK 500    LYS C 181     -134.62     56.68                                   
REMARK 500    ILE D   4       96.53     45.14                                   
REMARK 500    ALA D  94      -59.95    -23.13                                   
REMARK 500    ASN D 154     -147.40     58.46                                   
REMARK 500    ASN D 158        6.88     89.38                                   
REMARK 500    GLU D 162      -11.31     67.59                                   
REMARK 500    TYR D 176      -12.29   -149.30                                   
REMARK 500    LYS D 181     -135.15     56.69                                   
REMARK 500    ILE E   4       97.62     44.95                                   
REMARK 500    ALA E  94      -62.16    -21.25                                   
REMARK 500    ASN E 154     -149.40     60.07                                   
REMARK 500    ASN E 158        4.95     89.56                                   
REMARK 500    GLU E 162      -15.17     70.43                                   
REMARK 500    TYR E 176      -10.42   -150.33                                   
REMARK 500    LYS E 181     -134.98     57.19                                   
REMARK 500    ILE F   4       96.99     44.99                                   
REMARK 500    ALA F  94      -61.27    -21.64                                   
REMARK 500    ASN F 154     -146.05     59.75                                   
REMARK 500    ASN F 158        6.54     90.22                                   
REMARK 500    GLU F 162      -11.51     66.67                                   
REMARK 500    TYR F 176      -12.49   -149.32                                   
REMARK 500    LYS F 181     -135.57     58.18                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE A 322  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 377   O                                                      
REMARK 620 2 HIS A  33   NE2 176.1                                              
REMARK 620 3 HIS A  84   NE2  90.1  87.7                                        
REMARK 620 4 ASP A 170   OD2  88.6  89.0 107.6                                  
REMARK 620 5 HIS A 174   NE2  96.1  87.8 126.8 125.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE B 323  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B 368   O                                                      
REMARK 620 2 HIS B  33   NE2 178.4                                              
REMARK 620 3 ASP B 170   OD2  96.2  84.6                                        
REMARK 620 4 HIS B  84   NE2  97.1  83.9 108.4                                  
REMARK 620 5 HIS B 174   NE2  92.5  85.9 120.4 128.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE C 324  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH C 372   O                                                      
REMARK 620 2 ASP C 170   OD2  86.2                                              
REMARK 620 3 HIS C 174   NE2  96.4 121.5                                        
REMARK 620 4 HIS C  33   NE2 173.3  87.4  85.5                                  
REMARK 620 5 HIS C  84   NE2  96.7 111.8 125.7  87.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE D 325  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH D 377   O                                                      
REMARK 620 2 HIS D  33   NE2 172.6                                              
REMARK 620 3 HIS D 174   NE2  97.5  86.6                                        
REMARK 620 4 ASP D 170   OD2  86.5  86.1 121.7                                  
REMARK 620 5 HIS D  84   NE2  91.1  91.2 128.4 109.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE E 326  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH E 379   O                                                      
REMARK 620 2 HIS E  84   NE2  96.0                                              
REMARK 620 3 HIS E 174   NE2  90.9 126.8                                        
REMARK 620 4 ASP E 170   OD2  87.6 111.6 121.4                                  
REMARK 620 5 HIS E  33   NE2 169.2  93.0  88.4  83.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE F 327  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH F 395   O                                                      
REMARK 620 2 HIS F  33   NE2 172.5                                              
REMARK 620 3 ASP F 170   OD2  88.9  83.9                                        
REMARK 620 4 HIS F 174   NE2  93.1  88.5 118.9                                  
REMARK 620 5 HIS F  84   NE2  93.0  91.7 112.0 128.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE A 322                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE B 323                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE C 324                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE D 325                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE E 326                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE F 327                  
DBREF  1B06 A    1   210  UNP    Q08713   SODF_SULAC       2    211             
DBREF  1B06 B    1   210  UNP    Q08713   SODF_SULAC       2    211             
DBREF  1B06 C    1   210  UNP    Q08713   SODF_SULAC       2    211             
DBREF  1B06 D    1   210  UNP    Q08713   SODF_SULAC       2    211             
DBREF  1B06 E    1   210  UNP    Q08713   SODF_SULAC       2    211             
DBREF  1B06 F    1   210  UNP    Q08713   SODF_SULAC       2    211             
SEQADV 1B06 ASP A  110  UNP  Q08713    ASN   111 CONFLICT                       
SEQADV 1B06 ASP B  110  UNP  Q08713    ASN   111 CONFLICT                       
SEQADV 1B06 ASP C  110  UNP  Q08713    ASN   111 CONFLICT                       
SEQADV 1B06 ASP D  110  UNP  Q08713    ASN   111 CONFLICT                       
SEQADV 1B06 ASP E  110  UNP  Q08713    ASN   111 CONFLICT                       
SEQADV 1B06 ASP F  110  UNP  Q08713    ASN   111 CONFLICT                       
SEQRES   1 A  210  THR GLN VAL ILE GLN LEU LYS ARG TYR GLU PHE PRO GLN          
SEQRES   2 A  210  LEU PRO TYR LYS VAL ASP ALA LEU GLU PRO TYR ILE SER          
SEQRES   3 A  210  LYS ASP ILE ILE ASP VAL HIS TYR ASN GLY HIS HIS LYS          
SEQRES   4 A  210  GLY TYR VAL ASN GLY ALA ASN SER LEU LEU ASP ARG LEU          
SEQRES   5 A  210  GLU LYS LEU ILE LYS GLY ASP LEU PRO GLN GLY GLN TYR          
SEQRES   6 A  210  ASP LEU GLN GLY ILE LEU ARG GLY LEU THR PHE ASN ILE          
SEQRES   7 A  210  ASN GLY HIS LYS LEU HIS ALA ILE TYR TRP ASN ASN MET          
SEQRES   8 A  210  ALA PRO ALA GLY LYS GLY GLY GLY LYS PRO GLY GLY ALA          
SEQRES   9 A  210  LEU ALA ASP LEU ILE ASP LYS GLN TYR GLY SER PHE ASP          
SEQRES  10 A  210  ARG PHE LYS GLN VAL PHE SER GLU SER ALA ASN SER LEU          
SEQRES  11 A  210  PRO GLY SER GLY TRP THR VAL LEU TYR TYR ASP ASN GLU          
SEQRES  12 A  210  SER GLY ASN LEU GLN ILE MET THR VAL GLU ASN HIS PHE          
SEQRES  13 A  210  MET ASN HIS ILE ALA GLU LEU PRO VAL ILE LEU ILE VAL          
SEQRES  14 A  210  ASP GLU PHE GLU HIS ALA TYR TYR LEU GLN TYR LYS ASN          
SEQRES  15 A  210  LYS ARG GLY ASP TYR LEU ASN ALA TRP TRP ASN VAL VAL          
SEQRES  16 A  210  ASN TRP ASP ASP ALA GLU LYS ARG LEU GLN LYS TYR LEU          
SEQRES  17 A  210  ASN LYS                                                      
SEQRES   1 B  210  THR GLN VAL ILE GLN LEU LYS ARG TYR GLU PHE PRO GLN          
SEQRES   2 B  210  LEU PRO TYR LYS VAL ASP ALA LEU GLU PRO TYR ILE SER          
SEQRES   3 B  210  LYS ASP ILE ILE ASP VAL HIS TYR ASN GLY HIS HIS LYS          
SEQRES   4 B  210  GLY TYR VAL ASN GLY ALA ASN SER LEU LEU ASP ARG LEU          
SEQRES   5 B  210  GLU LYS LEU ILE LYS GLY ASP LEU PRO GLN GLY GLN TYR          
SEQRES   6 B  210  ASP LEU GLN GLY ILE LEU ARG GLY LEU THR PHE ASN ILE          
SEQRES   7 B  210  ASN GLY HIS LYS LEU HIS ALA ILE TYR TRP ASN ASN MET          
SEQRES   8 B  210  ALA PRO ALA GLY LYS GLY GLY GLY LYS PRO GLY GLY ALA          
SEQRES   9 B  210  LEU ALA ASP LEU ILE ASP LYS GLN TYR GLY SER PHE ASP          
SEQRES  10 B  210  ARG PHE LYS GLN VAL PHE SER GLU SER ALA ASN SER LEU          
SEQRES  11 B  210  PRO GLY SER GLY TRP THR VAL LEU TYR TYR ASP ASN GLU          
SEQRES  12 B  210  SER GLY ASN LEU GLN ILE MET THR VAL GLU ASN HIS PHE          
SEQRES  13 B  210  MET ASN HIS ILE ALA GLU LEU PRO VAL ILE LEU ILE VAL          
SEQRES  14 B  210  ASP GLU PHE GLU HIS ALA TYR TYR LEU GLN TYR LYS ASN          
SEQRES  15 B  210  LYS ARG GLY ASP TYR LEU ASN ALA TRP TRP ASN VAL VAL          
SEQRES  16 B  210  ASN TRP ASP ASP ALA GLU LYS ARG LEU GLN LYS TYR LEU          
SEQRES  17 B  210  ASN LYS                                                      
SEQRES   1 C  210  THR GLN VAL ILE GLN LEU LYS ARG TYR GLU PHE PRO GLN          
SEQRES   2 C  210  LEU PRO TYR LYS VAL ASP ALA LEU GLU PRO TYR ILE SER          
SEQRES   3 C  210  LYS ASP ILE ILE ASP VAL HIS TYR ASN GLY HIS HIS LYS          
SEQRES   4 C  210  GLY TYR VAL ASN GLY ALA ASN SER LEU LEU ASP ARG LEU          
SEQRES   5 C  210  GLU LYS LEU ILE LYS GLY ASP LEU PRO GLN GLY GLN TYR          
SEQRES   6 C  210  ASP LEU GLN GLY ILE LEU ARG GLY LEU THR PHE ASN ILE          
SEQRES   7 C  210  ASN GLY HIS LYS LEU HIS ALA ILE TYR TRP ASN ASN MET          
SEQRES   8 C  210  ALA PRO ALA GLY LYS GLY GLY GLY LYS PRO GLY GLY ALA          
SEQRES   9 C  210  LEU ALA ASP LEU ILE ASP LYS GLN TYR GLY SER PHE ASP          
SEQRES  10 C  210  ARG PHE LYS GLN VAL PHE SER GLU SER ALA ASN SER LEU          
SEQRES  11 C  210  PRO GLY SER GLY TRP THR VAL LEU TYR TYR ASP ASN GLU          
SEQRES  12 C  210  SER GLY ASN LEU GLN ILE MET THR VAL GLU ASN HIS PHE          
SEQRES  13 C  210  MET ASN HIS ILE ALA GLU LEU PRO VAL ILE LEU ILE VAL          
SEQRES  14 C  210  ASP GLU PHE GLU HIS ALA TYR TYR LEU GLN TYR LYS ASN          
SEQRES  15 C  210  LYS ARG GLY ASP TYR LEU ASN ALA TRP TRP ASN VAL VAL          
SEQRES  16 C  210  ASN TRP ASP ASP ALA GLU LYS ARG LEU GLN LYS TYR LEU          
SEQRES  17 C  210  ASN LYS                                                      
SEQRES   1 D  210  THR GLN VAL ILE GLN LEU LYS ARG TYR GLU PHE PRO GLN          
SEQRES   2 D  210  LEU PRO TYR LYS VAL ASP ALA LEU GLU PRO TYR ILE SER          
SEQRES   3 D  210  LYS ASP ILE ILE ASP VAL HIS TYR ASN GLY HIS HIS LYS          
SEQRES   4 D  210  GLY TYR VAL ASN GLY ALA ASN SER LEU LEU ASP ARG LEU          
SEQRES   5 D  210  GLU LYS LEU ILE LYS GLY ASP LEU PRO GLN GLY GLN TYR          
SEQRES   6 D  210  ASP LEU GLN GLY ILE LEU ARG GLY LEU THR PHE ASN ILE          
SEQRES   7 D  210  ASN GLY HIS LYS LEU HIS ALA ILE TYR TRP ASN ASN MET          
SEQRES   8 D  210  ALA PRO ALA GLY LYS GLY GLY GLY LYS PRO GLY GLY ALA          
SEQRES   9 D  210  LEU ALA ASP LEU ILE ASP LYS GLN TYR GLY SER PHE ASP          
SEQRES  10 D  210  ARG PHE LYS GLN VAL PHE SER GLU SER ALA ASN SER LEU          
SEQRES  11 D  210  PRO GLY SER GLY TRP THR VAL LEU TYR TYR ASP ASN GLU          
SEQRES  12 D  210  SER GLY ASN LEU GLN ILE MET THR VAL GLU ASN HIS PHE          
SEQRES  13 D  210  MET ASN HIS ILE ALA GLU LEU PRO VAL ILE LEU ILE VAL          
SEQRES  14 D  210  ASP GLU PHE GLU HIS ALA TYR TYR LEU GLN TYR LYS ASN          
SEQRES  15 D  210  LYS ARG GLY ASP TYR LEU ASN ALA TRP TRP ASN VAL VAL          
SEQRES  16 D  210  ASN TRP ASP ASP ALA GLU LYS ARG LEU GLN LYS TYR LEU          
SEQRES  17 D  210  ASN LYS                                                      
SEQRES   1 E  210  THR GLN VAL ILE GLN LEU LYS ARG TYR GLU PHE PRO GLN          
SEQRES   2 E  210  LEU PRO TYR LYS VAL ASP ALA LEU GLU PRO TYR ILE SER          
SEQRES   3 E  210  LYS ASP ILE ILE ASP VAL HIS TYR ASN GLY HIS HIS LYS          
SEQRES   4 E  210  GLY TYR VAL ASN GLY ALA ASN SER LEU LEU ASP ARG LEU          
SEQRES   5 E  210  GLU LYS LEU ILE LYS GLY ASP LEU PRO GLN GLY GLN TYR          
SEQRES   6 E  210  ASP LEU GLN GLY ILE LEU ARG GLY LEU THR PHE ASN ILE          
SEQRES   7 E  210  ASN GLY HIS LYS LEU HIS ALA ILE TYR TRP ASN ASN MET          
SEQRES   8 E  210  ALA PRO ALA GLY LYS GLY GLY GLY LYS PRO GLY GLY ALA          
SEQRES   9 E  210  LEU ALA ASP LEU ILE ASP LYS GLN TYR GLY SER PHE ASP          
SEQRES  10 E  210  ARG PHE LYS GLN VAL PHE SER GLU SER ALA ASN SER LEU          
SEQRES  11 E  210  PRO GLY SER GLY TRP THR VAL LEU TYR TYR ASP ASN GLU          
SEQRES  12 E  210  SER GLY ASN LEU GLN ILE MET THR VAL GLU ASN HIS PHE          
SEQRES  13 E  210  MET ASN HIS ILE ALA GLU LEU PRO VAL ILE LEU ILE VAL          
SEQRES  14 E  210  ASP GLU PHE GLU HIS ALA TYR TYR LEU GLN TYR LYS ASN          
SEQRES  15 E  210  LYS ARG GLY ASP TYR LEU ASN ALA TRP TRP ASN VAL VAL          
SEQRES  16 E  210  ASN TRP ASP ASP ALA GLU LYS ARG LEU GLN LYS TYR LEU          
SEQRES  17 E  210  ASN LYS                                                      
SEQRES   1 F  210  THR GLN VAL ILE GLN LEU LYS ARG TYR GLU PHE PRO GLN          
SEQRES   2 F  210  LEU PRO TYR LYS VAL ASP ALA LEU GLU PRO TYR ILE SER          
SEQRES   3 F  210  LYS ASP ILE ILE ASP VAL HIS TYR ASN GLY HIS HIS LYS          
SEQRES   4 F  210  GLY TYR VAL ASN GLY ALA ASN SER LEU LEU ASP ARG LEU          
SEQRES   5 F  210  GLU LYS LEU ILE LYS GLY ASP LEU PRO GLN GLY GLN TYR          
SEQRES   6 F  210  ASP LEU GLN GLY ILE LEU ARG GLY LEU THR PHE ASN ILE          
SEQRES   7 F  210  ASN GLY HIS LYS LEU HIS ALA ILE TYR TRP ASN ASN MET          
SEQRES   8 F  210  ALA PRO ALA GLY LYS GLY GLY GLY LYS PRO GLY GLY ALA          
SEQRES   9 F  210  LEU ALA ASP LEU ILE ASP LYS GLN TYR GLY SER PHE ASP          
SEQRES  10 F  210  ARG PHE LYS GLN VAL PHE SER GLU SER ALA ASN SER LEU          
SEQRES  11 F  210  PRO GLY SER GLY TRP THR VAL LEU TYR TYR ASP ASN GLU          
SEQRES  12 F  210  SER GLY ASN LEU GLN ILE MET THR VAL GLU ASN HIS PHE          
SEQRES  13 F  210  MET ASN HIS ILE ALA GLU LEU PRO VAL ILE LEU ILE VAL          
SEQRES  14 F  210  ASP GLU PHE GLU HIS ALA TYR TYR LEU GLN TYR LYS ASN          
SEQRES  15 F  210  LYS ARG GLY ASP TYR LEU ASN ALA TRP TRP ASN VAL VAL          
SEQRES  16 F  210  ASN TRP ASP ASP ALA GLU LYS ARG LEU GLN LYS TYR LEU          
SEQRES  17 F  210  ASN LYS                                                      
HET     FE  A 322       1                                                       
HET     FE  B 323       1                                                       
HET     FE  C 324       1                                                       
HET     FE  D 325       1                                                       
HET     FE  E 326       1                                                       
HET     FE  F 327       1                                                       
HETNAM      FE FE (III) ION                                                     
FORMUL   7   FE    6(FE 3+)                                                     
FORMUL  13  HOH   *321(H2 O)                                                    
HELIX    1  46 LYS A   27  ASN A   35  1                                   9    
HELIX    2  47 HIS A   37  LYS A   57  1                                  21    
HELIX    3  48 LEU A   67  ASN A   89  1                                  23    
HELIX    4  49 GLY A  103  TYR A  113  1                                  11    
HELIX    5  50 PHE A  116  SER A  129  1                                  14    
HELIX    6  51 GLU A  173  ALA A  175  5                                   3    
HELIX    7  52 TYR A  177  TYR A  180  1                                   4    
HELIX    8  44 ARG A  184  VAL A  194  1                                  11    
HELIX    9  54 TRP A  197  GLN A  205  1                                   9    
HELIX   10  46 LYS B   27  ASN B   35  1                                   9    
HELIX   11  47 HIS B   37  LYS B   57  1                                  21    
HELIX   12  48 LEU B   67  ASN B   89  1                                  23    
HELIX   13  49 GLY B  103  TYR B  113  1                                  11    
HELIX   14  50 PHE B  116  SER B  129  1                                  14    
HELIX   15  51 GLU B  173  ALA B  175  5                                   3    
HELIX   16  52 TYR B  177  TYR B  180  1                                   4    
HELIX   17  53 ARG B  184  ASN B  193  1                                  10    
HELIX   18  54 TRP B  197  GLN B  205  1                                   9    
HELIX   19  46 LYS C   27  ASN C   35  1                                   9    
HELIX   20  47 HIS C   37  LYS C   57  1                                  21    
HELIX   21  48 LEU C   67  ASN C   89  1                                  23    
HELIX   22  49 GLY C  103  TYR C  113  1                                  11    
HELIX   23  50 PHE C  116  SER C  129  1                                  14    
HELIX   24  51 GLU C  173  ALA C  175  5                                   3    
HELIX   25  52 TYR C  177  TYR C  180  1                                   4    
HELIX   26  44 ARG C  184  VAL C  194  1                                  11    
HELIX   27  54 TRP C  197  GLN C  205  1                                   9    
HELIX   28  46 LYS D   27  ASN D   35  1                                   9    
HELIX   29  47 HIS D   37  LYS D   57  1                                  21    
HELIX   30  48 LEU D   67  ASN D   89  1                                  23    
HELIX   31  49 GLY D  103  TYR D  113  1                                  11    
HELIX   32  50 PHE D  116  SER D  129  1                                  14    
HELIX   33  51 GLU D  173  ALA D  175  5                                   3    
HELIX   34  52 TYR D  177  TYR D  180  1                                   4    
HELIX   35  44 ARG D  184  VAL D  194  1                                  11    
HELIX   36  54 TRP D  197  GLN D  205  1                                   9    
HELIX   37  46 LYS E   27  ASN E   35  1                                   9    
HELIX   38  47 HIS E   37  LYS E   57  1                                  21    
HELIX   39  48 LEU E   67  ASN E   89  1                                  23    
HELIX   40  49 GLY E  103  TYR E  113  1                                  11    
HELIX   41  50 PHE E  116  SER E  129  1                                  14    
HELIX   42  51 GLU E  173  ALA E  175  5                                   3    
HELIX   43  52 TYR E  177  TYR E  180  1                                   4    
HELIX   44  44 ARG E  184  VAL E  194  1                                  11    
HELIX   45  54 TRP E  197  GLN E  205  1                                   9    
HELIX   46  46 LYS F   27  ASN F   35  1                                   9    
HELIX   47  47 HIS F   37  LYS F   57  1                                  21    
HELIX   48  48 LEU F   67  ASN F   89  1                                  23    
HELIX   49  49 GLY F  103  TYR F  113  1                                  11    
HELIX   50  50 PHE F  116  SER F  129  1                                  14    
HELIX   51  51 GLU F  173  ALA F  175  5                                   3    
HELIX   52  52 TYR F  177  TYR F  180  1                                   4    
HELIX   53  53 ARG F  184  ASN F  193  1                                  10    
HELIX   54  54 TRP F  197  GLN F  205  1                                   9    
SHEET    1   A 3 LEU A 147  GLU A 153  0                                        
SHEET    2   A 3 GLY A 134  TYR A 140 -1  N  TYR A 139   O  GLN A 148           
SHEET    3   A 3 PRO A 164  ASP A 170 -1  N  VAL A 169   O  THR A 136           
SHEET    1   B 3 LEU B 147  GLU B 153  0                                        
SHEET    2   B 3 GLY B 134  TYR B 140 -1  N  TYR B 139   O  GLN B 148           
SHEET    3   B 3 PRO B 164  ASP B 170 -1  N  VAL B 169   O  THR B 136           
SHEET    1   C 3 LEU C 147  GLU C 153  0                                        
SHEET    2   C 3 GLY C 134  TYR C 140 -1  N  TYR C 139   O  GLN C 148           
SHEET    3   C 3 PRO C 164  ASP C 170 -1  N  VAL C 169   O  THR C 136           
SHEET    1   D 3 LEU D 147  GLU D 153  0                                        
SHEET    2   D 3 GLY D 134  TYR D 140 -1  N  TYR D 139   O  GLN D 148           
SHEET    3   D 3 PRO D 164  ASP D 170 -1  N  VAL D 169   O  THR D 136           
SHEET    1   E 3 LEU E 147  GLU E 153  0                                        
SHEET    2   E 3 GLY E 134  TYR E 140 -1  N  TYR E 139   O  GLN E 148           
SHEET    3   E 3 PRO E 164  ASP E 170 -1  N  VAL E 169   O  THR E 136           
SHEET    1   F 3 LEU F 147  GLU F 153  0                                        
SHEET    2   F 3 GLY F 134  TYR F 140 -1  N  TYR F 139   O  GLN F 148           
SHEET    3   F 3 PRO F 164  ASP F 170 -1  N  VAL F 169   O  THR F 136           
LINK        FE    FE A 322                 O   HOH A 377     1555   1555  2.08  
LINK        FE    FE B 323                 O   HOH B 368     1555   1555  2.14  
LINK        FE    FE C 324                 O   HOH C 372     1555   1555  1.90  
LINK        FE    FE D 325                 O   HOH D 377     1555   1555  1.99  
LINK        FE    FE E 326                 O   HOH E 379     1555   1555  2.02  
LINK        FE    FE F 327                 O   HOH F 395     1555   1555  2.13  
LINK        FE    FE A 322                 NE2 HIS A  33     1555   1555  2.23  
LINK        FE    FE A 322                 NE2 HIS A  84     1555   1555  2.19  
LINK        FE    FE A 322                 OD2 ASP A 170     1555   1555  1.86  
LINK        FE    FE A 322                 NE2 HIS A 174     1555   1555  2.09  
LINK        FE    FE B 323                 NE2 HIS B  33     1555   1555  2.27  
LINK        FE    FE B 323                 OD2 ASP B 170     1555   1555  1.95  
LINK        FE    FE B 323                 NE2 HIS B  84     1555   1555  2.04  
LINK        FE    FE B 323                 NE2 HIS B 174     1555   1555  2.17  
LINK        FE    FE C 324                 OD2 ASP C 170     1555   1555  1.92  
LINK        FE    FE C 324                 NE2 HIS C 174     1555   1555  2.04  
LINK        FE    FE C 324                 NE2 HIS C  33     1555   1555  2.18  
LINK        FE    FE C 324                 NE2 HIS C  84     1555   1555  2.20  
LINK        FE    FE D 325                 NE2 HIS D  33     1555   1555  2.27  
LINK        FE    FE D 325                 NE2 HIS D 174     1555   1555  2.14  
LINK        FE    FE D 325                 OD2 ASP D 170     1555   1555  1.88  
LINK        FE    FE D 325                 NE2 HIS D  84     1555   1555  2.17  
LINK        FE    FE E 326                 NE2 HIS E  84     1555   1555  2.14  
LINK        FE    FE E 326                 NE2 HIS E 174     1555   1555  2.07  
LINK        FE    FE E 326                 OD2 ASP E 170     1555   1555  1.96  
LINK        FE    FE E 326                 NE2 HIS E  33     1555   1555  2.15  
LINK        FE    FE F 327                 NE2 HIS F  33     1555   1555  2.23  
LINK        FE    FE F 327                 OD2 ASP F 170     1555   1555  1.96  
LINK        FE    FE F 327                 NE2 HIS F 174     1555   1555  2.17  
LINK        FE    FE F 327                 NE2 HIS F  84     1555   1555  2.12  
CISPEP   1 GLU A   22    PRO A   23          0         0.25                     
CISPEP   2 GLU B   22    PRO B   23          0         0.21                     
CISPEP   3 GLU C   22    PRO C   23          0        -0.01                     
CISPEP   4 GLU D   22    PRO D   23          0         0.17                     
CISPEP   5 GLU E   22    PRO E   23          0         0.28                     
CISPEP   6 GLU F   22    PRO F   23          0         0.28                     
SITE     1 AC1  5 HIS A  33  HIS A  84  ASP A 170  HIS A 174                    
SITE     2 AC1  5 HOH A 377                                                     
SITE     1 AC2  5 HIS B  33  HIS B  84  ASP B 170  HIS B 174                    
SITE     2 AC2  5 HOH B 368                                                     
SITE     1 AC3  5 HIS C  33  HIS C  84  ASP C 170  HIS C 174                    
SITE     2 AC3  5 HOH C 372                                                     
SITE     1 AC4  5 HIS D  33  HIS D  84  ASP D 170  HIS D 174                    
SITE     2 AC4  5 HOH D 377                                                     
SITE     1 AC5  5 HIS E  33  HIS E  84  ASP E 170  HIS E 174                    
SITE     2 AC5  5 HOH E 379                                                     
SITE     1 AC6  5 HIS F  33  HIS F  84  ASP F 170  HIS F 174                    
SITE     2 AC6  5 HOH F 395                                                     
CRYST1  168.100   91.300   85.700  90.00  91.40  90.00 C 1 2 1      24          
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      0.005949  0.000000  0.000145        0.00000                         
SCALE2      0.000000  0.010953  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011672        0.00000                         
MTRIX1   1 -0.506638  0.005294  0.862142       88.40617    1                    
MTRIX2   1 -0.006206 -0.999978  0.002493       90.81549    1                    
MTRIX3   1  0.862136 -0.004088  0.506660      -50.50517    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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