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Entry: 1AOR
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HEADER    OXIDOREDUCTASE                          13-FEB-95   1AOR              
TITLE     STRUCTURE OF A HYPERTHERMOPHILIC TUNGSTOPTERIN ENZYME,                
TITLE    2 ALDEHYDE FERREDOXIN OXIDOREDUCTASE                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALDEHYDE FERREDOXIN OXIDOREDUCTASE;                        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PYROCOCCUS FURIOSUS;                            
SOURCE   3 ORGANISM_TAXID: 2261                                                 
KEYWDS    OXIDOREDUCTASE                                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.K.CHAN,S.MUKUND,A.KLETZIN,M.W.W.ADAMS,D.C.REES                      
REVDAT   4   24-MAR-09 1AOR    1       LINK   ATOM   CONECT                     
REVDAT   3   24-FEB-09 1AOR    1       VERSN                                    
REVDAT   2   01-APR-03 1AOR    1       JRNL                                     
REVDAT   1   20-APR-95 1AOR    0                                                
JRNL        AUTH   M.K.CHAN,S.MUKUND,A.KLETZIN,M.W.ADAMS,D.C.REES               
JRNL        TITL   STRUCTURE OF A HYPERTHERMOPHILIC TUNGSTOPTERIN               
JRNL        TITL 2 ENZYME, ALDEHYDE FERREDOXIN OXIDOREDUCTASE.                  
JRNL        REF    SCIENCE                       V. 267  1463 1995              
JRNL        REFN                   ISSN 0036-8075                               
JRNL        PMID   7878465                                                      
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   A.KLETZIN,S.MUKUND,T.L.KELLEY-CROUSE,M.K.CHAN,               
REMARK   1  AUTH 2 D.C.REES,M.W.W.ADAMS                                         
REMARK   1  TITL   MOLECULAR CHARACTERIZATION OF THE GENES ENCODING             
REMARK   1  TITL 2 TWO TUNGSTEN-CONTAINING ENZYMES FROM                         
REMARK   1  TITL 3 HYPERTHERMOPHILIC ARCHAEA: ALDEHYDE FERREDOXIN               
REMARK   1  TITL 4 OXIDOREDUCTASE FROM PYROCOCCUS FURIOSUS AND                  
REMARK   1  TITL 5 FORMALDEHYDE FERREDOXIN OXIDOREDUCTASE FROM                  
REMARK   1  TITL 6 THERMOCOCCUS LITORALIS                                       
REMARK   1  REF    TO BE PUBLISHED                                              
REMARK   1  REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR                                               
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 10.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 89.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 55520                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.155                           
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9386                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 129                                     
REMARK   3   SOLVENT ATOMS            : 373                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 2.58                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS:                                           
REMARK   3  PLEASE NOTE THAT ALL RESIDUES WERE BUILT TO FIT THE BEST            
REMARK   3  POSSIBLE OBSERVED DENSITY.  THOSE SIDE CHAIN ATOMS WHICH            
REMARK   3  SEEMED UNRELIABLE HAD THEIR OCCUPANCIES FIXED AT 0.0.               
REMARK   4                                                                      
REMARK   4 1AOR COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : NULL                               
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 56373                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.4                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: X-PLOR                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.12                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       40.46950            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       79.89600            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       54.16600            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       79.89600            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       40.46950            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       54.16600            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6250 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 35650 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -101.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     ARG A    7   NE    CZ    NH1   NH2                               
REMARK 480     GLU A   26   CG    CD    OE1   OE2                               
REMARK 480     LYS A  151   CG    CD    CE    NZ                                
REMARK 480     GLU A  156   CG    CD    OE1   OE2                               
REMARK 480     LYS A  214   CG    CD    CE    NZ                                
REMARK 480     ARG A  229   NE    CZ    NH1   NH2                               
REMARK 480     ASN A  230   CG    OD1   ND2                                     
REMARK 480     ARG A  300   NE    CZ    NH1   NH2                               
REMARK 480     GLU A  366   CG    CD    OE1   OE2                               
REMARK 480     ASP A  517   CG    OD1   OD2                                     
REMARK 480     ARG A  547   NE    CZ    NH1   NH2                               
REMARK 480     GLU A  587   CG    CD    OE1   OE2                               
REMARK 480     GLU A  594   CG    CD    OE1   OE2                               
REMARK 480     GLU A  597   CG    CD    OE1   OE2                               
REMARK 480     GLU A  603   CG    CD    OE1   OE2                               
REMARK 480     ARG B    7   NE    CZ    NH1   NH2                               
REMARK 480     GLU B   26   CG    CD    OE1   OE2                               
REMARK 480     GLU B  117   CG    CD    OE1   OE2                               
REMARK 480     LYS B  118   CG    CD    CE    NZ                                
REMARK 480     LYS B  125   CG    CD    CE    NZ                                
REMARK 480     LYS B  151   CG    CD    CE    NZ                                
REMARK 480     GLU B  156   CG    CD    OE1   OE2                               
REMARK 480     LYS B  157   CG    CD    CE    NZ                                
REMARK 480     LYS B  214   CG    CD    CE    NZ                                
REMARK 480     GLN B  215   CG    CD    OE1   NE2                               
REMARK 480     ARG B  300   NE    CZ    NH1   NH2                               
REMARK 480     GLU B  366   CG    CD    OE1   OE2                               
REMARK 480     ASP B  517   CG    OD1   OD2                                     
REMARK 480     ARG B  547   NE    CZ    NH1   NH2                               
REMARK 480     GLU B  587   CG    CD    OE1   OE2                               
REMARK 480     GLU B  594   CG    CD    OE1   OE2                               
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    ALA A 184   N   -  CA  -  C   ANGL. DEV. = -19.8 DEGREES          
REMARK 500    GLY A 185   N   -  CA  -  C   ANGL. DEV. =  19.2 DEGREES          
REMARK 500    LEU A 255   CA  -  CB  -  CG  ANGL. DEV. =  15.9 DEGREES          
REMARK 500    ALA B 184   N   -  CA  -  C   ANGL. DEV. = -23.6 DEGREES          
REMARK 500    GLY B 185   N   -  CA  -  C   ANGL. DEV. =  16.9 DEGREES          
REMARK 500    LEU B 255   CA  -  CB  -  CG  ANGL. DEV. =  17.2 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    LEU A  32      -61.45     67.08                                   
REMARK 500    SER A  34     -113.07     43.83                                   
REMARK 500    PRO A  48       -9.72    -57.64                                   
REMARK 500    ASP A 126     -117.52     58.57                                   
REMARK 500    ALA A 184       77.72   -101.75                                   
REMARK 500    ASP A 326      101.19    -54.49                                   
REMARK 500    ALA A 426       40.59    -66.28                                   
REMARK 500    ALA A 432       84.97   -161.53                                   
REMARK 500    ASN A 451       71.02   -163.12                                   
REMARK 500    LEU B  32      -60.73     59.54                                   
REMARK 500    SER B  34     -110.67     32.91                                   
REMARK 500    ASP B 126     -119.54     58.19                                   
REMARK 500    ARG B 284     -179.15   -173.14                                   
REMARK 500    ASP B 326      101.20    -53.60                                   
REMARK 500    ALA B 426       35.93    -64.78                                   
REMARK 500    ALA B 432       83.23   -163.71                                   
REMARK 500    ASN B 451       65.34   -165.80                                   
REMARK 500    TYR B 452       71.30    -66.97                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (11X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500   M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                
REMARK 500     ALA A 184        45.2      L          L   OUTSIDE RANGE          
REMARK 500     ILE A 449        22.8      L          L   OUTSIDE RANGE          
REMARK 500     ALA B 184        47.2      L          L   OUTSIDE RANGE          
REMARK 500     ILE B 449        22.8      L          L   OUTSIDE RANGE          
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                             PTE A 609  MG1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A  93   O                                                      
REMARK 620 2 ALA A 183   O    89.7                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE A 606  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 332   OE1                                                    
REMARK 620 2 HIS A 383   NE2  91.3                                              
REMARK 620 3 GLU B 332   OE1 134.7 111.9                                        
REMARK 620 4 HIS B 383   NE2 109.7 118.5  93.0                                  
REMARK 620 5 GLU A 332   OE2  52.4 141.7  91.2  88.7                            
REMARK 620 6 GLU B 332   OE2  92.4  88.4  52.2 143.6  82.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             PTE B 608  MG1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN B  93   O                                                      
REMARK 620 2 ALA B 183   O    90.6                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 607  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 181   O                                                      
REMARK 620 2 PTE A 609   O8  126.2                                              
REMARK 620 3 HOH A5011   O   108.2  88.3                                        
REMARK 620 4 HOH A5013   O    96.1 137.6  79.5                                  
REMARK 620 5 HOH A5012   O   112.9  75.8 137.7  86.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B 606  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 181   O                                                      
REMARK 620 2 PTE B 608   O8  102.7                                              
REMARK 620 3 HOH B5026   O   106.7  76.0                                        
REMARK 620 4 HOH B5024   O   123.2 133.2  82.4                                  
REMARK 620 5 HOH B5025   O   105.5  80.1 143.3  94.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 700                                                                      
REMARK 700 SHEET                                                                
REMARK 700 HELIX AND SHEET ENTRIES HAVE BEEN AUTOMATICALLY GENERATED            
REMARK 700 BY THE PDB USING A PROGRAM BASED ON DSSP OF W. KABSCH AND            
REMARK 700 C. SANDER                                                            
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: PT1                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: TUNGSTOPTERIN COFACTOR CONSISTING OF A SINGLE      
REMARK 800  TUNGSTEN CENTER BOUND TO TWO MOLYBDOPTERIN LIGANDS (SUBUNIT A)      
REMARK 800 SITE_IDENTIFIER: PT2                                                 
REMARK 800 EVIDENCE_CODE: UNKNOWN                                               
REMARK 800 SITE_DESCRIPTION: TUNGSTOPTERIN COFACTOR CONSISTING OF A SINGLE      
REMARK 800  TUNGSTEN CENTER BOUND TO TWO MOLYBDOPTERIN LIGANDS (SUBUNIT B).     
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE A 606                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 607                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 606                  
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 A 608                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PTE A 609                 
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 B 607                 
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PTE B 608                 
DBREF  1AOR A    1   605  UNP    Q51739   AOR_PYRFU        1    605             
DBREF  1AOR B    1   605  UNP    Q51739   AOR_PYRFU        1    605             
SEQRES   1 A  605  MET TYR GLY ASN TRP GLY ARG PHE ILE ARG VAL ASN LEU          
SEQRES   2 A  605  SER THR GLY ASP ILE LYS VAL GLU GLU TYR ASP GLU GLU          
SEQRES   3 A  605  LEU ALA LYS LYS TRP LEU GLY SER ARG GLY LEU ALA ILE          
SEQRES   4 A  605  TYR LEU LEU LEU LYS GLU MET ASP PRO THR VAL ASP PRO          
SEQRES   5 A  605  LEU SER PRO GLU ASN LYS LEU ILE ILE ALA ALA GLY PRO          
SEQRES   6 A  605  LEU THR GLY THR SER ALA PRO THR GLY GLY ARG TYR ASN          
SEQRES   7 A  605  VAL VAL THR LYS SER PRO LEU THR GLY PHE ILE THR MET          
SEQRES   8 A  605  ALA ASN SER GLY GLY TYR PHE GLY ALA GLU LEU LYS PHE          
SEQRES   9 A  605  ALA GLY TYR ASP ALA ILE VAL VAL GLU GLY LYS ALA GLU          
SEQRES  10 A  605  LYS PRO VAL TYR ILE TYR ILE LYS ASP GLU HIS ILE GLU          
SEQRES  11 A  605  ILE ARG ASP ALA SER HIS ILE TRP GLY LYS LYS VAL SER          
SEQRES  12 A  605  GLU THR GLU ALA THR ILE ARG LYS GLU VAL GLY SER GLU          
SEQRES  13 A  605  LYS VAL LYS ILE ALA SER ILE GLY PRO ALA GLY GLU ASN          
SEQRES  14 A  605  LEU VAL LYS PHE ALA ALA ILE MET ASN ASP GLY HIS ARG          
SEQRES  15 A  605  ALA ALA GLY ARG GLY GLY VAL GLY ALA VAL MET GLY SER          
SEQRES  16 A  605  LYS ASN LEU LYS ALA ILE ALA VAL GLU GLY SER LYS THR          
SEQRES  17 A  605  VAL PRO ILE ALA ASP LYS GLN LYS PHE MET LEU VAL VAL          
SEQRES  18 A  605  ARG GLU LYS VAL ASN LYS LEU ARG ASN ASP PRO VAL ALA          
SEQRES  19 A  605  GLY GLY GLY LEU PRO LYS TYR GLY THR ALA VAL LEU VAL          
SEQRES  20 A  605  ASN ILE ILE ASN GLU ASN GLY LEU TYR PRO VAL LYS ASN          
SEQRES  21 A  605  PHE GLN THR GLY VAL TYR PRO TYR ALA TYR GLU GLN SER          
SEQRES  22 A  605  GLY GLU ALA MET ALA ALA LYS TYR LEU VAL ARG ASN LYS          
SEQRES  23 A  605  PRO CYS TYR ALA CYS PRO ILE GLY CYS GLY ARG VAL ASN          
SEQRES  24 A  605  ARG LEU PRO THR VAL GLY GLU THR GLU GLY PRO GLU TYR          
SEQRES  25 A  605  GLU SER VAL TRP ALA LEU GLY ALA ASN LEU GLY ILE ASN          
SEQRES  26 A  605  ASP LEU ALA SER ILE ILE GLU ALA ASN HIS MET CYS ASP          
SEQRES  27 A  605  GLU LEU GLY LEU ASP THR ILE SER THR GLY GLY THR LEU          
SEQRES  28 A  605  ALA THR ALA MET GLU LEU TYR GLU LYS GLY HIS ILE LYS          
SEQRES  29 A  605  ASP GLU GLU LEU GLY ASP ALA PRO PRO PHE ARG TRP GLY          
SEQRES  30 A  605  ASN THR GLU VAL LEU HIS TYR TYR ILE GLU LYS ILE ALA          
SEQRES  31 A  605  LYS ARG GLU GLY PHE GLY ASP LYS LEU ALA GLU GLY SER          
SEQRES  32 A  605  TYR ARG LEU ALA GLU SER TYR GLY HIS PRO GLU LEU SER          
SEQRES  33 A  605  MET THR VAL LYS LYS LEU GLU LEU PRO ALA TYR ASP PRO          
SEQRES  34 A  605  ARG GLY ALA GLU GLY HIS GLY LEU GLY TYR ALA THR ASN          
SEQRES  35 A  605  ASN ARG GLY GLY CYS HIS ILE LYS ASN TYR MET ILE SER          
SEQRES  36 A  605  PRO GLU ILE LEU GLY TYR PRO TYR LYS MET ASP PRO HIS          
SEQRES  37 A  605  ASP VAL SER ASP ASP LYS ILE LYS MET LEU ILE LEU PHE          
SEQRES  38 A  605  GLN ASP LEU THR ALA LEU ILE ASP SER ALA GLY LEU CYS          
SEQRES  39 A  605  LEU PHE THR THR PHE GLY LEU GLY ALA ASP ASP TYR ARG          
SEQRES  40 A  605  ASP LEU LEU ASN ALA ALA LEU GLY TRP ASP PHE THR THR          
SEQRES  41 A  605  GLU ASP TYR LEU LYS ILE GLY GLU ARG ILE TRP ASN ALA          
SEQRES  42 A  605  GLU ARG LEU PHE ASN LEU LYS ALA GLY LEU ASP PRO ALA          
SEQRES  43 A  605  ARG ASP ASP THR LEU PRO LYS ARG PHE LEU GLU GLU PRO          
SEQRES  44 A  605  MET PRO GLU GLY PRO ASN LYS GLY HIS THR VAL ARG LEU          
SEQRES  45 A  605  LYS GLU MET LEU PRO ARG TYR TYR LYS LEU ARG GLY TRP          
SEQRES  46 A  605  THR GLU ASP GLY LYS ILE PRO LYS GLU LYS LEU GLU GLU          
SEQRES  47 A  605  LEU GLY ILE ALA GLU PHE TYR                                  
SEQRES   1 B  605  MET TYR GLY ASN TRP GLY ARG PHE ILE ARG VAL ASN LEU          
SEQRES   2 B  605  SER THR GLY ASP ILE LYS VAL GLU GLU TYR ASP GLU GLU          
SEQRES   3 B  605  LEU ALA LYS LYS TRP LEU GLY SER ARG GLY LEU ALA ILE          
SEQRES   4 B  605  TYR LEU LEU LEU LYS GLU MET ASP PRO THR VAL ASP PRO          
SEQRES   5 B  605  LEU SER PRO GLU ASN LYS LEU ILE ILE ALA ALA GLY PRO          
SEQRES   6 B  605  LEU THR GLY THR SER ALA PRO THR GLY GLY ARG TYR ASN          
SEQRES   7 B  605  VAL VAL THR LYS SER PRO LEU THR GLY PHE ILE THR MET          
SEQRES   8 B  605  ALA ASN SER GLY GLY TYR PHE GLY ALA GLU LEU LYS PHE          
SEQRES   9 B  605  ALA GLY TYR ASP ALA ILE VAL VAL GLU GLY LYS ALA GLU          
SEQRES  10 B  605  LYS PRO VAL TYR ILE TYR ILE LYS ASP GLU HIS ILE GLU          
SEQRES  11 B  605  ILE ARG ASP ALA SER HIS ILE TRP GLY LYS LYS VAL SER          
SEQRES  12 B  605  GLU THR GLU ALA THR ILE ARG LYS GLU VAL GLY SER GLU          
SEQRES  13 B  605  LYS VAL LYS ILE ALA SER ILE GLY PRO ALA GLY GLU ASN          
SEQRES  14 B  605  LEU VAL LYS PHE ALA ALA ILE MET ASN ASP GLY HIS ARG          
SEQRES  15 B  605  ALA ALA GLY ARG GLY GLY VAL GLY ALA VAL MET GLY SER          
SEQRES  16 B  605  LYS ASN LEU LYS ALA ILE ALA VAL GLU GLY SER LYS THR          
SEQRES  17 B  605  VAL PRO ILE ALA ASP LYS GLN LYS PHE MET LEU VAL VAL          
SEQRES  18 B  605  ARG GLU LYS VAL ASN LYS LEU ARG ASN ASP PRO VAL ALA          
SEQRES  19 B  605  GLY GLY GLY LEU PRO LYS TYR GLY THR ALA VAL LEU VAL          
SEQRES  20 B  605  ASN ILE ILE ASN GLU ASN GLY LEU TYR PRO VAL LYS ASN          
SEQRES  21 B  605  PHE GLN THR GLY VAL TYR PRO TYR ALA TYR GLU GLN SER          
SEQRES  22 B  605  GLY GLU ALA MET ALA ALA LYS TYR LEU VAL ARG ASN LYS          
SEQRES  23 B  605  PRO CYS TYR ALA CYS PRO ILE GLY CYS GLY ARG VAL ASN          
SEQRES  24 B  605  ARG LEU PRO THR VAL GLY GLU THR GLU GLY PRO GLU TYR          
SEQRES  25 B  605  GLU SER VAL TRP ALA LEU GLY ALA ASN LEU GLY ILE ASN          
SEQRES  26 B  605  ASP LEU ALA SER ILE ILE GLU ALA ASN HIS MET CYS ASP          
SEQRES  27 B  605  GLU LEU GLY LEU ASP THR ILE SER THR GLY GLY THR LEU          
SEQRES  28 B  605  ALA THR ALA MET GLU LEU TYR GLU LYS GLY HIS ILE LYS          
SEQRES  29 B  605  ASP GLU GLU LEU GLY ASP ALA PRO PRO PHE ARG TRP GLY          
SEQRES  30 B  605  ASN THR GLU VAL LEU HIS TYR TYR ILE GLU LYS ILE ALA          
SEQRES  31 B  605  LYS ARG GLU GLY PHE GLY ASP LYS LEU ALA GLU GLY SER          
SEQRES  32 B  605  TYR ARG LEU ALA GLU SER TYR GLY HIS PRO GLU LEU SER          
SEQRES  33 B  605  MET THR VAL LYS LYS LEU GLU LEU PRO ALA TYR ASP PRO          
SEQRES  34 B  605  ARG GLY ALA GLU GLY HIS GLY LEU GLY TYR ALA THR ASN          
SEQRES  35 B  605  ASN ARG GLY GLY CYS HIS ILE LYS ASN TYR MET ILE SER          
SEQRES  36 B  605  PRO GLU ILE LEU GLY TYR PRO TYR LYS MET ASP PRO HIS          
SEQRES  37 B  605  ASP VAL SER ASP ASP LYS ILE LYS MET LEU ILE LEU PHE          
SEQRES  38 B  605  GLN ASP LEU THR ALA LEU ILE ASP SER ALA GLY LEU CYS          
SEQRES  39 B  605  LEU PHE THR THR PHE GLY LEU GLY ALA ASP ASP TYR ARG          
SEQRES  40 B  605  ASP LEU LEU ASN ALA ALA LEU GLY TRP ASP PHE THR THR          
SEQRES  41 B  605  GLU ASP TYR LEU LYS ILE GLY GLU ARG ILE TRP ASN ALA          
SEQRES  42 B  605  GLU ARG LEU PHE ASN LEU LYS ALA GLY LEU ASP PRO ALA          
SEQRES  43 B  605  ARG ASP ASP THR LEU PRO LYS ARG PHE LEU GLU GLU PRO          
SEQRES  44 B  605  MET PRO GLU GLY PRO ASN LYS GLY HIS THR VAL ARG LEU          
SEQRES  45 B  605  LYS GLU MET LEU PRO ARG TYR TYR LYS LEU ARG GLY TRP          
SEQRES  46 B  605  THR GLU ASP GLY LYS ILE PRO LYS GLU LYS LEU GLU GLU          
SEQRES  47 B  605  LEU GLY ILE ALA GLU PHE TYR                                  
HET     FE  A 606       1                                                       
HET     NA  A 607       1                                                       
HET     NA  B 606       1                                                       
HET    SF4  A 608       8                                                       
HET    PTE  A 609      52                                                       
HET    SF4  B 607       8                                                       
HET    PTE  B 608      52                                                       
HETNAM      FE FE (III) ION                                                     
HETNAM      NA SODIUM ION                                                       
HETNAM     SF4 IRON/SULFUR CLUSTER                                              
HETNAM     PTE TUNGSTOPTERIN COFACTOR                                           
FORMUL   3   FE    FE 3+                                                        
FORMUL   4   NA    2(NA 1+)                                                     
FORMUL   6  SF4    2(FE4 S4)                                                    
FORMUL   7  PTE    2(C20 H29 MG N10 O14 P2 S4 W)                                
FORMUL  10  HOH   *379(H2 O)                                                    
HELIX    1   1 GLU A   25  TRP A   31  1                                   7    
HELIX    2   2 SER A   34  GLU A   45  1                                  12    
HELIX    3   3 PHE A   98  PHE A  104  1                                   7    
HELIX    4   4 VAL A  142  VAL A  153  1                                  12    
HELIX    5   5 PRO A  165  GLU A  168  1                                   4    
HELIX    6   6 VAL A  189  LYS A  196  1                                   8    
HELIX    7   7 LYS A  214  ASN A  230  1                                  17    
HELIX    8   8 PRO A  232  GLY A  235  1                                   4    
HELIX    9   9 GLY A  237  TYR A  241  1                                   5    
HELIX   10  10 THR A  243  GLU A  252  5                                  10    
HELIX   11  11 ALA A  269  GLN A  272  5                                   4    
HELIX   12  12 GLY A  274  LYS A  280  1                                   7    
HELIX   13  13 TYR A  312  LEU A  318  1                                   7    
HELIX   14  14 ALA A  320  LEU A  322  5                                   3    
HELIX   15  15 LEU A  327  LEU A  340  1                                  14    
HELIX   16  16 THR A  344  GLU A  359  1                                  16    
HELIX   17  17 ASP A  365  LEU A  368  1                                   4    
HELIX   18  18 THR A  379  ALA A  390  5                                  12    
HELIX   19  19 GLY A  394  GLU A  401  5                                   8    
HELIX   20  20 SER A  403  TYR A  410  1                                   8    
HELIX   21  21 PRO A  413  LEU A  415  5                                   3    
HELIX   22  22 PRO A  429  GLY A  431  5                                   3    
HELIX   23  23 GLU A  433  THR A  441  1                                   9    
HELIX   24  24 ILE A  449  ASN A  451  5                                   3    
HELIX   25  25 ILE A  454  GLU A  457  1                                   4    
HELIX   26  26 ASP A  472  ALA A  491  1                                  20    
HELIX   27  27 LEU A  495  THR A  498  5                                   4    
HELIX   28  28 ALA A  503  LEU A  514  1                                  12    
HELIX   29  29 THR A  520  ALA A  541  1                                  22    
HELIX   30  30 PRO A  545  ASP A  548  1                                   4    
HELIX   31  31 LYS A  553  GLU A  557  1                                   5    
HELIX   32  32 LEU A  572  ARG A  583  1                                  12    
HELIX   33  33 LYS A  593  LEU A  599  1                                   7    
HELIX   34  34 ALA A  602  PHE A  604  5                                   3    
HELIX   35  35 GLU B   25  TRP B   31  1                                   7    
HELIX   36  36 SER B   34  GLU B   45  1                                  12    
HELIX   37  37 PHE B   98  ALA B  105  1                                   8    
HELIX   38  38 VAL B  142  GLU B  152  1                                  11    
HELIX   39  39 PRO B  165  GLU B  168  1                                   4    
HELIX   40  40 VAL B  189  LYS B  196  1                                   8    
HELIX   41  41 LYS B  214  ASN B  230  1                                  17    
HELIX   42  42 PRO B  232  GLY B  235  1                                   4    
HELIX   43  43 GLY B  237  TYR B  241  1                                   5    
HELIX   44  44 THR B  243  GLU B  252  5                                  10    
HELIX   45  45 ALA B  269  GLN B  272  5                                   4    
HELIX   46  46 GLY B  274  LYS B  280  1                                   7    
HELIX   47  47 TYR B  312  ALA B  317  1                                   6    
HELIX   48  48 ALA B  320  LEU B  322  5                                   3    
HELIX   49  49 LEU B  327  LEU B  340  1                                  14    
HELIX   50  50 THR B  344  GLU B  359  1                                  16    
HELIX   51  51 ASP B  365  LEU B  368  1                                   4    
HELIX   52  52 THR B  379  ALA B  390  5                                  12    
HELIX   53  53 GLY B  394  GLU B  401  5                                   8    
HELIX   54  54 SER B  403  TYR B  410  1                                   8    
HELIX   55  55 PRO B  413  LEU B  415  5                                   3    
HELIX   56  56 PRO B  429  GLY B  431  5                                   3    
HELIX   57  57 GLU B  433  THR B  441  1                                   9    
HELIX   58  58 ILE B  449  ASN B  451  5                                   3    
HELIX   59  59 ILE B  454  GLU B  457  1                                   4    
HELIX   60  60 ASP B  472  ALA B  491  1                                  20    
HELIX   61  61 LEU B  495  THR B  498  5                                   4    
HELIX   62  62 ALA B  503  LEU B  514  1                                  12    
HELIX   63  63 THR B  520  ALA B  541  1                                  22    
HELIX   64  64 PRO B  545  ASP B  548  1                                   4    
HELIX   65  65 LYS B  553  GLU B  557  1                                   5    
HELIX   66  66 LEU B  572  ARG B  583  1                                  12    
HELIX   67  67 LYS B  593  GLU B  598  1                                   6    
SHEET    1   A 6 ASP A  17  GLU A  22  0                                        
SHEET    2   A 6 ARG A   7  ASN A  12 -1  N  ASN A  12   O  ASP A  17           
SHEET    3   A 6 ALA A 109  GLU A 113  1  N  ALA A 109   O  ILE A   9           
SHEET    4   A 6 LEU A  59  ALA A  63 -1  N  ILE A  61   O  ILE A 110           
SHEET    5   A 6 TYR A  77  LYS A  82 -1  N  VAL A  80   O  ILE A  60           
SHEET    6   A 6 ILE A  89  SER A  94 -1  N  SER A  94   O  TYR A  77           
SHEET    1   B 4 HIS A 128  ASP A 133  0                                        
SHEET    2   B 4 VAL A 120  LYS A 125 -1  N  LYS A 125   O  HIS A 128           
SHEET    3   B 4 LEU A 198  GLU A 204  1  N  LYS A 199   O  VAL A 120           
SHEET    4   B 4 LYS A 159  SER A 162 -1  N  ALA A 161   O  ILE A 201           
SHEET    1   C 2 ILE A 176  ASN A 178  0                                        
SHEET    2   C 2 ARG A 182  ALA A 184 -1  N  ALA A 184   O  ILE A 176           
SHEET    1   D 3 GLY A 305  GLU A 308  0                                        
SHEET    2   D 3 GLY A 296  LEU A 301 -1  N  LEU A 301   O  GLY A 305           
SHEET    3   D 3 LEU A 282  LYS A 286 -1  N  LYS A 286   O  GLY A 296           
SHEET    1   E 6 ASP B  17  GLU B  22  0                                        
SHEET    2   E 6 ARG B   7  ASN B  12 -1  N  ASN B  12   O  ASP B  17           
SHEET    3   E 6 ALA B 109  GLU B 113  1  N  ALA B 109   O  ILE B   9           
SHEET    4   E 6 LEU B  59  ALA B  63 -1  N  ILE B  61   O  ILE B 110           
SHEET    5   E 6 TYR B  77  LYS B  82 -1  N  VAL B  80   O  ILE B  60           
SHEET    6   E 6 ILE B  89  SER B  94 -1  N  SER B  94   O  TYR B  77           
SHEET    1   F 4 HIS B 128  ASP B 133  0                                        
SHEET    2   F 4 VAL B 120  LYS B 125 -1  N  LYS B 125   O  HIS B 128           
SHEET    3   F 4 LEU B 198  GLU B 204  1  N  LYS B 199   O  VAL B 120           
SHEET    4   F 4 LYS B 159  SER B 162 -1  N  ALA B 161   O  ILE B 201           
SHEET    1   G 2 ILE B 176  ASN B 178  0                                        
SHEET    2   G 2 ARG B 182  ALA B 184 -1  N  ALA B 184   O  ILE B 176           
SHEET    1   H 3 GLY B 305  GLU B 308  0                                        
SHEET    2   H 3 GLY B 296  LEU B 301 -1  N  LEU B 301   O  GLY B 305           
SHEET    3   H 3 LEU B 282  LYS B 286 -1  N  LYS B 286   O  GLY B 296           
LINK         O   ASN A  93                MG1  PTE A 609     1555   1555  2.05  
LINK         O   ALA A 183                MG1  PTE A 609     1555   1555  2.08  
LINK         SG  CYS A 288                FE1  SF4 A 608     1555   1555  2.31  
LINK         SG  CYS A 291                FE3  SF4 A 608     1555   1555  2.31  
LINK         SG  CYS A 295                FE4  SF4 A 608     1555   1555  2.32  
LINK         OE1 GLU A 332                FE    FE A 606     1555   1555  2.01  
LINK         NE2 HIS A 383                FE    FE A 606     1555   1555  2.07  
LINK         SG  CYS A 494                FE2  SF4 A 608     1555   1555  2.33  
LINK         O   ASN B  93                MG1  PTE B 608     1555   1555  2.08  
LINK         O   ALA B 183                MG1  PTE B 608     1555   1555  2.04  
LINK         SG  CYS B 288                FE1  SF4 B 607     1555   1555  2.31  
LINK         SG  CYS B 291                FE3  SF4 B 607     1555   1555  2.31  
LINK         SG  CYS B 295                FE4  SF4 B 607     1555   1555  2.31  
LINK         OE1 GLU B 332                FE    FE A 606     1555   1555  2.05  
LINK         NE2 HIS B 383                FE    FE A 606     1555   1555  2.05  
LINK         SG  CYS B 494                FE2  SF4 B 607     1555   1555  2.28  
LINK         O   HIS A 181                NA    NA A 607     1555   1555  2.14  
LINK         O   HIS B 181                NA    NA B 606     1555   1555  2.12  
LINK        NA    NA A 607                 O8  PTE A 609     1555   1555  2.46  
LINK        NA    NA B 606                 O8  PTE B 608     1555   1555  2.78  
LINK        NA    NA A 607                 O   HOH A5011     1555   1555  2.13  
LINK        NA    NA A 607                 O   HOH A5013     1555   1555  2.11  
LINK        NA    NA A 607                 O   HOH A5012     1555   1555  2.09  
LINK        NA    NA B 606                 O   HOH B5026     1555   1555  2.12  
LINK        NA    NA B 606                 O   HOH B5024     1555   1555  2.11  
LINK        NA    NA B 606                 O   HOH B5025     1555   1555  2.13  
LINK        FE    FE A 606                 OE2 GLU A 332     1555   1555  2.71  
LINK        FE    FE A 606                 OE2 GLU B 332     1555   1555  2.72  
CISPEP   1 GLY A  309    PRO A  310          0        -0.02                     
CISPEP   2 TYR A  461    PRO A  462          0         0.12                     
CISPEP   3 GLY B  309    PRO B  310          0         0.51                     
CISPEP   4 TYR B  461    PRO B  462          0         0.29                     
SITE     1 PT1  1 PTE A 609                                                     
SITE     1 PT2  1 PTE B 608                                                     
SITE     1 AC1  4 GLU A 332  HIS A 383  GLU B 332  HIS B 383                    
SITE     1 AC2  5 HIS A 181  PTE A 609  HOH A5011  HOH A5012                    
SITE     2 AC2  5 HOH A5013                                                     
SITE     1 AC3  5 HIS B 181  PTE B 608  HOH B5024  HOH B5025                    
SITE     2 AC3  5 HOH B5026                                                     
SITE     1 AC4  9 THR A  73  ARG A  76  ARG A 182  CYS A 288                    
SITE     2 AC4  9 CYS A 291  CYS A 295  CYS A 494  PHE A 496                    
SITE     3 AC4  9 PTE A 609                                                     
SITE     1 AC5 28 ARG A  76  ALA A  92  ASN A  93  SER A  94                    
SITE     2 AC5 28 GLY A  95  ARG A 182  ALA A 183  GLY A 185                    
SITE     3 AC5 28 ARG A 186  GLU A 311  GLU A 313  ASP A 338                    
SITE     4 AC5 28 LEU A 342  ASP A 343  THR A 344  ARG A 444                    
SITE     5 AC5 28 HIS A 448  ILE A 449  LYS A 450  ASP A 489                    
SITE     6 AC5 28 LEU A 493  CYS A 494  LEU A 495  PHE A 496                    
SITE     7 AC5 28  NA A 607  SF4 A 608  HOH A5012  HOH A5115                    
SITE     1 AC6  6 ARG B  76  CYS B 288  CYS B 291  CYS B 295                    
SITE     2 AC6  6 CYS B 494  PHE B 496                                          
SITE     1 AC7 27 ARG B  76  ALA B  92  ASN B  93  SER B  94                    
SITE     2 AC7 27 GLY B  95  ARG B 182  ALA B 183  ALA B 184                    
SITE     3 AC7 27 GLY B 185  ARG B 186  GLU B 311  GLU B 313                    
SITE     4 AC7 27 ASP B 338  LEU B 342  ASP B 343  THR B 344                    
SITE     5 AC7 27 ARG B 444  ILE B 449  LYS B 450  ASP B 489                    
SITE     6 AC7 27 LEU B 493  CYS B 494  LEU B 495  PHE B 496                    
SITE     7 AC7 27  NA B 606  HOH B5026  HOH B5032                               
CRYST1   80.939  108.332  159.792  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      0.012355  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009231  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006258        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system