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Database: PDB
Entry: 1KEK
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HEADER    OXIDOREDUCTASE                          16-NOV-01   1KEK              
TITLE     CRYSTAL STRUCTURE OF THE FREE RADICAL INTERMEDIATE OF                 
TITLE    2 PYRUVATE:FERREDOXIN OXIDOREDUCTASE                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PYRUVATE-FERREDOXIN OXIDOREDUCTASE;                        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 1.2.7.1                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: DESULFOVIBRIO AFRICANUS;                        
SOURCE   3 ORGANISM_TAXID: 873                                                  
KEYWDS    HOMODIMER, 7 DOMAINS, OXIDOREDUCTASE                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.CHABRIERE,X.VERNEDE,B.GUIGLIARELLI,M.-H.CHARON,                     
AUTHOR   2 E.C.HATCHIKIAN,J.C.FONTECILLA-CAMPS                                  
REVDAT   5   31-MAR-09 1KEK    1       ATOM   CONECT                            
REVDAT   4   24-FEB-09 1KEK    1       VERSN                                    
REVDAT   3   01-APR-03 1KEK    1       JRNL                                     
REVDAT   2   09-JAN-02 1KEK    1       JRNL                                     
REVDAT   1   21-DEC-01 1KEK    0                                                
JRNL        AUTH   E.CHABRIERE,X.VERNEDE,B.GUIGLIARELLI,M.H.CHARON,             
JRNL        AUTH 2 E.C.HATCHIKIAN,J.C.FONTECILLA-CAMPS                          
JRNL        TITL   CRYSTAL STRUCTURE OF THE FREE RADICAL INTERMEDIATE           
JRNL        TITL 2 OF PYRUVATE:FERREDOXIN OXIDOREDUCTASE.                       
JRNL        REF    SCIENCE                       V. 294  2559 2001              
JRNL        REFN                   ISSN 0036-8075                               
JRNL        PMID   11752578                                                     
JRNL        DOI    10.1126/SCIENCE.1066198                                      
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR, REFMAC                                       
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 27.38                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 210949                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.178                           
REMARK   3   R VALUE            (WORKING SET) : 0.178                           
REMARK   3   FREE R VALUE                     : 0.227                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 10008                           
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 18766                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 116                                     
REMARK   3   SOLVENT ATOMS            : 1893                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 16.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -4.53000                                             
REMARK   3    B22 (A**2) : 1.34000                                              
REMARK   3    B33 (A**2) : 3.18000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): NULL          
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : NULL  ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : NULL  ; NULL                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; 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  OTHER REFINEMENT REMARKS: THIS REFINED SET DIFFERS SLIGHTLY         
REMARK   3  FROM THE ONE REPORTED IN REF. FOR EXAMPLE, THE C2ALPHA-C2           
REMARK   3  DISTANCES OF THE RADICAL SPECIES DO NOT MATCH EXACTLY THE           
REMARK   3  PUBLISHED ONES.                                                     
REMARK   4                                                                      
REMARK   4 1KEK COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-NOV-01.                  
REMARK 100 THE RCSB ID CODE IS RCSB014871.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-DEC-98                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 9                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-3                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.005                              
REMARK 200  MONOCHROMATOR                  : DIAMOND                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 216598                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 27.380                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.4                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.87                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.97                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.29300                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.400                              
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   (%): 50.12                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.47                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 6000 10-15%, PH 9, VAPOR             
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 293K                           
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       43.05500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      105.13000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       72.88000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      105.13000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       43.05500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       72.88000            
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: 31700 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 74720 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -291.0 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     GLU A  184   CG    CD    OE1   OE2                               
REMARK 480     ARG A  532   C     CB    CG    CD    NE    CZ    NH1             
REMARK 480     ARG A  532   NH2                                                 
REMARK 480     LYS A  540   CE    NZ                                            
REMARK 480     MET A  601   C     CB    CG    SD    CE                          
REMARK 480     GLU A  637   C     CB    CG    CD    OE1   OE2                   
REMARK 480     GLU A  908   CG    CD    OE1   OE2                               
REMARK 480     LYS A  922   CE    NZ                                            
REMARK 480     ARG A 1147   CD    NE    CZ    NH1   NH2                         
REMARK 480     GLU B  245   C     CB    CG    CD    OE1   OE2                   
REMARK 480     GLN B  248   CG    CD    OE1   NE2                               
REMARK 480     GLU B  711   C     CB    CG    CD    OE1   OE2                   
REMARK 480     GLU B  712   C     CB    CG    CD    OE1   OE2                   
REMARK 480     LYS B  732   CB    CG    CE    NZ                                
REMARK 480     GLU B 1126   C     CB    CG    CD    OE1   OE2                   
REMARK 480     LYS B 1232   N     CA    C     O     CB    CG    CD              
REMARK 480     LYS B 1232   CE    NZ                                            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH B  3481     O    HOH B  4150              2.15            
REMARK 500   NH2  ARG A  1147     O    HOH A  2861              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ARG A 532   CA    ARG A 532   CB     -0.170                       
REMARK 500    ARG A 532   CA    ARG A 532   C       0.308                       
REMARK 500    MET A 601   CA    MET A 601   CB     -0.311                       
REMARK 500    MET A 601   CA    MET A 601   C       0.366                       
REMARK 500    MET A 601   C     MET A 601   O      -0.292                       
REMARK 500    GLU A 908   CB    GLU A 908   CG     -0.173                       
REMARK 500    ARG A1147   CG    ARG A1147   CD      0.238                       
REMARK 500    ARG B  48   CD    ARG B  48   NE     -0.128                       
REMARK 500    GLU B 711   CA    GLU B 711   CB     -0.276                       
REMARK 500    GLU B 711   CA    GLU B 711   C       0.196                       
REMARK 500    GLU B 711   C     GLU B 711   O      -0.286                       
REMARK 500    GLU B 712   CA    GLU B 712   CB     -0.202                       
REMARK 500    GLU B 712   CA    GLU B 712   C       0.267                       
REMARK 500    GLU B 712   C     GLU B 712   O      -0.261                       
REMARK 500    LYS B 732   CA    LYS B 732   CB     -0.241                       
REMARK 500    LYS B 732   CG    LYS B 732   CD     -0.693                       
REMARK 500    LYS B 732   CD    LYS B 732   CE      1.424                       
REMARK 500    GLU B1126   C     GLU B1126   O      -0.173                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    THR A   8   N   -  CA  -  CB  ANGL. DEV. =  14.3 DEGREES          
REMARK 500    ILE A  27   CA  -  CB  -  CG2 ANGL. DEV. =  17.7 DEGREES          
REMARK 500    GLU A  39   CA  -  CB  -  CG  ANGL. DEV. = -14.7 DEGREES          
REMARK 500    GLU A  39   OE1 -  CD  -  OE2 ANGL. DEV. =  10.0 DEGREES          
REMARK 500    GLU A  39   CG  -  CD  -  OE2 ANGL. DEV. = -13.7 DEGREES          
REMARK 500    ARG A  48   CD  -  NE  -  CZ  ANGL. DEV. =  20.4 DEGREES          
REMARK 500    ARG A  48   NH1 -  CZ  -  NH2 ANGL. DEV. =   9.8 DEGREES          
REMARK 500    ARG A  48   NE  -  CZ  -  NH2 ANGL. DEV. = -10.7 DEGREES          
REMARK 500    THR A  55   OG1 -  CB  -  CG2 ANGL. DEV. = -13.9 DEGREES          
REMARK 500    ARG A  59   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    THR A  82   CB  -  CA  -  C   ANGL. DEV. = -18.7 DEGREES          
REMARK 500    TYR A  98   CB  -  CG  -  CD1 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    LEU A 141   CA  -  CB  -  CG  ANGL. DEV. =  14.0 DEGREES          
REMARK 500    ILE A 180   CA  -  CB  -  CG2 ANGL. DEV. =  14.3 DEGREES          
REMARK 500    ASP A 187   CB  -  CG  -  OD2 ANGL. DEV. =  -6.4 DEGREES          
REMARK 500    ARG A 204   CD  -  NE  -  CZ  ANGL. DEV. =  42.0 DEGREES          
REMARK 500    ARG A 204   NE  -  CZ  -  NH1 ANGL. DEV. =  -7.7 DEGREES          
REMARK 500    ARG A 216   CD  -  NE  -  CZ  ANGL. DEV. =  15.2 DEGREES          
REMARK 500    PHE A 226   CB  -  CG  -  CD1 ANGL. DEV. =  -4.4 DEGREES          
REMARK 500    ARG A 256   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    VAL A 264   CA  -  CB  -  CG1 ANGL. DEV. =  10.2 DEGREES          
REMARK 500    VAL A 302   CA  -  CB  -  CG2 ANGL. DEV. =   9.7 DEGREES          
REMARK 500    ARG A 306   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES          
REMARK 500    ARG A 306   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ARG A 306   O   -  C   -  N   ANGL. DEV. =  11.5 DEGREES          
REMARK 500    LYS A 331   CA  -  CB  -  CG  ANGL. DEV. =  15.4 DEGREES          
REMARK 500    GLU A 350   OE1 -  CD  -  OE2 ANGL. DEV. =   7.3 DEGREES          
REMARK 500    ARG A 351   CD  -  NE  -  CZ  ANGL. DEV. =  14.4 DEGREES          
REMARK 500    ARG A 351   NE  -  CZ  -  NH1 ANGL. DEV. =  10.5 DEGREES          
REMARK 500    ARG A 351   NE  -  CZ  -  NH2 ANGL. DEV. =  -8.7 DEGREES          
REMARK 500    VAL A 392   CB  -  CA  -  C   ANGL. DEV. = -14.3 DEGREES          
REMARK 500    TYR A 455   CB  -  CG  -  CD2 ANGL. DEV. =  -4.9 DEGREES          
REMARK 500    TYR A 455   CB  -  CG  -  CD1 ANGL. DEV. =   4.4 DEGREES          
REMARK 500    TYR A 479   CB  -  CG  -  CD1 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500    ASP A 521   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ARG A 532   N   -  CA  -  CB  ANGL. DEV. =  11.9 DEGREES          
REMARK 500    ARG A 532   CA  -  C   -  O   ANGL. DEV. = -17.0 DEGREES          
REMARK 500    ARG A 532   O   -  C   -  N   ANGL. DEV. =  18.2 DEGREES          
REMARK 500    THR A 533   C   -  N   -  CA  ANGL. DEV. = -15.3 DEGREES          
REMARK 500    ARG A 558   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.1 DEGREES          
REMARK 500    MET A 601   N   -  CA  -  CB  ANGL. DEV. =  24.4 DEGREES          
REMARK 500    MET A 601   CA  -  C   -  N   ANGL. DEV. = -21.3 DEGREES          
REMARK 500    MET A 601   O   -  C   -  N   ANGL. DEV. =  30.4 DEGREES          
REMARK 500    ASN A 602   C   -  N   -  CA  ANGL. DEV. = -15.6 DEGREES          
REMARK 500    GLU A 637   CA  -  CB  -  CG  ANGL. DEV. =  14.6 DEGREES          
REMARK 500    VAL A 656   CA  -  CB  -  CG2 ANGL. DEV. =   9.5 DEGREES          
REMARK 500    ARG A 664   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.6 DEGREES          
REMARK 500    ARG A 675   CD  -  NE  -  CZ  ANGL. DEV. =  12.1 DEGREES          
REMARK 500    ARG A 675   NE  -  CZ  -  NH1 ANGL. DEV. =   4.7 DEGREES          
REMARK 500    ARG A 675   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.6 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     171 ANGLE DEVIATIONS.                             
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    SER A  87     -124.70     43.25                                   
REMARK 500    PRO A 106       44.53    -71.42                                   
REMARK 500    ALA A 118      -86.20   -135.04                                   
REMARK 500    PHE A 174      -56.50     67.37                                   
REMARK 500    ASN A 209      131.61   -171.77                                   
REMARK 500    HIS A 212       68.82   -153.53                                   
REMARK 500    ARG A 303      -61.51    -99.50                                   
REMARK 500    ARG A 329       50.94    -94.13                                   
REMARK 500    GLU A 353     -121.92   -127.10                                   
REMARK 500    LYS A 357      110.98     43.96                                   
REMARK 500    ILE A 497      -32.90   -132.54                                   
REMARK 500    TYR A 591      179.25     78.49                                   
REMARK 500    LYS A 594       66.02   -112.65                                   
REMARK 500    ASP A 624       53.15   -155.81                                   
REMARK 500    GLU A 628     -169.65   -108.98                                   
REMARK 500    ALA A 631       32.11    -70.99                                   
REMARK 500    THR A 635     -151.49   -130.67                                   
REMARK 500    VAL A 642      -55.09   -125.90                                   
REMARK 500    LYS A 674       56.46     33.32                                   
REMARK 500    LYS A 732      -60.01   -169.63                                   
REMARK 500    CYS A 755      109.95    -41.06                                   
REMARK 500    ALA A 846       52.59   -153.87                                   
REMARK 500    SER A 867      -84.86    -88.68                                   
REMARK 500    GLU A 899       50.14   -109.37                                   
REMARK 500    ASP A 968      -97.69   -115.45                                   
REMARK 500    ALA A1014       44.96   -147.09                                   
REMARK 500    SER A1045      115.32   -160.63                                   
REMARK 500    ALA A1178     -150.92    177.92                                   
REMARK 500    LYS A1181      -93.49     48.03                                   
REMARK 500    ALA A1182      179.51     70.00                                   
REMARK 500    LYS A1231     -101.96     40.34                                   
REMARK 500    THR B  85     -169.35   -160.62                                   
REMARK 500    SER B  87     -129.28     45.10                                   
REMARK 500    PRO B 106       45.78    -77.53                                   
REMARK 500    ALA B 118      -95.75   -128.21                                   
REMARK 500    PHE B 174      -58.21     67.67                                   
REMARK 500    HIS B 212       69.29   -158.29                                   
REMARK 500    ARG B 303      -68.78   -100.67                                   
REMARK 500    ARG B 329       45.75    -99.79                                   
REMARK 500    GLU B 353     -142.01   -118.87                                   
REMARK 500    PRO B 356       28.95    -77.86                                   
REMARK 500    LYS B 357      102.73     65.31                                   
REMARK 500    TYR B 591     -164.07     62.09                                   
REMARK 500    LYS B 594       72.04   -106.06                                   
REMARK 500    ASP B 624       42.48   -140.43                                   
REMARK 500    ALA B 631       39.71    -90.87                                   
REMARK 500    VAL B 642      -56.16   -122.17                                   
REMARK 500    LYS B 674       60.11     37.73                                   
REMARK 500    LYS B 732      -92.84    -12.71                                   
REMARK 500    ALA B 846       49.10   -160.54                                   
REMARK 500    SER B 867      -81.65    -85.94                                   
REMARK 500    ASP B 968      -93.59   -121.89                                   
REMARK 500    SER B1174     -174.72    -67.18                                   
REMARK 500    ALA B1178     -162.07    161.93                                   
REMARK 500    LYS B1181      -84.08     57.14                                   
REMARK 500    ALA B1182     -160.49     74.07                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER                       
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    ARG A 532        -15.76                                           
REMARK 500    GLU A 637        -23.04                                           
REMARK 500    ASP B 129        -10.41                                           
REMARK 500    GLU B 712        -10.44                                           
REMARK 500    VAL B1029        -10.31                                           
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     THR A  12        19.4      L          L   OUTSIDE RANGE          
REMARK 500     VAL A 239        22.0      L          L   OUTSIDE RANGE          
REMARK 500     VAL A 349        23.2      L          L   OUTSIDE RANGE          
REMARK 500     LYS A 357        24.5      L          L   OUTSIDE RANGE          
REMARK 500     MET A 601        19.8      L          L   OUTSIDE RANGE          
REMARK 500     VAL A 643        23.9      L          L   OUTSIDE RANGE          
REMARK 500     VAL A 656        24.1      L          L   OUTSIDE RANGE          
REMARK 500     VAL A 823        24.1      L          L   OUTSIDE RANGE          
REMARK 500     VAL A 986        24.4      L          L   OUTSIDE RANGE          
REMARK 500     VAL A1029        21.5      L          L   OUTSIDE RANGE          
REMARK 500     THR A1196        45.3      L          L   OUTSIDE RANGE          
REMARK 500     VAL B 239        22.0      L          L   OUTSIDE RANGE          
REMARK 500     THR B 325        22.0      L          L   OUTSIDE RANGE          
REMARK 500     VAL B 398        23.0      L          L   OUTSIDE RANGE          
REMARK 500     THR B 509        23.4      L          L   OUTSIDE RANGE          
REMARK 500     VAL B 643        21.6      L          L   OUTSIDE RANGE          
REMARK 500     VAL B 656        24.6      L          L   OUTSIDE RANGE          
REMARK 500     GLU B 711        21.3      L          L   OUTSIDE RANGE          
REMARK 500     GLU B 712         5.8      L          D   EXPECTING SP3          
REMARK 500     LYS B 732         1.2      L          D   EXPECTING SP3          
REMARK 500     VAL B 821        22.5      L          L   OUTSIDE RANGE          
REMARK 500     VAL B 823        23.9      L          L   OUTSIDE RANGE          
REMARK 500     THR B 953        23.4      L          L   OUTSIDE RANGE          
REMARK 500     VAL B 986        24.6      L          L   OUTSIDE RANGE          
REMARK 500     VAL B1029        20.8      L          L   OUTSIDE RANGE          
REMARK 500     GLU B1126        19.0      L          L   OUTSIDE RANGE          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B4265        DISTANCE =  5.26 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A2237  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 963   OD1                                                    
REMARK 620 2 THR A 991   OG1  89.1                                              
REMARK 620 3 VAL A 993   O    90.2  76.4                                        
REMARK 620 4 HTL A2236   O23 168.4  92.8 101.4                                  
REMARK 620 5 HOH A2375   O    82.3  89.9 164.5  86.3                            
REMARK 620 6 HTL A2236   O12  95.0 169.2  93.5  85.2 100.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2238  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 983   OD2                                                    
REMARK 620 2 ASN A 985   OD1 103.7                                              
REMARK 620 3 ALA A1056   O   150.6  72.3                                        
REMARK 620 4 PHE A1059   O    82.8 161.2  93.2                                  
REMARK 620 5 GLY A1061   O    81.6 127.9 124.5  70.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B3237  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 963   OD1                                                    
REMARK 620 2 THR B 991   OG1  92.6                                              
REMARK 620 3 VAL B 993   O    92.9  78.3                                        
REMARK 620 4 HTL B3236   O12  96.6 169.0  95.2                                  
REMARK 620 5 HTL B3236   O23 167.4  91.5  99.6  80.7                            
REMARK 620 6 HOH B3382   O    88.0  89.6 167.9  96.7  80.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B3238  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 983   OD2                                                    
REMARK 620 2 ASN B 985   OD1 106.1                                              
REMARK 620 3 ALA B1056   O   147.0  68.5                                        
REMARK 620 4 PHE B1059   O    80.8 153.4  91.5                                  
REMARK 620 5 GLY B1061   O    84.8 132.8 123.6  72.7                            
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 MG A 2237                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2238                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 3237                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 3238                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 A 2233                
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 A 2234                
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 A 2235                
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HTL A 2236                
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO2 A 2240                
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 B 3233                
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 B 3234                
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 B 3235                
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HTL B 3236                
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CO2 B 3240                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1B0P   RELATED DB: PDB                                   
REMARK 900 1B0P IS THE NATIVE STRUCTURE.                                        
REMARK 900 RELATED ID: 2PDA   RELATED DB: PDB                                   
REMARK 900 2PDA IS COMPLEXED WITH PYRUVATE.                                     
DBREF  1KEK A    2  1232  UNP    P94692   P94692_DESAF     2   1232             
DBREF  1KEK B    2  1232  UNP    P94692   P94692_DESAF     2   1232             
SEQRES   1 A 1231  GLY LYS LYS MET MET THR THR ASP GLY ASN THR ALA THR          
SEQRES   2 A 1231  ALA HIS VAL ALA TYR ALA MET SER GLU VAL ALA ALA ILE          
SEQRES   3 A 1231  TYR PRO ILE THR PRO SER SER THR MET GLY GLU GLU ALA          
SEQRES   4 A 1231  ASP ASP TRP ALA ALA GLN GLY ARG LYS ASN ILE PHE GLY          
SEQRES   5 A 1231  GLN THR LEU THR ILE ARG GLU MET GLN SER GLU ALA GLY          
SEQRES   6 A 1231  ALA ALA GLY ALA VAL HIS GLY ALA LEU ALA ALA GLY ALA          
SEQRES   7 A 1231  LEU THR THR THR PHE THR ALA SER GLN GLY LEU LEU LEU          
SEQRES   8 A 1231  MET ILE PRO ASN MET TYR LYS ILE SER GLY GLU LEU LEU          
SEQRES   9 A 1231  PRO GLY VAL PHE HIS VAL THR ALA ARG ALA ILE ALA ALA          
SEQRES  10 A 1231  HIS ALA LEU SER ILE PHE GLY ASP HIS GLN ASP ILE TYR          
SEQRES  11 A 1231  ALA ALA ARG GLN THR GLY PHE ALA MET LEU ALA SER SER          
SEQRES  12 A 1231  SER VAL GLN GLU ALA HIS ASP MET ALA LEU VAL ALA HIS          
SEQRES  13 A 1231  LEU ALA ALA ILE GLU SER ASN VAL PRO PHE MET HIS PHE          
SEQRES  14 A 1231  PHE ASP GLY PHE ARG THR SER HIS GLU ILE GLN LYS ILE          
SEQRES  15 A 1231  GLU VAL LEU ASP TYR ALA ASP MET ALA SER LEU VAL ASN          
SEQRES  16 A 1231  GLN LYS ALA LEU ALA GLU PHE ARG ALA LYS SER MET ASN          
SEQRES  17 A 1231  PRO GLU HIS PRO HIS VAL ARG GLY THR ALA GLN ASN PRO          
SEQRES  18 A 1231  ASP ILE TYR PHE GLN GLY ARG GLU ALA ALA ASN PRO TYR          
SEQRES  19 A 1231  TYR LEU LYS VAL PRO GLY ILE VAL ALA GLU TYR MET GLN          
SEQRES  20 A 1231  LYS VAL ALA SER LEU THR GLY ARG SER TYR LYS LEU PHE          
SEQRES  21 A 1231  ASP TYR VAL GLY ALA PRO ASP ALA GLU ARG VAL ILE VAL          
SEQRES  22 A 1231  SER MET GLY SER SER CYS GLU THR ILE GLU GLU VAL ILE          
SEQRES  23 A 1231  ASN HIS LEU ALA ALA LYS GLY GLU LYS ILE GLY LEU ILE          
SEQRES  24 A 1231  LYS VAL ARG LEU TYR ARG PRO PHE VAL SER GLU ALA PHE          
SEQRES  25 A 1231  PHE ALA ALA LEU PRO ALA SER ALA LYS VAL ILE THR VAL          
SEQRES  26 A 1231  LEU ASP ARG THR LYS GLU PRO GLY ALA PRO GLY ASP PRO          
SEQRES  27 A 1231  LEU TYR LEU ASP VAL CYS SER ALA PHE VAL GLU ARG GLY          
SEQRES  28 A 1231  GLU ALA MET PRO LYS ILE LEU ALA GLY ARG TYR GLY LEU          
SEQRES  29 A 1231  GLY SER LYS GLU PHE SER PRO ALA MET VAL LYS SER VAL          
SEQRES  30 A 1231  TYR ASP ASN MET SER GLY ALA LYS LYS ASN HIS PHE THR          
SEQRES  31 A 1231  VAL GLY ILE GLU ASP ASP VAL THR GLY THR SER LEU PRO          
SEQRES  32 A 1231  VAL ASP ASN ALA PHE ALA ASP THR THR PRO LYS GLY THR          
SEQRES  33 A 1231  ILE GLN CYS GLN PHE TRP GLY LEU GLY ALA ASP GLY THR          
SEQRES  34 A 1231  VAL GLY ALA ASN LYS GLN ALA ILE LYS ILE ILE GLY ASP          
SEQRES  35 A 1231  ASN THR ASP LEU PHE ALA GLN GLY TYR PHE SER TYR ASP          
SEQRES  36 A 1231  SER LYS LYS SER GLY GLY ILE THR ILE SER HIS LEU ARG          
SEQRES  37 A 1231  PHE GLY GLU LYS PRO ILE GLN SER THR TYR LEU VAL ASN          
SEQRES  38 A 1231  ARG ALA ASP TYR VAL ALA CYS HIS ASN PRO ALA TYR VAL          
SEQRES  39 A 1231  GLY ILE TYR ASP ILE LEU GLU GLY ILE LYS ASP GLY GLY          
SEQRES  40 A 1231  THR PHE VAL LEU ASN SER PRO TRP SER SER LEU GLU ASP          
SEQRES  41 A 1231  MET ASP LYS HIS LEU PRO SER GLY ILE LYS ARG THR ILE          
SEQRES  42 A 1231  ALA ASN LYS LYS LEU LYS PHE TYR ASN ILE ASP ALA VAL          
SEQRES  43 A 1231  LYS ILE ALA THR ASP VAL GLY LEU GLY GLY ARG ILE ASN          
SEQRES  44 A 1231  MET ILE MET GLN THR ALA PHE PHE LYS LEU ALA GLY VAL          
SEQRES  45 A 1231  LEU PRO PHE GLU LYS ALA VAL ASP LEU LEU LYS LYS SER          
SEQRES  46 A 1231  ILE HIS LYS ALA TYR GLY LYS LYS GLY GLU LYS ILE VAL          
SEQRES  47 A 1231  LYS MET ASN THR ASP ALA VAL ASP GLN ALA VAL THR SER          
SEQRES  48 A 1231  LEU GLN GLU PHE LYS TYR PRO ASP SER TRP LYS ASP ALA          
SEQRES  49 A 1231  PRO ALA GLU THR LYS ALA GLU PRO MET THR ASN GLU PHE          
SEQRES  50 A 1231  PHE LYS ASN VAL VAL LYS PRO ILE LEU THR GLN GLN GLY          
SEQRES  51 A 1231  ASP LYS LEU PRO VAL SER ALA PHE GLU ALA ASP GLY ARG          
SEQRES  52 A 1231  PHE PRO LEU GLY THR SER GLN PHE GLU LYS ARG GLY VAL          
SEQRES  53 A 1231  ALA ILE ASN VAL PRO GLN TRP VAL PRO GLU ASN CYS ILE          
SEQRES  54 A 1231  GLN CYS ASN GLN CYS ALA PHE VAL CYS PRO HIS SER ALA          
SEQRES  55 A 1231  ILE LEU PRO VAL LEU ALA LYS GLU GLU GLU LEU VAL GLY          
SEQRES  56 A 1231  ALA PRO ALA ASN PHE THR ALA LEU GLU ALA LYS GLY LYS          
SEQRES  57 A 1231  GLU LEU LYS GLY TYR LYS PHE ARG ILE GLN ILE ASN THR          
SEQRES  58 A 1231  LEU ASP CYS MET GLY CYS GLY ASN CYS ALA ASP ILE CYS          
SEQRES  59 A 1231  PRO PRO LYS GLU LYS ALA LEU VAL MET GLN PRO LEU ASP          
SEQRES  60 A 1231  THR GLN ARG ASP ALA GLN VAL PRO ASN LEU GLU TYR ALA          
SEQRES  61 A 1231  ALA ARG ILE PRO VAL LYS SER GLU VAL LEU PRO ARG ASP          
SEQRES  62 A 1231  SER LEU LYS GLY SER GLN PHE GLN GLU PRO LEU MET GLU          
SEQRES  63 A 1231  PHE SER GLY ALA CYS SER GLY CYS GLY GLU THR PRO TYR          
SEQRES  64 A 1231  VAL ARG VAL ILE THR GLN LEU PHE GLY GLU ARG MET PHE          
SEQRES  65 A 1231  ILE ALA ASN ALA THR GLY CYS SER SER ILE TRP GLY ALA          
SEQRES  66 A 1231  SER ALA PRO SER MET PRO TYR LYS THR ASN ARG LEU GLY          
SEQRES  67 A 1231  GLN GLY PRO ALA TRP GLY ASN SER LEU PHE GLU ASP ALA          
SEQRES  68 A 1231  ALA GLU TYR GLY PHE GLY MET ASN MET SER MET PHE ALA          
SEQRES  69 A 1231  ARG ARG THR HIS LEU ALA ASP LEU ALA ALA LYS ALA LEU          
SEQRES  70 A 1231  GLU SER ASP ALA SER GLY ASP VAL LYS GLU ALA LEU GLN          
SEQRES  71 A 1231  GLY TRP LEU ALA GLY LYS ASN ASP PRO ILE LYS SER LYS          
SEQRES  72 A 1231  GLU TYR GLY ASP LYS LEU LYS LYS LEU LEU ALA GLY GLN          
SEQRES  73 A 1231  LYS ASP GLY LEU LEU GLY GLN ILE ALA ALA MET SER ASP          
SEQRES  74 A 1231  LEU TYR THR LYS LYS SER VAL TRP ILE PHE GLY GLY ASP          
SEQRES  75 A 1231  GLY TRP ALA TYR ASP ILE GLY TYR GLY GLY LEU ASP HIS          
SEQRES  76 A 1231  VAL LEU ALA SER GLY GLU ASP VAL ASN VAL PHE VAL MET          
SEQRES  77 A 1231  ASP THR GLU VAL TYR SER ASN THR GLY GLY GLN SER SER          
SEQRES  78 A 1231  LYS ALA THR PRO THR GLY ALA VAL ALA LYS PHE ALA ALA          
SEQRES  79 A 1231  ALA GLY LYS ARG THR GLY LYS LYS ASP LEU ALA ARG MET          
SEQRES  80 A 1231  VAL MET THR TYR GLY TYR VAL TYR VAL ALA THR VAL SER          
SEQRES  81 A 1231  MET GLY TYR SER LYS GLN GLN PHE LEU LYS VAL LEU LYS          
SEQRES  82 A 1231  GLU ALA GLU SER PHE PRO GLY PRO SER LEU VAL ILE ALA          
SEQRES  83 A 1231  TYR ALA THR CYS ILE ASN GLN GLY LEU ARG LYS GLY MET          
SEQRES  84 A 1231  GLY LYS SER GLN ASP VAL MET ASN THR ALA VAL LYS SER          
SEQRES  85 A 1231  GLY TYR TRP PRO LEU PHE ARG TYR ASP PRO ARG LEU ALA          
SEQRES  86 A 1231  ALA GLN GLY LYS ASN PRO PHE GLN LEU ASP SER LYS ALA          
SEQRES  87 A 1231  PRO ASP GLY SER VAL GLU GLU PHE LEU MET ALA GLN ASN          
SEQRES  88 A 1231  ARG PHE ALA VAL LEU ASP ARG SER PHE PRO GLU ASP ALA          
SEQRES  89 A 1231  LYS ARG LEU ARG ALA GLN VAL ALA HIS GLU LEU ASP VAL          
SEQRES  90 A 1231  ARG PHE LYS GLU LEU GLU HIS MET ALA ALA THR ASN ILE          
SEQRES  91 A 1231  PHE GLU SER PHE ALA PRO ALA GLY GLY LYS ALA ASP GLY          
SEQRES  92 A 1231  SER VAL ASP PHE GLY GLU GLY ALA GLU PHE CYS THR ARG          
SEQRES  93 A 1231  ASP ASP THR PRO MET MET ALA ARG PRO ASP SER GLY GLU          
SEQRES  94 A 1231  ALA CYS ASP GLN ASN ARG ALA GLY THR SER GLU GLN GLN          
SEQRES  95 A 1231  GLY ASP LEU SER LYS ARG THR LYS LYS                          
SEQRES   1 B 1231  GLY LYS LYS MET MET THR THR ASP GLY ASN THR ALA THR          
SEQRES   2 B 1231  ALA HIS VAL ALA TYR ALA MET SER GLU VAL ALA ALA ILE          
SEQRES   3 B 1231  TYR PRO ILE THR PRO SER SER THR MET GLY GLU GLU ALA          
SEQRES   4 B 1231  ASP ASP TRP ALA ALA GLN GLY ARG LYS ASN ILE PHE GLY          
SEQRES   5 B 1231  GLN THR LEU THR ILE ARG GLU MET GLN SER GLU ALA GLY          
SEQRES   6 B 1231  ALA ALA GLY ALA VAL HIS GLY ALA LEU ALA ALA GLY ALA          
SEQRES   7 B 1231  LEU THR THR THR PHE THR ALA SER GLN GLY LEU LEU LEU          
SEQRES   8 B 1231  MET ILE PRO ASN MET TYR LYS ILE SER GLY GLU LEU LEU          
SEQRES   9 B 1231  PRO GLY VAL PHE HIS VAL THR ALA ARG ALA ILE ALA ALA          
SEQRES  10 B 1231  HIS ALA LEU SER ILE PHE GLY ASP HIS GLN ASP ILE TYR          
SEQRES  11 B 1231  ALA ALA ARG GLN THR GLY PHE ALA MET LEU ALA SER SER          
SEQRES  12 B 1231  SER VAL GLN GLU ALA HIS ASP MET ALA LEU VAL ALA HIS          
SEQRES  13 B 1231  LEU ALA ALA ILE GLU SER ASN VAL PRO PHE MET HIS PHE          
SEQRES  14 B 1231  PHE ASP GLY PHE ARG THR SER HIS GLU ILE GLN LYS ILE          
SEQRES  15 B 1231  GLU VAL LEU ASP TYR ALA ASP MET ALA SER LEU VAL ASN          
SEQRES  16 B 1231  GLN LYS ALA LEU ALA GLU PHE ARG ALA LYS SER MET ASN          
SEQRES  17 B 1231  PRO GLU HIS PRO HIS VAL ARG GLY THR ALA GLN ASN PRO          
SEQRES  18 B 1231  ASP ILE TYR PHE GLN GLY ARG GLU ALA ALA ASN PRO TYR          
SEQRES  19 B 1231  TYR LEU LYS VAL PRO GLY ILE VAL ALA GLU TYR MET GLN          
SEQRES  20 B 1231  LYS VAL ALA SER LEU THR GLY ARG SER TYR LYS LEU PHE          
SEQRES  21 B 1231  ASP TYR VAL GLY ALA PRO ASP ALA GLU ARG VAL ILE VAL          
SEQRES  22 B 1231  SER MET GLY SER SER CYS GLU THR ILE GLU GLU VAL ILE          
SEQRES  23 B 1231  ASN HIS LEU ALA ALA LYS GLY GLU LYS ILE GLY LEU ILE          
SEQRES  24 B 1231  LYS VAL ARG LEU TYR ARG PRO PHE VAL SER GLU ALA PHE          
SEQRES  25 B 1231  PHE ALA ALA LEU PRO ALA SER ALA LYS VAL ILE THR VAL          
SEQRES  26 B 1231  LEU ASP ARG THR LYS GLU PRO GLY ALA PRO GLY ASP PRO          
SEQRES  27 B 1231  LEU TYR LEU ASP VAL CYS SER ALA PHE VAL GLU ARG GLY          
SEQRES  28 B 1231  GLU ALA MET PRO LYS ILE LEU ALA GLY ARG TYR GLY LEU          
SEQRES  29 B 1231  GLY SER LYS GLU PHE SER PRO ALA MET VAL LYS SER VAL          
SEQRES  30 B 1231  TYR ASP ASN MET SER GLY ALA LYS LYS ASN HIS PHE THR          
SEQRES  31 B 1231  VAL GLY ILE GLU ASP ASP VAL THR GLY THR SER LEU PRO          
SEQRES  32 B 1231  VAL ASP ASN ALA PHE ALA ASP THR THR PRO LYS GLY THR          
SEQRES  33 B 1231  ILE GLN CYS GLN PHE TRP GLY LEU GLY ALA ASP GLY THR          
SEQRES  34 B 1231  VAL GLY ALA ASN LYS GLN ALA ILE LYS ILE ILE GLY ASP          
SEQRES  35 B 1231  ASN THR ASP LEU PHE ALA GLN GLY TYR PHE SER TYR ASP          
SEQRES  36 B 1231  SER LYS LYS SER GLY GLY ILE THR ILE SER HIS LEU ARG          
SEQRES  37 B 1231  PHE GLY GLU LYS PRO ILE GLN SER THR TYR LEU VAL ASN          
SEQRES  38 B 1231  ARG ALA ASP TYR VAL ALA CYS HIS ASN PRO ALA TYR VAL          
SEQRES  39 B 1231  GLY ILE TYR ASP ILE LEU GLU GLY ILE LYS ASP GLY GLY          
SEQRES  40 B 1231  THR PHE VAL LEU ASN SER PRO TRP SER SER LEU GLU ASP          
SEQRES  41 B 1231  MET ASP LYS HIS LEU PRO SER GLY ILE LYS ARG THR ILE          
SEQRES  42 B 1231  ALA ASN LYS LYS LEU LYS PHE TYR ASN ILE ASP ALA VAL          
SEQRES  43 B 1231  LYS ILE ALA THR ASP VAL GLY LEU GLY GLY ARG ILE ASN          
SEQRES  44 B 1231  MET ILE MET GLN THR ALA PHE PHE LYS LEU ALA GLY VAL          
SEQRES  45 B 1231  LEU PRO PHE GLU LYS ALA VAL ASP LEU LEU LYS LYS SER          
SEQRES  46 B 1231  ILE HIS LYS ALA TYR GLY LYS LYS GLY GLU LYS ILE VAL          
SEQRES  47 B 1231  LYS MET ASN THR ASP ALA VAL ASP GLN ALA VAL THR SER          
SEQRES  48 B 1231  LEU GLN GLU PHE LYS TYR PRO ASP SER TRP LYS ASP ALA          
SEQRES  49 B 1231  PRO ALA GLU THR LYS ALA GLU PRO MET THR ASN GLU PHE          
SEQRES  50 B 1231  PHE LYS ASN VAL VAL LYS PRO ILE LEU THR GLN GLN GLY          
SEQRES  51 B 1231  ASP LYS LEU PRO VAL SER ALA PHE GLU ALA ASP GLY ARG          
SEQRES  52 B 1231  PHE PRO LEU GLY THR SER GLN PHE GLU LYS ARG GLY VAL          
SEQRES  53 B 1231  ALA ILE ASN VAL PRO GLN TRP VAL PRO GLU ASN CYS ILE          
SEQRES  54 B 1231  GLN CYS ASN GLN CYS ALA PHE VAL CYS PRO HIS SER ALA          
SEQRES  55 B 1231  ILE LEU PRO VAL LEU ALA LYS GLU GLU GLU LEU VAL GLY          
SEQRES  56 B 1231  ALA PRO ALA ASN PHE THR ALA LEU GLU ALA LYS GLY LYS          
SEQRES  57 B 1231  GLU LEU LYS GLY TYR LYS PHE ARG ILE GLN ILE ASN THR          
SEQRES  58 B 1231  LEU ASP CYS MET GLY CYS GLY ASN CYS ALA ASP ILE CYS          
SEQRES  59 B 1231  PRO PRO LYS GLU LYS ALA LEU VAL MET GLN PRO LEU ASP          
SEQRES  60 B 1231  THR GLN ARG ASP ALA GLN VAL PRO ASN LEU GLU TYR ALA          
SEQRES  61 B 1231  ALA ARG ILE PRO VAL LYS SER GLU VAL LEU PRO ARG ASP          
SEQRES  62 B 1231  SER LEU LYS GLY SER GLN PHE GLN GLU PRO LEU MET GLU          
SEQRES  63 B 1231  PHE SER GLY ALA CYS SER GLY CYS GLY GLU THR PRO TYR          
SEQRES  64 B 1231  VAL ARG VAL ILE THR GLN LEU PHE GLY GLU ARG MET PHE          
SEQRES  65 B 1231  ILE ALA ASN ALA THR GLY CYS SER SER ILE TRP GLY ALA          
SEQRES  66 B 1231  SER ALA PRO SER MET PRO TYR LYS THR ASN ARG LEU GLY          
SEQRES  67 B 1231  GLN GLY PRO ALA TRP GLY ASN SER LEU PHE GLU ASP ALA          
SEQRES  68 B 1231  ALA GLU TYR GLY PHE GLY MET ASN MET SER MET PHE ALA          
SEQRES  69 B 1231  ARG ARG THR HIS LEU ALA ASP LEU ALA ALA LYS ALA LEU          
SEQRES  70 B 1231  GLU SER ASP ALA SER GLY ASP VAL LYS GLU ALA LEU GLN          
SEQRES  71 B 1231  GLY TRP LEU ALA GLY LYS ASN ASP PRO ILE LYS SER LYS          
SEQRES  72 B 1231  GLU TYR GLY ASP LYS LEU LYS LYS LEU LEU ALA GLY GLN          
SEQRES  73 B 1231  LYS ASP GLY LEU LEU GLY GLN ILE ALA ALA MET SER ASP          
SEQRES  74 B 1231  LEU TYR THR LYS LYS SER VAL TRP ILE PHE GLY GLY ASP          
SEQRES  75 B 1231  GLY TRP ALA TYR ASP ILE GLY TYR GLY GLY LEU ASP HIS          
SEQRES  76 B 1231  VAL LEU ALA SER GLY GLU ASP VAL ASN VAL PHE VAL MET          
SEQRES  77 B 1231  ASP THR GLU VAL TYR SER ASN THR GLY GLY GLN SER SER          
SEQRES  78 B 1231  LYS ALA THR PRO THR GLY ALA VAL ALA LYS PHE ALA ALA          
SEQRES  79 B 1231  ALA GLY LYS ARG THR GLY LYS LYS ASP LEU ALA ARG MET          
SEQRES  80 B 1231  VAL MET THR TYR GLY TYR VAL TYR VAL ALA THR VAL SER          
SEQRES  81 B 1231  MET GLY TYR SER LYS GLN GLN PHE LEU LYS VAL LEU LYS          
SEQRES  82 B 1231  GLU ALA GLU SER PHE PRO GLY PRO SER LEU VAL ILE ALA          
SEQRES  83 B 1231  TYR ALA THR CYS ILE ASN GLN GLY LEU ARG LYS GLY MET          
SEQRES  84 B 1231  GLY LYS SER GLN ASP VAL MET ASN THR ALA VAL LYS SER          
SEQRES  85 B 1231  GLY TYR TRP PRO LEU PHE ARG TYR ASP PRO ARG LEU ALA          
SEQRES  86 B 1231  ALA GLN GLY LYS ASN PRO PHE GLN LEU ASP SER LYS ALA          
SEQRES  87 B 1231  PRO ASP GLY SER VAL GLU GLU PHE LEU MET ALA GLN ASN          
SEQRES  88 B 1231  ARG PHE ALA VAL LEU ASP ARG SER PHE PRO GLU ASP ALA          
SEQRES  89 B 1231  LYS ARG LEU ARG ALA GLN VAL ALA HIS GLU LEU ASP VAL          
SEQRES  90 B 1231  ARG PHE LYS GLU LEU GLU HIS MET ALA ALA THR ASN ILE          
SEQRES  91 B 1231  PHE GLU SER PHE ALA PRO ALA GLY GLY LYS ALA ASP GLY          
SEQRES  92 B 1231  SER VAL ASP PHE GLY GLU GLY ALA GLU PHE CYS THR ARG          
SEQRES  93 B 1231  ASP ASP THR PRO MET MET ALA ARG PRO ASP SER GLY GLU          
SEQRES  94 B 1231  ALA CYS ASP GLN ASN ARG ALA GLY THR SER GLU GLN GLN          
SEQRES  95 B 1231  GLY ASP LEU SER LYS ARG THR LYS LYS                          
HET     MG  A2237       1                                                       
HET     CA  A2238       1                                                       
HET     MG  B3237       1                                                       
HET     CA  B3238       1                                                       
HET    SF4  A2233       8                                                       
HET    SF4  A2234       8                                                       
HET    SF4  A2235       8                                                       
HET    HTL  A2236      29                                                       
HET    CO2  A2240       3                                                       
HET    SF4  B3233       8                                                       
HET    SF4  B3234       8                                                       
HET    SF4  B3235       8                                                       
HET    HTL  B3236      29                                                       
HET    CO2  B3240       3                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM      CA CALCIUM ION                                                      
HETNAM     SF4 IRON/SULFUR CLUSTER                                              
HETNAM     HTL 2-ACETYL-THIAMINE DIPHOSPHATE                                    
HETNAM     CO2 CARBON DIOXIDE                                                   
HETSYN     HTL 2-ACETYL-3-[(4-AMINO-2-METHYL-5-PYRIMIDINYL)METHYL]-4-           
HETSYN   2 HTL  METHYL-5-(4,6,6-TRIHYDROXY-3,5-DIOXA-4,6-DIPHOSPHAHEX-          
HETSYN   3 HTL  1-YL)THIAZOLIUM INNER SALT P,P'-DIOXIDE                         
FORMUL   3   MG    2(MG 2+)                                                     
FORMUL   4   CA    2(CA 2+)                                                     
FORMUL   7  SF4    6(FE4 S4)                                                    
FORMUL  10  HTL    2(C14 H21 N4 O8 P2 S 1+)                                     
FORMUL  11  CO2    2(C O2)                                                      
FORMUL  17  HOH   *1893(H2 O)                                                   
HELIX    1   1 GLY A   10  SER A   22  1                                  13    
HELIX    2   2 SER A   33  GLY A   47  1                                  15    
HELIX    3   3 SER A   63  ALA A   77  1                                  15    
HELIX    4   4 ALA A   86  GLU A  103  1                                  18    
HELIX    5   5 HIS A  127  ALA A  133  1                                   7    
HELIX    6   6 SER A  145  ASN A  164  1                                  20    
HELIX    7   7 ASP A  187  VAL A  195  1                                   9    
HELIX    8   8 ASN A  196  SER A  207  1                                  12    
HELIX    9   9 ILE A  224  ALA A  231  1                                   8    
HELIX   10  10 ALA A  232  GLY A  255  1                                  24    
HELIX   11  11 SER A  278  ALA A  292  1                                  15    
HELIX   12  12 VAL A  309  LEU A  317  1                                   9    
HELIX   13  13 ASP A  338  GLY A  352  1                                  15    
HELIX   14  14 GLY A  364  LYS A  368  5                                   5    
HELIX   15  15 SER A  371  GLY A  384  1                                  14    
HELIX   16  16 GLY A  429  THR A  445  1                                  17    
HELIX   17  17 ASN A  491  ILE A  497  5                                   7    
HELIX   18  18 SER A  518  LEU A  526  1                                   9    
HELIX   19  19 PRO A  527  LYS A  537  1                                  11    
HELIX   20  20 ASP A  545  VAL A  553  1                                   9    
HELIX   21  21 ILE A  559  ALA A  571  1                                  13    
HELIX   22  22 PRO A  575  ALA A  590  1                                  16    
HELIX   23  23 GLU A  596  LEU A  613  1                                  18    
HELIX   24  24 PRO A  619  ALA A  625  5                                   7    
HELIX   25  25 ASN A  636  VAL A  642  1                                   7    
HELIX   26  26 VAL A  642  THR A  648  1                                   7    
HELIX   27  27 GLN A  650  LEU A  654  5                                   5    
HELIX   28  28 PRO A  655  PHE A  659  5                                   5    
HELIX   29  29 GLY A  668  GLU A  673  5                                   6    
HELIX   30  30 ASN A  693  CYS A  699  1                                   7    
HELIX   31  31 GLU A  712  VAL A  715  5                                   4    
HELIX   32  32 GLY A  749  CYS A  755  1                                   7    
HELIX   33  33 GLN A  770  ALA A  782  1                                  13    
HELIX   34  34 SER A  795  GLN A  800  1                                   6    
HELIX   35  35 GLU A  817  GLY A  829  1                                  13    
HELIX   36  36 GLY A  839  SER A  847  1                                   9    
HELIX   37  37 ASP A  871  GLU A  899  1                                  29    
HELIX   38  38 SER A  903  GLY A  916  1                                  14    
HELIX   39  39 ASP A  919  LEU A  934  1                                  16    
HELIX   40  40 ASP A  939  MET A  948  1                                  10    
HELIX   41  41 SER A  949  TYR A  952  5                                   4    
HELIX   42  42 ASP A  963  ASP A  968  1                                   6    
HELIX   43  43 GLY A  970  SER A  980  1                                  11    
HELIX   44  44 ASP A 1024  THR A 1031  1                                   8    
HELIX   45  45 SER A 1045  PHE A 1059  1                                  15    
HELIX   46  46 CYS A 1071  GLY A 1075  5                                   5    
HELIX   47  47 GLY A 1079  GLY A 1081  5                                   3    
HELIX   48  48 LYS A 1082  SER A 1093  1                                  12    
HELIX   49  49 ASP A 1102  GLN A 1108  1                                   7    
HELIX   50  50 SER A 1123  ALA A 1130  1                                   8    
HELIX   51  51 GLN A 1131  PHE A 1141  1                                  11    
HELIX   52  52 PHE A 1141  THR A 1169  1                                  29    
HELIX   53  53 THR A 1219  LYS A 1231  1                                  13    
HELIX   54  54 GLY B   10  SER B   22  1                                  13    
HELIX   55  55 SER B   33  GLN B   46  1                                  14    
HELIX   56  56 SER B   63  ALA B   77  1                                  15    
HELIX   57  57 ALA B   86  GLU B  103  1                                  18    
HELIX   58  58 HIS B  127  ALA B  133  1                                   7    
HELIX   59  59 SER B  145  ASN B  164  1                                  20    
HELIX   60  60 ASP B  187  LEU B  194  1                                   8    
HELIX   61  61 ASN B  196  SER B  207  1                                  12    
HELIX   62  62 ILE B  224  ALA B  231  1                                   8    
HELIX   63  63 ALA B  232  GLY B  255  1                                  24    
HELIX   64  64 SER B  278  ALA B  292  1                                  15    
HELIX   65  65 VAL B  309  ALA B  316  1                                   8    
HELIX   66  66 ASP B  338  GLY B  352  1                                  15    
HELIX   67  67 GLY B  364  LYS B  368  5                                   5    
HELIX   68  68 SER B  371  GLY B  384  1                                  14    
HELIX   69  69 GLY B  429  THR B  445  1                                  17    
HELIX   70  70 ASN B  491  ILE B  497  5                                   7    
HELIX   71  71 SER B  518  LEU B  526  1                                   9    
HELIX   72  72 PRO B  527  LYS B  537  1                                  11    
HELIX   73  73 ASP B  545  VAL B  553  1                                   9    
HELIX   74  74 ILE B  559  ALA B  571  1                                  13    
HELIX   75  75 PRO B  575  ALA B  590  1                                  16    
HELIX   76  76 GLU B  596  LEU B  613  1                                  18    
HELIX   77  77 PRO B  619  ALA B  625  5                                   7    
HELIX   78  78 ASN B  636  VAL B  642  1                                   7    
HELIX   79  79 VAL B  642  THR B  648  1                                   7    
HELIX   80  80 GLN B  650  LEU B  654  5                                   5    
HELIX   81  81 PRO B  655  PHE B  659  5                                   5    
HELIX   82  82 GLY B  668  GLU B  673  5                                   6    
HELIX   83  83 PRO B  686  CYS B  689  5                                   4    
HELIX   84  84 ASN B  693  CYS B  699  1                                   7    
HELIX   85  85 LYS B  710  VAL B  715  5                                   6    
HELIX   86  86 GLY B  728  LYS B  732  5                                   5    
HELIX   87  87 GLY B  749  CYS B  755  1                                   7    
HELIX   88  88 GLN B  770  ALA B  782  1                                  13    
HELIX   89  89 SER B  795  GLN B  800  1                                   6    
HELIX   90  90 GLU B  817  GLY B  829  1                                  13    
HELIX   91  91 GLY B  839  SER B  847  1                                   9    
HELIX   92  92 ASP B  871  LEU B  898  1                                  28    
HELIX   93  93 SER B  903  LYS B  917  1                                  15    
HELIX   94  94 ASP B  919  LEU B  934  1                                  16    
HELIX   95  95 ASP B  939  MET B  948  1                                  10    
HELIX   96  96 SER B  949  TYR B  952  5                                   4    
HELIX   97  97 ASP B  963  ASP B  968  1                                   6    
HELIX   98  98 GLY B  970  SER B  980  1                                  11    
HELIX   99  99 ASP B 1024  THR B 1031  1                                   8    
HELIX  100 100 SER B 1045  PHE B 1059  1                                  15    
HELIX  101 101 CYS B 1071  GLY B 1075  5                                   5    
HELIX  102 102 GLY B 1079  GLY B 1081  5                                   3    
HELIX  103 103 LYS B 1082  SER B 1093  1                                  12    
HELIX  104 104 ASP B 1102  GLN B 1108  1                                   7    
HELIX  105 105 SER B 1123  ALA B 1130  1                                   8    
HELIX  106 106 GLN B 1131  PHE B 1141  1                                  11    
HELIX  107 107 PHE B 1141  THR B 1169  1                                  29    
HELIX  108 108 THR B 1219  LYS B 1231  1                                  13    
SHEET    1   A 8 LYS A   3  ASP A   9  0                                        
SHEET    2   A 8 ILE A 180  LEU A 186 -1  O  ILE A 183   N  MET A   6           
SHEET    3   A 8 PHE A 448  TYR A 455 -1  O  GLY A 451   N  ILE A 180           
SHEET    4   A 8 ILE A 463  GLY A 471 -1  O  GLY A 471   N  PHE A 448           
SHEET    5   A 8 ILE A 418  LEU A 425 -1  N  GLY A 424   O  THR A 464           
SHEET    6   A 8 TYR A 486  CYS A 489  1  O  ALA A 488   N  TRP A 423           
SHEET    7   A 8 THR A 509  ASN A 513  1  O  VAL A 511   N  CYS A 489           
SHEET    8   A 8 LYS A 540  ILE A 544  1  O  TYR A 542   N  LEU A 512           
SHEET    1   B 7 THR A  57  GLU A  60  0                                        
SHEET    2   B 7 VAL A  24  ILE A  27  1  N  ALA A  25   O  THR A  57           
SHEET    3   B 7 THR A  81  THR A  85  1  O  THR A  82   N  VAL A  24           
SHEET    4   B 7 VAL A 108  ALA A 113  1  O  HIS A 110   N  THR A  83           
SHEET    5   B 7 PHE A 167  ASP A 172  1  O  PHE A 171   N  ALA A 113           
SHEET    6   B 7 ALA A 139  ALA A 142  1  N  LEU A 141   O  MET A 168           
SHEET    7   B 7 LEU A 304  ARG A 306 -1  O  ARG A 306   N  MET A 140           
SHEET    1   C 2 ALA A 120  LEU A 121  0                                        
SHEET    2   C 2 THR B 218  ALA B 219  1  O  THR B 218   N  LEU A 121           
SHEET    1   D 9 VAL A 215  ARG A 216  0                                        
SHEET    2   D 9 ALA B 863  GLY B 865  1  O  TRP B 864   N  ARG A 216           
SHEET    3   D 9 MET B 832  ASN B 836  1  N  ILE B 834   O  ALA B 863           
SHEET    4   D 9 SER B 956  GLY B 962  1  O  TRP B 958   N  PHE B 833           
SHEET    5   D 9 ASN B 985  ASP B 990  1  O  PHE B 987   N  ILE B 959           
SHEET    6   D 9 SER B1063  TYR B1068  1  O  SER B1063   N  VAL B 986           
SHEET    7   D 9 TYR B1036  VAL B1040  1  N  TYR B1036   O  LEU B1064           
SHEET    8   D 9 PHE B1099  TYR B1101 -1  O  TYR B1101   N  VAL B1037           
SHEET    9   D 9 PHE B1113  LEU B1115 -1  O  GLN B1114   N  ARG B1100           
SHEET    1   E 6 PHE A 261  GLY A 265  0                                        
SHEET    2   E 6 ILE A 297  VAL A 302 -1  O  LYS A 301   N  ASP A 262           
SHEET    3   E 6 ARG A 271  SER A 275  1  N  ILE A 273   O  ILE A 300           
SHEET    4   E 6 VAL A 323  ASP A 328  1  O  LEU A 327   N  VAL A 274           
SHEET    5   E 6 ILE A 358  ARG A 362  1  O  LEU A 359   N  VAL A 326           
SHEET    6   E 6 PHE A 390  THR A 391  1  O  PHE A 390   N  ARG A 362           
SHEET    1   F 2 ASN A 680  TRP A 684  0                                        
SHEET    2   F 2 LEU A 762  PRO A 766 -1  O  GLN A 765   N  VAL A 681           
SHEET    1   G 3 ILE A 704  LYS A 710  0                                        
SHEET    2   G 3 TYR A 734  ILE A 740 -1  O  LYS A 735   N  ALA A 709           
SHEET    3   G 3 LEU A 724  GLU A 725 -1  N  LEU A 724   O  PHE A 736           
SHEET    1   H 9 PHE A1113  LEU A1115  0                                        
SHEET    2   H 9 PHE A1099  TYR A1101 -1  N  ARG A1100   O  GLN A1114           
SHEET    3   H 9 TYR A1036  VAL A1040 -1  N  VAL A1037   O  TYR A1101           
SHEET    4   H 9 SER A1063  TYR A1068  1  O  LEU A1064   N  TYR A1036           
SHEET    5   H 9 ASN A 985  ASP A 990  1  N  VAL A 986   O  SER A1063           
SHEET    6   H 9 SER A 956  GLY A 962  1  N  ILE A 959   O  PHE A 987           
SHEET    7   H 9 MET A 832  ASN A 836  1  N  PHE A 833   O  TRP A 958           
SHEET    8   H 9 ALA A 863  GLY A 865  1  O  ALA A 863   N  ILE A 834           
SHEET    9   H 9 VAL B 215  ARG B 216  1  O  ARG B 216   N  TRP A 864           
SHEET    1   I 8 LYS B   3  ASP B   9  0                                        
SHEET    2   I 8 ILE B 180  LEU B 186 -1  O  ILE B 183   N  MET B   6           
SHEET    3   I 8 PHE B 448  TYR B 455 -1  O  GLY B 451   N  ILE B 180           
SHEET    4   I 8 ILE B 463  GLY B 471 -1  O  GLY B 471   N  PHE B 448           
SHEET    5   I 8 ILE B 418  LEU B 425 -1  N  CYS B 420   O  LEU B 468           
SHEET    6   I 8 TYR B 486  CYS B 489  1  O  ALA B 488   N  TRP B 423           
SHEET    7   I 8 THR B 509  ASN B 513  1  O  THR B 509   N  VAL B 487           
SHEET    8   I 8 LYS B 540  ILE B 544  1  O  ILE B 544   N  LEU B 512           
SHEET    1   J 7 THR B  57  GLU B  60  0                                        
SHEET    2   J 7 VAL B  24  ILE B  27  1  N  ALA B  25   O  THR B  57           
SHEET    3   J 7 THR B  81  THR B  85  1  O  THR B  82   N  VAL B  24           
SHEET    4   J 7 VAL B 108  ALA B 113  1  O  HIS B 110   N  THR B  83           
SHEET    5   J 7 PHE B 167  ASP B 172  1  O  PHE B 167   N  PHE B 109           
SHEET    6   J 7 ALA B 139  ALA B 142  1  N  LEU B 141   O  MET B 168           
SHEET    7   J 7 LEU B 304  ARG B 306 -1  O  ARG B 306   N  MET B 140           
SHEET    1   K 6 PHE B 261  GLY B 265  0                                        
SHEET    2   K 6 ILE B 297  VAL B 302 -1  O  LYS B 301   N  ASP B 262           
SHEET    3   K 6 ARG B 271  SER B 275  1  N  ILE B 273   O  ILE B 300           
SHEET    4   K 6 VAL B 323  ASP B 328  1  O  THR B 325   N  VAL B 274           
SHEET    5   K 6 ILE B 358  ARG B 362  1  O  LEU B 359   N  ILE B 324           
SHEET    6   K 6 PHE B 390  THR B 391  1  O  PHE B 390   N  ARG B 362           
SHEET    1   L 2 ASN B 680  TRP B 684  0                                        
SHEET    2   L 2 LEU B 762  PRO B 766 -1  O  GLN B 765   N  VAL B 681           
SHEET    1   M 3 ILE B 704  ALA B 709  0                                        
SHEET    2   M 3 LYS B 735  ILE B 740 -1  O  ARG B 737   N  VAL B 707           
SHEET    3   M 3 LEU B 724  GLU B 725 -1  N  LEU B 724   O  PHE B 736           
SSBOND   1 CYS A 1195    CYS A 1212                          1555   1555  2.01  
LINK         SG  CYS A 689                FE1  SF4 A2233     1555   1555  2.32  
LINK         SG  CYS A 692                FE2  SF4 A2233     1555   1555  2.25  
LINK         SG  CYS A 695                FE3  SF4 A2233     1555   1555  2.35  
LINK         SG  CYS A 699                FE1  SF4 A2234     1555   1555  2.30  
LINK         SG  CYS A 745                FE2  SF4 A2234     1555   1555  2.27  
LINK         SG  CYS A 748                FE4  SF4 A2234     1555   1555  2.32  
LINK         SG  CYS A 751                FE3  SF4 A2234     1555   1555  2.34  
LINK         SG  CYS A 755                FE4  SF4 A2233     1555   1555  2.28  
LINK         SG  CYS A 812                FE1  SF4 A2235     1555   1555  2.29  
LINK         SG  CYS A 815                FE2  SF4 A2235     1555   1555  2.35  
LINK         SG  CYS A 840                FE3  SF4 A2235     1555   1555  2.29  
LINK         OD1 ASP A 963                MG    MG A2237     1555   1555  2.06  
LINK         OD2 ASP A 983                CA    CA A2238     1555   1555  2.79  
LINK         OD1 ASN A 985                CA    CA A2238     1555   1555  2.72  
LINK         OG1 THR A 991                MG    MG A2237     1555   1555  2.33  
LINK         O   VAL A 993                MG    MG A2237     1555   1555  2.10  
LINK         O   ALA A1056                CA    CA A2238     1555   1555  2.88  
LINK         O   PHE A1059                CA    CA A2238     1555   1555  2.64  
LINK         O   GLY A1061                CA    CA A2238     1555   1555  3.04  
LINK         SG  CYS A1071                FE4  SF4 A2235     1555   1555  2.28  
LINK         SG  CYS B 689                FE1  SF4 B3233     1555   1555  2.32  
LINK         SG  CYS B 692                FE2  SF4 B3233     1555   1555  2.27  
LINK         SG  CYS B 695                FE3  SF4 B3233     1555   1555  2.35  
LINK         SG  CYS B 699                FE1  SF4 B3234     1555   1555  2.29  
LINK         SG  CYS B 745                FE2  SF4 B3234     1555   1555  2.29  
LINK         SG  CYS B 748                FE4  SF4 B3234     1555   1555  2.29  
LINK         SG  CYS B 751                FE3  SF4 B3234     1555   1555  2.30  
LINK         SG  CYS B 755                FE4  SF4 B3233     1555   1555  2.31  
LINK         SG  CYS B 812                FE1  SF4 B3235     1555   1555  2.30  
LINK         SG  CYS B 815                FE2  SF4 B3235     1555   1555  2.31  
LINK         SG  CYS B 840                FE3  SF4 B3235     1555   1555  2.29  
LINK         OD1 ASP B 963                MG    MG B3237     1555   1555  2.03  
LINK         OD2 ASP B 983                CA    CA B3238     1555   1555  2.84  
LINK         OD1 ASN B 985                CA    CA B3238     1555   1555  2.74  
LINK         OG1 THR B 991                MG    MG B3237     1555   1555  2.26  
LINK         O   VAL B 993                MG    MG B3237     1555   1555  2.21  
LINK         O   ALA B1056                CA    CA B3238     1555   1555  2.88  
LINK         O   PHE B1059                CA    CA B3238     1555   1555  2.71  
LINK         O   GLY B1061                CA    CA B3238     1555   1555  2.97  
LINK         SG  CYS B1071                FE4  SF4 B3235     1555   1555  2.28  
LINK        MG    MG A2237                 O23 HTL A2236     1555   1555  2.02  
LINK        MG    MG A2237                 O   HOH A2375     1555   1555  2.20  
LINK        MG    MG A2237                 O12 HTL A2236     1555   1555  2.13  
LINK        MG    MG B3237                 O12 HTL B3236     1555   1555  2.08  
LINK        MG    MG B3237                 O23 HTL B3236     1555   1555  2.16  
LINK        MG    MG B3237                 O   HOH B3382     1555   1555  2.24  
CISPEP   1 THR A   31    PRO A   32          0         7.53                     
CISPEP   2 ARG A  306    PRO A  307          0        -7.60                     
CISPEP   3 ALA A  848    PRO A  849          0         6.48                     
CISPEP   4 THR B   31    PRO B   32          0         4.66                     
CISPEP   5 ARG B  306    PRO B  307          0       -18.40                     
CISPEP   6 ALA B  848    PRO B  849          0        15.79                     
SITE     1 AC1  5 ASP A 963  THR A 991  VAL A 993  HTL A2236                    
SITE     2 AC1  5 HOH A2375                                                     
SITE     1 AC2  7 ASP A 983  ASN A 985  ALA A1056  GLU A1057                    
SITE     2 AC2  7 PHE A1059  GLY A1061  SER A1063                               
SITE     1 AC3  5 ASP B 963  THR B 991  VAL B 993  HTL B3236                    
SITE     2 AC3  5 HOH B3382                                                     
SITE     1 AC4  7 ASP B 983  ASN B 985  ALA B1056  GLU B1057                    
SITE     2 AC4  7 PHE B1059  GLY B1061  SER B1063                               
SITE     1 AC5  9 TRP A 684  CYS A 689  ILE A 690  CYS A 692                    
SITE     2 AC5  9 ASN A 693  CYS A 695  CYS A 755  PRO A 756                    
SITE     3 AC5  9 LEU A 762                                                     
SITE     1 AC6  7 CYS A 699  ILE A 704  CYS A 745  MET A 746                    
SITE     2 AC6  7 CYS A 748  GLY A 749  CYS A 751                               
SITE     1 AC7  8 LYS A 459  CYS A 812  CYS A 815  GLU A 817                    
SITE     2 AC7  8 CYS A 840  CYS A1071  ILE A1072  MET B1203                    
SITE     1 AC8 28 PRO A  29  ILE A  30  GLU A  64  GLN A  88                    
SITE     2 AC8 28 LEU A  92  ARG A 114  GLU A 817  THR A 838                    
SITE     3 AC8 28 GLY A 839  CYS A 840  PHE A 869  GLU A 870                    
SITE     4 AC8 28 GLY A 962  ASP A 963  GLY A 964  TRP A 965                    
SITE     5 AC8 28 THR A 991  VAL A 993  TYR A 994  SER A 995                    
SITE     6 AC8 28 ASN A 996  THR A 997   MG A2237  CO2 A2240                    
SITE     7 AC8 28 HOH A2248  HOH A2264  HOH A2265  HOH A2375                    
SITE     1 AC9  6 THR A  31  ARG A 114  ASN A 996  THR A 997                    
SITE     2 AC9  6 HTL A2236  MET B1202                                          
SITE     1 BC1 10 TRP B 684  CYS B 689  ILE B 690  CYS B 692                    
SITE     2 BC1 10 ASN B 693  CYS B 695  CYS B 755  PRO B 756                    
SITE     3 BC1 10 ALA B 761  LEU B 762                                          
SITE     1 BC2  8 CYS B 699  PRO B 700  ILE B 704  CYS B 745                    
SITE     2 BC2  8 MET B 746  CYS B 748  GLY B 749  CYS B 751                    
SITE     1 BC3  8 MET A1203  LYS B 459  CYS B 812  CYS B 815                    
SITE     2 BC3  8 GLU B 817  CYS B 840  CYS B1071  ILE B1072                    
SITE     1 BC4 27 PRO B  29  GLU B  64  GLN B  88  LEU B  92                    
SITE     2 BC4 27 ARG B 114  GLU B 817  THR B 838  GLY B 839                    
SITE     3 BC4 27 CYS B 840  PHE B 869  GLU B 870  GLY B 962                    
SITE     4 BC4 27 ASP B 963  GLY B 964  TRP B 965  THR B 991                    
SITE     5 BC4 27 VAL B 993  TYR B 994  SER B 995  ASN B 996                    
SITE     6 BC4 27 THR B 997   MG B3237  CO2 B3240  HOH B3273                    
SITE     7 BC4 27 HOH B3308  HOH B3340  HOH B3382                               
SITE     1 BC5  7 MET A1202  ILE B  30  THR B  31  ARG B 114                    
SITE     2 BC5  7 ASN B 996  THR B 997  HTL B3236                               
CRYST1   86.110  145.760  210.260  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      0.011613  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006861  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004756        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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