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Database: PDB
Entry: 1JSC
LinkDB: 1JSC
Original site: 1JSC 
HEADER    LYASE                                   17-AUG-01   1JSC              
TITLE     CRYSTAL STRUCTURE OF THE CATALYTIC SUBUNIT OF YEAST                   
TITLE    2 ACETOHYDROXYACID SYNTHASE: A TARGET FOR HERBICIDAL                   
TITLE    3 INHIBITORS                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACETOHYDROXY-ACID SYNTHASE;                                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: MATURE CATALYTIC SUBUNIT;                                  
COMPND   5 SYNONYM: ACETOLACTATE SYNTHASE;                                      
COMPND   6 EC: 4.1.3.18;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE   3 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE   4 ORGANISM_TAXID: 4932;                                                
SOURCE   5 GENE: ILV2;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET30C                                    
KEYWDS    ACETOHYDROXYACID SYNTHASE, ACETOLACTATE SYNTHASE, FAD,                
KEYWDS   2 THIAMIN DIPHOSPHATE, HERBICIDE INHIBITION, LYASE                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.S.PANG,R.G.DUGGLEBY,L.W.GUDDAT                                      
REVDAT   3   24-FEB-09 1JSC    1       VERSN                                    
REVDAT   2   27-MAR-02 1JSC    1       JRNL                                     
REVDAT   1   16-JAN-02 1JSC    0                                                
JRNL        AUTH   S.S.PANG,R.G.DUGGLEBY,L.W.GUDDAT                             
JRNL        TITL   CRYSTAL STRUCTURE OF YEAST ACETOHYDROXYACID                  
JRNL        TITL 2 SYNTHASE: A TARGET FOR HERBICIDAL INHIBITORS.                
JRNL        REF    J.MOL.BIOL.                   V. 317   249 2002              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   11902841                                                     
JRNL        DOI    10.1006/JMBI.2001.5419                                       
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 100.00                         
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)   (%) : 94.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 54927                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : R FREE THROUGHOUT               
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.188                           
REMARK   3   FREE R VALUE                     : 0.219                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.500                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5574                            
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) : 2.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.70                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 90.00                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 4664                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2470                       
REMARK   3   BIN FREE R VALUE                    : 0.2670                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 9.62                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 496                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.000                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8126                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 177                                     
REMARK   3   SOLVENT ATOMS            : 325                                     
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) : 1.24500                                              
REMARK   3    B22 (A**2) : -8.22800                                             
REMARK   3    B33 (A**2) : 6.98300                                              
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.29                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.30                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.33                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.35                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.27                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.45                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.79                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : ANISOTROPIC                               
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  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : JIANG ET AL.                                         
REMARK   3   KSOL        : -1.00                                                
REMARK   3   BSOL        : -1.00                                                
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: NULL                                      
REMARK   4                                                                      
REMARK   4 1JSC COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-AUG-01.                  
REMARK 100 THE RCSB ID CODE IS RCSB014131.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-DEC-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 5.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 14-BM-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00                               
REMARK 200  MONOCHROMATOR                  : GE(III)                            
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 214515                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.05800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.69                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.30100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1BFD                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 66.10                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.62                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, POTASSIUM PHOSPHATE,           
REMARK 280  THIAMIN DIPHOSPHATE, FAD, MAGNESIUM CHLORIDE, DTT, AMMONIUM         
REMARK 280  ACETATE, PH 5.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE         
REMARK 280  291K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       47.77600            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       89.42900            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       54.70050            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       89.42900            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       47.77600            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       54.70050            
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: 10760 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 39330 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -80.0 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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ALA A    58                                                      
REMARK 465     PRO A    59                                                      
REMARK 465     SER A    60                                                      
REMARK 465     PHE A    61                                                      
REMARK 465     ASN A    62                                                      
REMARK 465     VAL A    63                                                      
REMARK 465     ASP A    64                                                      
REMARK 465     PRO A    65                                                      
REMARK 465     LEU A    66                                                      
REMARK 465     GLU A    67                                                      
REMARK 465     GLN A    68                                                      
REMARK 465     PRO A    69                                                      
REMARK 465     ALA A    70                                                      
REMARK 465     GLU A    71                                                      
REMARK 465     PRO A    72                                                      
REMARK 465     SER A    73                                                      
REMARK 465     LYS A    74                                                      
REMARK 465     LEU A    75                                                      
REMARK 465     ALA A    76                                                      
REMARK 465     LYS A    77                                                      
REMARK 465     LYS A    78                                                      
REMARK 465     LEU A    79                                                      
REMARK 465     ARG A    80                                                      
REMARK 465     ALA A    81                                                      
REMARK 465     GLU A    82                                                      
REMARK 465     ASN A   271                                                      
REMARK 465     ALA A   272                                                      
REMARK 465     LEU A   273                                                      
REMARK 465     ASN A   274                                                      
REMARK 465     GLN A   275                                                      
REMARK 465     LEU A   276                                                      
REMARK 465     THR A   277                                                      
REMARK 465     SER A   278                                                      
REMARK 465     ARG A   279                                                      
REMARK 465     GLN A   580                                                      
REMARK 465     GLY A   581                                                      
REMARK 465     MET A   582                                                      
REMARK 465     VAL A   583                                                      
REMARK 465     THR A   584                                                      
REMARK 465     GLN A   585                                                      
REMARK 465     TRP A   586                                                      
REMARK 465     GLN A   587                                                      
REMARK 465     SER A   588                                                      
REMARK 465     LEU A   589                                                      
REMARK 465     PHE A   590                                                      
REMARK 465     TYR A   591                                                      
REMARK 465     GLU A   592                                                      
REMARK 465     HIS A   593                                                      
REMARK 465     ARG A   594                                                      
REMARK 465     TYR A   595                                                      
REMARK 465     VAL A   649                                                      
REMARK 465     PRO A   650                                                      
REMARK 465     VAL A   651                                                      
REMARK 465     LEU A   652                                                      
REMARK 465     PRO A   653                                                      
REMARK 465     MET A   654                                                      
REMARK 465     VAL A   655                                                      
REMARK 465     ALA A   656                                                      
REMARK 465     GLY A   657                                                      
REMARK 465     GLY A   658                                                      
REMARK 465     SER A   659                                                      
REMARK 465     GLY A   660                                                      
REMARK 465     LEU A   661                                                      
REMARK 465     ASP A   662                                                      
REMARK 465     GLU A   663                                                      
REMARK 465     PHE A   664                                                      
REMARK 465     ILE A   665                                                      
REMARK 465     ASN A   666                                                      
REMARK 465     PHE A   667                                                      
REMARK 465     ASP A   668                                                      
REMARK 465     PRO A   669                                                      
REMARK 465     GLU A   670                                                      
REMARK 465     VAL A   671                                                      
REMARK 465     GLU A   672                                                      
REMARK 465     ARG A   673                                                      
REMARK 465     GLN A   674                                                      
REMARK 465     GLN A   675                                                      
REMARK 465     THR A   676                                                      
REMARK 465     GLU A   677                                                      
REMARK 465     LEU A   678                                                      
REMARK 465     ARG A   679                                                      
REMARK 465     HIS A   680                                                      
REMARK 465     LYS A   681                                                      
REMARK 465     ARG A   682                                                      
REMARK 465     THR A   683                                                      
REMARK 465     GLY A   684                                                      
REMARK 465     GLY A   685                                                      
REMARK 465     LYS A   686                                                      
REMARK 465     HIS A   687                                                      
REMARK 465     ALA B    58                                                      
REMARK 465     PRO B    59                                                      
REMARK 465     SER B    60                                                      
REMARK 465     PHE B    61                                                      
REMARK 465     ASN B    62                                                      
REMARK 465     VAL B    63                                                      
REMARK 465     ASP B    64                                                      
REMARK 465     PRO B    65                                                      
REMARK 465     LEU B    66                                                      
REMARK 465     GLU B    67                                                      
REMARK 465     GLN B    68                                                      
REMARK 465     PRO B    69                                                      
REMARK 465     ALA B    70                                                      
REMARK 465     GLU B    71                                                      
REMARK 465     PRO B    72                                                      
REMARK 465     SER B    73                                                      
REMARK 465     LYS B    74                                                      
REMARK 465     LEU B    75                                                      
REMARK 465     ALA B    76                                                      
REMARK 465     LYS B    77                                                      
REMARK 465     LYS B    78                                                      
REMARK 465     LEU B    79                                                      
REMARK 465     ARG B    80                                                      
REMARK 465     ALA B    81                                                      
REMARK 465     LEU B   273                                                      
REMARK 465     ASN B   274                                                      
REMARK 465     GLN B   275                                                      
REMARK 465     LYS B   301                                                      
REMARK 465     ALA B   397                                                      
REMARK 465     GLU B   398                                                      
REMARK 465     GLY B   399                                                      
REMARK 465     ARG B   400                                                      
REMARK 465     GLY B   401                                                      
REMARK 465     GLY B   402                                                      
REMARK 465     LYS B   442                                                      
REMARK 465     GLU B   443                                                      
REMARK 465     PRO B   459                                                      
REMARK 465     TYR B   460                                                      
REMARK 465     ALA B   461                                                      
REMARK 465     TYR B   462                                                      
REMARK 465     MET B   463                                                      
REMARK 465     TYR B   591                                                      
REMARK 465     PRO B   650                                                      
REMARK 465     VAL B   651                                                      
REMARK 465     LEU B   652                                                      
REMARK 465     PRO B   653                                                      
REMARK 465     MET B   654                                                      
REMARK 465     VAL B   655                                                      
REMARK 465     ALA B   656                                                      
REMARK 465     GLY B   657                                                      
REMARK 465     GLY B   658                                                      
REMARK 465     SER B   659                                                      
REMARK 465     GLY B   660                                                      
REMARK 465     LEU B   661                                                      
REMARK 465     ASP B   662                                                      
REMARK 465     GLU B   663                                                      
REMARK 465     PHE B   664                                                      
REMARK 465     ILE B   665                                                      
REMARK 465     ASN B   666                                                      
REMARK 465     PHE B   667                                                      
REMARK 465     ASP B   668                                                      
REMARK 465     PRO B   669                                                      
REMARK 465     GLU B   670                                                      
REMARK 465     VAL B   671                                                      
REMARK 465     GLU B   672                                                      
REMARK 465     ARG B   673                                                      
REMARK 465     GLN B   674                                                      
REMARK 465     GLN B   675                                                      
REMARK 465     THR B   676                                                      
REMARK 465     GLU B   677                                                      
REMARK 465     LEU B   678                                                      
REMARK 465     ARG B   679                                                      
REMARK 465     HIS B   680                                                      
REMARK 465     LYS B   681                                                      
REMARK 465     ARG B   682                                                      
REMARK 465     THR B   683                                                      
REMARK 465     GLY B   684                                                      
REMARK 465     GLY B   685                                                      
REMARK 465     LYS B   686                                                      
REMARK 465     HIS B   687                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS(M=MODEL NUMBER;            
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 265    CG   CD   CE   NZ                                   
REMARK 470     LYS A 411    CG   CD   CE   NZ                                   
REMARK 470     LYS A 472    CG   CD   CE   NZ                                   
REMARK 470     GLU A 579    CG   CD   OE1  OE2                                  
REMARK 470     SER A 596    OG                                                  
REMARK 470     LYS A 647    CG   CD   CE   NZ                                   
REMARK 470     LYS A 648    CG   CD   CE   NZ                                   
REMARK 470     GLU B  82    CB   CG   CD   OE1  OE2                             
REMARK 470     ASN B 271    CG   OD1  ND2                                       
REMARK 470     ARG B 279    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL B 285    CG1  CG2                                            
REMARK 470     GLN B 287    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 291    CG   CD   CE   NZ                                   
REMARK 470     ILE B 296    CG1  CG2  CD1                                       
REMARK 470     ARG B 326    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL B 364    CG1  CG2                                            
REMARK 470     ASN B 366    CG   OD1  ND2                                       
REMARK 470     ASN B 384    CG   OD1  ND2                                       
REMARK 470     ILE B 385    CG1  CG2  CD1                                       
REMARK 470     LYS B 387    CG   CD   CE   NZ                                   
REMARK 470     PHE B 388    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU B 391    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 394    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 411    CG   CD   CE   NZ                                   
REMARK 470     LYS B 415    CG   CD   CE   NZ                                   
REMARK 470     VAL B 416    CG1  CG2                                            
REMARK 470     VAL B 417    CG1  CG2                                            
REMARK 470     LYS B 437    CG   CD   CE   NZ                                   
REMARK 470     ILE B 438    CG1  CG2  CD1                                       
REMARK 470     ARG B 444    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 453    CG   CD   CE   NZ                                   
REMARK 470     TRP B 454    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP B 454    CZ3  CH2                                            
REMARK 470     LYS B 455    CG   CD   CE   NZ                                   
REMARK 470     LYS B 456    CG   CD   CE   NZ                                   
REMARK 470     LYS B 478    CG   CD   CE   NZ                                   
REMARK 470     GLU B 592    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 594    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 647    CG   CD   CE   NZ                                   
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    PRO A 269      155.82    -44.50                                   
REMARK 500    ASP A 350     -156.76     71.96                                   
REMARK 500    ARG A 444       56.08   -142.40                                   
REMARK 500    PRO A 459       95.13    -55.61                                   
REMARK 500    TYR A 460      104.58    -56.58                                   
REMARK 500    TYR A 462     -165.04    -69.68                                   
REMARK 500    GLU A 464      177.16    -43.04                                   
REMARK 500    ARG A 511      -35.63   -133.14                                   
REMARK 500    HIS A 597       87.63     45.73                                   
REMARK 500    GLU A 623        2.36    -69.32                                   
REMARK 500    LYS A 647      152.56    -42.79                                   
REMARK 500    ASP B  84      -73.15    -70.08                                   
REMARK 500    ASN B 271     -163.00    -72.43                                   
REMARK 500    LEU B 295      -19.51    -49.10                                   
REMARK 500    ILE B 296      -75.98    -77.42                                   
REMARK 500    GLN B 328       78.16     43.90                                   
REMARK 500    ASP B 350     -147.38     67.18                                   
REMARK 500    PHE B 377       75.18     34.79                                   
REMARK 500    THR B 382       85.08   -151.72                                   
REMARK 500    ALA B 389       87.07     55.75                                   
REMARK 500    ARG B 394      -84.00   -176.26                                   
REMARK 500    ALA B 395       35.31    -75.49                                   
REMARK 500    VAL B 416      -58.60   -133.52                                   
REMARK 500    VAL B 423       76.53   -104.45                                   
REMARK 500    LYS B 433       20.77    -71.29                                   
REMARK 500    MET B 434        3.34   -150.37                                   
REMARK 500    LYS B 437       19.60    -68.19                                   
REMARK 500    PRO B 440      169.38    -48.31                                   
REMARK 500    SER B 445      -32.41   -142.05                                   
REMARK 500    ASN B 452      -38.94    -38.87                                   
REMARK 500    ARG B 511      -36.69   -132.28                                   
REMARK 500    GLU B 578      -18.84    -46.64                                   
REMARK 500    THR B 598       85.38     73.08                                   
REMARK 500    GLU B 623        2.90    -69.89                                   
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                               K A 696   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 350   OD2                                                    
REMARK 620 2 GLN A 343   OE1  70.3                                              
REMARK 620 3 GLN A 506   O   122.0 156.5                                        
REMARK 620 4 TRP A 508   O   147.5  80.3  90.4                                  
REMARK 620 5 HOH A 772   O    80.4  75.9  86.2 106.0                            
REMARK 620 6 HOH A1029   O    89.9  96.6 103.0  79.8 169.3                      
REMARK 620 7 HOH A1033   O    43.8 112.5  78.4 167.0  79.9  96.3                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 699  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A 577   OD1                                                    
REMARK 620 2 HOH A 796   O    81.4                                              
REMARK 620 3 TPP A 700   O1A 168.1  87.1                                        
REMARK 620 4 ASP A 550   OD2  96.4  86.6  85.9                                  
REMARK 620 5 TPP A 700   O3B  88.4 103.1  91.3 169.8                            
REMARK 620 6 HOH A 795   O    94.9 169.5  97.0  84.1  86.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K B1696   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B 802   O                                                      
REMARK 620 2 HOH B1028   O   163.4                                              
REMARK 620 3 ASP B 350   OD2  76.7  89.2                                        
REMARK 620 4 GLN B 343   NE2  54.4 124.7  58.2                                  
REMARK 620 5 GLN B 343   OE1  87.7  98.7  80.7  38.5                            
REMARK 620 6 TRP B 508   O   115.6  80.6 157.2 111.7  80.7                      
REMARK 620 7 HOH B1034   O    78.9  84.7  39.9  92.4 120.6 155.9                
REMARK 620 8 GLN B 506   O    84.3  93.2 112.4 138.5 162.4  88.7  73.1          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B1699  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN B 577   OD1                                                    
REMARK 620 2 TPP B1700   O1A 166.8                                              
REMARK 620 3 HOH B 794   O    84.9  86.3                                        
REMARK 620 4 TPP B1700   O3B  99.3  93.6 120.1                                  
REMARK 620 5 HOH B 748   O    88.9  95.3 156.3  83.5                            
REMARK 620 6 ASP B 550   OD2  82.1  85.7  69.8 170.1  86.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 696                   
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 699                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 1696                  
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1699                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2HP A 698                 
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2HP B 1697                
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 2HP B 1698                
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TPP A 700                 
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 701                 
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TPP B 1700                
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B 1701                
DBREF  1JSC A   58   687  UNP    P07342   ILVB_YEAST      58    687             
DBREF  1JSC B   58   687  UNP    P07342   ILVB_YEAST      58    687             
SEQRES   1 A  630  ALA PRO SER PHE ASN VAL ASP PRO LEU GLU GLN PRO ALA          
SEQRES   2 A  630  GLU PRO SER LYS LEU ALA LYS LYS LEU ARG ALA GLU PRO          
SEQRES   3 A  630  ASP MET ASP THR SER PHE VAL GLY LEU THR GLY GLY GLN          
SEQRES   4 A  630  ILE PHE ASN GLU MET MET SER ARG GLN ASN VAL ASP THR          
SEQRES   5 A  630  VAL PHE GLY TYR PRO GLY GLY ALA ILE LEU PRO VAL TYR          
SEQRES   6 A  630  ASP ALA ILE HIS ASN SER ASP LYS PHE ASN PHE VAL LEU          
SEQRES   7 A  630  PRO LYS HIS GLU GLN GLY ALA GLY HIS MET ALA GLU GLY          
SEQRES   8 A  630  TYR ALA ARG ALA SER GLY LYS PRO GLY VAL VAL LEU VAL          
SEQRES   9 A  630  THR SER GLY PRO GLY ALA THR ASN VAL VAL THR PRO MET          
SEQRES  10 A  630  ALA ASP ALA PHE ALA ASP GLY ILE PRO MET VAL VAL PHE          
SEQRES  11 A  630  THR GLY GLN VAL PRO THR SER ALA ILE GLY THR ASP ALA          
SEQRES  12 A  630  PHE GLN GLU ALA ASP VAL VAL GLY ILE SER ARG SER CYS          
SEQRES  13 A  630  THR LYS TRP ASN VAL MET VAL LYS SER VAL GLU GLU LEU          
SEQRES  14 A  630  PRO LEU ARG ILE ASN GLU ALA PHE GLU ILE ALA THR SER          
SEQRES  15 A  630  GLY ARG PRO GLY PRO VAL LEU VAL ASP LEU PRO LYS ASP          
SEQRES  16 A  630  VAL THR ALA ALA ILE LEU ARG ASN PRO ILE PRO THR LYS          
SEQRES  17 A  630  THR THR LEU PRO SER ASN ALA LEU ASN GLN LEU THR SER          
SEQRES  18 A  630  ARG ALA GLN ASP GLU PHE VAL MET GLN SER ILE ASN LYS          
SEQRES  19 A  630  ALA ALA ASP LEU ILE ASN LEU ALA LYS LYS PRO VAL LEU          
SEQRES  20 A  630  TYR VAL GLY ALA GLY ILE LEU ASN HIS ALA ASP GLY PRO          
SEQRES  21 A  630  ARG LEU LEU LYS GLU LEU SER ASP ARG ALA GLN ILE PRO          
SEQRES  22 A  630  VAL THR THR THR LEU GLN GLY LEU GLY SER PHE ASP GLN          
SEQRES  23 A  630  GLU ASP PRO LYS SER LEU ASP MET LEU GLY MET HIS GLY          
SEQRES  24 A  630  CYS ALA THR ALA ASN LEU ALA VAL GLN ASN ALA ASP LEU          
SEQRES  25 A  630  ILE ILE ALA VAL GLY ALA ARG PHE ASP ASP ARG VAL THR          
SEQRES  26 A  630  GLY ASN ILE SER LYS PHE ALA PRO GLU ALA ARG ARG ALA          
SEQRES  27 A  630  ALA ALA GLU GLY ARG GLY GLY ILE ILE HIS PHE GLU VAL          
SEQRES  28 A  630  SER PRO LYS ASN ILE ASN LYS VAL VAL GLN THR GLN ILE          
SEQRES  29 A  630  ALA VAL GLU GLY ASP ALA THR THR ASN LEU GLY LYS MET          
SEQRES  30 A  630  MET SER LYS ILE PHE PRO VAL LYS GLU ARG SER GLU TRP          
SEQRES  31 A  630  PHE ALA GLN ILE ASN LYS TRP LYS LYS GLU TYR PRO TYR          
SEQRES  32 A  630  ALA TYR MET GLU GLU THR PRO GLY SER LYS ILE LYS PRO          
SEQRES  33 A  630  GLN THR VAL ILE LYS LYS LEU SER LYS VAL ALA ASN ASP          
SEQRES  34 A  630  THR GLY ARG HIS VAL ILE VAL THR THR GLY VAL GLY GLN          
SEQRES  35 A  630  HIS GLN MET TRP ALA ALA GLN HIS TRP THR TRP ARG ASN          
SEQRES  36 A  630  PRO HIS THR PHE ILE THR SER GLY GLY LEU GLY THR MET          
SEQRES  37 A  630  GLY TYR GLY LEU PRO ALA ALA ILE GLY ALA GLN VAL ALA          
SEQRES  38 A  630  LYS PRO GLU SER LEU VAL ILE ASP ILE ASP GLY ASP ALA          
SEQRES  39 A  630  SER PHE ASN MET THR LEU THR GLU LEU SER SER ALA VAL          
SEQRES  40 A  630  GLN ALA GLY THR PRO VAL LYS ILE LEU ILE LEU ASN ASN          
SEQRES  41 A  630  GLU GLU GLN GLY MET VAL THR GLN TRP GLN SER LEU PHE          
SEQRES  42 A  630  TYR GLU HIS ARG TYR SER HIS THR HIS GLN LEU ASN PRO          
SEQRES  43 A  630  ASP PHE ILE LYS LEU ALA GLU ALA MET GLY LEU LYS GLY          
SEQRES  44 A  630  LEU ARG VAL LYS LYS GLN GLU GLU LEU ASP ALA LYS LEU          
SEQRES  45 A  630  LYS GLU PHE VAL SER THR LYS GLY PRO VAL LEU LEU GLU          
SEQRES  46 A  630  VAL GLU VAL ASP LYS LYS VAL PRO VAL LEU PRO MET VAL          
SEQRES  47 A  630  ALA GLY GLY SER GLY LEU ASP GLU PHE ILE ASN PHE ASP          
SEQRES  48 A  630  PRO GLU VAL GLU ARG GLN GLN THR GLU LEU ARG HIS LYS          
SEQRES  49 A  630  ARG THR GLY GLY LYS HIS                                      
SEQRES   1 B  630  ALA PRO SER PHE ASN VAL ASP PRO LEU GLU GLN PRO ALA          
SEQRES   2 B  630  GLU PRO SER LYS LEU ALA LYS LYS LEU ARG ALA GLU PRO          
SEQRES   3 B  630  ASP MET ASP THR SER PHE VAL GLY LEU THR GLY GLY GLN          
SEQRES   4 B  630  ILE PHE ASN GLU MET MET SER ARG GLN ASN VAL ASP THR          
SEQRES   5 B  630  VAL PHE GLY TYR PRO GLY GLY ALA ILE LEU PRO VAL TYR          
SEQRES   6 B  630  ASP ALA ILE HIS ASN SER ASP LYS PHE ASN PHE VAL LEU          
SEQRES   7 B  630  PRO LYS HIS GLU GLN GLY ALA GLY HIS MET ALA GLU GLY          
SEQRES   8 B  630  TYR ALA ARG ALA SER GLY LYS PRO GLY VAL VAL LEU VAL          
SEQRES   9 B  630  THR SER GLY PRO GLY ALA THR ASN VAL VAL THR PRO MET          
SEQRES  10 B  630  ALA ASP ALA PHE ALA ASP GLY ILE PRO MET VAL VAL PHE          
SEQRES  11 B  630  THR GLY GLN VAL PRO THR SER ALA ILE GLY THR ASP ALA          
SEQRES  12 B  630  PHE GLN GLU ALA ASP VAL VAL GLY ILE SER ARG SER CYS          
SEQRES  13 B  630  THR LYS TRP ASN VAL MET VAL LYS SER VAL GLU GLU LEU          
SEQRES  14 B  630  PRO LEU ARG ILE ASN GLU ALA PHE GLU ILE ALA THR SER          
SEQRES  15 B  630  GLY ARG PRO GLY PRO VAL LEU VAL ASP LEU PRO LYS ASP          
SEQRES  16 B  630  VAL THR ALA ALA ILE LEU ARG ASN PRO ILE PRO THR LYS          
SEQRES  17 B  630  THR THR LEU PRO SER ASN ALA LEU ASN GLN LEU THR SER          
SEQRES  18 B  630  ARG ALA GLN ASP GLU PHE VAL MET GLN SER ILE ASN LYS          
SEQRES  19 B  630  ALA ALA ASP LEU ILE ASN LEU ALA LYS LYS PRO VAL LEU          
SEQRES  20 B  630  TYR VAL GLY ALA GLY ILE LEU ASN HIS ALA ASP GLY PRO          
SEQRES  21 B  630  ARG LEU LEU LYS GLU LEU SER ASP ARG ALA GLN ILE PRO          
SEQRES  22 B  630  VAL THR THR THR LEU GLN GLY LEU GLY SER PHE ASP GLN          
SEQRES  23 B  630  GLU ASP PRO LYS SER LEU ASP MET LEU GLY MET HIS GLY          
SEQRES  24 B  630  CYS ALA THR ALA ASN LEU ALA VAL GLN ASN ALA ASP LEU          
SEQRES  25 B  630  ILE ILE ALA VAL GLY ALA ARG PHE ASP ASP ARG VAL THR          
SEQRES  26 B  630  GLY ASN ILE SER LYS PHE ALA PRO GLU ALA ARG ARG ALA          
SEQRES  27 B  630  ALA ALA GLU GLY ARG GLY GLY ILE ILE HIS PHE GLU VAL          
SEQRES  28 B  630  SER PRO LYS ASN ILE ASN LYS VAL VAL GLN THR GLN ILE          
SEQRES  29 B  630  ALA VAL GLU GLY ASP ALA THR THR ASN LEU GLY LYS MET          
SEQRES  30 B  630  MET SER LYS ILE PHE PRO VAL LYS GLU ARG SER GLU TRP          
SEQRES  31 B  630  PHE ALA GLN ILE ASN LYS TRP LYS LYS GLU TYR PRO TYR          
SEQRES  32 B  630  ALA TYR MET GLU GLU THR PRO GLY SER LYS ILE LYS PRO          
SEQRES  33 B  630  GLN THR VAL ILE LYS LYS LEU SER LYS VAL ALA ASN ASP          
SEQRES  34 B  630  THR GLY ARG HIS VAL ILE VAL THR THR GLY VAL GLY GLN          
SEQRES  35 B  630  HIS GLN MET TRP ALA ALA GLN HIS TRP THR TRP ARG ASN          
SEQRES  36 B  630  PRO HIS THR PHE ILE THR SER GLY GLY LEU GLY THR MET          
SEQRES  37 B  630  GLY TYR GLY LEU PRO ALA ALA ILE GLY ALA GLN VAL ALA          
SEQRES  38 B  630  LYS PRO GLU SER LEU VAL ILE ASP ILE ASP GLY ASP ALA          
SEQRES  39 B  630  SER PHE ASN MET THR LEU THR GLU LEU SER SER ALA VAL          
SEQRES  40 B  630  GLN ALA GLY THR PRO VAL LYS ILE LEU ILE LEU ASN ASN          
SEQRES  41 B  630  GLU GLU GLN GLY MET VAL THR GLN TRP GLN SER LEU PHE          
SEQRES  42 B  630  TYR GLU HIS ARG TYR SER HIS THR HIS GLN LEU ASN PRO          
SEQRES  43 B  630  ASP PHE ILE LYS LEU ALA GLU ALA MET GLY LEU LYS GLY          
SEQRES  44 B  630  LEU ARG VAL LYS LYS GLN GLU GLU LEU ASP ALA LYS LEU          
SEQRES  45 B  630  LYS GLU PHE VAL SER THR LYS GLY PRO VAL LEU LEU GLU          
SEQRES  46 B  630  VAL GLU VAL ASP LYS LYS VAL PRO VAL LEU PRO MET VAL          
SEQRES  47 B  630  ALA GLY GLY SER GLY LEU ASP GLU PHE ILE ASN PHE ASP          
SEQRES  48 B  630  PRO GLU VAL GLU ARG GLN GLN THR GLU LEU ARG HIS LYS          
SEQRES  49 B  630  ARG THR GLY GLY LYS HIS                                      
HET      K  A 696       1                                                       
HET     MG  A 699       1                                                       
HET      K  B1696       1                                                       
HET     MG  B1699       1                                                       
HET    2HP  A 698       5                                                       
HET    2HP  B1697       5                                                       
HET    2HP  B1698       5                                                       
HET    TPP  A 700      26                                                       
HET    FAD  A 701      53                                                       
HET    TPP  B1700      26                                                       
HET    FAD  B1701      53                                                       
HETNAM       K POTASSIUM ION                                                    
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     2HP DIHYDROGENPHOSPHATE ION                                          
HETNAM     TPP THIAMINE DIPHOSPHATE                                             
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
FORMUL   3    K    2(K 1+)                                                      
FORMUL   4   MG    2(MG 2+)                                                     
FORMUL   7  2HP    3(H2 O4 P 1-)                                                
FORMUL  10  TPP    2(C12 H19 N4 O7 P2 S 1+)                                     
FORMUL  11  FAD    2(C27 H33 N9 O15 P2)                                         
FORMUL  14  HOH   *325(H2 O)                                                    
HELIX    1   1 THR A   93  GLN A  105  1                                  13    
HELIX    2   2 GLY A  115  ALA A  117  5                                   3    
HELIX    3   3 ILE A  118  SER A  128  1                                  11    
HELIX    4   4 HIS A  138  GLY A  154  1                                  17    
HELIX    5   5 GLY A  164  ASN A  169  1                                   6    
HELIX    6   6 VAL A  170  GLY A  181  1                                  12    
HELIX    7   7 PRO A  192  ILE A  196  5                                   5    
HELIX    8   8 ASP A  205  SER A  210  1                                   6    
HELIX    9   9 SER A  222  GLU A  224  5                                   3    
HELIX   10  10 GLU A  225  SER A  239  1                                  15    
HELIX   11  11 LYS A  251  ALA A  256  1                                   6    
HELIX   12  12 LYS A  265  LEU A  268  5                                   4    
HELIX   13  13 GLN A  281  ALA A  299  1                                  19    
HELIX   14  14 ALA A  308  ASN A  312  5                                   5    
HELIX   15  15 ASP A  315  ALA A  327  1                                  13    
HELIX   16  16 CYS A  357  ALA A  367  1                                  11    
HELIX   17  17 ASP A  378  GLY A  383  1                                   6    
HELIX   18  18 ASN A  384  PHE A  388  5                                   5    
HELIX   19  19 ALA A  389  GLU A  398  1                                  10    
HELIX   20  20 SER A  409  ILE A  413  5                                   5    
HELIX   21  21 ASP A  426  MET A  435  1                                  10    
HELIX   22  22 SER A  436  ILE A  438  5                                   3    
HELIX   23  23 ARG A  444  LYS A  456  1                                  13    
HELIX   24  24 LYS A  472  THR A  487  1                                  16    
HELIX   25  25 GLY A  498  TRP A  508  1                                  11    
HELIX   26  26 TYR A  527  LYS A  539  1                                  13    
HELIX   27  27 ASP A  550  LEU A  557  1                                   8    
HELIX   28  28 GLU A  559  GLY A  567  1                                   9    
HELIX   29  29 ASP A  604  GLY A  613  1                                  10    
HELIX   30  30 LYS A  621  THR A  635  1                                  15    
HELIX   31  31 THR B   93  GLN B  105  1                                  13    
HELIX   32  32 GLY B  115  ALA B  117  5                                   3    
HELIX   33  33 ILE B  118  ASN B  127  1                                  10    
HELIX   34  34 HIS B  138  GLY B  154  1                                  17    
HELIX   35  35 GLY B  164  ASN B  169  1                                   6    
HELIX   36  36 VAL B  170  GLY B  181  1                                  12    
HELIX   37  37 PRO B  192  ILE B  196  5                                   5    
HELIX   38  38 ASP B  205  SER B  210  1                                   6    
HELIX   39  39 SER B  222  GLU B  224  5                                   3    
HELIX   40  40 GLU B  225  SER B  239  1                                  15    
HELIX   41  41 LYS B  251  ALA B  256  1                                   6    
HELIX   42  42 LYS B  265  THR B  267  5                                   3    
HELIX   43  43 SER B  278  LEU B  298  1                                  21    
HELIX   44  44 ALA B  308  HIS B  313  5                                   6    
HELIX   45  45 ASP B  315  ALA B  327  1                                  13    
HELIX   46  46 LEU B  335  LEU B  338  5                                   4    
HELIX   47  47 CYS B  357  VAL B  364  1                                   8    
HELIX   48  48 ASN B  384  PHE B  388  5                                   5    
HELIX   49  49 SER B  409  ILE B  413  5                                   5    
HELIX   50  50 ASP B  426  LYS B  433  1                                   8    
HELIX   51  51 SER B  445  GLU B  457  1                                  13    
HELIX   52  52 LYS B  472  THR B  487  1                                  16    
HELIX   53  53 GLY B  498  TRP B  508  1                                  11    
HELIX   54  54 TYR B  527  LYS B  539  1                                  13    
HELIX   55  55 ASP B  550  LEU B  557  1                                   8    
HELIX   56  56 GLU B  559  GLY B  567  1                                   9    
HELIX   57  57 ASP B  604  GLY B  613  1                                  10    
HELIX   58  58 LYS B  621  THR B  635  1                                  15    
SHEET    1   A 2 MET A  85  ASP A  86  0                                        
SHEET    2   A 2 ILE A 262  PRO A 263 -1  O  ILE A 262   N  ASP A  86           
SHEET    1   B 6 ASN A 132  VAL A 134  0                                        
SHEET    2   B 6 THR A 109  GLY A 112  1  N  VAL A 110   O  VAL A 134           
SHEET    3   B 6 GLY A 157  VAL A 161  1  O  VAL A 158   N  PHE A 111           
SHEET    4   B 6 MET A 184  GLN A 190  1  O  PHE A 187   N  VAL A 159           
SHEET    5   B 6 PRO A 244  PRO A 250  1  O  LEU A 249   N  THR A 188           
SHEET    6   B 6 TRP A 216  MET A 219  1  N  VAL A 218   O  ASP A 248           
SHEET    1   C 6 SER A 348  MET A 351  0                                        
SHEET    2   C 6 VAL A 331  THR A 333  1  N  VAL A 331   O  LEU A 349           
SHEET    3   C 6 PRO A 302  VAL A 306  1  N  LEU A 304   O  THR A 332           
SHEET    4   C 6 LEU A 369  VAL A 373  1  O  ILE A 371   N  VAL A 303           
SHEET    5   C 6 GLY A 402  GLU A 407  1  O  ILE A 404   N  ALA A 372           
SHEET    6   C 6 ILE A 421  GLU A 424  1  O  ILE A 421   N  HIS A 405           
SHEET    1   D 6 PHE A 516  ILE A 517  0                                        
SHEET    2   D 6 VAL A 491  THR A 495  1  N  VAL A 493   O  ILE A 517           
SHEET    3   D 6 LEU A 543  GLY A 549  1  O  ILE A 545   N  ILE A 492           
SHEET    4   D 6 LYS A 571  ASN A 576  1  O  LEU A 573   N  ASP A 548           
SHEET    5   D 6 VAL A 639  GLU A 644  1  O  LEU A 641   N  ILE A 572           
SHEET    6   D 6 LYS A 615  VAL A 619  1  N  LEU A 617   O  GLU A 642           
SHEET    1   E 2 MET B  85  ASP B  86  0                                        
SHEET    2   E 2 ILE B 262  PRO B 263 -1  O  ILE B 262   N  ASP B  86           
SHEET    1   F 6 ASN B 132  VAL B 134  0                                        
SHEET    2   F 6 THR B 109  GLY B 112  1  N  VAL B 110   O  VAL B 134           
SHEET    3   F 6 GLY B 157  VAL B 161  1  O  VAL B 158   N  PHE B 111           
SHEET    4   F 6 MET B 184  GLN B 190  1  O  PHE B 187   N  VAL B 159           
SHEET    5   F 6 PRO B 244  PRO B 250  1  O  LEU B 249   N  THR B 188           
SHEET    6   F 6 TRP B 216  MET B 219  1  N  VAL B 218   O  ASP B 248           
SHEET    1   G 6 SER B 348  MET B 351  0                                        
SHEET    2   G 6 VAL B 331  THR B 333  1  N  VAL B 331   O  LEU B 349           
SHEET    3   G 6 VAL B 303  VAL B 306  1  N  LEU B 304   O  THR B 332           
SHEET    4   G 6 ILE B 370  VAL B 373  1  O  VAL B 373   N  TYR B 305           
SHEET    5   G 6 ILE B 404  PHE B 406  1  O  PHE B 406   N  ALA B 372           
SHEET    6   G 6 ILE B 421  ALA B 422  1  O  ILE B 421   N  HIS B 405           
SHEET    1   H 6 PHE B 516  ILE B 517  0                                        
SHEET    2   H 6 VAL B 491  THR B 495  1  N  VAL B 493   O  ILE B 517           
SHEET    3   H 6 LEU B 543  GLY B 549  1  O  ILE B 545   N  ILE B 492           
SHEET    4   H 6 LYS B 571  ASN B 576  1  O  LEU B 573   N  ASP B 548           
SHEET    5   H 6 VAL B 639  GLU B 644  1  O  LEU B 641   N  ILE B 572           
SHEET    6   H 6 LYS B 615  VAL B 619  1  N  LEU B 617   O  GLU B 642           
SHEET    1   I 2 VAL B 583  GLN B 587  0                                        
SHEET    2   I 2 ARG B 594  HIS B 597 -1  O  HIS B 597   N  VAL B 583           
LINK         K     K A 696                 OD2 ASP A 350     1555   1555  3.63  
LINK         K     K A 696                 OE1 GLN A 343     1555   1555  2.90  
LINK         K     K A 696                 O   GLN A 506     1555   1555  2.70  
LINK         K     K A 696                 O   TRP A 508     1555   1555  2.50  
LINK         K     K A 696                 O   HOH A 772     1555   1555  2.68  
LINK         K     K A 696                 O   HOH A1029     1555   1555  2.76  
LINK         K     K A 696                 O   HOH A1033     1555   1555  2.85  
LINK        MG    MG A 699                 OD1 ASN A 577     1555   1555  2.32  
LINK        MG    MG A 699                 O   HOH A 796     1555   1555  2.09  
LINK        MG    MG A 699                 O1A TPP A 700     1555   1555  2.19  
LINK        MG    MG A 699                 OD2 ASP A 550     1555   1555  2.13  
LINK        MG    MG A 699                 O3B TPP A 700     1555   1555  2.11  
LINK        MG    MG A 699                 O   HOH A 795     1555   1555  1.99  
LINK         K     K B1696                 O   HOH B 802     1555   1555  2.42  
LINK         K     K B1696                 O   HOH B1028     1555   1555  2.49  
LINK         K     K B1696                 OD2 ASP B 350     1555   1555  3.72  
LINK         K     K B1696                 NE2 GLN B 343     1555   1555  3.62  
LINK         K     K B1696                 OE1 GLN B 343     1555   1555  2.87  
LINK         K     K B1696                 O   TRP B 508     1555   1555  2.57  
LINK         K     K B1696                 O   HOH B1034     1555   1555  2.39  
LINK         K     K B1696                 O   GLN B 506     1555   1555  2.72  
LINK        MG    MG B1699                 OD1 ASN B 577     1555   1555  2.08  
LINK        MG    MG B1699                 O1A TPP B1700     1555   1555  2.15  
LINK        MG    MG B1699                 O   HOH B 794     1555   1555  2.02  
LINK        MG    MG B1699                 O3B TPP B1700     1555   1555  2.01  
LINK        MG    MG B1699                 O   HOH B 748     1555   1555  2.10  
LINK        MG    MG B1699                 OD2 ASP B 550     1555   1555  2.29  
SITE     1 AC1  7 GLN A 343  ASP A 350  GLN A 506  TRP A 508                    
SITE     2 AC1  7 HOH A 772  HOH A1029  HOH A1033                               
SITE     1 AC2  5 ASP A 550  ASN A 577  TPP A 700  HOH A 795                    
SITE     2 AC2  5 HOH A 796                                                     
SITE     1 AC3  6 GLN B 343  GLN B 506  TRP B 508  HOH B 802                    
SITE     2 AC3  6 HOH B1028  HOH B1034                                          
SITE     1 AC4  5 ASP B 550  ASN B 577  HOH B 748  HOH B 794                    
SITE     2 AC4  5 TPP B1700                                                     
SITE     1 AC5  5 GLY A 115  GLY A 116  GLN A 202  HOH A 823                    
SITE     2 AC5  5 TPP B1700                                                     
SITE     1 AC6  4 HIS A 126  HIS B 597  THR B 598  HIS B 599                    
SITE     1 AC7  4 TPP A 700  GLY B 116  GLN B 202  HOH B 791                    
SITE     1 AC8 24 VAL A 497  GLY A 498  GLN A 499  HIS A 500                    
SITE     2 AC8 24 GLY A 523  MET A 525  GLY A 549  ASP A 550                    
SITE     3 AC8 24 ALA A 551  SER A 552  MET A 555  ASN A 577                    
SITE     4 AC8 24  MG A 699  HOH A 795  HOH A 796  HOH A 825                    
SITE     5 AC8 24 HOH A1011  TYR B 113  PRO B 114  GLU B 139                    
SITE     6 AC8 24 PRO B 165  ASN B 169  GLN B 202  2HP B1698                    
SITE     1 AC9 32 ARG A 241  GLY A 307  ALA A 308  GLY A 309                    
SITE     2 AC9 32 ASN A 312  THR A 334  LEU A 335  GLN A 336                    
SITE     3 AC9 32 LEU A 352  GLY A 353  MET A 354  HIS A 355                    
SITE     4 AC9 32 GLY A 356  GLY A 374  ALA A 375  ARG A 376                    
SITE     5 AC9 32 ASP A 378  ARG A 380  VAL A 381  GLU A 407                    
SITE     6 AC9 32 VAL A 408  ASN A 412  GLY A 425  ASP A 426                    
SITE     7 AC9 32 ALA A 427  HOH A 797  HOH A 798  HOH A 908                    
SITE     8 AC9 32 HOH A 963  HOH A1000  HOH A1003  PHE B 201                    
SITE     1 BC1 23 TYR A 113  PRO A 114  GLU A 139  PRO A 165                    
SITE     2 BC1 23 ASN A 169  GLN A 202  2HP A 698  VAL B 497                    
SITE     3 BC1 23 GLY B 498  GLN B 499  HIS B 500  GLY B 523                    
SITE     4 BC1 23 MET B 525  ASP B 550  ALA B 551  SER B 552                    
SITE     5 BC1 23 MET B 555  ASN B 577  HOH B 748  HOH B 794                    
SITE     6 BC1 23 HOH B 831  HOH B1027   MG B1699                               
SITE     1 BC2 34 PHE A 201  ARG B 241  GLY B 307  ALA B 308                    
SITE     2 BC2 34 GLY B 309  ASN B 312  THR B 334  LEU B 335                    
SITE     3 BC2 34 MET B 351  LEU B 352  GLY B 353  MET B 354                    
SITE     4 BC2 34 HIS B 355  GLY B 356  GLY B 374  ALA B 375                    
SITE     5 BC2 34 ARG B 376  ASP B 378  ARG B 380  VAL B 381                    
SITE     6 BC2 34 PHE B 406  GLU B 407  VAL B 408  ASN B 412                    
SITE     7 BC2 34 GLY B 425  ASP B 426  ALA B 427  MET B 502                    
SITE     8 BC2 34 GLY B 520  GLY B 521  HOH B 741  HOH B 777                    
SITE     9 BC2 34 HOH B 828  HOH B 863                                          
CRYST1   95.552  109.401  178.858  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      0.010466  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009141  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005591        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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