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Database: PDB
Entry: 1N0H
LinkDB: 1N0H
Original site: 1N0H 
HEADER    LYASE                                   14-OCT-02   1N0H              
TITLE     CRYSTAL STRUCTURE OF YEAST ACETOHYDROXYACID SYNTHASE IN COMPLEX WITH A
TITLE    2 SULFONYLUREA HERBICIDE, CHLORIMURON ETHYL                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACETOLACTATE SYNTHASE;                                     
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: MATURE CATALYTIC SUBUNIT;                                  
COMPND   5 SYNONYM: ACETOHYDROXY-ACID SYNTHASE, ALS, AHAS;                      
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, SULFONYLUREA, HERBICIDE INHIBITION,        
KEYWDS   2 THIAMINE DIPHOSPHATE, LYASE                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.S.PANG,L.W.GUDDAT,R.G.DUGGLEBY                                      
REVDAT   4   11-OCT-17 1N0H    1       REMARK                                   
REVDAT   3   24-FEB-09 1N0H    1       VERSN                                    
REVDAT   2   15-APR-03 1N0H    1       JRNL                                     
REVDAT   1   07-JAN-03 1N0H    0                                                
JRNL        AUTH   S.S.PANG,L.W.GUDDAT,R.G.DUGGLEBY                             
JRNL        TITL   MOLECULAR BASIS OF SULFONYLUREA HERBICIDE INHIBITION OF      
JRNL        TITL 2 ACETOHYDROXYACID SYNTHASE                                    
JRNL        REF    J.BIOL.CHEM.                  V. 278  7639 2003              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   14557277                                                     
JRNL        DOI    10.1074/JBC.M211648200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 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) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.70                          
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)   (%) : 95.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 50877                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.163                           
REMARK   3   FREE R VALUE                     : 0.205                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 5203                            
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) : 2.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.90                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 73.70                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2460                       
REMARK   3   BIN FREE R VALUE                    : 0.2780                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 386                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9106                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 230                                     
REMARK   3   SOLVENT ATOMS            : 832                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 31.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -3.17900                                             
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
REMARK   3    B12 (A**2) : -3.17900                                             
REMARK   3    B13 (A**2) : 6.35800                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.25                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.31                            
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) : 0.31                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.37                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.210                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.10                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.830                           
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 : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1N0H COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-OCT-02.                  
REMARK 100 THE DEPOSITION ID IS D_1000017365.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-JUL-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
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-D                            
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 : ADX                                
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 52457                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.700                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY                : 10.90                              
REMARK 200  R MERGE                    (I) : 0.09100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.91                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 81.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.26900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.700                              
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 1JSC                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 65.72                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.59                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: POTASSIUM PHOSPHATE, THIAMINE            
REMARK 280  DIPHOSPHATE, FAD, MAGNESIUM CHLORIDE, DTT, CHLORIMURON ETHYL,       
REMARK 280  TRIS-HCL, LITHIUM SULFATE, SODIUM POTASSIUM TARTRATE, PH 7.0,       
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 290K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 4 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -Y,X,Z                                                  
REMARK 290       4555   Y,-X,Z                                                  
REMARK 290       5555   -X,Y,-Z                                                 
REMARK 290       6555   X,-Y,-Z                                                 
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z                                                
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  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 300 REMARK: THE BIOLOGICAL UNIT IS A DIMER, WHICH IS THE SAME ASSEMBLY   
REMARK 300 FOUND IN THE ASYMMETRIC UNIT OF THE CRYSTAL STRUCTURE                
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: 14100 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 38750 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -99.0 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     MET A    11                                                      
REMARK 465     HIS A    12                                                      
REMARK 465     HIS A    13                                                      
REMARK 465     HIS A    14                                                      
REMARK 465     HIS A    15                                                      
REMARK 465     HIS A    16                                                      
REMARK 465     HIS A    17                                                      
REMARK 465     SER A    18                                                      
REMARK 465     SER A    19                                                      
REMARK 465     GLY A    20                                                      
REMARK 465     LEU A    21                                                      
REMARK 465     VAL A    22                                                      
REMARK 465     PRO A    23                                                      
REMARK 465     ARG A    24                                                      
REMARK 465     GLY A    25                                                      
REMARK 465     SER A    26                                                      
REMARK 465     GLY A    27                                                      
REMARK 465     MET A    28                                                      
REMARK 465     LYS A    29                                                      
REMARK 465     GLU A    30                                                      
REMARK 465     THR A    31                                                      
REMARK 465     ALA A    32                                                      
REMARK 465     ALA A    33                                                      
REMARK 465     ALA A    34                                                      
REMARK 465     LYS A    35                                                      
REMARK 465     PHE A    36                                                      
REMARK 465     GLU A    37                                                      
REMARK 465     ARG A    38                                                      
REMARK 465     GLN A    39                                                      
REMARK 465     HIS A    40                                                      
REMARK 465     MET A    41                                                      
REMARK 465     ASP A    42                                                      
REMARK 465     SER A    43                                                      
REMARK 465     PRO A    44                                                      
REMARK 465     ASP A    45                                                      
REMARK 465     LEU A    46                                                      
REMARK 465     GLY A    47                                                      
REMARK 465     THR A    48                                                      
REMARK 465     ASP A    49                                                      
REMARK 465     ASP A    50                                                      
REMARK 465     ASP A    51                                                      
REMARK 465     ASP A    52                                                      
REMARK 465     LYS A    53                                                      
REMARK 465     ALA A    54                                                      
REMARK 465     MET A    55                                                      
REMARK 465     GLY A    56                                                      
REMARK 465     SER A    57                                                      
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     MET B    11                                                      
REMARK 465     HIS B    12                                                      
REMARK 465     HIS B    13                                                      
REMARK 465     HIS B    14                                                      
REMARK 465     HIS B    15                                                      
REMARK 465     HIS B    16                                                      
REMARK 465     HIS B    17                                                      
REMARK 465     SER B    18                                                      
REMARK 465     SER B    19                                                      
REMARK 465     GLY B    20                                                      
REMARK 465     LEU B    21                                                      
REMARK 465     VAL B    22                                                      
REMARK 465     PRO B    23                                                      
REMARK 465     ARG B    24                                                      
REMARK 465     GLY B    25                                                      
REMARK 465     SER B    26                                                      
REMARK 465     GLY B    27                                                      
REMARK 465     MET B    28                                                      
REMARK 465     LYS B    29                                                      
REMARK 465     GLU B    30                                                      
REMARK 465     THR B    31                                                      
REMARK 465     ALA B    32                                                      
REMARK 465     ALA B    33                                                      
REMARK 465     ALA B    34                                                      
REMARK 465     LYS B    35                                                      
REMARK 465     PHE B    36                                                      
REMARK 465     GLU B    37                                                      
REMARK 465     ARG B    38                                                      
REMARK 465     GLN B    39                                                      
REMARK 465     HIS B    40                                                      
REMARK 465     MET B    41                                                      
REMARK 465     ASP B    42                                                      
REMARK 465     SER B    43                                                      
REMARK 465     PRO B    44                                                      
REMARK 465     ASP B    45                                                      
REMARK 465     LEU B    46                                                      
REMARK 465     GLY B    47                                                      
REMARK 465     THR B    48                                                      
REMARK 465     ASP B    49                                                      
REMARK 465     ASP B    50                                                      
REMARK 465     ASP B    51                                                      
REMARK 465     ASP B    52                                                      
REMARK 465     LYS B    53                                                      
REMARK 465     ALA B    54                                                      
REMARK 465     MET B    55                                                      
REMARK 465     GLY B    56                                                      
REMARK 465     SER B    57                                                      
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     GLU B    82                                                      
REMARK 465     ASN B   271                                                      
REMARK 465     ALA B   272                                                      
REMARK 465     LEU B   273                                                      
REMARK 465     ASN B   274                                                      
REMARK 465     GLN B   275                                                      
REMARK 465     LEU B   276                                                      
REMARK 465     THR B   277                                                      
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     THR A 277    OG1  CG2                                            
REMARK 470     LYS A 453    CG   CD   CE   NZ                                   
REMARK 470     LYS A 456    CG   CD   CE   NZ                                   
REMARK 470     SER B 278    OG                                                  
REMARK 470     ARG B 279    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 456    CG   CD   CE   NZ                                   
REMARK 470     LYS B 636    CG   CD   CE   NZ                                   
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    MET A 582   CA    MET A 582   CB      0.140                       
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    ASN A 127       16.37     55.80                                   
REMARK 500    THR A 266       -6.35    -52.88                                   
REMARK 500    PRO A 269      170.38    -47.26                                   
REMARK 500    ASP A 350     -168.51     76.93                                   
REMARK 500    ALA A 389       59.40     35.48                                   
REMARK 500    ARG A 444       58.90   -140.17                                   
REMARK 500    TYR A 460       68.74    -68.45                                   
REMARK 500    ARG A 511      -31.57   -141.60                                   
REMARK 500    PRO A 569       49.65    -69.06                                   
REMARK 500    GLU A 663       61.79   -112.70                                   
REMARK 500    ASN B 127       18.14     54.79                                   
REMARK 500    PRO B 269       99.35    -50.72                                   
REMARK 500    ARG B 279     -163.12     54.15                                   
REMARK 500    ASP B 350     -147.89     86.67                                   
REMARK 500    SER B 445      -35.68    -35.49                                   
REMARK 500    TYR B 458       72.74   -113.75                                   
REMARK 500    ARG B 511      -30.43   -141.64                                   
REMARK 500    GLU B 592       50.15     36.42                                   
REMARK 500    GLU B 663       45.75    -99.61                                   
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 HOH A 753   O                                                      
REMARK 620 2 GLN A 343   NE2  51.4                                              
REMARK 620 3 GLN A 343   OE1  78.7  38.0                                        
REMARK 620 4 GLN A 506   O    91.1 139.4 163.8                                  
REMARK 620 5 TRP A 508   O   101.4 107.0  76.0  93.9                            
REMARK 620 6 HOH A1382   O   172.5 121.4  96.1  95.1  82.5                      
REMARK 620 7 ASP A 350   OD2  75.2  55.6  84.5 105.2 160.6  99.0                
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 ASP A 550   OD1                                                    
REMARK 620 2 ASN A 577   OD1  86.4                                              
REMARK 620 3 HOH A 771   O    76.2  88.6                                        
REMARK 620 4 AYD A 700   O3B 159.5  97.7  83.8                                  
REMARK 620 5 AYD A 700   O1A  89.4 175.7  90.8  86.5                            
REMARK 620 6 GLU A 579   O   104.8  86.4 174.8  95.5  94.3                      
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 ASP B 350   OD2                                                    
REMARK 620 2 GLN B 506   O    98.6                                              
REMARK 620 3 HOH B1017   O    67.9  93.5                                        
REMARK 620 4 GLN B 343   NE2  63.0 143.4  51.0                                  
REMARK 620 5 TRP B 508   O   170.4  90.9 113.3 109.7                            
REMARK 620 6 GLN B 343   OE1  95.5 163.0  83.1  39.9  75.4                      
REMARK 620 N                    1     2     3     4     5                       
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 HOH B1032   O                                                      
REMARK 620 2 ASP B 550   OD1  78.6                                              
REMARK 620 3 TPP B1702   O3B  79.6 158.1                                        
REMARK 620 4 GLU B 579   O   172.1 108.6  93.0                                  
REMARK 620 5 TPP B1702   O3A  59.9 118.5  50.0 117.3                            
REMARK 620 6 TPP B1702   O1A  97.6  99.1  86.0  84.7  50.5                      
REMARK 620 7 ASN B 577   OD1  88.6  83.4  93.9  89.0 133.2 173.7                
REMARK 620 N                    1     2     3     4     5     6                 
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                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 699                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 1696                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1699                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIE A 695                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DTT A 698                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AYD A 700                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIE B 1695                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DTT B 1698                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TPP B 1702                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B 1701                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1JSC   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN IN THE ABSENCE OF THE HERBICIDAL INHIBITOR          
DBREF  1N0H A   58   687  UNP    P07342   ILVB_YEAST      58    687             
DBREF  1N0H B   58   687  UNP    P07342   ILVB_YEAST      58    687             
SEQRES   1 A  677  MET HIS HIS HIS HIS HIS HIS SER SER GLY LEU VAL PRO          
SEQRES   2 A  677  ARG GLY SER GLY MET LYS GLU THR ALA ALA ALA LYS PHE          
SEQRES   3 A  677  GLU ARG GLN HIS MET ASP SER PRO ASP LEU GLY THR ASP          
SEQRES   4 A  677  ASP ASP ASP LYS ALA MET GLY SER ALA PRO SER PHE ASN          
SEQRES   5 A  677  VAL ASP PRO LEU GLU GLN PRO ALA GLU PRO SER LYS LEU          
SEQRES   6 A  677  ALA LYS LYS LEU ARG ALA GLU PRO ASP MET ASP THR SER          
SEQRES   7 A  677  PHE VAL GLY LEU THR GLY GLY GLN ILE PHE ASN GLU MET          
SEQRES   8 A  677  MET SER ARG GLN ASN VAL ASP THR VAL PHE GLY TYR PRO          
SEQRES   9 A  677  GLY GLY ALA ILE LEU PRO VAL TYR ASP ALA ILE HIS ASN          
SEQRES  10 A  677  SER ASP LYS PHE ASN PHE VAL LEU PRO LYS HIS GLU GLN          
SEQRES  11 A  677  GLY ALA GLY HIS MET ALA GLU GLY TYR ALA ARG ALA SER          
SEQRES  12 A  677  GLY LYS PRO GLY VAL VAL LEU VAL THR SER GLY PRO GLY          
SEQRES  13 A  677  ALA THR ASN VAL VAL THR PRO MET ALA ASP ALA PHE ALA          
SEQRES  14 A  677  ASP GLY ILE PRO MET VAL VAL PHE THR GLY GLN VAL PRO          
SEQRES  15 A  677  THR SER ALA ILE GLY THR ASP ALA PHE GLN GLU ALA ASP          
SEQRES  16 A  677  VAL VAL GLY ILE SER ARG SER CYS THR LYS TRP ASN VAL          
SEQRES  17 A  677  MET VAL LYS SER VAL GLU GLU LEU PRO LEU ARG ILE ASN          
SEQRES  18 A  677  GLU ALA PHE GLU ILE ALA THR SER GLY ARG PRO GLY PRO          
SEQRES  19 A  677  VAL LEU VAL ASP LEU PRO LYS ASP VAL THR ALA ALA ILE          
SEQRES  20 A  677  LEU ARG ASN PRO ILE PRO THR LYS THR THR LEU PRO SER          
SEQRES  21 A  677  ASN ALA LEU ASN GLN LEU THR SER ARG ALA GLN ASP GLU          
SEQRES  22 A  677  PHE VAL MET GLN SER ILE ASN LYS ALA ALA ASP LEU ILE          
SEQRES  23 A  677  ASN LEU ALA LYS LYS PRO VAL LEU TYR VAL GLY ALA GLY          
SEQRES  24 A  677  ILE LEU ASN HIS ALA ASP GLY PRO ARG LEU LEU LYS GLU          
SEQRES  25 A  677  LEU SER ASP ARG ALA GLN ILE PRO VAL THR THR THR LEU          
SEQRES  26 A  677  GLN GLY LEU GLY SER PHE ASP GLN GLU ASP PRO LYS SER          
SEQRES  27 A  677  LEU ASP MET LEU GLY MET HIS GLY CYS ALA THR ALA ASN          
SEQRES  28 A  677  LEU ALA VAL GLN ASN ALA ASP LEU ILE ILE ALA VAL GLY          
SEQRES  29 A  677  ALA ARG PHE ASP ASP ARG VAL THR GLY ASN ILE SER LYS          
SEQRES  30 A  677  PHE ALA PRO GLU ALA ARG ARG ALA ALA ALA GLU GLY ARG          
SEQRES  31 A  677  GLY GLY ILE ILE HIS PHE GLU VAL SER PRO LYS ASN ILE          
SEQRES  32 A  677  ASN LYS VAL VAL GLN THR GLN ILE ALA VAL GLU GLY ASP          
SEQRES  33 A  677  ALA THR THR ASN LEU GLY LYS MET MET SER LYS ILE PHE          
SEQRES  34 A  677  PRO VAL LYS GLU ARG SER GLU TRP PHE ALA GLN ILE ASN          
SEQRES  35 A  677  LYS TRP LYS LYS GLU TYR PRO TYR ALA TYR MET GLU GLU          
SEQRES  36 A  677  THR PRO GLY SER LYS ILE LYS PRO GLN THR VAL ILE LYS          
SEQRES  37 A  677  LYS LEU SER LYS VAL ALA ASN ASP THR GLY ARG HIS VAL          
SEQRES  38 A  677  ILE VAL THR THR GLY VAL GLY GLN HIS GLN MET TRP ALA          
SEQRES  39 A  677  ALA GLN HIS TRP THR TRP ARG ASN PRO HIS THR PHE ILE          
SEQRES  40 A  677  THR SER GLY GLY LEU GLY THR MET GLY TYR GLY LEU PRO          
SEQRES  41 A  677  ALA ALA ILE GLY ALA GLN VAL ALA LYS PRO GLU SER LEU          
SEQRES  42 A  677  VAL ILE ASP ILE ASP GLY ASP ALA SER PHE ASN MET THR          
SEQRES  43 A  677  LEU THR GLU LEU SER SER ALA VAL GLN ALA GLY THR PRO          
SEQRES  44 A  677  VAL LYS ILE LEU ILE LEU ASN ASN GLU GLU GLN GLY MET          
SEQRES  45 A  677  VAL THR GLN TRP GLN SER LEU PHE TYR GLU HIS ARG TYR          
SEQRES  46 A  677  SER HIS THR HIS GLN LEU ASN PRO ASP PHE ILE LYS LEU          
SEQRES  47 A  677  ALA GLU ALA MET GLY LEU LYS GLY LEU ARG VAL LYS LYS          
SEQRES  48 A  677  GLN GLU GLU LEU ASP ALA LYS LEU LYS GLU PHE VAL SER          
SEQRES  49 A  677  THR LYS GLY PRO VAL LEU LEU GLU VAL GLU VAL ASP LYS          
SEQRES  50 A  677  LYS VAL PRO VAL LEU PRO MET VAL ALA GLY GLY SER GLY          
SEQRES  51 A  677  LEU ASP GLU PHE ILE ASN PHE ASP PRO GLU VAL GLU ARG          
SEQRES  52 A  677  GLN GLN THR GLU LEU ARG HIS LYS ARG THR GLY GLY LYS          
SEQRES  53 A  677  HIS                                                          
SEQRES   1 B  677  MET HIS HIS HIS HIS HIS HIS SER SER GLY LEU VAL PRO          
SEQRES   2 B  677  ARG GLY SER GLY MET LYS GLU THR ALA ALA ALA LYS PHE          
SEQRES   3 B  677  GLU ARG GLN HIS MET ASP SER PRO ASP LEU GLY THR ASP          
SEQRES   4 B  677  ASP ASP ASP LYS ALA MET GLY SER ALA PRO SER PHE ASN          
SEQRES   5 B  677  VAL ASP PRO LEU GLU GLN PRO ALA GLU PRO SER LYS LEU          
SEQRES   6 B  677  ALA LYS LYS LEU ARG ALA GLU PRO ASP MET ASP THR SER          
SEQRES   7 B  677  PHE VAL GLY LEU THR GLY GLY GLN ILE PHE ASN GLU MET          
SEQRES   8 B  677  MET SER ARG GLN ASN VAL ASP THR VAL PHE GLY TYR PRO          
SEQRES   9 B  677  GLY GLY ALA ILE LEU PRO VAL TYR ASP ALA ILE HIS ASN          
SEQRES  10 B  677  SER ASP LYS PHE ASN PHE VAL LEU PRO LYS HIS GLU GLN          
SEQRES  11 B  677  GLY ALA GLY HIS MET ALA GLU GLY TYR ALA ARG ALA SER          
SEQRES  12 B  677  GLY LYS PRO GLY VAL VAL LEU VAL THR SER GLY PRO GLY          
SEQRES  13 B  677  ALA THR ASN VAL VAL THR PRO MET ALA ASP ALA PHE ALA          
SEQRES  14 B  677  ASP GLY ILE PRO MET VAL VAL PHE THR GLY GLN VAL PRO          
SEQRES  15 B  677  THR SER ALA ILE GLY THR ASP ALA PHE GLN GLU ALA ASP          
SEQRES  16 B  677  VAL VAL GLY ILE SER ARG SER CYS THR LYS TRP ASN VAL          
SEQRES  17 B  677  MET VAL LYS SER VAL GLU GLU LEU PRO LEU ARG ILE ASN          
SEQRES  18 B  677  GLU ALA PHE GLU ILE ALA THR SER GLY ARG PRO GLY PRO          
SEQRES  19 B  677  VAL LEU VAL ASP LEU PRO LYS ASP VAL THR ALA ALA ILE          
SEQRES  20 B  677  LEU ARG ASN PRO ILE PRO THR LYS THR THR LEU PRO SER          
SEQRES  21 B  677  ASN ALA LEU ASN GLN LEU THR SER ARG ALA GLN ASP GLU          
SEQRES  22 B  677  PHE VAL MET GLN SER ILE ASN LYS ALA ALA ASP LEU ILE          
SEQRES  23 B  677  ASN LEU ALA LYS LYS PRO VAL LEU TYR VAL GLY ALA GLY          
SEQRES  24 B  677  ILE LEU ASN HIS ALA ASP GLY PRO ARG LEU LEU LYS GLU          
SEQRES  25 B  677  LEU SER ASP ARG ALA GLN ILE PRO VAL THR THR THR LEU          
SEQRES  26 B  677  GLN GLY LEU GLY SER PHE ASP GLN GLU ASP PRO LYS SER          
SEQRES  27 B  677  LEU ASP MET LEU GLY MET HIS GLY CYS ALA THR ALA ASN          
SEQRES  28 B  677  LEU ALA VAL GLN ASN ALA ASP LEU ILE ILE ALA VAL GLY          
SEQRES  29 B  677  ALA ARG PHE ASP ASP ARG VAL THR GLY ASN ILE SER LYS          
SEQRES  30 B  677  PHE ALA PRO GLU ALA ARG ARG ALA ALA ALA GLU GLY ARG          
SEQRES  31 B  677  GLY GLY ILE ILE HIS PHE GLU VAL SER PRO LYS ASN ILE          
SEQRES  32 B  677  ASN LYS VAL VAL GLN THR GLN ILE ALA VAL GLU GLY ASP          
SEQRES  33 B  677  ALA THR THR ASN LEU GLY LYS MET MET SER LYS ILE PHE          
SEQRES  34 B  677  PRO VAL LYS GLU ARG SER GLU TRP PHE ALA GLN ILE ASN          
SEQRES  35 B  677  LYS TRP LYS LYS GLU TYR PRO TYR ALA TYR MET GLU GLU          
SEQRES  36 B  677  THR PRO GLY SER LYS ILE LYS PRO GLN THR VAL ILE LYS          
SEQRES  37 B  677  LYS LEU SER LYS VAL ALA ASN ASP THR GLY ARG HIS VAL          
SEQRES  38 B  677  ILE VAL THR THR GLY VAL GLY GLN HIS GLN MET TRP ALA          
SEQRES  39 B  677  ALA GLN HIS TRP THR TRP ARG ASN PRO HIS THR PHE ILE          
SEQRES  40 B  677  THR SER GLY GLY LEU GLY THR MET GLY TYR GLY LEU PRO          
SEQRES  41 B  677  ALA ALA ILE GLY ALA GLN VAL ALA LYS PRO GLU SER LEU          
SEQRES  42 B  677  VAL ILE ASP ILE ASP GLY ASP ALA SER PHE ASN MET THR          
SEQRES  43 B  677  LEU THR GLU LEU SER SER ALA VAL GLN ALA GLY THR PRO          
SEQRES  44 B  677  VAL LYS ILE LEU ILE LEU ASN ASN GLU GLU GLN GLY MET          
SEQRES  45 B  677  VAL THR GLN TRP GLN SER LEU PHE TYR GLU HIS ARG TYR          
SEQRES  46 B  677  SER HIS THR HIS GLN LEU ASN PRO ASP PHE ILE LYS LEU          
SEQRES  47 B  677  ALA GLU ALA MET GLY LEU LYS GLY LEU ARG VAL LYS LYS          
SEQRES  48 B  677  GLN GLU GLU LEU ASP ALA LYS LEU LYS GLU PHE VAL SER          
SEQRES  49 B  677  THR LYS GLY PRO VAL LEU LEU GLU VAL GLU VAL ASP LYS          
SEQRES  50 B  677  LYS VAL PRO VAL LEU PRO MET VAL ALA GLY GLY SER GLY          
SEQRES  51 B  677  LEU ASP GLU PHE ILE ASN PHE ASP PRO GLU VAL GLU ARG          
SEQRES  52 B  677  GLN GLN THR GLU LEU ARG HIS LYS ARG THR GLY GLY LYS          
SEQRES  53 B  677  HIS                                                          
HET      K  A 696       1                                                       
HET     MG  A 699       1                                                       
HET    CIE  A 695      27                                                       
HET    DTT  A 698       8                                                       
HET    AYD  A 700      24                                                       
HET    FAD  A 701      53                                                       
HET      K  B1696       1                                                       
HET     MG  B1699       1                                                       
HET    CIE  B1695      27                                                       
HET    DTT  B1698       8                                                       
HET    TPP  B1702      26                                                       
HET    FAD  B1701      53                                                       
HETNAM       K POTASSIUM ION                                                    
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     CIE 2-[[[[(4-CHLORO-6-METHOXY-2-PYRIMIDINYL)                         
HETNAM   2 CIE  AMINO]CARBONYL]AMINO]SULFONYL]BENZOIC ACID ETHYL ESTER          
HETNAM     DTT 2,3-DIHYDROXY-1,4-DITHIOBUTANE                                   
HETNAM     AYD 4-{[(4'-AMINO-2'-METHYLPYRIMIDIN-5'-YL)                          
HETNAM   2 AYD  METHYL]AMINO}PENT-3-ENYL DIPHOSPHATE                            
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     TPP THIAMINE DIPHOSPHATE                                             
HETSYN     CIE CHLORIMURON ETHYL                                                
HETSYN     DTT 1,4-DITHIOTHREITOL                                               
FORMUL   3    K    2(K 1+)                                                      
FORMUL   4   MG    2(MG 2+)                                                     
FORMUL   5  CIE    2(C15 H15 CL N4 O6 S)                                        
FORMUL   6  DTT    2(C4 H10 O2 S2)                                              
FORMUL   7  AYD    C11 H20 N4 O7 P2                                             
FORMUL   8  FAD    2(C27 H33 N9 O15 P2)                                         
FORMUL  13  TPP    C12 H19 N4 O7 P2 S 1+                                        
FORMUL  15  HOH   *832(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  ILE A  125  1                                   8    
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  ASP A  180  1                                  11    
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 ARG A  211  THR A  214  5                                   4    
HELIX   10  10 SER A  222  GLU A  224  5                                   3    
HELIX   11  11 GLU A  225  SER A  239  1                                  15    
HELIX   12  12 LYS A  251  ALA A  256  1                                   6    
HELIX   13  14 SER A  278  ASN A  297  1                                  20    
HELIX   14  15 ALA A  308  HIS A  313  5                                   6    
HELIX   15  16 ASP A  315  GLN A  328  1                                  14    
HELIX   16  17 LEU A  335  LEU A  338  5                                   4    
HELIX   17  18 CYS A  357  ALA A  367  1                                  11    
HELIX   18  19 ASN A  384  PHE A  388  5                                   5    
HELIX   19  20 ALA A  389  GLU A  398  1                                  10    
HELIX   20  21 SER A  409  ILE A  413  5                                   5    
HELIX   21  22 ASP A  426  MET A  435  1                                  10    
HELIX   22  23 SER A  436  ILE A  438  5                                   3    
HELIX   23  24 ARG A  444  TYR A  458  1                                  15    
HELIX   24  25 LYS A  472  ASP A  486  1                                  15    
HELIX   25  26 GLY A  498  TRP A  508  1                                  11    
HELIX   26  27 TYR A  527  LYS A  539  1                                  13    
HELIX   27  28 ASP A  550  LEU A  557  1                                   8    
HELIX   28  29 GLU A  559  GLY A  567  1                                   9    
HELIX   29  30 GLN A  580  TYR A  591  1                                  12    
HELIX   30  31 ASP A  604  GLY A  613  1                                  10    
HELIX   31  32 LYS A  621  GLU A  623  5                                   3    
HELIX   32  33 GLU A  624  THR A  635  1                                  12    
HELIX   33  34 ASP A  668  THR A  683  1                                  16    
HELIX   34  35 THR B   93  GLN B  105  1                                  13    
HELIX   35  36 GLY B  115  ALA B  117  5                                   3    
HELIX   36  37 ILE B  118  ILE B  125  1                                   8    
HELIX   37  38 HIS B  138  GLY B  154  1                                  17    
HELIX   38  39 GLY B  164  ASN B  169  1                                   6    
HELIX   39  40 VAL B  170  ASP B  180  1                                  11    
HELIX   40  41 ASP B  205  SER B  210  1                                   6    
HELIX   41  42 ARG B  211  THR B  214  5                                   4    
HELIX   42  43 SER B  222  GLU B  224  5                                   3    
HELIX   43  44 GLU B  225  SER B  239  1                                  15    
HELIX   44  45 LYS B  251  ALA B  256  1                                   6    
HELIX   45  46 THR B  264  LEU B  268  1                                   5    
HELIX   46  47 GLN B  281  ALA B  299  1                                  19    
HELIX   47  48 ALA B  308  HIS B  313  5                                   6    
HELIX   48  49 ASP B  315  ALA B  327  1                                  13    
HELIX   49  50 LEU B  335  LEU B  338  5                                   4    
HELIX   50  51 CYS B  357  ALA B  367  1                                  11    
HELIX   51  52 ASP B  378  GLY B  383  1                                   6    
HELIX   52  53 ASN B  384  PHE B  388  5                                   5    
HELIX   53  54 ALA B  389  GLU B  398  1                                  10    
HELIX   54  55 SER B  409  ILE B  413  5                                   5    
HELIX   55  56 ASP B  426  SER B  436  1                                  11    
HELIX   56  57 ARG B  444  TYR B  458  1                                  15    
HELIX   57  58 LYS B  472  ASP B  486  1                                  15    
HELIX   58  59 GLY B  498  TRP B  508  1                                  11    
HELIX   59  60 TYR B  527  LYS B  539  1                                  13    
HELIX   60  61 ASP B  550  LEU B  557  1                                   8    
HELIX   61  62 GLU B  559  GLY B  567  1                                   9    
HELIX   62  63 GLN B  580  PHE B  590  1                                  11    
HELIX   63  64 ASP B  604  GLY B  613  1                                  10    
HELIX   64  65 LYS B  621  GLU B  623  5                                   3    
HELIX   65  66 GLU B  624  THR B  635  1                                  12    
HELIX   66  67 ASP B  668  THR B  683  1                                  16    
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  TYR A 113  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  VAL A 245   N  VAL A 186           
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  VAL A 306   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  PHE A 406   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  TYR B 113  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  VAL B 245   N  VAL B 186           
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 PRO B 302  VAL B 306  1  N  LEU B 304   O  THR B 332           
SHEET    4   G 6 LEU B 369  VAL B 373  1  O  ILE B 371   N  VAL B 303           
SHEET    5   G 6 GLY B 402  GLU B 407  1  O  PHE B 406   N  ALA B 372           
SHEET    6   G 6 ILE B 421  GLU B 424  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  VAL B 639   N  ILE B 572           
SHEET    6   H 6 LYS B 615  VAL B 619  1  N  LEU B 617   O  LEU B 640           
LINK         SG  CYS A 357                 S1  DTT A 698     1555   1555  2.04  
LINK         SG  CYS B 357                 S1  DTT B1698     1555   1555  2.04  
LINK         K     K A 696                 O   HOH A 753     1555   1555  2.74  
LINK         K     K A 696                 NE2 GLN A 343     1555   1555  3.66  
LINK         K     K A 696                 OE1 GLN A 343     1555   1555  2.80  
LINK         K     K A 696                 O   GLN A 506     1555   1555  2.66  
LINK         K     K A 696                 O   TRP A 508     1555   1555  2.61  
LINK         K     K A 696                 O   HOH A1382     1555   1555  3.06  
LINK         K     K A 696                 OD2 ASP A 350     1555   1555  2.94  
LINK        MG    MG A 699                 OD1 ASP A 550     1555   1555  2.12  
LINK        MG    MG A 699                 OD1 ASN A 577     1555   1555  2.07  
LINK        MG    MG A 699                 O   HOH A 771     1555   1555  2.19  
LINK        MG    MG A 699                 O3B AYD A 700     1555   1555  2.12  
LINK        MG    MG A 699                 O1A AYD A 700     1555   1555  2.20  
LINK        MG    MG A 699                 O   GLU A 579     1555   1555  2.17  
LINK         K     K B1696                 OD2 ASP B 350     1555   1555  3.04  
LINK         K     K B1696                 O   GLN B 506     1555   1555  2.72  
LINK         K     K B1696                 O   HOH B1017     1555   1555  2.85  
LINK         K     K B1696                 NE2 GLN B 343     1555   1555  3.49  
LINK         K     K B1696                 O   TRP B 508     1555   1555  2.66  
LINK         K     K B1696                 OE1 GLN B 343     1555   1555  2.82  
LINK        MG    MG B1699                 O   HOH B1032     1555   1555  2.34  
LINK        MG    MG B1699                 OD1 ASP B 550     1555   1555  2.17  
LINK        MG    MG B1699                 O3B TPP B1702     1555   1555  2.40  
LINK        MG    MG B1699                 O   GLU B 579     1555   1555  2.13  
LINK        MG    MG B1699                 O3A TPP B1702     1555   1555  3.09  
LINK        MG    MG B1699                 O1A TPP B1702     1555   1555  2.09  
LINK        MG    MG B1699                 OD1 ASN B 577     1555   1555  2.14  
CISPEP   1 LEU A  652    PRO A  653          0         0.91                     
CISPEP   2 LEU B  652    PRO B  653          0        -0.13                     
SITE     1 AC1  6 GLN A 343  ASP A 350  GLN A 506  TRP A 508                    
SITE     2 AC1  6 HOH A 753  HOH A1382                                          
SITE     1 AC2  5 ASP A 550  ASN A 577  GLU A 579  AYD A 700                    
SITE     2 AC2  5 HOH A 771                                                     
SITE     1 AC3  5 GLN B 343  ASP B 350  GLN B 506  TRP B 508                    
SITE     2 AC3  5 HOH B1017                                                     
SITE     1 AC4  5 ASP B 550  ASN B 577  GLU B 579  HOH B1032                    
SITE     2 AC4  5 TPP B1702                                                     
SITE     1 AC5 13 MET A 354  ASP A 379  ARG A 380  VAL A 583                    
SITE     2 AC5 13 TRP A 586  FAD A 701  GLY B 116  ALA B 117                    
SITE     3 AC5 13 VAL B 191  PRO B 192  PHE B 201  GLN B 202                    
SITE     4 AC5 13 LYS B 251                                                     
SITE     1 AC6  5 CYS A 357  THR A 359  LYS A 455  TYR A 458                    
SITE     2 AC6  5 TYR A 460                                                     
SITE     1 AC7 26 VAL A 497  GLY A 498  GLN A 499  HIS A 500                    
SITE     2 AC7 26 GLY A 523  MET A 525  GLY A 549  ASP A 550                    
SITE     3 AC7 26 ALA A 551  SER A 552  MET A 555  ASN A 577                    
SITE     4 AC7 26 GLU A 579  GLN A 580  GLY A 581  MET A 582                    
SITE     5 AC7 26 VAL A 583   MG A 699  HOH A 724  HOH A 771                    
SITE     6 AC7 26 HOH A1108  PRO B 114  GLU B 139  PRO B 165                    
SITE     7 AC7 26 ASN B 169  GLN B 202                                          
SITE     1 AC8 36 ASP A 180  ARG A 241  GLY A 307  ALA A 308                    
SITE     2 AC8 36 GLY A 309  ASN A 312  THR A 334  LEU A 335                    
SITE     3 AC8 36 LEU A 352  GLY A 353  MET A 354  HIS A 355                    
SITE     4 AC8 36 GLY A 374  ALA A 375  ARG A 376  ASP A 378                    
SITE     5 AC8 36 ARG A 380  VAL A 381  PHE A 406  GLU A 407                    
SITE     6 AC8 36 VAL A 408  ASN A 412  GLY A 425  ASP A 426                    
SITE     7 AC8 36 ALA A 427  GLN A 501  MET A 502  GLY A 520                    
SITE     8 AC8 36 GLY A 521  MET A 582  CIE A 695  HOH A 725                    
SITE     9 AC8 36 HOH A 726  HOH A 747  HOH A 892  PHE B 201                    
SITE     1 AC9 14 GLY A 116  ALA A 117  VAL A 191  PRO A 192                    
SITE     2 AC9 14 PHE A 201  GLN A 202  LYS A 251  MET B 354                    
SITE     3 AC9 14 ASP B 379  ARG B 380  MET B 582  TRP B 586                    
SITE     4 AC9 14 HOH B1520  FAD B1701                                          
SITE     1 BC1  7 ASP B 350  CYS B 357  THR B 359  LYS B 455                    
SITE     2 BC1  7 TYR B 458  PRO B 459  HOH B1018                               
SITE     1 BC2 25 TYR A 113  PRO A 114  GLU A 139  PRO A 165                    
SITE     2 BC2 25 ASN A 169  GLN A 202  VAL B 497  GLY B 498                    
SITE     3 BC2 25 GLN B 499  HIS B 500  GLY B 523  MET B 525                    
SITE     4 BC2 25 GLY B 549  ASP B 550  ALA B 551  SER B 552                    
SITE     5 BC2 25 MET B 555  ASN B 577  GLU B 579  GLN B 580                    
SITE     6 BC2 25 GLY B 581  MET B 582  VAL B 583  HOH B1032                    
SITE     7 BC2 25  MG B1699                                                     
SITE     1 BC3 36 PHE A 201  ASP B 180  ARG B 241  GLY B 307                    
SITE     2 BC3 36 ALA B 308  GLY B 309  ASN B 312  THR B 334                    
SITE     3 BC3 36 LEU B 335  LEU B 352  GLY B 353  MET B 354                    
SITE     4 BC3 36 HIS B 355  GLY B 374  ALA B 375  ARG B 376                    
SITE     5 BC3 36 ASP B 378  ARG B 380  VAL B 381  GLU B 407                    
SITE     6 BC3 36 VAL B 408  ASN B 412  GLY B 425  ASP B 426                    
SITE     7 BC3 36 ALA B 427  GLN B 501  MET B 502  GLY B 520                    
SITE     8 BC3 36 GLY B 521  MET B 582  HOH B 982  HOH B 991                    
SITE     9 BC3 36 HOH B1008  HOH B1013  HOH B1051  CIE B1695                    
CRYST1  153.976  153.976  178.298  90.00  90.00  90.00 P 4 2 2      16          
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      0.006495  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006495  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005609        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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