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Database: PDB
Entry: 1T9B
LinkDB: 1T9B
Original site: 1T9B 
HEADER    TRANSFERASE                             16-MAY-04   1T9B              
TITLE     CRYSTAL STRUCTURE OF YEAST ACETOHYDROXYACID SYNTHASE IN COMPLEX WITH A
TITLE    2 SULFONYLUREA HERBICIDE, CHLORSULFURON                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACETOLACTATE SYNTHASE, MITOCHONDRIAL;                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: CATALYTIC SUBUNIT;                                         
COMPND   5 SYNONYM: ACETOHYDROXY-ACID SYNTHASE, ALS, AHAS;                      
COMPND   6 EC: 2.2.1.6;                                                         
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, SMR1, YMR108W, YM9718.07;                                
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: PET30(C)                                  
KEYWDS    ACETOHYDROXYACID SYNTHASE, ACETOLACTATE SYNTHASE, HERBICIDE,          
KEYWDS   2 SULFONYLUREA, THIAMIN DIPHOSPHATE, FAD, INHIBITOR, CHLORSULFURON,    
KEYWDS   3 TRANSFERASE                                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.A.MCCOURT,S.S.PANG,L.W.GUDDAT,R.G.DUGGLEBY                          
REVDAT   4   11-OCT-17 1T9B    1       REMARK                                   
REVDAT   3   24-FEB-09 1T9B    1       VERSN                                    
REVDAT   2   01-MAR-05 1T9B    1       JRNL                                     
REVDAT   1   21-DEC-04 1T9B    0                                                
JRNL        AUTH   J.A.MCCOURT,S.S.PANG,L.W.GUDDAT,R.G.DUGGLEBY                 
JRNL        TITL   ELUCIDATING THE SPECIFICITY OF BINDING OF SULFONYLUREA       
JRNL        TITL 2 HERBICIDES TO ACETOHYDROXYACID SYNTHASE.                     
JRNL        REF    BIOCHEMISTRY                  V.  44  2330 2005              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   15709745                                                     
JRNL        DOI    10.1021/BI047980A                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 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) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
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)   (%) : 90.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 99442                          
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) : 0.162                           
REMARK   3   FREE R VALUE                     : 0.195                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 9986                            
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) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.28                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 53.00                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2180                       
REMARK   3   BIN FREE R VALUE                    : 0.2430                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 530                          
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            : 8929                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 205                                     
REMARK   3   SOLVENT ATOMS            : 1360                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 51.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.20                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.18                            
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) : 0.24                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.22                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : NULL                            
REMARK   3   BOND ANGLES            (DEGREES) : NULL                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : ISOTROPIC                                 
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 1T9B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-JUL-04.                  
REMARK 100 THE DEPOSITION ID IS D_1000022473.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-DEC-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-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.90                               
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   : 102885                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.190                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 99.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.9                               
REMARK 200  DATA REDUNDANCY                : 5.300                              
REMARK 200  R MERGE                    (I) : 0.05800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.19                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.28                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 53.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.21900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.110                              
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 1N0H                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 65.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.53                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: POTASSIUM PHOSPHATE, THIAMIN             
REMARK 280  DIPHOSPHATE, FAD, MAGNESIUM CHLORIDE, DTT, CHLORSULFURON, TRIS-     
REMARK 280  HCL, LITHIUM SULFATE, SODIUM POTASSIUM TARTRATE, PH 7.0, VAPOR      
REMARK 280  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 ASYMMETRIC UNIT CONTAINS THE MINIMUM BIOLOGICAL UNIT     
REMARK 300 REQUIRED FOR ACTIVITY, A DIMER.                                      
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: 13330 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 38260 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -81.0 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     PRO A    83                                                      
REMARK 465     ASP A    84                                                      
REMARK 465     THR A   264                                                      
REMARK 465     LYS A   265                                                      
REMARK 465     THR A   266                                                      
REMARK 465     THR A   267                                                      
REMARK 465     LEU A   268                                                      
REMARK 465     PRO A   269                                                      
REMARK 465     SER A   270                                                      
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     ALA A   280                                                      
REMARK 465     GLN A   281                                                      
REMARK 465     ASP A   282                                                      
REMARK 465     GLU A   283                                                      
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     PRO B    83                                                      
REMARK 465     ASP B    84                                                      
REMARK 465     SER B   270                                                      
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 221    CG   CD   CE   NZ                                   
REMARK 470     LYS A 300    CG   CD   CE   NZ                                   
REMARK 470     LYS A 411    CG   CD   CE   NZ                                   
REMARK 470     GLN A 418    CG   CD   OE1  NE2                                  
REMARK 470     PHE A 439    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS A 453    CG   CD   CE   NZ                                   
REMARK 470     LYS A 456    CG   CD   CE   NZ                                   
REMARK 470     GLU A 457    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 636    CG   CD   CE   NZ                                   
REMARK 470     LYS A 681    CG   CD   CE   NZ                                   
REMARK 470     LYS A 686    CG   CD   CE   NZ                                   
REMARK 470     LYS B 265    CG   CD   CE   NZ                                   
REMARK 470     LYS B 453    CG   CD   CE   NZ                                   
REMARK 470     LYS B 456    CG   CD   CE   NZ                                   
REMARK 470     LYS B 630    CG   CD   CE   NZ                                   
REMARK 470     GLU B 677    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   NH2  ARG B   511     NH2  ARG B   511     5556     2.19            
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    TRP A 216      149.66   -170.71                                   
REMARK 500    ASP A 350     -159.24     75.99                                   
REMARK 500    ASN A 384      106.25    -58.49                                   
REMARK 500    TYR A 460       75.73    -65.41                                   
REMARK 500    ARG A 511      -21.61   -143.98                                   
REMARK 500    GLU A 663       39.57    -98.63                                   
REMARK 500    ASP B 350     -164.67     72.26                                   
REMARK 500    ARG B 511      -25.39   -140.20                                   
REMARK 500    GLU B 592       50.70     39.03                                   
REMARK 500    GLU B 663       49.79   -106.80                                   
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 A1696   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN A 343   OE1                                                    
REMARK 620 2 HOH A4034   O    79.1                                              
REMARK 620 3 GLN A 506   O   158.9  88.8                                        
REMARK 620 4 ASP A 350   OD2  88.9  66.5 102.0                                  
REMARK 620 5 HOH A4147   O    61.0 126.2 138.7  77.7                            
REMARK 620 6 HOH A4492   O   131.1 144.0  67.2  91.7  71.5                      
REMARK 620 7 TRP A 508   O    74.5 105.5  92.5 163.0  97.3 102.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1699  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 579   O                                                      
REMARK 620 2 ASN A 577   OD1  84.4                                              
REMARK 620 3 ASP A 550   OD1 105.1  80.7                                        
REMARK 620 4 HOH A4051   O   166.9  86.5  82.7                                  
REMARK 620 5 P22 A1702   O3B  91.1  93.4 162.0  80.0                            
REMARK 620 6 P22 A1702   O1A  95.4 168.3  88.0  95.4  98.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K B 696   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B5202   O                                                      
REMARK 620 2 GLN B 506   O   128.0                                              
REMARK 620 3 HOH B4657   O    61.3  67.0                                        
REMARK 620 4 TRP B 508   O    87.9  92.5  97.4                                  
REMARK 620 5 GLN B 343   OE1  67.9 162.3 129.2  79.3                            
REMARK 620 6 HOH B4676   O    44.6 121.3  70.3 131.7  75.0                      
REMARK 620 7 HOH B4232   O   145.3  84.1 143.8 105.6  83.2 110.9                
REMARK 620 8 ASP B 350   OD2  90.6  99.2  93.9 166.2  87.5  46.1  68.7          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 699  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 P25 B 698   O3B                                                    
REMARK 620 2 HOH B4246   O    79.6                                              
REMARK 620 3 ASN B 577   OD1  93.1  86.1                                        
REMARK 620 4 GLU B 579   O    92.4 168.7  86.4                                  
REMARK 620 5 P25 B 698   O1A  91.8  92.7 174.6  95.6                            
REMARK 620 6 ASP B 550   OD1 160.5  81.4  81.3 105.8  93.3                      
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 B 696                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 699                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 1696                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1699                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1CS A 695                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P25 B 698                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NSP A 704                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1CS B 1695                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B 1701                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P22 A 1702                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE YF3 A 1705                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1N0H   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF YEAST ACETOHYDROXYACID SYNTHASE IN COMPLEX      
REMARK 900 WITH A SULFONYLUREA HERBICIDE, CHLORIMURON ETHYL                     
REMARK 900 RELATED ID: 1T9C   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF YEAST ACETOHYDROXYACID SYNTHASE IN COMPLEX      
REMARK 900 WITH A SULFONYLUREA HERBICIDE, SULFOMETURON METHYL                   
REMARK 900 RELATED ID: 1T9D   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF YEAST ACETOHYDROXYACID SYNTHASE IN COMPLEX      
REMARK 900 WITH A SULFONYLUREA HERBICIDE, METSULFURON METHYL                    
REMARK 900 RELATED ID: 1T9A   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF YEAST ACETOHYDROXYACID SYNTHASE IN COMPLEX      
REMARK 900 WITH A SULFONYLUREA HERBICIDE, TRIBENURON METHYL                     
DBREF  1T9B A   58   687  UNP    P07342   ILVB_YEAST      58    687             
DBREF  1T9B B   58   687  UNP    P07342   ILVB_YEAST      58    687             
SEQADV 1T9B MET A   11  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B HIS A   12  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B HIS A   13  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B HIS A   14  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B HIS A   15  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B HIS A   16  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B HIS A   17  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B SER A   18  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B SER A   19  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B GLY A   20  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B LEU A   21  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B VAL A   22  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B PRO A   23  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B ARG A   24  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B GLY A   25  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B SER A   26  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B GLY A   27  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B MET A   28  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B LYS A   29  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B GLU A   30  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B THR A   31  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B ALA A   32  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B ALA A   33  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B ALA A   34  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B LYS A   35  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B PHE A   36  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B GLU A   37  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B ARG A   38  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B GLN A   39  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B HIS A   40  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B MET A   41  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B ASP A   42  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B SER A   43  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B PRO A   44  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B ASP A   45  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B LEU A   46  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B GLY A   47  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B THR A   48  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B ASP A   49  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B ASP A   50  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B ASP A   51  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B ASP A   52  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B LYS A   53  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B ALA A   54  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B MET A   55  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B GLY A   56  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B SER A   57  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B MET B   11  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B HIS B   12  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B HIS B   13  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B HIS B   14  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B HIS B   15  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B HIS B   16  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B HIS B   17  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B SER B   18  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B SER B   19  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B GLY B   20  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B LEU B   21  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B VAL B   22  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B PRO B   23  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B ARG B   24  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B GLY B   25  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B SER B   26  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B GLY B   27  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B MET B   28  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B LYS B   29  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B GLU B   30  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B THR B   31  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B ALA B   32  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B ALA B   33  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B ALA B   34  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B LYS B   35  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B PHE B   36  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B GLU B   37  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B ARG B   38  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B GLN B   39  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B HIS B   40  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B MET B   41  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B ASP B   42  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B SER B   43  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B PRO B   44  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B ASP B   45  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B LEU B   46  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B GLY B   47  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B THR B   48  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B ASP B   49  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B ASP B   50  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B ASP B   51  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B ASP B   52  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B LYS B   53  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B ALA B   54  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B MET B   55  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B GLY B   56  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9B SER B   57  UNP  P07342              CLONING ARTIFACT               
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  A1696       1                                                       
HET     MG  A1699       1                                                       
HET    1CS  A 695      23                                                       
HET    FAD  A 701      53                                                       
HET    NSP  A 704      10                                                       
HET    P22  A1702      11                                                       
HET    YF3  A1705      14                                                       
HET      K  B 696       1                                                       
HET     MG  B 699       1                                                       
HET    P25  B 698      14                                                       
HET    1CS  B1695      23                                                       
HET    FAD  B1701      53                                                       
HETNAM       K POTASSIUM ION                                                    
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     1CS 1-(2-CHLOROPHENYLSULFONYL)-3-(4-METHOXY-6-METHYL-L,3,5-          
HETNAM   2 1CS  TRIAZIN-2-YL)UREA                                               
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     NSP 5-(AMINOMETHYL)-2-METHYLPYRIMIDIN-4-AMINE                        
HETNAM     P22 ETHYL DIHYDROGEN DIPHOSPHATE                                     
HETNAM     YF3 2-{[(4-AMINO-2-METHYLPYRIMIDIN-5-YL)                             
HETNAM   2 YF3  METHYL]AMINO}PROPANE-1-THIOL                                    
HETNAM     P25 PENTYL TRIHYDROGEN DIPHOSPHATE                                   
FORMUL   3    K    2(K 1+)                                                      
FORMUL   4   MG    2(MG 2+)                                                     
FORMUL   5  1CS    2(C12 H12 CL N5 O4 S)                                        
FORMUL   6  FAD    2(C27 H33 N9 O15 P2)                                         
FORMUL   7  NSP    C6 H10 N4                                                    
FORMUL   8  P22    C2 H8 O7 P2                                                  
FORMUL   9  YF3    C9 H16 N4 S                                                  
FORMUL  12  P25    C5 H14 O7 P2                                                 
FORMUL  15  HOH   *1360(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  GLY A  181  1                                  12    
HELIX    7   7 ASP A  205  SER A  210  1                                   6    
HELIX    8   8 ARG A  211  THR A  214  5                                   4    
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 PHE A  284  LEU A  298  1                                  15    
HELIX   13  13 ALA A  308  HIS A  313  5                                   6    
HELIX   14  14 ASP A  315  ALA A  327  1                                  13    
HELIX   15  15 LEU A  335  LEU A  338  5                                   4    
HELIX   16  16 CYS A  357  ALA A  367  1                                  11    
HELIX   17  17 ASN A  384  PHE A  388  5                                   5    
HELIX   18  18 ALA A  389  GLU A  398  1                                  10    
HELIX   19  19 SER A  409  ILE A  413  5                                   5    
HELIX   20  20 ASP A  426  SER A  436  1                                  11    
HELIX   21  21 ARG A  444  TYR A  458  1                                  15    
HELIX   22  22 LYS A  472  ASP A  486  1                                  15    
HELIX   23  23 GLY A  498  TRP A  508  1                                  11    
HELIX   24  24 TYR A  527  LYS A  539  1                                  13    
HELIX   25  25 ASP A  550  LEU A  557  1                                   8    
HELIX   26  26 GLU A  559  GLY A  567  1                                   9    
HELIX   27  27 GLN A  580  TYR A  591  1                                  12    
HELIX   28  28 ASP A  604  MET A  612  1                                   9    
HELIX   29  29 LYS A  621  GLU A  623  5                                   3    
HELIX   30  30 GLU A  624  THR A  635  1                                  12    
HELIX   31  31 ASP A  668  THR A  683  1                                  16    
HELIX   32  32 THR B   93  GLN B  105  1                                  13    
HELIX   33  33 ILE B  118  ILE B  125  1                                   8    
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 ASP B  205  SER B  210  1                                   6    
HELIX   38  38 ARG B  211  THR B  214  5                                   4    
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 PRO B  263  LEU B  268  5                                   6    
HELIX   43  43 SER B  278  ALA B  299  1                                  22    
HELIX   44  44 ALA B  308  HIS B  313  5                                   6    
HELIX   45  45 ASP B  315  GLN B  328  1                                  14    
HELIX   46  46 LEU B  335  LEU B  338  5                                   4    
HELIX   47  47 CYS B  357  ALA B  367  1                                  11    
HELIX   48  48 ASN B  384  PHE B  388  5                                   5    
HELIX   49  49 ALA B  389  GLU B  398  1                                  10    
HELIX   50  50 SER B  409  ILE B  413  5                                   5    
HELIX   51  51 ASP B  426  MET B  435  1                                  10    
HELIX   52  52 SER B  436  ILE B  438  5                                   3    
HELIX   53  53 ARG B  444  TYR B  458  1                                  15    
HELIX   54  54 LYS B  472  THR B  487  1                                  16    
HELIX   55  55 GLY B  498  TRP B  508  1                                  11    
HELIX   56  56 TYR B  527  LYS B  539  1                                  13    
HELIX   57  57 ASP B  550  LEU B  557  1                                   8    
HELIX   58  58 GLU B  559  GLY B  567  1                                   9    
HELIX   59  59 GLN B  580  TYR B  591  1                                  12    
HELIX   60  60 ASP B  604  MET B  612  1                                   9    
HELIX   61  61 LYS B  621  GLU B  623  5                                   3    
HELIX   62  62 GLU B  624  THR B  635  1                                  12    
HELIX   63  63 ASP B  668  THR B  683  1                                  16    
SHEET    1   A 6 ASN A 132  VAL A 134  0                                        
SHEET    2   A 6 THR A 109  GLY A 112  1  N  VAL A 110   O  VAL A 134           
SHEET    3   A 6 GLY A 157  VAL A 161  1  O  VAL A 158   N  PHE A 111           
SHEET    4   A 6 MET A 184  GLN A 190  1  O  PHE A 187   N  VAL A 159           
SHEET    5   A 6 PRO A 244  PRO A 250  1  O  LEU A 249   N  THR A 188           
SHEET    6   A 6 TRP A 216  MET A 219  1  N  VAL A 218   O  ASP A 248           
SHEET    1   B 6 SER A 348  MET A 351  0                                        
SHEET    2   B 6 VAL A 331  THR A 333  1  N  VAL A 331   O  LEU A 349           
SHEET    3   B 6 PRO A 302  VAL A 306  1  N  LEU A 304   O  THR A 332           
SHEET    4   B 6 LEU A 369  VAL A 373  1  O  ILE A 371   N  VAL A 303           
SHEET    5   B 6 GLY A 402  GLU A 407  1  O  PHE A 406   N  ALA A 372           
SHEET    6   B 6 ILE A 421  GLU A 424  1  O  ILE A 421   N  HIS A 405           
SHEET    1   C 6 PHE A 516  ILE A 517  0                                        
SHEET    2   C 6 VAL A 491  THR A 495  1  N  VAL A 493   O  ILE A 517           
SHEET    3   C 6 LEU A 543  GLY A 549  1  O  ILE A 545   N  ILE A 492           
SHEET    4   C 6 LYS A 571  ASN A 576  1  O  LEU A 573   N  ASP A 548           
SHEET    5   C 6 VAL A 639  GLU A 644  1  O  LEU A 641   N  ILE A 572           
SHEET    6   C 6 LYS A 615  VAL A 619  1  N  LEU A 617   O  LEU A 640           
SHEET    1   D 6 ASN B 132  VAL B 134  0                                        
SHEET    2   D 6 THR B 109  GLY B 112  1  N  VAL B 110   O  VAL B 134           
SHEET    3   D 6 GLY B 157  VAL B 161  1  O  VAL B 158   N  PHE B 111           
SHEET    4   D 6 MET B 184  GLN B 190  1  O  PHE B 187   N  VAL B 159           
SHEET    5   D 6 PRO B 244  PRO B 250  1  O  LEU B 249   N  THR B 188           
SHEET    6   D 6 TRP B 216  MET B 219  1  N  VAL B 218   O  ASP B 248           
SHEET    1   E 6 SER B 348  MET B 351  0                                        
SHEET    2   E 6 VAL B 331  THR B 333  1  N  VAL B 331   O  LEU B 349           
SHEET    3   E 6 PRO B 302  VAL B 306  1  N  VAL B 306   O  THR B 332           
SHEET    4   E 6 LEU B 369  VAL B 373  1  O  VAL B 373   N  TYR B 305           
SHEET    5   E 6 GLY B 402  GLU B 407  1  O  PHE B 406   N  ALA B 372           
SHEET    6   E 6 ILE B 421  GLU B 424  1  O  VAL B 423   N  HIS B 405           
SHEET    1   F 6 PHE B 516  ILE B 517  0                                        
SHEET    2   F 6 VAL B 491  THR B 495  1  N  VAL B 493   O  ILE B 517           
SHEET    3   F 6 LEU B 543  GLY B 549  1  O  ILE B 545   N  ILE B 492           
SHEET    4   F 6 LYS B 571  ASN B 576  1  O  LEU B 573   N  ASP B 548           
SHEET    5   F 6 VAL B 639  GLU B 644  1  O  LEU B 641   N  ILE B 572           
SHEET    6   F 6 LYS B 615  VAL B 619  1  N  LEU B 617   O  GLU B 642           
LINK         K     K A1696                 OE1 GLN A 343     1555   1555  2.79  
LINK         K     K A1696                 O   HOH A4034     1555   1555  2.69  
LINK         K     K A1696                 O   GLN A 506     1555   1555  2.58  
LINK         K     K A1696                 OD2 ASP A 350     1555   1555  2.89  
LINK         K     K A1696                 O   HOH A4147     1555   1555  3.48  
LINK         K     K A1696                 O   HOH A4492     1555   1555  2.93  
LINK         K     K A1696                 O   TRP A 508     1555   1555  2.66  
LINK        MG    MG A1699                 O   GLU A 579     1555   1555  2.23  
LINK        MG    MG A1699                 OD1 ASN A 577     1555   1555  2.16  
LINK        MG    MG A1699                 OD1 ASP A 550     1555   1555  2.19  
LINK        MG    MG A1699                 O   HOH A4051     1555   1555  2.13  
LINK        MG    MG A1699                 O3B P22 A1702     1555   1555  2.13  
LINK        MG    MG A1699                 O1A P22 A1702     1555   1555  2.08  
LINK         K     K B 696                 O   HOH B5202     1555   1555  3.02  
LINK         K     K B 696                 O   GLN B 506     1555   1555  2.72  
LINK         K     K B 696                 O   HOH B4657     1555   1555  3.67  
LINK         K     K B 696                 O   TRP B 508     1555   1555  2.67  
LINK         K     K B 696                 OE1 GLN B 343     1555   1555  2.75  
LINK         K     K B 696                 O   HOH B4676     1555   1555  3.71  
LINK         K     K B 696                 O   HOH B4232     1555   1555  2.74  
LINK         K     K B 696                 OD2 ASP B 350     1555   1555  2.84  
LINK         O3B P25 B 698                MG    MG B 699     1555   1555  2.03  
LINK        MG    MG B 699                 O   HOH B4246     1555   1555  2.18  
LINK        MG    MG B 699                 OD1 ASN B 577     1555   1555  2.22  
LINK        MG    MG B 699                 O   GLU B 579     1555   1555  2.17  
LINK        MG    MG B 699                 O1A P25 B 698     1555   1555  2.12  
LINK        MG    MG B 699                 OD1 ASP B 550     1555   1555  2.08  
CISPEP   1 LEU A  652    PRO A  653          0        -0.10                     
CISPEP   2 LEU B  652    PRO B  653          0         0.09                     
SITE     1 AC1  6 GLN B 343  ASP B 350  GLN B 506  TRP B 508                    
SITE     2 AC1  6 HOH B4232  HOH B5202                                          
SITE     1 AC2  5 ASP B 550  ASN B 577  GLU B 579  P25 B 698                    
SITE     2 AC2  5 HOH B4246                                                     
SITE     1 AC3  6 GLN A 343  ASP A 350  GLN A 506  TRP A 508                    
SITE     2 AC3  6 HOH A4034  HOH A4492                                          
SITE     1 AC4  5 ASP A 550  ASN A 577  GLU A 579  P22 A1702                    
SITE     2 AC4  5 HOH A4051                                                     
SITE     1 AC5 11 ASP A 379  ARG A 380  MET A 582  TRP A 586                    
SITE     2 AC5 11 FAD A 701  HOH A4808  HOH A5138  GLY B 116                    
SITE     3 AC5 11 VAL B 191  ALA B 200  PHE B 201                               
SITE     1 AC6 17 NSP A 704  VAL B 497  GLY B 498  GLN B 499                    
SITE     2 AC6 17 HIS B 500  MET B 525  GLY B 549  ASP B 550                    
SITE     3 AC6 17 ALA B 551  SER B 552  ASN B 577  GLU B 579                    
SITE     4 AC6 17 GLN B 580  GLY B 581  MET B 582   MG B 699                    
SITE     5 AC6 17 HOH B4246                                                     
SITE     1 AC7 37 ASP A 180  ARG A 241  GLY A 307  ALA A 308                    
SITE     2 AC7 37 GLY A 309  ASN A 312  THR A 334  LEU A 335                    
SITE     3 AC7 37 LEU A 352  MET A 354  HIS A 355  GLY A 374                    
SITE     4 AC7 37 ALA A 375  ARG A 376  ASP A 378  ARG A 380                    
SITE     5 AC7 37 VAL A 381  GLU A 407  VAL A 408  SER A 409                    
SITE     6 AC7 37 ASN A 412  GLY A 425  ASP A 426  ALA A 427                    
SITE     7 AC7 37 GLN A 501  MET A 502  SER A 519  GLY A 520                    
SITE     8 AC7 37 GLY A 521  1CS A 695  HOH A4014  HOH A4015                    
SITE     9 AC7 37 HOH A4031  HOH A4144  HOH A4325  HOH A4534                    
SITE    10 AC7 37 PHE B 201                                                     
SITE     1 AC8 10 GLU A 139  PRO A 165  ASN A 169  GLN A 202                    
SITE     2 AC8 10 GLY B 523  MET B 525  MET B 555  VAL B 583                    
SITE     3 AC8 10 P25 B 698  HOH B4820                                          
SITE     1 AC9 15 GLY A 116  VAL A 191  PRO A 192  ALA A 200                    
SITE     2 AC9 15 PHE A 201  LYS A 251  HOH A4076  MET B 354                    
SITE     3 AC9 15 ASP B 379  ARG B 380  MET B 582  TRP B 586                    
SITE     4 AC9 15 FAD B1701  HOH B4593  HOH B4816                               
SITE     1 BC1 40 PHE A 201  ASP B 180  ARG B 241  GLY B 307                    
SITE     2 BC1 40 ALA B 308  GLY B 309  ASN B 312  THR B 334                    
SITE     3 BC1 40 LEU B 335  GLN B 336  MET B 351  LEU B 352                    
SITE     4 BC1 40 GLY B 353  MET B 354  HIS B 355  GLY B 374                    
SITE     5 BC1 40 ALA B 375  ARG B 376  ASP B 378  ARG B 380                    
SITE     6 BC1 40 VAL B 381  PHE B 406  GLU B 407  VAL B 408                    
SITE     7 BC1 40 ASN B 412  GLY B 425  ASP B 426  ALA B 427                    
SITE     8 BC1 40 GLN B 501  MET B 502  SER B 519  GLY B 520                    
SITE     9 BC1 40 GLY B 521  1CS B1695  HOH B4204  HOH B4212                    
SITE    10 BC1 40 HOH B4229  HOH B4259  HOH B4539  HOH B5172                    
SITE     1 BC2 16 VAL A 497  GLY A 498  GLN A 499  HIS A 500                    
SITE     2 BC2 16 GLY A 549  ASP A 550  ALA A 551  SER A 552                    
SITE     3 BC2 16 ASN A 577  GLU A 579  GLN A 580  GLY A 581                    
SITE     4 BC2 16 MET A 582   MG A1699  YF3 A1705  HOH A4051                    
SITE     1 BC3 12 GLY A 523  MET A 525  MET A 555  GLN A 580                    
SITE     2 BC3 12 VAL A 583  P22 A1702  TYR B 113  PRO B 114                    
SITE     3 BC3 12 GLU B 139  PRO B 165  ASN B 169  GLN B 202                    
CRYST1  154.579  154.579  178.759  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      0.006469  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006469  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005594        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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