GenomeNet

Database: PDB
Entry: 1T9C
LinkDB: 1T9C
Original site: 1T9C 
HEADER    TRANSFERASE                             16-MAY-04   1T9C              
TITLE     CRYSTAL STRUCTURE OF YEAST ACETOHYDROXYACID SYNTHASE IN COMPLEX WITH A
TITLE    2 SULFONYLUREA HERBICIDE, SULFOMETURON METHYL                          
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, SULFOMETURON      
KEYWDS   3 METHYL, TRANSFERASE                                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.A.MCCOURT,S.S.PANG,L.W.GUDDAT,R.G.DUGGLEBY                          
REVDAT   4   11-OCT-17 1T9C    1       REMARK                                   
REVDAT   3   24-FEB-09 1T9C    1       VERSN                                    
REVDAT   2   01-MAR-05 1T9C    1                                                
REVDAT   1   21-DEC-04 1T9C    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.    2.34 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) : 2.34                           
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)   (%) : 96.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 88271                          
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                     : 0.191                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 8784                            
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) : 2.34                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.42                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 87.00                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1950                       
REMARK   3   BIN FREE R VALUE                    : 0.2370                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 738                          
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            : 9001                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 183                                     
REMARK   3   SOLVENT ATOMS            : 1176                                    
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) : 0.21                            
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) : 0.25                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.23                            
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 1T9C 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_1000022474.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-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   : 90495                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.340                              
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     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY                : 9.000                              
REMARK 200  R MERGE                    (I) : 0.07200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.34                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.42                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 86.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.26200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 8.520                              
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, SULFOMETURON METHYL,     
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 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: 12420 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 38620 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -80.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     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     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     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     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 465     SER B   278                                                      
REMARK 465     ARG B   279                                                      
REMARK 465     ALA B   280                                                      
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     ASP A 129    CG   OD1  OD2                                       
REMARK 470     ARG A 211    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 393    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 411    CG   CD   CE   NZ                                   
REMARK 470     GLU A 443    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 453    CG   CD   CE   NZ                                   
REMARK 470     LYS A 456    CG   CD   CE   NZ                                   
REMARK 470     GLU A 623    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 211    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B 281    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 283    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 393    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 411    CG   CD   CE   NZ                                   
REMARK 470     GLU B 443    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 446    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 456    CG   CD   CE   NZ                                   
REMARK 470     GLU B 457    CG   CD   OE1  OE2                                  
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    GLU A 610   CA    GLU A 610   CB      0.641                       
REMARK 500    GLU A 610   CB    GLU A 610   CG      0.131                       
REMARK 500    GLU A 610   CG    GLU A 610   CD     -0.125                       
REMARK 500    GLU A 610   CD    GLU A 610   OE1     0.909                       
REMARK 500    GLU A 610   CD    GLU A 610   OE2     0.344                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    GLU A 610   CB  -  CA  -  C   ANGL. DEV. =  34.6 DEGREES          
REMARK 500    GLU A 610   N   -  CA  -  CB  ANGL. DEV. = -22.9 DEGREES          
REMARK 500    GLU A 610   CA  -  CB  -  CG  ANGL. DEV. =  36.6 DEGREES          
REMARK 500    GLU A 610   CB  -  CG  -  CD  ANGL. DEV. = -57.5 DEGREES          
REMARK 500    GLU A 610   OE1 -  CD  -  OE2 ANGL. DEV. =  36.2 DEGREES          
REMARK 500    GLU A 610   CG  -  CD  -  OE1 ANGL. DEV. = 100.6 DEGREES          
REMARK 500    GLU A 610   CG  -  CD  -  OE2 ANGL. DEV. =  30.0 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A 350     -163.13     74.20                                   
REMARK 500    ARG A 511      -20.26   -140.49                                   
REMARK 500    GLU A 663       57.63   -110.11                                   
REMARK 500    ASP B 350     -156.95     73.44                                   
REMARK 500    ASN B 384      107.43    -59.06                                   
REMARK 500    ALA B 389       62.18     38.15                                   
REMARK 500    ARG B 444       59.21   -141.57                                   
REMARK 500    TYR B 460       74.67    -64.03                                   
REMARK 500    ASP B 486        1.40    -66.79                                   
REMARK 500    ARG B 511      -21.33   -141.56                                   
REMARK 500    GLU B 663       46.15   -103.59                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    GLU A 610         0.12    SIDE CHAIN                              
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 HOH A4061   O                                                      
REMARK 620 2 GLN A 343   NE2 151.2                                              
REMARK 620 3 ASP A 350   OD2  97.4  59.9                                        
REMARK 620 4 GLN A 506   O    59.6 138.0 102.8                                  
REMARK 620 5 HOH A4048   O   142.3  52.3  72.3  86.8                            
REMARK 620 6 TRP A 508   O    90.6 109.3 167.3  89.7 107.0                      
REMARK 620 7 GLN A 343   OE1 132.7  38.8  87.9 163.1  84.1  79.5                
REMARK 620 8 HOH A4778   O    44.1 119.3 103.0 101.2 171.6  76.0  88.8          
REMARK 620 N                    1     2     3     4     5     6     7           
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 P22 A1702   O3B                                                    
REMARK 620 2 HOH A4002   O    82.5                                              
REMARK 620 3 P22 A1702   O1A  92.5  91.1                                        
REMARK 620 4 GLU A 579   O    95.8 175.4  93.2                                  
REMARK 620 5 ASN A 577   OD1  98.0  90.0 169.5  86.0                            
REMARK 620 6 ASP A 550   OD1 167.4  85.1  85.6  96.7  84.1                      
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 ASP B 350   OD2                                                    
REMARK 620 2 HOH B4990   O    91.3                                              
REMARK 620 3 HOH B4977   O   116.1  45.5                                        
REMARK 620 4 GLN B 506   O   102.9  73.4 104.0                                  
REMARK 620 5 HOH B4254   O    68.1 150.7 162.8  90.5                            
REMARK 620 6 TRP B 508   O   161.0  99.3  63.7  95.2 106.6                      
REMARK 620 7 GLN B 343   OE1  83.2 123.3  87.4 162.4  76.4  77.8                
REMARK 620 N                    1     2     3     4     5     6                 
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 P23 B 700   O3B                                                    
REMARK 620 2 HOH B4006   O    80.3                                              
REMARK 620 3 ASP B 550   OD1 163.2  82.9                                        
REMARK 620 4 GLU B 579   O    94.7 172.7 102.2                                  
REMARK 620 5 P23 B 700   O1A  93.3  93.6  86.2  92.0                            
REMARK 620 6 ASN B 577   OD1  98.6  91.0  83.2  84.5 167.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K 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 1SM A 695                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P23 B 700                 
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 1SM B 1695                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B 1701                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P22 A 1702                
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: 1T9B   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF YEAST ACETOHYDROXYACID SYNTHASE IN COMPLEX      
REMARK 900 WITH A SULFONYLUREA HERBICIDE, CHLORSULFURON                         
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                     
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                    
DBREF  1T9C A   58   687  UNP    P07342   ILVB_YEAST      58    687             
DBREF  1T9C B   58   687  UNP    P07342   ILVB_YEAST      58    687             
SEQADV 1T9C MET A   11  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C HIS A   12  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C HIS A   13  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C HIS A   14  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C HIS A   15  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C HIS A   16  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C HIS A   17  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C SER A   18  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C SER A   19  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C GLY A   20  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C LEU A   21  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C VAL A   22  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C PRO A   23  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C ARG A   24  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C GLY A   25  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C SER A   26  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C GLY A   27  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C MET A   28  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C LYS A   29  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C GLU A   30  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C THR A   31  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C ALA A   32  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C ALA A   33  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C ALA A   34  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C LYS A   35  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C PHE A   36  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C GLU A   37  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C ARG A   38  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C GLN A   39  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C HIS A   40  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C MET A   41  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C ASP A   42  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C SER A   43  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C PRO A   44  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C ASP A   45  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C LEU A   46  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C GLY A   47  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C THR A   48  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C ASP A   49  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C ASP A   50  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C ASP A   51  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C ASP A   52  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C LYS A   53  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C ALA A   54  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C MET A   55  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C GLY A   56  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C SER A   57  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C MET B   11  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C HIS B   12  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C HIS B   13  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C HIS B   14  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C HIS B   15  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C HIS B   16  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C HIS B   17  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C SER B   18  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C SER B   19  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C GLY B   20  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C LEU B   21  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C VAL B   22  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C PRO B   23  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C ARG B   24  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C GLY B   25  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C SER B   26  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C GLY B   27  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C MET B   28  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C LYS B   29  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C GLU B   30  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C THR B   31  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C ALA B   32  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C ALA B   33  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C ALA B   34  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C LYS B   35  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C PHE B   36  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C GLU B   37  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C ARG B   38  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C GLN B   39  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C HIS B   40  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C MET B   41  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C ASP B   42  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C SER B   43  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C PRO B   44  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C ASP B   45  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C LEU B   46  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C GLY B   47  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C THR B   48  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C ASP B   49  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C ASP B   50  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C ASP B   51  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C ASP B   52  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C LYS B   53  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C ALA B   54  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C MET B   55  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C GLY B   56  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9C 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    1SM  A 695      25                                                       
HET    FAD  A 701      53                                                       
HET    P22  A1702      11                                                       
HET      K  B 696       1                                                       
HET     MG  B 699       1                                                       
HET    P23  B 700      12                                                       
HET    1SM  B1695      25                                                       
HET    FAD  B1701      53                                                       
HETNAM       K POTASSIUM ION                                                    
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     1SM METHYL 2-[({[(4,6-DIMETHYLPYRIMIDIN-2-YL)                        
HETNAM   2 1SM  AMINO]CARBONYL}AMINO)SULFONYL]BENZOATE                          
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     P22 ETHYL DIHYDROGEN DIPHOSPHATE                                     
HETNAM     P23 PROPYL TRIHYDROGEN DIPHOSPHATE                                   
HETSYN     1SM SULFOMETURON METHYL                                              
FORMUL   3    K    2(K 1+)                                                      
FORMUL   4   MG    2(MG 2+)                                                     
FORMUL   5  1SM    2(C15 H16 N4 O5 S)                                           
FORMUL   6  FAD    2(C27 H33 N9 O15 P2)                                         
FORMUL   7  P22    C2 H8 O7 P2                                                  
FORMUL  10  P23    C3 H10 O7 P2                                                 
FORMUL  13  HOH   *1176(H2 O)                                                   
HELIX    1   1 THR A   93  GLN A  105  1                                  13    
HELIX    2   2 ILE A  118  HIS A  126  1                                   9    
HELIX    3   3 HIS A  138  GLY A  154  1                                  17    
HELIX    4   4 GLY A  164  ASN A  169  1                                   6    
HELIX    5   5 VAL A  170  GLY A  181  1                                  12    
HELIX    6   6 ASP A  205  SER A  210  1                                   6    
HELIX    7   7 ARG A  211  THR A  214  5                                   4    
HELIX    8   8 SER A  222  GLU A  224  5                                   3    
HELIX    9   9 GLU A  225  SER A  239  1                                  15    
HELIX   10  10 LYS A  251  ALA A  256  1                                   6    
HELIX   11  11 THR A  264  LEU A  268  5                                   5    
HELIX   12  12 SER A  278  ASN A  297  1                                  20    
HELIX   13  13 ALA A  308  ASN A  312  5                                   5    
HELIX   14  14 ASP A  315  GLN A  328  1                                  14    
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  MET A  435  1                                  10    
HELIX   21  21 SER A  436  ILE A  438  5                                   3    
HELIX   22  22 ARG A  444  TYR A  458  1                                  15    
HELIX   23  23 LYS A  472  THR A  487  1                                  16    
HELIX   24  24 GLY A  498  TRP A  508  1                                  11    
HELIX   25  25 TYR A  527  LYS A  539  1                                  13    
HELIX   26  26 ASP A  550  LEU A  557  1                                   8    
HELIX   27  27 GLU A  559  GLY A  567  1                                   9    
HELIX   28  28 GLN A  580  TYR A  591  1                                  12    
HELIX   29  29 ASP A  604  MET A  612  1                                   9    
HELIX   30  30 LYS A  621  GLU A  623  5                                   3    
HELIX   31  31 GLU A  624  THR A  635  1                                  12    
HELIX   32  32 ASP A  668  THR A  683  1                                  16    
HELIX   33  33 THR B   93  GLN B  105  1                                  13    
HELIX   34  34 GLY B  115  ALA B  117  5                                   3    
HELIX   35  35 ILE B  118  ILE B  125  1                                   8    
HELIX   36  36 HIS B  138  GLY B  154  1                                  17    
HELIX   37  37 GLY B  164  ASN B  169  1                                   6    
HELIX   38  38 VAL B  170  GLY B  181  1                                  12    
HELIX   39  39 ASP B  205  SER B  210  1                                   6    
HELIX   40  40 ARG B  211  THR B  214  5                                   4    
HELIX   41  41 SER B  222  GLU B  224  5                                   3    
HELIX   42  42 GLU B  225  SER B  239  1                                  15    
HELIX   43  43 LYS B  251  ALA B  256  1                                   6    
HELIX   44  44 LYS B  265  LEU B  268  5                                   4    
HELIX   45  46 ALA B  308  HIS B  313  5                                   6    
HELIX   46  47 ASP B  315  ALA B  327  1                                  13    
HELIX   47  48 LEU B  335  LEU B  338  5                                   4    
HELIX   48  49 CYS B  357  ALA B  367  1                                  11    
HELIX   49  50 ASN B  384  PHE B  388  5                                   5    
HELIX   50  51 ALA B  389  GLU B  398  1                                  10    
HELIX   51  52 SER B  409  ILE B  413  5                                   5    
HELIX   52  53 ASP B  426  SER B  436  1                                  11    
HELIX   53  54 ARG B  444  TYR B  458  1                                  15    
HELIX   54  55 LYS B  472  ASP B  486  1                                  15    
HELIX   55  56 GLY B  498  TRP B  508  1                                  11    
HELIX   56  57 TYR B  527  LYS B  539  1                                  13    
HELIX   57  58 ASP B  550  LEU B  557  1                                   8    
HELIX   58  59 GLU B  559  GLY B  567  1                                   9    
HELIX   59  60 GLN B  580  TYR B  591  1                                  12    
HELIX   60  61 ASP B  604  MET B  612  1                                   9    
HELIX   61  62 LYS B  621  GLU B  623  5                                   3    
HELIX   62  63 GLU B  624  THR B  635  1                                  12    
HELIX   63  64 ASP B  668  GLY B  684  1                                  17    
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  VAL A 306   O  THR A 332           
SHEET    4   B 6 LEU A 369  VAL A 373  1  O  VAL A 373   N  TYR A 305           
SHEET    5   B 6 GLY A 402  GLU A 407  1  O  ILE A 404   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 546           
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 2 MET B  85  ASP B  86  0                                        
SHEET    2   D 2 ILE B 262  PRO B 263 -1  O  ILE B 262   N  ASP B  86           
SHEET    1   E 6 ASN B 132  VAL B 134  0                                        
SHEET    2   E 6 THR B 109  GLY B 112  1  N  VAL B 110   O  VAL B 134           
SHEET    3   E 6 GLY B 157  VAL B 161  1  O  VAL B 158   N  PHE B 111           
SHEET    4   E 6 MET B 184  GLN B 190  1  O  PHE B 187   N  VAL B 159           
SHEET    5   E 6 PRO B 244  PRO B 250  1  O  LEU B 249   N  THR B 188           
SHEET    6   E 6 TRP B 216  MET B 219  1  N  VAL B 218   O  ASP B 248           
SHEET    1   F 6 SER B 348  MET B 351  0                                        
SHEET    2   F 6 VAL B 331  THR B 333  1  N  VAL B 331   O  LEU B 349           
SHEET    3   F 6 PRO B 302  VAL B 306  1  N  LEU B 304   O  THR B 332           
SHEET    4   F 6 LEU B 369  VAL B 373  1  O  VAL B 373   N  TYR B 305           
SHEET    5   F 6 GLY B 402  GLU B 407  1  O  PHE B 406   N  ALA B 372           
SHEET    6   F 6 ILE B 421  GLU B 424  1  O  ILE B 421   N  HIS B 405           
SHEET    1   G 6 PHE B 516  ILE B 517  0                                        
SHEET    2   G 6 VAL B 491  THR B 495  1  N  VAL B 493   O  ILE B 517           
SHEET    3   G 6 LEU B 543  GLY B 549  1  O  ILE B 545   N  ILE B 492           
SHEET    4   G 6 LYS B 571  ASN B 576  1  O  LEU B 573   N  ASP B 548           
SHEET    5   G 6 VAL B 639  GLU B 644  1  O  LEU B 641   N  ILE B 572           
SHEET    6   G 6 LYS B 615  VAL B 619  1  N  LEU B 617   O  LEU B 640           
LINK         K     K A1696                 O   HOH A4061     1555   1555  3.71  
LINK         K     K A1696                 NE2 GLN A 343     1555   1555  3.59  
LINK         K     K A1696                 OD2 ASP A 350     1555   1555  2.84  
LINK         K     K A1696                 O   GLN A 506     1555   1555  2.76  
LINK         K     K A1696                 O   HOH A4048     1555   1555  2.73  
LINK         K     K A1696                 O   TRP A 508     1555   1555  2.66  
LINK         K     K A1696                 OE1 GLN A 343     1555   1555  2.74  
LINK         K     K A1696                 O   HOH A4778     1555   1555  2.87  
LINK        MG    MG A1699                 O3B P22 A1702     1555   1555  2.02  
LINK        MG    MG A1699                 O   HOH A4002     1555   1555  2.24  
LINK        MG    MG A1699                 O1A P22 A1702     1555   1555  2.14  
LINK        MG    MG A1699                 O   GLU A 579     1555   1555  2.18  
LINK        MG    MG A1699                 OD1 ASN A 577     1555   1555  2.15  
LINK        MG    MG A1699                 OD1 ASP A 550     1555   1555  2.09  
LINK         K     K B 696                 OD2 ASP B 350     1555   1555  2.97  
LINK         K     K B 696                 O   HOH B4990     1555   1555  3.01  
LINK         K     K B 696                 O   HOH B4977     1555   1555  3.66  
LINK         K     K B 696                 O   GLN B 506     1555   1555  2.57  
LINK         K     K B 696                 O   HOH B4254     1555   1555  2.70  
LINK         K     K B 696                 O   TRP B 508     1555   1555  2.61  
LINK         K     K B 696                 OE1 GLN B 343     1555   1555  2.71  
LINK        MG    MG B 699                 O3B P23 B 700     1555   1555  2.05  
LINK        MG    MG B 699                 O   HOH B4006     1555   1555  2.17  
LINK        MG    MG B 699                 OD1 ASP B 550     1555   1555  2.11  
LINK        MG    MG B 699                 O   GLU B 579     1555   1555  2.20  
LINK        MG    MG B 699                 O1A P23 B 700     1555   1555  2.11  
LINK        MG    MG B 699                 OD1 ASN B 577     1555   1555  2.18  
CISPEP   1 LEU A  652    PRO A  653          0        -0.23                     
CISPEP   2 LEU B  652    PRO B  653          0        -0.24                     
SITE     1 AC1  6 GLN B 343  ASP B 350  GLN B 506  TRP B 508                    
SITE     2 AC1  6 HOH B4254  HOH B4990                                          
SITE     1 AC2  5 ASP B 550  ASN B 577  GLU B 579  P23 B 700                    
SITE     2 AC2  5 HOH B4006                                                     
SITE     1 AC3  6 GLN A 343  ASP A 350  GLN A 506  TRP A 508                    
SITE     2 AC3  6 HOH A4048  HOH A4778                                          
SITE     1 AC4  5 ASP A 550  ASN A 577  GLU A 579  P22 A1702                    
SITE     2 AC4  5 HOH A4002                                                     
SITE     1 AC5 13 ASP A 379  ARG A 380  MET A 582  TRP A 586                    
SITE     2 AC5 13 HOH A4174  HOH A4421  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 16 VAL B 497  GLY B 498  GLN B 499  HIS B 500                    
SITE     2 AC6 16 MET B 525  GLY B 549  ASP B 550  ALA B 551                    
SITE     3 AC6 16 SER B 552  ASN B 577  GLU B 579  GLN B 580                    
SITE     4 AC6 16 GLY B 581  MET B 582   MG B 699  HOH B4006                    
SITE     1 AC7 38 ASP A 180  ARG A 241  GLY A 307  ALA A 308                    
SITE     2 AC7 38 GLY A 309  ASN A 312  THR A 334  LEU A 335                    
SITE     3 AC7 38 GLN A 336  LEU A 352  GLY A 353  MET A 354                    
SITE     4 AC7 38 HIS A 355  GLY A 374  ALA A 375  ARG A 376                    
SITE     5 AC7 38 ASP A 378  ARG A 380  VAL A 381  PHE A 406                    
SITE     6 AC7 38 GLU A 407  VAL A 408  ASN A 412  GLY A 425                    
SITE     7 AC7 38 ASP A 426  ALA A 427  GLN A 501  MET A 502                    
SITE     8 AC7 38 GLY A 520  GLY A 521  MET A 582  HOH A4022                    
SITE     9 AC7 38 HOH A4023  HOH A4042  HOH A4160  HOH A4342                    
SITE    10 AC7 38 HOH A5056  PHE B 201                                          
SITE     1 AC8 14 GLY A 116  ALA A 117  VAL A 191  PRO A 192                    
SITE     2 AC8 14 PHE A 201  GLN A 202  LYS A 251  HOH A4036                    
SITE     3 AC8 14 ASP B 379  ARG B 380  MET B 582  TRP B 586                    
SITE     4 AC8 14 HOH B4581  HOH B4820                                          
SITE     1 AC9 38 PHE A 201  ASP B 180  ARG B 241  GLY B 307                    
SITE     2 AC9 38 ALA B 308  GLY B 309  ASN B 312  THR B 334                    
SITE     3 AC9 38 LEU B 335  LEU B 352  GLY B 353  MET B 354                    
SITE     4 AC9 38 HIS B 355  GLY B 374  ALA B 375  ARG B 376                    
SITE     5 AC9 38 ASP B 378  ARG B 380  VAL B 381  GLU B 407                    
SITE     6 AC9 38 VAL B 408  SER B 409  ASN B 412  GLY B 425                    
SITE     7 AC9 38 ASP B 426  ALA B 427  GLN B 501  MET B 502                    
SITE     8 AC9 38 SER B 519  GLY B 520  GLY B 521  MET B 582                    
SITE     9 AC9 38 HOH B4226  HOH B4235  HOH B4248  HOH B4250                    
SITE    10 AC9 38 HOH B4281  HOH B4447                                          
SITE     1 BC1 15 VAL A 497  GLY A 498  GLN A 499  HIS A 500                    
SITE     2 BC1 15 GLY A 549  ASP A 550  ALA A 551  SER A 552                    
SITE     3 BC1 15 ASN A 577  GLU A 579  GLN A 580  GLY A 581                    
SITE     4 BC1 15 MET A 582   MG A1699  HOH A4002                               
CRYST1  154.486  154.486  178.796  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      0.006473  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006473  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005593        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system