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Database: PDB
Entry: 1T9D
LinkDB: 1T9D
Original site: 1T9D 
HEADER    TRANSFERASE                             16-MAY-04   1T9D              
TITLE     CRYSTAL STRUCTURE OF YEAST ACETOHYDROXYACID SYNTHASE IN COMPLEX WITH A
TITLE    2 SULFONYLUREA HERBICIDE, METSULFURON METHYL                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACETOLACTATE SYNTHASE, MITOCHONDRIAL;                      
COMPND   3 CHAIN: A, B, C, D;                                                   
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, METSULFURON       
KEYWDS   3 METHYL, TRANSFERASE                                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.A.MCCOURT,S.S.PANG,L.W.GUDDAT,R.G.DUGGLEBY                          
REVDAT   5   11-OCT-17 1T9D    1       REMARK                                   
REVDAT   4   01-SEP-09 1T9D    1       HETATM HETNAM                            
REVDAT   3   24-FEB-09 1T9D    1       VERSN                                    
REVDAT   2   01-MAR-05 1T9D    1       JRNL                                     
REVDAT   1   21-DEC-04 1T9D    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.    2.30 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) : 2.30                           
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)   (%) : 80.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 153191                         
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) : 0.164                           
REMARK   3   FREE R VALUE                     : 0.195                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 15236                           
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) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.38                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 64.00                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2150                       
REMARK   3   BIN FREE R VALUE                    : 0.2560                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 1109                         
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            : 17715                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 410                                     
REMARK   3   SOLVENT ATOMS            : 2176                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 56.80                          
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) : 0.22                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.22                            
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) : 0.26                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.26                            
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 1T9D 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_1000022475.                                   
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   : 160659                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.290                              
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     (%) : 83.6                               
REMARK 200  DATA REDUNDANCY                : 8.800                              
REMARK 200  R MERGE                    (I) : 0.05600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.29                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 64.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.25400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.710                              
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): 3.56                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: POTASSIUM PHOSPHATE, THIAMIN             
REMARK 280  DIPHOSPHATE, FAD, MAGNESIUM CHLORIDE, DTT, METSULFURON 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: I 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       9555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290      10555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290      11555   -Y+1/2,X+1/2,Z+1/2                                      
REMARK 290      12555   Y+1/2,-X+1/2,Z+1/2                                      
REMARK 290      13555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290      14555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290      15555   Y+1/2,X+1/2,-Z+1/2                                      
REMARK 290      16555   -Y+1/2,-X+1/2,-Z+1/2                                    
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   SMTRY1   9  1.000000  0.000000  0.000000      109.17350            
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000      109.17350            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000      180.76500            
REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000      109.17350            
REMARK 290   SMTRY2  10  0.000000 -1.000000  0.000000      109.17350            
REMARK 290   SMTRY3  10  0.000000  0.000000  1.000000      180.76500            
REMARK 290   SMTRY1  11  0.000000 -1.000000  0.000000      109.17350            
REMARK 290   SMTRY2  11  1.000000  0.000000  0.000000      109.17350            
REMARK 290   SMTRY3  11  0.000000  0.000000  1.000000      180.76500            
REMARK 290   SMTRY1  12  0.000000  1.000000  0.000000      109.17350            
REMARK 290   SMTRY2  12 -1.000000  0.000000  0.000000      109.17350            
REMARK 290   SMTRY3  12  0.000000  0.000000  1.000000      180.76500            
REMARK 290   SMTRY1  13 -1.000000  0.000000  0.000000      109.17350            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000      109.17350            
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000      180.76500            
REMARK 290   SMTRY1  14  1.000000  0.000000  0.000000      109.17350            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000      109.17350            
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000      180.76500            
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000      109.17350            
REMARK 290   SMTRY2  15  1.000000  0.000000  0.000000      109.17350            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000      180.76500            
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000      109.17350            
REMARK 290   SMTRY2  16 -1.000000  0.000000  0.000000      109.17350            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000      180.76500            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 ASSYMETRIC UNIT CONTAINS 4 MOLECULES ARRANGED AS TWO     
REMARK 300 DIMERS. A DIMER IS THE MINIMUM BIOLOGICAL UNIT REQUIRED FOR          
REMARK 300 ACTIVITY.                                                            
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: 13450 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 38180 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -53.0 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 13320 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 38010 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -65.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
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     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     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     MET B    85                                                      
REMARK 465     THR B   264                                                      
REMARK 465     LYS B   265                                                      
REMARK 465     THR B   266                                                      
REMARK 465     THR B   267                                                      
REMARK 465     LEU B   268                                                      
REMARK 465     PRO B   269                                                      
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 465     GLN B   281                                                      
REMARK 465     ASP B   282                                                      
REMARK 465     GLU B   283                                                      
REMARK 465     MET C    11                                                      
REMARK 465     HIS C    12                                                      
REMARK 465     HIS C    13                                                      
REMARK 465     HIS C    14                                                      
REMARK 465     HIS C    15                                                      
REMARK 465     HIS C    16                                                      
REMARK 465     HIS C    17                                                      
REMARK 465     SER C    18                                                      
REMARK 465     SER C    19                                                      
REMARK 465     GLY C    20                                                      
REMARK 465     LEU C    21                                                      
REMARK 465     VAL C    22                                                      
REMARK 465     PRO C    23                                                      
REMARK 465     ARG C    24                                                      
REMARK 465     GLY C    25                                                      
REMARK 465     SER C    26                                                      
REMARK 465     GLY C    27                                                      
REMARK 465     MET C    28                                                      
REMARK 465     LYS C    29                                                      
REMARK 465     GLU C    30                                                      
REMARK 465     THR C    31                                                      
REMARK 465     ALA C    32                                                      
REMARK 465     ALA C    33                                                      
REMARK 465     ALA C    34                                                      
REMARK 465     LYS C    35                                                      
REMARK 465     PHE C    36                                                      
REMARK 465     GLU C    37                                                      
REMARK 465     ARG C    38                                                      
REMARK 465     GLN C    39                                                      
REMARK 465     HIS C    40                                                      
REMARK 465     MET C    41                                                      
REMARK 465     ASP C    42                                                      
REMARK 465     SER C    43                                                      
REMARK 465     PRO C    44                                                      
REMARK 465     ASP C    45                                                      
REMARK 465     LEU C    46                                                      
REMARK 465     GLY C    47                                                      
REMARK 465     THR C    48                                                      
REMARK 465     ASP C    49                                                      
REMARK 465     ASP C    50                                                      
REMARK 465     ASP C    51                                                      
REMARK 465     ASP C    52                                                      
REMARK 465     LYS C    53                                                      
REMARK 465     ALA C    54                                                      
REMARK 465     MET C    55                                                      
REMARK 465     GLY C    56                                                      
REMARK 465     SER C    57                                                      
REMARK 465     ALA C    58                                                      
REMARK 465     PRO C    59                                                      
REMARK 465     SER C    60                                                      
REMARK 465     PHE C    61                                                      
REMARK 465     ASN C    62                                                      
REMARK 465     VAL C    63                                                      
REMARK 465     ASP C    64                                                      
REMARK 465     PRO C    65                                                      
REMARK 465     LEU C    66                                                      
REMARK 465     GLU C    67                                                      
REMARK 465     GLN C    68                                                      
REMARK 465     PRO C    69                                                      
REMARK 465     ALA C    70                                                      
REMARK 465     GLU C    71                                                      
REMARK 465     PRO C    72                                                      
REMARK 465     SER C    73                                                      
REMARK 465     LYS C    74                                                      
REMARK 465     LEU C    75                                                      
REMARK 465     ALA C    76                                                      
REMARK 465     LYS C    77                                                      
REMARK 465     LYS C    78                                                      
REMARK 465     LEU C    79                                                      
REMARK 465     ARG C    80                                                      
REMARK 465     ALA C    81                                                      
REMARK 465     GLU C    82                                                      
REMARK 465     PRO C    83                                                      
REMARK 465     ASP C    84                                                      
REMARK 465     MET C    85                                                      
REMARK 465     ASP C    86                                                      
REMARK 465     THR C    87                                                      
REMARK 465     SER C    88                                                      
REMARK 465     THR C   266                                                      
REMARK 465     THR C   267                                                      
REMARK 465     LEU C   268                                                      
REMARK 465     PRO C   269                                                      
REMARK 465     SER C   270                                                      
REMARK 465     ASN C   271                                                      
REMARK 465     ALA C   272                                                      
REMARK 465     LEU C   273                                                      
REMARK 465     ASN C   274                                                      
REMARK 465     GLN C   275                                                      
REMARK 465     LEU C   276                                                      
REMARK 465     THR C   277                                                      
REMARK 465     SER C   278                                                      
REMARK 465     ARG C   279                                                      
REMARK 465     ALA C   280                                                      
REMARK 465     GLN C   281                                                      
REMARK 465     ASP C   282                                                      
REMARK 465     GLU C   283                                                      
REMARK 465     PHE C   284                                                      
REMARK 465     VAL C   285                                                      
REMARK 465     MET C   286                                                      
REMARK 465     GLN C   287                                                      
REMARK 465     SER C   288                                                      
REMARK 465     ILE C   289                                                      
REMARK 465     MET D    11                                                      
REMARK 465     HIS D    12                                                      
REMARK 465     HIS D    13                                                      
REMARK 465     HIS D    14                                                      
REMARK 465     HIS D    15                                                      
REMARK 465     HIS D    16                                                      
REMARK 465     HIS D    17                                                      
REMARK 465     SER D    18                                                      
REMARK 465     SER D    19                                                      
REMARK 465     GLY D    20                                                      
REMARK 465     LEU D    21                                                      
REMARK 465     VAL D    22                                                      
REMARK 465     PRO D    23                                                      
REMARK 465     ARG D    24                                                      
REMARK 465     GLY D    25                                                      
REMARK 465     SER D    26                                                      
REMARK 465     GLY D    27                                                      
REMARK 465     MET D    28                                                      
REMARK 465     LYS D    29                                                      
REMARK 465     GLU D    30                                                      
REMARK 465     THR D    31                                                      
REMARK 465     ALA D    32                                                      
REMARK 465     ALA D    33                                                      
REMARK 465     ALA D    34                                                      
REMARK 465     LYS D    35                                                      
REMARK 465     PHE D    36                                                      
REMARK 465     GLU D    37                                                      
REMARK 465     ARG D    38                                                      
REMARK 465     GLN D    39                                                      
REMARK 465     HIS D    40                                                      
REMARK 465     MET D    41                                                      
REMARK 465     ASP D    42                                                      
REMARK 465     SER D    43                                                      
REMARK 465     PRO D    44                                                      
REMARK 465     ASP D    45                                                      
REMARK 465     LEU D    46                                                      
REMARK 465     GLY D    47                                                      
REMARK 465     THR D    48                                                      
REMARK 465     ASP D    49                                                      
REMARK 465     ASP D    50                                                      
REMARK 465     ASP D    51                                                      
REMARK 465     ASP D    52                                                      
REMARK 465     LYS D    53                                                      
REMARK 465     ALA D    54                                                      
REMARK 465     MET D    55                                                      
REMARK 465     GLY D    56                                                      
REMARK 465     SER D    57                                                      
REMARK 465     ALA D    58                                                      
REMARK 465     PRO D    59                                                      
REMARK 465     SER D    60                                                      
REMARK 465     PHE D    61                                                      
REMARK 465     ASN D    62                                                      
REMARK 465     VAL D    63                                                      
REMARK 465     ASP D    64                                                      
REMARK 465     PRO D    65                                                      
REMARK 465     LEU D    66                                                      
REMARK 465     GLU D    67                                                      
REMARK 465     GLN D    68                                                      
REMARK 465     PRO D    69                                                      
REMARK 465     ALA D    70                                                      
REMARK 465     GLU D    71                                                      
REMARK 465     PRO D    72                                                      
REMARK 465     SER D    73                                                      
REMARK 465     LYS D    74                                                      
REMARK 465     LEU D    75                                                      
REMARK 465     ALA D    76                                                      
REMARK 465     LYS D    77                                                      
REMARK 465     LYS D    78                                                      
REMARK 465     LEU D    79                                                      
REMARK 465     ARG D    80                                                      
REMARK 465     ALA D    81                                                      
REMARK 465     GLU D    82                                                      
REMARK 465     PRO D    83                                                      
REMARK 465     ASP D    84                                                      
REMARK 465     ASN D   271                                                      
REMARK 465     ALA D   272                                                      
REMARK 465     LEU D   273                                                      
REMARK 465     ASN D   274                                                      
REMARK 465     GLN D   275                                                      
REMARK 465     LEU D   276                                                      
REMARK 465     THR D   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     ARG A 104    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 151    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR A 277    OG1  CG2                                            
REMARK 470     ARG A 393    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 442    CG   CD   CE   NZ                                   
REMARK 470     LYS A 456    CG   CD   CE   NZ                                   
REMARK 470     LYS A 686    CG   CD   CE   NZ                                   
REMARK 470     THR B  87    OG1  CG2                                            
REMARK 470     ARG B 151    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     MET B 286    CG   SD   CE                                        
REMARK 470     GLN B 287    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 291    CG   CD   CE   NZ                                   
REMARK 470     LYS B 301    CG   CD   CE   NZ                                   
REMARK 470     ARG B 393    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 442    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 453    CG   CD   CE   NZ                                   
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 470     GLU B 677    CG   CD   OE1  OE2                                  
REMARK 470     ASN C 106    CG   OD1  ND2                                       
REMARK 470     ARG C 151    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C 221    CG   CD   CE   NZ                                   
REMARK 470     LYS C 265    CG   CD   CE   NZ                                   
REMARK 470     LYS C 291    CG   CD   CE   NZ                                   
REMARK 470     LYS C 300    CG   CD   CE   NZ                                   
REMARK 470     ARG C 393    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C 411    CG   CD   CE   NZ                                   
REMARK 470     GLN C 418    CG   CD   OE1  NE2                                  
REMARK 470     LYS C 437    CG   CD   CE   NZ                                   
REMARK 470     LYS C 442    CG   CD   CE   NZ                                   
REMARK 470     GLU C 443    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 446    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 453    CG   CD   CE   NZ                                   
REMARK 470     LYS C 456    CG   CD   CE   NZ                                   
REMARK 470     GLU C 457    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 630    CG   CD   CE   NZ                                   
REMARK 470     LYS C 636    CG   CD   CE   NZ                                   
REMARK 470     ARG D 104    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP D 129    CG   OD1  OD2                                       
REMARK 470     ARG D 151    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     MET D 184    CG   SD   CE                                        
REMARK 470     LYS D 265    CG   CD   CE   NZ                                   
REMARK 470     ARG D 279    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU D 283    CG   CD   OE1  OE2                                  
REMARK 470     ARG D 393    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D 453    CG   CD   CE   NZ                                   
REMARK 470     LYS D 456    CG   CD   CE   NZ                                   
REMARK 470     GLN D 600    CG   CD   OE1  NE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A 127       19.50     59.64                                   
REMARK 500    ASP A 350     -164.59     72.73                                   
REMARK 500    ALA A 389       60.30     39.75                                   
REMARK 500    ARG A 511      -19.97   -140.14                                   
REMARK 500    GLU A 592       53.41     36.60                                   
REMARK 500    GLU A 663       46.53   -103.01                                   
REMARK 500    TRP B 216      147.11   -175.74                                   
REMARK 500    PRO B 242      155.14    -49.71                                   
REMARK 500    ASP B 350     -156.85     78.15                                   
REMARK 500    TYR B 458       73.01   -118.91                                   
REMARK 500    ARG B 511      -27.44   -143.56                                   
REMARK 500    GLU B 663       41.66   -100.31                                   
REMARK 500    PRO C 242      153.98    -45.99                                   
REMARK 500    ASP C 350     -154.19     75.07                                   
REMARK 500    ASN C 366       52.38   -113.21                                   
REMARK 500    ALA C 389       62.48     39.17                                   
REMARK 500    LYS C 442      -72.36    -69.89                                   
REMARK 500    ARG C 511      -42.23   -132.44                                   
REMARK 500    GLU C 592       52.06     37.61                                   
REMARK 500    GLU C 663       48.44    -99.42                                   
REMARK 500    ASN D 127       15.44     59.07                                   
REMARK 500    PRO D 269      171.89    -58.28                                   
REMARK 500    ASP D 350     -162.11     71.26                                   
REMARK 500    GLU D 592       52.87     38.27                                   
REMARK 500    GLU D 663       51.38   -107.04                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 615                                                                      
REMARK 615 ZERO OCCUPANCY ATOM                                                  
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 615   M RES C  SSEQI                                                     
REMARK 615     HOH A  4751                                                      
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 ASP A 350   OD2                                                    
REMARK 620 2 HOH A4043   O    69.7                                              
REMARK 620 3 GLN A 343   OE1  84.2  78.4                                        
REMARK 620 4 GLN A 506   O   105.2  89.2 160.9                                  
REMARK 620 5 HOH A5543   O    92.7 136.3 141.3  56.2                            
REMARK 620 6 HOH A4595   O   103.0 162.9  85.6 107.7  57.4                      
REMARK 620 7 TRP A 508   O   164.9 109.0  80.8  89.7  97.7  73.9                
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 P25 A1698   O3B                                                    
REMARK 620 2 ASP A 550   OD1 160.1                                              
REMARK 620 3 ASN A 577   OD1  96.7  78.1                                        
REMARK 620 4 GLU A 579   O    95.2 104.3  93.8                                  
REMARK 620 5 P25 A1698   O1A  92.2  91.8 169.7  90.4                            
REMARK 620 6 HOH A4061   O    77.4  82.9  84.5 172.1  92.5                      
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 GLN B 343   OE1                                                    
REMARK 620 2 GLN B 343   NE2  37.4                                              
REMARK 620 3 TRP B 508   O    80.4 110.9                                        
REMARK 620 4 HOH B4274   O    87.7  58.1 109.1                                  
REMARK 620 5 ASP B 350   OD2  90.3  59.7 170.5  68.0                            
REMARK 620 6 GLN B 506   O   158.1 139.4  85.2  81.6 103.1                      
REMARK 620 7 HOH B5858   O    87.7 111.8  83.1 166.0  98.9 106.9                
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 GLU B 579   O                                                      
REMARK 620 2 ASN B 577   OD1  82.3                                              
REMARK 620 3 ASP B 550   OD1 103.7  84.7                                        
REMARK 620 4 HOH B4287   O   168.8  92.0  85.3                                  
REMARK 620 5 P25 B 698   O3B  92.0  94.1 163.8  78.7                            
REMARK 620 6 P25 B 698   O1A  95.2 173.6  90.2  91.4  91.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K C3696   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN C 343   OE1                                                    
REMARK 620 2 TRP C 508   O    67.8                                              
REMARK 620 3 GLN C 343   NE2  41.9 102.2                                        
REMARK 620 4 HOH C5037   O    83.1 105.6  49.6                                  
REMARK 620 5 GLN C 506   O   160.1  94.1 143.4  94.5                            
REMARK 620 6 ASP C 350   OD2 102.3 170.0  68.1  70.4  95.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C3699  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C 579   O                                                      
REMARK 620 2 P22 C3702   O1A  86.8                                              
REMARK 620 3 P22 C3702   O3B  89.1  93.9                                        
REMARK 620 4 HOH C5774   O   176.8  96.4  91.0                                  
REMARK 620 5 P22 C3702   O3A 108.7  51.8  49.5  73.7                            
REMARK 620 6 ASP C 550   OD1  94.6  84.9 176.0  85.4 127.6                      
REMARK 620 7 ASN C 577   OD1  75.6 157.8  99.1 101.2 147.0  83.2                
REMARK 620 8 ASN C 577   ND2 108.1 154.7  66.7  69.0 103.2 113.2  47.0          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K D2696   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 350   OD2                                                    
REMARK 620 2 HOH D4801   O    70.7                                              
REMARK 620 3 GLN D 506   O   101.4  87.8                                        
REMARK 620 4 HOH D6040   O    95.7 134.6  51.6                                  
REMARK 620 5 HOH D5353   O    93.8 163.6 101.1  50.1                            
REMARK 620 6 TRP D 508   O   165.5 106.2  92.5  96.1  87.4                      
REMARK 620 7 GLN D 343   OE1  85.6  82.8 165.7 140.8  90.7  79.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D2699  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU D 579   O                                                      
REMARK 620 2 P22 D2702   O1A  97.1                                              
REMARK 620 3 P22 D2702   O3B  99.5  93.1                                        
REMARK 620 4 HOH D4819   O   174.9  84.4  85.2                                  
REMARK 620 5 ASN D 577   OD1  91.6 162.6 100.3  85.7                            
REMARK 620 6 ASP D 550   OD1 101.7  83.9 158.8  73.6  79.6                      
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 K D 2696                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 2699                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 3696                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 3699                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1MM A 695                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P25 B 698                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 701                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PYD A 703                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1MM B 1695                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P25 A 1698                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD B 1701                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PYD B 1703                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1MM C 2695                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD C 2701                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P22 D 2702                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PYD C 2703                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1MM C 3695                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD D 3701                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE P22 C 3702                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PYD D 3703                
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: 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: 1T9A   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF YEAST ACETOHYDROXYACID SYNTHASE IN COMPLEX      
REMARK 900 WITH A SULFONYLUREA HERBICIDE,TRIBENURON METHYL                      
DBREF  1T9D A   58   687  UNP    P07342   ILVB_YEAST      58    687             
DBREF  1T9D B   58   687  UNP    P07342   ILVB_YEAST      58    687             
DBREF  1T9D C   58   687  UNP    P07342   ILVB_YEAST      58    687             
DBREF  1T9D D   58   687  UNP    P07342   ILVB_YEAST      58    687             
SEQADV 1T9D MET A   11  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D HIS A   12  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D HIS A   13  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D HIS A   14  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D HIS A   15  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D HIS A   16  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D HIS A   17  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D SER A   18  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D SER A   19  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D GLY A   20  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D LEU A   21  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D VAL A   22  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D PRO A   23  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D ARG A   24  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D GLY A   25  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D SER A   26  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D GLY A   27  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D MET A   28  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D LYS A   29  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D GLU A   30  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D THR A   31  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D ALA A   32  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D ALA A   33  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D ALA A   34  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D LYS A   35  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D PHE A   36  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D GLU A   37  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D ARG A   38  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D GLN A   39  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D HIS A   40  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D MET A   41  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D ASP A   42  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D SER A   43  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D PRO A   44  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D ASP A   45  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D LEU A   46  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D GLY A   47  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D THR A   48  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D ASP A   49  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D ASP A   50  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D ASP A   51  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D ASP A   52  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D LYS A   53  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D ALA A   54  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D MET A   55  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D GLY A   56  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D SER A   57  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D MET B   11  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D HIS B   12  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D HIS B   13  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D HIS B   14  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D HIS B   15  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D HIS B   16  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D HIS B   17  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D SER B   18  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D SER B   19  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D GLY B   20  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D LEU B   21  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D VAL B   22  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D PRO B   23  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D ARG B   24  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D GLY B   25  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D SER B   26  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D GLY B   27  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D MET B   28  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D LYS B   29  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D GLU B   30  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D THR B   31  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D ALA B   32  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D ALA B   33  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D ALA B   34  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D LYS B   35  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D PHE B   36  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D GLU B   37  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D ARG B   38  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D GLN B   39  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D HIS B   40  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D MET B   41  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D ASP B   42  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D SER B   43  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D PRO B   44  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D ASP B   45  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D LEU B   46  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D GLY B   47  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D THR B   48  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D ASP B   49  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D ASP B   50  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D ASP B   51  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D ASP B   52  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D LYS B   53  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D ALA B   54  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D MET B   55  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D GLY B   56  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D SER B   57  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D MET C   11  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D HIS C   12  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D HIS C   13  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D HIS C   14  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D HIS C   15  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D HIS C   16  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D HIS C   17  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D SER C   18  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D SER C   19  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D GLY C   20  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D LEU C   21  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D VAL C   22  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D PRO C   23  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D ARG C   24  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D GLY C   25  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D SER C   26  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D GLY C   27  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D MET C   28  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D LYS C   29  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D GLU C   30  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D THR C   31  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D ALA C   32  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D ALA C   33  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D ALA C   34  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D LYS C   35  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D PHE C   36  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D GLU C   37  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D ARG C   38  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D GLN C   39  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D HIS C   40  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D MET C   41  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D ASP C   42  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D SER C   43  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D PRO C   44  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D ASP C   45  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D LEU C   46  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D GLY C   47  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D THR C   48  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D ASP C   49  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D ASP C   50  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D ASP C   51  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D ASP C   52  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D LYS C   53  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D ALA C   54  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D MET C   55  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D GLY C   56  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D SER C   57  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D MET D   11  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D HIS D   12  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D HIS D   13  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D HIS D   14  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D HIS D   15  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D HIS D   16  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D HIS D   17  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D SER D   18  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D SER D   19  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D GLY D   20  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D LEU D   21  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D VAL D   22  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D PRO D   23  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D ARG D   24  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D GLY D   25  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D SER D   26  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D GLY D   27  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D MET D   28  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D LYS D   29  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D GLU D   30  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D THR D   31  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D ALA D   32  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D ALA D   33  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D ALA D   34  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D LYS D   35  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D PHE D   36  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D GLU D   37  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D ARG D   38  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D GLN D   39  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D HIS D   40  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D MET D   41  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D ASP D   42  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D SER D   43  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D PRO D   44  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D ASP D   45  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D LEU D   46  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D GLY D   47  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D THR D   48  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D ASP D   49  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D ASP D   50  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D ASP D   51  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D ASP D   52  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D LYS D   53  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D ALA D   54  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D MET D   55  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D GLY D   56  UNP  P07342              CLONING ARTIFACT               
SEQADV 1T9D SER D   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                                                          
SEQRES   1 C  677  MET HIS HIS HIS HIS HIS HIS SER SER GLY LEU VAL PRO          
SEQRES   2 C  677  ARG GLY SER GLY MET LYS GLU THR ALA ALA ALA LYS PHE          
SEQRES   3 C  677  GLU ARG GLN HIS MET ASP SER PRO ASP LEU GLY THR ASP          
SEQRES   4 C  677  ASP ASP ASP LYS ALA MET GLY SER ALA PRO SER PHE ASN          
SEQRES   5 C  677  VAL ASP PRO LEU GLU GLN PRO ALA GLU PRO SER LYS LEU          
SEQRES   6 C  677  ALA LYS LYS LEU ARG ALA GLU PRO ASP MET ASP THR SER          
SEQRES   7 C  677  PHE VAL GLY LEU THR GLY GLY GLN ILE PHE ASN GLU MET          
SEQRES   8 C  677  MET SER ARG GLN ASN VAL ASP THR VAL PHE GLY TYR PRO          
SEQRES   9 C  677  GLY GLY ALA ILE LEU PRO VAL TYR ASP ALA ILE HIS ASN          
SEQRES  10 C  677  SER ASP LYS PHE ASN PHE VAL LEU PRO LYS HIS GLU GLN          
SEQRES  11 C  677  GLY ALA GLY HIS MET ALA GLU GLY TYR ALA ARG ALA SER          
SEQRES  12 C  677  GLY LYS PRO GLY VAL VAL LEU VAL THR SER GLY PRO GLY          
SEQRES  13 C  677  ALA THR ASN VAL VAL THR PRO MET ALA ASP ALA PHE ALA          
SEQRES  14 C  677  ASP GLY ILE PRO MET VAL VAL PHE THR GLY GLN VAL PRO          
SEQRES  15 C  677  THR SER ALA ILE GLY THR ASP ALA PHE GLN GLU ALA ASP          
SEQRES  16 C  677  VAL VAL GLY ILE SER ARG SER CYS THR LYS TRP ASN VAL          
SEQRES  17 C  677  MET VAL LYS SER VAL GLU GLU LEU PRO LEU ARG ILE ASN          
SEQRES  18 C  677  GLU ALA PHE GLU ILE ALA THR SER GLY ARG PRO GLY PRO          
SEQRES  19 C  677  VAL LEU VAL ASP LEU PRO LYS ASP VAL THR ALA ALA ILE          
SEQRES  20 C  677  LEU ARG ASN PRO ILE PRO THR LYS THR THR LEU PRO SER          
SEQRES  21 C  677  ASN ALA LEU ASN GLN LEU THR SER ARG ALA GLN ASP GLU          
SEQRES  22 C  677  PHE VAL MET GLN SER ILE ASN LYS ALA ALA ASP LEU ILE          
SEQRES  23 C  677  ASN LEU ALA LYS LYS PRO VAL LEU TYR VAL GLY ALA GLY          
SEQRES  24 C  677  ILE LEU ASN HIS ALA ASP GLY PRO ARG LEU LEU LYS GLU          
SEQRES  25 C  677  LEU SER ASP ARG ALA GLN ILE PRO VAL THR THR THR LEU          
SEQRES  26 C  677  GLN GLY LEU GLY SER PHE ASP GLN GLU ASP PRO LYS SER          
SEQRES  27 C  677  LEU ASP MET LEU GLY MET HIS GLY CYS ALA THR ALA ASN          
SEQRES  28 C  677  LEU ALA VAL GLN ASN ALA ASP LEU ILE ILE ALA VAL GLY          
SEQRES  29 C  677  ALA ARG PHE ASP ASP ARG VAL THR GLY ASN ILE SER LYS          
SEQRES  30 C  677  PHE ALA PRO GLU ALA ARG ARG ALA ALA ALA GLU GLY ARG          
SEQRES  31 C  677  GLY GLY ILE ILE HIS PHE GLU VAL SER PRO LYS ASN ILE          
SEQRES  32 C  677  ASN LYS VAL VAL GLN THR GLN ILE ALA VAL GLU GLY ASP          
SEQRES  33 C  677  ALA THR THR ASN LEU GLY LYS MET MET SER LYS ILE PHE          
SEQRES  34 C  677  PRO VAL LYS GLU ARG SER GLU TRP PHE ALA GLN ILE ASN          
SEQRES  35 C  677  LYS TRP LYS LYS GLU TYR PRO TYR ALA TYR MET GLU GLU          
SEQRES  36 C  677  THR PRO GLY SER LYS ILE LYS PRO GLN THR VAL ILE LYS          
SEQRES  37 C  677  LYS LEU SER LYS VAL ALA ASN ASP THR GLY ARG HIS VAL          
SEQRES  38 C  677  ILE VAL THR THR GLY VAL GLY GLN HIS GLN MET TRP ALA          
SEQRES  39 C  677  ALA GLN HIS TRP THR TRP ARG ASN PRO HIS THR PHE ILE          
SEQRES  40 C  677  THR SER GLY GLY LEU GLY THR MET GLY TYR GLY LEU PRO          
SEQRES  41 C  677  ALA ALA ILE GLY ALA GLN VAL ALA LYS PRO GLU SER LEU          
SEQRES  42 C  677  VAL ILE ASP ILE ASP GLY ASP ALA SER PHE ASN MET THR          
SEQRES  43 C  677  LEU THR GLU LEU SER SER ALA VAL GLN ALA GLY THR PRO          
SEQRES  44 C  677  VAL LYS ILE LEU ILE LEU ASN ASN GLU GLU GLN GLY MET          
SEQRES  45 C  677  VAL THR GLN TRP GLN SER LEU PHE TYR GLU HIS ARG TYR          
SEQRES  46 C  677  SER HIS THR HIS GLN LEU ASN PRO ASP PHE ILE LYS LEU          
SEQRES  47 C  677  ALA GLU ALA MET GLY LEU LYS GLY LEU ARG VAL LYS LYS          
SEQRES  48 C  677  GLN GLU GLU LEU ASP ALA LYS LEU LYS GLU PHE VAL SER          
SEQRES  49 C  677  THR LYS GLY PRO VAL LEU LEU GLU VAL GLU VAL ASP LYS          
SEQRES  50 C  677  LYS VAL PRO VAL LEU PRO MET VAL ALA GLY GLY SER GLY          
SEQRES  51 C  677  LEU ASP GLU PHE ILE ASN PHE ASP PRO GLU VAL GLU ARG          
SEQRES  52 C  677  GLN GLN THR GLU LEU ARG HIS LYS ARG THR GLY GLY LYS          
SEQRES  53 C  677  HIS                                                          
SEQRES   1 D  677  MET HIS HIS HIS HIS HIS HIS SER SER GLY LEU VAL PRO          
SEQRES   2 D  677  ARG GLY SER GLY MET LYS GLU THR ALA ALA ALA LYS PHE          
SEQRES   3 D  677  GLU ARG GLN HIS MET ASP SER PRO ASP LEU GLY THR ASP          
SEQRES   4 D  677  ASP ASP ASP LYS ALA MET GLY SER ALA PRO SER PHE ASN          
SEQRES   5 D  677  VAL ASP PRO LEU GLU GLN PRO ALA GLU PRO SER LYS LEU          
SEQRES   6 D  677  ALA LYS LYS LEU ARG ALA GLU PRO ASP MET ASP THR SER          
SEQRES   7 D  677  PHE VAL GLY LEU THR GLY GLY GLN ILE PHE ASN GLU MET          
SEQRES   8 D  677  MET SER ARG GLN ASN VAL ASP THR VAL PHE GLY TYR PRO          
SEQRES   9 D  677  GLY GLY ALA ILE LEU PRO VAL TYR ASP ALA ILE HIS ASN          
SEQRES  10 D  677  SER ASP LYS PHE ASN PHE VAL LEU PRO LYS HIS GLU GLN          
SEQRES  11 D  677  GLY ALA GLY HIS MET ALA GLU GLY TYR ALA ARG ALA SER          
SEQRES  12 D  677  GLY LYS PRO GLY VAL VAL LEU VAL THR SER GLY PRO GLY          
SEQRES  13 D  677  ALA THR ASN VAL VAL THR PRO MET ALA ASP ALA PHE ALA          
SEQRES  14 D  677  ASP GLY ILE PRO MET VAL VAL PHE THR GLY GLN VAL PRO          
SEQRES  15 D  677  THR SER ALA ILE GLY THR ASP ALA PHE GLN GLU ALA ASP          
SEQRES  16 D  677  VAL VAL GLY ILE SER ARG SER CYS THR LYS TRP ASN VAL          
SEQRES  17 D  677  MET VAL LYS SER VAL GLU GLU LEU PRO LEU ARG ILE ASN          
SEQRES  18 D  677  GLU ALA PHE GLU ILE ALA THR SER GLY ARG PRO GLY PRO          
SEQRES  19 D  677  VAL LEU VAL ASP LEU PRO LYS ASP VAL THR ALA ALA ILE          
SEQRES  20 D  677  LEU ARG ASN PRO ILE PRO THR LYS THR THR LEU PRO SER          
SEQRES  21 D  677  ASN ALA LEU ASN GLN LEU THR SER ARG ALA GLN ASP GLU          
SEQRES  22 D  677  PHE VAL MET GLN SER ILE ASN LYS ALA ALA ASP LEU ILE          
SEQRES  23 D  677  ASN LEU ALA LYS LYS PRO VAL LEU TYR VAL GLY ALA GLY          
SEQRES  24 D  677  ILE LEU ASN HIS ALA ASP GLY PRO ARG LEU LEU LYS GLU          
SEQRES  25 D  677  LEU SER ASP ARG ALA GLN ILE PRO VAL THR THR THR LEU          
SEQRES  26 D  677  GLN GLY LEU GLY SER PHE ASP GLN GLU ASP PRO LYS SER          
SEQRES  27 D  677  LEU ASP MET LEU GLY MET HIS GLY CYS ALA THR ALA ASN          
SEQRES  28 D  677  LEU ALA VAL GLN ASN ALA ASP LEU ILE ILE ALA VAL GLY          
SEQRES  29 D  677  ALA ARG PHE ASP ASP ARG VAL THR GLY ASN ILE SER LYS          
SEQRES  30 D  677  PHE ALA PRO GLU ALA ARG ARG ALA ALA ALA GLU GLY ARG          
SEQRES  31 D  677  GLY GLY ILE ILE HIS PHE GLU VAL SER PRO LYS ASN ILE          
SEQRES  32 D  677  ASN LYS VAL VAL GLN THR GLN ILE ALA VAL GLU GLY ASP          
SEQRES  33 D  677  ALA THR THR ASN LEU GLY LYS MET MET SER LYS ILE PHE          
SEQRES  34 D  677  PRO VAL LYS GLU ARG SER GLU TRP PHE ALA GLN ILE ASN          
SEQRES  35 D  677  LYS TRP LYS LYS GLU TYR PRO TYR ALA TYR MET GLU GLU          
SEQRES  36 D  677  THR PRO GLY SER LYS ILE LYS PRO GLN THR VAL ILE LYS          
SEQRES  37 D  677  LYS LEU SER LYS VAL ALA ASN ASP THR GLY ARG HIS VAL          
SEQRES  38 D  677  ILE VAL THR THR GLY VAL GLY GLN HIS GLN MET TRP ALA          
SEQRES  39 D  677  ALA GLN HIS TRP THR TRP ARG ASN PRO HIS THR PHE ILE          
SEQRES  40 D  677  THR SER GLY GLY LEU GLY THR MET GLY TYR GLY LEU PRO          
SEQRES  41 D  677  ALA ALA ILE GLY ALA GLN VAL ALA LYS PRO GLU SER LEU          
SEQRES  42 D  677  VAL ILE ASP ILE ASP GLY ASP ALA SER PHE ASN MET THR          
SEQRES  43 D  677  LEU THR GLU LEU SER SER ALA VAL GLN ALA GLY THR PRO          
SEQRES  44 D  677  VAL LYS ILE LEU ILE LEU ASN ASN GLU GLU GLN GLY MET          
SEQRES  45 D  677  VAL THR GLN TRP GLN SER LEU PHE TYR GLU HIS ARG TYR          
SEQRES  46 D  677  SER HIS THR HIS GLN LEU ASN PRO ASP PHE ILE LYS LEU          
SEQRES  47 D  677  ALA GLU ALA MET GLY LEU LYS GLY LEU ARG VAL LYS LYS          
SEQRES  48 D  677  GLN GLU GLU LEU ASP ALA LYS LEU LYS GLU PHE VAL SER          
SEQRES  49 D  677  THR LYS GLY PRO VAL LEU LEU GLU VAL GLU VAL ASP LYS          
SEQRES  50 D  677  LYS VAL PRO VAL LEU PRO MET VAL ALA GLY GLY SER GLY          
SEQRES  51 D  677  LEU ASP GLU PHE ILE ASN PHE ASP PRO GLU VAL GLU ARG          
SEQRES  52 D  677  GLN GLN THR GLU LEU ARG HIS LYS ARG THR GLY GLY LYS          
SEQRES  53 D  677  HIS                                                          
HET      K  A1696       1                                                       
HET     MG  A1699       1                                                       
HET    1MM  A 695      26                                                       
HET    FAD  A 701      53                                                       
HET    PYD  A 703       9                                                       
HET    P25  A1698      14                                                       
HET      K  B 696       1                                                       
HET     MG  B 699       1                                                       
HET    P25  B 698      14                                                       
HET    1MM  B1695      26                                                       
HET    FAD  B1701      53                                                       
HET    PYD  B1703       9                                                       
HET      K  C3696       1                                                       
HET     MG  C3699       1                                                       
HET    1MM  C2695      26                                                       
HET    FAD  C2701      53                                                       
HET    PYD  C2703       9                                                       
HET    1MM  C3695      26                                                       
HET    P22  C3702      11                                                       
HET      K  D2696       1                                                       
HET     MG  D2699       1                                                       
HET    P22  D2702      11                                                       
HET    FAD  D3701      53                                                       
HET    PYD  D3703       9                                                       
HETNAM       K POTASSIUM ION                                                    
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     1MM METHYL 2-[({[(4-METHOXY-6-METHYL-1,3,5-TRIAZIN-2-YL)             
HETNAM   2 1MM  AMINO]CARBONYL}AMINO)SULFONYL]BENZOATE                          
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     PYD 2,5-DIMETHYL-PYRIMIDIN-4-YLAMINE                                 
HETNAM     P25 PENTYL TRIHYDROGEN DIPHOSPHATE                                   
HETNAM     P22 ETHYL DIHYDROGEN DIPHOSPHATE                                     
HETSYN     1MM METSULFURON METHYL                                               
FORMUL   5    K    4(K 1+)                                                      
FORMUL   6   MG    4(MG 2+)                                                     
FORMUL   7  1MM    4(C14 H15 N5 O6 S)                                           
FORMUL   8  FAD    4(C27 H33 N9 O15 P2)                                         
FORMUL   9  PYD    4(C6 H9 N3)                                                  
FORMUL  10  P25    2(C5 H14 O7 P2)                                              
FORMUL  23  P22    2(C2 H8 O7 P2)                                               
FORMUL  29  HOH   *2176(H2 O)                                                   
HELIX    1   1 THR A   93  GLN A  105  1                                  13    
HELIX    2   2 ILE A  118  ILE A  125  1                                   8    
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 PRO A  263  LEU A  268  1                                   6    
HELIX   12  12 SER A  278  LEU A  298  1                                  21    
HELIX   13  13 ALA A  308  HIS A  313  5                                   6    
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  ASP A  486  1                                  15    
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 PHE B  284  ALA B  299  1                                  16    
HELIX   45  45 ALA B  308  HIS B  313  5                                   6    
HELIX   46  46 ASP B  315  ALA B  327  1                                  13    
HELIX   47  47 LEU B  335  LEU B  338  5                                   4    
HELIX   48  48 CYS B  357  ALA B  367  1                                  11    
HELIX   49  49 ASN B  384  PHE B  388  5                                   5    
HELIX   50  50 ALA B  389  GLU B  398  1                                  10    
HELIX   51  51 SER B  409  ILE B  413  5                                   5    
HELIX   52  52 ASP B  426  MET B  435  1                                  10    
HELIX   53  53 SER B  436  ILE B  438  5                                   3    
HELIX   54  54 ARG B  444  TYR B  458  1                                  15    
HELIX   55  55 LYS B  472  ASP B  486  1                                  15    
HELIX   56  56 GLY B  498  TRP B  508  1                                  11    
HELIX   57  57 TYR B  527  LYS B  539  1                                  13    
HELIX   58  58 ASP B  550  LEU B  557  1                                   8    
HELIX   59  59 GLU B  559  GLY B  567  1                                   9    
HELIX   60  60 GLN B  580  TYR B  591  1                                  12    
HELIX   61  61 ASP B  604  GLY B  613  1                                  10    
HELIX   62  62 LYS B  621  THR B  635  1                                  15    
HELIX   63  63 ASP B  668  GLY B  684  1                                  17    
HELIX   64  64 THR C   93  GLN C  105  1                                  13    
HELIX   65  65 GLY C  115  ALA C  117  5                                   3    
HELIX   66  66 ILE C  118  ILE C  125  1                                   8    
HELIX   67  67 HIS C  138  GLY C  154  1                                  17    
HELIX   68  68 GLY C  164  ASN C  169  1                                   6    
HELIX   69  69 VAL C  170  ASP C  180  1                                  11    
HELIX   70  70 ASP C  205  SER C  210  1                                   6    
HELIX   71  71 ARG C  211  THR C  214  5                                   4    
HELIX   72  72 SER C  222  GLU C  224  5                                   3    
HELIX   73  73 GLU C  225  SER C  239  1                                  15    
HELIX   74  74 LYS C  251  ALA C  256  1                                   6    
HELIX   75  75 ALA C  292  ASN C  297  1                                   6    
HELIX   76  76 ALA C  308  HIS C  313  5                                   6    
HELIX   77  77 ASP C  315  ALA C  327  1                                  13    
HELIX   78  78 CYS C  357  ASN C  366  1                                  10    
HELIX   79  79 ASN C  384  PHE C  388  5                                   5    
HELIX   80  80 ALA C  389  ALA C  396  1                                   8    
HELIX   81  81 SER C  409  ILE C  413  5                                   5    
HELIX   82  82 ASP C  426  MET C  434  1                                   9    
HELIX   83  83 MET C  435  ILE C  438  5                                   4    
HELIX   84  84 ARG C  444  TYR C  458  1                                  15    
HELIX   85  85 LYS C  472  ASP C  486  1                                  15    
HELIX   86  86 GLY C  498  HIS C  507  1                                  10    
HELIX   87  87 TYR C  527  LYS C  539  1                                  13    
HELIX   88  88 ASP C  550  LEU C  557  1                                   8    
HELIX   89  89 GLU C  559  GLY C  567  1                                   9    
HELIX   90  90 GLN C  580  PHE C  590  1                                  11    
HELIX   91  91 ASP C  604  GLY C  613  1                                  10    
HELIX   92  92 LYS C  621  GLU C  623  5                                   3    
HELIX   93  93 GLU C  624  THR C  635  1                                  12    
HELIX   94  94 ASP C  668  GLY C  684  1                                  17    
HELIX   95  95 THR D   93  GLN D  105  1                                  13    
HELIX   96  96 ILE D  118  ILE D  125  1                                   8    
HELIX   97  97 HIS D  138  GLY D  154  1                                  17    
HELIX   98  98 GLY D  164  ASN D  169  1                                   6    
HELIX   99  99 VAL D  170  GLY D  181  1                                  12    
HELIX  100 100 ASP D  205  SER D  210  1                                   6    
HELIX  101 101 ARG D  211  THR D  214  5                                   4    
HELIX  102 102 SER D  222  GLU D  224  5                                   3    
HELIX  103 103 GLU D  225  SER D  239  1                                  15    
HELIX  104 104 LYS D  251  ALA D  256  1                                   6    
HELIX  105 105 PRO D  263  THR D  267  5                                   5    
HELIX  106 106 SER D  278  ALA D  299  1                                  22    
HELIX  107 107 ALA D  308  ASN D  312  5                                   5    
HELIX  108 108 ASP D  315  ALA D  327  1                                  13    
HELIX  109 109 LEU D  335  LEU D  338  5                                   4    
HELIX  110 110 CYS D  357  ALA D  367  1                                  11    
HELIX  111 111 ASP D  378  GLY D  383  1                                   6    
HELIX  112 112 ASN D  384  PHE D  388  5                                   5    
HELIX  113 113 ALA D  389  GLU D  398  1                                  10    
HELIX  114 114 SER D  409  ILE D  413  5                                   5    
HELIX  115 115 ASP D  426  MET D  435  1                                  10    
HELIX  116 116 SER D  436  ILE D  438  5                                   3    
HELIX  117 117 ARG D  444  TYR D  458  1                                  15    
HELIX  118 118 LYS D  472  ASP D  486  1                                  15    
HELIX  119 119 GLY D  498  TRP D  508  1                                  11    
HELIX  120 120 TYR D  527  LYS D  539  1                                  13    
HELIX  121 121 ASP D  550  LEU D  557  1                                   8    
HELIX  122 122 GLU D  559  GLY D  567  1                                   9    
HELIX  123 123 GLN D  580  TYR D  591  1                                  12    
HELIX  124 124 ASP D  604  GLY D  613  1                                  10    
HELIX  125 125 GLU D  624  THR D  635  1                                  12    
HELIX  126 126 ASP D  668  THR D  683  1                                  16    
SHEET    1   A 6 ASN A 132  VAL A 134  0                                        
SHEET    2   A 6 THR A 109  TYR A 113  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  VAL A 423   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  GLU A 642           
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  LEU B 304   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 547   N  THR B 494           
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           
SHEET    1   G 6 ASN C 132  VAL C 134  0                                        
SHEET    2   G 6 THR C 109  GLY C 112  1  N  VAL C 110   O  ASN C 132           
SHEET    3   G 6 GLY C 157  VAL C 161  1  O  VAL C 158   N  PHE C 111           
SHEET    4   G 6 MET C 184  GLN C 190  1  O  VAL C 185   N  GLY C 157           
SHEET    5   G 6 PRO C 244  PRO C 250  1  O  LEU C 249   N  THR C 188           
SHEET    6   G 6 TRP C 216  MET C 219  1  N  VAL C 218   O  ASP C 248           
SHEET    1   H 6 SER C 348  MET C 351  0                                        
SHEET    2   H 6 VAL C 331  THR C 333  1  N  VAL C 331   O  LEU C 349           
SHEET    3   H 6 PRO C 302  VAL C 306  1  N  LEU C 304   O  THR C 332           
SHEET    4   H 6 LEU C 369  VAL C 373  1  O  ILE C 371   N  VAL C 303           
SHEET    5   H 6 GLY C 402  GLU C 407  1  O  PHE C 406   N  ALA C 372           
SHEET    6   H 6 ILE C 421  GLU C 424  1  O  VAL C 423   N  HIS C 405           
SHEET    1   I 6 PHE C 516  ILE C 517  0                                        
SHEET    2   I 6 VAL C 491  THR C 495  1  N  VAL C 493   O  ILE C 517           
SHEET    3   I 6 LEU C 543  GLY C 549  1  O  ILE C 545   N  ILE C 492           
SHEET    4   I 6 LYS C 571  ASN C 576  1  O  LEU C 573   N  ASP C 548           
SHEET    5   I 6 VAL C 639  GLU C 644  1  O  LEU C 641   N  ILE C 572           
SHEET    6   I 6 LYS C 615  VAL C 619  1  N  LEU C 617   O  GLU C 642           
SHEET    1   J 6 ASN D 132  VAL D 134  0                                        
SHEET    2   J 6 THR D 109  TYR D 113  1  N  VAL D 110   O  VAL D 134           
SHEET    3   J 6 GLY D 157  VAL D 161  1  O  VAL D 158   N  PHE D 111           
SHEET    4   J 6 MET D 184  GLN D 190  1  O  PHE D 187   N  VAL D 159           
SHEET    5   J 6 PRO D 244  PRO D 250  1  O  LEU D 249   N  THR D 188           
SHEET    6   J 6 TRP D 216  MET D 219  1  N  VAL D 218   O  ASP D 248           
SHEET    1   K 6 SER D 348  MET D 351  0                                        
SHEET    2   K 6 VAL D 331  THR D 333  1  N  VAL D 331   O  LEU D 349           
SHEET    3   K 6 PRO D 302  VAL D 306  1  N  LEU D 304   O  THR D 332           
SHEET    4   K 6 LEU D 369  VAL D 373  1  O  ILE D 371   N  VAL D 303           
SHEET    5   K 6 GLY D 402  GLU D 407  1  O  GLY D 402   N  ILE D 370           
SHEET    6   K 6 ILE D 421  GLU D 424  1  O  ILE D 421   N  HIS D 405           
SHEET    1   L 6 PHE D 516  ILE D 517  0                                        
SHEET    2   L 6 VAL D 491  THR D 495  1  N  VAL D 493   O  ILE D 517           
SHEET    3   L 6 LEU D 543  GLY D 549  1  O  ILE D 545   N  ILE D 492           
SHEET    4   L 6 LYS D 571  ASN D 576  1  O  LEU D 573   N  ASP D 548           
SHEET    5   L 6 VAL D 639  GLU D 644  1  O  LEU D 641   N  ILE D 572           
SHEET    6   L 6 LYS D 615  VAL D 619  1  N  LEU D 617   O  GLU D 642           
LINK         K     K A1696                 OD2 ASP A 350     1555   1555  2.90  
LINK         K     K A1696                 O   HOH A4043     1555   1555  2.79  
LINK         K     K A1696                 OE1 GLN A 343     1555   1555  2.70  
LINK         K     K A1696                 O   GLN A 506     1555   1555  2.66  
LINK         K     K A1696                 O   HOH A5543     1555   1555  3.08  
LINK         K     K A1696                 O   HOH A4595     1555   1555  3.44  
LINK         K     K A1696                 O   TRP A 508     1555   1555  2.61  
LINK         O3B P25 A1698                MG    MG A1699     1555   1555  2.02  
LINK        MG    MG A1699                 OD1 ASP A 550     1555   1555  2.04  
LINK        MG    MG A1699                 OD1 ASN A 577     1555   1555  2.16  
LINK        MG    MG A1699                 O   GLU A 579     1555   1555  2.20  
LINK        MG    MG A1699                 O1A P25 A1698     1555   1555  2.09  
LINK        MG    MG A1699                 O   HOH A4061     1555   1555  2.09  
LINK         K     K B 696                 OE1 GLN B 343     1555   1555  2.65  
LINK         K     K B 696                 NE2 GLN B 343     1555   1555  3.67  
LINK         K     K B 696                 O   TRP B 508     1555   1555  2.64  
LINK         K     K B 696                 O   HOH B4274     1555   1555  2.76  
LINK         K     K B 696                 OD2 ASP B 350     1555   1555  2.89  
LINK         K     K B 696                 O   GLN B 506     1555   1555  2.68  
LINK         K     K B 696                 O   HOH B5858     1555   1555  2.89  
LINK        MG    MG B 699                 O   GLU B 579     1555   1555  2.13  
LINK        MG    MG B 699                 OD1 ASN B 577     1555   1555  2.16  
LINK        MG    MG B 699                 OD1 ASP B 550     1555   1555  2.17  
LINK        MG    MG B 699                 O   HOH B4287     1555   1555  2.27  
LINK        MG    MG B 699                 O3B P25 B 698     1555   1555  2.08  
LINK        MG    MG B 699                 O1A P25 B 698     1555   1555  2.06  
LINK         K     K C3696                 OE1 GLN C 343     1555   1555  2.78  
LINK         K     K C3696                 O   TRP C 508     1555   1555  2.67  
LINK         K     K C3696                 NE2 GLN C 343     1555   1555  3.33  
LINK         K     K C3696                 O   HOH C5037     1555   1555  2.72  
LINK         K     K C3696                 O   GLN C 506     1555   1555  2.67  
LINK         K     K C3696                 OD2 ASP C 350     1555   1555  3.29  
LINK        MG    MG C3699                 O   GLU C 579     1555   1555  2.34  
LINK        MG    MG C3699                 O1A P22 C3702     1555   1555  2.14  
LINK        MG    MG C3699                 O3B P22 C3702     1555   1555  2.02  
LINK        MG    MG C3699                 O   HOH C5774     1555   1555  2.13  
LINK        MG    MG C3699                 O3A P22 C3702     1555   1555  3.12  
LINK        MG    MG C3699                 OD1 ASP C 550     1555   1555  2.31  
LINK        MG    MG C3699                 OD1 ASN C 577     1555   1555  2.30  
LINK        MG    MG C3699                 ND2 ASN C 577     1555   1555  3.06  
LINK         K     K D2696                 OD2 ASP D 350     1555   1555  2.93  
LINK         K     K D2696                 O   HOH D4801     1555   1555  2.71  
LINK         K     K D2696                 O   GLN D 506     1555   1555  2.72  
LINK         K     K D2696                 O   HOH D6040     1555   1555  3.37  
LINK         K     K D2696                 O   HOH D5353     1555   1555  3.04  
LINK         K     K D2696                 O   TRP D 508     1555   1555  2.63  
LINK         K     K D2696                 OE1 GLN D 343     1555   1555  2.77  
LINK        MG    MG D2699                 O   GLU D 579     1555   1555  2.07  
LINK        MG    MG D2699                 O1A P22 D2702     1555   1555  2.14  
LINK        MG    MG D2699                 O3B P22 D2702     1555   1555  1.99  
LINK        MG    MG D2699                 O   HOH D4819     1555   1555  2.24  
LINK        MG    MG D2699                 OD1 ASN D 577     1555   1555  2.22  
LINK        MG    MG D2699                 OD1 ASP D 550     1555   1555  2.25  
CISPEP   1 LEU A  652    PRO A  653          0        -0.06                     
CISPEP   2 LEU B  652    PRO B  653          0        -0.14                     
CISPEP   3 LEU C  652    PRO C  653          0         0.05                     
CISPEP   4 LEU D  652    PRO D  653          0        -0.04                     
SITE     1 AC1  6 GLN B 343  ASP B 350  GLN B 506  TRP B 508                    
SITE     2 AC1  6 HOH B4274  HOH B5858                                          
SITE     1 AC2  5 ASP B 550  ASN B 577  GLU B 579  P25 B 698                    
SITE     2 AC2  5 HOH B4287                                                     
SITE     1 AC3  6 GLN A 343  ASP A 350  GLN A 506  TRP A 508                    
SITE     2 AC3  6 HOH A4043  HOH A5543                                          
SITE     1 AC4  5 ASP A 550  ASN A 577  GLU A 579  P25 A1698                    
SITE     2 AC4  5 HOH A4061                                                     
SITE     1 AC5  6 GLN D 343  ASP D 350  GLN D 506  TRP D 508                    
SITE     2 AC5  6 HOH D4801  HOH D5353                                          
SITE     1 AC6  5 ASP D 550  ASN D 577  GLU D 579  P22 D2702                    
SITE     2 AC6  5 HOH D4819                                                     
SITE     1 AC7  5 GLN C 343  ASP C 350  GLN C 506  TRP C 508                    
SITE     2 AC7  5 HOH C5037                                                     
SITE     1 AC8  5 ASP C 550  ASN C 577  GLU C 579  P22 C3702                    
SITE     2 AC8  5 HOH C5774                                                     
SITE     1 AC9 15 MET A 354  ASP A 379  ARG A 380  MET A 582                    
SITE     2 AC9 15 TRP A 586  FAD A 701  HOH A4173  GLY B 116                    
SITE     3 AC9 15 ALA B 117  VAL B 191  PRO B 192  PHE B 201                    
SITE     4 AC9 15 GLN B 202  LYS B 251  HOH B4143                               
SITE     1 BC1 15 VAL B 497  GLY B 498  GLN B 499  HIS B 500                    
SITE     2 BC1 15 GLY B 549  ASP B 550  ALA B 551  SER B 552                    
SITE     3 BC1 15 ASN B 577  GLU B 579  GLN B 580  GLY B 581                    
SITE     4 BC1 15 MET B 582   MG B 699  HOH B4287                               
SITE     1 BC2 39 ASP A 180  ARG A 241  GLY A 307  ALA A 308                    
SITE     2 BC2 39 GLY A 309  ASN A 312  THR A 334  LEU A 335                    
SITE     3 BC2 39 GLN A 336  LEU A 352  GLY A 353  MET A 354                    
SITE     4 BC2 39 HIS A 355  GLY A 374  ALA A 375  ARG A 376                    
SITE     5 BC2 39 ASP A 378  ARG A 380  VAL A 381  PHE A 406                    
SITE     6 BC2 39 GLU A 407  VAL A 408  ASN A 412  GLY A 425                    
SITE     7 BC2 39 ASP A 426  ALA A 427  VAL A 497  GLN A 501                    
SITE     8 BC2 39 MET A 502  GLY A 520  GLY A 521  1MM A 695                    
SITE     9 BC2 39 HOH A4015  HOH A4016  HOH A4037  HOH A4160                    
SITE    10 BC2 39 HOH A5915  HOH A6042  PHE B 201                               
SITE     1 BC3  9 GLY A 115  GLU A 139  PRO A 165  ASN A 169                    
SITE     2 BC3  9 GLN A 202  GLY B 523  MET B 525  MET B 555                    
SITE     3 BC3  9 GLN B 580                                                     
SITE     1 BC4 15 GLY A 116  ALA A 117  VAL A 191  PRO A 192                    
SITE     2 BC4 15 ALA A 200  PHE A 201  GLN A 202  LYS A 251                    
SITE     3 BC4 15 ASP B 379  ARG B 380  MET B 582  VAL B 583                    
SITE     4 BC4 15 TRP B 586  FAD B1701  HOH B5600                               
SITE     1 BC5 16 VAL A 497  GLY A 498  GLN A 499  HIS A 500                    
SITE     2 BC5 16 MET A 525  GLY A 549  ASP A 550  ALA A 551                    
SITE     3 BC5 16 SER A 552  ASN A 577  GLU A 579  GLN A 580                    
SITE     4 BC5 16 GLY A 581  MET A 582   MG A1699  HOH A4061                    
SITE     1 BC6 39 PHE A 201  ASP B 180  ARG B 241  GLY B 307                    
SITE     2 BC6 39 ALA B 308  GLY B 309  ASN B 312  THR B 334                    
SITE     3 BC6 39 LEU B 335  GLN B 336  LEU B 352  MET B 354                    
SITE     4 BC6 39 HIS B 355  GLY B 374  ALA B 375  ARG B 376                    
SITE     5 BC6 39 ASP B 378  ARG B 380  VAL B 381  PHE B 406                    
SITE     6 BC6 39 GLU B 407  VAL B 408  ASN B 412  GLY B 425                    
SITE     7 BC6 39 ASP B 426  ALA B 427  GLN B 501  MET B 502                    
SITE     8 BC6 39 SER B 519  GLY B 520  GLY B 521  MET B 582                    
SITE     9 BC6 39 1MM B1695  HOH B4248  HOH B4270  HOH B4302                    
SITE    10 BC6 39 HOH B4615  HOH B5940  HOH B5956                               
SITE     1 BC7  9 GLY A 523  MET A 525  MET A 555  PRO B 114                    
SITE     2 BC7  9 GLY B 115  GLU B 139  PRO B 165  ASN B 169                    
SITE     3 BC7  9 GLN B 202                                                     
SITE     1 BC8 14 GLY C 116  ALA C 117  VAL C 191  PRO C 192                    
SITE     2 BC8 14 PHE C 201  LYS C 251  HOH C4890  HOH C4944                    
SITE     3 BC8 14 HOH C5740  MET D 354  ASP D 379  ARG D 380                    
SITE     4 BC8 14 TRP D 586  FAD D3701                                          
SITE     1 BC9 37 ARG C 241  GLY C 307  ALA C 308  GLY C 309                    
SITE     2 BC9 37 ASN C 312  THR C 334  LEU C 335  LEU C 352                    
SITE     3 BC9 37 GLY C 353  MET C 354  HIS C 355  GLY C 374                    
SITE     4 BC9 37 ALA C 375  ARG C 376  ASP C 378  ARG C 380                    
SITE     5 BC9 37 VAL C 381  PHE C 406  GLU C 407  VAL C 408                    
SITE     6 BC9 37 ASN C 412  GLY C 425  ASP C 426  ALA C 427                    
SITE     7 BC9 37 GLN C 501  MET C 502  SER C 519  GLY C 520                    
SITE     8 BC9 37 GLY C 521  1MM C3695  HOH C5008  HOH C5017                    
SITE     9 BC9 37 HOH C5034  HOH C5067  HOH C5764  HOH C6001                    
SITE    10 BC9 37 PHE D 201                                                     
SITE     1 CC1 16 VAL D 497  GLY D 498  GLN D 499  HIS D 500                    
SITE     2 CC1 16 MET D 525  GLY D 549  ASP D 550  ALA D 551                    
SITE     3 CC1 16 SER D 552  ASN D 577  GLU D 579  GLN D 580                    
SITE     4 CC1 16 GLY D 581  MET D 582   MG D2699  HOH D4819                    
SITE     1 CC2  8 PRO C 114  GLY C 115  GLU C 139  PRO C 165                    
SITE     2 CC2  8 ASN C 169  GLN C 202  GLY D 523  MET D 525                    
SITE     1 CC3 16 MET C 354  ASP C 379  ARG C 380  MET C 582                    
SITE     2 CC3 16 VAL C 583  TRP C 586  FAD C2701  HOH C4789                    
SITE     3 CC3 16 HOH C5408  GLY D 116  ALA D 117  VAL D 191                    
SITE     4 CC3 16 PRO D 192  PHE D 201  GLN D 202  LYS D 251                    
SITE     1 CC4 39 PHE C 201  1MM C2695  ASP D 180  ARG D 241                    
SITE     2 CC4 39 GLY D 307  ALA D 308  GLY D 309  ASN D 312                    
SITE     3 CC4 39 THR D 334  LEU D 335  GLN D 336  LEU D 352                    
SITE     4 CC4 39 GLY D 353  MET D 354  HIS D 355  GLY D 374                    
SITE     5 CC4 39 ALA D 375  ARG D 376  ASP D 378  ARG D 380                    
SITE     6 CC4 39 VAL D 381  PHE D 406  GLU D 407  VAL D 408                    
SITE     7 CC4 39 ASN D 412  GLY D 425  ASP D 426  ALA D 427                    
SITE     8 CC4 39 GLN D 501  MET D 502  SER D 519  GLY D 520                    
SITE     9 CC4 39 GLY D 521  HOH D4774  HOH D4775  HOH D4795                    
SITE    10 CC4 39 HOH D4873  HOH D4926  HOH D5146                               
SITE     1 CC5 16 VAL C 497  GLY C 498  GLN C 499  HIS C 500                    
SITE     2 CC5 16 MET C 525  GLY C 549  ASP C 550  ALA C 551                    
SITE     3 CC5 16 SER C 552  ASN C 577  GLU C 579  GLN C 580                    
SITE     4 CC5 16 GLY C 581  MET C 582   MG C3699  HOH C5774                    
SITE     1 CC6  9 VAL C 497  GLY C 523  MET C 525  PRO D 114                    
SITE     2 CC6  9 GLY D 115  GLU D 139  PRO D 165  ASN D 169                    
SITE     3 CC6  9 GLN D 202                                                     
CRYST1  218.347  218.347  361.530  90.00  90.00  90.00 I 4 2 2      64          
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      0.004580  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004580  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002766        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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