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Database: PDB
Entry: 5IMS
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Original site: 5IMS 
HEADER    TRANSFERASE                             06-MAR-16   5IMS              
TITLE     SACCHAROMYCES CEREVISIAE ACETOHYDROXYACID SYNTHASE                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACETOLACTATE SYNTHASE CATALYTIC SUBUNIT, MITOCHONDRIAL;    
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 58-687;                                       
COMPND   5 SYNONYM: ACETOHYDROXY-ACID SYNTHASE CATALYTIC SUBUNIT,ALS;           
COMPND   6 EC: 2.2.1.6;                                                         
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /  
SOURCE   3 S288C);                                                              
SOURCE   4 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE   5 ORGANISM_TAXID: 559292;                                              
SOURCE   6 STRAIN: ATCC 204508 / S288C;                                         
SOURCE   7 GENE: ILV2, SMR1, YMR108W, YM9718.07;                                
SOURCE   8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   9 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  10 EXPRESSION_SYSTEM_STRAIN: BL21                                       
KEYWDS    AHAS, FAD, THDP, O2, TRANSFERASE                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.W.GUDDAT,T.LONHIENNE                                                
REVDAT   1   15-FEB-17 5IMS    0                                                
JRNL        AUTH   L.W.GUDDAT,T.LONHIENNE                                       
JRNL        TITL   A HIDDEN REDOX CYCLE CONTROLS CATALYSIS IN ACETOHYDROXYACID  
JRNL        TITL 2 SYNTHASE                                                     
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.98 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.98                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.18                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 130573                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.166                           
REMARK   3   R VALUE            (WORKING SET) : 0.166                           
REMARK   3   FREE R VALUE                     : 0.193                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.530                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2000                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 42.1853 -  4.7807    0.96     9350   146  0.1553 0.1799        
REMARK   3     2  4.7807 -  3.7954    0.98     9223   143  0.1354 0.1424        
REMARK   3     3  3.7954 -  3.3158    0.99     9203   143  0.1516 0.1763        
REMARK   3     4  3.3158 -  3.0128    0.99     9202   144  0.1619 0.1719        
REMARK   3     5  3.0128 -  2.7969    0.99     9192   143  0.1712 0.2287        
REMARK   3     6  2.7969 -  2.6320    0.99     9202   143  0.1719 0.2059        
REMARK   3     7  2.6320 -  2.5002    1.00     9204   142  0.1691 0.2103        
REMARK   3     8  2.5002 -  2.3914    1.00     9163   143  0.1781 0.2395        
REMARK   3     9  2.3914 -  2.2993    1.00     9202   143  0.1832 0.2128        
REMARK   3    10  2.2993 -  2.2200    1.00     9175   143  0.1864 0.2282        
REMARK   3    11  2.2200 -  2.1506    1.00     9201   143  0.1957 0.2210        
REMARK   3    12  2.1506 -  2.0891    1.00     9135   143  0.2070 0.2381        
REMARK   3    13  2.0891 -  2.0341    1.00     9163   142  0.2186 0.2427        
REMARK   3    14  2.0341 -  1.9845    0.97     8958   139  0.2379 0.2609        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.170            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.740           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.016           8802                                  
REMARK   3   ANGLE     :  1.485          11959                                  
REMARK   3   CHIRALITY :  0.085           1348                                  
REMARK   3   PLANARITY :  0.007           1535                                  
REMARK   3   DIHEDRAL  : 16.662           3239                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5IMS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-MAR-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000219081.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-MAR-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.7-5.9                            
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : AUSTRALIAN SYNCHROTRON             
REMARK 200  BEAMLINE                       : MX1                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9537                             
REMARK 200  MONOCHROMATOR                  : SI(III)                            
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 130638                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.980                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.840                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 5.400                              
REMARK 200  R MERGE                    (I) : 0.07500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.30                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.64500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: 1JSC                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.10                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.16                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 34 MG/ML ENZYME INCUBATED WITH 1.4 MM    
REMARK 280  THDP, 0.5 MM FAD, 14 MM MGCL2, AND 4.5 MM DTT. CRYSTALS WERE        
REMARK 280  OBTAINED MY MIXING EQUAL VOLUMES (1 UL) OF WELL SOLUTION (14 %      
REMARK 280  PEG 4000, 0.25-0.3 M POTASSIUM PHOSPHATE, 0.2 M AMMONIUM            
REMARK 280  ACETATE.) AND ENZYME SOLUTION, PH 5.8, VAPOR DIFFUSION, HANGING     
REMARK 280  DROP, TEMPERATURE 273K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       47.84150            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       90.00250            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       55.09000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       90.00250            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       47.84150            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       55.09000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 12310 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 39660 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -74.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A    11                                                      
REMARK 465     HIS A    12                                                      
REMARK 465     HIS A    13                                                      
REMARK 465     HIS A    14                                                      
REMARK 465     HIS A    15                                                      
REMARK 465     HIS A    16                                                      
REMARK 465     HIS A    17                                                      
REMARK 465     SER A    18                                                      
REMARK 465     SER A    19                                                      
REMARK 465     GLY A    20                                                      
REMARK 465     LEU A    21                                                      
REMARK 465     VAL A    22                                                      
REMARK 465     PRO A    23                                                      
REMARK 465     ARG A    24                                                      
REMARK 465     GLY A    25                                                      
REMARK 465     SER A    26                                                      
REMARK 465     GLY A    27                                                      
REMARK 465     MET A    28                                                      
REMARK 465     LYS A    29                                                      
REMARK 465     GLU A    30                                                      
REMARK 465     THR A    31                                                      
REMARK 465     ALA A    32                                                      
REMARK 465     ALA A    33                                                      
REMARK 465     ALA A    34                                                      
REMARK 465     LYS A    35                                                      
REMARK 465     PHE A    36                                                      
REMARK 465     GLU A    37                                                      
REMARK 465     ARG A    38                                                      
REMARK 465     GLN A    39                                                      
REMARK 465     HIS A    40                                                      
REMARK 465     MET A    41                                                      
REMARK 465     ASP A    42                                                      
REMARK 465     SER A    43                                                      
REMARK 465     PRO A    44                                                      
REMARK 465     ASP A    45                                                      
REMARK 465     LEU A    46                                                      
REMARK 465     GLY A    47                                                      
REMARK 465     THR A    48                                                      
REMARK 465     ASP A    49                                                      
REMARK 465     ASP A    50                                                      
REMARK 465     ASP A    51                                                      
REMARK 465     ASP A    52                                                      
REMARK 465     LYS A    53                                                      
REMARK 465     ALA A    54                                                      
REMARK 465     MET A    55                                                      
REMARK 465     GLY A    56                                                      
REMARK 465     SER A    57                                                      
REMARK 465     ALA A    58                                                      
REMARK 465     PRO A    59                                                      
REMARK 465     SER A    60                                                      
REMARK 465     PHE A    61                                                      
REMARK 465     ASN A    62                                                      
REMARK 465     VAL A    63                                                      
REMARK 465     ASP A    64                                                      
REMARK 465     PRO A    65                                                      
REMARK 465     LEU A    66                                                      
REMARK 465     GLU A    67                                                      
REMARK 465     GLN A    68                                                      
REMARK 465     PRO A    69                                                      
REMARK 465     ALA A    70                                                      
REMARK 465     GLU A    71                                                      
REMARK 465     PRO A    72                                                      
REMARK 465     SER A    73                                                      
REMARK 465     LYS A    74                                                      
REMARK 465     LEU A    75                                                      
REMARK 465     ALA A    76                                                      
REMARK 465     LYS A    77                                                      
REMARK 465     LYS A    78                                                      
REMARK 465     LEU A    79                                                      
REMARK 465     ARG A    80                                                      
REMARK 465     ALA A    81                                                      
REMARK 465     GLU A    82                                                      
REMARK 465     ALA A   272                                                      
REMARK 465     LEU A   273                                                      
REMARK 465     ASN A   274                                                      
REMARK 465     GLN A   275                                                      
REMARK 465     LEU A   276                                                      
REMARK 465     THR A   277                                                      
REMARK 465     SER A   278                                                      
REMARK 465     GLN A   580                                                      
REMARK 465     GLY A   581                                                      
REMARK 465     MET A   582                                                      
REMARK 465     VAL A   583                                                      
REMARK 465     THR A   584                                                      
REMARK 465     GLN A   585                                                      
REMARK 465     TRP A   586                                                      
REMARK 465     GLN A   587                                                      
REMARK 465     SER A   588                                                      
REMARK 465     LEU A   589                                                      
REMARK 465     PHE A   590                                                      
REMARK 465     TYR A   591                                                      
REMARK 465     GLU A   592                                                      
REMARK 465     HIS A   593                                                      
REMARK 465     ARG A   594                                                      
REMARK 465     TYR A   595                                                      
REMARK 465     SER A   596                                                      
REMARK 465     LYS A   648                                                      
REMARK 465     VAL A   649                                                      
REMARK 465     PRO A   650                                                      
REMARK 465     VAL A   651                                                      
REMARK 465     LEU A   652                                                      
REMARK 465     PRO A   653                                                      
REMARK 465     MET A   654                                                      
REMARK 465     VAL A   655                                                      
REMARK 465     ALA A   656                                                      
REMARK 465     GLY A   657                                                      
REMARK 465     GLY A   658                                                      
REMARK 465     SER A   659                                                      
REMARK 465     GLY A   660                                                      
REMARK 465     LEU A   661                                                      
REMARK 465     ASP A   662                                                      
REMARK 465     GLU A   663                                                      
REMARK 465     PHE A   664                                                      
REMARK 465     ILE A   665                                                      
REMARK 465     ASN A   666                                                      
REMARK 465     PHE A   667                                                      
REMARK 465     ASP A   668                                                      
REMARK 465     PRO A   669                                                      
REMARK 465     GLU A   670                                                      
REMARK 465     VAL A   671                                                      
REMARK 465     GLU A   672                                                      
REMARK 465     ARG A   673                                                      
REMARK 465     GLN A   674                                                      
REMARK 465     GLN A   675                                                      
REMARK 465     THR A   676                                                      
REMARK 465     GLU A   677                                                      
REMARK 465     LEU A   678                                                      
REMARK 465     ARG A   679                                                      
REMARK 465     HIS A   680                                                      
REMARK 465     LYS A   681                                                      
REMARK 465     ARG A   682                                                      
REMARK 465     THR A   683                                                      
REMARK 465     GLY A   684                                                      
REMARK 465     GLY A   685                                                      
REMARK 465     LYS A   686                                                      
REMARK 465     HIS A   687                                                      
REMARK 465     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   650                                                      
REMARK 465     VAL B   651                                                      
REMARK 465     LEU B   652                                                      
REMARK 465     PRO B   653                                                      
REMARK 465     MET B   654                                                      
REMARK 465     VAL B   655                                                      
REMARK 465     ALA B   656                                                      
REMARK 465     GLY B   657                                                      
REMARK 465     GLY B   658                                                      
REMARK 465     SER B   659                                                      
REMARK 465     GLY B   660                                                      
REMARK 465     LEU B   661                                                      
REMARK 465     ASP B   662                                                      
REMARK 465     GLU B   663                                                      
REMARK 465     PHE B   664                                                      
REMARK 465     ILE B   665                                                      
REMARK 465     ASN B   666                                                      
REMARK 465     PHE B   667                                                      
REMARK 465     ASP B   668                                                      
REMARK 465     PRO B   669                                                      
REMARK 465     GLU B   670                                                      
REMARK 465     VAL B   671                                                      
REMARK 465     GLU B   672                                                      
REMARK 465     ARG B   673                                                      
REMARK 465     GLN B   674                                                      
REMARK 465     GLN B   675                                                      
REMARK 465     THR B   676                                                      
REMARK 465     GLU B   677                                                      
REMARK 465     LEU B   678                                                      
REMARK 465     ARG B   679                                                      
REMARK 465     HIS B   680                                                      
REMARK 465     LYS B   681                                                      
REMARK 465     ARG B   682                                                      
REMARK 465     THR B   683                                                      
REMARK 465     GLY B   684                                                      
REMARK 465     GLY B   685                                                      
REMARK 465     LYS B   686                                                      
REMARK 465     HIS B   687                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A 279    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 579    CG   CD   OE1  OE2                                  
REMARK 470     ASN B 274    CG   OD1  ND2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   880     O    HOH A  1068              2.01            
REMARK 500   OD2  ASP B   368     NH2  ARG B   400              2.01            
REMARK 500   O    HOH B   856     O    HOH B   999              2.02            
REMARK 500   O    HOH A  1077     O    HOH B   856              2.02            
REMARK 500   O1   OXY B   708     O    HOH B   801              2.03            
REMARK 500   O    ALA B   327     NH1  ARG B   444              2.04            
REMARK 500   O    HOH A   808     O    HOH A   868              2.06            
REMARK 500   O    HOH A   844     O    HOH A  1225              2.07            
REMARK 500   O    HOH A  1213     O    HOH B  1043              2.07            
REMARK 500   O    HOH A  1162     O    HOH B   965              2.09            
REMARK 500   O    PHE A   388     NH1  ARG A   393              2.09            
REMARK 500   NH2  ARG B   151     O    HOH B   802              2.09            
REMARK 500   NH2  ARG B   326     O    ILE B   438              2.14            
REMARK 500   O    HOH B   955     O    HOH B  1044              2.15            
REMARK 500   O    HOH B   809     O    HOH B  1029              2.15            
REMARK 500   O    HOH A  1224     O    HOH A  1249              2.16            
REMARK 500   O    HOH B   972     O    HOH B  1052              2.16            
REMARK 500   O    HOH A  1179     O    HOH A  1188              2.17            
REMARK 500   O    HOH A   982     O    HOH A  1188              2.18            
REMARK 500   O    HOH A  1035     O    HOH A  1208              2.18            
REMARK 500   O    HOH A  1031     O    HOH A  1278              2.18            
REMARK 500   O    HOH A  1101     O    HOH A  1165              2.19            
REMARK 500   O    HOH A   880     O    HOH B   965              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A  1212     O    HOH B   824     3544     2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    MET B 555   CA  -  CB  -  CG  ANGL. DEV. = -15.6 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A 270     -128.53     23.16                                   
REMARK 500    ASP A 350     -150.96     66.52                                   
REMARK 500    ASN B 127       71.03   -107.31                                   
REMARK 500    ASN B 271      -60.20    -95.98                                   
REMARK 500    ALA B 272        5.96     59.49                                   
REMARK 500    LEU B 298      -77.12    -66.94                                   
REMARK 500    ALA B 314      -35.79    -38.31                                   
REMARK 500    ASP B 350     -150.15     61.75                                   
REMARK 500    ASN B 366     -133.75    -80.96                                   
REMARK 500    ALA B 367      127.97     60.05                                   
REMARK 500    TRP B 447      -63.52   -100.84                                   
REMARK 500    GLN B 450     -178.57    -66.86                                   
REMARK 500    ILE B 451      -55.74     62.36                                   
REMARK 500    PHE B 590      -99.19    -96.84                                   
REMARK 500    TYR B 591       41.12    -50.35                                   
REMARK 500    GLU B 592       50.88      6.53                                   
REMARK 500    THR B 598       87.21     71.63                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1289        DISTANCE =  6.57 ANGSTROMS                       
REMARK 525    HOH A1290        DISTANCE =  6.78 ANGSTROMS                       
REMARK 525    HOH A1291        DISTANCE =  7.72 ANGSTROMS                       
REMARK 525    HOH A1292        DISTANCE =  7.89 ANGSTROMS                       
REMARK 525    HOH B1127        DISTANCE =  5.96 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A 701   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN A 343   OE1                                                    
REMARK 620 2 GLN A 506   O   159.0                                              
REMARK 620 3 TRP A 508   O    82.1  92.3                                        
REMARK 620 4 HOH A 822   O   104.4  83.8 171.0                                  
REMARK 620 5 HOH A 964   O    79.7  82.2 104.7  82.9                            
REMARK 620 6 HOH A1108   O    91.7 107.9  83.8  89.6 166.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 703  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 550   OD1                                                    
REMARK 620 2 ASN A 577   OD1  80.9                                              
REMARK 620 3 TPP A 704   O2A  88.1 168.9                                        
REMARK 620 4 TPP A 704   O2B 163.9  96.2  94.0                                  
REMARK 620 5 HOH A 902   O    81.6  83.4  93.7  82.3                            
REMARK 620 6 HOH A1130   O    93.7  87.5  94.6 102.1 170.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K B 701   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN B 506   O                                                      
REMARK 620 2 TRP B 508   O    91.7                                              
REMARK 620 3 HOH B 866   O    86.1 108.8                                        
REMARK 620 4 HOH B 814   O    80.4 169.1  78.4                                  
REMARK 620 5 HOH B1018   O   107.3  82.6 162.5  92.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 703  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 550   OD2                                                    
REMARK 620 2 ASN B 577   OD1  86.2                                              
REMARK 620 3 TPP B 704   O2A  87.4 173.6                                        
REMARK 620 4 TPP B 704   O2B 168.9  96.3  90.1                                  
REMARK 620 5 HOH B 834   O    92.0  89.2  90.3  98.8                            
REMARK 620 6 HOH B 913   O    85.6  87.9  92.3  83.7 176.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue K A 701                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FAD A 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 703                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue TPP A 704                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OXY A 705                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OXY A 706                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OXY A 707                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 708                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue K B 701                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FAD B 702                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 703                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue TPP B 704                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OXY B 705                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OXY B 706                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OXY B 707                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OXY B 708                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OXY B 709                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OXY B 710                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 B 711                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT B 712                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT B 713                 
DBREF  5IMS A   58   687  UNP    P07342   ILVB_YEAST      58    687             
DBREF  5IMS B   58   687  UNP    P07342   ILVB_YEAST      58    687             
SEQADV 5IMS MET A   11  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS HIS A   12  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS HIS A   13  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS HIS A   14  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS HIS A   15  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS HIS A   16  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS HIS A   17  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS SER A   18  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS SER A   19  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS GLY A   20  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS LEU A   21  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS VAL A   22  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS PRO A   23  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS ARG A   24  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS GLY A   25  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS SER A   26  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS GLY A   27  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS MET A   28  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS LYS A   29  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS GLU A   30  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS THR A   31  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS ALA A   32  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS ALA A   33  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS ALA A   34  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS LYS A   35  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS PHE A   36  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS GLU A   37  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS ARG A   38  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS GLN A   39  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS HIS A   40  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS MET A   41  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS ASP A   42  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS SER A   43  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS PRO A   44  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS ASP A   45  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS LEU A   46  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS GLY A   47  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS THR A   48  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS ASP A   49  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS ASP A   50  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS ASP A   51  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS ASP A   52  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS LYS A   53  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS ALA A   54  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS MET A   55  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS GLY A   56  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS SER A   57  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS MET B   11  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS HIS B   12  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS HIS B   13  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS HIS B   14  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS HIS B   15  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS HIS B   16  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS HIS B   17  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS SER B   18  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS SER B   19  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS GLY B   20  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS LEU B   21  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS VAL B   22  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS PRO B   23  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS ARG B   24  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS GLY B   25  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS SER B   26  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS GLY B   27  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS MET B   28  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS LYS B   29  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS GLU B   30  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS THR B   31  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS ALA B   32  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS ALA B   33  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS ALA B   34  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS LYS B   35  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS PHE B   36  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS GLU B   37  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS ARG B   38  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS GLN B   39  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS HIS B   40  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS MET B   41  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS ASP B   42  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS SER B   43  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS PRO B   44  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS ASP B   45  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS LEU B   46  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS GLY B   47  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS THR B   48  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS ASP B   49  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS ASP B   50  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS ASP B   51  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS ASP B   52  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS LYS B   53  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS ALA B   54  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS MET B   55  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS GLY B   56  UNP  P07342              EXPRESSION TAG                 
SEQADV 5IMS SER B   57  UNP  P07342              EXPRESSION TAG                 
SEQRES   1 A  677  MET HIS HIS HIS HIS HIS HIS SER SER GLY LEU VAL PRO          
SEQRES   2 A  677  ARG GLY SER GLY MET LYS GLU THR ALA ALA ALA LYS PHE          
SEQRES   3 A  677  GLU ARG GLN HIS MET ASP SER PRO ASP LEU GLY THR ASP          
SEQRES   4 A  677  ASP ASP ASP LYS ALA MET GLY SER ALA PRO SER PHE ASN          
SEQRES   5 A  677  VAL ASP PRO LEU GLU GLN PRO ALA GLU PRO SER LYS LEU          
SEQRES   6 A  677  ALA LYS LYS LEU ARG ALA GLU PRO ASP MET ASP THR SER          
SEQRES   7 A  677  PHE VAL GLY LEU THR GLY GLY GLN ILE PHE ASN GLU MET          
SEQRES   8 A  677  MET SER ARG GLN ASN VAL ASP THR VAL PHE GLY TYR PRO          
SEQRES   9 A  677  GLY GLY ALA ILE LEU PRO VAL TYR ASP ALA ILE HIS ASN          
SEQRES  10 A  677  SER ASP LYS PHE ASN PHE VAL LEU PRO LYS HIS GLU GLN          
SEQRES  11 A  677  GLY ALA GLY HIS MET ALA GLU GLY TYR ALA ARG ALA SER          
SEQRES  12 A  677  GLY LYS PRO GLY VAL VAL LEU VAL THR SER GLY PRO GLY          
SEQRES  13 A  677  ALA THR ASN VAL VAL THR PRO MET ALA ASP ALA PHE ALA          
SEQRES  14 A  677  ASP GLY ILE PRO MET VAL VAL PHE THR GLY GLN VAL PRO          
SEQRES  15 A  677  THR SER ALA ILE GLY THR ASP ALA PHE GLN GLU ALA ASP          
SEQRES  16 A  677  VAL VAL GLY ILE SER ARG SER CYS THR LYS TRP ASN VAL          
SEQRES  17 A  677  MET VAL LYS SER VAL GLU GLU LEU PRO LEU ARG ILE ASN          
SEQRES  18 A  677  GLU ALA PHE GLU ILE ALA THR SER GLY ARG PRO GLY PRO          
SEQRES  19 A  677  VAL LEU VAL ASP LEU PRO LYS ASP VAL THR ALA ALA ILE          
SEQRES  20 A  677  LEU ARG ASN PRO ILE PRO THR LYS THR THR LEU PRO SER          
SEQRES  21 A  677  ASN ALA LEU ASN GLN LEU THR SER ARG ALA GLN ASP GLU          
SEQRES  22 A  677  PHE VAL MET GLN SER ILE ASN LYS ALA ALA ASP LEU ILE          
SEQRES  23 A  677  ASN LEU ALA LYS LYS PRO VAL LEU TYR VAL GLY ALA GLY          
SEQRES  24 A  677  ILE LEU ASN HIS ALA ASP GLY PRO ARG LEU LEU LYS GLU          
SEQRES  25 A  677  LEU SER ASP ARG ALA GLN ILE PRO VAL THR THR THR LEU          
SEQRES  26 A  677  GLN GLY LEU GLY SER PHE ASP GLN GLU ASP PRO LYS SER          
SEQRES  27 A  677  LEU ASP MET LEU GLY MET HIS GLY CYS ALA THR ALA ASN          
SEQRES  28 A  677  LEU ALA VAL GLN ASN ALA ASP LEU ILE ILE ALA VAL GLY          
SEQRES  29 A  677  ALA ARG PHE ASP ASP ARG VAL THR GLY ASN ILE SER LYS          
SEQRES  30 A  677  PHE ALA PRO GLU ALA ARG ARG ALA ALA ALA GLU GLY ARG          
SEQRES  31 A  677  GLY GLY ILE ILE HIS PHE GLU VAL SER PRO LYS ASN ILE          
SEQRES  32 A  677  ASN LYS VAL VAL GLN THR GLN ILE ALA VAL GLU GLY ASP          
SEQRES  33 A  677  ALA THR THR ASN LEU GLY LYS MET MET SER LYS ILE PHE          
SEQRES  34 A  677  PRO VAL LYS GLU ARG SER GLU TRP PHE ALA GLN ILE ASN          
SEQRES  35 A  677  LYS TRP LYS LYS GLU TYR PRO TYR ALA TYR MET GLU GLU          
SEQRES  36 A  677  THR PRO GLY SER LYS ILE LYS PRO GLN THR VAL ILE LYS          
SEQRES  37 A  677  LYS LEU SER LYS VAL ALA ASN ASP THR GLY ARG HIS VAL          
SEQRES  38 A  677  ILE VAL THR THR GLY VAL GLY GLN HIS GLN MET TRP ALA          
SEQRES  39 A  677  ALA GLN HIS TRP THR TRP ARG ASN PRO HIS THR PHE ILE          
SEQRES  40 A  677  THR SER GLY GLY LEU GLY THR MET GLY TYR GLY LEU PRO          
SEQRES  41 A  677  ALA ALA ILE GLY ALA GLN VAL ALA LYS PRO GLU SER LEU          
SEQRES  42 A  677  VAL ILE ASP ILE ASP GLY ASP ALA SER PHE ASN MET THR          
SEQRES  43 A  677  LEU THR GLU LEU SER SER ALA VAL GLN ALA GLY THR PRO          
SEQRES  44 A  677  VAL LYS ILE LEU ILE LEU ASN ASN GLU GLU GLN GLY MET          
SEQRES  45 A  677  VAL THR GLN TRP GLN SER LEU PHE TYR GLU HIS ARG TYR          
SEQRES  46 A  677  SER HIS THR HIS GLN LEU ASN PRO ASP PHE ILE LYS LEU          
SEQRES  47 A  677  ALA GLU ALA MET GLY LEU LYS GLY LEU ARG VAL LYS LYS          
SEQRES  48 A  677  GLN GLU GLU LEU ASP ALA LYS LEU LYS GLU PHE VAL SER          
SEQRES  49 A  677  THR LYS GLY PRO VAL LEU LEU GLU VAL GLU VAL ASP LYS          
SEQRES  50 A  677  LYS VAL PRO VAL LEU PRO MET VAL ALA GLY GLY SER GLY          
SEQRES  51 A  677  LEU ASP GLU PHE ILE ASN PHE ASP PRO GLU VAL GLU ARG          
SEQRES  52 A  677  GLN GLN THR GLU LEU ARG HIS LYS ARG THR GLY GLY LYS          
SEQRES  53 A  677  HIS                                                          
SEQRES   1 B  677  MET HIS HIS HIS HIS HIS HIS SER SER GLY LEU VAL PRO          
SEQRES   2 B  677  ARG GLY SER GLY MET LYS GLU THR ALA ALA ALA LYS PHE          
SEQRES   3 B  677  GLU ARG GLN HIS MET ASP SER PRO ASP LEU GLY THR ASP          
SEQRES   4 B  677  ASP ASP ASP LYS ALA MET GLY SER ALA PRO SER PHE ASN          
SEQRES   5 B  677  VAL ASP PRO LEU GLU GLN PRO ALA GLU PRO SER LYS LEU          
SEQRES   6 B  677  ALA LYS LYS LEU ARG ALA GLU PRO ASP MET ASP THR SER          
SEQRES   7 B  677  PHE VAL GLY LEU THR GLY GLY GLN ILE PHE ASN GLU MET          
SEQRES   8 B  677  MET SER ARG GLN ASN VAL ASP THR VAL PHE GLY TYR PRO          
SEQRES   9 B  677  GLY GLY ALA ILE LEU PRO VAL TYR ASP ALA ILE HIS ASN          
SEQRES  10 B  677  SER ASP LYS PHE ASN PHE VAL LEU PRO LYS HIS GLU GLN          
SEQRES  11 B  677  GLY ALA GLY HIS MET ALA GLU GLY TYR ALA ARG ALA SER          
SEQRES  12 B  677  GLY LYS PRO GLY VAL VAL LEU VAL THR SER GLY PRO GLY          
SEQRES  13 B  677  ALA THR ASN VAL VAL THR PRO MET ALA ASP ALA PHE ALA          
SEQRES  14 B  677  ASP GLY ILE PRO MET VAL VAL PHE THR GLY GLN VAL PRO          
SEQRES  15 B  677  THR SER ALA ILE GLY THR ASP ALA PHE GLN GLU ALA ASP          
SEQRES  16 B  677  VAL VAL GLY ILE SER ARG SER CYS THR LYS TRP ASN VAL          
SEQRES  17 B  677  MET VAL LYS SER VAL GLU GLU LEU PRO LEU ARG ILE ASN          
SEQRES  18 B  677  GLU ALA PHE GLU ILE ALA THR SER GLY ARG PRO GLY PRO          
SEQRES  19 B  677  VAL LEU VAL ASP LEU PRO LYS ASP VAL THR ALA ALA ILE          
SEQRES  20 B  677  LEU ARG ASN PRO ILE PRO THR LYS THR THR LEU PRO SER          
SEQRES  21 B  677  ASN ALA LEU ASN GLN LEU THR SER ARG ALA GLN ASP GLU          
SEQRES  22 B  677  PHE VAL MET GLN SER ILE ASN LYS ALA ALA ASP LEU ILE          
SEQRES  23 B  677  ASN LEU ALA LYS LYS PRO VAL LEU TYR VAL GLY ALA GLY          
SEQRES  24 B  677  ILE LEU ASN HIS ALA ASP GLY PRO ARG LEU LEU LYS GLU          
SEQRES  25 B  677  LEU SER ASP ARG ALA GLN ILE PRO VAL THR THR THR LEU          
SEQRES  26 B  677  GLN GLY LEU GLY SER PHE ASP GLN GLU ASP PRO LYS SER          
SEQRES  27 B  677  LEU ASP MET LEU GLY MET HIS GLY CYS ALA THR ALA ASN          
SEQRES  28 B  677  LEU ALA VAL GLN ASN ALA ASP LEU ILE ILE ALA VAL GLY          
SEQRES  29 B  677  ALA ARG PHE ASP ASP ARG VAL THR GLY ASN ILE SER LYS          
SEQRES  30 B  677  PHE ALA PRO GLU ALA ARG ARG ALA ALA ALA GLU GLY ARG          
SEQRES  31 B  677  GLY GLY ILE ILE HIS PHE GLU VAL SER PRO LYS ASN ILE          
SEQRES  32 B  677  ASN LYS VAL VAL GLN THR GLN ILE ALA VAL GLU GLY ASP          
SEQRES  33 B  677  ALA THR THR ASN LEU GLY LYS MET MET SER LYS ILE PHE          
SEQRES  34 B  677  PRO VAL LYS GLU ARG SER GLU TRP PHE ALA GLN ILE ASN          
SEQRES  35 B  677  LYS TRP LYS LYS GLU TYR PRO TYR ALA TYR MET GLU GLU          
SEQRES  36 B  677  THR PRO GLY SER LYS ILE LYS PRO GLN THR VAL ILE LYS          
SEQRES  37 B  677  LYS LEU SER LYS VAL ALA ASN ASP THR GLY ARG HIS VAL          
SEQRES  38 B  677  ILE VAL THR THR GLY VAL GLY GLN HIS GLN MET TRP ALA          
SEQRES  39 B  677  ALA GLN HIS TRP THR TRP ARG ASN PRO HIS THR PHE ILE          
SEQRES  40 B  677  THR SER GLY GLY LEU GLY THR MET GLY TYR GLY LEU PRO          
SEQRES  41 B  677  ALA ALA ILE GLY ALA GLN VAL ALA LYS PRO GLU SER LEU          
SEQRES  42 B  677  VAL ILE ASP ILE ASP GLY ASP ALA SER PHE ASN MET THR          
SEQRES  43 B  677  LEU THR GLU LEU SER SER ALA VAL GLN ALA GLY THR PRO          
SEQRES  44 B  677  VAL LYS ILE LEU ILE LEU ASN ASN GLU GLU GLN GLY MET          
SEQRES  45 B  677  VAL THR GLN TRP GLN SER LEU PHE TYR GLU HIS ARG TYR          
SEQRES  46 B  677  SER HIS THR HIS GLN LEU ASN PRO ASP PHE ILE LYS LEU          
SEQRES  47 B  677  ALA GLU ALA MET GLY LEU LYS GLY LEU ARG VAL LYS LYS          
SEQRES  48 B  677  GLN GLU GLU LEU ASP ALA LYS LEU LYS GLU PHE VAL SER          
SEQRES  49 B  677  THR LYS GLY PRO VAL LEU LEU GLU VAL GLU VAL ASP LYS          
SEQRES  50 B  677  LYS VAL PRO VAL LEU PRO MET VAL ALA GLY GLY SER GLY          
SEQRES  51 B  677  LEU ASP GLU PHE ILE ASN PHE ASP PRO GLU VAL GLU ARG          
SEQRES  52 B  677  GLN GLN THR GLU LEU ARG HIS LYS ARG THR GLY GLY LYS          
SEQRES  53 B  677  HIS                                                          
HET      K  A 701       1                                                       
HET    FAD  A 702      53                                                       
HET     MG  A 703       1                                                       
HET    TPP  A 704      26                                                       
HET    OXY  A 705       2                                                       
HET    OXY  A 706       2                                                       
HET    OXY  A 707       2                                                       
HET    ACT  A 708       4                                                       
HET      K  B 701       1                                                       
HET    FAD  B 702      53                                                       
HET     MG  B 703       1                                                       
HET    TPP  B 704      26                                                       
HET    OXY  B 705       2                                                       
HET    OXY  B 706       2                                                       
HET    OXY  B 707       2                                                       
HET    OXY  B 708       2                                                       
HET    OXY  B 709       2                                                       
HET    OXY  B 710       2                                                       
HET    PO4  B 711       5                                                       
HET    ACT  B 712       4                                                       
HET    ACT  B 713       4                                                       
HETNAM       K POTASSIUM ION                                                    
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     TPP THIAMINE DIPHOSPHATE                                             
HETNAM     OXY OXYGEN MOLECULE                                                  
HETNAM     ACT ACETATE ION                                                      
HETNAM     PO4 PHOSPHATE ION                                                    
FORMUL   3    K    2(K 1+)                                                      
FORMUL   4  FAD    2(C27 H33 N9 O15 P2)                                         
FORMUL   5   MG    2(MG 2+)                                                     
FORMUL   6  TPP    2(C12 H19 N4 O7 P2 S 1+)                                     
FORMUL   7  OXY    9(O2)                                                        
FORMUL  10  ACT    3(C2 H3 O2 1-)                                               
FORMUL  21  PO4    O4 P 3-                                                      
FORMUL  24  HOH   *819(H2 O)                                                    
HELIX    1 AA1 THR A   93  GLN A  105  1                                  13    
HELIX    2 AA2 GLY A  115  ALA A  117  5                                   3    
HELIX    3 AA3 ILE A  118  SER A  128  1                                  11    
HELIX    4 AA4 HIS A  138  GLY A  154  1                                  17    
HELIX    5 AA5 GLY A  164  ASN A  169  1                                   6    
HELIX    6 AA6 VAL A  170  GLY A  181  1                                  12    
HELIX    7 AA7 PRO A  192  ILE A  196  5                                   5    
HELIX    8 AA8 ASP A  205  ARG A  211  1                                   7    
HELIX    9 AA9 SER A  212  THR A  214  5                                   3    
HELIX   10 AB1 SER A  222  GLU A  224  5                                   3    
HELIX   11 AB2 GLU A  225  THR A  238  1                                  14    
HELIX   12 AB3 LYS A  251  ALA A  256  1                                   6    
HELIX   13 AB4 LYS A  265  LEU A  268  5                                   4    
HELIX   14 AB5 ALA A  280  ALA A  299  1                                  20    
HELIX   15 AB6 ALA A  308  HIS A  313  5                                   6    
HELIX   16 AB7 ASP A  315  GLN A  328  1                                  14    
HELIX   17 AB8 LEU A  335  LEU A  338  5                                   4    
HELIX   18 AB9 CYS A  357  ALA A  367  1                                  11    
HELIX   19 AC1 ASP A  378  GLY A  383  1                                   6    
HELIX   20 AC2 ASN A  384  PHE A  388  5                                   5    
HELIX   21 AC3 ALA A  389  GLU A  398  1                                  10    
HELIX   22 AC4 SER A  409  ILE A  413  5                                   5    
HELIX   23 AC5 ASP A  426  MET A  435  1                                  10    
HELIX   24 AC6 SER A  436  ILE A  438  5                                   3    
HELIX   25 AC7 ARG A  444  TYR A  458  1                                  15    
HELIX   26 AC8 LYS A  472  ASP A  486  1                                  15    
HELIX   27 AC9 GLY A  498  TRP A  508  1                                  11    
HELIX   28 AD1 TYR A  527  LYS A  539  1                                  13    
HELIX   29 AD2 ASP A  550  LEU A  557  1                                   8    
HELIX   30 AD3 GLU A  559  GLY A  567  1                                   9    
HELIX   31 AD4 ASP A  604  GLY A  613  1                                  10    
HELIX   32 AD5 LYS A  621  GLU A  623  5                                   3    
HELIX   33 AD6 GLU A  624  THR A  635  1                                  12    
HELIX   34 AD7 THR B   93  GLN B  105  1                                  13    
HELIX   35 AD8 GLY B  115  ALA B  117  5                                   3    
HELIX   36 AD9 ILE B  118  ASN B  127  1                                  10    
HELIX   37 AE1 HIS B  138  GLY B  154  1                                  17    
HELIX   38 AE2 GLY B  164  ASN B  169  1                                   6    
HELIX   39 AE3 VAL B  170  GLY B  181  1                                  12    
HELIX   40 AE4 PRO B  192  ILE B  196  5                                   5    
HELIX   41 AE5 ASP B  205  SER B  210  1                                   6    
HELIX   42 AE6 ARG B  211  THR B  214  5                                   4    
HELIX   43 AE7 SER B  222  GLU B  224  5                                   3    
HELIX   44 AE8 GLU B  225  SER B  239  1                                  15    
HELIX   45 AE9 LYS B  251  ALA B  256  1                                   6    
HELIX   46 AF1 THR B  264  LEU B  268  1                                   5    
HELIX   47 AF2 SER B  278  ALA B  299  1                                  22    
HELIX   48 AF3 ALA B  308  HIS B  313  5                                   6    
HELIX   49 AF4 ASP B  315  ALA B  327  1                                  13    
HELIX   50 AF5 LEU B  335  LEU B  338  5                                   4    
HELIX   51 AF6 CYS B  357  ASN B  366  1                                  10    
HELIX   52 AF7 ALA B  389  GLU B  398  1                                  10    
HELIX   53 AF8 SER B  409  ILE B  413  5                                   5    
HELIX   54 AF9 ASP B  426  MET B  435  1                                  10    
HELIX   55 AG1 SER B  436  ILE B  438  5                                   3    
HELIX   56 AG2 LYS B  453  TYR B  458  1                                   6    
HELIX   57 AG3 LYS B  472  THR B  487  1                                  16    
HELIX   58 AG4 GLY B  498  TRP B  508  1                                  11    
HELIX   59 AG5 TYR B  527  LYS B  539  1                                  13    
HELIX   60 AG6 ASP B  550  LEU B  557  1                                   8    
HELIX   61 AG7 THR B  558  GLY B  567  1                                  10    
HELIX   62 AG8 ASP B  604  MET B  612  1                                   9    
HELIX   63 AG9 LYS B  621  GLU B  623  5                                   3    
HELIX   64 AH1 GLU B  624  THR B  635  1                                  12    
SHEET    1 AA1 2 MET A  85  ASP A  86  0                                        
SHEET    2 AA1 2 ILE A 262  PRO A 263 -1  O  ILE A 262   N  ASP A  86           
SHEET    1 AA2 6 ASN A 132  VAL A 134  0                                        
SHEET    2 AA2 6 THR A 109  GLY A 112  1  N  VAL A 110   O  VAL A 134           
SHEET    3 AA2 6 GLY A 157  VAL A 161  1  O  VAL A 158   N  PHE A 111           
SHEET    4 AA2 6 MET A 184  GLN A 190  1  O  PHE A 187   N  VAL A 159           
SHEET    5 AA2 6 PRO A 244  PRO A 250  1  O  LEU A 249   N  THR A 188           
SHEET    6 AA2 6 TRP A 216  MET A 219  1  N  VAL A 218   O  ASP A 248           
SHEET    1 AA3 6 SER A 348  MET A 351  0                                        
SHEET    2 AA3 6 VAL A 331  THR A 333  1  N  VAL A 331   O  LEU A 349           
SHEET    3 AA3 6 PRO A 302  VAL A 306  1  N  LEU A 304   O  THR A 332           
SHEET    4 AA3 6 LEU A 369  VAL A 373  1  O  ILE A 371   N  VAL A 303           
SHEET    5 AA3 6 GLY A 402  GLU A 407  1  O  ILE A 404   N  ALA A 372           
SHEET    6 AA3 6 ILE A 421  GLU A 424  1  O  VAL A 423   N  HIS A 405           
SHEET    1 AA4 6 PHE A 516  ILE A 517  0                                        
SHEET    2 AA4 6 VAL A 491  THR A 495  1  N  VAL A 493   O  ILE A 517           
SHEET    3 AA4 6 LEU A 543  GLY A 549  1  O  ILE A 547   N  THR A 494           
SHEET    4 AA4 6 LYS A 571  ASN A 576  1  O  LEU A 573   N  ASP A 546           
SHEET    5 AA4 6 VAL A 639  GLU A 644  1  O  VAL A 639   N  ILE A 572           
SHEET    6 AA4 6 LYS A 615  VAL A 619  1  N  LEU A 617   O  LEU A 640           
SHEET    1 AA5 2 MET B  85  ASP B  86  0                                        
SHEET    2 AA5 2 ILE B 262  PRO B 263 -1  O  ILE B 262   N  ASP B  86           
SHEET    1 AA6 6 ASN B 132  VAL B 134  0                                        
SHEET    2 AA6 6 THR B 109  GLY B 112  1  N  VAL B 110   O  VAL B 134           
SHEET    3 AA6 6 GLY B 157  VAL B 161  1  O  VAL B 158   N  PHE B 111           
SHEET    4 AA6 6 MET B 184  GLN B 190  1  O  PHE B 187   N  VAL B 159           
SHEET    5 AA6 6 PRO B 244  PRO B 250  1  O  LEU B 249   N  THR B 188           
SHEET    6 AA6 6 TRP B 216  MET B 219  1  N  VAL B 218   O  ASP B 248           
SHEET    1 AA7 6 SER B 348  MET B 351  0                                        
SHEET    2 AA7 6 VAL B 331  THR B 333  1  N  VAL B 331   O  LEU B 349           
SHEET    3 AA7 6 PRO B 302  VAL B 306  1  N  VAL B 306   O  THR B 332           
SHEET    4 AA7 6 LEU B 369  VAL B 373  1  O  VAL B 373   N  TYR B 305           
SHEET    5 AA7 6 GLY B 402  GLU B 407  1  O  PHE B 406   N  ALA B 372           
SHEET    6 AA7 6 ILE B 421  GLU B 424  1  O  VAL B 423   N  HIS B 405           
SHEET    1 AA8 6 PHE B 516  ILE B 517  0                                        
SHEET    2 AA8 6 VAL B 491  THR B 495  1  N  VAL B 493   O  ILE B 517           
SHEET    3 AA8 6 LEU B 543  GLY B 549  1  O  ILE B 547   N  THR B 494           
SHEET    4 AA8 6 LYS B 571  ASN B 576  1  O  LEU B 573   N  ASP B 546           
SHEET    5 AA8 6 VAL B 639  GLU B 644  1  O  VAL B 639   N  ILE B 572           
SHEET    6 AA8 6 LYS B 615  VAL B 619  1  N  VAL B 619   O  GLU B 642           
SHEET    1 AA9 2 VAL B 583  GLN B 587  0                                        
SHEET    2 AA9 2 ARG B 594  HIS B 597 -1  O  TYR B 595   N  GLN B 585           
LINK         OE1 GLN A 343                 K     K A 701     1555   1555  2.93  
LINK         O   GLN A 506                 K     K A 701     1555   1555  2.74  
LINK         O   TRP A 508                 K     K A 701     1555   1555  2.66  
LINK         OD1 ASP A 550                MG    MG A 703     1555   1555  2.24  
LINK         OD1 ASN A 577                MG    MG A 703     1555   1555  2.31  
LINK         O   GLN B 506                 K     K B 701     1555   1555  2.76  
LINK         O   TRP B 508                 K     K B 701     1555   1555  2.63  
LINK         OD2 ASP B 550                MG    MG B 703     1555   1555  2.04  
LINK         OD1 ASN B 577                MG    MG B 703     1555   1555  2.11  
LINK         K     K A 701                 O   HOH A 822     1555   1555  2.86  
LINK         K     K A 701                 O   HOH A 964     1555   1555  2.79  
LINK         K     K A 701                 O   HOH A1108     1555   1555  2.65  
LINK        MG    MG A 703                 O2A TPP A 704     1555   1555  2.04  
LINK        MG    MG A 703                 O2B TPP A 704     1555   1555  2.06  
LINK        MG    MG A 703                 O   HOH A 902     1555   1555  2.03  
LINK        MG    MG A 703                 O   HOH A1130     1555   1555  2.18  
LINK         K     K B 701                 O   HOH B 866     1555   1555  2.69  
LINK         K     K B 701                 O   HOH B 814     1555   1555  2.82  
LINK         K     K B 701                 O   HOH B1018     1555   1555  2.89  
LINK        MG    MG B 703                 O2A TPP B 704     1555   1555  2.07  
LINK        MG    MG B 703                 O2B TPP B 704     1555   1555  1.93  
LINK        MG    MG B 703                 O   HOH B 834     1555   1555  2.16  
LINK        MG    MG B 703                 O   HOH B 913     1555   1555  2.17  
SITE     1 AC1  6 GLN A 343  GLN A 506  TRP A 508  HOH A 822                    
SITE     2 AC1  6 HOH A 964  HOH A1108                                          
SITE     1 AC2 33 ARG A 241  GLY A 307  ALA A 308  GLY A 309                    
SITE     2 AC2 33 ASN A 312  THR A 334  LEU A 335  LEU A 352                    
SITE     3 AC2 33 GLY A 353  MET A 354  HIS A 355  GLY A 356                    
SITE     4 AC2 33 GLY A 374  ALA A 375  ARG A 376  ASP A 378                    
SITE     5 AC2 33 ARG A 380  VAL A 381  GLU A 407  VAL A 408                    
SITE     6 AC2 33 SER A 409  ASN A 412  GLY A 425  ASP A 426                    
SITE     7 AC2 33 ALA A 427  HOH A 801  HOH A 868  HOH A 879                    
SITE     8 AC2 33 HOH A 886  HOH A 990  HOH A1009  HOH A1042                    
SITE     9 AC2 33 HOH A1095                                                     
SITE     1 AC3  5 ASP A 550  ASN A 577  TPP A 704  HOH A 902                    
SITE     2 AC3  5 HOH A1130                                                     
SITE     1 AC4 29 VAL A 497  GLY A 498  GLN A 499  HIS A 500                    
SITE     2 AC4 29 GLY A 523  MET A 525  GLY A 549  ASP A 550                    
SITE     3 AC4 29 ALA A 551  SER A 552  ASN A 577   MG A 703                    
SITE     4 AC4 29 HOH A 849  HOH A 902  HOH A1030  HOH A1040                    
SITE     5 AC4 29 HOH A1130  TYR B 113  PRO B 114  GLY B 115                    
SITE     6 AC4 29 GLU B 139  PRO B 165  ASN B 169  GLN B 202                    
SITE     7 AC4 29 OXY B 705  OXY B 707  ACT B 712  HOH B 833                    
SITE     8 AC4 29 HOH B 997                                                     
SITE     1 AC5  4 ACT A 708  HOH A 803  MET B 582  TPP B 704                    
SITE     1 AC6  6 GLY A 116  ALA A 117  THR A 162  SER A 163                    
SITE     2 AC6  6 GLN A 202  ACT A 708                                          
SITE     1 AC7  6 ALA A 551  GLN A 600  HOH A 806  HOH A 809                    
SITE     2 AC7  6 TYR B 113  LYS B 137                                          
SITE     1 AC8  9 GLY A 115  GLY A 116  PHE A 201  GLN A 202                    
SITE     2 AC8  9 OXY A 705  OXY A 706  HOH A1063  TPP B 704                    
SITE     3 AC8  9 HOH B 875                                                     
SITE     1 AC9  6 GLN B 343  GLN B 506  TRP B 508  HOH B 814                    
SITE     2 AC9  6 HOH B 866  HOH B1018                                          
SITE     1 AD1 32 ARG B 241  GLY B 307  ALA B 308  GLY B 309                    
SITE     2 AD1 32 ASN B 312  THR B 334  LEU B 335  LEU B 352                    
SITE     3 AD1 32 MET B 354  HIS B 355  GLY B 374  ALA B 375                    
SITE     4 AD1 32 ARG B 376  ARG B 380  VAL B 381  GLU B 407                    
SITE     5 AD1 32 VAL B 408  SER B 409  ASN B 412  GLY B 425                    
SITE     6 AD1 32 ASP B 426  ALA B 427  GLN B 501  MET B 502                    
SITE     7 AD1 32 GLY B 520  GLY B 521  HOH B 859  HOH B 897                    
SITE     8 AD1 32 HOH B 920  HOH B 934  HOH B 995  HOH B1020                    
SITE     1 AD2  6 ASP B 550  ASN B 577  TPP B 704  OXY B 708                    
SITE     2 AD2  6 HOH B 834  HOH B 913                                          
SITE     1 AD3 25 TYR A 113  PRO A 114  GLU A 139  PRO A 165                    
SITE     2 AD3 25 ASN A 169  OXY A 705  ACT A 708  VAL B 497                    
SITE     3 AD3 25 GLY B 498  GLN B 499  HIS B 500  GLY B 523                    
SITE     4 AD3 25 MET B 525  GLY B 549  ASP B 550  ALA B 551                    
SITE     5 AD3 25 SER B 552  ASN B 577   MG B 703  OXY B 708                    
SITE     6 AD3 25 HOH B 801  HOH B 834  HOH B 875  HOH B 913                    
SITE     7 AD3 25 HOH B 943                                                     
SITE     1 AD4  5 TPP A 704  GLY B 115  ACT B 712  HOH B 850                    
SITE     2 AD4  5 HOH B 930                                                     
SITE     1 AD5  7 GLY B 116  ALA B 117  THR B 162  SER B 163                    
SITE     2 AD5  7 GLN B 202  ACT B 712  ACT B 713                               
SITE     1 AD6  4 TPP A 704  TYR B 113  HOH B 850  HOH B 997                    
SITE     1 AD7  7 GLN B 499  GLY B 581   MG B 703  TPP B 704                    
SITE     2 AD7  7 HOH B 801  HOH B 803  HOH B 834                               
SITE     1 AD8  4 GLU B 578  GLN B 580  HIS B 599  GLN B 600                    
SITE     1 AD9  6 GLU B 578  GLN B 600  LEU B 601  ASN B 602                    
SITE     2 AD9  6 HOH B 836  HOH B 956                                          
SITE     1 AE1  6 HIS A 126  GLU B 541  HIS B 597  THR B 598                    
SITE     2 AE1  6 HIS B 599  HOH B1023                                          
SITE     1 AE2  7 TPP A 704  GLY B 116  OXY B 705  OXY B 706                    
SITE     2 AE2  7 ACT B 713  HOH B 833  HOH B 883                               
SITE     1 AE3  7 GLY B 116  ALA B 117  GLN B 202  LYS B 251                    
SITE     2 AE3  7 OXY B 706  ACT B 712  HOH B 909                               
CRYST1   95.683  110.180  180.005  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010451  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009076  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005555        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system